HEADER HYDROLASE/HYDROLASE INHIBITOR 11-APR-17 5PZR TITLE HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE 1,6-BISPHOSPHATE TITLE 2 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR TITLE 3 1-(3-CHLOROPHENYL)SULFONYL-3-[3-[3-[(3-CHLOROPHENYL) TITLE 4 SULFONYLCARBAMOYLAMINO]PROPOXY]PROPYL]UREA COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE 1; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: GROWTH-INHIBITING PROTEIN 17,CDNA FLJ75786,HIGHLY SIMILAR TO COMPND 5 HOMO SAPIENS FRUCTOSE-1,6-BISPHOSPHATASE 1 (FBP1),MRNA; COMPND 6 EC: 3.1.3.11; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FBP1, HCG_1640493; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS D3R DOCKING, HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN,M.G.RUDOLPH, AUTHOR 2 H.YANG,C.SHAO,S.K.BURLEY REVDAT 3 06-FEB-19 5PZR 1 AUTHOR JRNL REVDAT 2 16-JAN-19 5PZR 1 REMARK REVDAT 1 09-JAN-19 5PZR 0 JRNL AUTH A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN, JRNL AUTH 2 M.G.RUDOLPH JRNL TITL HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE JRNL TITL 2 1,6-BISPHOSPHATE 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH JRNL TITL 3 THE ALLOSTERIC INHIBITOR JRNL TITL 4 1-(3-CHLOROPHENYL)SULFONYL-3-[3-[3-[(3-CHLOROPHENYL) JRNL TITL 5 SULFONYLCARBAMOYLAMINO]PROPOXY]PROPYL]UREA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.83 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 115654 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 5812 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 29.8367 - 5.8891 0.98 4159 205 0.1913 0.2170 REMARK 3 2 5.8891 - 4.6802 1.00 4057 202 0.1570 0.1945 REMARK 3 3 4.6802 - 4.0903 1.00 3983 226 0.1388 0.1611 REMARK 3 4 4.0903 - 3.7171 1.00 3959 212 0.1431 0.1833 REMARK 3 5 3.7171 - 3.4511 1.00 3935 214 0.1475 0.1662 REMARK 3 6 3.4511 - 3.2478 1.00 3949 214 0.1472 0.1732 REMARK 3 7 3.2478 - 3.0854 1.00 3899 229 0.1507 0.1962 REMARK 3 8 3.0854 - 2.9512 1.00 3928 210 0.1661 0.1827 REMARK 3 9 2.9512 - 2.8377 1.00 3920 218 0.1631 0.2282 REMARK 3 10 2.8377 - 2.7398 1.00 3919 202 0.1637 0.1823 REMARK 3 11 2.7398 - 2.6542 1.00 3918 202 0.1651 0.2044 REMARK 3 12 2.6542 - 2.5784 1.00 3874 198 0.1676 0.2310 REMARK 3 13 2.5784 - 2.5105 1.00 3895 198 0.1741 0.2222 REMARK 3 14 2.5105 - 2.4493 1.00 3932 181 0.1778 0.2250 REMARK 3 15 2.4493 - 2.3937 1.00 3902 190 0.1752 0.2415 REMARK 3 16 2.3937 - 2.3427 1.00 3903 205 0.1762 0.2422 REMARK 3 17 2.3427 - 2.2959 1.00 3870 226 0.1833 0.2301 REMARK 3 18 2.2959 - 2.2526 1.00 3864 193 0.1855 0.2408 REMARK 3 19 2.2526 - 2.2124 1.00 3908 226 0.1886 0.2594 REMARK 3 20 2.2124 - 2.1749 0.97 3697 199 0.2021 0.2650 REMARK 3 21 2.1749 - 2.1398 0.95 3653 202 0.2117 0.2788 REMARK 3 22 2.1398 - 2.1069 0.94 3667 179 0.2297 0.2545 REMARK 3 23 2.1069 - 2.0759 0.92 3602 192 0.2310 0.2963 REMARK 3 24 2.0759 - 2.0467 0.89 3454 166 0.2442 0.2883 REMARK 3 25 2.0467 - 2.0190 0.83 3185 171 0.2532 0.3187 REMARK 3 26 2.0190 - 1.9928 0.80 3098 164 0.2767 0.3191 REMARK 3 27 1.9928 - 1.9679 0.75 2914 147 0.2773 0.3026 REMARK 3 28 1.9679 - 1.9442 0.71 2703 165 0.2929 0.3433 REMARK 3 29 1.9442 - 1.9216 0.68 2626 154 0.3169 0.3435 REMARK 3 30 1.9216 - 1.9000 0.63 2469 122 0.3267 0.3964 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.190 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.55 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 : 0.007 9973 REMARK 3 ANGLE : 0.871 13470 REMARK 3 CHIRALITY : 0.056 1528 REMARK 3 PLANARITY : 0.005 1719 REMARK 3 DIHEDRAL : 12.098 6072 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 21 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.1075 43.0544 16.4285 REMARK 3 T TENSOR REMARK 3 T11: 0.1302 T22: 0.0733 REMARK 3 T33: 0.0690 T12: 0.0180 REMARK 3 T13: 0.0172 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 0.0552 L22: 0.0070 REMARK 3 L33: 0.0139 L12: 0.0067 REMARK 3 L13: -0.0018 L23: -0.0107 REMARK 3 S TENSOR REMARK 3 S11: -0.0066 S12: 0.0387 S13: 0.0239 REMARK 3 S21: 0.0316 S22: 0.0330 S23: 0.0287 REMARK 3 S31: -0.1233 S32: -0.0486 S33: 0.0016 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.5587 45.5000 6.3344 REMARK 3 T TENSOR REMARK 3 T11: 0.1764 T22: 0.1413 REMARK 3 T33: 0.0877 T12: 0.0321 REMARK 3 T13: 0.0073 T23: 0.0175 REMARK 3 L TENSOR REMARK 3 L11: 0.0095 L22: 0.0056 REMARK 3 L33: 0.0045 L12: 0.0091 REMARK 3 L13: 0.0049 L23: 0.0030 REMARK 3 S TENSOR REMARK 3 S11: -0.0129 S12: 0.0678 S13: -0.0222 REMARK 3 S21: -0.0370 S22: -0.0092 S23: 0.0044 REMARK 3 S31: -0.0605 S32: 0.0054 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.2623 42.4692 12.7647 REMARK 3 T TENSOR REMARK 3 T11: 0.1039 T22: 0.1566 REMARK 3 T33: 0.0982 T12: -0.0980 REMARK 3 T13: 0.0823 T23: -0.0028 REMARK 3 L TENSOR REMARK 3 L11: 0.0270 L22: 0.0482 REMARK 3 L33: 0.0422 L12: 0.0283 REMARK 3 L13: -0.0247 L23: -0.0376 REMARK 3 S TENSOR REMARK 3 S11: -0.0411 S12: 0.0875 S13: 0.0657 REMARK 3 S21: -0.0546 S22: -0.0081 S23: -0.0803 REMARK 3 S31: -0.0840 S32: 0.0929 S33: -0.1092 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.9027 45.4933 2.8055 REMARK 3 T TENSOR REMARK 3 T11: 0.1388 T22: 0.1985 REMARK 3 T33: 0.1070 T12: -0.0890 REMARK 3 T13: 0.0493 T23: 0.0009 REMARK 3 L TENSOR REMARK 3 L11: 0.0338 L22: 0.0636 REMARK 3 L33: 0.0014 L12: -0.0458 REMARK 3 L13: 0.0039 L23: -0.0109 REMARK 3 S TENSOR REMARK 3 S11: 0.0175 S12: 0.0824 S13: 0.0220 REMARK 3 S21: -0.0918 S22: -0.0127 S23: -0.0814 REMARK 3 S31: -0.0294 S32: 0.0284 S33: 0.0123 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 9 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.3863 18.8415 36.9978 REMARK 3 T TENSOR REMARK 3 T11: 0.0357 T22: 0.0749 REMARK 3 T33: 0.0757 T12: 0.0193 REMARK 3 T13: 0.0047 T23: -0.0291 REMARK 3 L TENSOR REMARK 3 L11: 0.1242 L22: 0.0138 REMARK 3 L33: 0.0578 L12: -0.0302 REMARK 3 L13: -0.0078 L23: -0.0182 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: -0.0569 S13: -0.1088 REMARK 3 S21: 0.0415 S22: 0.0231 S23: 0.0309 REMARK 3 S31: 0.0149 S32: 0.0252 S33: 0.0678 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.4719 16.6082 32.5332 REMARK 3 T TENSOR REMARK 3 T11: 0.0316 T22: 0.1249 REMARK 3 T33: 0.1324 T12: 0.0250 REMARK 3 T13: 0.0357 T23: -0.0453 REMARK 3 L TENSOR REMARK 3 L11: 0.0089 L22: 0.0022 REMARK 3 L33: 0.0204 L12: 0.0033 REMARK 3 L13: 0.0038 L23: 0.0068 REMARK 3 S TENSOR REMARK 3 S11: 0.0187 S12: 0.0035 S13: 0.0173 REMARK 3 S21: 0.0040 S22: 0.0253 S23: -0.0177 REMARK 3 S31: -0.0190 S32: 0.0493 S33: 0.0306 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.6421 18.8225 13.8710 REMARK 3 T TENSOR REMARK 3 T11: 0.0222 T22: 0.1505 REMARK 3 T33: 0.0296 T12: 0.0452 REMARK 3 T13: 0.0961 T23: -0.1282 REMARK 3 L TENSOR REMARK 3 L11: 0.0562 L22: 0.0165 REMARK 3 L33: 0.0309 L12: -0.0296 REMARK 3 L13: -0.0391 L23: 0.0181 REMARK 3 S TENSOR REMARK 3 S11: 0.0209 S12: 0.1053 S13: -0.0666 REMARK 3 S21: -0.0375 S22: 0.0173 S23: -0.0183 REMARK 3 S31: 0.0173 S32: 0.1422 S33: 0.0327 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.4700 16.0306 16.1785 REMARK 3 T TENSOR REMARK 3 T11: 0.0329 T22: 0.2029 REMARK 3 T33: 0.0796 T12: 0.0855 REMARK 3 T13: 0.0327 T23: -0.0934 REMARK 3 L TENSOR REMARK 3 L11: 0.0054 L22: 0.0717 REMARK 3 L33: 0.0343 L12: 0.0031 REMARK 3 L13: 0.0118 L23: -0.0073 REMARK 3 S TENSOR REMARK 3 S11: -0.0216 S12: 0.0607 S13: -0.0720 REMARK 3 S21: 0.0196 S22: -0.0436 S23: -0.0525 REMARK 3 S31: 0.0346 S32: 0.0656 S33: -0.1061 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.0382 48.5063 41.5650 REMARK 3 T TENSOR REMARK 3 T11: 0.1186 T22: 0.0533 REMARK 3 T33: 0.0820 T12: 0.0136 REMARK 3 T13: 0.0335 T23: -0.0028 REMARK 3 L TENSOR REMARK 3 L11: 0.0266 L22: 0.0308 REMARK 3 L33: 0.0254 L12: -0.0040 REMARK 3 L13: -0.0032 L23: 0.0324 REMARK 3 S TENSOR REMARK 3 S11: 0.0327 S12: 0.0061 S13: 0.0611 REMARK 3 S21: -0.0608 S22: 0.0263 S23: -0.0141 REMARK 3 S31: -0.0846 S32: 0.0011 S33: 0.0259 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 132 THROUGH 290 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.3241 45.1227 48.2857 REMARK 3 T TENSOR REMARK 3 T11: 0.1083 T22: 0.0686 REMARK 3 T33: 0.0715 T12: 0.0200 REMARK 3 T13: 0.0242 T23: -0.0034 REMARK 3 L TENSOR REMARK 3 L11: 0.0438 L22: 0.0616 REMARK 3 L33: 0.0532 L12: -0.0148 REMARK 3 L13: 0.0305 L23: 0.0166 REMARK 3 S TENSOR REMARK 3 S11: 0.0536 S12: 0.0056 S13: 0.0537 REMARK 3 S21: 0.0262 S22: -0.0333 S23: 0.0444 REMARK 3 S31: -0.0733 S32: -0.0813 S33: 0.0112 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 291 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.4786 51.3920 55.0322 REMARK 3 T TENSOR REMARK 3 T11: 0.1143 T22: 0.0966 REMARK 3 T33: 0.1220 T12: 0.0808 REMARK 3 T13: 0.0293 T23: -0.0050 REMARK 3 L TENSOR REMARK 3 L11: 0.0094 L22: 0.0044 REMARK 3 L33: 0.0127 L12: 0.0009 REMARK 3 L13: 0.0001 L23: 0.0028 REMARK 3 S TENSOR REMARK 3 S11: 0.0186 S12: -0.0048 S13: 0.0099 REMARK 3 S21: 0.0485 S22: 0.0058 S23: 0.0464 REMARK 3 S31: -0.0432 S32: -0.0114 S33: 0.0239 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 28 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.4809 9.1877 46.9945 REMARK 3 T TENSOR REMARK 3 T11: 0.1543 T22: 0.1603 REMARK 3 T33: 0.2404 T12: 0.0682 REMARK 3 T13: 0.0174 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.0047 L22: 0.0065 REMARK 3 L33: 0.0046 L12: 0.0052 REMARK 3 L13: -0.0010 L23: 0.0013 REMARK 3 S TENSOR REMARK 3 S11: 0.0056 S12: -0.0097 S13: -0.0227 REMARK 3 S21: -0.0076 S22: -0.0090 S23: -0.0262 REMARK 3 S31: -0.0074 S32: 0.0121 S33: 0.0000 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 29 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.7237 18.9856 32.9616 REMARK 3 T TENSOR REMARK 3 T11: 0.0573 T22: 0.0626 REMARK 3 T33: 0.0511 T12: 0.0050 REMARK 3 T13: 0.0142 T23: -0.0128 REMARK 3 L TENSOR REMARK 3 L11: 0.0189 L22: 0.0058 REMARK 3 L33: 0.0125 L12: 0.0115 REMARK 3 L13: -0.0003 L23: -0.0025 REMARK 3 S TENSOR REMARK 3 S11: -0.0080 S12: 0.0291 S13: -0.0509 REMARK 3 S21: -0.0067 S22: 0.0257 S23: -0.0172 REMARK 3 S31: 0.0109 S32: 0.0164 S33: 0.0047 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 89 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.3005 4.7876 35.5171 REMARK 3 T TENSOR REMARK 3 T11: 0.1307 T22: 0.0663 REMARK 3 T33: 0.1448 T12: 0.0224 REMARK 3 T13: 0.0035 T23: -0.0059 REMARK 3 L TENSOR REMARK 3 L11: 0.0011 L22: 0.0011 REMARK 3 L33: 0.0021 L12: 0.0004 REMARK 3 L13: 0.0008 L23: -0.0013 REMARK 3 S TENSOR REMARK 3 S11: 0.0046 S12: 0.0049 S13: -0.0202 REMARK 3 S21: -0.0210 S22: 0.0015 S23: 0.0099 REMARK 3 S31: 0.0143 S32: -0.0395 S33: -0.0000 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 107 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.2142 7.6059 41.5215 REMARK 3 T TENSOR REMARK 3 T11: 0.0975 T22: 0.0229 REMARK 3 T33: 0.1141 T12: 0.0092 REMARK 3 T13: 0.0446 T23: 0.0145 REMARK 3 L TENSOR REMARK 3 L11: 0.0226 L22: 0.0432 REMARK 3 L33: 0.0423 L12: 0.0225 REMARK 3 L13: 0.0205 L23: -0.0003 REMARK 3 S TENSOR REMARK 3 S11: 0.0150 S12: 0.0289 S13: -0.0462 REMARK 3 S21: -0.0371 S22: 0.0123 S23: -0.0138 REMARK 3 S31: 0.0180 S32: -0.0184 S33: 0.0169 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 156 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.5193 14.6390 49.6021 REMARK 3 T TENSOR REMARK 3 T11: 0.0632 T22: 0.0349 REMARK 3 T33: 0.0611 T12: 0.0200 REMARK 3 T13: -0.0029 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 0.0055 L22: 0.0031 REMARK 3 L33: 0.0070 L12: 0.0041 REMARK 3 L13: -0.0004 L23: 0.0033 REMARK 3 S TENSOR REMARK 3 S11: -0.0185 S12: 0.0142 S13: -0.0692 REMARK 3 S21: -0.0176 S22: -0.0101 S23: 0.0022 REMARK 3 S31: 0.0035 S32: 0.0088 S33: -0.0002 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 180 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0040 22.3173 53.9565 REMARK 3 T TENSOR REMARK 3 T11: 0.1085 T22: 0.1010 REMARK 3 T33: 0.0939 T12: 0.0058 REMARK 3 T13: 0.0243 T23: 0.0091 REMARK 3 L TENSOR REMARK 3 L11: 0.0172 L22: 0.0288 REMARK 3 L33: 0.0160 L12: -0.0043 REMARK 3 L13: 0.0028 L23: 0.0235 REMARK 3 S TENSOR REMARK 3 S11: 0.0635 S12: 0.0100 S13: -0.0148 REMARK 3 S21: 0.0486 S22: 0.0236 S23: -0.0178 REMARK 3 S31: 0.0159 S32: 0.0017 S33: 0.0114 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 231 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.8108 24.5217 64.4329 REMARK 3 T TENSOR REMARK 3 T11: 0.1260 T22: 0.0904 REMARK 3 T33: 0.1069 T12: -0.0163 REMARK 3 T13: 0.0610 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 0.0133 L22: 0.0092 REMARK 3 L33: 0.0004 L12: -0.0046 REMARK 3 L13: -0.0011 L23: 0.0013 REMARK 3 S TENSOR REMARK 3 S11: 0.0097 S12: 0.0386 S13: 0.0113 REMARK 3 S21: 0.0300 S22: 0.0158 S23: -0.0084 REMARK 3 S31: 0.0091 S32: -0.0402 S33: 0.0170 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 232 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.1872 30.2475 66.3235 REMARK 3 T TENSOR REMARK 3 T11: 0.1493 T22: 0.1059 REMARK 3 T33: 0.0731 T12: -0.0007 REMARK 3 T13: 0.0357 T23: 0.0170 REMARK 3 L TENSOR REMARK 3 L11: 0.0052 L22: 0.0027 REMARK 3 L33: 0.0010 L12: -0.0036 REMARK 3 L13: -0.0003 L23: 0.0010 REMARK 3 S TENSOR REMARK 3 S11: 0.0230 S12: 0.0034 S13: -0.0093 REMARK 3 S21: 0.0486 S22: -0.0079 S23: 0.0067 REMARK 3 S31: -0.0015 S32: 0.0142 S33: 0.0000 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 248 THROUGH 274 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.7858 20.2522 56.0999 REMARK 3 T TENSOR REMARK 3 T11: 0.0979 T22: 0.0686 REMARK 3 T33: 0.0809 T12: -0.0066 REMARK 3 T13: 0.0226 T23: -0.0151 REMARK 3 L TENSOR REMARK 3 L11: 0.0010 L22: -0.0008 REMARK 3 L33: 0.0052 L12: -0.0001 REMARK 3 L13: -0.0008 L23: 0.0002 REMARK 3 S TENSOR REMARK 3 S11: 0.0101 S12: -0.0091 S13: 0.0081 REMARK 3 S21: -0.0010 S22: -0.0393 S23: 0.0422 REMARK 3 S31: 0.0111 S32: -0.0170 S33: -0.0011 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 275 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.8484 11.5607 58.8587 REMARK 3 T TENSOR REMARK 3 T11: 0.0803 T22: 0.0786 REMARK 3 T33: 0.0866 T12: -0.0193 REMARK 3 T13: 0.0308 T23: 0.0165 REMARK 3 L TENSOR REMARK 3 L11: 0.0160 L22: 0.0034 REMARK 3 L33: 0.0107 L12: -0.0006 REMARK 3 L13: 0.0058 L23: -0.0033 REMARK 3 S TENSOR REMARK 3 S11: 0.0062 S12: -0.0527 S13: -0.0731 REMARK 3 S21: 0.0418 S22: 0.0043 S23: 0.0428 REMARK 3 S31: 0.0358 S32: -0.0185 S33: 0.0075 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 1 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 61 OR RESID REMARK 3 72 THROUGH 335)) REMARK 3 SELECTION : CHAIN B REMARK 3 ATOM PAIRS NUMBER : 6094 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 61 OR RESID REMARK 3 72 THROUGH 335)) REMARK 3 SELECTION : (CHAIN C AND (RESID 9 THROUGH 61 OR RESID REMARK 3 72 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 6094 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 61 OR RESID REMARK 3 72 THROUGH 335)) REMARK 3 SELECTION : CHAIN D REMARK 3 ATOM PAIRS NUMBER : 6094 REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5PZR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-17. REMARK 100 THE DEPOSITION ID IS D_1001401317. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-MAR-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.987 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115654 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 29.833 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 0.1M AMMONIUM REMARK 280 ACETATE, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.65300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 138.83250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.57400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 138.83250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.65300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.57400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 44220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 ALA A 1 REMARK 465 ASP A 2 REMARK 465 GLN A 3 REMARK 465 ALA A 4 REMARK 465 PRO A 5 REMARK 465 PHE A 6 REMARK 465 ASP A 7 REMARK 465 THR A 8 REMARK 465 SER A 62 REMARK 465 THR A 63 REMARK 465 ASN A 64 REMARK 465 VAL A 65 REMARK 465 THR A 66 REMARK 465 GLY A 67 REMARK 465 ASP A 68 REMARK 465 GLN A 69 REMARK 465 ALA A 336 REMARK 465 GLN A 337 REMARK 465 MET B 0 REMARK 465 ALA B 1 REMARK 465 ASP B 2 REMARK 465 GLN B 3 REMARK 465 ALA B 4 REMARK 465 PRO B 5 REMARK 465 PHE B 6 REMARK 465 ASP B 7 REMARK 465 THR B 8 REMARK 465 SER B 62 REMARK 465 THR B 63 REMARK 465 ASN B 64 REMARK 465 VAL B 65 REMARK 465 THR B 66 REMARK 465 GLY B 67 REMARK 465 ASP B 68 REMARK 465 GLN B 69 REMARK 465 VAL B 70 REMARK 465 LYS B 71 REMARK 465 ALA B 336 REMARK 465 GLN B 337 REMARK 465 MET C 0 REMARK 465 ALA C 1 REMARK 465 ASP C 2 REMARK 465 GLN C 3 REMARK 465 ALA C 4 REMARK 465 PRO C 5 REMARK 465 PHE C 6 REMARK 465 ASP C 7 REMARK 465 THR C 8 REMARK 465 SER C 62 REMARK 465 THR C 63 REMARK 465 ASN C 64 REMARK 465 VAL C 65 REMARK 465 THR C 66 REMARK 465 GLY C 67 REMARK 465 ASP C 68 REMARK 465 GLN C 69 REMARK 465 VAL C 70 REMARK 465 ALA C 336 REMARK 465 GLN C 337 REMARK 465 MET D 0 REMARK 465 ALA D 1 REMARK 465 ASP D 2 REMARK 465 GLN D 3 REMARK 465 ALA D 4 REMARK 465 PRO D 5 REMARK 465 PHE D 6 REMARK 465 ASP D 7 REMARK 465 THR D 8 REMARK 465 SER D 62 REMARK 465 THR D 63 REMARK 465 ASN D 64 REMARK 465 VAL D 65 REMARK 465 THR D 66 REMARK 465 GLY D 67 REMARK 465 ASP D 68 REMARK 465 GLN D 69 REMARK 465 VAL D 70 REMARK 465 LYS D 71 REMARK 465 ALA D 336 REMARK 465 GLN D 337 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH C 421 O HOH D 670 1.87 REMARK 500 O HOH C 461 O HOH C 603 1.89 REMARK 500 O HOH B 604 O HOH B 707 1.91 REMARK 500 O HOH C 636 O HOH C 677 1.92 REMARK 500 N VAL A 70 O HOH A 501 1.93 REMARK 500 O HOH D 403 O HOH D 466 1.94 REMARK 500 OD2 ASP D 309 O HOH D 401 1.94 REMARK 500 O PRO A 188 O HOH A 502 1.95 REMARK 500 O HOH B 747 O HOH C 699 1.95 REMARK 500 O HOH D 659 O HOH D 674 1.96 REMARK 500 O HOH D 497 O HOH D 691 1.96 REMARK 500 O HOH A 628 O HOH A 694 1.96 REMARK 500 O HOH A 755 O HOH A 763 1.97 REMARK 500 O HOH B 711 O HOH B 733 1.98 REMARK 500 O HOH D 431 O HOH D 665 1.99 REMARK 500 O HOH C 658 O HOH C 668 1.99 REMARK 500 O HOH A 634 O HOH A 738 2.00 REMARK 500 O HOH D 564 O HOH D 676 2.00 REMARK 500 O HOH B 780 O HOH B 783 2.00 REMARK 500 NH1 ARG D 140 O HOH D 402 2.00 REMARK 500 O HOH A 720 O HOH D 689 2.01 REMARK 500 O HOH D 671 O HOH D 708 2.01 REMARK 500 O HOH D 661 O HOH D 669 2.01 REMARK 500 O HOH C 686 O HOH C 720 2.02 REMARK 500 O HOH B 745 O HOH B 783 2.02 REMARK 500 O HOH C 449 O HOH C 669 2.03 REMARK 500 OD1 ASP B 220 O HOH B 501 2.04 REMARK 500 O GLY D 61 O HOH D 403 2.04 REMARK 500 O PRO B 271 O HOH B 502 2.04 REMARK 500 O HOH C 426 O HOH C 640 2.06 REMARK 500 O HOH B 695 O HOH B 770 2.06 REMARK 500 O HOH A 548 O HOH A 579 2.06 REMARK 500 O HOH A 746 O HOH D 565 2.08 REMARK 500 O HOH B 772 O HOH B 782 2.09 REMARK 500 O HOH B 746 O HOH D 649 2.09 REMARK 500 NH2 ARG D 157 O HOH D 404 2.10 REMARK 500 O HOH B 551 O HOH B 697 2.10 REMARK 500 O HOH D 623 O HOH D 639 2.10 REMARK 500 O HOH B 725 O HOH B 732 2.10 REMARK 500 O HOH C 565 O HOH C 613 2.11 REMARK 500 O HOH A 505 O HOH A 729 2.12 REMARK 500 O HOH A 538 O HOH A 660 2.12 REMARK 500 O HOH A 743 O HOH A 754 2.12 REMARK 500 O HOH B 651 O HOH B 728 2.13 REMARK 500 O HOH A 504 O HOH A 707 2.13 REMARK 500 O HOH C 461 O HOH C 683 2.14 REMARK 500 O HOH C 564 O HOH C 601 2.15 REMARK 500 O HOH D 497 O HOH D 641 2.15 REMARK 500 O HOH B 632 O HOH B 662 2.16 REMARK 500 O HOH D 681 O HOH D 693 2.17 REMARK 500 REMARK 500 THIS ENTRY HAS 59 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 723 O HOH D 460 1655 1.93 REMARK 500 O HOH B 715 O HOH D 405 1655 2.05 REMARK 500 O HOH B 756 O HOH D 598 1655 2.08 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 GLU A 280 -59.20 -126.66 REMARK 500 PHE B 89 19.10 59.58 REMARK 500 GLU B 280 -59.45 -125.81 REMARK 500 GLU C 280 -59.72 -125.87 REMARK 500 TYR D 215 30.53 -96.51 REMARK 500 ASP D 235 -147.75 -106.11 REMARK 500 GLU D 280 -59.71 -127.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 763 DISTANCE = 6.03 ANGSTROMS REMARK 525 HOH A 764 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH A 765 DISTANCE = 6.96 ANGSTROMS REMARK 525 HOH B 789 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH B 790 DISTANCE = 7.25 ANGSTROMS REMARK 525 HOH C 725 DISTANCE = 5.82 ANGSTROMS REMARK 525 HOH C 726 DISTANCE = 5.99 ANGSTROMS REMARK 525 HOH C 727 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH C 728 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH C 729 DISTANCE = 7.48 ANGSTROMS REMARK 525 HOH C 730 DISTANCE = 7.60 ANGSTROMS REMARK 525 HOH D 719 DISTANCE = 6.72 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 93S A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 93S B 401 DBREF 5PZR A 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5PZR B 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5PZR C 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5PZR D 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 SEQRES 1 A 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 A 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 A 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 A 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 A 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 A 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 A 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 A 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 A 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 A 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 A 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 A 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 A 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 A 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 A 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 A 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 A 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 A 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 A 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 A 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 A 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 A 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 A 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 A 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 A 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 A 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 B 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 B 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 B 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 B 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 B 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 B 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 B 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 B 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 B 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 B 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 B 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 B 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 B 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 B 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 B 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 B 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 B 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 B 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 B 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 B 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 B 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 B 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 B 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 B 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 B 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 B 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 C 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 C 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 C 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 C 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 C 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 C 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 C 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 C 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 C 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 C 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 C 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 C 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 C 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 C 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 C 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 C 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 C 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 C 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 C 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 C 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 C 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 C 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 C 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 C 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 C 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 C 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 D 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 D 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 D 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 D 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 D 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 D 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 D 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 D 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 D 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 D 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 D 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 D 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 D 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 D 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 D 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 D 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 D 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 D 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 D 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 D 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 D 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 D 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 D 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 D 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 D 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 D 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN HET 93S A 401 35 HET 93S B 401 35 HETNAM 93S N,N'-{OXYBIS[(PROPANE-3,1-DIYL)CARBAMOYL]}BIS(3- HETNAM 2 93S CHLOROBENZENE-1-SULFONAMIDE) FORMUL 5 93S 2(C20 H24 CL2 N4 O7 S2) FORMUL 7 HOH *1204(H2 O) HELIX 1 AA1 THR A 12 ARG A 25 1 14 HELIX 2 AA2 GLY A 28 ARG A 49 1 22 HELIX 3 AA3 GLY A 52 TYR A 57 1 6 HELIX 4 AA4 LYS A 72 SER A 87 1 16 HELIX 5 AA5 GLU A 106 GLU A 108 5 3 HELIX 6 AA6 GLY A 122 LEU A 129 5 8 HELIX 7 AA7 SER A 148 LEU A 153 5 6 HELIX 8 AA8 PRO A 155 LEU A 159 5 5 HELIX 9 AA9 ASN A 212 PHE A 219 5 8 HELIX 10 AB1 ASP A 220 PHE A 232 1 13 HELIX 11 AB2 SER A 247 GLY A 259 1 13 HELIX 12 AB3 GLU A 280 ALA A 291 1 12 HELIX 13 AB4 ALA A 301 VAL A 305 5 5 HELIX 14 AB5 SER A 320 HIS A 334 1 15 HELIX 15 AB6 THR B 12 ALA B 24 1 13 HELIX 16 AB7 GLY B 28 ARG B 49 1 22 HELIX 17 AB8 GLY B 52 TYR B 57 1 6 HELIX 18 AB9 LEU B 73 SER B 87 1 15 HELIX 19 AC1 GLU B 106 GLU B 108 5 3 HELIX 20 AC2 GLY B 122 LEU B 129 5 8 HELIX 21 AC3 SER B 148 LEU B 153 5 6 HELIX 22 AC4 PRO B 155 LEU B 159 5 5 HELIX 23 AC5 ASN B 212 PHE B 219 5 8 HELIX 24 AC6 ASP B 220 PHE B 232 1 13 HELIX 25 AC7 SER B 247 GLY B 259 1 13 HELIX 26 AC8 GLU B 280 ALA B 291 1 12 HELIX 27 AC9 ALA B 301 VAL B 305 5 5 HELIX 28 AD1 SER B 320 HIS B 334 1 15 HELIX 29 AD2 THR C 12 ALA C 24 1 13 HELIX 30 AD3 GLY C 28 ARG C 49 1 22 HELIX 31 AD4 GLY C 52 TYR C 57 1 6 HELIX 32 AD5 LYS C 72 SER C 87 1 16 HELIX 33 AD6 GLU C 106 GLU C 108 5 3 HELIX 34 AD7 GLY C 122 LEU C 129 5 8 HELIX 35 AD8 SER C 148 LEU C 153 5 6 HELIX 36 AD9 PRO C 155 LEU C 159 5 5 HELIX 37 AE1 ASN C 212 PHE C 219 5 8 HELIX 38 AE2 ASP C 220 PHE C 232 1 13 HELIX 39 AE3 SER C 247 GLY C 259 1 13 HELIX 40 AE4 GLU C 280 ALA C 291 1 12 HELIX 41 AE5 ALA C 301 VAL C 305 5 5 HELIX 42 AE6 SER C 320 HIS C 334 1 15 HELIX 43 AE7 THR D 12 ARG D 25 1 14 HELIX 44 AE8 GLY D 28 ARG D 49 1 22 HELIX 45 AE9 GLY D 52 TYR D 57 1 6 HELIX 46 AF1 LEU D 73 SER D 87 1 15 HELIX 47 AF2 GLU D 106 GLU D 108 5 3 HELIX 48 AF3 GLY D 122 LEU D 129 5 8 HELIX 49 AF4 SER D 148 LEU D 153 5 6 HELIX 50 AF5 PRO D 155 LEU D 159 5 5 HELIX 51 AF6 ASN D 212 PHE D 219 5 8 HELIX 52 AF7 ASP D 220 PHE D 232 1 13 HELIX 53 AF8 SER D 247 GLY D 259 1 13 HELIX 54 AF9 GLU D 280 ALA D 291 1 12 HELIX 55 AG1 ALA D 301 VAL D 305 5 5 HELIX 56 AG2 SER D 320 HIS D 334 1 15 SHEET 1 AA1 8 ILE A 103 ILE A 104 0 SHEET 2 AA1 8 THR A 91 SER A 96 -1 N LEU A 94 O ILE A 103 SHEET 3 AA1 8 ARG A 110 ASP A 121 1 O VAL A 115 N VAL A 95 SHEET 4 AA1 8 VAL A 132 ARG A 140 -1 O TYR A 139 N VAL A 114 SHEET 5 AA1 8 ALA A 161 TYR A 167 -1 O ALA A 161 N ILE A 138 SHEET 6 AA1 8 THR A 171 MET A 177 -1 O VAL A 174 N TYR A 164 SHEET 7 AA1 8 GLY A 180 LEU A 186 -1 O LEU A 186 N THR A 171 SHEET 8 AA1 8 PHE A 193 ASP A 197 -1 O ILE A 194 N MET A 185 SHEET 1 AA2 5 GLY A 241 ALA A 242 0 SHEET 2 AA2 5 ILE A 208 SER A 210 1 N TYR A 209 O GLY A 241 SHEET 3 AA2 5 ILE A 261 TYR A 264 1 O LEU A 263 N SER A 210 SHEET 4 AA2 5 VAL A 316 GLY A 319 -1 O VAL A 316 N TYR A 264 SHEET 5 AA2 5 MET A 294 THR A 296 -1 N THR A 296 O ILE A 317 SHEET 1 AA3 8 ILE B 103 ILE B 104 0 SHEET 2 AA3 8 THR B 91 SER B 96 -1 N LEU B 94 O ILE B 103 SHEET 3 AA3 8 ARG B 110 ASP B 121 1 O VAL B 115 N VAL B 95 SHEET 4 AA3 8 VAL B 132 ARG B 140 -1 O TYR B 139 N VAL B 114 SHEET 5 AA3 8 ALA B 161 TYR B 167 -1 O TYR B 167 N VAL B 132 SHEET 6 AA3 8 THR B 171 MET B 177 -1 O ALA B 176 N ALA B 162 SHEET 7 AA3 8 GLY B 180 LEU B 186 -1 O LEU B 186 N THR B 171 SHEET 8 AA3 8 PHE B 193 ASP B 197 -1 O ILE B 194 N MET B 185 SHEET 1 AA4 5 GLY B 241 ALA B 242 0 SHEET 2 AA4 5 ILE B 208 SER B 210 1 N TYR B 209 O GLY B 241 SHEET 3 AA4 5 ILE B 261 TYR B 264 1 O LEU B 263 N SER B 210 SHEET 4 AA4 5 VAL B 316 GLY B 319 -1 O VAL B 316 N TYR B 264 SHEET 5 AA4 5 MET B 294 THR B 296 -1 N THR B 296 O ILE B 317 SHEET 1 AA5 8 ILE C 103 ILE C 104 0 SHEET 2 AA5 8 THR C 91 SER C 96 -1 N LEU C 94 O ILE C 103 SHEET 3 AA5 8 ARG C 110 ASP C 121 1 O VAL C 115 N VAL C 95 SHEET 4 AA5 8 VAL C 132 ARG C 140 -1 O TYR C 139 N VAL C 114 SHEET 5 AA5 8 ALA C 161 TYR C 167 -1 O TYR C 167 N VAL C 132 SHEET 6 AA5 8 THR C 171 MET C 177 -1 O VAL C 174 N TYR C 164 SHEET 7 AA5 8 GLY C 180 LEU C 186 -1 O ASN C 182 N LEU C 175 SHEET 8 AA5 8 PHE C 193 ASP C 197 -1 O ILE C 194 N MET C 185 SHEET 1 AA6 5 GLY C 241 ALA C 242 0 SHEET 2 AA6 5 ILE C 208 SER C 210 1 N TYR C 209 O GLY C 241 SHEET 3 AA6 5 ILE C 261 TYR C 264 1 O LEU C 263 N SER C 210 SHEET 4 AA6 5 VAL C 316 GLY C 319 -1 O LEU C 318 N PHE C 262 SHEET 5 AA6 5 MET C 294 THR C 296 -1 N THR C 296 O ILE C 317 SHEET 1 AA7 8 ILE D 103 ILE D 104 0 SHEET 2 AA7 8 THR D 91 SER D 96 -1 N LEU D 94 O ILE D 103 SHEET 3 AA7 8 ARG D 110 ASP D 121 1 O PHE D 117 N VAL D 95 SHEET 4 AA7 8 VAL D 132 ARG D 140 -1 O TYR D 139 N VAL D 114 SHEET 5 AA7 8 ALA D 161 TYR D 167 -1 O ALA D 161 N ILE D 138 SHEET 6 AA7 8 THR D 171 MET D 177 -1 O VAL D 174 N TYR D 164 SHEET 7 AA7 8 GLY D 180 LEU D 186 -1 O PHE D 184 N LEU D 173 SHEET 8 AA7 8 PHE D 193 ASP D 197 -1 O ILE D 194 N MET D 185 SHEET 1 AA8 5 GLY D 241 ALA D 242 0 SHEET 2 AA8 5 ILE D 208 SER D 210 1 N TYR D 209 O GLY D 241 SHEET 3 AA8 5 ILE D 261 TYR D 264 1 O LEU D 263 N SER D 210 SHEET 4 AA8 5 VAL D 316 GLY D 319 -1 O VAL D 316 N TYR D 264 SHEET 5 AA8 5 MET D 294 THR D 296 -1 N THR D 296 O ILE D 317 SITE 1 AC1 24 VAL A 17 MET A 18 GLY A 21 ARG A 22 SITE 2 AC1 24 GLY A 26 THR A 27 GLY A 28 GLU A 29 SITE 3 AC1 24 LEU A 30 THR A 31 MET A 177 HOH A 552 SITE 4 AC1 24 HOH A 562 VAL C 17 MET C 18 GLY C 21 SITE 5 AC1 24 ARG C 22 GLY C 26 THR C 27 GLY C 28 SITE 6 AC1 24 GLU C 29 LEU C 30 THR C 31 MET C 177 SITE 1 AC2 21 VAL B 17 GLY B 21 ARG B 22 GLY B 26 SITE 2 AC2 21 THR B 27 GLY B 28 GLU B 29 LEU B 30 SITE 3 AC2 21 THR B 31 HOH B 532 HOH B 592 VAL D 17 SITE 4 AC2 21 MET D 18 GLY D 21 ARG D 22 GLY D 26 SITE 5 AC2 21 THR D 27 GLY D 28 GLU D 29 LEU D 30 SITE 6 AC2 21 THR D 31 CRYST1 67.306 83.148 277.665 90.00 90.00 90.00 P 21 21 21 16 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 0.014858 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012027 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003601 0.00000 ATOM 1 N ASP A 9 30.581 54.467 37.153 1.00 61.42 N ANISOU 1 N ASP A 9 8622 7266 7451 58 191 -46 N ATOM 2 CA ASP A 9 29.207 53.984 37.268 1.00 58.05 C ANISOU 2 CA ASP A 9 8190 6838 7026 81 199 -42 C ATOM 3 C ASP A 9 28.879 52.958 36.193 1.00 46.54 C ANISOU 3 C ASP A 9 6714 5390 5578 78 197 -42 C ATOM 4 O ASP A 9 29.266 53.118 35.033 1.00 38.72 O ANISOU 4 O ASP A 9 5726 4399 4586 68 192 -42 O ATOM 5 CB ASP A 9 28.215 55.147 37.177 1.00 61.22 C ANISOU 5 CB ASP A 9 8616 7225 7418 107 209 -34 C ATOM 6 CG ASP A 9 27.722 55.605 38.538 1.00 68.40 C ANISOU 6 CG ASP A 9 9536 8130 8323 123 217 -33 C ATOM 7 OD1 ASP A 9 28.197 55.064 39.563 1.00 71.02 O ANISOU 7 OD1 ASP A 9 9857 8468 8658 113 214 -38 O ATOM 8 OD2 ASP A 9 26.853 56.503 38.580 1.00 68.31 O ANISOU 8 OD2 ASP A 9 9542 8107 8304 145 226 -26 O ATOM 9 N VAL A 10 28.136 51.918 36.578 1.00 35.89 N ANISOU 9 N VAL A 10 5349 4050 4237 88 200 -43 N ATOM 10 CA VAL A 10 27.732 50.911 35.609 1.00 32.29 C ANISOU 10 CA VAL A 10 4875 3603 3791 87 199 -44 C ATOM 11 C VAL A 10 26.892 51.565 34.518 1.00 23.41 C ANISOU 11 C VAL A 10 3766 2469 2661 105 204 -36 C ATOM 12 O VAL A 10 26.144 52.522 34.754 1.00 25.66 O ANISOU 12 O VAL A 10 4069 2743 2937 127 213 -28 O ATOM 13 CB VAL A 10 26.970 49.764 36.295 1.00 29.53 C ANISOU 13 CB VAL A 10 4506 3264 3451 98 203 -45 C ATOM 14 CG1 VAL A 10 25.633 50.256 36.834 1.00 33.27 C ANISOU 14 CG1 VAL A 10 4991 3730 3919 131 215 -37 C ATOM 15 CG2 VAL A 10 26.749 48.627 35.325 1.00 20.76 C ANISOU 15 CG2 VAL A 10 3374 2163 2350 93 200 -48 C ATOM 16 N ASN A 11 27.052 51.082 33.301 1.00 17.12 N ANISOU 16 N ASN A 11 2959 1676 1868 95 199 -37 N ATOM 17 CA ASN A 11 26.299 51.617 32.185 1.00 20.61 C ANISOU 17 CA ASN A 11 3414 2111 2307 111 204 -28 C ATOM 18 C ASN A 11 25.845 50.441 31.344 1.00 21.20 C ANISOU 18 C ASN A 11 3468 2195 2392 111 203 -29 C ATOM 19 O ASN A 11 26.647 49.561 31.016 1.00 31.68 O ANISOU 19 O ASN A 11 4777 3534 3727 87 194 -38 O ATOM 20 CB ASN A 11 27.154 52.595 31.366 1.00 30.25 C ANISOU 20 CB ASN A 11 4651 3323 3520 96 197 -27 C ATOM 21 CG ASN A 11 26.332 53.682 30.704 1.00 37.61 C ANISOU 21 CG ASN A 11 5603 4241 4444 118 205 -17 C ATOM 22 OD1 ASN A 11 25.103 53.692 30.791 1.00 40.88 O ANISOU 22 OD1 ASN A 11 6019 4653 4859 146 214 -9 O ATOM 23 ND2 ASN A 11 27.013 54.621 30.055 1.00 40.97 N ANISOU 23 ND2 ASN A 11 6045 4659 4863 107 200 -15 N ATOM 24 N THR A 12 24.567 50.437 30.995 1.00 19.07 N ANISOU 24 N THR A 12 3199 1924 2124 139 212 -20 N ATOM 25 CA THR A 12 23.985 49.411 30.151 1.00 23.75 C ANISOU 25 CA THR A 12 3773 2524 2725 144 212 -19 C ATOM 26 C THR A 12 23.702 50.002 28.781 1.00 24.99 C ANISOU 26 C THR A 12 3943 2674 2880 150 212 -10 C ATOM 27 O THR A 12 23.666 51.224 28.602 1.00 19.61 O ANISOU 27 O THR A 12 3282 1980 2188 158 214 -2 O ATOM 28 CB THR A 12 22.696 48.854 30.752 1.00 19.73 C ANISOU 28 CB THR A 12 3252 2022 2222 173 223 -14 C ATOM 29 OG1 THR A 12 21.707 49.889 30.768 1.00 22.74 O ANISOU 29 OG1 THR A 12 3650 2393 2595 203 232 0 O ATOM 30 CG2 THR A 12 22.921 48.323 32.174 1.00 18.31 C ANISOU 30 CG2 THR A 12 3062 1849 2044 168 223 -22 C ATOM 31 N LEU A 13 23.498 49.114 27.810 1.00 22.45 N ANISOU 31 N LEU A 13 3592 2373 2566 143 207 -8 N ATOM 32 CA LEU A 13 23.190 49.580 26.466 1.00 18.69 C ANISOU 32 CA LEU A 13 3109 1905 2087 146 204 4 C ATOM 33 C LEU A 13 21.987 50.515 26.471 1.00 24.57 C ANISOU 33 C LEU A 13 3868 2642 2826 180 214 20 C ATOM 34 O LEU A 13 22.044 51.614 25.907 1.00 18.44 O ANISOU 34 O LEU A 13 3114 1850 2041 184 215 28 O ATOM 35 CB LEU A 13 22.944 48.383 25.562 1.00 12.79 C ANISOU 35 CB LEU A 13 2319 1191 1350 136 197 5 C ATOM 36 CG LEU A 13 22.835 48.581 24.055 1.00 22.61 C ANISOU 36 CG LEU A 13 3550 2449 2594 130 190 14 C ATOM 37 CD1 LEU A 13 23.570 49.804 23.584 1.00 24.65 C ANISOU 37 CD1 LEU A 13 3840 2684 2841 121 188 16 C ATOM 38 CD2 LEU A 13 23.487 47.371 23.462 1.00 39.03 C ANISOU 38 CD2 LEU A 13 5596 4551 4682 102 180 4 C ATOM 39 N THR A 14 20.906 50.109 27.151 1.00 31.91 N ANISOU 39 N THR A 14 4785 3580 3760 205 223 25 N ATOM 40 CA THR A 14 19.691 50.923 27.213 1.00 33.64 C ANISOU 40 CA THR A 14 5015 3791 3974 239 233 41 C ATOM 41 C THR A 14 19.977 52.297 27.809 1.00 31.81 C ANISOU 41 C THR A 14 4828 3526 3731 248 240 41 C ATOM 42 O THR A 14 19.587 53.323 27.242 1.00 32.30 O ANISOU 42 O THR A 14 4908 3579 3788 261 243 54 O ATOM 43 CB THR A 14 18.593 50.213 28.018 1.00 36.55 C ANISOU 43 CB THR A 14 5364 4173 4349 263 241 44 C ATOM 44 OG1 THR A 14 18.898 50.277 29.416 1.00 51.00 O ANISOU 44 OG1 THR A 14 7215 5986 6177 265 247 34 O ATOM 45 CG2 THR A 14 18.458 48.744 27.603 1.00 25.44 C ANISOU 45 CG2 THR A 14 3914 2799 2954 251 235 41 C ATOM 46 N ARG A 15 20.670 52.339 28.952 1.00 20.19 N ANISOU 46 N ARG A 15 3367 2047 2257 236 239 29 N ATOM 47 CA ARG A 15 20.978 53.628 29.574 1.00 30.29 C ANISOU 47 CA ARG A 15 4670 3315 3525 236 241 28 C ATOM 48 C ARG A 15 21.870 54.480 28.679 1.00 29.85 C ANISOU 48 C ARG A 15 4630 3248 3462 218 234 28 C ATOM 49 O ARG A 15 21.667 55.694 28.553 1.00 27.33 O ANISOU 49 O ARG A 15 4330 2918 3135 228 237 36 O ATOM 50 CB ARG A 15 21.649 53.399 30.927 1.00 34.21 C ANISOU 50 CB ARG A 15 5164 3813 4020 222 239 16 C ATOM 51 CG ARG A 15 22.147 54.654 31.620 1.00 38.93 C ANISOU 51 CG ARG A 15 5785 4398 4607 219 240 14 C ATOM 52 CD ARG A 15 22.832 54.294 32.934 1.00 41.68 C ANISOU 52 CD ARG A 15 6129 4751 4956 205 237 4 C ATOM 53 NE ARG A 15 21.840 54.053 33.978 1.00 40.80 N ANISOU 53 NE ARG A 15 6012 4644 4846 227 246 7 N ATOM 54 CZ ARG A 15 22.088 53.469 35.146 1.00 42.83 C ANISOU 54 CZ ARG A 15 6259 4907 5106 221 245 0 C ATOM 55 NH1 ARG A 15 23.307 53.040 35.434 1.00 45.38 N ANISOU 55 NH1 ARG A 15 6576 5233 5431 193 236 -11 N ATOM 56 NH2 ARG A 15 21.109 53.314 36.029 1.00 38.47 N ANISOU 56 NH2 ARG A 15 5703 4359 4554 243 254 4 N ATOM 57 N PHE A 16 22.852 53.851 28.035 1.00 21.12 N ANISOU 57 N PHE A 16 3517 2146 2361 190 224 20 N ATOM 58 CA PHE A 16 23.782 54.563 27.164 1.00 16.14 C ANISOU 58 CA PHE A 16 2899 1507 1725 170 216 19 C ATOM 59 C PHE A 16 23.054 55.257 26.020 1.00 25.05 C ANISOU 59 C PHE A 16 4038 2630 2851 187 219 35 C ATOM 60 O PHE A 16 23.312 56.431 25.728 1.00 23.69 O ANISOU 60 O PHE A 16 3885 2447 2671 187 219 39 O ATOM 61 CB PHE A 16 24.829 53.579 26.634 1.00 22.78 C ANISOU 61 CB PHE A 16 3726 2358 2573 138 205 8 C ATOM 62 CG PHE A 16 25.774 54.165 25.626 1.00 21.03 C ANISOU 62 CG PHE A 16 3514 2130 2346 116 196 7 C ATOM 63 CD1 PHE A 16 25.516 54.052 24.263 1.00 28.07 C ANISOU 63 CD1 PHE A 16 4404 3022 3240 116 194 16 C ATOM 64 CD2 PHE A 16 26.944 54.777 26.032 1.00 22.21 C ANISOU 64 CD2 PHE A 16 3673 2276 2488 95 190 -1 C ATOM 65 CE1 PHE A 16 26.392 54.573 23.332 1.00 23.87 C ANISOU 65 CE1 PHE A 16 3881 2486 2704 95 185 16 C ATOM 66 CE2 PHE A 16 27.827 55.303 25.104 1.00 17.44 C ANISOU 66 CE2 PHE A 16 3076 1669 1880 75 182 -2 C ATOM 67 CZ PHE A 16 27.543 55.212 23.754 1.00 17.74 C ANISOU 67 CZ PHE A 16 3114 1706 1920 74 179 7 C ATOM 68 N VAL A 17 22.156 54.541 25.338 1.00 25.27 N ANISOU 68 N VAL A 17 4049 2666 2886 202 222 46 N ATOM 69 CA VAL A 17 21.514 55.129 24.164 1.00 29.72 C ANISOU 69 CA VAL A 17 4609 3237 3447 214 222 62 C ATOM 70 C VAL A 17 20.535 56.232 24.566 1.00 28.18 C ANISOU 70 C VAL A 17 4436 3025 3245 247 234 75 C ATOM 71 O VAL A 17 20.423 57.256 23.875 1.00 30.34 O ANISOU 71 O VAL A 17 4723 3292 3514 252 234 85 O ATOM 72 CB VAL A 17 20.839 54.039 23.305 1.00 22.62 C ANISOU 72 CB VAL A 17 3665 2373 2556 214 218 68 C ATOM 73 CG1 VAL A 17 21.892 53.077 22.750 1.00 22.32 C ANISOU 73 CG1 VAL A 17 3605 2351 2523 179 205 55 C ATOM 74 CG2 VAL A 17 19.770 53.292 24.094 1.00 25.50 C ANISOU 74 CG2 VAL A 17 4011 2751 2928 237 225 70 C ATOM 75 N MET A 18 19.816 56.053 25.683 1.00 24.67 N ANISOU 75 N MET A 18 3986 2584 2802 266 242 73 N ATOM 76 CA MET A 18 18.951 57.121 26.185 1.00 23.71 C ANISOU 76 CA MET A 18 3877 2456 2674 292 251 81 C ATOM 77 C MET A 18 19.744 58.403 26.422 1.00 30.65 C ANISOU 77 C MET A 18 4781 3320 3544 280 249 76 C ATOM 78 O MET A 18 19.287 59.507 26.096 1.00 23.25 O ANISOU 78 O MET A 18 3857 2375 2601 295 253 86 O ATOM 79 CB MET A 18 18.278 56.694 27.492 1.00 27.80 C ANISOU 79 CB MET A 18 4387 2981 3195 308 259 77 C ATOM 80 CG MET A 18 17.074 55.775 27.372 1.00 28.53 C ANISOU 80 CG MET A 18 4456 3089 3295 331 265 87 C ATOM 81 SD MET A 18 15.622 56.544 26.640 1.00 44.00 S ANISOU 81 SD MET A 18 6414 5052 5253 365 273 110 S ATOM 82 CE MET A 18 15.004 57.567 27.977 1.00 30.68 C ANISOU 82 CE MET A 18 4742 3358 3559 385 283 108 C ATOM 83 N GLU A 19 20.935 58.272 26.997 1.00 28.20 N ANISOU 83 N GLU A 19 4477 3007 3232 254 243 60 N ATOM 84 CA GLU A 19 21.725 59.444 27.333 1.00 28.05 C ANISOU 84 CA GLU A 19 4479 2974 3203 243 241 55 C ATOM 85 C GLU A 19 22.349 60.068 26.092 1.00 33.56 C ANISOU 85 C GLU A 19 5187 3665 3898 229 234 59 C ATOM 86 O GLU A 19 22.429 61.297 25.986 1.00 37.02 O ANISOU 86 O GLU A 19 5644 4092 4330 233 235 62 O ATOM 87 CB GLU A 19 22.767 59.053 28.377 1.00 33.05 C ANISOU 87 CB GLU A 19 5112 3610 3836 221 236 39 C ATOM 88 CG GLU A 19 22.098 58.705 29.713 1.00 48.41 C ANISOU 88 CG GLU A 19 7051 5559 5782 237 244 37 C ATOM 89 CD GLU A 19 23.027 58.047 30.717 1.00 66.10 C ANISOU 89 CD GLU A 19 9284 7806 8024 215 238 23 C ATOM 90 OE1 GLU A 19 24.101 57.549 30.310 1.00 72.16 O ANISOU 90 OE1 GLU A 19 10046 8578 8795 188 228 15 O ATOM 91 OE2 GLU A 19 22.669 58.017 31.917 1.00 69.70 O ANISOU 91 OE2 GLU A 19 9740 8264 8480 225 244 21 O ATOM 92 N GLU A 20 22.778 59.247 25.131 1.00 31.51 N ANISOU 92 N GLU A 20 4915 3413 3644 212 226 58 N ATOM 93 CA GLU A 20 23.227 59.801 23.858 1.00 34.43 C ANISOU 93 CA GLU A 20 5292 3778 4012 201 220 65 C ATOM 94 C GLU A 20 22.077 60.516 23.156 1.00 34.58 C ANISOU 94 C GLU A 20 5316 3795 4030 228 226 83 C ATOM 95 O GLU A 20 22.274 61.555 22.515 1.00 30.15 O ANISOU 95 O GLU A 20 4769 3225 3463 227 225 90 O ATOM 96 CB GLU A 20 23.797 58.693 22.971 1.00 32.76 C ANISOU 96 CB GLU A 20 5064 3576 3806 178 210 62 C ATOM 97 CG GLU A 20 25.142 58.152 23.449 1.00 41.24 C ANISOU 97 CG GLU A 20 6135 4653 4881 146 202 43 C ATOM 98 CD GLU A 20 26.245 59.202 23.474 1.00 50.92 C ANISOU 98 CD GLU A 20 7379 5870 6099 128 196 37 C ATOM 99 OE1 GLU A 20 26.352 59.980 22.500 1.00 53.41 O ANISOU 99 OE1 GLU A 20 7705 6179 6411 127 193 45 O ATOM 100 OE2 GLU A 20 26.992 59.259 24.480 1.00 52.25 O ANISOU 100 OE2 GLU A 20 7550 6039 6265 116 194 25 O ATOM 101 N GLY A 21 20.860 59.984 23.294 1.00 29.20 N ANISOU 101 N GLY A 21 4620 3122 3352 253 234 93 N ATOM 102 CA GLY A 21 19.711 60.620 22.673 1.00 26.18 C ANISOU 102 CA GLY A 21 4237 2741 2969 280 240 112 C ATOM 103 C GLY A 21 19.325 61.937 23.322 1.00 31.49 C ANISOU 103 C GLY A 21 4929 3401 3635 297 248 113 C ATOM 104 O GLY A 21 18.987 62.901 22.632 1.00 22.16 O ANISOU 104 O GLY A 21 3756 2214 2450 307 250 125 O ATOM 105 N ARG A 22 19.366 62.001 24.656 1.00 33.88 N ANISOU 105 N ARG A 22 5237 3700 3936 300 253 102 N ATOM 106 CA ARG A 22 19.053 63.259 25.323 1.00 42.37 C ANISOU 106 CA ARG A 22 6331 4763 5004 315 260 103 C ATOM 107 C ARG A 22 20.082 64.326 24.969 1.00 38.22 C ANISOU 107 C ARG A 22 5827 4224 4473 296 254 99 C ATOM 108 O ARG A 22 19.729 65.492 24.769 1.00 40.49 O ANISOU 108 O ARG A 22 6128 4501 4755 309 258 107 O ATOM 109 CB ARG A 22 18.964 63.056 26.839 1.00 55.18 C ANISOU 109 CB ARG A 22 7955 6385 6625 319 265 93 C ATOM 110 CG ARG A 22 17.791 62.162 27.260 1.00 66.27 C ANISOU 110 CG ARG A 22 9340 7804 8036 341 273 98 C ATOM 111 CD ARG A 22 17.522 62.152 28.769 1.00 72.33 C ANISOU 111 CD ARG A 22 10111 8572 8801 350 279 91 C ATOM 112 NE ARG A 22 16.836 63.363 29.220 1.00 78.32 N ANISOU 112 NE ARG A 22 10885 9321 9553 370 288 97 N ATOM 113 CZ ARG A 22 16.558 63.641 30.492 1.00 86.47 C ANISOU 113 CZ ARG A 22 11923 10350 10581 379 295 92 C ATOM 114 NH1 ARG A 22 16.906 62.796 31.453 1.00 88.22 N ANISOU 114 NH1 ARG A 22 12136 10578 10804 370 293 82 N ATOM 115 NH2 ARG A 22 15.928 64.765 30.808 1.00 89.04 N ANISOU 115 NH2 ARG A 22 12263 10667 10902 398 302 98 N ATOM 116 N LYS A 23 21.355 63.935 24.847 1.00 38.31 N ANISOU 116 N LYS A 23 5838 4234 4482 267 244 87 N ATOM 117 CA LYS A 23 22.378 64.865 24.373 1.00 41.55 C ANISOU 117 CA LYS A 23 6266 4634 4888 248 238 84 C ATOM 118 C LYS A 23 22.013 65.437 23.009 1.00 45.08 C ANISOU 118 C LYS A 23 6715 5079 5336 254 236 99 C ATOM 119 O LYS A 23 22.145 66.646 22.774 1.00 51.14 O ANISOU 119 O LYS A 23 7499 5834 6097 257 237 102 O ATOM 120 CB LYS A 23 23.734 64.162 24.292 1.00 41.19 C ANISOU 120 CB LYS A 23 6215 4592 4843 214 227 70 C ATOM 121 CG LYS A 23 24.417 63.921 25.619 1.00 45.64 C ANISOU 121 CG LYS A 23 6780 5156 5404 203 226 55 C ATOM 122 CD LYS A 23 25.773 63.260 25.391 1.00 58.96 C ANISOU 122 CD LYS A 23 8460 6850 7093 169 214 43 C ATOM 123 CE LYS A 23 26.393 62.782 26.697 1.00 66.13 C ANISOU 123 CE LYS A 23 9364 7762 8000 158 213 30 C ATOM 124 NZ LYS A 23 25.685 61.593 27.253 1.00 69.30 N ANISOU 124 NZ LYS A 23 9747 8175 8409 168 217 29 N ATOM 125 N ALA A 24 21.546 64.585 22.100 1.00 38.46 N ANISOU 125 N ALA A 24 5859 4252 4503 257 234 108 N ATOM 126 CA ALA A 24 21.216 65.014 20.752 1.00 35.81 C ANISOU 126 CA ALA A 24 5521 3917 4167 262 232 124 C ATOM 127 C ALA A 24 19.822 65.617 20.657 1.00 34.14 C ANISOU 127 C ALA A 24 5309 3706 3956 295 242 140 C ATOM 128 O ALA A 24 19.429 66.054 19.570 1.00 28.94 O ANISOU 128 O ALA A 24 4649 3050 3297 301 241 155 O ATOM 129 CB ALA A 24 21.343 63.833 19.786 1.00 40.14 C ANISOU 129 CB ALA A 24 6050 4481 4721 249 225 129 C ATOM 130 N ARG A 25 19.082 65.660 21.767 1.00 31.25 N ANISOU 130 N ARG A 25 4944 3340 3591 315 251 138 N ATOM 131 CA ARG A 25 17.718 66.188 21.798 1.00 41.90 C ANISOU 131 CA ARG A 25 6291 4691 4940 346 261 152 C ATOM 132 C ARG A 25 16.807 65.401 20.858 1.00 37.00 C ANISOU 132 C ARG A 25 5646 4087 4324 359 262 168 C ATOM 133 O ARG A 25 15.928 65.964 20.205 1.00 35.94 O ANISOU 133 O ARG A 25 5510 3957 4190 378 266 183 O ATOM 134 CB ARG A 25 17.698 67.686 21.469 1.00 53.16 C ANISOU 134 CB ARG A 25 7736 6102 6360 352 264 158 C ATOM 135 CG ARG A 25 18.544 68.527 22.419 1.00 60.62 C ANISOU 135 CG ARG A 25 8704 7031 7300 341 264 144 C ATOM 136 CD ARG A 25 18.446 70.018 22.128 1.00 67.53 C ANISOU 136 CD ARG A 25 9598 7891 8170 349 266 151 C ATOM 137 NE ARG A 25 17.193 70.592 22.612 1.00 74.30 N ANISOU 137 NE ARG A 25 10456 8747 9027 379 278 160 N ATOM 138 CZ ARG A 25 16.193 70.981 21.827 1.00 75.94 C ANISOU 138 CZ ARG A 25 10657 8958 9237 399 282 177 C ATOM 139 NH1 ARG A 25 16.297 70.865 20.509 1.00 74.59 N ANISOU 139 NH1 ARG A 25 10479 8794 9069 392 276 187 N ATOM 140 NH2 ARG A 25 15.089 71.490 22.360 1.00 76.61 N ANISOU 140 NH2 ARG A 25 10744 9043 9322 425 292 183 N ATOM 141 N GLY A 26 17.043 64.077 20.763 1.00 31.44 N ANISOU 141 N GLY A 26 4925 3396 3625 348 257 164 N ATOM 142 CA GLY A 26 16.253 63.243 19.882 1.00 24.19 C ANISOU 142 CA GLY A 26 3984 2497 2712 359 256 178 C ATOM 143 C GLY A 26 14.907 62.842 20.474 1.00 28.78 C ANISOU 143 C GLY A 26 4549 3089 3296 388 266 185 C ATOM 144 O GLY A 26 14.675 62.912 21.682 1.00 26.08 O ANISOU 144 O GLY A 26 4212 2742 2954 397 273 176 O ATOM 145 N THR A 27 14.018 62.372 19.597 1.00 20.54 N ANISOU 145 N THR A 27 3485 2063 2256 402 267 202 N ATOM 146 CA THR A 27 12.679 61.969 20.012 1.00 34.75 C ANISOU 146 CA THR A 27 5267 3877 4061 431 276 210 C ATOM 147 C THR A 27 12.628 60.570 20.610 1.00 33.43 C ANISOU 147 C THR A 27 5081 3721 3899 429 276 203 C ATOM 148 O THR A 27 11.550 60.155 21.052 1.00 26.76 O ANISOU 148 O THR A 27 4221 2889 3058 451 283 208 O ATOM 149 CB THR A 27 11.692 62.016 18.838 1.00 42.06 C ANISOU 149 CB THR A 27 6174 4818 4987 448 277 232 C ATOM 150 OG1 THR A 27 12.037 61.005 17.875 1.00 50.25 O ANISOU 150 OG1 THR A 27 7194 5872 6026 433 268 237 O ATOM 151 CG2 THR A 27 11.701 63.377 18.174 1.00 44.38 C ANISOU 151 CG2 THR A 27 6485 5101 5275 450 277 240 C ATOM 152 N GLY A 28 13.736 59.823 20.594 1.00 30.35 N ANISOU 152 N GLY A 28 4692 3330 3510 402 267 191 N ATOM 153 CA GLY A 28 13.766 58.477 21.129 1.00 27.07 C ANISOU 153 CA GLY A 28 4251 2931 3102 395 265 180 C ATOM 154 C GLY A 28 13.522 57.362 20.132 1.00 25.37 C ANISOU 154 C GLY A 28 3994 2752 2894 384 257 183 C ATOM 155 O GLY A 28 13.573 56.184 20.520 1.00 18.68 O ANISOU 155 O GLY A 28 3122 1922 2054 375 255 172 O ATOM 156 N GLU A 29 13.248 57.685 18.867 1.00 20.19 N ANISOU 156 N GLU A 29 3328 2108 2236 384 253 196 N ATOM 157 CA GLU A 29 12.886 56.650 17.900 1.00 23.04 C ANISOU 157 CA GLU A 29 3647 2503 2603 377 247 199 C ATOM 158 C GLU A 29 14.050 55.704 17.627 1.00 24.18 C ANISOU 158 C GLU A 29 3776 2660 2753 341 235 183 C ATOM 159 O GLU A 29 13.865 54.482 17.559 1.00 18.14 O ANISOU 159 O GLU A 29 2978 1921 1996 334 231 177 O ATOM 160 CB GLU A 29 12.416 57.298 16.600 1.00 25.07 C ANISOU 160 CB GLU A 29 3901 2769 2857 384 245 217 C ATOM 161 CG GLU A 29 11.855 56.325 15.579 1.00 31.50 C ANISOU 161 CG GLU A 29 4672 3619 3677 380 239 223 C ATOM 162 CD GLU A 29 11.139 57.031 14.434 1.00 36.13 C ANISOU 162 CD GLU A 29 5255 4213 4259 394 240 244 C ATOM 163 OE1 GLU A 29 10.968 58.269 14.500 1.00 45.80 O ANISOU 163 OE1 GLU A 29 6510 5415 5478 409 246 254 O ATOM 164 OE2 GLU A 29 10.735 56.347 13.474 1.00 31.12 O ANISOU 164 OE2 GLU A 29 4587 3607 3628 390 234 249 O ATOM 165 N LEU A 30 15.262 56.243 17.478 1.00 19.26 N ANISOU 165 N LEU A 30 3175 2019 2123 318 229 174 N ATOM 166 CA LEU A 30 16.411 55.374 17.262 1.00 25.48 C ANISOU 166 CA LEU A 30 3949 2817 2915 283 218 158 C ATOM 167 C LEU A 30 16.693 54.510 18.492 1.00 21.31 C ANISOU 167 C LEU A 30 3416 2287 2393 278 219 142 C ATOM 168 O LEU A 30 17.074 53.341 18.361 1.00 20.60 O ANISOU 168 O LEU A 30 3298 2217 2310 259 212 131 O ATOM 169 CB LEU A 30 17.635 56.206 16.892 1.00 21.70 C ANISOU 169 CB LEU A 30 3498 2318 2430 261 211 153 C ATOM 170 CG LEU A 30 18.935 55.418 16.710 1.00 23.20 C ANISOU 170 CG LEU A 30 3677 2515 2622 224 200 136 C ATOM 171 CD1 LEU A 30 18.774 54.345 15.625 1.00 23.09 C ANISOU 171 CD1 LEU A 30 3621 2536 2615 212 191 137 C ATOM 172 CD2 LEU A 30 20.089 56.340 16.379 1.00 22.25 C ANISOU 172 CD2 LEU A 30 3587 2373 2495 204 194 132 C ATOM 173 N THR A 31 16.500 55.060 19.693 1.00 24.99 N ANISOU 173 N THR A 31 3910 2730 2856 295 229 140 N ATOM 174 CA THR A 31 16.632 54.257 20.911 1.00 24.31 C ANISOU 174 CA THR A 31 3819 2643 2775 294 231 126 C ATOM 175 C THR A 31 15.629 53.106 20.938 1.00 23.29 C ANISOU 175 C THR A 31 3652 2543 2655 306 233 130 C ATOM 176 O THR A 31 15.967 51.990 21.358 1.00 21.64 O ANISOU 176 O THR A 31 3422 2347 2454 292 229 117 O ATOM 177 CB THR A 31 16.478 55.153 22.145 1.00 24.09 C ANISOU 177 CB THR A 31 3827 2585 2742 313 242 126 C ATOM 178 OG1 THR A 31 17.695 55.887 22.348 1.00 18.59 O ANISOU 178 OG1 THR A 31 3162 1862 2038 293 238 116 O ATOM 179 CG2 THR A 31 16.130 54.332 23.415 1.00 15.05 C ANISOU 179 CG2 THR A 31 2672 1443 1601 322 248 117 C ATOM 180 N GLN A 32 14.393 53.352 20.497 1.00 19.62 N ANISOU 180 N GLN A 32 3177 2089 2191 333 239 147 N ATOM 181 CA GLN A 32 13.422 52.262 20.408 1.00 20.60 C ANISOU 181 CA GLN A 32 3263 2242 2324 344 240 151 C ATOM 182 C GLN A 32 13.872 51.186 19.432 1.00 18.52 C ANISOU 182 C GLN A 32 2965 2007 2067 319 229 145 C ATOM 183 O GLN A 32 13.713 49.992 19.701 1.00 16.85 O ANISOU 183 O GLN A 32 2724 1815 1864 314 227 138 O ATOM 184 CB GLN A 32 12.047 52.780 19.993 1.00 20.38 C ANISOU 184 CB GLN A 32 3230 2220 2294 376 248 171 C ATOM 185 CG GLN A 32 11.385 53.601 21.039 1.00 36.50 C ANISOU 185 CG GLN A 32 5299 4239 4330 405 261 177 C ATOM 186 CD GLN A 32 9.889 53.600 20.889 1.00 52.29 C ANISOU 186 CD GLN A 32 7282 6252 6332 437 269 193 C ATOM 187 OE1 GLN A 32 9.313 54.441 20.201 1.00 58.11 O ANISOU 187 OE1 GLN A 32 8028 6987 7065 452 272 209 O ATOM 188 NE2 GLN A 32 9.243 52.647 21.548 1.00 60.52 N ANISOU 188 NE2 GLN A 32 8303 7310 7382 448 273 191 N ATOM 189 N LEU A 33 14.384 51.588 18.268 1.00 17.82 N ANISOU 189 N LEU A 33 2876 1920 1973 303 221 148 N ATOM 190 CA LEU A 33 14.951 50.614 17.344 1.00 22.23 C ANISOU 190 CA LEU A 33 3404 2504 2539 276 209 141 C ATOM 191 C LEU A 33 16.038 49.792 18.024 1.00 18.73 C ANISOU 191 C LEU A 33 2958 2059 2100 250 204 121 C ATOM 192 O LEU A 33 16.004 48.555 17.989 1.00 12.92 O ANISOU 192 O LEU A 33 2189 1345 1373 240 199 113 O ATOM 193 CB LEU A 33 15.509 51.320 16.099 1.00 20.76 C ANISOU 193 CB LEU A 33 3226 2317 2346 261 202 147 C ATOM 194 CG LEU A 33 15.877 50.494 14.852 1.00 16.07 C ANISOU 194 CG LEU A 33 2599 1752 1757 237 191 144 C ATOM 195 CD1 LEU A 33 15.994 51.442 13.625 1.00 13.73 C ANISOU 195 CD1 LEU A 33 2313 1453 1452 234 187 157 C ATOM 196 CD2 LEU A 33 17.184 49.712 15.001 1.00 23.22 C ANISOU 196 CD2 LEU A 33 3498 2658 2666 203 181 124 C ATOM 197 N LEU A 34 17.009 50.466 18.656 1.00 15.02 N ANISOU 197 N LEU A 34 2522 1561 1624 238 204 112 N ATOM 198 CA LEU A 34 18.152 49.760 19.230 1.00 13.47 C ANISOU 198 CA LEU A 34 2325 1362 1432 211 198 93 C ATOM 199 C LEU A 34 17.730 48.861 20.389 1.00 11.36 C ANISOU 199 C LEU A 34 2044 1099 1172 221 203 85 C ATOM 200 O LEU A 34 18.275 47.759 20.558 1.00 14.86 O ANISOU 200 O LEU A 34 2465 1556 1624 201 197 72 O ATOM 201 CB LEU A 34 19.212 50.763 19.688 1.00 14.22 C ANISOU 201 CB LEU A 34 2460 1425 1519 199 197 86 C ATOM 202 CG LEU A 34 19.910 51.518 18.551 1.00 15.41 C ANISOU 202 CG LEU A 34 2623 1571 1663 183 190 89 C ATOM 203 CD1 LEU A 34 20.832 52.592 19.092 1.00 17.09 C ANISOU 203 CD1 LEU A 34 2877 1749 1866 175 191 84 C ATOM 204 CD2 LEU A 34 20.684 50.567 17.646 1.00 17.32 C ANISOU 204 CD2 LEU A 34 2836 1834 1909 152 178 80 C ATOM 205 N ASN A 35 16.765 49.310 21.196 1.00 20.09 N ANISOU 205 N ASN A 35 3162 2195 2276 251 214 94 N ATOM 206 CA ASN A 35 16.212 48.452 22.238 1.00 15.91 C ANISOU 206 CA ASN A 35 2618 1674 1754 263 219 89 C ATOM 207 C ASN A 35 15.600 47.196 21.639 1.00 13.61 C ANISOU 207 C ASN A 35 2281 1416 1473 262 215 91 C ATOM 208 O ASN A 35 15.823 46.087 22.134 1.00 15.65 O ANISOU 208 O ASN A 35 2518 1687 1740 251 213 80 O ATOM 209 CB ASN A 35 15.154 49.191 23.056 1.00 13.96 C ANISOU 209 CB ASN A 35 2390 1413 1503 298 233 100 C ATOM 210 CG ASN A 35 15.733 50.244 23.972 1.00 26.57 C ANISOU 210 CG ASN A 35 4030 2975 3090 300 238 95 C ATOM 211 OD1 ASN A 35 16.928 50.237 24.286 1.00 32.19 O ANISOU 211 OD1 ASN A 35 4755 3674 3800 276 232 81 O ATOM 212 ND2 ASN A 35 14.864 51.143 24.451 1.00 22.54 N ANISOU 212 ND2 ASN A 35 3540 2449 2574 330 249 106 N ATOM 213 N SER A 36 14.784 47.356 20.593 1.00 13.53 N ANISOU 213 N SER A 36 2256 1423 1463 274 215 106 N ATOM 214 CA SER A 36 14.175 46.185 19.969 1.00 17.09 C ANISOU 214 CA SER A 36 2664 1907 1924 273 211 108 C ATOM 215 C SER A 36 15.239 45.260 19.407 1.00 12.01 C ANISOU 215 C SER A 36 1999 1278 1287 238 199 94 C ATOM 216 O SER A 36 15.140 44.030 19.523 1.00 12.31 O ANISOU 216 O SER A 36 2006 1337 1336 230 196 86 O ATOM 217 CB SER A 36 13.205 46.616 18.870 1.00 21.95 C ANISOU 217 CB SER A 36 3268 2535 2536 290 213 126 C ATOM 218 OG SER A 36 12.136 47.367 19.422 1.00 27.73 O ANISOU 218 OG SER A 36 4016 3256 3264 324 225 139 O ATOM 219 N LEU A 37 16.277 45.840 18.808 1.00 13.66 N ANISOU 219 N LEU A 37 2225 1475 1489 216 192 89 N ATOM 220 CA LEU A 37 17.360 45.034 18.263 1.00 20.22 C ANISOU 220 CA LEU A 37 3039 2319 2326 182 181 75 C ATOM 221 C LEU A 37 18.076 44.261 19.366 1.00 14.91 C ANISOU 221 C LEU A 37 2365 1640 1659 168 179 58 C ATOM 222 O LEU A 37 18.409 43.084 19.194 1.00 16.76 O ANISOU 222 O LEU A 37 2571 1895 1904 150 173 48 O ATOM 223 CB LEU A 37 18.322 45.937 17.499 1.00 11.44 C ANISOU 223 CB LEU A 37 1950 1193 1204 164 174 75 C ATOM 224 CG LEU A 37 19.412 45.272 16.677 1.00 20.10 C ANISOU 224 CG LEU A 37 3029 2303 2305 129 162 63 C ATOM 225 CD1 LEU A 37 18.824 44.235 15.711 1.00 17.77 C ANISOU 225 CD1 LEU A 37 2691 2043 2019 126 157 66 C ATOM 226 CD2 LEU A 37 20.181 46.366 15.929 1.00 19.93 C ANISOU 226 CD2 LEU A 37 3034 2266 2273 116 158 66 C ATOM 227 N CYS A 38 18.283 44.895 20.521 1.00 14.79 N ANISOU 227 N CYS A 38 2382 1598 1638 176 186 55 N ATOM 228 CA CYS A 38 18.958 44.221 21.621 1.00 15.49 C ANISOU 228 CA CYS A 38 2472 1681 1733 163 186 39 C ATOM 229 C CYS A 38 18.133 43.067 22.164 1.00 15.12 C ANISOU 229 C CYS A 38 2394 1655 1697 175 189 39 C ATOM 230 O CYS A 38 18.694 42.034 22.544 1.00 13.49 O ANISOU 230 O CYS A 38 2170 1457 1500 157 184 26 O ATOM 231 CB CYS A 38 19.278 45.211 22.731 1.00 22.10 C ANISOU 231 CB CYS A 38 3350 2485 2561 172 193 37 C ATOM 232 SG CYS A 38 20.627 46.257 22.233 1.00 28.50 S ANISOU 232 SG CYS A 38 4194 3273 3361 148 186 32 S ATOM 233 N THR A 39 16.808 43.230 22.229 1.00 13.53 N ANISOU 233 N THR A 39 2186 1460 1496 206 197 53 N ATOM 234 CA THR A 39 15.949 42.124 22.639 1.00 12.52 C ANISOU 234 CA THR A 39 2025 1353 1378 218 200 54 C ATOM 235 C THR A 39 16.085 40.942 21.686 1.00 13.27 C ANISOU 235 C THR A 39 2080 1477 1484 198 191 49 C ATOM 236 O THR A 39 16.228 39.794 22.119 1.00 11.13 O ANISOU 236 O THR A 39 1785 1220 1224 189 188 39 O ATOM 237 CB THR A 39 14.504 42.597 22.720 1.00 18.97 C ANISOU 237 CB THR A 39 2843 2172 2193 254 210 71 C ATOM 238 OG1 THR A 39 14.398 43.576 23.762 1.00 20.39 O ANISOU 238 OG1 THR A 39 3059 2324 2363 271 220 73 O ATOM 239 CG2 THR A 39 13.584 41.416 23.020 1.00 12.91 C ANISOU 239 CG2 THR A 39 2040 1429 1437 266 213 72 C ATOM 240 N ALA A 40 16.063 41.205 20.370 1.00 16.85 N ANISOU 240 N ALA A 40 2525 1943 1935 192 185 56 N ATOM 241 CA ALA A 40 16.238 40.113 19.414 1.00 11.80 C ANISOU 241 CA ALA A 40 1848 1332 1305 173 176 51 C ATOM 242 C ALA A 40 17.598 39.444 19.582 1.00 14.25 C ANISOU 242 C ALA A 40 2154 1640 1620 139 167 32 C ATOM 243 O ALA A 40 17.695 38.211 19.543 1.00 10.72 O ANISOU 243 O ALA A 40 1675 1213 1185 126 162 24 O ATOM 244 CB ALA A 40 16.050 40.616 17.981 1.00 11.08 C ANISOU 244 CB ALA A 40 1751 1250 1208 171 171 61 C ATOM 245 N VAL A 41 18.653 40.237 19.813 1.00 11.53 N ANISOU 245 N VAL A 41 1843 1272 1268 125 165 26 N ATOM 246 CA VAL A 41 20.003 39.678 19.937 1.00 6.43 C ANISOU 246 CA VAL A 41 1196 623 626 92 156 8 C ATOM 247 C VAL A 41 20.118 38.774 21.157 1.00 13.15 C ANISOU 247 C VAL A 41 2037 1473 1486 90 158 -3 C ATOM 248 O VAL A 41 20.726 37.697 21.093 1.00 13.89 O ANISOU 248 O VAL A 41 2108 1581 1590 68 151 -15 O ATOM 249 CB VAL A 41 21.045 40.815 19.976 1.00 13.03 C ANISOU 249 CB VAL A 41 2070 1430 1449 79 154 5 C ATOM 250 CG1 VAL A 41 22.386 40.328 20.598 1.00 11.74 C ANISOU 250 CG1 VAL A 41 1914 1258 1290 50 148 -14 C ATOM 251 CG2 VAL A 41 21.255 41.354 18.591 1.00 14.93 C ANISOU 251 CG2 VAL A 41 2311 1677 1684 70 148 11 C ATOM 252 N LYS A 42 19.543 39.188 22.290 1.00 11.41 N ANISOU 252 N LYS A 42 1835 1237 1262 113 168 2 N ATOM 253 CA LYS A 42 19.551 38.315 23.463 1.00 14.81 C ANISOU 253 CA LYS A 42 2256 1670 1701 113 171 -7 C ATOM 254 C LYS A 42 18.805 37.020 23.182 1.00 15.77 C ANISOU 254 C LYS A 42 2334 1822 1837 117 169 -6 C ATOM 255 O LYS A 42 19.201 35.949 23.660 1.00 12.00 O ANISOU 255 O LYS A 42 1836 1352 1369 103 166 -18 O ATOM 256 CB LYS A 42 18.939 39.020 24.671 1.00 17.83 C ANISOU 256 CB LYS A 42 2665 2032 2077 140 183 -1 C ATOM 257 CG LYS A 42 19.759 40.183 25.205 1.00 13.09 C ANISOU 257 CG LYS A 42 2109 1400 1465 136 185 -5 C ATOM 258 CD LYS A 42 19.158 40.729 26.502 1.00 11.47 C ANISOU 258 CD LYS A 42 1927 1176 1255 162 196 -1 C ATOM 259 CE LYS A 42 17.838 41.422 26.271 1.00 16.06 C ANISOU 259 CE LYS A 42 2513 1759 1831 195 205 16 C ATOM 260 NZ LYS A 42 17.237 41.920 27.575 1.00 15.36 N ANISOU 260 NZ LYS A 42 2447 1653 1738 220 217 20 N ATOM 261 N ALA A 43 17.718 37.102 22.414 1.00 11.69 N ANISOU 261 N ALA A 43 1801 1320 1319 136 172 8 N ATOM 262 CA ALA A 43 16.986 35.899 22.054 1.00 7.68 C ANISOU 262 CA ALA A 43 1251 842 825 139 170 9 C ATOM 263 C ALA A 43 17.797 35.045 21.094 1.00 11.52 C ANISOU 263 C ALA A 43 1711 1347 1319 108 158 -1 C ATOM 264 O ALA A 43 17.802 33.816 21.202 1.00 11.34 O ANISOU 264 O ALA A 43 1657 1343 1310 98 154 -9 O ATOM 265 CB ALA A 43 15.637 36.260 21.444 1.00 8.00 C ANISOU 265 CB ALA A 43 1283 895 863 167 175 27 C ATOM 266 N ILE A 44 18.499 35.672 20.149 1.00 7.40 N ANISOU 266 N ILE A 44 1201 820 789 92 152 -2 N ATOM 267 CA ILE A 44 19.370 34.891 19.280 1.00 10.80 C ANISOU 267 CA ILE A 44 1609 1267 1227 61 140 -13 C ATOM 268 C ILE A 44 20.447 34.198 20.108 1.00 12.20 C ANISOU 268 C ILE A 44 1787 1437 1412 38 136 -30 C ATOM 269 O ILE A 44 20.721 33.007 19.933 1.00 11.15 O ANISOU 269 O ILE A 44 1623 1323 1292 21 130 -40 O ATOM 270 CB ILE A 44 19.992 35.777 18.187 1.00 13.14 C ANISOU 270 CB ILE A 44 1923 1558 1514 48 135 -11 C ATOM 271 CG1 ILE A 44 18.930 36.281 17.202 1.00 16.08 C ANISOU 271 CG1 ILE A 44 2287 1942 1880 68 137 6 C ATOM 272 CG2 ILE A 44 21.091 35.003 17.476 1.00 9.32 C ANISOU 272 CG2 ILE A 44 1419 1086 1036 13 123 -25 C ATOM 273 CD1 ILE A 44 19.456 37.375 16.253 1.00 6.19 C ANISOU 273 CD1 ILE A 44 1057 680 616 59 133 11 C ATOM 274 N SER A 45 21.085 34.943 21.014 1.00 11.84 N ANISOU 274 N SER A 45 1777 1364 1358 37 139 -35 N ATOM 275 CA SER A 45 22.143 34.375 21.848 1.00 13.13 C ANISOU 275 CA SER A 45 1944 1519 1527 15 136 -51 C ATOM 276 C SER A 45 21.638 33.157 22.608 1.00 15.85 C ANISOU 276 C SER A 45 2259 1878 1885 21 138 -55 C ATOM 277 O SER A 45 22.294 32.106 22.645 1.00 15.80 O ANISOU 277 O SER A 45 2231 1883 1890 -2 131 -67 O ATOM 278 CB SER A 45 22.669 35.450 22.816 1.00 11.02 C ANISOU 278 CB SER A 45 1720 1219 1248 19 141 -52 C ATOM 279 OG SER A 45 23.787 35.000 23.558 1.00 11.65 O ANISOU 279 OG SER A 45 1806 1290 1332 -4 137 -68 O ATOM 280 N SER A 46 20.457 33.276 23.210 1.00 13.31 N ANISOU 280 N SER A 46 1937 1557 1563 51 148 -44 N ATOM 281 CA SER A 46 19.894 32.165 23.957 1.00 13.46 C ANISOU 281 CA SER A 46 1929 1590 1595 58 150 -46 C ATOM 282 C SER A 46 19.759 30.923 23.076 1.00 13.76 C ANISOU 282 C SER A 46 1924 1658 1648 45 143 -50 C ATOM 283 O SER A 46 20.167 29.823 23.467 1.00 11.51 O ANISOU 283 O SER A 46 1616 1382 1374 30 139 -61 O ATOM 284 CB SER A 46 18.546 32.587 24.547 1.00 14.23 C ANISOU 284 CB SER A 46 2033 1685 1689 95 162 -32 C ATOM 285 OG SER A 46 17.929 31.531 25.250 1.00 14.32 O ANISOU 285 OG SER A 46 2018 1710 1713 104 165 -33 O ATOM 286 N ALA A 47 19.238 31.094 21.860 1.00 16.64 N ANISOU 286 N ALA A 47 2275 2037 2010 50 140 -41 N ATOM 287 CA ALA A 47 19.034 29.954 20.974 1.00 17.81 C ANISOU 287 CA ALA A 47 2381 2215 2171 39 134 -44 C ATOM 288 C ALA A 47 20.358 29.400 20.476 1.00 16.83 C ANISOU 288 C ALA A 47 2248 2095 2052 3 123 -60 C ATOM 289 O ALA A 47 20.526 28.179 20.363 1.00 15.31 O ANISOU 289 O ALA A 47 2022 1920 1873 -12 117 -68 O ATOM 290 CB ALA A 47 18.145 30.361 19.797 1.00 15.08 C ANISOU 290 CB ALA A 47 2026 1884 1821 53 134 -30 C ATOM 291 N VAL A 48 21.319 30.283 20.208 1.00 12.79 N ANISOU 291 N VAL A 48 1765 1564 1529 -12 119 -63 N ATOM 292 CA VAL A 48 22.625 29.861 19.713 1.00 15.53 C ANISOU 292 CA VAL A 48 2107 1914 1880 -46 109 -78 C ATOM 293 C VAL A 48 23.372 29.051 20.765 1.00 18.71 C ANISOU 293 C VAL A 48 2506 2311 2293 -62 107 -92 C ATOM 294 O VAL A 48 24.067 28.083 20.438 1.00 11.41 O ANISOU 294 O VAL A 48 1557 1399 1378 -86 99 -104 O ATOM 295 CB VAL A 48 23.432 31.094 19.269 1.00 10.90 C ANISOU 295 CB VAL A 48 1555 1307 1278 -56 107 -77 C ATOM 296 CG1 VAL A 48 24.915 30.756 19.069 1.00 8.03 C ANISOU 296 CG1 VAL A 48 1193 940 918 -92 97 -93 C ATOM 297 CG2 VAL A 48 22.816 31.692 18.003 1.00 15.53 C ANISOU 297 CG2 VAL A 48 2139 1905 1858 -47 106 -65 C ATOM 298 N ARG A 49 23.263 29.437 22.034 1.00 8.52 N ANISOU 298 N ARG A 49 1239 1002 998 -48 115 -91 N ATOM 299 CA ARG A 49 23.869 28.648 23.101 1.00 10.25 C ANISOU 299 CA ARG A 49 1453 1216 1227 -60 114 -103 C ATOM 300 C ARG A 49 23.057 27.400 23.445 1.00 13.69 C ANISOU 300 C ARG A 49 1851 1673 1678 -51 116 -102 C ATOM 301 O ARG A 49 23.413 26.696 24.400 1.00 13.16 O ANISOU 301 O ARG A 49 1778 1603 1619 -58 116 -111 O ATOM 302 CB ARG A 49 24.071 29.500 24.366 1.00 14.40 C ANISOU 302 CB ARG A 49 2016 1713 1742 -50 122 -102 C ATOM 303 CG ARG A 49 25.345 30.386 24.377 1.00 9.03 C ANISOU 303 CG ARG A 49 1372 1010 1051 -69 118 -110 C ATOM 304 CD ARG A 49 25.277 31.599 23.401 1.00 15.21 C ANISOU 304 CD ARG A 49 2176 1784 1819 -64 117 -100 C ATOM 305 NE ARG A 49 26.266 32.650 23.699 1.00 13.92 N ANISOU 305 NE ARG A 49 2052 1593 1643 -75 117 -105 N ATOM 306 CZ ARG A 49 27.524 32.649 23.249 1.00 14.29 C ANISOU 306 CZ ARG A 49 2104 1636 1689 -105 108 -116 C ATOM 307 NH1 ARG A 49 27.967 31.644 22.493 1.00 12.09 N ANISOU 307 NH1 ARG A 49 1794 1378 1421 -127 99 -124 N ATOM 308 NH2 ARG A 49 28.355 33.637 23.563 1.00 8.87 N ANISOU 308 NH2 ARG A 49 1455 924 990 -113 108 -119 N ATOM 309 N LYS A 50 21.974 27.130 22.711 1.00 11.70 N ANISOU 309 N LYS A 50 1575 1441 1430 -35 117 -92 N ATOM 310 CA LYS A 50 21.229 25.859 22.772 1.00 14.79 C ANISOU 310 CA LYS A 50 1926 1856 1837 -30 117 -92 C ATOM 311 C LYS A 50 20.399 25.712 24.047 1.00 11.50 C ANISOU 311 C LYS A 50 1511 1434 1422 -5 127 -86 C ATOM 312 O LYS A 50 20.159 24.596 24.516 1.00 15.64 O ANISOU 312 O LYS A 50 2008 1972 1961 -6 127 -91 O ATOM 313 CB LYS A 50 22.153 24.646 22.604 1.00 6.89 C ANISOU 313 CB LYS A 50 899 869 851 -60 108 -108 C ATOM 314 CG LYS A 50 22.855 24.602 21.260 1.00 13.07 C ANISOU 314 CG LYS A 50 1671 1661 1633 -84 98 -114 C ATOM 315 CD LYS A 50 21.873 24.409 20.095 1.00 14.72 C ANISOU 315 CD LYS A 50 1855 1894 1844 -73 97 -104 C ATOM 316 CE LYS A 50 22.584 24.510 18.733 1.00 18.20 C ANISOU 316 CE LYS A 50 2290 2344 2283 -96 88 -109 C ATOM 317 NZ LYS A 50 21.693 24.103 17.593 1.00 24.71 N ANISOU 317 NZ LYS A 50 3083 3195 3111 -88 86 -102 N ATOM 318 N ALA A 51 19.946 26.824 24.615 1.00 10.87 N ANISOU 318 N ALA A 51 1464 1336 1330 17 135 -77 N ATOM 319 CA ALA A 51 18.952 26.764 25.678 1.00 13.73 C ANISOU 319 CA ALA A 51 1827 1696 1693 45 145 -69 C ATOM 320 C ALA A 51 17.744 25.990 25.176 1.00 14.92 C ANISOU 320 C ALA A 51 1941 1873 1854 61 147 -60 C ATOM 321 O ALA A 51 17.220 26.277 24.097 1.00 11.73 O ANISOU 321 O ALA A 51 1529 1480 1446 67 145 -52 O ATOM 322 CB ALA A 51 18.531 28.180 26.084 1.00 10.31 C ANISOU 322 CB ALA A 51 1433 1241 1243 68 154 -58 C ATOM 323 N GLY A 52 17.332 24.974 25.927 1.00 10.97 N ANISOU 323 N GLY A 52 1417 1383 1367 66 149 -62 N ATOM 324 CA GLY A 52 16.177 24.187 25.547 1.00 17.11 C ANISOU 324 CA GLY A 52 2159 2186 2155 81 150 -54 C ATOM 325 C GLY A 52 16.454 23.051 24.587 1.00 19.22 C ANISOU 325 C GLY A 52 2388 2478 2437 59 140 -62 C ATOM 326 O GLY A 52 15.524 22.305 24.256 1.00 19.61 O ANISOU 326 O GLY A 52 2406 2550 2497 70 141 -56 O ATOM 327 N ILE A 53 17.711 22.851 24.182 1.00 14.92 N ANISOU 327 N ILE A 53 1846 1931 1894 29 132 -75 N ATOM 328 CA ILE A 53 18.027 21.800 23.215 1.00 11.14 C ANISOU 328 CA ILE A 53 1330 1474 1428 7 122 -84 C ATOM 329 C ILE A 53 17.559 20.437 23.718 1.00 12.69 C ANISOU 329 C ILE A 53 1490 1688 1643 8 122 -87 C ATOM 330 O ILE A 53 17.268 19.545 22.915 1.00 16.26 O ANISOU 330 O ILE A 53 1907 2164 2108 2 117 -89 O ATOM 331 CB ILE A 53 19.540 21.807 22.910 1.00 16.19 C ANISOU 331 CB ILE A 53 1979 2104 2067 -27 113 -99 C ATOM 332 CG1 ILE A 53 19.873 20.963 21.673 1.00 17.18 C ANISOU 332 CG1 ILE A 53 2072 2253 2202 -49 103 -106 C ATOM 333 CG2 ILE A 53 20.327 21.327 24.121 1.00 15.43 C ANISOU 333 CG2 ILE A 53 1890 1996 1977 -39 113 -110 C ATOM 334 CD1 ILE A 53 19.277 21.492 20.379 1.00 25.30 C ANISOU 334 CD1 ILE A 53 3096 3293 3223 -41 102 -97 C ATOM 335 N ALA A 54 17.448 20.263 25.046 1.00 9.31 N ANISOU 335 N ALA A 54 1070 1249 1218 18 128 -87 N ATOM 336 CA ALA A 54 16.965 19.002 25.604 1.00 13.38 C ANISOU 336 CA ALA A 54 1552 1781 1751 21 129 -89 C ATOM 337 C ALA A 54 15.559 18.669 25.122 1.00 12.93 C ANISOU 337 C ALA A 54 1469 1745 1699 44 132 -77 C ATOM 338 O ALA A 54 15.226 17.486 24.975 1.00 15.92 O ANISOU 338 O ALA A 54 1810 2144 2094 40 129 -80 O ATOM 339 CB ALA A 54 17.006 19.044 27.142 1.00 11.35 C ANISOU 339 CB ALA A 54 1312 1507 1493 31 136 -90 C ATOM 340 N HIS A 55 14.719 19.688 24.874 1.00 6.11 N ANISOU 340 N HIS A 55 623 876 821 69 139 -63 N ATOM 341 CA HIS A 55 13.376 19.413 24.379 1.00 12.78 C ANISOU 341 CA HIS A 55 1444 1741 1670 91 142 -50 C ATOM 342 C HIS A 55 13.410 18.853 22.967 1.00 21.27 C ANISOU 342 C HIS A 55 2490 2840 2753 76 134 -54 C ATOM 343 O HIS A 55 12.553 18.036 22.617 1.00 21.16 O ANISOU 343 O HIS A 55 2442 2848 2750 84 134 -49 O ATOM 344 CB HIS A 55 12.484 20.653 24.482 1.00 19.37 C ANISOU 344 CB HIS A 55 2306 2565 2489 121 152 -34 C ATOM 345 CG HIS A 55 12.098 20.969 25.893 1.00 34.48 C ANISOU 345 CG HIS A 55 4240 4463 4399 141 161 -30 C ATOM 346 ND1 HIS A 55 11.017 20.382 26.514 1.00 35.87 N ANISOU 346 ND1 HIS A 55 4396 4650 4584 163 167 -22 N ATOM 347 CD2 HIS A 55 12.673 21.774 26.819 1.00 36.17 C ANISOU 347 CD2 HIS A 55 4490 4651 4602 143 165 -32 C ATOM 348 CE1 HIS A 55 10.934 20.822 27.757 1.00 34.40 C ANISOU 348 CE1 HIS A 55 4233 4446 4391 177 175 -19 C ATOM 349 NE2 HIS A 55 11.930 21.663 27.969 1.00 36.45 N ANISOU 349 NE2 HIS A 55 4527 4683 4639 165 174 -26 N ATOM 350 N LEU A 56 14.386 19.262 22.149 1.00 22.30 N ANISOU 350 N LEU A 56 2631 2965 2877 54 127 -61 N ATOM 351 CA LEU A 56 14.525 18.661 20.821 1.00 26.55 C ANISOU 351 CA LEU A 56 3140 3525 3422 36 118 -66 C ATOM 352 C LEU A 56 14.920 17.191 20.880 1.00 18.81 C ANISOU 352 C LEU A 56 2124 2561 2462 16 111 -79 C ATOM 353 O LEU A 56 14.685 16.449 19.920 1.00 22.01 O ANISOU 353 O LEU A 56 2496 2989 2876 8 106 -81 O ATOM 354 CB LEU A 56 15.553 19.417 19.980 1.00 20.26 C ANISOU 354 CB LEU A 56 2365 2719 2614 16 112 -72 C ATOM 355 CG LEU A 56 15.059 20.477 19.014 1.00 35.97 C ANISOU 355 CG LEU A 56 4369 4709 4589 28 113 -60 C ATOM 356 CD1 LEU A 56 16.250 21.184 18.399 1.00 39.35 C ANISOU 356 CD1 LEU A 56 4821 5125 5007 5 107 -67 C ATOM 357 CD2 LEU A 56 14.231 19.809 17.928 1.00 40.34 C ANISOU 357 CD2 LEU A 56 4886 5292 5151 32 110 -55 C ATOM 358 N TYR A 57 15.584 16.766 21.948 1.00 16.69 N ANISOU 358 N TYR A 57 1860 2281 2200 6 112 -88 N ATOM 359 CA TYR A 57 16.073 15.405 22.044 1.00 15.86 C ANISOU 359 CA TYR A 57 1734 2181 2110 -14 101 -95 C ATOM 360 C TYR A 57 15.219 14.533 22.952 1.00 20.41 C ANISOU 360 C TYR A 57 2309 2753 2693 3 100 -79 C ATOM 361 O TYR A 57 15.665 13.461 23.370 1.00 27.87 O ANISOU 361 O TYR A 57 3260 3688 3642 -9 88 -76 O ATOM 362 CB TYR A 57 17.537 15.422 22.490 1.00 13.02 C ANISOU 362 CB TYR A 57 1387 1809 1752 -40 98 -112 C ATOM 363 CG TYR A 57 18.425 15.796 21.324 1.00 17.65 C ANISOU 363 CG TYR A 57 1978 2397 2333 -63 91 -120 C ATOM 364 CD1 TYR A 57 18.587 17.127 20.938 1.00 11.79 C ANISOU 364 CD1 TYR A 57 1265 1641 1572 -59 94 -116 C ATOM 365 CD2 TYR A 57 19.059 14.818 20.575 1.00 20.36 C ANISOU 365 CD2 TYR A 57 2328 2733 2675 -78 71 -115 C ATOM 366 CE1 TYR A 57 19.388 17.464 19.853 1.00 12.93 C ANISOU 366 CE1 TYR A 57 1415 1788 1711 -80 86 -122 C ATOM 367 CE2 TYR A 57 19.854 15.149 19.488 1.00 16.47 C ANISOU 367 CE2 TYR A 57 1842 2240 2175 -95 64 -120 C ATOM 368 CZ TYR A 57 20.011 16.464 19.129 1.00 17.09 C ANISOU 368 CZ TYR A 57 1918 2326 2248 -104 75 -132 C ATOM 369 OH TYR A 57 20.811 16.776 18.046 1.00 19.93 O ANISOU 369 OH TYR A 57 2286 2685 2600 -122 67 -136 O ATOM 370 N GLY A 58 13.991 14.954 23.236 1.00 17.08 N ANISOU 370 N GLY A 58 1882 2337 2270 32 111 -69 N ATOM 371 CA GLY A 58 13.014 14.085 23.858 1.00 16.16 C ANISOU 371 CA GLY A 58 1764 2216 2161 46 110 -51 C ATOM 372 C GLY A 58 12.975 14.058 25.368 1.00 19.63 C ANISOU 372 C GLY A 58 2210 2648 2602 56 117 -52 C ATOM 373 O GLY A 58 12.431 13.102 25.931 1.00 17.62 O ANISOU 373 O GLY A 58 1954 2387 2353 60 113 -37 O ATOM 374 N ILE A 59 13.500 15.080 26.049 1.00 13.50 N ANISOU 374 N ILE A 59 1442 1868 1820 62 131 -69 N ATOM 375 CA ILE A 59 13.463 15.070 27.511 1.00 17.63 C ANISOU 375 CA ILE A 59 1974 2380 2344 73 139 -70 C ATOM 376 C ILE A 59 12.035 14.959 28.030 1.00 18.73 C ANISOU 376 C ILE A 59 2113 2521 2484 102 145 -50 C ATOM 377 O ILE A 59 11.795 14.348 29.079 1.00 26.01 O ANISOU 377 O ILE A 59 3036 3435 3409 106 145 -42 O ATOM 378 CB ILE A 59 14.184 16.311 28.086 1.00 19.95 C ANISOU 378 CB ILE A 59 2310 2648 2622 73 145 -74 C ATOM 379 CG1 ILE A 59 14.345 16.190 29.602 1.00 17.76 C ANISOU 379 CG1 ILE A 59 2046 2357 2346 79 150 -76 C ATOM 380 CG2 ILE A 59 13.462 17.606 27.733 1.00 14.35 C ANISOU 380 CG2 ILE A 59 1626 1930 1894 97 151 -61 C ATOM 381 CD1 ILE A 59 15.108 17.360 30.203 1.00 18.08 C ANISOU 381 CD1 ILE A 59 2131 2370 2370 76 153 -78 C ATOM 382 N ALA A 60 11.063 15.525 27.316 1.00 14.06 N ANISOU 382 N ALA A 60 1518 1935 1889 120 150 -44 N ATOM 383 CA ALA A 60 9.673 15.435 27.743 1.00 21.31 C ANISOU 383 CA ALA A 60 2438 2850 2810 138 150 -37 C ATOM 384 C ALA A 60 8.871 14.463 26.888 1.00 26.24 C ANISOU 384 C ALA A 60 3047 3473 3450 125 138 -35 C ATOM 385 O ALA A 60 7.654 14.611 26.775 1.00 21.32 O ANISOU 385 O ALA A 60 2424 2854 2821 140 137 -29 O ATOM 386 CB ALA A 60 9.012 16.812 27.737 1.00 11.31 C ANISOU 386 CB ALA A 60 1190 1584 1521 172 163 -22 C ATOM 387 N GLY A 61 9.533 13.503 26.248 1.00 24.56 N ANISOU 387 N GLY A 61 2829 3253 3250 101 129 -28 N ATOM 388 CA GLY A 61 8.850 12.562 25.380 1.00 29.64 C ANISOU 388 CA GLY A 61 3467 3891 3904 90 118 -21 C ATOM 389 C GLY A 61 9.000 12.940 23.920 1.00 35.14 C ANISOU 389 C GLY A 61 4156 4600 4597 86 115 -20 C ATOM 390 O GLY A 61 9.237 14.111 23.604 1.00 39.26 O ANISOU 390 O GLY A 61 4677 5136 5104 97 122 -26 O ATOM 391 N VAL A 70 12.441 24.283 16.710 1.00 31.25 N ANISOU 391 N VAL A 70 3826 4106 3941 99 128 -6 N ATOM 392 CA VAL A 70 12.679 23.310 15.649 1.00 34.45 C ANISOU 392 CA VAL A 70 4195 4537 4357 78 119 -14 C ATOM 393 C VAL A 70 13.080 23.997 14.327 1.00 31.81 C ANISOU 393 C VAL A 70 3869 4206 4012 66 113 -12 C ATOM 394 O VAL A 70 13.477 23.339 13.359 1.00 38.14 O ANISOU 394 O VAL A 70 4645 5026 4820 45 104 -20 O ATOM 395 CB VAL A 70 11.446 22.413 15.459 1.00 45.30 C ANISOU 395 CB VAL A 70 5533 5937 5743 94 121 -7 C ATOM 396 CG1 VAL A 70 11.843 21.071 14.869 1.00 55.21 C ANISOU 396 CG1 VAL A 70 6748 7214 7013 70 111 -20 C ATOM 397 CG2 VAL A 70 10.711 22.234 16.778 1.00 51.76 C ANISOU 397 CG2 VAL A 70 6354 6747 6565 117 130 -1 C ATOM 398 N LYS A 71 12.987 25.321 14.283 1.00 22.07 N ANISOU 398 N LYS A 71 2669 2955 2762 79 117 -2 N ATOM 399 CA LYS A 71 13.555 26.058 13.162 1.00 19.09 C ANISOU 399 CA LYS A 71 2303 2576 2373 66 112 -1 C ATOM 400 C LYS A 71 15.082 26.048 13.228 1.00 17.54 C ANISOU 400 C LYS A 71 2122 2367 2177 34 104 -17 C ATOM 401 O LYS A 71 15.681 26.107 14.302 1.00 19.32 O ANISOU 401 O LYS A 71 2366 2572 2403 30 107 -24 O ATOM 402 CB LYS A 71 13.065 27.505 13.165 1.00 19.48 C ANISOU 402 CB LYS A 71 2388 2608 2407 88 119 15 C ATOM 403 CG LYS A 71 11.574 27.699 13.035 1.00 30.37 C ANISOU 403 CG LYS A 71 3757 3998 3784 120 126 32 C ATOM 404 CD LYS A 71 11.232 29.185 13.179 1.00 39.00 C ANISOU 404 CD LYS A 71 4888 5071 4861 141 134 47 C ATOM 405 CE LYS A 71 9.742 29.466 13.016 1.00 40.03 C ANISOU 405 CE LYS A 71 5011 5211 4989 173 141 65 C ATOM 406 NZ LYS A 71 9.410 30.884 13.389 1.00 42.03 N ANISOU 406 NZ LYS A 71 5302 5440 5227 195 150 78 N ATOM 407 N LYS A 72 15.715 25.993 12.062 1.00 10.74 N ANISOU 407 N LYS A 72 1251 1516 1314 12 96 -22 N ATOM 408 CA LYS A 72 17.147 26.243 12.004 1.00 11.98 C ANISOU 408 CA LYS A 72 1426 1658 1467 -15 89 -35 C ATOM 409 C LYS A 72 17.454 27.624 12.564 1.00 15.03 C ANISOU 409 C LYS A 72 1859 2014 1838 -6 95 -29 C ATOM 410 O LYS A 72 16.637 28.544 12.481 1.00 15.08 O ANISOU 410 O LYS A 72 1882 2015 1834 18 101 -14 O ATOM 411 CB LYS A 72 17.659 26.129 10.563 1.00 24.41 C ANISOU 411 CB LYS A 72 2986 3250 3040 -37 80 -39 C ATOM 412 CG LYS A 72 18.506 24.890 10.325 1.00 32.21 C ANISOU 412 CG LYS A 72 3945 4251 4042 -67 71 -57 C ATOM 413 CD LYS A 72 17.756 23.635 10.740 1.00 40.77 C ANISOU 413 CD LYS A 72 4993 5354 5142 -59 72 -60 C ATOM 414 CE LYS A 72 18.708 22.542 11.195 1.00 50.06 C ANISOU 414 CE LYS A 72 6155 6533 6334 -85 67 -78 C ATOM 415 NZ LYS A 72 19.791 22.313 10.197 1.00 57.22 N ANISOU 415 NZ LYS A 72 7054 7447 7241 -116 56 -91 N ATOM 416 N LEU A 73 18.661 27.771 13.122 1.00 16.38 N ANISOU 416 N LEU A 73 2051 2166 2008 -26 92 -41 N ATOM 417 CA LEU A 73 18.995 29.003 13.836 1.00 17.88 C ANISOU 417 CA LEU A 73 2285 2326 2184 -18 97 -37 C ATOM 418 C LEU A 73 18.975 30.229 12.929 1.00 21.42 C ANISOU 418 C LEU A 73 2754 2767 2616 -13 97 -26 C ATOM 419 O LEU A 73 18.567 31.311 13.363 1.00 17.59 O ANISOU 419 O LEU A 73 2300 2264 2121 7 105 -15 O ATOM 420 CB LEU A 73 20.343 28.870 14.530 1.00 13.03 C ANISOU 420 CB LEU A 73 1686 1694 1571 -42 93 -52 C ATOM 421 CG LEU A 73 20.267 27.961 15.760 1.00 23.20 C ANISOU 421 CG LEU A 73 2964 2981 2872 -39 97 -60 C ATOM 422 CD1 LEU A 73 21.631 27.856 16.429 1.00 25.40 C ANISOU 422 CD1 LEU A 73 3258 3241 3151 -64 93 -75 C ATOM 423 CD2 LEU A 73 19.204 28.454 16.744 1.00 25.23 C ANISOU 423 CD2 LEU A 73 3236 3227 3125 -6 108 -48 C ATOM 424 N ASP A 74 19.418 30.099 11.675 1.00 22.73 N ANISOU 424 N ASP A 74 2907 2948 2782 -32 89 -29 N ATOM 425 CA ASP A 74 19.413 31.277 10.809 1.00 20.81 C ANISOU 425 CA ASP A 74 2684 2699 2524 -29 88 -18 C ATOM 426 C ASP A 74 17.996 31.720 10.467 1.00 26.69 C ANISOU 426 C ASP A 74 3425 3453 3265 2 95 1 C ATOM 427 O ASP A 74 17.736 32.922 10.346 1.00 21.18 O ANISOU 427 O ASP A 74 2755 2741 2554 17 100 13 O ATOM 428 CB ASP A 74 20.204 31.001 9.527 1.00 27.79 C ANISOU 428 CB ASP A 74 3552 3598 3408 -57 77 -26 C ATOM 429 CG ASP A 74 19.678 29.801 8.755 1.00 33.84 C ANISOU 429 CG ASP A 74 4274 4398 4187 -61 73 -28 C ATOM 430 OD1 ASP A 74 18.780 29.101 9.264 1.00 38.72 O ANISOU 430 OD1 ASP A 74 4871 5026 4814 -45 77 -26 O ATOM 431 OD2 ASP A 74 20.173 29.545 7.640 1.00 36.26 O ANISOU 431 OD2 ASP A 74 4564 4720 4493 -82 64 -33 O ATOM 432 N VAL A 75 17.067 30.771 10.341 1.00 21.67 N ANISOU 432 N VAL A 75 2754 2841 2640 13 96 3 N ATOM 433 CA VAL A 75 15.663 31.107 10.139 1.00 22.51 C ANISOU 433 CA VAL A 75 2854 2956 2742 43 103 21 C ATOM 434 C VAL A 75 15.091 31.755 11.397 1.00 21.30 C ANISOU 434 C VAL A 75 2728 2781 2585 70 114 29 C ATOM 435 O VAL A 75 14.385 32.774 11.336 1.00 12.14 O ANISOU 435 O VAL A 75 1588 1611 1414 93 121 44 O ATOM 436 CB VAL A 75 14.878 29.838 9.752 1.00 24.80 C ANISOU 436 CB VAL A 75 3099 3277 3046 46 101 20 C ATOM 437 CG1 VAL A 75 13.369 30.092 9.770 1.00 16.08 C ANISOU 437 CG1 VAL A 75 1988 2182 1940 79 110 38 C ATOM 438 CG2 VAL A 75 15.355 29.308 8.395 1.00 23.49 C ANISOU 438 CG2 VAL A 75 2908 3135 2884 21 91 13 C ATOM 439 N LEU A 76 15.387 31.169 12.559 1.00 12.90 N ANISOU 439 N LEU A 76 1665 1708 1529 67 116 19 N ATOM 440 CA LEU A 76 14.898 31.729 13.814 1.00 11.92 C ANISOU 440 CA LEU A 76 1565 1562 1401 91 127 25 C ATOM 441 C LEU A 76 15.436 33.142 14.029 1.00 9.97 C ANISOU 441 C LEU A 76 1363 1286 1138 93 130 29 C ATOM 442 O LEU A 76 14.684 34.068 14.379 1.00 12.10 O ANISOU 442 O LEU A 76 1655 1543 1400 119 138 43 O ATOM 443 CB LEU A 76 15.289 30.813 14.975 1.00 13.41 C ANISOU 443 CB LEU A 76 1747 1748 1601 83 127 12 C ATOM 444 CG LEU A 76 14.872 31.363 16.333 1.00 16.47 C ANISOU 444 CG LEU A 76 2160 2112 1984 106 138 17 C ATOM 445 CD1 LEU A 76 13.353 31.461 16.370 1.00 19.94 C ANISOU 445 CD1 LEU A 76 2589 2562 2423 139 146 34 C ATOM 446 CD2 LEU A 76 15.363 30.468 17.461 1.00 20.72 C ANISOU 446 CD2 LEU A 76 2692 2647 2533 96 138 4 C ATOM 447 N SER A 77 16.736 33.325 13.794 1.00 9.04 N ANISOU 447 N SER A 77 1259 1158 1018 66 123 18 N ATOM 448 CA SER A 77 17.357 34.637 13.934 1.00 14.11 C ANISOU 448 CA SER A 77 1943 1773 1646 65 124 20 C ATOM 449 C SER A 77 16.722 35.663 13.011 1.00 16.34 C ANISOU 449 C SER A 77 2236 2056 1917 80 127 37 C ATOM 450 O SER A 77 16.486 36.805 13.425 1.00 11.44 O ANISOU 450 O SER A 77 1647 1413 1285 98 134 46 O ATOM 451 CB SER A 77 18.863 34.558 13.676 1.00 12.10 C ANISOU 451 CB SER A 77 1696 1510 1390 31 115 5 C ATOM 452 OG SER A 77 19.522 33.779 14.659 1.00 14.24 O ANISOU 452 OG SER A 77 1964 1776 1670 17 114 -10 O ATOM 453 N ASN A 78 16.465 35.289 11.750 1.00 14.66 N ANISOU 453 N ASN A 78 1995 1868 1706 74 121 40 N ATOM 454 CA ASN A 78 15.828 36.235 10.844 1.00 18.89 C ANISOU 454 CA ASN A 78 2540 2407 2232 89 122 57 C ATOM 455 C ASN A 78 14.442 36.607 11.353 1.00 11.15 C ANISOU 455 C ASN A 78 1563 1425 1250 125 133 73 C ATOM 456 O ASN A 78 14.088 37.791 11.383 1.00 15.51 O ANISOU 456 O ASN A 78 2142 1959 1790 142 139 85 O ATOM 457 CB ASN A 78 15.776 35.674 9.417 1.00 13.89 C ANISOU 457 CB ASN A 78 1874 1802 1601 75 114 57 C ATOM 458 CG ASN A 78 15.397 36.739 8.388 1.00 20.05 C ANISOU 458 CG ASN A 78 2665 2582 2369 84 114 73 C ATOM 459 OD1 ASN A 78 16.069 37.776 8.258 1.00 19.07 O ANISOU 459 OD1 ASN A 78 2573 2439 2234 78 114 75 O ATOM 460 ND2 ASN A 78 14.293 36.511 7.687 1.00 16.70 N ANISOU 460 ND2 ASN A 78 2218 2182 1947 100 116 85 N ATOM 461 N ASP A 79 13.660 35.607 11.796 1.00 11.39 N ANISOU 461 N ASP A 79 1565 1471 1291 136 136 72 N ATOM 462 CA ASP A 79 12.332 35.866 12.357 1.00 15.52 C ANISOU 462 CA ASP A 79 2090 1993 1813 170 147 86 C ATOM 463 C ASP A 79 12.402 36.782 13.576 1.00 17.83 C ANISOU 463 C ASP A 79 2421 2254 2098 185 156 89 C ATOM 464 O ASP A 79 11.551 37.656 13.746 1.00 13.12 O ANISOU 464 O ASP A 79 1842 1649 1495 212 164 104 O ATOM 465 CB ASP A 79 11.654 34.547 12.746 1.00 16.77 C ANISOU 465 CB ASP A 79 2213 2174 1987 176 148 83 C ATOM 466 CG ASP A 79 11.290 33.676 11.543 1.00 20.00 C ANISOU 466 CG ASP A 79 2581 2615 2402 167 141 83 C ATOM 467 OD1 ASP A 79 11.177 34.196 10.409 1.00 21.79 O ANISOU 467 OD1 ASP A 79 2807 2851 2623 165 137 92 O ATOM 468 OD2 ASP A 79 11.159 32.449 11.736 1.00 18.45 O ANISOU 468 OD2 ASP A 79 2354 2437 2220 160 138 75 O ATOM 469 N LEU A 80 13.391 36.576 14.453 1.00 23.74 N ANISOU 469 N LEU A 80 3184 2987 2849 169 154 74 N ATOM 470 CA LEU A 80 13.521 37.410 15.650 1.00 13.89 C ANISOU 470 CA LEU A 80 1974 1709 1595 182 162 75 C ATOM 471 C LEU A 80 13.838 38.860 15.291 1.00 10.93 C ANISOU 471 C LEU A 80 1635 1313 1206 185 164 82 C ATOM 472 O LEU A 80 13.173 39.784 15.776 1.00 11.28 O ANISOU 472 O LEU A 80 1703 1340 1242 210 173 94 O ATOM 473 CB LEU A 80 14.594 36.847 16.582 1.00 8.44 C ANISOU 473 CB LEU A 80 1289 1008 911 161 159 56 C ATOM 474 CG LEU A 80 14.278 35.565 17.348 1.00 6.32 C ANISOU 474 CG LEU A 80 992 752 655 162 160 49 C ATOM 475 CD1 LEU A 80 15.576 34.972 17.916 1.00 15.43 C ANISOU 475 CD1 LEU A 80 2149 1899 1815 133 154 30 C ATOM 476 CD2 LEU A 80 13.247 35.804 18.455 1.00 9.18 C ANISOU 476 CD2 LEU A 80 1365 1106 1017 193 172 58 C ATOM 477 N VAL A 81 14.834 39.080 14.421 1.00 10.83 N ANISOU 477 N VAL A 81 1626 1299 1188 159 155 77 N ATOM 478 CA VAL A 81 15.197 40.443 14.057 1.00 11.91 C ANISOU 478 CA VAL A 81 1797 1415 1312 161 156 84 C ATOM 479 C VAL A 81 14.048 41.117 13.314 1.00 16.53 C ANISOU 479 C VAL A 81 2381 2008 1891 186 160 104 C ATOM 480 O VAL A 81 13.673 42.254 13.623 1.00 12.40 O ANISOU 480 O VAL A 81 1887 1464 1358 206 168 115 O ATOM 481 CB VAL A 81 16.484 40.465 13.214 1.00 12.65 C ANISOU 481 CB VAL A 81 1893 1509 1403 128 145 74 C ATOM 482 CG1 VAL A 81 16.824 41.916 12.862 1.00 12.59 C ANISOU 482 CG1 VAL A 81 1922 1479 1381 130 146 82 C ATOM 483 CG2 VAL A 81 17.639 39.783 13.935 1.00 14.98 C ANISOU 483 CG2 VAL A 81 2190 1798 1705 102 140 54 C ATOM 484 N MET A 82 13.478 40.424 12.318 1.00 15.87 N ANISOU 484 N MET A 82 2263 1954 1813 185 156 108 N ATOM 485 CA MET A 82 12.374 40.992 11.551 1.00 16.34 C ANISOU 485 CA MET A 82 2318 2024 1868 208 160 127 C ATOM 486 C MET A 82 11.230 41.407 12.461 1.00 13.65 C ANISOU 486 C MET A 82 1988 1673 1526 242 172 139 C ATOM 487 O MET A 82 10.736 42.540 12.383 1.00 15.22 O ANISOU 487 O MET A 82 2210 1857 1714 262 179 153 O ATOM 488 CB MET A 82 11.875 39.995 10.497 1.00 12.47 C ANISOU 488 CB MET A 82 1784 1569 1385 202 154 129 C ATOM 489 CG MET A 82 12.689 39.992 9.221 1.00 22.83 C ANISOU 489 CG MET A 82 3088 2892 2695 175 143 125 C ATOM 490 SD MET A 82 12.514 41.546 8.306 1.00 23.56 S ANISOU 490 SD MET A 82 3207 2973 2771 186 145 143 S ATOM 491 CE MET A 82 13.590 41.186 6.925 1.00 37.47 C ANISOU 491 CE MET A 82 4952 4752 4533 150 131 134 C ATOM 492 N ASN A 83 10.817 40.515 13.356 1.00 8.84 N ANISOU 492 N ASN A 83 1363 1070 926 250 176 134 N ATOM 493 CA ASN A 83 9.623 40.799 14.140 1.00 11.84 C ANISOU 493 CA ASN A 83 1748 1444 1305 283 187 145 C ATOM 494 C ASN A 83 9.881 41.902 15.151 1.00 18.13 C ANISOU 494 C ASN A 83 2588 2207 2093 295 195 146 C ATOM 495 O ASN A 83 9.051 42.802 15.315 1.00 17.48 O ANISOU 495 O ASN A 83 2524 2115 2004 322 204 161 O ATOM 496 CB ASN A 83 9.140 39.542 14.857 1.00 21.93 C ANISOU 496 CB ASN A 83 2998 2738 2596 288 189 139 C ATOM 497 CG ASN A 83 7.837 39.768 15.584 1.00 34.02 C ANISOU 497 CG ASN A 83 4531 4267 4127 323 201 152 C ATOM 498 OD1 ASN A 83 6.800 39.981 14.960 1.00 39.02 O ANISOU 498 OD1 ASN A 83 5153 4914 4759 342 204 167 O ATOM 499 ND2 ASN A 83 7.883 39.741 16.912 1.00 36.73 N ANISOU 499 ND2 ASN A 83 4890 4594 4472 331 207 146 N ATOM 500 N MET A 84 11.036 41.870 15.820 1.00 16.38 N ANISOU 500 N MET A 84 2384 1968 1871 275 192 131 N ATOM 501 CA MET A 84 11.327 42.921 16.792 1.00 15.75 C ANISOU 501 CA MET A 84 2346 1855 1783 284 199 131 C ATOM 502 C MET A 84 11.473 44.283 16.117 1.00 18.98 C ANISOU 502 C MET A 84 2784 2249 2180 288 200 142 C ATOM 503 O MET A 84 11.023 45.300 16.661 1.00 14.11 O ANISOU 503 O MET A 84 2195 1611 1555 311 209 151 O ATOM 504 CB MET A 84 12.583 42.576 17.600 1.00 17.88 C ANISOU 504 CB MET A 84 2628 2112 2055 260 195 112 C ATOM 505 CG MET A 84 12.409 41.417 18.573 1.00 17.81 C ANISOU 505 CG MET A 84 2598 2111 2057 260 197 102 C ATOM 506 SD MET A 84 10.959 41.578 19.646 1.00 17.89 S ANISOU 506 SD MET A 84 2612 2118 2068 301 211 114 S ATOM 507 CE MET A 84 11.236 43.175 20.386 1.00 10.94 C ANISOU 507 CE MET A 84 1785 1199 1174 314 219 118 C ATOM 508 N LEU A 85 12.106 44.331 14.938 1.00 19.60 N ANISOU 508 N LEU A 85 2855 2336 2256 267 191 141 N ATOM 509 CA LEU A 85 12.262 45.611 14.251 1.00 18.98 C ANISOU 509 CA LEU A 85 2802 2243 2166 269 191 151 C ATOM 510 C LEU A 85 10.925 46.153 13.763 1.00 15.47 C ANISOU 510 C LEU A 85 2353 1807 1718 299 198 172 C ATOM 511 O LEU A 85 10.664 47.355 13.894 1.00 15.24 O ANISOU 511 O LEU A 85 2355 1757 1680 317 204 182 O ATOM 512 CB LEU A 85 13.247 45.493 13.083 1.00 18.85 C ANISOU 512 CB LEU A 85 2778 2237 2148 239 179 145 C ATOM 513 CG LEU A 85 14.727 45.439 13.457 1.00 21.65 C ANISOU 513 CG LEU A 85 3149 2576 2502 209 172 127 C ATOM 514 CD1 LEU A 85 15.562 45.335 12.211 1.00 12.41 C ANISOU 514 CD1 LEU A 85 1968 1417 1330 182 161 124 C ATOM 515 CD2 LEU A 85 15.124 46.693 14.277 1.00 17.15 C ANISOU 515 CD2 LEU A 85 2624 1969 1922 217 179 128 C ATOM 516 N LYS A 86 10.071 45.297 13.185 1.00 13.04 N ANISOU 516 N LYS A 86 2009 1529 1418 306 196 177 N ATOM 517 CA LYS A 86 8.752 45.755 12.748 1.00 24.11 C ANISOU 517 CA LYS A 86 3404 2939 2816 335 203 197 C ATOM 518 C LYS A 86 7.975 46.355 13.910 1.00 29.87 C ANISOU 518 C LYS A 86 4157 3649 3544 366 216 204 C ATOM 519 O LYS A 86 7.341 47.411 13.779 1.00 25.83 O ANISOU 519 O LYS A 86 3664 3126 3024 388 222 220 O ATOM 520 CB LYS A 86 7.941 44.611 12.142 1.00 27.52 C ANISOU 520 CB LYS A 86 3792 3406 3258 338 200 200 C ATOM 521 CG LYS A 86 8.368 44.143 10.781 1.00 31.90 C ANISOU 521 CG LYS A 86 4322 3984 3814 315 189 198 C ATOM 522 CD LYS A 86 7.606 42.876 10.435 1.00 35.75 C ANISOU 522 CD LYS A 86 4766 4505 4312 318 187 198 C ATOM 523 CE LYS A 86 8.007 42.331 9.084 1.00 43.11 C ANISOU 523 CE LYS A 86 5672 5463 5247 294 176 195 C ATOM 524 NZ LYS A 86 7.246 41.097 8.758 1.00 50.18 N ANISOU 524 NZ LYS A 86 6523 6389 6152 297 174 195 N ATOM 525 N SER A 87 7.996 45.678 15.055 1.00 20.67 N ANISOU 525 N SER A 87 2988 2481 2385 368 219 194 N ATOM 526 CA SER A 87 7.206 46.097 16.199 1.00 22.62 C ANISOU 526 CA SER A 87 3252 2712 2630 397 231 200 C ATOM 527 C SER A 87 7.832 47.260 16.967 1.00 24.52 C ANISOU 527 C SER A 87 3538 2918 2862 399 236 197 C ATOM 528 O SER A 87 7.222 47.734 17.933 1.00 27.47 O ANISOU 528 O SER A 87 3929 3275 3233 423 246 202 O ATOM 529 CB SER A 87 6.974 44.898 17.118 1.00 23.71 C ANISOU 529 CB SER A 87 3368 2861 2779 398 232 190 C ATOM 530 OG SER A 87 8.201 44.368 17.594 1.00 26.00 O ANISOU 530 OG SER A 87 3661 3144 3072 370 226 171 O ATOM 531 N SER A 88 9.011 47.745 16.552 1.00 19.65 N ANISOU 531 N SER A 88 2939 2287 2239 375 229 190 N ATOM 532 CA SER A 88 9.641 48.896 17.199 1.00 19.78 C ANISOU 532 CA SER A 88 2998 2269 2246 376 233 187 C ATOM 533 C SER A 88 8.965 50.209 16.849 1.00 19.02 C ANISOU 533 C SER A 88 2926 2160 2142 400 240 205 C ATOM 534 O SER A 88 9.211 51.211 17.525 1.00 22.07 O ANISOU 534 O SER A 88 3347 2516 2520 408 246 205 O ATOM 535 CB SER A 88 11.112 48.996 16.805 1.00 15.14 C ANISOU 535 CB SER A 88 2422 1673 1656 342 223 174 C ATOM 536 OG SER A 88 11.234 49.433 15.458 1.00 14.05 O ANISOU 536 OG SER A 88 2281 1544 1514 333 217 183 O ATOM 537 N PHE A 89 8.137 50.228 15.802 1.00 23.64 N ANISOU 537 N PHE A 89 3490 2764 2727 410 239 220 N ATOM 538 CA PHE A 89 7.534 51.441 15.263 1.00 30.57 C ANISOU 538 CA PHE A 89 4387 3632 3597 430 244 238 C ATOM 539 C PHE A 89 8.600 52.420 14.788 1.00 28.32 C ANISOU 539 C PHE A 89 4130 3326 3303 412 239 236 C ATOM 540 O PHE A 89 8.328 53.603 14.588 1.00 24.49 O ANISOU 540 O PHE A 89 3670 2824 2810 427 244 249 O ATOM 541 CB PHE A 89 6.606 52.102 16.295 1.00 31.01 C ANISOU 541 CB PHE A 89 4464 3670 3650 464 258 247 C ATOM 542 CG PHE A 89 5.378 51.291 16.593 1.00 43.84 C ANISOU 542 CG PHE A 89 6059 5316 5282 486 263 253 C ATOM 543 CD1 PHE A 89 4.254 51.380 15.786 1.00 50.39 C ANISOU 543 CD1 PHE A 89 6870 6163 6111 505 266 271 C ATOM 544 CD2 PHE A 89 5.355 50.420 17.670 1.00 52.21 C ANISOU 544 CD2 PHE A 89 7111 6379 6349 486 266 242 C ATOM 545 CE1 PHE A 89 3.125 50.619 16.055 1.00 55.27 C ANISOU 545 CE1 PHE A 89 7462 6802 6737 525 271 277 C ATOM 546 CE2 PHE A 89 4.228 49.655 17.946 1.00 55.51 C ANISOU 546 CE2 PHE A 89 7502 6816 6774 506 271 248 C ATOM 547 CZ PHE A 89 3.115 49.753 17.136 1.00 55.26 C ANISOU 547 CZ PHE A 89 7451 6802 6742 525 273 265 C ATOM 548 N ALA A 90 9.821 51.939 14.571 1.00 21.86 N ANISOU 548 N ALA A 90 3309 2510 2487 380 229 221 N ATOM 549 CA ALA A 90 10.917 52.823 14.218 1.00 23.25 C ANISOU 549 CA ALA A 90 3514 2666 2655 361 224 217 C ATOM 550 C ALA A 90 11.433 52.624 12.800 1.00 21.26 C ANISOU 550 C ALA A 90 3243 2432 2402 338 213 219 C ATOM 551 O ALA A 90 12.289 53.405 12.364 1.00 22.67 O ANISOU 551 O ALA A 90 3445 2596 2574 323 209 218 O ATOM 552 CB ALA A 90 12.064 52.655 15.224 1.00 20.84 C ANISOU 552 CB ALA A 90 3227 2341 2350 342 222 198 C ATOM 553 N THR A 91 10.917 51.640 12.050 1.00 18.38 N ANISOU 553 N THR A 91 2839 2100 2043 335 208 221 N ATOM 554 CA THR A 91 11.476 51.282 10.745 1.00 19.62 C ANISOU 554 CA THR A 91 2976 2277 2201 310 197 220 C ATOM 555 C THR A 91 10.413 51.312 9.643 1.00 22.40 C ANISOU 555 C THR A 91 3305 2653 2552 326 197 238 C ATOM 556 O THR A 91 9.203 51.283 9.906 1.00 13.43 O ANISOU 556 O THR A 91 2161 1524 1419 354 206 249 O ATOM 557 CB THR A 91 12.153 49.892 10.780 1.00 24.98 C ANISOU 557 CB THR A 91 3627 2976 2889 284 189 202 C ATOM 558 OG1 THR A 91 11.167 48.856 10.908 1.00 15.81 O ANISOU 558 OG1 THR A 91 2432 1839 1736 297 191 204 O ATOM 559 CG2 THR A 91 13.142 49.804 11.936 1.00 18.94 C ANISOU 559 CG2 THR A 91 2884 2188 2125 270 189 184 C ATOM 560 N CYS A 92 10.886 51.386 8.389 1.00 23.51 N ANISOU 560 N CYS A 92 3436 2807 2690 307 188 240 N ATOM 561 CA CYS A 92 9.990 51.395 7.229 1.00 23.92 C ANISOU 561 CA CYS A 92 3465 2883 2741 318 187 257 C ATOM 562 C CYS A 92 10.418 50.429 6.121 1.00 18.81 C ANISOU 562 C CYS A 92 2783 2267 2098 292 176 250 C ATOM 563 O CYS A 92 9.582 49.972 5.333 1.00 21.45 O ANISOU 563 O CYS A 92 3088 2628 2435 300 174 260 O ATOM 564 CB CYS A 92 9.865 52.819 6.668 1.00 22.11 C ANISOU 564 CB CYS A 92 3263 2637 2501 329 190 274 C ATOM 565 SG CYS A 92 11.425 53.633 6.215 1.00 23.74 S ANISOU 565 SG CYS A 92 3497 2822 2699 299 182 266 S ATOM 566 N VAL A 93 11.716 50.162 6.002 1.00 15.92 N ANISOU 566 N VAL A 93 2420 1896 1731 261 167 234 N ATOM 567 CA VAL A 93 12.248 49.235 5.007 1.00 17.09 C ANISOU 567 CA VAL A 93 2538 2072 1884 234 156 226 C ATOM 568 C VAL A 93 13.285 48.350 5.690 1.00 18.98 C ANISOU 568 C VAL A 93 2774 2309 2131 209 150 204 C ATOM 569 O VAL A 93 14.160 48.851 6.402 1.00 19.44 O ANISOU 569 O VAL A 93 2862 2340 2186 200 151 195 O ATOM 570 CB VAL A 93 12.878 49.972 3.805 1.00 22.49 C ANISOU 570 CB VAL A 93 3230 2756 2559 218 148 232 C ATOM 571 CG1 VAL A 93 13.426 48.975 2.780 1.00 14.23 C ANISOU 571 CG1 VAL A 93 2151 1740 1518 190 137 223 C ATOM 572 CG2 VAL A 93 11.873 50.931 3.149 1.00 23.54 C ANISOU 572 CG2 VAL A 93 3369 2891 2686 243 154 255 C ATOM 573 N LEU A 94 13.188 47.040 5.477 1.00 10.65 N ANISOU 573 N LEU A 94 1682 1280 1085 198 145 194 N ATOM 574 CA LEU A 94 14.055 46.067 6.131 1.00 17.53 C ANISOU 574 CA LEU A 94 2544 2151 1963 176 141 174 C ATOM 575 C LEU A 94 14.675 45.177 5.068 1.00 24.22 C ANISOU 575 C LEU A 94 3362 3025 2815 147 129 164 C ATOM 576 O LEU A 94 13.957 44.557 4.278 1.00 27.11 O ANISOU 576 O LEU A 94 3696 3420 3186 151 127 170 O ATOM 577 CB LEU A 94 13.296 45.221 7.155 1.00 14.64 C ANISOU 577 CB LEU A 94 2164 1792 1608 192 147 170 C ATOM 578 CG LEU A 94 12.650 46.001 8.308 1.00 24.48 C ANISOU 578 CG LEU A 94 3438 3012 2850 221 159 178 C ATOM 579 CD1 LEU A 94 11.750 45.100 9.150 1.00 23.30 C ANISOU 579 CD1 LEU A 94 3268 2873 2710 239 166 176 C ATOM 580 CD2 LEU A 94 13.703 46.689 9.171 1.00 23.36 C ANISOU 580 CD2 LEU A 94 3334 2837 2703 211 160 168 C ATOM 581 N VAL A 95 16.000 45.164 5.017 1.00 22.15 N ANISOU 581 N VAL A 95 3111 2754 2552 119 122 150 N ATOM 582 CA VAL A 95 16.757 44.313 4.114 1.00 17.50 C ANISOU 582 CA VAL A 95 2496 2187 1968 89 110 139 C ATOM 583 C VAL A 95 17.455 43.250 4.944 1.00 25.02 C ANISOU 583 C VAL A 95 3437 3139 2929 71 108 119 C ATOM 584 O VAL A 95 18.170 43.570 5.903 1.00 18.45 O ANISOU 584 O VAL A 95 2632 2281 2096 66 110 110 O ATOM 585 CB VAL A 95 17.771 45.119 3.285 1.00 14.82 C ANISOU 585 CB VAL A 95 2175 1838 1618 68 103 139 C ATOM 586 CG1 VAL A 95 18.788 44.188 2.611 1.00 17.88 C ANISOU 586 CG1 VAL A 95 2539 2244 2011 33 92 123 C ATOM 587 CG2 VAL A 95 17.046 45.947 2.235 1.00 16.73 C ANISOU 587 CG2 VAL A 95 2417 2088 1851 82 105 159 C ATOM 588 N SER A 96 17.248 41.991 4.574 1.00 21.47 N ANISOU 588 N SER A 96 2949 2718 2490 62 103 111 N ATOM 589 CA SER A 96 17.880 40.867 5.244 1.00 22.14 C ANISOU 589 CA SER A 96 3020 2806 2586 44 99 92 C ATOM 590 C SER A 96 18.612 40.007 4.233 1.00 19.63 C ANISOU 590 C SER A 96 2674 2512 2273 14 88 81 C ATOM 591 O SER A 96 18.104 39.747 3.134 1.00 24.09 O ANISOU 591 O SER A 96 3213 3101 2838 14 84 88 O ATOM 592 CB SER A 96 16.861 39.986 5.979 1.00 21.87 C ANISOU 592 CB SER A 96 2963 2784 2562 63 105 93 C ATOM 593 OG SER A 96 17.477 38.770 6.381 1.00 18.56 O ANISOU 593 OG SER A 96 2523 2373 2155 43 100 75 O ATOM 594 N GLU A 97 19.787 39.532 4.645 1.00 18.97 N ANISOU 594 N GLU A 97 2594 2421 2194 -12 82 63 N ATOM 595 CA GLU A 97 20.489 38.493 3.912 1.00 24.40 C ANISOU 595 CA GLU A 97 3252 3131 2889 -41 72 49 C ATOM 596 C GLU A 97 19.559 37.352 3.533 1.00 22.91 C ANISOU 596 C GLU A 97 3020 2973 2710 -33 71 50 C ATOM 597 O GLU A 97 19.740 36.731 2.485 1.00 19.94 O ANISOU 597 O GLU A 97 2616 2621 2337 -50 64 46 O ATOM 598 CB GLU A 97 21.651 37.972 4.762 1.00 22.06 C ANISOU 598 CB GLU A 97 2963 2821 2599 -63 69 30 C ATOM 599 CG GLU A 97 22.618 37.064 4.034 1.00 27.27 C ANISOU 599 CG GLU A 97 3598 3498 3265 -96 58 14 C ATOM 600 CD GLU A 97 22.197 35.610 4.055 1.00 30.73 C ANISOU 600 CD GLU A 97 3996 3963 3718 -99 55 6 C ATOM 601 OE1 GLU A 97 21.517 35.198 5.016 1.00 34.84 O ANISOU 601 OE1 GLU A 97 4512 4481 4246 -81 62 6 O ATOM 602 OE2 GLU A 97 22.542 34.879 3.109 1.00 39.47 O ANISOU 602 OE2 GLU A 97 5075 5093 4830 -119 47 -2 O ATOM 603 N GLU A 98 18.535 37.095 4.343 1.00 17.83 N ANISOU 603 N GLU A 98 2372 2330 2073 -8 80 56 N ATOM 604 CA GLU A 98 17.676 35.940 4.133 1.00 23.04 C ANISOU 604 CA GLU A 98 2991 3018 2744 -2 80 55 C ATOM 605 C GLU A 98 16.566 36.170 3.121 1.00 22.22 C ANISOU 605 C GLU A 98 2871 2935 2637 16 81 72 C ATOM 606 O GLU A 98 15.925 35.197 2.719 1.00 19.49 O ANISOU 606 O GLU A 98 2489 2616 2300 18 79 71 O ATOM 607 CB GLU A 98 17.043 35.505 5.459 1.00 26.99 C ANISOU 607 CB GLU A 98 3491 3510 3252 18 88 54 C ATOM 608 CG GLU A 98 18.046 34.888 6.407 1.00 39.30 C ANISOU 608 CG GLU A 98 5055 5058 4819 -2 85 36 C ATOM 609 CD GLU A 98 18.538 33.551 5.892 1.00 48.02 C ANISOU 609 CD GLU A 98 6123 6187 5937 -27 76 21 C ATOM 610 OE1 GLU A 98 17.693 32.700 5.549 1.00 49.73 O ANISOU 610 OE1 GLU A 98 6305 6428 6161 -19 76 23 O ATOM 611 OE2 GLU A 98 19.764 33.363 5.790 1.00 47.49 O ANISOU 611 OE2 GLU A 98 6061 6114 5870 -55 69 7 O ATOM 612 N ASP A 99 16.323 37.398 2.676 1.00 21.73 N ANISOU 612 N ASP A 99 2833 2863 2562 28 84 87 N ATOM 613 CA ASP A 99 15.130 37.675 1.886 1.00 24.04 C ANISOU 613 CA ASP A 99 3111 3172 2850 49 87 105 C ATOM 614 C ASP A 99 15.494 38.355 0.576 1.00 21.55 C ANISOU 614 C ASP A 99 2800 2864 2524 38 81 112 C ATOM 615 O ASP A 99 16.225 39.353 0.568 1.00 21.67 O ANISOU 615 O ASP A 99 2847 2857 2530 31 80 113 O ATOM 616 CB ASP A 99 14.140 38.525 2.690 1.00 29.92 C ANISOU 616 CB ASP A 99 3879 3899 3590 83 98 120 C ATOM 617 CG ASP A 99 13.525 37.745 3.858 1.00 36.56 C ANISOU 617 CG ASP A 99 4710 4740 4442 98 105 116 C ATOM 618 OD1 ASP A 99 12.735 36.819 3.602 1.00 38.27 O ANISOU 618 OD1 ASP A 99 4892 4982 4667 105 105 117 O ATOM 619 OD2 ASP A 99 13.823 38.058 5.030 1.00 32.49 O ANISOU 619 OD2 ASP A 99 4220 4200 3927 104 110 112 O ATOM 620 N LYS A 100 14.956 37.825 -0.531 1.00 16.76 N ANISOU 620 N LYS A 100 2161 2288 1920 36 76 116 N ATOM 621 CA LYS A 100 15.313 38.345 -1.852 1.00 15.62 C ANISOU 621 CA LYS A 100 2015 2154 1766 23 70 122 C ATOM 622 C LYS A 100 14.956 39.829 -1.985 1.00 15.31 C ANISOU 622 C LYS A 100 2009 2096 1714 42 75 141 C ATOM 623 O LYS A 100 15.755 40.621 -2.492 1.00 18.98 O ANISOU 623 O LYS A 100 2494 2549 2168 28 71 142 O ATOM 624 CB LYS A 100 14.634 37.521 -2.944 1.00 23.02 C ANISOU 624 CB LYS A 100 2910 3128 2708 21 65 125 C ATOM 625 CG LYS A 100 14.996 37.970 -4.362 1.00 26.04 C ANISOU 625 CG LYS A 100 3289 3524 3081 6 58 130 C ATOM 626 CD LYS A 100 16.483 37.746 -4.639 1.00 24.23 C ANISOU 626 CD LYS A 100 3063 3290 2851 -28 48 112 C ATOM 627 CE LYS A 100 16.891 38.329 -5.991 1.00 37.48 C ANISOU 627 CE LYS A 100 4742 4980 4519 -42 41 119 C ATOM 628 NZ LYS A 100 18.375 38.287 -6.194 1.00 37.69 N ANISOU 628 NZ LYS A 100 4779 4999 4545 -75 33 103 N ATOM 629 N HIS A 101 13.777 40.226 -1.521 1.00 14.23 N ANISOU 629 N HIS A 101 1877 1954 1575 73 85 156 N ATOM 630 CA HIS A 101 13.341 41.613 -1.590 1.00 23.92 C ANISOU 630 CA HIS A 101 3135 3164 2791 94 91 174 C ATOM 631 C HIS A 101 13.295 42.251 -0.205 1.00 19.60 C ANISOU 631 C HIS A 101 2621 2584 2242 111 100 175 C ATOM 632 O HIS A 101 13.129 41.580 0.816 1.00 16.83 O ANISOU 632 O HIS A 101 2266 2229 1901 117 104 167 O ATOM 633 CB HIS A 101 11.955 41.735 -2.227 1.00 24.20 C ANISOU 633 CB HIS A 101 3152 3219 2824 119 95 193 C ATOM 634 CG HIS A 101 11.881 41.211 -3.625 1.00 42.81 C ANISOU 634 CG HIS A 101 5477 5609 5182 105 87 194 C ATOM 635 ND1 HIS A 101 12.497 41.841 -4.686 1.00 46.40 N ANISOU 635 ND1 HIS A 101 5938 6066 5626 89 80 198 N ATOM 636 CD2 HIS A 101 11.260 40.123 -4.139 1.00 43.81 C ANISOU 636 CD2 HIS A 101 5563 5767 5316 104 84 192 C ATOM 637 CE1 HIS A 101 12.258 41.163 -5.794 1.00 47.16 C ANISOU 637 CE1 HIS A 101 6000 6194 5725 79 74 198 C ATOM 638 NE2 HIS A 101 11.509 40.117 -5.490 1.00 47.44 N ANISOU 638 NE2 HIS A 101 6007 6248 5771 88 76 194 N ATOM 639 N ALA A 102 13.416 43.577 -0.200 1.00 16.00 N ANISOU 639 N ALA A 102 2200 2105 1776 120 104 187 N ATOM 640 CA ALA A 102 13.228 44.352 1.014 1.00 21.46 C ANISOU 640 CA ALA A 102 2926 2765 2464 140 113 191 C ATOM 641 C ALA A 102 11.825 44.135 1.554 1.00 27.52 C ANISOU 641 C ALA A 102 3681 3539 3236 172 123 202 C ATOM 642 O ALA A 102 10.864 43.950 0.802 1.00 32.44 O ANISOU 642 O ALA A 102 4282 4185 3860 185 123 214 O ATOM 643 CB ALA A 102 13.451 45.841 0.742 1.00 17.52 C ANISOU 643 CB ALA A 102 2462 2243 1952 146 116 203 C ATOM 644 N ILE A 103 11.716 44.131 2.866 1.00 25.77 N ANISOU 644 N ILE A 103 3477 3298 3019 184 130 197 N ATOM 645 CA ILE A 103 10.423 44.080 3.531 1.00 21.21 C ANISOU 645 CA ILE A 103 2893 2721 2443 216 140 208 C ATOM 646 C ILE A 103 9.965 45.505 3.797 1.00 23.13 C ANISOU 646 C ILE A 103 3173 2940 2677 241 149 224 C ATOM 647 O ILE A 103 10.716 46.321 4.347 1.00 25.08 O ANISOU 647 O ILE A 103 3454 3158 2918 236 150 221 O ATOM 648 CB ILE A 103 10.490 43.258 4.833 1.00 19.05 C ANISOU 648 CB ILE A 103 2617 2441 2180 218 144 194 C ATOM 649 CG1 ILE A 103 10.522 41.746 4.542 1.00 26.54 C ANISOU 649 CG1 ILE A 103 3523 3419 3140 201 137 182 C ATOM 650 CG2 ILE A 103 9.317 43.587 5.747 1.00 25.20 C ANISOU 650 CG2 ILE A 103 3405 3211 2960 252 156 206 C ATOM 651 CD1 ILE A 103 11.766 41.226 3.873 1.00 26.57 C ANISOU 651 CD1 ILE A 103 3517 3432 3146 166 125 166 C ATOM 652 N ILE A 104 8.748 45.817 3.369 1.00 19.23 N ANISOU 652 N ILE A 104 2670 2458 2181 266 154 243 N ATOM 653 CA ILE A 104 8.155 47.128 3.582 1.00 15.08 C ANISOU 653 CA ILE A 104 2173 1910 1646 292 163 260 C ATOM 654 C ILE A 104 7.279 47.018 4.818 1.00 21.38 C ANISOU 654 C ILE A 104 2977 2699 2449 319 174 263 C ATOM 655 O ILE A 104 6.360 46.191 4.867 1.00 27.53 O ANISOU 655 O ILE A 104 3726 3498 3234 331 176 265 O ATOM 656 CB ILE A 104 7.349 47.584 2.355 1.00 18.45 C ANISOU 656 CB ILE A 104 2587 2354 2067 303 162 279 C ATOM 657 CG1 ILE A 104 8.190 47.440 1.091 1.00 24.73 C ANISOU 657 CG1 ILE A 104 3370 3165 2859 274 151 275 C ATOM 658 CG2 ILE A 104 6.825 49.010 2.532 1.00 24.14 C ANISOU 658 CG2 ILE A 104 3342 3052 2779 329 171 297 C ATOM 659 CD1 ILE A 104 9.501 48.205 1.129 1.00 29.64 C ANISOU 659 CD1 ILE A 104 4025 3763 3475 254 147 267 C ATOM 660 N VAL A 105 7.592 47.809 5.841 1.00 20.93 N ANISOU 660 N VAL A 105 2956 2609 2388 327 180 261 N ATOM 661 CA VAL A 105 6.821 47.761 7.072 1.00 18.78 C ANISOU 661 CA VAL A 105 2691 2326 2119 352 191 263 C ATOM 662 C VAL A 105 5.427 48.321 6.820 1.00 22.60 C ANISOU 662 C VAL A 105 3172 2815 2600 385 199 284 C ATOM 663 O VAL A 105 5.249 49.299 6.080 1.00 21.78 O ANISOU 663 O VAL A 105 3081 2706 2488 392 200 299 O ATOM 664 CB VAL A 105 7.556 48.519 8.193 1.00 17.12 C ANISOU 664 CB VAL A 105 2520 2079 1904 352 196 255 C ATOM 665 CG1 VAL A 105 6.754 48.500 9.483 1.00 19.02 C ANISOU 665 CG1 VAL A 105 2770 2309 2149 379 207 257 C ATOM 666 CG2 VAL A 105 8.920 47.900 8.424 1.00 18.50 C ANISOU 666 CG2 VAL A 105 2696 2251 2083 319 187 233 C ATOM 667 N GLU A 106 4.426 47.679 7.414 1.00 27.35 N ANISOU 667 N GLU A 106 3755 3427 3208 406 206 287 N ATOM 668 CA GLU A 106 3.044 48.089 7.234 1.00 32.99 C ANISOU 668 CA GLU A 106 4464 4149 3920 438 214 307 C ATOM 669 C GLU A 106 2.822 49.491 7.799 1.00 35.52 C ANISOU 669 C GLU A 106 4825 4438 4233 459 223 318 C ATOM 670 O GLU A 106 3.535 49.925 8.710 1.00 35.24 O ANISOU 670 O GLU A 106 4819 4375 4195 455 226 309 O ATOM 671 CB GLU A 106 2.103 47.070 7.883 1.00 36.09 C ANISOU 671 CB GLU A 106 4831 4558 4323 453 219 306 C ATOM 672 CG GLU A 106 2.445 46.678 9.300 1.00 48.80 C ANISOU 672 CG GLU A 106 6452 6151 5938 453 223 292 C ATOM 673 CD GLU A 106 1.537 45.573 9.809 1.00 68.59 C ANISOU 673 CD GLU A 106 8929 8678 8455 467 226 291 C ATOM 674 OE1 GLU A 106 0.635 45.153 9.052 1.00 75.29 O ANISOU 674 OE1 GLU A 106 9748 9553 9307 476 226 302 O ATOM 675 OE2 GLU A 106 1.735 45.103 10.949 1.00 73.80 O ANISOU 675 OE2 GLU A 106 9592 9328 9120 467 230 279 O ATOM 676 N PRO A 107 1.862 50.237 7.240 1.00 34.61 N ANISOU 676 N PRO A 107 4712 4326 4112 483 228 339 N ATOM 677 CA PRO A 107 1.757 51.670 7.571 1.00 25.25 C ANISOU 677 CA PRO A 107 3565 3109 2918 500 236 350 C ATOM 678 C PRO A 107 1.632 51.964 9.052 1.00 30.96 C ANISOU 678 C PRO A 107 4315 3808 3643 517 246 345 C ATOM 679 O PRO A 107 2.292 52.888 9.547 1.00 30.90 O ANISOU 679 O PRO A 107 4343 3770 3629 515 249 342 O ATOM 680 CB PRO A 107 0.496 52.104 6.808 1.00 31.79 C ANISOU 680 CB PRO A 107 4382 3952 3743 526 241 373 C ATOM 681 CG PRO A 107 0.385 51.130 5.676 1.00 28.97 C ANISOU 681 CG PRO A 107 3986 3632 3391 510 231 373 C ATOM 682 CD PRO A 107 0.880 49.825 6.219 1.00 31.16 C ANISOU 682 CD PRO A 107 4243 3920 3678 492 227 352 C ATOM 683 N GLU A 108 0.831 51.185 9.787 1.00 34.74 N ANISOU 683 N GLU A 108 4776 4297 4129 533 252 344 N ATOM 684 CA GLU A 108 0.585 51.508 11.187 1.00 35.81 C ANISOU 684 CA GLU A 108 4934 4408 4264 552 262 341 C ATOM 685 C GLU A 108 1.828 51.336 12.049 1.00 42.13 C ANISOU 685 C GLU A 108 5753 5189 5065 530 259 320 C ATOM 686 O GLU A 108 1.862 51.855 13.170 1.00 41.47 O ANISOU 686 O GLU A 108 5697 5080 4979 542 267 317 O ATOM 687 CB GLU A 108 -0.553 50.645 11.746 1.00 41.04 C ANISOU 687 CB GLU A 108 5571 5088 4934 573 268 344 C ATOM 688 CG GLU A 108 -0.338 49.130 11.638 1.00 53.88 C ANISOU 688 CG GLU A 108 7160 6742 6571 554 260 331 C ATOM 689 CD GLU A 108 -0.743 48.548 10.282 1.00 68.72 C ANISOU 689 CD GLU A 108 9003 8654 8452 547 253 338 C ATOM 690 OE1 GLU A 108 -0.908 49.318 9.308 1.00 72.39 O ANISOU 690 OE1 GLU A 108 9474 9121 8911 550 252 352 O ATOM 691 OE2 GLU A 108 -0.895 47.310 10.193 1.00 70.54 O ANISOU 691 OE2 GLU A 108 9200 8909 8692 538 248 331 O ATOM 692 N LYS A 109 2.843 50.621 11.561 1.00 40.80 N ANISOU 692 N LYS A 109 5570 5032 4899 498 248 306 N ATOM 693 CA LYS A 109 4.064 50.402 12.324 1.00 38.96 C ANISOU 693 CA LYS A 109 5353 4782 4667 475 244 286 C ATOM 694 C LYS A 109 5.277 51.093 11.718 1.00 33.61 C ANISOU 694 C LYS A 109 4697 4090 3983 450 237 281 C ATOM 695 O LYS A 109 6.406 50.816 12.138 1.00 29.98 O ANISOU 695 O LYS A 109 4247 3621 3525 427 232 264 O ATOM 696 CB LYS A 109 4.336 48.909 12.459 1.00 40.72 C ANISOU 696 CB LYS A 109 5543 5028 4901 457 238 271 C ATOM 697 CG LYS A 109 3.252 48.171 13.201 1.00 44.55 C ANISOU 697 CG LYS A 109 6008 5525 5393 479 245 274 C ATOM 698 CD LYS A 109 3.565 46.695 13.222 1.00 48.06 C ANISOU 698 CD LYS A 109 6418 5993 5848 459 238 259 C ATOM 699 CE LYS A 109 2.437 45.916 13.843 1.00 52.53 C ANISOU 699 CE LYS A 109 6962 6575 6423 481 244 263 C ATOM 700 NZ LYS A 109 2.738 44.457 13.783 1.00 49.45 N ANISOU 700 NZ LYS A 109 6537 6208 6044 461 237 250 N ATOM 701 N ARG A 110 5.076 51.988 10.755 1.00 28.48 N ANISOU 701 N ARG A 110 4056 3440 3327 456 236 296 N ATOM 702 CA ARG A 110 6.190 52.575 10.027 1.00 29.38 C ANISOU 702 CA ARG A 110 4185 3543 3433 431 228 292 C ATOM 703 C ARG A 110 6.878 53.667 10.834 1.00 29.21 C ANISOU 703 C ARG A 110 4208 3484 3406 432 233 288 C ATOM 704 O ARG A 110 6.238 54.621 11.285 1.00 24.91 O ANISOU 704 O ARG A 110 3688 2921 2857 458 242 300 O ATOM 705 CB ARG A 110 5.721 53.151 8.693 1.00 31.78 C ANISOU 705 CB ARG A 110 4482 3859 3732 437 226 310 C ATOM 706 CG ARG A 110 5.894 52.213 7.541 1.00 39.22 C ANISOU 706 CG ARG A 110 5388 4835 4679 416 215 308 C ATOM 707 CD ARG A 110 5.323 52.794 6.266 1.00 33.92 C ANISOU 707 CD ARG A 110 4710 4177 4003 424 213 327 C ATOM 708 NE ARG A 110 4.900 51.717 5.383 1.00 32.87 N ANISOU 708 NE ARG A 110 4534 4081 3875 416 207 327 N ATOM 709 CZ ARG A 110 4.164 51.888 4.296 1.00 31.82 C ANISOU 709 CZ ARG A 110 4384 3968 3740 425 206 344 C ATOM 710 NH1 ARG A 110 3.765 53.102 3.952 1.00 31.24 N ANISOU 710 NH1 ARG A 110 4331 3880 3658 442 211 361 N ATOM 711 NH2 ARG A 110 3.824 50.841 3.561 1.00 34.47 N ANISOU 711 NH2 ARG A 110 4680 4337 4081 417 200 342 N ATOM 712 N GLY A 111 8.199 53.543 10.961 1.00 21.81 N ANISOU 712 N GLY A 111 3283 2537 2468 403 225 272 N ATOM 713 CA GLY A 111 9.047 54.607 11.437 1.00 21.92 C ANISOU 713 CA GLY A 111 3337 2517 2474 397 227 268 C ATOM 714 C GLY A 111 9.955 55.101 10.325 1.00 26.73 C ANISOU 714 C GLY A 111 3953 3126 3078 374 217 269 C ATOM 715 O GLY A 111 9.766 54.792 9.148 1.00 31.11 O ANISOU 715 O GLY A 111 4483 3704 3633 367 211 276 O ATOM 716 N LYS A 112 10.968 55.867 10.717 1.00 23.24 N ANISOU 716 N LYS A 112 3544 2655 2630 361 216 261 N ATOM 717 CA LYS A 112 11.735 56.612 9.731 1.00 26.57 C ANISOU 717 CA LYS A 112 3979 3071 3045 344 209 265 C ATOM 718 C LYS A 112 13.027 55.929 9.300 1.00 25.83 C ANISOU 718 C LYS A 112 3876 2987 2954 307 197 248 C ATOM 719 O LYS A 112 13.736 56.481 8.451 1.00 25.27 O ANISOU 719 O LYS A 112 3814 2912 2877 290 190 251 O ATOM 720 CB LYS A 112 12.052 58.019 10.247 1.00 28.11 C ANISOU 720 CB LYS A 112 4219 3229 3233 353 215 269 C ATOM 721 CG LYS A 112 12.948 58.060 11.472 1.00 41.87 C ANISOU 721 CG LYS A 112 5987 4947 4975 342 217 251 C ATOM 722 CD LYS A 112 13.149 59.497 11.964 1.00 54.96 C ANISOU 722 CD LYS A 112 7689 6569 6626 354 224 257 C ATOM 723 CE LYS A 112 13.909 59.525 13.289 1.00 62.37 C ANISOU 723 CE LYS A 112 8652 7482 7564 347 226 240 C ATOM 724 NZ LYS A 112 14.154 60.900 13.802 1.00 62.20 N ANISOU 724 NZ LYS A 112 8673 7424 7535 357 233 243 N ATOM 725 N TYR A 113 13.353 54.758 9.841 1.00 27.11 N ANISOU 725 N TYR A 113 4018 3159 3122 293 194 232 N ATOM 726 CA TYR A 113 14.664 54.153 9.631 1.00 22.90 C ANISOU 726 CA TYR A 113 3479 2631 2592 258 183 215 C ATOM 727 C TYR A 113 14.631 52.950 8.687 1.00 18.53 C ANISOU 727 C TYR A 113 2882 2113 2044 242 174 211 C ATOM 728 O TYR A 113 13.643 52.217 8.602 1.00 23.19 O ANISOU 728 O TYR A 113 3445 2726 2641 256 177 216 O ATOM 729 CB TYR A 113 15.285 53.738 10.963 1.00 16.10 C ANISOU 729 CB TYR A 113 2630 1753 1734 250 185 197 C ATOM 730 CG TYR A 113 15.707 54.908 11.805 1.00 21.16 C ANISOU 730 CG TYR A 113 3315 2357 2368 257 191 196 C ATOM 731 CD1 TYR A 113 16.837 55.648 11.480 1.00 20.08 C ANISOU 731 CD1 TYR A 113 3203 2202 2224 236 186 192 C ATOM 732 CD2 TYR A 113 14.976 55.272 12.930 1.00 20.64 C ANISOU 732 CD2 TYR A 113 3266 2275 2302 284 203 199 C ATOM 733 CE1 TYR A 113 17.228 56.727 12.252 1.00 20.76 C ANISOU 733 CE1 TYR A 113 3330 2254 2304 242 191 191 C ATOM 734 CE2 TYR A 113 15.350 56.341 13.703 1.00 20.50 C ANISOU 734 CE2 TYR A 113 3289 2224 2278 290 208 198 C ATOM 735 CZ TYR A 113 16.476 57.069 13.363 1.00 21.68 C ANISOU 735 CZ TYR A 113 3462 2355 2421 270 203 194 C ATOM 736 OH TYR A 113 16.842 58.133 14.146 1.00 20.27 O ANISOU 736 OH TYR A 113 3323 2142 2236 276 208 193 O ATOM 737 N VAL A 114 15.747 52.757 7.988 1.00 24.13 N ANISOU 737 N VAL A 114 3588 2827 2752 211 164 202 N ATOM 738 CA VAL A 114 15.989 51.620 7.103 1.00 22.69 C ANISOU 738 CA VAL A 114 3368 2676 2576 189 154 195 C ATOM 739 C VAL A 114 17.054 50.763 7.762 1.00 16.86 C ANISOU 739 C VAL A 114 2627 1935 1843 164 148 173 C ATOM 740 O VAL A 114 18.098 51.286 8.169 1.00 21.24 O ANISOU 740 O VAL A 114 3210 2467 2394 149 146 164 O ATOM 741 CB VAL A 114 16.465 52.087 5.712 1.00 23.55 C ANISOU 741 CB VAL A 114 3476 2795 2679 173 146 201 C ATOM 742 CG1 VAL A 114 16.794 50.896 4.812 1.00 18.35 C ANISOU 742 CG1 VAL A 114 2778 2168 2026 149 135 193 C ATOM 743 CG2 VAL A 114 15.416 52.956 5.046 1.00 19.50 C ANISOU 743 CG2 VAL A 114 2965 2283 2159 198 151 224 C ATOM 744 N VAL A 115 16.802 49.456 7.886 1.00 15.76 N ANISOU 744 N VAL A 115 2453 1819 1714 159 146 164 N ATOM 745 CA VAL A 115 17.758 48.554 8.524 1.00 19.11 C ANISOU 745 CA VAL A 115 2873 2244 2145 135 141 143 C ATOM 746 C VAL A 115 18.134 47.436 7.559 1.00 12.48 C ANISOU 746 C VAL A 115 1995 1434 1312 111 130 135 C ATOM 747 O VAL A 115 17.259 46.772 6.996 1.00 15.82 O ANISOU 747 O VAL A 115 2386 1884 1739 120 130 141 O ATOM 748 CB VAL A 115 17.224 47.969 9.847 1.00 18.98 C ANISOU 748 CB VAL A 115 2853 2223 2136 151 149 138 C ATOM 749 CG1 VAL A 115 18.338 47.210 10.555 1.00 17.22 C ANISOU 749 CG1 VAL A 115 2630 1995 1919 126 144 117 C ATOM 750 CG2 VAL A 115 16.700 49.067 10.746 1.00 16.81 C ANISOU 750 CG2 VAL A 115 2612 1919 1854 178 160 147 C ATOM 751 N CYS A 116 19.436 47.252 7.357 1.00 14.66 N ANISOU 751 N CYS A 116 2276 1706 1587 80 122 121 N ATOM 752 CA CYS A 116 19.997 46.119 6.638 1.00 12.18 C ANISOU 752 CA CYS A 116 1930 1419 1281 53 111 109 C ATOM 753 C CYS A 116 20.729 45.239 7.639 1.00 8.91 C ANISOU 753 C CYS A 116 1512 999 875 38 110 90 C ATOM 754 O CYS A 116 21.547 45.735 8.421 1.00 19.75 O ANISOU 754 O CYS A 116 2915 2346 2244 30 111 82 O ATOM 755 CB CYS A 116 20.973 46.572 5.540 1.00 15.25 C ANISOU 755 CB CYS A 116 2323 1808 1662 28 102 108 C ATOM 756 SG CYS A 116 20.361 47.897 4.453 1.00 22.14 S ANISOU 756 SG CYS A 116 3210 2679 2523 45 104 131 S ATOM 757 N PHE A 117 20.453 43.942 7.610 1.00 12.93 N ANISOU 757 N PHE A 117 1985 1533 1395 32 107 82 N ATOM 758 CA PHE A 117 21.076 43.073 8.588 1.00 12.73 C ANISOU 758 CA PHE A 117 1955 1503 1378 19 106 64 C ATOM 759 C PHE A 117 21.313 41.693 8.007 1.00 16.37 C ANISOU 759 C PHE A 117 2376 1994 1851 -2 97 53 C ATOM 760 O PHE A 117 20.619 41.249 7.086 1.00 15.79 O ANISOU 760 O PHE A 117 2273 1946 1779 3 95 60 O ATOM 761 CB PHE A 117 20.233 42.985 9.867 1.00 7.37 C ANISOU 761 CB PHE A 117 1282 814 703 45 116 67 C ATOM 762 CG PHE A 117 18.842 42.451 9.642 1.00 14.73 C ANISOU 762 CG PHE A 117 2185 1769 1641 69 121 78 C ATOM 763 CD1 PHE A 117 18.581 41.094 9.762 1.00 21.75 C ANISOU 763 CD1 PHE A 117 3039 2682 2543 64 119 70 C ATOM 764 CD2 PHE A 117 17.793 43.314 9.324 1.00 16.14 C ANISOU 764 CD2 PHE A 117 2373 1946 1813 96 128 97 C ATOM 765 CE1 PHE A 117 17.301 40.591 9.566 1.00 16.48 C ANISOU 765 CE1 PHE A 117 2346 2036 1882 85 123 80 C ATOM 766 CE2 PHE A 117 16.515 42.831 9.127 1.00 14.24 C ANISOU 766 CE2 PHE A 117 2106 1727 1577 118 132 108 C ATOM 767 CZ PHE A 117 16.268 41.454 9.247 1.00 14.69 C ANISOU 767 CZ PHE A 117 2128 1808 1647 112 129 99 C ATOM 768 N ASP A 118 22.318 41.031 8.576 1.00 15.72 N ANISOU 768 N ASP A 118 2292 1907 1774 -24 93 35 N ATOM 769 CA ASP A 118 22.629 39.622 8.389 1.00 18.67 C ANISOU 769 CA ASP A 118 2629 2303 2160 -44 86 22 C ATOM 770 C ASP A 118 22.348 38.946 9.727 1.00 18.29 C ANISOU 770 C ASP A 118 2578 2250 2122 -34 92 15 C ATOM 771 O ASP A 118 23.113 39.137 10.684 1.00 16.64 O ANISOU 771 O ASP A 118 2392 2018 1911 -42 93 5 O ATOM 772 CB ASP A 118 24.097 39.456 7.991 1.00 18.61 C ANISOU 772 CB ASP A 118 2626 2293 2152 -79 76 7 C ATOM 773 CG ASP A 118 24.383 38.135 7.326 1.00 28.06 C ANISOU 773 CG ASP A 118 3782 3519 3360 -101 67 -5 C ATOM 774 OD1 ASP A 118 23.809 37.113 7.747 1.00 33.47 O ANISOU 774 OD1 ASP A 118 4441 4219 4057 -94 69 -9 O ATOM 775 OD2 ASP A 118 25.189 38.127 6.373 1.00 36.34 O ANISOU 775 OD2 ASP A 118 4827 4576 4407 -124 59 -10 O ATOM 776 N PRO A 119 21.246 38.202 9.869 1.00 16.88 N ANISOU 776 N PRO A 119 2372 2090 1951 -16 96 19 N ATOM 777 CA PRO A 119 20.812 37.801 11.221 1.00 10.18 C ANISOU 777 CA PRO A 119 1526 1233 1109 -1 103 16 C ATOM 778 C PRO A 119 21.704 36.773 11.893 1.00 11.99 C ANISOU 778 C PRO A 119 1744 1463 1349 -23 99 -3 C ATOM 779 O PRO A 119 21.828 36.802 13.123 1.00 13.13 O ANISOU 779 O PRO A 119 1905 1589 1494 -17 104 -7 O ATOM 780 CB PRO A 119 19.395 37.248 10.991 1.00 9.61 C ANISOU 780 CB PRO A 119 1424 1184 1043 23 108 27 C ATOM 781 CG PRO A 119 19.377 36.846 9.528 1.00 11.08 C ANISOU 781 CG PRO A 119 1582 1397 1231 10 100 29 C ATOM 782 CD PRO A 119 20.268 37.830 8.830 1.00 14.94 C ANISOU 782 CD PRO A 119 2096 1873 1708 -6 95 30 C ATOM 783 N LEU A 120 22.306 35.842 11.158 1.00 12.71 N ANISOU 783 N LEU A 120 1808 1574 1448 -49 89 -13 N ATOM 784 CA LEU A 120 23.215 34.885 11.792 1.00 17.20 C ANISOU 784 CA LEU A 120 2366 2142 2026 -71 85 -32 C ATOM 785 C LEU A 120 24.357 34.603 10.816 1.00 21.46 C ANISOU 785 C LEU A 120 2897 2690 2567 -104 73 -42 C ATOM 786 O LEU A 120 24.504 33.509 10.279 1.00 24.46 O ANISOU 786 O LEU A 120 3242 3093 2957 -120 67 -51 O ATOM 787 CB LEU A 120 22.502 33.598 12.209 1.00 13.47 C ANISOU 787 CB LEU A 120 1859 1689 1569 -64 86 -35 C ATOM 788 CG LEU A 120 23.203 32.800 13.320 1.00 14.18 C ANISOU 788 CG LEU A 120 1947 1773 1669 -78 85 -51 C ATOM 789 CD1 LEU A 120 23.367 33.645 14.591 1.00 15.64 C ANISOU 789 CD1 LEU A 120 2170 1926 1846 -66 93 -49 C ATOM 790 CD2 LEU A 120 22.472 31.510 13.619 1.00 17.63 C ANISOU 790 CD2 LEU A 120 2347 2231 2121 -71 87 -53 C ATOM 791 N ASP A 121 25.188 35.615 10.631 1.00 13.73 N ANISOU 791 N ASP A 121 1949 1691 1576 -115 71 -42 N ATOM 792 CA ASP A 121 26.377 35.514 9.804 1.00 14.37 C ANISOU 792 CA ASP A 121 2028 1777 1656 -146 61 -53 C ATOM 793 C ASP A 121 27.276 34.385 10.296 1.00 21.05 C ANISOU 793 C ASP A 121 2858 2627 2514 -171 55 -71 C ATOM 794 O ASP A 121 27.531 34.253 11.499 1.00 18.04 O ANISOU 794 O ASP A 121 2489 2228 2135 -169 59 -78 O ATOM 795 CB ASP A 121 27.134 36.840 9.885 1.00 20.41 C ANISOU 795 CB ASP A 121 2835 2513 2407 -151 61 -50 C ATOM 796 CG ASP A 121 28.028 37.069 8.707 1.00 34.53 C ANISOU 796 CG ASP A 121 4622 4307 4189 -176 52 -53 C ATOM 797 OD1 ASP A 121 27.586 37.809 7.793 1.00 32.20 O ANISOU 797 OD1 ASP A 121 4332 4018 3887 -167 52 -40 O ATOM 798 OD2 ASP A 121 29.143 36.494 8.681 1.00 32.56 O ANISOU 798 OD2 ASP A 121 4367 4059 3945 -204 44 -69 O ATOM 799 N GLY A 122 27.768 33.576 9.362 1.00 18.20 N ANISOU 799 N GLY A 122 2468 2287 2159 -194 46 -80 N ATOM 800 CA GLY A 122 28.637 32.475 9.712 1.00 12.28 C ANISOU 800 CA GLY A 122 1701 1542 1421 -219 40 -98 C ATOM 801 C GLY A 122 27.914 31.202 10.080 1.00 22.85 C ANISOU 801 C GLY A 122 3004 2901 2775 -211 42 -102 C ATOM 802 O GLY A 122 28.574 30.217 10.432 1.00 23.53 O ANISOU 802 O GLY A 122 3074 2993 2873 -231 38 -116 O ATOM 803 N SER A 123 26.575 31.196 10.032 1.00 26.13 N ANISOU 803 N SER A 123 3479 3398 3051 274 196 53 N ATOM 804 CA SER A 123 25.809 30.056 10.522 1.00 25.99 C ANISOU 804 CA SER A 123 3443 3379 3055 283 198 38 C ATOM 805 C SER A 123 25.972 28.811 9.659 1.00 23.11 C ANISOU 805 C SER A 123 3057 3029 2695 282 206 20 C ATOM 806 O SER A 123 25.667 27.714 10.133 1.00 26.48 O ANISOU 806 O SER A 123 3466 3454 3142 286 210 8 O ATOM 807 CB SER A 123 24.321 30.400 10.607 1.00 23.19 C ANISOU 807 CB SER A 123 3094 3019 2698 298 187 35 C ATOM 808 OG SER A 123 23.774 30.636 9.319 1.00 28.51 O ANISOU 808 OG SER A 123 3773 3706 3353 303 182 29 O ATOM 809 N SER A 124 26.450 28.945 8.418 1.00 22.14 N ANISOU 809 N SER A 124 2937 2920 2555 277 208 19 N ATOM 810 CA SER A 124 26.561 27.771 7.550 1.00 37.19 C ANISOU 810 CA SER A 124 4824 4841 4466 276 215 1 C ATOM 811 C SER A 124 27.486 26.708 8.125 1.00 33.09 C ANISOU 811 C SER A 124 4285 4320 3966 268 226 -4 C ATOM 812 O SER A 124 27.333 25.526 7.803 1.00 36.88 O ANISOU 812 O SER A 124 4747 4809 4458 271 232 -20 O ATOM 813 CB SER A 124 27.040 28.184 6.157 1.00 50.87 C ANISOU 813 CB SER A 124 6563 6589 6175 270 215 3 C ATOM 814 OG SER A 124 28.435 28.427 6.152 1.00 56.04 O ANISOU 814 OG SER A 124 7221 7245 6825 256 223 12 O ATOM 815 N ASN A 125 28.409 27.093 9.003 1.00 36.83 N ANISOU 815 N ASN A 125 4766 4784 4445 258 230 10 N ATOM 816 CA ASN A 125 29.319 26.159 9.648 1.00 38.65 C ANISOU 816 CA ASN A 125 4980 5012 4695 250 241 6 C ATOM 817 C ASN A 125 29.046 26.030 11.147 1.00 38.86 C ANISOU 817 C ASN A 125 5003 5021 4741 253 240 10 C ATOM 818 O ASN A 125 29.920 25.580 11.896 1.00 43.22 O ANISOU 818 O ASN A 125 5547 5568 5308 245 248 13 O ATOM 819 CB ASN A 125 30.770 26.588 9.405 1.00 40.83 C ANISOU 819 CB ASN A 125 5261 5291 4961 235 248 18 C ATOM 820 CG ASN A 125 31.159 26.541 7.931 1.00 42.09 C ANISOU 820 CG ASN A 125 5420 5468 5103 230 250 12 C ATOM 821 OD1 ASN A 125 31.709 27.501 7.396 1.00 44.95 O ANISOU 821 OD1 ASN A 125 5799 5834 5445 223 248 24 O ATOM 822 ND2 ASN A 125 30.852 25.429 7.267 1.00 42.41 N ANISOU 822 ND2 ASN A 125 5443 5520 5150 234 254 -6 N ATOM 823 N ILE A 126 27.846 26.410 11.602 1.00 31.85 N ANISOU 823 N ILE A 126 4122 4125 3855 265 231 11 N ATOM 824 CA ILE A 126 27.547 26.378 13.030 1.00 25.73 C ANISOU 824 CA ILE A 126 3346 3333 3097 269 229 15 C ATOM 825 C ILE A 126 27.519 24.971 13.599 1.00 23.38 C ANISOU 825 C ILE A 126 3025 3034 2825 270 236 1 C ATOM 826 O ILE A 126 27.533 24.813 14.822 1.00 24.52 O ANISOU 826 O ILE A 126 3166 3165 2986 270 237 5 O ATOM 827 CB ILE A 126 26.214 27.095 13.335 1.00 28.16 C ANISOU 827 CB ILE A 126 3666 3632 3400 282 217 18 C ATOM 828 CG1 ILE A 126 26.206 27.588 14.788 1.00 21.94 C ANISOU 828 CG1 ILE A 126 2887 2826 2624 281 215 30 C ATOM 829 CG2 ILE A 126 25.024 26.188 13.040 1.00 24.69 C ANISOU 829 CG2 ILE A 126 3213 3199 2970 295 215 0 C ATOM 830 CD1 ILE A 126 25.069 28.500 15.115 1.00 26.11 C ANISOU 830 CD1 ILE A 126 3430 3345 3145 292 203 36 C ATOM 831 N ASP A 127 27.482 23.946 12.741 1.00 24.21 N ANISOU 831 N ASP A 127 3113 3152 2933 272 241 -15 N ATOM 832 CA ASP A 127 27.544 22.566 13.205 1.00 29.94 C ANISOU 832 CA ASP A 127 3816 3878 3682 272 249 -29 C ATOM 833 C ASP A 127 28.863 22.230 13.894 1.00 22.46 C ANISOU 833 C ASP A 127 2862 2926 2747 259 259 -22 C ATOM 834 O ASP A 127 28.916 21.247 14.638 1.00 27.83 O ANISOU 834 O ASP A 127 3525 3601 3449 259 264 -30 O ATOM 835 CB ASP A 127 27.304 21.611 12.036 1.00 45.42 C ANISOU 835 CB ASP A 127 5760 5855 5641 276 253 -47 C ATOM 836 CG ASP A 127 25.853 21.589 11.590 1.00 57.48 C ANISOU 836 CG ASP A 127 7288 7386 7164 290 244 -56 C ATOM 837 OD1 ASP A 127 24.959 21.592 12.464 1.00 60.56 O ANISOU 837 OD1 ASP A 127 7679 7765 7566 299 238 -57 O ATOM 838 OD2 ASP A 127 25.608 21.579 10.366 1.00 62.17 O ANISOU 838 OD2 ASP A 127 7884 7995 7745 293 242 -64 O ATOM 839 N CYS A 128 29.930 23.001 13.661 1.00 15.40 N ANISOU 839 N CYS A 128 1979 2032 1838 247 261 -9 N ATOM 840 CA CYS A 128 31.170 22.823 14.402 1.00 11.94 C ANISOU 840 CA CYS A 128 1537 1588 1411 235 270 -1 C ATOM 841 C CYS A 128 31.332 23.842 15.530 1.00 18.75 C ANISOU 841 C CYS A 128 2416 2434 2273 232 266 17 C ATOM 842 O CYS A 128 32.403 23.909 16.140 1.00 21.66 O ANISOU 842 O CYS A 128 2786 2797 2648 221 272 26 O ATOM 843 CB CYS A 128 32.373 22.880 13.458 1.00 21.13 C ANISOU 843 CB CYS A 128 2701 2764 2562 223 277 1 C ATOM 844 SG CYS A 128 32.726 24.538 12.867 1.00 24.38 S ANISOU 844 SG CYS A 128 3141 3177 2945 217 271 20 S ATOM 845 N LEU A 129 30.274 24.593 15.847 1.00 16.22 N ANISOU 845 N LEU A 129 2110 2106 1948 242 255 22 N ATOM 846 CA LEU A 129 30.230 25.514 16.980 1.00 18.15 C ANISOU 846 CA LEU A 129 2368 2334 2193 242 250 38 C ATOM 847 C LEU A 129 31.171 26.699 16.815 1.00 17.84 C ANISOU 847 C LEU A 129 2348 2293 2136 231 250 56 C ATOM 848 O LEU A 129 31.628 27.267 17.808 1.00 18.96 O ANISOU 848 O LEU A 129 2499 2422 2281 226 250 70 O ATOM 849 CB LEU A 129 30.545 24.782 18.289 1.00 10.91 C ANISOU 849 CB LEU A 129 1439 1405 1301 239 256 37 C ATOM 850 CG LEU A 129 29.708 23.535 18.510 1.00 17.35 C ANISOU 850 CG LEU A 129 2234 2221 2136 249 257 19 C ATOM 851 CD1 LEU A 129 30.058 22.936 19.860 1.00 12.42 C ANISOU 851 CD1 LEU A 129 1599 1584 1536 245 262 21 C ATOM 852 CD2 LEU A 129 28.231 23.872 18.414 1.00 11.11 C ANISOU 852 CD2 LEU A 129 1450 1429 1341 263 247 15 C ATOM 853 N VAL A 130 31.462 27.066 15.563 1.00 12.85 N ANISOU 853 N VAL A 130 1724 1675 1485 228 250 56 N ATOM 854 CA VAL A 130 32.223 28.270 15.276 1.00 19.93 C ANISOU 854 CA VAL A 130 2640 2572 2362 219 248 73 C ATOM 855 C VAL A 130 31.457 29.486 15.787 1.00 18.92 C ANISOU 855 C VAL A 130 2533 2432 2225 226 237 85 C ATOM 856 O VAL A 130 30.221 29.487 15.854 1.00 18.07 O ANISOU 856 O VAL A 130 2426 2322 2119 238 229 79 O ATOM 857 CB VAL A 130 32.501 28.384 13.764 1.00 24.70 C ANISOU 857 CB VAL A 130 3246 3193 2946 216 249 68 C ATOM 858 CG1 VAL A 130 31.198 28.560 12.954 1.00 23.20 C ANISOU 858 CG1 VAL A 130 3060 3010 2744 229 240 60 C ATOM 859 CG2 VAL A 130 33.435 29.534 13.472 1.00 19.54 C ANISOU 859 CG2 VAL A 130 2612 2540 2273 205 249 85 C ATOM 860 N SER A 131 32.202 30.519 16.192 1.00 24.71 N ANISOU 860 N SER A 131 3282 3157 2948 217 236 103 N ATOM 861 CA SER A 131 31.599 31.813 16.492 1.00 16.51 C ANISOU 861 CA SER A 131 2265 2110 1896 222 226 116 C ATOM 862 C SER A 131 30.728 32.265 15.321 1.00 18.70 C ANISOU 862 C SER A 131 2552 2398 2155 231 218 112 C ATOM 863 O SER A 131 31.123 32.150 14.164 1.00 19.94 O ANISOU 863 O SER A 131 2708 2570 2300 227 220 107 O ATOM 864 CB SER A 131 32.695 32.846 16.761 1.00 19.91 C ANISOU 864 CB SER A 131 2713 2535 2316 210 227 136 C ATOM 865 OG SER A 131 33.494 32.476 17.879 1.00 24.60 O ANISOU 865 OG SER A 131 3300 3119 2928 202 234 141 O ATOM 866 N VAL A 132 29.547 32.798 15.626 1.00 11.11 N ANISOU 866 N VAL A 132 1600 1430 1192 242 208 113 N ATOM 867 CA VAL A 132 28.663 33.398 14.638 1.00 13.04 C ANISOU 867 CA VAL A 132 1856 1682 1418 251 198 111 C ATOM 868 C VAL A 132 28.254 34.773 15.154 1.00 12.91 C ANISOU 868 C VAL A 132 1861 1653 1390 254 189 127 C ATOM 869 O VAL A 132 28.637 35.177 16.248 1.00 13.02 O ANISOU 869 O VAL A 132 1881 1653 1411 249 189 139 O ATOM 870 CB VAL A 132 27.428 32.524 14.357 1.00 14.07 C ANISOU 870 CB VAL A 132 1972 1818 1558 264 196 93 C ATOM 871 CG1 VAL A 132 27.856 31.235 13.652 1.00 15.18 C ANISOU 871 CG1 VAL A 132 2091 1972 1706 261 205 77 C ATOM 872 CG2 VAL A 132 26.684 32.228 15.666 1.00 12.98 C ANISOU 872 CG2 VAL A 132 1828 1664 1439 272 193 91 C ATOM 873 N GLY A 133 27.489 35.501 14.348 1.00 14.22 N ANISOU 873 N GLY A 133 2040 1824 1538 261 180 128 N ATOM 874 CA GLY A 133 27.137 36.851 14.738 1.00 9.59 C ANISOU 874 CA GLY A 133 1476 1227 940 263 170 143 C ATOM 875 C GLY A 133 25.963 37.407 13.967 1.00 19.41 C ANISOU 875 C GLY A 133 2730 2476 2169 275 159 140 C ATOM 876 O GLY A 133 25.485 36.822 12.993 1.00 18.46 O ANISOU 876 O GLY A 133 2601 2369 2045 280 159 127 O ATOM 877 N THR A 134 25.501 38.562 14.441 1.00 15.47 N ANISOU 877 N THR A 134 2250 1966 1661 279 150 153 N ATOM 878 CA THR A 134 24.456 39.353 13.807 1.00 10.23 C ANISOU 878 CA THR A 134 1600 1305 981 289 139 154 C ATOM 879 C THR A 134 25.056 40.694 13.403 1.00 16.60 C ANISOU 879 C THR A 134 2429 2111 1765 281 135 171 C ATOM 880 O THR A 134 25.694 41.346 14.228 1.00 17.80 O ANISOU 880 O THR A 134 2592 2252 1918 274 135 186 O ATOM 881 CB THR A 134 23.282 39.565 14.771 1.00 14.08 C ANISOU 881 CB THR A 134 2091 1779 1479 301 131 154 C ATOM 882 OG1 THR A 134 22.757 38.301 15.167 1.00 14.60 O ANISOU 882 OG1 THR A 134 2136 1845 1567 308 135 138 O ATOM 883 CG2 THR A 134 22.166 40.416 14.141 1.00 14.07 C ANISOU 883 CG2 THR A 134 2104 1779 1461 312 118 155 C ATOM 884 N ILE A 135 24.895 41.087 12.138 1.00 14.64 N ANISOU 884 N ILE A 135 2188 1875 1497 282 131 170 N ATOM 885 CA ILE A 135 25.450 42.340 11.628 1.00 16.94 C ANISOU 885 CA ILE A 135 2501 2168 1766 275 126 185 C ATOM 886 C ILE A 135 24.293 43.233 11.221 1.00 20.38 C ANISOU 886 C ILE A 135 2953 2604 2188 286 114 188 C ATOM 887 O ILE A 135 23.338 42.760 10.597 1.00 19.79 O ANISOU 887 O ILE A 135 2870 2536 2113 297 110 174 O ATOM 888 CB ILE A 135 26.367 42.108 10.412 1.00 17.34 C ANISOU 888 CB ILE A 135 2548 2235 1804 265 133 183 C ATOM 889 CG1 ILE A 135 27.364 40.993 10.680 1.00 13.81 C ANISOU 889 CG1 ILE A 135 2082 1792 1373 256 146 176 C ATOM 890 CG2 ILE A 135 27.141 43.376 10.077 1.00 17.66 C ANISOU 890 CG2 ILE A 135 2610 2276 1824 256 130 200 C ATOM 891 CD1 ILE A 135 28.122 40.585 9.410 1.00 14.13 C ANISOU 891 CD1 ILE A 135 2116 1850 1402 248 152 170 C ATOM 892 N PHE A 136 24.389 44.529 11.525 1.00 15.04 N ANISOU 892 N PHE A 136 2297 1918 1499 284 107 205 N ATOM 893 CA PHE A 136 23.319 45.456 11.188 1.00 14.36 C ANISOU 893 CA PHE A 136 2227 1830 1399 295 94 208 C ATOM 894 C PHE A 136 23.875 46.828 10.816 1.00 13.90 C ANISOU 894 C PHE A 136 2192 1771 1319 287 89 226 C ATOM 895 O PHE A 136 24.922 47.259 11.313 1.00 14.56 O ANISOU 895 O PHE A 136 2282 1848 1401 276 94 239 O ATOM 896 CB PHE A 136 22.315 45.608 12.344 1.00 11.94 C ANISOU 896 CB PHE A 136 1922 1508 1106 305 88 209 C ATOM 897 CG PHE A 136 22.929 46.130 13.617 1.00 16.71 C ANISOU 897 CG PHE A 136 2534 2096 1718 299 90 224 C ATOM 898 CD1 PHE A 136 22.932 47.493 13.901 1.00 14.48 C ANISOU 898 CD1 PHE A 136 2274 1804 1422 298 82 241 C ATOM 899 CD2 PHE A 136 23.487 45.256 14.541 1.00 14.68 C ANISOU 899 CD2 PHE A 136 2262 1834 1482 294 99 220 C ATOM 900 CE1 PHE A 136 23.496 47.965 15.082 1.00 17.70 C ANISOU 900 CE1 PHE A 136 2689 2198 1838 292 83 254 C ATOM 901 CE2 PHE A 136 24.048 45.729 15.718 1.00 16.44 C ANISOU 901 CE2 PHE A 136 2491 2041 1712 288 101 234 C ATOM 902 CZ PHE A 136 24.057 47.080 15.982 1.00 17.68 C ANISOU 902 CZ PHE A 136 2671 2190 1856 287 93 250 C ATOM 903 N GLY A 137 23.162 47.499 9.915 1.00 11.59 N ANISOU 903 N GLY A 137 1911 1484 1008 294 80 226 N ATOM 904 CA GLY A 137 23.437 48.878 9.542 1.00 14.31 C ANISOU 904 CA GLY A 137 2278 1827 1330 289 73 243 C ATOM 905 C GLY A 137 22.146 49.668 9.438 1.00 18.41 C ANISOU 905 C GLY A 137 2812 2342 1842 302 60 244 C ATOM 906 O GLY A 137 21.171 49.178 8.854 1.00 14.69 O ANISOU 906 O GLY A 137 2332 1877 1370 313 56 231 O ATOM 907 N ILE A 138 22.113 50.887 9.981 1.00 21.50 N ANISOU 907 N ILE A 138 3223 2722 2225 302 53 261 N ATOM 908 CA ILE A 138 20.873 51.647 10.146 1.00 18.77 C ANISOU 908 CA ILE A 138 2889 2368 1874 314 40 263 C ATOM 909 C ILE A 138 20.977 52.950 9.366 1.00 17.71 C ANISOU 909 C ILE A 138 2778 2238 1715 312 32 276 C ATOM 910 O ILE A 138 21.906 53.737 9.593 1.00 20.66 O ANISOU 910 O ILE A 138 3164 2606 2079 301 33 292 O ATOM 911 CB ILE A 138 20.579 51.924 11.629 1.00 17.51 C ANISOU 911 CB ILE A 138 2734 2191 1730 318 38 270 C ATOM 912 CG1 ILE A 138 20.423 50.599 12.392 1.00 16.76 C ANISOU 912 CG1 ILE A 138 2616 2093 1660 321 46 257 C ATOM 913 CG2 ILE A 138 19.346 52.809 11.779 1.00 13.83 C ANISOU 913 CG2 ILE A 138 2282 1717 1258 330 25 274 C ATOM 914 CD1 ILE A 138 20.616 50.742 13.913 1.00 15.20 C ANISOU 914 CD1 ILE A 138 2419 1877 1479 320 47 265 C ATOM 915 N TYR A 139 20.024 53.177 8.449 1.00 17.67 N ANISOU 915 N TYR A 139 2777 2240 1697 321 23 270 N ATOM 916 CA TYR A 139 19.941 54.399 7.658 1.00 19.71 C ANISOU 916 CA TYR A 139 3056 2501 1932 320 14 281 C ATOM 917 C TYR A 139 18.687 55.202 7.992 1.00 24.52 C ANISOU 917 C TYR A 139 3678 3100 2538 333 1 285 C ATOM 918 O TYR A 139 17.666 54.657 8.418 1.00 21.97 O ANISOU 918 O TYR A 139 3346 2773 2228 345 -1 274 O ATOM 919 CB TYR A 139 19.944 54.103 6.150 1.00 19.82 C ANISOU 919 CB TYR A 139 3066 2533 1931 319 15 272 C ATOM 920 CG TYR A 139 21.206 53.451 5.662 1.00 16.92 C ANISOU 920 CG TYR A 139 2689 2177 1563 306 27 270 C ATOM 921 CD1 TYR A 139 22.305 54.213 5.308 1.00 15.36 C ANISOU 921 CD1 TYR A 139 2504 1982 1349 293 29 284 C ATOM 922 CD2 TYR A 139 21.308 52.068 5.570 1.00 22.53 C ANISOU 922 CD2 TYR A 139 3376 2895 2288 306 36 254 C ATOM 923 CE1 TYR A 139 23.475 53.618 4.868 1.00 16.35 C ANISOU 923 CE1 TYR A 139 2620 2118 1474 281 40 281 C ATOM 924 CE2 TYR A 139 22.467 51.467 5.135 1.00 16.29 C ANISOU 924 CE2 TYR A 139 2576 2115 1498 294 47 251 C ATOM 925 CZ TYR A 139 23.549 52.244 4.787 1.00 21.17 C ANISOU 925 CZ TYR A 139 3208 2736 2100 282 49 265 C ATOM 926 OH TYR A 139 24.715 51.647 4.361 1.00 28.11 O ANISOU 926 OH TYR A 139 4077 3625 2980 269 60 263 O ATOM 927 N ARG A 140 18.771 56.513 7.788 1.00 19.41 N ANISOU 927 N ARG A 140 3054 2450 1873 331 -7 300 N ATOM 928 CA ARG A 140 17.588 57.356 7.793 1.00 22.28 C ANISOU 928 CA ARG A 140 3431 2807 2229 343 -20 303 C ATOM 929 C ARG A 140 16.995 57.334 6.389 1.00 29.10 C ANISOU 929 C ARG A 140 4294 3684 3076 348 -25 294 C ATOM 930 O ARG A 140 17.731 57.433 5.401 1.00 33.10 O ANISOU 930 O ARG A 140 4804 4203 3568 340 -22 296 O ATOM 931 CB ARG A 140 17.957 58.780 8.220 1.00 38.59 C ANISOU 931 CB ARG A 140 5519 4861 4282 338 -26 323 C ATOM 932 CG ARG A 140 16.789 59.692 8.538 1.00 57.23 C ANISOU 932 CG ARG A 140 7894 7211 6638 350 -39 328 C ATOM 933 CD ARG A 140 17.250 60.936 9.302 1.00 73.48 C ANISOU 933 CD ARG A 140 9973 9256 8691 345 -44 348 C ATOM 934 NE ARG A 140 17.736 60.630 10.648 1.00 86.02 N ANISOU 934 NE ARG A 140 11555 10832 10298 341 -37 352 N ATOM 935 CZ ARG A 140 18.988 60.828 11.054 1.00 95.93 C ANISOU 935 CZ ARG A 140 12814 12084 11553 327 -29 363 C ATOM 936 NH1 ARG A 140 19.888 61.335 10.218 1.00100.65 N ANISOU 936 NH1 ARG A 140 13421 12690 12133 317 -28 371 N ATOM 937 NH2 ARG A 140 19.343 60.521 12.297 1.00 96.57 N ANISOU 937 NH2 ARG A 140 12889 12153 11652 324 -24 366 N ATOM 938 N LYS A 141 15.680 57.150 6.293 1.00 25.27 N ANISOU 938 N LYS A 141 3807 3200 2596 363 -33 284 N ATOM 939 CA LYS A 141 15.031 57.241 4.995 1.00 34.21 C ANISOU 939 CA LYS A 141 4942 4345 3712 368 -39 277 C ATOM 940 C LYS A 141 15.160 58.668 4.487 1.00 46.53 C ANISOU 940 C LYS A 141 6526 5903 5249 365 -48 293 C ATOM 941 O LYS A 141 14.789 59.617 5.183 1.00 44.74 O ANISOU 941 O LYS A 141 6314 5663 5021 369 -56 305 O ATOM 942 CB LYS A 141 13.564 56.819 5.081 1.00 24.08 C ANISOU 942 CB LYS A 141 3651 3059 2438 385 -46 264 C ATOM 943 CG LYS A 141 12.814 56.898 3.759 1.00 25.13 C ANISOU 943 CG LYS A 141 3786 3205 2555 391 -53 257 C ATOM 944 CD LYS A 141 11.337 56.541 3.939 1.00 31.77 C ANISOU 944 CD LYS A 141 4621 4044 3407 408 -60 244 C ATOM 945 CE LYS A 141 10.550 56.645 2.624 1.00 34.12 C ANISOU 945 CE LYS A 141 4922 4354 3689 415 -68 237 C ATOM 946 NZ LYS A 141 11.327 57.309 1.535 1.00 42.72 N ANISOU 946 NZ LYS A 141 6022 5453 4754 405 -68 246 N ATOM 947 N LYS A 142 15.711 58.814 3.278 1.00 54.47 N ANISOU 947 N LYS A 142 7536 6924 6238 358 -47 294 N ATOM 948 CA LYS A 142 16.089 60.116 2.736 1.00 56.17 C ANISOU 948 CA LYS A 142 7773 7140 6430 352 -54 310 C ATOM 949 C LYS A 142 15.018 60.740 1.852 1.00 57.66 C ANISOU 949 C LYS A 142 7972 7333 6603 362 -66 308 C ATOM 950 O LYS A 142 14.913 61.970 1.792 1.00 60.30 O ANISOU 950 O LYS A 142 8327 7661 6922 362 -75 322 O ATOM 951 CB LYS A 142 17.384 59.993 1.924 1.00 56.57 C ANISOU 951 CB LYS A 142 7822 7202 6468 338 -45 313 C ATOM 952 CG LYS A 142 18.595 59.499 2.696 1.00 56.40 C ANISOU 952 CG LYS A 142 7792 7177 6460 326 -33 317 C ATOM 953 CD LYS A 142 19.121 60.554 3.654 1.00 56.19 C ANISOU 953 CD LYS A 142 7782 7135 6431 320 -36 335 C ATOM 954 CE LYS A 142 20.449 60.124 4.259 1.00 55.10 C ANISOU 954 CE LYS A 142 7637 6996 6304 307 -23 340 C ATOM 955 NZ LYS A 142 21.094 61.231 5.019 1.00 55.09 N ANISOU 955 NZ LYS A 142 7653 6981 6297 299 -25 359 N ATOM 956 N SER A 143 14.213 59.930 1.179 1.00 56.95 N ANISOU 956 N SER A 143 7869 7252 6515 371 -67 292 N ATOM 957 CA SER A 143 13.230 60.424 0.230 1.00 58.29 C ANISOU 957 CA SER A 143 8049 7429 6671 380 -78 289 C ATOM 958 C SER A 143 11.852 60.531 0.867 1.00 62.11 C ANISOU 958 C SER A 143 8533 7902 7164 396 -87 285 C ATOM 959 O SER A 143 11.564 59.925 1.901 1.00 65.51 O ANISOU 959 O SER A 143 8953 8324 7615 400 -84 279 O ATOM 960 CB SER A 143 13.163 59.503 -0.993 1.00 59.90 C ANISOU 960 CB SER A 143 8237 7651 6869 380 -74 274 C ATOM 961 OG SER A 143 12.417 58.328 -0.708 1.00 58.97 O ANISOU 961 OG SER A 143 8100 7535 6771 390 -71 256 O ATOM 962 N THR A 144 11.007 61.341 0.242 1.00 66.61 N ANISOU 962 N THR A 144 9116 8473 7718 403 -99 287 N ATOM 963 CA THR A 144 9.613 61.472 0.634 1.00 67.73 C ANISOU 963 CA THR A 144 9260 8607 7868 419 -109 282 C ATOM 964 C THR A 144 8.696 60.526 -0.134 1.00 59.98 C ANISOU 964 C THR A 144 8263 7637 6890 429 -110 263 C ATOM 965 O THR A 144 7.488 60.516 0.121 1.00 57.53 O ANISOU 965 O THR A 144 7952 7322 6586 442 -118 257 O ATOM 966 CB THR A 144 9.154 62.926 0.450 1.00 74.78 C ANISOU 966 CB THR A 144 10177 9493 8743 422 -122 296 C ATOM 967 OG1 THR A 144 8.629 63.108 -0.872 1.00 78.60 O ANISOU 967 OG1 THR A 144 10664 9990 9209 426 -129 291 O ATOM 968 CG2 THR A 144 10.317 63.884 0.666 1.00 76.53 C ANISOU 968 CG2 THR A 144 10414 9710 8953 409 -121 315 C ATOM 969 N ASP A 145 9.244 59.716 -1.039 1.00 55.67 N ANISOU 969 N ASP A 145 7705 7107 6341 422 -102 254 N ATOM 970 CA ASP A 145 8.447 58.747 -1.770 1.00 56.68 C ANISOU 970 CA ASP A 145 7817 7246 6472 431 -102 236 C ATOM 971 C ASP A 145 7.857 57.707 -0.818 1.00 51.69 C ANISOU 971 C ASP A 145 7167 6608 5865 439 -97 223 C ATOM 972 O ASP A 145 8.243 57.592 0.348 1.00 46.88 O ANISOU 972 O ASP A 145 6555 5987 5271 437 -92 228 O ATOM 973 CB ASP A 145 9.293 58.033 -2.826 1.00 62.90 C ANISOU 973 CB ASP A 145 8595 8052 7253 421 -92 229 C ATOM 974 CG ASP A 145 9.946 58.985 -3.803 1.00 73.88 C ANISOU 974 CG ASP A 145 10003 9450 8620 412 -96 240 C ATOM 975 OD1 ASP A 145 9.459 60.125 -3.943 1.00 78.64 O ANISOU 975 OD1 ASP A 145 10624 10047 9208 416 -107 251 O ATOM 976 OD2 ASP A 145 10.946 58.586 -4.440 1.00 76.98 O ANISOU 976 OD2 ASP A 145 10388 9853 9005 401 -87 239 O ATOM 977 N GLU A 146 6.888 56.956 -1.332 1.00 48.00 N ANISOU 977 N GLU A 146 6688 6148 5403 450 -99 207 N ATOM 978 CA GLU A 146 6.412 55.786 -0.617 1.00 45.22 C ANISOU 978 CA GLU A 146 6315 5793 5074 457 -93 193 C ATOM 979 C GLU A 146 7.600 54.877 -0.319 1.00 39.22 C ANISOU 979 C GLU A 146 5541 5037 4325 445 -79 190 C ATOM 980 O GLU A 146 8.496 54.735 -1.162 1.00 30.83 O ANISOU 980 O GLU A 146 4476 3985 3251 435 -73 190 O ATOM 981 CB GLU A 146 5.377 55.025 -1.445 1.00 57.75 C ANISOU 981 CB GLU A 146 7890 7390 6661 468 -96 175 C ATOM 982 CG GLU A 146 4.076 55.770 -1.674 1.00 72.77 C ANISOU 982 CG GLU A 146 9805 9289 8556 481 -110 176 C ATOM 983 CD GLU A 146 3.366 56.106 -0.382 1.00 85.90 C ANISOU 983 CD GLU A 146 11471 10934 10232 490 -116 180 C ATOM 984 OE1 GLU A 146 3.274 55.218 0.496 1.00 88.00 O ANISOU 984 OE1 GLU A 146 11721 11195 10519 492 -109 171 O ATOM 985 OE2 GLU A 146 2.900 57.257 -0.246 1.00 92.32 O ANISOU 985 OE2 GLU A 146 12303 11739 11035 494 -126 191 O ATOM 986 N PRO A 147 7.669 54.283 0.871 1.00 32.97 N ANISOU 986 N PRO A 147 4738 4234 3555 446 -73 187 N ATOM 987 CA PRO A 147 8.823 53.436 1.189 1.00 35.36 C ANISOU 987 CA PRO A 147 5027 4540 3869 435 -60 184 C ATOM 988 C PRO A 147 8.929 52.275 0.209 1.00 35.20 C ANISOU 988 C PRO A 147 4988 4536 3849 434 -52 168 C ATOM 989 O PRO A 147 7.930 51.674 -0.188 1.00 32.62 O ANISOU 989 O PRO A 147 4652 4216 3527 445 -55 154 O ATOM 990 CB PRO A 147 8.530 52.954 2.616 1.00 33.99 C ANISOU 990 CB PRO A 147 4844 4353 3719 440 -57 182 C ATOM 991 CG PRO A 147 7.059 53.138 2.794 1.00 34.24 C ANISOU 991 CG PRO A 147 4878 4378 3754 455 -67 176 C ATOM 992 CD PRO A 147 6.696 54.337 1.972 1.00 27.29 C ANISOU 992 CD PRO A 147 4018 3501 2851 458 -79 186 C ATOM 993 N SER A 148 10.158 51.978 -0.195 1.00 32.32 N ANISOU 993 N SER A 148 4619 4180 3481 420 -43 170 N ATOM 994 CA SER A 148 10.392 50.929 -1.174 1.00 28.46 C ANISOU 994 CA SER A 148 4114 3708 2992 418 -35 156 C ATOM 995 C SER A 148 11.814 50.427 -0.997 1.00 26.59 C ANISOU 995 C SER A 148 3869 3475 2761 403 -22 158 C ATOM 996 O SER A 148 12.592 50.964 -0.206 1.00 24.01 O ANISOU 996 O SER A 148 3550 3138 2435 395 -20 172 O ATOM 997 CB SER A 148 10.171 51.427 -2.606 1.00 32.02 C ANISOU 997 CB SER A 148 4574 4173 3420 418 -42 155 C ATOM 998 OG SER A 148 11.210 52.310 -2.998 1.00 31.73 O ANISOU 998 OG SER A 148 4553 4139 3366 406 -41 170 O ATOM 999 N GLU A 149 12.139 49.386 -1.762 1.00 27.21 N ANISOU 999 N GLU A 149 3930 3567 2840 400 -14 145 N ATOM 1000 CA GLU A 149 13.473 48.804 -1.714 1.00 28.08 C ANISOU 1000 CA GLU A 149 4031 3682 2956 386 -1 145 C ATOM 1001 C GLU A 149 14.554 49.843 -2.002 1.00 31.19 C ANISOU 1001 C GLU A 149 4442 4077 3332 373 -1 163 C ATOM 1002 O GLU A 149 15.664 49.747 -1.461 1.00 23.28 O ANISOU 1002 O GLU A 149 3439 3072 2336 362 7 169 O ATOM 1003 CB GLU A 149 13.541 47.631 -2.698 1.00 31.99 C ANISOU 1003 CB GLU A 149 4508 4195 3453 386 6 128 C ATOM 1004 CG GLU A 149 14.792 46.778 -2.601 1.00 23.05 C ANISOU 1004 CG GLU A 149 3361 3067 2329 373 20 125 C ATOM 1005 CD GLU A 149 14.598 45.395 -3.212 1.00 27.07 C ANISOU 1005 CD GLU A 149 3847 3590 2848 376 27 105 C ATOM 1006 OE1 GLU A 149 13.626 44.698 -2.827 1.00 22.56 O ANISOU 1006 OE1 GLU A 149 3264 3015 2291 387 25 93 O ATOM 1007 OE2 GLU A 149 15.413 45.006 -4.076 1.00 23.57 O ANISOU 1007 OE2 GLU A 149 3399 3161 2398 367 34 101 O ATOM 1008 N LYS A 150 14.246 50.852 -2.829 1.00 34.28 N ANISOU 1008 N LYS A 150 4852 4473 3702 375 -11 170 N ATOM 1009 CA LYS A 150 15.235 51.862 -3.208 1.00 29.90 C ANISOU 1009 CA LYS A 150 4313 3919 3127 363 -11 186 C ATOM 1010 C LYS A 150 15.777 52.632 -2.012 1.00 24.62 C ANISOU 1010 C LYS A 150 3656 3234 2463 358 -12 203 C ATOM 1011 O LYS A 150 16.883 53.176 -2.085 1.00 19.71 O ANISOU 1011 O LYS A 150 3044 2613 1832 345 -8 215 O ATOM 1012 CB LYS A 150 14.618 52.878 -4.179 1.00 47.03 C ANISOU 1012 CB LYS A 150 6501 6093 5274 367 -23 192 C ATOM 1013 CG LYS A 150 13.992 52.300 -5.439 1.00 61.62 C ANISOU 1013 CG LYS A 150 8341 7958 7115 373 -25 177 C ATOM 1014 CD LYS A 150 14.992 51.545 -6.300 1.00 68.69 C ANISOU 1014 CD LYS A 150 9224 8869 8006 362 -14 170 C ATOM 1015 CE LYS A 150 14.312 50.975 -7.539 1.00 66.28 C ANISOU 1015 CE LYS A 150 8910 8579 7693 368 -16 155 C ATOM 1016 NZ LYS A 150 13.808 52.055 -8.434 1.00 64.58 N ANISOU 1016 NZ LYS A 150 8714 8368 7455 371 -28 162 N ATOM 1017 N ASP A 151 15.025 52.699 -0.916 1.00 25.07 N ANISOU 1017 N ASP A 151 3714 3277 2535 367 -16 203 N ATOM 1018 CA ASP A 151 15.486 53.441 0.249 1.00 23.23 C ANISOU 1018 CA ASP A 151 3492 3027 2306 362 -16 219 C ATOM 1019 C ASP A 151 16.697 52.790 0.898 1.00 22.55 C ANISOU 1019 C ASP A 151 3394 2939 2234 351 -4 220 C ATOM 1020 O ASP A 151 17.392 53.447 1.675 1.00 16.52 O ANISOU 1020 O ASP A 151 2642 2165 1471 343 -2 234 O ATOM 1021 CB ASP A 151 14.346 53.578 1.259 1.00 26.50 C ANISOU 1021 CB ASP A 151 3908 3428 2735 376 -24 217 C ATOM 1022 CG ASP A 151 13.218 54.454 0.740 1.00 29.99 C ANISOU 1022 CG ASP A 151 4364 3869 3162 386 -38 220 C ATOM 1023 OD1 ASP A 151 13.508 55.573 0.276 1.00 30.44 O ANISOU 1023 OD1 ASP A 151 4441 3926 3200 382 -44 233 O ATOM 1024 OD2 ASP A 151 12.049 54.021 0.784 1.00 29.22 O ANISOU 1024 OD2 ASP A 151 4259 3770 3072 399 -43 208 O ATOM 1025 N ALA A 152 16.956 51.515 0.606 1.00 19.76 N ANISOU 1025 N ALA A 152 3021 2596 1892 349 6 205 N ATOM 1026 CA ALA A 152 18.128 50.839 1.132 1.00 20.40 C ANISOU 1026 CA ALA A 152 3089 2676 1985 338 19 205 C ATOM 1027 C ALA A 152 19.358 51.000 0.249 1.00 20.75 C ANISOU 1027 C ALA A 152 3137 2733 2014 323 25 211 C ATOM 1028 O ALA A 152 20.452 50.603 0.662 1.00 24.88 O ANISOU 1028 O ALA A 152 3654 3255 2545 312 35 213 O ATOM 1029 CB ALA A 152 17.830 49.349 1.328 1.00 19.70 C ANISOU 1029 CB ALA A 152 2976 2592 1917 342 27 187 C ATOM 1030 N LEU A 153 19.214 51.580 -0.940 1.00 24.06 N ANISOU 1030 N LEU A 153 3568 3163 2412 323 19 212 N ATOM 1031 CA LEU A 153 20.339 51.742 -1.859 1.00 24.26 C ANISOU 1031 CA LEU A 153 3596 3199 2421 310 25 217 C ATOM 1032 C LEU A 153 21.097 53.035 -1.562 1.00 33.12 C ANISOU 1032 C LEU A 153 4739 4314 3530 301 22 238 C ATOM 1033 O LEU A 153 21.190 53.941 -2.382 1.00 36.86 O ANISOU 1033 O LEU A 153 5229 4794 3983 298 15 246 O ATOM 1034 CB LEU A 153 19.855 51.706 -3.303 1.00 18.31 C ANISOU 1034 CB LEU A 153 2844 2463 1652 313 20 209 C ATOM 1035 CG LEU A 153 19.239 50.379 -3.741 1.00 25.78 C ANISOU 1035 CG LEU A 153 3767 3418 2609 321 25 188 C ATOM 1036 CD1 LEU A 153 18.791 50.463 -5.196 1.00 25.59 C ANISOU 1036 CD1 LEU A 153 3746 3410 2567 323 20 181 C ATOM 1037 CD2 LEU A 153 20.199 49.216 -3.559 1.00 22.54 C ANISOU 1037 CD2 LEU A 153 3337 3014 2213 312 39 179 C ATOM 1038 N GLN A 154 21.623 53.109 -0.342 1.00 36.07 N ANISOU 1038 N GLN A 154 5113 4674 3917 296 26 246 N ATOM 1039 CA GLN A 154 22.444 54.216 0.105 1.00 30.23 C ANISOU 1039 CA GLN A 154 4392 3926 3168 287 24 265 C ATOM 1040 C GLN A 154 23.888 53.767 0.302 1.00 29.57 C ANISOU 1040 C GLN A 154 4301 3846 3090 272 37 268 C ATOM 1041 O GLN A 154 24.144 52.606 0.640 1.00 26.45 O ANISOU 1041 O GLN A 154 3886 3452 2713 271 47 257 O ATOM 1042 CB GLN A 154 21.918 54.806 1.420 1.00 27.24 C ANISOU 1042 CB GLN A 154 4022 3528 2800 293 18 274 C ATOM 1043 CG GLN A 154 20.518 55.348 1.311 1.00 24.90 C ANISOU 1043 CG GLN A 154 3735 3228 2498 308 5 273 C ATOM 1044 CD GLN A 154 20.077 56.088 2.553 1.00 26.76 C ANISOU 1044 CD GLN A 154 3982 3445 2742 313 -1 284 C ATOM 1045 OE1 GLN A 154 20.843 56.856 3.135 1.00 33.91 O ANISOU 1045 OE1 GLN A 154 4899 4341 3643 305 0 299 O ATOM 1046 NE2 GLN A 154 18.832 55.866 2.966 1.00 26.23 N ANISOU 1046 NE2 GLN A 154 3910 3371 2684 327 -7 276 N ATOM 1047 N PRO A 155 24.856 54.652 0.072 1.00 29.37 N ANISOU 1047 N PRO A 155 4291 3821 3049 260 38 283 N ATOM 1048 CA PRO A 155 26.249 54.309 0.380 1.00 20.79 C ANISOU 1048 CA PRO A 155 3197 2735 1968 246 49 288 C ATOM 1049 C PRO A 155 26.459 54.250 1.884 1.00 20.92 C ANISOU 1049 C PRO A 155 3211 2734 2003 246 52 294 C ATOM 1050 O PRO A 155 25.767 54.920 2.650 1.00 21.51 O ANISOU 1050 O PRO A 155 3297 2796 2081 253 44 301 O ATOM 1051 CB PRO A 155 27.045 55.458 -0.251 1.00 23.54 C ANISOU 1051 CB PRO A 155 3565 3086 2292 236 47 304 C ATOM 1052 CG PRO A 155 26.099 56.620 -0.197 1.00 17.85 C ANISOU 1052 CG PRO A 155 2864 2358 1560 245 33 313 C ATOM 1053 CD PRO A 155 24.725 56.032 -0.439 1.00 21.13 C ANISOU 1053 CD PRO A 155 3270 2776 1982 260 27 298 C ATOM 1054 N GLY A 156 27.422 53.425 2.308 1.00 23.76 N ANISOU 1054 N GLY A 156 3146 3130 2750 -661 425 109 N ATOM 1055 CA GLY A 156 27.700 53.294 3.732 1.00 25.15 C ANISOU 1055 CA GLY A 156 3319 3296 2941 -658 418 95 C ATOM 1056 C GLY A 156 28.020 54.605 4.432 1.00 25.48 C ANISOU 1056 C GLY A 156 3367 3319 2995 -676 409 107 C ATOM 1057 O GLY A 156 27.823 54.710 5.649 1.00 25.55 O ANISOU 1057 O GLY A 156 3380 3313 3014 -674 400 95 O ATOM 1058 N ARG A 157 28.497 55.613 3.685 1.00 21.87 N ANISOU 1058 N ARG A 157 2910 2860 2539 -694 411 130 N ATOM 1059 CA ARG A 157 28.714 56.952 4.241 1.00 26.72 C ANISOU 1059 CA ARG A 157 3532 3455 3166 -711 402 144 C ATOM 1060 C ARG A 157 27.487 57.497 4.949 1.00 22.53 C ANISOU 1060 C ARG A 157 3022 2901 2637 -709 387 137 C ATOM 1061 O ARG A 157 27.613 58.324 5.860 1.00 28.83 O ANISOU 1061 O ARG A 157 3826 3680 3449 -717 377 140 O ATOM 1062 CB ARG A 157 29.093 57.942 3.135 1.00 26.30 C ANISOU 1062 CB ARG A 157 3480 3402 3109 -729 405 169 C ATOM 1063 CG ARG A 157 30.488 57.782 2.584 1.00 50.57 C ANISOU 1063 CG ARG A 157 6534 6493 6187 -736 417 180 C ATOM 1064 CD ARG A 157 31.590 58.094 3.605 1.00 54.77 C ANISOU 1064 CD ARG A 157 7054 7018 6737 -745 414 181 C ATOM 1065 NE ARG A 157 32.912 57.742 3.082 1.00 49.15 N ANISOU 1065 NE ARG A 157 6322 6325 6028 -749 427 189 N ATOM 1066 CZ ARG A 157 33.976 57.487 3.836 1.00 36.95 C ANISOU 1066 CZ ARG A 157 4761 4782 4496 -751 429 185 C ATOM 1067 NH1 ARG A 157 33.882 57.545 5.155 1.00 32.89 N ANISOU 1067 NH1 ARG A 157 4249 4254 3994 -748 418 173 N ATOM 1068 NH2 ARG A 157 35.132 57.160 3.271 1.00 32.41 N ANISOU 1068 NH2 ARG A 157 4168 4224 3923 -754 441 194 N ATOM 1069 N ASN A 158 26.296 57.084 4.519 1.00 17.81 N ANISOU 1069 N ASN A 158 2436 2305 2026 -697 387 130 N ATOM 1070 CA ASN A 158 25.051 57.614 5.048 1.00 19.93 C ANISOU 1070 CA ASN A 158 2725 2552 2294 -694 374 126 C ATOM 1071 C ASN A 158 24.600 56.929 6.328 1.00 22.60 C ANISOU 1071 C ASN A 158 3066 2882 2638 -679 368 101 C ATOM 1072 O ASN A 158 23.536 57.287 6.843 1.00 25.39 O ANISOU 1072 O ASN A 158 3438 3218 2993 -674 358 95 O ATOM 1073 CB ASN A 158 23.934 57.491 4.009 1.00 23.50 C ANISOU 1073 CB ASN A 158 3190 3009 2730 -687 375 130 C ATOM 1074 CG ASN A 158 24.059 58.504 2.873 1.00 27.54 C ANISOU 1074 CG ASN A 158 3706 3520 3237 -703 377 156 C ATOM 1075 OD1 ASN A 158 25.045 59.244 2.767 1.00 23.01 O ANISOU 1075 OD1 ASN A 158 3125 2945 2672 -718 379 171 O ATOM 1076 ND2 ASN A 158 23.049 58.533 2.015 1.00 25.85 N ANISOU 1076 ND2 ASN A 158 3503 3308 3010 -698 377 161 N ATOM 1077 N LEU A 159 25.360 55.961 6.843 1.00 20.10 N ANISOU 1077 N LEU A 159 2734 2578 2326 -671 374 86 N ATOM 1078 CA LEU A 159 24.911 55.205 8.008 1.00 22.35 C ANISOU 1078 CA LEU A 159 3021 2857 2615 -656 369 61 C ATOM 1079 C LEU A 159 24.753 56.108 9.224 1.00 22.58 C ANISOU 1079 C LEU A 159 3061 2861 2659 -661 356 60 C ATOM 1080 O LEU A 159 25.587 56.977 9.491 1.00 23.26 O ANISOU 1080 O LEU A 159 3142 2939 2757 -676 353 74 O ATOM 1081 CB LEU A 159 25.890 54.065 8.317 1.00 21.06 C ANISOU 1081 CB LEU A 159 2837 2712 2455 -647 378 48 C ATOM 1082 CG LEU A 159 25.747 52.787 7.481 1.00 16.78 C ANISOU 1082 CG LEU A 159 2285 2191 1899 -632 389 38 C ATOM 1083 CD1 LEU A 159 27.012 51.938 7.546 1.00 14.59 C ANISOU 1083 CD1 LEU A 159 1984 1931 1626 -628 398 34 C ATOM 1084 CD2 LEU A 159 24.539 51.966 7.939 1.00 16.41 C ANISOU 1084 CD2 LEU A 159 2249 2141 1847 -613 384 15 C ATOM 1085 N VAL A 160 23.664 55.878 9.958 1.00 20.79 N ANISOU 1085 N VAL A 160 2848 2621 2431 -649 348 44 N ATOM 1086 CA VAL A 160 23.368 56.543 11.224 1.00 21.91 C ANISOU 1086 CA VAL A 160 3000 2739 2587 -649 335 39 C ATOM 1087 C VAL A 160 23.929 55.752 12.402 1.00 19.78 C ANISOU 1087 C VAL A 160 2719 2471 2326 -639 336 18 C ATOM 1088 O VAL A 160 24.302 56.332 13.425 1.00 18.62 O ANISOU 1088 O VAL A 160 2572 2309 2194 -643 327 18 O ATOM 1089 CB VAL A 160 21.837 56.729 11.349 1.00 21.73 C ANISOU 1089 CB VAL A 160 2999 2699 2557 -639 327 32 C ATOM 1090 CG1 VAL A 160 21.419 57.028 12.767 1.00 24.49 C ANISOU 1090 CG1 VAL A 160 3358 3026 2920 -631 315 20 C ATOM 1091 CG2 VAL A 160 21.355 57.836 10.428 1.00 26.66 C ANISOU 1091 CG2 VAL A 160 3637 3315 3179 -650 323 56 C ATOM 1092 N ALA A 161 23.960 54.429 12.286 1.00 17.23 N ANISOU 1092 N ALA A 161 2386 2167 1994 -626 345 1 N ATOM 1093 CA ALA A 161 24.519 53.551 13.295 1.00 15.29 C ANISOU 1093 CA ALA A 161 2127 1926 1756 -615 346 -19 C ATOM 1094 C ALA A 161 24.742 52.187 12.648 1.00 18.07 C ANISOU 1094 C ALA A 161 2466 2303 2098 -603 358 -30 C ATOM 1095 O ALA A 161 24.021 51.806 11.717 1.00 22.14 O ANISOU 1095 O ALA A 161 2987 2826 2600 -597 362 -30 O ATOM 1096 CB ALA A 161 23.587 53.442 14.510 1.00 12.75 C ANISOU 1096 CB ALA A 161 1820 1587 1439 -602 337 -38 C ATOM 1097 N ALA A 162 25.737 51.455 13.144 1.00 15.97 N ANISOU 1097 N ALA A 162 2182 2048 1838 -599 363 -39 N ATOM 1098 CA ALA A 162 26.023 50.125 12.591 1.00 14.71 C ANISOU 1098 CA ALA A 162 2008 1911 1672 -586 373 -49 C ATOM 1099 C ALA A 162 26.774 49.308 13.630 1.00 22.85 C ANISOU 1099 C ALA A 162 3025 2946 2713 -576 373 -66 C ATOM 1100 O ALA A 162 27.287 49.849 14.610 1.00 17.77 O ANISOU 1100 O ALA A 162 2379 2292 2081 -583 367 -64 O ATOM 1101 CB ALA A 162 26.851 50.209 11.303 1.00 18.23 C ANISOU 1101 CB ALA A 162 2441 2374 2112 -595 383 -29 C ATOM 1102 N GLY A 163 26.827 47.996 13.419 1.00 13.71 N ANISOU 1102 N GLY A 163 1856 1803 1550 -559 379 -80 N ATOM 1103 CA GLY A 163 27.621 47.192 14.322 1.00 18.67 C ANISOU 1103 CA GLY A 163 2469 2436 2188 -550 379 -94 C ATOM 1104 C GLY A 163 27.267 45.722 14.214 1.00 20.60 C ANISOU 1104 C GLY A 163 2708 2690 2427 -528 381 -113 C ATOM 1105 O GLY A 163 26.760 45.257 13.194 1.00 12.71 O ANISOU 1105 O GLY A 163 1711 1701 1419 -521 385 -111 O ATOM 1106 N TYR A 164 27.558 45.012 15.292 1.00 16.09 N ANISOU 1106 N TYR A 164 2130 2118 1865 -517 378 -131 N ATOM 1107 CA TYR A 164 27.367 43.576 15.274 1.00 14.31 C ANISOU 1107 CA TYR A 164 1898 1901 1638 -498 379 -150 C ATOM 1108 C TYR A 164 27.278 43.046 16.694 1.00 7.22 C ANISOU 1108 C TYR A 164 1002 993 750 -487 372 -172 C ATOM 1109 O TYR A 164 27.803 43.633 17.635 1.00 11.20 O ANISOU 1109 O TYR A 164 1503 1490 1263 -492 368 -170 O ATOM 1110 CB TYR A 164 28.496 42.870 14.520 1.00 15.14 C ANISOU 1110 CB TYR A 164 1986 2026 1740 -501 390 -145 C ATOM 1111 CG TYR A 164 29.883 43.191 15.018 1.00 14.57 C ANISOU 1111 CG TYR A 164 1899 1960 1679 -511 394 -135 C ATOM 1112 CD1 TYR A 164 30.444 42.481 16.080 1.00 15.65 C ANISOU 1112 CD1 TYR A 164 2027 2096 1823 -504 392 -151 C ATOM 1113 CD2 TYR A 164 30.645 44.193 14.422 1.00 16.85 C ANISOU 1113 CD2 TYR A 164 2181 2252 1968 -529 398 -109 C ATOM 1114 CE1 TYR A 164 31.718 42.758 16.525 1.00 16.29 C ANISOU 1114 CE1 TYR A 164 2093 2182 1914 -514 394 -141 C ATOM 1115 CE2 TYR A 164 31.913 44.484 14.868 1.00 13.61 C ANISOU 1115 CE2 TYR A 164 1756 1846 1568 -539 401 -99 C ATOM 1116 CZ TYR A 164 32.444 43.759 15.921 1.00 18.12 C ANISOU 1116 CZ TYR A 164 2319 2418 2148 -531 399 -115 C ATOM 1117 OH TYR A 164 33.705 44.042 16.372 1.00 20.90 O ANISOU 1117 OH TYR A 164 2656 2774 2510 -541 401 -105 O ATOM 1118 N ALA A 165 26.614 41.904 16.816 1.00 17.18 N ANISOU 1118 N ALA A 165 2265 2253 2009 -472 369 -195 N ATOM 1119 CA ALA A 165 26.687 41.064 17.992 1.00 10.86 C ANISOU 1119 CA ALA A 165 1462 1447 1217 -461 364 -218 C ATOM 1120 C ALA A 165 27.511 39.840 17.624 1.00 15.29 C ANISOU 1120 C ALA A 165 2006 2023 1779 -457 370 -225 C ATOM 1121 O ALA A 165 27.285 39.233 16.574 1.00 14.23 O ANISOU 1121 O ALA A 165 1871 1899 1638 -455 375 -223 O ATOM 1122 CB ALA A 165 25.292 40.647 18.466 1.00 11.61 C ANISOU 1122 CB ALA A 165 1571 1525 1314 -448 354 -238 C ATOM 1123 N LEU A 166 28.482 39.508 18.463 1.00 16.16 N ANISOU 1123 N LEU A 166 2105 2137 1898 -457 371 -231 N ATOM 1124 CA LEU A 166 29.301 38.317 18.296 1.00 18.67 C ANISOU 1124 CA LEU A 166 2408 2468 2218 -453 376 -239 C ATOM 1125 C LEU A 166 28.874 37.297 19.350 1.00 15.92 C ANISOU 1125 C LEU A 166 2061 2108 1879 -440 367 -265 C ATOM 1126 O LEU A 166 28.900 37.594 20.549 1.00 13.81 O ANISOU 1126 O LEU A 166 1798 1831 1620 -437 360 -273 O ATOM 1127 CB LEU A 166 30.788 38.656 18.430 1.00 12.80 C ANISOU 1127 CB LEU A 166 1649 1736 1478 -463 384 -224 C ATOM 1128 CG LEU A 166 31.750 37.457 18.495 1.00 18.30 C ANISOU 1128 CG LEU A 166 2329 2445 2179 -458 389 -232 C ATOM 1129 CD1 LEU A 166 31.663 36.646 17.199 1.00 14.11 C ANISOU 1129 CD1 LEU A 166 1795 1928 1640 -455 397 -230 C ATOM 1130 CD2 LEU A 166 33.181 37.917 18.745 1.00 19.66 C ANISOU 1130 CD2 LEU A 166 2486 2628 2357 -468 396 -217 C ATOM 1131 N TYR A 167 28.443 36.118 18.903 1.00 12.36 N ANISOU 1131 N TYR A 167 1607 1659 1429 -432 365 -275 N ATOM 1132 CA TYR A 167 28.155 34.995 19.802 1.00 15.61 C ANISOU 1132 CA TYR A 167 2017 2061 1853 -422 355 -297 C ATOM 1133 C TYR A 167 29.392 34.107 19.794 1.00 15.53 C ANISOU 1133 C TYR A 167 1990 2066 1846 -421 361 -298 C ATOM 1134 O TYR A 167 29.500 33.152 19.029 1.00 16.20 O ANISOU 1134 O TYR A 167 2067 2160 1929 -418 365 -298 O ATOM 1135 CB TYR A 167 26.894 34.239 19.366 1.00 11.17 C ANISOU 1135 CB TYR A 167 1460 1489 1293 -416 347 -305 C ATOM 1136 CG TYR A 167 25.803 35.191 18.939 1.00 17.21 C ANISOU 1136 CG TYR A 167 2241 2246 2053 -418 345 -297 C ATOM 1137 CD1 TYR A 167 25.107 35.947 19.879 1.00 20.27 C ANISOU 1137 CD1 TYR A 167 2641 2615 2445 -418 336 -303 C ATOM 1138 CD2 TYR A 167 25.497 35.368 17.594 1.00 15.11 C ANISOU 1138 CD2 TYR A 167 1977 1990 1773 -421 352 -283 C ATOM 1139 CE1 TYR A 167 24.125 36.851 19.491 1.00 15.98 C ANISOU 1139 CE1 TYR A 167 2112 2063 1895 -419 334 -295 C ATOM 1140 CE2 TYR A 167 24.514 36.266 17.195 1.00 16.12 C ANISOU 1140 CE2 TYR A 167 2120 2110 1895 -423 350 -275 C ATOM 1141 CZ TYR A 167 23.832 36.997 18.141 1.00 13.39 C ANISOU 1141 CZ TYR A 167 1787 1746 1555 -422 341 -281 C ATOM 1142 OH TYR A 167 22.864 37.890 17.749 1.00 18.54 O ANISOU 1142 OH TYR A 167 2454 2391 2201 -424 339 -272 O ATOM 1143 N GLY A 168 30.372 34.487 20.612 1.00 16.55 N ANISOU 1143 N GLY A 168 2112 2197 1979 -424 364 -297 N ATOM 1144 CA GLY A 168 31.613 33.738 20.723 1.00 14.84 C ANISOU 1144 CA GLY A 168 1879 1994 1766 -423 370 -297 C ATOM 1145 C GLY A 168 31.739 33.074 22.077 1.00 12.37 C ANISOU 1145 C GLY A 168 1564 1671 1466 -416 360 -316 C ATOM 1146 O GLY A 168 30.761 32.518 22.583 1.00 10.66 O ANISOU 1146 O GLY A 168 1354 1439 1257 -410 348 -332 O ATOM 1147 N SER A 169 32.925 33.133 22.690 1.00 17.38 N ANISOU 1147 N SER A 169 2187 2313 2104 -418 365 -313 N ATOM 1148 CA SER A 169 33.051 32.604 24.046 1.00 15.20 C ANISOU 1148 CA SER A 169 1910 2027 1840 -412 355 -331 C ATOM 1149 C SER A 169 32.097 33.334 24.989 1.00 20.22 C ANISOU 1149 C SER A 169 2561 2642 2478 -410 344 -341 C ATOM 1150 O SER A 169 31.506 32.716 25.879 1.00 16.19 O ANISOU 1150 O SER A 169 2055 2117 1978 -403 332 -359 O ATOM 1151 CB SER A 169 34.511 32.684 24.526 1.00 15.74 C ANISOU 1151 CB SER A 169 1962 2107 1910 -415 363 -323 C ATOM 1152 OG SER A 169 35.019 34.013 24.574 1.00 14.94 O ANISOU 1152 OG SER A 169 1861 2010 1806 -426 368 -305 O ATOM 1153 N ALA A 170 31.906 34.641 24.784 1.00 14.49 N ANISOU 1153 N ALA A 170 1843 1916 1745 -416 348 -328 N ATOM 1154 CA ALA A 170 30.789 35.368 25.372 1.00 9.35 C ANISOU 1154 CA ALA A 170 1210 1247 1094 -414 340 -335 C ATOM 1155 C ALA A 170 30.083 36.142 24.261 1.00 14.46 C ANISOU 1155 C ALA A 170 1867 1895 1732 -419 344 -321 C ATOM 1156 O ALA A 170 30.575 36.239 23.138 1.00 12.50 O ANISOU 1156 O ALA A 170 1610 1661 1476 -427 353 -304 O ATOM 1157 CB ALA A 170 31.237 36.315 26.498 1.00 11.08 C ANISOU 1157 CB ALA A 170 1432 1463 1315 -414 340 -333 C ATOM 1158 N THR A 171 28.924 36.709 24.574 1.00 13.02 N ANISOU 1158 N THR A 171 1702 1697 1549 -416 337 -327 N ATOM 1159 CA THR A 171 28.170 37.491 23.604 1.00 19.06 C ANISOU 1159 CA THR A 171 2477 2461 2304 -421 339 -313 C ATOM 1160 C THR A 171 28.437 38.967 23.829 1.00 9.57 C ANISOU 1160 C THR A 171 1280 1260 1098 -429 343 -295 C ATOM 1161 O THR A 171 28.263 39.467 24.941 1.00 11.93 O ANISOU 1161 O THR A 171 1586 1548 1399 -425 339 -301 O ATOM 1162 CB THR A 171 26.673 37.204 23.702 1.00 14.69 C ANISOU 1162 CB THR A 171 1932 1892 1758 -405 325 -313 C ATOM 1163 OG1 THR A 171 26.437 35.864 23.278 1.00 13.44 O ANISOU 1163 OG1 THR A 171 1762 1737 1608 -396 320 -315 O ATOM 1164 CG2 THR A 171 25.852 38.204 22.831 1.00 9.24 C ANISOU 1164 CG2 THR A 171 1258 1197 1054 -416 330 -308 C ATOM 1165 N MET A 172 28.855 39.657 22.771 1.00 8.22 N ANISOU 1165 N MET A 172 1104 1099 920 -442 351 -271 N ATOM 1166 CA MET A 172 29.191 41.069 22.850 1.00 12.38 C ANISOU 1166 CA MET A 172 1633 1624 1447 -454 352 -249 C ATOM 1167 C MET A 172 28.511 41.828 21.727 1.00 18.11 C ANISOU 1167 C MET A 172 2368 2348 2164 -462 354 -232 C ATOM 1168 O MET A 172 28.450 41.353 20.585 1.00 14.55 O ANISOU 1168 O MET A 172 1914 1908 1707 -463 359 -228 O ATOM 1169 CB MET A 172 30.708 41.294 22.775 1.00 12.37 C ANISOU 1169 CB MET A 172 1613 1636 1452 -467 358 -232 C ATOM 1170 CG MET A 172 31.133 42.767 22.611 1.00 19.27 C ANISOU 1170 CG MET A 172 2487 2507 2330 -485 357 -204 C ATOM 1171 SD MET A 172 32.916 43.057 22.823 1.00 21.11 S ANISOU 1171 SD MET A 172 2697 2750 2573 -501 361 -186 S ATOM 1172 CE MET A 172 33.080 42.968 24.602 1.00 12.62 C ANISOU 1172 CE MET A 172 1622 1665 1510 -493 352 -202 C ATOM 1173 N LEU A 173 27.982 42.996 22.066 1.00 13.97 N ANISOU 1173 N LEU A 173 1856 1811 1640 -468 349 -222 N ATOM 1174 CA LEU A 173 27.434 43.913 21.086 1.00 16.46 C ANISOU 1174 CA LEU A 173 2183 2124 1948 -481 352 -206 C ATOM 1175 C LEU A 173 28.417 45.058 20.891 1.00 20.26 C ANISOU 1175 C LEU A 173 2657 2606 2434 -502 353 -180 C ATOM 1176 O LEU A 173 28.805 45.726 21.856 1.00 16.30 O ANISOU 1176 O LEU A 173 2156 2096 1943 -508 347 -177 O ATOM 1177 CB LEU A 173 26.065 44.448 21.505 1.00 22.47 C ANISOU 1177 CB LEU A 173 2967 2867 2703 -477 347 -216 C ATOM 1178 CG LEU A 173 25.483 45.235 20.322 1.00 31.86 C ANISOU 1178 CG LEU A 173 4167 4055 3884 -490 349 -199 C ATOM 1179 CD1 LEU A 173 24.136 44.748 19.881 1.00 36.11 C ANISOU 1179 CD1 LEU A 173 4720 4588 4412 -478 348 -213 C ATOM 1180 CD2 LEU A 173 25.410 46.690 20.692 1.00 36.64 C ANISOU 1180 CD2 LEU A 173 4783 4645 4493 -504 344 -183 C ATOM 1181 N VAL A 174 28.827 45.264 19.644 1.00 13.74 N ANISOU 1181 N VAL A 174 1825 1792 1604 -513 359 -162 N ATOM 1182 CA VAL A 174 29.674 46.381 19.260 1.00 11.23 C ANISOU 1182 CA VAL A 174 1501 1475 1291 -534 361 -136 C ATOM 1183 C VAL A 174 28.782 47.347 18.497 1.00 8.78 C ANISOU 1183 C VAL A 174 1209 1156 973 -545 359 -124 C ATOM 1184 O VAL A 174 28.199 46.976 17.470 1.00 12.68 O ANISOU 1184 O VAL A 174 1706 1656 1455 -540 365 -124 O ATOM 1185 CB VAL A 174 30.868 45.919 18.412 1.00 14.34 C ANISOU 1185 CB VAL A 174 1874 1889 1686 -537 370 -122 C ATOM 1186 CG1 VAL A 174 31.687 47.117 17.952 1.00 18.32 C ANISOU 1186 CG1 VAL A 174 2374 2393 2196 -560 371 -95 C ATOM 1187 CG2 VAL A 174 31.735 44.947 19.203 1.00 14.14 C ANISOU 1187 CG2 VAL A 174 1833 1872 1669 -527 371 -134 C ATOM 1188 N LEU A 175 28.650 48.572 19.014 1.00 16.07 N ANISOU 1188 N LEU A 175 2141 2061 1903 -557 351 -114 N ATOM 1189 CA LEU A 175 27.791 49.597 18.436 1.00 19.64 C ANISOU 1189 CA LEU A 175 2612 2501 2350 -567 347 -101 C ATOM 1190 C LEU A 175 28.637 50.809 18.064 1.00 17.74 C ANISOU 1190 C LEU A 175 2367 2257 2118 -589 345 -74 C ATOM 1191 O LEU A 175 29.267 51.425 18.930 1.00 17.55 O ANISOU 1191 O LEU A 175 2339 2222 2108 -597 337 -69 O ATOM 1192 CB LEU A 175 26.680 49.997 19.409 1.00 23.14 C ANISOU 1192 CB LEU A 175 3074 2922 2794 -560 337 -113 C ATOM 1193 CG LEU A 175 25.796 51.174 18.967 1.00 20.06 C ANISOU 1193 CG LEU A 175 2704 2516 2402 -569 331 -99 C ATOM 1194 CD1 LEU A 175 25.020 50.853 17.685 1.00 19.26 C ANISOU 1194 CD1 LEU A 175 2610 2423 2284 -567 338 -97 C ATOM 1195 CD2 LEU A 175 24.834 51.564 20.069 1.00 15.21 C ANISOU 1195 CD2 LEU A 175 2107 1880 1793 -559 320 -109 C ATOM 1196 N ALA A 176 28.654 51.143 16.781 1.00 15.06 N ANISOU 1196 N ALA A 176 2028 1924 1769 -599 352 -58 N ATOM 1197 CA ALA A 176 29.387 52.295 16.278 1.00 18.35 C ANISOU 1197 CA ALA A 176 2441 2338 2193 -621 350 -32 C ATOM 1198 C ALA A 176 28.384 53.363 15.878 1.00 19.58 C ANISOU 1198 C ALA A 176 2618 2477 2344 -628 343 -21 C ATOM 1199 O ALA A 176 27.417 53.072 15.170 1.00 29.68 O ANISOU 1199 O ALA A 176 3909 3759 3610 -622 347 -25 O ATOM 1200 CB ALA A 176 30.257 51.912 15.081 1.00 16.85 C ANISOU 1200 CB ALA A 176 2235 2170 1996 -626 363 -19 C ATOM 1201 N MET A 177 28.615 54.592 16.331 1.00 20.14 N ANISOU 1201 N MET A 177 2694 2529 2428 -642 333 -7 N ATOM 1202 CA MET A 177 27.793 55.733 15.952 1.00 20.50 C ANISOU 1202 CA MET A 177 2759 2557 2472 -651 325 7 C ATOM 1203 C MET A 177 28.718 56.925 15.771 1.00 24.18 C ANISOU 1203 C MET A 177 3220 3016 2950 -671 321 31 C ATOM 1204 O MET A 177 29.944 56.797 15.820 1.00 22.77 O ANISOU 1204 O MET A 177 3024 2849 2780 -679 326 37 O ATOM 1205 CB MET A 177 26.710 56.030 16.999 1.00 20.99 C ANISOU 1205 CB MET A 177 2840 2597 2539 -640 312 -6 C ATOM 1206 CG MET A 177 25.700 54.919 17.197 1.00 23.37 C ANISOU 1206 CG MET A 177 3148 2903 2828 -619 316 -29 C ATOM 1207 SD MET A 177 24.307 55.426 18.208 1.00 26.52 S ANISOU 1207 SD MET A 177 3571 3275 3233 -607 302 -40 S ATOM 1208 CE MET A 177 25.164 55.726 19.747 1.00 17.73 C ANISOU 1208 CE MET A 177 2447 2149 2140 -606 291 -44 C ATOM 1209 N ASP A 178 28.125 58.101 15.567 1.00 22.47 N ANISOU 1209 N ASP A 178 3021 2781 2737 -680 312 44 N ATOM 1210 CA ASP A 178 28.938 59.306 15.435 1.00 26.57 C ANISOU 1210 CA ASP A 178 3537 3291 3268 -700 307 66 C ATOM 1211 C ASP A 178 29.849 59.493 16.645 1.00 27.44 C ANISOU 1211 C ASP A 178 3636 3393 3396 -702 300 63 C ATOM 1212 O ASP A 178 31.021 59.859 16.497 1.00 21.20 O ANISOU 1212 O ASP A 178 2832 2609 2615 -716 302 77 O ATOM 1213 CB ASP A 178 28.036 60.518 15.242 1.00 27.92 C ANISOU 1213 CB ASP A 178 3729 3439 3441 -705 297 79 C ATOM 1214 CG ASP A 178 28.235 61.166 13.903 1.00 36.66 C ANISOU 1214 CG ASP A 178 4836 4552 4540 -720 303 101 C ATOM 1215 OD1 ASP A 178 28.325 60.425 12.891 1.00 29.94 O ANISOU 1215 OD1 ASP A 178 3979 3723 3675 -719 317 102 O ATOM 1216 OD2 ASP A 178 28.311 62.412 13.860 1.00 42.79 O ANISOU 1216 OD2 ASP A 178 5621 5311 5326 -733 295 118 O ATOM 1217 N CYS A 179 29.363 59.152 17.837 1.00 27.27 N ANISOU 1217 N CYS A 179 3620 3361 3381 -688 291 45 N ATOM 1218 CA CYS A 179 30.174 59.327 19.034 1.00 31.60 C ANISOU 1218 CA CYS A 179 4158 3901 3947 -689 283 41 C ATOM 1219 C CYS A 179 31.329 58.333 19.148 1.00 28.52 C ANISOU 1219 C CYS A 179 3745 3534 3559 -688 293 36 C ATOM 1220 O CYS A 179 32.108 58.447 20.100 1.00 29.92 O ANISOU 1220 O CYS A 179 3912 3706 3751 -690 286 34 O ATOM 1221 CB CYS A 179 29.289 59.227 20.273 1.00 31.93 C ANISOU 1221 CB CYS A 179 4212 3926 3995 -672 270 24 C ATOM 1222 SG CYS A 179 28.482 57.624 20.445 1.00 32.82 S ANISOU 1222 SG CYS A 179 4325 4053 4092 -649 279 -4 S ATOM 1223 N GLY A 180 31.460 57.367 18.247 1.00 30.22 N ANISOU 1223 N GLY A 180 3951 3772 3758 -684 308 32 N ATOM 1224 CA GLY A 180 32.525 56.381 18.300 1.00 19.91 C ANISOU 1224 CA GLY A 180 2623 2487 2454 -681 317 27 C ATOM 1225 C GLY A 180 31.984 54.972 18.441 1.00 21.52 C ANISOU 1225 C GLY A 180 2826 2706 2647 -660 325 4 C ATOM 1226 O GLY A 180 30.788 54.715 18.283 1.00 22.43 O ANISOU 1226 O GLY A 180 2957 2817 2751 -649 324 -7 O ATOM 1227 N VAL A 181 32.887 54.051 18.784 1.00 22.90 N ANISOU 1227 N VAL A 181 2981 2896 2825 -654 331 -4 N ATOM 1228 CA VAL A 181 32.598 52.622 18.889 1.00 14.90 C ANISOU 1228 CA VAL A 181 1963 1898 1802 -634 338 -25 C ATOM 1229 C VAL A 181 32.566 52.212 20.358 1.00 14.98 C ANISOU 1229 C VAL A 181 1971 1899 1821 -622 330 -43 C ATOM 1230 O VAL A 181 33.525 52.458 21.096 1.00 18.79 O ANISOU 1230 O VAL A 181 2442 2379 2319 -628 325 -38 O ATOM 1231 CB VAL A 181 33.647 51.786 18.134 1.00 20.65 C ANISOU 1231 CB VAL A 181 2670 2651 2527 -634 352 -20 C ATOM 1232 CG1 VAL A 181 33.369 50.282 18.318 1.00 18.07 C ANISOU 1232 CG1 VAL A 181 2337 2337 2191 -612 359 -43 C ATOM 1233 CG2 VAL A 181 33.660 52.153 16.657 1.00 21.35 C ANISOU 1233 CG2 VAL A 181 2759 2747 2604 -644 361 -2 C ATOM 1234 N ASN A 182 31.497 51.534 20.772 1.00 18.33 N ANISOU 1234 N ASN A 182 2407 2320 2237 -604 329 -65 N ATOM 1235 CA ASN A 182 31.378 51.080 22.152 1.00 18.12 C ANISOU 1235 CA ASN A 182 2381 2286 2219 -590 321 -83 C ATOM 1236 C ASN A 182 31.000 49.606 22.203 1.00 21.03 C ANISOU 1236 C ASN A 182 2745 2668 2576 -569 330 -107 C ATOM 1237 O ASN A 182 30.203 49.128 21.388 1.00 16.79 O ANISOU 1237 O ASN A 182 2216 2138 2025 -562 337 -113 O ATOM 1238 CB ASN A 182 30.370 51.942 22.923 1.00 8.23 C ANISOU 1238 CB ASN A 182 1148 1009 971 -588 308 -86 C ATOM 1239 CG ASN A 182 30.884 53.356 23.107 1.00 22.83 C ANISOU 1239 CG ASN A 182 2999 2842 2835 -607 296 -64 C ATOM 1240 OD1 ASN A 182 31.769 53.600 23.939 1.00 19.01 O ANISOU 1240 OD1 ASN A 182 2504 2354 2366 -611 289 -60 O ATOM 1241 ND2 ASN A 182 30.381 54.285 22.293 1.00 19.61 N ANISOU 1241 ND2 ASN A 182 2604 2425 2423 -618 295 -49 N ATOM 1242 N CYS A 183 31.600 48.890 23.153 1.00 12.94 N ANISOU 1242 N CYS A 183 1708 1648 1558 -559 328 -118 N ATOM 1243 CA CYS A 183 31.461 47.446 23.267 1.00 14.85 C ANISOU 1243 CA CYS A 183 1945 1905 1794 -540 336 -140 C ATOM 1244 C CYS A 183 30.737 47.120 24.560 1.00 18.85 C ANISOU 1244 C CYS A 183 2460 2399 2302 -523 328 -161 C ATOM 1245 O CYS A 183 31.159 47.558 25.637 1.00 18.63 O ANISOU 1245 O CYS A 183 2429 2361 2287 -524 319 -159 O ATOM 1246 CB CYS A 183 32.830 46.757 23.247 1.00 21.17 C ANISOU 1246 CB CYS A 183 2722 2723 2601 -540 341 -136 C ATOM 1247 SG CYS A 183 33.867 47.230 21.849 1.00 23.75 S ANISOU 1247 SG CYS A 183 3035 3063 2927 -559 350 -107 S ATOM 1248 N PHE A 184 29.669 46.330 24.444 1.00 13.63 N ANISOU 1248 N PHE A 184 1810 1739 1629 -506 332 -182 N ATOM 1249 CA PHE A 184 28.801 45.960 25.554 1.00 12.48 C ANISOU 1249 CA PHE A 184 1676 1584 1483 -488 328 -203 C ATOM 1250 C PHE A 184 28.792 44.439 25.667 1.00 13.39 C ANISOU 1250 C PHE A 184 1783 1711 1593 -468 334 -226 C ATOM 1251 O PHE A 184 28.486 43.742 24.692 1.00 16.70 O ANISOU 1251 O PHE A 184 2204 2139 2004 -465 339 -232 O ATOM 1252 CB PHE A 184 27.364 46.459 25.353 1.00 12.10 C ANISOU 1252 CB PHE A 184 1649 1522 1426 -484 326 -206 C ATOM 1253 CG PHE A 184 27.241 47.945 25.133 1.00 11.46 C ANISOU 1253 CG PHE A 184 1578 1426 1351 -501 318 -183 C ATOM 1254 CD1 PHE A 184 26.843 48.777 26.163 1.00 10.77 C ANISOU 1254 CD1 PHE A 184 1499 1320 1274 -498 305 -179 C ATOM 1255 CD2 PHE A 184 27.482 48.495 23.875 1.00 11.57 C ANISOU 1255 CD2 PHE A 184 1592 1445 1361 -519 321 -165 C ATOM 1256 CE1 PHE A 184 26.700 50.161 25.966 1.00 9.90 C ANISOU 1256 CE1 PHE A 184 1399 1193 1171 -514 295 -158 C ATOM 1257 CE2 PHE A 184 27.348 49.873 23.667 1.00 21.83 C ANISOU 1257 CE2 PHE A 184 2901 2729 2666 -535 313 -144 C ATOM 1258 CZ PHE A 184 26.959 50.703 24.716 1.00 22.50 C ANISOU 1258 CZ PHE A 184 2995 2793 2762 -533 299 -141 C ATOM 1259 N MET A 185 29.124 43.926 26.850 1.00 12.08 N ANISOU 1259 N MET A 185 1611 1544 1433 -456 331 -239 N ATOM 1260 CA MET A 185 29.092 42.490 27.102 1.00 13.51 C ANISOU 1260 CA MET A 185 1788 1733 1610 -440 335 -265 C ATOM 1261 C MET A 185 27.706 42.090 27.587 1.00 10.94 C ANISOU 1261 C MET A 185 1480 1399 1277 -420 334 -287 C ATOM 1262 O MET A 185 27.160 42.726 28.493 1.00 17.69 O ANISOU 1262 O MET A 185 2343 2245 2134 -413 332 -285 O ATOM 1263 CB MET A 185 30.128 42.086 28.153 1.00 13.95 C ANISOU 1263 CB MET A 185 1831 1794 1675 -438 335 -272 C ATOM 1264 CG MET A 185 30.343 40.570 28.234 1.00 14.97 C ANISOU 1264 CG MET A 185 1954 1932 1803 -425 338 -296 C ATOM 1265 SD MET A 185 31.356 39.972 26.869 1.00 18.28 S ANISOU 1265 SD MET A 185 2356 2368 2222 -438 345 -284 S ATOM 1266 CE MET A 185 33.012 40.408 27.434 1.00 12.79 C ANISOU 1266 CE MET A 185 1640 1681 1537 -451 347 -267 C ATOM 1267 N LEU A 186 27.141 41.039 26.995 1.00 13.35 N ANISOU 1267 N LEU A 186 1788 1706 1580 -409 333 -302 N ATOM 1268 CA LEU A 186 25.884 40.490 27.494 1.00 15.49 C ANISOU 1268 CA LEU A 186 2053 1968 1865 -372 313 -287 C ATOM 1269 C LEU A 186 26.140 39.694 28.777 1.00 14.30 C ANISOU 1269 C LEU A 186 1887 1818 1729 -348 300 -285 C ATOM 1270 O LEU A 186 26.930 38.742 28.788 1.00 15.59 O ANISOU 1270 O LEU A 186 2038 1986 1898 -348 299 -292 O ATOM 1271 CB LEU A 186 25.201 39.627 26.430 1.00 14.95 C ANISOU 1271 CB LEU A 186 1981 1899 1799 -365 304 -284 C ATOM 1272 CG LEU A 186 23.890 38.931 26.850 1.00 19.57 C ANISOU 1272 CG LEU A 186 2560 2475 2400 -331 280 -269 C ATOM 1273 CD1 LEU A 186 22.865 39.935 27.363 1.00 14.99 C ANISOU 1273 CD1 LEU A 186 1991 1888 1817 -319 278 -259 C ATOM 1274 CD2 LEU A 186 23.309 38.110 25.693 1.00 16.88 C ANISOU 1274 CD2 LEU A 186 2217 2135 2062 -335 278 -268 C ATOM 1275 N ASP A 187 25.509 40.107 29.860 1.00 14.38 N ANISOU 1275 N ASP A 187 1897 1823 1744 -329 294 -274 N ATOM 1276 CA ASP A 187 25.499 39.338 31.100 1.00 10.39 C ANISOU 1276 CA ASP A 187 1377 1319 1251 -301 281 -268 C ATOM 1277 C ASP A 187 24.263 38.454 31.053 1.00 15.89 C ANISOU 1277 C ASP A 187 2069 2012 1955 -267 258 -252 C ATOM 1278 O ASP A 187 23.141 38.942 31.268 1.00 11.17 O ANISOU 1278 O ASP A 187 1470 1418 1356 -256 262 -235 O ATOM 1279 CB ASP A 187 25.490 40.262 32.324 1.00 11.90 C ANISOU 1279 CB ASP A 187 1569 1508 1443 -305 290 -265 C ATOM 1280 CG ASP A 187 25.600 39.488 33.655 1.00 19.88 C ANISOU 1280 CG ASP A 187 2564 2522 2466 -282 281 -259 C ATOM 1281 OD1 ASP A 187 25.285 38.279 33.692 1.00 13.24 O ANISOU 1281 OD1 ASP A 187 1712 1686 1631 -254 264 -248 O ATOM 1282 OD2 ASP A 187 26.000 40.091 34.669 1.00 17.45 O ANISOU 1282 OD2 ASP A 187 2256 2212 2161 -292 289 -264 O ATOM 1283 N PRO A 188 24.409 37.165 30.731 1.00 14.64 N ANISOU 1283 N PRO A 188 1904 1847 1812 -264 238 -254 N ATOM 1284 CA PRO A 188 23.214 36.320 30.568 1.00 14.75 C ANISOU 1284 CA PRO A 188 1904 1849 1852 -262 215 -232 C ATOM 1285 C PRO A 188 22.463 36.037 31.861 1.00 12.18 C ANISOU 1285 C PRO A 188 1574 1552 1503 -218 239 -227 C ATOM 1286 O PRO A 188 21.297 35.635 31.786 1.00 20.11 O ANISOU 1286 O PRO A 188 2558 2531 2550 -250 215 -203 O ATOM 1287 CB PRO A 188 23.767 35.033 29.935 1.00 18.62 C ANISOU 1287 CB PRO A 188 2385 2348 2343 -270 222 -243 C ATOM 1288 CG PRO A 188 25.202 35.012 30.269 1.00 15.91 C ANISOU 1288 CG PRO A 188 2043 2012 1992 -276 232 -260 C ATOM 1289 CD PRO A 188 25.659 36.428 30.490 1.00 13.77 C ANISOU 1289 CD PRO A 188 1785 1744 1704 -281 247 -268 C ATOM 1290 N ALA A 189 23.066 36.255 33.039 1.00 7.29 N ANISOU 1290 N ALA A 189 946 920 903 -307 298 -286 N ATOM 1291 CA ALA A 189 22.314 36.088 34.277 1.00 11.13 C ANISOU 1291 CA ALA A 189 1414 1394 1423 -244 214 -206 C ATOM 1292 C ALA A 189 21.165 37.080 34.373 1.00 17.50 C ANISOU 1292 C ALA A 189 2229 2193 2226 -241 213 -198 C ATOM 1293 O ALA A 189 20.167 36.801 35.047 1.00 16.45 O ANISOU 1293 O ALA A 189 2107 2065 2079 -277 284 -263 O ATOM 1294 CB ALA A 189 23.225 36.227 35.490 1.00 8.15 C ANISOU 1294 CB ALA A 189 1030 1018 1048 -243 214 -209 C ATOM 1295 N ILE A 190 21.300 38.257 33.756 1.00 19.93 N ANISOU 1295 N ILE A 190 2545 2525 2501 -235 251 -197 N ATOM 1296 CA ILE A 190 20.302 39.314 33.886 1.00 15.08 C ANISOU 1296 CA ILE A 190 1947 1902 1882 -242 258 -200 C ATOM 1297 C ILE A 190 19.858 39.892 32.553 1.00 16.53 C ANISOU 1297 C ILE A 190 2145 2082 2054 -251 263 -200 C ATOM 1298 O ILE A 190 19.001 40.779 32.537 1.00 21.80 O ANISOU 1298 O ILE A 190 2827 2740 2716 -258 268 -201 O ATOM 1299 CB ILE A 190 20.811 40.446 34.800 1.00 17.49 C ANISOU 1299 CB ILE A 190 2264 2200 2181 -255 270 -214 C ATOM 1300 CG1 ILE A 190 22.045 41.095 34.183 1.00 8.83 C ANISOU 1300 CG1 ILE A 190 1179 1104 1071 -274 282 -229 C ATOM 1301 CG2 ILE A 190 21.106 39.925 36.190 1.00 16.74 C ANISOU 1301 CG2 ILE A 190 2154 2107 2098 -245 265 -214 C ATOM 1302 CD1 ILE A 190 22.537 42.292 34.943 1.00 10.51 C ANISOU 1302 CD1 ILE A 190 1405 1309 1279 -296 296 -242 C ATOM 1303 N GLY A 191 20.396 39.419 31.427 1.00 18.18 N ANISOU 1303 N GLY A 191 2350 2298 2258 -251 261 -198 N ATOM 1304 CA GLY A 191 19.969 39.952 30.140 1.00 9.70 C ANISOU 1304 CA GLY A 191 1291 1222 1172 -259 265 -199 C ATOM 1305 C GLY A 191 20.201 41.443 30.024 1.00 17.69 C ANISOU 1305 C GLY A 191 2329 2225 2167 -280 278 -216 C ATOM 1306 O GLY A 191 19.289 42.218 29.718 1.00 21.64 O ANISOU 1306 O GLY A 191 2843 2716 2662 -287 282 -212 O ATOM 1307 N GLU A 192 21.404 41.867 30.352 1.00 14.16 N ANISOU 1307 N GLU A 192 1888 1778 1716 -297 287 -231 N ATOM 1308 CA GLU A 192 21.798 43.254 30.212 1.00 22.69 C ANISOU 1308 CA GLU A 192 2990 2849 2783 -329 302 -242 C ATOM 1309 C GLU A 192 23.090 43.297 29.425 1.00 19.56 C ANISOU 1309 C GLU A 192 2598 2458 2377 -354 312 -257 C ATOM 1310 O GLU A 192 23.986 42.474 29.644 1.00 16.54 O ANISOU 1310 O GLU A 192 2201 2083 2001 -349 309 -263 O ATOM 1311 CB GLU A 192 22.002 43.937 31.574 1.00 22.28 C ANISOU 1311 CB GLU A 192 2940 2790 2733 -336 310 -246 C ATOM 1312 CG GLU A 192 20.720 44.234 32.312 1.00 26.35 C ANISOU 1312 CG GLU A 192 3459 3298 3255 -324 307 -236 C ATOM 1313 CD GLU A 192 19.881 45.293 31.613 1.00 28.38 C ANISOU 1313 CD GLU A 192 3740 3543 3499 -338 312 -233 C ATOM 1314 OE1 GLU A 192 20.411 46.034 30.745 1.00 23.55 O ANISOU 1314 OE1 GLU A 192 3145 2929 2874 -361 318 -238 O ATOM 1315 OE2 GLU A 192 18.676 45.364 31.923 1.00 30.75 O ANISOU 1315 OE2 GLU A 192 4043 3838 3804 -326 308 -224 O ATOM 1316 N PHE A 193 23.178 44.256 28.508 1.00 16.34 N ANISOU 1316 N PHE A 193 2211 2046 1952 -384 325 -263 N ATOM 1317 CA PHE A 193 24.418 44.537 27.799 1.00 11.05 C ANISOU 1317 CA PHE A 193 1541 1380 1276 -413 331 -268 C ATOM 1318 C PHE A 193 25.196 45.574 28.601 1.00 23.25 C ANISOU 1318 C PHE A 193 3079 2916 2840 -424 319 -247 C ATOM 1319 O PHE A 193 24.764 46.723 28.722 1.00 21.79 O ANISOU 1319 O PHE A 193 2903 2715 2660 -431 309 -231 O ATOM 1320 CB PHE A 193 24.117 45.015 26.381 1.00 11.09 C ANISOU 1320 CB PHE A 193 1556 1384 1275 -430 332 -258 C ATOM 1321 CG PHE A 193 23.657 43.923 25.464 1.00 15.09 C ANISOU 1321 CG PHE A 193 2066 1897 1770 -424 338 -277 C ATOM 1322 CD1 PHE A 193 24.573 43.101 24.837 1.00 11.69 C ANISOU 1322 CD1 PHE A 193 1619 1478 1343 -429 337 -279 C ATOM 1323 CD2 PHE A 193 22.310 43.716 25.238 1.00 17.65 C ANISOU 1323 CD2 PHE A 193 2392 2216 2100 -403 327 -267 C ATOM 1324 CE1 PHE A 193 24.156 42.085 23.991 1.00 16.76 C ANISOU 1324 CE1 PHE A 193 2257 2123 1987 -421 333 -285 C ATOM 1325 CE2 PHE A 193 21.880 42.711 24.392 1.00 20.00 C ANISOU 1325 CE2 PHE A 193 2681 2515 2403 -391 317 -265 C ATOM 1326 CZ PHE A 193 22.801 41.888 23.777 1.00 16.27 C ANISOU 1326 CZ PHE A 193 2198 2053 1932 -401 321 -274 C ATOM 1327 N ILE A 194 26.344 45.178 29.142 1.00 14.24 N ANISOU 1327 N ILE A 194 1922 1781 1707 -425 318 -249 N ATOM 1328 CA ILE A 194 27.101 46.009 30.071 1.00 12.38 C ANISOU 1328 CA ILE A 194 1680 1536 1487 -436 308 -237 C ATOM 1329 C ILE A 194 28.247 46.666 29.322 1.00 19.32 C ANISOU 1329 C ILE A 194 2550 2417 2373 -461 304 -217 C ATOM 1330 O ILE A 194 29.047 45.973 28.682 1.00 23.61 O ANISOU 1330 O ILE A 194 3080 2975 2913 -466 312 -219 O ATOM 1331 CB ILE A 194 27.630 45.171 31.249 1.00 11.10 C ANISOU 1331 CB ILE A 194 1507 1381 1328 -423 312 -252 C ATOM 1332 CG1 ILE A 194 26.482 44.465 31.974 1.00 15.43 C ANISOU 1332 CG1 ILE A 194 2061 1932 1869 -397 320 -269 C ATOM 1333 CG2 ILE A 194 28.470 46.024 32.188 1.00 14.60 C ANISOU 1333 CG2 ILE A 194 1945 1815 1788 -435 300 -239 C ATOM 1334 CD1 ILE A 194 25.420 45.405 32.555 1.00 19.20 C ANISOU 1334 CD1 ILE A 194 2551 2394 2352 -392 311 -257 C ATOM 1335 N LEU A 195 28.361 47.996 29.438 1.00 16.92 N ANISOU 1335 N LEU A 195 2251 2097 2081 -476 291 -196 N ATOM 1336 CA LEU A 195 29.429 48.720 28.753 1.00 10.85 C ANISOU 1336 CA LEU A 195 1473 1330 1320 -500 289 -175 C ATOM 1337 C LEU A 195 30.784 48.360 29.362 1.00 14.93 C ANISOU 1337 C LEU A 195 1972 1856 1846 -506 290 -175 C ATOM 1338 O LEU A 195 31.037 48.640 30.537 1.00 15.83 O ANISOU 1338 O LEU A 195 2085 1961 1970 -504 281 -178 O ATOM 1339 CB LEU A 195 29.185 50.233 28.839 1.00 12.20 C ANISOU 1339 CB LEU A 195 1655 1479 1501 -513 274 -156 C ATOM 1340 CG LEU A 195 30.176 51.128 28.091 1.00 15.59 C ANISOU 1340 CG LEU A 195 2077 1909 1939 -538 273 -132 C ATOM 1341 CD1 LEU A 195 30.236 50.755 26.625 1.00 11.08 C ANISOU 1341 CD1 LEU A 195 1503 1353 1352 -547 288 -128 C ATOM 1342 CD2 LEU A 195 29.831 52.604 28.251 1.00 21.13 C ANISOU 1342 CD2 LEU A 195 2791 2587 2651 -549 258 -116 C ATOM 1343 N VAL A 196 31.662 47.753 28.570 1.00 14.96 N ANISOU 1343 N VAL A 196 1960 1878 1846 -512 300 -172 N ATOM 1344 CA VAL A 196 32.963 47.330 29.070 1.00 16.91 C ANISOU 1344 CA VAL A 196 2189 2135 2101 -518 302 -172 C ATOM 1345 C VAL A 196 34.127 47.940 28.302 1.00 15.48 C ANISOU 1345 C VAL A 196 1995 1961 1927 -540 303 -148 C ATOM 1346 O VAL A 196 35.264 47.881 28.790 1.00 23.44 O ANISOU 1346 O VAL A 196 2988 2974 2945 -548 303 -143 O ATOM 1347 CB VAL A 196 33.094 45.785 29.078 1.00 15.45 C ANISOU 1347 CB VAL A 196 1996 1968 1907 -501 314 -194 C ATOM 1348 CG1 VAL A 196 32.002 45.154 29.922 1.00 16.37 C ANISOU 1348 CG1 VAL A 196 2125 2079 2017 -478 314 -219 C ATOM 1349 CG2 VAL A 196 33.084 45.228 27.647 1.00 7.12 C ANISOU 1349 CG2 VAL A 196 938 928 841 -502 325 -192 C ATOM 1350 N ASP A 197 33.912 48.502 27.115 1.00 19.61 N ANISOU 1350 N ASP A 197 2521 2484 2445 -550 306 -133 N ATOM 1351 CA ASP A 197 34.981 49.123 26.331 1.00 21.45 C ANISOU 1351 CA ASP A 197 2742 2724 2685 -571 309 -109 C ATOM 1352 C ASP A 197 34.448 50.394 25.693 1.00 16.61 C ANISOU 1352 C ASP A 197 2142 2096 2073 -584 303 -91 C ATOM 1353 O ASP A 197 33.637 50.325 24.766 1.00 17.57 O ANISOU 1353 O ASP A 197 2275 2220 2181 -582 310 -93 O ATOM 1354 CB ASP A 197 35.507 48.176 25.258 1.00 24.79 C ANISOU 1354 CB ASP A 197 3152 3170 3098 -569 325 -109 C ATOM 1355 CG ASP A 197 36.718 47.413 25.708 1.00 46.27 C ANISOU 1355 CG ASP A 197 5852 5904 5823 -569 330 -112 C ATOM 1356 OD1 ASP A 197 37.823 47.998 25.640 1.00 50.09 O ANISOU 1356 OD1 ASP A 197 6324 6390 6318 -586 329 -94 O ATOM 1357 OD2 ASP A 197 36.565 46.247 26.140 1.00 50.17 O ANISOU 1357 OD2 ASP A 197 6345 6407 6312 -552 334 -134 O ATOM 1358 N LYS A 198 34.940 51.541 26.143 1.00 17.18 N ANISOU 1358 N LYS A 198 2215 2154 2161 -599 292 -75 N ATOM 1359 CA LYS A 198 34.427 52.828 25.696 1.00 25.22 C ANISOU 1359 CA LYS A 198 3248 3155 3180 -612 285 -61 C ATOM 1360 C LYS A 198 35.325 53.419 24.621 1.00 18.04 C ANISOU 1360 C LYS A 198 2328 2253 2272 -633 292 -38 C ATOM 1361 O LYS A 198 36.557 53.395 24.734 1.00 19.74 O ANISOU 1361 O LYS A 198 2526 2478 2498 -642 294 -28 O ATOM 1362 CB LYS A 198 34.319 53.818 26.860 1.00 25.27 C ANISOU 1362 CB LYS A 198 3261 3137 3202 -615 267 -57 C ATOM 1363 CG LYS A 198 33.491 53.344 28.036 1.00 32.77 C ANISOU 1363 CG LYS A 198 4222 4079 4152 -595 260 -79 C ATOM 1364 CD LYS A 198 33.480 54.406 29.132 1.00 38.23 C ANISOU 1364 CD LYS A 198 4922 4747 4858 -601 242 -75 C ATOM 1365 CE LYS A 198 32.892 53.873 30.438 1.00 47.00 C ANISOU 1365 CE LYS A 198 6039 5851 5969 -582 236 -96 C ATOM 1366 NZ LYS A 198 32.928 54.895 31.529 1.00 52.49 N ANISOU 1366 NZ LYS A 198 6741 6524 6678 -587 219 -92 N ATOM 1367 N ASP A 199 34.693 53.985 23.598 1.00 18.65 N ANISOU 1367 N ASP A 199 2418 2328 2340 -641 295 -29 N ATOM 1368 CA ASP A 199 35.386 54.758 22.571 1.00 22.84 C ANISOU 1368 CA ASP A 199 2943 2862 2872 -661 300 -5 C ATOM 1369 C ASP A 199 36.598 53.995 22.024 1.00 26.39 C ANISOU 1369 C ASP A 199 3369 3335 3321 -664 314 0 C ATOM 1370 O ASP A 199 37.742 54.446 22.090 1.00 21.14 O ANISOU 1370 O ASP A 199 2691 2672 2668 -677 313 15 O ATOM 1371 CB ASP A 199 35.801 56.119 23.136 1.00 26.06 C ANISOU 1371 CB ASP A 199 3354 3249 3297 -677 287 10 C ATOM 1372 CG ASP A 199 36.013 57.164 22.058 1.00 34.96 C ANISOU 1372 CG ASP A 199 4486 4374 4425 -696 289 32 C ATOM 1373 OD1 ASP A 199 35.715 56.882 20.876 1.00 34.79 O ANISOU 1373 OD1 ASP A 199 4466 4365 4388 -697 301 36 O ATOM 1374 OD2 ASP A 199 36.455 58.280 22.402 1.00 41.75 O ANISOU 1374 OD2 ASP A 199 5347 5218 5298 -710 279 46 O ATOM 1375 N VAL A 200 36.325 52.807 21.486 1.00 25.54 N ANISOU 1375 N VAL A 200 3259 3247 3200 -650 326 -12 N ATOM 1376 CA VAL A 200 37.395 51.908 21.078 1.00 21.84 C ANISOU 1376 CA VAL A 200 2768 2800 2730 -647 338 -9 C ATOM 1377 C VAL A 200 38.090 52.436 19.824 1.00 22.47 C ANISOU 1377 C VAL A 200 2840 2890 2809 -663 347 14 C ATOM 1378 O VAL A 200 37.441 52.930 18.890 1.00 29.69 O ANISOU 1378 O VAL A 200 3766 3801 3712 -669 350 21 O ATOM 1379 CB VAL A 200 36.809 50.500 20.864 1.00 29.56 C ANISOU 1379 CB VAL A 200 3745 3792 3694 -625 347 -30 C ATOM 1380 CG1 VAL A 200 37.801 49.590 20.188 1.00 31.79 C ANISOU 1380 CG1 VAL A 200 4007 4098 3973 -623 360 -26 C ATOM 1381 CG2 VAL A 200 36.376 49.919 22.203 1.00 26.44 C ANISOU 1381 CG2 VAL A 200 3354 3390 3303 -609 338 -52 C ATOM 1382 N LYS A 201 39.427 52.325 19.796 1.00 19.43 N ANISOU 1382 N LYS A 201 2433 2514 2433 -670 352 26 N ATOM 1383 CA LYS A 201 40.247 52.659 18.636 1.00 24.77 C ANISOU 1383 CA LYS A 201 3099 3203 3109 -683 363 47 C ATOM 1384 C LYS A 201 41.119 51.460 18.295 1.00 26.97 C ANISOU 1384 C LYS A 201 3359 3505 3384 -675 377 43 C ATOM 1385 O LYS A 201 41.611 50.766 19.189 1.00 30.41 O ANISOU 1385 O LYS A 201 3784 3945 3825 -669 376 31 O ATOM 1386 CB LYS A 201 41.147 53.882 18.879 1.00 21.67 C ANISOU 1386 CB LYS A 201 2702 2799 2733 -705 356 67 C ATOM 1387 CG LYS A 201 40.414 55.172 19.244 1.00 26.95 C ANISOU 1387 CG LYS A 201 3390 3443 3406 -716 342 71 C ATOM 1388 CD LYS A 201 39.453 55.638 18.160 1.00 24.27 C ANISOU 1388 CD LYS A 201 3069 3102 3053 -720 346 76 C ATOM 1389 CE LYS A 201 38.614 56.816 18.662 1.00 23.11 C ANISOU 1389 CE LYS A 201 2942 2928 2910 -727 331 78 C ATOM 1390 NZ LYS A 201 37.542 57.235 17.701 1.00 22.67 N ANISOU 1390 NZ LYS A 201 2905 2868 2840 -729 333 82 N ATOM 1391 N ILE A 202 41.283 51.201 17.010 1.00 21.72 N ANISOU 1391 N ILE A 202 2689 2855 2708 -677 391 52 N ATOM 1392 CA ILE A 202 42.112 50.089 16.555 1.00 21.96 C ANISOU 1392 CA ILE A 202 2702 2908 2733 -670 405 49 C ATOM 1393 C ILE A 202 43.580 50.510 16.546 1.00 21.47 C ANISOU 1393 C ILE A 202 2621 2851 2684 -686 409 67 C ATOM 1394 O ILE A 202 43.906 51.690 16.376 1.00 26.09 O ANISOU 1394 O ILE A 202 3209 3426 3279 -703 405 86 O ATOM 1395 CB ILE A 202 41.645 49.613 15.164 1.00 19.66 C ANISOU 1395 CB ILE A 202 2416 2631 2425 -665 418 51 C ATOM 1396 CG1 ILE A 202 42.225 48.237 14.826 1.00 22.25 C ANISOU 1396 CG1 ILE A 202 2728 2980 2745 -653 432 41 C ATOM 1397 CG2 ILE A 202 41.997 50.643 14.098 1.00 24.71 C ANISOU 1397 CG2 ILE A 202 3054 3270 3064 -682 423 76 C ATOM 1398 CD1 ILE A 202 41.716 47.676 13.531 1.00 21.21 C ANISOU 1398 CD1 ILE A 202 2601 2861 2596 -645 443 40 C ATOM 1399 N LYS A 203 44.473 49.538 16.760 1.00 23.78 N ANISOU 1399 N LYS A 203 2896 3159 2978 -680 417 62 N ATOM 1400 CA LYS A 203 45.911 49.768 16.636 1.00 24.45 C ANISOU 1400 CA LYS A 203 2963 3253 3076 -694 424 79 C ATOM 1401 C LYS A 203 46.256 50.316 15.258 1.00 22.74 C ANISOU 1401 C LYS A 203 2743 3042 2853 -706 435 100 C ATOM 1402 O LYS A 203 45.651 49.933 14.253 1.00 25.48 O ANISOU 1402 O LYS A 203 3097 3398 3185 -699 444 98 O ATOM 1403 CB LYS A 203 46.693 48.470 16.837 1.00 27.89 C ANISOU 1403 CB LYS A 203 3380 3706 3510 -682 434 69 C ATOM 1404 CG LYS A 203 46.770 47.929 18.233 1.00 39.09 C ANISOU 1404 CG LYS A 203 4796 5121 4937 -674 425 53 C ATOM 1405 CD LYS A 203 47.702 46.712 18.239 1.00 47.90 C ANISOU 1405 CD LYS A 203 5893 6256 6053 -664 436 48 C ATOM 1406 CE LYS A 203 47.686 45.986 19.574 1.00 50.33 C ANISOU 1406 CE LYS A 203 6198 6560 6366 -653 428 28 C ATOM 1407 NZ LYS A 203 47.701 44.502 19.405 1.00 50.19 N ANISOU 1407 NZ LYS A 203 6174 6559 6338 -634 438 12 N ATOM 1408 N LYS A 204 47.257 51.201 15.214 1.00 19.74 N ANISOU 1408 N LYS A 204 2354 2659 2487 -724 435 120 N ATOM 1409 CA LYS A 204 47.691 51.795 13.950 1.00 24.82 C ANISOU 1409 CA LYS A 204 2994 3308 3127 -737 446 140 C ATOM 1410 C LYS A 204 48.277 50.747 13.014 1.00 17.25 C ANISOU 1410 C LYS A 204 2022 2373 2159 -729 464 141 C ATOM 1411 O LYS A 204 48.096 50.821 11.795 1.00 23.73 O ANISOU 1411 O LYS A 204 2847 3202 2969 -731 474 150 O ATOM 1412 CB LYS A 204 48.691 52.921 14.238 1.00 32.60 C ANISOU 1412 CB LYS A 204 3971 4284 4130 -757 441 159 C ATOM 1413 CG LYS A 204 48.976 53.849 13.069 1.00 36.50 C ANISOU 1413 CG LYS A 204 4467 4778 4622 -773 448 181 C ATOM 1414 CD LYS A 204 49.711 55.110 13.551 1.00 36.34 C ANISOU 1414 CD LYS A 204 4444 4743 4621 -793 439 197 C ATOM 1415 CE LYS A 204 51.156 55.185 13.074 1.00 34.10 C ANISOU 1415 CE LYS A 204 4140 4471 4345 -806 452 214 C ATOM 1416 NZ LYS A 204 51.240 55.560 11.645 1.00 29.61 N ANISOU 1416 NZ LYS A 204 3573 3909 3767 -813 464 229 N ATOM 1417 N LYS A 205 48.947 49.749 13.567 1.00 16.10 N ANISOU 1417 N LYS A 205 1862 2239 2017 -720 469 132 N ATOM 1418 CA LYS A 205 49.511 48.673 12.778 1.00 26.42 C ANISOU 1418 CA LYS A 205 3156 3568 3316 -711 486 131 C ATOM 1419 C LYS A 205 49.418 47.413 13.617 1.00 24.49 C ANISOU 1419 C LYS A 205 2906 3328 3069 -693 484 109 C ATOM 1420 O LYS A 205 49.643 47.453 14.828 1.00 23.26 O ANISOU 1420 O LYS A 205 2747 3165 2926 -693 474 102 O ATOM 1421 CB LYS A 205 50.961 48.964 12.382 1.00 32.15 C ANISOU 1421 CB LYS A 205 3862 4301 4051 -725 496 151 C ATOM 1422 CG LYS A 205 51.544 47.995 11.366 1.00 35.62 C ANISOU 1422 CG LYS A 205 4290 4762 4482 -718 515 153 C ATOM 1423 CD LYS A 205 52.964 48.398 10.990 1.00 37.76 C ANISOU 1423 CD LYS A 205 4543 5040 4765 -733 525 174 C ATOM 1424 CE LYS A 205 53.621 47.338 10.130 1.00 45.81 C ANISOU 1424 CE LYS A 205 5549 6081 5777 -724 544 176 C ATOM 1425 NZ LYS A 205 53.099 47.353 8.741 1.00 51.19 N ANISOU 1425 NZ LYS A 205 6240 6769 6442 -724 555 180 N ATOM 1426 N GLY A 206 49.049 46.306 12.975 1.00 20.40 N ANISOU 1426 N GLY A 206 2390 2825 2537 -678 495 97 N ATOM 1427 CA GLY A 206 48.890 45.041 13.649 1.00 16.76 C ANISOU 1427 CA GLY A 206 1926 2370 2073 -659 494 75 C ATOM 1428 C GLY A 206 49.960 44.047 13.247 1.00 25.57 C ANISOU 1428 C GLY A 206 3023 3505 3189 -654 510 77 C ATOM 1429 O GLY A 206 50.912 44.366 12.530 1.00 23.93 O ANISOU 1429 O GLY A 206 2803 3305 2985 -665 521 97 O ATOM 1430 N LYS A 207 49.768 42.809 13.710 1.00 21.68 N ANISOU 1430 N LYS A 207 2528 3019 2692 -636 511 57 N ATOM 1431 CA LYS A 207 50.708 41.719 13.473 1.00 27.60 C ANISOU 1431 CA LYS A 207 3260 3784 3442 -628 524 56 C ATOM 1432 C LYS A 207 50.005 40.428 13.061 1.00 26.43 C ANISOU 1432 C LYS A 207 3119 3645 3279 -608 530 36 C ATOM 1433 O LYS A 207 50.584 39.342 13.195 1.00 23.01 O ANISOU 1433 O LYS A 207 2674 3222 2847 -597 537 28 O ATOM 1434 CB LYS A 207 51.568 41.479 14.721 1.00 36.22 C ANISOU 1434 CB LYS A 207 4338 4875 4550 -628 519 54 C ATOM 1435 CG LYS A 207 52.616 42.562 14.965 1.00 47.23 C ANISOU 1435 CG LYS A 207 5720 6265 5961 -648 517 77 C ATOM 1436 CD LYS A 207 53.281 42.420 16.326 1.00 54.17 C ANISOU 1436 CD LYS A 207 6587 7140 6856 -648 508 73 C ATOM 1437 CE LYS A 207 54.249 43.569 16.596 1.00 55.45 C ANISOU 1437 CE LYS A 207 6738 7295 7034 -669 505 95 C ATOM 1438 NZ LYS A 207 54.767 43.549 17.996 1.00 56.96 N ANISOU 1438 NZ LYS A 207 6920 7480 7241 -670 494 91 N ATOM 1439 N ILE A 208 48.775 40.518 12.558 1.00 21.02 N ANISOU 1439 N ILE A 208 2452 2954 2580 -603 526 27 N ATOM 1440 CA ILE A 208 47.994 39.355 12.144 1.00 19.76 C ANISOU 1440 CA ILE A 208 2302 2801 2407 -585 530 7 C ATOM 1441 C ILE A 208 47.338 39.664 10.806 1.00 15.03 C ANISOU 1441 C ILE A 208 1713 2204 1793 -588 536 14 C ATOM 1442 O ILE A 208 46.851 40.778 10.592 1.00 18.90 O ANISOU 1442 O ILE A 208 2214 2685 2282 -600 531 24 O ATOM 1443 CB ILE A 208 46.926 38.984 13.189 1.00 19.43 C ANISOU 1443 CB ILE A 208 2273 2746 2363 -573 515 -17 C ATOM 1444 CG1 ILE A 208 47.577 38.603 14.519 1.00 16.16 C ANISOU 1444 CG1 ILE A 208 1848 2330 1963 -569 509 -25 C ATOM 1445 CG2 ILE A 208 45.996 37.878 12.649 1.00 13.17 C ANISOU 1445 CG2 ILE A 208 1491 1958 1557 -555 518 -37 C ATOM 1446 CD1 ILE A 208 46.607 38.585 15.661 1.00 28.76 C ANISOU 1446 CD1 ILE A 208 3457 3911 3560 -561 494 -45 C ATOM 1447 N TYR A 209 47.363 38.702 9.888 1.00 15.67 N ANISOU 1447 N TYR A 209 1792 2298 1863 -579 549 9 N ATOM 1448 CA TYR A 209 46.611 38.806 8.644 1.00 15.71 C ANISOU 1448 CA TYR A 209 1810 2306 1853 -579 554 12 C ATOM 1449 C TYR A 209 45.574 37.687 8.581 1.00 17.11 C ANISOU 1449 C TYR A 209 1999 2484 2019 -561 551 -12 C ATOM 1450 O TYR A 209 45.778 36.601 9.130 1.00 16.93 O ANISOU 1450 O TYR A 209 1970 2464 1999 -548 552 -28 O ATOM 1451 CB TYR A 209 47.543 38.758 7.412 1.00 18.14 C ANISOU 1451 CB TYR A 209 2106 2629 2157 -586 572 31 C ATOM 1452 CG TYR A 209 48.149 37.394 7.126 1.00 21.83 C ANISOU 1452 CG TYR A 209 2562 3110 2622 -574 584 23 C ATOM 1453 CD1 TYR A 209 49.353 37.013 7.707 1.00 18.12 C ANISOU 1453 CD1 TYR A 209 2073 2646 2164 -574 589 27 C ATOM 1454 CD2 TYR A 209 47.528 36.497 6.258 1.00 19.51 C ANISOU 1454 CD2 TYR A 209 2276 2823 2314 -562 590 11 C ATOM 1455 CE1 TYR A 209 49.912 35.781 7.444 1.00 25.17 C ANISOU 1455 CE1 TYR A 209 2955 3551 3055 -562 600 21 C ATOM 1456 CE2 TYR A 209 48.084 35.251 5.987 1.00 12.88 C ANISOU 1456 CE2 TYR A 209 1427 1996 1473 -551 601 5 C ATOM 1457 CZ TYR A 209 49.284 34.905 6.576 1.00 24.31 C ANISOU 1457 CZ TYR A 209 2855 3448 2932 -551 606 9 C ATOM 1458 OH TYR A 209 49.859 33.670 6.336 1.00 25.10 O ANISOU 1458 OH TYR A 209 2946 3560 3032 -540 618 3 O ATOM 1459 N SER A 210 44.454 37.955 7.905 1.00 19.92 N ANISOU 1459 N SER A 210 2372 2835 2363 -560 548 -15 N ATOM 1460 CA SER A 210 43.285 37.076 7.970 1.00 18.69 C ANISOU 1460 CA SER A 210 2229 2675 2197 -544 542 -39 C ATOM 1461 C SER A 210 42.629 36.979 6.598 1.00 16.23 C ANISOU 1461 C SER A 210 1927 2369 1869 -543 549 -35 C ATOM 1462 O SER A 210 42.019 37.950 6.138 1.00 17.66 O ANISOU 1462 O SER A 210 2120 2545 2046 -552 546 -25 O ATOM 1463 CB SER A 210 42.286 37.607 9.006 1.00 18.96 C ANISOU 1463 CB SER A 210 2277 2692 2236 -542 525 -50 C ATOM 1464 OG SER A 210 41.221 36.704 9.241 1.00 22.14 O ANISOU 1464 OG SER A 210 2692 3090 2632 -526 518 -74 O ATOM 1465 N LEU A 211 42.723 35.806 5.967 1.00 17.44 N ANISOU 1465 N LEU A 211 2078 2534 2017 -533 558 -44 N ATOM 1466 CA LEU A 211 42.037 35.493 4.714 1.00 15.30 C ANISOU 1466 CA LEU A 211 1816 2268 1729 -530 564 -45 C ATOM 1467 C LEU A 211 42.150 33.992 4.467 1.00 17.72 C ANISOU 1467 C LEU A 211 2118 2582 2032 -516 571 -60 C ATOM 1468 O LEU A 211 42.990 33.316 5.064 1.00 15.60 O ANISOU 1468 O LEU A 211 1837 2319 1773 -510 574 -64 O ATOM 1469 CB LEU A 211 42.618 36.280 3.534 1.00 23.37 C ANISOU 1469 CB LEU A 211 2834 3299 2746 -544 577 -20 C ATOM 1470 CG LEU A 211 43.873 35.715 2.866 1.00 16.98 C ANISOU 1470 CG LEU A 211 2008 2506 1937 -546 594 -10 C ATOM 1471 CD1 LEU A 211 44.265 36.527 1.606 1.00 19.22 C ANISOU 1471 CD1 LEU A 211 2291 2797 2214 -560 605 13 C ATOM 1472 CD2 LEU A 211 45.044 35.621 3.838 1.00 19.88 C ANISOU 1472 CD2 LEU A 211 2359 2875 2321 -547 595 -7 C ATOM 1473 N ASN A 212 41.304 33.478 3.575 1.00 22.06 N ANISOU 1473 N ASN A 212 2679 3135 2570 -510 573 -67 N ATOM 1474 CA ASN A 212 41.356 32.057 3.221 1.00 20.39 C ANISOU 1474 CA ASN A 212 2463 2930 2353 -497 579 -80 C ATOM 1475 C ASN A 212 42.471 31.834 2.209 1.00 18.52 C ANISOU 1475 C ASN A 212 2213 2709 2113 -502 598 -65 C ATOM 1476 O ASN A 212 42.266 32.004 1.011 1.00 25.83 O ANISOU 1476 O ASN A 212 3144 3642 3027 -507 606 -55 O ATOM 1477 CB ASN A 212 40.028 31.575 2.648 1.00 20.33 C ANISOU 1477 CB ASN A 212 2472 2918 2334 -489 574 -93 C ATOM 1478 CG ASN A 212 40.012 30.055 2.398 1.00 22.16 C ANISOU 1478 CG ASN A 212 2700 3155 2563 -476 578 -108 C ATOM 1479 OD1 ASN A 212 41.038 29.377 2.490 1.00 16.01 O ANISOU 1479 OD1 ASN A 212 1908 2385 1790 -473 588 -107 O ATOM 1480 ND2 ASN A 212 38.841 29.526 2.074 1.00 27.30 N ANISOU 1480 ND2 ASN A 212 3364 3801 3207 -468 571 -121 N ATOM 1481 N GLU A 213 43.640 31.383 2.682 1.00 21.15 N ANISOU 1481 N GLU A 213 2530 3049 2456 -501 605 -62 N ATOM 1482 CA GLU A 213 44.770 31.102 1.801 1.00 25.10 C ANISOU 1482 CA GLU A 213 3018 3565 2955 -505 623 -48 C ATOM 1483 C GLU A 213 44.642 29.786 1.047 1.00 24.26 C ANISOU 1483 C GLU A 213 2912 3466 2839 -493 632 -58 C ATOM 1484 O GLU A 213 45.469 29.514 0.173 1.00 27.56 O ANISOU 1484 O GLU A 213 3321 3897 3254 -496 648 -47 O ATOM 1485 CB GLU A 213 46.072 31.051 2.599 1.00 27.52 C ANISOU 1485 CB GLU A 213 3305 3875 3276 -506 628 -41 C ATOM 1486 CG GLU A 213 46.594 32.382 3.090 1.00 23.99 C ANISOU 1486 CG GLU A 213 2853 3423 2838 -521 624 -24 C ATOM 1487 CD GLU A 213 48.010 32.250 3.623 1.00 26.88 C ANISOU 1487 CD GLU A 213 3199 3796 3218 -524 632 -14 C ATOM 1488 OE1 GLU A 213 48.944 32.022 2.819 1.00 26.44 O ANISOU 1488 OE1 GLU A 213 3131 3753 3161 -527 648 -1 O ATOM 1489 OE2 GLU A 213 48.180 32.329 4.854 1.00 27.95 O ANISOU 1489 OE2 GLU A 213 3330 3925 3366 -522 622 -20 O ATOM 1490 N GLY A 214 43.643 28.964 1.362 1.00 21.12 N ANISOU 1490 N GLY A 214 2525 3061 2439 -481 622 -79 N ATOM 1491 CA GLY A 214 43.439 27.741 0.609 1.00 19.96 C ANISOU 1491 CA GLY A 214 2379 2920 2284 -471 629 -89 C ATOM 1492 C GLY A 214 43.129 27.983 -0.854 1.00 29.05 C ANISOU 1492 C GLY A 214 3538 4080 3420 -478 639 -79 C ATOM 1493 O GLY A 214 43.373 27.116 -1.696 1.00 30.62 O ANISOU 1493 O GLY A 214 3734 4288 3612 -473 651 -80 O ATOM 1494 N TYR A 215 42.583 29.155 -1.176 1.00 30.89 N ANISOU 1494 N TYR A 215 3780 4308 3647 -488 634 -68 N ATOM 1495 CA TYR A 215 42.254 29.514 -2.546 1.00 22.94 C ANISOU 1495 CA TYR A 215 2781 3308 2626 -495 643 -58 C ATOM 1496 C TYR A 215 43.352 30.351 -3.191 1.00 19.02 C ANISOU 1496 C TYR A 215 2274 2822 2129 -509 657 -33 C ATOM 1497 O TYR A 215 43.082 31.141 -4.103 1.00 32.51 O ANISOU 1497 O TYR A 215 3990 4533 3828 -519 660 -20 O ATOM 1498 CB TYR A 215 40.902 30.225 -2.574 1.00 23.56 C ANISOU 1498 CB TYR A 215 2877 3376 2698 -497 629 -61 C ATOM 1499 CG TYR A 215 39.779 29.303 -2.122 1.00 34.75 C ANISOU 1499 CG TYR A 215 4304 4784 4114 -484 616 -84 C ATOM 1500 CD1 TYR A 215 39.971 27.922 -2.083 1.00 36.91 C ANISOU 1500 CD1 TYR A 215 4574 5062 4390 -472 620 -98 C ATOM 1501 CD2 TYR A 215 38.549 29.803 -1.708 1.00 36.80 C ANISOU 1501 CD2 TYR A 215 4579 5031 4373 -483 601 -92 C ATOM 1502 CE1 TYR A 215 38.975 27.068 -1.659 1.00 41.91 C ANISOU 1502 CE1 TYR A 215 5216 5686 5024 -460 609 -118 C ATOM 1503 CE2 TYR A 215 37.539 28.950 -1.274 1.00 43.83 C ANISOU 1503 CE2 TYR A 215 5477 5912 5264 -470 589 -112 C ATOM 1504 CZ TYR A 215 37.761 27.580 -1.254 1.00 47.07 C ANISOU 1504 CZ TYR A 215 5882 6326 5676 -460 593 -125 C ATOM 1505 OH TYR A 215 36.778 26.709 -0.836 1.00 47.45 O ANISOU 1505 OH TYR A 215 5937 6364 5726 -448 581 -145 O ATOM 1506 N ALA A 216 44.595 30.169 -2.736 1.00 22.18 N ANISOU 1506 N ALA A 216 2658 3228 2541 -510 665 -27 N ATOM 1507 CA ALA A 216 45.714 30.982 -3.212 1.00 23.37 C ANISOU 1507 CA ALA A 216 2798 3388 2695 -523 677 -3 C ATOM 1508 C ALA A 216 45.895 30.930 -4.719 1.00 28.94 C ANISOU 1508 C ALA A 216 3504 4104 3386 -528 693 8 C ATOM 1509 O ALA A 216 46.354 31.915 -5.314 1.00 26.44 O ANISOU 1509 O ALA A 216 3185 3792 3068 -542 700 28 O ATOM 1510 CB ALA A 216 47.006 30.543 -2.521 1.00 20.46 C ANISOU 1510 CB ALA A 216 2409 3023 2340 -521 685 0 C ATOM 1511 N LYS A 217 45.558 29.804 -5.350 1.00 32.10 N ANISOU 1511 N LYS A 217 3908 4510 3777 -518 699 -4 N ATOM 1512 CA LYS A 217 45.747 29.694 -6.792 1.00 29.57 C ANISOU 1512 CA LYS A 217 3590 4201 3444 -523 714 7 C ATOM 1513 C LYS A 217 44.896 30.701 -7.559 1.00 29.51 C ANISOU 1513 C LYS A 217 3597 4191 3425 -534 710 16 C ATOM 1514 O LYS A 217 45.204 31.009 -8.716 1.00 30.64 O ANISOU 1514 O LYS A 217 3741 4343 3559 -542 723 30 O ATOM 1515 CB LYS A 217 45.444 28.277 -7.294 1.00 21.96 C ANISOU 1515 CB LYS A 217 2630 3243 2473 -511 720 -8 C ATOM 1516 CG LYS A 217 43.968 27.918 -7.465 1.00 37.15 C ANISOU 1516 CG LYS A 217 4570 5158 4385 -504 708 -25 C ATOM 1517 CD LYS A 217 43.829 26.569 -8.194 1.00 40.52 C ANISOU 1517 CD LYS A 217 5000 5592 4805 -494 717 -36 C ATOM 1518 CE LYS A 217 42.372 26.181 -8.438 1.00 42.56 C ANISOU 1518 CE LYS A 217 5275 5843 5052 -488 705 -52 C ATOM 1519 NZ LYS A 217 42.242 24.791 -9.001 1.00 34.01 N ANISOU 1519 NZ LYS A 217 4193 4765 3964 -478 713 -64 N ATOM 1520 N ASP A 218 43.825 31.207 -6.948 1.00 25.76 N ANISOU 1520 N ASP A 218 3135 3704 2951 -533 693 7 N ATOM 1521 CA ASP A 218 42.938 32.203 -7.548 1.00 26.15 C ANISOU 1521 CA ASP A 218 3198 3749 2990 -542 686 15 C ATOM 1522 C ASP A 218 43.266 33.636 -7.124 1.00 31.92 C ANISOU 1522 C ASP A 218 3926 4473 3728 -556 681 33 C ATOM 1523 O ASP A 218 42.579 34.570 -7.563 1.00 22.84 O ANISOU 1523 O ASP A 218 2788 3319 2571 -564 676 41 O ATOM 1524 CB ASP A 218 41.475 31.889 -7.225 1.00 28.14 C ANISOU 1524 CB ASP A 218 3466 3990 3236 -533 671 -3 C ATOM 1525 CG ASP A 218 40.999 30.605 -7.889 1.00 33.52 C ANISOU 1525 CG ASP A 218 4153 4677 3908 -522 675 -18 C ATOM 1526 OD1 ASP A 218 41.711 30.097 -8.772 1.00 36.21 O ANISOU 1526 OD1 ASP A 218 4486 5029 4242 -523 691 -11 O ATOM 1527 OD2 ASP A 218 39.911 30.103 -7.526 1.00 41.96 O ANISOU 1527 OD2 ASP A 218 5231 5736 4974 -512 663 -35 O ATOM 1528 N PHE A 219 44.267 33.833 -6.258 1.00 28.34 N ANISOU 1528 N PHE A 219 3459 4019 3290 -558 683 38 N ATOM 1529 CA PHE A 219 44.581 35.167 -5.753 1.00 22.71 C ANISOU 1529 CA PHE A 219 2743 3299 2586 -571 677 53 C ATOM 1530 C PHE A 219 44.882 36.147 -6.875 1.00 30.89 C ANISOU 1530 C PHE A 219 3781 4341 3616 -587 686 76 C ATOM 1531 O PHE A 219 45.527 35.811 -7.874 1.00 35.10 O ANISOU 1531 O PHE A 219 4309 4887 4143 -590 702 85 O ATOM 1532 CB PHE A 219 45.793 35.138 -4.812 1.00 25.35 C ANISOU 1532 CB PHE A 219 3060 3635 2938 -572 679 58 C ATOM 1533 CG PHE A 219 45.488 34.650 -3.427 1.00 29.31 C ANISOU 1533 CG PHE A 219 3560 4127 3449 -561 666 39 C ATOM 1534 CD1 PHE A 219 44.185 34.362 -3.037 1.00 27.19 C ANISOU 1534 CD1 PHE A 219 3306 3848 3175 -552 652 20 C ATOM 1535 CD2 PHE A 219 46.507 34.531 -2.494 1.00 24.66 C ANISOU 1535 CD2 PHE A 219 2956 3538 2876 -561 667 41 C ATOM 1536 CE1 PHE A 219 43.913 33.933 -1.742 1.00 24.97 C ANISOU 1536 CE1 PHE A 219 3025 3558 2904 -542 639 3 C ATOM 1537 CE2 PHE A 219 46.240 34.099 -1.206 1.00 23.29 C ANISOU 1537 CE2 PHE A 219 2781 3356 2712 -551 655 24 C ATOM 1538 CZ PHE A 219 44.947 33.800 -0.831 1.00 22.54 C ANISOU 1538 CZ PHE A 219 2702 3252 2612 -541 641 5 C ATOM 1539 N ASP A 220 44.421 37.375 -6.686 1.00 31.65 N ANISOU 1539 N ASP A 220 3886 4428 3713 -597 676 86 N ATOM 1540 CA ASP A 220 44.921 38.481 -7.474 1.00 30.38 C ANISOU 1540 CA ASP A 220 3723 4269 3550 -614 683 110 C ATOM 1541 C ASP A 220 46.408 38.667 -7.162 1.00 31.35 C ANISOU 1541 C ASP A 220 3826 4397 3687 -622 693 123 C ATOM 1542 O ASP A 220 46.840 38.428 -6.031 1.00 29.37 O ANISOU 1542 O ASP A 220 3566 4142 3450 -617 688 117 O ATOM 1543 CB ASP A 220 44.118 39.739 -7.128 1.00 37.01 C ANISOU 1543 CB ASP A 220 4576 5096 4392 -623 668 116 C ATOM 1544 CG ASP A 220 44.500 40.935 -7.961 1.00 52.73 C ANISOU 1544 CG ASP A 220 6567 7087 6381 -641 674 141 C ATOM 1545 OD1 ASP A 220 45.615 41.467 -7.771 1.00 57.17 O ANISOU 1545 OD1 ASP A 220 7116 7651 6955 -652 680 156 O ATOM 1546 OD2 ASP A 220 43.673 41.347 -8.801 1.00 59.27 O ANISOU 1546 OD2 ASP A 220 7410 7915 7197 -645 672 145 O ATOM 1547 N PRO A 221 47.215 39.091 -8.144 1.00 32.09 N ANISOU 1547 N PRO A 221 3914 4499 3779 -633 707 143 N ATOM 1548 CA PRO A 221 48.665 39.217 -7.896 1.00 33.89 C ANISOU 1548 CA PRO A 221 4123 4733 4021 -640 717 156 C ATOM 1549 C PRO A 221 49.028 40.162 -6.763 1.00 29.98 C ANISOU 1549 C PRO A 221 3621 4226 3543 -649 706 164 C ATOM 1550 O PRO A 221 50.059 39.958 -6.108 1.00 26.54 O ANISOU 1550 O PRO A 221 3169 3793 3122 -649 710 167 O ATOM 1551 CB PRO A 221 49.208 39.711 -9.247 1.00 34.43 C ANISOU 1551 CB PRO A 221 4189 4811 4082 -653 733 176 C ATOM 1552 CG PRO A 221 48.247 39.178 -10.241 1.00 34.01 C ANISOU 1552 CG PRO A 221 4151 4762 4009 -646 735 168 C ATOM 1553 CD PRO A 221 46.892 39.201 -9.577 1.00 32.50 C ANISOU 1553 CD PRO A 221 3975 4560 3815 -638 716 151 C ATOM 1554 N ALA A 222 48.242 41.216 -6.540 1.00 29.28 N ANISOU 1554 N ALA A 222 3545 4125 3454 -657 693 168 N ATOM 1555 CA ALA A 222 48.529 42.126 -5.435 1.00 24.98 C ANISOU 1555 CA ALA A 222 2996 3568 2926 -665 681 174 C ATOM 1556 C ALA A 222 48.351 41.423 -4.096 1.00 28.52 C ANISOU 1556 C ALA A 222 3441 4011 3383 -652 671 154 C ATOM 1557 O ALA A 222 49.132 41.644 -3.159 1.00 24.07 O ANISOU 1557 O ALA A 222 2865 3443 2836 -656 668 158 O ATOM 1558 CB ALA A 222 47.633 43.360 -5.515 1.00 34.45 C ANISOU 1558 CB ALA A 222 4212 4755 4123 -676 669 182 C ATOM 1559 N VAL A 223 47.319 40.581 -3.989 1.00 26.85 N ANISOU 1559 N VAL A 223 3240 3798 3161 -637 665 134 N ATOM 1560 CA VAL A 223 47.106 39.804 -2.776 1.00 23.30 C ANISOU 1560 CA VAL A 223 2788 3344 2720 -623 655 113 C ATOM 1561 C VAL A 223 48.261 38.834 -2.561 1.00 28.55 C ANISOU 1561 C VAL A 223 3435 4021 3393 -617 667 111 C ATOM 1562 O VAL A 223 48.800 38.718 -1.453 1.00 26.94 O ANISOU 1562 O VAL A 223 3221 3813 3203 -615 662 107 O ATOM 1563 CB VAL A 223 45.756 39.067 -2.846 1.00 23.59 C ANISOU 1563 CB VAL A 223 2841 3378 2743 -609 648 92 C ATOM 1564 CG1 VAL A 223 45.570 38.166 -1.615 1.00 18.91 C ANISOU 1564 CG1 VAL A 223 2246 2781 2158 -594 639 70 C ATOM 1565 CG2 VAL A 223 44.605 40.060 -2.981 1.00 21.23 C ANISOU 1565 CG2 VAL A 223 2561 3068 2438 -615 635 95 C ATOM 1566 N THR A 224 48.664 38.128 -3.622 1.00 30.27 N ANISOU 1566 N THR A 224 3649 4252 3601 -614 683 114 N ATOM 1567 CA THR A 224 49.795 37.210 -3.521 1.00 31.24 C ANISOU 1567 CA THR A 224 3754 4386 3731 -608 696 113 C ATOM 1568 C THR A 224 51.028 37.925 -2.985 1.00 35.01 C ANISOU 1568 C THR A 224 4214 4862 4225 -620 699 131 C ATOM 1569 O THR A 224 51.691 37.442 -2.060 1.00 33.14 O ANISOU 1569 O THR A 224 3965 4626 4001 -614 698 126 O ATOM 1570 CB THR A 224 50.085 36.584 -4.889 1.00 33.44 C ANISOU 1570 CB THR A 224 4031 4678 3997 -606 714 118 C ATOM 1571 OG1 THR A 224 48.947 35.829 -5.316 1.00 28.26 O ANISOU 1571 OG1 THR A 224 3390 4022 3325 -594 710 100 O ATOM 1572 CG2 THR A 224 51.319 35.670 -4.826 1.00 25.42 C ANISOU 1572 CG2 THR A 224 2996 3673 2988 -600 728 120 C ATOM 1573 N GLU A 225 51.335 39.099 -3.542 1.00 31.94 N ANISOU 1573 N GLU A 225 3826 4472 3838 -637 701 152 N ATOM 1574 CA GLU A 225 52.513 39.831 -3.088 1.00 27.63 C ANISOU 1574 CA GLU A 225 3264 3924 3309 -650 704 169 C ATOM 1575 C GLU A 225 52.350 40.319 -1.655 1.00 29.53 C ANISOU 1575 C GLU A 225 3505 4152 3564 -651 687 164 C ATOM 1576 O GLU A 225 53.292 40.234 -0.859 1.00 31.89 O ANISOU 1576 O GLU A 225 3788 4450 3878 -652 687 167 O ATOM 1577 CB GLU A 225 52.804 41.015 -4.006 1.00 21.64 C ANISOU 1577 CB GLU A 225 2507 3165 2548 -668 710 192 C ATOM 1578 CG GLU A 225 54.055 41.773 -3.587 1.00 26.76 C ANISOU 1578 CG GLU A 225 3140 3813 3216 -682 713 211 C ATOM 1579 CD GLU A 225 54.423 42.892 -4.527 1.00 29.66 C ANISOU 1579 CD GLU A 225 3509 4180 3582 -700 720 234 C ATOM 1580 OE1 GLU A 225 53.927 42.904 -5.677 1.00 33.14 O ANISOU 1580 OE1 GLU A 225 3960 4625 4006 -701 726 237 O ATOM 1581 OE2 GLU A 225 55.213 43.767 -4.106 1.00 36.45 O ANISOU 1581 OE2 GLU A 225 4360 5034 4458 -714 718 249 O ATOM 1582 N TYR A 226 51.177 40.858 -1.308 1.00 29.17 N ANISOU 1582 N TYR A 226 3476 4093 3513 -651 671 156 N ATOM 1583 CA TYR A 226 50.994 41.366 0.049 1.00 31.34 C ANISOU 1583 CA TYR A 226 3751 4355 3801 -653 654 151 C ATOM 1584 C TYR A 226 51.151 40.249 1.081 1.00 27.87 C ANISOU 1584 C TYR A 226 3303 3916 3368 -637 651 132 C ATOM 1585 O TYR A 226 51.882 40.395 2.069 1.00 26.84 O ANISOU 1585 O TYR A 226 3161 3783 3254 -641 647 135 O ATOM 1586 CB TYR A 226 49.633 42.050 0.193 1.00 24.92 C ANISOU 1586 CB TYR A 226 2959 3528 2981 -654 639 144 C ATOM 1587 CG TYR A 226 49.414 42.576 1.597 1.00 31.08 C ANISOU 1587 CG TYR A 226 3740 4293 3775 -656 622 139 C ATOM 1588 CD1 TYR A 226 50.049 43.741 2.034 1.00 32.40 C ANISOU 1588 CD1 TYR A 226 3902 4453 3957 -673 617 156 C ATOM 1589 CD2 TYR A 226 48.600 41.897 2.496 1.00 29.76 C ANISOU 1589 CD2 TYR A 226 3580 4120 3606 -641 611 116 C ATOM 1590 CE1 TYR A 226 49.865 44.214 3.326 1.00 27.48 C ANISOU 1590 CE1 TYR A 226 3280 3815 3346 -675 601 151 C ATOM 1591 CE2 TYR A 226 48.410 42.359 3.785 1.00 23.82 C ANISOU 1591 CE2 TYR A 226 2830 3355 2867 -643 595 110 C ATOM 1592 CZ TYR A 226 49.043 43.516 4.193 1.00 27.48 C ANISOU 1592 CZ TYR A 226 3287 3810 3343 -660 591 128 C ATOM 1593 OH TYR A 226 48.850 43.959 5.473 1.00 21.15 O ANISOU 1593 OH TYR A 226 2487 2994 2553 -661 576 122 O ATOM 1594 N ILE A 227 50.518 39.101 0.840 1.00 22.97 N ANISOU 1594 N ILE A 227 2689 3301 2735 -621 653 113 N ATOM 1595 CA ILE A 227 50.607 38.007 1.802 1.00 25.57 C ANISOU 1595 CA ILE A 227 3013 3633 3071 -606 650 95 C ATOM 1596 C ILE A 227 52.030 37.470 1.856 1.00 22.63 C ANISOU 1596 C ILE A 227 2619 3270 2708 -606 663 103 C ATOM 1597 O ILE A 227 52.538 37.116 2.930 1.00 21.73 O ANISOU 1597 O ILE A 227 2494 3155 2607 -601 658 98 O ATOM 1598 CB ILE A 227 49.590 36.909 1.449 1.00 21.94 C ANISOU 1598 CB ILE A 227 2565 3175 2596 -589 649 73 C ATOM 1599 CG1 ILE A 227 48.147 37.435 1.542 1.00 17.84 C ANISOU 1599 CG1 ILE A 227 2067 2643 2068 -588 634 64 C ATOM 1600 CG2 ILE A 227 49.762 35.701 2.373 1.00 20.42 C ANISOU 1600 CG2 ILE A 227 2366 2984 2410 -573 646 54 C ATOM 1601 CD1 ILE A 227 47.750 37.980 2.903 1.00 19.68 C ANISOU 1601 CD1 ILE A 227 2304 2861 2312 -589 617 56 C ATOM 1602 N GLN A 228 52.708 37.439 0.706 1.00 23.96 N ANISOU 1602 N GLN A 228 2780 3451 2872 -611 680 118 N ATOM 1603 CA GLN A 228 54.125 37.092 0.679 1.00 29.82 C ANISOU 1603 CA GLN A 228 3501 4203 3625 -614 694 130 C ATOM 1604 C GLN A 228 54.938 38.044 1.559 1.00 27.73 C ANISOU 1604 C GLN A 228 3225 3931 3379 -627 688 144 C ATOM 1605 O GLN A 228 55.849 37.617 2.284 1.00 29.47 O ANISOU 1605 O GLN A 228 3429 4155 3613 -624 690 145 O ATOM 1606 CB GLN A 228 54.622 37.123 -0.765 1.00 39.13 C ANISOU 1606 CB GLN A 228 4678 5395 4796 -620 712 146 C ATOM 1607 CG GLN A 228 56.023 36.620 -0.987 1.00 54.01 C ANISOU 1607 CG GLN A 228 6542 7291 6689 -620 729 158 C ATOM 1608 CD GLN A 228 56.122 35.120 -0.861 1.00 68.17 C ANISOU 1608 CD GLN A 228 8330 9092 8479 -602 736 141 C ATOM 1609 OE1 GLN A 228 55.141 34.403 -1.076 1.00 72.82 O ANISOU 1609 OE1 GLN A 228 8933 9681 9056 -589 732 123 O ATOM 1610 NE2 GLN A 228 57.311 34.631 -0.543 1.00 75.50 N ANISOU 1610 NE2 GLN A 228 9239 10028 9420 -599 746 148 N ATOM 1611 N ARG A 229 54.615 39.340 1.525 1.00 24.77 N ANISOU 1611 N ARG A 229 2858 3546 3006 -642 679 156 N ATOM 1612 CA ARG A 229 55.322 40.288 2.383 1.00 26.94 C ANISOU 1612 CA ARG A 229 3123 3812 3299 -656 672 168 C ATOM 1613 C ARG A 229 55.039 40.033 3.856 1.00 29.93 C ANISOU 1613 C ARG A 229 3503 4183 3688 -648 656 153 C ATOM 1614 O ARG A 229 55.897 40.306 4.706 1.00 25.68 O ANISOU 1614 O ARG A 229 2949 3641 3165 -654 653 160 O ATOM 1615 CB ARG A 229 54.940 41.724 2.032 1.00 27.83 C ANISOU 1615 CB ARG A 229 3247 3915 3412 -673 665 183 C ATOM 1616 CG ARG A 229 55.433 42.214 0.691 1.00 30.34 C ANISOU 1616 CG ARG A 229 3563 4241 3724 -684 680 202 C ATOM 1617 CD ARG A 229 54.861 43.599 0.368 1.00 40.41 C ANISOU 1617 CD ARG A 229 4852 5505 4998 -700 671 214 C ATOM 1618 NE ARG A 229 55.119 44.579 1.423 1.00 51.45 N ANISOU 1618 NE ARG A 229 6247 6888 6412 -712 658 220 N ATOM 1619 CZ ARG A 229 56.197 45.357 1.486 1.00 53.15 C ANISOU 1619 CZ ARG A 229 6450 7102 6642 -728 661 239 C ATOM 1620 NH1 ARG A 229 57.130 45.281 0.546 1.00 51.25 N ANISOU 1620 NH1 ARG A 229 6199 6874 6402 -734 679 254 N ATOM 1621 NH2 ARG A 229 56.341 46.217 2.486 1.00 52.04 N ANISOU 1621 NH2 ARG A 229 6308 6947 6517 -738 647 243 N ATOM 1622 N LYS A 230 53.847 39.515 4.184 1.00 21.83 N ANISOU 1622 N LYS A 230 2491 3152 2652 -635 646 131 N ATOM 1623 CA LYS A 230 53.542 39.241 5.586 1.00 19.32 C ANISOU 1623 CA LYS A 230 2174 2824 2342 -627 631 115 C ATOM 1624 C LYS A 230 54.305 38.028 6.096 1.00 23.23 C ANISOU 1624 C LYS A 230 2654 3329 2844 -614 638 107 C ATOM 1625 O LYS A 230 54.735 38.007 7.254 1.00 24.03 O ANISOU 1625 O LYS A 230 2746 3425 2958 -614 630 104 O ATOM 1626 CB LYS A 230 52.039 39.046 5.777 1.00 21.81 C ANISOU 1626 CB LYS A 230 2510 3131 2645 -616 619 95 C ATOM 1627 CG LYS A 230 51.204 40.290 5.466 1.00 21.93 C ANISOU 1627 CG LYS A 230 2542 3135 2656 -628 610 102 C ATOM 1628 CD LYS A 230 51.659 41.500 6.288 1.00 17.00 C ANISOU 1628 CD LYS A 230 1913 2499 2048 -644 600 116 C ATOM 1629 CE LYS A 230 52.446 42.487 5.424 1.00 26.49 C ANISOU 1629 CE LYS A 230 3108 3703 3253 -663 609 142 C ATOM 1630 NZ LYS A 230 53.070 43.562 6.243 1.00 29.92 N ANISOU 1630 NZ LYS A 230 3535 4127 3705 -678 600 155 N ATOM 1631 N LYS A 231 54.501 37.020 5.241 1.00 22.08 N ANISOU 1631 N LYS A 231 2505 3197 2689 -604 652 103 N ATOM 1632 CA LYS A 231 55.219 35.821 5.651 1.00 29.65 C ANISOU 1632 CA LYS A 231 3449 4163 3652 -592 659 96 C ATOM 1633 C LYS A 231 56.731 35.965 5.525 1.00 30.83 C ANISOU 1633 C LYS A 231 3576 4321 3815 -601 672 117 C ATOM 1634 O LYS A 231 57.467 35.401 6.341 1.00 30.80 O ANISOU 1634 O LYS A 231 3559 4321 3823 -595 673 114 O ATOM 1635 CB LYS A 231 54.779 34.619 4.816 1.00 30.58 C ANISOU 1635 CB LYS A 231 3573 4291 3755 -576 669 83 C ATOM 1636 CG LYS A 231 53.307 34.262 4.871 1.00 33.47 C ANISOU 1636 CG LYS A 231 3960 4650 4109 -566 658 61 C ATOM 1637 CD LYS A 231 53.052 33.161 3.868 1.00 36.85 C ANISOU 1637 CD LYS A 231 4392 5088 4523 -554 670 52 C ATOM 1638 CE LYS A 231 51.653 32.644 3.967 1.00 39.36 C ANISOU 1638 CE LYS A 231 4729 5398 4829 -542 659 29 C ATOM 1639 NZ LYS A 231 51.373 31.633 2.916 1.00 42.20 N ANISOU 1639 NZ LYS A 231 5093 5766 5175 -532 670 22 N ATOM 1640 N PHE A 232 57.211 36.688 4.513 1.00 33.57 N ANISOU 1640 N PHE A 232 3920 4673 4161 -614 683 137 N ATOM 1641 CA PHE A 232 58.644 36.837 4.251 1.00 36.36 C ANISOU 1641 CA PHE A 232 4253 5035 4527 -623 698 158 C ATOM 1642 C PHE A 232 58.956 38.324 4.199 1.00 32.43 C ANISOU 1642 C PHE A 232 3755 4530 4038 -644 693 177 C ATOM 1643 O PHE A 232 59.139 38.896 3.118 1.00 36.12 O ANISOU 1643 O PHE A 232 4224 5000 4500 -654 703 192 O ATOM 1644 CB PHE A 232 59.045 36.128 2.956 1.00 33.80 C ANISOU 1644 CB PHE A 232 3925 4725 4192 -618 718 163 C ATOM 1645 CG PHE A 232 58.678 34.664 2.931 1.00 30.46 C ANISOU 1645 CG PHE A 232 3504 4309 3760 -598 722 143 C ATOM 1646 CD1 PHE A 232 59.591 33.699 3.330 1.00 24.29 C ANISOU 1646 CD1 PHE A 232 2706 3536 2987 -588 731 142 C ATOM 1647 CD2 PHE A 232 57.418 34.257 2.522 1.00 27.65 C ANISOU 1647 CD2 PHE A 232 3168 3952 3388 -588 717 126 C ATOM 1648 CE1 PHE A 232 59.253 32.358 3.317 1.00 31.18 C ANISOU 1648 CE1 PHE A 232 3581 4414 3852 -570 734 124 C ATOM 1649 CE2 PHE A 232 57.073 32.915 2.515 1.00 31.71 C ANISOU 1649 CE2 PHE A 232 3684 4470 3893 -570 720 107 C ATOM 1650 CZ PHE A 232 57.993 31.965 2.910 1.00 27.93 C ANISOU 1650 CZ PHE A 232 3190 4000 3424 -561 728 106 C ATOM 1651 N PRO A 233 59.022 38.982 5.351 1.00 29.32 N ANISOU 1651 N PRO A 233 3358 4123 3657 -651 678 178 N ATOM 1652 CA PRO A 233 59.166 40.435 5.369 1.00 36.26 C ANISOU 1652 CA PRO A 233 4240 4993 4545 -671 672 194 C ATOM 1653 C PRO A 233 60.485 40.852 4.748 1.00 43.23 C ANISOU 1653 C PRO A 233 5106 5882 5437 -685 687 218 C ATOM 1654 O PRO A 233 61.538 40.279 5.058 1.00 55.02 O ANISOU 1654 O PRO A 233 6581 7383 6942 -682 696 222 O ATOM 1655 CB PRO A 233 59.130 40.774 6.868 1.00 37.64 C ANISOU 1655 CB PRO A 233 4413 5155 4734 -673 654 188 C ATOM 1656 CG PRO A 233 58.503 39.589 7.516 1.00 35.45 C ANISOU 1656 CG PRO A 233 4141 4880 4450 -653 648 164 C ATOM 1657 CD PRO A 233 58.962 38.423 6.710 1.00 34.03 C ANISOU 1657 CD PRO A 233 3952 4716 4263 -641 667 162 C ATOM 1658 N PRO A 234 60.469 41.821 3.834 1.00 41.22 N ANISOU 1658 N PRO A 234 4857 5626 5179 -699 691 233 N ATOM 1659 CA PRO A 234 61.723 42.251 3.200 1.00 49.86 C ANISOU 1659 CA PRO A 234 5935 6726 6282 -713 706 255 C ATOM 1660 C PRO A 234 62.636 43.071 4.107 1.00 49.15 C ANISOU 1660 C PRO A 234 5833 6628 6215 -727 699 268 C ATOM 1661 O PRO A 234 63.796 43.284 3.739 1.00 54.74 O ANISOU 1661 O PRO A 234 6525 7341 6933 -737 712 285 O ATOM 1662 CB PRO A 234 61.240 43.084 2.005 1.00 46.08 C ANISOU 1662 CB PRO A 234 5471 6246 5792 -723 710 266 C ATOM 1663 CG PRO A 234 59.921 43.619 2.447 1.00 47.66 C ANISOU 1663 CG PRO A 234 5691 6433 5984 -723 691 254 C ATOM 1664 CD PRO A 234 59.300 42.549 3.311 1.00 43.73 C ANISOU 1664 CD PRO A 234 5196 5935 5483 -704 683 231 C ATOM 1665 N ASP A 235 62.161 43.555 5.259 1.00 54.43 N ANISOU 1665 N ASP A 235 6508 7283 6891 -730 680 260 N ATOM 1666 CA ASP A 235 62.963 44.402 6.138 1.00 58.97 C ANISOU 1666 CA ASP A 235 7071 7848 7486 -745 672 271 C ATOM 1667 C ASP A 235 63.409 43.715 7.428 1.00 61.61 C ANISOU 1667 C ASP A 235 7394 8183 7834 -736 665 261 C ATOM 1668 O ASP A 235 63.678 44.403 8.418 1.00 65.10 O ANISOU 1668 O ASP A 235 7832 8613 8291 -747 652 264 O ATOM 1669 CB ASP A 235 62.200 45.681 6.483 1.00 62.64 C ANISOU 1669 CB ASP A 235 7553 8296 7952 -758 654 272 C ATOM 1670 CG ASP A 235 60.954 45.412 7.312 1.00 64.45 C ANISOU 1670 CG ASP A 235 7798 8517 8175 -746 637 251 C ATOM 1671 OD1 ASP A 235 60.549 44.236 7.429 1.00 61.65 O ANISOU 1671 OD1 ASP A 235 7444 8170 7811 -727 640 235 O ATOM 1672 OD2 ASP A 235 60.394 46.380 7.868 1.00 65.68 O ANISOU 1672 OD2 ASP A 235 7964 8656 8334 -756 621 251 O ATOM 1673 N ASN A 236 63.477 42.385 7.452 1.00 60.31 N ANISOU 1673 N ASN A 236 7222 8029 7663 -718 673 250 N ATOM 1674 CA ASN A 236 63.913 41.629 8.631 1.00 67.34 C ANISOU 1674 CA ASN A 236 8100 8921 8565 -708 668 241 C ATOM 1675 C ASN A 236 63.018 41.849 9.853 1.00 59.53 C ANISOU 1675 C ASN A 236 7122 7918 7577 -705 646 225 C ATOM 1676 O ASN A 236 63.434 41.579 10.985 1.00 60.72 O ANISOU 1676 O ASN A 236 7264 8066 7741 -702 638 220 O ATOM 1677 CB ASN A 236 65.371 41.941 9.000 1.00 83.02 C ANISOU 1677 CB ASN A 236 10064 10908 10572 -720 674 258 C ATOM 1678 CG ASN A 236 66.365 41.081 8.244 1.00 95.00 C ANISOU 1678 CG ASN A 236 11564 12441 12091 -714 697 267 C ATOM 1679 OD1 ASN A 236 67.185 41.585 7.478 1.00101.97 O ANISOU 1679 OD1 ASN A 236 12438 13328 12979 -727 710 285 O ATOM 1680 ND2 ASN A 236 66.299 39.772 8.461 1.00 97.78 N ANISOU 1680 ND2 ASN A 236 11912 12803 12438 -695 701 254 N ATOM 1681 N SER A 237 61.802 42.352 9.666 1.00 49.90 N ANISOU 1681 N SER A 237 5925 6690 6346 -706 636 217 N ATOM 1682 CA SER A 237 60.839 42.369 10.755 1.00 48.56 C ANISOU 1682 CA SER A 237 5767 6509 6175 -699 616 199 C ATOM 1683 C SER A 237 60.273 40.963 10.959 1.00 43.46 C ANISOU 1683 C SER A 237 5125 5871 5517 -676 618 177 C ATOM 1684 O SER A 237 60.513 40.049 10.167 1.00 47.35 O ANISOU 1684 O SER A 237 5612 6376 6001 -666 633 176 O ATOM 1685 CB SER A 237 59.718 43.369 10.474 1.00 48.41 C ANISOU 1685 CB SER A 237 5771 6478 6147 -707 605 197 C ATOM 1686 OG SER A 237 59.097 43.103 9.228 1.00 51.45 O ANISOU 1686 OG SER A 237 6165 6869 6513 -701 616 196 O ATOM 1687 N ALA A 238 59.537 40.779 12.050 1.00 42.11 N ANISOU 1687 N ALA A 238 4963 5691 5347 -668 602 159 N ATOM 1688 CA ALA A 238 58.947 39.474 12.310 1.00 37.33 C ANISOU 1688 CA ALA A 238 4362 5091 4731 -647 602 137 C ATOM 1689 C ALA A 238 57.796 39.221 11.340 1.00 32.38 C ANISOU 1689 C ALA A 238 3754 4466 4084 -639 605 126 C ATOM 1690 O ALA A 238 57.056 40.150 10.997 1.00 25.71 O ANISOU 1690 O ALA A 238 2924 3612 3234 -647 598 130 O ATOM 1691 CB ALA A 238 58.437 39.379 13.744 1.00 29.71 C ANISOU 1691 CB ALA A 238 3402 4114 3771 -641 584 120 C ATOM 1692 N PRO A 239 57.641 37.990 10.854 1.00 29.13 N ANISOU 1692 N PRO A 239 3342 4065 3661 -622 615 115 N ATOM 1693 CA PRO A 239 56.471 37.679 10.033 1.00 28.99 C ANISOU 1693 CA PRO A 239 3342 4048 3623 -613 616 102 C ATOM 1694 C PRO A 239 55.221 37.828 10.880 1.00 18.16 C ANISOU 1694 C PRO A 239 1989 2662 2248 -607 598 83 C ATOM 1695 O PRO A 239 55.239 37.599 12.087 1.00 24.05 O ANISOU 1695 O PRO A 239 2732 3403 3003 -602 587 72 O ATOM 1696 CB PRO A 239 56.703 36.223 9.607 1.00 30.52 C ANISOU 1696 CB PRO A 239 3530 4256 3811 -596 629 92 C ATOM 1697 CG PRO A 239 58.169 35.994 9.779 1.00 32.58 C ANISOU 1697 CG PRO A 239 3768 4525 4086 -600 640 107 C ATOM 1698 CD PRO A 239 58.579 36.859 10.941 1.00 29.86 C ANISOU 1698 CD PRO A 239 3417 4170 3759 -612 627 114 C ATOM 1699 N TYR A 240 54.138 38.238 10.237 1.00 23.27 N ANISOU 1699 N TYR A 240 2655 3305 2883 -608 595 79 N ATOM 1700 CA TYR A 240 52.839 38.280 10.893 1.00 25.38 C ANISOU 1700 CA TYR A 240 2941 3560 3144 -601 579 59 C ATOM 1701 C TYR A 240 52.355 36.874 11.210 1.00 25.07 C ANISOU 1701 C TYR A 240 2905 3524 3098 -580 578 35 C ATOM 1702 O TYR A 240 52.669 35.915 10.501 1.00 22.46 O ANISOU 1702 O TYR A 240 2568 3205 2760 -571 591 33 O ATOM 1703 CB TYR A 240 51.804 38.952 9.998 1.00 25.18 C ANISOU 1703 CB TYR A 240 2933 3529 3105 -605 577 61 C ATOM 1704 CG TYR A 240 51.829 40.462 9.938 1.00 26.09 C ANISOU 1704 CG TYR A 240 3053 3634 3226 -625 571 80 C ATOM 1705 CD1 TYR A 240 53.024 41.176 9.948 1.00 26.34 C ANISOU 1705 CD1 TYR A 240 3069 3668 3272 -640 576 101 C ATOM 1706 CD2 TYR A 240 50.639 41.175 9.812 1.00 20.61 C ANISOU 1706 CD2 TYR A 240 2378 2928 2524 -627 561 76 C ATOM 1707 CE1 TYR A 240 53.025 42.574 9.878 1.00 21.31 C ANISOU 1707 CE1 TYR A 240 2437 3020 2641 -659 569 118 C ATOM 1708 CE2 TYR A 240 50.631 42.551 9.731 1.00 22.82 C ANISOU 1708 CE2 TYR A 240 2663 3198 2810 -645 555 93 C ATOM 1709 CZ TYR A 240 51.817 43.247 9.765 1.00 22.46 C ANISOU 1709 CZ TYR A 240 2602 3153 2778 -661 559 113 C ATOM 1710 OH TYR A 240 51.778 44.623 9.685 1.00 27.64 O ANISOU 1710 OH TYR A 240 3265 3798 3441 -678 552 129 O ATOM 1711 N GLY A 241 51.576 36.756 12.290 1.00 21.10 N ANISOU 1711 N GLY A 241 2412 3009 2596 -572 563 16 N ATOM 1712 CA GLY A 241 50.777 35.568 12.483 1.00 22.94 C ANISOU 1712 CA GLY A 241 2654 3243 2820 -553 560 -9 C ATOM 1713 C GLY A 241 49.541 35.567 11.591 1.00 25.11 C ANISOU 1713 C GLY A 241 2948 3515 3079 -549 560 -17 C ATOM 1714 O GLY A 241 49.078 36.605 11.129 1.00 17.33 O ANISOU 1714 O GLY A 241 1972 2524 2089 -560 557 -6 O ATOM 1715 N ALA A 242 49.015 34.373 11.332 1.00 19.50 N ANISOU 1715 N ALA A 242 2242 2807 2358 -533 563 -35 N ATOM 1716 CA ALA A 242 47.803 34.197 10.545 1.00 25.11 C ANISOU 1716 CA ALA A 242 2971 3515 3054 -527 561 -45 C ATOM 1717 C ALA A 242 46.685 33.648 11.427 1.00 19.13 C ANISOU 1717 C ALA A 242 2228 2746 2295 -513 547 -71 C ATOM 1718 O ALA A 242 46.919 32.775 12.262 1.00 22.23 O ANISOU 1718 O ALA A 242 2615 3138 2694 -503 543 -85 O ATOM 1719 CB ALA A 242 48.040 33.253 9.358 1.00 24.65 C ANISOU 1719 CB ALA A 242 2909 3472 2986 -520 577 -45 C ATOM 1720 N ARG A 243 45.477 34.189 11.252 1.00 16.82 N ANISOU 1720 N ARG A 243 1953 2444 1995 -514 538 -77 N ATOM 1721 CA ARG A 243 44.263 33.703 11.896 1.00 22.14 C ANISOU 1721 CA ARG A 243 2642 3105 2665 -502 525 -101 C ATOM 1722 C ARG A 243 43.124 33.829 10.898 1.00 21.76 C ANISOU 1722 C ARG A 243 2609 3054 2603 -500 525 -103 C ATOM 1723 O ARG A 243 42.949 34.895 10.306 1.00 24.52 O ANISOU 1723 O ARG A 243 2965 3403 2948 -512 526 -88 O ATOM 1724 CB ARG A 243 43.920 34.513 13.157 1.00 16.48 C ANISOU 1724 CB ARG A 243 1931 2373 1957 -506 510 -105 C ATOM 1725 CG ARG A 243 44.952 34.483 14.256 1.00 19.43 C ANISOU 1725 CG ARG A 243 2290 2747 2346 -508 508 -103 C ATOM 1726 CD ARG A 243 44.974 33.151 14.974 1.00 21.72 C ANISOU 1726 CD ARG A 243 2577 3037 2639 -492 505 -124 C ATOM 1727 NE ARG A 243 45.831 33.216 16.161 1.00 21.22 N ANISOU 1727 NE ARG A 243 2501 2972 2589 -493 501 -123 N ATOM 1728 CZ ARG A 243 47.156 33.137 16.124 1.00 30.51 C ANISOU 1728 CZ ARG A 243 3659 4161 3774 -499 510 -108 C ATOM 1729 NH1 ARG A 243 47.785 32.991 14.964 1.00 21.23 N ANISOU 1729 NH1 ARG A 243 2475 2999 2594 -503 525 -93 N ATOM 1730 NH2 ARG A 243 47.855 33.209 17.246 1.00 43.24 N ANISOU 1730 NH2 ARG A 243 5260 5770 5398 -501 505 -108 N ATOM 1731 N TYR A 244 42.316 32.780 10.749 1.00 15.08 N ANISOU 1731 N TYR A 244 1772 2207 1750 -486 522 -123 N ATOM 1732 CA TYR A 244 41.149 32.876 9.871 1.00 15.45 C ANISOU 1732 CA TYR A 244 1835 2251 1785 -485 520 -126 C ATOM 1733 C TYR A 244 40.064 31.955 10.420 1.00 16.48 C ANISOU 1733 C TYR A 244 1976 2371 1914 -470 508 -151 C ATOM 1734 O TYR A 244 40.095 30.740 10.198 1.00 15.49 O ANISOU 1734 O TYR A 244 1848 2250 1787 -459 512 -162 O ATOM 1735 CB TYR A 244 41.504 32.536 8.431 1.00 20.54 C ANISOU 1735 CB TYR A 244 2475 2910 2419 -487 535 -115 C ATOM 1736 CG TYR A 244 40.373 32.843 7.484 1.00 17.17 C ANISOU 1736 CG TYR A 244 2064 2480 1979 -488 534 -114 C ATOM 1737 CD1 TYR A 244 39.972 34.155 7.267 1.00 22.08 C ANISOU 1737 CD1 TYR A 244 2695 3097 2598 -500 530 -101 C ATOM 1738 CD2 TYR A 244 39.708 31.830 6.802 1.00 17.09 C ANISOU 1738 CD2 TYR A 244 2060 2473 1959 -477 536 -126 C ATOM 1739 CE1 TYR A 244 38.935 34.456 6.411 1.00 17.77 C ANISOU 1739 CE1 TYR A 244 2164 2549 2040 -501 529 -99 C ATOM 1740 CE2 TYR A 244 38.658 32.121 5.947 1.00 22.74 C ANISOU 1740 CE2 TYR A 244 2790 3186 2663 -479 534 -125 C ATOM 1741 CZ TYR A 244 38.277 33.445 5.755 1.00 24.74 C ANISOU 1741 CZ TYR A 244 3052 3435 2913 -490 530 -111 C ATOM 1742 OH TYR A 244 37.240 33.766 4.900 1.00 28.77 O ANISOU 1742 OH TYR A 244 3577 3943 3412 -491 528 -109 O ATOM 1743 N VAL A 245 39.108 32.544 11.138 1.00 14.23 N ANISOU 1743 N VAL A 245 1704 2070 1631 -470 495 -160 N ATOM 1744 CA VAL A 245 38.039 31.737 11.716 1.00 20.77 C ANISOU 1744 CA VAL A 245 2544 2887 2461 -456 483 -183 C ATOM 1745 C VAL A 245 37.104 31.239 10.626 1.00 22.75 C ANISOU 1745 C VAL A 245 2804 3139 2700 -451 484 -187 C ATOM 1746 O VAL A 245 36.584 30.111 10.702 1.00 17.41 O ANISOU 1746 O VAL A 245 2131 2460 2024 -440 480 -204 O ATOM 1747 CB VAL A 245 37.278 32.539 12.788 1.00 17.25 C ANISOU 1747 CB VAL A 245 2110 2425 2021 -457 468 -190 C ATOM 1748 CG1 VAL A 245 36.120 31.713 13.332 1.00 17.25 C ANISOU 1748 CG1 VAL A 245 2120 2411 2023 -444 455 -214 C ATOM 1749 CG2 VAL A 245 38.218 32.951 13.911 1.00 16.51 C ANISOU 1749 CG2 VAL A 245 2005 2328 1939 -462 466 -187 C ATOM 1750 N GLY A 246 36.901 32.040 9.583 1.00 19.72 N ANISOU 1750 N GLY A 246 2426 2761 2306 -460 490 -171 N ATOM 1751 CA GLY A 246 35.924 31.712 8.571 1.00 19.80 C ANISOU 1751 CA GLY A 246 2447 2772 2305 -457 491 -174 C ATOM 1752 C GLY A 246 34.533 32.202 8.887 1.00 17.53 C ANISOU 1752 C GLY A 246 2176 2469 2016 -455 477 -182 C ATOM 1753 O GLY A 246 33.590 31.837 8.183 1.00 23.95 O ANISOU 1753 O GLY A 246 2999 3281 2821 -450 475 -186 O ATOM 1754 N SER A 247 34.378 32.969 9.959 1.00 16.57 N ANISOU 1754 N SER A 247 2058 2335 1902 -457 468 -184 N ATOM 1755 CA SER A 247 33.132 33.617 10.334 1.00 14.24 C ANISOU 1755 CA SER A 247 1779 2025 1607 -456 455 -189 C ATOM 1756 C SER A 247 33.445 35.101 10.427 1.00 18.65 C ANISOU 1756 C SER A 247 2339 2581 2165 -470 456 -171 C ATOM 1757 O SER A 247 34.277 35.502 11.249 1.00 19.91 O ANISOU 1757 O SER A 247 2491 2740 2334 -475 456 -167 O ATOM 1758 CB SER A 247 32.614 33.067 11.667 1.00 18.18 C ANISOU 1758 CB SER A 247 2282 2509 2117 -446 441 -211 C ATOM 1759 OG SER A 247 31.395 33.673 12.062 1.00 23.23 O ANISOU 1759 OG SER A 247 2937 3133 2758 -445 430 -216 O ATOM 1760 N MET A 248 32.789 35.907 9.585 1.00 18.52 N ANISOU 1760 N MET A 248 2220 2799 2016 -741 252 -152 N ATOM 1761 CA MET A 248 33.222 37.289 9.392 1.00 20.91 C ANISOU 1761 CA MET A 248 2527 3094 2324 -744 261 -134 C ATOM 1762 C MET A 248 33.221 38.078 10.698 1.00 13.21 C ANISOU 1762 C MET A 248 1548 2100 1371 -736 246 -126 C ATOM 1763 O MET A 248 34.156 38.834 10.965 1.00 17.36 O ANISOU 1763 O MET A 248 2067 2612 1915 -734 253 -117 O ATOM 1764 CB MET A 248 32.341 37.997 8.364 1.00 21.80 C ANISOU 1764 CB MET A 248 2656 3217 2408 -753 267 -124 C ATOM 1765 CG MET A 248 32.913 39.364 7.971 1.00 29.69 C ANISOU 1765 CG MET A 248 3661 4209 3411 -756 280 -106 C ATOM 1766 SD MET A 248 31.723 40.523 7.256 1.00 25.05 S ANISOU 1766 SD MET A 248 3094 3627 2796 -762 278 -91 S ATOM 1767 CE MET A 248 32.833 41.787 6.641 1.00 29.36 C ANISOU 1767 CE MET A 248 3641 4165 3351 -763 301 -73 C ATOM 1768 N VAL A 249 32.180 37.930 11.517 1.00 13.91 N ANISOU 1768 N VAL A 249 1640 2186 1458 -731 224 -129 N ATOM 1769 CA VAL A 249 32.104 38.719 12.748 1.00 16.40 C ANISOU 1769 CA VAL A 249 1955 2484 1794 -721 209 -120 C ATOM 1770 C VAL A 249 33.263 38.381 13.681 1.00 13.60 C ANISOU 1770 C VAL A 249 1584 2114 1469 -710 209 -124 C ATOM 1771 O VAL A 249 33.852 39.264 14.317 1.00 16.33 O ANISOU 1771 O VAL A 249 1925 2445 1834 -706 209 -114 O ATOM 1772 CB VAL A 249 30.735 38.513 13.429 1.00 16.10 C ANISOU 1772 CB VAL A 249 1924 2446 1748 -715 187 -122 C ATOM 1773 CG1 VAL A 249 30.662 39.305 14.717 1.00 15.96 C ANISOU 1773 CG1 VAL A 249 1904 2409 1749 -703 173 -113 C ATOM 1774 CG2 VAL A 249 29.625 38.963 12.496 1.00 19.35 C ANISOU 1774 CG2 VAL A 249 2352 2871 2130 -727 187 -117 C ATOM 1775 N ALA A 250 33.593 37.098 13.797 1.00 17.00 N ANISOU 1775 N ALA A 250 2006 2549 1905 -705 210 -138 N ATOM 1776 CA ALA A 250 34.696 36.693 14.663 1.00 15.04 C ANISOU 1776 CA ALA A 250 1744 2287 1685 -693 210 -142 C ATOM 1777 C ALA A 250 36.022 37.269 14.177 1.00 13.69 C ANISOU 1777 C ALA A 250 1565 2111 1525 -699 229 -135 C ATOM 1778 O ALA A 250 36.834 37.736 14.983 1.00 15.77 O ANISOU 1778 O ALA A 250 1819 2359 1813 -692 227 -129 O ATOM 1779 CB ALA A 250 34.753 35.162 14.755 1.00 9.53 C ANISOU 1779 CB ALA A 250 1039 1595 987 -687 207 -159 C ATOM 1780 N ASP A 251 36.263 37.232 12.863 1.00 11.98 N ANISOU 1780 N ASP A 251 1352 1909 1291 -712 248 -135 N ATOM 1781 CA ASP A 251 37.528 37.720 12.334 1.00 15.77 C ANISOU 1781 CA ASP A 251 1825 2384 1782 -716 268 -128 C ATOM 1782 C ASP A 251 37.608 39.237 12.415 1.00 16.81 C ANISOU 1782 C ASP A 251 1961 2506 1920 -719 270 -110 C ATOM 1783 O ASP A 251 38.657 39.791 12.749 1.00 13.72 O ANISOU 1783 O ASP A 251 1560 2102 1550 -717 276 -103 O ATOM 1784 CB ASP A 251 37.724 37.260 10.884 1.00 20.28 C ANISOU 1784 CB ASP A 251 2400 2973 2332 -726 288 -132 C ATOM 1785 CG ASP A 251 38.083 35.795 10.777 1.00 15.60 C ANISOU 1785 CG ASP A 251 1800 2389 1741 -723 291 -149 C ATOM 1786 OD1 ASP A 251 39.008 35.363 11.489 1.00 17.22 O ANISOU 1786 OD1 ASP A 251 1991 2583 1969 -715 290 -153 O ATOM 1787 OD2 ASP A 251 37.453 35.087 9.968 1.00 16.41 O ANISOU 1787 OD2 ASP A 251 1908 2507 1819 -728 294 -157 O ATOM 1788 N VAL A 252 36.511 39.926 12.109 1.00 17.58 N ANISOU 1788 N VAL A 252 2073 2609 1998 -725 264 -103 N ATOM 1789 CA VAL A 252 36.538 41.380 12.181 1.00 14.82 C ANISOU 1789 CA VAL A 252 1728 2250 1653 -727 265 -86 C ATOM 1790 C VAL A 252 36.713 41.835 13.627 1.00 17.79 C ANISOU 1790 C VAL A 252 2097 2608 2056 -716 248 -83 C ATOM 1791 O VAL A 252 37.491 42.754 13.910 1.00 18.34 O ANISOU 1791 O VAL A 252 2161 2665 2144 -716 253 -72 O ATOM 1792 CB VAL A 252 35.261 41.971 11.552 1.00 15.37 C ANISOU 1792 CB VAL A 252 1815 2329 1695 -735 261 -80 C ATOM 1793 CG1 VAL A 252 35.169 43.448 11.833 1.00 15.66 C ANISOU 1793 CG1 VAL A 252 1856 2355 1738 -735 259 -63 C ATOM 1794 CG2 VAL A 252 35.221 41.719 10.048 1.00 20.53 C ANISOU 1794 CG2 VAL A 252 2477 3001 2324 -744 281 -80 C ATOM 1795 N HIS A 253 36.034 41.173 14.571 1.00 12.57 N ANISOU 1795 N HIS A 253 1435 1944 1397 -707 229 -92 N ATOM 1796 CA HIS A 253 36.170 41.585 15.965 1.00 9.78 C ANISOU 1796 CA HIS A 253 1076 1573 1068 -695 213 -88 C ATOM 1797 C HIS A 253 37.590 41.375 16.489 1.00 10.84 C ANISOU 1797 C HIS A 253 1194 1695 1231 -688 219 -89 C ATOM 1798 O HIS A 253 38.099 42.207 17.242 1.00 17.22 O ANISOU 1798 O HIS A 253 1996 2488 2061 -684 215 -80 O ATOM 1799 CB HIS A 253 35.174 40.846 16.853 1.00 11.45 C ANISOU 1799 CB HIS A 253 1290 1783 1277 -684 192 -97 C ATOM 1800 CG HIS A 253 35.159 41.352 18.255 1.00 11.98 C ANISOU 1800 CG HIS A 253 1353 1832 1366 -670 176 -91 C ATOM 1801 ND1 HIS A 253 34.761 42.633 18.574 1.00 14.52 N ANISOU 1801 ND1 HIS A 253 1681 2146 1689 -671 170 -79 N ATOM 1802 CD2 HIS A 253 35.506 40.761 19.423 1.00 16.86 C ANISOU 1802 CD2 HIS A 253 1962 2438 2006 -655 165 -97 C ATOM 1803 CE1 HIS A 253 34.849 42.801 19.882 1.00 19.67 C ANISOU 1803 CE1 HIS A 253 2328 2782 2363 -657 156 -77 C ATOM 1804 NE2 HIS A 253 35.299 41.680 20.419 1.00 14.57 N ANISOU 1804 NE2 HIS A 253 1673 2134 1731 -647 153 -87 N ATOM 1805 N ARG A 254 38.226 40.253 16.150 1.00 16.37 N ANISOU 1805 N ARG A 254 1886 2401 1933 -688 228 -101 N ATOM 1806 CA ARG A 254 39.635 40.074 16.503 1.00 15.14 C ANISOU 1806 CA ARG A 254 1714 2234 1802 -684 236 -101 C ATOM 1807 C ARG A 254 40.484 41.190 15.899 1.00 17.35 C ANISOU 1807 C ARG A 254 1992 2510 2089 -692 253 -87 C ATOM 1808 O ARG A 254 41.364 41.743 16.565 1.00 17.92 O ANISOU 1808 O ARG A 254 2055 2568 2188 -688 252 -80 O ATOM 1809 CB ARG A 254 40.128 38.707 16.025 1.00 16.05 C ANISOU 1809 CB ARG A 254 1824 2360 1914 -684 245 -115 C ATOM 1810 CG ARG A 254 41.546 38.349 16.469 1.00 15.09 C ANISOU 1810 CG ARG A 254 1686 2227 1820 -678 251 -116 C ATOM 1811 CD ARG A 254 42.157 37.239 15.632 1.00 16.22 C ANISOU 1811 CD ARG A 254 1825 2383 1957 -682 266 -127 C ATOM 1812 NE ARG A 254 42.131 37.607 14.223 1.00 19.29 N ANISOU 1812 NE ARG A 254 2220 2785 2325 -695 286 -123 N ATOM 1813 CZ ARG A 254 41.371 37.025 13.304 1.00 20.10 C ANISOU 1813 CZ ARG A 254 2332 2904 2400 -702 290 -131 C ATOM 1814 NH1 ARG A 254 40.589 35.997 13.633 1.00 20.11 N ANISOU 1814 NH1 ARG A 254 2336 2913 2393 -697 277 -144 N ATOM 1815 NH2 ARG A 254 41.398 37.475 12.054 1.00 17.82 N ANISOU 1815 NH2 ARG A 254 2050 2626 2094 -713 309 -124 N ATOM 1816 N THR A 255 40.206 41.548 14.643 1.00 17.14 N ANISOU 1816 N THR A 255 1974 2496 2040 -704 268 -83 N ATOM 1817 CA THR A 255 40.901 42.656 13.995 1.00 21.91 C ANISOU 1817 CA THR A 255 2579 3097 2650 -712 285 -68 C ATOM 1818 C THR A 255 40.722 43.960 14.773 1.00 21.91 C ANISOU 1818 C THR A 255 2580 3082 2663 -709 274 -55 C ATOM 1819 O THR A 255 41.677 44.721 14.950 1.00 22.03 O ANISOU 1819 O THR A 255 2586 3085 2699 -709 281 -45 O ATOM 1820 CB THR A 255 40.388 42.807 12.558 1.00 19.73 C ANISOU 1820 CB THR A 255 2315 2837 2344 -723 300 -65 C ATOM 1821 OG1 THR A 255 40.534 41.566 11.857 1.00 22.74 O ANISOU 1821 OG1 THR A 255 2694 3232 2712 -725 310 -78 O ATOM 1822 CG2 THR A 255 41.144 43.893 11.805 1.00 22.84 C ANISOU 1822 CG2 THR A 255 2708 3227 2742 -730 320 -49 C ATOM 1823 N LEU A 256 39.515 44.227 15.266 1.00 22.09 N ANISOU 1823 N LEU A 256 2613 3105 2675 -707 257 -55 N ATOM 1824 CA LEU A 256 39.291 45.448 16.044 1.00 25.22 C ANISOU 1824 CA LEU A 256 3011 3487 3083 -703 246 -43 C ATOM 1825 C LEU A 256 40.090 45.441 17.341 1.00 21.73 C ANISOU 1825 C LEU A 256 2555 3027 2673 -692 235 -44 C ATOM 1826 O LEU A 256 40.697 46.457 17.712 1.00 21.20 O ANISOU 1826 O LEU A 256 2483 2948 2626 -691 237 -33 O ATOM 1827 CB LEU A 256 37.804 45.598 16.350 1.00 23.56 C ANISOU 1827 CB LEU A 256 2816 3282 2855 -702 228 -44 C ATOM 1828 CG LEU A 256 37.294 46.755 17.203 1.00 13.22 C ANISOU 1828 CG LEU A 256 1509 1959 1553 -697 214 -34 C ATOM 1829 CD1 LEU A 256 37.486 48.080 16.503 1.00 18.30 C ANISOU 1829 CD1 LEU A 256 2159 2602 2194 -706 226 -18 C ATOM 1830 CD2 LEU A 256 35.840 46.522 17.525 1.00 14.38 C ANISOU 1830 CD2 LEU A 256 1669 2112 1681 -694 196 -38 C ATOM 1831 N VAL A 257 40.110 44.300 18.035 1.00 18.99 N ANISOU 1831 N VAL A 257 2202 2680 2334 -682 225 -57 N ATOM 1832 CA VAL A 257 40.696 44.209 19.372 1.00 23.19 C ANISOU 1832 CA VAL A 257 2723 3195 2894 -669 212 -58 C ATOM 1833 C VAL A 257 42.219 44.144 19.310 1.00 25.46 C ANISOU 1833 C VAL A 257 2994 3474 3204 -670 225 -56 C ATOM 1834 O VAL A 257 42.908 44.770 20.125 1.00 23.26 O ANISOU 1834 O VAL A 257 2706 3180 2950 -664 221 -50 O ATOM 1835 CB VAL A 257 40.112 42.993 20.124 1.00 28.55 C ANISOU 1835 CB VAL A 257 3401 3875 3570 -657 197 -72 C ATOM 1836 CG1 VAL A 257 40.926 42.690 21.378 1.00 29.24 C ANISOU 1836 CG1 VAL A 257 3475 3946 3687 -644 187 -74 C ATOM 1837 CG2 VAL A 257 38.659 43.252 20.509 1.00 17.14 C ANISOU 1837 CG2 VAL A 257 1969 2432 2109 -654 180 -71 C ATOM 1838 N TYR A 258 42.777 43.367 18.376 1.00 22.81 N ANISOU 1838 N TYR A 258 2656 3151 2861 -676 242 -62 N ATOM 1839 CA TYR A 258 44.220 43.155 18.323 1.00 18.04 C ANISOU 1839 CA TYR A 258 2036 2539 2278 -676 254 -62 C ATOM 1840 C TYR A 258 44.911 43.913 17.201 1.00 21.80 C ANISOU 1840 C TYR A 258 2512 3019 2752 -688 277 -51 C ATOM 1841 O TYR A 258 46.146 43.974 17.186 1.00 27.20 O ANISOU 1841 O TYR A 258 3183 3696 3457 -688 287 -47 O ATOM 1842 CB TYR A 258 44.535 41.660 18.175 1.00 22.65 C ANISOU 1842 CB TYR A 258 2615 3131 2858 -672 257 -76 C ATOM 1843 CG TYR A 258 44.326 40.869 19.445 1.00 36.86 C ANISOU 1843 CG TYR A 258 4411 4924 4671 -658 237 -85 C ATOM 1844 CD1 TYR A 258 45.193 40.989 20.520 1.00 46.96 C ANISOU 1844 CD1 TYR A 258 5678 6187 5979 -648 229 -82 C ATOM 1845 CD2 TYR A 258 43.237 40.026 19.578 1.00 31.43 C ANISOU 1845 CD2 TYR A 258 3732 4245 3965 -653 226 -96 C ATOM 1846 CE1 TYR A 258 44.988 40.260 21.684 1.00 48.40 C ANISOU 1846 CE1 TYR A 258 5857 6361 6171 -634 211 -90 C ATOM 1847 CE2 TYR A 258 43.024 39.305 20.728 1.00 30.80 C ANISOU 1847 CE2 TYR A 258 3648 4157 3895 -639 208 -103 C ATOM 1848 CZ TYR A 258 43.897 39.416 21.779 1.00 41.97 C ANISOU 1848 CZ TYR A 258 5052 5555 5338 -629 201 -100 C ATOM 1849 OH TYR A 258 43.657 38.683 22.925 1.00 39.23 O ANISOU 1849 OH TYR A 258 4703 5202 5002 -614 184 -106 O ATOM 1850 N GLY A 259 44.165 44.466 16.257 1.00 19.54 N ANISOU 1850 N GLY A 259 2238 2744 2443 -697 285 -45 N ATOM 1851 CA GLY A 259 44.772 45.075 15.096 1.00 21.99 C ANISOU 1851 CA GLY A 259 2549 3058 2748 -707 308 -35 C ATOM 1852 C GLY A 259 45.103 44.062 14.017 1.00 21.01 C ANISOU 1852 C GLY A 259 2424 2949 2609 -712 325 -43 C ATOM 1853 O GLY A 259 44.901 42.848 14.148 1.00 27.08 O ANISOU 1853 O GLY A 259 3192 3725 3371 -708 319 -57 O ATOM 1854 N GLY A 260 45.608 44.588 12.908 1.00 22.03 N ANISOU 1854 N GLY A 260 2555 3083 2732 -720 347 -33 N ATOM 1855 CA GLY A 260 45.955 43.744 11.790 1.00 18.07 C ANISOU 1855 CA GLY A 260 2054 2596 2216 -725 366 -39 C ATOM 1856 C GLY A 260 45.048 43.992 10.613 1.00 17.77 C ANISOU 1856 C GLY A 260 2032 2573 2145 -732 376 -35 C ATOM 1857 O GLY A 260 44.487 45.082 10.469 1.00 18.55 O ANISOU 1857 O GLY A 260 2140 2669 2237 -736 375 -23 O ATOM 1858 N ILE A 261 44.875 42.984 9.769 1.00 23.27 N ANISOU 1858 N ILE A 261 2734 3286 2823 -735 385 -45 N ATOM 1859 CA ILE A 261 44.175 43.170 8.512 1.00 21.77 C ANISOU 1859 CA ILE A 261 2559 3111 2601 -741 398 -41 C ATOM 1860 C ILE A 261 43.320 41.943 8.245 1.00 18.67 C ANISOU 1860 C ILE A 261 2174 2734 2186 -742 391 -58 C ATOM 1861 O ILE A 261 43.712 40.813 8.549 1.00 18.45 O ANISOU 1861 O ILE A 261 2137 2708 2165 -738 389 -72 O ATOM 1862 CB ILE A 261 45.167 43.444 7.357 1.00 16.18 C ANISOU 1862 CB ILE A 261 1849 2407 1893 -745 427 -31 C ATOM 1863 CG1 ILE A 261 44.427 43.865 6.085 1.00 18.83 C ANISOU 1863 CG1 ILE A 261 2203 2756 2197 -750 440 -23 C ATOM 1864 CG2 ILE A 261 46.036 42.221 7.087 1.00 17.41 C ANISOU 1864 CG2 ILE A 261 1995 2568 2054 -742 437 -43 C ATOM 1865 CD1 ILE A 261 45.342 44.502 5.062 1.00 16.85 C ANISOU 1865 CD1 ILE A 261 1950 2504 1947 -751 467 -8 C ATOM 1866 N PHE A 262 42.136 42.178 7.703 1.00 22.99 N ANISOU 1866 N PHE A 262 2737 3292 2706 -746 388 -56 N ATOM 1867 CA PHE A 262 41.210 41.131 7.304 1.00 22.45 C ANISOU 1867 CA PHE A 262 2677 3240 2612 -747 382 -70 C ATOM 1868 C PHE A 262 40.935 41.304 5.822 1.00 24.36 C ANISOU 1868 C PHE A 262 2933 3497 2826 -752 401 -64 C ATOM 1869 O PHE A 262 40.694 42.427 5.367 1.00 19.22 O ANISOU 1869 O PHE A 262 2292 2844 2168 -755 408 -49 O ATOM 1870 CB PHE A 262 39.908 41.209 8.112 1.00 21.40 C ANISOU 1870 CB PHE A 262 2552 3106 2472 -746 357 -74 C ATOM 1871 CG PHE A 262 38.822 40.315 7.593 1.00 13.91 C ANISOU 1871 CG PHE A 262 1615 2175 1496 -749 351 -86 C ATOM 1872 CD1 PHE A 262 38.798 38.961 7.911 1.00 16.14 C ANISOU 1872 CD1 PHE A 262 1890 2463 1780 -746 344 -104 C ATOM 1873 CD2 PHE A 262 37.837 40.825 6.769 1.00 16.21 C ANISOU 1873 CD2 PHE A 262 1923 2477 1760 -754 353 -79 C ATOM 1874 CE1 PHE A 262 37.799 38.137 7.426 1.00 22.55 C ANISOU 1874 CE1 PHE A 262 2710 3291 2566 -748 339 -115 C ATOM 1875 CE2 PHE A 262 36.830 40.015 6.275 1.00 18.24 C ANISOU 1875 CE2 PHE A 262 2190 2750 1992 -756 348 -90 C ATOM 1876 CZ PHE A 262 36.805 38.667 6.606 1.00 25.17 C ANISOU 1876 CZ PHE A 262 3059 3633 2871 -754 340 -108 C ATOM 1877 N LEU A 263 40.983 40.210 5.059 1.00 17.89 N ANISOU 1877 N LEU A 263 2114 2691 1991 -753 411 -75 N ATOM 1878 CA LEU A 263 40.823 40.332 3.617 1.00 19.96 C ANISOU 1878 CA LEU A 263 2390 2967 2226 -755 431 -69 C ATOM 1879 C LEU A 263 39.782 39.346 3.113 1.00 23.97 C ANISOU 1879 C LEU A 263 2908 3492 2705 -756 425 -83 C ATOM 1880 O LEU A 263 39.822 38.160 3.455 1.00 20.65 O ANISOU 1880 O LEU A 263 2480 3076 2288 -754 418 -100 O ATOM 1881 CB LEU A 263 42.145 40.109 2.877 1.00 25.34 C ANISOU 1881 CB LEU A 263 3063 3649 2915 -753 457 -66 C ATOM 1882 CG LEU A 263 43.358 40.895 3.377 1.00 29.72 C ANISOU 1882 CG LEU A 263 3605 4187 3502 -752 464 -54 C ATOM 1883 CD1 LEU A 263 44.147 40.035 4.372 1.00 24.48 C ANISOU 1883 CD1 LEU A 263 2922 3515 2864 -748 456 -67 C ATOM 1884 CD2 LEU A 263 44.239 41.405 2.240 1.00 30.62 C ANISOU 1884 CD2 LEU A 263 3720 4302 3611 -751 492 -41 C ATOM 1885 N TYR A 264 38.836 39.846 2.322 1.00 21.55 N ANISOU 1885 N TYR A 264 2620 3195 2372 -757 427 -76 N ATOM 1886 CA TYR A 264 38.018 39.014 1.446 1.00 18.74 C ANISOU 1886 CA TYR A 264 2276 2857 1985 -757 428 -85 C ATOM 1887 C TYR A 264 38.028 39.726 0.101 1.00 27.29 C ANISOU 1887 C TYR A 264 3376 3947 3046 -755 448 -71 C ATOM 1888 O TYR A 264 37.054 40.393 -0.279 1.00 25.51 O ANISOU 1888 O TYR A 264 3167 3726 2801 -755 443 -63 O ATOM 1889 CB TYR A 264 36.604 38.809 1.996 1.00 17.05 C ANISOU 1889 CB TYR A 264 2071 2648 1759 -759 403 -93 C ATOM 1890 CG TYR A 264 36.045 37.459 1.615 1.00 23.13 C ANISOU 1890 CG TYR A 264 2843 3434 2510 -759 399 -110 C ATOM 1891 CD1 TYR A 264 36.077 37.027 0.292 1.00 30.84 C ANISOU 1891 CD1 TYR A 264 3830 4425 3462 -755 417 -112 C ATOM 1892 CD2 TYR A 264 35.546 36.590 2.581 1.00 28.89 C ANISOU 1892 CD2 TYR A 264 3565 4164 3249 -760 379 -126 C ATOM 1893 CE1 TYR A 264 35.589 35.791 -0.066 1.00 31.09 C ANISOU 1893 CE1 TYR A 264 3865 4472 3478 -753 413 -129 C ATOM 1894 CE2 TYR A 264 35.058 35.347 2.234 1.00 32.31 C ANISOU 1894 CE2 TYR A 264 3999 4612 3666 -759 375 -142 C ATOM 1895 CZ TYR A 264 35.084 34.953 0.907 1.00 32.31 C ANISOU 1895 CZ TYR A 264 4010 4626 3641 -756 393 -144 C ATOM 1896 OH TYR A 264 34.603 33.716 0.552 1.00 40.13 O ANISOU 1896 OH TYR A 264 5001 5630 4615 -754 389 -160 O ATOM 1897 N PRO A 265 39.113 39.599 -0.649 1.00 25.12 N ANISOU 1897 N PRO A 265 3096 3673 2774 -751 472 -67 N ATOM 1898 CA PRO A 265 39.290 40.405 -1.855 1.00 29.02 C ANISOU 1898 CA PRO A 265 3604 4171 3251 -747 493 -51 C ATOM 1899 C PRO A 265 38.690 39.771 -3.106 1.00 29.94 C ANISOU 1899 C PRO A 265 3737 4305 3332 -742 501 -57 C ATOM 1900 O PRO A 265 38.398 38.573 -3.160 1.00 24.95 O ANISOU 1900 O PRO A 265 3104 3684 2691 -741 495 -74 O ATOM 1901 CB PRO A 265 40.814 40.482 -1.982 1.00 25.78 C ANISOU 1901 CB PRO A 265 3179 3753 2863 -746 514 -46 C ATOM 1902 CG PRO A 265 41.276 39.157 -1.438 1.00 27.74 C ANISOU 1902 CG PRO A 265 3412 4003 3124 -746 508 -65 C ATOM 1903 CD PRO A 265 40.293 38.770 -0.351 1.00 22.51 C ANISOU 1903 CD PRO A 265 2747 3339 2465 -750 480 -77 C ATOM 1904 N ALA A 266 38.562 40.609 -4.131 1.00 29.87 N ANISOU 1904 N ALA A 266 3745 4299 3306 -737 515 -41 N ATOM 1905 CA ALA A 266 38.146 40.164 -5.448 1.00 30.86 C ANISOU 1905 CA ALA A 266 3887 4439 3398 -728 526 -43 C ATOM 1906 C ALA A 266 39.238 39.318 -6.090 1.00 39.41 C ANISOU 1906 C ALA A 266 4963 5528 4483 -723 547 -49 C ATOM 1907 O ALA A 266 40.422 39.434 -5.759 1.00 38.33 O ANISOU 1907 O ALA A 266 4810 5383 4372 -725 559 -46 O ATOM 1908 CB ALA A 266 37.824 41.359 -6.339 1.00 35.22 C ANISOU 1908 CB ALA A 266 4458 4992 3933 -723 536 -24 C ATOM 1909 N ASN A 267 38.825 38.453 -7.012 1.00 47.94 N ANISOU 1909 N ASN A 267 6055 6623 5536 -715 551 -59 N ATOM 1910 CA ASN A 267 39.752 37.737 -7.880 1.00 52.24 C ANISOU 1910 CA ASN A 267 6597 7175 6076 -708 573 -63 C ATOM 1911 C ASN A 267 39.133 37.665 -9.273 1.00 52.76 C ANISOU 1911 C ASN A 267 6687 7255 6106 -695 581 -61 C ATOM 1912 O ASN A 267 38.109 38.296 -9.553 1.00 46.06 O ANISOU 1912 O ASN A 267 5855 6407 5238 -693 572 -54 O ATOM 1913 CB ASN A 267 40.080 36.351 -7.309 1.00 52.79 C ANISOU 1913 CB ASN A 267 6652 7249 6158 -711 566 -84 C ATOM 1914 CG ASN A 267 38.847 35.494 -7.099 1.00 48.09 C ANISOU 1914 CG ASN A 267 6063 6664 5545 -711 544 -101 C ATOM 1915 OD1 ASN A 267 38.031 35.322 -8.004 1.00 45.84 O ANISOU 1915 OD1 ASN A 267 5798 6391 5230 -703 543 -103 O ATOM 1916 ND2 ASN A 267 38.720 34.930 -5.906 1.00 44.96 N ANISOU 1916 ND2 ASN A 267 5651 6263 5167 -719 526 -114 N ATOM 1917 N LYS A 268 39.785 36.921 -10.171 1.00 55.78 N ANISOU 1917 N LYS A 268 7071 7645 6478 -687 600 -66 N ATOM 1918 CA LYS A 268 39.276 36.810 -11.535 1.00 57.09 C ANISOU 1918 CA LYS A 268 7260 7824 6609 -673 608 -63 C ATOM 1919 C LYS A 268 38.015 35.956 -11.591 1.00 49.56 C ANISOU 1919 C LYS A 268 6317 6881 5633 -669 586 -80 C ATOM 1920 O LYS A 268 37.130 36.215 -12.414 1.00 46.06 O ANISOU 1920 O LYS A 268 5895 6444 5162 -659 583 -77 O ATOM 1921 CB LYS A 268 40.364 36.237 -12.448 1.00 66.16 C ANISOU 1921 CB LYS A 268 8406 8977 7754 -663 634 -64 C ATOM 1922 CG LYS A 268 41.512 37.204 -12.730 1.00 69.63 C ANISOU 1922 CG LYS A 268 8840 9408 8209 -663 658 -44 C ATOM 1923 CD LYS A 268 42.662 36.531 -13.475 1.00 71.29 C ANISOU 1923 CD LYS A 268 9044 9622 8419 -655 682 -46 C ATOM 1924 CE LYS A 268 42.275 36.020 -14.852 1.00 74.64 C ANISOU 1924 CE LYS A 268 9489 10061 8808 -639 691 -49 C ATOM 1925 NZ LYS A 268 43.484 35.563 -15.606 1.00 74.13 N ANISOU 1925 NZ LYS A 268 9421 10001 8746 -630 718 -47 N ATOM 1926 N LYS A 269 37.902 34.955 -10.711 1.00 46.43 N ANISOU 1926 N LYS A 269 5906 6486 5249 -676 571 -99 N ATOM 1927 CA LYS A 269 36.668 34.178 -10.615 1.00 48.24 C ANISOU 1927 CA LYS A 269 6144 6724 5460 -674 548 -115 C ATOM 1928 C LYS A 269 35.551 34.952 -9.911 1.00 47.14 C ANISOU 1928 C LYS A 269 6011 6579 5321 -681 526 -109 C ATOM 1929 O LYS A 269 34.366 34.686 -10.151 1.00 40.03 O ANISOU 1929 O LYS A 269 5125 5686 4400 -676 509 -116 O ATOM 1930 CB LYS A 269 36.945 32.844 -9.913 1.00 53.77 C ANISOU 1930 CB LYS A 269 6827 7428 6175 -679 540 -136 C ATOM 1931 CG LYS A 269 37.749 31.855 -10.765 1.00 58.25 C ANISOU 1931 CG LYS A 269 7393 8004 6734 -670 558 -145 C ATOM 1932 CD LYS A 269 37.791 30.455 -10.151 1.00 62.86 C ANISOU 1932 CD LYS A 269 7962 8593 7328 -673 547 -168 C ATOM 1933 CE LYS A 269 38.616 29.485 -11.006 1.00 62.69 C ANISOU 1933 CE LYS A 269 7941 8581 7300 -663 565 -177 C ATOM 1934 NZ LYS A 269 38.836 28.157 -10.347 1.00 60.77 N ANISOU 1934 NZ LYS A 269 7680 8340 7070 -667 556 -198 N ATOM 1935 N SER A 270 35.900 35.909 -9.051 1.00 40.86 N ANISOU 1935 N SER A 270 5205 5771 4550 -692 525 -97 N ATOM 1936 CA SER A 270 34.922 36.673 -8.271 1.00 37.77 C ANISOU 1936 CA SER A 270 4817 5373 4161 -699 504 -91 C ATOM 1937 C SER A 270 35.320 38.139 -8.317 1.00 33.21 C ANISOU 1937 C SER A 270 4241 4784 3593 -701 515 -69 C ATOM 1938 O SER A 270 35.939 38.668 -7.385 1.00 29.38 O ANISOU 1938 O SER A 270 3740 4286 3135 -711 515 -63 O ATOM 1939 CB SER A 270 34.824 36.159 -6.831 1.00 34.15 C ANISOU 1939 CB SER A 270 4339 4909 3727 -711 485 -104 C ATOM 1940 OG SER A 270 34.438 34.800 -6.812 1.00 47.14 O ANISOU 1940 OG SER A 270 5982 6565 5363 -709 476 -124 O ATOM 1941 N PRO A 271 34.988 38.832 -9.410 1.00 34.15 N ANISOU 1941 N PRO A 271 4380 4906 3688 -691 525 -56 N ATOM 1942 CA PRO A 271 35.459 40.219 -9.579 1.00 31.71 C ANISOU 1942 CA PRO A 271 4074 4587 3388 -692 538 -34 C ATOM 1943 C PRO A 271 34.870 41.203 -8.592 1.00 29.70 C ANISOU 1943 C PRO A 271 3816 4320 3146 -701 521 -26 C ATOM 1944 O PRO A 271 35.405 42.315 -8.455 1.00 28.01 O ANISOU 1944 O PRO A 271 3599 4095 2947 -704 530 -9 O ATOM 1945 CB PRO A 271 35.019 40.564 -11.006 1.00 37.01 C ANISOU 1945 CB PRO A 271 4769 5266 4027 -677 549 -25 C ATOM 1946 CG PRO A 271 33.822 39.665 -11.245 1.00 32.60 C ANISOU 1946 CG PRO A 271 4223 4719 3445 -671 530 -41 C ATOM 1947 CD PRO A 271 34.116 38.392 -10.510 1.00 28.49 C ANISOU 1947 CD PRO A 271 3686 4202 2938 -678 522 -61 C ATOM 1948 N ASN A 272 33.782 40.845 -7.911 1.00 26.95 N ANISOU 1948 N ASN A 272 3471 3975 2795 -706 495 -36 N ATOM 1949 CA ASN A 272 33.201 41.712 -6.899 1.00 30.68 C ANISOU 1949 CA ASN A 272 3940 4436 3280 -714 477 -29 C ATOM 1950 C ASN A 272 33.358 41.172 -5.479 1.00 23.00 C ANISOU 1950 C ASN A 272 2947 3458 2335 -726 462 -41 C ATOM 1951 O ASN A 272 32.587 41.564 -4.602 1.00 31.52 O ANISOU 1951 O ASN A 272 4025 4531 3420 -732 441 -40 O ATOM 1952 CB ASN A 272 31.721 41.937 -7.206 1.00 29.49 C ANISOU 1952 CB ASN A 272 3810 4291 3105 -709 459 -28 C ATOM 1953 CG ASN A 272 31.516 42.760 -8.453 1.00 38.95 C ANISOU 1953 CG ASN A 272 5028 5491 4280 -698 472 -13 C ATOM 1954 OD1 ASN A 272 30.876 42.310 -9.404 1.00 46.96 O ANISOU 1954 OD1 ASN A 272 6059 6516 5268 -687 471 -18 O ATOM 1955 ND2 ASN A 272 32.081 43.967 -8.470 1.00 34.95 N ANISOU 1955 ND2 ASN A 272 4520 4974 3785 -700 485 5 N ATOM 1956 N GLY A 273 34.300 40.239 -5.234 1.00 28.83 N ANISOU 1956 N GLY A 273 3669 4197 3088 -728 470 -53 N ATOM 1957 CA GLY A 273 34.346 39.640 -3.911 1.00 28.89 C ANISOU 1957 CA GLY A 273 3658 4200 3118 -737 453 -65 C ATOM 1958 C GLY A 273 33.142 38.725 -3.717 1.00 32.84 C ANISOU 1958 C GLY A 273 4165 4711 3603 -737 432 -81 C ATOM 1959 O GLY A 273 32.375 38.437 -4.631 1.00 35.05 O ANISOU 1959 O GLY A 273 4461 5002 3854 -729 431 -84 O ATOM 1960 N LYS A 274 33.020 38.210 -2.491 1.00 34.45 N ANISOU 1960 N LYS A 274 4353 4910 3826 -744 415 -92 N ATOM 1961 CA LYS A 274 31.849 37.409 -2.097 1.00 27.16 C ANISOU 1961 CA LYS A 274 3433 3995 2892 -745 393 -106 C ATOM 1962 C LYS A 274 30.976 38.014 -1.014 1.00 23.72 C ANISOU 1962 C LYS A 274 2997 3551 2465 -752 370 -102 C ATOM 1963 O LYS A 274 29.776 37.722 -0.998 1.00 21.36 O ANISOU 1963 O LYS A 274 2708 3258 2149 -751 353 -107 O ATOM 1964 CB LYS A 274 32.214 35.986 -1.605 1.00 38.74 C ANISOU 1964 CB LYS A 274 4883 5467 4369 -747 389 -127 C ATOM 1965 CG LYS A 274 32.418 35.108 -2.827 1.00 55.82 C ANISOU 1965 CG LYS A 274 7054 7644 6510 -739 404 -135 C ATOM 1966 CD LYS A 274 32.481 33.665 -2.408 1.00 72.07 C ANISOU 1966 CD LYS A 274 9099 9709 8574 -740 397 -157 C ATOM 1967 CE LYS A 274 32.406 32.841 -3.633 1.00 79.00 C ANISOU 1967 CE LYS A 274 9988 10601 9427 -729 407 -165 C ATOM 1968 NZ LYS A 274 33.376 31.737 -3.451 1.00 80.59 N ANISOU 1968 NZ LYS A 274 10172 10805 9643 -730 416 -180 N ATOM 1969 N LEU A 275 31.551 38.706 -0.032 1.00 22.33 N ANISOU 1969 N LEU A 275 2808 3360 2317 -757 367 -95 N ATOM 1970 CA LEU A 275 30.733 39.248 1.045 1.00 22.24 C ANISOU 1970 CA LEU A 275 2796 3340 2314 -762 345 -91 C ATOM 1971 C LEU A 275 29.779 40.319 0.506 1.00 23.53 C ANISOU 1971 C LEU A 275 2980 3504 2458 -760 340 -77 C ATOM 1972 O LEU A 275 30.035 40.955 -0.521 1.00 25.35 O ANISOU 1972 O LEU A 275 3222 3736 2675 -755 357 -65 O ATOM 1973 CB LEU A 275 31.614 39.827 2.139 1.00 22.75 C ANISOU 1973 CB LEU A 275 2843 3387 2412 -765 343 -86 C ATOM 1974 CG LEU A 275 32.552 38.773 2.754 1.00 21.02 C ANISOU 1974 CG LEU A 275 2605 3167 2216 -765 345 -101 C ATOM 1975 CD1 LEU A 275 33.463 39.385 3.795 1.00 21.23 C ANISOU 1975 CD1 LEU A 275 2616 3174 2275 -765 343 -95 C ATOM 1976 CD2 LEU A 275 31.768 37.605 3.357 1.00 26.28 C ANISOU 1976 CD2 LEU A 275 3267 3840 2880 -766 326 -119 C ATOM 1977 N ARG A 276 28.646 40.493 1.195 1.00 22.45 N ANISOU 1977 N ARG A 276 2847 3364 2317 -763 318 -77 N ATOM 1978 CA ARG A 276 27.567 41.361 0.725 1.00 14.39 C ANISOU 1978 CA ARG A 276 1846 2344 1277 -760 310 -65 C ATOM 1979 C ARG A 276 27.733 42.785 1.240 1.00 16.19 C ANISOU 1979 C ARG A 276 2074 2557 1519 -763 308 -48 C ATOM 1980 O ARG A 276 27.983 42.998 2.433 1.00 20.29 O ANISOU 1980 O ARG A 276 2580 3065 2063 -767 298 -48 O ATOM 1981 CB ARG A 276 26.218 40.799 1.153 1.00 18.15 C ANISOU 1981 CB ARG A 276 2329 2827 1742 -761 286 -74 C ATOM 1982 CG ARG A 276 26.016 39.337 0.790 1.00 17.46 C ANISOU 1982 CG ARG A 276 2239 2753 1642 -758 285 -92 C ATOM 1983 CD ARG A 276 25.771 39.154 -0.716 1.00 28.03 C ANISOU 1983 CD ARG A 276 3595 4102 2951 -747 297 -92 C ATOM 1984 NE ARG A 276 25.506 37.748 -1.017 1.00 30.43 N ANISOU 1984 NE ARG A 276 3898 4419 3244 -743 293 -111 N ATOM 1985 CZ ARG A 276 24.920 37.292 -2.119 1.00 29.00 C ANISOU 1985 CZ ARG A 276 3733 4248 3037 -732 293 -115 C ATOM 1986 NH1 ARG A 276 24.510 38.128 -3.066 1.00 25.32 N ANISOU 1986 NH1 ARG A 276 3286 3781 2552 -723 297 -102 N ATOM 1987 NH2 ARG A 276 24.730 35.983 -2.262 1.00 25.64 N ANISOU 1987 NH2 ARG A 276 3304 3832 2604 -728 288 -133 N ATOM 1988 N LEU A 277 27.571 43.755 0.333 1.00 16.83 N ANISOU 1988 N LEU A 277 2171 2638 1585 -758 318 -33 N ATOM 1989 CA LEU A 277 27.858 45.155 0.647 1.00 11.86 C ANISOU 1989 CA LEU A 277 1542 1995 970 -759 321 -16 C ATOM 1990 C LEU A 277 26.934 45.717 1.724 1.00 15.79 C ANISOU 1990 C LEU A 277 2041 2484 1475 -763 296 -13 C ATOM 1991 O LEU A 277 27.398 46.381 2.654 1.00 15.21 O ANISOU 1991 O LEU A 277 1957 2397 1425 -766 292 -7 O ATOM 1992 CB LEU A 277 27.761 46.021 -0.611 1.00 13.76 C ANISOU 1992 CB LEU A 277 1800 2237 1190 -753 335 -1 C ATOM 1993 CG LEU A 277 27.943 47.535 -0.390 1.00 19.59 C ANISOU 1993 CG LEU A 277 2542 2963 1940 -754 338 17 C ATOM 1994 CD1 LEU A 277 29.329 47.839 0.158 1.00 24.06 C ANISOU 1994 CD1 LEU A 277 3089 3518 2535 -758 351 21 C ATOM 1995 CD2 LEU A 277 27.715 48.313 -1.694 1.00 21.55 C ANISOU 1995 CD2 LEU A 277 2808 3214 2165 -746 351 31 C ATOM 1996 N LEU A 278 25.615 45.530 1.576 1.00 19.50 N ANISOU 1996 N LEU A 278 2524 2960 1925 -761 280 -15 N ATOM 1997 CA LEU A 278 24.679 46.297 2.397 1.00 15.92 C ANISOU 1997 CA LEU A 278 2075 2499 1476 -763 259 -8 C ATOM 1998 C LEU A 278 24.705 45.862 3.861 1.00 18.52 C ANISOU 1998 C LEU A 278 2388 2821 1828 -769 242 -17 C ATOM 1999 O LEU A 278 24.671 46.712 4.756 1.00 21.60 O ANISOU 1999 O LEU A 278 2774 3198 2234 -770 232 -10 O ATOM 2000 CB LEU A 278 23.255 46.207 1.839 1.00 15.76 C ANISOU 2000 CB LEU A 278 2073 2486 1429 -759 245 -8 C ATOM 2001 CG LEU A 278 22.889 47.336 0.850 1.00 20.18 C ANISOU 2001 CG LEU A 278 2651 3044 1972 -752 252 8 C ATOM 2002 CD1 LEU A 278 23.601 47.184 -0.480 1.00 18.90 C ANISOU 2002 CD1 LEU A 278 2496 2890 1797 -745 277 9 C ATOM 2003 CD2 LEU A 278 21.390 47.460 0.639 1.00 18.93 C ANISOU 2003 CD2 LEU A 278 2510 2888 1796 -746 233 9 C ATOM 2004 N TYR A 279 24.798 44.558 4.134 1.00 19.50 N ANISOU 2004 N TYR A 279 2502 2953 1955 -770 239 -34 N ATOM 2005 CA TYR A 279 24.636 44.046 5.493 1.00 21.48 C ANISOU 2005 CA TYR A 279 2739 3197 2224 -773 220 -44 C ATOM 2006 C TYR A 279 25.833 43.220 5.965 1.00 22.76 C ANISOU 2006 C TYR A 279 2882 3357 2408 -773 229 -55 C ATOM 2007 O TYR A 279 25.758 42.577 7.021 1.00 22.01 O ANISOU 2007 O TYR A 279 2775 3259 2329 -772 214 -65 O ATOM 2008 CB TYR A 279 23.353 43.210 5.599 1.00 18.13 C ANISOU 2008 CB TYR A 279 2321 2783 1784 -774 202 -53 C ATOM 2009 CG TYR A 279 23.146 42.293 4.417 1.00 19.16 C ANISOU 2009 CG TYR A 279 2459 2930 1891 -771 212 -62 C ATOM 2010 CD1 TYR A 279 22.315 42.659 3.367 1.00 20.23 C ANISOU 2010 CD1 TYR A 279 2615 3072 2000 -766 212 -55 C ATOM 2011 CD2 TYR A 279 23.811 41.075 4.335 1.00 19.15 C ANISOU 2011 CD2 TYR A 279 2445 2936 1893 -772 220 -77 C ATOM 2012 CE1 TYR A 279 22.140 41.828 2.267 1.00 25.63 C ANISOU 2012 CE1 TYR A 279 3307 3768 2662 -760 220 -63 C ATOM 2013 CE2 TYR A 279 23.650 40.246 3.248 1.00 13.14 C ANISOU 2013 CE2 TYR A 279 1693 2190 1111 -768 229 -86 C ATOM 2014 CZ TYR A 279 22.813 40.626 2.214 1.00 23.18 C ANISOU 2014 CZ TYR A 279 2984 3466 2355 -761 228 -79 C ATOM 2015 OH TYR A 279 22.646 39.806 1.128 1.00 24.82 O ANISOU 2015 OH TYR A 279 3201 3687 2542 -753 235 -88 O ATOM 2016 N GLU A 280 26.943 43.234 5.233 1.00 16.08 N ANISOU 2016 N GLU A 280 2032 2513 1565 -772 251 -53 N ATOM 2017 CA GLU A 280 28.170 42.663 5.765 1.00 19.89 C ANISOU 2017 CA GLU A 280 2495 2989 2071 -771 259 -62 C ATOM 2018 C GLU A 280 29.294 43.686 5.676 1.00 21.49 C ANISOU 2018 C GLU A 280 2693 3180 2290 -770 275 -49 C ATOM 2019 O GLU A 280 29.863 44.075 6.697 1.00 20.01 O ANISOU 2019 O GLU A 280 2495 2979 2130 -768 269 -46 O ATOM 2020 CB GLU A 280 28.553 41.366 5.034 1.00 18.36 C ANISOU 2020 CB GLU A 280 2297 2809 1868 -771 271 -76 C ATOM 2021 CG GLU A 280 27.535 40.239 5.199 1.00 20.47 C ANISOU 2021 CG GLU A 280 2566 3088 2122 -772 256 -91 C ATOM 2022 CD GLU A 280 27.989 38.928 4.558 1.00 23.99 C ANISOU 2022 CD GLU A 280 3007 3548 2562 -772 267 -106 C ATOM 2023 OE1 GLU A 280 28.262 38.900 3.339 1.00 27.77 O ANISOU 2023 OE1 GLU A 280 3494 4035 3021 -770 286 -103 O ATOM 2024 OE2 GLU A 280 28.073 37.913 5.275 1.00 31.18 O ANISOU 2024 OE2 GLU A 280 3905 4459 3485 -771 258 -121 O ATOM 2025 N CYS A 281 29.599 44.148 4.459 1.00 19.62 N ANISOU 2025 N CYS A 281 2466 2949 2038 -770 295 -39 N ATOM 2026 CA CYS A 281 30.762 45.002 4.255 1.00 17.23 C ANISOU 2026 CA CYS A 281 2159 2637 1752 -769 313 -27 C ATOM 2027 C CYS A 281 30.557 46.392 4.846 1.00 14.10 C ANISOU 2027 C CYS A 281 1766 2227 1366 -769 304 -12 C ATOM 2028 O CYS A 281 31.401 46.878 5.607 1.00 16.96 O ANISOU 2028 O CYS A 281 2115 2574 1754 -768 305 -8 O ATOM 2029 CB CYS A 281 31.073 45.094 2.764 1.00 21.77 C ANISOU 2029 CB CYS A 281 2744 3222 2306 -767 336 -21 C ATOM 2030 SG CYS A 281 31.545 43.519 2.115 1.00 25.50 S ANISOU 2030 SG CYS A 281 3211 3709 2769 -766 348 -38 S ATOM 2031 N ASN A 282 29.457 47.055 4.493 1.00 15.58 N ANISOU 2031 N ASN A 282 1970 2417 1534 -769 296 -3 N ATOM 2032 CA ASN A 282 29.226 48.416 4.982 1.00 18.68 C ANISOU 2032 CA ASN A 282 2367 2797 1935 -769 289 11 C ATOM 2033 C ASN A 282 29.238 48.515 6.500 1.00 21.78 C ANISOU 2033 C ASN A 282 2747 3176 2353 -768 269 7 C ATOM 2034 O ASN A 282 29.978 49.360 7.031 1.00 16.86 O ANISOU 2034 O ASN A 282 2115 2539 1751 -767 272 16 O ATOM 2035 CB ASN A 282 27.917 48.967 4.391 1.00 11.40 C ANISOU 2035 CB ASN A 282 1465 1880 987 -768 281 19 C ATOM 2036 CG ASN A 282 28.152 49.698 3.102 1.00 18.84 C ANISOU 2036 CG ASN A 282 2419 2826 1914 -766 301 32 C ATOM 2037 OD1 ASN A 282 29.265 50.147 2.846 1.00 20.97 O ANISOU 2037 OD1 ASN A 282 2682 3090 2197 -765 319 40 O ATOM 2038 ND2 ASN A 282 27.123 49.808 2.273 1.00 15.65 N ANISOU 2038 ND2 ASN A 282 2034 2431 1482 -763 298 36 N ATOM 2039 N PRO A 283 28.481 47.707 7.255 1.00 27.14 N ANISOU 2039 N PRO A 283 3423 3858 3031 -768 250 -5 N ATOM 2040 CA PRO A 283 28.532 47.852 8.722 1.00 21.38 C ANISOU 2040 CA PRO A 283 2683 3114 2326 -764 232 -7 C ATOM 2041 C PRO A 283 29.921 47.665 9.311 1.00 22.67 C ANISOU 2041 C PRO A 283 2828 3267 2518 -760 240 -11 C ATOM 2042 O PRO A 283 30.314 48.420 10.216 1.00 18.70 O ANISOU 2042 O PRO A 283 2319 2750 2038 -756 234 -4 O ATOM 2043 CB PRO A 283 27.543 46.782 9.205 1.00 13.74 C ANISOU 2043 CB PRO A 283 1717 2155 1349 -763 213 -21 C ATOM 2044 CG PRO A 283 26.584 46.658 8.094 1.00 11.76 C ANISOU 2044 CG PRO A 283 1482 1918 1067 -768 215 -20 C ATOM 2045 CD PRO A 283 27.435 46.752 6.851 1.00 17.90 C ANISOU 2045 CD PRO A 283 2262 2702 1837 -770 241 -15 C ATOM 2046 N MET A 284 30.677 46.679 8.826 1.00 10.86 N ANISOU 2046 N MET A 284 1324 1779 1023 -761 254 -21 N ATOM 2047 CA MET A 284 32.035 46.477 9.325 1.00 10.25 C ANISOU 2047 CA MET A 284 1230 1692 974 -757 262 -24 C ATOM 2048 C MET A 284 32.966 47.613 8.906 1.00 16.96 C ANISOU 2048 C MET A 284 2077 2532 1834 -759 280 -9 C ATOM 2049 O MET A 284 33.847 48.014 9.674 1.00 15.46 O ANISOU 2049 O MET A 284 1875 2329 1672 -755 280 -5 O ATOM 2050 CB MET A 284 32.568 45.132 8.842 1.00 14.75 C ANISOU 2050 CB MET A 284 1791 2272 1540 -758 273 -38 C ATOM 2051 CG MET A 284 31.718 43.962 9.323 1.00 18.74 C ANISOU 2051 CG MET A 284 2297 2785 2038 -756 255 -54 C ATOM 2052 SD MET A 284 31.485 44.033 11.123 1.00 19.71 S ANISOU 2052 SD MET A 284 2411 2892 2187 -746 230 -57 S ATOM 2053 CE MET A 284 31.066 42.320 11.433 1.00 16.97 C ANISOU 2053 CE MET A 284 2058 2554 1835 -741 219 -78 C ATOM 2054 N ALA A 285 32.811 48.129 7.686 1.00 22.56 N ANISOU 2054 N ALA A 285 2798 3249 2522 -763 295 1 N ATOM 2055 CA ALA A 285 33.615 49.277 7.276 1.00 19.06 C ANISOU 2055 CA ALA A 285 2355 2798 2089 -764 312 17 C ATOM 2056 C ALA A 285 33.344 50.477 8.177 1.00 19.09 C ANISOU 2056 C ALA A 285 2359 2787 2107 -762 298 28 C ATOM 2057 O ALA A 285 34.265 51.214 8.540 1.00 13.08 O ANISOU 2057 O ALA A 285 1589 2013 1370 -760 305 36 O ATOM 2058 CB ALA A 285 33.330 49.625 5.813 1.00 18.85 C ANISOU 2058 CB ALA A 285 2344 2783 2036 -766 329 27 C ATOM 2059 N TYR A 286 32.086 50.667 8.561 1.00 18.13 N ANISOU 2059 N TYR A 286 2249 2667 1973 -762 278 28 N ATOM 2060 CA TYR A 286 31.700 51.787 9.408 1.00 20.81 C ANISOU 2060 CA TYR A 286 2590 2994 2323 -759 264 37 C ATOM 2061 C TYR A 286 32.284 51.649 10.806 1.00 20.94 C ANISOU 2061 C TYR A 286 2591 2996 2370 -753 252 31 C ATOM 2062 O TYR A 286 32.769 52.630 11.379 1.00 21.76 O ANISOU 2062 O TYR A 286 2689 3086 2494 -751 251 41 O ATOM 2063 CB TYR A 286 30.177 51.858 9.473 1.00 18.88 C ANISOU 2063 CB TYR A 286 2361 2756 2057 -760 246 37 C ATOM 2064 CG TYR A 286 29.620 53.030 10.237 1.00 20.40 C ANISOU 2064 CG TYR A 286 2559 2936 2256 -757 231 47 C ATOM 2065 CD1 TYR A 286 29.359 54.240 9.596 1.00 18.75 C ANISOU 2065 CD1 TYR A 286 2361 2725 2037 -759 238 63 C ATOM 2066 CD2 TYR A 286 29.322 52.926 11.592 1.00 24.45 C ANISOU 2066 CD2 TYR A 286 3065 3440 2785 -751 210 42 C ATOM 2067 CE1 TYR A 286 28.835 55.316 10.291 1.00 17.60 C ANISOU 2067 CE1 TYR A 286 2219 2569 1898 -757 224 72 C ATOM 2068 CE2 TYR A 286 28.791 53.997 12.296 1.00 12.87 C ANISOU 2068 CE2 TYR A 286 1604 1963 1324 -748 196 51 C ATOM 2069 CZ TYR A 286 28.559 55.188 11.639 1.00 18.43 C ANISOU 2069 CZ TYR A 286 2318 2665 2019 -752 203 66 C ATOM 2070 OH TYR A 286 28.031 56.247 12.327 1.00 26.31 O ANISOU 2070 OH TYR A 286 3321 3653 3022 -748 190 75 O ATOM 2071 N VAL A 287 32.220 50.442 11.381 1.00 14.98 N ANISOU 2071 N VAL A 287 1828 2244 1619 -749 242 16 N ATOM 2072 CA VAL A 287 32.834 50.200 12.682 1.00 11.02 C ANISOU 2072 CA VAL A 287 1311 1729 1146 -741 232 10 C ATOM 2073 C VAL A 287 34.326 50.489 12.615 1.00 17.24 C ANISOU 2073 C VAL A 287 2086 2508 1958 -741 249 14 C ATOM 2074 O VAL A 287 34.890 51.153 13.496 1.00 17.80 O ANISOU 2074 O VAL A 287 2147 2562 2053 -736 244 20 O ATOM 2075 CB VAL A 287 32.557 48.757 13.150 1.00 15.73 C ANISOU 2075 CB VAL A 287 1904 2333 1742 -737 221 -7 C ATOM 2076 CG1 VAL A 287 33.345 48.469 14.416 1.00 10.25 C ANISOU 2076 CG1 VAL A 287 1193 1623 1078 -726 213 -13 C ATOM 2077 CG2 VAL A 287 31.055 48.536 13.385 1.00 17.20 C ANISOU 2077 CG2 VAL A 287 2102 2525 1908 -736 202 -11 C ATOM 2078 N MET A 288 34.988 49.983 11.566 1.00 11.56 N ANISOU 2078 N MET A 288 1364 1797 1231 -746 269 13 N ATOM 2079 CA MET A 288 36.430 50.183 11.413 1.00 14.37 C ANISOU 2079 CA MET A 288 1706 2146 1609 -746 287 17 C ATOM 2080 C MET A 288 36.777 51.664 11.341 1.00 17.37 C ANISOU 2080 C MET A 288 2087 2514 1999 -748 294 35 C ATOM 2081 O MET A 288 37.661 52.141 12.058 1.00 19.03 O ANISOU 2081 O MET A 288 2285 2710 2238 -744 294 39 O ATOM 2082 CB MET A 288 36.930 49.450 10.168 1.00 15.96 C ANISOU 2082 CB MET A 288 1907 2359 1796 -751 309 14 C ATOM 2083 CG MET A 288 37.044 47.960 10.396 1.00 21.00 C ANISOU 2083 CG MET A 288 2538 3005 2434 -748 304 -4 C ATOM 2084 SD MET A 288 38.323 47.631 11.620 1.00 22.71 S ANISOU 2084 SD MET A 288 2733 3206 2690 -740 300 -10 S ATOM 2085 CE MET A 288 37.625 46.184 12.451 1.00 17.39 C ANISOU 2085 CE MET A 288 2058 2537 2013 -733 279 -30 C ATOM 2086 N GLU A 289 36.075 52.415 10.489 1.00 19.07 N ANISOU 2086 N GLU A 289 2317 2735 2192 -753 299 45 N ATOM 2087 CA GLU A 289 36.409 53.826 10.332 1.00 24.52 C ANISOU 2087 CA GLU A 289 3010 3416 2892 -754 307 63 C ATOM 2088 C GLU A 289 36.099 54.605 11.605 1.00 20.25 C ANISOU 2088 C GLU A 289 2466 2860 2369 -749 287 66 C ATOM 2089 O GLU A 289 36.843 55.519 11.975 1.00 21.22 O ANISOU 2089 O GLU A 289 2581 2969 2514 -748 291 76 O ATOM 2090 CB GLU A 289 35.678 54.418 9.117 1.00 20.22 C ANISOU 2090 CB GLU A 289 2483 2882 2319 -759 317 73 C ATOM 2091 CG GLU A 289 36.252 53.923 7.777 1.00 19.62 C ANISOU 2091 CG GLU A 289 2408 2817 2229 -762 342 74 C ATOM 2092 CD GLU A 289 36.006 54.864 6.593 1.00 24.25 C ANISOU 2092 CD GLU A 289 3009 3408 2796 -764 358 90 C ATOM 2093 OE1 GLU A 289 35.551 56.008 6.806 1.00 28.57 O ANISOU 2093 OE1 GLU A 289 3563 3948 3345 -764 351 102 O ATOM 2094 OE2 GLU A 289 36.294 54.458 5.443 1.00 27.60 O ANISOU 2094 OE2 GLU A 289 3438 3843 3205 -765 377 91 O ATOM 2095 N LYS A 290 35.014 54.254 12.302 1.00 18.92 N ANISOU 2095 N LYS A 290 2303 2693 2190 -746 265 58 N ATOM 2096 CA LYS A 290 34.736 54.931 13.563 1.00 16.81 C ANISOU 2096 CA LYS A 290 2034 2412 1940 -740 246 60 C ATOM 2097 C LYS A 290 35.786 54.608 14.621 1.00 20.22 C ANISOU 2097 C LYS A 290 2447 2831 2405 -733 242 54 C ATOM 2098 O LYS A 290 35.980 55.403 15.548 1.00 23.48 O ANISOU 2098 O LYS A 290 2854 3228 2837 -728 233 60 O ATOM 2099 CB LYS A 290 33.324 54.590 14.049 1.00 20.63 C ANISOU 2099 CB LYS A 290 2529 2902 2406 -737 224 54 C ATOM 2100 CG LYS A 290 32.205 55.227 13.210 1.00 18.88 C ANISOU 2100 CG LYS A 290 2328 2690 2157 -743 224 63 C ATOM 2101 CD LYS A 290 32.364 56.756 13.122 1.00 28.29 C ANISOU 2101 CD LYS A 290 3523 3872 3356 -744 229 79 C ATOM 2102 CE LYS A 290 31.228 57.404 12.322 1.00 30.46 C ANISOU 2102 CE LYS A 290 3817 4155 3603 -748 227 88 C ATOM 2103 NZ LYS A 290 31.445 58.865 12.060 1.00 27.10 N ANISOU 2103 NZ LYS A 290 3395 3720 3183 -750 235 105 N ATOM 2104 N ALA A 291 36.501 53.492 14.477 1.00 16.57 N ANISOU 2104 N ALA A 291 1976 2374 1949 -732 250 44 N ATOM 2105 CA ALA A 291 37.606 53.139 15.364 1.00 16.84 C ANISOU 2105 CA ALA A 291 1991 2395 2013 -725 248 38 C ATOM 2106 C ALA A 291 38.959 53.634 14.864 1.00 19.31 C ANISOU 2106 C ALA A 291 2292 2701 2343 -729 269 47 C ATOM 2107 O ALA A 291 39.993 53.219 15.397 1.00 24.91 O ANISOU 2107 O ALA A 291 2986 3402 3077 -725 271 43 O ATOM 2108 CB ALA A 291 37.678 51.616 15.556 1.00 16.76 C ANISOU 2108 CB ALA A 291 1975 2392 2000 -721 245 22 C ATOM 2109 N GLY A 292 38.987 54.483 13.845 1.00 24.22 N ANISOU 2109 N GLY A 292 2922 3326 2954 -736 285 60 N ATOM 2110 CA GLY A 292 40.255 54.906 13.292 1.00 17.40 C ANISOU 2110 CA GLY A 292 2047 2457 2107 -740 306 70 C ATOM 2111 C GLY A 292 40.903 53.906 12.361 1.00 18.75 C ANISOU 2111 C GLY A 292 2215 2639 2270 -743 325 64 C ATOM 2112 O GLY A 292 42.098 54.023 12.085 1.00 25.16 O ANISOU 2112 O GLY A 292 3014 3445 3100 -744 341 69 O ATOM 2113 N GLY A 293 40.162 52.908 11.877 1.00 23.10 N ANISOU 2113 N GLY A 293 2774 3206 2796 -744 323 53 N ATOM 2114 CA GLY A 293 40.686 51.953 10.928 1.00 23.12 C ANISOU 2114 CA GLY A 293 2775 3220 2788 -747 341 47 C ATOM 2115 C GLY A 293 40.296 52.313 9.508 1.00 22.08 C ANISOU 2115 C GLY A 293 2658 3102 2630 -753 359 56 C ATOM 2116 O GLY A 293 39.751 53.384 9.234 1.00 21.41 O ANISOU 2116 O GLY A 293 2584 3015 2536 -756 359 68 O ATOM 2117 N MET A 294 40.544 51.373 8.597 1.00 19.01 N ANISOU 2117 N MET A 294 2270 2726 2226 -755 373 49 N ATOM 2118 CA MET A 294 40.218 51.561 7.190 1.00 20.57 C ANISOU 2118 CA MET A 294 2481 2937 2396 -759 391 57 C ATOM 2119 C MET A 294 39.500 50.334 6.640 1.00 24.00 C ANISOU 2119 C MET A 294 2925 3389 2805 -760 390 42 C ATOM 2120 O MET A 294 39.586 49.233 7.186 1.00 17.85 O ANISOU 2120 O MET A 294 2137 2612 2031 -758 380 27 O ATOM 2121 CB MET A 294 41.464 51.832 6.346 1.00 22.77 C ANISOU 2121 CB MET A 294 2753 3214 2685 -760 418 67 C ATOM 2122 CG MET A 294 42.132 53.151 6.627 1.00 30.39 C ANISOU 2122 CG MET A 294 3711 4163 3673 -760 424 83 C ATOM 2123 SD MET A 294 43.625 53.321 5.626 1.00 38.03 S ANISOU 2123 SD MET A 294 4668 5129 4652 -760 456 95 S ATOM 2124 CE MET A 294 44.228 54.910 6.200 1.00 47.10 C ANISOU 2124 CE MET A 294 5809 6258 5830 -761 456 113 C ATOM 2125 N ALA A 295 38.760 50.547 5.554 1.00 24.58 N ANISOU 2125 N ALA A 295 3015 3475 2848 -763 398 48 N ATOM 2126 CA ALA A 295 38.106 49.449 4.851 1.00 21.25 C ANISOU 2126 CA ALA A 295 2604 3071 2400 -763 399 36 C ATOM 2127 C ALA A 295 37.963 49.848 3.393 1.00 22.00 C ANISOU 2127 C ALA A 295 2713 3176 2469 -764 419 47 C ATOM 2128 O ALA A 295 37.313 50.852 3.085 1.00 18.84 O ANISOU 2128 O ALA A 295 2325 2774 2057 -764 418 60 O ATOM 2129 CB ALA A 295 36.748 49.125 5.453 1.00 14.80 C ANISOU 2129 CB ALA A 295 1795 2258 1569 -764 374 27 C ATOM 2130 N THR A 296 38.581 49.078 2.512 1.00 19.40 N ANISOU 2130 N THR A 296 2383 2857 2133 -762 438 43 N ATOM 2131 CA THR A 296 38.642 49.401 1.097 1.00 20.40 C ANISOU 2131 CA THR A 296 2521 2992 2237 -760 460 54 C ATOM 2132 C THR A 296 38.260 48.181 0.278 1.00 25.83 C ANISOU 2132 C THR A 296 3218 3698 2899 -758 465 41 C ATOM 2133 O THR A 296 38.396 47.040 0.725 1.00 19.93 O ANISOU 2133 O THR A 296 2461 2954 2157 -759 458 24 O ATOM 2134 CB THR A 296 40.037 49.894 0.682 1.00 22.22 C ANISOU 2134 CB THR A 296 2741 3215 2486 -759 484 66 C ATOM 2135 OG1 THR A 296 40.059 50.130 -0.734 1.00 24.29 O ANISOU 2135 OG1 THR A 296 3017 3487 2724 -755 506 76 O ATOM 2136 CG2 THR A 296 41.100 48.871 1.043 1.00 17.96 C ANISOU 2136 CG2 THR A 296 2184 2675 1966 -758 490 54 C ATOM 2137 N THR A 297 37.744 48.441 -0.920 1.00 27.36 N ANISOU 2137 N THR A 297 3429 3902 3064 -755 476 48 N ATOM 2138 CA THR A 297 37.561 47.397 -1.915 1.00 30.12 C ANISOU 2138 CA THR A 297 3788 4268 3389 -751 486 39 C ATOM 2139 C THR A 297 38.833 47.123 -2.692 1.00 23.41 C ANISOU 2139 C THR A 297 2930 3420 2544 -747 513 42 C ATOM 2140 O THR A 297 38.868 46.171 -3.481 1.00 24.90 O ANISOU 2140 O THR A 297 3124 3622 2715 -743 523 33 O ATOM 2141 CB THR A 297 36.470 47.798 -2.906 1.00 33.68 C ANISOU 2141 CB THR A 297 4263 4730 3806 -746 486 46 C ATOM 2142 OG1 THR A 297 36.943 48.903 -3.695 1.00 28.14 O ANISOU 2142 OG1 THR A 297 3567 4023 3103 -742 506 65 O ATOM 2143 CG2 THR A 297 35.196 48.197 -2.163 1.00 32.35 C ANISOU 2143 CG2 THR A 297 4101 4557 3632 -750 460 44 C ATOM 2144 N GLY A 298 39.865 47.932 -2.483 1.00 27.98 N ANISOU 2144 N GLY A 298 3497 3985 3147 -748 525 55 N ATOM 2145 CA GLY A 298 41.028 47.929 -3.341 1.00 32.32 C ANISOU 2145 CA GLY A 298 4043 4537 3702 -744 553 62 C ATOM 2146 C GLY A 298 41.029 49.167 -4.214 1.00 34.62 C ANISOU 2146 C GLY A 298 4345 4825 3982 -740 568 84 C ATOM 2147 O GLY A 298 42.072 49.787 -4.427 1.00 40.85 O ANISOU 2147 O GLY A 298 5126 5606 4788 -739 587 97 O ATOM 2148 N LYS A 299 39.850 49.524 -4.730 1.00 35.65 N ANISOU 2148 N LYS A 299 4497 4964 4086 -737 561 87 N ATOM 2149 CA LYS A 299 39.682 50.663 -5.622 1.00 39.33 C ANISOU 2149 CA LYS A 299 4977 5428 4538 -732 574 106 C ATOM 2150 C LYS A 299 39.077 51.894 -4.951 1.00 37.20 C ANISOU 2150 C LYS A 299 4711 5148 4277 -736 559 117 C ATOM 2151 O LYS A 299 39.292 53.008 -5.441 1.00 42.13 O ANISOU 2151 O LYS A 299 5340 5766 4902 -733 572 136 O ATOM 2152 CB LYS A 299 38.809 50.258 -6.815 1.00 36.36 C ANISOU 2152 CB LYS A 299 4623 5069 4124 -723 578 104 C ATOM 2153 CG LYS A 299 39.461 49.204 -7.693 1.00 45.94 C ANISOU 2153 CG LYS A 299 5836 6293 5326 -717 597 96 C ATOM 2154 CD LYS A 299 38.525 48.694 -8.785 1.00 55.58 C ANISOU 2154 CD LYS A 299 7079 7530 6509 -708 598 92 C ATOM 2155 CE LYS A 299 39.222 47.636 -9.644 1.00 61.96 C ANISOU 2155 CE LYS A 299 7886 8350 7307 -701 617 84 C ATOM 2156 NZ LYS A 299 38.304 46.961 -10.606 1.00 63.83 N ANISOU 2156 NZ LYS A 299 8143 8602 7507 -691 614 75 N ATOM 2157 N GLU A 300 38.334 51.730 -3.857 1.00 23.74 N ANISOU 2157 N GLU A 300 3003 3439 2579 -741 533 107 N ATOM 2158 CA GLU A 300 37.719 52.855 -3.164 1.00 24.71 C ANISOU 2158 CA GLU A 300 3129 3551 2709 -745 517 117 C ATOM 2159 C GLU A 300 37.355 52.413 -1.753 1.00 31.09 C ANISOU 2159 C GLU A 300 3926 4354 3534 -751 491 103 C ATOM 2160 O GLU A 300 37.408 51.225 -1.418 1.00 26.73 O ANISOU 2160 O GLU A 300 3366 3807 2982 -753 485 86 O ATOM 2161 CB GLU A 300 36.468 53.361 -3.898 1.00 28.21 C ANISOU 2161 CB GLU A 300 3595 4002 3122 -740 512 123 C ATOM 2162 CG GLU A 300 35.349 52.329 -4.022 1.00 33.34 C ANISOU 2162 CG GLU A 300 4257 4666 3747 -739 496 107 C ATOM 2163 CD GLU A 300 34.272 52.735 -5.019 1.00 44.69 C ANISOU 2163 CD GLU A 300 5718 6111 5151 -732 496 114 C ATOM 2164 OE1 GLU A 300 33.822 53.907 -4.981 1.00 48.91 O ANISOU 2164 OE1 GLU A 300 6260 6638 5685 -731 491 128 O ATOM 2165 OE2 GLU A 300 33.870 51.876 -5.837 1.00 42.04 O ANISOU 2165 OE2 GLU A 300 5393 5789 4791 -726 499 106 O ATOM 2166 N ALA A 301 36.986 53.391 -0.924 1.00 24.10 N ANISOU 2166 N ALA A 301 3039 3455 2661 -754 477 110 N ATOM 2167 CA ALA A 301 36.445 53.080 0.394 1.00 22.51 C ANISOU 2167 CA ALA A 301 2831 3249 2473 -759 450 98 C ATOM 2168 C ALA A 301 35.113 52.349 0.248 1.00 26.74 C ANISOU 2168 C ALA A 301 3381 3798 2980 -758 434 87 C ATOM 2169 O ALA A 301 34.249 52.761 -0.535 1.00 23.09 O ANISOU 2169 O ALA A 301 2938 3343 2493 -755 434 94 O ATOM 2170 CB ALA A 301 36.268 54.356 1.213 1.00 24.92 C ANISOU 2170 CB ALA A 301 3134 3539 2795 -760 438 110 C ATOM 2171 N VAL A 302 34.961 51.251 0.998 1.00 23.65 N ANISOU 2171 N VAL A 302 2981 3409 2594 -761 419 69 N ATOM 2172 CA VAL A 302 33.700 50.507 1.030 1.00 26.84 C ANISOU 2172 CA VAL A 302 3396 3825 2976 -761 401 57 C ATOM 2173 C VAL A 302 32.514 51.451 1.226 1.00 25.71 C ANISOU 2173 C VAL A 302 3267 3679 2822 -761 385 66 C ATOM 2174 O VAL A 302 31.493 51.359 0.528 1.00 17.88 O ANISOU 2174 O VAL A 302 2293 2697 1803 -759 381 66 O ATOM 2175 CB VAL A 302 33.740 49.431 2.134 1.00 22.54 C ANISOU 2175 CB VAL A 302 2837 3279 2447 -764 385 39 C ATOM 2176 CG1 VAL A 302 32.381 48.773 2.261 1.00 15.72 C ANISOU 2176 CG1 VAL A 302 1985 2426 1563 -765 365 29 C ATOM 2177 CG2 VAL A 302 34.810 48.376 1.840 1.00 16.91 C ANISOU 2177 CG2 VAL A 302 2112 2572 1742 -763 400 29 C ATOM 2178 N LEU A 303 32.632 52.375 2.185 1.00 20.99 N ANISOU 2178 N LEU A 303 2662 3066 2246 -763 375 74 N ATOM 2179 CA LEU A 303 31.516 53.250 2.515 1.00 18.70 C ANISOU 2179 CA LEU A 303 2385 2773 1949 -763 357 81 C ATOM 2180 C LEU A 303 31.154 54.216 1.390 1.00 18.64 C ANISOU 2180 C LEU A 303 2394 2767 1920 -759 369 97 C ATOM 2181 O LEU A 303 30.063 54.794 1.430 1.00 20.75 O ANISOU 2181 O LEU A 303 2674 3034 2174 -758 355 102 O ATOM 2182 CB LEU A 303 31.825 54.023 3.797 1.00 21.24 C ANISOU 2182 CB LEU A 303 2695 3077 2299 -765 345 86 C ATOM 2183 CG LEU A 303 32.052 53.166 5.042 1.00 15.98 C ANISOU 2183 CG LEU A 303 2013 2406 1653 -766 330 70 C ATOM 2184 CD1 LEU A 303 32.421 54.004 6.237 1.00 18.70 C ANISOU 2184 CD1 LEU A 303 2346 2733 2026 -765 319 76 C ATOM 2185 CD2 LEU A 303 30.832 52.308 5.363 1.00 18.08 C ANISOU 2185 CD2 LEU A 303 2285 2681 1902 -767 309 58 C ATOM 2186 N ASP A 304 32.004 54.364 0.368 1.00 20.75 N ANISOU 2186 N ASP A 304 2663 3038 2185 -756 395 105 N ATOM 2187 CA ASP A 304 31.717 55.247 -0.755 1.00 29.59 C ANISOU 2187 CA ASP A 304 3798 4159 3285 -751 408 120 C ATOM 2188 C ASP A 304 31.080 54.530 -1.937 1.00 31.20 C ANISOU 2188 C ASP A 304 4018 4379 3456 -745 413 115 C ATOM 2189 O ASP A 304 30.582 55.199 -2.848 1.00 28.08 O ANISOU 2189 O ASP A 304 3640 3988 3042 -739 420 126 O ATOM 2190 CB ASP A 304 33.001 55.954 -1.224 1.00 30.78 C ANISOU 2190 CB ASP A 304 3941 4302 3451 -750 433 134 C ATOM 2191 CG ASP A 304 33.436 57.056 -0.271 1.00 28.70 C ANISOU 2191 CG ASP A 304 3666 4022 3216 -753 428 144 C ATOM 2192 OD1 ASP A 304 32.558 57.683 0.356 1.00 27.01 O ANISOU 2192 OD1 ASP A 304 3458 3802 3002 -754 408 146 O ATOM 2193 OD2 ASP A 304 34.654 57.301 -0.153 1.00 32.37 O ANISOU 2193 OD2 ASP A 304 4117 4479 3704 -754 443 149 O ATOM 2194 N VAL A 305 31.066 53.196 -1.945 1.00 28.84 N ANISOU 2194 N VAL A 305 3716 4091 3151 -746 411 99 N ATOM 2195 CA VAL A 305 30.396 52.484 -3.020 1.00 27.83 C ANISOU 2195 CA VAL A 305 3605 3979 2993 -739 414 93 C ATOM 2196 C VAL A 305 28.908 52.798 -2.981 1.00 24.74 C ANISOU 2196 C VAL A 305 3229 3589 2582 -737 393 94 C ATOM 2197 O VAL A 305 28.268 52.729 -1.925 1.00 23.87 O ANISOU 2197 O VAL A 305 3115 3475 2481 -743 370 88 O ATOM 2198 CB VAL A 305 30.652 50.978 -2.900 1.00 22.49 C ANISOU 2198 CB VAL A 305 2919 3312 2315 -741 413 74 C ATOM 2199 CG1 VAL A 305 29.973 50.252 -4.059 1.00 21.27 C ANISOU 2199 CG1 VAL A 305 2782 3173 2128 -733 416 68 C ATOM 2200 CG2 VAL A 305 32.146 50.704 -2.872 1.00 26.66 C ANISOU 2200 CG2 VAL A 305 3430 3836 2864 -743 433 73 C ATOM 2201 N ILE A 306 28.343 53.142 -4.134 1.00 23.67 N ANISOU 2201 N ILE A 306 3113 3461 2421 -728 399 101 N ATOM 2202 CA ILE A 306 26.913 53.417 -4.245 1.00 25.84 C ANISOU 2202 CA ILE A 306 3404 3737 2677 -724 380 102 C ATOM 2203 C ILE A 306 26.237 52.152 -4.776 1.00 29.88 C ANISOU 2203 C ILE A 306 3924 4264 3166 -719 373 87 C ATOM 2204 O ILE A 306 26.478 51.780 -5.933 1.00 32.77 O ANISOU 2204 O ILE A 306 4299 4639 3514 -710 390 87 O ATOM 2205 CB ILE A 306 26.630 54.624 -5.149 1.00 35.13 C ANISOU 2205 CB ILE A 306 4596 4911 3840 -716 389 120 C ATOM 2206 CG1 ILE A 306 27.320 55.868 -4.587 1.00 34.29 C ANISOU 2206 CG1 ILE A 306 4481 4791 3758 -721 396 135 C ATOM 2207 CG2 ILE A 306 25.115 54.851 -5.288 1.00 32.84 C ANISOU 2207 CG2 ILE A 306 4324 4624 3531 -710 369 120 C ATOM 2208 CD1 ILE A 306 26.957 57.138 -5.316 1.00 43.98 C ANISOU 2208 CD1 ILE A 306 5722 6013 4974 -713 402 152 C ATOM 2209 N PRO A 307 25.415 51.472 -3.981 1.00 21.68 N ANISOU 2209 N PRO A 307 2883 3227 2128 -723 350 75 N ATOM 2210 CA PRO A 307 24.863 50.194 -4.438 1.00 20.08 C ANISOU 2210 CA PRO A 307 2686 3037 1906 -719 344 59 C ATOM 2211 C PRO A 307 23.777 50.389 -5.481 1.00 21.79 C ANISOU 2211 C PRO A 307 2926 3260 2095 -706 339 63 C ATOM 2212 O PRO A 307 23.093 51.416 -5.533 1.00 25.06 O ANISOU 2212 O PRO A 307 3349 3667 2504 -703 332 75 O ATOM 2213 CB PRO A 307 24.294 49.567 -3.160 1.00 19.98 C ANISOU 2213 CB PRO A 307 2663 3022 1905 -727 320 47 C ATOM 2214 CG PRO A 307 24.008 50.735 -2.260 1.00 26.14 C ANISOU 2214 CG PRO A 307 3441 3790 2702 -733 308 58 C ATOM 2215 CD PRO A 307 25.008 51.807 -2.602 1.00 19.79 C ANISOU 2215 CD PRO A 307 2634 2977 1907 -732 329 74 C ATOM 2216 N THR A 308 23.634 49.381 -6.325 1.00 20.27 N ANISOU 2216 N THR A 308 2740 3080 1883 -698 343 52 N ATOM 2217 CA THR A 308 22.513 49.304 -7.246 1.00 26.12 C ANISOU 2217 CA THR A 308 3501 3827 2598 -685 335 52 C ATOM 2218 C THR A 308 21.633 48.081 -7.003 1.00 22.90 C ANISOU 2218 C THR A 308 3093 3426 2182 -683 315 34 C ATOM 2219 O THR A 308 20.529 48.008 -7.555 1.00 23.91 O ANISOU 2219 O THR A 308 3237 3557 2292 -673 302 33 O ATOM 2220 CB THR A 308 23.030 49.332 -8.697 1.00 29.94 C ANISOU 2220 CB THR A 308 3996 4317 3062 -673 358 57 C ATOM 2221 OG1 THR A 308 23.869 48.199 -8.939 1.00 31.11 O ANISOU 2221 OG1 THR A 308 4136 4475 3211 -673 371 45 O ATOM 2222 CG2 THR A 308 23.858 50.603 -8.931 1.00 20.10 C ANISOU 2222 CG2 THR A 308 2749 3063 1825 -674 378 76 C ATOM 2223 N ASP A 309 22.065 47.149 -6.160 1.00 20.20 N ANISOU 2223 N ASP A 309 2735 3086 1854 -693 311 21 N ATOM 2224 CA ASP A 309 21.303 45.945 -5.842 1.00 19.07 C ANISOU 2224 CA ASP A 309 2590 2949 1706 -692 292 4 C ATOM 2225 C ASP A 309 21.522 45.652 -4.365 1.00 17.07 C ANISOU 2225 C ASP A 309 2318 2692 1477 -707 281 -3 C ATOM 2226 O ASP A 309 22.665 45.659 -3.905 1.00 21.24 O ANISOU 2226 O ASP A 309 2831 3217 2023 -716 294 -3 O ATOM 2227 CB ASP A 309 21.757 44.772 -6.739 1.00 24.95 C ANISOU 2227 CB ASP A 309 3336 3706 2436 -684 304 -9 C ATOM 2228 CG ASP A 309 21.093 43.437 -6.391 1.00 41.28 C ANISOU 2228 CG ASP A 309 5400 5782 4501 -683 286 -28 C ATOM 2229 OD1 ASP A 309 20.239 43.362 -5.487 1.00 41.15 O ANISOU 2229 OD1 ASP A 309 5381 5762 4494 -688 264 -32 O ATOM 2230 OD2 ASP A 309 21.415 42.445 -7.075 1.00 52.49 O ANISOU 2230 OD2 ASP A 309 6821 7211 5910 -677 294 -40 O ATOM 2231 N ILE A 310 20.437 45.388 -3.624 1.00 16.33 N ANISOU 2231 N ILE A 310 2224 2596 1386 -709 256 -9 N ATOM 2232 CA ILE A 310 20.556 45.251 -2.172 1.00 21.48 C ANISOU 2232 CA ILE A 310 2859 3242 2061 -722 244 -13 C ATOM 2233 C ILE A 310 21.407 44.045 -1.765 1.00 28.32 C ANISOU 2233 C ILE A 310 3707 4114 2937 -728 251 -28 C ATOM 2234 O ILE A 310 21.889 43.979 -0.626 1.00 26.91 O ANISOU 2234 O ILE A 310 3513 3931 2781 -739 247 -31 O ATOM 2235 CB ILE A 310 19.163 45.168 -1.511 1.00 16.77 C ANISOU 2235 CB ILE A 310 2266 2642 1463 -721 216 -16 C ATOM 2236 CG1 ILE A 310 18.374 43.967 -2.045 1.00 19.00 C ANISOU 2236 CG1 ILE A 310 2555 2934 1730 -712 206 -30 C ATOM 2237 CG2 ILE A 310 18.377 46.468 -1.711 1.00 13.05 C ANISOU 2237 CG2 ILE A 310 1809 2162 987 -716 209 0 C ATOM 2238 CD1 ILE A 310 17.092 43.699 -1.267 1.00 16.98 C ANISOU 2238 CD1 ILE A 310 2299 2674 1477 -711 178 -35 C ATOM 2239 N HIS A 311 21.579 43.069 -2.655 1.00 17.99 N ANISOU 2239 N HIS A 311 2403 2818 1615 -721 259 -39 N ATOM 2240 CA HIS A 311 22.363 41.875 -2.359 1.00 18.29 C ANISOU 2240 CA HIS A 311 2426 2863 1662 -726 266 -55 C ATOM 2241 C HIS A 311 23.686 41.843 -3.106 1.00 26.13 C ANISOU 2241 C HIS A 311 3415 3859 2655 -724 293 -53 C ATOM 2242 O HIS A 311 24.292 40.770 -3.247 1.00 19.62 O ANISOU 2242 O HIS A 311 2581 3042 1831 -724 302 -66 O ATOM 2243 CB HIS A 311 21.543 40.628 -2.668 1.00 23.32 C ANISOU 2243 CB HIS A 311 3067 3510 2284 -718 253 -71 C ATOM 2244 CG HIS A 311 20.325 40.484 -1.809 1.00 20.55 C ANISOU 2244 CG HIS A 311 2716 3155 1936 -720 226 -75 C ATOM 2245 ND1 HIS A 311 20.397 40.300 -0.445 1.00 20.59 N ANISOU 2245 ND1 HIS A 311 2705 3156 1963 -732 215 -79 N ATOM 2246 CD2 HIS A 311 19.007 40.498 -2.118 1.00 19.32 C ANISOU 2246 CD2 HIS A 311 2575 2999 1768 -710 207 -75 C ATOM 2247 CE1 HIS A 311 19.175 40.197 0.049 1.00 20.89 C ANISOU 2247 CE1 HIS A 311 2747 3191 1999 -730 191 -81 C ATOM 2248 NE2 HIS A 311 18.313 40.314 -0.945 1.00 20.01 N ANISOU 2248 NE2 HIS A 311 2654 3081 1868 -716 186 -78 N ATOM 2249 N GLN A 312 24.152 42.998 -3.576 1.00 22.35 N ANISOU 2249 N GLN A 312 2942 3373 2176 -723 308 -36 N ATOM 2250 CA GLN A 312 25.368 43.031 -4.359 1.00 20.41 C ANISOU 2250 CA GLN A 312 2694 3131 1931 -720 335 -33 C ATOM 2251 C GLN A 312 26.575 42.770 -3.467 1.00 26.78 C ANISOU 2251 C GLN A 312 3478 3932 2765 -731 343 -37 C ATOM 2252 O GLN A 312 26.579 43.061 -2.265 1.00 21.26 O ANISOU 2252 O GLN A 312 2766 3223 2087 -740 331 -36 O ATOM 2253 CB GLN A 312 25.512 44.366 -5.094 1.00 21.97 C ANISOU 2253 CB GLN A 312 2905 3322 2122 -714 347 -13 C ATOM 2254 CG GLN A 312 26.167 45.478 -4.314 1.00 21.96 C ANISOU 2254 CG GLN A 312 2893 3308 2144 -724 352 1 C ATOM 2255 CD GLN A 312 26.275 46.763 -5.131 1.00 26.36 C ANISOU 2255 CD GLN A 312 3463 3859 2693 -717 365 20 C ATOM 2256 OE1 GLN A 312 25.288 47.239 -5.702 1.00 24.23 O ANISOU 2256 OE1 GLN A 312 3210 3591 2404 -709 357 26 O ATOM 2257 NE2 GLN A 312 27.472 47.316 -5.198 1.00 15.81 N ANISOU 2257 NE2 GLN A 312 2118 2518 1372 -720 386 29 N ATOM 2258 N ARG A 313 27.593 42.183 -4.068 1.00 21.11 N ANISOU 2258 N ARG A 313 2754 3219 2047 -728 364 -42 N ATOM 2259 CA ARG A 313 28.796 41.808 -3.358 1.00 24.03 C ANISOU 2259 CA ARG A 313 3102 3585 2443 -736 373 -47 C ATOM 2260 C ARG A 313 29.820 42.927 -3.455 1.00 24.86 C ANISOU 2260 C ARG A 313 3203 3679 2563 -737 391 -30 C ATOM 2261 O ARG A 313 29.762 43.781 -4.343 1.00 24.56 O ANISOU 2261 O ARG A 313 3180 3641 2512 -731 402 -16 O ATOM 2262 CB ARG A 313 29.371 40.517 -3.941 1.00 28.82 C ANISOU 2262 CB ARG A 313 3704 4203 3043 -732 385 -62 C ATOM 2263 CG ARG A 313 28.380 39.347 -4.017 1.00 32.52 C ANISOU 2263 CG ARG A 313 4178 4683 3494 -728 368 -79 C ATOM 2264 CD ARG A 313 29.048 38.158 -4.693 1.00 33.03 C ANISOU 2264 CD ARG A 313 4238 4758 3552 -722 382 -93 C ATOM 2265 NE ARG A 313 28.157 37.019 -4.910 1.00 36.18 N ANISOU 2265 NE ARG A 313 4643 5169 3934 -717 368 -110 N ATOM 2266 CZ ARG A 313 27.963 36.033 -4.040 1.00 41.06 C ANISOU 2266 CZ ARG A 313 5248 5789 4563 -722 354 -126 C ATOM 2267 NH1 ARG A 313 28.586 36.036 -2.866 1.00 36.64 N ANISOU 2267 NH1 ARG A 313 4668 5221 4032 -734 352 -128 N ATOM 2268 NH2 ARG A 313 27.141 35.038 -4.343 1.00 45.54 N ANISOU 2268 NH2 ARG A 313 5823 6367 5115 -716 341 -140 N ATOM 2269 N ALA A 314 30.771 42.911 -2.525 1.00 20.87 N ANISOU 2269 N ALA A 314 2678 3165 2088 -745 394 -32 N ATOM 2270 CA ALA A 314 31.855 43.865 -2.558 1.00 19.26 C ANISOU 2270 CA ALA A 314 2467 2950 1902 -746 411 -18 C ATOM 2271 C ALA A 314 33.091 43.179 -2.009 1.00 19.32 C ANISOU 2271 C ALA A 314 2453 2954 1935 -749 420 -26 C ATOM 2272 O ALA A 314 32.989 42.417 -1.034 1.00 21.24 O ANISOU 2272 O ALA A 314 2684 3196 2192 -754 405 -40 O ATOM 2273 CB ALA A 314 31.555 45.124 -1.734 1.00 19.22 C ANISOU 2273 CB ALA A 314 2461 2930 1911 -750 399 -4 C ATOM 2274 N PRO A 315 34.258 43.434 -2.587 1.00 25.97 N ANISOU 2274 N PRO A 315 3290 3793 2784 -747 444 -19 N ATOM 2275 CA PRO A 315 35.499 43.030 -1.928 1.00 24.87 C ANISOU 2275 CA PRO A 315 3129 3646 2674 -750 451 -24 C ATOM 2276 C PRO A 315 35.723 43.905 -0.710 1.00 23.94 C ANISOU 2276 C PRO A 315 3001 3511 2585 -756 439 -17 C ATOM 2277 O PRO A 315 35.222 45.030 -0.625 1.00 22.93 O ANISOU 2277 O PRO A 315 2881 3377 2455 -756 433 -3 O ATOM 2278 CB PRO A 315 36.577 43.266 -2.995 1.00 23.53 C ANISOU 2278 CB PRO A 315 2961 3478 2503 -745 479 -14 C ATOM 2279 CG PRO A 315 35.837 43.629 -4.258 1.00 22.09 C ANISOU 2279 CG PRO A 315 2801 3305 2287 -737 487 -6 C ATOM 2280 CD PRO A 315 34.512 44.167 -3.836 1.00 23.25 C ANISOU 2280 CD PRO A 315 2960 3451 2424 -740 465 -4 C ATOM 2281 N VAL A 316 36.445 43.363 0.263 1.00 23.15 N ANISOU 2281 N VAL A 316 2880 3403 2511 -758 434 -26 N ATOM 2282 CA VAL A 316 36.703 44.108 1.486 1.00 19.21 C ANISOU 2282 CA VAL A 316 2370 2887 2041 -761 421 -21 C ATOM 2283 C VAL A 316 38.093 43.760 2.016 1.00 15.91 C ANISOU 2283 C VAL A 316 1931 2460 1653 -761 430 -25 C ATOM 2284 O VAL A 316 38.458 42.589 2.147 1.00 19.38 O ANISOU 2284 O VAL A 316 2362 2905 2097 -760 430 -40 O ATOM 2285 CB VAL A 316 35.601 43.859 2.532 1.00 18.39 C ANISOU 2285 CB VAL A 316 2268 2783 1938 -764 393 -30 C ATOM 2286 CG1 VAL A 316 35.464 42.373 2.826 1.00 28.85 C ANISOU 2286 CG1 VAL A 316 3585 4116 3261 -764 384 -50 C ATOM 2287 CG2 VAL A 316 35.877 44.653 3.801 1.00 20.98 C ANISOU 2287 CG2 VAL A 316 2585 3093 2295 -764 380 -24 C ATOM 2288 N ILE A 317 38.864 44.803 2.305 1.00 15.33 N ANISOU 2288 N ILE A 317 1851 2372 1600 -761 437 -11 N ATOM 2289 CA ILE A 317 40.149 44.730 2.987 1.00 21.68 C ANISOU 2289 CA ILE A 317 2635 3163 2437 -759 441 -11 C ATOM 2290 C ILE A 317 40.090 45.770 4.094 1.00 30.18 C ANISOU 2290 C ILE A 317 3707 4224 3536 -760 426 -3 C ATOM 2291 O ILE A 317 39.910 46.963 3.815 1.00 26.51 O ANISOU 2291 O ILE A 317 3251 3754 3069 -761 430 13 O ATOM 2292 CB ILE A 317 41.321 45.021 2.032 1.00 25.26 C ANISOU 2292 CB ILE A 317 3086 3617 2895 -758 470 -1 C ATOM 2293 CG1 ILE A 317 41.385 43.977 0.911 1.00 21.03 C ANISOU 2293 CG1 ILE A 317 2556 3098 2336 -756 485 -9 C ATOM 2294 CG2 ILE A 317 42.635 45.137 2.806 1.00 27.71 C ANISOU 2294 CG2 ILE A 317 3375 3912 3241 -757 473 1 C ATOM 2295 CD1 ILE A 317 40.608 44.358 -0.314 1.00 23.24 C ANISOU 2295 CD1 ILE A 317 2856 3390 2583 -754 495 -1 C ATOM 2296 N LEU A 318 40.192 45.331 5.348 1.00 28.62 N ANISOU 2296 N LEU A 318 3497 4017 3359 -758 408 -13 N ATOM 2297 CA LEU A 318 39.958 46.265 6.439 1.00 24.57 C ANISOU 2297 CA LEU A 318 2982 3490 2865 -757 391 -6 C ATOM 2298 C LEU A 318 40.882 45.983 7.616 1.00 19.61 C ANISOU 2298 C LEU A 318 2335 2847 2270 -753 383 -12 C ATOM 2299 O LEU A 318 41.442 44.896 7.760 1.00 23.17 O ANISOU 2299 O LEU A 318 2776 3301 2729 -750 384 -24 O ATOM 2300 CB LEU A 318 38.488 46.236 6.902 1.00 22.61 C ANISOU 2300 CB LEU A 318 2746 3246 2600 -758 367 -11 C ATOM 2301 CG LEU A 318 37.880 44.949 7.474 1.00 19.85 C ANISOU 2301 CG LEU A 318 2393 2902 2245 -756 350 -30 C ATOM 2302 CD1 LEU A 318 38.340 44.692 8.890 1.00 22.17 C ANISOU 2302 CD1 LEU A 318 2672 3182 2568 -750 335 -37 C ATOM 2303 CD2 LEU A 318 36.376 45.051 7.446 1.00 12.82 C ANISOU 2303 CD2 LEU A 318 1519 2020 1331 -758 334 -31 C ATOM 2304 N GLY A 319 40.996 46.973 8.489 1.00 18.65 N ANISOU 2304 N GLY A 319 2208 2709 2168 -751 372 -2 N ATOM 2305 CA GLY A 319 41.767 46.778 9.696 1.00 18.94 C ANISOU 2305 CA GLY A 319 2229 2732 2237 -745 362 -7 C ATOM 2306 C GLY A 319 42.634 47.962 10.040 1.00 21.56 C ANISOU 2306 C GLY A 319 2551 3047 2593 -744 368 8 C ATOM 2307 O GLY A 319 42.237 49.119 9.843 1.00 21.63 O ANISOU 2307 O GLY A 319 2569 3053 2598 -747 368 21 O ATOM 2308 N SER A 320 43.799 47.676 10.598 1.00 18.60 N ANISOU 2308 N SER A 320 2159 2661 2245 -740 370 5 N ATOM 2309 CA SER A 320 44.682 48.738 11.055 1.00 18.55 C ANISOU 2309 CA SER A 320 2144 2639 2267 -739 374 19 C ATOM 2310 C SER A 320 45.116 49.598 9.873 1.00 20.78 C ANISOU 2310 C SER A 320 2430 2924 2543 -745 398 35 C ATOM 2311 O SER A 320 45.368 49.071 8.786 1.00 22.65 O ANISOU 2311 O SER A 320 2669 3173 2764 -748 416 34 O ATOM 2312 CB SER A 320 45.884 48.139 11.772 1.00 22.19 C ANISOU 2312 CB SER A 320 2584 3089 2756 -734 373 13 C ATOM 2313 OG SER A 320 45.441 47.411 12.910 1.00 21.18 O ANISOU 2313 OG SER A 320 2455 2959 2635 -726 350 -1 O ATOM 2314 N PRO A 321 45.175 50.927 10.036 1.00 22.07 N ANISOU 2314 N PRO A 321 2593 3075 2716 -746 398 50 N ATOM 2315 CA PRO A 321 45.409 51.793 8.862 1.00 19.91 C ANISOU 2315 CA PRO A 321 2326 2805 2433 -751 420 66 C ATOM 2316 C PRO A 321 46.756 51.589 8.174 1.00 25.25 C ANISOU 2316 C PRO A 321 2991 3482 3122 -752 444 72 C ATOM 2317 O PRO A 321 46.803 51.588 6.938 1.00 23.37 O ANISOU 2317 O PRO A 321 2761 3254 2865 -755 465 78 O ATOM 2318 CB PRO A 321 45.236 53.212 9.433 1.00 23.47 C ANISOU 2318 CB PRO A 321 2778 3242 2898 -751 412 80 C ATOM 2319 CG PRO A 321 45.396 53.071 10.929 1.00 25.68 C ANISOU 2319 CG PRO A 321 3046 3508 3203 -746 390 72 C ATOM 2320 CD PRO A 321 44.849 51.698 11.249 1.00 19.74 C ANISOU 2320 CD PRO A 321 2296 2766 2438 -743 377 53 C ATOM 2321 N ASP A 322 47.853 51.414 8.917 1.00 20.72 N ANISOU 2321 N ASP A 322 2398 2895 2578 -749 443 70 N ATOM 2322 CA ASP A 322 49.130 51.159 8.257 1.00 19.06 C ANISOU 2322 CA ASP A 322 2177 2686 2380 -750 465 75 C ATOM 2323 C ASP A 322 49.079 49.871 7.443 1.00 26.79 C ANISOU 2323 C ASP A 322 3160 3682 3338 -750 476 63 C ATOM 2324 O ASP A 322 49.614 49.810 6.331 1.00 28.91 O ANISOU 2324 O ASP A 322 3430 3958 3598 -751 500 69 O ATOM 2325 CB ASP A 322 50.253 51.107 9.293 1.00 30.15 C ANISOU 2325 CB ASP A 322 3560 4074 3820 -746 458 74 C ATOM 2326 CG ASP A 322 50.591 52.480 9.858 1.00 34.90 C ANISOU 2326 CG ASP A 322 4156 4659 4446 -746 454 90 C ATOM 2327 OD1 ASP A 322 49.939 53.467 9.453 1.00 35.20 O ANISOU 2327 OD1 ASP A 322 4205 4697 4472 -749 457 101 O ATOM 2328 OD2 ASP A 322 51.492 52.570 10.717 1.00 36.57 O ANISOU 2328 OD2 ASP A 322 4350 4856 4687 -743 447 91 O ATOM 2329 N ASP A 323 48.393 48.846 7.953 1.00 26.45 N ANISOU 2329 N ASP A 323 3121 3646 3285 -747 459 45 N ATOM 2330 CA ASP A 323 48.343 47.579 7.230 1.00 20.48 C ANISOU 2330 CA ASP A 323 2367 2905 2509 -747 468 32 C ATOM 2331 C ASP A 323 47.536 47.731 5.950 1.00 24.73 C ANISOU 2331 C ASP A 323 2924 3459 3013 -751 481 37 C ATOM 2332 O ASP A 323 47.965 47.289 4.880 1.00 27.88 O ANISOU 2332 O ASP A 323 3325 3868 3400 -752 502 38 O ATOM 2333 CB ASP A 323 47.747 46.488 8.120 1.00 17.25 C ANISOU 2333 CB ASP A 323 1958 2499 2099 -744 446 13 C ATOM 2334 CG ASP A 323 48.659 46.110 9.283 1.00 21.73 C ANISOU 2334 CG ASP A 323 2506 3052 2698 -738 435 7 C ATOM 2335 OD1 ASP A 323 49.854 45.801 9.049 1.00 20.79 O ANISOU 2335 OD1 ASP A 323 2374 2929 2594 -738 449 9 O ATOM 2336 OD2 ASP A 323 48.187 46.133 10.438 1.00 16.82 O ANISOU 2336 OD2 ASP A 323 1883 2422 2086 -734 412 1 O ATOM 2337 N VAL A 324 46.374 48.386 6.034 1.00 21.93 N ANISOU 2337 N VAL A 324 2584 3105 2643 -753 469 40 N ATOM 2338 CA VAL A 324 45.550 48.585 4.845 1.00 21.57 C ANISOU 2338 CA VAL A 324 2558 3075 2565 -756 480 46 C ATOM 2339 C VAL A 324 46.288 49.431 3.813 1.00 29.22 C ANISOU 2339 C VAL A 324 3527 4042 3533 -756 506 64 C ATOM 2340 O VAL A 324 46.281 49.122 2.615 1.00 27.96 O ANISOU 2340 O VAL A 324 3377 3896 3352 -756 525 66 O ATOM 2341 CB VAL A 324 44.203 49.215 5.234 1.00 23.94 C ANISOU 2341 CB VAL A 324 2872 3375 2850 -757 461 47 C ATOM 2342 CG1 VAL A 324 43.390 49.532 3.992 1.00 27.51 C ANISOU 2342 CG1 VAL A 324 3343 3840 3268 -759 472 55 C ATOM 2343 CG2 VAL A 324 43.431 48.283 6.158 1.00 29.42 C ANISOU 2343 CG2 VAL A 324 3565 4071 3541 -756 436 29 C ATOM 2344 N LEU A 325 46.939 50.510 4.259 1.00 26.20 N ANISOU 2344 N LEU A 325 3136 3644 3176 -757 508 78 N ATOM 2345 CA LEU A 325 47.689 51.347 3.330 1.00 29.11 C ANISOU 2345 CA LEU A 325 3503 4011 3547 -757 533 97 C ATOM 2346 C LEU A 325 48.792 50.552 2.651 1.00 26.05 C ANISOU 2346 C LEU A 325 3107 3629 3164 -755 555 94 C ATOM 2347 O LEU A 325 49.013 50.682 1.439 1.00 30.41 O ANISOU 2347 O LEU A 325 3665 4188 3699 -754 577 104 O ATOM 2348 CB LEU A 325 48.293 52.548 4.058 1.00 28.70 C ANISOU 2348 CB LEU A 325 3439 3939 3525 -758 530 111 C ATOM 2349 CG LEU A 325 47.369 53.642 4.573 1.00 35.24 C ANISOU 2349 CG LEU A 325 4278 4761 4352 -759 514 118 C ATOM 2350 CD1 LEU A 325 48.177 54.660 5.386 1.00 32.92 C ANISOU 2350 CD1 LEU A 325 3969 4447 4093 -759 510 130 C ATOM 2351 CD2 LEU A 325 46.606 54.302 3.440 1.00 39.26 C ANISOU 2351 CD2 LEU A 325 4806 5279 4831 -760 525 130 C ATOM 2352 N GLU A 326 49.478 49.700 3.406 1.00 21.22 N ANISOU 2352 N GLU A 326 2479 3012 2573 -754 547 82 N ATOM 2353 CA GLU A 326 50.495 48.856 2.790 1.00 27.65 C ANISOU 2353 CA GLU A 326 3285 3832 3391 -752 567 79 C ATOM 2354 C GLU A 326 49.868 47.963 1.729 1.00 30.55 C ANISOU 2354 C GLU A 326 3666 4219 3723 -751 576 70 C ATOM 2355 O GLU A 326 50.413 47.809 0.628 1.00 26.34 O ANISOU 2355 O GLU A 326 3136 3694 3180 -749 600 76 O ATOM 2356 CB GLU A 326 51.210 48.023 3.858 1.00 26.84 C ANISOU 2356 CB GLU A 326 3163 3721 3314 -750 554 66 C ATOM 2357 CG GLU A 326 52.347 47.166 3.317 1.00 33.55 C ANISOU 2357 CG GLU A 326 4002 4575 4170 -748 573 62 C ATOM 2358 CD GLU A 326 53.046 46.349 4.392 1.00 35.84 C ANISOU 2358 CD GLU A 326 4275 4857 4486 -745 559 50 C ATOM 2359 OE1 GLU A 326 52.928 46.687 5.589 1.00 36.62 O ANISOU 2359 OE1 GLU A 326 4367 4943 4604 -745 538 48 O ATOM 2360 OE2 GLU A 326 53.714 45.362 4.035 1.00 38.88 O ANISOU 2360 OE2 GLU A 326 4653 5248 4871 -743 570 42 O ATOM 2361 N PHE A 327 48.703 47.388 2.028 1.00 26.10 N ANISOU 2361 N PHE A 327 3113 3663 3140 -751 557 56 N ATOM 2362 CA PHE A 327 48.014 46.627 0.999 1.00 26.90 C ANISOU 2362 CA PHE A 327 3230 3783 3207 -750 565 48 C ATOM 2363 C PHE A 327 47.712 47.489 -0.219 1.00 29.01 C ANISOU 2363 C PHE A 327 3514 4057 3453 -749 584 65 C ATOM 2364 O PHE A 327 47.888 47.044 -1.358 1.00 31.28 O ANISOU 2364 O PHE A 327 3808 4357 3721 -746 603 65 O ATOM 2365 CB PHE A 327 46.715 46.040 1.531 1.00 24.40 C ANISOU 2365 CB PHE A 327 2923 3473 2874 -752 541 33 C ATOM 2366 CG PHE A 327 45.886 45.416 0.457 1.00 28.29 C ANISOU 2366 CG PHE A 327 3433 3985 3331 -751 548 26 C ATOM 2367 CD1 PHE A 327 46.175 44.135 0.006 1.00 28.79 C ANISOU 2367 CD1 PHE A 327 3494 4060 3385 -749 555 12 C ATOM 2368 CD2 PHE A 327 44.855 46.121 -0.143 1.00 23.26 C ANISOU 2368 CD2 PHE A 327 2815 3354 2668 -751 547 35 C ATOM 2369 CE1 PHE A 327 45.430 43.558 -1.004 1.00 32.40 C ANISOU 2369 CE1 PHE A 327 3967 4535 3809 -747 561 7 C ATOM 2370 CE2 PHE A 327 44.102 45.550 -1.155 1.00 24.58 C ANISOU 2370 CE2 PHE A 327 2999 3539 2802 -749 552 30 C ATOM 2371 CZ PHE A 327 44.385 44.268 -1.586 1.00 27.05 C ANISOU 2371 CZ PHE A 327 3309 3862 3105 -747 560 15 C ATOM 2372 N LEU A 328 47.227 48.718 0.002 1.00 26.77 N ANISOU 2372 N LEU A 328 3236 3765 3171 -751 577 78 N ATOM 2373 CA LEU A 328 46.852 49.578 -1.119 1.00 29.59 C ANISOU 2373 CA LEU A 328 3609 4128 3506 -750 593 94 C ATOM 2374 C LEU A 328 48.064 49.982 -1.944 1.00 27.27 C ANISOU 2374 C LEU A 328 3309 3832 3222 -747 622 109 C ATOM 2375 O LEU A 328 47.961 50.111 -3.166 1.00 27.39 O ANISOU 2375 O LEU A 328 3336 3856 3213 -742 641 118 O ATOM 2376 CB LEU A 328 46.100 50.819 -0.618 1.00 22.42 C ANISOU 2376 CB LEU A 328 2708 3210 2599 -752 579 105 C ATOM 2377 CG LEU A 328 44.660 50.598 -0.126 1.00 26.74 C ANISOU 2377 CG LEU A 328 3268 3763 3128 -754 554 94 C ATOM 2378 CD1 LEU A 328 44.097 51.858 0.515 1.00 26.94 C ANISOU 2378 CD1 LEU A 328 3297 3777 3162 -757 540 105 C ATOM 2379 CD2 LEU A 328 43.739 50.132 -1.262 1.00 33.79 C ANISOU 2379 CD2 LEU A 328 4182 4674 3982 -751 560 90 C ATOM 2380 N LYS A 329 49.218 50.158 -1.301 1.00 32.39 N ANISOU 2380 N LYS A 329 3936 4466 3903 -748 624 113 N ATOM 2381 CA LYS A 329 50.451 50.413 -2.036 1.00 30.35 C ANISOU 2381 CA LYS A 329 3670 4206 3657 -745 651 127 C ATOM 2382 C LYS A 329 50.793 49.243 -2.953 1.00 31.31 C ANISOU 2382 C LYS A 329 3793 4342 3761 -741 668 118 C ATOM 2383 O LYS A 329 51.159 49.442 -4.117 1.00 35.51 O ANISOU 2383 O LYS A 329 4332 4881 4280 -736 692 130 O ATOM 2384 CB LYS A 329 51.586 50.702 -1.053 1.00 36.25 C ANISOU 2384 CB LYS A 329 4393 4935 4444 -747 648 131 C ATOM 2385 CG LYS A 329 51.606 52.143 -0.556 1.00 45.08 C ANISOU 2385 CG LYS A 329 5509 6040 5581 -750 642 147 C ATOM 2386 CD LYS A 329 52.769 52.406 0.396 1.00 55.70 C ANISOU 2386 CD LYS A 329 6830 7367 6966 -751 638 151 C ATOM 2387 CE LYS A 329 52.872 53.894 0.738 1.00 61.94 C ANISOU 2387 CE LYS A 329 7617 8143 7774 -754 636 169 C ATOM 2388 NZ LYS A 329 53.517 54.147 2.060 1.00 62.72 N ANISOU 2388 NZ LYS A 329 7697 8225 7909 -755 620 168 N ATOM 2389 N VAL A 330 50.676 48.016 -2.446 1.00 21.66 N ANISOU 2389 N VAL A 330 2566 3125 2538 -741 655 97 N ATOM 2390 CA VAL A 330 50.895 46.848 -3.290 1.00 28.14 C ANISOU 2390 CA VAL A 330 3391 3960 3342 -737 669 87 C ATOM 2391 C VAL A 330 49.853 46.788 -4.399 1.00 32.80 C ANISOU 2391 C VAL A 330 4004 4566 3892 -733 675 88 C ATOM 2392 O VAL A 330 50.168 46.461 -5.550 1.00 36.00 O ANISOU 2392 O VAL A 330 4416 4982 4279 -727 697 91 O ATOM 2393 CB VAL A 330 50.895 45.571 -2.431 1.00 27.88 C ANISOU 2393 CB VAL A 330 3348 3929 3318 -739 652 65 C ATOM 2394 CG1 VAL A 330 50.940 44.323 -3.315 1.00 26.25 C ANISOU 2394 CG1 VAL A 330 3148 3739 3089 -734 664 52 C ATOM 2395 CG2 VAL A 330 52.081 45.601 -1.467 1.00 25.52 C ANISOU 2395 CG2 VAL A 330 3025 3614 3057 -740 649 65 C ATOM 2396 N TYR A 331 48.601 47.109 -4.071 1.00 31.58 N ANISOU 2396 N TYR A 331 3863 4413 3722 -736 656 84 N ATOM 2397 CA TYR A 331 47.526 47.055 -5.057 1.00 33.91 C ANISOU 2397 CA TYR A 331 4181 4724 3980 -732 659 84 C ATOM 2398 C TYR A 331 47.759 48.055 -6.190 1.00 42.84 C ANISOU 2398 C TYR A 331 5323 5856 5099 -726 682 106 C ATOM 2399 O TYR A 331 47.592 47.724 -7.372 1.00 39.55 O ANISOU 2399 O TYR A 331 4920 5452 4656 -719 698 108 O ATOM 2400 CB TYR A 331 46.186 47.315 -4.368 1.00 36.46 C ANISOU 2400 CB TYR A 331 4514 5046 4293 -736 632 78 C ATOM 2401 CG TYR A 331 44.994 47.146 -5.276 1.00 40.47 C ANISOU 2401 CG TYR A 331 5045 5569 4762 -732 631 76 C ATOM 2402 CD1 TYR A 331 44.418 48.242 -5.907 1.00 43.65 C ANISOU 2402 CD1 TYR A 331 5465 5973 5149 -729 636 93 C ATOM 2403 CD2 TYR A 331 44.447 45.891 -5.507 1.00 43.05 C ANISOU 2403 CD2 TYR A 331 5378 5910 5068 -730 624 58 C ATOM 2404 CE1 TYR A 331 43.329 48.094 -6.742 1.00 44.81 C ANISOU 2404 CE1 TYR A 331 5633 6133 5260 -724 634 91 C ATOM 2405 CE2 TYR A 331 43.362 45.732 -6.342 1.00 44.63 C ANISOU 2405 CE2 TYR A 331 5599 6123 5233 -726 622 56 C ATOM 2406 CZ TYR A 331 42.807 46.836 -6.956 1.00 47.97 C ANISOU 2406 CZ TYR A 331 6039 6547 5641 -722 627 72 C ATOM 2407 OH TYR A 331 41.723 46.683 -7.788 1.00 54.26 O ANISOU 2407 OH TYR A 331 6857 7356 6403 -716 624 70 O ATOM 2408 N GLU A 332 48.108 49.298 -5.838 1.00 39.51 N ANISOU 2408 N GLU A 332 4894 5420 4697 -729 684 123 N ATOM 2409 CA GLU A 332 48.405 50.321 -6.836 1.00 48.39 C ANISOU 2409 CA GLU A 332 6027 6544 5815 -724 706 145 C ATOM 2410 C GLU A 332 49.613 49.943 -7.686 1.00 50.55 C ANISOU 2410 C GLU A 332 6293 6821 6093 -718 734 151 C ATOM 2411 O GLU A 332 49.650 50.233 -8.887 1.00 46.15 O ANISOU 2411 O GLU A 332 5748 6271 5514 -710 755 163 O ATOM 2412 CB GLU A 332 48.633 51.658 -6.135 1.00 59.97 C ANISOU 2412 CB GLU A 332 7485 7993 7307 -729 701 160 C ATOM 2413 CG GLU A 332 47.394 52.204 -5.440 1.00 70.05 C ANISOU 2413 CG GLU A 332 8772 9266 8577 -733 676 158 C ATOM 2414 CD GLU A 332 47.730 53.240 -4.378 1.00 80.27 C ANISOU 2414 CD GLU A 332 10053 10543 9903 -739 665 167 C ATOM 2415 OE1 GLU A 332 48.868 53.759 -4.388 1.00 83.63 O ANISOU 2415 OE1 GLU A 332 10463 10958 10353 -739 680 180 O ATOM 2416 OE2 GLU A 332 46.862 53.520 -3.521 1.00 82.94 O ANISOU 2416 OE2 GLU A 332 10394 10876 10242 -743 641 161 O ATOM 2417 N LYS A 333 50.607 49.285 -7.079 1.00 50.78 N ANISOU 2417 N LYS A 333 6302 6845 6147 -721 735 143 N ATOM 2418 CA LYS A 333 51.798 48.865 -7.813 1.00 45.71 C ANISOU 2418 CA LYS A 333 5652 6206 5511 -716 760 148 C ATOM 2419 C LYS A 333 51.444 47.914 -8.949 1.00 47.09 C ANISOU 2419 C LYS A 333 5841 6398 5651 -708 772 140 C ATOM 2420 O LYS A 333 52.086 47.935 -10.005 1.00 50.27 O ANISOU 2420 O LYS A 333 6248 6808 6046 -700 797 150 O ATOM 2421 CB LYS A 333 52.789 48.207 -6.851 1.00 47.02 C ANISOU 2421 CB LYS A 333 5794 6363 5710 -720 754 138 C ATOM 2422 CG LYS A 333 53.827 47.307 -7.510 1.00 50.11 C ANISOU 2422 CG LYS A 333 6176 6760 6102 -715 775 135 C ATOM 2423 CD LYS A 333 54.764 46.695 -6.476 1.00 50.29 C ANISOU 2423 CD LYS A 333 6177 6774 6158 -719 767 125 C ATOM 2424 CE LYS A 333 55.658 45.632 -7.095 1.00 45.86 C ANISOU 2424 CE LYS A 333 5609 6220 5595 -714 785 119 C ATOM 2425 NZ LYS A 333 56.591 45.048 -6.090 1.00 42.47 N ANISOU 2425 NZ LYS A 333 5157 5781 5199 -718 776 109 N ATOM 2426 N HIS A 334 50.425 47.080 -8.760 1.00 46.32 N ANISOU 2426 N HIS A 334 5754 6311 5534 -708 754 121 N ATOM 2427 CA HIS A 334 49.938 46.207 -9.814 1.00 47.14 C ANISOU 2427 CA HIS A 334 5875 6432 5604 -700 762 112 C ATOM 2428 C HIS A 334 48.849 46.874 -10.644 1.00 49.34 C ANISOU 2428 C HIS A 334 6178 6719 5850 -695 763 121 C ATOM 2429 O HIS A 334 48.138 46.188 -11.388 1.00 43.95 O ANISOU 2429 O HIS A 334 5512 6051 5137 -688 763 112 O ATOM 2430 CB HIS A 334 49.440 44.890 -9.209 1.00 45.00 C ANISOU 2430 CB HIS A 334 5602 6169 5328 -704 743 87 C ATOM 2431 CG HIS A 334 50.523 44.086 -8.557 1.00 45.76 C ANISOU 2431 CG HIS A 334 5675 6258 5451 -707 744 77 C ATOM 2432 ND1 HIS A 334 51.039 42.939 -9.120 1.00 46.78 N ANISOU 2432 ND1 HIS A 334 5803 6398 5574 -701 756 66 N ATOM 2433 CD2 HIS A 334 51.222 44.291 -7.415 1.00 45.70 C ANISOU 2433 CD2 HIS A 334 5648 6236 5480 -714 735 77 C ATOM 2434 CE1 HIS A 334 51.993 42.459 -8.341 1.00 47.55 C ANISOU 2434 CE1 HIS A 334 5880 6488 5701 -705 754 60 C ATOM 2435 NE2 HIS A 334 52.123 43.261 -7.299 1.00 43.17 N ANISOU 2435 NE2 HIS A 334 5314 5918 5173 -713 741 66 N ATOM 2436 N SER A 335 48.738 48.200 -10.552 1.00 61.41 N ANISOU 2436 N SER A 335 7709 8238 7386 -697 764 139 N ATOM 2437 CA SER A 335 47.743 48.995 -11.269 1.00 72.07 C ANISOU 2437 CA SER A 335 9081 9593 8709 -691 764 150 C ATOM 2438 C SER A 335 46.332 48.469 -11.061 1.00 77.21 C ANISOU 2438 C SER A 335 9747 10252 9335 -692 740 134 C ATOM 2439 O SER A 335 45.705 47.996 -12.007 1.00 80.46 O ANISOU 2439 O SER A 335 10177 10678 9715 -684 744 130 O ATOM 2440 CB SER A 335 48.068 49.039 -12.765 1.00 75.61 C ANISOU 2440 CB SER A 335 9542 10052 9134 -678 792 162 C ATOM 2441 OG SER A 335 49.190 49.868 -13.018 1.00 78.68 O ANISOU 2441 OG SER A 335 9920 10432 9544 -677 813 182 O TER 2442 SER A 335 ATOM 2443 N ASP B 9 15.503 7.480 22.813 1.00 50.35 N ANISOU 2443 N ASP B 9 6019 6119 6992 61 -47 -224 N ATOM 2444 CA ASP B 9 15.313 8.046 24.143 1.00 44.09 C ANISOU 2444 CA ASP B 9 5227 5335 6191 68 -31 -199 C ATOM 2445 C ASP B 9 16.424 9.022 24.525 1.00 36.72 C ANISOU 2445 C ASP B 9 4306 4427 5220 75 -24 -205 C ATOM 2446 O ASP B 9 17.598 8.793 24.248 1.00 35.46 O ANISOU 2446 O ASP B 9 4150 4270 5052 76 -35 -220 O ATOM 2447 CB ASP B 9 15.221 6.937 25.188 1.00 47.19 C ANISOU 2447 CB ASP B 9 5606 5708 6618 72 -34 -174 C ATOM 2448 CG ASP B 9 13.791 6.622 25.574 1.00 54.49 C ANISOU 2448 CG ASP B 9 6519 6617 7568 69 -27 -151 C ATOM 2449 OD1 ASP B 9 12.867 7.225 24.985 1.00 58.87 O ANISOU 2449 OD1 ASP B 9 7077 7177 8115 64 -20 -155 O ATOM 2450 OD2 ASP B 9 13.595 5.774 26.468 1.00 56.05 O ANISOU 2450 OD2 ASP B 9 6705 6798 7794 71 -29 -126 O ATOM 2451 N VAL B 10 16.022 10.103 25.194 1.00 29.35 N ANISOU 2451 N VAL B 10 3379 3510 4264 78 -5 -191 N ATOM 2452 CA VAL B 10 16.964 11.116 25.640 1.00 26.62 C ANISOU 2452 CA VAL B 10 3045 3188 3883 84 3 -196 C ATOM 2453 C VAL B 10 17.997 10.522 26.600 1.00 25.63 C ANISOU 2453 C VAL B 10 2914 3058 3765 93 -2 -188 C ATOM 2454 O VAL B 10 17.719 9.581 27.353 1.00 20.55 O ANISOU 2454 O VAL B 10 2259 2399 3152 96 -5 -168 O ATOM 2455 CB VAL B 10 16.203 12.281 26.294 1.00 21.25 C ANISOU 2455 CB VAL B 10 2371 2523 3181 86 24 -180 C ATOM 2456 CG1 VAL B 10 15.580 11.836 27.640 1.00 16.09 C ANISOU 2456 CG1 VAL B 10 1705 1861 2549 92 33 -149 C ATOM 2457 CG2 VAL B 10 17.116 13.503 26.430 1.00 18.56 C ANISOU 2457 CG2 VAL B 10 2045 2208 2799 89 32 -190 C ATOM 2458 N ASN B 11 19.221 11.034 26.523 1.00 17.46 N ANISOU 2458 N ASN B 11 1890 2041 2704 96 -4 -203 N ATOM 2459 CA ASN B 11 20.307 10.563 27.370 1.00 12.69 C ANISOU 2459 CA ASN B 11 1282 1436 2103 104 -9 -197 C ATOM 2460 C ASN B 11 21.193 11.731 27.786 1.00 22.41 C ANISOU 2460 C ASN B 11 2526 2693 3296 109 1 -203 C ATOM 2461 O ASN B 11 21.438 12.652 26.999 1.00 26.79 O ANISOU 2461 O ASN B 11 3093 3263 3823 104 3 -221 O ATOM 2462 CB ASN B 11 21.127 9.481 26.668 1.00 17.00 C ANISOU 2462 CB ASN B 11 1825 1968 2666 102 -30 -214 C ATOM 2463 CG ASN B 11 21.679 8.461 27.644 1.00 28.69 C ANISOU 2463 CG ASN B 11 3295 3436 4171 111 -37 -198 C ATOM 2464 OD1 ASN B 11 21.489 8.586 28.853 1.00 35.00 O ANISOU 2464 OD1 ASN B 11 4089 4238 4972 118 -26 -175 O ATOM 2465 ND2 ASN B 11 22.349 7.438 27.125 1.00 30.70 N ANISOU 2465 ND2 ASN B 11 3546 3677 4442 110 -54 -210 N ATOM 2466 N THR B 12 21.622 11.717 29.044 1.00 17.29 N ANISOU 2466 N THR B 12 1873 2049 2647 119 7 -187 N ATOM 2467 CA THR B 12 22.526 12.712 29.593 1.00 16.95 C ANISOU 2467 CA THR B 12 1840 2030 2571 124 16 -192 C ATOM 2468 C THR B 12 23.908 12.108 29.821 1.00 18.09 C ANISOU 2468 C THR B 12 1982 2174 2716 130 4 -199 C ATOM 2469 O THR B 12 24.087 10.887 29.834 1.00 13.95 O ANISOU 2469 O THR B 12 1448 1631 2222 132 -10 -195 O ATOM 2470 CB THR B 12 21.971 13.268 30.908 1.00 17.50 C ANISOU 2470 CB THR B 12 1905 2109 2634 131 35 -168 C ATOM 2471 OG1 THR B 12 21.964 12.231 31.906 1.00 15.61 O ANISOU 2471 OG1 THR B 12 1651 1856 2424 138 32 -145 O ATOM 2472 CG2 THR B 12 20.543 13.757 30.695 1.00 14.88 C ANISOU 2472 CG2 THR B 12 1574 1776 2303 125 48 -159 C ATOM 2473 N LEU B 13 24.901 12.989 29.971 1.00 14.04 N ANISOU 2473 N LEU B 13 1480 1682 2171 132 8 -211 N ATOM 2474 CA LEU B 13 26.248 12.531 30.303 1.00 13.98 C ANISOU 2474 CA LEU B 13 1471 1677 2163 139 -2 -217 C ATOM 2475 C LEU B 13 26.237 11.730 31.599 1.00 15.23 C ANISOU 2475 C LEU B 13 1615 1827 2344 150 -2 -193 C ATOM 2476 O LEU B 13 26.836 10.650 31.682 1.00 16.39 O ANISOU 2476 O LEU B 13 1755 1962 2512 154 -16 -191 O ATOM 2477 CB LEU B 13 27.194 13.724 30.397 1.00 22.10 C ANISOU 2477 CB LEU B 13 2513 2731 3152 139 5 -230 C ATOM 2478 CG LEU B 13 28.704 13.520 30.473 1.00 32.38 C ANISOU 2478 CG LEU B 13 3818 4041 4444 143 -6 -243 C ATOM 2479 CD1 LEU B 13 29.169 12.226 29.843 1.00 30.32 C ANISOU 2479 CD1 LEU B 13 3551 3762 4209 143 -26 -250 C ATOM 2480 CD2 LEU B 13 29.315 14.679 29.729 1.00 48.97 C ANISOU 2480 CD2 LEU B 13 5936 6161 6510 135 -4 -262 C ATOM 2481 N THR B 14 25.523 12.234 32.607 1.00 16.25 N ANISOU 2481 N THR B 14 1740 1965 2471 154 15 -172 N ATOM 2482 CA THR B 14 25.429 11.555 33.894 1.00 20.94 C ANISOU 2482 CA THR B 14 2319 2552 3085 164 17 -144 C ATOM 2483 C THR B 14 24.916 10.132 33.725 1.00 19.50 C ANISOU 2483 C THR B 14 2124 2341 2943 162 3 -130 C ATOM 2484 O THR B 14 25.500 9.179 34.250 1.00 28.07 O ANISOU 2484 O THR B 14 3202 3417 4048 169 -7 -119 O ATOM 2485 CB THR B 14 24.490 12.326 34.824 1.00 27.90 C ANISOU 2485 CB THR B 14 3197 3444 3958 166 39 -123 C ATOM 2486 OG1 THR B 14 24.902 13.695 34.912 1.00 29.78 O ANISOU 2486 OG1 THR B 14 3448 3709 4157 165 53 -138 O ATOM 2487 CG2 THR B 14 24.485 11.703 36.211 1.00 30.30 C ANISOU 2487 CG2 THR B 14 3486 3745 4281 175 42 -91 C ATOM 2488 N ARG B 15 23.802 9.982 33.014 1.00 19.09 N ANISOU 2488 N ARG B 15 2073 2276 2906 154 4 -130 N ATOM 2489 CA ARG B 15 23.201 8.673 32.810 1.00 15.62 C ANISOU 2489 CA ARG B 15 1622 1809 2506 150 -8 -118 C ATOM 2490 C ARG B 15 24.067 7.794 31.920 1.00 16.56 C ANISOU 2490 C ARG B 15 1742 1915 2635 148 -29 -139 C ATOM 2491 O ARG B 15 24.224 6.593 32.190 1.00 15.87 O ANISOU 2491 O ARG B 15 1644 1808 2576 151 -41 -127 O ATOM 2492 CB ARG B 15 21.801 8.864 32.232 1.00 23.20 C ANISOU 2492 CB ARG B 15 2581 2759 3474 141 -2 -115 C ATOM 2493 CG ARG B 15 21.103 7.599 31.842 1.00 34.64 C ANISOU 2493 CG ARG B 15 4019 4179 4962 135 -14 -106 C ATOM 2494 CD ARG B 15 19.766 7.905 31.158 1.00 40.11 C ANISOU 2494 CD ARG B 15 4713 4867 5661 126 -8 -107 C ATOM 2495 NE ARG B 15 18.642 8.156 32.046 1.00 36.28 N ANISOU 2495 NE ARG B 15 4220 4381 5182 127 8 -77 N ATOM 2496 CZ ARG B 15 17.492 8.696 31.653 1.00 32.58 C ANISOU 2496 CZ ARG B 15 3754 3914 4711 120 18 -76 C ATOM 2497 NH1 ARG B 15 17.317 9.075 30.384 1.00 30.08 N ANISOU 2497 NH1 ARG B 15 3446 3600 4384 112 14 -103 N ATOM 2498 NH2 ARG B 15 16.506 8.844 32.525 1.00 23.54 N ANISOU 2498 NH2 ARG B 15 2601 2768 3573 121 32 -46 N ATOM 2499 N PHE B 16 24.659 8.383 30.869 1.00 11.58 N ANISOU 2499 N PHE B 16 1124 1296 1981 143 -33 -169 N ATOM 2500 CA PHE B 16 25.486 7.633 29.921 1.00 19.34 C ANISOU 2500 CA PHE B 16 2108 2268 2971 140 -51 -190 C ATOM 2501 C PHE B 16 26.678 6.966 30.605 1.00 20.30 C ANISOU 2501 C PHE B 16 2226 2390 3098 149 -60 -186 C ATOM 2502 O PHE B 16 26.930 5.767 30.415 1.00 13.74 O ANISOU 2502 O PHE B 16 1389 1540 2294 150 -75 -185 O ATOM 2503 CB PHE B 16 25.978 8.570 28.811 1.00 19.74 C ANISOU 2503 CB PHE B 16 2174 2336 2990 133 -51 -219 C ATOM 2504 CG PHE B 16 26.946 7.934 27.847 1.00 16.78 C ANISOU 2504 CG PHE B 16 1802 1957 2618 130 -69 -242 C ATOM 2505 CD1 PHE B 16 26.487 7.283 26.712 1.00 25.56 C ANISOU 2505 CD1 PHE B 16 2911 3053 3748 120 -81 -254 C ATOM 2506 CD2 PHE B 16 28.314 7.996 28.072 1.00 20.92 C ANISOU 2506 CD2 PHE B 16 2330 2492 3126 136 -75 -251 C ATOM 2507 CE1 PHE B 16 27.380 6.701 25.815 1.00 22.35 C ANISOU 2507 CE1 PHE B 16 2505 2643 3344 117 -97 -275 C ATOM 2508 CE2 PHE B 16 29.211 7.415 27.185 1.00 24.96 C ANISOU 2508 CE2 PHE B 16 2844 3000 3640 132 -91 -271 C ATOM 2509 CZ PHE B 16 28.745 6.770 26.055 1.00 23.64 C ANISOU 2509 CZ PHE B 16 2673 2817 3491 123 -102 -283 C ATOM 2510 N VAL B 17 27.453 7.728 31.380 1.00 14.94 N ANISOU 2510 N VAL B 17 1552 1733 2393 157 -52 -184 N ATOM 2511 CA VAL B 17 28.651 7.127 31.963 1.00 18.98 C ANISOU 2511 CA VAL B 17 2060 2245 2907 167 -62 -181 C ATOM 2512 C VAL B 17 28.260 6.125 33.039 1.00 23.93 C ANISOU 2512 C VAL B 17 2672 2855 3565 173 -63 -149 C ATOM 2513 O VAL B 17 28.884 5.068 33.183 1.00 21.65 O ANISOU 2513 O VAL B 17 2378 2554 3295 178 -77 -145 O ATOM 2514 CB VAL B 17 29.608 8.206 32.502 1.00 26.70 C ANISOU 2514 CB VAL B 17 3045 3251 3849 173 -53 -189 C ATOM 2515 CG1 VAL B 17 30.078 9.094 31.360 1.00 20.76 C ANISOU 2515 CG1 VAL B 17 2308 2512 3067 164 -53 -219 C ATOM 2516 CG2 VAL B 17 28.968 9.015 33.619 1.00 21.02 C ANISOU 2516 CG2 VAL B 17 2323 2545 3119 178 -34 -168 C ATOM 2517 N MET B 18 27.209 6.441 33.798 1.00 31.82 N ANISOU 2517 N MET B 18 3665 3854 4570 174 -50 -125 N ATOM 2518 CA MET B 18 26.659 5.507 34.772 1.00 36.00 C ANISOU 2518 CA MET B 18 4181 4368 5130 178 -50 -91 C ATOM 2519 C MET B 18 26.258 4.197 34.107 1.00 33.28 C ANISOU 2519 C MET B 18 3830 3993 4821 172 -65 -90 C ATOM 2520 O MET B 18 26.530 3.113 34.638 1.00 35.27 O ANISOU 2520 O MET B 18 4074 4230 5097 176 -75 -72 O ATOM 2521 CB MET B 18 25.457 6.155 35.466 1.00 31.97 C ANISOU 2521 CB MET B 18 3666 3862 4618 177 -32 -67 C ATOM 2522 CG MET B 18 24.965 5.422 36.668 1.00 40.14 C ANISOU 2522 CG MET B 18 4688 4886 5677 182 -29 -27 C ATOM 2523 SD MET B 18 26.004 5.671 38.100 1.00 40.55 S ANISOU 2523 SD MET B 18 4736 4959 5711 197 -24 -8 S ATOM 2524 CE MET B 18 25.211 4.571 39.257 1.00 39.47 C ANISOU 2524 CE MET B 18 4585 4804 5609 199 -23 43 C ATOM 2525 N GLU B 19 25.624 4.276 32.934 1.00 25.18 N ANISOU 2525 N GLU B 19 2810 2959 3799 161 -68 -109 N ATOM 2526 CA GLU B 19 25.198 3.056 32.260 1.00 28.81 C ANISOU 2526 CA GLU B 19 3263 3392 4294 154 -82 -111 C ATOM 2527 C GLU B 19 26.388 2.305 31.673 1.00 28.50 C ANISOU 2527 C GLU B 19 3226 3346 4258 155 -99 -131 C ATOM 2528 O GLU B 19 26.414 1.073 31.704 1.00 26.78 O ANISOU 2528 O GLU B 19 2998 3105 4070 155 -111 -122 O ATOM 2529 CB GLU B 19 24.169 3.371 31.164 1.00 29.39 C ANISOU 2529 CB GLU B 19 3339 3459 4369 142 -80 -126 C ATOM 2530 CG GLU B 19 22.804 3.822 31.683 1.00 40.10 C ANISOU 2530 CG GLU B 19 4691 4815 5732 139 -65 -103 C ATOM 2531 CD GLU B 19 21.877 4.376 30.590 1.00 47.48 C ANISOU 2531 CD GLU B 19 5630 5749 6660 129 -61 -120 C ATOM 2532 OE1 GLU B 19 22.363 4.734 29.493 1.00 45.81 O ANISOU 2532 OE1 GLU B 19 5427 5546 6431 124 -67 -151 O ATOM 2533 OE2 GLU B 19 20.653 4.450 30.832 1.00 45.29 O ANISOU 2533 OE2 GLU B 19 5347 5465 6395 125 -52 -102 O ATOM 2534 N GLU B 20 27.390 3.021 31.141 1.00 24.10 N ANISOU 2534 N GLU B 20 2678 2808 3669 157 -101 -157 N ATOM 2535 CA GLU B 20 28.601 2.344 30.680 1.00 21.47 C ANISOU 2535 CA GLU B 20 2348 2472 3339 159 -116 -175 C ATOM 2536 C GLU B 20 29.320 1.670 31.841 1.00 25.64 C ANISOU 2536 C GLU B 20 2869 2997 3876 170 -120 -153 C ATOM 2537 O GLU B 20 29.878 0.576 31.688 1.00 26.51 O ANISOU 2537 O GLU B 20 2974 3091 4006 172 -134 -154 O ATOM 2538 CB GLU B 20 29.542 3.328 29.981 1.00 24.68 C ANISOU 2538 CB GLU B 20 2768 2902 3708 158 -115 -204 C ATOM 2539 CG GLU B 20 29.097 3.783 28.596 1.00 31.22 C ANISOU 2539 CG GLU B 20 3604 3733 4527 146 -117 -229 C ATOM 2540 CD GLU B 20 28.983 2.645 27.604 1.00 39.89 C ANISOU 2540 CD GLU B 20 4696 4808 5652 139 -133 -241 C ATOM 2541 OE1 GLU B 20 29.873 1.775 27.600 1.00 39.69 O ANISOU 2541 OE1 GLU B 20 4667 4775 5638 143 -146 -245 O ATOM 2542 OE2 GLU B 20 28.004 2.624 26.825 1.00 45.49 O ANISOU 2542 OE2 GLU B 20 5403 5508 6371 129 -133 -248 O ATOM 2543 N GLY B 21 29.297 2.296 33.018 1.00 19.49 N ANISOU 2543 N GLY B 21 2089 2234 3084 179 -107 -131 N ATOM 2544 CA GLY B 21 29.955 1.700 34.164 1.00 22.28 C ANISOU 2544 CA GLY B 21 2435 2587 3446 190 -110 -108 C ATOM 2545 C GLY B 21 29.257 0.439 34.641 1.00 31.16 C ANISOU 2545 C GLY B 21 3546 3683 4609 189 -115 -80 C ATOM 2546 O GLY B 21 29.912 -0.535 35.022 1.00 29.36 O ANISOU 2546 O GLY B 21 3313 3445 4397 194 -126 -70 O ATOM 2547 N ARG B 22 27.922 0.446 34.642 1.00 29.15 N ANISOU 2547 N ARG B 22 3287 3417 4371 181 -108 -66 N ATOM 2548 CA ARG B 22 27.176 -0.742 35.037 1.00 33.04 C ANISOU 2548 CA ARG B 22 3769 3884 4902 179 -113 -39 C ATOM 2549 C ARG B 22 27.395 -1.880 34.051 1.00 36.30 C ANISOU 2549 C ARG B 22 4180 4274 5341 172 -130 -57 C ATOM 2550 O ARG B 22 27.489 -3.044 34.454 1.00 40.36 O ANISOU 2550 O ARG B 22 4684 4768 5882 174 -139 -39 O ATOM 2551 CB ARG B 22 25.691 -0.411 35.172 1.00 36.72 C ANISOU 2551 CB ARG B 22 4230 4343 5377 171 -101 -22 C ATOM 2552 CG ARG B 22 25.369 0.525 36.343 1.00 44.21 C ANISOU 2552 CG ARG B 22 5179 5313 6307 178 -83 4 C ATOM 2553 CD ARG B 22 23.865 0.645 36.548 1.00 54.88 C ANISOU 2553 CD ARG B 22 6524 6655 7673 171 -72 25 C ATOM 2554 NE ARG B 22 23.295 -0.553 37.157 1.00 65.11 N ANISOU 2554 NE ARG B 22 7808 7928 9005 169 -77 58 N ATOM 2555 CZ ARG B 22 21.993 -0.750 37.334 1.00 72.87 C ANISOU 2555 CZ ARG B 22 8784 8897 10007 162 -70 80 C ATOM 2556 NH1 ARG B 22 21.126 0.174 36.941 1.00 76.24 N ANISOU 2556 NH1 ARG B 22 9213 9332 10421 156 -58 73 N ATOM 2557 NH2 ARG B 22 21.555 -1.873 37.891 1.00 71.86 N ANISOU 2557 NH2 ARG B 22 8644 8748 9911 160 -74 110 N ATOM 2558 N LYS B 23 27.481 -1.563 32.755 1.00 35.50 N ANISOU 2558 N LYS B 23 4086 4174 5230 165 -136 -91 N ATOM 2559 CA LYS B 23 27.828 -2.581 31.769 1.00 32.25 C ANISOU 2559 CA LYS B 23 3672 3744 4838 159 -152 -111 C ATOM 2560 C LYS B 23 29.170 -3.221 32.089 1.00 40.90 C ANISOU 2560 C LYS B 23 4767 4840 5933 168 -163 -112 C ATOM 2561 O LYS B 23 29.316 -4.448 32.006 1.00 46.80 O ANISOU 2561 O LYS B 23 5507 5566 6710 167 -175 -108 O ATOM 2562 CB LYS B 23 27.852 -1.982 30.363 1.00 35.74 C ANISOU 2562 CB LYS B 23 4122 4193 5263 150 -155 -148 C ATOM 2563 CG LYS B 23 26.484 -1.710 29.745 1.00 50.36 C ANISOU 2563 CG LYS B 23 5972 6038 7125 139 -150 -150 C ATOM 2564 CD LYS B 23 26.642 -1.200 28.304 1.00 62.15 C ANISOU 2564 CD LYS B 23 7474 7541 8600 131 -155 -187 C ATOM 2565 CE LYS B 23 25.328 -0.713 27.691 1.00 65.50 C ANISOU 2565 CE LYS B 23 7898 7962 9027 121 -148 -190 C ATOM 2566 NZ LYS B 23 24.846 0.583 28.250 1.00 68.15 N ANISOU 2566 NZ LYS B 23 8239 8317 9335 123 -129 -180 N ATOM 2567 N ALA B 24 30.161 -2.407 32.460 1.00 31.26 N ANISOU 2567 N ALA B 24 3554 3644 4680 177 -158 -119 N ATOM 2568 CA ALA B 24 31.509 -2.883 32.736 1.00 28.14 C ANISOU 2568 CA ALA B 24 3160 3253 4279 186 -167 -122 C ATOM 2569 C ALA B 24 31.686 -3.399 34.152 1.00 30.90 C ANISOU 2569 C ALA B 24 3500 3599 4639 197 -165 -87 C ATOM 2570 O ALA B 24 32.794 -3.811 34.500 1.00 34.86 O ANISOU 2570 O ALA B 24 4003 4105 5138 206 -172 -86 O ATOM 2571 CB ALA B 24 32.526 -1.776 32.476 1.00 21.39 C ANISOU 2571 CB ALA B 24 2316 2426 3384 191 -164 -146 C ATOM 2572 N ARG B 25 30.639 -3.380 34.977 1.00 33.70 N ANISOU 2572 N ARG B 25 3849 3949 5008 196 -155 -56 N ATOM 2573 CA ARG B 25 30.731 -3.836 36.366 1.00 30.64 C ANISOU 2573 CA ARG B 25 3453 3560 4630 205 -151 -19 C ATOM 2574 C ARG B 25 31.750 -3.022 37.158 1.00 29.79 C ANISOU 2574 C ARG B 25 3350 3481 4489 217 -146 -16 C ATOM 2575 O ARG B 25 32.463 -3.551 38.012 1.00 26.50 O ANISOU 2575 O ARG B 25 2928 3066 4075 227 -149 2 O ATOM 2576 CB ARG B 25 31.059 -5.329 36.445 1.00 43.83 C ANISOU 2576 CB ARG B 25 5115 5205 6332 206 -165 -8 C ATOM 2577 CG ARG B 25 30.037 -6.231 35.796 1.00 54.14 C ANISOU 2577 CG ARG B 25 6414 6482 7674 194 -171 -7 C ATOM 2578 CD ARG B 25 28.749 -6.243 36.601 1.00 66.32 C ANISOU 2578 CD ARG B 25 7949 8016 9233 190 -160 28 C ATOM 2579 NE ARG B 25 27.821 -7.261 36.122 1.00 77.57 N ANISOU 2579 NE ARG B 25 9365 9411 10696 179 -167 32 N ATOM 2580 CZ ARG B 25 26.921 -7.061 35.165 1.00 85.88 C ANISOU 2580 CZ ARG B 25 10418 10456 11757 167 -167 15 C ATOM 2581 NH1 ARG B 25 26.825 -5.875 34.579 1.00 86.04 N ANISOU 2581 NH1 ARG B 25 10448 10496 11749 165 -160 -8 N ATOM 2582 NH2 ARG B 25 26.115 -8.047 34.794 1.00 91.38 N ANISOU 2582 NH2 ARG B 25 11105 11126 12491 157 -174 21 N ATOM 2583 N GLY B 26 31.826 -1.719 36.877 1.00 25.84 N ANISOU 2583 N GLY B 26 2858 3004 3956 217 -136 -35 N ATOM 2584 CA GLY B 26 32.781 -0.882 37.568 1.00 17.55 C ANISOU 2584 CA GLY B 26 1811 1983 2874 228 -131 -36 C ATOM 2585 C GLY B 26 32.320 -0.504 38.965 1.00 14.79 C ANISOU 2585 C GLY B 26 1454 1645 2520 234 -118 0 C ATOM 2586 O GLY B 26 31.171 -0.679 39.346 1.00 25.16 O ANISOU 2586 O GLY B 26 2762 2946 3851 230 -111 24 O ATOM 2587 N THR B 27 33.261 -0.011 39.762 1.00 24.21 N ANISOU 2587 N THR B 27 2647 2862 3690 245 -115 5 N ATOM 2588 CA THR B 27 32.957 0.385 41.129 1.00 27.24 C ANISOU 2588 CA THR B 27 3023 3260 4066 252 -102 39 C ATOM 2589 C THR B 27 32.355 1.783 41.226 1.00 26.52 C ANISOU 2589 C THR B 27 2936 3190 3951 249 -86 34 C ATOM 2590 O THR B 27 31.954 2.188 42.324 1.00 25.12 O ANISOU 2590 O THR B 27 2760 3028 3755 249 -71 63 O ATOM 2591 CB THR B 27 34.226 0.327 41.981 1.00 33.24 C ANISOU 2591 CB THR B 27 3781 4039 4811 265 -106 48 C ATOM 2592 OG1 THR B 27 35.160 1.314 41.512 1.00 36.93 O ANISOU 2592 OG1 THR B 27 4255 4530 5246 267 -106 13 O ATOM 2593 CG2 THR B 27 34.858 -1.060 41.918 1.00 29.59 C ANISOU 2593 CG2 THR B 27 3315 3557 4372 268 -122 54 C ATOM 2594 N GLY B 28 32.304 2.525 40.118 1.00 18.59 N ANISOU 2594 N GLY B 28 1942 2190 2932 242 -84 -2 N ATOM 2595 CA GLY B 28 31.776 3.881 40.088 1.00 19.86 C ANISOU 2595 CA GLY B 28 2108 2370 3067 238 -68 -11 C ATOM 2596 C GLY B 28 32.784 5.007 40.232 1.00 20.83 C ANISOU 2596 C GLY B 28 2244 2526 3142 239 -62 -32 C ATOM 2597 O GLY B 28 32.395 6.177 40.115 1.00 21.65 O ANISOU 2597 O GLY B 28 2359 2649 3218 233 -47 -43 O ATOM 2598 N GLU B 29 34.066 4.704 40.454 1.00 12.74 N ANISOU 2598 N GLU B 29 1219 1511 2109 247 -72 -39 N ATOM 2599 CA GLU B 29 35.031 5.766 40.733 1.00 18.49 C ANISOU 2599 CA GLU B 29 1961 2273 2792 248 -65 -56 C ATOM 2600 C GLU B 29 35.269 6.661 39.513 1.00 23.08 C ANISOU 2600 C GLU B 29 2549 2861 3360 243 -65 -97 C ATOM 2601 O GLU B 29 35.382 7.888 39.646 1.00 16.31 O ANISOU 2601 O GLU B 29 1704 2029 2465 239 -52 -109 O ATOM 2602 CB GLU B 29 36.338 5.152 41.231 1.00 16.70 C ANISOU 2602 CB GLU B 29 1730 2053 2562 257 -77 -52 C ATOM 2603 CG GLU B 29 37.374 6.140 41.690 1.00 28.26 C ANISOU 2603 CG GLU B 29 3206 3552 3979 258 -71 -65 C ATOM 2604 CD GLU B 29 38.471 5.472 42.493 1.00 37.59 C ANISOU 2604 CD GLU B 29 4384 4742 5158 268 -80 -51 C ATOM 2605 OE1 GLU B 29 38.331 4.273 42.816 1.00 45.99 O ANISOU 2605 OE1 GLU B 29 5436 5785 6253 273 -89 -27 O ATOM 2606 OE2 GLU B 29 39.463 6.147 42.817 1.00 42.46 O ANISOU 2606 OE2 GLU B 29 5008 5386 5739 269 -77 -63 O ATOM 2607 N LEU B 30 35.372 6.071 38.320 1.00 19.70 N ANISOU 2607 N LEU B 30 2119 2413 2955 242 -79 -119 N ATOM 2608 CA LEU B 30 35.573 6.879 37.122 1.00 20.51 C ANISOU 2608 CA LEU B 30 2236 2522 3034 232 -78 -154 C ATOM 2609 C LEU B 30 34.357 7.756 36.852 1.00 21.68 C ANISOU 2609 C LEU B 30 2388 2672 3175 224 -63 -155 C ATOM 2610 O LEU B 30 34.495 8.902 36.406 1.00 14.80 O ANISOU 2610 O LEU B 30 1528 1819 2274 218 -54 -177 O ATOM 2611 CB LEU B 30 35.858 5.974 35.919 1.00 17.76 C ANISOU 2611 CB LEU B 30 1892 2153 2702 226 -94 -170 C ATOM 2612 CG LEU B 30 36.013 6.689 34.574 1.00 20.37 C ANISOU 2612 CG LEU B 30 2238 2490 3013 214 -94 -203 C ATOM 2613 CD1 LEU B 30 37.146 7.713 34.649 1.00 16.52 C ANISOU 2613 CD1 LEU B 30 1759 2030 2488 216 -90 -222 C ATOM 2614 CD2 LEU B 30 36.264 5.696 33.435 1.00 16.06 C ANISOU 2614 CD2 LEU B 30 1694 1922 2486 208 -110 -218 C ATOM 2615 N THR B 31 33.160 7.230 37.122 1.00 16.01 N ANISOU 2615 N THR B 31 1662 1935 2485 222 -59 -131 N ATOM 2616 CA THR B 31 31.939 8.017 36.994 1.00 20.36 C ANISOU 2616 CA THR B 31 2216 2488 3032 215 -44 -128 C ATOM 2617 C THR B 31 31.946 9.212 37.941 1.00 12.57 C ANISOU 2617 C THR B 31 1234 1531 2012 217 -25 -121 C ATOM 2618 O THR B 31 31.546 10.322 37.558 1.00 15.45 O ANISOU 2618 O THR B 31 1607 1907 2354 211 -13 -136 O ATOM 2619 CB THR B 31 30.730 7.124 37.272 1.00 24.89 C ANISOU 2619 CB THR B 31 2779 3037 3641 213 -44 -99 C ATOM 2620 OG1 THR B 31 30.537 6.231 36.174 1.00 22.16 O ANISOU 2620 OG1 THR B 31 2436 2668 3317 205 -58 -111 O ATOM 2621 CG2 THR B 31 29.465 7.959 37.455 1.00 22.10 C ANISOU 2621 CG2 THR B 31 2426 2688 3282 208 -26 -89 C ATOM 2622 N GLN B 32 32.398 9.009 39.183 1.00 14.19 N ANISOU 2622 N GLN B 32 1440 1747 2203 221 -23 -96 N ATOM 2623 CA GLN B 32 32.501 10.123 40.125 1.00 17.54 C ANISOU 2623 CA GLN B 32 1878 2202 2585 218 -5 -88 C ATOM 2624 C GLN B 32 33.446 11.179 39.592 1.00 17.65 C ANISOU 2624 C GLN B 32 1903 2238 2566 217 -3 -123 C ATOM 2625 O GLN B 32 33.178 12.385 39.688 1.00 15.45 O ANISOU 2625 O GLN B 32 1635 1979 2257 212 12 -131 O ATOM 2626 CB GLN B 32 33.004 9.631 41.489 1.00 15.11 C ANISOU 2626 CB GLN B 32 1568 1904 2268 224 -5 -57 C ATOM 2627 CG GLN B 32 32.045 8.785 42.267 1.00 29.60 C ANISOU 2627 CG GLN B 32 3395 3724 4128 225 -3 -18 C ATOM 2628 CD GLN B 32 32.426 8.709 43.733 1.00 50.29 C ANISOU 2628 CD GLN B 32 6017 6364 6728 230 3 12 C ATOM 2629 OE1 GLN B 32 33.161 7.809 44.143 1.00 47.99 O ANISOU 2629 OE1 GLN B 32 5717 6067 6448 237 -8 24 O ATOM 2630 NE2 GLN B 32 31.954 9.671 44.525 1.00 60.59 N ANISOU 2630 NE2 GLN B 32 7331 7691 8000 226 22 25 N ATOM 2631 N LEU B 33 34.577 10.735 39.050 1.00 12.89 N ANISOU 2631 N LEU B 33 1295 1632 1968 223 -19 -144 N ATOM 2632 CA LEU B 33 35.506 11.649 38.402 1.00 14.51 C ANISOU 2632 CA LEU B 33 1509 1856 2146 222 -20 -179 C ATOM 2633 C LEU B 33 34.822 12.400 37.270 1.00 12.92 C ANISOU 2633 C LEU B 33 1312 1652 1946 215 -14 -203 C ATOM 2634 O LEU B 33 34.854 13.633 37.221 1.00 13.98 O ANISOU 2634 O LEU B 33 1459 1806 2047 210 0 -216 O ATOM 2635 CB LEU B 33 36.725 10.864 37.900 1.00 16.95 C ANISOU 2635 CB LEU B 33 1811 2159 2469 230 -40 -196 C ATOM 2636 CG LEU B 33 37.983 11.628 37.463 1.00 10.95 C ANISOU 2636 CG LEU B 33 1063 1421 1676 228 -42 -225 C ATOM 2637 CD1 LEU B 33 39.141 10.678 37.431 1.00 15.25 C ANISOU 2637 CD1 LEU B 33 1603 1961 2231 235 -60 -227 C ATOM 2638 CD2 LEU B 33 37.821 12.266 36.105 1.00 11.93 C ANISOU 2638 CD2 LEU B 33 1204 1541 1789 213 -41 -248 C ATOM 2639 N LEU B 34 34.177 11.674 36.353 1.00 13.26 N ANISOU 2639 N LEU B 34 1355 1668 2015 209 -22 -202 N ATOM 2640 CA LEU B 34 33.609 12.351 35.195 1.00 9.60 C ANISOU 2640 CA LEU B 34 906 1202 1541 196 -18 -219 C ATOM 2641 C LEU B 34 32.459 13.271 35.599 1.00 10.82 C ANISOU 2641 C LEU B 34 1061 1364 1685 193 2 -209 C ATOM 2642 O LEU B 34 32.313 14.361 35.031 1.00 8.93 O ANISOU 2642 O LEU B 34 838 1137 1420 183 11 -224 O ATOM 2643 CB LEU B 34 33.172 11.331 34.143 1.00 15.42 C ANISOU 2643 CB LEU B 34 1640 1912 2307 190 -32 -221 C ATOM 2644 CG LEU B 34 34.343 10.625 33.453 1.00 15.49 C ANISOU 2644 CG LEU B 34 1651 1914 2318 189 -51 -238 C ATOM 2645 CD1 LEU B 34 33.840 9.486 32.593 1.00 17.49 C ANISOU 2645 CD1 LEU B 34 1901 2141 2604 184 -64 -238 C ATOM 2646 CD2 LEU B 34 35.108 11.641 32.598 1.00 13.24 C ANISOU 2646 CD2 LEU B 34 1383 1648 2001 181 -50 -265 C ATOM 2647 N ASN B 35 31.649 12.866 36.590 1.00 13.43 N ANISOU 2647 N ASN B 35 1377 1688 2036 200 9 -182 N ATOM 2648 CA ASN B 35 30.601 13.754 37.105 1.00 10.04 C ANISOU 2648 CA ASN B 35 953 1269 1592 195 30 -169 C ATOM 2649 C ASN B 35 31.198 15.044 37.638 1.00 9.89 C ANISOU 2649 C ASN B 35 949 1281 1527 193 44 -178 C ATOM 2650 O ASN B 35 30.681 16.136 37.369 1.00 16.24 O ANISOU 2650 O ASN B 35 1762 2096 2312 188 59 -188 O ATOM 2651 CB ASN B 35 29.801 13.078 38.221 1.00 16.61 C ANISOU 2651 CB ASN B 35 1780 2093 2438 196 35 -128 C ATOM 2652 CG ASN B 35 28.922 11.944 37.720 1.00 27.25 C ANISOU 2652 CG ASN B 35 3113 3409 3831 195 25 -117 C ATOM 2653 OD1 ASN B 35 28.597 11.864 36.537 1.00 30.72 O ANISOU 2653 OD1 ASN B 35 3550 3835 4287 192 18 -137 O ATOM 2654 ND2 ASN B 35 28.550 11.044 38.629 1.00 19.12 N ANISOU 2654 ND2 ASN B 35 2075 2369 2819 198 23 -82 N ATOM 2655 N SER B 36 32.256 14.925 38.454 1.00 13.80 N ANISOU 2655 N SER B 36 1447 1791 2006 198 40 -173 N ATOM 2656 CA SER B 36 32.923 16.095 39.007 1.00 15.38 C ANISOU 2656 CA SER B 36 1660 2020 2162 196 52 -182 C ATOM 2657 C SER B 36 33.490 16.965 37.904 1.00 19.54 C ANISOU 2657 C SER B 36 2194 2557 2675 193 51 -220 C ATOM 2658 O SER B 36 33.502 18.199 38.011 1.00 18.40 O ANISOU 2658 O SER B 36 2064 2431 2498 187 65 -229 O ATOM 2659 CB SER B 36 34.041 15.678 39.962 1.00 8.80 C ANISOU 2659 CB SER B 36 827 1201 1317 202 45 -171 C ATOM 2660 OG SER B 36 33.506 15.005 41.082 1.00 25.78 O ANISOU 2660 OG SER B 36 2972 3346 3475 204 47 -134 O ATOM 2661 N LEU B 37 34.025 16.335 36.866 1.00 15.65 N ANISOU 2661 N LEU B 37 1700 2047 2197 191 33 -234 N ATOM 2662 CA LEU B 37 34.554 17.096 35.748 1.00 19.92 C ANISOU 2662 CA LEU B 37 2261 2592 2716 178 29 -256 C ATOM 2663 C LEU B 37 33.435 17.859 35.033 1.00 15.72 C ANISOU 2663 C LEU B 37 1740 2054 2179 166 39 -255 C ATOM 2664 O LEU B 37 33.618 19.013 34.634 1.00 16.15 O ANISOU 2664 O LEU B 37 1812 2120 2204 155 44 -264 O ATOM 2665 CB LEU B 37 35.301 16.152 34.811 1.00 22.76 C ANISOU 2665 CB LEU B 37 2619 2937 3094 177 7 -267 C ATOM 2666 CG LEU B 37 36.166 16.795 33.734 1.00 31.39 C ANISOU 2666 CG LEU B 37 3726 4035 4164 165 -1 -289 C ATOM 2667 CD1 LEU B 37 37.131 17.793 34.354 1.00 30.99 C ANISOU 2667 CD1 LEU B 37 3686 4011 4079 163 6 -295 C ATOM 2668 CD2 LEU B 37 36.926 15.719 32.989 1.00 32.55 C ANISOU 2668 CD2 LEU B 37 3869 4170 4330 166 -21 -299 C ATOM 2669 N CYS B 38 32.260 17.240 34.890 1.00 16.66 N ANISOU 2669 N CYS B 38 1849 2155 2326 167 40 -242 N ATOM 2670 CA CYS B 38 31.150 17.905 34.201 1.00 19.25 C ANISOU 2670 CA CYS B 38 2187 2478 2649 157 49 -241 C ATOM 2671 C CYS B 38 30.646 19.114 34.970 1.00 17.41 C ANISOU 2671 C CYS B 38 1963 2263 2390 155 70 -233 C ATOM 2672 O CYS B 38 30.327 20.148 34.373 1.00 17.31 O ANISOU 2672 O CYS B 38 1967 2255 2356 144 76 -238 O ATOM 2673 CB CYS B 38 30.010 16.923 33.984 1.00 25.49 C ANISOU 2673 CB CYS B 38 2963 3246 3476 159 46 -228 C ATOM 2674 SG CYS B 38 30.405 15.789 32.693 1.00 44.17 S ANISOU 2674 SG CYS B 38 5326 5590 5867 155 22 -241 S ATOM 2675 N THR B 39 30.574 18.997 36.293 1.00 11.51 N ANISOU 2675 N THR B 39 1205 1526 1641 166 81 -219 N ATOM 2676 CA THR B 39 30.194 20.121 37.127 1.00 13.16 C ANISOU 2676 CA THR B 39 1424 1755 1822 164 102 -212 C ATOM 2677 C THR B 39 31.151 21.279 36.937 1.00 15.72 C ANISOU 2677 C THR B 39 1770 2095 2108 154 103 -226 C ATOM 2678 O THR B 39 30.724 22.433 36.802 1.00 8.74 O ANISOU 2678 O THR B 39 904 1216 1202 144 113 -223 O ATOM 2679 CB THR B 39 30.197 19.686 38.590 1.00 11.67 C ANISOU 2679 CB THR B 39 1220 1578 1636 175 110 -194 C ATOM 2680 OG1 THR B 39 29.171 18.709 38.797 1.00 14.01 O ANISOU 2680 OG1 THR B 39 1506 1853 1964 176 108 -166 O ATOM 2681 CG2 THR B 39 30.009 20.870 39.494 1.00 4.96 C ANISOU 2681 CG2 THR B 39 385 752 750 172 131 -187 C ATOM 2682 N ALA B 40 32.460 20.985 36.933 1.00 17.12 N ANISOU 2682 N ALA B 40 1947 2278 2280 157 90 -238 N ATOM 2683 CA ALA B 40 33.458 22.026 36.735 1.00 12.35 C ANISOU 2683 CA ALA B 40 1361 1686 1643 146 87 -250 C ATOM 2684 C ALA B 40 33.310 22.676 35.362 1.00 13.65 C ANISOU 2684 C ALA B 40 1541 1841 1805 131 80 -257 C ATOM 2685 O ALA B 40 33.435 23.899 35.235 1.00 16.43 O ANISOU 2685 O ALA B 40 1910 2200 2133 121 84 -255 O ATOM 2686 CB ALA B 40 34.867 21.456 36.918 1.00 9.89 C ANISOU 2686 CB ALA B 40 1044 1383 1331 152 73 -261 C ATOM 2687 N VAL B 41 33.050 21.873 34.325 1.00 12.58 N ANISOU 2687 N VAL B 41 1398 1689 1694 131 67 -262 N ATOM 2688 CA VAL B 41 32.904 22.412 32.969 1.00 10.32 C ANISOU 2688 CA VAL B 41 1122 1395 1404 117 59 -268 C ATOM 2689 C VAL B 41 31.710 23.365 32.885 1.00 19.70 C ANISOU 2689 C VAL B 41 2320 2582 2582 111 74 -255 C ATOM 2690 O VAL B 41 31.789 24.434 32.261 1.00 14.76 O ANISOU 2690 O VAL B 41 1709 1960 1940 100 73 -254 O ATOM 2691 CB VAL B 41 32.778 21.246 31.968 1.00 15.63 C ANISOU 2691 CB VAL B 41 1783 2051 2105 119 44 -276 C ATOM 2692 CG1 VAL B 41 32.177 21.694 30.678 1.00 6.78 C ANISOU 2692 CG1 VAL B 41 668 923 984 107 40 -277 C ATOM 2693 CG2 VAL B 41 34.138 20.572 31.738 1.00 15.15 C ANISOU 2693 CG2 VAL B 41 1717 1993 2048 121 27 -289 C ATOM 2694 N LYS B 42 30.589 23.008 33.524 1.00 18.67 N ANISOU 2694 N LYS B 42 2181 2447 2464 119 86 -244 N ATOM 2695 CA LYS B 42 29.432 23.902 33.530 1.00 10.68 C ANISOU 2695 CA LYS B 42 1181 1435 1444 114 100 -231 C ATOM 2696 C LYS B 42 29.742 25.216 34.248 1.00 15.05 C ANISOU 2696 C LYS B 42 1751 2003 1966 109 111 -225 C ATOM 2697 O LYS B 42 29.261 26.281 33.842 1.00 14.41 O ANISOU 2697 O LYS B 42 1684 1920 1871 101 116 -218 O ATOM 2698 CB LYS B 42 28.234 23.201 34.173 1.00 12.80 C ANISOU 2698 CB LYS B 42 1434 1697 1731 123 112 -219 C ATOM 2699 CG LYS B 42 27.735 21.987 33.387 1.00 16.46 C ANISOU 2699 CG LYS B 42 1882 2142 2229 126 100 -222 C ATOM 2700 CD LYS B 42 26.427 21.403 33.958 1.00 16.99 C ANISOU 2700 CD LYS B 42 1935 2202 2320 133 111 -205 C ATOM 2701 CE LYS B 42 26.629 20.762 35.317 1.00 14.68 C ANISOU 2701 CE LYS B 42 1626 1914 2038 145 118 -194 C ATOM 2702 NZ LYS B 42 25.335 20.300 35.914 1.00 8.88 N ANISOU 2702 NZ LYS B 42 876 1172 1326 150 129 -172 N ATOM 2703 N ALA B 43 30.524 25.162 35.330 1.00 11.82 N ANISOU 2703 N ALA B 43 1340 1606 1546 115 115 -225 N ATOM 2704 CA ALA B 43 30.867 26.397 36.023 1.00 11.83 C ANISOU 2704 CA ALA B 43 1358 1618 1518 109 124 -219 C ATOM 2705 C ALA B 43 31.832 27.227 35.191 1.00 11.16 C ANISOU 2705 C ALA B 43 1286 1533 1422 98 111 -226 C ATOM 2706 O ALA B 43 31.752 28.461 35.187 1.00 13.60 O ANISOU 2706 O ALA B 43 1611 1841 1714 90 116 -217 O ATOM 2707 CB ALA B 43 31.423 26.101 37.422 1.00 9.84 C ANISOU 2707 CB ALA B 43 1100 1382 1258 118 132 -217 C ATOM 2708 N ILE B 44 32.758 26.574 34.484 1.00 9.40 N ANISOU 2708 N ILE B 44 1055 1309 1208 97 95 -239 N ATOM 2709 CA ILE B 44 33.638 27.300 33.570 1.00 9.31 C ANISOU 2709 CA ILE B 44 1052 1297 1189 86 82 -243 C ATOM 2710 C ILE B 44 32.818 27.953 32.457 1.00 9.92 C ANISOU 2710 C ILE B 44 1128 1369 1270 77 79 -245 C ATOM 2711 O ILE B 44 32.962 29.152 32.167 1.00 11.17 O ANISOU 2711 O ILE B 44 1290 1535 1419 67 77 -248 O ATOM 2712 CB ILE B 44 34.718 26.362 33.007 1.00 14.85 C ANISOU 2712 CB ILE B 44 1741 2000 1901 88 65 -258 C ATOM 2713 CG1 ILE B 44 35.654 25.915 34.127 1.00 12.07 C ANISOU 2713 CG1 ILE B 44 1384 1660 1542 96 65 -264 C ATOM 2714 CG2 ILE B 44 35.489 27.038 31.854 1.00 6.04 C ANISOU 2714 CG2 ILE B 44 623 890 783 76 50 -269 C ATOM 2715 CD1 ILE B 44 36.608 24.823 33.712 1.00 12.32 C ANISOU 2715 CD1 ILE B 44 1403 1693 1587 101 49 -278 C ATOM 2716 N SER B 45 31.917 27.185 31.846 1.00 9.38 N ANISOU 2716 N SER B 45 1055 1289 1220 80 79 -244 N ATOM 2717 CA SER B 45 31.066 27.725 30.792 1.00 10.65 C ANISOU 2717 CA SER B 45 1214 1446 1385 71 76 -246 C ATOM 2718 C SER B 45 30.289 28.950 31.282 1.00 17.11 C ANISOU 2718 C SER B 45 2043 2268 2190 68 90 -236 C ATOM 2719 O SER B 45 30.173 29.955 30.574 1.00 13.39 O ANISOU 2719 O SER B 45 1573 1801 1715 58 86 -241 O ATOM 2720 CB SER B 45 30.117 26.639 30.288 1.00 11.51 C ANISOU 2720 CB SER B 45 1316 1541 1515 77 76 -244 C ATOM 2721 OG SER B 45 29.343 27.109 29.203 1.00 8.46 O ANISOU 2721 OG SER B 45 928 1152 1134 68 72 -248 O ATOM 2722 N SER B 46 29.714 28.866 32.481 1.00 18.83 N ANISOU 2722 N SER B 46 2268 2485 2403 77 106 -222 N ATOM 2723 CA SER B 46 28.982 29.998 33.029 1.00 21.51 C ANISOU 2723 CA SER B 46 2618 2828 2728 75 119 -212 C ATOM 2724 C SER B 46 29.890 31.229 33.126 1.00 19.37 C ANISOU 2724 C SER B 46 2352 2567 2441 65 114 -219 C ATOM 2725 O SER B 46 29.516 32.326 32.698 1.00 14.92 O ANISOU 2725 O SER B 46 1792 2005 1873 58 114 -219 O ATOM 2726 CB SER B 46 28.390 29.614 34.394 1.00 13.03 C ANISOU 2726 CB SER B 46 1548 1753 1650 87 136 -195 C ATOM 2727 OG SER B 46 27.664 30.700 34.952 1.00 17.40 O ANISOU 2727 OG SER B 46 2111 2310 2190 85 148 -186 O ATOM 2728 N ALA B 47 31.112 31.051 33.636 1.00 11.92 N ANISOU 2728 N ALA B 47 1407 1631 1491 67 109 -224 N ATOM 2729 CA ALA B 47 32.037 32.180 33.776 1.00 12.22 C ANISOU 2729 CA ALA B 47 1448 1680 1516 59 104 -230 C ATOM 2730 C ALA B 47 32.549 32.673 32.423 1.00 15.41 C ANISOU 2730 C ALA B 47 1843 2086 1926 48 89 -241 C ATOM 2731 O ALA B 47 32.752 33.881 32.228 1.00 14.45 O ANISOU 2731 O ALA B 47 1723 1970 1798 40 89 -243 O ATOM 2732 CB ALA B 47 33.201 31.792 34.677 1.00 9.26 C ANISOU 2732 CB ALA B 47 1073 1312 1132 63 102 -232 C ATOM 2733 N VAL B 48 32.762 31.761 31.478 1.00 12.58 N ANISOU 2733 N VAL B 48 1474 1724 1582 48 78 -250 N ATOM 2734 CA VAL B 48 33.257 32.163 30.165 1.00 11.51 C ANISOU 2734 CA VAL B 48 1327 1592 1453 39 64 -260 C ATOM 2735 C VAL B 48 32.199 32.979 29.425 1.00 11.47 C ANISOU 2735 C VAL B 48 1324 1583 1451 33 68 -257 C ATOM 2736 O VAL B 48 32.515 33.993 28.799 1.00 14.00 O ANISOU 2736 O VAL B 48 1640 1909 1769 25 64 -261 O ATOM 2737 CB VAL B 48 33.721 30.927 29.371 1.00 18.43 C ANISOU 2737 CB VAL B 48 2193 2467 2345 42 51 -269 C ATOM 2738 CG1 VAL B 48 33.958 31.255 27.891 1.00 13.97 C ANISOU 2738 CG1 VAL B 48 1615 1905 1788 33 38 -279 C ATOM 2739 CG2 VAL B 48 34.985 30.335 30.004 1.00 15.02 C ANISOU 2739 CG2 VAL B 48 1758 2040 1907 47 45 -274 C ATOM 2740 N ARG B 49 30.924 32.609 29.550 1.00 6.43 N ANISOU 2740 N ARG B 49 690 935 817 37 77 -249 N ATOM 2741 CA ARG B 49 29.869 33.405 28.928 1.00 9.57 C ANISOU 2741 CA ARG B 49 1091 1329 1216 32 82 -246 C ATOM 2742 C ARG B 49 29.535 34.679 29.698 1.00 14.67 C ANISOU 2742 C ARG B 49 1748 1977 1848 30 94 -237 C ATOM 2743 O ARG B 49 28.588 35.388 29.310 1.00 10.69 O ANISOU 2743 O ARG B 49 1247 1470 1345 26 99 -233 O ATOM 2744 CB ARG B 49 28.603 32.565 28.743 1.00 9.88 C ANISOU 2744 CB ARG B 49 1131 1358 1267 37 88 -240 C ATOM 2745 CG ARG B 49 28.580 31.694 27.468 1.00 12.75 C ANISOU 2745 CG ARG B 49 1482 1717 1647 34 75 -250 C ATOM 2746 CD ARG B 49 29.565 30.528 27.538 1.00 10.15 C ANISOU 2746 CD ARG B 49 1145 1388 1324 39 65 -258 C ATOM 2747 NE ARG B 49 29.263 29.444 26.600 1.00 13.82 N ANISOU 2747 NE ARG B 49 1600 1844 1806 39 55 -265 N ATOM 2748 CZ ARG B 49 29.677 29.404 25.334 1.00 16.96 C ANISOU 2748 CZ ARG B 49 1986 2245 2212 32 41 -277 C ATOM 2749 NH1 ARG B 49 30.399 30.396 24.831 1.00 13.99 N ANISOU 2749 NH1 ARG B 49 1607 1881 1829 25 35 -281 N ATOM 2750 NH2 ARG B 49 29.357 28.375 24.565 1.00 12.56 N ANISOU 2750 NH2 ARG B 49 1421 1681 1671 33 32 -283 N ATOM 2751 N LYS B 50 30.273 34.954 30.781 1.00 16.28 N ANISOU 2751 N LYS B 50 1957 2187 2040 32 98 -235 N ATOM 2752 CA LYS B 50 30.256 36.221 31.522 1.00 16.35 C ANISOU 2752 CA LYS B 50 1975 2200 2036 30 106 -230 C ATOM 2753 C LYS B 50 28.981 36.410 32.341 1.00 13.56 C ANISOU 2753 C LYS B 50 1634 1842 1677 36 122 -217 C ATOM 2754 O LYS B 50 28.539 37.537 32.559 1.00 15.09 O ANISOU 2754 O LYS B 50 1835 2035 1863 33 128 -212 O ATOM 2755 CB LYS B 50 30.489 37.422 30.599 1.00 14.89 C ANISOU 2755 CB LYS B 50 1786 2018 1852 20 101 -235 C ATOM 2756 CG LYS B 50 31.855 37.422 29.903 1.00 12.41 C ANISOU 2756 CG LYS B 50 1461 1713 1543 14 87 -246 C ATOM 2757 CD LYS B 50 33.017 37.557 30.894 1.00 16.53 C ANISOU 2757 CD LYS B 50 1984 2242 2053 16 87 -248 C ATOM 2758 CE LYS B 50 34.367 37.419 30.163 1.00 20.45 C ANISOU 2758 CE LYS B 50 2466 2747 2555 12 73 -259 C ATOM 2759 NZ LYS B 50 35.529 37.745 31.031 1.00 24.04 N ANISOU 2759 NZ LYS B 50 2923 3212 3001 12 72 -261 N ATOM 2760 N ALA B 51 28.368 35.318 32.790 1.00 12.55 N ANISOU 2760 N ALA B 51 1508 1709 1553 45 128 -210 N ATOM 2761 CA ALA B 51 27.306 35.425 33.775 1.00 12.68 C ANISOU 2761 CA ALA B 51 1534 1722 1563 53 144 -196 C ATOM 2762 C ALA B 51 27.835 36.137 35.009 1.00 16.58 C ANISOU 2762 C ALA B 51 2036 2224 2041 54 150 -192 C ATOM 2763 O ALA B 51 28.838 35.721 35.592 1.00 15.93 O ANISOU 2763 O ALA B 51 1952 2146 1953 56 147 -195 O ATOM 2764 CB ALA B 51 26.776 34.037 34.148 1.00 12.30 C ANISOU 2764 CB ALA B 51 1482 1669 1523 64 150 -188 C ATOM 2765 N GLY B 52 27.145 37.203 35.417 1.00 18.96 N ANISOU 2765 N GLY B 52 2346 2525 2333 54 159 -185 N ATOM 2766 CA GLY B 52 27.528 37.962 36.585 1.00 15.67 C ANISOU 2766 CA GLY B 52 1938 2115 1902 55 166 -181 C ATOM 2767 C GLY B 52 28.543 39.059 36.351 1.00 19.87 C ANISOU 2767 C GLY B 52 2469 2652 2429 45 158 -191 C ATOM 2768 O GLY B 52 28.923 39.728 37.316 1.00 20.29 O ANISOU 2768 O GLY B 52 2529 2710 2469 45 163 -190 O ATOM 2769 N ILE B 53 28.977 39.284 35.103 1.00 9.95 N ANISOU 2769 N ILE B 53 1204 1395 1182 36 146 -201 N ATOM 2770 CA ILE B 53 29.991 40.297 34.829 1.00 12.33 C ANISOU 2770 CA ILE B 53 1503 1702 1480 27 139 -210 C ATOM 2771 C ILE B 53 29.511 41.683 35.260 1.00 14.36 C ANISOU 2771 C ILE B 53 1769 1959 1729 25 148 -206 C ATOM 2772 O ILE B 53 30.325 42.559 35.572 1.00 17.44 O ANISOU 2772 O ILE B 53 2159 2354 2112 20 146 -211 O ATOM 2773 CB ILE B 53 30.382 40.249 33.335 1.00 12.09 C ANISOU 2773 CB ILE B 53 1460 1671 1463 20 127 -220 C ATOM 2774 CG1 ILE B 53 31.662 41.033 33.062 1.00 15.15 C ANISOU 2774 CG1 ILE B 53 1841 2066 1848 12 119 -229 C ATOM 2775 CG2 ILE B 53 29.240 40.714 32.465 1.00 4.81 C ANISOU 2775 CG2 ILE B 53 539 741 547 17 129 -217 C ATOM 2776 CD1 ILE B 53 32.862 40.444 33.753 1.00 23.12 C ANISOU 2776 CD1 ILE B 53 2848 3084 2853 14 114 -233 C ATOM 2777 N ALA B 54 28.192 41.897 35.297 1.00 8.73 N ANISOU 2777 N ALA B 54 1062 1239 1016 29 157 -197 N ATOM 2778 CA ALA B 54 27.644 43.179 35.732 1.00 17.04 C ANISOU 2778 CA ALA B 54 2122 2290 2060 28 165 -192 C ATOM 2779 C ALA B 54 28.080 43.528 37.148 1.00 14.39 C ANISOU 2779 C ALA B 54 1795 1961 1711 32 172 -189 C ATOM 2780 O ALA B 54 28.217 44.708 37.482 1.00 15.15 O ANISOU 2780 O ALA B 54 1896 2060 1800 28 175 -191 O ATOM 2781 CB ALA B 54 26.121 43.151 35.641 1.00 12.85 C ANISOU 2781 CB ALA B 54 1597 1753 1532 34 174 -182 C ATOM 2782 N HIS B 55 28.303 42.519 37.990 1.00 17.56 N ANISOU 2782 N HIS B 55 2198 2367 2108 39 174 -186 N ATOM 2783 CA HIS B 55 28.769 42.790 39.344 1.00 18.42 C ANISOU 2783 CA HIS B 55 2314 2482 2203 42 180 -183 C ATOM 2784 C HIS B 55 30.199 43.318 39.339 1.00 27.96 C ANISOU 2784 C HIS B 55 3518 3698 3408 34 171 -195 C ATOM 2785 O HIS B 55 30.540 44.212 40.127 1.00 28.56 O ANISOU 2785 O HIS B 55 3600 3779 3474 33 175 -196 O ATOM 2786 CB HIS B 55 28.628 41.530 40.194 1.00 16.56 C ANISOU 2786 CB HIS B 55 2080 2248 1963 52 186 -175 C ATOM 2787 CG HIS B 55 27.206 41.199 40.527 1.00 31.54 C ANISOU 2787 CG HIS B 55 3983 4140 3862 60 198 -161 C ATOM 2788 ND1 HIS B 55 26.559 41.718 41.627 1.00 38.28 N ANISOU 2788 ND1 HIS B 55 4846 4996 4704 66 211 -151 N ATOM 2789 CD2 HIS B 55 26.289 40.445 39.875 1.00 34.82 C ANISOU 2789 CD2 HIS B 55 4394 4549 4287 65 200 -156 C ATOM 2790 CE1 HIS B 55 25.314 41.273 41.657 1.00 35.94 C ANISOU 2790 CE1 HIS B 55 4550 4694 4411 74 220 -139 C ATOM 2791 NE2 HIS B 55 25.124 40.501 40.602 1.00 34.63 N ANISOU 2791 NE2 HIS B 55 4376 4523 4258 73 214 -141 N ATOM 2792 N LEU B 56 31.034 42.829 38.416 1.00 19.29 N ANISOU 2792 N LEU B 56 2409 2601 2319 29 159 -204 N ATOM 2793 CA LEU B 56 32.399 43.348 38.302 1.00 18.50 C ANISOU 2793 CA LEU B 56 2303 2508 2218 22 151 -214 C ATOM 2794 C LEU B 56 32.410 44.804 37.862 1.00 21.04 C ANISOU 2794 C LEU B 56 2626 2829 2540 14 151 -218 C ATOM 2795 O LEU B 56 33.378 45.527 38.133 1.00 21.28 O ANISOU 2795 O LEU B 56 2654 2865 2566 8 149 -225 O ATOM 2796 CB LEU B 56 33.224 42.500 37.328 1.00 29.50 C ANISOU 2796 CB LEU B 56 3684 3903 3621 19 138 -222 C ATOM 2797 CG LEU B 56 34.044 41.360 37.928 1.00 43.26 C ANISOU 2797 CG LEU B 56 5424 5652 5361 24 134 -224 C ATOM 2798 CD1 LEU B 56 34.697 40.520 36.832 1.00 43.60 C ANISOU 2798 CD1 LEU B 56 5454 5695 5416 22 121 -232 C ATOM 2799 CD2 LEU B 56 35.098 41.900 38.882 1.00 47.89 C ANISOU 2799 CD2 LEU B 56 6012 6248 5935 22 134 -228 C ATOM 2800 N TYR B 57 31.367 45.247 37.165 1.00 20.54 N ANISOU 2800 N TYR B 57 2565 2758 2483 12 155 -214 N ATOM 2801 CA TYR B 57 31.307 46.611 36.665 1.00 19.18 C ANISOU 2801 CA TYR B 57 2392 2582 2312 5 156 -217 C ATOM 2802 C TYR B 57 30.407 47.507 37.517 1.00 23.39 C ANISOU 2802 C TYR B 57 2938 3114 2836 8 168 -210 C ATOM 2803 O TYR B 57 29.981 48.573 37.057 1.00 21.93 O ANISOU 2803 O TYR B 57 2755 2925 2654 4 170 -211 O ATOM 2804 CB TYR B 57 30.879 46.596 35.196 1.00 19.06 C ANISOU 2804 CB TYR B 57 2370 2562 2311 0 150 -219 C ATOM 2805 CG TYR B 57 32.030 46.177 34.297 1.00 18.92 C ANISOU 2805 CG TYR B 57 2339 2549 2301 -6 138 -229 C ATOM 2806 CD1 TYR B 57 32.386 44.836 34.159 1.00 16.58 C ANISOU 2806 CD1 TYR B 57 2037 2255 2009 -2 131 -230 C ATOM 2807 CD2 TYR B 57 32.782 47.120 33.620 1.00 16.32 C ANISOU 2807 CD2 TYR B 57 2002 2222 1975 -15 134 -236 C ATOM 2808 CE1 TYR B 57 33.450 44.454 33.344 1.00 15.43 C ANISOU 2808 CE1 TYR B 57 1877 2114 1870 -7 120 -239 C ATOM 2809 CE2 TYR B 57 33.842 46.752 32.816 1.00 15.58 C ANISOU 2809 CE2 TYR B 57 1896 2134 1889 -20 123 -244 C ATOM 2810 CZ TYR B 57 34.174 45.430 32.680 1.00 20.83 C ANISOU 2810 CZ TYR B 57 2555 2802 2559 -15 115 -245 C ATOM 2811 OH TYR B 57 35.232 45.107 31.867 1.00 23.37 O ANISOU 2811 OH TYR B 57 2863 3129 2887 -19 104 -253 O ATOM 2812 N GLY B 58 30.122 47.097 38.752 1.00 21.14 N ANISOU 2812 N GLY B 58 2660 2831 2540 17 175 -204 N ATOM 2813 CA GLY B 58 29.534 47.978 39.743 1.00 25.58 C ANISOU 2813 CA GLY B 58 3233 3394 3092 21 185 -198 C ATOM 2814 C GLY B 58 28.022 48.042 39.791 1.00 27.80 C ANISOU 2814 C GLY B 58 3520 3669 3373 28 195 -187 C ATOM 2815 O GLY B 58 27.481 49.029 40.311 1.00 18.91 O ANISOU 2815 O GLY B 58 2402 2543 2240 30 202 -184 O ATOM 2816 N ILE B 59 27.316 47.025 39.287 1.00 19.22 N ANISOU 2816 N ILE B 59 2431 2578 2294 33 194 -182 N ATOM 2817 CA ILE B 59 25.852 47.091 39.292 1.00 12.12 C ANISOU 2817 CA ILE B 59 1537 1673 1395 40 203 -171 C ATOM 2818 C ILE B 59 25.311 47.282 40.704 1.00 13.80 C ANISOU 2818 C ILE B 59 1759 1891 1594 49 214 -161 C ATOM 2819 O ILE B 59 24.271 47.929 40.898 1.00 17.03 O ANISOU 2819 O ILE B 59 2172 2298 1999 54 222 -154 O ATOM 2820 CB ILE B 59 25.238 45.851 38.616 1.00 12.85 C ANISOU 2820 CB ILE B 59 1624 1762 1498 43 201 -166 C ATOM 2821 CG1 ILE B 59 23.726 46.051 38.408 1.00 11.86 C ANISOU 2821 CG1 ILE B 59 1501 1632 1374 49 208 -156 C ATOM 2822 CG2 ILE B 59 25.492 44.593 39.442 1.00 11.80 C ANISOU 2822 CG2 ILE B 59 1491 1632 1360 51 203 -161 C ATOM 2823 CD1 ILE B 59 23.079 44.903 37.659 1.00 12.00 C ANISOU 2823 CD1 ILE B 59 1513 1645 1402 52 206 -152 C ATOM 2824 N ALA B 60 26.002 46.752 41.706 1.00 11.29 N ANISOU 2824 N ALA B 60 1444 1579 1268 52 216 -161 N ATOM 2825 CA ALA B 60 25.579 46.887 43.090 1.00 16.36 C ANISOU 2825 CA ALA B 60 2094 2225 1896 61 227 -152 C ATOM 2826 C ALA B 60 26.402 47.914 43.854 1.00 26.67 C ANISOU 2826 C ALA B 60 3405 3537 3192 57 228 -159 C ATOM 2827 O ALA B 60 26.443 47.866 45.085 1.00 30.26 O ANISOU 2827 O ALA B 60 3866 3998 3635 62 235 -155 O ATOM 2828 CB ALA B 60 25.648 45.528 43.787 1.00 16.08 C ANISOU 2828 CB ALA B 60 2059 2191 1858 68 232 -145 C ATOM 2829 N GLY B 61 27.049 48.845 43.154 1.00 29.75 N ANISOU 2829 N GLY B 61 3791 3927 3586 47 220 -170 N ATOM 2830 CA GLY B 61 27.885 49.836 43.805 1.00 32.36 C ANISOU 2830 CA GLY B 61 4124 4262 3907 42 220 -178 C ATOM 2831 C GLY B 61 29.362 49.499 43.728 1.00 42.62 C ANISOU 2831 C GLY B 61 5417 5567 5208 35 211 -189 C ATOM 2832 O GLY B 61 29.765 48.376 44.041 1.00 44.38 O ANISOU 2832 O GLY B 61 5639 5795 5430 38 208 -187 O ATOM 2833 N LYS B 72 42.465 36.131 35.062 1.00 35.52 N ANISOU 2833 N LYS B 72 4362 4719 4415 29 49 -281 N ATOM 2834 CA LYS B 72 41.680 35.574 36.161 1.00 31.87 C ANISOU 2834 CA LYS B 72 3912 4251 3944 36 59 -273 C ATOM 2835 C LYS B 72 40.803 34.420 35.698 1.00 27.21 C ANISOU 2835 C LYS B 72 3322 3651 3364 42 58 -271 C ATOM 2836 O LYS B 72 40.559 33.466 36.445 1.00 27.28 O ANISOU 2836 O LYS B 72 3337 3657 3369 50 63 -266 O ATOM 2837 CB LYS B 72 40.807 36.646 36.801 1.00 27.25 C ANISOU 2837 CB LYS B 72 3340 3664 3351 32 71 -266 C ATOM 2838 CG LYS B 72 39.948 36.128 37.929 1.00 35.86 C ANISOU 2838 CG LYS B 72 4442 4750 4432 40 83 -256 C ATOM 2839 CD LYS B 72 40.823 35.540 39.034 1.00 47.26 C ANISOU 2839 CD LYS B 72 5887 6203 5865 45 82 -256 C ATOM 2840 CE LYS B 72 39.991 34.804 40.075 1.00 45.48 C ANISOU 2840 CE LYS B 72 5673 5975 5633 54 94 -246 C ATOM 2841 NZ LYS B 72 38.855 35.645 40.556 1.00 49.33 N ANISOU 2841 NZ LYS B 72 6171 6457 6114 53 107 -237 N ATOM 2842 N LEU B 73 40.297 34.529 34.474 1.00 24.43 N ANISOU 2842 N LEU B 73 2965 3294 3025 37 54 -273 N ATOM 2843 CA LEU B 73 39.381 33.514 33.985 1.00 25.90 C ANISOU 2843 CA LEU B 73 3151 3468 3221 42 54 -272 C ATOM 2844 C LEU B 73 40.086 32.167 33.876 1.00 24.43 C ANISOU 2844 C LEU B 73 2957 3283 3041 49 45 -277 C ATOM 2845 O LEU B 73 39.540 31.141 34.285 1.00 13.31 O ANISOU 2845 O LEU B 73 1554 1868 1636 57 49 -273 O ATOM 2846 CB LEU B 73 38.781 33.958 32.653 1.00 30.22 C ANISOU 2846 CB LEU B 73 3691 4010 3780 35 50 -274 C ATOM 2847 CG LEU B 73 37.381 33.454 32.314 1.00 24.85 C ANISOU 2847 CG LEU B 73 3015 3317 3107 38 55 -269 C ATOM 2848 CD1 LEU B 73 36.497 33.400 33.542 1.00 34.69 C ANISOU 2848 CD1 LEU B 73 4276 4559 4344 44 71 -258 C ATOM 2849 CD2 LEU B 73 36.749 34.361 31.272 1.00 20.26 C ANISOU 2849 CD2 LEU B 73 2431 2734 2533 29 55 -270 C ATOM 2850 N ASP B 74 41.332 32.152 33.401 1.00 22.20 N ANISOU 2850 N ASP B 74 2664 3009 2761 48 33 -286 N ATOM 2851 CA ASP B 74 42.033 30.877 33.340 1.00 23.19 C ANISOU 2851 CA ASP B 74 2783 3136 2893 55 23 -291 C ATOM 2852 C ASP B 74 42.379 30.372 34.735 1.00 21.39 C ANISOU 2852 C ASP B 74 2563 2911 2652 63 30 -287 C ATOM 2853 O ASP B 74 42.387 29.159 34.967 1.00 19.93 O ANISOU 2853 O ASP B 74 2379 2722 2472 72 28 -287 O ATOM 2854 CB ASP B 74 43.291 30.982 32.476 1.00 37.35 C ANISOU 2854 CB ASP B 74 4561 4939 4692 53 10 -301 C ATOM 2855 CG ASP B 74 44.241 32.063 32.945 1.00 49.02 C ANISOU 2855 CG ASP B 74 6037 6429 6158 48 11 -301 C ATOM 2856 OD1 ASP B 74 43.870 32.846 33.847 1.00 46.58 O ANISOU 2856 OD1 ASP B 74 5739 6120 5837 45 22 -295 O ATOM 2857 OD2 ASP B 74 45.375 32.115 32.416 1.00 57.10 O ANISOU 2857 OD2 ASP B 74 7049 7462 7186 47 2 -308 O ATOM 2858 N VAL B 75 42.625 31.283 35.678 1.00 25.11 N ANISOU 2858 N VAL B 75 3042 3390 3109 60 37 -282 N ATOM 2859 CA VAL B 75 42.904 30.896 37.060 1.00 22.17 C ANISOU 2859 CA VAL B 75 2678 3023 2724 67 44 -277 C ATOM 2860 C VAL B 75 41.660 30.302 37.715 1.00 17.27 C ANISOU 2860 C VAL B 75 2068 2393 2102 74 58 -267 C ATOM 2861 O VAL B 75 41.731 29.268 38.394 1.00 21.35 O ANISOU 2861 O VAL B 75 2586 2908 2618 83 61 -264 O ATOM 2862 CB VAL B 75 43.447 32.103 37.848 1.00 29.31 C ANISOU 2862 CB VAL B 75 3585 3938 3612 61 49 -276 C ATOM 2863 CG1 VAL B 75 43.518 31.804 39.335 1.00 21.83 C ANISOU 2863 CG1 VAL B 75 2648 2997 2650 67 58 -269 C ATOM 2864 CG2 VAL B 75 44.816 32.511 37.310 1.00 28.44 C ANISOU 2864 CG2 VAL B 75 3464 3839 3504 57 37 -285 C ATOM 2865 N LEU B 76 40.504 30.946 37.522 1.00 12.69 N ANISOU 2865 N LEU B 76 1494 1805 1524 70 66 -261 N ATOM 2866 CA LEU B 76 39.253 30.419 38.061 1.00 15.71 C ANISOU 2866 CA LEU B 76 1883 2178 1907 76 80 -250 C ATOM 2867 C LEU B 76 38.955 29.034 37.494 1.00 14.04 C ANISOU 2867 C LEU B 76 1666 1956 1713 84 77 -252 C ATOM 2868 O LEU B 76 38.558 28.121 38.228 1.00 16.45 O ANISOU 2868 O LEU B 76 1963 2268 2021 95 83 -254 O ATOM 2869 CB LEU B 76 38.092 31.379 37.761 1.00 8.93 C ANISOU 2869 CB LEU B 76 1031 1313 1049 70 88 -245 C ATOM 2870 CG LEU B 76 36.730 30.846 38.229 1.00 21.43 C ANISOU 2870 CG LEU B 76 2620 2886 2636 78 103 -233 C ATOM 2871 CD1 LEU B 76 36.684 30.693 39.756 1.00 18.96 C ANISOU 2871 CD1 LEU B 76 2315 2580 2310 85 117 -222 C ATOM 2872 CD2 LEU B 76 35.562 31.718 37.738 1.00 26.93 C ANISOU 2872 CD2 LEU B 76 3321 3575 3335 72 109 -228 C ATOM 2873 N SER B 77 39.120 28.870 36.179 1.00 11.10 N ANISOU 2873 N SER B 77 1285 1579 1355 80 63 -261 N ATOM 2874 CA SER B 77 38.911 27.566 35.547 1.00 12.87 C ANISOU 2874 CA SER B 77 1500 1795 1597 87 57 -266 C ATOM 2875 C SER B 77 39.823 26.508 36.159 1.00 13.91 C ANISOU 2875 C SER B 77 1619 1938 1729 97 50 -278 C ATOM 2876 O SER B 77 39.397 25.374 36.416 1.00 15.39 O ANISOU 2876 O SER B 77 1795 2124 1929 109 50 -283 O ATOM 2877 CB SER B 77 39.176 27.676 34.046 1.00 8.93 C ANISOU 2877 CB SER B 77 992 1292 1109 79 42 -276 C ATOM 2878 OG SER B 77 38.308 28.613 33.435 1.00 18.22 O ANISOU 2878 OG SER B 77 2170 2466 2287 71 45 -274 O ATOM 2879 N ASN B 78 41.091 26.854 36.387 1.00 14.12 N ANISOU 2879 N ASN B 78 1646 1975 1743 94 43 -281 N ATOM 2880 CA ASN B 78 42.003 25.912 37.021 1.00 13.72 C ANISOU 2880 CA ASN B 78 1584 1937 1691 105 36 -292 C ATOM 2881 C ASN B 78 41.513 25.551 38.421 1.00 20.79 C ANISOU 2881 C ASN B 78 2478 2845 2578 116 49 -288 C ATOM 2882 O ASN B 78 41.468 24.370 38.790 1.00 16.25 O ANISOU 2882 O ASN B 78 1889 2273 2012 131 47 -294 O ATOM 2883 CB ASN B 78 43.414 26.500 37.071 1.00 16.05 C ANISOU 2883 CB ASN B 78 1882 2243 1974 99 28 -294 C ATOM 2884 CG ASN B 78 44.471 25.455 37.409 1.00 19.24 C ANISOU 2884 CG ASN B 78 2273 2659 2378 110 16 -307 C ATOM 2885 OD1 ASN B 78 44.598 24.450 36.713 1.00 20.52 O ANISOU 2885 OD1 ASN B 78 2424 2815 2556 116 5 -317 O ATOM 2886 ND2 ASN B 78 45.227 25.685 38.478 1.00 9.90 N ANISOU 2886 ND2 ASN B 78 1091 1493 1178 113 19 -306 N ATOM 2887 N ASP B 79 41.109 26.563 39.202 1.00 17.92 N ANISOU 2887 N ASP B 79 2126 2484 2197 110 62 -276 N ATOM 2888 CA ASP B 79 40.570 26.324 40.540 1.00 13.55 C ANISOU 2888 CA ASP B 79 1571 1944 1633 120 76 -269 C ATOM 2889 C ASP B 79 39.335 25.440 40.483 1.00 18.35 C ANISOU 2889 C ASP B 79 2168 2544 2259 130 84 -265 C ATOM 2890 O ASP B 79 39.155 24.559 41.329 1.00 16.59 O ANISOU 2890 O ASP B 79 1932 2333 2039 145 90 -262 O ATOM 2891 CB ASP B 79 40.200 27.643 41.223 1.00 11.74 C ANISOU 2891 CB ASP B 79 1359 1716 1386 110 89 -256 C ATOM 2892 CG ASP B 79 41.406 28.492 41.571 1.00 23.81 C ANISOU 2892 CG ASP B 79 2897 3252 2899 102 83 -256 C ATOM 2893 OD1 ASP B 79 42.533 27.964 41.635 1.00 21.28 O ANISOU 2893 OD1 ASP B 79 2567 2943 2575 106 72 -266 O ATOM 2894 OD2 ASP B 79 41.214 29.707 41.775 1.00 20.54 O ANISOU 2894 OD2 ASP B 79 2497 2831 2475 92 90 -247 O ATOM 2895 N LEU B 80 38.462 25.668 39.500 1.00 13.30 N ANISOU 2895 N LEU B 80 1533 1887 1634 124 85 -263 N ATOM 2896 CA LEU B 80 37.260 24.849 39.408 1.00 15.48 C ANISOU 2896 CA LEU B 80 1797 2153 1931 133 92 -259 C ATOM 2897 C LEU B 80 37.610 23.384 39.161 1.00 13.70 C ANISOU 2897 C LEU B 80 1552 1924 1730 147 81 -267 C ATOM 2898 O LEU B 80 37.100 22.497 39.848 1.00 13.41 O ANISOU 2898 O LEU B 80 1498 1890 1708 161 87 -259 O ATOM 2899 CB LEU B 80 36.332 25.386 38.322 1.00 12.10 C ANISOU 2899 CB LEU B 80 1379 1707 1513 122 93 -255 C ATOM 2900 CG LEU B 80 35.647 26.693 38.751 1.00 12.79 C ANISOU 2900 CG LEU B 80 1484 1794 1582 113 108 -241 C ATOM 2901 CD1 LEU B 80 35.033 27.391 37.565 1.00 11.67 C ANISOU 2901 CD1 LEU B 80 1352 1635 1446 103 105 -238 C ATOM 2902 CD2 LEU B 80 34.593 26.378 39.823 1.00 15.11 C ANISOU 2902 CD2 LEU B 80 1771 2094 1876 123 126 -229 C ATOM 2903 N VAL B 81 38.483 23.108 38.185 1.00 15.46 N ANISOU 2903 N VAL B 81 1774 2140 1960 143 63 -281 N ATOM 2904 CA VAL B 81 38.818 21.717 37.872 1.00 14.46 C ANISOU 2904 CA VAL B 81 1630 2005 1860 155 50 -288 C ATOM 2905 C VAL B 81 39.600 21.061 39.010 1.00 15.41 C ANISOU 2905 C VAL B 81 1736 2142 1975 171 49 -287 C ATOM 2906 O VAL B 81 39.335 19.910 39.388 1.00 17.48 O ANISOU 2906 O VAL B 81 1979 2399 2263 186 46 -280 O ATOM 2907 CB VAL B 81 39.588 21.626 36.548 1.00 16.23 C ANISOU 2907 CB VAL B 81 1857 2219 2090 146 31 -302 C ATOM 2908 CG1 VAL B 81 39.945 20.182 36.304 1.00 8.71 C ANISOU 2908 CG1 VAL B 81 888 1256 1166 159 17 -309 C ATOM 2909 CG2 VAL B 81 38.750 22.216 35.381 1.00 10.23 C ANISOU 2909 CG2 VAL B 81 1107 1444 1336 132 32 -300 C ATOM 2910 N MET B 82 40.614 21.745 39.531 1.00 15.70 N ANISOU 2910 N MET B 82 1783 2199 1983 166 48 -292 N ATOM 2911 CA MET B 82 41.389 21.172 40.634 1.00 11.94 C ANISOU 2911 CA MET B 82 1295 1743 1499 181 48 -290 C ATOM 2912 C MET B 82 40.485 20.794 41.803 1.00 18.36 C ANISOU 2912 C MET B 82 2094 2565 2315 195 63 -270 C ATOM 2913 O MET B 82 40.603 19.702 42.377 1.00 18.18 O ANISOU 2913 O MET B 82 2062 2537 2309 203 54 -250 O ATOM 2914 CB MET B 82 42.446 22.161 41.113 1.00 14.60 C ANISOU 2914 CB MET B 82 1646 2100 1801 171 48 -295 C ATOM 2915 CG MET B 82 43.685 22.226 40.286 1.00 17.14 C ANISOU 2915 CG MET B 82 1972 2420 2121 164 30 -310 C ATOM 2916 SD MET B 82 44.663 20.721 40.351 1.00 18.90 S ANISOU 2916 SD MET B 82 2174 2646 2361 184 14 -319 S ATOM 2917 CE MET B 82 45.989 21.256 39.276 1.00 28.18 C ANISOU 2917 CE MET B 82 3359 3820 3527 168 -4 -335 C ATOM 2918 N ASN B 83 39.592 21.699 42.192 1.00 10.34 N ANISOU 2918 N ASN B 83 1090 1553 1283 186 80 -261 N ATOM 2919 CA ASN B 83 38.843 21.460 43.418 1.00 8.30 C ANISOU 2919 CA ASN B 83 829 1303 1022 191 91 -232 C ATOM 2920 C ASN B 83 37.805 20.372 43.225 1.00 14.85 C ANISOU 2920 C ASN B 83 1648 2106 1890 194 86 -209 C ATOM 2921 O ASN B 83 37.643 19.514 44.101 1.00 14.49 O ANISOU 2921 O ASN B 83 1596 2057 1854 199 83 -180 O ATOM 2922 CB ASN B 83 38.184 22.739 43.923 1.00 20.88 C ANISOU 2922 CB ASN B 83 2435 2912 2587 185 113 -231 C ATOM 2923 CG ASN B 83 37.505 22.527 45.255 1.00 34.18 C ANISOU 2923 CG ASN B 83 4120 4603 4264 187 122 -196 C ATOM 2924 OD1 ASN B 83 38.161 22.455 46.295 1.00 40.06 O ANISOU 2924 OD1 ASN B 83 4866 5367 4990 190 122 -185 O ATOM 2925 ND2 ASN B 83 36.187 22.388 45.228 1.00 28.29 N ANISOU 2925 ND2 ASN B 83 3372 3842 3534 185 131 -178 N ATOM 2926 N MET B 84 37.106 20.370 42.078 1.00 11.53 N ANISOU 2926 N MET B 84 1225 1666 1491 192 86 -221 N ATOM 2927 CA MET B 84 36.110 19.326 41.833 1.00 15.34 C ANISOU 2927 CA MET B 84 1696 2122 2012 194 80 -202 C ATOM 2928 C MET B 84 36.763 17.948 41.718 1.00 18.17 C ANISOU 2928 C MET B 84 2041 2465 2397 201 60 -196 C ATOM 2929 O MET B 84 36.222 16.952 42.218 1.00 12.50 O ANISOU 2929 O MET B 84 1314 1732 1702 205 55 -167 O ATOM 2930 CB MET B 84 35.303 19.639 40.574 1.00 16.14 C ANISOU 2930 CB MET B 84 1797 2207 2130 189 83 -219 C ATOM 2931 CG MET B 84 34.345 20.806 40.708 1.00 16.98 C ANISOU 2931 CG MET B 84 1914 2322 2217 182 104 -218 C ATOM 2932 SD MET B 84 33.248 20.679 42.132 1.00 19.31 S ANISOU 2932 SD MET B 84 2210 2620 2507 182 118 -176 S ATOM 2933 CE MET B 84 32.429 19.102 41.865 1.00 17.86 C ANISOU 2933 CE MET B 84 2010 2405 2373 186 105 -152 C ATOM 2934 N LEU B 85 37.919 17.864 41.060 1.00 8.59 N ANISOU 2934 N LEU B 85 827 1256 1183 204 47 -221 N ATOM 2935 CA LEU B 85 38.593 16.568 40.942 1.00 14.67 C ANISOU 2935 CA LEU B 85 1584 2012 1978 212 27 -217 C ATOM 2936 C LEU B 85 39.123 16.092 42.297 1.00 16.66 C ANISOU 2936 C LEU B 85 1835 2277 2219 217 25 -191 C ATOM 2937 O LEU B 85 39.044 14.900 42.614 1.00 19.10 O ANISOU 2937 O LEU B 85 2133 2571 2554 223 15 -169 O ATOM 2938 CB LEU B 85 39.732 16.653 39.917 1.00 14.59 C ANISOU 2938 CB LEU B 85 1573 2003 1966 214 14 -251 C ATOM 2939 CG LEU B 85 39.359 16.721 38.428 1.00 11.00 C ANISOU 2939 CG LEU B 85 1120 1530 1530 208 9 -273 C ATOM 2940 CD1 LEU B 85 40.591 16.815 37.541 1.00 19.46 C ANISOU 2940 CD1 LEU B 85 2202 2603 2590 201 -6 -294 C ATOM 2941 CD2 LEU B 85 38.511 15.520 38.020 1.00 13.24 C ANISOU 2941 CD2 LEU B 85 1389 1784 1857 213 0 -260 C ATOM 2942 N LYS B 86 39.720 16.994 43.088 1.00 18.91 N ANISOU 2942 N LYS B 86 2130 2590 2465 215 35 -193 N ATOM 2943 CA LYS B 86 40.174 16.603 44.422 1.00 22.03 C ANISOU 2943 CA LYS B 86 2523 3000 2847 220 35 -168 C ATOM 2944 C LYS B 86 39.017 16.067 45.249 1.00 19.13 C ANISOU 2944 C LYS B 86 2151 2623 2494 222 42 -131 C ATOM 2945 O LYS B 86 39.136 15.030 45.907 1.00 19.49 O ANISOU 2945 O LYS B 86 2188 2663 2555 228 34 -105 O ATOM 2946 CB LYS B 86 40.827 17.778 45.152 1.00 24.90 C ANISOU 2946 CB LYS B 86 2899 3396 3165 217 46 -177 C ATOM 2947 CG LYS B 86 42.208 18.163 44.679 1.00 16.81 C ANISOU 2947 CG LYS B 86 1877 2386 2123 217 37 -207 C ATOM 2948 CD LYS B 86 42.586 19.481 45.334 1.00 22.15 C ANISOU 2948 CD LYS B 86 2567 3094 2757 212 51 -217 C ATOM 2949 CE LYS B 86 43.943 19.961 44.892 1.00 31.65 C ANISOU 2949 CE LYS B 86 3773 4312 3940 211 44 -247 C ATOM 2950 NZ LYS B 86 44.283 21.259 45.546 1.00 37.02 N ANISOU 2950 NZ LYS B 86 4466 5021 4579 205 58 -257 N ATOM 2951 N SER B 87 37.887 16.764 45.231 1.00 20.04 N ANISOU 2951 N SER B 87 2273 2736 2604 215 58 -126 N ATOM 2952 CA SER B 87 36.766 16.360 46.062 1.00 24.16 C ANISOU 2952 CA SER B 87 2791 3252 3137 216 67 -90 C ATOM 2953 C SER B 87 35.973 15.209 45.454 1.00 30.71 C ANISOU 2953 C SER B 87 3609 4048 4012 218 57 -78 C ATOM 2954 O SER B 87 34.986 14.767 46.056 1.00 26.66 O ANISOU 2954 O SER B 87 3091 3527 3513 218 63 -47 O ATOM 2955 CB SER B 87 35.864 17.565 46.334 1.00 23.17 C ANISOU 2955 CB SER B 87 2678 3139 2988 209 88 -90 C ATOM 2956 OG SER B 87 35.357 18.091 45.127 1.00 29.15 O ANISOU 2956 OG SER B 87 3438 3883 3754 203 90 -114 O ATOM 2957 N SER B 88 36.368 14.720 44.274 1.00 25.00 N ANISOU 2957 N SER B 88 2879 3307 3313 219 42 -100 N ATOM 2958 CA SER B 88 35.712 13.543 43.715 1.00 17.86 C ANISOU 2958 CA SER B 88 1962 2370 2453 221 31 -89 C ATOM 2959 C SER B 88 36.140 12.265 44.427 1.00 22.80 C ANISOU 2959 C SER B 88 2576 2988 3099 230 19 -63 C ATOM 2960 O SER B 88 35.498 11.227 44.252 1.00 19.30 O ANISOU 2960 O SER B 88 2121 2518 2692 232 12 -46 O ATOM 2961 CB SER B 88 36.016 13.407 42.227 1.00 16.48 C ANISOU 2961 CB SER B 88 1784 2180 2298 220 19 -122 C ATOM 2962 OG SER B 88 37.353 12.976 42.042 1.00 13.91 O ANISOU 2962 OG SER B 88 1455 1858 1971 227 3 -137 O ATOM 2963 N PHE B 89 37.226 12.314 45.195 1.00 25.23 N ANISOU 2963 N PHE B 89 2886 3317 3382 234 16 -61 N ATOM 2964 CA PHE B 89 37.815 11.140 45.831 1.00 27.81 C ANISOU 2964 CA PHE B 89 3202 3639 3725 243 4 -39 C ATOM 2965 C PHE B 89 38.239 10.088 44.815 1.00 19.85 C ANISOU 2965 C PHE B 89 2183 2604 2754 248 -16 -52 C ATOM 2966 O PHE B 89 38.458 8.934 45.173 1.00 21.03 O ANISOU 2966 O PHE B 89 2322 2741 2928 255 -27 -32 O ATOM 2967 CB PHE B 89 36.868 10.538 46.884 1.00 25.29 C ANISOU 2967 CB PHE B 89 2878 3314 3419 245 11 4 C ATOM 2968 CG PHE B 89 36.727 11.390 48.115 1.00 25.46 C ANISOU 2968 CG PHE B 89 2908 3365 3402 244 28 21 C ATOM 2969 CD1 PHE B 89 36.047 12.602 48.070 1.00 38.93 C ANISOU 2969 CD1 PHE B 89 4625 5083 5083 236 45 12 C ATOM 2970 CD2 PHE B 89 37.297 10.997 49.316 1.00 31.33 C ANISOU 2970 CD2 PHE B 89 3648 4125 4132 251 27 46 C ATOM 2971 CE1 PHE B 89 35.927 13.402 49.209 1.00 31.78 C ANISOU 2971 CE1 PHE B 89 3729 4206 4142 235 61 26 C ATOM 2972 CE2 PHE B 89 37.175 11.787 50.454 1.00 34.31 C ANISOU 2972 CE2 PHE B 89 4033 4530 4472 250 43 61 C ATOM 2973 CZ PHE B 89 36.491 12.996 50.395 1.00 32.62 C ANISOU 2973 CZ PHE B 89 3831 4329 4235 242 59 50 C ATOM 2974 N ALA B 90 38.403 10.472 43.549 1.00 17.72 N ANISOU 2974 N ALA B 90 1917 2328 2489 245 -21 -87 N ATOM 2975 CA ALA B 90 38.764 9.536 42.498 1.00 20.69 C ANISOU 2975 CA ALA B 90 2283 2679 2900 249 -40 -103 C ATOM 2976 C ALA B 90 40.174 9.748 41.965 1.00 15.27 C ANISOU 2976 C ALA B 90 1599 2005 2198 253 -51 -134 C ATOM 2977 O ALA B 90 40.600 8.997 41.086 1.00 14.43 O ANISOU 2977 O ALA B 90 1484 1881 2118 257 -67 -150 O ATOM 2978 CB ALA B 90 37.773 9.635 41.327 1.00 11.97 C ANISOU 2978 CB ALA B 90 1177 1553 1819 243 -39 -119 C ATOM 2979 N THR B 91 40.898 10.763 42.432 1.00 14.93 N ANISOU 2979 N THR B 91 1566 1993 2114 251 -43 -144 N ATOM 2980 CA THR B 91 42.158 11.138 41.801 1.00 19.93 C ANISOU 2980 CA THR B 91 2203 2640 2731 253 -51 -177 C ATOM 2981 C THR B 91 43.291 11.194 42.813 1.00 16.68 C ANISOU 2981 C THR B 91 1793 2253 2292 258 -53 -169 C ATOM 2982 O THR B 91 43.075 11.327 44.019 1.00 21.07 O ANISOU 2982 O THR B 91 2351 2823 2831 258 -43 -142 O ATOM 2983 CB THR B 91 42.045 12.487 41.077 1.00 19.98 C ANISOU 2983 CB THR B 91 2220 2659 2713 244 -41 -207 C ATOM 2984 OG1 THR B 91 41.911 13.545 42.041 1.00 17.86 O ANISOU 2984 OG1 THR B 91 1964 2417 2407 239 -23 -198 O ATOM 2985 CG2 THR B 91 40.855 12.475 40.127 1.00 17.24 C ANISOU 2985 CG2 THR B 91 1871 2288 2391 239 -38 -213 C ATOM 2986 N CYS B 92 44.516 11.094 42.294 1.00 16.06 N ANISOU 2986 N CYS B 92 1712 2181 2208 262 -65 -192 N ATOM 2987 CA CYS B 92 45.689 11.123 43.154 1.00 19.79 C ANISOU 2987 CA CYS B 92 2186 2678 2655 267 -69 -188 C ATOM 2988 C CYS B 92 46.771 12.060 42.628 1.00 14.11 C ANISOU 2988 C CYS B 92 1474 1981 1906 265 -70 -222 C ATOM 2989 O CYS B 92 47.541 12.598 43.420 1.00 16.74 O ANISOU 2989 O CYS B 92 1812 2341 2206 264 -66 -221 O ATOM 2990 CB CYS B 92 46.264 9.715 43.331 1.00 17.63 C ANISOU 2990 CB CYS B 92 1899 2390 2409 278 -86 -173 C ATOM 2991 SG CYS B 92 46.739 8.885 41.793 1.00 23.50 S ANISOU 2991 SG CYS B 92 2634 3108 3188 284 -106 -201 S ATOM 2992 N VAL B 93 46.863 12.254 41.310 1.00 16.69 N ANISOU 2992 N VAL B 93 1801 2297 2244 263 -76 -253 N ATOM 2993 CA VAL B 93 47.855 13.156 40.719 1.00 13.20 C ANISOU 2993 CA VAL B 93 1365 1875 1775 260 -77 -286 C ATOM 2994 C VAL B 93 47.165 14.013 39.669 1.00 19.17 C ANISOU 2994 C VAL B 93 2129 2623 2530 250 -69 -308 C ATOM 2995 O VAL B 93 46.423 13.495 38.828 1.00 16.21 O ANISOU 2995 O VAL B 93 1755 2221 2184 245 -73 -307 O ATOM 2996 CB VAL B 93 49.036 12.383 40.098 1.00 14.67 C ANISOU 2996 CB VAL B 93 1543 2056 1974 268 -96 -302 C ATOM 2997 CG1 VAL B 93 50.042 13.339 39.482 1.00 18.97 C ANISOU 2997 CG1 VAL B 93 2103 2617 2487 257 -96 -329 C ATOM 2998 CG2 VAL B 93 49.722 11.524 41.154 1.00 14.57 C ANISOU 2998 CG2 VAL B 93 1524 2051 1962 278 -104 -278 C ATOM 2999 N LEU B 94 47.407 15.322 39.716 1.00 12.30 N ANISOU 2999 N LEU B 94 1273 1776 1625 240 -57 -322 N ATOM 3000 CA LEU B 94 46.739 16.272 38.838 1.00 15.66 C ANISOU 3000 CA LEU B 94 1715 2193 2042 223 -48 -334 C ATOM 3001 C LEU B 94 47.799 17.122 38.155 1.00 14.44 C ANISOU 3001 C LEU B 94 1576 2050 1861 209 -54 -354 C ATOM 3002 O LEU B 94 48.566 17.823 38.821 1.00 14.86 O ANISOU 3002 O LEU B 94 1633 2127 1885 208 -50 -358 O ATOM 3003 CB LEU B 94 45.748 17.153 39.626 1.00 16.25 C ANISOU 3003 CB LEU B 94 1795 2280 2101 220 -27 -323 C ATOM 3004 CG LEU B 94 44.634 16.368 40.342 1.00 17.71 C ANISOU 3004 CG LEU B 94 1967 2453 2311 230 -22 -295 C ATOM 3005 CD1 LEU B 94 43.838 17.244 41.286 1.00 15.54 C ANISOU 3005 CD1 LEU B 94 1702 2192 2011 223 -2 -279 C ATOM 3006 CD2 LEU B 94 43.717 15.677 39.320 1.00 10.87 C ANISOU 3006 CD2 LEU B 94 1093 1555 1483 230 -29 -296 C ATOM 3007 N VAL B 95 47.841 17.059 36.833 1.00 13.26 N ANISOU 3007 N VAL B 95 1432 1883 1723 198 -64 -365 N ATOM 3008 CA VAL B 95 48.746 17.878 36.043 1.00 16.79 C ANISOU 3008 CA VAL B 95 1889 2340 2151 183 -73 -378 C ATOM 3009 C VAL B 95 47.902 18.905 35.304 1.00 19.02 C ANISOU 3009 C VAL B 95 2182 2616 2430 166 -65 -373 C ATOM 3010 O VAL B 95 46.939 18.550 34.612 1.00 20.09 O ANISOU 3010 O VAL B 95 2317 2731 2585 163 -65 -371 O ATOM 3011 CB VAL B 95 49.583 17.020 35.081 1.00 16.78 C ANISOU 3011 CB VAL B 95 1883 2327 2164 185 -92 -390 C ATOM 3012 CG1 VAL B 95 50.300 17.875 34.069 1.00 13.92 C ANISOU 3012 CG1 VAL B 95 1525 1974 1789 168 -101 -397 C ATOM 3013 CG2 VAL B 95 50.580 16.192 35.873 1.00 14.00 C ANISOU 3013 CG2 VAL B 95 1523 1985 1812 201 -99 -392 C ATOM 3014 N SER B 96 48.252 20.175 35.466 1.00 18.68 N ANISOU 3014 N SER B 96 2145 2587 2363 154 -59 -368 N ATOM 3015 CA SER B 96 47.552 21.276 34.825 1.00 19.13 C ANISOU 3015 CA SER B 96 2211 2638 2418 138 -51 -359 C ATOM 3016 C SER B 96 48.535 22.148 34.060 1.00 22.66 C ANISOU 3016 C SER B 96 2658 3092 2859 126 -58 -356 C ATOM 3017 O SER B 96 49.676 22.358 34.495 1.00 19.95 O ANISOU 3017 O SER B 96 2313 2764 2504 128 -61 -357 O ATOM 3018 CB SER B 96 46.798 22.127 35.857 1.00 20.14 C ANISOU 3018 CB SER B 96 2350 2774 2531 135 -32 -347 C ATOM 3019 OG SER B 96 46.328 23.343 35.285 1.00 20.23 O ANISOU 3019 OG SER B 96 2371 2779 2538 120 -25 -336 O ATOM 3020 N GLU B 97 48.082 22.638 32.906 1.00 23.30 N ANISOU 3020 N GLU B 97 2741 3162 2949 115 -58 -350 N ATOM 3021 CA GLU B 97 48.822 23.657 32.172 1.00 22.36 C ANISOU 3021 CA GLU B 97 2622 3047 2826 105 -59 -341 C ATOM 3022 C GLU B 97 49.232 24.814 33.069 1.00 19.95 C ANISOU 3022 C GLU B 97 2322 2755 2502 101 -49 -335 C ATOM 3023 O GLU B 97 50.289 25.421 32.857 1.00 21.69 O ANISOU 3023 O GLU B 97 2533 2990 2720 99 -54 -338 O ATOM 3024 CB GLU B 97 47.969 24.172 31.009 1.00 23.84 C ANISOU 3024 CB GLU B 97 2805 3229 3024 97 -60 -342 C ATOM 3025 CG GLU B 97 48.753 24.977 29.992 1.00 26.06 C ANISOU 3025 CG GLU B 97 3070 3522 3308 92 -68 -347 C ATOM 3026 CD GLU B 97 48.909 26.414 30.417 1.00 33.08 C ANISOU 3026 CD GLU B 97 3962 4424 4185 85 -58 -341 C ATOM 3027 OE1 GLU B 97 48.027 26.908 31.160 1.00 33.45 O ANISOU 3027 OE1 GLU B 97 4022 4465 4223 81 -45 -334 O ATOM 3028 OE2 GLU B 97 49.931 27.028 30.040 1.00 30.32 O ANISOU 3028 OE2 GLU B 97 3606 4081 3832 83 -59 -341 O ATOM 3029 N GLU B 98 48.431 25.110 34.094 1.00 12.27 N ANISOU 3029 N GLU B 98 1364 1780 1520 100 -34 -327 N ATOM 3030 CA GLU B 98 48.611 26.274 34.957 1.00 25.39 C ANISOU 3030 CA GLU B 98 3031 3452 3164 95 -24 -320 C ATOM 3031 C GLU B 98 49.617 26.067 36.084 1.00 27.92 C ANISOU 3031 C GLU B 98 3353 3785 3470 101 -24 -320 C ATOM 3032 O GLU B 98 49.954 27.038 36.764 1.00 26.65 O ANISOU 3032 O GLU B 98 3196 3633 3295 95 -17 -316 O ATOM 3033 CB GLU B 98 47.264 26.660 35.582 1.00 25.99 C ANISOU 3033 CB GLU B 98 3121 3520 3235 92 -9 -311 C ATOM 3034 CG GLU B 98 46.265 27.242 34.617 1.00 35.43 C ANISOU 3034 CG GLU B 98 4315 4707 4440 85 -8 -310 C ATOM 3035 CD GLU B 98 46.663 28.619 34.149 1.00 45.98 C ANISOU 3035 CD GLU B 98 5645 6053 5773 75 -9 -312 C ATOM 3036 OE1 GLU B 98 46.978 29.461 35.013 1.00 46.37 O ANISOU 3036 OE1 GLU B 98 5700 6111 5809 72 -2 -308 O ATOM 3037 OE2 GLU B 98 46.661 28.864 32.927 1.00 53.13 O ANISOU 3037 OE2 GLU B 98 6540 6957 6690 70 -16 -317 O ATOM 3038 N ASP B 99 50.100 24.848 36.316 1.00 23.44 N ANISOU 3038 N ASP B 99 2775 3227 2906 113 -34 -333 N ATOM 3039 CA ASP B 99 50.891 24.539 37.503 1.00 20.72 C ANISOU 3039 CA ASP B 99 2427 2901 2546 122 -35 -337 C ATOM 3040 C ASP B 99 52.231 23.932 37.121 1.00 25.45 C ANISOU 3040 C ASP B 99 3014 3508 3149 128 -50 -347 C ATOM 3041 O ASP B 99 52.290 22.970 36.348 1.00 24.03 O ANISOU 3041 O ASP B 99 2825 3322 2985 135 -62 -357 O ATOM 3042 CB ASP B 99 50.127 23.596 38.443 1.00 18.08 C ANISOU 3042 CB ASP B 99 2090 2571 2208 135 -31 -342 C ATOM 3043 CG ASP B 99 48.985 24.300 39.180 1.00 26.86 C ANISOU 3043 CG ASP B 99 3214 3682 3310 131 -14 -331 C ATOM 3044 OD1 ASP B 99 49.271 25.088 40.106 1.00 31.24 O ANISOU 3044 OD1 ASP B 99 3775 4247 3846 126 -5 -323 O ATOM 3045 OD2 ASP B 99 47.808 24.094 38.817 1.00 31.17 O ANISOU 3045 OD2 ASP B 99 3762 4213 3867 131 -8 -329 O ATOM 3046 N LYS B 100 53.301 24.486 37.696 1.00 22.49 N ANISOU 3046 N LYS B 100 2638 3145 2761 126 -48 -344 N ATOM 3047 CA LYS B 100 54.649 24.042 37.357 1.00 24.97 C ANISOU 3047 CA LYS B 100 2941 3469 3079 132 -60 -351 C ATOM 3048 C LYS B 100 54.832 22.565 37.657 1.00 14.74 C ANISOU 3048 C LYS B 100 1634 2181 1785 149 -73 -366 C ATOM 3049 O LYS B 100 55.339 21.813 36.820 1.00 18.66 O ANISOU 3049 O LYS B 100 2121 2673 2295 155 -86 -375 O ATOM 3050 CB LYS B 100 55.675 24.880 38.132 1.00 29.66 C ANISOU 3050 CB LYS B 100 3538 4075 3656 127 -55 -344 C ATOM 3051 CG LYS B 100 57.136 24.526 37.875 1.00 44.43 C ANISOU 3051 CG LYS B 100 5397 5955 5529 133 -64 -350 C ATOM 3052 CD LYS B 100 57.542 24.797 36.436 1.00 56.21 C ANISOU 3052 CD LYS B 100 6883 7435 7038 128 -69 -349 C ATOM 3053 CE LYS B 100 58.971 24.334 36.155 1.00 56.88 C ANISOU 3053 CE LYS B 100 6955 7530 7126 136 -78 -356 C ATOM 3054 NZ LYS B 100 59.309 24.452 34.705 1.00 56.54 N ANISOU 3054 NZ LYS B 100 6910 7476 7097 133 -81 -357 N ATOM 3055 N HIS B 101 54.376 22.123 38.820 1.00 16.65 N ANISOU 3055 N HIS B 101 1878 2433 2014 158 -68 -367 N ATOM 3056 CA HIS B 101 54.536 20.749 39.269 1.00 23.53 C ANISOU 3056 CA HIS B 101 2741 3312 2886 177 -78 -380 C ATOM 3057 C HIS B 101 53.182 20.067 39.360 1.00 18.12 C ANISOU 3057 C HIS B 101 2058 2614 2213 185 -72 -380 C ATOM 3058 O HIS B 101 52.154 20.720 39.541 1.00 22.92 O ANISOU 3058 O HIS B 101 2675 3216 2819 177 -58 -370 O ATOM 3059 CB HIS B 101 55.223 20.720 40.635 1.00 30.85 C ANISOU 3059 CB HIS B 101 3666 4265 3789 186 -74 -378 C ATOM 3060 CG HIS B 101 56.494 21.502 40.668 1.00 35.76 C ANISOU 3060 CG HIS B 101 4287 4897 4402 178 -76 -374 C ATOM 3061 ND1 HIS B 101 57.622 21.121 39.977 1.00 39.40 N ANISOU 3061 ND1 HIS B 101 4737 5360 4872 182 -88 -381 N ATOM 3062 CD2 HIS B 101 56.802 22.671 41.277 1.00 38.10 C ANISOU 3062 CD2 HIS B 101 4592 5201 4684 165 -64 -362 C ATOM 3063 CE1 HIS B 101 58.577 22.011 40.176 1.00 36.62 C ANISOU 3063 CE1 HIS B 101 4387 5016 4512 173 -83 -374 C ATOM 3064 NE2 HIS B 101 58.104 22.964 40.958 1.00 39.17 N ANISOU 3064 NE2 HIS B 101 4722 5340 4821 163 -69 -362 N ATOM 3065 N ALA B 102 53.198 18.736 39.280 1.00 19.19 N ANISOU 3065 N ALA B 102 2185 2741 2365 202 -80 -388 N ATOM 3066 CA ALA B 102 51.981 17.966 39.493 1.00 20.19 C ANISOU 3066 CA ALA B 102 2306 2852 2514 214 -72 -379 C ATOM 3067 C ALA B 102 51.421 18.242 40.884 1.00 24.94 C ANISOU 3067 C ALA B 102 2905 3471 3100 222 -55 -365 C ATOM 3068 O ALA B 102 52.166 18.449 41.843 1.00 21.20 O ANISOU 3068 O ALA B 102 2429 3023 2602 227 -53 -363 O ATOM 3069 CB ALA B 102 52.252 16.470 39.324 1.00 13.80 C ANISOU 3069 CB ALA B 102 1482 2027 1734 231 -86 -378 C ATOM 3070 N ILE B 103 50.100 18.263 40.985 1.00 22.68 N ANISOU 3070 N ILE B 103 2618 3172 2826 222 -43 -353 N ATOM 3071 CA ILE B 103 49.430 18.416 42.268 1.00 12.28 C ANISOU 3071 CA ILE B 103 1296 1871 1497 230 -27 -336 C ATOM 3072 C ILE B 103 49.145 17.018 42.804 1.00 19.83 C ANISOU 3072 C ILE B 103 2241 2811 2482 239 -36 -306 C ATOM 3073 O ILE B 103 48.507 16.208 42.125 1.00 21.18 O ANISOU 3073 O ILE B 103 2405 2955 2687 243 -43 -302 O ATOM 3074 CB ILE B 103 48.138 19.230 42.112 1.00 12.81 C ANISOU 3074 CB ILE B 103 1376 1928 1563 217 -11 -330 C ATOM 3075 CG1 ILE B 103 48.464 20.690 41.758 1.00 24.25 C ANISOU 3075 CG1 ILE B 103 2847 3382 2986 194 -9 -337 C ATOM 3076 CG2 ILE B 103 47.323 19.175 43.379 1.00 11.72 C ANISOU 3076 CG2 ILE B 103 1236 1798 1418 221 2 -303 C ATOM 3077 CD1 ILE B 103 49.646 21.278 42.520 1.00 32.36 C ANISOU 3077 CD1 ILE B 103 3880 4434 3983 190 -11 -338 C ATOM 3078 N ILE B 104 49.608 16.735 44.019 1.00 17.37 N ANISOU 3078 N ILE B 104 1929 2516 2156 243 -36 -285 N ATOM 3079 CA ILE B 104 49.402 15.444 44.666 1.00 24.21 C ANISOU 3079 CA ILE B 104 2784 3370 3045 252 -44 -254 C ATOM 3080 C ILE B 104 48.223 15.581 45.616 1.00 24.12 C ANISOU 3080 C ILE B 104 2777 3358 3031 249 -29 -224 C ATOM 3081 O ILE B 104 48.227 16.455 46.491 1.00 22.87 O ANISOU 3081 O ILE B 104 2627 3223 2839 245 -16 -220 O ATOM 3082 CB ILE B 104 50.656 14.979 45.421 1.00 24.74 C ANISOU 3082 CB ILE B 104 2847 3456 3098 260 -54 -247 C ATOM 3083 CG1 ILE B 104 51.901 15.112 44.534 1.00 23.76 C ANISOU 3083 CG1 ILE B 104 2721 3338 2968 262 -67 -279 C ATOM 3084 CG2 ILE B 104 50.445 13.565 45.940 1.00 19.55 C ANISOU 3084 CG2 ILE B 104 2177 2781 2470 270 -64 -215 C ATOM 3085 CD1 ILE B 104 51.816 14.364 43.214 1.00 22.07 C ANISOU 3085 CD1 ILE B 104 2499 3095 2791 266 -80 -294 C ATOM 3086 N VAL B 105 47.197 14.750 45.421 1.00 14.33 N ANISOU 3086 N VAL B 105 1530 2090 1825 252 -31 -206 N ATOM 3087 CA VAL B 105 45.995 14.832 46.248 1.00 21.73 C ANISOU 3087 CA VAL B 105 2469 3025 2763 249 -17 -177 C ATOM 3088 C VAL B 105 46.309 14.368 47.665 1.00 20.14 C ANISOU 3088 C VAL B 105 2264 2840 2549 255 -16 -146 C ATOM 3089 O VAL B 105 47.098 13.437 47.874 1.00 19.83 O ANISOU 3089 O VAL B 105 2216 2799 2521 264 -30 -138 O ATOM 3090 CB VAL B 105 44.860 14.007 45.618 1.00 19.82 C ANISOU 3090 CB VAL B 105 2219 2748 2562 250 -20 -165 C ATOM 3091 CG1 VAL B 105 43.621 14.070 46.467 1.00 23.27 C ANISOU 3091 CG1 VAL B 105 2658 3183 3000 247 -5 -134 C ATOM 3092 CG2 VAL B 105 44.573 14.494 44.181 1.00 16.32 C ANISOU 3092 CG2 VAL B 105 1779 2291 2130 244 -21 -197 C ATOM 3093 N GLU B 106 45.741 15.050 48.654 1.00 20.33 N ANISOU 3093 N GLU B 106 2295 2881 2548 251 0 -130 N ATOM 3094 CA GLU B 106 46.012 14.657 50.025 1.00 23.06 C ANISOU 3094 CA GLU B 106 2638 3245 2880 258 2 -100 C ATOM 3095 C GLU B 106 45.433 13.267 50.292 1.00 22.55 C ANISOU 3095 C GLU B 106 2560 3156 2853 266 -6 -67 C ATOM 3096 O GLU B 106 44.440 12.873 49.672 1.00 16.38 O ANISOU 3096 O GLU B 106 1775 2347 2102 264 -5 -62 O ATOM 3097 CB GLU B 106 45.453 15.672 51.017 1.00 23.78 C ANISOU 3097 CB GLU B 106 2739 3359 2938 252 21 -90 C ATOM 3098 CG GLU B 106 43.994 16.032 50.854 1.00 33.86 C ANISOU 3098 CG GLU B 106 4020 4621 4225 246 35 -81 C ATOM 3099 CD GLU B 106 43.577 17.127 51.825 1.00 47.71 C ANISOU 3099 CD GLU B 106 5785 6401 5942 241 54 -74 C ATOM 3100 OE1 GLU B 106 44.434 17.577 52.612 1.00 56.88 O ANISOU 3100 OE1 GLU B 106 6950 7591 7071 242 55 -77 O ATOM 3101 OE2 GLU B 106 42.399 17.532 51.818 1.00 54.18 O ANISOU 3101 OE2 GLU B 106 6608 7212 6764 236 67 -66 O ATOM 3102 N PRO B 107 46.045 12.506 51.211 1.00 21.14 N ANISOU 3102 N PRO B 107 2373 2987 2672 274 -12 -44 N ATOM 3103 CA PRO B 107 45.693 11.083 51.361 1.00 23.13 C ANISOU 3103 CA PRO B 107 2612 3215 2963 283 -22 -14 C ATOM 3104 C PRO B 107 44.214 10.795 51.573 1.00 27.63 C ANISOU 3104 C PRO B 107 3179 3765 3554 280 -12 12 C ATOM 3105 O PRO B 107 43.703 9.825 51.007 1.00 32.34 O ANISOU 3105 O PRO B 107 3766 4331 4192 283 -21 21 O ATOM 3106 CB PRO B 107 46.523 10.657 52.582 1.00 26.37 C ANISOU 3106 CB PRO B 107 3016 3648 3355 292 -25 8 C ATOM 3107 CG PRO B 107 47.703 11.588 52.573 1.00 27.08 C ANISOU 3107 CG PRO B 107 3115 3768 3407 289 -26 -21 C ATOM 3108 CD PRO B 107 47.167 12.897 52.088 1.00 22.23 C ANISOU 3108 CD PRO B 107 2514 3159 2773 277 -12 -45 C ATOM 3109 N GLU B 108 43.510 11.590 52.373 1.00 21.44 N ANISOU 3109 N GLU B 108 2402 2998 2745 276 5 25 N ATOM 3110 CA GLU B 108 42.120 11.257 52.665 1.00 30.01 C ANISOU 3110 CA GLU B 108 3484 4067 3851 274 14 54 C ATOM 3111 C GLU B 108 41.207 11.424 51.455 1.00 30.08 C ANISOU 3111 C GLU B 108 3495 4049 3885 267 15 37 C ATOM 3112 O GLU B 108 40.086 10.911 51.477 1.00 27.15 O ANISOU 3112 O GLU B 108 3118 3656 3540 266 19 59 O ATOM 3113 CB GLU B 108 41.601 12.102 53.835 1.00 35.47 C ANISOU 3113 CB GLU B 108 4184 4786 4508 272 32 72 C ATOM 3114 CG GLU B 108 41.714 13.607 53.629 1.00 55.68 C ANISOU 3114 CG GLU B 108 6758 7366 7030 263 44 41 C ATOM 3115 CD GLU B 108 43.090 14.156 53.989 1.00 71.51 C ANISOU 3115 CD GLU B 108 8768 9402 9000 264 41 22 C ATOM 3116 OE1 GLU B 108 44.052 13.361 54.109 1.00 71.87 O ANISOU 3116 OE1 GLU B 108 8806 9449 9053 272 27 26 O ATOM 3117 OE2 GLU B 108 43.205 15.390 54.149 1.00 76.08 O ANISOU 3117 OE2 GLU B 108 9359 10002 9544 258 53 4 O ATOM 3118 N LYS B 109 41.649 12.124 50.411 1.00 30.85 N ANISOU 3118 N LYS B 109 3600 4146 3975 262 12 -1 N ATOM 3119 CA LYS B 109 40.834 12.344 49.224 1.00 22.54 C ANISOU 3119 CA LYS B 109 2550 3071 2944 255 14 -20 C ATOM 3120 C LYS B 109 41.359 11.590 48.006 1.00 25.63 C ANISOU 3120 C LYS B 109 2934 3438 3366 258 -5 -41 C ATOM 3121 O LYS B 109 40.913 11.849 46.882 1.00 30.58 O ANISOU 3121 O LYS B 109 3562 4048 4007 252 -5 -63 O ATOM 3122 CB LYS B 109 40.744 13.845 48.916 1.00 19.72 C ANISOU 3122 CB LYS B 109 2208 2732 2554 246 27 -47 C ATOM 3123 CG LYS B 109 40.074 14.656 50.003 1.00 22.81 C ANISOU 3123 CG LYS B 109 2607 3144 2916 242 47 -29 C ATOM 3124 CD LYS B 109 40.079 16.137 49.673 1.00 34.07 C ANISOU 3124 CD LYS B 109 4048 4587 4310 233 59 -57 C ATOM 3125 CE LYS B 109 39.491 16.962 50.815 1.00 44.99 C ANISOU 3125 CE LYS B 109 5439 5993 5661 231 78 -40 C ATOM 3126 NZ LYS B 109 38.108 16.545 51.145 1.00 47.92 N ANISOU 3126 NZ LYS B 109 5805 6348 6052 231 87 -9 N ATOM 3127 N ARG B 110 42.286 10.657 48.199 1.00 23.75 N ANISOU 3127 N ARG B 110 2687 3198 3139 266 -19 -35 N ATOM 3128 CA ARG B 110 42.939 9.989 47.083 1.00 23.05 C ANISOU 3128 CA ARG B 110 2591 3090 3077 270 -37 -57 C ATOM 3129 C ARG B 110 42.086 8.898 46.467 1.00 30.14 C ANISOU 3129 C ARG B 110 3478 3951 4022 272 -45 -46 C ATOM 3130 O ARG B 110 41.573 8.024 47.168 1.00 39.40 O ANISOU 3130 O ARG B 110 4642 5112 5215 276 -46 -12 O ATOM 3131 CB ARG B 110 44.258 9.371 47.517 1.00 29.33 C ANISOU 3131 CB ARG B 110 3381 3897 3867 280 -50 -55 C ATOM 3132 CG ARG B 110 45.411 10.233 47.231 1.00 36.31 C ANISOU 3132 CG ARG B 110 4273 4805 4718 278 -52 -86 C ATOM 3133 CD ARG B 110 46.644 9.632 47.779 1.00 31.26 C ANISOU 3133 CD ARG B 110 3628 4179 4072 287 -63 -80 C ATOM 3134 NE ARG B 110 47.539 10.719 48.125 1.00 34.19 N ANISOU 3134 NE ARG B 110 4008 4584 4399 284 -57 -98 N ATOM 3135 CZ ARG B 110 48.622 10.569 48.858 1.00 27.45 C ANISOU 3135 CZ ARG B 110 3152 3752 3525 290 -63 -93 C ATOM 3136 NH1 ARG B 110 48.935 9.366 49.319 1.00 20.39 N ANISOU 3136 NH1 ARG B 110 2246 2849 2652 300 -73 -69 N ATOM 3137 NH2 ARG B 110 49.366 11.624 49.142 1.00 34.62 N ANISOU 3137 NH2 ARG B 110 4070 4691 4394 286 -57 -111 N ATOM 3138 N GLY B 111 41.965 8.950 45.142 1.00 22.56 N ANISOU 3138 N GLY B 111 2518 2972 3080 269 -52 -74 N ATOM 3139 CA GLY B 111 41.503 7.840 44.346 1.00 23.53 C ANISOU 3139 CA GLY B 111 2630 3061 3250 272 -65 -72 C ATOM 3140 C GLY B 111 42.613 7.320 43.449 1.00 21.11 C ANISOU 3140 C GLY B 111 2318 2747 2956 278 -83 -99 C ATOM 3141 O GLY B 111 43.793 7.627 43.627 1.00 18.73 O ANISOU 3141 O GLY B 111 2020 2468 2630 281 -87 -112 O ATOM 3142 N LYS B 112 42.220 6.511 42.471 1.00 21.92 N ANISOU 3142 N LYS B 112 2411 2818 3098 279 -95 -107 N ATOM 3143 CA LYS B 112 43.205 5.762 41.692 1.00 24.27 C ANISOU 3143 CA LYS B 112 2702 3105 3415 287 -114 -127 C ATOM 3144 C LYS B 112 43.579 6.414 40.360 1.00 17.89 C ANISOU 3144 C LYS B 112 1899 2299 2601 284 -118 -170 C ATOM 3145 O LYS B 112 44.398 5.856 39.627 1.00 17.01 O ANISOU 3145 O LYS B 112 1786 2179 2499 287 -132 -187 O ATOM 3146 CB LYS B 112 42.711 4.321 41.474 1.00 32.22 C ANISOU 3146 CB LYS B 112 3695 4076 4471 293 -126 -110 C ATOM 3147 CG LYS B 112 41.399 4.198 40.715 1.00 44.10 C ANISOU 3147 CG LYS B 112 5196 5554 6004 286 -124 -112 C ATOM 3148 CD LYS B 112 40.914 2.742 40.662 1.00 48.46 C ANISOU 3148 CD LYS B 112 5736 6072 6602 290 -135 -90 C ATOM 3149 CE LYS B 112 39.509 2.648 40.075 1.00 50.68 C ANISOU 3149 CE LYS B 112 6020 6331 6904 279 -129 -87 C ATOM 3150 NZ LYS B 112 39.000 1.251 39.972 1.00 55.70 N ANISOU 3150 NZ LYS B 112 6650 6935 7579 277 -138 -67 N ATOM 3151 N TYR B 113 43.011 7.570 40.020 1.00 15.78 N ANISOU 3151 N TYR B 113 1641 2042 2312 274 -105 -184 N ATOM 3152 CA TYR B 113 43.176 8.125 38.684 1.00 15.89 C ANISOU 3152 CA TYR B 113 1663 2053 2319 267 -107 -219 C ATOM 3153 C TYR B 113 44.120 9.320 38.667 1.00 16.14 C ANISOU 3153 C TYR B 113 1706 2116 2309 264 -101 -242 C ATOM 3154 O TYR B 113 44.243 10.059 39.647 1.00 16.46 O ANISOU 3154 O TYR B 113 1750 2183 2322 265 -90 -234 O ATOM 3155 CB TYR B 113 41.822 8.526 38.087 1.00 17.23 C ANISOU 3155 CB TYR B 113 1838 2210 2499 256 -96 -220 C ATOM 3156 CG TYR B 113 40.975 7.327 37.738 1.00 11.32 C ANISOU 3156 CG TYR B 113 1082 1427 1791 255 -104 -204 C ATOM 3157 CD1 TYR B 113 39.924 6.930 38.556 1.00 20.90 C ANISOU 3157 CD1 TYR B 113 2284 2630 3028 260 -98 -174 C ATOM 3158 CD2 TYR B 113 41.258 6.562 36.615 1.00 15.76 C ANISOU 3158 CD2 TYR B 113 1650 1969 2369 249 -117 -217 C ATOM 3159 CE1 TYR B 113 39.164 5.829 38.248 1.00 22.65 C ANISOU 3159 CE1 TYR B 113 2500 2820 3285 257 -105 -159 C ATOM 3160 CE2 TYR B 113 40.496 5.454 36.291 1.00 17.34 C ANISOU 3160 CE2 TYR B 113 1844 2140 2604 247 -123 -204 C ATOM 3161 CZ TYR B 113 39.458 5.095 37.109 1.00 22.95 C ANISOU 3161 CZ TYR B 113 2544 2840 3337 251 -118 -175 C ATOM 3162 OH TYR B 113 38.712 3.999 36.796 1.00 15.38 O ANISOU 3162 OH TYR B 113 1580 1852 2413 248 -125 -162 O ATOM 3163 N VAL B 114 44.780 9.487 37.522 1.00 13.92 N ANISOU 3163 N VAL B 114 1437 1832 2019 255 -107 -267 N ATOM 3164 CA VAL B 114 45.656 10.616 37.213 1.00 15.50 C ANISOU 3164 CA VAL B 114 1651 2057 2182 248 -103 -292 C ATOM 3165 C VAL B 114 44.988 11.450 36.127 1.00 14.21 C ANISOU 3165 C VAL B 114 1501 1887 2009 232 -96 -308 C ATOM 3166 O VAL B 114 44.586 10.906 35.091 1.00 16.28 O ANISOU 3166 O VAL B 114 1766 2126 2292 226 -103 -314 O ATOM 3167 CB VAL B 114 47.030 10.104 36.741 1.00 20.72 C ANISOU 3167 CB VAL B 114 2314 2719 2839 250 -118 -306 C ATOM 3168 CG1 VAL B 114 47.924 11.251 36.355 1.00 17.71 C ANISOU 3168 CG1 VAL B 114 1947 2361 2421 241 -115 -330 C ATOM 3169 CG2 VAL B 114 47.662 9.217 37.822 1.00 16.78 C ANISOU 3169 CG2 VAL B 114 1801 2225 2349 265 -126 -286 C ATOM 3170 N VAL B 115 44.884 12.770 36.335 1.00 11.51 N ANISOU 3170 N VAL B 115 1169 1567 1637 226 -82 -317 N ATOM 3171 CA VAL B 115 44.230 13.635 35.359 1.00 10.33 C ANISOU 3171 CA VAL B 115 1033 1413 1478 210 -75 -329 C ATOM 3172 C VAL B 115 45.218 14.705 34.913 1.00 19.70 C ANISOU 3172 C VAL B 115 2234 2621 2631 200 -75 -349 C ATOM 3173 O VAL B 115 45.825 15.384 35.751 1.00 19.48 O ANISOU 3173 O VAL B 115 2209 2617 2577 203 -69 -350 O ATOM 3174 CB VAL B 115 42.946 14.269 35.923 1.00 13.45 C ANISOU 3174 CB VAL B 115 1428 1811 1872 209 -57 -316 C ATOM 3175 CG1 VAL B 115 42.141 14.949 34.801 1.00 16.82 C ANISOU 3175 CG1 VAL B 115 1867 2228 2295 193 -52 -324 C ATOM 3176 CG2 VAL B 115 42.098 13.222 36.652 1.00 18.88 C ANISOU 3176 CG2 VAL B 115 2099 2483 2592 221 -57 -291 C ATOM 3177 N CYS B 116 45.412 14.824 33.601 1.00 16.39 N ANISOU 3177 N CYS B 116 1822 2192 2211 187 -85 -363 N ATOM 3178 CA CYS B 116 46.158 15.928 33.004 1.00 17.49 C ANISOU 3178 CA CYS B 116 1974 2350 2323 174 -87 -377 C ATOM 3179 C CYS B 116 45.158 16.783 32.255 1.00 18.80 C ANISOU 3179 C CYS B 116 2146 2511 2485 159 -80 -374 C ATOM 3180 O CYS B 116 44.377 16.251 31.463 1.00 15.69 O ANISOU 3180 O CYS B 116 1751 2098 2112 156 -83 -373 O ATOM 3181 CB CYS B 116 47.231 15.447 32.026 1.00 13.75 C ANISOU 3181 CB CYS B 116 1500 1875 1852 170 -105 -391 C ATOM 3182 SG CYS B 116 48.286 14.101 32.616 1.00 18.78 S ANISOU 3182 SG CYS B 116 2127 2507 2502 188 -117 -393 S ATOM 3183 N PHE B 117 45.185 18.094 32.480 1.00 13.51 N ANISOU 3183 N PHE B 117 1485 1859 1790 149 -70 -370 N ATOM 3184 CA PHE B 117 44.188 18.932 31.835 1.00 10.67 C ANISOU 3184 CA PHE B 117 1132 1494 1428 136 -62 -363 C ATOM 3185 C PHE B 117 44.752 20.315 31.527 1.00 18.65 C ANISOU 3185 C PHE B 117 2149 2521 2416 123 -60 -359 C ATOM 3186 O PHE B 117 45.735 20.769 32.123 1.00 15.93 O ANISOU 3186 O PHE B 117 1805 2193 2055 124 -60 -359 O ATOM 3187 CB PHE B 117 42.902 19.037 32.681 1.00 12.83 C ANISOU 3187 CB PHE B 117 1407 1761 1705 141 -44 -351 C ATOM 3188 CG PHE B 117 43.114 19.629 34.054 1.00 16.26 C ANISOU 3188 CG PHE B 117 1845 2214 2119 147 -31 -345 C ATOM 3189 CD1 PHE B 117 43.050 21.012 34.254 1.00 16.03 C ANISOU 3189 CD1 PHE B 117 1827 2197 2065 135 -21 -338 C ATOM 3190 CD2 PHE B 117 43.359 18.809 35.141 1.00 17.46 C ANISOU 3190 CD2 PHE B 117 1986 2370 2277 163 -29 -343 C ATOM 3191 CE1 PHE B 117 43.238 21.560 35.508 1.00 20.42 C ANISOU 3191 CE1 PHE B 117 2388 2770 2602 138 -9 -332 C ATOM 3192 CE2 PHE B 117 43.551 19.347 36.407 1.00 20.02 C ANISOU 3192 CE2 PHE B 117 2312 2714 2579 169 -17 -337 C ATOM 3193 CZ PHE B 117 43.487 20.731 36.590 1.00 26.16 C ANISOU 3193 CZ PHE B 117 3105 3506 3331 155 -7 -333 C ATOM 3194 N ASP B 118 44.141 20.951 30.528 1.00 15.01 N ANISOU 3194 N ASP B 118 1692 2055 1958 111 -58 -352 N ATOM 3195 CA ASP B 118 44.360 22.356 30.219 1.00 16.47 C ANISOU 3195 CA ASP B 118 1883 2249 2127 99 -52 -341 C ATOM 3196 C ASP B 118 43.049 23.071 30.521 1.00 13.53 C ANISOU 3196 C ASP B 118 1521 1870 1751 95 -36 -329 C ATOM 3197 O ASP B 118 42.093 22.962 29.740 1.00 17.17 O ANISOU 3197 O ASP B 118 1983 2319 2223 91 -35 -327 O ATOM 3198 CB ASP B 118 44.762 22.515 28.748 1.00 25.39 C ANISOU 3198 CB ASP B 118 3001 3381 3265 92 -66 -346 C ATOM 3199 CG ASP B 118 45.477 23.814 28.465 1.00 28.32 C ANISOU 3199 CG ASP B 118 3365 3771 3626 86 -67 -347 C ATOM 3200 OD1 ASP B 118 45.074 24.855 29.022 1.00 30.30 O ANISOU 3200 OD1 ASP B 118 3623 4026 3865 81 -54 -339 O ATOM 3201 OD2 ASP B 118 46.464 23.787 27.696 1.00 33.49 O ANISOU 3201 OD2 ASP B 118 4016 4426 4281 87 -72 -346 O ATOM 3202 N PRO B 119 42.940 23.795 31.638 1.00 19.61 N ANISOU 3202 N PRO B 119 2300 2648 2505 95 -22 -322 N ATOM 3203 CA PRO B 119 41.610 24.222 32.100 1.00 16.16 C ANISOU 3203 CA PRO B 119 1871 2203 2065 94 -7 -312 C ATOM 3204 C PRO B 119 40.936 25.243 31.201 1.00 15.71 C ANISOU 3204 C PRO B 119 1817 2144 2008 82 -4 -307 C ATOM 3205 O PRO B 119 39.706 25.216 31.089 1.00 12.03 O ANISOU 3205 O PRO B 119 1356 1667 1549 82 4 -301 O ATOM 3206 CB PRO B 119 41.886 24.789 33.501 1.00 8.91 C ANISOU 3206 CB PRO B 119 960 1297 1128 97 5 -307 C ATOM 3207 CG PRO B 119 43.322 25.151 33.487 1.00 14.00 C ANISOU 3207 CG PRO B 119 1603 1954 1763 94 -4 -310 C ATOM 3208 CD PRO B 119 43.999 24.149 32.599 1.00 15.43 C ANISOU 3208 CD PRO B 119 1772 2133 1959 98 -21 -322 C ATOM 3209 N LEU B 120 41.681 26.140 30.550 1.00 15.72 N ANISOU 3209 N LEU B 120 1810 2157 2004 74 -13 -313 N ATOM 3210 CA LEU B 120 41.069 27.074 29.600 1.00 15.23 C ANISOU 3210 CA LEU B 120 1745 2097 1946 65 -13 -313 C ATOM 3211 C LEU B 120 42.013 27.280 28.413 1.00 15.72 C ANISOU 3211 C LEU B 120 1789 2169 2014 61 -28 -323 C ATOM 3212 O LEU B 120 42.587 28.349 28.209 1.00 14.52 O ANISOU 3212 O LEU B 120 1632 2028 1856 55 -28 -323 O ATOM 3213 CB LEU B 120 40.695 28.406 30.256 1.00 19.33 C ANISOU 3213 CB LEU B 120 2273 2621 2451 59 0 -305 C ATOM 3214 CG LEU B 120 39.633 29.148 29.439 1.00 14.70 C ANISOU 3214 CG LEU B 120 1686 2030 1869 51 4 -303 C ATOM 3215 CD1 LEU B 120 38.429 28.256 29.267 1.00 13.70 C ANISOU 3215 CD1 LEU B 120 1564 1889 1754 55 7 -300 C ATOM 3216 CD2 LEU B 120 39.238 30.454 30.101 1.00 14.64 C ANISOU 3216 CD2 LEU B 120 1689 2027 1849 46 17 -294 C ATOM 3217 N ASP B 121 42.122 26.241 27.590 1.00 15.17 N ANISOU 3217 N ASP B 121 1711 2094 1959 64 -40 -331 N ATOM 3218 CA ASP B 121 42.944 26.303 26.392 1.00 16.17 C ANISOU 3218 CA ASP B 121 1825 2226 2092 62 -52 -336 C ATOM 3219 C ASP B 121 42.482 27.415 25.463 1.00 17.89 C ANISOU 3219 C ASP B 121 2045 2444 2309 54 -46 -329 C ATOM 3220 O ASP B 121 41.291 27.559 25.191 1.00 15.50 O ANISOU 3220 O ASP B 121 1743 2135 2011 50 -43 -329 O ATOM 3221 CB ASP B 121 42.893 24.964 25.661 1.00 20.89 C ANISOU 3221 CB ASP B 121 2423 2810 2703 67 -60 -338 C ATOM 3222 CG ASP B 121 44.060 24.783 24.743 1.00 30.88 C ANISOU 3222 CG ASP B 121 3689 4075 3968 70 -65 -335 C ATOM 3223 OD1 ASP B 121 43.943 25.195 23.572 1.00 33.73 O ANISOU 3223 OD1 ASP B 121 4051 4432 4331 66 -64 -329 O ATOM 3224 OD2 ASP B 121 45.107 24.293 25.222 1.00 28.95 O ANISOU 3224 OD2 ASP B 121 3444 3834 3721 76 -69 -337 O ATOM 3225 N GLY B 122 43.441 28.182 24.953 1.00 27.64 N ANISOU 3225 N GLY B 122 3281 3685 3538 52 -45 -325 N ATOM 3226 CA GLY B 122 43.174 29.299 24.071 1.00 23.09 C ANISOU 3226 CA GLY B 122 2706 3109 2960 45 -41 -319 C ATOM 3227 C GLY B 122 42.921 30.620 24.765 1.00 24.56 C ANISOU 3227 C GLY B 122 2890 3303 3137 39 -33 -318 C ATOM 3228 O GLY B 122 42.710 31.625 24.079 1.00 26.34 O ANISOU 3228 O GLY B 122 3118 3530 3362 33 -29 -314 O ATOM 3229 N SER B 123 42.969 30.661 26.100 1.00 21.34 N ANISOU 3229 N SER B 123 2296 2854 2957 110 367 -244 N ATOM 3230 CA SER B 123 42.544 31.842 26.845 1.00 23.41 C ANISOU 3230 CA SER B 123 2562 3109 3222 105 375 -244 C ATOM 3231 C SER B 123 43.449 33.043 26.616 1.00 25.09 C ANISOU 3231 C SER B 123 2773 3323 3439 93 385 -253 C ATOM 3232 O SER B 123 43.042 34.176 26.897 1.00 25.91 O ANISOU 3232 O SER B 123 2881 3420 3546 87 393 -252 O ATOM 3233 CB SER B 123 42.494 31.526 28.339 1.00 29.30 C ANISOU 3233 CB SER B 123 3309 3855 3969 108 370 -248 C ATOM 3234 OG SER B 123 43.788 31.214 28.826 1.00 33.97 O ANISOU 3234 OG SER B 123 3894 4452 4560 105 367 -260 O ATOM 3235 N SER B 124 44.657 32.831 26.102 1.00 20.75 N ANISOU 3235 N SER B 124 2216 2780 2887 89 384 -261 N ATOM 3236 CA SER B 124 45.547 33.960 25.874 1.00 28.68 C ANISOU 3236 CA SER B 124 3218 3785 3894 78 393 -270 C ATOM 3237 C SER B 124 44.942 34.972 24.903 1.00 33.13 C ANISOU 3237 C SER B 124 3786 4343 4460 73 402 -263 C ATOM 3238 O SER B 124 45.331 36.146 24.932 1.00 33.60 O ANISOU 3238 O SER B 124 3845 4399 4521 63 411 -268 O ATOM 3239 CB SER B 124 46.909 33.459 25.381 1.00 29.59 C ANISOU 3239 CB SER B 124 3325 3910 4007 76 389 -280 C ATOM 3240 OG SER B 124 46.859 33.113 24.010 1.00 37.67 O ANISOU 3240 OG SER B 124 4347 4936 5028 77 389 -274 O ATOM 3241 N ASN B 125 43.981 34.557 24.068 1.00 32.17 N ANISOU 3241 N ASN B 125 3668 4219 4337 79 400 -252 N ATOM 3242 CA ASN B 125 43.302 35.451 23.134 1.00 31.38 C ANISOU 3242 CA ASN B 125 3572 4113 4238 75 409 -244 C ATOM 3243 C ASN B 125 41.820 35.650 23.462 1.00 36.16 C ANISOU 3243 C ASN B 125 4186 4709 4845 79 410 -233 C ATOM 3244 O ASN B 125 41.057 36.094 22.595 1.00 34.78 O ANISOU 3244 O ASN B 125 4016 4530 4671 78 414 -225 O ATOM 3245 CB ASN B 125 43.442 34.936 21.700 1.00 35.93 C ANISOU 3245 CB ASN B 125 4146 4694 4811 76 407 -240 C ATOM 3246 CG ASN B 125 44.882 34.946 21.205 1.00 43.45 C ANISOU 3246 CG ASN B 125 5091 5654 5762 71 408 -251 C ATOM 3247 OD1 ASN B 125 45.625 35.902 21.431 1.00 40.50 O ANISOU 3247 OD1 ASN B 125 4715 5280 5391 61 415 -259 O ATOM 3248 ND2 ASN B 125 45.273 33.890 20.505 1.00 44.39 N ANISOU 3248 ND2 ASN B 125 5206 5781 5878 76 401 -251 N ATOM 3249 N ILE B 126 41.393 35.354 24.695 1.00 35.79 N ANISOU 3249 N ILE B 126 4140 4659 4798 84 405 -233 N ATOM 3250 CA ILE B 126 39.977 35.460 25.047 1.00 26.88 C ANISOU 3250 CA ILE B 126 3019 3522 3670 88 405 -223 C ATOM 3251 C ILE B 126 39.468 36.898 25.048 1.00 31.54 C ANISOU 3251 C ILE B 126 3615 4103 4265 80 416 -221 C ATOM 3252 O ILE B 126 38.245 37.121 25.070 1.00 23.80 O ANISOU 3252 O ILE B 126 2641 3114 3286 83 418 -212 O ATOM 3253 CB ILE B 126 39.721 34.788 26.415 1.00 31.33 C ANISOU 3253 CB ILE B 126 3584 4086 4234 95 398 -224 C ATOM 3254 CG1 ILE B 126 38.268 34.306 26.511 1.00 29.43 C ANISOU 3254 CG1 ILE B 126 3350 3841 3993 103 393 -213 C ATOM 3255 CG2 ILE B 126 40.065 35.742 27.572 1.00 28.03 C ANISOU 3255 CG2 ILE B 126 3167 3665 3820 88 404 -232 C ATOM 3256 CD1 ILE B 126 37.991 33.430 27.702 1.00 28.29 C ANISOU 3256 CD1 ILE B 126 3205 3697 3846 111 385 -213 C ATOM 3257 N ASP B 127 40.372 37.880 25.036 1.00 25.44 N ANISOU 3257 N ASP B 127 2841 3331 3496 70 424 -229 N ATOM 3258 CA ASP B 127 39.964 39.276 24.943 1.00 29.25 C ANISOU 3258 CA ASP B 127 3328 3804 3983 62 436 -227 C ATOM 3259 C ASP B 127 39.264 39.584 23.629 1.00 27.79 C ANISOU 3259 C ASP B 127 3147 3615 3797 61 440 -218 C ATOM 3260 O ASP B 127 38.516 40.566 23.548 1.00 27.32 O ANISOU 3260 O ASP B 127 3094 3546 3742 57 448 -213 O ATOM 3261 CB ASP B 127 41.175 40.188 25.102 1.00 40.26 C ANISOU 3261 CB ASP B 127 4719 5201 5379 51 443 -238 C ATOM 3262 CG ASP B 127 41.688 40.227 26.520 1.00 58.59 C ANISOU 3262 CG ASP B 127 7037 7522 7701 50 441 -247 C ATOM 3263 OD1 ASP B 127 40.855 40.271 27.450 1.00 60.78 O ANISOU 3263 OD1 ASP B 127 7320 7794 7981 54 440 -243 O ATOM 3264 OD2 ASP B 127 42.929 40.203 26.698 1.00 66.74 O ANISOU 3264 OD2 ASP B 127 8064 8562 8733 46 441 -258 O ATOM 3265 N CYS B 128 39.472 38.773 22.597 1.00 21.48 N ANISOU 3265 N CYS B 128 2345 2823 2995 65 435 -216 N ATOM 3266 CA CYS B 128 38.693 38.933 21.378 1.00 26.37 C ANISOU 3266 CA CYS B 128 2968 3438 3614 65 438 -206 C ATOM 3267 C CYS B 128 37.556 37.934 21.302 1.00 15.39 C ANISOU 3267 C CYS B 128 1581 2047 2221 76 429 -196 C ATOM 3268 O CYS B 128 36.957 37.781 20.234 1.00 17.23 O ANISOU 3268 O CYS B 128 1815 2278 2453 78 429 -188 O ATOM 3269 CB CYS B 128 39.571 38.827 20.126 1.00 22.73 C ANISOU 3269 CB CYS B 128 2502 2985 3151 62 439 -209 C ATOM 3270 SG CYS B 128 40.110 37.170 19.718 1.00 23.33 S ANISOU 3270 SG CYS B 128 2571 3073 3222 71 426 -210 S ATOM 3271 N LEU B 129 37.244 37.259 22.416 1.00 14.64 N ANISOU 3271 N LEU B 129 1486 1951 2125 83 422 -196 N ATOM 3272 CA LEU B 129 36.110 36.333 22.514 1.00 9.47 C ANISOU 3272 CA LEU B 129 835 1296 1468 93 414 -187 C ATOM 3273 C LEU B 129 36.263 35.136 21.584 1.00 19.91 C ANISOU 3273 C LEU B 129 2154 2626 2785 99 406 -185 C ATOM 3274 O LEU B 129 35.271 34.573 21.112 1.00 13.79 O ANISOU 3274 O LEU B 129 1382 1850 2009 106 401 -176 O ATOM 3275 CB LEU B 129 34.767 37.034 22.260 1.00 14.34 C ANISOU 3275 CB LEU B 129 1459 1900 2087 92 419 -177 C ATOM 3276 CG LEU B 129 34.480 38.263 23.110 1.00 20.38 C ANISOU 3276 CG LEU B 129 2230 2656 2858 85 428 -178 C ATOM 3277 CD1 LEU B 129 33.095 38.783 22.771 1.00 24.51 C ANISOU 3277 CD1 LEU B 129 2761 3168 3384 85 432 -168 C ATOM 3278 CD2 LEU B 129 34.581 37.948 24.597 1.00 16.89 C ANISOU 3278 CD2 LEU B 129 1787 2215 2416 88 423 -183 C ATOM 3279 N VAL B 130 37.504 34.747 21.294 1.00 21.88 N ANISOU 3279 N VAL B 130 2396 2885 3033 98 404 -192 N ATOM 3280 CA VAL B 130 37.727 33.518 20.550 1.00 24.66 C ANISOU 3280 CA VAL B 130 2745 3246 3381 105 395 -191 C ATOM 3281 C VAL B 130 37.149 32.344 21.339 1.00 23.08 C ANISOU 3281 C VAL B 130 2545 3047 3177 115 385 -187 C ATOM 3282 O VAL B 130 37.086 32.369 22.574 1.00 17.03 O ANISOU 3282 O VAL B 130 1780 2278 2412 117 383 -190 O ATOM 3283 CB VAL B 130 39.230 33.307 20.286 1.00 20.76 C ANISOU 3283 CB VAL B 130 2242 2760 2885 101 395 -201 C ATOM 3284 CG1 VAL B 130 39.999 33.113 21.606 1.00 15.14 C ANISOU 3284 CG1 VAL B 130 1527 2051 2174 101 392 -210 C ATOM 3285 CG2 VAL B 130 39.468 32.118 19.342 1.00 11.96 C ANISOU 3285 CG2 VAL B 130 1123 1654 1766 108 387 -198 C ATOM 3286 N SER B 131 36.690 31.318 20.618 1.00 14.92 N ANISOU 3286 N SER B 131 1512 2017 2139 123 377 -181 N ATOM 3287 CA SER B 131 36.348 30.059 21.269 1.00 17.80 C ANISOU 3287 CA SER B 131 1878 2386 2502 133 367 -178 C ATOM 3288 C SER B 131 37.493 29.614 22.164 1.00 16.05 C ANISOU 3288 C SER B 131 1649 2169 2279 133 363 -188 C ATOM 3289 O SER B 131 38.667 29.749 21.804 1.00 20.58 O ANISOU 3289 O SER B 131 2218 2748 2853 128 365 -196 O ATOM 3290 CB SER B 131 36.051 28.967 20.228 1.00 19.47 C ANISOU 3290 CB SER B 131 2088 2602 2708 140 359 -172 C ATOM 3291 OG SER B 131 34.903 29.271 19.449 1.00 26.68 O ANISOU 3291 OG SER B 131 3006 3509 3621 141 362 -163 O ATOM 3292 N VAL B 132 37.153 29.117 23.352 1.00 12.25 N ANISOU 3292 N VAL B 132 1171 1687 1798 139 357 -188 N ATOM 3293 CA VAL B 132 38.125 28.500 24.243 1.00 17.34 C ANISOU 3293 CA VAL B 132 1810 2337 2442 140 352 -196 C ATOM 3294 C VAL B 132 37.587 27.136 24.677 1.00 17.91 C ANISOU 3294 C VAL B 132 1884 2411 2510 151 341 -191 C ATOM 3295 O VAL B 132 36.455 26.777 24.362 1.00 13.47 O ANISOU 3295 O VAL B 132 1326 1845 1945 157 338 -182 O ATOM 3296 CB VAL B 132 38.449 29.389 25.462 1.00 18.99 C ANISOU 3296 CB VAL B 132 2019 2542 2654 134 357 -204 C ATOM 3297 CG1 VAL B 132 39.251 30.640 25.024 1.00 14.48 C ANISOU 3297 CG1 VAL B 132 1445 1969 2086 123 367 -211 C ATOM 3298 CG2 VAL B 132 37.166 29.755 26.202 1.00 15.94 C ANISOU 3298 CG2 VAL B 132 1639 2147 2269 137 358 -197 C ATOM 3299 N GLY B 133 38.400 26.382 25.421 1.00 9.64 N ANISOU 3299 N GLY B 133 833 1369 1462 154 334 -198 N ATOM 3300 CA GLY B 133 37.981 25.037 25.782 1.00 16.68 C ANISOU 3300 CA GLY B 133 1725 2262 2350 164 324 -193 C ATOM 3301 C GLY B 133 38.750 24.459 26.951 1.00 21.31 C ANISOU 3301 C GLY B 133 2308 2851 2937 166 318 -201 C ATOM 3302 O GLY B 133 39.743 25.022 27.415 1.00 22.51 O ANISOU 3302 O GLY B 133 2457 3006 3092 159 322 -211 O ATOM 3303 N THR B 134 38.256 23.320 27.444 1.00 15.78 N ANISOU 3303 N THR B 134 1611 2152 2234 175 309 -196 N ATOM 3304 CA THR B 134 38.916 22.547 28.495 1.00 10.32 C ANISOU 3304 CA THR B 134 916 1462 1542 177 302 -203 C ATOM 3305 C THR B 134 39.276 21.181 27.931 1.00 12.41 C ANISOU 3305 C THR B 134 1179 1733 1805 184 294 -201 C ATOM 3306 O THR B 134 38.406 20.506 27.387 1.00 17.22 O ANISOU 3306 O THR B 134 1791 2340 2410 190 290 -191 O ATOM 3307 CB THR B 134 37.999 22.384 29.714 1.00 10.85 C ANISOU 3307 CB THR B 134 988 1525 1609 182 299 -199 C ATOM 3308 OG1 THR B 134 37.585 23.672 30.177 1.00 14.80 O ANISOU 3308 OG1 THR B 134 1491 2019 2112 176 307 -199 O ATOM 3309 CG2 THR B 134 38.734 21.682 30.846 1.00 10.20 C ANISOU 3309 CG2 THR B 134 903 1446 1528 184 292 -206 C ATOM 3310 N ILE B 135 40.542 20.772 28.069 1.00 7.94 N ANISOU 3310 N ILE B 135 606 1172 1239 181 291 -212 N ATOM 3311 CA ILE B 135 41.050 19.500 27.554 1.00 7.85 C ANISOU 3311 CA ILE B 135 592 1165 1226 186 282 -212 C ATOM 3312 C ILE B 135 41.474 18.627 28.724 1.00 11.63 C ANISOU 3312 C ILE B 135 1069 1645 1704 189 274 -218 C ATOM 3313 O ILE B 135 42.079 19.121 29.676 1.00 11.92 O ANISOU 3313 O ILE B 135 1103 1682 1743 185 276 -227 O ATOM 3314 CB ILE B 135 42.240 19.719 26.599 1.00 13.64 C ANISOU 3314 CB ILE B 135 1318 1904 1959 180 285 -220 C ATOM 3315 CG1 ILE B 135 41.898 20.737 25.518 1.00 18.87 C ANISOU 3315 CG1 ILE B 135 1982 2565 2622 175 295 -216 C ATOM 3316 CG2 ILE B 135 42.687 18.403 25.978 1.00 9.46 C ANISOU 3316 CG2 ILE B 135 787 1379 1428 184 277 -220 C ATOM 3317 CD1 ILE B 135 43.110 21.150 24.679 1.00 22.48 C ANISOU 3317 CD1 ILE B 135 2434 3028 3081 167 299 -225 C ATOM 3318 N PHE B 136 41.160 17.331 28.667 1.00 14.18 N ANISOU 3318 N PHE B 136 1394 1969 2025 197 265 -212 N ATOM 3319 CA PHE B 136 41.529 16.461 29.781 1.00 10.25 C ANISOU 3319 CA PHE B 136 895 1471 1527 200 257 -218 C ATOM 3320 C PHE B 136 41.873 15.061 29.285 1.00 17.54 C ANISOU 3320 C PHE B 136 1817 2399 2449 205 248 -217 C ATOM 3321 O PHE B 136 41.297 14.569 28.314 1.00 9.85 O ANISOU 3321 O PHE B 136 845 1423 1473 209 246 -208 O ATOM 3322 CB PHE B 136 40.392 16.377 30.807 1.00 8.33 C ANISOU 3322 CB PHE B 136 658 1222 1283 205 255 -210 C ATOM 3323 CG PHE B 136 39.126 15.784 30.245 1.00 13.79 C ANISOU 3323 CG PHE B 136 1356 1911 1972 213 253 -196 C ATOM 3324 CD1 PHE B 136 38.193 16.588 29.604 1.00 16.87 C ANISOU 3324 CD1 PHE B 136 1751 2298 2362 212 259 -187 C ATOM 3325 CD2 PHE B 136 38.864 14.415 30.364 1.00 7.07 C ANISOU 3325 CD2 PHE B 136 507 1060 1120 220 243 -191 C ATOM 3326 CE1 PHE B 136 37.034 16.052 29.072 1.00 21.08 C ANISOU 3326 CE1 PHE B 136 2290 2829 2892 219 257 -174 C ATOM 3327 CE2 PHE B 136 37.696 13.875 29.837 1.00 14.73 C ANISOU 3327 CE2 PHE B 136 1483 2026 2087 227 241 -177 C ATOM 3328 CZ PHE B 136 36.781 14.698 29.188 1.00 13.57 C ANISOU 3328 CZ PHE B 136 1340 1877 1938 226 248 -169 C ATOM 3329 N GLY B 137 42.791 14.411 29.997 1.00 18.21 N ANISOU 3329 N GLY B 137 1898 2488 2534 205 241 -227 N ATOM 3330 CA GLY B 137 43.133 13.019 29.764 1.00 16.71 C ANISOU 3330 CA GLY B 137 1706 2300 2342 209 231 -228 C ATOM 3331 C GLY B 137 43.273 12.289 31.090 1.00 23.63 C ANISOU 3331 C GLY B 137 2583 3176 3218 212 222 -232 C ATOM 3332 O GLY B 137 43.889 12.819 32.026 1.00 14.30 O ANISOU 3332 O GLY B 137 1399 1997 2039 208 223 -242 O ATOM 3333 N ILE B 138 42.714 11.081 31.186 1.00 16.42 N ANISOU 3333 N ILE B 138 1674 2262 2304 219 214 -226 N ATOM 3334 CA ILE B 138 42.578 10.363 32.452 1.00 18.39 C ANISOU 3334 CA ILE B 138 1925 2509 2553 223 206 -227 C ATOM 3335 C ILE B 138 43.354 9.051 32.372 1.00 24.87 C ANISOU 3335 C ILE B 138 2742 3334 3372 225 195 -234 C ATOM 3336 O ILE B 138 43.090 8.222 31.492 1.00 18.29 O ANISOU 3336 O ILE B 138 1910 2501 2537 229 192 -227 O ATOM 3337 CB ILE B 138 41.097 10.124 32.774 1.00 17.35 C ANISOU 3337 CB ILE B 138 1801 2370 2420 229 206 -213 C ATOM 3338 CG1 ILE B 138 40.391 11.488 32.921 1.00 12.37 C ANISOU 3338 CG1 ILE B 138 1174 1735 1791 227 217 -208 C ATOM 3339 CG2 ILE B 138 40.932 9.191 33.997 1.00 15.25 C ANISOU 3339 CG2 ILE B 138 1537 2102 2154 234 197 -214 C ATOM 3340 CD1 ILE B 138 38.878 11.443 32.718 1.00 15.02 C ANISOU 3340 CD1 ILE B 138 1517 2065 2126 232 218 -193 C ATOM 3341 N TYR B 139 44.313 8.869 33.288 1.00 21.08 N ANISOU 3341 N TYR B 139 2258 2859 2892 223 190 -246 N ATOM 3342 CA TYR B 139 45.095 7.646 33.409 1.00 12.58 C ANISOU 3342 CA TYR B 139 1178 1788 1813 225 179 -254 C ATOM 3343 C TYR B 139 44.791 6.956 34.737 1.00 17.11 C ANISOU 3343 C TYR B 139 1754 2359 2386 229 171 -254 C ATOM 3344 O TYR B 139 44.466 7.603 35.735 1.00 18.56 O ANISOU 3344 O TYR B 139 1941 2541 2572 228 175 -255 O ATOM 3345 CB TYR B 139 46.605 7.934 33.345 1.00 20.24 C ANISOU 3345 CB TYR B 139 2140 2766 2783 219 179 -270 C ATOM 3346 CG TYR B 139 47.081 8.580 32.058 1.00 20.36 C ANISOU 3346 CG TYR B 139 2152 2785 2799 215 186 -271 C ATOM 3347 CD1 TYR B 139 47.480 7.811 30.985 1.00 13.72 C ANISOU 3347 CD1 TYR B 139 1308 1947 1956 216 181 -271 C ATOM 3348 CD2 TYR B 139 47.131 9.968 31.927 1.00 23.17 C ANISOU 3348 CD2 TYR B 139 2507 3140 3157 209 197 -272 C ATOM 3349 CE1 TYR B 139 47.917 8.389 29.808 1.00 10.12 C ANISOU 3349 CE1 TYR B 139 850 1494 1501 212 188 -273 C ATOM 3350 CE2 TYR B 139 47.565 10.561 30.753 1.00 23.91 C ANISOU 3350 CE2 TYR B 139 2597 3236 3251 204 203 -274 C ATOM 3351 CZ TYR B 139 47.960 9.753 29.694 1.00 22.53 C ANISOU 3351 CZ TYR B 139 2420 3066 3075 206 199 -274 C ATOM 3352 OH TYR B 139 48.393 10.319 28.520 1.00 23.61 O ANISOU 3352 OH TYR B 139 2554 3205 3212 202 205 -275 O ATOM 3353 N ARG B 140 44.930 5.638 34.759 1.00 20.42 N ANISOU 3353 N ARG B 140 2175 2781 2804 234 161 -255 N ATOM 3354 CA ARG B 140 44.916 4.902 36.018 1.00 19.95 C ANISOU 3354 CA ARG B 140 2117 2721 2743 237 152 -258 C ATOM 3355 C ARG B 140 46.334 4.858 36.586 1.00 24.38 C ANISOU 3355 C ARG B 140 2670 3290 3303 233 147 -275 C ATOM 3356 O ARG B 140 47.300 4.676 35.840 1.00 24.75 O ANISOU 3356 O ARG B 140 2712 3343 3348 231 146 -283 O ATOM 3357 CB ARG B 140 44.352 3.492 35.804 1.00 27.62 C ANISOU 3357 CB ARG B 140 3093 3690 3713 243 143 -251 C ATOM 3358 CG ARG B 140 44.042 2.709 37.074 1.00 39.06 C ANISOU 3358 CG ARG B 140 4545 5137 5161 247 134 -251 C ATOM 3359 CD ARG B 140 43.143 1.484 36.806 1.00 58.33 C ANISOU 3359 CD ARG B 140 6991 7573 7600 253 127 -240 C ATOM 3360 NE ARG B 140 41.760 1.806 36.431 1.00 72.82 N ANISOU 3360 NE ARG B 140 8832 9399 9436 256 134 -224 N ATOM 3361 CZ ARG B 140 41.202 1.520 35.253 1.00 73.41 C ANISOU 3361 CZ ARG B 140 8909 9471 9511 257 136 -214 C ATOM 3362 NH1 ARG B 140 41.908 0.904 34.310 1.00 78.37 N ANISOU 3362 NH1 ARG B 140 9534 10105 10138 257 132 -219 N ATOM 3363 NH2 ARG B 140 39.933 1.845 35.014 1.00 60.16 N ANISOU 3363 NH2 ARG B 140 7237 7786 7834 260 142 -201 N ATOM 3364 N LYS B 141 46.473 5.113 37.892 1.00 15.34 N ANISOU 3364 N LYS B 141 1525 2145 2159 232 146 -281 N ATOM 3365 CA LYS B 141 47.784 4.972 38.522 1.00 21.86 C ANISOU 3365 CA LYS B 141 2344 2978 2982 230 140 -297 C ATOM 3366 C LYS B 141 48.211 3.514 38.517 1.00 28.08 C ANISOU 3366 C LYS B 141 3132 3771 3767 234 128 -300 C ATOM 3367 O LYS B 141 47.505 2.652 39.041 1.00 27.95 O ANISOU 3367 O LYS B 141 3121 3751 3750 239 121 -294 O ATOM 3368 CB LYS B 141 47.781 5.517 39.947 1.00 28.70 C ANISOU 3368 CB LYS B 141 3211 3844 3850 228 141 -302 C ATOM 3369 CG LYS B 141 49.105 5.323 40.668 1.00 25.80 C ANISOU 3369 CG LYS B 141 2837 3485 3480 225 135 -318 C ATOM 3370 CD LYS B 141 49.020 5.815 42.098 1.00 30.65 C ANISOU 3370 CD LYS B 141 3451 4097 4096 224 136 -322 C ATOM 3371 CE LYS B 141 50.296 5.531 42.878 1.00 30.51 C ANISOU 3371 CE LYS B 141 3428 4088 4076 222 129 -338 C ATOM 3372 NZ LYS B 141 51.523 5.616 42.053 1.00 37.23 N ANISOU 3372 NZ LYS B 141 4272 4947 4925 218 129 -348 N ATOM 3373 N LYS B 142 49.396 3.254 37.969 1.00 42.94 N ANISOU 3373 N LYS B 142 5008 5661 5647 232 124 -311 N ATOM 3374 CA LYS B 142 49.845 1.898 37.680 1.00 50.56 C ANISOU 3374 CA LYS B 142 5972 6630 6608 236 113 -314 C ATOM 3375 C LYS B 142 50.654 1.280 38.813 1.00 57.30 C ANISOU 3375 C LYS B 142 6822 7488 7459 236 103 -326 C ATOM 3376 O LYS B 142 50.640 0.055 38.978 1.00 65.51 O ANISOU 3376 O LYS B 142 7865 8530 8497 241 93 -326 O ATOM 3377 CB LYS B 142 50.693 1.893 36.402 1.00 53.24 C ANISOU 3377 CB LYS B 142 6307 6976 6947 233 114 -319 C ATOM 3378 CG LYS B 142 49.981 2.399 35.154 1.00 62.05 C ANISOU 3378 CG LYS B 142 7425 8087 8065 232 123 -308 C ATOM 3379 CD LYS B 142 48.937 1.407 34.659 1.00 75.08 C ANISOU 3379 CD LYS B 142 9082 9731 9715 238 118 -295 C ATOM 3380 CE LYS B 142 48.379 1.824 33.302 1.00 80.87 C ANISOU 3380 CE LYS B 142 9817 10462 10450 237 126 -285 C ATOM 3381 NZ LYS B 142 47.524 0.764 32.685 1.00 83.27 N ANISOU 3381 NZ LYS B 142 10126 10761 10753 243 122 -273 N ATOM 3382 N SER B 143 51.345 2.093 39.598 1.00 54.00 N ANISOU 3382 N SER B 143 6401 7074 7042 232 106 -337 N ATOM 3383 CA SER B 143 52.232 1.624 40.651 1.00 46.84 C ANISOU 3383 CA SER B 143 5491 6174 6133 232 97 -349 C ATOM 3384 C SER B 143 51.562 1.669 42.021 1.00 42.27 C ANISOU 3384 C SER B 143 4916 5590 5555 234 96 -346 C ATOM 3385 O SER B 143 50.541 2.330 42.229 1.00 44.72 O ANISOU 3385 O SER B 143 5231 5893 5868 234 103 -336 O ATOM 3386 CB SER B 143 53.502 2.471 40.678 1.00 46.10 C ANISOU 3386 CB SER B 143 5388 6087 6039 226 101 -363 C ATOM 3387 OG SER B 143 53.245 3.710 41.318 1.00 47.41 O ANISOU 3387 OG SER B 143 5555 6251 6208 221 111 -363 O ATOM 3388 N THR B 144 52.140 0.922 42.954 1.00 36.40 N ANISOU 3388 N THR B 144 4171 4852 4809 237 86 -355 N ATOM 3389 CA THR B 144 51.721 0.946 44.349 1.00 36.68 C ANISOU 3389 CA THR B 144 4209 4883 4844 238 84 -355 C ATOM 3390 C THR B 144 52.525 1.941 45.190 1.00 33.74 C ANISOU 3390 C THR B 144 3832 4516 4474 233 88 -367 C ATOM 3391 O THR B 144 52.266 2.074 46.391 1.00 37.16 O ANISOU 3391 O THR B 144 4266 4947 4907 233 86 -368 O ATOM 3392 CB THR B 144 51.828 -0.466 44.936 1.00 46.51 C ANISOU 3392 CB THR B 144 5455 6130 6085 244 70 -357 C ATOM 3393 OG1 THR B 144 51.591 -0.426 46.349 1.00 49.69 O ANISOU 3393 OG1 THR B 144 5861 6532 6488 245 67 -359 O ATOM 3394 CG2 THR B 144 53.208 -1.055 44.652 1.00 45.15 C ANISOU 3394 CG2 THR B 144 5278 5969 5910 243 63 -371 C ATOM 3395 N ASP B 145 53.479 2.645 44.586 1.00 31.02 N ANISOU 3395 N ASP B 145 3481 4177 4129 227 93 -376 N ATOM 3396 CA ASP B 145 54.261 3.667 45.271 1.00 34.04 C ANISOU 3396 CA ASP B 145 3858 4563 4513 221 98 -387 C ATOM 3397 C ASP B 145 53.374 4.842 45.685 1.00 26.67 C ANISOU 3397 C ASP B 145 2927 3622 3584 218 109 -379 C ATOM 3398 O ASP B 145 52.242 4.985 45.223 1.00 24.04 O ANISOU 3398 O ASP B 145 2600 3281 3253 220 114 -366 O ATOM 3399 CB ASP B 145 55.376 4.168 44.358 1.00 49.78 C ANISOU 3399 CB ASP B 145 5845 6564 6507 215 102 -396 C ATOM 3400 CG ASP B 145 56.253 3.045 43.834 1.00 60.48 C ANISOU 3400 CG ASP B 145 7196 7926 7857 218 92 -403 C ATOM 3401 OD1 ASP B 145 56.290 1.963 44.460 1.00 62.70 O ANISOU 3401 OD1 ASP B 145 7479 8209 8135 223 81 -405 O ATOM 3402 OD2 ASP B 145 56.892 3.247 42.779 1.00 64.69 O ANISOU 3402 OD2 ASP B 145 7725 8464 8389 215 94 -407 O ATOM 3403 N GLU B 146 53.896 5.686 46.575 1.00 22.05 N ANISOU 3403 N GLU B 146 2339 3040 3000 214 113 -388 N ATOM 3404 CA GLU B 146 53.210 6.936 46.888 1.00 26.46 C ANISOU 3404 CA GLU B 146 2900 3592 3563 210 124 -383 C ATOM 3405 C GLU B 146 53.019 7.761 45.612 1.00 22.27 C ANISOU 3405 C GLU B 146 2369 3059 3034 206 134 -377 C ATOM 3406 O GLU B 146 53.952 7.885 44.811 1.00 22.06 O ANISOU 3406 O GLU B 146 2337 3038 3007 202 135 -384 O ATOM 3407 CB GLU B 146 53.995 7.738 47.932 1.00 21.06 C ANISOU 3407 CB GLU B 146 2211 2912 2879 205 126 -395 C ATOM 3408 CG GLU B 146 53.186 8.856 48.582 1.00 30.68 C ANISOU 3408 CG GLU B 146 3432 4122 4101 202 136 -389 C ATOM 3409 CD GLU B 146 53.982 9.686 49.585 1.00 35.92 C ANISOU 3409 CD GLU B 146 4092 4791 4766 196 139 -401 C ATOM 3410 OE1 GLU B 146 55.120 9.308 49.906 1.00 31.35 O ANISOU 3410 OE1 GLU B 146 3508 4220 4185 195 132 -414 O ATOM 3411 OE2 GLU B 146 53.463 10.720 50.055 1.00 38.83 O ANISOU 3411 OE2 GLU B 146 4462 5154 5138 193 148 -398 O ATOM 3412 N PRO B 147 51.845 8.359 45.402 1.00 23.14 N ANISOU 3412 N PRO B 147 2484 3160 3147 207 142 -364 N ATOM 3413 CA PRO B 147 51.614 9.107 44.156 1.00 19.39 C ANISOU 3413 CA PRO B 147 2010 2683 2674 203 152 -358 C ATOM 3414 C PRO B 147 52.598 10.254 43.999 1.00 18.62 C ANISOU 3414 C PRO B 147 1906 2590 2577 195 160 -369 C ATOM 3415 O PRO B 147 52.993 10.895 44.973 1.00 21.71 O ANISOU 3415 O PRO B 147 2295 2983 2970 191 162 -377 O ATOM 3416 CB PRO B 147 50.169 9.608 44.300 1.00 26.21 C ANISOU 3416 CB PRO B 147 2881 3537 3541 206 159 -344 C ATOM 3417 CG PRO B 147 49.874 9.538 45.756 1.00 30.28 C ANISOU 3417 CG PRO B 147 3399 4051 4057 207 156 -345 C ATOM 3418 CD PRO B 147 50.665 8.380 46.284 1.00 25.39 C ANISOU 3418 CD PRO B 147 2776 3438 3434 210 143 -355 C ATOM 3419 N SER B 148 53.029 10.480 42.759 1.00 24.06 N ANISOU 3419 N SER B 148 2592 3282 3266 192 164 -370 N ATOM 3420 CA SER B 148 54.038 11.495 42.476 1.00 24.43 C ANISOU 3420 CA SER B 148 2633 3334 3315 184 171 -380 C ATOM 3421 C SER B 148 53.888 11.972 41.040 1.00 19.42 C ANISOU 3421 C SER B 148 1998 2698 2681 181 179 -374 C ATOM 3422 O SER B 148 53.111 11.424 40.260 1.00 16.92 O ANISOU 3422 O SER B 148 1687 2379 2365 186 178 -363 O ATOM 3423 CB SER B 148 55.456 10.961 42.695 1.00 30.89 C ANISOU 3423 CB SER B 148 3444 4163 4130 182 163 -396 C ATOM 3424 OG SER B 148 55.797 10.013 41.689 1.00 36.64 O ANISOU 3424 OG SER B 148 4172 4896 4856 185 157 -396 O ATOM 3425 N GLU B 149 54.668 13.003 40.699 1.00 29.12 N ANISOU 3425 N GLU B 149 3222 3931 3911 173 187 -382 N ATOM 3426 CA GLU B 149 54.634 13.556 39.350 1.00 26.40 C ANISOU 3426 CA GLU B 149 2878 3586 3568 170 194 -378 C ATOM 3427 C GLU B 149 54.919 12.498 38.293 1.00 30.20 C ANISOU 3427 C GLU B 149 3357 4071 4045 174 187 -377 C ATOM 3428 O GLU B 149 54.371 12.565 37.185 1.00 31.02 O ANISOU 3428 O GLU B 149 3463 4172 4150 175 192 -368 O ATOM 3429 CB GLU B 149 55.636 14.703 39.240 1.00 24.00 C ANISOU 3429 CB GLU B 149 2568 3287 3265 161 202 -389 C ATOM 3430 CG GLU B 149 55.563 15.479 37.939 1.00 20.94 C ANISOU 3430 CG GLU B 149 2179 2897 2878 156 212 -385 C ATOM 3431 CD GLU B 149 56.215 16.839 38.056 1.00 25.70 C ANISOU 3431 CD GLU B 149 2779 3502 3483 146 222 -393 C ATOM 3432 OE1 GLU B 149 55.850 17.602 38.983 1.00 21.38 O ANISOU 3432 OE1 GLU B 149 2234 2951 2938 144 227 -393 O ATOM 3433 OE2 GLU B 149 57.099 17.139 37.231 1.00 19.70 O ANISOU 3433 OE2 GLU B 149 2014 2748 2722 141 224 -400 O ATOM 3434 N LYS B 150 55.766 11.516 38.614 1.00 25.72 N ANISOU 3434 N LYS B 150 2786 3510 3475 176 177 -386 N ATOM 3435 CA LYS B 150 56.130 10.478 37.654 1.00 23.77 C ANISOU 3435 CA LYS B 150 2537 3268 3225 180 170 -387 C ATOM 3436 C LYS B 150 54.944 9.630 37.218 1.00 21.00 C ANISOU 3436 C LYS B 150 2193 2911 2874 187 166 -372 C ATOM 3437 O LYS B 150 55.007 8.999 36.155 1.00 23.99 O ANISOU 3437 O LYS B 150 2572 3292 3252 190 163 -369 O ATOM 3438 CB LYS B 150 57.221 9.575 38.240 1.00 37.55 C ANISOU 3438 CB LYS B 150 4278 5022 4967 181 158 -400 C ATOM 3439 CG LYS B 150 58.459 10.347 38.674 1.00 53.14 C ANISOU 3439 CG LYS B 150 6246 7004 6942 173 161 -415 C ATOM 3440 CD LYS B 150 59.092 11.094 37.505 1.00 58.92 C ANISOU 3440 CD LYS B 150 6974 7740 7675 167 169 -418 C ATOM 3441 CE LYS B 150 60.292 11.916 37.956 1.00 57.42 C ANISOU 3441 CE LYS B 150 6777 7557 7484 159 172 -433 C ATOM 3442 NZ LYS B 150 61.383 11.060 38.461 1.00 49.69 N ANISOU 3442 NZ LYS B 150 5792 6586 6501 160 161 -446 N ATOM 3443 N ASP B 151 53.872 9.571 38.013 1.00 20.85 N ANISOU 3443 N ASP B 151 2180 2885 2857 191 166 -363 N ATOM 3444 CA ASP B 151 52.714 8.784 37.603 1.00 14.83 C ANISOU 3444 CA ASP B 151 1425 2116 2094 199 163 -349 C ATOM 3445 C ASP B 151 52.008 9.362 36.380 1.00 21.44 C ANISOU 3445 C ASP B 151 2265 2949 2934 197 172 -338 C ATOM 3446 O ASP B 151 51.252 8.638 35.729 1.00 19.55 O ANISOU 3446 O ASP B 151 2029 2705 2693 203 169 -327 O ATOM 3447 CB ASP B 151 51.720 8.663 38.749 1.00 15.76 C ANISOU 3447 CB ASP B 151 1548 2227 2213 203 161 -342 C ATOM 3448 CG ASP B 151 52.228 7.783 39.861 1.00 29.23 C ANISOU 3448 CG ASP B 151 3253 3937 3917 206 150 -350 C ATOM 3449 OD1 ASP B 151 52.643 6.649 39.545 1.00 30.85 O ANISOU 3449 OD1 ASP B 151 3456 4146 4118 209 141 -353 O ATOM 3450 OD2 ASP B 151 52.218 8.219 41.036 1.00 24.71 O ANISOU 3450 OD2 ASP B 151 2680 3364 3345 204 151 -354 O ATOM 3451 N ALA B 152 52.218 10.640 36.063 1.00 12.27 N ANISOU 3451 N ALA B 152 1101 1787 1774 191 183 -340 N ATOM 3452 CA ALA B 152 51.630 11.222 34.862 1.00 16.27 C ANISOU 3452 CA ALA B 152 1610 2290 2282 189 191 -330 C ATOM 3453 C ALA B 152 52.504 11.032 33.633 1.00 17.05 C ANISOU 3453 C ALA B 152 1704 2395 2380 187 191 -335 C ATOM 3454 O ALA B 152 52.059 11.311 32.513 1.00 18.42 O ANISOU 3454 O ALA B 152 1879 2567 2554 186 197 -327 O ATOM 3455 CB ALA B 152 51.365 12.717 35.070 1.00 13.95 C ANISOU 3455 CB ALA B 152 1317 1992 1992 183 204 -329 C ATOM 3456 N LEU B 153 53.716 10.520 33.806 1.00 16.61 N ANISOU 3456 N LEU B 153 1641 2347 2321 185 184 -349 N ATOM 3457 CA LEU B 153 54.629 10.301 32.689 1.00 25.26 C ANISOU 3457 CA LEU B 153 2732 3450 3415 183 183 -355 C ATOM 3458 C LEU B 153 54.327 8.952 32.032 1.00 23.93 C ANISOU 3458 C LEU B 153 2566 3282 3244 190 174 -349 C ATOM 3459 O LEU B 153 55.104 8.003 32.110 1.00 24.51 O ANISOU 3459 O LEU B 153 2636 3361 3314 192 164 -357 O ATOM 3460 CB LEU B 153 56.075 10.387 33.157 1.00 20.90 C ANISOU 3460 CB LEU B 153 2173 2907 2862 178 180 -372 C ATOM 3461 CG LEU B 153 56.557 11.732 33.686 1.00 23.35 C ANISOU 3461 CG LEU B 153 2479 3218 3173 170 189 -379 C ATOM 3462 CD1 LEU B 153 58.003 11.631 34.106 1.00 22.84 C ANISOU 3462 CD1 LEU B 153 2408 3164 3108 166 184 -396 C ATOM 3463 CD2 LEU B 153 56.382 12.827 32.637 1.00 19.92 C ANISOU 3463 CD2 LEU B 153 2045 2781 2741 164 200 -375 C ATOM 3464 N GLN B 154 53.112 8.852 31.482 1.00 19.67 N ANISOU 3464 N GLN B 154 2033 2735 2706 194 177 -334 N ATOM 3465 CA GLN B 154 52.631 7.695 30.729 1.00 18.50 C ANISOU 3465 CA GLN B 154 1888 2586 2557 200 170 -326 C ATOM 3466 C GLN B 154 52.357 8.056 29.270 1.00 16.77 C ANISOU 3466 C GLN B 154 1668 2364 2338 199 177 -318 C ATOM 3467 O GLN B 154 51.946 9.184 28.975 1.00 16.90 O ANISOU 3467 O GLN B 154 1686 2377 2356 195 188 -314 O ATOM 3468 CB GLN B 154 51.353 7.127 31.351 1.00 23.64 C ANISOU 3468 CB GLN B 154 2547 3229 3208 207 167 -313 C ATOM 3469 CG GLN B 154 51.524 6.627 32.755 1.00 26.84 C ANISOU 3469 CG GLN B 154 2951 3634 3612 209 159 -319 C ATOM 3470 CD GLN B 154 50.274 5.941 33.248 1.00 25.28 C ANISOU 3470 CD GLN B 154 2762 3429 3415 216 155 -307 C ATOM 3471 OE1 GLN B 154 49.637 5.197 32.507 1.00 31.41 O ANISOU 3471 OE1 GLN B 154 3541 4202 4190 221 153 -298 O ATOM 3472 NE2 GLN B 154 49.917 6.179 34.504 1.00 21.67 N ANISOU 3472 NE2 GLN B 154 2306 2968 2958 217 155 -307 N ATOM 3473 N PRO B 155 52.552 7.121 28.338 1.00 18.53 N ANISOU 3473 N PRO B 155 1892 2591 2559 202 172 -317 N ATOM 3474 CA PRO B 155 52.164 7.381 26.947 1.00 11.37 C ANISOU 3474 CA PRO B 155 985 1682 1653 201 178 -309 C ATOM 3475 C PRO B 155 50.653 7.426 26.812 1.00 14.14 C ANISOU 3475 C PRO B 155 1343 2023 2005 206 182 -292 C ATOM 3476 O PRO B 155 49.923 6.778 27.564 1.00 16.35 O ANISOU 3476 O PRO B 155 1628 2299 2285 211 176 -286 O ATOM 3477 CB PRO B 155 52.750 6.186 26.187 1.00 18.20 C ANISOU 3477 CB PRO B 155 1848 2553 2515 204 169 -312 C ATOM 3478 CG PRO B 155 52.772 5.100 27.186 1.00 19.34 C ANISOU 3478 CG PRO B 155 1993 2697 2657 209 158 -315 C ATOM 3479 CD PRO B 155 53.115 5.768 28.498 1.00 23.40 C ANISOU 3479 CD PRO B 155 2507 3213 3173 206 159 -323 C ATOM 3480 N GLY B 156 50.186 8.216 25.840 1.00 18.66 N ANISOU 3480 N GLY B 156 1993 2798 2298 219 186 -637 N ATOM 3481 CA GLY B 156 48.760 8.347 25.591 1.00 17.11 C ANISOU 3481 CA GLY B 156 1811 2577 2112 213 188 -625 C ATOM 3482 C GLY B 156 48.066 7.028 25.316 1.00 19.22 C ANISOU 3482 C GLY B 156 2083 2830 2388 227 184 -629 C ATOM 3483 O GLY B 156 46.855 6.919 25.533 1.00 21.19 O ANISOU 3483 O GLY B 156 2347 3054 2649 225 185 -617 O ATOM 3484 N ARG B 157 48.811 6.019 24.859 1.00 18.71 N ANISOU 3484 N ARG B 157 2008 2782 2320 242 180 -647 N ATOM 3485 CA ARG B 157 48.255 4.675 24.712 1.00 25.29 C ANISOU 3485 CA ARG B 157 2845 3602 3162 257 176 -652 C ATOM 3486 C ARG B 157 47.567 4.193 25.981 1.00 23.61 C ANISOU 3486 C ARG B 157 2645 3361 2963 262 176 -638 C ATOM 3487 O ARG B 157 46.625 3.398 25.909 1.00 22.98 O ANISOU 3487 O ARG B 157 2575 3262 2894 268 174 -635 O ATOM 3488 CB ARG B 157 49.354 3.658 24.356 1.00 23.28 C ANISOU 3488 CB ARG B 157 2576 3369 2901 274 172 -672 C ATOM 3489 CG ARG B 157 49.885 3.727 22.951 1.00 35.39 C ANISOU 3489 CG ARG B 157 4096 4927 4423 273 172 -688 C ATOM 3490 CD ARG B 157 48.843 3.384 21.888 1.00 35.49 C ANISOU 3490 CD ARG B 157 4113 4930 4440 273 171 -691 C ATOM 3491 NE ARG B 157 49.392 3.637 20.555 1.00 35.36 N ANISOU 3491 NE ARG B 157 4084 4940 4411 271 171 -705 N ATOM 3492 CZ ARG B 157 48.671 3.881 19.467 1.00 35.02 C ANISOU 3492 CZ ARG B 157 4042 4896 4366 265 172 -707 C ATOM 3493 NH1 ARG B 157 47.343 3.913 19.529 1.00 29.74 N ANISOU 3493 NH1 ARG B 157 3388 4202 3709 261 173 -695 N ATOM 3494 NH2 ARG B 157 49.285 4.114 18.314 1.00 27.75 N ANISOU 3494 NH2 ARG B 157 3109 4001 3433 264 172 -720 N ATOM 3495 N ASN B 158 48.023 4.657 27.146 1.00 14.52 N ANISOU 3495 N ASN B 158 1496 2208 1812 259 177 -629 N ATOM 3496 CA ASN B 158 47.519 4.208 28.440 1.00 13.30 C ANISOU 3496 CA ASN B 158 1354 2030 1670 264 177 -615 C ATOM 3497 C ASN B 158 46.254 4.930 28.881 1.00 19.90 C ANISOU 3497 C ASN B 158 2206 2840 2515 250 180 -595 C ATOM 3498 O ASN B 158 45.782 4.687 30.002 1.00 18.69 O ANISOU 3498 O ASN B 158 2063 2666 2371 253 180 -582 O ATOM 3499 CB ASN B 158 48.601 4.414 29.514 1.00 16.15 C ANISOU 3499 CB ASN B 158 1710 2401 2026 267 177 -615 C ATOM 3500 CG ASN B 158 49.759 3.438 29.374 1.00 21.81 C ANISOU 3500 CG ASN B 158 2413 3138 2736 284 173 -633 C ATOM 3501 OD1 ASN B 158 49.825 2.673 28.410 1.00 23.59 O ANISOU 3501 OD1 ASN B 158 2632 3371 2960 292 170 -646 O ATOM 3502 ND2 ASN B 158 50.681 3.467 30.335 1.00 27.84 N ANISOU 3502 ND2 ASN B 158 3172 3911 3496 288 172 -632 N ATOM 3503 N LEU B 159 45.724 5.849 28.072 1.00 19.47 N ANISOU 3503 N LEU B 159 2154 2787 2457 236 183 -592 N ATOM 3504 CA LEU B 159 44.572 6.624 28.508 1.00 19.11 C ANISOU 3504 CA LEU B 159 2123 2719 2420 223 186 -572 C ATOM 3505 C LEU B 159 43.345 5.741 28.721 1.00 19.21 C ANISOU 3505 C LEU B 159 2148 2704 2446 229 184 -565 C ATOM 3506 O LEU B 159 43.050 4.842 27.934 1.00 21.67 O ANISOU 3506 O LEU B 159 2458 3016 2760 238 182 -575 O ATOM 3507 CB LEU B 159 44.260 7.728 27.502 1.00 16.01 C ANISOU 3507 CB LEU B 159 1729 2333 2020 207 189 -571 C ATOM 3508 CG LEU B 159 45.118 8.989 27.593 1.00 12.44 C ANISOU 3508 CG LEU B 159 1271 1900 1558 194 192 -570 C ATOM 3509 CD1 LEU B 159 45.001 9.788 26.307 1.00 13.53 C ANISOU 3509 CD1 LEU B 159 1404 2050 1687 183 195 -575 C ATOM 3510 CD2 LEU B 159 44.716 9.848 28.820 1.00 15.26 C ANISOU 3510 CD2 LEU B 159 1638 2239 1920 183 195 -550 C ATOM 3511 N VAL B 160 42.628 6.021 29.802 1.00 14.92 N ANISOU 3511 N VAL B 160 1618 2138 1912 224 186 -546 N ATOM 3512 CA VAL B 160 41.356 5.378 30.092 1.00 16.44 C ANISOU 3512 CA VAL B 160 1824 2304 2118 227 185 -536 C ATOM 3513 C VAL B 160 40.197 6.168 29.493 1.00 20.18 C ANISOU 3513 C VAL B 160 2306 2766 2594 212 187 -526 C ATOM 3514 O VAL B 160 39.186 5.586 29.090 1.00 20.83 O ANISOU 3514 O VAL B 160 2396 2835 2685 215 186 -525 O ATOM 3515 CB VAL B 160 41.221 5.236 31.621 1.00 23.31 C ANISOU 3515 CB VAL B 160 2703 3157 2996 229 185 -522 C ATOM 3516 CG1 VAL B 160 39.799 4.950 32.029 1.00 25.87 C ANISOU 3516 CG1 VAL B 160 3043 3452 3333 227 185 -507 C ATOM 3517 CG2 VAL B 160 42.150 4.128 32.115 1.00 27.65 C ANISOU 3517 CG2 VAL B 160 3247 3715 3546 247 183 -533 C ATOM 3518 N ALA B 161 40.327 7.488 29.427 1.00 22.29 N ANISOU 3518 N ALA B 161 2574 3040 2855 197 190 -519 N ATOM 3519 CA ALA B 161 39.304 8.352 28.859 1.00 18.79 C ANISOU 3519 CA ALA B 161 2138 2588 2414 182 193 -509 C ATOM 3520 C ALA B 161 39.944 9.696 28.565 1.00 16.58 C ANISOU 3520 C ALA B 161 1852 2324 2122 168 196 -509 C ATOM 3521 O ALA B 161 40.939 10.069 29.197 1.00 14.07 O ANISOU 3521 O ALA B 161 1529 2018 1799 167 197 -510 O ATOM 3522 CB ALA B 161 38.120 8.533 29.813 1.00 19.10 C ANISOU 3522 CB ALA B 161 2194 2599 2465 175 193 -488 C ATOM 3523 N ALA B 162 39.396 10.395 27.575 1.00 12.29 N ANISOU 3523 N ALA B 162 1310 1783 1576 157 198 -508 N ATOM 3524 CA ALA B 162 39.900 11.724 27.247 1.00 14.79 C ANISOU 3524 CA ALA B 162 1622 2114 1883 142 202 -507 C ATOM 3525 C ALA B 162 38.827 12.490 26.494 1.00 16.00 C ANISOU 3525 C ALA B 162 1784 2259 2037 129 205 -498 C ATOM 3526 O ALA B 162 37.860 11.915 25.988 1.00 16.11 O ANISOU 3526 O ALA B 162 1804 2261 2058 133 203 -498 O ATOM 3527 CB ALA B 162 41.196 11.672 26.424 1.00 11.68 C ANISOU 3527 CB ALA B 162 1211 1751 1475 147 202 -526 C ATOM 3528 N GLY B 163 39.020 13.802 26.412 1.00 16.60 N ANISOU 3528 N GLY B 163 1859 2341 2107 114 209 -492 N ATOM 3529 CA GLY B 163 38.108 14.605 25.629 1.00 13.93 C ANISOU 3529 CA GLY B 163 1528 1996 1768 101 212 -485 C ATOM 3530 C GLY B 163 38.280 16.071 25.946 1.00 15.55 C ANISOU 3530 C GLY B 163 1736 2203 1969 83 216 -474 C ATOM 3531 O GLY B 163 39.326 16.500 26.425 1.00 16.68 O ANISOU 3531 O GLY B 163 1872 2360 2107 81 218 -478 O ATOM 3532 N TYR B 164 37.236 16.828 25.662 1.00 16.06 N ANISOU 3532 N TYR B 164 1810 2254 2038 70 219 -462 N ATOM 3533 CA TYR B 164 37.344 18.264 25.832 1.00 13.04 C ANISOU 3533 CA TYR B 164 1431 1872 1651 53 223 -453 C ATOM 3534 C TYR B 164 35.951 18.855 25.943 1.00 13.86 C ANISOU 3534 C TYR B 164 1550 1952 1764 41 224 -435 C ATOM 3535 O TYR B 164 34.971 18.278 25.475 1.00 8.69 O ANISOU 3535 O TYR B 164 901 1287 1115 45 222 -433 O ATOM 3536 CB TYR B 164 38.107 18.924 24.673 1.00 10.37 C ANISOU 3536 CB TYR B 164 1081 1559 1299 47 227 -465 C ATOM 3537 CG TYR B 164 37.555 18.595 23.292 1.00 13.20 C ANISOU 3537 CG TYR B 164 1439 1923 1654 51 227 -472 C ATOM 3538 CD1 TYR B 164 36.485 19.311 22.754 1.00 14.33 C ANISOU 3538 CD1 TYR B 164 1592 2054 1799 39 230 -462 C ATOM 3539 CD2 TYR B 164 38.113 17.578 22.521 1.00 13.70 C ANISOU 3539 CD2 TYR B 164 1491 2003 1712 65 225 -490 C ATOM 3540 CE1 TYR B 164 35.972 19.010 21.486 1.00 14.69 C ANISOU 3540 CE1 TYR B 164 1636 2105 1841 43 230 -469 C ATOM 3541 CE2 TYR B 164 37.617 17.276 21.244 1.00 13.75 C ANISOU 3541 CE2 TYR B 164 1495 2014 1714 69 225 -498 C ATOM 3542 CZ TYR B 164 36.559 18.003 20.733 1.00 12.43 C ANISOU 3542 CZ TYR B 164 1338 1836 1549 58 227 -487 C ATOM 3543 OH TYR B 164 36.072 17.699 19.490 1.00 12.08 O ANISOU 3543 OH TYR B 164 1292 1798 1501 61 227 -495 O ATOM 3544 N ALA B 165 35.885 20.029 26.553 1.00 15.83 N ANISOU 3544 N ALA B 165 1805 2195 2015 25 227 -423 N ATOM 3545 CA ALA B 165 34.714 20.882 26.476 1.00 14.07 C ANISOU 3545 CA ALA B 165 1595 1953 1798 10 229 -407 C ATOM 3546 C ALA B 165 35.066 22.052 25.575 1.00 14.00 C ANISOU 3546 C ALA B 165 1582 1960 1779 -3 234 -411 C ATOM 3547 O ALA B 165 36.117 22.674 25.749 1.00 10.72 O ANISOU 3547 O ALA B 165 1159 1559 1355 -8 236 -416 O ATOM 3548 CB ALA B 165 34.291 21.365 27.868 1.00 11.17 C ANISOU 3548 CB ALA B 165 1238 1565 1442 1 228 -390 C ATOM 3549 N LEU B 166 34.211 22.338 24.605 1.00 8.32 N ANISOU 3549 N LEU B 166 867 1235 1058 -8 235 -408 N ATOM 3550 CA LEU B 166 34.399 23.483 23.727 1.00 15.13 C ANISOU 3550 CA LEU B 166 1728 2110 1911 -21 240 -410 C ATOM 3551 C LEU B 166 33.407 24.559 24.138 1.00 8.12 C ANISOU 3551 C LEU B 166 854 1200 1032 -39 242 -392 C ATOM 3552 O LEU B 166 32.198 24.317 24.145 1.00 11.10 O ANISOU 3552 O LEU B 166 1242 1558 1419 -40 240 -382 O ATOM 3553 CB LEU B 166 34.209 23.096 22.257 1.00 8.96 C ANISOU 3553 CB LEU B 166 941 1341 1122 -14 241 -421 C ATOM 3554 CG LEU B 166 34.111 24.262 21.257 1.00 16.38 C ANISOU 3554 CG LEU B 166 1882 2290 2053 -28 247 -420 C ATOM 3555 CD1 LEU B 166 35.359 25.128 21.274 1.00 10.53 C ANISOU 3555 CD1 LEU B 166 1132 1568 1301 -36 251 -426 C ATOM 3556 CD2 LEU B 166 33.883 23.730 19.846 1.00 16.74 C ANISOU 3556 CD2 LEU B 166 1922 2348 2091 -19 247 -432 C ATOM 3557 N TYR B 167 33.914 25.736 24.496 1.00 13.84 N ANISOU 3557 N TYR B 167 1579 1927 1753 -53 245 -388 N ATOM 3558 CA TYR B 167 33.043 26.885 24.751 1.00 9.89 C ANISOU 3558 CA TYR B 167 1091 1406 1259 -72 247 -372 C ATOM 3559 C TYR B 167 33.047 27.745 23.493 1.00 12.93 C ANISOU 3559 C TYR B 167 1475 1804 1634 -81 252 -376 C ATOM 3560 O TYR B 167 33.765 28.735 23.383 1.00 15.25 O ANISOU 3560 O TYR B 167 1766 2109 1920 -91 255 -379 O ATOM 3561 CB TYR B 167 33.494 27.665 25.982 1.00 11.47 C ANISOU 3561 CB TYR B 167 1295 1599 1464 -84 247 -364 C ATOM 3562 CG TYR B 167 33.851 26.762 27.107 1.00 11.65 C ANISOU 3562 CG TYR B 167 1316 1618 1493 -72 243 -364 C ATOM 3563 CD1 TYR B 167 32.861 26.105 27.839 1.00 9.03 C ANISOU 3563 CD1 TYR B 167 993 1263 1175 -69 239 -353 C ATOM 3564 CD2 TYR B 167 35.179 26.538 27.433 1.00 12.12 C ANISOU 3564 CD2 TYR B 167 1363 1698 1545 -65 242 -376 C ATOM 3565 CE1 TYR B 167 33.203 25.246 28.870 1.00 16.59 C ANISOU 3565 CE1 TYR B 167 1948 2217 2137 -58 235 -353 C ATOM 3566 CE2 TYR B 167 35.529 25.680 28.459 1.00 13.51 C ANISOU 3566 CE2 TYR B 167 1537 1870 1726 -54 239 -376 C ATOM 3567 CZ TYR B 167 34.543 25.037 29.164 1.00 11.80 C ANISOU 3567 CZ TYR B 167 1331 1631 1523 -50 235 -365 C ATOM 3568 OH TYR B 167 34.904 24.196 30.188 1.00 12.13 O ANISOU 3568 OH TYR B 167 1370 1670 1568 -38 231 -365 O ATOM 3569 N GLY B 168 32.235 27.333 22.525 1.00 17.26 N ANISOU 3569 N GLY B 168 2026 2351 2181 -76 252 -377 N ATOM 3570 CA GLY B 168 32.110 28.053 21.273 1.00 15.68 C ANISOU 3570 CA GLY B 168 1825 2161 1971 -82 256 -381 C ATOM 3571 C GLY B 168 30.757 28.725 21.164 1.00 17.62 C ANISOU 3571 C GLY B 168 2086 2384 2226 -95 257 -366 C ATOM 3572 O GLY B 168 30.279 29.309 22.139 1.00 12.05 O ANISOU 3572 O GLY B 168 1390 1657 1531 -107 256 -352 O ATOM 3573 N SER B 169 30.118 28.646 19.993 1.00 15.74 N ANISOU 3573 N SER B 169 1848 2150 1983 -92 258 -368 N ATOM 3574 CA SER B 169 28.783 29.216 19.860 1.00 13.76 C ANISOU 3574 CA SER B 169 1611 1877 1740 -103 259 -354 C ATOM 3575 C SER B 169 27.831 28.570 20.854 1.00 12.20 C ANISOU 3575 C SER B 169 1422 1653 1559 -102 254 -342 C ATOM 3576 O SER B 169 26.949 29.237 21.413 1.00 10.74 O ANISOU 3576 O SER B 169 1250 1444 1385 -117 254 -327 O ATOM 3577 CB SER B 169 28.283 29.057 18.420 1.00 21.08 C ANISOU 3577 CB SER B 169 2537 2814 2659 -98 261 -360 C ATOM 3578 OG SER B 169 28.214 27.696 18.048 1.00 16.62 O ANISOU 3578 OG SER B 169 1966 2257 2094 -79 257 -370 O ATOM 3579 N ALA B 170 28.014 27.273 21.103 1.00 11.87 N ANISOU 3579 N ALA B 170 1374 1616 1519 -86 250 -349 N ATOM 3580 CA ALA B 170 27.424 26.591 22.239 1.00 13.82 C ANISOU 3580 CA ALA B 170 1627 1842 1781 -83 246 -339 C ATOM 3581 C ALA B 170 28.540 25.853 22.954 1.00 15.32 C ANISOU 3581 C ALA B 170 1808 2044 1970 -71 243 -348 C ATOM 3582 O ALA B 170 29.674 25.791 22.479 1.00 12.60 O ANISOU 3582 O ALA B 170 1452 1723 1613 -64 245 -362 O ATOM 3583 CB ALA B 170 26.312 25.621 21.821 1.00 13.86 C ANISOU 3583 CB ALA B 170 1636 1838 1793 -74 243 -337 C ATOM 3584 N THR B 171 28.219 25.304 24.114 1.00 14.22 N ANISOU 3584 N THR B 171 1674 1888 1842 -69 240 -340 N ATOM 3585 CA THR B 171 29.171 24.524 24.888 1.00 11.79 C ANISOU 3585 CA THR B 171 1358 1588 1534 -57 237 -347 C ATOM 3586 C THR B 171 28.924 23.033 24.646 1.00 10.66 C ANISOU 3586 C THR B 171 1210 1447 1392 -37 233 -355 C ATOM 3587 O THR B 171 27.809 22.543 24.845 1.00 9.40 O ANISOU 3587 O THR B 171 1058 1269 1243 -36 231 -346 O ATOM 3588 CB THR B 171 29.062 24.862 26.371 1.00 5.28 C ANISOU 3588 CB THR B 171 541 745 721 -66 235 -333 C ATOM 3589 OG1 THR B 171 29.501 26.217 26.580 1.00 11.36 O ANISOU 3589 OG1 THR B 171 1312 1515 1487 -83 239 -329 O ATOM 3590 CG2 THR B 171 29.923 23.879 27.188 1.00 6.45 C ANISOU 3590 CG2 THR B 171 682 901 869 -50 232 -340 C ATOM 3591 N MET B 172 29.961 22.317 24.218 1.00 11.91 N ANISOU 3591 N MET B 172 1357 1628 1542 -22 232 -372 N ATOM 3592 CA MET B 172 29.852 20.892 23.934 1.00 14.28 C ANISOU 3592 CA MET B 172 1652 1930 1843 -4 229 -382 C ATOM 3593 C MET B 172 30.979 20.126 24.603 1.00 13.89 C ANISOU 3593 C MET B 172 1595 1891 1792 9 226 -392 C ATOM 3594 O MET B 172 32.144 20.532 24.546 1.00 13.03 O ANISOU 3594 O MET B 172 1476 1800 1673 8 229 -401 O ATOM 3595 CB MET B 172 29.876 20.600 22.430 1.00 14.08 C ANISOU 3595 CB MET B 172 1621 1922 1808 3 230 -396 C ATOM 3596 CG MET B 172 30.049 19.092 22.100 1.00 13.91 C ANISOU 3596 CG MET B 172 1591 1906 1786 23 226 -411 C ATOM 3597 SD MET B 172 29.735 18.714 20.363 1.00 19.11 S ANISOU 3597 SD MET B 172 2245 2579 2437 30 226 -425 S ATOM 3598 CE MET B 172 27.941 18.725 20.313 1.00 17.72 C ANISOU 3598 CE MET B 172 2084 2378 2273 24 225 -410 C ATOM 3599 N LEU B 173 30.632 18.987 25.197 1.00 10.44 N ANISOU 3599 N LEU B 173 1160 1443 1363 21 222 -391 N ATOM 3600 CA LEU B 173 31.609 18.082 25.772 1.00 7.84 C ANISOU 3600 CA LEU B 173 823 1123 1033 35 219 -401 C ATOM 3601 C LEU B 173 31.743 16.879 24.851 1.00 12.69 C ANISOU 3601 C LEU B 173 1429 1748 1644 52 217 -418 C ATOM 3602 O LEU B 173 30.748 16.211 24.552 1.00 14.90 O ANISOU 3602 O LEU B 173 1715 2016 1931 57 214 -416 O ATOM 3603 CB LEU B 173 31.203 17.638 27.178 1.00 13.06 C ANISOU 3603 CB LEU B 173 1492 1765 1707 37 216 -389 C ATOM 3604 CG LEU B 173 32.385 16.930 27.869 1.00 27.92 C ANISOU 3604 CG LEU B 173 3365 3657 3585 50 214 -398 C ATOM 3605 CD1 LEU B 173 32.656 17.517 29.240 1.00 29.39 C ANISOU 3605 CD1 LEU B 173 3556 3835 3776 43 215 -386 C ATOM 3606 CD2 LEU B 173 32.201 15.432 27.934 1.00 37.87 C ANISOU 3606 CD2 LEU B 173 4624 4913 4851 68 210 -406 C ATOM 3607 N VAL B 174 32.969 16.609 24.411 1.00 12.29 N ANISOU 3607 N VAL B 174 1366 1721 1583 60 217 -435 N ATOM 3608 CA VAL B 174 33.291 15.441 23.591 1.00 11.07 C ANISOU 3608 CA VAL B 174 1202 1579 1425 76 214 -453 C ATOM 3609 C VAL B 174 34.070 14.486 24.483 1.00 18.42 C ANISOU 3609 C VAL B 174 2128 2512 2359 90 211 -459 C ATOM 3610 O VAL B 174 35.127 14.852 25.010 1.00 14.07 O ANISOU 3610 O VAL B 174 1571 1972 1803 88 212 -461 O ATOM 3611 CB VAL B 174 34.102 15.825 22.340 1.00 11.72 C ANISOU 3611 CB VAL B 174 1272 1687 1493 76 217 -468 C ATOM 3612 CG1 VAL B 174 34.483 14.598 21.546 1.00 17.87 C ANISOU 3612 CG1 VAL B 174 2042 2480 2269 92 214 -487 C ATOM 3613 CG2 VAL B 174 33.316 16.806 21.456 1.00 10.96 C ANISOU 3613 CG2 VAL B 174 1182 1589 1394 62 221 -461 C ATOM 3614 N LEU B 175 33.544 13.278 24.676 1.00 14.41 N ANISOU 3614 N LEU B 175 1623 1992 1860 102 207 -461 N ATOM 3615 CA LEU B 175 34.135 12.286 25.569 1.00 17.95 C ANISOU 3615 CA LEU B 175 2069 2439 2313 115 204 -465 C ATOM 3616 C LEU B 175 34.505 11.046 24.762 1.00 18.87 C ANISOU 3616 C LEU B 175 2175 2567 2427 132 200 -484 C ATOM 3617 O LEU B 175 33.647 10.449 24.095 1.00 11.72 O ANISOU 3617 O LEU B 175 1273 1654 1526 136 198 -487 O ATOM 3618 CB LEU B 175 33.171 11.913 26.697 1.00 14.63 C ANISOU 3618 CB LEU B 175 1661 1992 1906 116 202 -449 C ATOM 3619 CG LEU B 175 33.635 10.785 27.620 1.00 15.01 C ANISOU 3619 CG LEU B 175 1707 2036 1959 130 199 -452 C ATOM 3620 CD1 LEU B 175 34.885 11.215 28.368 1.00 16.29 C ANISOU 3620 CD1 LEU B 175 1863 2211 2115 130 200 -454 C ATOM 3621 CD2 LEU B 175 32.546 10.391 28.611 1.00 17.74 C ANISOU 3621 CD2 LEU B 175 2066 2355 2318 130 197 -436 C ATOM 3622 N ALA B 176 35.785 10.690 24.790 1.00 13.51 N ANISOU 3622 N ALA B 176 1485 1908 1741 141 200 -498 N ATOM 3623 CA ALA B 176 36.291 9.508 24.110 1.00 20.14 C ANISOU 3623 CA ALA B 176 2314 2760 2578 156 196 -517 C ATOM 3624 C ALA B 176 36.652 8.477 25.161 1.00 19.68 C ANISOU 3624 C ALA B 176 2256 2694 2526 170 193 -518 C ATOM 3625 O ALA B 176 37.326 8.798 26.144 1.00 16.96 O ANISOU 3625 O ALA B 176 1911 2351 2181 168 194 -513 O ATOM 3626 CB ALA B 176 37.520 9.821 23.252 1.00 10.30 C ANISOU 3626 CB ALA B 176 1052 1543 1317 157 197 -533 C ATOM 3627 N MET B 177 36.187 7.252 24.960 1.00 16.71 N ANISOU 3627 N MET B 177 1882 2310 2158 182 189 -525 N ATOM 3628 CA MET B 177 36.560 6.126 25.800 1.00 17.86 C ANISOU 3628 CA MET B 177 2027 2450 2310 196 186 -529 C ATOM 3629 C MET B 177 36.695 4.917 24.891 1.00 20.60 C ANISOU 3629 C MET B 177 2366 2806 2657 211 182 -547 C ATOM 3630 O MET B 177 36.594 5.029 23.661 1.00 18.49 O ANISOU 3630 O MET B 177 2093 2550 2384 209 182 -557 O ATOM 3631 CB MET B 177 35.536 5.889 26.914 1.00 20.73 C ANISOU 3631 CB MET B 177 2405 2786 2687 195 186 -511 C ATOM 3632 CG MET B 177 35.408 7.040 27.870 1.00 24.15 C ANISOU 3632 CG MET B 177 2846 3210 3120 181 189 -492 C ATOM 3633 SD MET B 177 34.429 6.609 29.300 1.00 22.80 S ANISOU 3633 SD MET B 177 2690 3009 2964 182 188 -473 S ATOM 3634 CE MET B 177 32.811 6.336 28.567 1.00 12.69 C ANISOU 3634 CE MET B 177 1419 1712 1692 178 187 -468 C ATOM 3635 N ASP B 178 36.903 3.747 25.507 1.00 18.58 N ANISOU 3635 N ASP B 178 2109 2543 2408 225 179 -552 N ATOM 3636 CA ASP B 178 37.015 2.520 24.726 1.00 24.75 C ANISOU 3636 CA ASP B 178 2883 3329 3190 239 175 -570 C ATOM 3637 C ASP B 178 35.789 2.300 23.852 1.00 22.57 C ANISOU 3637 C ASP B 178 2612 3043 2920 236 174 -570 C ATOM 3638 O ASP B 178 35.911 1.800 22.731 1.00 22.54 O ANISOU 3638 O ASP B 178 2600 3052 2913 243 171 -586 O ATOM 3639 CB ASP B 178 37.229 1.319 25.645 1.00 32.90 C ANISOU 3639 CB ASP B 178 3917 4352 4231 254 173 -571 C ATOM 3640 CG ASP B 178 38.583 0.674 25.437 1.00 46.04 C ANISOU 3640 CG ASP B 178 5567 6037 5887 267 171 -590 C ATOM 3641 OD1 ASP B 178 39.562 1.151 26.046 1.00 45.66 O ANISOU 3641 OD1 ASP B 178 5515 6002 5833 266 172 -588 O ATOM 3642 OD2 ASP B 178 38.669 -0.299 24.655 1.00 53.74 O ANISOU 3642 OD2 ASP B 178 6536 7019 6864 278 167 -605 O ATOM 3643 N CYS B 179 34.599 2.668 24.346 1.00 21.33 N ANISOU 3643 N CYS B 179 2469 2864 2772 227 175 -552 N ATOM 3644 CA CYS B 179 33.377 2.459 23.574 1.00 19.31 C ANISOU 3644 CA CYS B 179 2218 2597 2523 224 174 -551 C ATOM 3645 C CYS B 179 33.227 3.416 22.394 1.00 32.64 C ANISOU 3645 C CYS B 179 3903 4298 4201 214 176 -554 C ATOM 3646 O CYS B 179 32.280 3.242 21.620 1.00 24.70 O ANISOU 3646 O CYS B 179 2900 3286 3199 212 174 -556 O ATOM 3647 CB CYS B 179 32.157 2.589 24.484 1.00 20.07 C ANISOU 3647 CB CYS B 179 2330 2666 2630 217 174 -531 C ATOM 3648 SG CYS B 179 31.968 4.271 25.191 1.00 22.83 S ANISOU 3648 SG CYS B 179 2688 3011 2976 198 179 -509 S ATOM 3649 N GLY B 180 34.119 4.400 22.231 1.00 19.26 N ANISOU 3649 N GLY B 180 2202 2622 2494 206 179 -555 N ATOM 3650 CA GLY B 180 34.035 5.379 21.156 1.00 16.08 C ANISOU 3650 CA GLY B 180 1795 2232 2082 196 181 -557 C ATOM 3651 C GLY B 180 33.931 6.811 21.643 1.00 17.57 C ANISOU 3651 C GLY B 180 1991 2418 2268 179 186 -540 C ATOM 3652 O GLY B 180 34.214 7.129 22.800 1.00 14.91 O ANISOU 3652 O GLY B 180 1659 2073 1933 176 188 -529 O ATOM 3653 N VAL B 181 33.527 7.687 20.721 1.00 16.89 N ANISOU 3653 N VAL B 181 1906 2338 2175 169 189 -539 N ATOM 3654 CA VAL B 181 33.455 9.133 20.947 1.00 15.42 C ANISOU 3654 CA VAL B 181 1725 2151 1985 152 194 -525 C ATOM 3655 C VAL B 181 31.992 9.557 20.998 1.00 16.10 C ANISOU 3655 C VAL B 181 1824 2215 2078 142 195 -508 C ATOM 3656 O VAL B 181 31.209 9.207 20.109 1.00 15.50 O ANISOU 3656 O VAL B 181 1748 2136 2004 144 193 -513 O ATOM 3657 CB VAL B 181 34.198 9.916 19.847 1.00 16.89 C ANISOU 3657 CB VAL B 181 1900 2362 2155 147 197 -535 C ATOM 3658 CG1 VAL B 181 34.121 11.420 20.100 1.00 11.30 C ANISOU 3658 CG1 VAL B 181 1198 1653 1443 129 203 -520 C ATOM 3659 CG2 VAL B 181 35.661 9.457 19.761 1.00 11.86 C ANISOU 3659 CG2 VAL B 181 1249 1749 1510 157 196 -552 C ATOM 3660 N ASN B 182 31.618 10.310 22.026 1.00 12.51 N ANISOU 3660 N ASN B 182 1380 1745 1629 131 197 -490 N ATOM 3661 CA ASN B 182 30.248 10.779 22.163 1.00 14.38 C ANISOU 3661 CA ASN B 182 1629 1961 1873 121 198 -473 C ATOM 3662 C ASN B 182 30.242 12.269 22.473 1.00 21.11 C ANISOU 3662 C ASN B 182 2487 2813 2722 104 203 -459 C ATOM 3663 O ASN B 182 31.101 12.765 23.215 1.00 16.39 O ANISOU 3663 O ASN B 182 1887 2221 2121 100 205 -456 O ATOM 3664 CB ASN B 182 29.521 9.966 23.240 1.00 14.75 C ANISOU 3664 CB ASN B 182 1685 1985 1934 126 195 -463 C ATOM 3665 CG ASN B 182 29.353 8.514 22.818 1.00 19.38 C ANISOU 3665 CG ASN B 182 2267 2571 2525 142 190 -477 C ATOM 3666 OD1 ASN B 182 28.493 8.196 22.011 1.00 12.77 O ANISOU 3666 OD1 ASN B 182 1432 1729 1691 143 188 -481 O ATOM 3667 ND2 ASN B 182 30.240 7.650 23.289 1.00 20.30 N ANISOU 3667 ND2 ASN B 182 2378 2694 2643 155 188 -487 N ATOM 3668 N CYS B 183 29.287 12.978 21.874 1.00 12.00 N ANISOU 3668 N CYS B 183 1339 1652 1567 93 205 -451 N ATOM 3669 CA CYS B 183 29.204 14.432 21.957 1.00 14.50 C ANISOU 3669 CA CYS B 183 1660 1968 1880 76 210 -438 C ATOM 3670 C CYS B 183 27.943 14.853 22.693 1.00 15.07 C ANISOU 3670 C CYS B 183 1746 2015 1963 65 210 -417 C ATOM 3671 O CYS B 183 26.829 14.473 22.308 1.00 17.00 O ANISOU 3671 O CYS B 183 1997 2249 2215 66 208 -414 O ATOM 3672 CB CYS B 183 29.231 15.058 20.563 1.00 11.17 C ANISOU 3672 CB CYS B 183 1234 1562 1447 71 213 -446 C ATOM 3673 SG CYS B 183 30.683 14.538 19.625 1.00 20.83 S ANISOU 3673 SG CYS B 183 2440 2817 2657 83 213 -471 S ATOM 3674 N PHE B 184 28.127 15.674 23.721 1.00 6.63 N ANISOU 3674 N PHE B 184 682 939 897 54 212 -404 N ATOM 3675 CA PHE B 184 27.061 16.103 24.610 1.00 10.30 C ANISOU 3675 CA PHE B 184 1159 1381 1373 43 211 -384 C ATOM 3676 C PHE B 184 26.972 17.620 24.526 1.00 13.03 C ANISOU 3676 C PHE B 184 1509 1726 1715 24 216 -373 C ATOM 3677 O PHE B 184 27.978 18.312 24.706 1.00 16.26 O ANISOU 3677 O PHE B 184 1914 2147 2117 19 218 -376 O ATOM 3678 CB PHE B 184 27.337 15.650 26.044 1.00 13.21 C ANISOU 3678 CB PHE B 184 1531 1740 1750 47 209 -376 C ATOM 3679 CG PHE B 184 27.497 14.164 26.187 1.00 19.68 C ANISOU 3679 CG PHE B 184 2346 2559 2572 65 205 -387 C ATOM 3680 CD1 PHE B 184 28.703 13.544 25.870 1.00 13.78 C ANISOU 3680 CD1 PHE B 184 1589 1831 1818 79 204 -405 C ATOM 3681 CD2 PHE B 184 26.455 13.391 26.660 1.00 14.37 C ANISOU 3681 CD2 PHE B 184 1681 1867 1911 69 201 -379 C ATOM 3682 CE1 PHE B 184 28.852 12.191 26.001 1.00 14.28 C ANISOU 3682 CE1 PHE B 184 1648 1893 1884 95 200 -415 C ATOM 3683 CE2 PHE B 184 26.604 12.016 26.803 1.00 12.74 C ANISOU 3683 CE2 PHE B 184 1472 1661 1709 85 197 -389 C ATOM 3684 CZ PHE B 184 27.797 11.422 26.469 1.00 12.18 C ANISOU 3684 CZ PHE B 184 1389 1607 1630 98 197 -407 C ATOM 3685 N MET B 185 25.788 18.128 24.208 1.00 8.00 N ANISOU 3685 N MET B 185 880 1075 1082 13 217 -361 N ATOM 3686 CA MET B 185 25.560 19.566 24.172 1.00 14.42 C ANISOU 3686 CA MET B 185 1700 1886 1895 -6 221 -350 C ATOM 3687 C MET B 185 25.124 20.027 25.552 1.00 10.10 C ANISOU 3687 C MET B 185 1160 1317 1359 -19 221 -331 C ATOM 3688 O MET B 185 24.214 19.436 26.143 1.00 14.95 O ANISOU 3688 O MET B 185 1781 1914 1984 -18 218 -321 O ATOM 3689 CB MET B 185 24.491 19.924 23.135 1.00 16.58 C ANISOU 3689 CB MET B 185 1977 2154 2167 -13 222 -346 C ATOM 3690 CG MET B 185 24.392 21.422 22.861 1.00 18.85 C ANISOU 3690 CG MET B 185 2270 2441 2452 -32 227 -338 C ATOM 3691 SD MET B 185 25.794 21.995 21.864 1.00 16.23 S ANISOU 3691 SD MET B 185 1926 2138 2101 -29 231 -355 S ATOM 3692 CE MET B 185 25.263 21.410 20.243 1.00 13.90 C ANISOU 3692 CE MET B 185 1628 1855 1799 -18 231 -368 C ATOM 3693 N LEU B 186 25.759 21.078 26.071 1.00 8.77 N ANISOU 3693 N LEU B 186 993 1150 1188 -31 224 -325 N ATOM 3694 CA LEU B 186 25.269 21.657 27.319 1.00 10.06 C ANISOU 3694 CA LEU B 186 1166 1293 1364 -46 224 -306 C ATOM 3695 C LEU B 186 23.997 22.443 27.027 1.00 17.41 C ANISOU 3695 C LEU B 186 2107 2207 2302 -64 226 -291 C ATOM 3696 O LEU B 186 24.008 23.347 26.183 1.00 15.73 O ANISOU 3696 O LEU B 186 1895 1999 2082 -73 230 -293 O ATOM 3697 CB LEU B 186 26.314 22.561 27.962 1.00 7.07 C ANISOU 3697 CB LEU B 186 785 920 981 -54 226 -306 C ATOM 3698 CG LEU B 186 25.848 23.231 29.264 1.00 8.93 C ANISOU 3698 CG LEU B 186 1031 1133 1229 -71 227 -286 C ATOM 3699 CD1 LEU B 186 25.370 22.204 30.323 1.00 10.04 C ANISOU 3699 CD1 LEU B 186 1174 1260 1381 -64 223 -278 C ATOM 3700 CD2 LEU B 186 27.003 24.025 29.808 1.00 12.47 C ANISOU 3700 CD2 LEU B 186 1476 1590 1672 -77 228 -290 C ATOM 3701 N ASP B 187 22.884 22.055 27.679 1.00 10.86 N ANISOU 3701 N ASP B 187 1285 1356 1485 -68 225 -276 N ATOM 3702 CA ASP B 187 21.661 22.849 27.663 1.00 12.49 C ANISOU 3702 CA ASP B 187 1501 1543 1700 -88 228 -258 C ATOM 3703 C ASP B 187 21.723 23.783 28.863 1.00 12.29 C ANISOU 3703 C ASP B 187 1484 1501 1684 -106 231 -241 C ATOM 3704 O ASP B 187 21.467 23.362 30.003 1.00 13.51 O ANISOU 3704 O ASP B 187 1641 1643 1848 -108 230 -230 O ATOM 3705 CB ASP B 187 20.408 21.963 27.705 1.00 9.71 C ANISOU 3705 CB ASP B 187 1153 1179 1358 -84 227 -250 C ATOM 3706 CG ASP B 187 19.102 22.746 27.582 1.00 11.25 C ANISOU 3706 CG ASP B 187 1359 1355 1562 -104 231 -231 C ATOM 3707 OD1 ASP B 187 19.058 23.967 27.871 1.00 15.08 O ANISOU 3707 OD1 ASP B 187 1851 1829 2050 -124 236 -218 O ATOM 3708 OD2 ASP B 187 18.081 22.121 27.212 1.00 16.21 O ANISOU 3708 OD2 ASP B 187 1988 1978 2193 -101 231 -227 O ATOM 3709 N PRO B 188 22.077 25.052 28.653 1.00 13.70 N ANISOU 3709 N PRO B 188 1666 1679 1859 -121 234 -240 N ATOM 3710 CA PRO B 188 22.211 25.961 29.799 1.00 14.65 C ANISOU 3710 CA PRO B 188 1795 1783 1989 -138 236 -225 C ATOM 3711 C PRO B 188 20.892 26.271 30.480 1.00 15.83 C ANISOU 3711 C PRO B 188 1962 1915 2138 -136 228 -191 C ATOM 3712 O PRO B 188 20.916 26.741 31.617 1.00 16.56 O ANISOU 3712 O PRO B 188 2064 2004 2223 -128 217 -170 O ATOM 3713 CB PRO B 188 22.833 27.220 29.192 1.00 15.29 C ANISOU 3713 CB PRO B 188 1877 1871 2062 -149 239 -232 C ATOM 3714 CG PRO B 188 22.497 27.140 27.701 1.00 14.25 C ANISOU 3714 CG PRO B 188 1742 1752 1921 -143 240 -242 C ATOM 3715 CD PRO B 188 22.320 25.704 27.353 1.00 11.17 C ANISOU 3715 CD PRO B 188 1343 1373 1528 -122 236 -251 C ATOM 3716 N ALA B 189 19.743 26.003 29.852 1.00 15.34 N ANISOU 3716 N ALA B 189 1905 1850 2076 -132 226 -182 N ATOM 3717 CA ALA B 189 18.484 26.231 30.555 1.00 13.51 C ANISOU 3717 CA ALA B 189 1688 1612 1833 -118 208 -148 C ATOM 3718 C ALA B 189 18.349 25.329 31.774 1.00 18.07 C ANISOU 3718 C ALA B 189 2265 2187 2415 -111 204 -139 C ATOM 3719 O ALA B 189 17.752 25.736 32.777 1.00 23.20 O ANISOU 3719 O ALA B 189 2925 2838 3053 -101 186 -113 O ATOM 3720 CB ALA B 189 17.297 26.025 29.608 1.00 15.84 C ANISOU 3720 CB ALA B 189 1986 1907 2127 -117 207 -143 C ATOM 3721 N ILE B 190 18.915 24.119 31.730 1.00 15.51 N ANISOU 3721 N ILE B 190 1926 1861 2107 -117 219 -164 N ATOM 3722 CA ILE B 190 18.730 23.147 32.799 1.00 11.10 C ANISOU 3722 CA ILE B 190 1365 1298 1554 -111 218 -158 C ATOM 3723 C ILE B 190 20.043 22.606 33.335 1.00 15.44 C ANISOU 3723 C ILE B 190 1902 1848 2117 -116 227 -181 C ATOM 3724 O ILE B 190 20.026 21.741 34.215 1.00 19.48 O ANISOU 3724 O ILE B 190 2410 2356 2636 -112 228 -179 O ATOM 3725 CB ILE B 190 17.837 21.969 32.352 1.00 15.08 C ANISOU 3725 CB ILE B 190 1864 1798 2068 -110 223 -164 C ATOM 3726 CG1 ILE B 190 18.511 21.200 31.214 1.00 13.14 C ANISOU 3726 CG1 ILE B 190 1602 1562 1827 -106 230 -198 C ATOM 3727 CG2 ILE B 190 16.445 22.449 31.946 1.00 15.38 C ANISOU 3727 CG2 ILE B 190 1915 1837 2093 -104 212 -141 C ATOM 3728 CD1 ILE B 190 17.777 19.904 30.819 1.00 17.79 C ANISOU 3728 CD1 ILE B 190 2187 2154 2417 -91 226 -204 C ATOM 3729 N GLY B 191 21.180 23.068 32.824 1.00 12.05 N ANISOU 3729 N GLY B 191 1465 1429 1684 -120 231 -200 N ATOM 3730 CA GLY B 191 22.482 22.590 33.258 1.00 15.33 C ANISOU 3730 CA GLY B 191 1872 1860 2093 -103 227 -216 C ATOM 3731 C GLY B 191 22.691 21.103 33.078 1.00 18.60 C ANISOU 3731 C GLY B 191 2279 2287 2503 -79 221 -230 C ATOM 3732 O GLY B 191 23.169 20.418 33.989 1.00 18.31 O ANISOU 3732 O GLY B 191 2239 2251 2467 -69 219 -231 O ATOM 3733 N GLU B 192 22.344 20.588 31.898 1.00 15.95 N ANISOU 3733 N GLU B 192 1939 1959 2161 -69 220 -241 N ATOM 3734 CA GLU B 192 22.527 19.186 31.547 1.00 25.21 C ANISOU 3734 CA GLU B 192 3106 3143 3331 -46 215 -256 C ATOM 3735 C GLU B 192 23.276 19.065 30.235 1.00 19.37 C ANISOU 3735 C GLU B 192 2357 2424 2577 -34 215 -277 C ATOM 3736 O GLU B 192 22.993 19.798 29.282 1.00 17.70 O ANISOU 3736 O GLU B 192 2147 2216 2362 -42 217 -278 O ATOM 3737 CB GLU B 192 21.198 18.429 31.368 1.00 30.38 C ANISOU 3737 CB GLU B 192 3764 3786 3993 -45 214 -249 C ATOM 3738 CG GLU B 192 20.465 18.060 32.605 1.00 38.05 C ANISOU 3738 CG GLU B 192 4740 4741 4976 -51 215 -232 C ATOM 3739 CD GLU B 192 21.182 17.007 33.422 1.00 32.06 C ANISOU 3739 CD GLU B 192 3978 3986 4217 -33 210 -240 C ATOM 3740 OE1 GLU B 192 22.096 16.329 32.906 1.00 31.72 O ANISOU 3740 OE1 GLU B 192 3928 3959 4165 -14 206 -259 O ATOM 3741 OE2 GLU B 192 20.811 16.859 34.590 1.00 22.01 O ANISOU 3741 OE2 GLU B 192 2709 2702 2953 -39 211 -225 O ATOM 3742 N PHE B 193 24.189 18.101 30.184 1.00 16.86 N ANISOU 3742 N PHE B 193 2033 2121 2254 -14 211 -293 N ATOM 3743 CA PHE B 193 24.836 17.685 28.946 1.00 13.45 C ANISOU 3743 CA PHE B 193 1591 1709 1809 0 211 -314 C ATOM 3744 C PHE B 193 23.976 16.623 28.274 1.00 13.33 C ANISOU 3744 C PHE B 193 1577 1690 1798 11 208 -319 C ATOM 3745 O PHE B 193 23.831 15.512 28.790 1.00 28.28 O ANISOU 3745 O PHE B 193 3470 3578 3697 23 204 -321 O ATOM 3746 CB PHE B 193 26.234 17.145 29.216 1.00 15.27 C ANISOU 3746 CB PHE B 193 1813 1955 2032 15 210 -328 C ATOM 3747 CG PHE B 193 27.250 18.207 29.525 1.00 18.84 C ANISOU 3747 CG PHE B 193 2263 2418 2478 6 213 -328 C ATOM 3748 CD1 PHE B 193 27.864 18.897 28.500 1.00 14.29 C ANISOU 3748 CD1 PHE B 193 1680 1858 1890 3 216 -339 C ATOM 3749 CD2 PHE B 193 27.604 18.495 30.834 1.00 17.44 C ANISOU 3749 CD2 PHE B 193 2088 2233 2305 1 213 -319 C ATOM 3750 CE1 PHE B 193 28.811 19.882 28.775 1.00 17.82 C ANISOU 3750 CE1 PHE B 193 2124 2315 2331 -6 219 -339 C ATOM 3751 CE2 PHE B 193 28.544 19.469 31.102 1.00 16.69 C ANISOU 3751 CE2 PHE B 193 1990 2147 2204 -7 215 -320 C ATOM 3752 CZ PHE B 193 29.148 20.152 30.063 1.00 13.70 C ANISOU 3752 CZ PHE B 193 1605 1786 1815 -11 218 -330 C ATOM 3753 N ILE B 194 23.433 16.957 27.107 1.00 15.34 N ANISOU 3753 N ILE B 194 1832 1949 2049 7 210 -322 N ATOM 3754 CA ILE B 194 22.505 16.104 26.382 1.00 16.96 C ANISOU 3754 CA ILE B 194 2038 2150 2257 15 207 -326 C ATOM 3755 C ILE B 194 23.274 15.394 25.276 1.00 18.73 C ANISOU 3755 C ILE B 194 2252 2393 2470 31 206 -349 C ATOM 3756 O ILE B 194 23.932 16.044 24.457 1.00 19.05 O ANISOU 3756 O ILE B 194 2287 2449 2500 29 209 -357 O ATOM 3757 CB ILE B 194 21.352 16.926 25.789 1.00 8.64 C ANISOU 3757 CB ILE B 194 990 1086 1205 -1 210 -315 C ATOM 3758 CG1 ILE B 194 20.594 17.714 26.870 1.00 10.80 C ANISOU 3758 CG1 ILE B 194 1273 1340 1490 -20 212 -292 C ATOM 3759 CG2 ILE B 194 20.434 16.022 24.955 1.00 10.67 C ANISOU 3759 CG2 ILE B 194 1248 1342 1465 8 207 -322 C ATOM 3760 CD1 ILE B 194 19.913 16.875 27.919 1.00 13.54 C ANISOU 3760 CD1 ILE B 194 1624 1672 1849 -18 209 -281 C ATOM 3761 N LEU B 195 23.160 14.069 25.207 1.00 14.32 N ANISOU 3761 N LEU B 195 1691 1834 1916 47 202 -359 N ATOM 3762 CA LEU B 195 23.845 13.335 24.145 1.00 9.36 C ANISOU 3762 CA LEU B 195 1053 1223 1279 62 200 -380 C ATOM 3763 C LEU B 195 23.225 13.672 22.787 1.00 15.64 C ANISOU 3763 C LEU B 195 1849 2025 2070 58 202 -385 C ATOM 3764 O LEU B 195 22.048 13.388 22.543 1.00 12.22 O ANISOU 3764 O LEU B 195 1420 1579 1643 57 200 -380 O ATOM 3765 CB LEU B 195 23.776 11.832 24.410 1.00 15.91 C ANISOU 3765 CB LEU B 195 1881 2049 2116 78 196 -389 C ATOM 3766 CG LEU B 195 24.463 10.933 23.379 1.00 20.60 C ANISOU 3766 CG LEU B 195 2464 2659 2703 94 194 -412 C ATOM 3767 CD1 LEU B 195 25.916 11.329 23.205 1.00 25.15 C ANISOU 3767 CD1 LEU B 195 3031 3256 3268 96 196 -422 C ATOM 3768 CD2 LEU B 195 24.353 9.484 23.819 1.00 28.49 C ANISOU 3768 CD2 LEU B 195 3463 3651 3711 108 189 -418 C ATOM 3769 N VAL B 196 24.006 14.261 21.887 1.00 11.71 N ANISOU 3769 N VAL B 196 1343 1545 1560 57 205 -395 N ATOM 3770 CA VAL B 196 23.471 14.639 20.586 1.00 18.45 C ANISOU 3770 CA VAL B 196 2196 2405 2407 54 206 -400 C ATOM 3771 C VAL B 196 24.174 13.945 19.425 1.00 23.00 C ANISOU 3771 C VAL B 196 2762 3002 2975 67 205 -422 C ATOM 3772 O VAL B 196 23.613 13.914 18.317 1.00 22.08 O ANISOU 3772 O VAL B 196 2644 2890 2855 68 205 -428 O ATOM 3773 CB VAL B 196 23.475 16.177 20.385 1.00 14.59 C ANISOU 3773 CB VAL B 196 1711 1919 1912 37 212 -390 C ATOM 3774 CG1 VAL B 196 22.633 16.845 21.440 1.00 8.78 C ANISOU 3774 CG1 VAL B 196 987 1162 1187 22 213 -368 C ATOM 3775 CG2 VAL B 196 24.877 16.746 20.420 1.00 13.09 C ANISOU 3775 CG2 VAL B 196 1514 1747 1712 36 215 -397 C ATOM 3776 N ASP B 197 25.347 13.347 19.638 1.00 18.76 N ANISOU 3776 N ASP B 197 2216 2478 2434 78 204 -435 N ATOM 3777 CA ASP B 197 26.089 12.644 18.593 1.00 15.70 C ANISOU 3777 CA ASP B 197 1817 2111 2039 91 203 -457 C ATOM 3778 C ASP B 197 26.699 11.398 19.213 1.00 23.34 C ANISOU 3778 C ASP B 197 2778 3078 3011 105 199 -466 C ATOM 3779 O ASP B 197 27.604 11.511 20.044 1.00 25.40 O ANISOU 3779 O ASP B 197 3037 3343 3271 106 199 -465 O ATOM 3780 CB ASP B 197 27.186 13.525 18.004 1.00 25.15 C ANISOU 3780 CB ASP B 197 3005 3330 3221 86 207 -464 C ATOM 3781 CG ASP B 197 26.732 14.299 16.802 1.00 46.26 C ANISOU 3781 CG ASP B 197 5678 6011 5886 78 210 -465 C ATOM 3782 OD1 ASP B 197 26.103 15.367 16.988 1.00 51.67 O ANISOU 3782 OD1 ASP B 197 6373 6688 6573 64 214 -449 O ATOM 3783 OD2 ASP B 197 27.029 13.839 15.674 1.00 49.91 O ANISOU 3783 OD2 ASP B 197 6132 6491 6341 87 209 -481 O ATOM 3784 N LYS B 198 26.227 10.220 18.803 1.00 19.47 N ANISOU 3784 N LYS B 198 2286 2584 2526 117 194 -476 N ATOM 3785 CA LYS B 198 26.667 8.961 19.387 1.00 21.50 C ANISOU 3785 CA LYS B 198 2540 2839 2791 131 190 -485 C ATOM 3786 C LYS B 198 27.722 8.294 18.510 1.00 16.41 C ANISOU 3786 C LYS B 198 1880 2217 2137 143 188 -508 C ATOM 3787 O LYS B 198 27.611 8.302 17.286 1.00 20.70 O ANISOU 3787 O LYS B 198 2419 2773 2674 144 188 -519 O ATOM 3788 CB LYS B 198 25.493 7.996 19.578 1.00 23.66 C ANISOU 3788 CB LYS B 198 2820 3094 3078 136 185 -482 C ATOM 3789 CG LYS B 198 24.342 8.514 20.406 1.00 33.61 C ANISOU 3789 CG LYS B 198 4094 4331 4347 124 186 -460 C ATOM 3790 CD LYS B 198 23.269 7.440 20.528 1.00 47.08 C ANISOU 3790 CD LYS B 198 5803 6020 6064 131 182 -459 C ATOM 3791 CE LYS B 198 23.875 6.123 21.023 1.00 53.45 C ANISOU 3791 CE LYS B 198 6606 6827 6877 146 178 -471 C ATOM 3792 NZ LYS B 198 22.873 5.023 21.139 1.00 57.47 N ANISOU 3792 NZ LYS B 198 7119 7320 7398 153 174 -471 N ATOM 3793 N ASP B 199 28.738 7.714 19.148 1.00 18.01 N ANISOU 3793 N ASP B 199 2077 2426 2340 152 187 -515 N ATOM 3794 CA ASP B 199 29.737 6.868 18.480 1.00 19.54 C ANISOU 3794 CA ASP B 199 2257 2639 2527 166 184 -536 C ATOM 3795 C ASP B 199 30.263 7.531 17.204 1.00 20.97 C ANISOU 3795 C ASP B 199 2429 2844 2694 162 186 -547 C ATOM 3796 O ASP B 199 30.214 6.986 16.101 1.00 18.76 O ANISOU 3796 O ASP B 199 2142 2575 2410 169 184 -563 O ATOM 3797 CB ASP B 199 29.157 5.480 18.189 1.00 25.82 C ANISOU 3797 CB ASP B 199 3052 3427 3332 178 178 -547 C ATOM 3798 CG ASP B 199 30.234 4.425 18.002 1.00 27.60 C ANISOU 3798 CG ASP B 199 3266 3667 3555 194 175 -566 C ATOM 3799 OD1 ASP B 199 31.421 4.744 18.224 1.00 28.75 O ANISOU 3799 OD1 ASP B 199 3403 3828 3692 195 177 -571 O ATOM 3800 OD2 ASP B 199 29.895 3.286 17.625 1.00 31.80 O ANISOU 3800 OD2 ASP B 199 3794 4194 4092 205 170 -577 O ATOM 3801 N VAL B 200 30.795 8.736 17.391 1.00 24.03 N ANISOU 3801 N VAL B 200 2817 3240 3074 151 191 -539 N ATOM 3802 CA VAL B 200 31.169 9.606 16.283 1.00 19.55 C ANISOU 3802 CA VAL B 200 2243 2693 2493 144 195 -546 C ATOM 3803 C VAL B 200 32.394 9.054 15.562 1.00 16.00 C ANISOU 3803 C VAL B 200 1778 2269 2033 155 193 -567 C ATOM 3804 O VAL B 200 33.306 8.503 16.188 1.00 20.72 O ANISOU 3804 O VAL B 200 2369 2872 2630 163 191 -573 O ATOM 3805 CB VAL B 200 31.416 11.018 16.853 1.00 25.08 C ANISOU 3805 CB VAL B 200 2948 3392 3188 129 201 -530 C ATOM 3806 CG1 VAL B 200 32.028 11.935 15.836 1.00 25.25 C ANISOU 3806 CG1 VAL B 200 2962 3436 3194 122 205 -537 C ATOM 3807 CG2 VAL B 200 30.095 11.588 17.387 1.00 18.30 C ANISOU 3807 CG2 VAL B 200 2105 2509 2339 118 202 -510 C ATOM 3808 N LYS B 201 32.396 9.156 14.225 1.00 20.52 N ANISOU 3808 N LYS B 201 2343 2857 2596 156 194 -579 N ATOM 3809 CA LYS B 201 33.541 8.789 13.397 1.00 22.28 C ANISOU 3809 CA LYS B 201 2551 3108 2808 164 192 -598 C ATOM 3810 C LYS B 201 33.861 9.943 12.460 1.00 20.91 C ANISOU 3810 C LYS B 201 2373 2953 2620 154 198 -599 C ATOM 3811 O LYS B 201 32.957 10.538 11.866 1.00 16.12 O ANISOU 3811 O LYS B 201 1772 2340 2012 146 200 -592 O ATOM 3812 CB LYS B 201 33.285 7.514 12.564 1.00 22.00 C ANISOU 3812 CB LYS B 201 2509 3076 2775 178 187 -616 C ATOM 3813 CG LYS B 201 32.947 6.273 13.368 1.00 23.26 C ANISOU 3813 CG LYS B 201 2672 3217 2949 189 181 -617 C ATOM 3814 CD LYS B 201 34.066 5.868 14.316 1.00 26.29 C ANISOU 3814 CD LYS B 201 3050 3605 3332 196 180 -620 C ATOM 3815 CE LYS B 201 33.575 4.765 15.242 1.00 18.52 C ANISOU 3815 CE LYS B 201 2073 2601 2364 205 176 -617 C ATOM 3816 NZ LYS B 201 34.552 4.382 16.297 1.00 17.87 N ANISOU 3816 NZ LYS B 201 1988 2520 2283 212 175 -617 N ATOM 3817 N ILE B 202 35.141 10.216 12.283 1.00 17.44 N ANISOU 3817 N ILE B 202 1921 2536 2168 155 199 -609 N ATOM 3818 CA ILE B 202 35.574 11.298 11.412 1.00 17.17 C ANISOU 3818 CA ILE B 202 1881 2522 2120 145 205 -610 C ATOM 3819 C ILE B 202 35.534 10.822 9.965 1.00 21.34 C ANISOU 3819 C ILE B 202 2401 3067 2641 152 203 -627 C ATOM 3820 O ILE B 202 35.713 9.629 9.670 1.00 19.82 O ANISOU 3820 O ILE B 202 2201 2879 2451 166 197 -642 O ATOM 3821 CB ILE B 202 36.988 11.780 11.816 1.00 12.44 C ANISOU 3821 CB ILE B 202 1273 1942 1512 142 207 -613 C ATOM 3822 CG1 ILE B 202 37.310 13.163 11.235 1.00 15.53 C ANISOU 3822 CG1 ILE B 202 1662 2348 1890 128 214 -609 C ATOM 3823 CG2 ILE B 202 38.073 10.746 11.404 1.00 14.36 C ANISOU 3823 CG2 ILE B 202 1500 2206 1749 157 203 -635 C ATOM 3824 CD1 ILE B 202 38.635 13.725 11.747 1.00 9.22 C ANISOU 3824 CD1 ILE B 202 855 1565 1083 124 217 -610 C ATOM 3825 N LYS B 203 35.287 11.764 9.054 1.00 18.52 N ANISOU 3825 N LYS B 203 2044 2719 2274 143 207 -624 N ATOM 3826 CA LYS B 203 35.362 11.470 7.626 1.00 25.09 C ANISOU 3826 CA LYS B 203 2867 3571 3096 149 206 -640 C ATOM 3827 C LYS B 203 36.730 10.892 7.285 1.00 21.03 C ANISOU 3827 C LYS B 203 2336 3082 2573 159 204 -659 C ATOM 3828 O LYS B 203 37.753 11.294 7.856 1.00 14.69 O ANISOU 3828 O LYS B 203 1528 2290 1765 156 206 -658 O ATOM 3829 CB LYS B 203 35.153 12.735 6.791 1.00 23.93 C ANISOU 3829 CB LYS B 203 2722 3433 2938 136 213 -634 C ATOM 3830 CG LYS B 203 33.758 13.324 6.763 1.00 35.04 C ANISOU 3830 CG LYS B 203 4143 4819 4351 127 215 -618 C ATOM 3831 CD LYS B 203 33.736 14.515 5.793 1.00 40.87 C ANISOU 3831 CD LYS B 203 4881 5571 5076 117 222 -615 C ATOM 3832 CE LYS B 203 32.432 15.298 5.851 1.00 48.33 C ANISOU 3832 CE LYS B 203 5841 6495 6026 106 225 -597 C ATOM 3833 NZ LYS B 203 32.667 16.778 5.766 1.00 47.33 N ANISOU 3833 NZ LYS B 203 5718 6374 5889 91 233 -585 N ATOM 3834 N LYS B 204 36.744 9.957 6.329 1.00 18.31 N ANISOU 3834 N LYS B 204 1982 2748 2225 171 199 -676 N ATOM 3835 CA LYS B 204 38.005 9.378 5.873 1.00 18.04 C ANISOU 3835 CA LYS B 204 1932 2740 2182 181 197 -695 C ATOM 3836 C LYS B 204 38.924 10.435 5.280 1.00 19.99 C ANISOU 3836 C LYS B 204 2170 3012 2412 172 203 -696 C ATOM 3837 O LYS B 204 40.152 10.317 5.369 1.00 20.30 O ANISOU 3837 O LYS B 204 2198 3071 2444 176 202 -706 O ATOM 3838 CB LYS B 204 37.723 8.290 4.833 1.00 26.98 C ANISOU 3838 CB LYS B 204 3057 3880 3314 194 191 -712 C ATOM 3839 CG LYS B 204 38.916 7.411 4.471 1.00 42.68 C ANISOU 3839 CG LYS B 204 5029 5891 5296 207 186 -732 C ATOM 3840 CD LYS B 204 38.485 6.206 3.628 1.00 44.82 C ANISOU 3840 CD LYS B 204 5295 6163 5570 221 180 -749 C ATOM 3841 CE LYS B 204 39.685 5.436 3.075 1.00 43.74 C ANISOU 3841 CE LYS B 204 5141 6052 5425 233 176 -770 C ATOM 3842 NZ LYS B 204 40.221 6.063 1.831 1.00 45.12 N ANISOU 3842 NZ LYS B 204 5306 6255 5582 230 179 -778 N ATOM 3843 N LYS B 205 38.353 11.444 4.629 1.00 26.69 N ANISOU 3843 N LYS B 205 3024 3861 3254 161 208 -688 N ATOM 3844 CA LYS B 205 39.129 12.514 4.023 1.00 19.85 C ANISOU 3844 CA LYS B 205 2151 3018 2372 152 215 -688 C ATOM 3845 C LYS B 205 38.294 13.783 4.051 1.00 17.63 C ANISOU 3845 C LYS B 205 1884 2725 2092 136 221 -670 C ATOM 3846 O LYS B 205 37.085 13.738 3.812 1.00 24.26 O ANISOU 3846 O LYS B 205 2733 3547 2938 136 221 -663 O ATOM 3847 CB LYS B 205 39.535 12.149 2.592 1.00 24.49 C ANISOU 3847 CB LYS B 205 2726 3631 2948 160 213 -707 C ATOM 3848 CG LYS B 205 40.533 13.089 1.940 1.00 30.43 C ANISOU 3848 CG LYS B 205 3469 4411 3683 153 219 -710 C ATOM 3849 CD LYS B 205 40.854 12.603 0.522 1.00 47.05 C ANISOU 3849 CD LYS B 205 5560 6539 5776 162 217 -728 C ATOM 3850 CE LYS B 205 41.687 13.607 -0.279 1.00 56.46 C ANISOU 3850 CE LYS B 205 6744 7758 6950 154 224 -731 C ATOM 3851 NZ LYS B 205 43.123 13.634 0.130 1.00 62.19 N ANISOU 3851 NZ LYS B 205 7458 8503 7670 154 225 -737 N ATOM 3852 N GLY B 206 38.938 14.908 4.369 1.00 19.48 N ANISOU 3852 N GLY B 206 2117 2967 2319 124 228 -661 N ATOM 3853 CA GLY B 206 38.281 16.190 4.440 1.00 18.27 C ANISOU 3853 CA GLY B 206 1975 2802 2163 109 235 -644 C ATOM 3854 C GLY B 206 38.707 17.121 3.317 1.00 21.32 C ANISOU 3854 C GLY B 206 2356 3212 2534 101 241 -647 C ATOM 3855 O GLY B 206 39.387 16.725 2.368 1.00 18.38 O ANISOU 3855 O GLY B 206 1970 2863 2150 109 240 -663 O ATOM 3856 N LYS B 207 38.286 18.393 3.445 1.00 22.32 N ANISOU 3856 N LYS B 207 2492 3330 2658 86 248 -631 N ATOM 3857 CA LYS B 207 38.571 19.432 2.456 1.00 19.94 C ANISOU 3857 CA LYS B 207 2188 3047 2342 77 255 -630 C ATOM 3858 C LYS B 207 39.025 20.737 3.109 1.00 19.66 C ANISOU 3858 C LYS B 207 2156 3010 2302 61 262 -617 C ATOM 3859 O LYS B 207 38.900 21.808 2.501 1.00 17.76 O ANISOU 3859 O LYS B 207 1918 2775 2053 51 269 -610 O ATOM 3860 CB LYS B 207 37.347 19.673 1.560 1.00 24.20 C ANISOU 3860 CB LYS B 207 2736 3579 2881 76 257 -625 C ATOM 3861 CG LYS B 207 37.106 18.537 0.571 1.00 43.23 C ANISOU 3861 CG LYS B 207 5139 5999 5289 91 251 -642 C ATOM 3862 CD LYS B 207 35.768 18.618 -0.154 1.00 50.34 C ANISOU 3862 CD LYS B 207 6049 6888 6191 91 251 -637 C ATOM 3863 CE LYS B 207 35.576 17.388 -1.048 1.00 52.41 C ANISOU 3863 CE LYS B 207 6303 7159 6453 107 244 -655 C ATOM 3864 NZ LYS B 207 34.223 17.293 -1.661 1.00 54.54 N ANISOU 3864 NZ LYS B 207 6581 7416 6726 108 243 -651 N ATOM 3865 N ILE B 208 39.533 20.672 4.339 1.00 15.05 N ANISOU 3865 N ILE B 208 1574 2419 1727 59 261 -613 N ATOM 3866 CA ILE B 208 40.008 21.833 5.084 1.00 19.01 C ANISOU 3866 CA ILE B 208 2078 2918 2226 44 266 -601 C ATOM 3867 C ILE B 208 41.343 21.458 5.708 1.00 19.38 C ANISOU 3867 C ILE B 208 2113 2980 2272 49 264 -611 C ATOM 3868 O ILE B 208 41.478 20.364 6.264 1.00 15.40 O ANISOU 3868 O ILE B 208 1605 2470 1775 60 257 -617 O ATOM 3869 CB ILE B 208 39.011 22.265 6.188 1.00 20.09 C ANISOU 3869 CB ILE B 208 2232 3024 2377 36 266 -582 C ATOM 3870 CG1 ILE B 208 37.661 22.685 5.605 1.00 21.48 C ANISOU 3870 CG1 ILE B 208 2421 3186 2556 31 269 -571 C ATOM 3871 CG2 ILE B 208 39.598 23.378 7.086 1.00 12.26 C ANISOU 3871 CG2 ILE B 208 1242 2030 1385 21 271 -571 C ATOM 3872 CD1 ILE B 208 36.545 22.759 6.695 1.00 21.27 C ANISOU 3872 CD1 ILE B 208 2410 3125 2545 27 267 -554 C ATOM 3873 N TYR B 209 42.329 22.355 5.615 1.00 14.08 N ANISOU 3873 N TYR B 209 1434 2327 1589 39 270 -611 N ATOM 3874 CA TYR B 209 43.579 22.232 6.358 1.00 15.20 C ANISOU 3874 CA TYR B 209 1565 2480 1729 40 268 -618 C ATOM 3875 C TYR B 209 43.700 23.407 7.321 1.00 14.95 C ANISOU 3875 C TYR B 209 1541 2438 1700 24 273 -603 C ATOM 3876 O TYR B 209 43.195 24.499 7.059 1.00 18.01 O ANISOU 3876 O TYR B 209 1938 2821 2085 10 279 -591 O ATOM 3877 CB TYR B 209 44.812 22.170 5.433 1.00 11.56 C ANISOU 3877 CB TYR B 209 1087 2053 1252 43 270 -634 C ATOM 3878 CG TYR B 209 45.162 23.481 4.757 1.00 18.26 C ANISOU 3878 CG TYR B 209 1934 2916 2088 29 279 -630 C ATOM 3879 CD1 TYR B 209 44.573 23.844 3.544 1.00 16.82 C ANISOU 3879 CD1 TYR B 209 1755 2739 1897 28 283 -630 C ATOM 3880 CD2 TYR B 209 46.080 24.353 5.327 1.00 19.25 C ANISOU 3880 CD2 TYR B 209 2056 3050 2208 18 283 -627 C ATOM 3881 CE1 TYR B 209 44.897 25.040 2.930 1.00 21.85 C ANISOU 3881 CE1 TYR B 209 2391 3389 2523 15 291 -625 C ATOM 3882 CE2 TYR B 209 46.393 25.553 4.730 1.00 18.19 C ANISOU 3882 CE2 TYR B 209 1920 2928 2062 5 292 -623 C ATOM 3883 CZ TYR B 209 45.803 25.889 3.524 1.00 21.50 C ANISOU 3883 CZ TYR B 209 2343 3353 2475 3 296 -622 C ATOM 3884 OH TYR B 209 46.120 27.087 2.924 1.00 26.22 O ANISOU 3884 OH TYR B 209 2940 3962 3061 -9 304 -618 O ATOM 3885 N SER B 210 44.359 23.170 8.455 1.00 17.12 N ANISOU 3885 N SER B 210 1813 2711 1980 25 270 -603 N ATOM 3886 CA SER B 210 44.363 24.128 9.552 1.00 22.06 C ANISOU 3886 CA SER B 210 2448 3323 2612 11 273 -588 C ATOM 3887 C SER B 210 45.748 24.177 10.183 1.00 21.80 C ANISOU 3887 C SER B 210 2402 3307 2573 10 273 -596 C ATOM 3888 O SER B 210 46.160 23.198 10.815 1.00 15.80 O ANISOU 3888 O SER B 210 1637 2547 1819 21 267 -603 O ATOM 3889 CB SER B 210 43.317 23.755 10.598 1.00 21.31 C ANISOU 3889 CB SER B 210 2366 3196 2533 12 269 -576 C ATOM 3890 OG SER B 210 43.206 24.792 11.562 1.00 17.72 O ANISOU 3890 OG SER B 210 1921 2728 2083 -3 272 -561 O ATOM 3891 N LEU B 211 46.443 25.311 10.029 1.00 12.80 N ANISOU 3891 N LEU B 211 1259 2182 1425 -4 279 -594 N ATOM 3892 CA LEU B 211 47.728 25.588 10.675 1.00 19.29 C ANISOU 3892 CA LEU B 211 2070 3019 2241 -8 280 -600 C ATOM 3893 C LEU B 211 48.036 27.071 10.513 1.00 20.32 C ANISOU 3893 C LEU B 211 2202 3155 2363 -26 288 -593 C ATOM 3894 O LEU B 211 47.429 27.762 9.692 1.00 21.86 O ANISOU 3894 O LEU B 211 2403 3349 2554 -34 293 -587 O ATOM 3895 CB LEU B 211 48.889 24.752 10.102 1.00 19.63 C ANISOU 3895 CB LEU B 211 2095 3091 2275 5 277 -620 C ATOM 3896 CG LEU B 211 49.623 25.254 8.846 1.00 25.56 C ANISOU 3896 CG LEU B 211 2835 3870 3009 1 283 -629 C ATOM 3897 CD1 LEU B 211 50.824 24.374 8.500 1.00 19.91 C ANISOU 3897 CD1 LEU B 211 2100 3180 2284 14 279 -648 C ATOM 3898 CD2 LEU B 211 48.696 25.355 7.653 1.00 24.26 C ANISOU 3898 CD2 LEU B 211 2675 3702 2840 2 285 -627 C ATOM 3899 N ASN B 212 48.982 27.554 11.315 1.00 11.77 N ANISOU 3899 N ASN B 212 1113 2080 1278 -34 289 -593 N ATOM 3900 CA ASN B 212 49.407 28.953 11.251 1.00 14.22 C ANISOU 3900 CA ASN B 212 1424 2398 1582 -51 296 -587 C ATOM 3901 C ASN B 212 50.398 29.101 10.101 1.00 18.54 C ANISOU 3901 C ASN B 212 1955 2976 2111 -51 301 -601 C ATOM 3902 O ASN B 212 51.576 28.765 10.239 1.00 22.77 O ANISOU 3902 O ASN B 212 2478 3533 2642 -47 299 -613 O ATOM 3903 CB ASN B 212 50.017 29.374 12.585 1.00 9.83 C ANISOU 3903 CB ASN B 212 867 1837 1030 -59 295 -583 C ATOM 3904 CG ASN B 212 50.310 30.865 12.669 1.00 22.63 C ANISOU 3904 CG ASN B 212 2492 3461 2646 -79 303 -576 C ATOM 3905 OD1 ASN B 212 50.226 31.598 11.680 1.00 18.19 O ANISOU 3905 OD1 ASN B 212 1930 2908 2075 -87 309 -575 O ATOM 3906 ND2 ASN B 212 50.658 31.318 13.868 1.00 20.26 N ANISOU 3906 ND2 ASN B 212 2194 3154 2352 -87 302 -571 N ATOM 3907 N GLU B 213 49.935 29.606 8.950 1.00 17.18 N ANISOU 3907 N GLU B 213 1786 2808 1932 -55 306 -599 N ATOM 3908 CA GLU B 213 50.853 29.798 7.829 1.00 22.50 C ANISOU 3908 CA GLU B 213 2446 3512 2589 -55 311 -611 C ATOM 3909 C GLU B 213 51.753 31.015 8.019 1.00 28.11 C ANISOU 3909 C GLU B 213 3153 4235 3292 -71 317 -609 C ATOM 3910 O GLU B 213 52.656 31.240 7.202 1.00 22.56 O ANISOU 3910 O GLU B 213 2437 3558 2576 -73 322 -620 O ATOM 3911 CB GLU B 213 50.086 29.892 6.500 1.00 18.76 C ANISOU 3911 CB GLU B 213 1978 3040 2111 -53 314 -610 C ATOM 3912 CG GLU B 213 49.532 28.547 6.041 1.00 20.07 C ANISOU 3912 CG GLU B 213 2142 3204 2281 -35 308 -618 C ATOM 3913 CD GLU B 213 48.957 28.583 4.629 1.00 23.77 C ANISOU 3913 CD GLU B 213 2612 3679 2741 -32 311 -620 C ATOM 3914 OE1 GLU B 213 49.719 28.709 3.646 1.00 26.37 O ANISOU 3914 OE1 GLU B 213 2929 4034 3056 -31 315 -630 O ATOM 3915 OE2 GLU B 213 47.722 28.528 4.512 1.00 22.88 O ANISOU 3915 OE2 GLU B 213 2512 3546 2635 -31 310 -610 O ATOM 3916 N GLY B 214 51.545 31.789 9.087 1.00 29.75 N ANISOU 3916 N GLY B 214 3370 4426 3508 -84 318 -597 N ATOM 3917 CA GLY B 214 52.463 32.868 9.403 1.00 27.07 C ANISOU 3917 CA GLY B 214 3026 4098 3162 -99 324 -597 C ATOM 3918 C GLY B 214 53.886 32.404 9.620 1.00 27.90 C ANISOU 3918 C GLY B 214 3113 4228 3260 -93 322 -612 C ATOM 3919 O GLY B 214 54.817 33.190 9.430 1.00 37.11 O ANISOU 3919 O GLY B 214 4272 5413 4417 -104 327 -616 O ATOM 3920 N TYR B 215 54.080 31.135 9.986 1.00 23.54 N ANISOU 3920 N TYR B 215 2555 3678 2713 -77 313 -621 N ATOM 3921 CA TYR B 215 55.407 30.563 10.184 1.00 34.15 C ANISOU 3921 CA TYR B 215 3881 5045 4050 -70 310 -636 C ATOM 3922 C TYR B 215 55.945 29.877 8.935 1.00 22.19 C ANISOU 3922 C TYR B 215 2352 3555 2523 -59 310 -652 C ATOM 3923 O TYR B 215 56.786 28.978 9.059 1.00 29.14 O ANISOU 3923 O TYR B 215 3219 4451 3401 -47 305 -665 O ATOM 3924 CB TYR B 215 55.396 29.512 11.303 1.00 44.30 C ANISOU 3924 CB TYR B 215 5166 6319 5347 -58 301 -638 C ATOM 3925 CG TYR B 215 55.112 29.995 12.705 1.00 53.71 C ANISOU 3925 CG TYR B 215 6367 7489 6549 -67 300 -626 C ATOM 3926 CD1 TYR B 215 56.107 30.588 13.472 1.00 53.57 C ANISOU 3926 CD1 TYR B 215 6343 7482 6529 -76 301 -628 C ATOM 3927 CD2 TYR B 215 53.861 29.805 13.283 1.00 50.18 C ANISOU 3927 CD2 TYR B 215 5938 7013 6117 -65 297 -613 C ATOM 3928 CE1 TYR B 215 55.852 31.012 14.759 1.00 55.35 C ANISOU 3928 CE1 TYR B 215 6578 7688 6764 -83 299 -618 C ATOM 3929 CE2 TYR B 215 53.598 30.224 14.570 1.00 50.35 C ANISOU 3929 CE2 TYR B 215 5968 7014 6149 -73 295 -602 C ATOM 3930 CZ TYR B 215 54.598 30.829 15.304 1.00 55.48 C ANISOU 3930 CZ TYR B 215 6610 7674 6795 -82 296 -604 C ATOM 3931 OH TYR B 215 54.343 31.248 16.589 1.00 60.63 O ANISOU 3931 OH TYR B 215 7271 8307 7457 -89 295 -594 O ATOM 3932 N ALA B 216 55.475 30.258 7.742 1.00 18.90 N ANISOU 3932 N ALA B 216 1938 3142 2099 -61 316 -650 N ATOM 3933 CA ALA B 216 55.901 29.552 6.535 1.00 17.15 C ANISOU 3933 CA ALA B 216 1704 2943 1867 -49 315 -664 C ATOM 3934 C ALA B 216 57.408 29.626 6.339 1.00 25.11 C ANISOU 3934 C ALA B 216 2695 3983 2863 -50 317 -678 C ATOM 3935 O ALA B 216 58.016 28.672 5.837 1.00 29.27 O ANISOU 3935 O ALA B 216 3209 4527 3384 -37 312 -693 O ATOM 3936 CB ALA B 216 55.177 30.105 5.307 1.00 19.55 C ANISOU 3936 CB ALA B 216 2015 3247 2164 -54 322 -659 C ATOM 3937 N LYS B 217 58.032 30.735 6.750 1.00 27.49 N ANISOU 3937 N LYS B 217 2995 4289 3160 -66 322 -674 N ATOM 3938 CA LYS B 217 59.477 30.867 6.597 1.00 32.56 C ANISOU 3938 CA LYS B 217 3620 4961 3791 -68 324 -687 C ATOM 3939 C LYS B 217 60.215 29.826 7.429 1.00 34.81 C ANISOU 3939 C LYS B 217 3894 5252 4079 -56 316 -698 C ATOM 3940 O LYS B 217 61.322 29.406 7.065 1.00 26.89 O ANISOU 3940 O LYS B 217 2876 4275 3067 -49 314 -713 O ATOM 3941 CB LYS B 217 59.907 32.280 7.009 1.00 38.62 C ANISOU 3941 CB LYS B 217 4390 5729 4555 -88 332 -680 C ATOM 3942 CG LYS B 217 61.372 32.622 6.758 1.00 42.38 C ANISOU 3942 CG LYS B 217 4849 6236 5018 -93 336 -692 C ATOM 3943 CD LYS B 217 61.672 34.068 7.129 1.00 35.73 C ANISOU 3943 CD LYS B 217 4010 5392 4173 -114 344 -684 C ATOM 3944 CE LYS B 217 61.632 34.272 8.634 1.00 35.26 C ANISOU 3944 CE LYS B 217 3957 5316 4125 -120 340 -677 C ATOM 3945 NZ LYS B 217 61.953 35.679 9.046 1.00 29.51 N ANISOU 3945 NZ LYS B 217 3233 4587 3394 -140 347 -670 N ATOM 3946 N ASP B 218 59.590 29.354 8.509 1.00 27.99 N ANISOU 3946 N ASP B 218 3040 4365 3230 -51 309 -691 N ATOM 3947 CA ASP B 218 60.199 28.391 9.411 1.00 25.51 C ANISOU 3947 CA ASP B 218 2718 4054 2921 -39 301 -700 C ATOM 3948 C ASP B 218 59.798 26.960 9.130 1.00 27.18 C ANISOU 3948 C ASP B 218 2929 4263 3137 -19 293 -707 C ATOM 3949 O ASP B 218 60.393 26.050 9.720 1.00 29.09 O ANISOU 3949 O ASP B 218 3161 4510 3381 -7 286 -716 O ATOM 3950 CB ASP B 218 59.810 28.711 10.858 1.00 30.74 C ANISOU 3950 CB ASP B 218 3391 4692 3595 -46 299 -687 C ATOM 3951 CG ASP B 218 60.325 30.043 11.314 1.00 35.89 C ANISOU 3951 CG ASP B 218 4044 5349 4244 -65 305 -682 C ATOM 3952 OD1 ASP B 218 61.168 30.632 10.597 1.00 26.87 O ANISOU 3952 OD1 ASP B 218 2891 4230 3089 -72 311 -689 O ATOM 3953 OD2 ASP B 218 59.870 30.509 12.382 1.00 50.80 O ANISOU 3953 OD2 ASP B 218 5943 7216 6142 -73 304 -670 O ATOM 3954 N PHE B 219 58.845 26.736 8.222 1.00 24.44 N ANISOU 3954 N PHE B 219 2589 3908 2791 -15 294 -704 N ATOM 3955 CA PHE B 219 58.338 25.392 7.978 1.00 23.23 C ANISOU 3955 CA PHE B 219 2435 3748 2643 4 287 -710 C ATOM 3956 C PHE B 219 59.458 24.447 7.572 1.00 33.27 C ANISOU 3956 C PHE B 219 3689 5046 3906 18 282 -730 C ATOM 3957 O PHE B 219 60.382 24.826 6.847 1.00 37.12 O ANISOU 3957 O PHE B 219 4163 5559 4380 14 286 -739 O ATOM 3958 CB PHE B 219 57.279 25.403 6.872 1.00 25.14 C ANISOU 3958 CB PHE B 219 2685 3982 2884 5 289 -706 C ATOM 3959 CG PHE B 219 55.930 25.896 7.317 1.00 27.82 C ANISOU 3959 CG PHE B 219 3044 4291 3236 -2 291 -688 C ATOM 3960 CD1 PHE B 219 55.677 26.162 8.649 1.00 29.78 C ANISOU 3960 CD1 PHE B 219 3302 4518 3495 -8 289 -677 C ATOM 3961 CD2 PHE B 219 54.909 26.068 6.398 1.00 31.77 C ANISOU 3961 CD2 PHE B 219 3553 4782 3735 -3 294 -682 C ATOM 3962 CE1 PHE B 219 54.440 26.606 9.057 1.00 29.63 C ANISOU 3962 CE1 PHE B 219 3300 4471 3487 -15 291 -661 C ATOM 3963 CE2 PHE B 219 53.663 26.514 6.802 1.00 33.83 C ANISOU 3963 CE2 PHE B 219 3832 5014 4006 -10 296 -666 C ATOM 3964 CZ PHE B 219 53.437 26.788 8.129 1.00 30.27 C ANISOU 3964 CZ PHE B 219 3390 4543 3567 -16 294 -655 C ATOM 3965 N ASP B 220 59.374 23.212 8.050 1.00 29.62 N ANISOU 3965 N ASP B 220 3225 4577 3452 34 274 -736 N ATOM 3966 CA ASP B 220 60.169 22.154 7.459 1.00 33.46 C ANISOU 3966 CA ASP B 220 3697 5086 3932 50 268 -754 C ATOM 3967 C ASP B 220 59.702 21.918 6.020 1.00 32.87 C ANISOU 3967 C ASP B 220 3620 5018 3850 55 270 -759 C ATOM 3968 O ASP B 220 58.545 22.191 5.684 1.00 27.27 O ANISOU 3968 O ASP B 220 2925 4291 3146 51 273 -749 O ATOM 3969 CB ASP B 220 60.067 20.879 8.299 1.00 42.54 C ANISOU 3969 CB ASP B 220 4847 6224 5092 66 259 -758 C ATOM 3970 CG ASP B 220 59.515 19.701 7.526 1.00 58.93 C ANISOU 3970 CG ASP B 220 6923 8298 7171 83 254 -766 C ATOM 3971 OD1 ASP B 220 60.271 19.064 6.765 1.00 64.47 O ANISOU 3971 OD1 ASP B 220 7610 9022 7862 93 251 -782 O ATOM 3972 OD2 ASP B 220 58.317 19.400 7.692 1.00 69.31 O ANISOU 3972 OD2 ASP B 220 8251 9588 8496 86 252 -757 O ATOM 3973 N PRO B 221 60.597 21.452 5.140 1.00 31.63 N ANISOU 3973 N PRO B 221 3448 4889 3681 63 269 -775 N ATOM 3974 CA PRO B 221 60.210 21.263 3.733 1.00 33.13 C ANISOU 3974 CA PRO B 221 3636 5087 3863 67 271 -781 C ATOM 3975 C PRO B 221 59.014 20.350 3.537 1.00 30.09 C ANISOU 3975 C PRO B 221 3261 4682 3489 79 266 -779 C ATOM 3976 O PRO B 221 58.258 20.537 2.574 1.00 21.28 O ANISOU 3976 O PRO B 221 2151 3564 2371 78 269 -777 O ATOM 3977 CB PRO B 221 61.475 20.660 3.104 1.00 35.76 C ANISOU 3977 CB PRO B 221 3950 5453 4185 77 269 -800 C ATOM 3978 CG PRO B 221 62.594 21.155 3.955 1.00 33.12 C ANISOU 3978 CG PRO B 221 3608 5130 3847 69 270 -802 C ATOM 3979 CD PRO B 221 62.042 21.233 5.352 1.00 35.20 C ANISOU 3979 CD PRO B 221 3883 5366 4125 66 267 -789 C ATOM 3980 N ALA B 222 58.828 19.350 4.403 1.00 31.55 N ANISOU 3980 N ALA B 222 3448 4853 3685 91 258 -781 N ATOM 3981 CA ALA B 222 57.694 18.444 4.243 1.00 28.42 C ANISOU 3981 CA ALA B 222 3062 4437 3300 103 252 -780 C ATOM 3982 C ALA B 222 56.368 19.169 4.465 1.00 26.84 C ANISOU 3982 C ALA B 222 2879 4209 3108 92 256 -761 C ATOM 3983 O ALA B 222 55.398 18.933 3.738 1.00 26.39 O ANISOU 3983 O ALA B 222 2830 4144 3054 95 256 -759 O ATOM 3984 CB ALA B 222 57.833 17.252 5.190 1.00 24.09 C ANISOU 3984 CB ALA B 222 2512 3880 2762 117 244 -785 C ATOM 3985 N VAL B 223 56.299 20.044 5.470 1.00 27.72 N ANISOU 3985 N VAL B 223 2999 4308 3225 79 260 -748 N ATOM 3986 CA VAL B 223 55.083 20.829 5.683 1.00 23.05 C ANISOU 3986 CA VAL B 223 2425 3691 2641 67 264 -730 C ATOM 3987 C VAL B 223 54.850 21.768 4.506 1.00 22.10 C ANISOU 3987 C VAL B 223 2305 3580 2510 57 272 -727 C ATOM 3988 O VAL B 223 53.727 21.894 4.003 1.00 19.61 O ANISOU 3988 O VAL B 223 2002 3251 2199 55 274 -719 O ATOM 3989 CB VAL B 223 55.154 21.598 7.015 1.00 21.92 C ANISOU 3989 CB VAL B 223 2289 3533 2505 55 266 -716 C ATOM 3990 CG1 VAL B 223 53.936 22.522 7.167 1.00 17.76 C ANISOU 3990 CG1 VAL B 223 1780 2982 1985 42 271 -698 C ATOM 3991 CG2 VAL B 223 55.251 20.628 8.195 1.00 20.22 C ANISOU 3991 CG2 VAL B 223 2075 3306 2301 66 258 -718 C ATOM 3992 N THR B 224 55.913 22.443 4.054 1.00 23.46 N ANISOU 3992 N THR B 224 2466 3778 2669 49 277 -733 N ATOM 3993 CA THR B 224 55.819 23.354 2.915 1.00 21.72 C ANISOU 3993 CA THR B 224 2246 3569 2437 40 286 -730 C ATOM 3994 C THR B 224 55.216 22.658 1.704 1.00 27.19 C ANISOU 3994 C THR B 224 2938 4266 3127 51 284 -738 C ATOM 3995 O THR B 224 54.308 23.187 1.055 1.00 25.73 O ANISOU 3995 O THR B 224 2763 4072 2940 45 288 -729 O ATOM 3996 CB THR B 224 57.209 23.897 2.563 1.00 26.22 C ANISOU 3996 CB THR B 224 2801 4170 2993 34 290 -740 C ATOM 3997 OG1 THR B 224 57.733 24.652 3.660 1.00 25.58 O ANISOU 3997 OG1 THR B 224 2721 4084 2914 21 293 -732 O ATOM 3998 CG2 THR B 224 57.150 24.763 1.309 1.00 29.19 C ANISOU 3998 CG2 THR B 224 3176 4559 3355 25 299 -738 C ATOM 3999 N GLU B 225 55.716 21.457 1.390 1.00 23.07 N ANISOU 3999 N GLU B 225 2404 3757 2602 67 277 -754 N ATOM 4000 CA GLU B 225 55.217 20.715 0.240 1.00 17.18 C ANISOU 4000 CA GLU B 225 1657 3018 1854 79 274 -763 C ATOM 4001 C GLU B 225 53.771 20.282 0.444 1.00 16.07 C ANISOU 4001 C GLU B 225 1531 2848 1727 83 270 -754 C ATOM 4002 O GLU B 225 52.950 20.397 -0.472 1.00 22.30 O ANISOU 4002 O GLU B 225 2325 3634 2513 84 272 -752 O ATOM 4003 CB GLU B 225 56.110 19.501 -0.023 1.00 18.39 C ANISOU 4003 CB GLU B 225 1794 3190 2003 96 266 -783 C ATOM 4004 CG GLU B 225 55.702 18.701 -1.234 1.00 26.49 C ANISOU 4004 CG GLU B 225 2816 4223 3024 108 263 -794 C ATOM 4005 CD GLU B 225 56.672 17.587 -1.545 1.00 36.54 C ANISOU 4005 CD GLU B 225 4073 5518 4293 124 256 -814 C ATOM 4006 OE1 GLU B 225 57.820 17.642 -1.053 1.00 42.73 O ANISOU 4006 OE1 GLU B 225 4846 6317 5072 123 256 -819 O ATOM 4007 OE2 GLU B 225 56.274 16.641 -2.255 1.00 39.37 O ANISOU 4007 OE2 GLU B 225 4429 5878 4652 137 251 -824 O ATOM 4008 N TYR B 226 53.439 19.784 1.636 1.00 22.42 N ANISOU 4008 N TYR B 226 2342 3631 2545 87 265 -749 N ATOM 4009 CA TYR B 226 52.070 19.334 1.884 1.00 26.40 C ANISOU 4009 CA TYR B 226 2861 4107 3063 91 261 -740 C ATOM 4010 C TYR B 226 51.076 20.472 1.701 1.00 18.54 C ANISOU 4010 C TYR B 226 1880 3096 2068 77 268 -723 C ATOM 4011 O TYR B 226 50.010 20.287 1.104 1.00 25.37 O ANISOU 4011 O TYR B 226 2753 3949 2936 80 268 -720 O ATOM 4012 CB TYR B 226 51.946 18.727 3.279 1.00 22.03 C ANISOU 4012 CB TYR B 226 2314 3534 2524 96 255 -736 C ATOM 4013 CG TYR B 226 50.537 18.272 3.578 1.00 18.42 C ANISOU 4013 CG TYR B 226 1871 3047 2081 100 252 -726 C ATOM 4014 CD1 TYR B 226 50.024 17.120 3.003 1.00 17.97 C ANISOU 4014 CD1 TYR B 226 1814 2988 2028 115 246 -736 C ATOM 4015 CD2 TYR B 226 49.718 19.008 4.421 1.00 16.72 C ANISOU 4015 CD2 TYR B 226 1671 2806 1875 88 255 -708 C ATOM 4016 CE1 TYR B 226 48.724 16.709 3.264 1.00 18.85 C ANISOU 4016 CE1 TYR B 226 1938 3071 2152 118 242 -728 C ATOM 4017 CE2 TYR B 226 48.425 18.611 4.679 1.00 23.82 C ANISOU 4017 CE2 TYR B 226 2585 3679 2788 92 252 -699 C ATOM 4018 CZ TYR B 226 47.935 17.464 4.110 1.00 22.22 C ANISOU 4018 CZ TYR B 226 2380 3473 2588 106 246 -709 C ATOM 4019 OH TYR B 226 46.640 17.087 4.383 1.00 28.83 O ANISOU 4019 OH TYR B 226 3231 4285 3439 109 243 -700 O ATOM 4020 N ILE B 227 51.404 21.659 2.202 1.00 22.75 N ANISOU 4020 N ILE B 227 2417 3629 2599 61 275 -712 N ATOM 4021 CA ILE B 227 50.487 22.783 2.056 1.00 21.15 C ANISOU 4021 CA ILE B 227 2228 3411 2397 47 282 -696 C ATOM 4022 C ILE B 227 50.380 23.186 0.590 1.00 22.35 C ANISOU 4022 C ILE B 227 2376 3579 2535 45 287 -700 C ATOM 4023 O ILE B 227 49.301 23.549 0.112 1.00 19.67 O ANISOU 4023 O ILE B 227 2048 3227 2198 42 290 -691 O ATOM 4024 CB ILE B 227 50.932 23.951 2.955 1.00 15.30 C ANISOU 4024 CB ILE B 227 1490 2666 1656 30 288 -684 C ATOM 4025 CG1 ILE B 227 50.892 23.526 4.422 1.00 15.46 C ANISOU 4025 CG1 ILE B 227 1516 2668 1691 32 282 -679 C ATOM 4026 CG2 ILE B 227 50.077 25.215 2.720 1.00 21.93 C ANISOU 4026 CG2 ILE B 227 2344 3493 2495 15 296 -667 C ATOM 4027 CD1 ILE B 227 49.541 22.965 4.876 1.00 22.82 C ANISOU 4027 CD1 ILE B 227 2462 3569 2637 38 278 -670 C ATOM 4028 N GLN B 228 51.487 23.090 -0.155 1.00 20.08 N ANISOU 4028 N GLN B 228 2073 3322 2235 49 289 -714 N ATOM 4029 CA GLN B 228 51.424 23.320 -1.597 1.00 21.79 C ANISOU 4029 CA GLN B 228 2285 3556 2438 50 293 -719 C ATOM 4030 C GLN B 228 50.447 22.368 -2.275 1.00 21.03 C ANISOU 4030 C GLN B 228 2193 3452 2346 63 287 -725 C ATOM 4031 O GLN B 228 49.694 22.774 -3.166 1.00 20.45 O ANISOU 4031 O GLN B 228 2125 3377 2268 61 291 -720 O ATOM 4032 CB GLN B 228 52.818 23.188 -2.219 1.00 38.11 C ANISOU 4032 CB GLN B 228 4334 5656 4491 53 294 -735 C ATOM 4033 CG GLN B 228 53.795 24.293 -1.820 1.00 53.33 C ANISOU 4033 CG GLN B 228 6257 7595 6411 39 301 -731 C ATOM 4034 CD GLN B 228 53.262 25.684 -2.110 1.00 62.08 C ANISOU 4034 CD GLN B 228 7377 8696 7516 22 311 -715 C ATOM 4035 OE1 GLN B 228 52.962 26.450 -1.192 1.00 71.49 O ANISOU 4035 OE1 GLN B 228 8578 9869 8714 10 314 -701 O ATOM 4036 NE2 GLN B 228 53.145 26.020 -3.389 1.00 58.84 N ANISOU 4036 NE2 GLN B 228 6963 8300 7093 22 316 -718 N ATOM 4037 N ARG B 229 50.431 21.098 -1.855 1.00 26.51 N ANISOU 4037 N ARG B 229 2883 4140 3049 77 278 -734 N ATOM 4038 CA ARG B 229 49.498 20.140 -2.444 1.00 22.89 C ANISOU 4038 CA ARG B 229 2428 3673 2596 90 272 -739 C ATOM 4039 C ARG B 229 48.051 20.519 -2.152 1.00 25.01 C ANISOU 4039 C ARG B 229 2714 3912 2875 84 274 -723 C ATOM 4040 O ARG B 229 47.155 20.258 -2.970 1.00 20.79 O ANISOU 4040 O ARG B 229 2185 3374 2340 89 272 -724 O ATOM 4041 CB ARG B 229 49.784 18.747 -1.890 1.00 26.42 C ANISOU 4041 CB ARG B 229 2868 4118 3052 106 262 -751 C ATOM 4042 CG ARG B 229 51.136 18.171 -2.284 1.00 28.96 C ANISOU 4042 CG ARG B 229 3172 4468 3363 114 260 -770 C ATOM 4043 CD ARG B 229 51.393 16.870 -1.538 1.00 21.75 C ANISOU 4043 CD ARG B 229 2255 3550 2461 129 250 -779 C ATOM 4044 NE ARG B 229 50.325 15.904 -1.749 1.00 27.90 N ANISOU 4044 NE ARG B 229 3040 4312 3250 140 244 -782 N ATOM 4045 CZ ARG B 229 50.319 15.007 -2.730 1.00 34.68 C ANISOU 4045 CZ ARG B 229 3891 5183 4104 153 239 -797 C ATOM 4046 NH1 ARG B 229 51.337 14.943 -3.580 1.00 34.25 N ANISOU 4046 NH1 ARG B 229 3821 5159 4036 157 240 -811 N ATOM 4047 NH2 ARG B 229 49.302 14.169 -2.853 1.00 34.35 N ANISOU 4047 NH2 ARG B 229 3855 5125 4072 162 233 -799 N ATOM 4048 N LYS B 230 47.807 21.153 -1.002 1.00 27.88 N ANISOU 4048 N LYS B 230 3089 4257 3248 73 276 -708 N ATOM 4049 CA LYS B 230 46.457 21.552 -0.639 1.00 20.92 C ANISOU 4049 CA LYS B 230 2225 3346 2377 67 277 -691 C ATOM 4050 C LYS B 230 45.975 22.719 -1.481 1.00 19.24 C ANISOU 4050 C LYS B 230 2019 3137 2155 55 286 -682 C ATOM 4051 O LYS B 230 44.776 22.830 -1.758 1.00 17.45 O ANISOU 4051 O LYS B 230 1804 2893 1933 54 286 -673 O ATOM 4052 CB LYS B 230 46.387 21.911 0.851 1.00 23.47 C ANISOU 4052 CB LYS B 230 2557 3648 2711 59 277 -678 C ATOM 4053 CG LYS B 230 46.699 20.759 1.787 1.00 20.75 C ANISOU 4053 CG LYS B 230 2209 3297 2378 70 268 -685 C ATOM 4054 CD LYS B 230 45.809 19.567 1.501 1.00 22.26 C ANISOU 4054 CD LYS B 230 2403 3477 2578 85 261 -691 C ATOM 4055 CE LYS B 230 46.578 18.460 0.746 1.00 21.66 C ANISOU 4055 CE LYS B 230 2311 3423 2495 100 256 -712 C ATOM 4056 NZ LYS B 230 45.662 17.396 0.223 1.00 23.65 N ANISOU 4056 NZ LYS B 230 2565 3666 2753 113 249 -719 N ATOM 4057 N LYS B 231 46.879 23.610 -1.865 1.00 17.60 N ANISOU 4057 N LYS B 231 1804 2949 1934 46 293 -683 N ATOM 4058 CA LYS B 231 46.507 24.759 -2.674 1.00 17.84 C ANISOU 4058 CA LYS B 231 1840 2983 1954 35 302 -674 C ATOM 4059 C LYS B 231 46.508 24.452 -4.164 1.00 22.58 C ANISOU 4059 C LYS B 231 2432 3604 2542 43 302 -685 C ATOM 4060 O LYS B 231 45.730 25.054 -4.911 1.00 28.27 O ANISOU 4060 O LYS B 231 3161 4321 3258 39 307 -678 O ATOM 4061 CB LYS B 231 47.452 25.925 -2.380 1.00 16.26 C ANISOU 4061 CB LYS B 231 1637 2795 1747 20 309 -668 C ATOM 4062 CG LYS B 231 47.435 26.367 -0.918 1.00 24.78 C ANISOU 4062 CG LYS B 231 2724 3853 2837 11 309 -656 C ATOM 4063 CD LYS B 231 48.523 27.380 -0.645 1.00 22.73 C ANISOU 4063 CD LYS B 231 2458 3608 2569 -2 316 -654 C ATOM 4064 CE LYS B 231 48.402 27.956 0.758 1.00 24.36 C ANISOU 4064 CE LYS B 231 2674 3793 2787 -14 316 -640 C ATOM 4065 NZ LYS B 231 49.524 28.879 1.047 1.00 26.12 N ANISOU 4065 NZ LYS B 231 2891 4031 3002 -26 322 -640 N ATOM 4066 N PHE B 232 47.403 23.567 -4.609 1.00 24.73 N ANISOU 4066 N PHE B 232 2689 3898 2808 55 298 -703 N ATOM 4067 CA PHE B 232 47.576 23.211 -6.022 1.00 22.44 C ANISOU 4067 CA PHE B 232 2389 3631 2506 64 298 -716 C ATOM 4068 C PHE B 232 47.508 21.690 -6.136 1.00 21.53 C ANISOU 4068 C PHE B 232 2267 3517 2396 82 287 -732 C ATOM 4069 O PHE B 232 48.544 21.014 -6.205 1.00 28.28 O ANISOU 4069 O PHE B 232 3107 4391 3247 91 283 -747 O ATOM 4070 CB PHE B 232 48.901 23.763 -6.542 1.00 18.65 C ANISOU 4070 CB PHE B 232 1895 3181 2010 60 304 -724 C ATOM 4071 CG PHE B 232 49.054 25.258 -6.336 1.00 26.65 C ANISOU 4071 CG PHE B 232 2916 4192 3018 41 314 -709 C ATOM 4072 CD1 PHE B 232 48.707 26.154 -7.334 1.00 26.13 C ANISOU 4072 CD1 PHE B 232 2854 4133 2941 35 323 -703 C ATOM 4073 CD2 PHE B 232 49.538 25.764 -5.138 1.00 32.09 C ANISOU 4073 CD2 PHE B 232 3607 4873 3713 31 316 -701 C ATOM 4074 CE1 PHE B 232 48.846 27.524 -7.138 1.00 20.57 C ANISOU 4074 CE1 PHE B 232 2156 3427 2232 18 332 -689 C ATOM 4075 CE2 PHE B 232 49.672 27.137 -4.942 1.00 26.16 C ANISOU 4075 CE2 PHE B 232 2862 4120 2958 14 325 -688 C ATOM 4076 CZ PHE B 232 49.326 28.007 -5.943 1.00 25.84 C ANISOU 4076 CZ PHE B 232 2826 4086 2907 8 333 -682 C ATOM 4077 N PRO B 233 46.311 21.115 -6.102 1.00 19.34 N ANISOU 4077 N PRO B 233 1999 3219 2129 88 282 -729 N ATOM 4078 CA PRO B 233 46.184 19.644 -6.002 1.00 23.24 C ANISOU 4078 CA PRO B 233 2488 3710 2632 105 272 -742 C ATOM 4079 C PRO B 233 46.742 18.925 -7.219 1.00 23.27 C ANISOU 4079 C PRO B 233 2476 3740 2624 117 269 -762 C ATOM 4080 O PRO B 233 46.461 19.288 -8.370 1.00 28.17 O ANISOU 4080 O PRO B 233 3096 4374 3235 117 273 -764 O ATOM 4081 CB PRO B 233 44.668 19.427 -5.852 1.00 21.12 C ANISOU 4081 CB PRO B 233 2235 3414 2376 106 269 -733 C ATOM 4082 CG PRO B 233 44.151 20.757 -5.342 1.00 21.27 C ANISOU 4082 CG PRO B 233 2267 3417 2397 89 277 -712 C ATOM 4083 CD PRO B 233 45.009 21.787 -6.013 1.00 16.46 C ANISOU 4083 CD PRO B 233 1652 2832 1772 80 286 -712 C ATOM 4084 N PRO B 234 47.567 17.902 -6.993 1.00 26.14 N ANISOU 4084 N PRO B 234 2828 4115 2989 129 262 -777 N ATOM 4085 CA PRO B 234 48.186 17.171 -8.115 1.00 29.49 C ANISOU 4085 CA PRO B 234 3237 4566 3403 141 258 -796 C ATOM 4086 C PRO B 234 47.240 16.240 -8.862 1.00 29.87 C ANISOU 4086 C PRO B 234 3287 4609 3455 154 252 -805 C ATOM 4087 O PRO B 234 47.605 15.758 -9.942 1.00 26.80 O ANISOU 4087 O PRO B 234 2886 4242 3056 163 250 -820 O ATOM 4088 CB PRO B 234 49.316 16.385 -7.436 1.00 26.62 C ANISOU 4088 CB PRO B 234 2861 4211 3041 149 253 -808 C ATOM 4089 CG PRO B 234 48.837 16.194 -6.030 1.00 36.51 C ANISOU 4089 CG PRO B 234 4125 5436 4311 147 250 -797 C ATOM 4090 CD PRO B 234 48.043 17.436 -5.679 1.00 25.80 C ANISOU 4090 CD PRO B 234 2785 4062 2958 130 257 -776 C ATOM 4091 N ASP B 235 46.057 15.953 -8.322 1.00 30.18 N ANISOU 4091 N ASP B 235 3339 4620 3508 154 248 -796 N ATOM 4092 CA ASP B 235 45.103 15.048 -8.955 1.00 30.82 C ANISOU 4092 CA ASP B 235 3422 4694 3595 166 242 -804 C ATOM 4093 C ASP B 235 43.886 15.762 -9.540 1.00 28.40 C ANISOU 4093 C ASP B 235 3127 4376 3286 159 246 -792 C ATOM 4094 O ASP B 235 42.859 15.116 -9.768 1.00 41.53 O ANISOU 4094 O ASP B 235 4797 6026 4958 166 241 -794 O ATOM 4095 CB ASP B 235 44.657 13.989 -7.946 1.00 33.92 C ANISOU 4095 CB ASP B 235 3820 5064 4006 174 233 -805 C ATOM 4096 CG ASP B 235 43.887 14.586 -6.790 1.00 32.75 C ANISOU 4096 CG ASP B 235 3688 4886 3870 163 236 -785 C ATOM 4097 OD1 ASP B 235 43.860 15.832 -6.680 1.00 34.37 O ANISOU 4097 OD1 ASP B 235 3900 5090 4070 149 244 -771 O ATOM 4098 OD2 ASP B 235 43.346 13.817 -5.971 1.00 31.63 O ANISOU 4098 OD2 ASP B 235 3553 4723 3744 169 230 -783 O ATOM 4099 N ASN B 236 43.965 17.077 -9.762 1.00 31.44 N ANISOU 4099 N ASN B 236 3517 4766 3662 145 256 -780 N ATOM 4100 CA ASN B 236 42.884 17.905 -10.313 1.00 54.90 C ANISOU 4100 CA ASN B 236 6500 7729 6631 138 261 -767 C ATOM 4101 C ASN B 236 41.664 18.028 -9.412 1.00 54.03 C ANISOU 4101 C ASN B 236 6408 7585 6537 132 260 -752 C ATOM 4102 O ASN B 236 40.608 18.479 -9.881 1.00 61.91 O ANISOU 4102 O ASN B 236 7415 8573 7534 129 263 -743 O ATOM 4103 CB ASN B 236 42.371 17.408 -11.669 1.00 72.19 C ANISOU 4103 CB ASN B 236 8686 9931 8814 148 258 -779 C ATOM 4104 CG ASN B 236 43.143 17.967 -12.820 1.00 88.64 C ANISOU 4104 CG ASN B 236 10758 12044 10878 147 264 -786 C ATOM 4105 OD1 ASN B 236 43.762 17.226 -13.579 1.00 97.71 O ANISOU 4105 OD1 ASN B 236 11893 13215 12019 158 260 -803 O ATOM 4106 ND2 ASN B 236 43.113 19.287 -12.965 1.00 91.85 N ANISOU 4106 ND2 ASN B 236 11171 12452 11276 133 275 -772 N ATOM 4107 N SER B 237 41.764 17.665 -8.140 1.00 43.78 N ANISOU 4107 N SER B 237 5113 6269 5251 132 257 -747 N ATOM 4108 CA SER B 237 40.676 17.962 -7.226 1.00 32.20 C ANISOU 4108 CA SER B 237 3664 4772 3800 125 257 -730 C ATOM 4109 C SER B 237 40.709 19.446 -6.866 1.00 23.54 C ANISOU 4109 C SER B 237 2576 3670 2698 107 267 -712 C ATOM 4110 O SER B 237 41.669 20.157 -7.162 1.00 28.39 O ANISOU 4110 O SER B 237 3183 4304 3300 101 273 -713 O ATOM 4111 CB SER B 237 40.770 17.071 -5.989 1.00 28.14 C ANISOU 4111 CB SER B 237 3151 4241 3301 130 250 -731 C ATOM 4112 OG SER B 237 42.056 17.168 -5.397 1.00 28.81 O ANISOU 4112 OG SER B 237 3226 4338 3383 128 251 -735 O ATOM 4113 N ALA B 238 39.638 19.924 -6.240 1.00 18.94 N ANISOU 4113 N ALA B 238 2009 3061 2126 99 269 -695 N ATOM 4114 CA ALA B 238 39.592 21.329 -5.857 1.00 27.58 C ANISOU 4114 CA ALA B 238 3114 4149 3218 83 278 -677 C ATOM 4115 C ALA B 238 40.531 21.586 -4.675 1.00 29.48 C ANISOU 4115 C ALA B 238 3352 4387 3463 76 279 -673 C ATOM 4116 O ALA B 238 40.724 20.708 -3.828 1.00 26.11 O ANISOU 4116 O ALA B 238 2922 3952 3046 83 272 -678 O ATOM 4117 CB ALA B 238 38.172 21.755 -5.503 1.00 28.05 C ANISOU 4117 CB ALA B 238 3191 4180 3287 76 279 -660 C ATOM 4118 N PRO B 239 41.142 22.775 -4.608 1.00 25.51 N ANISOU 4118 N PRO B 239 2849 3893 2951 63 287 -665 N ATOM 4119 CA PRO B 239 41.994 23.101 -3.457 1.00 24.18 C ANISOU 4119 CA PRO B 239 2679 3723 2787 56 288 -660 C ATOM 4120 C PRO B 239 41.192 23.035 -2.169 1.00 25.47 C ANISOU 4120 C PRO B 239 2856 3854 2967 52 285 -647 C ATOM 4121 O PRO B 239 39.992 23.307 -2.158 1.00 18.08 O ANISOU 4121 O PRO B 239 1934 2899 2038 49 286 -635 O ATOM 4122 CB PRO B 239 42.443 24.541 -3.739 1.00 24.53 C ANISOU 4122 CB PRO B 239 2724 3776 2818 41 299 -651 C ATOM 4123 CG PRO B 239 42.235 24.735 -5.202 1.00 26.21 C ANISOU 4123 CG PRO B 239 2933 4006 3018 44 302 -657 C ATOM 4124 CD PRO B 239 41.051 23.885 -5.568 1.00 21.45 C ANISOU 4124 CD PRO B 239 2337 3391 2423 54 296 -659 C ATOM 4125 N TYR B 240 41.868 22.651 -1.084 1.00 23.15 N ANISOU 4125 N TYR B 240 2558 3557 2681 53 282 -649 N ATOM 4126 CA TYR B 240 41.268 22.696 0.245 1.00 22.43 C ANISOU 4126 CA TYR B 240 2479 3437 2605 49 279 -635 C ATOM 4127 C TYR B 240 41.022 24.139 0.681 1.00 21.44 C ANISOU 4127 C TYR B 240 2365 3301 2479 31 287 -617 C ATOM 4128 O TYR B 240 41.801 25.046 0.377 1.00 19.28 O ANISOU 4128 O TYR B 240 2087 3044 2194 21 294 -616 O ATOM 4129 CB TYR B 240 42.185 22.021 1.283 1.00 18.26 C ANISOU 4129 CB TYR B 240 1944 2911 2084 54 274 -642 C ATOM 4130 CG TYR B 240 42.191 20.491 1.323 1.00 24.84 C ANISOU 4130 CG TYR B 240 2770 3743 2923 71 265 -656 C ATOM 4131 CD1 TYR B 240 42.123 19.731 0.159 1.00 19.31 C ANISOU 4131 CD1 TYR B 240 2062 3058 2217 83 262 -670 C ATOM 4132 CD2 TYR B 240 42.311 19.814 2.534 1.00 18.58 C ANISOU 4132 CD2 TYR B 240 1979 2936 2143 76 260 -655 C ATOM 4133 CE1 TYR B 240 42.144 18.349 0.198 1.00 19.96 C ANISOU 4133 CE1 TYR B 240 2139 3140 2306 99 253 -684 C ATOM 4134 CE2 TYR B 240 42.330 18.424 2.585 1.00 18.45 C ANISOU 4134 CE2 TYR B 240 1958 2919 2133 92 251 -667 C ATOM 4135 CZ TYR B 240 42.244 17.699 1.412 1.00 24.81 C ANISOU 4135 CZ TYR B 240 2755 3738 2932 103 248 -682 C ATOM 4136 OH TYR B 240 42.270 16.324 1.443 1.00 23.33 O ANISOU 4136 OH TYR B 240 2562 3551 2752 119 240 -695 O ATOM 4137 N GLY B 241 39.958 24.342 1.444 1.00 21.41 N ANISOU 4137 N GLY B 241 2377 3269 2489 26 286 -602 N ATOM 4138 CA GLY B 241 39.823 25.575 2.187 1.00 18.68 C ANISOU 4138 CA GLY B 241 2041 2910 2145 9 292 -585 C ATOM 4139 C GLY B 241 40.729 25.577 3.408 1.00 19.15 C ANISOU 4139 C GLY B 241 2097 2969 2210 6 291 -584 C ATOM 4140 O GLY B 241 41.141 24.533 3.910 1.00 22.56 O ANISOU 4140 O GLY B 241 2522 3402 2648 17 284 -594 O ATOM 4141 N ALA B 242 41.069 26.772 3.872 1.00 17.56 N ANISOU 4141 N ALA B 242 1899 2766 2006 -9 297 -574 N ATOM 4142 CA ALA B 242 41.892 26.942 5.060 1.00 15.91 C ANISOU 4142 CA ALA B 242 1688 2556 1802 -14 296 -572 C ATOM 4143 C ALA B 242 41.077 27.583 6.176 1.00 21.98 C ANISOU 4143 C ALA B 242 2472 3295 2583 -25 296 -554 C ATOM 4144 O ALA B 242 40.298 28.509 5.938 1.00 20.83 O ANISOU 4144 O ALA B 242 2339 3139 2438 -36 301 -541 O ATOM 4145 CB ALA B 242 43.129 27.789 4.771 1.00 17.98 C ANISOU 4145 CB ALA B 242 1939 2842 2050 -23 302 -577 C ATOM 4146 N ARG B 243 41.256 27.070 7.389 1.00 19.10 N ANISOU 4146 N ARG B 243 2108 2919 2229 -22 291 -552 N ATOM 4147 CA ARG B 243 40.666 27.640 8.592 1.00 18.74 C ANISOU 4147 CA ARG B 243 2076 2847 2196 -33 291 -536 C ATOM 4148 C ARG B 243 41.692 27.530 9.704 1.00 21.94 C ANISOU 4148 C ARG B 243 2474 3257 2604 -34 289 -539 C ATOM 4149 O ARG B 243 42.291 26.468 9.882 1.00 16.84 O ANISOU 4149 O ARG B 243 1818 2619 1959 -21 283 -551 O ATOM 4150 CB ARG B 243 39.392 26.889 8.999 1.00 14.75 C ANISOU 4150 CB ARG B 243 1583 2316 1705 -25 285 -528 C ATOM 4151 CG ARG B 243 38.280 26.900 7.975 1.00 19.01 C ANISOU 4151 CG ARG B 243 2130 2850 2244 -24 287 -525 C ATOM 4152 CD ARG B 243 37.587 28.237 7.898 1.00 18.64 C ANISOU 4152 CD ARG B 243 2096 2791 2196 -40 292 -510 C ATOM 4153 NE ARG B 243 36.385 28.177 7.070 1.00 20.19 N ANISOU 4153 NE ARG B 243 2301 2979 2394 -37 293 -505 N ATOM 4154 CZ ARG B 243 36.382 28.209 5.739 1.00 29.09 C ANISOU 4154 CZ ARG B 243 3422 4122 3508 -33 296 -513 C ATOM 4155 NH1 ARG B 243 37.513 28.300 5.063 1.00 24.08 N ANISOU 4155 NH1 ARG B 243 2774 3516 2860 -32 299 -525 N ATOM 4156 NH2 ARG B 243 35.241 28.145 5.079 1.00 35.14 N ANISOU 4156 NH2 ARG B 243 4197 4879 4276 -31 296 -508 N ATOM 4157 N TYR B 244 41.892 28.603 10.465 1.00 14.32 N ANISOU 4157 N TYR B 244 1515 2285 1641 -48 292 -528 N ATOM 4158 CA TYR B 244 42.774 28.496 11.625 1.00 12.30 C ANISOU 4158 CA TYR B 244 1254 2030 1389 -49 290 -530 C ATOM 4159 C TYR B 244 42.285 29.489 12.672 1.00 13.98 C ANISOU 4159 C TYR B 244 1480 2221 1611 -64 291 -513 C ATOM 4160 O TYR B 244 42.587 30.682 12.595 1.00 17.06 O ANISOU 4160 O TYR B 244 1872 2616 1995 -79 297 -508 O ATOM 4161 CB TYR B 244 44.226 28.747 11.255 1.00 16.84 C ANISOU 4161 CB TYR B 244 1812 2635 1950 -51 293 -543 C ATOM 4162 CG TYR B 244 45.173 28.427 12.371 1.00 15.02 C ANISOU 4162 CG TYR B 244 1575 2409 1723 -49 289 -547 C ATOM 4163 CD1 TYR B 244 45.375 27.113 12.780 1.00 19.75 C ANISOU 4163 CD1 TYR B 244 2168 3008 2328 -32 282 -556 C ATOM 4164 CD2 TYR B 244 45.846 29.437 13.041 1.00 21.91 C ANISOU 4164 CD2 TYR B 244 2446 3284 2593 -62 292 -543 C ATOM 4165 CE1 TYR B 244 46.244 26.815 13.814 1.00 13.99 C ANISOU 4165 CE1 TYR B 244 1432 2283 1601 -30 279 -560 C ATOM 4166 CE2 TYR B 244 46.716 29.153 14.082 1.00 17.50 C ANISOU 4166 CE2 TYR B 244 1881 2730 2037 -60 289 -547 C ATOM 4167 CZ TYR B 244 46.909 27.843 14.462 1.00 14.89 C ANISOU 4167 CZ TYR B 244 1545 2400 1712 -44 282 -556 C ATOM 4168 OH TYR B 244 47.777 27.569 15.492 1.00 25.59 O ANISOU 4168 OH TYR B 244 2893 3760 3069 -41 279 -560 O ATOM 4169 N VAL B 245 41.538 28.977 13.647 1.00 15.50 N ANISOU 4169 N VAL B 245 1682 2389 1818 -60 286 -505 N ATOM 4170 CA VAL B 245 40.993 29.823 14.696 1.00 18.12 C ANISOU 4170 CA VAL B 245 2028 2698 2160 -74 287 -488 C ATOM 4171 C VAL B 245 42.096 30.302 15.626 1.00 17.44 C ANISOU 4171 C VAL B 245 1935 2620 2072 -81 287 -490 C ATOM 4172 O VAL B 245 42.050 31.430 16.135 1.00 20.80 O ANISOU 4172 O VAL B 245 2367 3036 2498 -97 290 -480 O ATOM 4173 CB VAL B 245 39.912 29.050 15.472 1.00 14.32 C ANISOU 4173 CB VAL B 245 1557 2189 1694 -67 281 -479 C ATOM 4174 CG1 VAL B 245 39.397 29.887 16.610 1.00 11.92 C ANISOU 4174 CG1 VAL B 245 1266 1862 1401 -80 281 -463 C ATOM 4175 CG2 VAL B 245 38.783 28.612 14.553 1.00 13.36 C ANISOU 4175 CG2 VAL B 245 1442 2059 1574 -60 280 -478 C ATOM 4176 N GLY B 246 43.105 29.474 15.850 1.00 16.20 N ANISOU 4176 N GLY B 246 1764 2479 1911 -70 284 -503 N ATOM 4177 CA GLY B 246 44.140 29.753 16.823 1.00 26.26 C ANISOU 4177 CA GLY B 246 3032 3761 3185 -74 283 -506 C ATOM 4178 C GLY B 246 43.829 29.258 18.215 1.00 22.36 C ANISOU 4178 C GLY B 246 2545 3246 2705 -70 278 -498 C ATOM 4179 O GLY B 246 44.610 29.503 19.141 1.00 28.00 O ANISOU 4179 O GLY B 246 3254 3964 3419 -74 277 -499 O ATOM 4180 N SER B 247 42.728 28.545 18.385 1.00 17.21 N ANISOU 4180 N SER B 247 1902 2572 2064 -62 274 -491 N ATOM 4181 CA SER B 247 42.384 27.921 19.648 1.00 16.93 C ANISOU 4181 CA SER B 247 1873 2517 2041 -57 268 -485 C ATOM 4182 C SER B 247 42.266 26.437 19.364 1.00 15.03 C ANISOU 4182 C SER B 247 1628 2279 1804 -37 263 -494 C ATOM 4183 O SER B 247 41.428 26.033 18.554 1.00 16.76 O ANISOU 4183 O SER B 247 1852 2493 2025 -32 263 -494 O ATOM 4184 CB SER B 247 41.085 28.500 20.201 1.00 13.51 C ANISOU 4184 CB SER B 247 1458 2053 1620 -67 268 -466 C ATOM 4185 OG SER B 247 40.752 27.917 21.440 1.00 23.00 O ANISOU 4185 OG SER B 247 2667 3237 2836 -61 263 -459 O ATOM 4186 N MET B 248 43.120 25.631 20.009 1.00 12.05 N ANISOU 4186 N MET B 248 1144 2168 1265 330 -130 -494 N ATOM 4187 CA MET B 248 43.258 24.234 19.595 1.00 15.62 C ANISOU 4187 CA MET B 248 1598 2610 1726 335 -113 -502 C ATOM 4188 C MET B 248 41.928 23.494 19.650 1.00 12.65 C ANISOU 4188 C MET B 248 1225 2218 1364 330 -107 -512 C ATOM 4189 O MET B 248 41.593 22.743 18.729 1.00 15.68 O ANISOU 4189 O MET B 248 1604 2600 1752 330 -99 -523 O ATOM 4190 CB MET B 248 44.284 23.510 20.461 1.00 18.35 C ANISOU 4190 CB MET B 248 1953 2946 2074 346 -101 -494 C ATOM 4191 CG MET B 248 44.631 22.142 19.921 1.00 22.74 C ANISOU 4191 CG MET B 248 2508 3494 2638 353 -83 -502 C ATOM 4192 SD MET B 248 45.328 21.053 21.161 1.00 23.85 S ANISOU 4192 SD MET B 248 2659 3614 2788 363 -67 -494 S ATOM 4193 CE MET B 248 45.935 19.714 20.143 1.00 24.94 C ANISOU 4193 CE MET B 248 2792 3752 2934 372 -49 -502 C ATOM 4194 N VAL B 249 41.141 23.716 20.704 1.00 14.06 N ANISOU 4194 N VAL B 249 1409 2384 1547 326 -110 -509 N ATOM 4195 CA VAL B 249 39.884 22.989 20.848 1.00 15.20 C ANISOU 4195 CA VAL B 249 1558 2513 1706 320 -103 -518 C ATOM 4196 C VAL B 249 38.938 23.338 19.712 1.00 18.22 C ANISOU 4196 C VAL B 249 1929 2904 2089 312 -110 -528 C ATOM 4197 O VAL B 249 38.264 22.467 19.150 1.00 15.05 O ANISOU 4197 O VAL B 249 1527 2495 1696 310 -101 -539 O ATOM 4198 CB VAL B 249 39.256 23.273 22.223 1.00 13.33 C ANISOU 4198 CB VAL B 249 1330 2262 1474 317 -105 -511 C ATOM 4199 CG1 VAL B 249 37.970 22.464 22.388 1.00 17.98 C ANISOU 4199 CG1 VAL B 249 1922 2833 2075 312 -96 -521 C ATOM 4200 CG2 VAL B 249 40.254 22.960 23.310 1.00 14.96 C ANISOU 4200 CG2 VAL B 249 1546 2459 1678 326 -98 -501 C ATOM 4201 N ALA B 250 38.867 24.615 19.357 1.00 11.78 N ANISOU 4201 N ALA B 250 1105 2105 1265 307 -126 -525 N ATOM 4202 CA ALA B 250 37.997 25.007 18.260 1.00 11.61 C ANISOU 4202 CA ALA B 250 1072 2093 1245 300 -133 -534 C ATOM 4203 C ALA B 250 38.450 24.377 16.948 1.00 11.67 C ANISOU 4203 C ALA B 250 1075 2110 1251 303 -127 -543 C ATOM 4204 O ALA B 250 37.626 23.859 16.188 1.00 14.20 O ANISOU 4204 O ALA B 250 1390 2427 1577 299 -123 -554 O ATOM 4205 CB ALA B 250 37.955 26.533 18.144 1.00 11.86 C ANISOU 4205 CB ALA B 250 1106 2128 1273 293 -141 -519 C ATOM 4206 N ASP B 251 39.760 24.392 16.670 1.00 14.96 N ANISOU 4206 N ASP B 251 1491 2536 1657 311 -125 -538 N ATOM 4207 CA ASP B 251 40.232 23.859 15.392 1.00 19.15 C ANISOU 4207 CA ASP B 251 2015 3076 2185 314 -119 -546 C ATOM 4208 C ASP B 251 40.091 22.342 15.334 1.00 18.10 C ANISOU 4208 C ASP B 251 1887 2926 2063 319 -101 -554 C ATOM 4209 O ASP B 251 39.651 21.788 14.317 1.00 10.96 O ANISOU 4209 O ASP B 251 978 2023 1163 317 -97 -566 O ATOM 4210 CB ASP B 251 41.683 24.281 15.151 1.00 17.19 C ANISOU 4210 CB ASP B 251 1765 2842 1923 321 -121 -538 C ATOM 4211 CG ASP B 251 41.814 25.759 14.770 1.00 16.22 C ANISOU 4211 CG ASP B 251 1635 2740 1789 316 -139 -533 C ATOM 4212 OD1 ASP B 251 41.108 26.207 13.841 1.00 13.46 O ANISOU 4212 OD1 ASP B 251 1282 2390 1443 308 -140 -535 O ATOM 4213 OD2 ASP B 251 42.639 26.464 15.396 1.00 15.99 O ANISOU 4213 OD2 ASP B 251 1613 2710 1754 318 -140 -517 O ATOM 4214 N VAL B 252 40.412 21.655 16.431 1.00 15.71 N ANISOU 4214 N VAL B 252 1595 2608 1765 324 -91 -549 N ATOM 4215 CA VAL B 252 40.286 20.203 16.446 1.00 19.13 C ANISOU 4215 CA VAL B 252 2033 3024 2209 329 -74 -556 C ATOM 4216 C VAL B 252 38.816 19.786 16.355 1.00 14.39 C ANISOU 4216 C VAL B 252 1434 2414 1621 321 -72 -566 C ATOM 4217 O VAL B 252 38.476 18.818 15.665 1.00 13.75 O ANISOU 4217 O VAL B 252 1352 2327 1546 322 -62 -577 O ATOM 4218 CB VAL B 252 40.982 19.627 17.694 1.00 17.91 C ANISOU 4218 CB VAL B 252 1889 2856 2058 337 -64 -547 C ATOM 4219 CG1 VAL B 252 40.668 18.144 17.853 1.00 16.82 C ANISOU 4219 CG1 VAL B 252 1757 2700 1934 341 -46 -554 C ATOM 4220 CG2 VAL B 252 42.501 19.859 17.598 1.00 21.19 C ANISOU 4220 CG2 VAL B 252 2303 3283 2465 346 -63 -538 C ATOM 4221 N HIS B 253 37.915 20.512 17.022 1.00 15.30 N ANISOU 4221 N HIS B 253 1551 2526 1738 313 -82 -564 N ATOM 4222 CA HIS B 253 36.510 20.108 16.953 1.00 14.75 C ANISOU 4222 CA HIS B 253 1481 2445 1678 305 -79 -573 C ATOM 4223 C HIS B 253 35.947 20.253 15.541 1.00 15.20 C ANISOU 4223 C HIS B 253 1527 2514 1735 300 -84 -584 C ATOM 4224 O HIS B 253 35.193 19.386 15.080 1.00 18.84 O ANISOU 4224 O HIS B 253 1987 2966 2204 298 -76 -595 O ATOM 4225 CB HIS B 253 35.654 20.890 17.945 1.00 13.98 C ANISOU 4225 CB HIS B 253 1387 2342 1584 298 -88 -568 C ATOM 4226 CG HIS B 253 34.249 20.384 18.023 1.00 13.16 C ANISOU 4226 CG HIS B 253 1285 2225 1492 291 -83 -576 C ATOM 4227 ND1 HIS B 253 33.937 19.132 18.513 1.00 18.56 N ANISOU 4227 ND1 HIS B 253 1978 2889 2185 293 -68 -581 N ATOM 4228 CD2 HIS B 253 33.084 20.918 17.590 1.00 12.26 C ANISOU 4228 CD2 HIS B 253 1164 2114 1381 281 -91 -582 C ATOM 4229 CE1 HIS B 253 32.634 18.933 18.416 1.00 12.76 C ANISOU 4229 CE1 HIS B 253 1242 2147 1459 285 -67 -588 C ATOM 4230 NE2 HIS B 253 32.093 20.005 17.858 1.00 15.42 N ANISOU 4230 NE2 HIS B 253 1569 2498 1793 278 -81 -589 N ATOM 4231 N ARG B 254 36.281 21.345 14.843 1.00 16.13 N ANISOU 4231 N ARG B 254 1636 2651 1843 298 -98 -582 N ATOM 4232 CA ARG B 254 35.919 21.444 13.430 1.00 10.96 C ANISOU 4232 CA ARG B 254 969 2008 1186 294 -101 -592 C ATOM 4233 C ARG B 254 36.505 20.280 12.643 1.00 10.25 C ANISOU 4233 C ARG B 254 881 1917 1098 301 -87 -600 C ATOM 4234 O ARG B 254 35.845 19.728 11.759 1.00 12.55 O ANISOU 4234 O ARG B 254 1167 2207 1395 299 -83 -611 O ATOM 4235 CB ARG B 254 36.401 22.768 12.835 1.00 11.96 C ANISOU 4235 CB ARG B 254 1087 2157 1301 292 -117 -587 C ATOM 4236 CG ARG B 254 35.965 23.019 11.361 1.00 12.79 C ANISOU 4236 CG ARG B 254 1180 2276 1405 288 -122 -597 C ATOM 4237 CD ARG B 254 36.837 24.124 10.700 1.00 13.51 C ANISOU 4237 CD ARG B 254 1263 2388 1482 289 -134 -592 C ATOM 4238 NE ARG B 254 38.260 23.778 10.777 1.00 14.58 N ANISOU 4238 NE ARG B 254 1403 2527 1609 299 -127 -586 N ATOM 4239 CZ ARG B 254 39.158 24.376 11.557 1.00 10.98 C ANISOU 4239 CZ ARG B 254 951 2075 1145 303 -132 -573 C ATOM 4240 NH1 ARG B 254 38.823 25.405 12.326 1.00 14.56 N ANISOU 4240 NH1 ARG B 254 1407 2526 1598 297 -141 -563 N ATOM 4241 NH2 ARG B 254 40.405 23.951 11.556 1.00 14.35 N ANISOU 4241 NH2 ARG B 254 1382 2505 1566 312 -123 -569 N ATOM 4242 N THR B 255 37.757 19.911 12.934 1.00 15.40 N ANISOU 4242 N THR B 255 1537 2569 1745 311 -80 -593 N ATOM 4243 CA THR B 255 38.372 18.780 12.242 1.00 11.70 C ANISOU 4243 CA THR B 255 1069 2098 1280 319 -66 -599 C ATOM 4244 C THR B 255 37.575 17.498 12.463 1.00 12.83 C ANISOU 4244 C THR B 255 1218 2221 1436 319 -52 -607 C ATOM 4245 O THR B 255 37.401 16.703 11.531 1.00 16.32 O ANISOU 4245 O THR B 255 1657 2663 1882 321 -44 -617 O ATOM 4246 CB THR B 255 39.824 18.609 12.689 1.00 19.70 C ANISOU 4246 CB THR B 255 2086 3113 2287 330 -59 -589 C ATOM 4247 OG1 THR B 255 40.547 19.828 12.455 1.00 19.52 O ANISOU 4247 OG1 THR B 255 2058 3109 2251 329 -72 -581 O ATOM 4248 CG2 THR B 255 40.503 17.463 11.919 1.00 19.20 C ANISOU 4248 CG2 THR B 255 2021 3047 2226 339 -44 -594 C ATOM 4249 N LEU B 256 37.090 17.280 13.695 1.00 12.92 N ANISOU 4249 N LEU B 256 1238 2217 1454 317 -49 -603 N ATOM 4250 CA LEU B 256 36.248 16.121 13.992 1.00 19.15 C ANISOU 4250 CA LEU B 256 2033 2987 2256 316 -37 -611 C ATOM 4251 C LEU B 256 34.923 16.182 13.245 1.00 21.68 C ANISOU 4251 C LEU B 256 2348 3309 2581 306 -41 -622 C ATOM 4252 O LEU B 256 34.442 15.165 12.730 1.00 28.00 O ANISOU 4252 O LEU B 256 3148 4101 3389 307 -31 -632 O ATOM 4253 CB LEU B 256 35.998 16.020 15.503 1.00 20.97 C ANISOU 4253 CB LEU B 256 2274 3201 2491 316 -34 -603 C ATOM 4254 CG LEU B 256 35.009 14.934 15.976 1.00 21.01 C ANISOU 4254 CG LEU B 256 2287 3187 2510 313 -22 -610 C ATOM 4255 CD1 LEU B 256 35.499 13.520 15.651 1.00 19.79 C ANISOU 4255 CD1 LEU B 256 2135 3023 2361 322 -5 -615 C ATOM 4256 CD2 LEU B 256 34.761 15.052 17.459 1.00 15.31 C ANISOU 4256 CD2 LEU B 256 1575 2450 1791 312 -22 -601 C ATOM 4257 N VAL B 257 34.299 17.359 13.202 1.00 22.03 N ANISOU 4257 N VAL B 257 2386 3362 2621 298 -56 -621 N ATOM 4258 CA VAL B 257 32.952 17.468 12.653 1.00 15.62 C ANISOU 4258 CA VAL B 257 1569 2550 1816 288 -61 -630 C ATOM 4259 C VAL B 257 32.971 17.462 11.122 1.00 16.97 C ANISOU 4259 C VAL B 257 1729 2735 1983 288 -63 -640 C ATOM 4260 O VAL B 257 32.154 16.792 10.482 1.00 20.40 O ANISOU 4260 O VAL B 257 2161 3165 2425 285 -58 -651 O ATOM 4261 CB VAL B 257 32.278 18.734 13.216 1.00 19.43 C ANISOU 4261 CB VAL B 257 2048 3037 2297 280 -75 -624 C ATOM 4262 CG1 VAL B 257 30.994 19.042 12.468 1.00 25.33 C ANISOU 4262 CG1 VAL B 257 2787 3789 3050 270 -82 -634 C ATOM 4263 CG2 VAL B 257 32.011 18.561 14.716 1.00 13.88 C ANISOU 4263 CG2 VAL B 257 1357 2317 1599 280 -71 -617 C ATOM 4264 N TYR B 258 33.898 18.194 10.501 1.00 16.84 N ANISOU 4264 N TYR B 258 1707 2737 1957 291 -71 -636 N ATOM 4265 CA TYR B 258 33.868 18.356 9.052 1.00 17.65 C ANISOU 4265 CA TYR B 258 1799 2854 2055 290 -75 -644 C ATOM 4266 C TYR B 258 34.913 17.525 8.332 1.00 18.78 C ANISOU 4266 C TYR B 258 1943 2999 2195 300 -63 -647 C ATOM 4267 O TYR B 258 34.845 17.407 7.105 1.00 16.78 O ANISOU 4267 O TYR B 258 1682 2755 1940 299 -63 -656 O ATOM 4268 CB TYR B 258 34.052 19.829 8.666 1.00 27.72 C ANISOU 4268 CB TYR B 258 3065 4148 3320 286 -92 -639 C ATOM 4269 CG TYR B 258 32.819 20.658 8.931 1.00 41.08 C ANISOU 4269 CG TYR B 258 4752 5840 5016 275 -103 -640 C ATOM 4270 CD1 TYR B 258 31.669 20.484 8.174 1.00 54.50 C ANISOU 4270 CD1 TYR B 258 6445 7538 6723 268 -104 -651 C ATOM 4271 CD2 TYR B 258 32.800 21.613 9.934 1.00 38.48 C ANISOU 4271 CD2 TYR B 258 4424 5511 4684 272 -113 -629 C ATOM 4272 CE1 TYR B 258 30.530 21.236 8.417 1.00 56.99 C ANISOU 4272 CE1 TYR B 258 6756 7855 7044 259 -114 -651 C ATOM 4273 CE2 TYR B 258 31.665 22.369 10.182 1.00 42.13 C ANISOU 4273 CE2 TYR B 258 4882 5973 5152 264 -123 -629 C ATOM 4274 CZ TYR B 258 30.536 22.178 9.424 1.00 49.28 C ANISOU 4274 CZ TYR B 258 5780 6878 6065 257 -123 -640 C ATOM 4275 OH TYR B 258 29.405 22.927 9.672 1.00 50.47 O ANISOU 4275 OH TYR B 258 5926 7028 6222 248 -132 -639 O ATOM 4276 N GLY B 259 35.856 16.939 9.061 1.00 21.03 N ANISOU 4276 N GLY B 259 2235 3276 2479 308 -53 -640 N ATOM 4277 CA GLY B 259 36.985 16.277 8.450 1.00 16.45 C ANISOU 4277 CA GLY B 259 1655 2700 1896 319 -42 -641 C ATOM 4278 C GLY B 259 38.081 17.281 8.126 1.00 19.86 C ANISOU 4278 C GLY B 259 2082 3151 2315 322 -51 -632 C ATOM 4279 O GLY B 259 37.953 18.497 8.300 1.00 20.11 O ANISOU 4279 O GLY B 259 2109 3192 2338 316 -66 -627 O ATOM 4280 N GLY B 260 39.179 16.754 7.636 1.00 15.52 N ANISOU 4280 N GLY B 260 1531 2604 1761 331 -42 -631 N ATOM 4281 CA GLY B 260 40.325 17.558 7.295 1.00 15.13 C ANISOU 4281 CA GLY B 260 1477 2572 1699 336 -48 -623 C ATOM 4282 C GLY B 260 41.525 17.258 8.175 1.00 21.76 C ANISOU 4282 C GLY B 260 2323 3407 2538 345 -39 -612 C ATOM 4283 O GLY B 260 41.681 16.163 8.734 1.00 16.85 O ANISOU 4283 O GLY B 260 1707 2769 1925 352 -25 -612 O ATOM 4284 N ILE B 261 42.391 18.264 8.304 1.00 15.79 N ANISOU 4284 N ILE B 261 1564 2665 1770 347 -48 -602 N ATOM 4285 CA ILE B 261 43.683 18.076 8.954 1.00 15.03 C ANISOU 4285 CA ILE B 261 1472 2568 1671 357 -40 -591 C ATOM 4286 C ILE B 261 44.054 19.324 9.735 1.00 15.39 C ANISOU 4286 C ILE B 261 1518 2621 1706 354 -54 -579 C ATOM 4287 O ILE B 261 43.815 20.453 9.290 1.00 16.90 O ANISOU 4287 O ILE B 261 1704 2828 1889 347 -69 -578 O ATOM 4288 CB ILE B 261 44.762 17.717 7.913 1.00 20.36 C ANISOU 4288 CB ILE B 261 2141 3253 2342 366 -31 -592 C ATOM 4289 CG1 ILE B 261 46.078 17.311 8.577 1.00 20.47 C ANISOU 4289 CG1 ILE B 261 2158 3264 2357 377 -20 -580 C ATOM 4290 CG2 ILE B 261 44.977 18.862 6.941 1.00 19.22 C ANISOU 4290 CG2 ILE B 261 1987 3130 2184 362 -44 -592 C ATOM 4291 CD1 ILE B 261 46.973 16.587 7.605 1.00 13.14 C ANISOU 4291 CD1 ILE B 261 1224 2341 1429 387 -7 -583 C ATOM 4292 N PHE B 262 44.622 19.114 10.916 1.00 15.91 N ANISOU 4292 N PHE B 262 1592 2678 1776 359 -49 -569 N ATOM 4293 CA PHE B 262 45.109 20.174 11.781 1.00 18.49 C ANISOU 4293 CA PHE B 262 1920 3011 2093 358 -60 -556 C ATOM 4294 C PHE B 262 46.589 19.933 12.023 1.00 23.06 C ANISOU 4294 C PHE B 262 2500 3593 2668 369 -51 -546 C ATOM 4295 O PHE B 262 46.997 18.790 12.257 1.00 21.12 O ANISOU 4295 O PHE B 262 2257 3335 2433 378 -35 -546 O ATOM 4296 CB PHE B 262 44.336 20.192 13.101 1.00 17.50 C ANISOU 4296 CB PHE B 262 1804 2870 1974 353 -63 -553 C ATOM 4297 CG PHE B 262 44.911 21.124 14.127 1.00 15.07 C ANISOU 4297 CG PHE B 262 1500 2566 1659 354 -72 -539 C ATOM 4298 CD1 PHE B 262 44.635 22.486 14.080 1.00 20.99 C ANISOU 4298 CD1 PHE B 262 2247 3330 2398 346 -90 -536 C ATOM 4299 CD2 PHE B 262 45.721 20.643 15.144 1.00 21.37 C ANISOU 4299 CD2 PHE B 262 2304 3354 2460 362 -63 -530 C ATOM 4300 CE1 PHE B 262 45.157 23.341 15.024 1.00 16.27 C ANISOU 4300 CE1 PHE B 262 1653 2736 1793 346 -99 -523 C ATOM 4301 CE2 PHE B 262 46.262 21.500 16.090 1.00 16.81 C ANISOU 4301 CE2 PHE B 262 1732 2781 1875 362 -71 -517 C ATOM 4302 CZ PHE B 262 45.978 22.851 16.028 1.00 18.08 C ANISOU 4302 CZ PHE B 262 1889 2955 2024 355 -89 -514 C ATOM 4303 N LEU B 263 47.399 20.990 11.920 1.00 13.19 N ANISOU 4303 N LEU B 263 1246 2360 1405 370 -61 -537 N ATOM 4304 CA LEU B 263 48.843 20.849 12.047 1.00 17.40 C ANISOU 4304 CA LEU B 263 1778 2898 1935 380 -52 -527 C ATOM 4305 C LEU B 263 49.398 21.893 13.000 1.00 20.32 C ANISOU 4305 C LEU B 263 2152 3275 2295 379 -62 -513 C ATOM 4306 O LEU B 263 49.146 23.092 12.841 1.00 22.30 O ANISOU 4306 O LEU B 263 2401 3539 2535 372 -78 -511 O ATOM 4307 CB LEU B 263 49.557 20.979 10.699 1.00 15.94 C ANISOU 4307 CB LEU B 263 1583 2730 1742 384 -50 -529 C ATOM 4308 CG LEU B 263 49.080 20.122 9.533 1.00 20.91 C ANISOU 4308 CG LEU B 263 2208 3358 2379 384 -41 -543 C ATOM 4309 CD1 LEU B 263 48.062 20.883 8.737 1.00 14.95 C ANISOU 4309 CD1 LEU B 263 1450 2613 1618 373 -55 -552 C ATOM 4310 CD2 LEU B 263 50.254 19.682 8.651 1.00 25.91 C ANISOU 4310 CD2 LEU B 263 2834 3999 3010 394 -29 -541 C ATOM 4311 N TYR B 264 50.193 21.452 13.954 1.00 16.03 N ANISOU 4311 N TYR B 264 1612 2722 1756 387 -53 -503 N ATOM 4312 CA TYR B 264 51.069 22.358 14.686 1.00 21.32 C ANISOU 4312 CA TYR B 264 2285 3400 2417 389 -60 -489 C ATOM 4313 C TYR B 264 52.450 21.728 14.686 1.00 18.49 C ANISOU 4313 C TYR B 264 1921 3041 2061 402 -45 -481 C ATOM 4314 O TYR B 264 52.847 21.051 15.644 1.00 18.55 O ANISOU 4314 O TYR B 264 1933 3035 2079 408 -36 -474 O ATOM 4315 CB TYR B 264 50.550 22.684 16.089 1.00 21.25 C ANISOU 4315 CB TYR B 264 2285 3379 2409 385 -67 -483 C ATOM 4316 CG TYR B 264 50.987 24.082 16.474 1.00 27.28 C ANISOU 4316 CG TYR B 264 3050 4158 3158 382 -82 -472 C ATOM 4317 CD1 TYR B 264 52.324 24.463 16.333 1.00 32.87 C ANISOU 4317 CD1 TYR B 264 3753 4878 3856 388 -79 -462 C ATOM 4318 CD2 TYR B 264 50.070 25.038 16.903 1.00 21.29 C ANISOU 4318 CD2 TYR B 264 2296 3401 2393 371 -98 -473 C ATOM 4319 CE1 TYR B 264 52.746 25.735 16.643 1.00 37.11 C ANISOU 4319 CE1 TYR B 264 4292 5429 4378 385 -92 -452 C ATOM 4320 CE2 TYR B 264 50.481 26.326 17.219 1.00 24.56 C ANISOU 4320 CE2 TYR B 264 2711 3829 2793 368 -112 -463 C ATOM 4321 CZ TYR B 264 51.828 26.664 17.085 1.00 38.79 C ANISOU 4321 CZ TYR B 264 4511 5644 4585 375 -108 -452 C ATOM 4322 OH TYR B 264 52.274 27.932 17.380 1.00 40.00 O ANISOU 4322 OH TYR B 264 4666 5811 4722 371 -121 -443 O ATOM 4323 N PRO B 265 53.192 21.900 13.594 1.00 19.38 N ANISOU 4323 N PRO B 265 2025 3170 2168 405 -43 -481 N ATOM 4324 CA PRO B 265 54.505 21.280 13.449 1.00 22.46 C ANISOU 4324 CA PRO B 265 2408 3561 2563 417 -28 -473 C ATOM 4325 C PRO B 265 55.583 22.166 14.067 1.00 28.31 C ANISOU 4325 C PRO B 265 3149 4312 3295 420 -32 -457 C ATOM 4326 O PRO B 265 55.339 23.309 14.466 1.00 25.91 O ANISOU 4326 O PRO B 265 2850 4017 2979 412 -47 -452 O ATOM 4327 CB PRO B 265 54.670 21.185 11.926 1.00 24.91 C ANISOU 4327 CB PRO B 265 2710 3885 2870 418 -24 -481 C ATOM 4328 CG PRO B 265 53.938 22.376 11.423 1.00 27.87 C ANISOU 4328 CG PRO B 265 3086 4274 3231 406 -43 -486 C ATOM 4329 CD PRO B 265 52.797 22.625 12.375 1.00 19.38 C ANISOU 4329 CD PRO B 265 2019 3187 2156 398 -53 -488 C ATOM 4330 N ALA B 266 56.792 21.616 14.126 1.00 32.21 N ANISOU 4330 N ALA B 266 3636 4806 3796 431 -19 -448 N ATOM 4331 CA ALA B 266 57.919 22.373 14.653 1.00 45.71 C ANISOU 4331 CA ALA B 266 5344 6526 5500 434 -22 -431 C ATOM 4332 C ALA B 266 58.268 23.569 13.768 1.00 52.49 C ANISOU 4332 C ALA B 266 6197 7406 6339 429 -32 -429 C ATOM 4333 O ALA B 266 58.079 23.549 12.548 1.00 54.57 O ANISOU 4333 O ALA B 266 6455 7680 6599 427 -32 -438 O ATOM 4334 CB ALA B 266 59.142 21.465 14.791 1.00 44.01 C ANISOU 4334 CB ALA B 266 5120 6305 5299 447 -5 -422 C ATOM 4335 N ASN B 267 58.802 24.611 14.407 1.00 62.01 N ANISOU 4335 N ASN B 267 7405 8622 7534 427 -41 -416 N ATOM 4336 CA ASN B 267 59.385 25.767 13.733 1.00 65.53 C ANISOU 4336 CA ASN B 267 7847 9090 7963 424 -48 -410 C ATOM 4337 C ASN B 267 60.614 26.202 14.532 1.00 72.98 C ANISOU 4337 C ASN B 267 8788 10037 8906 429 -45 -391 C ATOM 4338 O ASN B 267 61.015 25.541 15.495 1.00 70.34 O ANISOU 4338 O ASN B 267 8453 9687 8585 436 -37 -383 O ATOM 4339 CB ASN B 267 58.342 26.886 13.559 1.00 60.43 C ANISOU 4339 CB ASN B 267 7208 8452 7300 411 -67 -417 C ATOM 4340 CG ASN B 267 57.748 27.384 14.884 1.00 56.10 C ANISOU 4340 CG ASN B 267 6672 7895 6748 405 -77 -413 C ATOM 4341 OD1 ASN B 267 58.468 27.801 15.797 1.00 47.77 O ANISOU 4341 OD1 ASN B 267 5620 6839 5690 408 -77 -399 O ATOM 4342 ND2 ASN B 267 56.422 27.356 14.980 1.00 49.68 N ANISOU 4342 ND2 ASN B 267 5866 7074 5937 397 -86 -425 N ATOM 4343 N LYS B 268 61.235 27.318 14.136 1.00 83.68 N ANISOU 4343 N LYS B 268 10140 11411 10245 426 -52 -382 N ATOM 4344 CA LYS B 268 62.462 27.729 14.818 1.00 92.29 C ANISOU 4344 CA LYS B 268 11226 12505 11335 431 -48 -363 C ATOM 4345 C LYS B 268 62.190 28.286 16.213 1.00 94.58 C ANISOU 4345 C LYS B 268 11528 12787 11622 427 -56 -356 C ATOM 4346 O LYS B 268 63.056 28.188 17.089 1.00 98.04 O ANISOU 4346 O LYS B 268 11962 13219 12069 433 -51 -341 O ATOM 4347 CB LYS B 268 63.267 28.711 13.967 1.00 95.63 C ANISOU 4347 CB LYS B 268 11641 12950 11743 429 -51 -356 C ATOM 4348 CG LYS B 268 63.884 28.026 12.749 1.00 99.57 C ANISOU 4348 CG LYS B 268 12126 13456 12249 436 -39 -359 C ATOM 4349 CD LYS B 268 64.684 28.971 11.874 1.00101.46 C ANISOU 4349 CD LYS B 268 12358 13717 12475 434 -41 -351 C ATOM 4350 CE LYS B 268 65.895 29.487 12.645 1.00102.05 C ANISOU 4350 CE LYS B 268 12427 13796 12551 437 -38 -330 C ATOM 4351 NZ LYS B 268 66.855 30.232 11.785 1.00102.52 N ANISOU 4351 NZ LYS B 268 12476 13875 12601 437 -37 -320 N ATOM 4352 N LYS B 269 61.016 28.877 16.448 1.00 94.37 N ANISOU 4352 N LYS B 269 11514 12759 11583 417 -69 -365 N ATOM 4353 CA LYS B 269 60.680 29.243 17.821 1.00 93.07 C ANISOU 4353 CA LYS B 269 11361 12584 11418 414 -75 -359 C ATOM 4354 C LYS B 269 60.367 28.011 18.662 1.00 89.42 C ANISOU 4354 C LYS B 269 10900 12098 10976 420 -67 -362 C ATOM 4355 O LYS B 269 60.553 28.031 19.885 1.00 88.68 O ANISOU 4355 O LYS B 269 10812 11994 10888 422 -67 -352 O ATOM 4356 CB LYS B 269 59.482 30.195 17.868 1.00 92.30 C ANISOU 4356 CB LYS B 269 11277 12491 11303 402 -92 -369 C ATOM 4357 CG LYS B 269 59.736 31.620 17.412 1.00 92.63 C ANISOU 4357 CG LYS B 269 11322 12554 11321 395 -100 -364 C ATOM 4358 CD LYS B 269 58.540 32.490 17.776 1.00 90.86 C ANISOU 4358 CD LYS B 269 11113 12311 11099 379 -107 -364 C ATOM 4359 CE LYS B 269 58.719 33.931 17.333 1.00 87.12 C ANISOU 4359 CE LYS B 269 10645 11831 10625 365 -103 -349 C ATOM 4360 NZ LYS B 269 57.463 34.711 17.536 1.00 83.39 N ANISOU 4360 NZ LYS B 269 10188 11328 10167 348 -104 -344 N ATOM 4361 N SER B 270 59.895 26.937 18.032 1.00 82.52 N ANISOU 4361 N SER B 270 10022 11217 10114 423 -60 -374 N ATOM 4362 CA SER B 270 59.476 25.727 18.737 1.00 72.37 C ANISOU 4362 CA SER B 270 8740 9910 8849 428 -52 -379 C ATOM 4363 C SER B 270 59.938 24.487 17.980 1.00 70.15 C ANISOU 4363 C SER B 270 8448 9624 8583 437 -36 -383 C ATOM 4364 O SER B 270 59.160 23.859 17.252 1.00 74.61 O ANISOU 4364 O SER B 270 9013 10185 9152 435 -33 -398 O ATOM 4365 CB SER B 270 57.958 25.718 18.934 1.00 67.50 C ANISOU 4365 CB SER B 270 8135 9284 8230 419 -61 -393 C ATOM 4366 OG SER B 270 57.521 26.858 19.657 1.00 63.59 O ANISOU 4366 OG SER B 270 7650 8793 7721 411 -76 -389 O ATOM 4367 N PRO B 271 61.214 24.109 18.117 1.00 62.27 N ANISOU 4367 N PRO B 271 7439 8626 7595 447 -25 -370 N ATOM 4368 CA PRO B 271 61.729 22.946 17.366 1.00 50.53 C ANISOU 4368 CA PRO B 271 5941 7135 6122 457 -10 -374 C ATOM 4369 C PRO B 271 61.127 21.612 17.789 1.00 43.43 C ANISOU 4369 C PRO B 271 5047 6215 5241 461 0 -383 C ATOM 4370 O PRO B 271 61.323 20.618 17.083 1.00 37.43 O ANISOU 4370 O PRO B 271 4279 5451 4492 468 13 -389 O ATOM 4371 CB PRO B 271 63.234 22.984 17.645 1.00 57.11 C ANISOU 4371 CB PRO B 271 6762 7974 6963 466 -3 -356 C ATOM 4372 CG PRO B 271 63.357 23.722 18.942 1.00 64.94 C ANISOU 4372 CG PRO B 271 7761 8962 7951 463 -12 -343 C ATOM 4373 CD PRO B 271 62.254 24.745 18.943 1.00 64.11 C ANISOU 4373 CD PRO B 271 7669 8863 7826 450 -27 -351 C ATOM 4374 N ASN B 272 60.448 21.544 18.936 1.00 44.10 N ANISOU 4374 N ASN B 272 5142 6284 5328 458 -4 -383 N ATOM 4375 CA ASN B 272 59.708 20.360 19.363 1.00 39.16 C ANISOU 4375 CA ASN B 272 4523 5638 4718 461 4 -393 C ATOM 4376 C ASN B 272 58.203 20.594 19.280 1.00 32.97 C ANISOU 4376 C ASN B 272 3751 4851 3927 449 -6 -407 C ATOM 4377 O ASN B 272 57.425 19.913 19.956 1.00 26.46 O ANISOU 4377 O ASN B 272 2934 4007 3111 449 -3 -413 O ATOM 4378 CB ASN B 272 60.098 19.952 20.785 1.00 44.17 C ANISOU 4378 CB ASN B 272 5161 6256 5365 467 8 -382 C ATOM 4379 CG ASN B 272 61.500 19.361 20.873 1.00 48.22 C ANISOU 4379 CG ASN B 272 5660 6768 5892 479 20 -369 C ATOM 4380 OD1 ASN B 272 61.819 18.381 20.198 1.00 53.40 O ANISOU 4380 OD1 ASN B 272 6309 7421 6559 486 33 -374 O ATOM 4381 ND2 ASN B 272 62.336 19.947 21.727 1.00 37.78 N ANISOU 4381 ND2 ASN B 272 4336 5448 4571 482 15 -352 N ATOM 4382 N GLY B 273 57.787 21.545 18.453 1.00 29.47 N ANISOU 4382 N GLY B 273 3307 4423 3467 441 -17 -413 N ATOM 4383 CA GLY B 273 56.427 22.026 18.434 1.00 21.57 C ANISOU 4383 CA GLY B 273 2316 3422 2458 429 -30 -424 C ATOM 4384 C GLY B 273 56.144 22.943 19.605 1.00 24.01 C ANISOU 4384 C GLY B 273 2634 3728 2759 424 -42 -416 C ATOM 4385 O GLY B 273 56.979 23.176 20.483 1.00 30.72 O ANISOU 4385 O GLY B 273 3485 4577 3610 429 -41 -402 O ATOM 4386 N LYS B 274 54.909 23.427 19.644 1.00 22.50 N ANISOU 4386 N LYS B 274 2450 3536 2562 413 -55 -425 N ATOM 4387 CA LYS B 274 54.465 24.344 20.681 1.00 26.27 C ANISOU 4387 CA LYS B 274 2938 4012 3031 407 -68 -419 C ATOM 4388 C LYS B 274 53.441 23.734 21.624 1.00 23.34 C ANISOU 4388 C LYS B 274 2576 3619 2672 404 -66 -424 C ATOM 4389 O LYS B 274 53.443 24.061 22.812 1.00 27.53 O ANISOU 4389 O LYS B 274 3115 4143 3203 404 -71 -416 O ATOM 4390 CB LYS B 274 53.846 25.596 20.046 1.00 38.34 C ANISOU 4390 CB LYS B 274 4467 5557 4543 395 -85 -423 C ATOM 4391 CG LYS B 274 53.245 26.588 21.046 1.00 51.14 C ANISOU 4391 CG LYS B 274 6097 7177 6155 388 -100 -419 C ATOM 4392 CD LYS B 274 52.456 27.674 20.332 1.00 61.49 C ANISOU 4392 CD LYS B 274 7408 8504 7454 377 -117 -425 C ATOM 4393 CE LYS B 274 51.829 28.676 21.282 1.00 68.53 C ANISOU 4393 CE LYS B 274 8308 9390 8340 369 -130 -418 C ATOM 4394 NZ LYS B 274 52.859 29.474 21.998 1.00 71.71 N ANISOU 4394 NZ LYS B 274 8719 9792 8737 369 -126 -400 N ATOM 4395 N LEU B 275 52.564 22.866 21.126 1.00 19.91 N ANISOU 4395 N LEU B 275 2141 3175 2247 402 -61 -437 N ATOM 4396 CA LEU B 275 51.527 22.289 21.966 1.00 21.09 C ANISOU 4396 CA LEU B 275 2300 3306 2409 399 -59 -443 C ATOM 4397 C LEU B 275 52.110 21.291 22.965 1.00 20.17 C ANISOU 4397 C LEU B 275 2188 3172 2306 409 -45 -436 C ATOM 4398 O LEU B 275 53.138 20.651 22.723 1.00 20.13 O ANISOU 4398 O LEU B 275 2175 3166 2306 419 -33 -432 O ATOM 4399 CB LEU B 275 50.461 21.644 21.084 1.00 18.24 C ANISOU 4399 CB LEU B 275 1936 2939 2054 394 -56 -458 C ATOM 4400 CG LEU B 275 49.848 22.695 20.159 1.00 19.49 C ANISOU 4400 CG LEU B 275 2090 3115 2200 384 -71 -464 C ATOM 4401 CD1 LEU B 275 48.806 22.088 19.205 1.00 22.43 C ANISOU 4401 CD1 LEU B 275 2459 3484 2580 379 -68 -479 C ATOM 4402 CD2 LEU B 275 49.234 23.850 20.971 1.00 17.80 C ANISOU 4402 CD2 LEU B 275 1882 2903 1978 376 -87 -459 C ATOM 4403 N ARG B 276 51.433 21.153 24.100 1.00 16.97 N ANISOU 4403 N ARG B 276 1792 2750 1906 407 -46 -435 N ATOM 4404 CA ARG B 276 51.942 20.340 25.196 1.00 15.20 C ANISOU 4404 CA ARG B 276 1573 2508 1694 416 -35 -428 C ATOM 4405 C ARG B 276 51.456 18.902 25.051 1.00 15.03 C ANISOU 4405 C ARG B 276 1553 2469 1689 419 -20 -438 C ATOM 4406 O ARG B 276 50.268 18.658 24.818 1.00 16.59 O ANISOU 4406 O ARG B 276 1754 2660 1889 412 -21 -449 O ATOM 4407 CB ARG B 276 51.515 20.916 26.549 1.00 9.43 C ANISOU 4407 CB ARG B 276 854 1768 962 412 -43 -421 C ATOM 4408 CG ARG B 276 51.850 22.408 26.758 1.00 17.23 C ANISOU 4408 CG ARG B 276 1841 2772 1932 407 -59 -411 C ATOM 4409 CD ARG B 276 53.342 22.640 26.985 1.00 24.67 C ANISOU 4409 CD ARG B 276 2780 3724 2872 416 -56 -397 C ATOM 4410 NE ARG B 276 53.603 24.052 27.274 1.00 29.45 N ANISOU 4410 NE ARG B 276 3387 4343 3460 411 -71 -388 N ATOM 4411 CZ ARG B 276 54.725 24.531 27.803 1.00 32.60 C ANISOU 4411 CZ ARG B 276 3785 4748 3855 417 -71 -374 C ATOM 4412 NH1 ARG B 276 55.732 23.720 28.105 1.00 30.53 N ANISOU 4412 NH1 ARG B 276 3517 4478 3605 428 -59 -366 N ATOM 4413 NH2 ARG B 276 54.840 25.832 28.029 1.00 37.04 N ANISOU 4413 NH2 ARG B 276 4350 5322 4399 411 -85 -367 N ATOM 4414 N LEU B 277 52.377 17.955 25.209 1.00 12.52 N ANISOU 4414 N LEU B 277 1232 2145 1382 430 -5 -433 N ATOM 4415 CA LEU B 277 52.054 16.554 24.953 1.00 11.93 C ANISOU 4415 CA LEU B 277 1157 2055 1322 434 10 -442 C ATOM 4416 C LEU B 277 50.956 16.048 25.893 1.00 14.91 C ANISOU 4416 C LEU B 277 1547 2412 1708 430 12 -447 C ATOM 4417 O LEU B 277 49.945 15.496 25.444 1.00 19.65 O ANISOU 4417 O LEU B 277 2149 3005 2312 425 16 -459 O ATOM 4418 CB LEU B 277 53.318 15.700 25.095 1.00 9.85 C ANISOU 4418 CB LEU B 277 887 1787 1069 448 24 -434 C ATOM 4419 CG LEU B 277 53.068 14.192 24.902 1.00 14.44 C ANISOU 4419 CG LEU B 277 1469 2352 1667 454 41 -443 C ATOM 4420 CD1 LEU B 277 52.582 13.940 23.480 1.00 12.99 C ANISOU 4420 CD1 LEU B 277 1279 2177 1480 450 43 -456 C ATOM 4421 CD2 LEU B 277 54.319 13.354 25.188 1.00 18.34 C ANISOU 4421 CD2 LEU B 277 1956 2840 2173 467 55 -434 C ATOM 4422 N LEU B 278 51.113 16.272 27.202 1.00 14.42 N ANISOU 4422 N LEU B 278 1492 2339 1646 432 10 -437 N ATOM 4423 CA LEU B 278 50.296 15.544 28.175 1.00 19.86 C ANISOU 4423 CA LEU B 278 2194 3007 2347 431 16 -441 C ATOM 4424 C LEU B 278 48.833 15.964 28.148 1.00 20.17 C ANISOU 4424 C LEU B 278 2240 3043 2381 418 8 -450 C ATOM 4425 O LEU B 278 47.946 15.123 28.309 1.00 16.81 O ANISOU 4425 O LEU B 278 1820 2601 1965 416 16 -458 O ATOM 4426 CB LEU B 278 50.854 15.731 29.584 1.00 20.69 C ANISOU 4426 CB LEU B 278 2305 3101 2453 436 15 -428 C ATOM 4427 CG LEU B 278 51.867 14.690 30.035 1.00 16.97 C ANISOU 4427 CG LEU B 278 1831 2619 1996 449 30 -421 C ATOM 4428 CD1 LEU B 278 53.140 14.880 29.251 1.00 20.08 C ANISOU 4428 CD1 LEU B 278 2211 3030 2388 456 31 -415 C ATOM 4429 CD2 LEU B 278 52.107 14.805 31.545 1.00 15.37 C ANISOU 4429 CD2 LEU B 278 1638 2403 1797 452 28 -410 C ATOM 4430 N TYR B 279 48.555 17.259 27.993 1.00 17.55 N ANISOU 4430 N TYR B 279 1907 2725 2036 410 -8 -448 N ATOM 4431 CA TYR B 279 47.200 17.749 28.205 1.00 13.67 C ANISOU 4431 CA TYR B 279 1421 2229 1542 398 -17 -454 C ATOM 4432 C TYR B 279 46.654 18.561 27.040 1.00 12.84 C ANISOU 4432 C TYR B 279 1308 2142 1427 390 -29 -461 C ATOM 4433 O TYR B 279 45.624 19.220 27.202 1.00 15.43 O ANISOU 4433 O TYR B 279 1640 2470 1752 380 -39 -464 O ATOM 4434 CB TYR B 279 47.129 18.575 29.496 1.00 8.08 C ANISOU 4434 CB TYR B 279 723 1517 829 396 -27 -443 C ATOM 4435 CG TYR B 279 48.305 19.499 29.683 1.00 16.06 C ANISOU 4435 CG TYR B 279 1730 2543 1830 401 -35 -431 C ATOM 4436 CD1 TYR B 279 48.369 20.715 29.016 1.00 19.32 C ANISOU 4436 CD1 TYR B 279 2137 2977 2229 395 -50 -429 C ATOM 4437 CD2 TYR B 279 49.345 19.165 30.539 1.00 18.69 C ANISOU 4437 CD2 TYR B 279 2066 2869 2168 411 -29 -420 C ATOM 4438 CE1 TYR B 279 49.449 21.574 29.190 1.00 16.76 C ANISOU 4438 CE1 TYR B 279 1809 2665 1892 399 -57 -418 C ATOM 4439 CE2 TYR B 279 50.427 20.013 30.721 1.00 21.48 C ANISOU 4439 CE2 TYR B 279 2415 3236 2511 415 -36 -408 C ATOM 4440 CZ TYR B 279 50.470 21.217 30.042 1.00 22.03 C ANISOU 4440 CZ TYR B 279 2479 3326 2565 409 -50 -407 C ATOM 4441 OH TYR B 279 51.545 22.054 30.211 1.00 21.94 O ANISOU 4441 OH TYR B 279 2464 3328 2543 412 -57 -395 O ATOM 4442 N GLU B 280 47.319 18.537 25.880 1.00 15.55 N ANISOU 4442 N GLU B 280 1641 2500 1766 393 -28 -464 N ATOM 4443 CA GLU B 280 46.750 19.043 24.637 1.00 18.28 C ANISOU 4443 CA GLU B 280 1979 2861 2105 385 -36 -473 C ATOM 4444 C GLU B 280 46.828 17.949 23.580 1.00 21.73 C ANISOU 4444 C GLU B 280 2409 3297 2549 389 -23 -483 C ATOM 4445 O GLU B 280 45.797 17.487 23.079 1.00 19.08 O ANISOU 4445 O GLU B 280 2074 2956 2220 384 -21 -494 O ATOM 4446 CB GLU B 280 47.483 20.300 24.150 1.00 15.21 C ANISOU 4446 CB GLU B 280 1583 2495 1701 384 -50 -466 C ATOM 4447 CG GLU B 280 47.381 21.493 25.070 1.00 16.70 C ANISOU 4447 CG GLU B 280 1777 2687 1881 379 -64 -456 C ATOM 4448 CD GLU B 280 48.092 22.737 24.511 1.00 16.40 C ANISOU 4448 CD GLU B 280 1732 2673 1826 378 -77 -450 C ATOM 4449 OE1 GLU B 280 49.307 22.688 24.265 1.00 20.82 O ANISOU 4449 OE1 GLU B 280 2287 3241 2381 386 -72 -443 O ATOM 4450 OE2 GLU B 280 47.429 23.759 24.276 1.00 24.72 O ANISOU 4450 OE2 GLU B 280 2785 3737 2872 369 -92 -451 O ATOM 4451 N CYS B 281 48.045 17.485 23.278 1.00 17.47 N ANISOU 4451 N CYS B 281 1865 2762 2012 400 -14 -478 N ATOM 4452 CA CYS B 281 48.228 16.569 22.152 1.00 18.49 C ANISOU 4452 CA CYS B 281 1987 2893 2147 404 -3 -487 C ATOM 4453 C CYS B 281 47.630 15.200 22.435 1.00 16.64 C ANISOU 4453 C CYS B 281 1758 2638 1927 406 12 -495 C ATOM 4454 O CYS B 281 46.808 14.704 21.651 1.00 14.32 O ANISOU 4454 O CYS B 281 1462 2341 1636 402 15 -507 O ATOM 4455 CB CYS B 281 49.706 16.444 21.816 1.00 23.58 C ANISOU 4455 CB CYS B 281 2623 3547 2789 415 4 -479 C ATOM 4456 SG CYS B 281 50.364 17.992 21.234 1.00 22.06 S ANISOU 4456 SG CYS B 281 2424 3381 2579 411 -12 -472 S ATOM 4457 N ASN B 282 48.015 14.581 23.558 1.00 10.98 N ANISOU 4457 N ASN B 282 1048 1906 1219 413 21 -488 N ATOM 4458 CA ASN B 282 47.512 13.240 23.869 1.00 17.74 C ANISOU 4458 CA ASN B 282 1910 2741 2089 416 36 -494 C ATOM 4459 C ASN B 282 45.989 13.179 23.930 1.00 16.34 C ANISOU 4459 C ASN B 282 1740 2555 1915 405 32 -504 C ATOM 4460 O ASN B 282 45.401 12.277 23.301 1.00 11.62 O ANISOU 4460 O ASN B 282 1141 1951 1324 405 41 -515 O ATOM 4461 CB ASN B 282 48.138 12.722 25.174 1.00 16.79 C ANISOU 4461 CB ASN B 282 1797 2605 1977 425 44 -484 C ATOM 4462 CG ASN B 282 49.423 11.944 24.944 1.00 15.71 C ANISOU 4462 CG ASN B 282 1653 2469 1848 438 57 -479 C ATOM 4463 OD1 ASN B 282 49.703 11.469 23.836 1.00 14.00 O ANISOU 4463 OD1 ASN B 282 1428 2259 1632 441 63 -485 O ATOM 4464 ND2 ASN B 282 50.190 11.777 26.002 1.00 13.38 N ANISOU 4464 ND2 ASN B 282 1361 2165 1557 445 61 -468 N ATOM 4465 N PRO B 283 45.288 14.056 24.660 1.00 15.83 N ANISOU 4465 N PRO B 283 1681 2488 1844 397 21 -501 N ATOM 4466 CA PRO B 283 43.815 13.935 24.663 1.00 15.82 C ANISOU 4466 CA PRO B 283 1685 2478 1847 387 19 -511 C ATOM 4467 C PRO B 283 43.198 14.046 23.272 1.00 15.07 C ANISOU 4467 C PRO B 283 1581 2395 1749 380 15 -522 C ATOM 4468 O PRO B 283 42.335 13.234 22.909 1.00 16.60 O ANISOU 4468 O PRO B 283 1776 2579 1951 377 22 -533 O ATOM 4469 CB PRO B 283 43.373 15.074 25.593 1.00 9.92 C ANISOU 4469 CB PRO B 283 944 1732 1094 379 5 -503 C ATOM 4470 CG PRO B 283 44.554 15.265 26.527 1.00 16.47 C ANISOU 4470 CG PRO B 283 1777 2560 1921 388 6 -490 C ATOM 4471 CD PRO B 283 45.759 15.077 25.623 1.00 9.64 C ANISOU 4471 CD PRO B 283 901 1708 1053 397 10 -489 C ATOM 4472 N MET B 284 43.661 14.997 22.460 1.00 12.92 N ANISOU 4472 N MET B 284 1300 2144 1466 379 4 -521 N ATOM 4473 CA MET B 284 43.144 15.133 21.101 1.00 10.93 C ANISOU 4473 CA MET B 284 1038 1903 1210 373 0 -532 C ATOM 4474 C MET B 284 43.532 13.943 20.222 1.00 15.10 C ANISOU 4474 C MET B 284 1563 2430 1746 381 14 -539 C ATOM 4475 O MET B 284 42.728 13.484 19.396 1.00 21.77 O ANISOU 4475 O MET B 284 2404 3273 2594 376 17 -551 O ATOM 4476 CB MET B 284 43.652 16.438 20.494 1.00 17.30 C ANISOU 4476 CB MET B 284 1837 2733 2003 371 -16 -527 C ATOM 4477 CG MET B 284 43.200 17.689 21.262 1.00 15.36 C ANISOU 4477 CG MET B 284 1595 2491 1751 363 -31 -520 C ATOM 4478 SD MET B 284 41.424 17.718 21.536 1.00 18.94 S ANISOU 4478 SD MET B 284 2053 2932 2211 351 -35 -529 S ATOM 4479 CE MET B 284 41.155 19.474 21.823 1.00 25.10 C ANISOU 4479 CE MET B 284 2830 3727 2979 342 -57 -521 C ATOM 4480 N ALA B 285 44.758 13.430 20.375 1.00 19.72 N ANISOU 4480 N ALA B 285 2146 3013 2332 392 24 -533 N ATOM 4481 CA ALA B 285 45.148 12.246 19.620 1.00 15.43 C ANISOU 4481 CA ALA B 285 1599 2466 1796 400 39 -539 C ATOM 4482 C ALA B 285 44.246 11.066 19.955 1.00 20.98 C ANISOU 4482 C ALA B 285 2310 3150 2513 399 51 -547 C ATOM 4483 O ALA B 285 43.866 10.281 19.074 1.00 16.71 O ANISOU 4483 O ALA B 285 1765 2606 1976 399 59 -558 O ATOM 4484 CB ALA B 285 46.606 11.895 19.910 1.00 12.05 C ANISOU 4484 CB ALA B 285 1169 2040 1371 413 48 -529 C ATOM 4485 N TYR B 286 43.893 10.932 21.231 1.00 17.65 N ANISOU 4485 N TYR B 286 1899 2713 2097 398 52 -542 N ATOM 4486 CA TYR B 286 43.051 9.830 21.669 1.00 16.59 C ANISOU 4486 CA TYR B 286 1772 2558 1973 397 64 -549 C ATOM 4487 C TYR B 286 41.626 9.968 21.139 1.00 15.51 C ANISOU 4487 C TYR B 286 1635 2421 1837 385 58 -560 C ATOM 4488 O TYR B 286 41.019 8.979 20.725 1.00 18.60 O ANISOU 4488 O TYR B 286 2028 2803 2236 385 68 -570 O ATOM 4489 CB TYR B 286 43.079 9.766 23.191 1.00 9.42 C ANISOU 4489 CB TYR B 286 874 1634 1069 399 66 -539 C ATOM 4490 CG TYR B 286 42.300 8.645 23.802 1.00 14.56 C ANISOU 4490 CG TYR B 286 1535 2263 1732 399 78 -544 C ATOM 4491 CD1 TYR B 286 42.895 7.412 24.064 1.00 14.38 C ANISOU 4491 CD1 TYR B 286 1515 2228 1719 409 94 -544 C ATOM 4492 CD2 TYR B 286 40.969 8.825 24.158 1.00 17.29 C ANISOU 4492 CD2 TYR B 286 1888 2602 2080 388 74 -549 C ATOM 4493 CE1 TYR B 286 42.169 6.393 24.660 1.00 16.58 C ANISOU 4493 CE1 TYR B 286 1804 2487 2009 409 105 -548 C ATOM 4494 CE2 TYR B 286 40.248 7.822 24.746 1.00 19.11 C ANISOU 4494 CE2 TYR B 286 2128 2813 2321 387 85 -554 C ATOM 4495 CZ TYR B 286 40.846 6.611 24.997 1.00 19.38 C ANISOU 4495 CZ TYR B 286 2165 2834 2364 398 101 -553 C ATOM 4496 OH TYR B 286 40.100 5.619 25.579 1.00 27.69 O ANISOU 4496 OH TYR B 286 3227 3867 3426 397 112 -557 O ATOM 4497 N VAL B 287 41.056 11.172 21.179 1.00 16.76 N ANISOU 4497 N VAL B 287 1792 2588 1987 376 42 -559 N ATOM 4498 CA VAL B 287 39.743 11.383 20.563 1.00 14.79 C ANISOU 4498 CA VAL B 287 1540 2341 1738 365 36 -569 C ATOM 4499 C VAL B 287 39.797 11.049 19.079 1.00 16.79 C ANISOU 4499 C VAL B 287 1784 2605 1990 366 38 -579 C ATOM 4500 O VAL B 287 38.919 10.359 18.543 1.00 16.38 O ANISOU 4500 O VAL B 287 1731 2547 1944 362 44 -590 O ATOM 4501 CB VAL B 287 39.260 12.824 20.791 1.00 13.55 C ANISOU 4501 CB VAL B 287 1381 2194 1572 355 18 -565 C ATOM 4502 CG1 VAL B 287 38.006 13.102 19.963 1.00 13.88 C ANISOU 4502 CG1 VAL B 287 1418 2242 1615 344 11 -576 C ATOM 4503 CG2 VAL B 287 39.010 13.076 22.284 1.00 15.66 C ANISOU 4503 CG2 VAL B 287 1659 2448 1841 353 17 -556 C ATOM 4504 N MET B 288 40.822 11.552 18.386 1.00 12.53 N ANISOU 4504 N MET B 288 1236 2082 1442 370 34 -576 N ATOM 4505 CA MET B 288 40.936 11.289 16.955 1.00 10.58 C ANISOU 4505 CA MET B 288 980 1847 1193 372 36 -585 C ATOM 4506 C MET B 288 40.984 9.786 16.670 1.00 16.23 C ANISOU 4506 C MET B 288 1698 2550 1920 379 54 -592 C ATOM 4507 O MET B 288 40.215 9.277 15.848 1.00 13.90 O ANISOU 4507 O MET B 288 1400 2253 1628 375 57 -603 O ATOM 4508 CB MET B 288 42.173 11.991 16.399 1.00 10.53 C ANISOU 4508 CB MET B 288 966 1859 1177 377 31 -578 C ATOM 4509 CG MET B 288 41.967 13.501 16.213 1.00 17.97 C ANISOU 4509 CG MET B 288 1903 2818 2107 369 12 -575 C ATOM 4510 SD MET B 288 40.760 13.788 14.912 1.00 19.43 S ANISOU 4510 SD MET B 288 2080 3011 2290 358 4 -589 S ATOM 4511 CE MET B 288 39.957 15.301 15.445 1.00 16.99 C ANISOU 4511 CE MET B 288 1772 2710 1974 346 -16 -585 C ATOM 4512 N GLU B 289 41.858 9.051 17.363 1.00 16.15 N ANISOU 4512 N GLU B 289 1692 2529 1915 389 66 -585 N ATOM 4513 CA GLU B 289 41.965 7.616 17.090 1.00 15.60 C ANISOU 4513 CA GLU B 289 1624 2448 1856 397 84 -591 C ATOM 4514 C GLU B 289 40.685 6.879 17.457 1.00 12.55 C ANISOU 4514 C GLU B 289 1246 2044 1479 391 89 -599 C ATOM 4515 O GLU B 289 40.258 5.963 16.740 1.00 18.23 O ANISOU 4515 O GLU B 289 1964 2758 2204 392 98 -609 O ATOM 4516 CB GLU B 289 43.157 7.015 17.829 1.00 11.70 C ANISOU 4516 CB GLU B 289 1133 1946 1367 410 95 -581 C ATOM 4517 CG GLU B 289 44.479 7.388 17.193 1.00 16.38 C ANISOU 4517 CG GLU B 289 1716 2554 1953 418 94 -575 C ATOM 4518 CD GLU B 289 45.571 6.386 17.483 1.00 25.08 C ANISOU 4518 CD GLU B 289 2818 3648 3064 431 110 -570 C ATOM 4519 OE1 GLU B 289 45.258 5.290 17.999 1.00 27.74 O ANISOU 4519 OE1 GLU B 289 3162 3967 3411 435 122 -572 O ATOM 4520 OE2 GLU B 289 46.749 6.701 17.207 1.00 28.97 O ANISOU 4520 OE2 GLU B 289 3303 4152 3552 439 111 -562 O ATOM 4521 N LYS B 290 40.030 7.277 18.543 1.00 10.43 N ANISOU 4521 N LYS B 290 984 1766 1211 385 83 -595 N ATOM 4522 CA LYS B 290 38.765 6.626 18.854 1.00 15.76 C ANISOU 4522 CA LYS B 290 1667 2427 1895 378 88 -603 C ATOM 4523 C LYS B 290 37.696 6.915 17.807 1.00 19.59 C ANISOU 4523 C LYS B 290 2146 2920 2378 368 81 -614 C ATOM 4524 O LYS B 290 36.757 6.122 17.665 1.00 20.07 O ANISOU 4524 O LYS B 290 2210 2970 2447 365 88 -623 O ATOM 4525 CB LYS B 290 38.289 7.043 20.246 1.00 14.13 C ANISOU 4525 CB LYS B 290 1470 2209 1690 373 84 -595 C ATOM 4526 CG LYS B 290 39.136 6.463 21.374 1.00 19.71 C ANISOU 4526 CG LYS B 290 2185 2902 2401 383 94 -586 C ATOM 4527 CD LYS B 290 39.231 4.926 21.273 1.00 25.12 C ANISOU 4527 CD LYS B 290 2874 3573 3098 391 112 -591 C ATOM 4528 CE LYS B 290 40.033 4.346 22.444 1.00 23.41 C ANISOU 4528 CE LYS B 290 2665 3343 2887 401 122 -581 C ATOM 4529 NZ LYS B 290 40.321 2.897 22.302 1.00 22.97 N ANISOU 4529 NZ LYS B 290 2612 3275 2841 410 140 -585 N ATOM 4530 N ALA B 291 37.834 8.006 17.050 1.00 14.78 N ANISOU 4530 N ALA B 291 1527 2329 1759 364 67 -614 N ATOM 4531 CA ALA B 291 36.915 8.344 15.967 1.00 13.58 C ANISOU 4531 CA ALA B 291 1368 2186 1605 355 60 -625 C ATOM 4532 C ALA B 291 37.367 7.833 14.606 1.00 12.96 C ANISOU 4532 C ALA B 291 1282 2118 1525 360 65 -633 C ATOM 4533 O ALA B 291 36.856 8.308 13.586 1.00 14.95 O ANISOU 4533 O ALA B 291 1526 2381 1773 354 57 -641 O ATOM 4534 CB ALA B 291 36.697 9.862 15.900 1.00 13.27 C ANISOU 4534 CB ALA B 291 1323 2162 1555 346 41 -621 C ATOM 4535 N GLY B 292 38.359 6.946 14.552 1.00 22.41 N ANISOU 4535 N GLY B 292 2479 3309 2725 372 78 -631 N ATOM 4536 CA GLY B 292 38.857 6.481 13.271 1.00 18.56 C ANISOU 4536 CA GLY B 292 1984 2831 2236 378 84 -638 C ATOM 4537 C GLY B 292 39.784 7.451 12.580 1.00 21.83 C ANISOU 4537 C GLY B 292 2389 3266 2639 380 75 -633 C ATOM 4538 O GLY B 292 40.041 7.300 11.376 1.00 14.79 O ANISOU 4538 O GLY B 292 1491 2385 1745 382 77 -639 O ATOM 4539 N GLY B 293 40.279 8.458 13.304 1.00 19.70 N ANISOU 4539 N GLY B 293 2120 3002 2362 379 65 -622 N ATOM 4540 CA GLY B 293 41.229 9.402 12.771 1.00 14.49 C ANISOU 4540 CA GLY B 293 1453 2361 1691 381 57 -616 C ATOM 4541 C GLY B 293 42.647 9.040 13.154 1.00 14.33 C ANISOU 4541 C GLY B 293 1433 2341 1672 394 67 -606 C ATOM 4542 O GLY B 293 42.933 7.948 13.650 1.00 18.42 O ANISOU 4542 O GLY B 293 1956 2844 2200 402 81 -605 O ATOM 4543 N MET B 294 43.552 9.976 12.897 1.00 11.81 N ANISOU 4543 N MET B 294 1107 2037 1342 396 59 -598 N ATOM 4544 CA MET B 294 44.966 9.756 13.160 1.00 12.38 C ANISOU 4544 CA MET B 294 1178 2113 1415 408 67 -588 C ATOM 4545 C MET B 294 45.573 10.996 13.797 1.00 17.56 C ANISOU 4545 C MET B 294 1834 2779 2061 406 54 -576 C ATOM 4546 O MET B 294 45.031 12.100 13.699 1.00 13.14 O ANISOU 4546 O MET B 294 1272 2229 1491 397 39 -576 O ATOM 4547 CB MET B 294 45.718 9.377 11.878 1.00 13.75 C ANISOU 4547 CB MET B 294 1343 2297 1586 415 75 -592 C ATOM 4548 CG MET B 294 45.355 7.995 11.333 1.00 16.46 C ANISOU 4548 CG MET B 294 1686 2627 1939 420 90 -603 C ATOM 4549 SD MET B 294 46.183 7.657 9.760 1.00 23.16 S ANISOU 4549 SD MET B 294 2525 3490 2785 428 98 -608 S ATOM 4550 CE MET B 294 47.893 7.568 10.301 1.00 17.82 C ANISOU 4550 CE MET B 294 1845 2817 2110 441 107 -593 C ATOM 4551 N ALA B 295 46.694 10.785 14.483 1.00 22.33 N ANISOU 4551 N ALA B 295 2438 3379 2666 416 61 -565 N ATOM 4552 CA ALA B 295 47.466 11.860 15.098 1.00 19.22 C ANISOU 4552 CA ALA B 295 2043 2996 2264 417 51 -552 C ATOM 4553 C ALA B 295 48.911 11.412 15.203 1.00 16.81 C ANISOU 4553 C ALA B 295 1734 2692 1962 430 63 -542 C ATOM 4554 O ALA B 295 49.200 10.430 15.898 1.00 21.22 O ANISOU 4554 O ALA B 295 2297 3235 2532 437 75 -540 O ATOM 4555 CB ALA B 295 46.932 12.211 16.482 1.00 16.68 C ANISOU 4555 CB ALA B 295 1731 2662 1944 412 45 -546 C ATOM 4556 N THR B 296 49.806 12.145 14.546 1.00 19.60 N ANISOU 4556 N THR B 296 2078 3063 2305 432 58 -537 N ATOM 4557 CA THR B 296 51.211 11.784 14.440 1.00 20.84 C ANISOU 4557 CA THR B 296 2229 3225 2466 445 69 -528 C ATOM 4558 C THR B 296 52.067 12.993 14.780 1.00 17.72 C ANISOU 4558 C THR B 296 1830 2844 2059 445 58 -515 C ATOM 4559 O THR B 296 51.631 14.136 14.634 1.00 16.26 O ANISOU 4559 O THR B 296 1645 2670 1862 435 42 -516 O ATOM 4560 CB THR B 296 51.540 11.284 13.014 1.00 22.57 C ANISOU 4560 CB THR B 296 2438 3452 2684 449 77 -536 C ATOM 4561 OG1 THR B 296 52.925 10.923 12.924 1.00 18.26 O ANISOU 4561 OG1 THR B 296 1886 2910 2143 462 88 -527 O ATOM 4562 CG2 THR B 296 51.222 12.382 11.985 1.00 14.89 C ANISOU 4562 CG2 THR B 296 1461 2500 1698 441 63 -541 C ATOM 4563 N THR B 297 53.283 12.739 15.268 1.00 19.64 N ANISOU 4563 N THR B 297 2069 3086 2307 455 66 -504 N ATOM 4564 CA THR B 297 54.274 13.806 15.380 1.00 23.85 C ANISOU 4564 CA THR B 297 2596 3634 2830 457 58 -491 C ATOM 4565 C THR B 297 55.033 14.041 14.083 1.00 28.98 C ANISOU 4565 C THR B 297 3235 4303 3475 460 60 -491 C ATOM 4566 O THR B 297 55.797 15.012 13.993 1.00 23.27 O ANISOU 4566 O THR B 297 2505 3594 2740 460 52 -482 O ATOM 4567 CB THR B 297 55.297 13.484 16.470 1.00 24.25 C ANISOU 4567 CB THR B 297 2647 3677 2890 467 65 -477 C ATOM 4568 OG1 THR B 297 56.074 12.356 16.047 1.00 27.85 O ANISOU 4568 OG1 THR B 297 3095 4127 3358 478 82 -477 O ATOM 4569 CG2 THR B 297 54.608 13.165 17.781 1.00 17.12 C ANISOU 4569 CG2 THR B 297 1756 2755 1994 464 64 -476 C ATOM 4570 N GLY B 298 54.832 13.184 13.087 1.00 23.87 N ANISOU 4570 N GLY B 298 2584 3654 2833 463 70 -502 N ATOM 4571 CA GLY B 298 55.678 13.130 11.916 1.00 19.56 C ANISOU 4571 CA GLY B 298 2027 3122 2284 469 77 -502 C ATOM 4572 C GLY B 298 56.528 11.876 11.954 1.00 27.74 C ANISOU 4572 C GLY B 298 3057 4147 3335 483 96 -499 C ATOM 4573 O GLY B 298 56.613 11.153 10.964 1.00 33.63 O ANISOU 4573 O GLY B 298 3798 4894 4085 487 106 -507 O ATOM 4574 N LYS B 299 57.100 11.568 13.118 1.00 27.70 N ANISOU 4574 N LYS B 299 3054 4131 3339 489 101 -488 N ATOM 4575 CA LYS B 299 57.954 10.398 13.292 1.00 26.57 C ANISOU 4575 CA LYS B 299 2906 3977 3212 502 118 -484 C ATOM 4576 C LYS B 299 57.256 9.221 13.956 1.00 29.42 C ANISOU 4576 C LYS B 299 3277 4316 3587 504 128 -490 C ATOM 4577 O LYS B 299 57.701 8.078 13.773 1.00 27.14 O ANISOU 4577 O LYS B 299 2984 4018 3311 514 144 -492 O ATOM 4578 CB LYS B 299 59.196 10.755 14.115 1.00 30.65 C ANISOU 4578 CB LYS B 299 3417 4497 3733 510 119 -466 C ATOM 4579 CG LYS B 299 60.140 11.711 13.407 1.00 43.24 C ANISOU 4579 CG LYS B 299 4999 6112 5317 510 113 -458 C ATOM 4580 CD LYS B 299 61.311 12.108 14.293 1.00 55.65 C ANISOU 4580 CD LYS B 299 6565 7687 6893 517 113 -440 C ATOM 4581 CE LYS B 299 62.274 13.031 13.557 1.00 62.36 C ANISOU 4581 CE LYS B 299 7403 8558 7733 518 108 -431 C ATOM 4582 NZ LYS B 299 63.341 13.564 14.449 1.00 66.82 N ANISOU 4582 NZ LYS B 299 7961 9126 8300 522 105 -413 N ATOM 4583 N GLU B 300 56.183 9.461 14.715 1.00 19.83 N ANISOU 4583 N GLU B 300 2074 3092 2370 495 119 -494 N ATOM 4584 CA GLU B 300 55.467 8.388 15.390 1.00 16.18 C ANISOU 4584 CA GLU B 300 1620 2607 1919 496 127 -500 C ATOM 4585 C GLU B 300 54.074 8.873 15.767 1.00 20.68 C ANISOU 4585 C GLU B 300 2201 3173 2482 483 115 -508 C ATOM 4586 O GLU B 300 53.770 10.068 15.708 1.00 19.64 O ANISOU 4586 O GLU B 300 2071 3055 2338 474 99 -507 O ATOM 4587 CB GLU B 300 56.206 7.930 16.639 1.00 20.36 C ANISOU 4587 CB GLU B 300 2151 3124 2460 505 134 -488 C ATOM 4588 CG GLU B 300 56.389 9.034 17.649 1.00 27.83 C ANISOU 4588 CG GLU B 300 3100 4074 3399 500 120 -477 C ATOM 4589 CD GLU B 300 57.379 8.669 18.722 1.00 43.58 C ANISOU 4589 CD GLU B 300 5092 6059 5405 510 127 -463 C ATOM 4590 OE1 GLU B 300 57.267 7.548 19.268 1.00 51.22 O ANISOU 4590 OE1 GLU B 300 6065 7009 6387 516 139 -465 O ATOM 4591 OE2 GLU B 300 58.284 9.491 18.998 1.00 43.15 O ANISOU 4591 OE2 GLU B 300 5032 6017 5347 513 121 -450 O ATOM 4592 N ALA B 301 53.229 7.921 16.168 1.00 19.40 N ANISOU 4592 N ALA B 301 2049 2994 2330 482 122 -516 N ATOM 4593 CA ALA B 301 51.934 8.280 16.728 1.00 20.69 C ANISOU 4593 CA ALA B 301 2223 3150 2490 470 112 -522 C ATOM 4594 C ALA B 301 52.144 9.060 18.021 1.00 20.56 C ANISOU 4594 C ALA B 301 2211 3131 2471 468 103 -509 C ATOM 4595 O ALA B 301 52.981 8.687 18.847 1.00 27.37 O ANISOU 4595 O ALA B 301 3074 3985 3341 477 110 -499 O ATOM 4596 CB ALA B 301 51.099 7.025 16.990 1.00 19.66 C ANISOU 4596 CB ALA B 301 2100 2999 2372 471 123 -531 C ATOM 4597 N VAL B 302 51.417 10.175 18.164 1.00 16.61 N ANISOU 4597 N VAL B 302 1715 2638 1958 457 86 -510 N ATOM 4598 CA VAL B 302 51.432 10.960 19.406 1.00 16.08 C ANISOU 4598 CA VAL B 302 1655 2568 1888 453 76 -500 C ATOM 4599 C VAL B 302 51.247 10.055 20.621 1.00 17.12 C ANISOU 4599 C VAL B 302 1795 2677 2033 458 86 -498 C ATOM 4600 O VAL B 302 51.961 10.172 21.626 1.00 12.40 O ANISOU 4600 O VAL B 302 1199 2075 1438 463 87 -486 O ATOM 4601 CB VAL B 302 50.344 12.050 19.353 1.00 18.08 C ANISOU 4601 CB VAL B 302 1912 2829 2130 440 59 -505 C ATOM 4602 CG1 VAL B 302 50.249 12.795 20.671 1.00 13.53 C ANISOU 4602 CG1 VAL B 302 1343 2247 1549 436 50 -495 C ATOM 4603 CG2 VAL B 302 50.598 12.992 18.176 1.00 19.57 C ANISOU 4603 CG2 VAL B 302 2091 3039 2304 436 49 -507 C ATOM 4604 N LEU B 303 50.272 9.146 20.549 1.00 12.50 N ANISOU 4604 N LEU B 303 1217 2078 1455 455 93 -509 N ATOM 4605 CA LEU B 303 49.938 8.289 21.682 1.00 23.41 C ANISOU 4605 CA LEU B 303 2608 3438 2849 458 102 -507 C ATOM 4606 C LEU B 303 51.051 7.307 22.032 1.00 20.25 C ANISOU 4606 C LEU B 303 2205 3029 2461 472 117 -500 C ATOM 4607 O LEU B 303 50.971 6.665 23.084 1.00 18.79 O ANISOU 4607 O LEU B 303 2028 2826 2285 475 124 -497 O ATOM 4608 CB LEU B 303 48.640 7.520 21.403 1.00 16.94 C ANISOU 4608 CB LEU B 303 1796 2607 2035 451 107 -521 C ATOM 4609 CG LEU B 303 47.346 8.327 21.181 1.00 23.27 C ANISOU 4609 CG LEU B 303 2601 3413 2827 437 93 -529 C ATOM 4610 CD1 LEU B 303 46.185 7.395 20.812 1.00 13.43 C ANISOU 4610 CD1 LEU B 303 1360 2155 1589 433 101 -542 C ATOM 4611 CD2 LEU B 303 46.964 9.186 22.411 1.00 16.23 C ANISOU 4611 CD2 LEU B 303 1717 2517 1931 431 82 -521 C ATOM 4612 N ASP B 304 52.068 7.159 21.179 1.00 12.48 N ANISOU 4612 N ASP B 304 1209 2056 1477 480 123 -498 N ATOM 4613 CA ASP B 304 53.196 6.291 21.476 1.00 18.62 C ANISOU 4613 CA ASP B 304 1981 2826 2266 493 137 -490 C ATOM 4614 C ASP B 304 54.379 7.030 22.083 1.00 20.34 C ANISOU 4614 C ASP B 304 2193 3052 2483 499 131 -475 C ATOM 4615 O ASP B 304 55.336 6.375 22.504 1.00 19.27 O ANISOU 4615 O ASP B 304 2053 2910 2359 510 141 -466 O ATOM 4616 CB ASP B 304 53.671 5.565 20.213 1.00 20.57 C ANISOU 4616 CB ASP B 304 2218 3079 2517 500 148 -497 C ATOM 4617 CG ASP B 304 52.757 4.432 19.813 1.00 24.04 C ANISOU 4617 CG ASP B 304 2664 3507 2965 499 158 -510 C ATOM 4618 OD1 ASP B 304 52.176 3.800 20.717 1.00 25.75 O ANISOU 4618 OD1 ASP B 304 2891 3705 3189 499 163 -511 O ATOM 4619 OD2 ASP B 304 52.629 4.176 18.598 1.00 26.57 O ANISOU 4619 OD2 ASP B 304 2979 3835 3283 499 162 -519 O ATOM 4620 N VAL B 305 54.371 8.368 22.085 1.00 15.00 N ANISOU 4620 N VAL B 305 1516 2391 1792 492 116 -470 N ATOM 4621 CA VAL B 305 55.461 9.100 22.717 1.00 17.33 C ANISOU 4621 CA VAL B 305 1805 2693 2085 496 110 -454 C ATOM 4622 C VAL B 305 55.455 8.804 24.207 1.00 21.57 C ANISOU 4622 C VAL B 305 2352 3212 2631 499 112 -447 C ATOM 4623 O VAL B 305 54.405 8.869 24.859 1.00 21.18 O ANISOU 4623 O VAL B 305 2315 3152 2580 491 107 -452 O ATOM 4624 CB VAL B 305 55.339 10.608 22.448 1.00 16.04 C ANISOU 4624 CB VAL B 305 1641 2548 1904 487 92 -452 C ATOM 4625 CG1 VAL B 305 56.454 11.344 23.154 1.00 19.90 C ANISOU 4625 CG1 VAL B 305 2125 3044 2391 492 87 -435 C ATOM 4626 CG2 VAL B 305 55.406 10.892 20.970 1.00 14.18 C ANISOU 4626 CG2 VAL B 305 1397 2332 1661 485 91 -459 C ATOM 4627 N ILE B 306 56.620 8.463 24.749 1.00 16.69 N ANISOU 4627 N ILE B 306 1727 2591 2024 510 118 -435 N ATOM 4628 CA ILE B 306 56.776 8.247 26.185 1.00 16.68 C ANISOU 4628 CA ILE B 306 1734 2574 2031 514 119 -426 C ATOM 4629 C ILE B 306 57.338 9.539 26.790 1.00 15.64 C ANISOU 4629 C ILE B 306 1599 2453 1890 512 105 -412 C ATOM 4630 O ILE B 306 58.490 9.888 26.500 1.00 21.99 O ANISOU 4630 O ILE B 306 2390 3269 2694 518 104 -402 O ATOM 4631 CB ILE B 306 57.673 7.043 26.477 1.00 28.75 C ANISOU 4631 CB ILE B 306 3256 4090 3578 528 135 -420 C ATOM 4632 CG1 ILE B 306 57.065 5.794 25.821 1.00 28.61 C ANISOU 4632 CG1 ILE B 306 3241 4061 3568 529 149 -434 C ATOM 4633 CG2 ILE B 306 57.816 6.850 27.977 1.00 29.47 C ANISOU 4633 CG2 ILE B 306 3355 4165 3679 531 135 -411 C ATOM 4634 CD1 ILE B 306 57.763 4.517 26.173 1.00 35.58 C ANISOU 4634 CD1 ILE B 306 4120 4929 4469 542 164 -431 C ATOM 4635 N PRO B 307 56.561 10.274 27.576 1.00 16.45 N ANISOU 4635 N PRO B 307 1714 2553 1985 503 93 -412 N ATOM 4636 CA PRO B 307 57.036 11.567 28.084 1.00 14.64 C ANISOU 4636 CA PRO B 307 1483 2334 1744 500 79 -400 C ATOM 4637 C PRO B 307 58.054 11.412 29.201 1.00 24.56 C ANISOU 4637 C PRO B 307 2736 3583 3012 510 81 -384 C ATOM 4638 O PRO B 307 58.045 10.432 29.951 1.00 19.61 O ANISOU 4638 O PRO B 307 2115 2937 2400 516 91 -383 O ATOM 4639 CB PRO B 307 55.760 12.224 28.620 1.00 23.13 C ANISOU 4639 CB PRO B 307 2572 3405 2809 488 68 -406 C ATOM 4640 CG PRO B 307 54.852 11.082 28.941 1.00 20.70 C ANISOU 4640 CG PRO B 307 2275 3077 2512 488 79 -416 C ATOM 4641 CD PRO B 307 55.178 9.975 27.983 1.00 14.23 C ANISOU 4641 CD PRO B 307 1447 2257 1702 495 93 -423 C ATOM 4642 N THR B 308 58.943 12.412 29.300 1.00 17.07 N ANISOU 4642 N THR B 308 1780 2649 2058 511 71 -371 N ATOM 4643 CA THR B 308 59.864 12.538 30.429 1.00 21.95 C ANISOU 4643 CA THR B 308 2394 3260 2684 518 69 -354 C ATOM 4644 C THR B 308 59.673 13.823 31.227 1.00 22.27 C ANISOU 4644 C THR B 308 2442 3306 2712 511 53 -346 C ATOM 4645 O THR B 308 60.324 13.986 32.266 1.00 18.87 O ANISOU 4645 O THR B 308 2011 2869 2288 517 49 -332 O ATOM 4646 CB THR B 308 61.334 12.441 29.975 1.00 20.67 C ANISOU 4646 CB THR B 308 2214 3109 2531 529 73 -342 C ATOM 4647 OG1 THR B 308 61.653 13.516 29.082 1.00 22.06 O ANISOU 4647 OG1 THR B 308 2381 3308 2692 523 64 -340 O ATOM 4648 CG2 THR B 308 61.601 11.086 29.289 1.00 15.08 C ANISOU 4648 CG2 THR B 308 1499 2394 1838 537 90 -349 C ATOM 4649 N ASP B 309 58.840 14.752 30.759 1.00 17.39 N ANISOU 4649 N ASP B 309 1831 2700 2076 500 42 -354 N ATOM 4650 CA ASP B 309 58.574 15.988 31.485 1.00 21.95 C ANISOU 4650 CA ASP B 309 2417 3283 2641 493 27 -347 C ATOM 4651 C ASP B 309 57.103 16.323 31.288 1.00 17.66 C ANISOU 4651 C ASP B 309 1887 2739 2085 480 21 -362 C ATOM 4652 O ASP B 309 56.612 16.296 30.158 1.00 22.82 O ANISOU 4652 O ASP B 309 2537 3401 2732 475 22 -373 O ATOM 4653 CB ASP B 309 59.481 17.128 30.987 1.00 20.77 C ANISOU 4653 CB ASP B 309 2256 3156 2480 492 17 -336 C ATOM 4654 CG ASP B 309 59.239 18.439 31.716 1.00 36.52 C ANISOU 4654 CG ASP B 309 4259 5156 4460 484 1 -329 C ATOM 4655 OD1 ASP B 309 58.187 19.075 31.522 1.00 32.52 O ANISOU 4655 OD1 ASP B 309 3762 4654 3939 474 -7 -338 O ATOM 4656 OD2 ASP B 309 60.117 18.821 32.520 1.00 44.05 O ANISOU 4656 OD2 ASP B 309 5206 6118 5412 494 -7 -317 O ATOM 4657 N ILE B 310 56.398 16.638 32.376 1.00 18.83 N ANISOU 4657 N ILE B 310 2049 2876 2231 476 15 -361 N ATOM 4658 CA ILE B 310 54.948 16.794 32.275 1.00 16.08 C ANISOU 4658 CA ILE B 310 1712 2522 1874 464 11 -374 C ATOM 4659 C ILE B 310 54.541 17.965 31.395 1.00 19.29 C ANISOU 4659 C ILE B 310 2117 2950 2263 454 -3 -378 C ATOM 4660 O ILE B 310 53.399 18.006 30.929 1.00 20.82 O ANISOU 4660 O ILE B 310 2315 3142 2452 445 -5 -391 O ATOM 4661 CB ILE B 310 54.313 16.934 33.667 1.00 18.02 C ANISOU 4661 CB ILE B 310 1973 2752 2122 462 7 -371 C ATOM 4662 CG1 ILE B 310 54.873 18.168 34.395 1.00 18.52 C ANISOU 4662 CG1 ILE B 310 2037 2823 2175 461 -7 -357 C ATOM 4663 CG2 ILE B 310 54.552 15.647 34.469 1.00 22.31 C ANISOU 4663 CG2 ILE B 310 2520 3273 2684 471 21 -369 C ATOM 4664 CD1 ILE B 310 54.126 18.513 35.684 1.00 19.73 C ANISOU 4664 CD1 ILE B 310 2208 2963 2327 457 -13 -355 C ATOM 4665 N HIS B 311 55.433 18.929 31.166 1.00 17.38 N ANISOU 4665 N HIS B 311 1867 2726 2011 455 -11 -368 N ATOM 4666 CA HIS B 311 55.147 20.079 30.319 1.00 20.80 C ANISOU 4666 CA HIS B 311 2298 3180 2427 446 -24 -371 C ATOM 4667 C HIS B 311 55.859 20.007 28.979 1.00 20.31 C ANISOU 4667 C HIS B 311 2221 3134 2362 449 -19 -373 C ATOM 4668 O HIS B 311 56.017 21.035 28.317 1.00 19.97 O ANISOU 4668 O HIS B 311 2174 3110 2304 444 -29 -372 O ATOM 4669 CB HIS B 311 55.528 21.377 31.036 1.00 13.48 C ANISOU 4669 CB HIS B 311 1373 2261 1486 443 -37 -359 C ATOM 4670 CG HIS B 311 54.740 21.613 32.276 1.00 11.16 C ANISOU 4670 CG HIS B 311 1094 1953 1192 439 -43 -358 C ATOM 4671 ND1 HIS B 311 53.375 21.803 32.251 1.00 14.58 N ANISOU 4671 ND1 HIS B 311 1536 2381 1620 429 -49 -369 N ATOM 4672 CD2 HIS B 311 55.105 21.644 33.581 1.00 11.45 C ANISOU 4672 CD2 HIS B 311 1137 1981 1232 446 -45 -348 C ATOM 4673 CE1 HIS B 311 52.936 21.972 33.487 1.00 15.96 C ANISOU 4673 CE1 HIS B 311 1724 2543 1797 428 -53 -365 C ATOM 4674 NE2 HIS B 311 53.962 21.868 34.313 1.00 15.50 N ANISOU 4674 NE2 HIS B 311 1664 2482 1743 439 -51 -353 N ATOM 4675 N GLN B 312 56.292 18.824 28.564 1.00 17.56 N ANISOU 4675 N GLN B 312 1865 2778 2027 457 -5 -376 N ATOM 4676 CA GLN B 312 57.059 18.731 27.336 1.00 22.62 C ANISOU 4676 CA GLN B 312 2493 3435 2668 461 0 -377 C ATOM 4677 C GLN B 312 56.151 18.975 26.136 1.00 21.96 C ANISOU 4677 C GLN B 312 2408 3361 2573 452 -4 -391 C ATOM 4678 O GLN B 312 54.943 18.744 26.184 1.00 16.03 O ANISOU 4678 O GLN B 312 1666 2601 1823 445 -6 -403 O ATOM 4679 CB GLN B 312 57.773 17.376 27.241 1.00 17.40 C ANISOU 4679 CB GLN B 312 1824 2763 2026 473 17 -375 C ATOM 4680 CG GLN B 312 56.974 16.234 26.666 1.00 23.45 C ANISOU 4680 CG GLN B 312 2593 3518 2801 473 28 -391 C ATOM 4681 CD GLN B 312 57.788 14.945 26.603 1.00 29.84 C ANISOU 4681 CD GLN B 312 3394 4318 3628 486 45 -388 C ATOM 4682 OE1 GLN B 312 58.379 14.525 27.597 1.00 33.55 O ANISOU 4682 OE1 GLN B 312 3863 4775 4109 493 50 -378 O ATOM 4683 NE2 GLN B 312 57.844 14.328 25.427 1.00 27.84 N ANISOU 4683 NE2 GLN B 312 3133 4069 3378 488 54 -397 N ATOM 4684 N ARG B 313 56.735 19.519 25.081 1.00 26.74 N ANISOU 4684 N ARG B 313 3004 3986 3170 452 -7 -390 N ATOM 4685 CA ARG B 313 56.011 19.864 23.870 1.00 24.29 C ANISOU 4685 CA ARG B 313 2692 3688 2849 444 -13 -403 C ATOM 4686 C ARG B 313 56.114 18.732 22.851 1.00 22.66 C ANISOU 4686 C ARG B 313 2478 3479 2653 449 2 -412 C ATOM 4687 O ARG B 313 56.988 17.867 22.930 1.00 20.73 O ANISOU 4687 O ARG B 313 2227 3229 2422 460 15 -407 O ATOM 4688 CB ARG B 313 56.549 21.181 23.299 1.00 16.14 C ANISOU 4688 CB ARG B 313 1655 2679 1800 440 -24 -396 C ATOM 4689 CG ARG B 313 56.515 22.326 24.313 1.00 21.12 C ANISOU 4689 CG ARG B 313 2293 3312 2419 435 -38 -386 C ATOM 4690 CD ARG B 313 57.138 23.612 23.753 1.00 33.58 C ANISOU 4690 CD ARG B 313 3866 4914 3979 431 -48 -379 C ATOM 4691 NE ARG B 313 57.210 24.702 24.734 1.00 33.24 N ANISOU 4691 NE ARG B 313 3831 4873 3924 427 -59 -369 N ATOM 4692 CZ ARG B 313 56.262 25.619 24.932 1.00 42.53 C ANISOU 4692 CZ ARG B 313 5018 6054 5088 416 -74 -373 C ATOM 4693 NH1 ARG B 313 55.137 25.600 24.222 1.00 33.65 N ANISOU 4693 NH1 ARG B 313 3895 4930 3961 409 -79 -388 N ATOM 4694 NH2 ARG B 313 56.440 26.571 25.844 1.00 47.75 N ANISOU 4694 NH2 ARG B 313 5686 6717 5739 414 -82 -363 N ATOM 4695 N ALA B 314 55.174 18.721 21.907 1.00 28.31 N ANISOU 4695 N ALA B 314 3194 4199 3364 442 -1 -426 N ATOM 4696 CA ALA B 314 55.219 17.760 20.820 1.00 21.41 C ANISOU 4696 CA ALA B 314 2313 3325 2498 446 11 -436 C ATOM 4697 C ALA B 314 54.601 18.381 19.575 1.00 24.32 C ANISOU 4697 C ALA B 314 2678 3709 2853 437 2 -446 C ATOM 4698 O ALA B 314 53.606 19.115 19.687 1.00 20.73 O ANISOU 4698 O ALA B 314 2229 3256 2390 427 -11 -451 O ATOM 4699 CB ALA B 314 54.486 16.467 21.180 1.00 21.65 C ANISOU 4699 CB ALA B 314 2349 3333 2543 448 22 -445 C ATOM 4700 N PRO B 315 55.151 18.118 18.390 1.00 24.48 N ANISOU 4700 N PRO B 315 2689 3741 2874 442 8 -450 N ATOM 4701 CA PRO B 315 54.442 18.484 17.162 1.00 21.62 C ANISOU 4701 CA PRO B 315 2324 3390 2503 434 2 -462 C ATOM 4702 C PRO B 315 53.236 17.580 17.002 1.00 21.42 C ANISOU 4702 C PRO B 315 2302 3349 2486 430 7 -476 C ATOM 4703 O PRO B 315 53.206 16.452 17.505 1.00 20.90 O ANISOU 4703 O PRO B 315 2241 3266 2435 436 20 -478 O ATOM 4704 CB PRO B 315 55.477 18.236 16.050 1.00 22.29 C ANISOU 4704 CB PRO B 315 2395 3487 2586 442 11 -460 C ATOM 4705 CG PRO B 315 56.764 17.874 16.749 1.00 25.10 C ANISOU 4705 CG PRO B 315 2748 3840 2951 453 21 -446 C ATOM 4706 CD PRO B 315 56.378 17.362 18.106 1.00 21.91 C ANISOU 4706 CD PRO B 315 2353 3415 2557 454 23 -443 C ATOM 4707 N VAL B 316 52.224 18.083 16.309 1.00 18.69 N ANISOU 4707 N VAL B 316 1958 3010 2133 420 -4 -487 N ATOM 4708 CA VAL B 316 51.008 17.296 16.139 1.00 22.90 C ANISOU 4708 CA VAL B 316 2495 3530 2675 415 0 -500 C ATOM 4709 C VAL B 316 50.421 17.576 14.763 1.00 21.52 C ANISOU 4709 C VAL B 316 2315 3368 2495 409 -5 -512 C ATOM 4710 O VAL B 316 50.272 18.733 14.356 1.00 23.82 O ANISOU 4710 O VAL B 316 2603 3674 2772 402 -20 -511 O ATOM 4711 CB VAL B 316 49.990 17.569 17.272 1.00 22.65 C ANISOU 4711 CB VAL B 316 2475 3486 2646 408 -8 -500 C ATOM 4712 CG1 VAL B 316 49.639 19.055 17.358 1.00 19.61 C ANISOU 4712 CG1 VAL B 316 2090 3114 2246 398 -27 -496 C ATOM 4713 CG2 VAL B 316 48.725 16.726 17.088 1.00 25.06 C ANISOU 4713 CG2 VAL B 316 2784 3777 2961 403 -3 -513 C ATOM 4714 N ILE B 317 50.107 16.497 14.052 1.00 17.90 N ANISOU 4714 N ILE B 317 1854 2902 2045 412 7 -522 N ATOM 4715 CA ILE B 317 49.355 16.523 12.804 1.00 20.90 C ANISOU 4715 CA ILE B 317 2229 3289 2422 406 3 -535 C ATOM 4716 C ILE B 317 48.243 15.495 12.957 1.00 22.27 C ANISOU 4716 C ILE B 317 2409 3445 2608 403 11 -546 C ATOM 4717 O ILE B 317 48.520 14.305 13.145 1.00 21.53 O ANISOU 4717 O ILE B 317 2316 3337 2525 411 26 -547 O ATOM 4718 CB ILE B 317 50.235 16.195 11.581 1.00 16.63 C ANISOU 4718 CB ILE B 317 1679 2760 1879 413 12 -537 C ATOM 4719 CG1 ILE B 317 51.351 17.224 11.414 1.00 16.16 C ANISOU 4719 CG1 ILE B 317 1614 2720 1807 416 5 -526 C ATOM 4720 CG2 ILE B 317 49.393 16.071 10.317 1.00 23.54 C ANISOU 4720 CG2 ILE B 317 2550 3641 2753 407 10 -551 C ATOM 4721 CD1 ILE B 317 52.628 16.837 12.114 1.00 22.67 C ANISOU 4721 CD1 ILE B 317 2437 3540 2637 427 16 -513 C ATOM 4722 N LEU B 318 46.992 15.943 12.895 1.00 23.03 N ANISOU 4722 N LEU B 318 2508 3541 2703 392 0 -553 N ATOM 4723 CA LEU B 318 45.889 15.050 13.215 1.00 17.50 C ANISOU 4723 CA LEU B 318 1814 2822 2015 388 6 -562 C ATOM 4724 C LEU B 318 44.707 15.318 12.296 1.00 13.89 C ANISOU 4724 C LEU B 318 1353 2370 1556 378 -2 -575 C ATOM 4725 O LEU B 318 44.597 16.368 11.659 1.00 17.29 O ANISOU 4725 O LEU B 318 1777 2816 1975 372 -15 -575 O ATOM 4726 CB LEU B 318 45.465 15.178 14.699 1.00 20.98 C ANISOU 4726 CB LEU B 318 2264 3248 2459 385 3 -556 C ATOM 4727 CG LEU B 318 44.908 16.496 15.279 1.00 18.97 C ANISOU 4727 CG LEU B 318 2011 3000 2196 375 -15 -551 C ATOM 4728 CD1 LEU B 318 43.451 16.714 14.872 1.00 16.68 C ANISOU 4728 CD1 LEU B 318 1721 2709 1909 364 -23 -562 C ATOM 4729 CD2 LEU B 318 45.039 16.541 16.811 1.00 16.00 C ANISOU 4729 CD2 LEU B 318 1645 2611 1823 377 -15 -541 C ATOM 4730 N GLY B 319 43.803 14.356 12.257 1.00 15.11 N ANISOU 4730 N GLY B 319 1511 2509 1721 376 6 -584 N ATOM 4731 CA GLY B 319 42.572 14.538 11.519 1.00 16.17 C ANISOU 4731 CA GLY B 319 1641 2646 1855 366 -1 -596 C ATOM 4732 C GLY B 319 42.162 13.313 10.731 1.00 18.18 C ANISOU 4732 C GLY B 319 1896 2893 2120 369 12 -608 C ATOM 4733 O GLY B 319 42.414 12.182 11.162 1.00 16.87 O ANISOU 4733 O GLY B 319 1734 2712 1962 376 27 -608 O ATOM 4734 N SER B 320 41.534 13.539 9.577 1.00 14.46 N ANISOU 4734 N SER B 320 1417 2431 1645 363 7 -618 N ATOM 4735 CA SER B 320 41.019 12.442 8.764 1.00 16.69 C ANISOU 4735 CA SER B 320 1699 2706 1936 364 18 -631 C ATOM 4736 C SER B 320 42.155 11.510 8.343 1.00 19.66 C ANISOU 4736 C SER B 320 2073 3081 2314 377 34 -629 C ATOM 4737 O SER B 320 43.248 11.981 8.001 1.00 18.14 O ANISOU 4737 O SER B 320 1876 2902 2113 383 33 -623 O ATOM 4738 CB SER B 320 40.321 13.000 7.524 1.00 23.00 C ANISOU 4738 CB SER B 320 2490 3519 2731 356 8 -640 C ATOM 4739 OG SER B 320 39.215 13.815 7.890 1.00 18.18 O ANISOU 4739 OG SER B 320 1880 2908 2119 345 -6 -641 O ATOM 4740 N PRO B 321 41.939 10.187 8.347 1.00 14.79 N ANISOU 4740 N PRO B 321 1461 2449 1708 382 49 -636 N ATOM 4741 CA PRO B 321 43.074 9.275 8.102 1.00 19.71 C ANISOU 4741 CA PRO B 321 2084 3071 2336 395 65 -633 C ATOM 4742 C PRO B 321 43.717 9.446 6.733 1.00 19.67 C ANISOU 4742 C PRO B 321 2068 3081 2323 399 66 -637 C ATOM 4743 O PRO B 321 44.952 9.443 6.641 1.00 22.09 O ANISOU 4743 O PRO B 321 2373 3395 2627 409 72 -629 O ATOM 4744 CB PRO B 321 42.451 7.879 8.274 1.00 23.88 C ANISOU 4744 CB PRO B 321 2617 3579 2876 398 79 -641 C ATOM 4745 CG PRO B 321 40.971 8.079 8.070 1.00 19.82 C ANISOU 4745 CG PRO B 321 2104 3062 2364 385 70 -651 C ATOM 4746 CD PRO B 321 40.685 9.460 8.603 1.00 18.13 C ANISOU 4746 CD PRO B 321 1890 2857 2142 376 53 -645 C ATOM 4747 N ASP B 322 42.923 9.614 5.670 1.00 22.80 N ANISOU 4747 N ASP B 322 2461 3485 2717 393 60 -648 N ATOM 4748 CA ASP B 322 43.503 9.856 4.347 1.00 23.97 C ANISOU 4748 CA ASP B 322 2600 3650 2858 396 61 -651 C ATOM 4749 C ASP B 322 44.346 11.122 4.322 1.00 16.50 C ANISOU 4749 C ASP B 322 1649 2721 1899 396 49 -641 C ATOM 4750 O ASP B 322 45.342 11.192 3.598 1.00 17.08 O ANISOU 4750 O ASP B 322 1717 2806 1967 403 54 -638 O ATOM 4751 CB ASP B 322 42.415 9.940 3.271 1.00 25.10 C ANISOU 4751 CB ASP B 322 2739 3797 3000 387 55 -665 C ATOM 4752 CG ASP B 322 41.854 8.580 2.889 1.00 35.87 C ANISOU 4752 CG ASP B 322 4106 5147 4374 390 69 -675 C ATOM 4753 OD1 ASP B 322 42.295 7.558 3.462 1.00 31.48 O ANISOU 4753 OD1 ASP B 322 3556 4578 3827 399 83 -673 O ATOM 4754 OD2 ASP B 322 40.979 8.540 1.997 1.00 37.79 O ANISOU 4754 OD2 ASP B 322 4347 5394 4618 384 65 -687 O ATOM 4755 N ASP B 323 43.933 12.156 5.062 1.00 20.29 N ANISOU 4755 N ASP B 323 2131 3204 2374 387 34 -636 N ATOM 4756 CA ASP B 323 44.687 13.407 5.048 1.00 16.92 C ANISOU 4756 CA ASP B 323 1700 2795 1934 386 22 -626 C ATOM 4757 C ASP B 323 45.998 13.274 5.804 1.00 19.95 C ANISOU 4757 C ASP B 323 2085 3177 2317 396 30 -613 C ATOM 4758 O ASP B 323 47.032 13.769 5.345 1.00 21.53 O ANISOU 4758 O ASP B 323 2279 3392 2510 401 30 -607 O ATOM 4759 CB ASP B 323 43.858 14.554 5.627 1.00 21.27 C ANISOU 4759 CB ASP B 323 2252 3349 2480 374 4 -624 C ATOM 4760 CG ASP B 323 42.696 14.948 4.734 1.00 25.76 C ANISOU 4760 CG ASP B 323 2816 3924 3048 364 -6 -635 C ATOM 4761 OD1 ASP B 323 42.915 15.176 3.521 1.00 20.17 O ANISOU 4761 OD1 ASP B 323 2101 3230 2334 365 -7 -640 O ATOM 4762 OD2 ASP B 323 41.567 15.048 5.255 1.00 26.18 O ANISOU 4762 OD2 ASP B 323 2873 3968 3106 356 -12 -639 O ATOM 4763 N VAL B 324 45.970 12.656 6.989 1.00 15.54 N ANISOU 4763 N VAL B 324 1534 2602 1768 399 37 -608 N ATOM 4764 CA VAL B 324 47.206 12.480 7.749 1.00 21.74 C ANISOU 4764 CA VAL B 324 2320 3384 2554 410 45 -596 C ATOM 4765 C VAL B 324 48.186 11.611 6.971 1.00 20.49 C ANISOU 4765 C VAL B 324 2157 3229 2401 422 61 -597 C ATOM 4766 O VAL B 324 49.386 11.908 6.901 1.00 17.83 O ANISOU 4766 O VAL B 324 1815 2901 2059 429 64 -587 O ATOM 4767 CB VAL B 324 46.916 11.883 9.139 1.00 19.43 C ANISOU 4767 CB VAL B 324 2038 3073 2273 411 50 -592 C ATOM 4768 CG1 VAL B 324 48.221 11.636 9.876 1.00 16.28 C ANISOU 4768 CG1 VAL B 324 1639 2671 1877 422 59 -579 C ATOM 4769 CG2 VAL B 324 45.987 12.802 9.960 1.00 22.02 C ANISOU 4769 CG2 VAL B 324 2371 3399 2597 399 34 -590 C ATOM 4770 N LEU B 325 47.683 10.522 6.378 1.00 23.48 N ANISOU 4770 N LEU B 325 2536 3597 2787 424 72 -608 N ATOM 4771 CA LEU B 325 48.522 9.621 5.597 1.00 20.61 C ANISOU 4771 CA LEU B 325 2167 3234 2428 435 88 -609 C ATOM 4772 C LEU B 325 49.167 10.350 4.434 1.00 15.28 C ANISOU 4772 C LEU B 325 1484 2581 1743 436 84 -609 C ATOM 4773 O LEU B 325 50.327 10.091 4.100 1.00 25.98 O ANISOU 4773 O LEU B 325 2833 3941 3098 446 94 -603 O ATOM 4774 CB LEU B 325 47.685 8.440 5.094 1.00 28.56 C ANISOU 4774 CB LEU B 325 3177 4228 3445 435 99 -623 C ATOM 4775 CG LEU B 325 47.251 7.411 6.143 1.00 21.43 C ANISOU 4775 CG LEU B 325 2283 3304 2555 437 108 -623 C ATOM 4776 CD1 LEU B 325 46.232 6.441 5.576 1.00 24.87 C ANISOU 4776 CD1 LEU B 325 2722 3730 2999 435 115 -637 C ATOM 4777 CD2 LEU B 325 48.476 6.665 6.655 1.00 21.29 C ANISOU 4777 CD2 LEU B 325 2265 3280 2545 451 123 -614 C ATOM 4778 N GLU B 326 48.433 11.264 3.796 1.00 18.45 N ANISOU 4778 N GLU B 326 1882 2994 2134 425 69 -615 N ATOM 4779 CA GLU B 326 49.043 12.042 2.726 1.00 15.09 C ANISOU 4779 CA GLU B 326 1449 2589 1698 426 64 -614 C ATOM 4780 C GLU B 326 50.197 12.887 3.258 1.00 25.47 C ANISOU 4780 C GLU B 326 2759 3913 3004 430 60 -599 C ATOM 4781 O GLU B 326 51.276 12.920 2.655 1.00 24.12 O ANISOU 4781 O GLU B 326 2582 3753 2830 438 66 -594 O ATOM 4782 CB GLU B 326 48.006 12.924 2.042 1.00 17.33 C ANISOU 4782 CB GLU B 326 1730 2882 1972 414 48 -623 C ATOM 4783 CG GLU B 326 48.552 13.686 0.836 1.00 20.96 C ANISOU 4783 CG GLU B 326 2180 3362 2420 414 43 -623 C ATOM 4784 CD GLU B 326 47.518 14.599 0.193 1.00 26.35 C ANISOU 4784 CD GLU B 326 2861 4055 3095 401 26 -631 C ATOM 4785 OE1 GLU B 326 46.307 14.417 0.437 1.00 30.33 O ANISOU 4785 OE1 GLU B 326 3370 4550 3606 393 21 -639 O ATOM 4786 OE2 GLU B 326 47.923 15.491 -0.575 1.00 32.77 O ANISOU 4786 OE2 GLU B 326 3667 4886 3897 400 18 -629 O ATOM 4787 N PHE B 327 50.004 13.553 4.406 1.00 23.61 N ANISOU 4787 N PHE B 327 2530 3675 2767 425 49 -591 N ATOM 4788 CA PHE B 327 51.110 14.289 5.014 1.00 25.04 C ANISOU 4788 CA PHE B 327 2709 3865 2942 429 46 -577 C ATOM 4789 C PHE B 327 52.286 13.369 5.322 1.00 17.57 C ANISOU 4789 C PHE B 327 1760 2911 2004 442 63 -569 C ATOM 4790 O PHE B 327 53.448 13.737 5.103 1.00 17.95 O ANISOU 4790 O PHE B 327 1801 2971 2048 449 66 -559 O ATOM 4791 CB PHE B 327 50.671 15.004 6.297 1.00 20.18 C ANISOU 4791 CB PHE B 327 2100 3244 2323 421 33 -570 C ATOM 4792 CG PHE B 327 51.829 15.596 7.059 1.00 20.56 C ANISOU 4792 CG PHE B 327 2147 3298 2367 427 32 -554 C ATOM 4793 CD1 PHE B 327 52.412 14.913 8.116 1.00 25.14 C ANISOU 4793 CD1 PHE B 327 2731 3865 2957 435 42 -546 C ATOM 4794 CD2 PHE B 327 52.374 16.803 6.675 1.00 21.09 C ANISOU 4794 CD2 PHE B 327 2209 3385 2419 424 20 -547 C ATOM 4795 CE1 PHE B 327 53.504 15.442 8.787 1.00 21.89 C ANISOU 4795 CE1 PHE B 327 2317 3459 2542 440 41 -531 C ATOM 4796 CE2 PHE B 327 53.463 17.333 7.342 1.00 18.95 C ANISOU 4796 CE2 PHE B 327 1936 3119 2144 429 19 -533 C ATOM 4797 CZ PHE B 327 54.025 16.649 8.399 1.00 20.13 C ANISOU 4797 CZ PHE B 327 2089 3255 2304 437 30 -524 C ATOM 4798 N LEU B 328 52.009 12.185 5.869 1.00 20.75 N ANISOU 4798 N LEU B 328 2169 3296 2421 447 76 -572 N ATOM 4799 CA LEU B 328 53.091 11.264 6.217 1.00 24.32 C ANISOU 4799 CA LEU B 328 2617 3739 2883 460 93 -565 C ATOM 4800 C LEU B 328 53.806 10.766 4.979 1.00 25.16 C ANISOU 4800 C LEU B 328 2715 3854 2990 469 105 -568 C ATOM 4801 O LEU B 328 55.012 10.497 5.023 1.00 30.73 O ANISOU 4801 O LEU B 328 3415 4562 3700 479 115 -559 O ATOM 4802 CB LEU B 328 52.552 10.064 6.998 1.00 20.39 C ANISOU 4802 CB LEU B 328 2128 3219 2400 463 103 -569 C ATOM 4803 CG LEU B 328 52.111 10.296 8.439 1.00 26.84 C ANISOU 4803 CG LEU B 328 2953 4024 3219 458 96 -563 C ATOM 4804 CD1 LEU B 328 51.457 9.028 8.976 1.00 20.61 C ANISOU 4804 CD1 LEU B 328 2172 3213 2444 461 108 -569 C ATOM 4805 CD2 LEU B 328 53.285 10.745 9.312 1.00 24.57 C ANISOU 4805 CD2 LEU B 328 2664 3739 2931 465 96 -546 C ATOM 4806 N LYS B 329 53.071 10.614 3.878 1.00 29.64 N ANISOU 4806 N LYS B 329 3282 4425 3555 464 104 -581 N ATOM 4807 CA LYS B 329 53.694 10.247 2.618 1.00 23.98 C ANISOU 4807 CA LYS B 329 2557 3718 2838 471 114 -585 C ATOM 4808 C LYS B 329 54.689 11.314 2.190 1.00 29.49 C ANISOU 4808 C LYS B 329 3246 4436 3524 472 108 -575 C ATOM 4809 O LYS B 329 55.826 11.004 1.815 1.00 24.05 O ANISOU 4809 O LYS B 329 2550 3752 2838 483 120 -569 O ATOM 4810 CB LYS B 329 52.615 10.018 1.562 1.00 25.93 C ANISOU 4810 CB LYS B 329 2804 3965 3082 465 112 -601 C ATOM 4811 CG LYS B 329 53.140 9.853 0.160 1.00 28.86 C ANISOU 4811 CG LYS B 329 3167 4348 3450 470 120 -605 C ATOM 4812 CD LYS B 329 52.068 9.279 -0.749 1.00 29.81 C ANISOU 4812 CD LYS B 329 3289 4463 3572 466 121 -622 C ATOM 4813 CE LYS B 329 52.622 9.043 -2.144 1.00 39.14 C ANISOU 4813 CE LYS B 329 4464 5656 4751 472 131 -626 C ATOM 4814 NZ LYS B 329 51.665 9.542 -3.173 1.00 44.83 N ANISOU 4814 NZ LYS B 329 5184 6386 5464 462 120 -638 N ATOM 4815 N VAL B 330 54.291 12.587 2.282 1.00 24.85 N ANISOU 4815 N VAL B 330 2659 3859 2923 462 90 -573 N ATOM 4816 CA VAL B 330 55.220 13.670 1.974 1.00 21.53 C ANISOU 4816 CA VAL B 330 2232 3458 2491 462 83 -563 C ATOM 4817 C VAL B 330 56.366 13.676 2.972 1.00 23.42 C ANISOU 4817 C VAL B 330 2468 3695 2734 471 88 -548 C ATOM 4818 O VAL B 330 57.530 13.867 2.604 1.00 26.43 O ANISOU 4818 O VAL B 330 2842 4088 3114 478 94 -539 O ATOM 4819 CB VAL B 330 54.491 15.031 1.961 1.00 20.53 C ANISOU 4819 CB VAL B 330 2107 3343 2350 449 62 -565 C ATOM 4820 CG1 VAL B 330 55.490 16.153 1.797 1.00 16.82 C ANISOU 4820 CG1 VAL B 330 1631 2893 1868 450 55 -553 C ATOM 4821 CG2 VAL B 330 53.441 15.091 0.845 1.00 18.40 C ANISOU 4821 CG2 VAL B 330 1838 3079 2077 441 56 -580 C ATOM 4822 N TYR B 331 56.056 13.450 4.249 1.00 25.17 N ANISOU 4822 N TYR B 331 2698 3902 2963 470 87 -544 N ATOM 4823 CA TYR B 331 57.077 13.499 5.286 1.00 27.35 C ANISOU 4823 CA TYR B 331 2973 4176 3244 477 91 -528 C ATOM 4824 C TYR B 331 58.151 12.446 5.051 1.00 27.25 C ANISOU 4824 C TYR B 331 2953 4158 3244 491 110 -524 C ATOM 4825 O TYR B 331 59.347 12.751 5.110 1.00 24.01 O ANISOU 4825 O TYR B 331 2533 3756 2832 498 114 -512 O ATOM 4826 CB TYR B 331 56.438 13.314 6.661 1.00 31.21 C ANISOU 4826 CB TYR B 331 3472 4648 3739 473 87 -526 C ATOM 4827 CG TYR B 331 57.406 13.493 7.814 1.00 37.58 C ANISOU 4827 CG TYR B 331 4278 5452 4550 479 88 -510 C ATOM 4828 CD1 TYR B 331 57.713 14.757 8.302 1.00 35.46 C ANISOU 4828 CD1 TYR B 331 4010 5195 4270 474 74 -500 C ATOM 4829 CD2 TYR B 331 58.006 12.397 8.416 1.00 40.53 C ANISOU 4829 CD2 TYR B 331 4650 5810 4938 490 104 -505 C ATOM 4830 CE1 TYR B 331 58.603 14.922 9.362 1.00 37.94 C ANISOU 4830 CE1 TYR B 331 4322 5506 4587 479 76 -485 C ATOM 4831 CE2 TYR B 331 58.887 12.553 9.475 1.00 42.08 C ANISOU 4831 CE2 TYR B 331 4845 6003 5140 496 105 -490 C ATOM 4832 CZ TYR B 331 59.181 13.812 9.944 1.00 41.93 C ANISOU 4832 CZ TYR B 331 4826 5996 5109 490 91 -480 C ATOM 4833 OH TYR B 331 60.061 13.950 10.998 1.00 46.90 O ANISOU 4833 OH TYR B 331 5454 6623 5744 496 92 -465 O ATOM 4834 N GLU B 332 57.737 11.203 4.765 1.00 22.29 N ANISOU 4834 N GLU B 332 2326 3516 2627 495 123 -534 N ATOM 4835 CA GLU B 332 58.688 10.134 4.468 1.00 29.18 C ANISOU 4835 CA GLU B 332 3191 4383 3511 509 143 -531 C ATOM 4836 C GLU B 332 59.531 10.461 3.244 1.00 36.76 C ANISOU 4836 C GLU B 332 4140 5361 4466 513 147 -530 C ATOM 4837 O GLU B 332 60.680 10.018 3.148 1.00 41.09 O ANISOU 4837 O GLU B 332 4679 5910 5022 524 160 -522 O ATOM 4838 CB GLU B 332 57.959 8.800 4.267 1.00 30.51 C ANISOU 4838 CB GLU B 332 3366 4535 3692 512 155 -544 C ATOM 4839 CG GLU B 332 57.293 8.227 5.512 1.00 36.88 C ANISOU 4839 CG GLU B 332 4183 5322 4509 510 155 -544 C ATOM 4840 CD GLU B 332 56.262 7.163 5.173 1.00 54.54 C ANISOU 4840 CD GLU B 332 6426 7544 6752 509 162 -559 C ATOM 4841 OE1 GLU B 332 56.283 6.660 4.027 1.00 60.58 O ANISOU 4841 OE1 GLU B 332 7187 8313 7517 512 171 -568 O ATOM 4842 OE2 GLU B 332 55.432 6.826 6.046 1.00 58.02 O ANISOU 4842 OE2 GLU B 332 6876 7970 7197 504 160 -562 O ATOM 4843 N LYS B 333 58.964 11.189 2.278 1.00 34.66 N ANISOU 4843 N LYS B 333 3875 5109 4187 505 137 -538 N ATOM 4844 CA LYS B 333 59.726 11.571 1.094 1.00 40.95 C ANISOU 4844 CA LYS B 333 4660 5923 4976 508 140 -537 C ATOM 4845 C LYS B 333 60.932 12.421 1.463 1.00 47.58 C ANISOU 4845 C LYS B 333 5492 6775 5811 512 137 -520 C ATOM 4846 O LYS B 333 61.992 12.300 0.841 1.00 50.12 O ANISOU 4846 O LYS B 333 5803 7105 6134 520 147 -514 O ATOM 4847 CB LYS B 333 58.828 12.330 0.120 1.00 44.88 C ANISOU 4847 CB LYS B 333 5161 6433 5460 497 127 -548 C ATOM 4848 CG LYS B 333 59.565 13.191 -0.897 1.00 53.33 C ANISOU 4848 CG LYS B 333 6221 7524 6518 498 124 -544 C ATOM 4849 CD LYS B 333 58.581 13.901 -1.820 1.00 57.12 C ANISOU 4849 CD LYS B 333 6704 8015 6985 487 111 -556 C ATOM 4850 CE LYS B 333 59.274 14.922 -2.707 1.00 58.47 C ANISOU 4850 CE LYS B 333 6866 8208 7143 486 105 -551 C ATOM 4851 NZ LYS B 333 58.301 15.573 -3.626 1.00 63.36 N ANISOU 4851 NZ LYS B 333 7487 8837 7749 475 93 -562 N ATOM 4852 N HIS B 334 60.798 13.264 2.484 1.00 50.07 N ANISOU 4852 N HIS B 334 5812 7091 6121 505 123 -512 N ATOM 4853 CA HIS B 334 61.899 14.067 2.988 1.00 50.80 C ANISOU 4853 CA HIS B 334 5898 7194 6209 508 120 -495 C ATOM 4854 C HIS B 334 62.668 13.373 4.099 1.00 65.76 C ANISOU 4854 C HIS B 334 7790 9075 8119 517 130 -484 C ATOM 4855 O HIS B 334 63.330 14.059 4.886 1.00 68.77 O ANISOU 4855 O HIS B 334 8169 9461 8499 518 124 -470 O ATOM 4856 CB HIS B 334 61.386 15.415 3.482 1.00 40.64 C ANISOU 4856 CB HIS B 334 4617 5916 4907 496 99 -492 C ATOM 4857 CG HIS B 334 60.795 16.257 2.404 1.00 45.17 C ANISOU 4857 CG HIS B 334 5192 6506 5465 487 88 -501 C ATOM 4858 ND1 HIS B 334 61.428 17.368 1.892 1.00 44.13 N ANISOU 4858 ND1 HIS B 334 5053 6394 5320 484 80 -493 N ATOM 4859 CD2 HIS B 334 59.644 16.121 1.706 1.00 45.88 C ANISOU 4859 CD2 HIS B 334 5286 6594 5551 480 83 -516 C ATOM 4860 CE1 HIS B 334 60.674 17.902 0.948 1.00 45.90 C ANISOU 4860 CE1 HIS B 334 5278 6628 5532 476 71 -504 C ATOM 4861 NE2 HIS B 334 59.586 17.164 0.815 1.00 46.80 N ANISOU 4861 NE2 HIS B 334 5399 6729 5652 473 72 -518 N ATOM 4862 N SER B 335 62.549 12.045 4.199 1.00 76.30 N ANISOU 4862 N SER B 335 9127 10393 9469 525 145 -490 N ATOM 4863 CA SER B 335 63.223 11.211 5.191 1.00 85.12 C ANISOU 4863 CA SER B 335 10242 11496 10604 535 156 -480 C ATOM 4864 C SER B 335 62.552 11.315 6.566 1.00 88.44 C ANISOU 4864 C SER B 335 10674 11903 11026 529 147 -478 C ATOM 4865 O SER B 335 62.195 10.294 7.159 1.00 90.42 O ANISOU 4865 O SER B 335 10930 12136 11290 533 155 -482 O ATOM 4866 CB SER B 335 64.737 11.570 5.249 1.00 89.07 C ANISOU 4866 CB SER B 335 10729 12008 11108 543 160 -463 C ATOM 4867 OG SER B 335 65.261 11.970 3.987 1.00 92.63 O ANISOU 4867 OG SER B 335 11169 12475 11550 545 163 -464 O TER 4868 SER B 335 ATOM 4869 N ASP C 9 0.914 42.156 18.987 1.00 37.96 N ANISOU 4869 N ASP C 9 5249 4593 4582 324 89 287 N ATOM 4870 CA ASP C 9 2.364 42.285 18.895 1.00 36.24 C ANISOU 4870 CA ASP C 9 5048 4362 4358 316 107 284 C ATOM 4871 C ASP C 9 3.037 42.139 20.247 1.00 29.76 C ANISOU 4871 C ASP C 9 4224 3541 3543 313 113 276 C ATOM 4872 O ASP C 9 2.538 42.637 21.253 1.00 31.34 O ANISOU 4872 O ASP C 9 4419 3737 3750 318 114 275 O ATOM 4873 CB ASP C 9 2.743 43.628 18.289 1.00 45.65 C ANISOU 4873 CB ASP C 9 6267 5531 5546 317 129 290 C ATOM 4874 CG ASP C 9 3.087 43.522 16.827 1.00 52.90 C ANISOU 4874 CG ASP C 9 7197 6448 6456 313 131 295 C ATOM 4875 OD1 ASP C 9 2.991 42.406 16.269 1.00 55.46 O ANISOU 4875 OD1 ASP C 9 7507 6789 6777 311 116 294 O ATOM 4876 OD2 ASP C 9 3.447 44.558 16.237 1.00 51.02 O ANISOU 4876 OD2 ASP C 9 6981 6191 6213 313 149 299 O ATOM 4877 N VAL C 10 4.183 41.458 20.252 1.00 23.68 N ANISOU 4877 N VAL C 10 3456 2773 2770 304 118 270 N ATOM 4878 CA VAL C 10 4.939 41.289 21.480 1.00 23.80 C ANISOU 4878 CA VAL C 10 3469 2785 2788 300 125 262 C ATOM 4879 C VAL C 10 5.331 42.657 22.025 1.00 26.35 C ANISOU 4879 C VAL C 10 3813 3084 3115 300 149 262 C ATOM 4880 O VAL C 10 5.627 43.596 21.277 1.00 23.49 O ANISOU 4880 O VAL C 10 3472 2705 2750 298 166 267 O ATOM 4881 CB VAL C 10 6.170 40.400 21.229 1.00 18.49 C ANISOU 4881 CB VAL C 10 2799 2117 2110 289 128 257 C ATOM 4882 CG1 VAL C 10 7.188 41.119 20.334 1.00 18.95 C ANISOU 4882 CG1 VAL C 10 2884 2155 2161 281 151 259 C ATOM 4883 CG2 VAL C 10 6.794 39.951 22.541 1.00 21.98 C ANISOU 4883 CG2 VAL C 10 3233 2561 2556 286 130 248 C ATOM 4884 N ASN C 11 5.319 42.780 23.342 1.00 23.03 N ANISOU 4884 N ASN C 11 3386 2662 2703 302 151 257 N ATOM 4885 CA ASN C 11 5.664 44.032 23.987 1.00 16.89 C ANISOU 4885 CA ASN C 11 2624 1861 1930 302 173 256 C ATOM 4886 C ASN C 11 6.499 43.725 25.216 1.00 19.63 C ANISOU 4886 C ASN C 11 2968 2205 2283 296 180 246 C ATOM 4887 O ASN C 11 6.224 42.760 25.931 1.00 25.65 O ANISOU 4887 O ASN C 11 3711 2987 3049 299 163 242 O ATOM 4888 CB ASN C 11 4.423 44.832 24.366 1.00 21.11 C ANISOU 4888 CB ASN C 11 3154 2394 2471 313 168 260 C ATOM 4889 CG ASN C 11 4.682 46.322 24.349 1.00 31.77 C ANISOU 4889 CG ASN C 11 4528 3720 3824 312 192 262 C ATOM 4890 OD1 ASN C 11 5.808 46.750 24.121 1.00 31.23 O ANISOU 4890 OD1 ASN C 11 4478 3634 3754 302 213 259 O ATOM 4891 ND2 ASN C 11 3.638 47.119 24.554 1.00 38.55 N ANISOU 4891 ND2 ASN C 11 5385 4576 4687 322 189 267 N ATOM 4892 N THR C 12 7.558 44.500 25.411 1.00 15.84 N ANISOU 4892 N THR C 12 2510 1704 1806 286 207 242 N ATOM 4893 CA THR C 12 8.406 44.375 26.582 1.00 16.54 C ANISOU 4893 CA THR C 12 2594 1788 1903 277 216 229 C ATOM 4894 C THR C 12 8.219 45.589 27.468 1.00 16.31 C ANISOU 4894 C THR C 12 2569 1741 1885 279 231 225 C ATOM 4895 O THR C 12 7.756 46.633 27.015 1.00 18.79 O ANISOU 4895 O THR C 12 2901 2040 2199 286 241 235 O ATOM 4896 CB THR C 12 9.879 44.252 26.188 1.00 18.60 C ANISOU 4896 CB THR C 12 2857 2047 2164 255 232 213 C ATOM 4897 OG1 THR C 12 10.325 45.494 25.625 1.00 19.36 O ANISOU 4897 OG1 THR C 12 2979 2118 2260 249 258 215 O ATOM 4898 CG2 THR C 12 10.062 43.142 25.167 1.00 21.31 C ANISOU 4898 CG2 THR C 12 3198 2404 2495 253 219 218 C ATOM 4899 N LEU C 13 8.627 45.462 28.732 1.00 14.94 N ANISOU 4899 N LEU C 13 2376 1576 1724 270 232 206 N ATOM 4900 CA LEU C 13 8.557 46.610 29.630 1.00 17.23 C ANISOU 4900 CA LEU C 13 2671 1851 2027 270 247 200 C ATOM 4901 C LEU C 13 9.283 47.810 29.036 1.00 15.35 C ANISOU 4901 C LEU C 13 2457 1587 1789 260 275 199 C ATOM 4902 O LEU C 13 8.764 48.931 29.047 1.00 16.18 O ANISOU 4902 O LEU C 13 2578 1673 1896 269 286 208 O ATOM 4903 CB LEU C 13 9.152 46.246 30.985 1.00 21.85 C ANISOU 4903 CB LEU C 13 3230 2447 2623 257 246 177 C ATOM 4904 CG LEU C 13 8.910 47.135 32.203 1.00 24.77 C ANISOU 4904 CG LEU C 13 3596 2809 3007 259 255 170 C ATOM 4905 CD1 LEU C 13 7.607 47.866 32.141 1.00 15.72 C ANISOU 4905 CD1 LEU C 13 2462 1652 1860 280 251 189 C ATOM 4906 CD2 LEU C 13 8.860 46.190 33.378 1.00 37.33 C ANISOU 4906 CD2 LEU C 13 5158 4422 4605 257 238 156 C ATOM 4907 N THR C 14 10.483 47.580 28.492 1.00 17.56 N ANISOU 4907 N THR C 14 2740 1866 2066 242 287 188 N ATOM 4908 CA THR C 14 11.274 48.656 27.902 1.00 25.09 C ANISOU 4908 CA THR C 14 3716 2796 3020 231 314 186 C ATOM 4909 C THR C 14 10.510 49.364 26.792 1.00 27.49 C ANISOU 4909 C THR C 14 4048 3083 3314 245 318 210 C ATOM 4910 O THR C 14 10.413 50.595 26.777 1.00 26.69 O ANISOU 4910 O THR C 14 3965 2960 3216 247 336 214 O ATOM 4911 CB THR C 14 12.582 48.096 27.346 1.00 34.21 C ANISOU 4911 CB THR C 14 4870 3956 4172 210 322 172 C ATOM 4912 OG1 THR C 14 13.223 47.285 28.332 1.00 30.54 O ANISOU 4912 OG1 THR C 14 4378 3509 3715 198 315 151 O ATOM 4913 CG2 THR C 14 13.506 49.229 26.931 1.00 42.90 C ANISOU 4913 CG2 THR C 14 5992 5033 5276 196 352 166 C ATOM 4914 N ARG C 15 9.970 48.597 25.843 1.00 27.28 N ANISOU 4914 N ARG C 15 4024 3067 3274 256 301 225 N ATOM 4915 CA ARG C 15 9.213 49.195 24.749 1.00 25.79 C ANISOU 4915 CA ARG C 15 3847 2875 3077 266 299 239 C ATOM 4916 C ARG C 15 7.952 49.868 25.259 1.00 23.13 C ANISOU 4916 C ARG C 15 3503 2540 2745 281 289 245 C ATOM 4917 O ARG C 15 7.574 50.943 24.780 1.00 20.38 O ANISOU 4917 O ARG C 15 3168 2180 2397 284 298 251 O ATOM 4918 CB ARG C 15 8.856 48.124 23.719 1.00 38.63 C ANISOU 4918 CB ARG C 15 5464 4522 4691 270 277 247 C ATOM 4919 CG ARG C 15 7.948 48.596 22.587 1.00 40.41 C ANISOU 4919 CG ARG C 15 5695 4749 4909 280 269 258 C ATOM 4920 CD ARG C 15 7.568 47.437 21.674 1.00 43.63 C ANISOU 4920 CD ARG C 15 6091 5179 5308 283 247 263 C ATOM 4921 NE ARG C 15 8.630 47.110 20.732 1.00 51.73 N ANISOU 4921 NE ARG C 15 7129 6201 6326 271 257 261 N ATOM 4922 CZ ARG C 15 8.687 45.984 20.023 1.00 50.45 C ANISOU 4922 CZ ARG C 15 6957 6056 6155 270 242 263 C ATOM 4923 NH1 ARG C 15 7.743 45.058 20.160 1.00 40.26 N ANISOU 4923 NH1 ARG C 15 5645 4788 4866 279 215 266 N ATOM 4924 NH2 ARG C 15 9.695 45.783 19.182 1.00 47.96 N ANISOU 4924 NH2 ARG C 15 6655 5736 5834 258 253 261 N ATOM 4925 N PHE C 16 7.281 49.246 26.233 1.00 17.25 N ANISOU 4925 N PHE C 16 2738 1811 2007 289 271 244 N ATOM 4926 CA PHE C 16 6.014 49.780 26.728 1.00 21.70 C ANISOU 4926 CA PHE C 16 3293 2379 2575 303 260 249 C ATOM 4927 C PHE C 16 6.178 51.170 27.332 1.00 18.88 C ANISOU 4927 C PHE C 16 2948 1998 2226 301 282 245 C ATOM 4928 O PHE C 16 5.402 52.083 27.021 1.00 21.02 O ANISOU 4928 O PHE C 16 3226 2264 2497 309 283 252 O ATOM 4929 CB PHE C 16 5.406 48.822 27.752 1.00 18.51 C ANISOU 4929 CB PHE C 16 2864 1994 2175 310 239 245 C ATOM 4930 CG PHE C 16 4.130 49.322 28.383 1.00 16.08 C ANISOU 4930 CG PHE C 16 2545 1691 1873 322 228 249 C ATOM 4931 CD1 PHE C 16 2.905 49.039 27.808 1.00 24.70 C ANISOU 4931 CD1 PHE C 16 3625 2799 2959 332 206 258 C ATOM 4932 CD2 PHE C 16 4.156 50.039 29.565 1.00 22.41 C ANISOU 4932 CD2 PHE C 16 3347 2482 2686 323 238 243 C ATOM 4933 CE1 PHE C 16 1.732 49.472 28.384 1.00 23.80 C ANISOU 4933 CE1 PHE C 16 3502 2690 2852 342 197 260 C ATOM 4934 CE2 PHE C 16 2.978 50.497 30.147 1.00 21.53 C ANISOU 4934 CE2 PHE C 16 3225 2375 2579 334 228 246 C ATOM 4935 CZ PHE C 16 1.767 50.203 29.556 1.00 25.23 C ANISOU 4935 CZ PHE C 16 3683 2860 3042 344 207 255 C ATOM 4936 N VAL C 17 7.147 51.349 28.235 1.00 14.29 N ANISOU 4936 N VAL C 17 2371 1404 1655 291 300 233 N ATOM 4937 CA VAL C 17 7.223 52.646 28.906 1.00 16.03 C ANISOU 4937 CA VAL C 17 2601 1605 1886 289 320 229 C ATOM 4938 C VAL C 17 7.686 53.720 27.928 1.00 22.03 C ANISOU 4938 C VAL C 17 3384 2346 2642 282 341 232 C ATOM 4939 O VAL C 17 7.179 54.846 27.934 1.00 24.63 O ANISOU 4939 O VAL C 17 3721 2664 2974 287 348 236 O ATOM 4940 CB VAL C 17 8.132 52.579 30.150 1.00 22.34 C ANISOU 4940 CB VAL C 17 3395 2394 2698 278 333 213 C ATOM 4941 CG1 VAL C 17 7.569 51.600 31.179 1.00 23.02 C ANISOU 4941 CG1 VAL C 17 3453 2506 2789 285 310 207 C ATOM 4942 CG2 VAL C 17 9.554 52.225 29.774 1.00 23.25 C ANISOU 4942 CG2 VAL C 17 3509 2511 2812 256 346 197 C ATOM 4943 N MET C 18 8.616 53.372 27.039 1.00 22.29 N ANISOU 4943 N MET C 18 3428 2376 2668 270 350 230 N ATOM 4944 CA MET C 18 9.064 54.311 26.017 1.00 23.20 C ANISOU 4944 CA MET C 18 3564 2474 2778 264 369 233 C ATOM 4945 C MET C 18 7.887 54.812 25.186 1.00 32.58 C ANISOU 4945 C MET C 18 4756 3667 3958 279 357 248 C ATOM 4946 O MET C 18 7.797 56.006 24.870 1.00 27.75 O ANISOU 4946 O MET C 18 4158 3038 3346 279 371 251 O ATOM 4947 CB MET C 18 10.108 53.631 25.139 1.00 32.04 C ANISOU 4947 CB MET C 18 4691 3594 3889 251 375 230 C ATOM 4948 CG MET C 18 10.880 54.553 24.265 1.00 46.91 C ANISOU 4948 CG MET C 18 6596 5458 5769 239 399 229 C ATOM 4949 SD MET C 18 12.232 55.318 25.153 1.00 42.11 S ANISOU 4949 SD MET C 18 5997 4827 5175 219 431 211 S ATOM 4950 CE MET C 18 13.113 56.048 23.784 1.00 36.32 C ANISOU 4950 CE MET C 18 5288 4079 4434 206 454 211 C ATOM 4951 N GLU C 19 6.966 53.914 24.833 1.00 26.33 N ANISOU 4951 N GLU C 19 3949 2895 3158 290 330 256 N ATOM 4952 CA GLU C 19 5.824 54.313 24.023 1.00 30.46 C ANISOU 4952 CA GLU C 19 4474 3423 3675 303 318 268 C ATOM 4953 C GLU C 19 4.806 55.108 24.837 1.00 25.70 C ANISOU 4953 C GLU C 19 3866 2819 3081 314 314 271 C ATOM 4954 O GLU C 19 4.188 56.040 24.312 1.00 23.71 O ANISOU 4954 O GLU C 19 3624 2559 2826 321 317 278 O ATOM 4955 CB GLU C 19 5.186 53.077 23.388 1.00 35.09 C ANISOU 4955 CB GLU C 19 5045 4034 4253 310 291 274 C ATOM 4956 CG GLU C 19 6.093 52.424 22.340 1.00 47.96 C ANISOU 4956 CG GLU C 19 6683 5666 5874 300 295 274 C ATOM 4957 CD GLU C 19 5.596 51.062 21.872 1.00 56.05 C ANISOU 4957 CD GLU C 19 7690 6715 6892 305 269 277 C ATOM 4958 OE1 GLU C 19 4.741 50.465 22.564 1.00 60.21 O ANISOU 4958 OE1 GLU C 19 8197 7259 7423 313 249 278 O ATOM 4959 OE2 GLU C 19 6.070 50.587 20.815 1.00 52.58 O ANISOU 4959 OE2 GLU C 19 7255 6278 6443 299 268 280 O ATOM 4960 N GLU C 20 4.596 54.756 26.114 1.00 25.00 N ANISOU 4960 N GLU C 20 3761 2737 3001 317 307 264 N ATOM 4961 CA GLU C 20 3.731 55.583 26.957 1.00 31.60 C ANISOU 4961 CA GLU C 20 4592 3569 3845 326 306 265 C ATOM 4962 C GLU C 20 4.314 56.982 27.122 1.00 30.83 C ANISOU 4962 C GLU C 20 4515 3446 3754 319 333 262 C ATOM 4963 O GLU C 20 3.580 57.978 27.120 1.00 32.98 O ANISOU 4963 O GLU C 20 4793 3711 4028 327 335 267 O ATOM 4964 CB GLU C 20 3.524 54.934 28.331 1.00 30.72 C ANISOU 4964 CB GLU C 20 4461 3469 3743 328 295 258 C ATOM 4965 CG GLU C 20 2.589 53.750 28.325 1.00 32.48 C ANISOU 4965 CG GLU C 20 4662 3718 3962 337 266 262 C ATOM 4966 CD GLU C 20 1.182 54.131 27.890 1.00 40.33 C ANISOU 4966 CD GLU C 20 5652 4720 4953 350 251 272 C ATOM 4967 OE1 GLU C 20 0.677 55.174 28.360 1.00 34.82 O ANISOU 4967 OE1 GLU C 20 4958 4010 4260 355 258 273 O ATOM 4968 OE2 GLU C 20 0.591 53.401 27.062 1.00 41.85 O ANISOU 4968 OE2 GLU C 20 5836 4927 5137 354 232 278 O ATOM 4969 N GLY C 21 5.638 57.078 27.222 1.00 20.75 N ANISOU 4969 N GLY C 21 3248 2156 2480 304 354 252 N ATOM 4970 CA GLY C 21 6.266 58.376 27.367 1.00 24.49 C ANISOU 4970 CA GLY C 21 3739 2607 2961 296 381 247 C ATOM 4971 C GLY C 21 6.164 59.232 26.117 1.00 31.54 C ANISOU 4971 C GLY C 21 4651 3488 3844 297 390 256 C ATOM 4972 O GLY C 21 5.990 60.452 26.208 1.00 23.89 O ANISOU 4972 O GLY C 21 3693 2504 2880 299 403 257 O ATOM 4973 N ARG C 22 6.315 58.616 24.936 1.00 26.83 N ANISOU 4973 N ARG C 22 4060 2899 3236 296 383 262 N ATOM 4974 CA ARG C 22 6.153 59.358 23.690 1.00 26.87 C ANISOU 4974 CA ARG C 22 4082 2895 3232 298 389 271 C ATOM 4975 C ARG C 22 4.724 59.857 23.549 1.00 33.30 C ANISOU 4975 C ARG C 22 4893 3715 4045 315 374 282 C ATOM 4976 O ARG C 22 4.496 60.984 23.099 1.00 48.12 O ANISOU 4976 O ARG C 22 6785 5577 5921 318 385 287 O ATOM 4977 CB ARG C 22 6.532 58.483 22.493 1.00 29.22 C ANISOU 4977 CB ARG C 22 4383 3202 3518 295 383 275 C ATOM 4978 CG ARG C 22 8.017 58.142 22.401 1.00 44.02 C ANISOU 4978 CG ARG C 22 6264 5068 5392 276 401 264 C ATOM 4979 CD ARG C 22 8.373 57.437 21.089 1.00 57.28 C ANISOU 4979 CD ARG C 22 7949 6755 7059 273 396 269 C ATOM 4980 NE ARG C 22 8.416 58.330 19.932 1.00 67.86 N ANISOU 4980 NE ARG C 22 9310 8083 8393 273 407 276 N ATOM 4981 CZ ARG C 22 8.604 57.919 18.679 1.00 77.31 C ANISOU 4981 CZ ARG C 22 10513 9284 9578 271 403 281 C ATOM 4982 NH1 ARG C 22 8.763 56.626 18.419 1.00 85.49 N ANISOU 4982 NH1 ARG C 22 11537 10336 10608 269 388 281 N ATOM 4983 NH2 ARG C 22 8.633 58.794 17.681 1.00 74.37 N ANISOU 4983 NH2 ARG C 22 10159 8898 9199 271 414 287 N ATOM 4984 N LYS C 23 3.749 59.043 23.958 1.00 31.72 N ANISOU 4984 N LYS C 23 4673 3535 3846 326 349 285 N ATOM 4985 CA LYS C 23 2.368 59.510 23.995 1.00 34.23 C ANISOU 4985 CA LYS C 23 4986 3858 4164 341 335 294 C ATOM 4986 C LYS C 23 2.232 60.754 24.861 1.00 40.70 C ANISOU 4986 C LYS C 23 5811 4661 4993 342 349 291 C ATOM 4987 O LYS C 23 1.544 61.711 24.486 1.00 47.90 O ANISOU 4987 O LYS C 23 6732 5565 5904 350 351 298 O ATOM 4988 CB LYS C 23 1.445 58.410 24.520 1.00 37.47 C ANISOU 4988 CB LYS C 23 5371 4291 4575 350 308 295 C ATOM 4989 CG LYS C 23 1.138 57.292 23.535 1.00 45.56 C ANISOU 4989 CG LYS C 23 6386 5334 5589 352 288 300 C ATOM 4990 CD LYS C 23 0.145 56.296 24.138 1.00 51.44 C ANISOU 4990 CD LYS C 23 7106 6102 6337 360 262 301 C ATOM 4991 CE LYS C 23 -0.009 55.061 23.264 1.00 60.97 C ANISOU 4991 CE LYS C 23 8302 7327 7535 360 243 304 C ATOM 4992 NZ LYS C 23 1.204 54.190 23.304 1.00 63.94 N ANISOU 4992 NZ LYS C 23 8678 7706 7909 349 249 297 N ATOM 4993 N ALA C 24 2.881 60.762 26.022 1.00 36.53 N ANISOU 4993 N ALA C 24 5278 4128 4475 335 360 280 N ATOM 4994 CA ALA C 24 2.760 61.870 26.960 1.00 33.96 C ANISOU 4994 CA ALA C 24 4955 3787 4160 336 373 276 C ATOM 4995 C ALA C 24 3.706 63.027 26.661 1.00 32.11 C ANISOU 4995 C ALA C 24 4743 3530 3929 325 402 272 C ATOM 4996 O ALA C 24 3.673 64.020 27.391 1.00 39.29 O ANISOU 4996 O ALA C 24 5656 4426 4847 324 415 268 O ATOM 4997 CB ALA C 24 2.985 61.372 28.392 1.00 22.09 C ANISOU 4997 CB ALA C 24 3434 2289 2668 333 372 265 C ATOM 4998 N ARG C 25 4.520 62.935 25.608 1.00 30.00 N ANISOU 4998 N ARG C 25 4489 3256 3652 316 413 273 N ATOM 4999 CA ARG C 25 5.498 63.970 25.235 1.00 43.87 C ANISOU 4999 CA ARG C 25 6267 4991 5411 304 440 269 C ATOM 5000 C ARG C 25 6.556 64.184 26.318 1.00 42.47 C ANISOU 5000 C ARG C 25 6088 4803 5246 290 460 253 C ATOM 5001 O ARG C 25 7.068 65.295 26.483 1.00 39.34 O ANISOU 5001 O ARG C 25 5704 4388 4855 282 483 248 O ATOM 5002 CB ARG C 25 4.813 65.312 24.936 1.00 50.93 C ANISOU 5002 CB ARG C 25 7174 5872 6305 312 447 276 C ATOM 5003 CG ARG C 25 3.753 65.341 23.837 1.00 61.79 C ANISOU 5003 CG ARG C 25 8554 7255 7669 326 430 291 C ATOM 5004 CD ARG C 25 4.319 65.182 22.438 1.00 70.47 C ANISOU 5004 CD ARG C 25 9667 8351 8756 321 435 296 C ATOM 5005 NE ARG C 25 3.303 65.465 21.425 1.00 74.79 N ANISOU 5005 NE ARG C 25 10220 8901 9294 334 422 309 N ATOM 5006 CZ ARG C 25 2.460 64.568 20.921 1.00 80.54 C ANISOU 5006 CZ ARG C 25 10937 9649 10016 344 398 317 C ATOM 5007 NH1 ARG C 25 2.500 63.307 21.329 1.00 82.72 N ANISOU 5007 NH1 ARG C 25 11195 9943 10293 343 383 313 N ATOM 5008 NH2 ARG C 25 1.573 64.934 20.004 1.00 83.48 N ANISOU 5008 NH2 ARG C 25 11316 10023 10381 355 388 328 N ATOM 5009 N GLY C 26 6.943 63.118 27.026 1.00 38.94 N ANISOU 5009 N GLY C 26 5625 4367 4803 284 453 245 N ATOM 5010 CA GLY C 26 7.886 63.259 28.118 1.00 26.24 C ANISOU 5010 CA GLY C 26 4013 2749 3207 271 470 228 C ATOM 5011 C GLY C 26 9.334 63.364 27.673 1.00 26.38 C ANISOU 5011 C GLY C 26 4043 2754 3225 251 494 218 C ATOM 5012 O GLY C 26 9.701 63.047 26.542 1.00 24.13 O ANISOU 5012 O GLY C 26 3769 2470 2929 247 495 223 O ATOM 5013 N THR C 27 10.174 63.810 28.611 1.00 26.75 N ANISOU 5013 N THR C 27 4088 2790 3285 238 513 202 N ATOM 5014 CA THR C 27 11.597 63.994 28.365 1.00 29.58 C ANISOU 5014 CA THR C 27 4457 3136 3646 217 537 189 C ATOM 5015 C THR C 27 12.396 62.704 28.470 1.00 21.58 C ANISOU 5015 C THR C 27 3434 2133 2633 206 533 180 C ATOM 5016 O THR C 27 13.605 62.732 28.220 1.00 26.65 O ANISOU 5016 O THR C 27 4083 2767 3277 188 551 168 O ATOM 5017 CB THR C 27 12.200 64.986 29.361 1.00 34.65 C ANISOU 5017 CB THR C 27 5099 3764 4304 206 559 174 C ATOM 5018 OG1 THR C 27 12.191 64.398 30.672 1.00 46.15 O ANISOU 5018 OG1 THR C 27 6535 5228 5772 205 551 162 O ATOM 5019 CG2 THR C 27 11.412 66.281 29.381 1.00 33.62 C ANISOU 5019 CG2 THR C 27 4977 3623 4174 216 563 182 C ATOM 5020 N GLY C 28 11.776 61.601 28.882 1.00 22.83 N ANISOU 5020 N GLY C 28 3576 2309 2790 216 509 183 N ATOM 5021 CA GLY C 28 12.469 60.340 29.027 1.00 24.98 C ANISOU 5021 CA GLY C 28 3838 2591 3063 207 503 175 C ATOM 5022 C GLY C 28 13.008 60.044 30.414 1.00 25.07 C ANISOU 5022 C GLY C 28 3834 2603 3090 198 508 156 C ATOM 5023 O GLY C 28 13.529 58.948 30.632 1.00 14.99 O ANISOU 5023 O GLY C 28 2543 1340 1813 191 499 146 O ATOM 5024 N GLU C 29 12.885 60.973 31.363 1.00 19.03 N ANISOU 5024 N GLU C 29 3065 1829 2337 198 518 148 N ATOM 5025 CA GLU C 29 13.502 60.778 32.675 1.00 18.28 C ANISOU 5025 CA GLU C 29 2953 1734 2257 188 524 126 C ATOM 5026 C GLU C 29 12.837 59.648 33.467 1.00 17.38 C ANISOU 5026 C GLU C 29 2812 1647 2144 197 495 124 C ATOM 5027 O GLU C 29 13.528 58.829 34.090 1.00 14.56 O ANISOU 5027 O GLU C 29 2433 1308 1791 185 489 106 O ATOM 5028 CB GLU C 29 13.459 62.094 33.450 1.00 21.39 C ANISOU 5028 CB GLU C 29 3349 2116 2664 186 539 118 C ATOM 5029 CG GLU C 29 14.186 62.084 34.781 1.00 30.49 C ANISOU 5029 CG GLU C 29 4484 3268 3832 173 548 94 C ATOM 5030 CD GLU C 29 14.384 63.495 35.333 1.00 29.13 C ANISOU 5030 CD GLU C 29 4317 3082 3671 167 568 86 C ATOM 5031 OE1 GLU C 29 14.817 63.637 36.490 1.00 23.63 O ANISOU 5031 OE1 GLU C 29 3604 2387 2987 158 573 66 O ATOM 5032 OE2 GLU C 29 14.094 64.462 34.603 1.00 39.36 O ANISOU 5032 OE2 GLU C 29 5630 4366 4960 171 577 98 O ATOM 5033 N LEU C 30 11.498 59.580 33.462 1.00 15.90 N ANISOU 5033 N LEU C 30 2626 1463 1952 219 477 143 N ATOM 5034 CA LEU C 30 10.823 58.504 34.195 1.00 16.44 C ANISOU 5034 CA LEU C 30 2668 1557 2020 229 451 142 C ATOM 5035 C LEU C 30 11.104 57.145 33.558 1.00 17.06 C ANISOU 5035 C LEU C 30 2737 1656 2088 225 434 143 C ATOM 5036 O LEU C 30 11.235 56.138 34.260 1.00 18.69 O ANISOU 5036 O LEU C 30 2918 1884 2297 221 418 132 O ATOM 5037 CB LEU C 30 9.313 58.762 34.281 1.00 14.20 C ANISOU 5037 CB LEU C 30 2389 1273 1735 253 436 162 C ATOM 5038 CG LEU C 30 8.504 57.640 34.935 1.00 16.19 C ANISOU 5038 CG LEU C 30 2617 1550 1986 264 407 164 C ATOM 5039 CD1 LEU C 30 8.995 57.354 36.362 1.00 18.83 C ANISOU 5039 CD1 LEU C 30 2925 1897 2333 253 406 141 C ATOM 5040 CD2 LEU C 30 7.001 57.895 34.909 1.00 18.10 C ANISOU 5040 CD2 LEU C 30 2857 1799 2223 285 390 182 C ATOM 5041 N THR C 31 11.188 57.099 32.226 1.00 13.92 N ANISOU 5041 N THR C 31 2359 1252 1679 226 437 157 N ATOM 5042 CA THR C 31 11.598 55.877 31.547 1.00 16.17 C ANISOU 5042 CA THR C 31 2636 1555 1953 220 424 157 C ATOM 5043 C THR C 31 13.012 55.472 31.953 1.00 12.34 C ANISOU 5043 C THR C 31 2137 1076 1474 197 434 131 C ATOM 5044 O THR C 31 13.295 54.281 32.140 1.00 16.02 O ANISOU 5044 O THR C 31 2584 1565 1938 191 418 123 O ATOM 5045 CB THR C 31 11.502 56.074 30.029 1.00 20.72 C ANISOU 5045 CB THR C 31 3238 2119 2515 225 429 175 C ATOM 5046 OG1 THR C 31 10.128 56.013 29.624 1.00 17.56 O ANISOU 5046 OG1 THR C 31 2842 1724 2106 247 411 197 O ATOM 5047 CG2 THR C 31 12.318 55.011 29.276 1.00 19.11 C ANISOU 5047 CG2 THR C 31 3030 1929 2302 213 424 170 C ATOM 5048 N GLN C 32 13.922 56.448 32.083 1.00 14.11 N ANISOU 5048 N GLN C 32 2372 1282 1707 182 461 119 N ATOM 5049 CA GLN C 32 15.263 56.121 32.560 1.00 20.44 C ANISOU 5049 CA GLN C 32 3160 2091 2516 159 471 93 C ATOM 5050 C GLN C 32 15.195 55.515 33.957 1.00 18.49 C ANISOU 5050 C GLN C 32 2884 1863 2279 158 457 77 C ATOM 5051 O GLN C 32 15.828 54.487 34.235 1.00 15.11 O ANISOU 5051 O GLN C 32 2436 1453 1851 148 447 63 O ATOM 5052 CB GLN C 32 16.145 57.368 32.550 1.00 24.77 C ANISOU 5052 CB GLN C 32 3725 2615 3073 145 502 83 C ATOM 5053 CG GLN C 32 16.492 57.861 31.160 1.00 43.81 C ANISOU 5053 CG GLN C 32 6164 5008 5474 141 518 94 C ATOM 5054 CD GLN C 32 17.671 58.812 31.145 1.00 56.65 C ANISOU 5054 CD GLN C 32 7801 6614 7107 121 548 78 C ATOM 5055 OE1 GLN C 32 17.496 60.025 31.249 1.00 57.24 O ANISOU 5055 OE1 GLN C 32 7893 6668 7189 124 566 82 O ATOM 5056 NE2 GLN C 32 18.878 58.269 31.011 1.00 66.02 N ANISOU 5056 NE2 GLN C 32 8981 7809 8296 101 555 60 N ATOM 5057 N LEU C 33 14.384 56.106 34.832 1.00 10.29 N ANISOU 5057 N LEU C 33 1841 819 1248 170 454 80 N ATOM 5058 CA LEU C 33 14.190 55.533 36.161 1.00 10.59 C ANISOU 5058 CA LEU C 33 1853 877 1295 171 439 67 C ATOM 5059 C LEU C 33 13.692 54.086 36.079 1.00 10.37 C ANISOU 5059 C LEU C 33 1807 875 1258 179 411 73 C ATOM 5060 O LEU C 33 14.257 53.180 36.707 1.00 17.51 O ANISOU 5060 O LEU C 33 2689 1798 2167 169 401 57 O ATOM 5061 CB LEU C 33 13.216 56.406 36.951 1.00 11.17 C ANISOU 5061 CB LEU C 33 1927 940 1376 185 440 74 C ATOM 5062 CG LEU C 33 13.124 56.195 38.466 1.00 14.76 C ANISOU 5062 CG LEU C 33 2358 1408 1844 184 432 58 C ATOM 5063 CD1 LEU C 33 12.437 57.407 39.085 1.00 12.58 C ANISOU 5063 CD1 LEU C 33 2089 1115 1576 194 442 62 C ATOM 5064 CD2 LEU C 33 12.368 54.923 38.831 1.00 9.61 C ANISOU 5064 CD2 LEU C 33 1684 782 1186 195 402 63 C ATOM 5065 N LEU C 34 12.621 53.858 35.321 1.00 9.26 N ANISOU 5065 N LEU C 34 1675 735 1107 197 396 97 N ATOM 5066 CA LEU C 34 12.005 52.536 35.278 1.00 11.16 C ANISOU 5066 CA LEU C 34 1900 1001 1340 206 368 104 C ATOM 5067 C LEU C 34 12.919 51.512 34.615 1.00 10.62 C ANISOU 5067 C LEU C 34 1825 945 1264 193 364 96 C ATOM 5068 O LEU C 34 12.919 50.342 35.005 1.00 16.39 O ANISOU 5068 O LEU C 34 2534 1698 1993 192 345 90 O ATOM 5069 CB LEU C 34 10.655 52.615 34.566 1.00 15.23 C ANISOU 5069 CB LEU C 34 2428 1513 1845 229 355 130 C ATOM 5070 CG LEU C 34 9.557 53.349 35.354 1.00 14.19 C ANISOU 5070 CG LEU C 34 2296 1375 1721 245 352 138 C ATOM 5071 CD1 LEU C 34 8.308 53.561 34.488 1.00 19.13 C ANISOU 5071 CD1 LEU C 34 2939 1994 2337 267 343 165 C ATOM 5072 CD2 LEU C 34 9.190 52.613 36.658 1.00 7.63 C ANISOU 5072 CD2 LEU C 34 1437 565 897 248 334 128 C ATOM 5073 N ASN C 35 13.681 51.922 33.593 1.00 16.34 N ANISOU 5073 N ASN C 35 2570 1656 1984 183 382 97 N ATOM 5074 CA ASN C 35 14.680 51.022 33.018 1.00 18.87 C ANISOU 5074 CA ASN C 35 2884 1987 2298 168 380 88 C ATOM 5075 C ASN C 35 15.686 50.594 34.072 1.00 17.56 C ANISOU 5075 C ASN C 35 2695 1833 2143 150 383 61 C ATOM 5076 O ASN C 35 16.006 49.412 34.194 1.00 12.23 O ANISOU 5076 O ASN C 35 2003 1180 1466 145 367 53 O ATOM 5077 CB ASN C 35 15.424 51.690 31.853 1.00 13.49 C ANISOU 5077 CB ASN C 35 2227 1286 1611 158 403 91 C ATOM 5078 CG ASN C 35 14.578 51.842 30.618 1.00 24.83 C ANISOU 5078 CG ASN C 35 3685 2715 3034 173 398 117 C ATOM 5079 OD1 ASN C 35 13.559 51.163 30.460 1.00 21.64 O ANISOU 5079 OD1 ASN C 35 3275 2323 2623 190 375 132 O ATOM 5080 ND2 ASN C 35 15.005 52.730 29.716 1.00 29.92 N ANISOU 5080 ND2 ASN C 35 4355 3337 3675 168 420 122 N ATOM 5081 N SER C 36 16.224 51.560 34.823 1.00 13.44 N ANISOU 5081 N SER C 36 2175 1297 1634 141 403 46 N ATOM 5082 CA SER C 36 17.192 51.250 35.869 1.00 18.61 C ANISOU 5082 CA SER C 36 2809 1962 2300 125 406 20 C ATOM 5083 C SER C 36 16.589 50.334 36.918 1.00 15.41 C ANISOU 5083 C SER C 36 2378 1580 1898 133 382 16 C ATOM 5084 O SER C 36 17.261 49.427 37.423 1.00 16.52 O ANISOU 5084 O SER C 36 2498 1738 2040 122 373 -1 O ATOM 5085 CB SER C 36 17.666 52.540 36.536 1.00 19.23 C ANISOU 5085 CB SER C 36 2894 2021 2391 116 431 7 C ATOM 5086 OG SER C 36 18.296 53.383 35.588 1.00 26.90 O ANISOU 5086 OG SER C 36 3889 2971 3359 107 454 9 O ATOM 5087 N LEU C 37 15.330 50.575 37.279 1.00 7.51 N ANISOU 5087 N LEU C 37 1377 578 896 152 371 31 N ATOM 5088 CA LEU C 37 14.688 49.738 38.277 1.00 12.94 C ANISOU 5088 CA LEU C 37 2042 1288 1588 160 348 29 C ATOM 5089 C LEU C 37 14.555 48.307 37.776 1.00 15.39 C ANISOU 5089 C LEU C 37 2340 1620 1887 163 325 34 C ATOM 5090 O LEU C 37 14.808 47.357 38.522 1.00 16.71 O ANISOU 5090 O LEU C 37 2485 1807 2058 158 310 21 O ATOM 5091 CB LEU C 37 13.322 50.315 38.632 1.00 17.39 C ANISOU 5091 CB LEU C 37 2610 1845 2152 180 341 45 C ATOM 5092 CG LEU C 37 12.609 49.725 39.842 1.00 26.45 C ANISOU 5092 CG LEU C 37 3734 3011 3305 189 321 42 C ATOM 5093 CD1 LEU C 37 13.528 49.723 41.060 1.00 18.05 C ANISOU 5093 CD1 LEU C 37 2652 1952 2253 174 328 16 C ATOM 5094 CD2 LEU C 37 11.381 50.578 40.117 1.00 23.74 C ANISOU 5094 CD2 LEU C 37 3399 2656 2964 208 320 57 C ATOM 5095 N CYS C 38 14.201 48.138 36.496 1.00 18.20 N ANISOU 5095 N CYS C 38 2711 1972 2230 170 321 52 N ATOM 5096 CA CYS C 38 14.035 46.800 35.934 1.00 12.60 C ANISOU 5096 CA CYS C 38 1993 1283 1511 173 299 59 C ATOM 5097 C CYS C 38 15.347 46.051 35.883 1.00 9.44 C ANISOU 5097 C CYS C 38 1582 894 1112 154 302 39 C ATOM 5098 O CYS C 38 15.368 44.825 36.038 1.00 10.25 O ANISOU 5098 O CYS C 38 1665 1017 1210 153 282 35 O ATOM 5099 CB CYS C 38 13.406 46.880 34.547 1.00 25.54 C ANISOU 5099 CB CYS C 38 3652 2914 3136 185 297 82 C ATOM 5100 SG CYS C 38 11.657 47.212 34.705 1.00 42.17 S ANISOU 5100 SG CYS C 38 5764 5019 5241 212 282 106 S ATOM 5101 N THR C 39 16.440 46.756 35.600 1.00 13.20 N ANISOU 5101 N THR C 39 2068 1354 1591 137 326 27 N ATOM 5102 CA THR C 39 17.749 46.122 35.659 1.00 16.11 C ANISOU 5102 CA THR C 39 2426 1733 1962 118 330 6 C ATOM 5103 C THR C 39 18.041 45.635 37.071 1.00 18.09 C ANISOU 5103 C THR C 39 2651 1999 2224 112 321 -14 C ATOM 5104 O THR C 39 18.506 44.506 37.265 1.00 17.32 O ANISOU 5104 O THR C 39 2535 1920 2125 105 307 -25 O ATOM 5105 CB THR C 39 18.831 47.087 35.173 1.00 14.26 C ANISOU 5105 CB THR C 39 2209 1477 1731 101 359 -4 C ATOM 5106 OG1 THR C 39 18.619 47.384 33.788 1.00 18.06 O ANISOU 5106 OG1 THR C 39 2714 1947 2202 106 365 14 O ATOM 5107 CG2 THR C 39 20.201 46.461 35.336 1.00 16.70 C ANISOU 5107 CG2 THR C 39 2505 1797 2044 80 363 -28 C ATOM 5108 N ALA C 40 17.750 46.463 38.076 1.00 12.25 N ANISOU 5108 N ALA C 40 1908 1250 1494 115 329 -19 N ATOM 5109 CA ALA C 40 17.947 46.025 39.454 1.00 12.99 C ANISOU 5109 CA ALA C 40 1978 1359 1598 111 320 -37 C ATOM 5110 C ALA C 40 17.085 44.799 39.779 1.00 13.47 C ANISOU 5110 C ALA C 40 2021 1443 1653 123 291 -29 C ATOM 5111 O ALA C 40 17.570 43.837 40.384 1.00 12.61 O ANISOU 5111 O ALA C 40 1891 1353 1547 116 279 -44 O ATOM 5112 CB ALA C 40 17.628 47.173 40.410 1.00 10.92 C ANISOU 5112 CB ALA C 40 1719 1084 1348 114 333 -41 C ATOM 5113 N VAL C 41 15.822 44.793 39.340 1.00 10.49 N ANISOU 5113 N VAL C 41 1651 1065 1268 142 279 -6 N ATOM 5114 CA VAL C 41 14.911 43.687 39.657 1.00 7.23 C ANISOU 5114 CA VAL C 41 1222 675 852 156 251 3 C ATOM 5115 C VAL C 41 15.382 42.379 39.019 1.00 17.59 C ANISOU 5115 C VAL C 41 2524 2003 2154 150 236 1 C ATOM 5116 O VAL C 41 15.282 41.306 39.632 1.00 13.15 O ANISOU 5116 O VAL C 41 1941 1462 1592 150 217 -5 O ATOM 5117 CB VAL C 41 13.471 44.039 39.237 1.00 13.50 C ANISOU 5117 CB VAL C 41 2028 1462 1639 177 242 29 C ATOM 5118 CG1 VAL C 41 12.584 42.775 39.147 1.00 14.87 C ANISOU 5118 CG1 VAL C 41 2189 1658 1805 190 214 41 C ATOM 5119 CG2 VAL C 41 12.890 45.079 40.179 1.00 9.52 C ANISOU 5119 CG2 VAL C 41 1525 946 1145 184 251 29 C ATOM 5120 N LYS C 42 15.886 42.433 37.779 1.00 10.87 N ANISOU 5120 N LYS C 42 1690 1145 1296 144 245 6 N ATOM 5121 CA LYS C 42 16.438 41.218 37.181 1.00 6.00 C ANISOU 5121 CA LYS C 42 1063 544 671 136 233 3 C ATOM 5122 C LYS C 42 17.642 40.700 37.965 1.00 12.85 C ANISOU 5122 C LYS C 42 1913 1423 1547 118 235 -24 C ATOM 5123 O LYS C 42 17.790 39.485 38.162 1.00 13.82 O ANISOU 5123 O LYS C 42 2018 1566 1668 116 217 -30 O ATOM 5124 CB LYS C 42 16.823 41.455 35.719 1.00 6.51 C ANISOU 5124 CB LYS C 42 1150 597 726 132 244 12 C ATOM 5125 CG LYS C 42 15.620 41.699 34.809 1.00 9.56 C ANISOU 5125 CG LYS C 42 1553 977 1103 151 238 39 C ATOM 5126 CD LYS C 42 16.021 41.797 33.337 1.00 10.50 C ANISOU 5126 CD LYS C 42 1693 1087 1212 147 247 49 C ATOM 5127 CE LYS C 42 16.819 43.073 33.087 1.00 15.27 C ANISOU 5127 CE LYS C 42 2315 1667 1820 135 277 41 C ATOM 5128 NZ LYS C 42 17.267 43.197 31.673 1.00 17.42 N ANISOU 5128 NZ LYS C 42 2607 1929 2082 130 287 49 N ATOM 5129 N ALA C 43 18.492 41.603 38.458 1.00 10.13 N ANISOU 5129 N ALA C 43 1572 1065 1213 105 257 -41 N ATOM 5130 CA ALA C 43 19.639 41.171 39.254 1.00 9.04 C ANISOU 5130 CA ALA C 43 1416 937 1083 88 260 -67 C ATOM 5131 C ALA C 43 19.194 40.605 40.597 1.00 7.96 C ANISOU 5131 C ALA C 43 1256 816 952 94 242 -74 C ATOM 5132 O ALA C 43 19.778 39.628 41.091 1.00 9.08 O ANISOU 5132 O ALA C 43 1378 975 1095 85 231 -89 O ATOM 5133 CB ALA C 43 20.610 42.332 39.451 1.00 6.07 C ANISOU 5133 CB ALA C 43 1049 541 715 73 288 -83 C ATOM 5134 N ILE C 44 18.176 41.217 41.205 1.00 9.15 N ANISOU 5134 N ILE C 44 1408 961 1106 107 241 -64 N ATOM 5135 CA ILE C 44 17.599 40.684 42.437 1.00 8.67 C ANISOU 5135 CA ILE C 44 1327 916 1050 115 223 -68 C ATOM 5136 C ILE C 44 17.003 39.301 42.189 1.00 13.59 C ANISOU 5136 C ILE C 44 1938 1561 1664 124 196 -58 C ATOM 5137 O ILE C 44 17.222 38.366 42.971 1.00 10.06 O ANISOU 5137 O ILE C 44 1470 1133 1220 120 181 -70 O ATOM 5138 CB ILE C 44 16.548 41.654 43.009 1.00 7.65 C ANISOU 5138 CB ILE C 44 1205 776 926 129 227 -57 C ATOM 5139 CG1 ILE C 44 17.217 42.915 43.554 1.00 17.16 C ANISOU 5139 CG1 ILE C 44 2416 1961 2141 118 252 -72 C ATOM 5140 CG2 ILE C 44 15.751 40.990 44.135 1.00 7.51 C ANISOU 5140 CG2 ILE C 44 1167 776 912 139 206 -58 C ATOM 5141 CD1 ILE C 44 16.224 43.989 43.945 1.00 13.90 C ANISOU 5141 CD1 ILE C 44 2013 1535 1733 132 259 -60 C ATOM 5142 N SER C 45 16.218 39.159 41.112 1.00 8.48 N ANISOU 5142 N SER C 45 1304 912 1007 136 189 -36 N ATOM 5143 CA SER C 45 15.637 37.857 40.783 1.00 18.20 C ANISOU 5143 CA SER C 45 2524 2163 2229 145 163 -26 C ATOM 5144 C SER C 45 16.724 36.794 40.644 1.00 16.01 C ANISOU 5144 C SER C 45 2234 1900 1950 130 157 -42 C ATOM 5145 O SER C 45 16.609 35.695 41.194 1.00 11.90 O ANISOU 5145 O SER C 45 1693 1400 1429 131 138 -46 O ATOM 5146 CB SER C 45 14.815 37.947 39.489 1.00 12.50 C ANISOU 5146 CB SER C 45 1820 1434 1495 158 160 -1 C ATOM 5147 OG SER C 45 14.180 36.713 39.208 1.00 9.69 O ANISOU 5147 OG SER C 45 1454 1098 1132 167 135 9 O ATOM 5148 N SER C 46 17.794 37.122 39.919 1.00 13.62 N ANISOU 5148 N SER C 46 1941 1587 1646 115 175 -50 N ATOM 5149 CA SER C 46 18.910 36.197 39.718 1.00 13.60 C ANISOU 5149 CA SER C 46 1928 1597 1643 100 171 -66 C ATOM 5150 C SER C 46 19.504 35.734 41.046 1.00 14.89 C ANISOU 5150 C SER C 46 2069 1773 1815 91 166 -89 C ATOM 5151 O SER C 46 19.776 34.539 41.233 1.00 10.74 O ANISOU 5151 O SER C 46 1526 1267 1288 88 149 -96 O ATOM 5152 CB SER C 46 19.978 36.879 38.854 1.00 16.57 C ANISOU 5152 CB SER C 46 2320 1957 2018 85 195 -73 C ATOM 5153 OG SER C 46 21.119 36.067 38.661 1.00 19.08 O ANISOU 5153 OG SER C 46 2628 2285 2335 70 193 -90 O ATOM 5154 N ALA C 47 19.716 36.670 41.975 1.00 9.24 N ANISOU 5154 N ALA C 47 1353 1047 1110 87 180 -100 N ATOM 5155 CA ALA C 47 20.285 36.349 43.281 1.00 12.41 C ANISOU 5155 CA ALA C 47 1733 1459 1521 79 177 -122 C ATOM 5156 C ALA C 47 19.295 35.592 44.163 1.00 6.28 C ANISOU 5156 C ALA C 47 941 701 745 92 153 -116 C ATOM 5157 O ALA C 47 19.687 34.698 44.929 1.00 15.72 O ANISOU 5157 O ALA C 47 2116 1913 1943 87 141 -130 O ATOM 5158 CB ALA C 47 20.748 37.637 43.969 1.00 10.30 C ANISOU 5158 CB ALA C 47 1473 1176 1266 71 200 -135 C ATOM 5159 N VAL C 48 18.013 35.927 44.071 1.00 8.16 N ANISOU 5159 N VAL C 48 1186 934 979 109 147 -95 N ATOM 5160 CA VAL C 48 17.016 35.254 44.898 1.00 11.68 C ANISOU 5160 CA VAL C 48 1617 1396 1426 122 125 -89 C ATOM 5161 C VAL C 48 16.869 33.794 44.481 1.00 15.90 C ANISOU 5161 C VAL C 48 2139 1951 1951 125 102 -84 C ATOM 5162 O VAL C 48 16.678 32.914 45.332 1.00 10.04 O ANISOU 5162 O VAL C 48 1378 1227 1211 127 85 -89 O ATOM 5163 CB VAL C 48 15.676 36.009 44.842 1.00 12.27 C ANISOU 5163 CB VAL C 48 1702 1460 1498 140 125 -68 C ATOM 5164 CG1 VAL C 48 14.567 35.146 45.400 1.00 8.81 C ANISOU 5164 CG1 VAL C 48 1250 1039 1057 155 101 -57 C ATOM 5165 CG2 VAL C 48 15.773 37.303 45.642 1.00 13.55 C ANISOU 5165 CG2 VAL C 48 1870 1607 1671 138 145 -76 C ATOM 5166 N ARG C 49 16.950 33.510 43.172 1.00 8.55 N ANISOU 5166 N ARG C 49 1220 1019 1011 125 101 -73 N ATOM 5167 CA ARG C 49 16.921 32.133 42.677 1.00 9.46 C ANISOU 5167 CA ARG C 49 1325 1153 1118 126 81 -69 C ATOM 5168 C ARG C 49 18.257 31.416 42.860 1.00 10.84 C ANISOU 5168 C ARG C 49 1486 1337 1295 109 81 -91 C ATOM 5169 O ARG C 49 18.415 30.292 42.369 1.00 13.77 O ANISOU 5169 O ARG C 49 1850 1722 1660 107 66 -90 O ATOM 5170 CB ARG C 49 16.512 32.082 41.197 1.00 9.58 C ANISOU 5170 CB ARG C 49 1357 1162 1122 133 80 -49 C ATOM 5171 CG ARG C 49 14.978 32.146 40.910 1.00 10.15 C ANISOU 5171 CG ARG C 49 1435 1233 1188 154 67 -24 C ATOM 5172 CD ARG C 49 14.388 33.554 41.179 1.00 6.99 C ANISOU 5172 CD ARG C 49 1049 814 792 162 83 -16 C ATOM 5173 NE ARG C 49 13.106 33.762 40.492 1.00 11.99 N ANISOU 5173 NE ARG C 49 1695 1443 1419 180 76 9 N ATOM 5174 CZ ARG C 49 11.927 33.414 40.998 1.00 12.99 C ANISOU 5174 CZ ARG C 49 1813 1578 1544 196 59 20 C ATOM 5175 NH1 ARG C 49 11.858 32.831 42.189 1.00 16.68 N ANISOU 5175 NH1 ARG C 49 2259 2060 2017 195 47 9 N ATOM 5176 NH2 ARG C 49 10.819 33.648 40.320 1.00 11.47 N ANISOU 5176 NH2 ARG C 49 1633 1381 1345 212 54 42 N ATOM 5177 N LYS C 50 19.231 32.063 43.496 1.00 8.76 N ANISOU 5177 N LYS C 50 1222 1066 1041 95 98 -112 N ATOM 5178 CA LYS C 50 20.463 31.423 43.952 1.00 13.00 C ANISOU 5178 CA LYS C 50 1744 1614 1583 79 97 -135 C ATOM 5179 C LYS C 50 21.427 31.088 42.814 1.00 12.40 C ANISOU 5179 C LYS C 50 1675 1536 1502 67 103 -140 C ATOM 5180 O LYS C 50 22.228 30.154 42.930 1.00 13.58 O ANISOU 5180 O LYS C 50 1810 1699 1651 57 95 -155 O ATOM 5181 CB LYS C 50 20.135 30.165 44.767 1.00 14.21 C ANISOU 5181 CB LYS C 50 1875 1790 1736 83 72 -139 C ATOM 5182 CG LYS C 50 19.315 30.476 46.024 1.00 13.35 C ANISOU 5182 CG LYS C 50 1757 1682 1633 93 67 -138 C ATOM 5183 CD LYS C 50 20.125 31.311 46.996 1.00 11.09 C ANISOU 5183 CD LYS C 50 1468 1387 1358 82 85 -159 C ATOM 5184 CE LYS C 50 19.315 31.717 48.210 1.00 19.33 C ANISOU 5184 CE LYS C 50 2505 2432 2409 92 81 -157 C ATOM 5185 NZ LYS C 50 20.188 32.346 49.252 1.00 24.12 N ANISOU 5185 NZ LYS C 50 3105 3033 3026 80 96 -180 N ATOM 5186 N ALA C 51 21.384 31.833 41.706 1.00 16.09 N ANISOU 5186 N ALA C 51 2163 1987 1964 67 118 -128 N ATOM 5187 CA ALA C 51 22.425 31.682 40.690 1.00 19.24 C ANISOU 5187 CA ALA C 51 2569 2382 2359 54 128 -136 C ATOM 5188 C ALA C 51 23.794 31.947 41.309 1.00 15.10 C ANISOU 5188 C ALA C 51 2038 1856 1845 35 143 -163 C ATOM 5189 O ALA C 51 24.001 32.964 41.968 1.00 17.46 O ANISOU 5189 O ALA C 51 2340 2141 2152 31 159 -172 O ATOM 5190 CB ALA C 51 22.177 32.630 39.517 1.00 19.82 C ANISOU 5190 CB ALA C 51 2667 2435 2426 57 145 -120 C ATOM 5191 N GLY C 52 24.722 31.015 41.134 1.00 17.22 N ANISOU 5191 N GLY C 52 2295 2136 2112 23 136 -178 N ATOM 5192 CA GLY C 52 26.052 31.192 41.684 1.00 11.24 C ANISOU 5192 CA GLY C 52 1529 1377 1363 5 149 -205 C ATOM 5193 C GLY C 52 26.227 30.754 43.124 1.00 9.96 C ANISOU 5193 C GLY C 52 1346 1229 1210 3 139 -221 C ATOM 5194 O GLY C 52 27.312 30.958 43.680 1.00 17.45 O ANISOU 5194 O GLY C 52 2288 2177 2167 -11 150 -245 O ATOM 5195 N ILE C 53 25.192 30.190 43.756 1.00 15.40 N ANISOU 5195 N ILE C 53 2024 1930 1896 17 119 -211 N ATOM 5196 CA ILE C 53 25.303 29.772 45.152 1.00 15.24 C ANISOU 5196 CA ILE C 53 1984 1923 1884 16 108 -226 C ATOM 5197 C ILE C 53 26.400 28.723 45.328 1.00 18.99 C ANISOU 5197 C ILE C 53 2442 2413 2360 3 100 -246 C ATOM 5198 O ILE C 53 26.992 28.607 46.410 1.00 14.46 O ANISOU 5198 O ILE C 53 1854 1846 1795 -4 99 -266 O ATOM 5199 CB ILE C 53 23.943 29.264 45.675 1.00 13.08 C ANISOU 5199 CB ILE C 53 1702 1660 1607 34 87 -208 C ATOM 5200 CG1 ILE C 53 23.976 29.182 47.207 1.00 15.17 C ANISOU 5200 CG1 ILE C 53 1951 1934 1881 34 82 -223 C ATOM 5201 CG2 ILE C 53 23.559 27.886 45.049 1.00 7.47 C ANISOU 5201 CG2 ILE C 53 984 967 886 41 63 -197 C ATOM 5202 CD1 ILE C 53 24.160 30.565 47.852 1.00 17.17 C ANISOU 5202 CD1 ILE C 53 2211 2169 2144 30 104 -231 C ATOM 5203 N ALA C 54 26.707 27.966 44.273 1.00 12.07 N ANISOU 5203 N ALA C 54 1568 1542 1476 0 93 -242 N ATOM 5204 CA ALA C 54 27.775 26.975 44.364 1.00 17.10 C ANISOU 5204 CA ALA C 54 2190 2193 2113 -13 85 -262 C ATOM 5205 C ALA C 54 29.105 27.618 44.733 1.00 22.11 C ANISOU 5205 C ALA C 54 2823 2819 2757 -30 106 -288 C ATOM 5206 O ALA C 54 29.934 26.991 45.400 1.00 17.37 O ANISOU 5206 O ALA C 54 2206 2230 2164 -38 95 -295 O ATOM 5207 CB ALA C 54 27.903 26.210 43.042 1.00 13.75 C ANISOU 5207 CB ALA C 54 1770 1774 1679 -14 78 -253 C ATOM 5208 N HIS C 55 29.324 28.869 44.325 1.00 19.19 N ANISOU 5208 N HIS C 55 2471 2429 2391 -35 130 -287 N ATOM 5209 CA HIS C 55 30.569 29.528 44.692 1.00 20.45 C ANISOU 5209 CA HIS C 55 2629 2581 2561 -50 145 -300 C ATOM 5210 C HIS C 55 30.628 29.794 46.187 1.00 17.43 C ANISOU 5210 C HIS C 55 2232 2201 2189 -49 140 -304 C ATOM 5211 O HIS C 55 31.702 29.701 46.787 1.00 24.15 O ANISOU 5211 O HIS C 55 3070 3057 3049 -60 138 -309 O ATOM 5212 CB HIS C 55 30.745 30.821 43.893 1.00 26.25 C ANISOU 5212 CB HIS C 55 3386 3293 3296 -55 173 -299 C ATOM 5213 CG HIS C 55 31.053 30.581 42.448 1.00 34.62 C ANISOU 5213 CG HIS C 55 4459 4348 4346 -61 180 -296 C ATOM 5214 ND1 HIS C 55 32.335 30.376 41.983 1.00 35.65 N ANISOU 5214 ND1 HIS C 55 4584 4480 4480 -75 182 -302 N ATOM 5215 CD2 HIS C 55 30.241 30.480 41.368 1.00 31.72 C ANISOU 5215 CD2 HIS C 55 4106 3978 3969 -50 176 -274 C ATOM 5216 CE1 HIS C 55 32.300 30.162 40.679 1.00 34.88 C ANISOU 5216 CE1 HIS C 55 4501 4379 4372 -77 187 -298 C ATOM 5217 NE2 HIS C 55 31.041 30.223 40.280 1.00 34.73 N ANISOU 5217 NE2 HIS C 55 4494 4358 4345 -61 182 -278 N ATOM 5218 N LEU C 56 29.493 30.088 46.816 1.00 19.70 N ANISOU 5218 N LEU C 56 2521 2488 2477 -36 138 -300 N ATOM 5219 CA LEU C 56 29.504 30.278 48.261 1.00 23.12 C ANISOU 5219 CA LEU C 56 2940 2925 2919 -35 132 -303 C ATOM 5220 C LEU C 56 29.845 28.997 48.991 1.00 26.40 C ANISOU 5220 C LEU C 56 3332 3361 3335 -37 108 -304 C ATOM 5221 O LEU C 56 30.425 29.049 50.078 1.00 34.28 O ANISOU 5221 O LEU C 56 4317 4363 4343 -42 105 -307 O ATOM 5222 CB LEU C 56 28.157 30.815 48.748 1.00 33.25 C ANISOU 5222 CB LEU C 56 4229 4204 4201 -20 134 -299 C ATOM 5223 CG LEU C 56 28.076 32.323 48.943 1.00 47.87 C ANISOU 5223 CG LEU C 56 6095 6035 6060 -21 158 -299 C ATOM 5224 CD1 LEU C 56 28.979 32.732 50.109 1.00 45.63 C ANISOU 5224 CD1 LEU C 56 5799 5753 5788 -31 158 -306 C ATOM 5225 CD2 LEU C 56 28.474 33.051 47.666 1.00 50.45 C ANISOU 5225 CD2 LEU C 56 6442 6343 6383 -27 179 -297 C ATOM 5226 N TYR C 57 29.539 27.846 48.397 1.00 25.31 N ANISOU 5226 N TYR C 57 3191 3236 3189 -32 92 -299 N ATOM 5227 CA TYR C 57 29.759 26.567 49.046 1.00 20.70 C ANISOU 5227 CA TYR C 57 2587 2672 2608 -32 69 -297 C ATOM 5228 C TYR C 57 31.033 25.882 48.573 1.00 20.82 C ANISOU 5228 C TYR C 57 2594 2692 2624 -45 66 -298 C ATOM 5229 O TYR C 57 31.186 24.668 48.750 1.00 23.94 O ANISOU 5229 O TYR C 57 2975 3102 3020 -43 49 -293 O ATOM 5230 CB TYR C 57 28.533 25.676 48.866 1.00 20.27 C ANISOU 5230 CB TYR C 57 2529 2630 2543 -18 50 -289 C ATOM 5231 CG TYR C 57 27.424 26.077 49.817 1.00 17.44 C ANISOU 5231 CG TYR C 57 2169 2273 2186 -6 46 -287 C ATOM 5232 CD1 TYR C 57 26.605 27.164 49.533 1.00 15.82 C ANISOU 5232 CD1 TYR C 57 1980 2053 1977 3 62 -287 C ATOM 5233 CD2 TYR C 57 27.215 25.390 51.015 1.00 19.05 C ANISOU 5233 CD2 TYR C 57 2355 2489 2394 -2 29 -284 C ATOM 5234 CE1 TYR C 57 25.598 27.551 50.384 1.00 16.70 C ANISOU 5234 CE1 TYR C 57 2090 2165 2092 16 58 -280 C ATOM 5235 CE2 TYR C 57 26.211 25.783 51.893 1.00 21.44 C ANISOU 5235 CE2 TYR C 57 2656 2793 2699 9 26 -283 C ATOM 5236 CZ TYR C 57 25.403 26.871 51.567 1.00 19.30 C ANISOU 5236 CZ TYR C 57 2401 2509 2424 19 41 -283 C ATOM 5237 OH TYR C 57 24.386 27.282 52.400 1.00 22.41 O ANISOU 5237 OH TYR C 57 2794 2902 2820 31 38 -278 O ATOM 5238 N GLY C 58 31.957 26.644 47.999 1.00 21.81 N ANISOU 5238 N GLY C 58 2729 2806 2754 -56 84 -304 N ATOM 5239 CA GLY C 58 33.309 26.172 47.796 1.00 22.93 C ANISOU 5239 CA GLY C 58 2861 2952 2900 -68 84 -307 C ATOM 5240 C GLY C 58 33.576 25.433 46.507 1.00 25.06 C ANISOU 5240 C GLY C 58 3135 3225 3163 -70 80 -304 C ATOM 5241 O GLY C 58 34.574 24.711 46.431 1.00 19.76 O ANISOU 5241 O GLY C 58 2452 2561 2495 -77 75 -304 O ATOM 5242 N ILE C 59 32.743 25.609 45.478 1.00 23.19 N ANISOU 5242 N ILE C 59 2914 2982 2915 -64 84 -301 N ATOM 5243 CA ILE C 59 32.973 24.896 44.225 1.00 20.08 C ANISOU 5243 CA ILE C 59 2525 2592 2513 -67 80 -298 C ATOM 5244 C ILE C 59 34.368 25.190 43.668 1.00 16.39 C ANISOU 5244 C ILE C 59 2059 2119 2051 -82 93 -304 C ATOM 5245 O ILE C 59 34.987 24.322 43.041 1.00 20.09 O ANISOU 5245 O ILE C 59 2522 2595 2518 -86 86 -302 O ATOM 5246 CB ILE C 59 31.864 25.234 43.204 1.00 19.28 C ANISOU 5246 CB ILE C 59 2443 2484 2398 -59 85 -294 C ATOM 5247 CG1 ILE C 59 31.944 24.310 41.989 1.00 24.42 C ANISOU 5247 CG1 ILE C 59 3096 3143 3038 -60 76 -290 C ATOM 5248 CG2 ILE C 59 31.941 26.679 42.754 1.00 18.12 C ANISOU 5248 CG2 ILE C 59 2317 2316 2252 -63 112 -298 C ATOM 5249 CD1 ILE C 59 30.846 24.558 40.970 1.00 23.53 C ANISOU 5249 CD1 ILE C 59 3003 3026 2911 -51 81 -285 C ATOM 5250 N ALA C 60 34.906 26.384 43.906 1.00 18.39 N ANISOU 5250 N ALA C 60 2318 2358 2311 -89 112 -310 N ATOM 5251 CA ALA C 60 36.237 26.702 43.403 1.00 21.04 C ANISOU 5251 CA ALA C 60 2654 2688 2652 -103 125 -316 C ATOM 5252 C ALA C 60 37.311 26.618 44.488 1.00 29.63 C ANISOU 5252 C ALA C 60 3722 3782 3752 -110 123 -321 C ATOM 5253 O ALA C 60 38.385 27.208 44.333 1.00 32.83 O ANISOU 5253 O ALA C 60 4128 4181 4163 -121 137 -327 O ATOM 5254 CB ALA C 60 36.244 28.089 42.756 1.00 15.35 C ANISOU 5254 CB ALA C 60 1953 1947 1930 -108 150 -319 C ATOM 5255 N GLY C 61 37.058 25.863 45.556 1.00 24.78 N ANISOU 5255 N GLY C 61 3092 3181 3141 -103 107 -317 N ATOM 5256 CA GLY C 61 37.983 25.758 46.672 1.00 22.82 C ANISOU 5256 CA GLY C 61 2827 2940 2904 -107 105 -321 C ATOM 5257 C GLY C 61 37.611 26.566 47.905 1.00 23.41 C ANISOU 5257 C GLY C 61 2899 3011 2985 -104 109 -324 C ATOM 5258 O GLY C 61 36.805 27.496 47.836 1.00 32.40 O ANISOU 5258 O GLY C 61 4052 4138 4121 -101 118 -325 O ATOM 5259 N LYS C 71 27.184 39.172 50.562 1.00 44.23 N ANISOU 5259 N LYS C 71 5689 5484 5634 -17 252 -292 N ATOM 5260 CA LYS C 71 26.131 39.946 51.218 1.00 41.87 C ANISOU 5260 CA LYS C 71 5395 5176 5339 -4 257 -285 C ATOM 5261 C LYS C 71 24.869 39.110 51.438 1.00 38.00 C ANISOU 5261 C LYS C 71 4899 4696 4841 14 239 -275 C ATOM 5262 O LYS C 71 24.533 38.241 50.625 1.00 33.71 O ANISOU 5262 O LYS C 71 4357 4163 4289 19 225 -262 O ATOM 5263 CB LYS C 71 25.781 41.196 50.397 1.00 30.76 C ANISOU 5263 CB LYS C 71 4013 3743 3931 -1 282 -275 C ATOM 5264 CG LYS C 71 26.951 42.133 50.129 1.00 33.39 C ANISOU 5264 CG LYS C 71 4351 4064 4270 -18 299 -282 C ATOM 5265 CD LYS C 71 26.602 43.175 49.065 1.00 39.09 C ANISOU 5265 CD LYS C 71 5100 4761 4989 -15 322 -270 C ATOM 5266 CE LYS C 71 27.778 44.111 48.776 1.00 40.65 C ANISOU 5266 CE LYS C 71 5304 4948 5194 -32 340 -277 C ATOM 5267 NZ LYS C 71 27.505 45.042 47.644 1.00 40.09 N ANISOU 5267 NZ LYS C 71 5260 4853 5120 -30 362 -266 N ATOM 5268 N LYS C 72 24.184 39.380 52.548 1.00 24.86 N ANISOU 5268 N LYS C 72 3228 3036 3184 22 234 -275 N ATOM 5269 CA LYS C 72 22.830 38.880 52.730 1.00 24.17 C ANISOU 5269 CA LYS C 72 3136 2958 3089 40 214 -254 C ATOM 5270 C LYS C 72 21.953 39.385 51.591 1.00 23.66 C ANISOU 5270 C LYS C 72 3093 2880 3018 51 218 -229 C ATOM 5271 O LYS C 72 22.195 40.447 51.016 1.00 21.12 O ANISOU 5271 O LYS C 72 2788 2538 2698 48 239 -227 O ATOM 5272 CB LYS C 72 22.269 39.329 54.080 1.00 33.29 C ANISOU 5272 CB LYS C 72 4282 4115 4253 47 212 -259 C ATOM 5273 CG LYS C 72 22.175 38.205 55.111 1.00 45.23 C ANISOU 5273 CG LYS C 72 5771 5649 5765 49 190 -267 C ATOM 5274 CD LYS C 72 21.490 38.660 56.398 1.00 45.89 C ANISOU 5274 CD LYS C 72 5847 5734 5856 57 188 -269 C ATOM 5275 CE LYS C 72 22.149 39.906 56.978 1.00 43.39 C ANISOU 5275 CE LYS C 72 5534 5403 5549 47 208 -281 C ATOM 5276 NZ LYS C 72 21.311 41.119 56.794 1.00 34.54 N ANISOU 5276 NZ LYS C 72 4430 4262 4432 57 225 -271 N ATOM 5277 N LEU C 73 20.911 38.620 51.277 1.00 18.91 N ANISOU 5277 N LEU C 73 2489 2290 2408 66 197 -209 N ATOM 5278 CA LEU C 73 20.111 38.923 50.097 1.00 17.62 C ANISOU 5278 CA LEU C 73 2344 2115 2235 76 198 -185 C ATOM 5279 C LEU C 73 19.427 40.281 50.209 1.00 16.68 C ANISOU 5279 C LEU C 73 2240 1977 2121 85 214 -175 C ATOM 5280 O LEU C 73 19.375 41.044 49.232 1.00 17.71 O ANISOU 5280 O LEU C 73 2390 2090 2248 85 228 -164 O ATOM 5281 CB LEU C 73 19.073 37.827 49.894 1.00 22.75 C ANISOU 5281 CB LEU C 73 2986 2783 2876 91 172 -167 C ATOM 5282 CG LEU C 73 18.940 37.222 48.503 1.00 29.66 C ANISOU 5282 CG LEU C 73 3870 3659 3739 93 165 -152 C ATOM 5283 CD1 LEU C 73 20.263 37.268 47.756 1.00 30.37 C ANISOU 5283 CD1 LEU C 73 3967 3744 3830 76 179 -165 C ATOM 5284 CD2 LEU C 73 18.439 35.788 48.643 1.00 27.23 C ANISOU 5284 CD2 LEU C 73 3546 3374 3425 101 137 -146 C ATOM 5285 N ASP C 74 18.905 40.616 51.387 1.00 15.58 N ANISOU 5285 N ASP C 74 2091 1839 1989 91 211 -178 N ATOM 5286 CA ASP C 74 18.201 41.894 51.490 1.00 25.84 C ANISOU 5286 CA ASP C 74 3405 3120 3292 99 225 -168 C ATOM 5287 C ASP C 74 19.163 43.078 51.406 1.00 18.84 C ANISOU 5287 C ASP C 74 2530 2214 2414 86 253 -182 C ATOM 5288 O ASP C 74 18.804 44.128 50.865 1.00 22.79 O ANISOU 5288 O ASP C 74 3050 2695 2915 91 268 -171 O ATOM 5289 CB ASP C 74 17.328 41.916 52.752 1.00 26.26 C ANISOU 5289 CB ASP C 74 3445 3181 3351 110 214 -168 C ATOM 5290 CG ASP C 74 18.100 41.630 54.018 1.00 34.21 C ANISOU 5290 CG ASP C 74 4432 4199 4366 99 214 -192 C ATOM 5291 OD1 ASP C 74 19.312 41.317 53.953 1.00 34.92 O ANISOU 5291 OD1 ASP C 74 4517 4292 4458 84 219 -211 O ATOM 5292 OD2 ASP C 74 17.457 41.663 55.088 1.00 36.49 O ANISOU 5292 OD2 ASP C 74 4710 4494 4659 107 206 -193 O ATOM 5293 N VAL C 75 20.395 42.913 51.880 1.00 18.23 N ANISOU 5293 N VAL C 75 2443 2140 2343 69 260 -206 N ATOM 5294 CA VAL C 75 21.408 43.950 51.714 1.00 16.53 C ANISOU 5294 CA VAL C 75 2239 1907 2136 55 287 -220 C ATOM 5295 C VAL C 75 21.799 44.091 50.243 1.00 20.61 C ANISOU 5295 C VAL C 75 2773 2412 2644 50 297 -211 C ATOM 5296 O VAL C 75 21.861 45.205 49.707 1.00 14.48 O ANISOU 5296 O VAL C 75 2017 1615 1871 49 318 -206 O ATOM 5297 CB VAL C 75 22.625 43.643 52.602 1.00 20.30 C ANISOU 5297 CB VAL C 75 2699 2393 2621 39 290 -249 C ATOM 5298 CG1 VAL C 75 23.820 44.486 52.200 1.00 14.47 C ANISOU 5298 CG1 VAL C 75 1969 1641 1888 22 312 -260 C ATOM 5299 CG2 VAL C 75 22.259 43.900 54.054 1.00 20.76 C ANISOU 5299 CG2 VAL C 75 2743 2456 2688 43 287 -258 C ATOM 5300 N LEU C 76 22.045 42.965 49.562 1.00 18.26 N ANISOU 5300 N LEU C 76 2471 2128 2338 48 283 -209 N ATOM 5301 CA LEU C 76 22.388 43.026 48.143 1.00 16.69 C ANISOU 5301 CA LEU C 76 2289 1920 2131 44 292 -200 C ATOM 5302 C LEU C 76 21.260 43.656 47.341 1.00 12.44 C ANISOU 5302 C LEU C 76 1771 1368 1586 59 293 -173 C ATOM 5303 O LEU C 76 21.507 44.486 46.456 1.00 15.59 O ANISOU 5303 O LEU C 76 2190 1748 1984 55 312 -167 O ATOM 5304 CB LEU C 76 22.696 41.631 47.601 1.00 15.30 C ANISOU 5304 CB LEU C 76 2103 1763 1947 41 273 -200 C ATOM 5305 CG LEU C 76 23.036 41.488 46.103 1.00 14.28 C ANISOU 5305 CG LEU C 76 1991 1628 1809 37 278 -190 C ATOM 5306 CD1 LEU C 76 24.338 42.216 45.745 1.00 16.81 C ANISOU 5306 CD1 LEU C 76 2320 1933 2134 18 304 -207 C ATOM 5307 CD2 LEU C 76 23.134 40.019 45.664 1.00 15.27 C ANISOU 5307 CD2 LEU C 76 2103 1773 1924 36 257 -188 C ATOM 5308 N SER C 77 20.015 43.259 47.629 1.00 12.51 N ANISOU 5308 N SER C 77 1774 1386 1591 76 274 -156 N ATOM 5309 CA SER C 77 18.874 43.832 46.925 1.00 9.70 C ANISOU 5309 CA SER C 77 1437 1019 1230 92 275 -131 C ATOM 5310 C SER C 77 18.827 45.338 47.111 1.00 16.92 C ANISOU 5310 C SER C 77 2367 1910 2153 92 298 -131 C ATOM 5311 O SER C 77 18.560 46.080 46.160 1.00 16.31 O ANISOU 5311 O SER C 77 2311 1816 2072 96 310 -117 O ATOM 5312 CB SER C 77 17.575 43.183 47.400 1.00 8.80 C ANISOU 5312 CB SER C 77 1313 920 1113 110 250 -116 C ATOM 5313 OG SER C 77 17.581 41.792 47.094 1.00 22.51 O ANISOU 5313 OG SER C 77 3037 2677 2841 111 229 -114 O ATOM 5314 N ASN C 78 19.072 45.805 48.337 1.00 8.89 N ANISOU 5314 N ASN C 78 1339 893 1147 88 305 -148 N ATOM 5315 CA ASN C 78 19.082 47.237 48.586 1.00 12.86 C ANISOU 5315 CA ASN C 78 1855 1373 1658 87 327 -150 C ATOM 5316 C ASN C 78 20.182 47.919 47.789 1.00 16.94 C ANISOU 5316 C ASN C 78 2388 1873 2177 71 351 -158 C ATOM 5317 O ASN C 78 19.959 48.973 47.184 1.00 15.81 O ANISOU 5317 O ASN C 78 2265 1709 2033 74 368 -148 O ATOM 5318 CB ASN C 78 19.253 47.499 50.081 1.00 12.15 C ANISOU 5318 CB ASN C 78 1749 1287 1580 83 329 -168 C ATOM 5319 CG ASN C 78 18.951 48.928 50.457 1.00 18.44 C ANISOU 5319 CG ASN C 78 2557 2063 2385 86 348 -167 C ATOM 5320 OD1 ASN C 78 17.866 49.424 50.173 1.00 22.36 O ANISOU 5320 OD1 ASN C 78 3065 2551 2879 101 346 -147 O ATOM 5321 ND2 ASN C 78 19.890 49.585 51.137 1.00 13.36 N ANISOU 5321 ND2 ASN C 78 1910 1412 1753 73 366 -189 N ATOM 5322 N ASP C 79 21.383 47.331 47.783 1.00 15.13 N ANISOU 5322 N ASP C 79 2148 1651 1948 55 354 -178 N ATOM 5323 CA ASP C 79 22.488 47.912 47.035 1.00 15.53 C ANISOU 5323 CA ASP C 79 2214 1688 2001 39 376 -187 C ATOM 5324 C ASP C 79 22.177 47.992 45.553 1.00 18.24 C ANISOU 5324 C ASP C 79 2577 2020 2332 44 379 -166 C ATOM 5325 O ASP C 79 22.484 48.997 44.901 1.00 14.48 O ANISOU 5325 O ASP C 79 2121 1523 1857 39 401 -163 O ATOM 5326 CB ASP C 79 23.770 47.107 47.253 1.00 10.71 C ANISOU 5326 CB ASP C 79 1587 1090 1393 21 375 -211 C ATOM 5327 CG ASP C 79 24.302 47.229 48.674 1.00 17.35 C ANISOU 5327 CG ASP C 79 2409 1937 2245 14 377 -234 C ATOM 5328 OD1 ASP C 79 23.866 48.142 49.409 1.00 20.46 O ANISOU 5328 OD1 ASP C 79 2803 2323 2647 18 383 -232 O ATOM 5329 OD2 ASP C 79 25.205 46.457 49.029 1.00 21.70 O ANISOU 5329 OD2 ASP C 79 2941 2506 2798 1 366 -248 O ATOM 5330 N LEU C 80 21.564 46.946 45.003 1.00 10.10 N ANISOU 5330 N LEU C 80 1542 1004 1290 54 357 -151 N ATOM 5331 CA LEU C 80 21.236 46.952 43.583 1.00 14.69 C ANISOU 5331 CA LEU C 80 2143 1578 1860 59 358 -131 C ATOM 5332 C LEU C 80 20.241 48.067 43.261 1.00 14.97 C ANISOU 5332 C LEU C 80 2199 1594 1895 73 367 -111 C ATOM 5333 O LEU C 80 20.455 48.853 42.334 1.00 16.23 O ANISOU 5333 O LEU C 80 2380 1734 2051 70 385 -103 O ATOM 5334 CB LEU C 80 20.688 45.586 43.182 1.00 19.14 C ANISOU 5334 CB LEU C 80 2696 2162 2412 68 331 -119 C ATOM 5335 CG LEU C 80 21.680 44.420 43.125 1.00 12.97 C ANISOU 5335 CG LEU C 80 1899 1399 1629 55 322 -135 C ATOM 5336 CD1 LEU C 80 20.931 43.084 43.117 1.00 11.10 C ANISOU 5336 CD1 LEU C 80 1649 1185 1384 66 293 -125 C ATOM 5337 CD2 LEU C 80 22.594 44.545 41.893 1.00 7.86 C ANISOU 5337 CD2 LEU C 80 1268 742 977 42 337 -137 C ATOM 5338 N VAL C 81 19.158 48.171 44.037 1.00 9.95 N ANISOU 5338 N VAL C 81 1557 962 1262 88 355 -102 N ATOM 5339 CA VAL C 81 18.161 49.206 43.770 1.00 11.96 C ANISOU 5339 CA VAL C 81 1830 1200 1516 103 363 -83 C ATOM 5340 C VAL C 81 18.761 50.596 43.982 1.00 12.72 C ANISOU 5340 C VAL C 81 1939 1272 1622 93 391 -93 C ATOM 5341 O VAL C 81 18.608 51.487 43.140 1.00 11.39 O ANISOU 5341 O VAL C 81 1793 1084 1451 96 406 -81 O ATOM 5342 CB VAL C 81 16.900 48.999 44.630 1.00 12.79 C ANISOU 5342 CB VAL C 81 1923 1314 1622 120 344 -73 C ATOM 5343 CG1 VAL C 81 15.938 50.163 44.402 1.00 7.65 C ANISOU 5343 CG1 VAL C 81 1292 644 972 134 353 -55 C ATOM 5344 CG2 VAL C 81 16.196 47.691 44.252 1.00 7.67 C ANISOU 5344 CG2 VAL C 81 1265 687 963 131 317 -60 C ATOM 5345 N MET C 82 19.468 50.792 45.104 1.00 12.58 N ANISOU 5345 N MET C 82 1907 1257 1616 82 398 -116 N ATOM 5346 CA MET C 82 20.087 52.085 45.389 1.00 18.03 C ANISOU 5346 CA MET C 82 2608 1926 2317 72 425 -128 C ATOM 5347 C MET C 82 21.022 52.523 44.265 1.00 17.38 C ANISOU 5347 C MET C 82 2544 1828 2231 58 446 -130 C ATOM 5348 O MET C 82 20.949 53.665 43.791 1.00 15.60 O ANISOU 5348 O MET C 82 2339 1580 2007 59 465 -123 O ATOM 5349 CB MET C 82 20.847 52.035 46.720 1.00 13.37 C ANISOU 5349 CB MET C 82 1997 1344 1739 60 429 -155 C ATOM 5350 CG MET C 82 19.968 52.189 47.959 1.00 22.54 C ANISOU 5350 CG MET C 82 3146 2512 2908 72 418 -155 C ATOM 5351 SD MET C 82 19.190 53.824 48.133 1.00 17.71 S ANISOU 5351 SD MET C 82 2552 1874 2302 82 437 -143 S ATOM 5352 CE MET C 82 18.298 53.565 49.646 1.00 17.29 C ANISOU 5352 CE MET C 82 2478 1836 2256 94 419 -147 C ATOM 5353 N ASN C 83 21.907 51.626 43.819 1.00 10.95 N ANISOU 5353 N ASN C 83 1723 1026 1413 46 442 -140 N ATOM 5354 CA ASN C 83 22.934 52.036 42.871 1.00 7.20 C ANISOU 5354 CA ASN C 83 1263 536 936 31 463 -146 C ATOM 5355 C ASN C 83 22.346 52.293 41.489 1.00 11.93 C ANISOU 5355 C ASN C 83 1886 1124 1523 40 465 -121 C ATOM 5356 O ASN C 83 22.707 53.277 40.831 1.00 17.21 O ANISOU 5356 O ASN C 83 2576 1771 2193 35 487 -119 O ATOM 5357 CB ASN C 83 24.048 50.990 42.782 1.00 28.60 C ANISOU 5357 CB ASN C 83 3958 3263 3645 15 457 -164 C ATOM 5358 CG ASN C 83 25.191 51.439 41.866 1.00 37.38 C ANISOU 5358 CG ASN C 83 5086 4361 4757 -2 480 -173 C ATOM 5359 OD1 ASN C 83 26.053 52.226 42.265 1.00 45.82 O ANISOU 5359 OD1 ASN C 83 6156 5419 5835 -16 501 -190 O ATOM 5360 ND2 ASN C 83 25.187 50.952 40.627 1.00 29.71 N ANISOU 5360 ND2 ASN C 83 4125 3390 3772 -1 476 -160 N ATOM 5361 N MET C 84 21.422 51.442 41.050 1.00 12.54 N ANISOU 5361 N MET C 84 1961 1215 1590 55 442 -102 N ATOM 5362 CA MET C 84 20.781 51.636 39.750 1.00 16.95 C ANISOU 5362 CA MET C 84 2542 1763 2137 66 442 -78 C ATOM 5363 C MET C 84 19.964 52.928 39.718 1.00 17.46 C ANISOU 5363 C MET C 84 2626 1806 2204 77 454 -63 C ATOM 5364 O MET C 84 19.969 53.652 38.712 1.00 13.04 O ANISOU 5364 O MET C 84 2089 1227 1638 78 469 -51 O ATOM 5365 CB MET C 84 19.895 50.423 39.417 1.00 7.14 C ANISOU 5365 CB MET C 84 1290 540 882 80 413 -61 C ATOM 5366 CG MET C 84 20.657 49.106 39.085 1.00 7.41 C ANISOU 5366 CG MET C 84 1310 594 911 69 401 -71 C ATOM 5367 SD MET C 84 21.941 49.325 37.821 1.00 17.09 S ANISOU 5367 SD MET C 84 2554 1808 2132 51 422 -78 S ATOM 5368 CE MET C 84 20.989 50.021 36.459 1.00 14.23 C ANISOU 5368 CE MET C 84 2222 1427 1758 66 427 -47 C ATOM 5369 N LEU C 85 19.250 53.236 40.803 1.00 16.25 N ANISOU 5369 N LEU C 85 2462 1654 2057 87 448 -63 N ATOM 5370 CA LEU C 85 18.449 54.457 40.831 1.00 14.13 C ANISOU 5370 CA LEU C 85 2211 1366 1793 99 459 -50 C ATOM 5371 C LEU C 85 19.334 55.699 40.880 1.00 19.05 C ANISOU 5371 C LEU C 85 2847 1965 2425 85 490 -63 C ATOM 5372 O LEU C 85 19.044 56.698 40.211 1.00 20.87 O ANISOU 5372 O LEU C 85 3101 2174 2653 89 505 -50 O ATOM 5373 CB LEU C 85 17.466 54.428 42.005 1.00 18.61 C ANISOU 5373 CB LEU C 85 2763 1942 2366 113 445 -48 C ATOM 5374 CG LEU C 85 16.274 53.474 41.825 1.00 21.07 C ANISOU 5374 CG LEU C 85 3067 2271 2668 131 416 -29 C ATOM 5375 CD1 LEU C 85 15.313 53.505 43.023 1.00 12.14 C ANISOU 5375 CD1 LEU C 85 1921 1147 1543 144 403 -28 C ATOM 5376 CD2 LEU C 85 15.508 53.750 40.531 1.00 26.74 C ANISOU 5376 CD2 LEU C 85 3808 2977 3374 144 415 -3 C ATOM 5377 N LYS C 86 20.402 55.664 41.682 1.00 18.97 N ANISOU 5377 N LYS C 86 2823 1960 2425 68 499 -89 N ATOM 5378 CA LYS C 86 21.338 56.783 41.740 1.00 21.06 C ANISOU 5378 CA LYS C 86 3099 2204 2699 53 528 -103 C ATOM 5379 C LYS C 86 21.924 57.087 40.366 1.00 24.65 C ANISOU 5379 C LYS C 86 3576 2643 3146 44 544 -97 C ATOM 5380 O LYS C 86 22.028 58.251 39.962 1.00 26.72 O ANISOU 5380 O LYS C 86 3859 2882 3411 42 566 -92 O ATOM 5381 CB LYS C 86 22.468 56.489 42.729 1.00 14.00 C ANISOU 5381 CB LYS C 86 2184 1320 1816 35 533 -133 C ATOM 5382 CG LYS C 86 22.099 56.541 44.199 1.00 22.24 C ANISOU 5382 CG LYS C 86 3208 2372 2870 40 525 -144 C ATOM 5383 CD LYS C 86 23.272 56.039 45.036 1.00 19.25 C ANISOU 5383 CD LYS C 86 2802 2014 2499 20 520 -168 C ATOM 5384 CE LYS C 86 22.957 56.089 46.508 1.00 22.27 C ANISOU 5384 CE LYS C 86 3162 2409 2891 23 508 -176 C ATOM 5385 NZ LYS C 86 24.109 55.657 47.348 1.00 27.75 N ANISOU 5385 NZ LYS C 86 3830 3122 3592 4 502 -199 N ATOM 5386 N SER C 87 22.350 56.053 39.655 1.00 14.49 N ANISOU 5386 N SER C 87 2286 1371 1851 39 534 -96 N ATOM 5387 CA SER C 87 23.000 56.216 38.365 1.00 14.46 C ANISOU 5387 CA SER C 87 2300 1354 1838 29 548 -92 C ATOM 5388 C SER C 87 22.021 56.453 37.226 1.00 14.54 C ANISOU 5388 C SER C 87 2333 1355 1836 45 544 -63 C ATOM 5389 O SER C 87 22.459 56.687 36.099 1.00 21.12 O ANISOU 5389 O SER C 87 3185 2176 2662 39 557 -57 O ATOM 5390 CB SER C 87 23.862 54.986 38.085 1.00 25.42 C ANISOU 5390 CB SER C 87 3675 2763 3222 17 538 -105 C ATOM 5391 OG SER C 87 23.069 53.822 38.069 1.00 23.59 O ANISOU 5391 OG SER C 87 3430 2553 2982 30 509 -93 O ATOM 5392 N SER C 88 20.712 56.425 37.491 1.00 19.48 N ANISOU 5392 N SER C 88 2958 1984 2459 66 527 -45 N ATOM 5393 CA SER C 88 19.726 56.738 36.458 1.00 14.73 C ANISOU 5393 CA SER C 88 2378 1372 1846 82 524 -18 C ATOM 5394 C SER C 88 19.663 58.232 36.143 1.00 19.47 C ANISOU 5394 C SER C 88 3003 1943 2450 83 549 -11 C ATOM 5395 O SER C 88 19.099 58.609 35.111 1.00 21.20 O ANISOU 5395 O SER C 88 3245 2150 2660 93 551 10 O ATOM 5396 CB SER C 88 18.339 56.259 36.883 1.00 13.31 C ANISOU 5396 CB SER C 88 2189 1206 1663 104 498 -2 C ATOM 5397 OG SER C 88 17.821 57.058 37.941 1.00 16.00 O ANISOU 5397 OG SER C 88 2525 1539 2014 111 503 -5 O ATOM 5398 N PHE C 89 20.209 59.083 37.010 1.00 17.96 N ANISOU 5398 N PHE C 89 2810 1742 2273 73 567 -28 N ATOM 5399 CA PHE C 89 20.095 60.537 36.899 1.00 22.65 C ANISOU 5399 CA PHE C 89 3425 2308 2872 74 590 -23 C ATOM 5400 C PHE C 89 18.640 61.001 36.959 1.00 23.38 C ANISOU 5400 C PHE C 89 3527 2394 2962 98 580 0 C ATOM 5401 O PHE C 89 18.318 62.116 36.532 1.00 34.47 O ANISOU 5401 O PHE C 89 4954 3775 4367 103 596 11 O ATOM 5402 CB PHE C 89 20.777 61.053 35.621 1.00 25.99 C ANISOU 5402 CB PHE C 89 3874 2713 3289 64 611 -18 C ATOM 5403 CG PHE C 89 22.276 60.907 35.634 1.00 31.60 C ANISOU 5403 CG PHE C 89 4579 3424 4005 40 627 -42 C ATOM 5404 CD1 PHE C 89 23.078 61.861 36.239 1.00 41.30 C ANISOU 5404 CD1 PHE C 89 5805 4642 5245 25 649 -60 C ATOM 5405 CD2 PHE C 89 22.885 59.815 35.037 1.00 39.35 C ANISOU 5405 CD2 PHE C 89 5552 4421 4977 31 618 -47 C ATOM 5406 CE1 PHE C 89 24.459 61.726 36.259 1.00 41.10 C ANISOU 5406 CE1 PHE C 89 5770 4623 5223 2 660 -81 C ATOM 5407 CE2 PHE C 89 24.268 59.672 35.054 1.00 43.83 C ANISOU 5407 CE2 PHE C 89 6114 4989 5550 9 633 -70 C ATOM 5408 CZ PHE C 89 25.053 60.628 35.666 1.00 36.78 C ANISOU 5408 CZ PHE C 89 5220 4087 4670 -6 654 -87 C ATOM 5409 N ALA C 90 17.741 60.174 37.500 1.00 18.20 N ANISOU 5409 N ALA C 90 2852 1758 2303 112 554 6 N ATOM 5410 CA ALA C 90 16.327 60.509 37.535 1.00 17.26 C ANISOU 5410 CA ALA C 90 2740 1635 2182 134 542 27 C ATOM 5411 C ALA C 90 15.800 60.777 38.937 1.00 10.42 C ANISOU 5411 C ALA C 90 1858 774 1328 141 536 19 C ATOM 5412 O ALA C 90 14.634 61.145 39.077 1.00 14.71 O ANISOU 5412 O ALA C 90 2406 1313 1870 159 528 35 O ATOM 5413 CB ALA C 90 15.502 59.379 36.907 1.00 15.04 C ANISOU 5413 CB ALA C 90 2456 1373 1888 149 515 45 C ATOM 5414 N THR C 91 16.610 60.591 39.975 1.00 16.98 N ANISOU 5414 N THR C 91 2668 1613 2169 127 540 -5 N ATOM 5415 CA THR C 91 16.116 60.615 41.346 1.00 22.25 C ANISOU 5415 CA THR C 91 3316 2289 2847 133 531 -14 C ATOM 5416 C THR C 91 16.933 61.582 42.196 1.00 12.66 C ANISOU 5416 C THR C 91 2101 1062 1648 119 554 -35 C ATOM 5417 O THR C 91 18.063 61.929 41.863 1.00 14.56 O ANISOU 5417 O THR C 91 2347 1293 1891 101 574 -48 O ATOM 5418 CB THR C 91 16.147 59.203 41.974 1.00 21.58 C ANISOU 5418 CB THR C 91 3203 2234 2761 132 507 -23 C ATOM 5419 OG1 THR C 91 17.501 58.821 42.223 1.00 17.46 O ANISOU 5419 OG1 THR C 91 2671 1719 2244 111 516 -47 O ATOM 5420 CG2 THR C 91 15.515 58.185 41.024 1.00 14.87 C ANISOU 5420 CG2 THR C 91 2356 1398 1896 143 486 -4 C ATOM 5421 N CYS C 92 16.341 62.012 43.309 1.00 9.15 N ANISOU 5421 N CYS C 92 1645 617 1213 127 551 -39 N ATOM 5422 CA CYS C 92 17.016 62.925 44.220 1.00 18.91 C ANISOU 5422 CA CYS C 92 2872 1852 2462 112 566 -56 C ATOM 5423 C CYS C 92 16.914 62.458 45.671 1.00 15.10 C ANISOU 5423 C CYS C 92 2361 1389 1988 111 552 -71 C ATOM 5424 O CYS C 92 17.801 62.751 46.475 1.00 21.59 O ANISOU 5424 O CYS C 92 3168 2216 2819 95 560 -91 O ATOM 5425 CB CYS C 92 16.458 64.343 44.068 1.00 15.05 C ANISOU 5425 CB CYS C 92 2400 1344 1975 118 579 -43 C ATOM 5426 SG CYS C 92 14.667 64.426 44.291 1.00 18.84 S ANISOU 5426 SG CYS C 92 2883 1824 2452 147 560 -20 S ATOM 5427 N VAL C 93 15.854 61.735 46.025 1.00 16.70 N ANISOU 5427 N VAL C 93 2556 1601 2187 130 532 -62 N ATOM 5428 CA VAL C 93 15.681 61.220 47.380 1.00 16.03 C ANISOU 5428 CA VAL C 93 2444 1535 2110 131 517 -76 C ATOM 5429 C VAL C 93 15.236 59.764 47.280 1.00 17.58 C ANISOU 5429 C VAL C 93 2628 1753 2297 139 492 -70 C ATOM 5430 O VAL C 93 14.313 59.442 46.523 1.00 12.81 O ANISOU 5430 O VAL C 93 2033 1152 1683 154 479 -48 O ATOM 5431 CB VAL C 93 14.652 62.040 48.190 1.00 16.55 C ANISOU 5431 CB VAL C 93 2509 1598 2183 144 514 -68 C ATOM 5432 CG1 VAL C 93 14.518 61.480 49.600 1.00 20.45 C ANISOU 5432 CG1 VAL C 93 2975 2111 2684 144 500 -83 C ATOM 5433 CG2 VAL C 93 15.024 63.529 48.238 1.00 15.61 C ANISOU 5433 CG2 VAL C 93 2400 1460 2070 134 536 -71 C ATOM 5434 N LEU C 94 15.887 58.885 48.039 1.00 10.89 N ANISOU 5434 N LEU C 94 1758 926 1454 129 483 -89 N ATOM 5435 CA LEU C 94 15.585 57.458 47.989 1.00 14.77 C ANISOU 5435 CA LEU C 94 2233 1442 1936 134 457 -85 C ATOM 5436 C LEU C 94 15.311 56.980 49.404 1.00 17.61 C ANISOU 5436 C LEU C 94 2567 1820 2302 136 443 -97 C ATOM 5437 O LEU C 94 16.188 57.066 50.265 1.00 12.99 O ANISOU 5437 O LEU C 94 1970 1238 1727 123 452 -120 O ATOM 5438 CB LEU C 94 16.747 56.673 47.373 1.00 11.34 C ANISOU 5438 CB LEU C 94 1796 1017 1497 117 459 -96 C ATOM 5439 CG LEU C 94 17.101 57.140 45.952 1.00 17.20 C ANISOU 5439 CG LEU C 94 2564 1741 2232 113 474 -85 C ATOM 5440 CD1 LEU C 94 18.402 56.503 45.479 1.00 23.49 C ANISOU 5440 CD1 LEU C 94 3357 2544 3026 95 479 -100 C ATOM 5441 CD2 LEU C 94 15.981 56.855 44.988 1.00 11.46 C ANISOU 5441 CD2 LEU C 94 1848 1014 1491 131 459 -57 C ATOM 5442 N VAL C 95 14.109 56.469 49.647 1.00 10.44 N ANISOU 5442 N VAL C 95 1652 924 1390 154 421 -82 N ATOM 5443 CA VAL C 95 13.755 55.909 50.943 1.00 10.39 C ANISOU 5443 CA VAL C 95 1623 937 1390 157 406 -92 C ATOM 5444 C VAL C 95 13.640 54.399 50.789 1.00 14.80 C ANISOU 5444 C VAL C 95 2166 1520 1939 159 381 -89 C ATOM 5445 O VAL C 95 12.918 53.904 49.915 1.00 20.63 O ANISOU 5445 O VAL C 95 2911 2262 2666 171 368 -69 O ATOM 5446 CB VAL C 95 12.465 56.538 51.499 1.00 17.57 C ANISOU 5446 CB VAL C 95 2534 1841 2303 175 401 -79 C ATOM 5447 CG1 VAL C 95 11.938 55.734 52.679 1.00 14.71 C ANISOU 5447 CG1 VAL C 95 2146 1501 1942 181 380 -85 C ATOM 5448 CG2 VAL C 95 12.753 57.983 51.929 1.00 14.95 C ANISOU 5448 CG2 VAL C 95 2212 1487 1982 170 426 -88 C ATOM 5449 N SER C 96 14.371 53.676 51.626 1.00 11.68 N ANISOU 5449 N SER C 96 1750 1142 1548 148 375 -109 N ATOM 5450 CA SER C 96 14.393 52.224 51.605 1.00 12.55 C ANISOU 5450 CA SER C 96 1843 1275 1649 148 353 -110 C ATOM 5451 C SER C 96 14.068 51.676 52.982 1.00 10.97 C ANISOU 5451 C SER C 96 1619 1094 1455 151 337 -120 C ATOM 5452 O SER C 96 14.548 52.191 53.990 1.00 9.58 O ANISOU 5452 O SER C 96 1435 915 1290 143 348 -138 O ATOM 5453 CB SER C 96 15.763 51.705 51.178 1.00 13.59 C ANISOU 5453 CB SER C 96 1972 1411 1780 129 359 -125 C ATOM 5454 OG SER C 96 15.855 50.319 51.433 1.00 12.78 O ANISOU 5454 OG SER C 96 1850 1333 1672 128 337 -130 O ATOM 5455 N GLU C 97 13.286 50.597 53.013 1.00 14.09 N ANISOU 5455 N GLU C 97 2003 1508 1843 162 313 -109 N ATOM 5456 CA GLU C 97 13.091 49.839 54.248 1.00 12.12 C ANISOU 5456 CA GLU C 97 1730 1279 1597 163 296 -120 C ATOM 5457 C GLU C 97 14.415 49.526 54.947 1.00 17.26 C ANISOU 5457 C GLU C 97 2366 1937 2254 145 302 -147 C ATOM 5458 O GLU C 97 14.456 49.407 56.175 1.00 18.08 O ANISOU 5458 O GLU C 97 2453 2051 2365 143 298 -160 O ATOM 5459 CB GLU C 97 12.340 48.532 53.932 1.00 15.62 C ANISOU 5459 CB GLU C 97 2164 1743 2029 174 270 -106 C ATOM 5460 CG GLU C 97 11.775 47.789 55.151 1.00 27.56 C ANISOU 5460 CG GLU C 97 3654 3275 3544 180 250 -111 C ATOM 5461 CD GLU C 97 12.766 46.851 55.812 1.00 38.35 C ANISOU 5461 CD GLU C 97 5001 4660 4912 166 244 -132 C ATOM 5462 OE1 GLU C 97 13.679 46.348 55.118 1.00 26.50 O ANISOU 5462 OE1 GLU C 97 3501 3160 3406 155 246 -138 O ATOM 5463 OE2 GLU C 97 12.622 46.611 57.036 1.00 51.47 O ANISOU 5463 OE2 GLU C 97 6645 6333 6580 167 236 -142 O ATOM 5464 N GLU C 98 15.504 49.394 54.188 1.00 11.68 N ANISOU 5464 N GLU C 98 1666 1227 1545 131 313 -155 N ATOM 5465 CA GLU C 98 16.799 48.966 54.719 1.00 17.11 C ANISOU 5465 CA GLU C 98 2340 1924 2238 113 317 -180 C ATOM 5466 C GLU C 98 17.615 50.090 55.344 1.00 19.29 C ANISOU 5466 C GLU C 98 2619 2185 2527 101 341 -199 C ATOM 5467 O GLU C 98 18.641 49.813 55.972 1.00 27.94 O ANISOU 5467 O GLU C 98 3700 3289 3627 86 342 -220 O ATOM 5468 CB GLU C 98 17.631 48.329 53.607 1.00 17.26 C ANISOU 5468 CB GLU C 98 2364 1945 2250 103 317 -181 C ATOM 5469 CG GLU C 98 17.100 47.000 53.162 1.00 32.60 C ANISOU 5469 CG GLU C 98 4299 3907 4181 111 292 -168 C ATOM 5470 CD GLU C 98 17.255 45.968 54.237 1.00 41.39 C ANISOU 5470 CD GLU C 98 5388 5043 5296 108 274 -182 C ATOM 5471 OE1 GLU C 98 18.377 45.843 54.781 1.00 46.01 O ANISOU 5471 OE1 GLU C 98 5963 5633 5888 93 281 -205 O ATOM 5472 OE2 GLU C 98 16.252 45.305 54.554 1.00 46.14 O ANISOU 5472 OE2 GLU C 98 5980 5659 5894 122 254 -170 O ATOM 5473 N ASP C 99 17.196 51.341 55.206 1.00 20.09 N ANISOU 5473 N ASP C 99 2736 2264 2632 106 357 -191 N ATOM 5474 CA ASP C 99 18.008 52.480 55.607 1.00 23.65 C ANISOU 5474 CA ASP C 99 3189 2704 3093 92 375 -204 C ATOM 5475 C ASP C 99 17.227 53.351 56.579 1.00 19.53 C ANISOU 5475 C ASP C 99 2664 2177 2579 101 376 -201 C ATOM 5476 O ASP C 99 16.094 53.759 56.288 1.00 16.40 O ANISOU 5476 O ASP C 99 2281 1770 2181 118 378 -184 O ATOM 5477 CB ASP C 99 18.421 53.286 54.383 1.00 14.24 C ANISOU 5477 CB ASP C 99 2021 1491 1899 87 396 -197 C ATOM 5478 CG ASP C 99 19.450 52.575 53.535 1.00 17.15 C ANISOU 5478 CG ASP C 99 2390 1864 2262 74 397 -203 C ATOM 5479 OD1 ASP C 99 20.622 52.505 53.946 1.00 20.72 O ANISOU 5479 OD1 ASP C 99 2829 2326 2719 55 398 -220 O ATOM 5480 OD2 ASP C 99 19.088 52.089 52.449 1.00 19.73 O ANISOU 5480 OD2 ASP C 99 2731 2187 2579 82 395 -190 O ATOM 5481 N LYS C 100 17.844 53.653 57.723 1.00 17.49 N ANISOU 5481 N LYS C 100 2389 1929 2329 89 375 -217 N ATOM 5482 CA LYS C 100 17.139 54.406 58.754 1.00 24.38 C ANISOU 5482 CA LYS C 100 3256 2799 3208 96 375 -216 C ATOM 5483 C LYS C 100 16.703 55.776 58.240 1.00 19.96 C ANISOU 5483 C LYS C 100 2717 2214 2651 101 393 -204 C ATOM 5484 O LYS C 100 15.557 56.193 58.451 1.00 14.09 O ANISOU 5484 O LYS C 100 1979 1464 1909 117 392 -192 O ATOM 5485 CB LYS C 100 18.018 54.549 59.994 1.00 28.91 C ANISOU 5485 CB LYS C 100 3810 3385 3789 81 371 -235 C ATOM 5486 CG LYS C 100 17.340 55.280 61.134 1.00 39.72 C ANISOU 5486 CG LYS C 100 5172 4753 5165 88 370 -235 C ATOM 5487 CD LYS C 100 18.210 55.296 62.383 1.00 50.71 C ANISOU 5487 CD LYS C 100 6545 6160 6563 74 364 -253 C ATOM 5488 CE LYS C 100 17.505 55.995 63.534 1.00 61.49 C ANISOU 5488 CE LYS C 100 7903 7525 7935 81 363 -253 C ATOM 5489 NZ LYS C 100 18.338 56.006 64.770 1.00 70.28 N ANISOU 5489 NZ LYS C 100 8998 8652 9052 68 357 -269 N ATOM 5490 N HIS C 101 17.585 56.465 57.531 1.00 14.78 N ANISOU 5490 N HIS C 101 2073 1544 1996 88 411 -207 N ATOM 5491 CA HIS C 101 17.314 57.793 57.001 1.00 19.24 C ANISOU 5491 CA HIS C 101 2660 2086 2565 91 430 -197 C ATOM 5492 C HIS C 101 17.224 57.746 55.483 1.00 20.03 C ANISOU 5492 C HIS C 101 2782 2171 2657 95 439 -182 C ATOM 5493 O HIS C 101 17.705 56.810 54.836 1.00 17.27 O ANISOU 5493 O HIS C 101 2432 1829 2300 91 434 -184 O ATOM 5494 CB HIS C 101 18.390 58.785 57.442 1.00 15.28 C ANISOU 5494 CB HIS C 101 2155 1579 2072 72 445 -210 C ATOM 5495 CG HIS C 101 18.507 58.903 58.932 1.00 25.50 C ANISOU 5495 CG HIS C 101 3428 2887 3375 68 436 -224 C ATOM 5496 ND1 HIS C 101 17.529 59.490 59.708 1.00 25.22 N ANISOU 5496 ND1 HIS C 101 3390 2848 3343 80 434 -219 N ATOM 5497 CD2 HIS C 101 19.460 58.469 59.791 1.00 28.27 C ANISOU 5497 CD2 HIS C 101 3758 3255 3729 54 429 -241 C ATOM 5498 CE1 HIS C 101 17.887 59.434 60.979 1.00 33.13 C ANISOU 5498 CE1 HIS C 101 4373 3865 4352 73 426 -233 C ATOM 5499 NE2 HIS C 101 19.054 58.819 61.056 1.00 31.37 N ANISOU 5499 NE2 HIS C 101 4138 3654 4128 58 422 -246 N ATOM 5500 N ALA C 102 16.551 58.749 54.926 1.00 22.37 N ANISOU 5500 N ALA C 102 3100 2447 2954 105 451 -167 N ATOM 5501 CA ALA C 102 16.512 58.902 53.478 1.00 20.50 C ANISOU 5501 CA ALA C 102 2887 2193 2708 108 462 -153 C ATOM 5502 C ALA C 102 17.918 59.105 52.936 1.00 19.64 C ANISOU 5502 C ALA C 102 2781 2080 2600 87 476 -165 C ATOM 5503 O ALA C 102 18.740 59.797 53.543 1.00 18.85 O ANISOU 5503 O ALA C 102 2674 1980 2509 72 486 -178 O ATOM 5504 CB ALA C 102 15.633 60.092 53.091 1.00 14.09 C ANISOU 5504 CB ALA C 102 2096 1360 1898 121 473 -136 C ATOM 5505 N ILE C 103 18.176 58.518 51.771 1.00 13.05 N ANISOU 5505 N ILE C 103 1959 1243 1757 86 478 -158 N ATOM 5506 CA ILE C 103 19.421 58.715 51.038 1.00 16.18 C ANISOU 5506 CA ILE C 103 2362 1633 2152 67 493 -166 C ATOM 5507 C ILE C 103 19.224 59.879 50.078 1.00 17.99 C ANISOU 5507 C ILE C 103 2619 1837 2379 70 513 -152 C ATOM 5508 O ILE C 103 18.245 59.907 49.320 1.00 20.35 O ANISOU 5508 O ILE C 103 2936 2125 2672 87 511 -133 O ATOM 5509 CB ILE C 103 19.820 57.439 50.275 1.00 19.91 C ANISOU 5509 CB ILE C 103 2833 2117 2615 65 483 -168 C ATOM 5510 CG1 ILE C 103 20.366 56.372 51.229 1.00 20.37 C ANISOU 5510 CG1 ILE C 103 2863 2201 2676 56 466 -185 C ATOM 5511 CG2 ILE C 103 20.850 57.759 49.190 1.00 20.80 C ANISOU 5511 CG2 ILE C 103 2961 2218 2725 50 501 -170 C ATOM 5512 CD1 ILE C 103 19.368 55.827 52.195 1.00 17.93 C ANISOU 5512 CD1 ILE C 103 2540 1905 2368 71 447 -183 C ATOM 5513 N ILE C 104 20.121 60.860 50.142 1.00 19.63 N ANISOU 5513 N ILE C 104 2829 2035 2594 54 531 -161 N ATOM 5514 CA ILE C 104 20.088 62.031 49.272 1.00 14.61 C ANISOU 5514 CA ILE C 104 2219 1375 1958 54 551 -150 C ATOM 5515 C ILE C 104 21.080 61.807 48.141 1.00 13.59 C ANISOU 5515 C ILE C 104 2100 1241 1822 40 562 -152 C ATOM 5516 O ILE C 104 22.283 61.639 48.385 1.00 30.43 O ANISOU 5516 O ILE C 104 4220 3383 3959 21 566 -170 O ATOM 5517 CB ILE C 104 20.417 63.316 50.051 1.00 20.04 C ANISOU 5517 CB ILE C 104 2902 2054 2656 45 565 -158 C ATOM 5518 CG1 ILE C 104 19.575 63.411 51.326 1.00 21.58 C ANISOU 5518 CG1 ILE C 104 3082 2258 2858 56 553 -160 C ATOM 5519 CG2 ILE C 104 20.196 64.533 49.169 1.00 18.00 C ANISOU 5519 CG2 ILE C 104 2671 1771 2397 48 586 -144 C ATOM 5520 CD1 ILE C 104 18.066 63.380 51.099 1.00 14.53 C ANISOU 5520 CD1 ILE C 104 2200 1359 1960 80 543 -139 C ATOM 5521 N VAL C 105 20.590 61.810 46.899 1.00 12.50 N ANISOU 5521 N VAL C 105 1986 1089 1674 50 567 -134 N ATOM 5522 CA VAL C 105 21.454 61.554 45.758 1.00 12.80 C ANISOU 5522 CA VAL C 105 2036 1122 1705 39 577 -135 C ATOM 5523 C VAL C 105 22.434 62.704 45.591 1.00 23.16 C ANISOU 5523 C VAL C 105 3355 2421 3023 21 600 -143 C ATOM 5524 O VAL C 105 22.082 63.878 45.762 1.00 26.63 O ANISOU 5524 O VAL C 105 3805 2845 3467 24 613 -137 O ATOM 5525 CB VAL C 105 20.621 61.343 44.481 1.00 17.55 C ANISOU 5525 CB VAL C 105 2663 1711 2295 55 576 -112 C ATOM 5526 CG1 VAL C 105 21.522 61.132 43.275 1.00 15.39 C ANISOU 5526 CG1 VAL C 105 2403 1432 2014 42 587 -113 C ATOM 5527 CG2 VAL C 105 19.650 60.155 44.647 1.00 15.64 C ANISOU 5527 CG2 VAL C 105 2413 1483 2047 73 552 -104 C ATOM 5528 N GLU C 106 23.672 62.373 45.244 1.00 22.55 N ANISOU 5528 N GLU C 106 3273 2349 2945 2 607 -156 N ATOM 5529 CA GLU C 106 24.679 63.405 45.091 1.00 26.02 C ANISOU 5529 CA GLU C 106 3717 2777 3390 -16 629 -164 C ATOM 5530 C GLU C 106 24.290 64.362 43.965 1.00 26.26 C ANISOU 5530 C GLU C 106 3779 2783 3415 -10 647 -146 C ATOM 5531 O GLU C 106 23.604 63.970 43.013 1.00 20.16 O ANISOU 5531 O GLU C 106 3025 2004 2633 3 643 -130 O ATOM 5532 CB GLU C 106 26.052 62.789 44.825 1.00 27.18 C ANISOU 5532 CB GLU C 106 3854 2936 3538 -36 631 -180 C ATOM 5533 CG GLU C 106 26.125 61.790 43.703 1.00 48.47 C ANISOU 5533 CG GLU C 106 6560 5635 6222 -35 626 -174 C ATOM 5534 CD GLU C 106 27.502 61.149 43.622 1.00 68.35 C ANISOU 5534 CD GLU C 106 9062 8166 8741 -56 626 -191 C ATOM 5535 OE1 GLU C 106 28.373 61.507 44.442 1.00 75.97 O ANISOU 5535 OE1 GLU C 106 10010 9139 9717 -70 629 -207 O ATOM 5536 OE2 GLU C 106 27.721 60.291 42.746 1.00 75.87 O ANISOU 5536 OE2 GLU C 106 10020 9123 9684 -57 621 -189 O ATOM 5537 N PRO C 107 24.712 65.633 44.059 1.00 27.68 N ANISOU 5537 N PRO C 107 3967 2949 3602 -19 667 -149 N ATOM 5538 CA PRO C 107 24.179 66.661 43.149 1.00 26.44 C ANISOU 5538 CA PRO C 107 3838 2768 3440 -11 684 -131 C ATOM 5539 C PRO C 107 24.318 66.333 41.678 1.00 24.49 C ANISOU 5539 C PRO C 107 3613 2512 3180 -10 690 -119 C ATOM 5540 O PRO C 107 23.375 66.538 40.906 1.00 31.95 O ANISOU 5540 O PRO C 107 4578 3444 4116 6 689 -99 O ATOM 5541 CB PRO C 107 25.015 67.902 43.511 1.00 28.14 C ANISOU 5541 CB PRO C 107 4053 2975 3665 -27 705 -141 C ATOM 5542 CG PRO C 107 25.435 67.666 44.921 1.00 28.22 C ANISOU 5542 CG PRO C 107 4033 3002 3686 -35 695 -160 C ATOM 5543 CD PRO C 107 25.658 66.197 45.041 1.00 25.78 C ANISOU 5543 CD PRO C 107 3708 2715 3374 -36 675 -168 C ATOM 5544 N GLU C 108 25.466 65.800 41.269 1.00 21.07 N ANISOU 5544 N GLU C 108 3174 2086 2745 -28 694 -132 N ATOM 5545 CA GLU C 108 25.714 65.590 39.851 1.00 36.45 C ANISOU 5545 CA GLU C 108 5144 4025 4682 -30 703 -122 C ATOM 5546 C GLU C 108 24.818 64.518 39.256 1.00 36.52 C ANISOU 5546 C GLU C 108 5159 4037 4678 -13 684 -107 C ATOM 5547 O GLU C 108 24.677 64.462 38.030 1.00 33.64 O ANISOU 5547 O GLU C 108 4817 3663 4304 -9 689 -93 O ATOM 5548 CB GLU C 108 27.191 65.246 39.629 1.00 50.95 C ANISOU 5548 CB GLU C 108 6971 5869 6519 -54 712 -140 C ATOM 5549 CG GLU C 108 27.703 64.072 40.456 1.00 66.02 C ANISOU 5549 CG GLU C 108 8850 7803 8433 -61 693 -157 C ATOM 5550 CD GLU C 108 28.144 64.476 41.865 1.00 77.90 C ANISOU 5550 CD GLU C 108 10329 9317 9951 -70 691 -174 C ATOM 5551 OE1 GLU C 108 27.785 65.584 42.323 1.00 79.28 O ANISOU 5551 OE1 GLU C 108 10509 9480 10132 -66 701 -171 O ATOM 5552 OE2 GLU C 108 28.855 63.679 42.515 1.00 81.83 O ANISOU 5552 OE2 GLU C 108 10803 9835 10454 -81 679 -191 O ATOM 5553 N LYS C 109 24.187 63.695 40.093 1.00 31.19 N ANISOU 5553 N LYS C 109 4466 3379 4006 -2 662 -110 N ATOM 5554 CA LYS C 109 23.317 62.624 39.631 1.00 26.16 C ANISOU 5554 CA LYS C 109 3834 2748 3360 15 643 -96 C ATOM 5555 C LYS C 109 21.851 62.889 39.946 1.00 24.10 C ANISOU 5555 C LYS C 109 3577 2481 3097 39 632 -78 C ATOM 5556 O LYS C 109 21.022 61.978 39.826 1.00 23.08 O ANISOU 5556 O LYS C 109 3448 2361 2963 55 613 -68 O ATOM 5557 CB LYS C 109 23.768 61.290 40.232 1.00 24.02 C ANISOU 5557 CB LYS C 109 3537 2501 3090 9 625 -113 C ATOM 5558 CG LYS C 109 25.161 60.894 39.763 1.00 30.64 C ANISOU 5558 CG LYS C 109 4370 3345 3927 -13 634 -128 C ATOM 5559 CD LYS C 109 25.662 59.603 40.390 1.00 36.46 C ANISOU 5559 CD LYS C 109 5080 4109 4666 -20 615 -145 C ATOM 5560 CE LYS C 109 27.090 59.327 39.930 1.00 43.24 C ANISOU 5560 CE LYS C 109 5933 4973 5524 -43 624 -160 C ATOM 5561 NZ LYS C 109 27.677 58.114 40.567 1.00 44.18 N ANISOU 5561 NZ LYS C 109 6023 5117 5645 -51 606 -177 N ATOM 5562 N ARG C 110 21.508 64.119 40.318 1.00 18.12 N ANISOU 5562 N ARG C 110 2827 1712 2347 42 643 -74 N ATOM 5563 CA ARG C 110 20.164 64.427 40.785 1.00 18.42 C ANISOU 5563 CA ARG C 110 2866 1746 2385 63 632 -59 C ATOM 5564 C ARG C 110 19.175 64.540 39.638 1.00 27.97 C ANISOU 5564 C ARG C 110 4101 2944 3583 81 628 -32 C ATOM 5565 O ARG C 110 19.395 65.287 38.677 1.00 34.19 O ANISOU 5565 O ARG C 110 4910 3715 4364 77 644 -23 O ATOM 5566 CB ARG C 110 20.163 65.717 41.601 1.00 24.39 C ANISOU 5566 CB ARG C 110 3619 2494 3152 59 644 -64 C ATOM 5567 CG ARG C 110 20.264 65.441 43.067 1.00 30.50 C ANISOU 5567 CG ARG C 110 4366 3286 3938 56 634 -82 C ATOM 5568 CD ARG C 110 20.388 66.677 43.905 1.00 25.06 C ANISOU 5568 CD ARG C 110 3672 2589 3260 50 647 -89 C ATOM 5569 NE ARG C 110 21.101 66.338 45.131 1.00 21.50 N ANISOU 5569 NE ARG C 110 3193 2155 2819 37 642 -112 N ATOM 5570 CZ ARG C 110 21.563 67.223 46.002 1.00 25.46 C ANISOU 5570 CZ ARG C 110 3686 2656 3333 26 652 -124 C ATOM 5571 NH1 ARG C 110 21.383 68.522 45.787 1.00 30.30 N ANISOU 5571 NH1 ARG C 110 4315 3250 3948 28 669 -116 N ATOM 5572 NH2 ARG C 110 22.196 66.805 47.090 1.00 24.93 N ANISOU 5572 NH2 ARG C 110 3593 2606 3274 15 644 -143 N ATOM 5573 N GLY C 111 18.078 63.793 39.751 1.00 17.26 N ANISOU 5573 N GLY C 111 2741 1596 2222 100 606 -19 N ATOM 5574 CA GLY C 111 16.929 63.973 38.891 1.00 14.14 C ANISOU 5574 CA GLY C 111 2364 1191 1815 120 598 8 C ATOM 5575 C GLY C 111 15.723 64.406 39.694 1.00 21.20 C ANISOU 5575 C GLY C 111 3252 2087 2714 138 587 17 C ATOM 5576 O GLY C 111 15.850 64.744 40.873 1.00 22.85 O ANISOU 5576 O GLY C 111 3445 2301 2935 133 589 2 O ATOM 5577 N LYS C 112 14.540 64.356 39.107 1.00 17.35 N ANISOU 5577 N LYS C 112 2775 1598 2217 158 573 41 N ATOM 5578 CA LYS C 112 13.399 65.001 39.737 1.00 21.44 C ANISOU 5578 CA LYS C 112 3291 2116 2739 173 566 51 C ATOM 5579 C LYS C 112 12.525 64.070 40.566 1.00 16.65 C ANISOU 5579 C LYS C 112 2665 1527 2135 188 541 52 C ATOM 5580 O LYS C 112 11.582 64.550 41.204 1.00 16.24 O ANISOU 5580 O LYS C 112 2608 1476 2087 200 534 59 O ATOM 5581 CB LYS C 112 12.551 65.702 38.669 1.00 29.53 C ANISOU 5581 CB LYS C 112 4337 3130 3753 187 565 75 C ATOM 5582 CG LYS C 112 11.927 64.797 37.631 1.00 40.83 C ANISOU 5582 CG LYS C 112 5775 4568 5169 200 547 95 C ATOM 5583 CD LYS C 112 11.207 65.639 36.573 1.00 50.74 C ANISOU 5583 CD LYS C 112 7051 5814 6413 211 549 116 C ATOM 5584 CE LYS C 112 10.699 64.795 35.416 1.00 59.22 C ANISOU 5584 CE LYS C 112 8132 6897 7471 221 532 134 C ATOM 5585 NZ LYS C 112 9.967 65.606 34.399 1.00 64.29 N ANISOU 5585 NZ LYS C 112 8792 7532 8103 232 532 153 N ATOM 5586 N TYR C 113 12.820 62.772 40.625 1.00 9.62 N ANISOU 5586 N TYR C 113 1762 650 1241 186 528 46 N ATOM 5587 CA TYR C 113 11.883 61.841 41.234 1.00 9.38 C ANISOU 5587 CA TYR C 113 1712 644 1210 200 501 51 C ATOM 5588 C TYR C 113 12.351 61.397 42.609 1.00 13.49 C ANISOU 5588 C TYR C 113 2205 1181 1741 190 496 28 C ATOM 5589 O TYR C 113 13.552 61.345 42.897 1.00 16.57 O ANISOU 5589 O TYR C 113 2588 1571 2137 171 509 7 O ATOM 5590 CB TYR C 113 11.667 60.617 40.341 1.00 8.90 C ANISOU 5590 CB TYR C 113 1648 599 1133 204 481 63 C ATOM 5591 CG TYR C 113 10.903 60.970 39.082 1.00 16.89 C ANISOU 5591 CG TYR C 113 2685 1598 2133 219 480 89 C ATOM 5592 CD1 TYR C 113 9.537 61.239 39.129 1.00 13.19 C ANISOU 5592 CD1 TYR C 113 2221 1128 1663 241 468 107 C ATOM 5593 CD2 TYR C 113 11.546 61.057 37.856 1.00 14.04 C ANISOU 5593 CD2 TYR C 113 2343 1227 1764 211 492 94 C ATOM 5594 CE1 TYR C 113 8.838 61.578 37.991 1.00 16.55 C ANISOU 5594 CE1 TYR C 113 2664 1549 2077 252 464 129 C ATOM 5595 CE2 TYR C 113 10.848 61.380 36.715 1.00 16.68 C ANISOU 5595 CE2 TYR C 113 2700 1551 2088 224 490 117 C ATOM 5596 CZ TYR C 113 9.497 61.644 36.792 1.00 18.33 C ANISOU 5596 CZ TYR C 113 2907 1765 2293 243 474 134 C ATOM 5597 OH TYR C 113 8.804 61.982 35.659 1.00 19.17 O ANISOU 5597 OH TYR C 113 3027 1869 2385 253 469 154 O ATOM 5598 N VAL C 114 11.375 61.085 43.456 1.00 12.34 N ANISOU 5598 N VAL C 114 2044 1047 1598 204 478 31 N ATOM 5599 CA VAL C 114 11.596 60.521 44.780 1.00 8.80 C ANISOU 5599 CA VAL C 114 1568 617 1157 198 469 12 C ATOM 5600 C VAL C 114 11.074 59.090 44.739 1.00 12.91 C ANISOU 5600 C VAL C 114 2071 1163 1669 206 440 19 C ATOM 5601 O VAL C 114 9.955 58.858 44.271 1.00 13.15 O ANISOU 5601 O VAL C 114 2107 1197 1691 224 425 40 O ATOM 5602 CB VAL C 114 10.874 61.343 45.865 1.00 14.37 C ANISOU 5602 CB VAL C 114 2269 1316 1874 208 471 10 C ATOM 5603 CG1 VAL C 114 11.073 60.717 47.245 1.00 12.45 C ANISOU 5603 CG1 VAL C 114 1997 1093 1639 202 461 -9 C ATOM 5604 CG2 VAL C 114 11.337 62.832 45.852 1.00 9.80 C ANISOU 5604 CG2 VAL C 114 1707 712 1304 200 498 6 C ATOM 5605 N VAL C 115 11.876 58.129 45.195 1.00 12.57 N ANISOU 5605 N VAL C 115 2009 1140 1627 193 433 2 N ATOM 5606 CA VAL C 115 11.484 56.714 45.172 1.00 11.04 C ANISOU 5606 CA VAL C 115 1798 971 1425 199 407 6 C ATOM 5607 C VAL C 115 11.514 56.140 46.581 1.00 11.39 C ANISOU 5607 C VAL C 115 1816 1035 1478 196 395 -11 C ATOM 5608 O VAL C 115 12.543 56.213 47.261 1.00 12.84 O ANISOU 5608 O VAL C 115 1989 1219 1670 180 406 -33 O ATOM 5609 CB VAL C 115 12.376 55.861 44.250 1.00 9.63 C ANISOU 5609 CB VAL C 115 1621 800 1237 187 405 3 C ATOM 5610 CG1 VAL C 115 11.807 54.424 44.160 1.00 7.27 C ANISOU 5610 CG1 VAL C 115 1306 527 929 195 377 11 C ATOM 5611 CG2 VAL C 115 12.444 56.476 42.881 1.00 16.01 C ANISOU 5611 CG2 VAL C 115 2456 1589 2038 188 419 18 C ATOM 5612 N CYS C 116 10.395 55.540 46.998 1.00 10.36 N ANISOU 5612 N CYS C 116 1673 919 1344 212 373 0 N ATOM 5613 CA CYS C 116 10.302 54.757 48.225 1.00 11.39 C ANISOU 5613 CA CYS C 116 1777 1071 1480 211 357 -13 C ATOM 5614 C CYS C 116 10.143 53.292 47.841 1.00 11.70 C ANISOU 5614 C CYS C 116 1804 1132 1508 214 334 -7 C ATOM 5615 O CYS C 116 9.264 52.954 47.036 1.00 13.93 O ANISOU 5615 O CYS C 116 2095 1418 1781 228 321 13 O ATOM 5616 CB CYS C 116 9.104 55.183 49.077 1.00 8.97 C ANISOU 5616 CB CYS C 116 1466 765 1179 227 349 -6 C ATOM 5617 SG CYS C 116 8.959 56.985 49.299 1.00 15.93 S ANISOU 5617 SG CYS C 116 2366 1616 2071 230 375 -5 S ATOM 5618 N PHE C 117 10.969 52.426 48.422 1.00 10.22 N ANISOU 5618 N PHE C 117 1598 962 1323 201 328 -26 N ATOM 5619 CA PHE C 117 10.935 51.025 48.011 1.00 9.91 C ANISOU 5619 CA PHE C 117 1547 944 1274 202 307 -21 C ATOM 5620 C PHE C 117 11.255 50.101 49.174 1.00 12.25 C ANISOU 5620 C PHE C 117 1816 1262 1574 195 293 -39 C ATOM 5621 O PHE C 117 11.894 50.485 50.157 1.00 6.73 O ANISOU 5621 O PHE C 117 1109 562 887 185 303 -58 O ATOM 5622 CB PHE C 117 11.901 50.739 46.843 1.00 12.30 C ANISOU 5622 CB PHE C 117 1861 1244 1570 190 314 -23 C ATOM 5623 CG PHE C 117 13.357 51.028 47.145 1.00 10.53 C ANISOU 5623 CG PHE C 117 1634 1014 1353 168 333 -46 C ATOM 5624 CD1 PHE C 117 13.880 52.301 46.949 1.00 13.04 C ANISOU 5624 CD1 PHE C 117 1969 1309 1678 161 359 -51 C ATOM 5625 CD2 PHE C 117 14.212 50.016 47.572 1.00 14.42 C ANISOU 5625 CD2 PHE C 117 2108 1525 1847 155 325 -64 C ATOM 5626 CE1 PHE C 117 15.226 52.561 47.190 1.00 10.99 C ANISOU 5626 CE1 PHE C 117 1707 1043 1425 141 377 -73 C ATOM 5627 CE2 PHE C 117 15.556 50.266 47.827 1.00 8.01 C ANISOU 5627 CE2 PHE C 117 1292 708 1041 136 342 -87 C ATOM 5628 CZ PHE C 117 16.069 51.547 47.629 1.00 7.44 C ANISOU 5628 CZ PHE C 117 1237 613 976 128 369 -91 C ATOM 5629 N ASP C 118 10.761 48.864 49.052 1.00 13.92 N ANISOU 5629 N ASP C 118 2016 1495 1778 202 269 -31 N ATOM 5630 CA ASP C 118 11.129 47.763 49.935 1.00 18.17 C ANISOU 5630 CA ASP C 118 2530 2056 2319 196 254 -46 C ATOM 5631 C ASP C 118 11.899 46.756 49.082 1.00 11.44 C ANISOU 5631 C ASP C 118 1677 1214 1458 186 248 -49 C ATOM 5632 O ASP C 118 11.281 46.019 48.302 1.00 16.16 O ANISOU 5632 O ASP C 118 2275 1819 2044 196 232 -32 O ATOM 5633 CB ASP C 118 9.862 47.136 50.533 1.00 15.97 C ANISOU 5633 CB ASP C 118 2239 1793 2038 212 231 -35 C ATOM 5634 CG ASP C 118 10.118 46.358 51.814 1.00 20.14 C ANISOU 5634 CG ASP C 118 2741 2340 2570 207 219 -53 C ATOM 5635 OD1 ASP C 118 11.127 45.645 51.908 1.00 16.59 O ANISOU 5635 OD1 ASP C 118 2282 1901 2121 193 218 -68 O ATOM 5636 OD2 ASP C 118 9.311 46.504 52.757 1.00 27.18 O ANISOU 5636 OD2 ASP C 118 3624 3236 3467 216 212 -51 O ATOM 5637 N PRO C 119 13.232 46.683 49.183 1.00 13.25 N ANISOU 5637 N PRO C 119 1901 1442 1691 168 260 -69 N ATOM 5638 CA PRO C 119 14.003 45.969 48.149 1.00 11.47 C ANISOU 5638 CA PRO C 119 1680 1222 1458 158 258 -70 C ATOM 5639 C PRO C 119 13.785 44.466 48.151 1.00 12.21 C ANISOU 5639 C PRO C 119 1756 1340 1544 161 233 -67 C ATOM 5640 O PRO C 119 13.860 43.845 47.086 1.00 11.51 O ANISOU 5640 O PRO C 119 1673 1255 1444 162 226 -58 O ATOM 5641 CB PRO C 119 15.458 46.312 48.485 1.00 12.04 C ANISOU 5641 CB PRO C 119 1748 1288 1537 138 277 -94 C ATOM 5642 CG PRO C 119 15.440 46.661 49.938 1.00 12.33 C ANISOU 5642 CG PRO C 119 1771 1327 1585 136 279 -109 C ATOM 5643 CD PRO C 119 14.112 47.331 50.177 1.00 16.09 C ANISOU 5643 CD PRO C 119 2254 1796 2062 154 276 -92 C ATOM 5644 N LEU C 120 13.554 43.852 49.308 1.00 9.19 N ANISOU 5644 N LEU C 120 1352 974 1165 163 218 -76 N ATOM 5645 CA LEU C 120 13.250 42.429 49.353 1.00 13.02 C ANISOU 5645 CA LEU C 120 1822 1483 1644 167 193 -73 C ATOM 5646 C LEU C 120 12.218 42.195 50.451 1.00 16.47 C ANISOU 5646 C LEU C 120 2244 1930 2083 180 178 -69 C ATOM 5647 O LEU C 120 12.503 41.685 51.529 1.00 16.52 O ANISOU 5647 O LEU C 120 2232 1951 2095 175 170 -84 O ATOM 5648 CB LEU C 120 14.513 41.589 49.545 1.00 7.19 C ANISOU 5648 CB LEU C 120 1069 756 906 150 191 -93 C ATOM 5649 CG LEU C 120 14.359 40.118 49.126 1.00 11.28 C ANISOU 5649 CG LEU C 120 1576 1295 1414 153 168 -88 C ATOM 5650 CD1 LEU C 120 13.870 39.976 47.704 1.00 9.71 C ANISOU 5650 CD1 LEU C 120 1393 1092 1204 161 164 -67 C ATOM 5651 CD2 LEU C 120 15.714 39.472 49.275 1.00 10.38 C ANISOU 5651 CD2 LEU C 120 1451 1190 1302 135 170 -109 C ATOM 5652 N ASP C 121 10.997 42.614 50.163 1.00 13.88 N ANISOU 5652 N ASP C 121 1926 1597 1753 197 174 -49 N ATOM 5653 CA ASP C 121 9.883 42.413 51.077 1.00 13.83 C ANISOU 5653 CA ASP C 121 1907 1599 1747 210 159 -43 C ATOM 5654 C ASP C 121 9.668 40.931 51.332 1.00 16.85 C ANISOU 5654 C ASP C 121 2271 2007 2125 213 134 -43 C ATOM 5655 O ASP C 121 9.629 40.133 50.391 1.00 11.87 O ANISOU 5655 O ASP C 121 1642 1383 1484 214 123 -34 O ATOM 5656 CB ASP C 121 8.614 43.008 50.472 1.00 20.85 C ANISOU 5656 CB ASP C 121 2812 2478 2633 229 157 -19 C ATOM 5657 CG ASP C 121 7.571 43.330 51.519 1.00 30.66 C ANISOU 5657 CG ASP C 121 4046 3723 3881 241 151 -16 C ATOM 5658 OD1 ASP C 121 7.635 44.452 52.061 1.00 22.11 O ANISOU 5658 OD1 ASP C 121 2969 2625 2806 240 167 -22 O ATOM 5659 OD2 ASP C 121 6.700 42.471 51.790 1.00 25.33 O ANISOU 5659 OD2 ASP C 121 3360 3064 3202 252 129 -8 O ATOM 5660 N GLY C 122 9.470 40.576 52.601 1.00 13.16 N ANISOU 5660 N GLY C 122 1785 1552 1663 213 125 -53 N ATOM 5661 CA GLY C 122 9.227 39.211 52.991 1.00 16.69 C ANISOU 5661 CA GLY C 122 2213 2023 2106 216 101 -54 C ATOM 5662 C GLY C 122 10.464 38.398 53.266 1.00 19.83 C ANISOU 5662 C GLY C 122 2598 2432 2504 199 99 -74 C ATOM 5663 O GLY C 122 10.338 37.223 53.623 1.00 23.59 O ANISOU 5663 O GLY C 122 3058 2929 2977 200 80 -76 O ATOM 5664 N SER C 123 11.654 38.998 53.149 1.00 16.36 N ANISOU 5664 N SER C 123 2165 1982 2070 184 119 -89 N ATOM 5665 CA SER C 123 12.892 38.236 53.235 1.00 20.03 C ANISOU 5665 CA SER C 123 2619 2457 2535 168 117 -108 C ATOM 5666 C SER C 123 13.134 37.645 54.617 1.00 21.11 C ANISOU 5666 C SER C 123 2733 2609 2677 164 107 -125 C ATOM 5667 O SER C 123 13.927 36.705 54.733 1.00 24.04 O ANISOU 5667 O SER C 123 3092 2994 3047 154 99 -137 O ATOM 5668 CB SER C 123 14.071 39.129 52.846 1.00 25.16 C ANISOU 5668 CB SER C 123 3280 3089 3189 153 142 -121 C ATOM 5669 OG SER C 123 14.213 40.198 53.765 1.00 30.59 O ANISOU 5669 OG SER C 123 3969 3766 3888 150 158 -132 O ATOM 5670 N SER C 124 12.460 38.138 55.659 1.00 22.44 N ANISOU 5670 N SER C 124 2896 2777 2852 171 107 -125 N ATOM 5671 CA SER C 124 12.706 37.591 56.996 1.00 38.93 C ANISOU 5671 CA SER C 124 4964 4881 4946 167 98 -142 C ATOM 5672 C SER C 124 12.407 36.093 57.074 1.00 40.63 C ANISOU 5672 C SER C 124 5165 5119 5154 170 73 -138 C ATOM 5673 O SER C 124 12.942 35.411 57.956 1.00 36.81 O ANISOU 5673 O SER C 124 4664 4650 4673 163 65 -154 O ATOM 5674 CB SER C 124 11.885 38.343 58.049 1.00 39.58 C ANISOU 5674 CB SER C 124 5044 4959 5035 176 101 -141 C ATOM 5675 OG SER C 124 10.537 37.912 58.061 1.00 44.17 O ANISOU 5675 OG SER C 124 5622 5548 5611 192 84 -122 O ATOM 5676 N ASN C 125 11.578 35.564 56.170 1.00 40.75 N ANISOU 5676 N ASN C 125 5186 5139 5160 182 60 -118 N ATOM 5677 CA ASN C 125 11.282 34.137 56.108 1.00 38.09 C ANISOU 5677 CA ASN C 125 4835 4822 4815 185 36 -113 C ATOM 5678 C ASN C 125 11.825 33.486 54.840 1.00 33.46 C ANISOU 5678 C ASN C 125 4255 4238 4221 180 33 -108 C ATOM 5679 O ASN C 125 11.383 32.391 54.466 1.00 26.55 O ANISOU 5679 O ASN C 125 3373 3377 3338 186 14 -99 O ATOM 5680 CB ASN C 125 9.776 33.891 56.212 1.00 41.34 C ANISOU 5680 CB ASN C 125 5245 5240 5223 203 21 -93 C ATOM 5681 CG ASN C 125 9.209 34.299 57.555 1.00 52.12 C ANISOU 5681 CG ASN C 125 6601 6607 6596 209 20 -98 C ATOM 5682 OD1 ASN C 125 8.219 35.027 57.627 1.00 53.23 O ANISOU 5682 OD1 ASN C 125 6748 6739 6737 221 23 -85 O ATOM 5683 ND2 ASN C 125 9.834 33.829 58.632 1.00 53.61 N ANISOU 5683 ND2 ASN C 125 6773 6808 6789 200 16 -116 N ATOM 5684 N ILE C 126 12.791 34.127 54.176 1.00 21.89 N ANISOU 5684 N ILE C 126 2801 2758 2757 169 52 -116 N ATOM 5685 CA ILE C 126 13.297 33.576 52.930 1.00 27.23 C ANISOU 5685 CA ILE C 126 3484 3435 3425 164 50 -111 C ATOM 5686 C ILE C 126 14.028 32.263 53.164 1.00 23.30 C ANISOU 5686 C ILE C 126 2970 2958 2926 155 35 -124 C ATOM 5687 O ILE C 126 14.265 31.516 52.211 1.00 15.94 O ANISOU 5687 O ILE C 126 2039 2031 1986 153 28 -119 O ATOM 5688 CB ILE C 126 14.229 34.582 52.232 1.00 31.25 C ANISOU 5688 CB ILE C 126 4010 3925 3937 152 74 -118 C ATOM 5689 CG1 ILE C 126 14.241 34.353 50.719 1.00 25.49 C ANISOU 5689 CG1 ILE C 126 3295 3192 3199 154 74 -104 C ATOM 5690 CG2 ILE C 126 15.639 34.455 52.773 1.00 31.21 C ANISOU 5690 CG2 ILE C 126 3995 3923 3939 134 83 -144 C ATOM 5691 CD1 ILE C 126 14.964 35.454 49.955 1.00 19.66 C ANISOU 5691 CD1 ILE C 126 2575 2431 2462 145 99 -107 C ATOM 5692 N ASP C 127 14.400 31.965 54.413 1.00 18.94 N ANISOU 5692 N ASP C 127 2401 2416 2380 149 31 -141 N ATOM 5693 CA ASP C 127 15.044 30.694 54.712 1.00 19.77 C ANISOU 5693 CA ASP C 127 2489 2539 2482 141 16 -154 C ATOM 5694 C ASP C 127 14.109 29.502 54.483 1.00 22.37 C ANISOU 5694 C ASP C 127 2811 2886 2804 153 -9 -138 C ATOM 5695 O ASP C 127 14.587 28.368 54.396 1.00 22.74 O ANISOU 5695 O ASP C 127 2846 2947 2847 147 -23 -144 O ATOM 5696 CB ASP C 127 15.622 30.720 56.132 1.00 19.68 C ANISOU 5696 CB ASP C 127 2463 2534 2480 133 17 -175 C ATOM 5697 CG ASP C 127 14.652 31.226 57.151 1.00 32.37 C ANISOU 5697 CG ASP C 127 4066 4140 4091 144 16 -170 C ATOM 5698 OD1 ASP C 127 13.617 31.803 56.756 1.00 38.38 O ANISOU 5698 OD1 ASP C 127 4838 4892 4850 157 18 -152 O ATOM 5699 OD2 ASP C 127 14.926 31.052 58.359 1.00 44.81 O ANISOU 5699 OD2 ASP C 127 5628 5725 5673 140 12 -185 O ATOM 5700 N CYS C 128 12.792 29.719 54.414 1.00 17.54 N ANISOU 5700 N CYS C 128 2203 2272 2189 169 -16 -118 N ATOM 5701 CA CYS C 128 11.859 28.678 53.990 1.00 23.23 C ANISOU 5701 CA CYS C 128 2919 3006 2901 180 -38 -101 C ATOM 5702 C CYS C 128 11.425 28.841 52.528 1.00 18.64 C ANISOU 5702 C CYS C 128 2355 2416 2312 187 -36 -82 C ATOM 5703 O CYS C 128 10.452 28.205 52.106 1.00 13.27 O ANISOU 5703 O CYS C 128 1673 1744 1624 200 -52 -65 O ATOM 5704 CB CYS C 128 10.628 28.642 54.907 1.00 19.59 C ANISOU 5704 CB CYS C 128 2450 2551 2441 194 -49 -93 C ATOM 5705 SG CYS C 128 9.465 30.011 54.721 1.00 22.55 S ANISOU 5705 SG CYS C 128 2842 2909 2819 208 -37 -75 S ATOM 5706 N LEU C 129 12.115 29.698 51.766 1.00 21.96 N ANISOU 5706 N LEU C 129 2791 2820 2734 180 -16 -85 N ATOM 5707 CA LEU C 129 11.890 29.904 50.327 1.00 18.58 C ANISOU 5707 CA LEU C 129 2380 2382 2297 184 -12 -68 C ATOM 5708 C LEU C 129 10.502 30.468 50.030 1.00 17.43 C ANISOU 5708 C LEU C 129 2244 2228 2148 202 -14 -46 C ATOM 5709 O LEU C 129 9.975 30.324 48.925 1.00 15.12 O ANISOU 5709 O LEU C 129 1963 1934 1848 210 -19 -29 O ATOM 5710 CB LEU C 129 12.137 28.620 49.525 1.00 13.31 C ANISOU 5710 CB LEU C 129 1707 1729 1621 182 -28 -65 C ATOM 5711 CG LEU C 129 13.511 27.976 49.768 1.00 20.95 C ANISOU 5711 CG LEU C 129 2663 2705 2591 165 -28 -87 C ATOM 5712 CD1 LEU C 129 13.690 26.774 48.885 1.00 28.19 C ANISOU 5712 CD1 LEU C 129 3577 3635 3500 163 -43 -82 C ATOM 5713 CD2 LEU C 129 14.668 28.957 49.576 1.00 19.73 C ANISOU 5713 CD2 LEU C 129 2519 2534 2442 150 -3 -101 C ATOM 5714 N VAL C 130 9.919 31.180 50.990 1.00 15.32 N ANISOU 5714 N VAL C 130 1976 1957 1889 208 -10 -47 N ATOM 5715 CA VAL C 130 8.655 31.843 50.734 1.00 20.96 C ANISOU 5715 CA VAL C 130 2701 2662 2601 224 -10 -27 C ATOM 5716 C VAL C 130 8.832 32.825 49.578 1.00 15.09 C ANISOU 5716 C VAL C 130 1980 1898 1854 224 8 -18 C ATOM 5717 O VAL C 130 9.930 33.353 49.350 1.00 15.43 O ANISOU 5717 O VAL C 130 2031 1931 1902 210 26 -31 O ATOM 5718 CB VAL C 130 8.192 32.550 52.019 1.00 21.25 C ANISOU 5718 CB VAL C 130 2732 2695 2647 228 -5 -33 C ATOM 5719 CG1 VAL C 130 9.159 33.675 52.384 1.00 21.17 C ANISOU 5719 CG1 VAL C 130 2729 2670 2646 216 19 -49 C ATOM 5720 CG2 VAL C 130 6.780 33.056 51.892 1.00 15.52 C ANISOU 5720 CG2 VAL C 130 2013 1963 1918 247 -9 -13 C ATOM 5721 N SER C 131 7.762 33.036 48.808 1.00 15.04 N ANISOU 5721 N SER C 131 1985 1887 1843 239 3 3 N ATOM 5722 CA SER C 131 7.775 34.100 47.805 1.00 18.82 C ANISOU 5722 CA SER C 131 2487 2345 2319 241 21 13 C ATOM 5723 C SER C 131 8.243 35.389 48.455 1.00 15.00 C ANISOU 5723 C SER C 131 2010 1844 1846 234 43 1 C ATOM 5724 O SER C 131 7.851 35.698 49.575 1.00 15.87 O ANISOU 5724 O SER C 131 2111 1955 1963 238 43 -4 O ATOM 5725 CB SER C 131 6.380 34.329 47.221 1.00 17.91 C ANISOU 5725 CB SER C 131 2381 2225 2198 260 13 37 C ATOM 5726 OG SER C 131 5.881 33.190 46.566 1.00 27.44 O ANISOU 5726 OG SER C 131 3584 3448 3396 267 -7 49 O ATOM 5727 N VAL C 132 9.105 36.132 47.772 1.00 17.56 N ANISOU 5727 N VAL C 132 2525 2074 2072 -38 63 -29 N ATOM 5728 CA VAL C 132 9.480 37.466 48.229 1.00 12.77 C ANISOU 5728 CA VAL C 132 1939 1442 1471 -33 84 -31 C ATOM 5729 C VAL C 132 9.304 38.429 47.068 1.00 11.31 C ANISOU 5729 C VAL C 132 1753 1254 1292 -1 92 -18 C ATOM 5730 O VAL C 132 8.968 38.031 45.952 1.00 10.71 O ANISOU 5730 O VAL C 132 1660 1194 1216 15 81 -9 O ATOM 5731 CB VAL C 132 10.907 37.516 48.803 1.00 11.36 C ANISOU 5731 CB VAL C 132 1783 1241 1291 -58 81 -35 C ATOM 5732 CG1 VAL C 132 10.941 36.781 50.142 1.00 15.78 C ANISOU 5732 CG1 VAL C 132 2348 1803 1845 -87 78 -48 C ATOM 5733 CG2 VAL C 132 11.917 36.891 47.828 1.00 14.90 C ANISOU 5733 CG2 VAL C 132 2230 1692 1739 -62 61 -27 C ATOM 5734 N GLY C 133 9.494 39.720 47.350 1.00 13.18 N ANISOU 5734 N GLY C 133 2006 1468 1533 8 112 -18 N ATOM 5735 CA GLY C 133 9.238 40.700 46.312 1.00 11.30 C ANISOU 5735 CA GLY C 133 1767 1225 1301 39 121 -7 C ATOM 5736 C GLY C 133 9.905 42.031 46.585 1.00 13.79 C ANISOU 5736 C GLY C 133 2106 1512 1622 43 139 -6 C ATOM 5737 O GLY C 133 10.436 42.287 47.665 1.00 16.77 O ANISOU 5737 O GLY C 133 2501 1873 1999 24 146 -15 O ATOM 5738 N THR C 134 9.883 42.874 45.561 1.00 10.04 N ANISOU 5738 N THR C 134 1632 1031 1152 69 145 6 N ATOM 5739 CA THR C 134 10.344 44.254 45.630 1.00 14.69 C ANISOU 5739 CA THR C 134 2241 1593 1747 79 162 9 C ATOM 5740 C THR C 134 9.149 45.168 45.398 1.00 18.66 C ANISOU 5740 C THR C 134 2738 2098 2254 109 178 12 C ATOM 5741 O THR C 134 8.430 45.003 44.406 1.00 24.18 O ANISOU 5741 O THR C 134 3420 2814 2953 131 173 21 O ATOM 5742 CB THR C 134 11.413 44.521 44.567 1.00 17.03 C ANISOU 5742 CB THR C 134 2546 1879 2047 84 156 21 C ATOM 5743 OG1 THR C 134 12.514 43.617 44.751 1.00 18.61 O ANISOU 5743 OG1 THR C 134 2750 2078 2243 57 140 18 O ATOM 5744 CG2 THR C 134 11.888 45.963 44.635 1.00 13.10 C ANISOU 5744 CG2 THR C 134 2069 1353 1556 94 174 25 C ATOM 5745 N ILE C 135 8.940 46.130 46.297 1.00 12.87 N ANISOU 5745 N ILE C 135 2019 1348 1524 110 197 5 N ATOM 5746 CA ILE C 135 7.818 47.059 46.215 1.00 6.51 C ANISOU 5746 CA ILE C 135 1209 543 722 137 214 6 C ATOM 5747 C ILE C 135 8.365 48.461 45.993 1.00 15.02 C ANISOU 5747 C ILE C 135 2307 1592 1806 151 228 12 C ATOM 5748 O ILE C 135 9.354 48.845 46.620 1.00 12.92 O ANISOU 5748 O ILE C 135 2062 1305 1543 133 233 8 O ATOM 5749 CB ILE C 135 6.952 47.017 47.488 1.00 15.35 C ANISOU 5749 CB ILE C 135 2327 1667 1839 130 224 -8 C ATOM 5750 CG1 ILE C 135 6.557 45.579 47.813 1.00 16.31 C ANISOU 5750 CG1 ILE C 135 2429 1813 1953 112 209 -14 C ATOM 5751 CG2 ILE C 135 5.707 47.920 47.323 1.00 14.12 C ANISOU 5751 CG2 ILE C 135 2164 1515 1688 160 240 -7 C ATOM 5752 CD1 ILE C 135 5.833 45.419 49.160 1.00 14.02 C ANISOU 5752 CD1 ILE C 135 2138 1528 1660 99 219 -29 C ATOM 5753 N PHE C 136 7.721 49.235 45.121 1.00 12.38 N ANISOU 5753 N PHE C 136 1968 1259 1477 182 236 22 N ATOM 5754 CA PHE C 136 8.222 50.580 44.863 1.00 12.23 C ANISOU 5754 CA PHE C 136 1968 1213 1464 195 249 29 C ATOM 5755 C PHE C 136 7.081 51.564 44.625 1.00 10.10 C ANISOU 5755 C PHE C 136 1695 943 1198 227 264 31 C ATOM 5756 O PHE C 136 6.019 51.202 44.125 1.00 12.26 O ANISOU 5756 O PHE C 136 1948 1239 1471 245 261 33 O ATOM 5757 CB PHE C 136 9.196 50.594 43.671 1.00 7.59 C ANISOU 5757 CB PHE C 136 1386 620 879 199 239 43 C ATOM 5758 CG PHE C 136 8.582 50.143 42.364 1.00 9.82 C ANISOU 5758 CG PHE C 136 1647 924 1159 222 228 55 C ATOM 5759 CD1 PHE C 136 8.024 51.063 41.498 1.00 11.15 C ANISOU 5759 CD1 PHE C 136 1815 1090 1332 253 237 65 C ATOM 5760 CD2 PHE C 136 8.580 48.805 41.999 1.00 8.85 C ANISOU 5760 CD2 PHE C 136 1506 825 1030 211 209 55 C ATOM 5761 CE1 PHE C 136 7.463 50.662 40.280 1.00 14.63 C ANISOU 5761 CE1 PHE C 136 2238 1551 1771 274 226 75 C ATOM 5762 CE2 PHE C 136 8.046 48.402 40.773 1.00 8.31 C ANISOU 5762 CE2 PHE C 136 1420 777 960 232 198 65 C ATOM 5763 CZ PHE C 136 7.471 49.327 39.930 1.00 16.69 C ANISOU 5763 CZ PHE C 136 2480 1835 2025 264 207 75 C ATOM 5764 N GLY C 137 7.320 52.817 45.008 1.00 10.11 N ANISOU 5764 N GLY C 137 1716 918 1206 234 281 30 N ATOM 5765 CA GLY C 137 6.422 53.915 44.722 1.00 14.78 C ANISOU 5765 CA GLY C 137 2308 1505 1803 264 296 34 C ATOM 5766 C GLY C 137 7.228 55.121 44.288 1.00 17.24 C ANISOU 5766 C GLY C 137 2641 1788 2121 274 305 43 C ATOM 5767 O GLY C 137 8.276 55.407 44.875 1.00 9.64 O ANISOU 5767 O GLY C 137 1691 812 1159 249 304 40 O ATOM 5768 N ILE C 138 6.784 55.812 43.240 1.00 20.25 N ANISOU 5768 N ILE C 138 3016 2173 2506 301 306 55 N ATOM 5769 CA ILE C 138 7.568 56.865 42.603 1.00 18.91 C ANISOU 5769 CA ILE C 138 2852 1994 2339 301 305 66 C ATOM 5770 C ILE C 138 6.787 58.170 42.654 1.00 13.45 C ANISOU 5770 C ILE C 138 2162 1296 1652 322 318 67 C ATOM 5771 O ILE C 138 5.659 58.246 42.154 1.00 13.89 O ANISOU 5771 O ILE C 138 2207 1363 1709 349 321 70 O ATOM 5772 CB ILE C 138 7.932 56.481 41.161 1.00 15.78 C ANISOU 5772 CB ILE C 138 2446 1609 1941 310 292 82 C ATOM 5773 CG1 ILE C 138 8.790 55.208 41.172 1.00 10.65 C ANISOU 5773 CG1 ILE C 138 1795 964 1286 287 277 80 C ATOM 5774 CG2 ILE C 138 8.649 57.606 40.463 1.00 11.57 C ANISOU 5774 CG2 ILE C 138 1917 1067 1410 312 292 92 C ATOM 5775 CD1 ILE C 138 8.818 54.489 39.801 1.00 13.17 C ANISOU 5775 CD1 ILE C 138 2101 1300 1602 299 263 93 C ATOM 5776 N TYR C 139 7.389 59.199 43.246 1.00 11.95 N ANISOU 5776 N TYR C 139 1985 1089 1465 310 326 64 N ATOM 5777 CA TYR C 139 6.812 60.537 43.304 1.00 10.42 C ANISOU 5777 CA TYR C 139 1795 888 1277 328 337 65 C ATOM 5778 C TYR C 139 7.685 61.524 42.543 1.00 16.42 C ANISOU 5778 C TYR C 139 2561 1639 2039 327 335 77 C ATOM 5779 O TYR C 139 8.890 61.328 42.397 1.00 16.89 O ANISOU 5779 O TYR C 139 2625 1695 2099 307 327 80 O ATOM 5780 CB TYR C 139 6.686 61.041 44.750 1.00 9.69 C ANISOU 5780 CB TYR C 139 1713 782 1185 316 349 51 C ATOM 5781 CG TYR C 139 5.808 60.206 45.641 1.00 13.97 C ANISOU 5781 CG TYR C 139 2251 1333 1725 316 354 37 C ATOM 5782 CD1 TYR C 139 6.319 59.103 46.312 1.00 18.10 C ANISOU 5782 CD1 TYR C 139 2776 1858 2244 291 349 29 C ATOM 5783 CD2 TYR C 139 4.472 60.530 45.826 1.00 15.60 C ANISOU 5783 CD2 TYR C 139 2450 1545 1933 339 364 32 C ATOM 5784 CE1 TYR C 139 5.517 58.335 47.135 1.00 20.71 C ANISOU 5784 CE1 TYR C 139 3102 2196 2571 290 354 15 C ATOM 5785 CE2 TYR C 139 3.655 59.768 46.643 1.00 18.41 C ANISOU 5785 CE2 TYR C 139 2799 1911 2286 339 370 19 C ATOM 5786 CZ TYR C 139 4.186 58.674 47.296 1.00 15.13 C ANISOU 5786 CZ TYR C 139 2386 1496 1865 314 365 10 C ATOM 5787 OH TYR C 139 3.375 57.928 48.096 1.00 16.72 O ANISOU 5787 OH TYR C 139 2582 1708 2062 312 371 -4 O ATOM 5788 N ARG C 140 7.062 62.608 42.089 1.00 16.39 N ANISOU 5788 N ARG C 140 2557 1631 2039 349 342 82 N ATOM 5789 CA ARG C 140 7.800 63.793 41.675 1.00 18.88 C ANISOU 5789 CA ARG C 140 2881 1934 2358 348 343 90 C ATOM 5790 C ARG C 140 8.140 64.617 42.917 1.00 16.90 C ANISOU 5790 C ARG C 140 2644 1667 2111 334 352 79 C ATOM 5791 O ARG C 140 7.293 64.803 43.798 1.00 15.47 O ANISOU 5791 O ARG C 140 2464 1483 1931 340 362 69 O ATOM 5792 CB ARG C 140 6.955 64.606 40.693 1.00 25.65 C ANISOU 5792 CB ARG C 140 3733 2796 3218 377 346 99 C ATOM 5793 CG ARG C 140 7.579 65.871 40.105 1.00 40.40 C ANISOU 5793 CG ARG C 140 5609 4651 5090 379 347 108 C ATOM 5794 CD ARG C 140 8.962 65.702 39.518 1.00 52.45 C ANISOU 5794 CD ARG C 140 7137 6176 6615 361 338 116 C ATOM 5795 NE ARG C 140 9.405 66.932 38.848 1.00 55.60 N ANISOU 5795 NE ARG C 140 7543 6565 7017 367 341 124 N ATOM 5796 CZ ARG C 140 10.168 67.873 39.405 1.00 42.12 C ANISOU 5796 CZ ARG C 140 5847 4841 5314 354 345 121 C ATOM 5797 NH1 ARG C 140 10.590 67.738 40.657 1.00 26.70 N ANISOU 5797 NH1 ARG C 140 3901 2880 3362 334 348 110 N ATOM 5798 NH2 ARG C 140 10.518 68.947 38.701 1.00 34.09 N ANISOU 5798 NH2 ARG C 140 4836 3817 4302 361 347 130 N ATOM 5799 N LYS C 141 9.387 65.078 43.013 1.00 14.61 N ANISOU 5799 N LYS C 141 2363 1367 1823 314 350 81 N ATOM 5800 CA LYS C 141 9.744 65.958 44.120 1.00 16.22 C ANISOU 5800 CA LYS C 141 2579 1555 2030 302 357 72 C ATOM 5801 C LYS C 141 8.916 67.231 44.020 1.00 15.92 C ANISOU 5801 C LYS C 141 2544 1507 1996 325 368 74 C ATOM 5802 O LYS C 141 8.871 67.864 42.965 1.00 17.50 O ANISOU 5802 O LYS C 141 2743 1707 2199 340 366 86 O ATOM 5803 CB LYS C 141 11.237 66.287 44.088 1.00 19.90 C ANISOU 5803 CB LYS C 141 3050 2013 2498 279 351 75 C ATOM 5804 CG LYS C 141 11.709 67.233 45.211 1.00 21.15 C ANISOU 5804 CG LYS C 141 3221 2156 2660 266 358 66 C ATOM 5805 CD LYS C 141 13.187 67.603 44.992 1.00 19.45 C ANISOU 5805 CD LYS C 141 3009 1935 2448 247 350 70 C ATOM 5806 CE LYS C 141 13.761 68.569 46.044 1.00 23.78 C ANISOU 5806 CE LYS C 141 3566 2468 2999 234 355 62 C ATOM 5807 NZ LYS C 141 12.767 69.167 46.967 1.00 27.63 N ANISOU 5807 NZ LYS C 141 4062 2948 3489 244 366 54 N ATOM 5808 N LYS C 142 8.217 67.575 45.107 1.00 18.07 N ANISOU 5808 N LYS C 142 2822 1774 2271 328 377 63 N ATOM 5809 CA LYS C 142 7.232 68.651 45.069 1.00 25.34 C ANISOU 5809 CA LYS C 142 3743 2688 3195 352 387 63 C ATOM 5810 C LYS C 142 7.782 69.992 45.519 1.00 24.73 C ANISOU 5810 C LYS C 142 3680 2594 3124 347 392 62 C ATOM 5811 O LYS C 142 7.404 71.021 44.955 1.00 22.34 O ANISOU 5811 O LYS C 142 3380 2285 2825 365 396 68 O ATOM 5812 CB LYS C 142 6.021 68.314 45.945 1.00 29.84 C ANISOU 5812 CB LYS C 142 4310 3264 3764 361 395 51 C ATOM 5813 CG LYS C 142 4.752 67.977 45.170 1.00 43.80 C ANISOU 5813 CG LYS C 142 6064 5048 5532 389 395 55 C ATOM 5814 CD LYS C 142 3.629 68.985 45.443 1.00 48.19 C ANISOU 5814 CD LYS C 142 6620 5599 6091 412 405 50 C ATOM 5815 CE LYS C 142 3.783 70.253 44.601 1.00 59.28 C ANISOU 5815 CE LYS C 142 8029 6993 7500 425 405 61 C ATOM 5816 NZ LYS C 142 2.595 71.167 44.679 1.00 60.18 N ANISOU 5816 NZ LYS C 142 8141 7106 7618 450 413 58 N ATOM 5817 N SER C 143 8.709 70.017 46.461 1.00 20.28 N ANISOU 5817 N SER C 143 3124 2021 2560 322 392 54 N ATOM 5818 CA SER C 143 9.201 71.297 46.935 1.00 30.18 C ANISOU 5818 CA SER C 143 4390 3257 3818 317 396 52 C ATOM 5819 C SER C 143 10.481 71.647 46.184 1.00 26.08 C ANISOU 5819 C SER C 143 3873 2734 3301 306 388 62 C ATOM 5820 O SER C 143 11.166 70.777 45.642 1.00 19.86 O ANISOU 5820 O SER C 143 3079 1956 2510 294 379 67 O ATOM 5821 CB SER C 143 9.445 71.246 48.447 1.00 31.30 C ANISOU 5821 CB SER C 143 4540 3394 3960 298 400 38 C ATOM 5822 OG SER C 143 10.760 71.642 48.787 1.00 32.83 O ANISOU 5822 OG SER C 143 4740 3578 4155 276 395 37 O ATOM 5823 N THR C 144 10.791 72.942 46.142 1.00 22.15 N ANISOU 5823 N THR C 144 3385 2223 2810 310 392 65 N ATOM 5824 CA THR C 144 12.040 73.401 45.549 1.00 12.75 C ANISOU 5824 CA THR C 144 2197 1026 1622 298 385 73 C ATOM 5825 C THR C 144 13.159 73.491 46.570 1.00 18.64 C ANISOU 5825 C THR C 144 2948 1765 2369 271 382 65 C ATOM 5826 O THR C 144 14.270 73.898 46.218 1.00 24.21 O ANISOU 5826 O THR C 144 3655 2465 3078 260 376 70 O ATOM 5827 CB THR C 144 11.858 74.775 44.878 1.00 15.86 C ANISOU 5827 CB THR C 144 2596 1408 2021 316 389 82 C ATOM 5828 OG1 THR C 144 11.169 75.659 45.778 1.00 15.21 O ANISOU 5828 OG1 THR C 144 2522 1314 1943 325 399 73 O ATOM 5829 CG2 THR C 144 11.060 74.627 43.603 1.00 16.67 C ANISOU 5829 CG2 THR C 144 2691 1520 2123 340 389 93 C ATOM 5830 N ASP C 145 12.896 73.131 47.820 1.00 18.79 N ANISOU 5830 N ASP C 145 2970 1784 2386 261 385 52 N ATOM 5831 CA ASP C 145 13.956 73.143 48.815 1.00 26.32 C ANISOU 5831 CA ASP C 145 3927 2732 3340 236 381 43 C ATOM 5832 C ASP C 145 15.036 72.137 48.439 1.00 24.61 C ANISOU 5832 C ASP C 145 3703 2528 3121 216 369 46 C ATOM 5833 O ASP C 145 14.864 71.291 47.560 1.00 21.41 O ANISOU 5833 O ASP C 145 3289 2134 2712 221 365 53 O ATOM 5834 CB ASP C 145 13.409 72.836 50.211 1.00 26.42 C ANISOU 5834 CB ASP C 145 3944 2745 3350 229 387 29 C ATOM 5835 CG ASP C 145 12.314 73.795 50.634 1.00 34.02 C ANISOU 5835 CG ASP C 145 4914 3697 4316 249 399 25 C ATOM 5836 OD1 ASP C 145 12.224 74.909 50.067 1.00 32.61 O ANISOU 5836 OD1 ASP C 145 4739 3508 4143 264 402 32 O ATOM 5837 OD2 ASP C 145 11.545 73.433 51.547 1.00 41.57 O ANISOU 5837 OD2 ASP C 145 5870 4655 5269 250 405 14 O ATOM 5838 N GLU C 146 16.169 72.254 49.109 1.00 24.02 N ANISOU 5838 N GLU C 146 3630 2449 3047 193 363 41 N ATOM 5839 CA GLU C 146 17.210 71.255 48.961 1.00 24.40 C ANISOU 5839 CA GLU C 146 3670 2509 3093 173 351 41 C ATOM 5840 C GLU C 146 16.627 69.870 49.250 1.00 15.85 C ANISOU 5840 C GLU C 146 2580 1439 2002 169 349 36 C ATOM 5841 O GLU C 146 15.763 69.736 50.124 1.00 16.64 O ANISOU 5841 O GLU C 146 2684 1539 2100 172 356 27 O ATOM 5842 CB GLU C 146 18.376 71.573 49.901 1.00 31.87 C ANISOU 5842 CB GLU C 146 4618 3449 4041 150 345 34 C ATOM 5843 CG GLU C 146 19.095 72.873 49.536 1.00 42.05 C ANISOU 5843 CG GLU C 146 5913 4725 5339 152 345 40 C ATOM 5844 CD GLU C 146 19.652 72.845 48.124 1.00 50.73 C ANISOU 5844 CD GLU C 146 7006 5829 6440 156 340 53 C ATOM 5845 OE1 GLU C 146 20.279 71.829 47.750 1.00 55.50 O ANISOU 5845 OE1 GLU C 146 7601 6446 7041 144 330 54 O ATOM 5846 OE2 GLU C 146 19.429 73.823 47.377 1.00 52.86 O ANISOU 5846 OE2 GLU C 146 7281 6090 6715 172 345 61 O ATOM 5847 N PRO C 147 17.006 68.841 48.494 1.00 21.15 N ANISOU 5847 N PRO C 147 3242 2124 2670 163 340 41 N ATOM 5848 CA PRO C 147 16.408 67.519 48.720 1.00 18.65 C ANISOU 5848 CA PRO C 147 2920 1821 2347 160 338 37 C ATOM 5849 C PRO C 147 16.680 67.038 50.138 1.00 21.90 C ANISOU 5849 C PRO C 147 3333 2233 2755 139 335 23 C ATOM 5850 O PRO C 147 17.776 67.212 50.682 1.00 21.98 O ANISOU 5850 O PRO C 147 3342 2241 2766 120 329 19 O ATOM 5851 CB PRO C 147 17.095 66.625 47.679 1.00 21.53 C ANISOU 5851 CB PRO C 147 3274 2198 2710 154 326 44 C ATOM 5852 CG PRO C 147 18.378 67.336 47.331 1.00 19.94 C ANISOU 5852 CG PRO C 147 3073 1991 2513 144 320 49 C ATOM 5853 CD PRO C 147 18.052 68.818 47.457 1.00 18.47 C ANISOU 5853 CD PRO C 147 2897 1788 2333 158 330 51 C ATOM 5854 N SER C 148 15.657 66.437 50.736 1.00 18.96 N ANISOU 5854 N SER C 148 2961 1865 2378 143 341 16 N ATOM 5855 CA SER C 148 15.730 65.968 52.110 1.00 22.62 C ANISOU 5855 CA SER C 148 3426 2330 2837 125 341 3 C ATOM 5856 C SER C 148 14.678 64.889 52.295 1.00 20.31 C ANISOU 5856 C SER C 148 3130 2047 2539 130 344 -2 C ATOM 5857 O SER C 148 13.842 64.639 51.422 1.00 14.60 O ANISOU 5857 O SER C 148 2404 1328 1817 149 347 5 O ATOM 5858 CB SER C 148 15.509 67.104 53.114 1.00 22.27 C ANISOU 5858 CB SER C 148 3392 2272 2797 128 351 -4 C ATOM 5859 OG SER C 148 14.154 67.511 53.103 1.00 20.70 O ANISOU 5859 OG SER C 148 3198 2068 2599 150 364 -5 O ATOM 5860 N GLU C 149 14.704 64.294 53.480 1.00 16.47 N ANISOU 5860 N GLU C 149 2645 1565 2049 112 343 -13 N ATOM 5861 CA GLU C 149 13.761 63.244 53.836 1.00 13.73 C ANISOU 5861 CA GLU C 149 2295 1226 1695 113 345 -19 C ATOM 5862 C GLU C 149 12.306 63.688 53.665 1.00 20.77 C ANISOU 5862 C GLU C 149 3190 2113 2589 140 360 -20 C ATOM 5863 O GLU C 149 11.447 62.868 53.320 1.00 19.12 O ANISOU 5863 O GLU C 149 2975 1913 2377 150 362 -20 O ATOM 5864 CB GLU C 149 14.060 62.835 55.276 1.00 21.96 C ANISOU 5864 CB GLU C 149 3340 2271 2734 91 343 -32 C ATOM 5865 CG GLU C 149 13.358 61.648 55.779 1.00 29.91 C ANISOU 5865 CG GLU C 149 4343 3287 3733 84 343 -40 C ATOM 5866 CD GLU C 149 14.068 61.062 56.985 1.00 31.06 C ANISOU 5866 CD GLU C 149 4488 3440 3874 57 335 -49 C ATOM 5867 OE1 GLU C 149 15.290 60.764 56.894 1.00 18.78 O ANISOU 5867 OE1 GLU C 149 2927 1890 2318 40 321 -46 O ATOM 5868 OE2 GLU C 149 13.397 60.926 58.025 1.00 29.39 O ANISOU 5868 OE2 GLU C 149 4281 3228 3659 54 343 -59 O ATOM 5869 N LYS C 150 12.012 64.980 53.886 1.00 15.53 N ANISOU 5869 N LYS C 150 2534 1437 1931 153 370 -20 N ATOM 5870 CA LYS C 150 10.647 65.484 53.751 1.00 14.18 C ANISOU 5870 CA LYS C 150 2364 1263 1762 179 383 -21 C ATOM 5871 C LYS C 150 10.102 65.328 52.342 1.00 13.87 C ANISOU 5871 C LYS C 150 2317 1229 1724 202 382 -9 C ATOM 5872 O LYS C 150 8.877 65.342 52.153 1.00 14.54 O ANISOU 5872 O LYS C 150 2398 1317 1809 224 391 -10 O ATOM 5873 CB LYS C 150 10.565 66.972 54.134 1.00 25.56 C ANISOU 5873 CB LYS C 150 3815 2688 3209 189 392 -22 C ATOM 5874 CG LYS C 150 11.019 67.298 55.542 1.00 44.18 C ANISOU 5874 CG LYS C 150 6181 5041 5566 170 393 -34 C ATOM 5875 CD LYS C 150 10.168 66.556 56.573 1.00 59.70 C ANISOU 5875 CD LYS C 150 8146 7012 7526 166 400 -47 C ATOM 5876 CE LYS C 150 10.608 66.857 57.999 1.00 62.49 C ANISOU 5876 CE LYS C 150 8506 7360 7877 147 401 -58 C ATOM 5877 NZ LYS C 150 10.384 68.293 58.338 1.00 59.40 N ANISOU 5877 NZ LYS C 150 8123 6953 7491 160 410 -60 N ATOM 5878 N ASP C 151 10.968 65.206 51.341 1.00 15.32 N ANISOU 5878 N ASP C 151 2497 1415 1908 198 372 2 N ATOM 5879 CA ASP C 151 10.454 65.043 49.984 1.00 22.48 C ANISOU 5879 CA ASP C 151 3396 2328 2816 220 371 14 C ATOM 5880 C ASP C 151 9.728 63.723 49.800 1.00 22.34 C ANISOU 5880 C ASP C 151 3369 2324 2793 224 368 12 C ATOM 5881 O ASP C 151 8.897 63.606 48.892 1.00 21.97 O ANISOU 5881 O ASP C 151 3315 2285 2747 247 370 19 O ATOM 5882 CB ASP C 151 11.592 65.177 48.981 1.00 16.95 C ANISOU 5882 CB ASP C 151 2694 1628 2118 214 360 26 C ATOM 5883 CG ASP C 151 12.122 66.584 48.942 1.00 20.39 C ANISOU 5883 CG ASP C 151 3137 2050 2559 216 364 30 C ATOM 5884 OD1 ASP C 151 11.283 67.491 48.786 1.00 18.99 O ANISOU 5884 OD1 ASP C 151 2964 1866 2386 238 373 31 O ATOM 5885 OD2 ASP C 151 13.337 66.786 49.122 1.00 17.98 O ANISOU 5885 OD2 ASP C 151 2835 1741 2256 197 357 30 O ATOM 5886 N ALA C 152 9.977 62.756 50.670 1.00 14.61 N ANISOU 5886 N ALA C 152 2390 1351 1810 202 364 2 N ATOM 5887 CA ALA C 152 9.293 61.470 50.612 1.00 13.80 C ANISOU 5887 CA ALA C 152 2279 1261 1702 204 362 -2 C ATOM 5888 C ALA C 152 8.006 61.445 51.423 1.00 13.71 C ANISOU 5888 C ALA C 152 2267 1252 1689 215 375 -14 C ATOM 5889 O ALA C 152 7.294 60.442 51.392 1.00 19.48 O ANISOU 5889 O ALA C 152 2991 1995 2417 219 374 -18 O ATOM 5890 CB ALA C 152 10.235 60.354 51.089 1.00 11.89 C ANISOU 5890 CB ALA C 152 2037 1026 1455 173 350 -7 C ATOM 5891 N LEU C 153 7.693 62.506 52.170 1.00 18.31 N ANISOU 5891 N LEU C 153 2857 1824 2275 220 385 -20 N ATOM 5892 CA LEU C 153 6.489 62.510 53.001 1.00 18.58 C ANISOU 5892 CA LEU C 153 2890 1862 2308 230 398 -32 C ATOM 5893 C LEU C 153 5.281 63.016 52.210 1.00 22.21 C ANISOU 5893 C LEU C 153 3341 2326 2771 265 405 -27 C ATOM 5894 O LEU C 153 4.571 63.922 52.623 1.00 25.56 O ANISOU 5894 O LEU C 153 3768 2745 3199 279 416 -32 O ATOM 5895 CB LEU C 153 6.726 63.349 54.250 1.00 10.95 C ANISOU 5895 CB LEU C 153 1934 883 1342 219 405 -42 C ATOM 5896 CG LEU C 153 7.812 62.796 55.179 1.00 18.28 C ANISOU 5896 CG LEU C 153 2869 1811 2267 185 397 -48 C ATOM 5897 CD1 LEU C 153 7.972 63.709 56.366 1.00 21.47 C ANISOU 5897 CD1 LEU C 153 3283 2203 2671 177 404 -57 C ATOM 5898 CD2 LEU C 153 7.451 61.399 55.638 1.00 15.99 C ANISOU 5898 CD2 LEU C 153 2573 1534 1969 172 394 -57 C ATOM 5899 N GLN C 154 5.011 62.361 51.098 1.00 20.34 N ANISOU 5899 N GLN C 154 3094 2101 2534 278 399 -18 N ATOM 5900 CA GLN C 154 3.861 62.761 50.313 1.00 16.87 C ANISOU 5900 CA GLN C 154 2644 1670 2098 310 404 -13 C ATOM 5901 C GLN C 154 2.765 61.708 50.441 1.00 16.95 C ANISOU 5901 C GLN C 154 2639 1698 2103 320 407 -21 C ATOM 5902 O GLN C 154 3.063 60.514 50.554 1.00 16.21 O ANISOU 5902 O GLN C 154 2543 1613 2005 304 400 -25 O ATOM 5903 CB GLN C 154 4.219 62.917 48.827 1.00 16.66 C ANISOU 5903 CB GLN C 154 2613 1645 2074 323 395 5 C ATOM 5904 CG GLN C 154 5.304 63.941 48.525 1.00 12.03 C ANISOU 5904 CG GLN C 154 2038 1042 1491 316 392 14 C ATOM 5905 CD GLN C 154 5.471 64.178 47.030 1.00 17.54 C ANISOU 5905 CD GLN C 154 2730 1744 2191 332 384 31 C ATOM 5906 OE1 GLN C 154 4.487 64.283 46.301 1.00 19.33 O ANISOU 5906 OE1 GLN C 154 2946 1980 2419 358 386 35 O ATOM 5907 NE2 GLN C 154 6.722 64.257 46.567 1.00 10.92 N ANISOU 5907 NE2 GLN C 154 1898 900 1353 316 376 39 N ATOM 5908 N PRO C 155 1.496 62.104 50.408 1.00 18.50 N ANISOU 5908 N PRO C 155 2826 1903 2302 345 416 -25 N ATOM 5909 CA PRO C 155 0.423 61.104 50.423 1.00 19.46 C ANISOU 5909 CA PRO C 155 2929 2045 2418 355 418 -32 C ATOM 5910 C PRO C 155 0.429 60.308 49.134 1.00 10.96 C ANISOU 5910 C PRO C 155 1840 982 1341 366 406 -20 C ATOM 5911 O PRO C 155 0.852 60.795 48.082 1.00 16.82 O ANISOU 5911 O PRO C 155 2584 1720 2087 375 399 -5 O ATOM 5912 CB PRO C 155 -0.852 61.949 50.551 1.00 15.86 C ANISOU 5912 CB PRO C 155 2464 1595 1966 381 429 -36 C ATOM 5913 CG PRO C 155 -0.480 63.265 49.941 1.00 18.17 C ANISOU 5913 CG PRO C 155 2767 1873 2266 392 428 -25 C ATOM 5914 CD PRO C 155 0.970 63.479 50.330 1.00 21.67 C ANISOU 5914 CD PRO C 155 3229 2296 2708 365 424 -22 C ATOM 5915 N GLY C 156 -0.006 59.051 49.243 1.00 14.27 N ANISOU 5915 N GLY C 156 2247 1420 1755 362 404 -26 N ATOM 5916 CA GLY C 156 -0.011 58.146 48.105 1.00 15.46 C ANISOU 5916 CA GLY C 156 2381 1589 1903 367 388 -15 C ATOM 5917 C GLY C 156 -0.819 58.631 46.923 1.00 17.76 C ANISOU 5917 C GLY C 156 2661 1889 2200 403 388 -4 C ATOM 5918 O GLY C 156 -0.574 58.185 45.794 1.00 15.92 O ANISOU 5918 O GLY C 156 2419 1664 1965 409 375 9 O ATOM 5919 N ARG C 157 -1.808 59.503 47.161 1.00 12.82 N ANISOU 5919 N ARG C 157 2030 1264 1577 422 399 -8 N ATOM 5920 CA ARG C 157 -2.537 60.150 46.068 1.00 19.40 C ANISOU 5920 CA ARG C 157 2851 2105 2414 451 395 3 C ATOM 5921 C ARG C 157 -1.594 60.795 45.062 1.00 12.28 C ANISOU 5921 C ARG C 157 1961 1190 1516 452 387 19 C ATOM 5922 O ARG C 157 -1.956 60.971 43.894 1.00 18.22 O ANISOU 5922 O ARG C 157 2702 1951 2269 472 379 32 O ATOM 5923 CB ARG C 157 -3.483 61.223 46.610 1.00 23.75 C ANISOU 5923 CB ARG C 157 3401 2654 2970 466 408 -5 C ATOM 5924 CG ARG C 157 -4.743 60.714 47.311 1.00 44.12 C ANISOU 5924 CG ARG C 157 5963 5254 5547 474 416 -19 C ATOM 5925 CD ARG C 157 -5.731 59.997 46.380 1.00 48.14 C ANISOU 5925 CD ARG C 157 6446 5790 6056 495 408 -14 C ATOM 5926 NE ARG C 157 -6.826 59.359 47.120 1.00 44.38 N ANISOU 5926 NE ARG C 157 5952 5334 5576 497 416 -28 N ATOM 5927 CZ ARG C 157 -7.561 58.352 46.650 1.00 37.76 C ANISOU 5927 CZ ARG C 157 5089 4523 4735 504 407 -28 C ATOM 5928 NH1 ARG C 157 -7.322 57.874 45.434 1.00 26.31 N ANISOU 5928 NH1 ARG C 157 3631 3082 3285 511 392 -14 N ATOM 5929 NH2 ARG C 157 -8.534 57.815 47.391 1.00 29.65 N ANISOU 5929 NH2 ARG C 157 4044 3517 3705 500 412 -40 N ATOM 5930 N ASN C 158 -0.400 61.185 45.500 1.00 10.79 N ANISOU 5930 N ASN C 158 1792 980 1328 430 387 20 N ATOM 5931 CA ASN C 158 0.542 61.916 44.664 1.00 10.96 C ANISOU 5931 CA ASN C 158 1824 988 1352 429 381 35 C ATOM 5932 C ASN C 158 1.426 61.019 43.810 1.00 12.20 C ANISOU 5932 C ASN C 158 1980 1151 1506 418 367 45 C ATOM 5933 O ASN C 158 2.239 61.543 43.045 1.00 16.43 O ANISOU 5933 O ASN C 158 2523 1678 2043 416 361 57 O ATOM 5934 CB ASN C 158 1.435 62.813 45.541 1.00 11.87 C ANISOU 5934 CB ASN C 158 1960 1079 1469 409 388 30 C ATOM 5935 CG ASN C 158 0.688 64.011 46.104 1.00 19.68 C ANISOU 5935 CG ASN C 158 2953 2061 2463 423 400 24 C ATOM 5936 OD1 ASN C 158 -0.534 64.111 45.968 1.00 19.18 O ANISOU 5936 OD1 ASN C 158 2876 2010 2401 445 404 21 O ATOM 5937 ND2 ASN C 158 1.417 64.927 46.731 1.00 17.28 N ANISOU 5937 ND2 ASN C 158 2666 1737 2162 409 405 22 N ATOM 5938 N LEU C 159 1.291 59.693 43.908 1.00 17.00 N ANISOU 5938 N LEU C 159 2578 1772 2109 412 361 40 N ATOM 5939 CA LEU C 159 2.191 58.792 43.193 1.00 12.81 C ANISOU 5939 CA LEU C 159 2047 1245 1575 400 347 49 C ATOM 5940 C LEU C 159 2.077 58.986 41.681 1.00 14.85 C ANISOU 5940 C LEU C 159 2295 1513 1834 420 337 66 C ATOM 5941 O LEU C 159 0.998 59.233 41.136 1.00 11.17 O ANISOU 5941 O LEU C 159 1814 1060 1368 445 338 69 O ATOM 5942 CB LEU C 159 1.895 57.332 43.557 1.00 15.45 C ANISOU 5942 CB LEU C 159 2371 1596 1904 392 342 41 C ATOM 5943 CG LEU C 159 2.427 56.755 44.873 1.00 11.94 C ANISOU 5943 CG LEU C 159 1933 1148 1456 357 343 27 C ATOM 5944 CD1 LEU C 159 1.656 55.507 45.231 1.00 10.91 C ANISOU 5944 CD1 LEU C 159