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Diffstat (limited to 'plip/test/pdb/4rao.pdb')
| -rw-r--r-- | plip/test/pdb/4rao.pdb | 14899 |
1 files changed, 0 insertions, 14899 deletions
diff --git a/plip/test/pdb/4rao.pdb b/plip/test/pdb/4rao.pdb deleted file mode 100644 index 2a432be..0000000 --- a/plip/test/pdb/4rao.pdb +++ /dev/null @@ -1,14899 +0,0 @@ -HEADER TRANSFERASE/TRANSFERASE INHIBITOR 10-SEP-14 4RAO -TITLE AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND PHOSPHONATE -TITLE 2 GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM FALCIPARUM AND VIVAX 6- -TITLE 3 OXOPURINE PHOSPHORIBOSYLTRANSFERASES AND THEIR PRO-DRUGS AS -TITLE 4 ANTIMALARIAL AGENTS -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; -COMPND 3 CHAIN: A, B, C, D; -COMPND 4 SYNONYM: HGPRT, HGPRTASE; -COMPND 5 EC: 2.4.2.8; -COMPND 6 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: HPRT1, HPRT; -SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; -SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 -KEYWDS 6-OXOPURINE PHOSPHORIBOSYLTRANSFERASE, 9-[(N-PHOSPHONOETHYL-N- -KEYWDS 2 PHOSPHONOETHOXYETHYL)-2-AMINOETHYL]HYPOXANTHINE, CYTOPLASMIC, -KEYWDS 3 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX -EXPDTA X-RAY DIFFRACTION -AUTHOR D.T.KEOUGH,D.HOCKOV,Z.JANEBA,T-H.WANG,L.NAESENS,M.D.EDSTEIN, -AUTHOR 2 M.CHAVCHICH,L.W.GUDDAT -REVDAT 1 07-JAN-15 4RAO 0 -JRNL AUTH D.T.KEOUGH,D.HOCKOVA,Z.JANEBA,T.WANG,L.NAESENS,M.D.EDSTEIN, -JRNL AUTH 2 M.CHAVCHICH,L.W.GUDDAT -JRNL TITL AZA-ACYCLIC NUCLEOSIDE PHOSPHONATES CONTAINING A SECOND -JRNL TITL 2 PHOSPHONATE GROUP AS INHIBITORS OF THE HUMAN, PLASMODIUM -JRNL TITL 3 FALCIPARUM AND VIVAX 6-OXOPURINE PHOSPHORIBOSYLTRANSFERASES -JRNL TITL 4 AND THEIR PRODRUGS AS ANTIMALARIAL AGENTS. -JRNL REF J.MED.CHEM. 2014 -JRNL REFN ISSN 0022-2623 -JRNL PMID 25494538 -JRNL DOI 10.1021/JM501416T -REMARK 2 -REMARK 2 RESOLUTION. 1.87 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309) -REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN -REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- -REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, -REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL -REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE -REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM -REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, -REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER -REMARK 3 : ZWART -REMARK 3 -REMARK 3 REFINEMENT TARGET : MLHL -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.41 -REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 -REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 -REMARK 3 NUMBER OF REFLECTIONS : 68117 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 -REMARK 3 R VALUE (WORKING SET) : 0.201 -REMARK 3 FREE R VALUE : 0.230 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.940 -REMARK 3 FREE R VALUE TEST SET COUNT : 2000 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). -REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE -REMARK 3 1 35.4134 - 4.5060 0.99 4936 149 0.1807 0.2057 -REMARK 3 2 4.5060 - 3.5776 1.00 4836 146 0.1615 0.1763 -REMARK 3 3 3.5776 - 3.1257 1.00 4767 145 0.1953 0.2231 -REMARK 3 4 3.1257 - 2.8400 1.00 4737 143 0.2116 0.2582 -REMARK 3 5 2.8400 - 2.6365 1.00 4706 143 0.2255 0.2502 -REMARK 3 6 2.6365 - 2.4811 1.00 4727 142 0.2233 0.2280 -REMARK 3 7 2.4811 - 2.3569 1.00 4713 143 0.2191 0.2645 -REMARK 3 8 2.3569 - 2.2543 1.00 4684 142 0.2253 0.2528 -REMARK 3 9 2.2543 - 2.1676 1.00 4694 142 0.2235 0.2826 -REMARK 3 10 2.1676 - 2.0928 1.00 4710 142 0.2168 0.2730 -REMARK 3 11 2.0928 - 2.0273 1.00 4653 141 0.2352 0.2856 -REMARK 3 12 2.0273 - 1.9694 1.00 4654 141 0.2295 0.2647 -REMARK 3 13 1.9694 - 1.9176 1.00 4669 141 0.2360 0.2575 -REMARK 3 14 1.9176 - 1.8710 0.99 4631 140 0.2623 0.2810 -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) : 0.190 -REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : NULL -REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : NULL -REMARK 3 B22 (A**2) : NULL -REMARK 3 B33 (A**2) : NULL -REMARK 3 B12 (A**2) : NULL -REMARK 3 B13 (A**2) : NULL -REMARK 3 B23 (A**2) : NULL -REMARK 3 -REMARK 3 TWINNING INFORMATION. -REMARK 3 FRACTION: NULL -REMARK 3 OPERATOR: NULL -REMARK 3 -REMARK 3 DEVIATIONS FROM IDEAL VALUES. -REMARK 3 RMSD COUNT -REMARK 3 BOND : 0.007 6832 -REMARK 3 ANGLE : 1.222 9287 -REMARK 3 CHIRALITY : 0.078 1037 -REMARK 3 PLANARITY : 0.004 1170 -REMARK 3 DIHEDRAL : 15.853 2652 -REMARK 3 -REMARK 3 TLS DETAILS -REMARK 3 NUMBER OF TLS GROUPS : 31 -REMARK 3 TLS GROUP : 1 -REMARK 3 SELECTION: chain 'A' and (resid 1 through 24 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 18.4722 2.5508 -3.4232 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2761 T22: 0.3888 -REMARK 3 T33: 0.1914 T12: -0.0331 -REMARK 3 T13: 0.0513 T23: -0.0546 -REMARK 3 L TENSOR -REMARK 3 L11: 5.9643 L22: 4.4104 -REMARK 3 L33: 1.8046 L12: -1.1905 -REMARK 3 L13: 1.0296 L23: -1.2136 -REMARK 3 S TENSOR -REMARK 3 S11: 0.3593 S12: 0.5049 S13: -0.0274 -REMARK 3 S21: -0.2290 S22: -0.3701 S23: -0.2974 -REMARK 3 S31: 0.0652 S32: 0.6322 S33: -0.0160 -REMARK 3 TLS GROUP : 2 -REMARK 3 SELECTION: chain 'A' and (resid 25 through 37 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 15.5740 15.0112 -2.1731 -REMARK 3 T TENSOR -REMARK 3 T11: 0.5345 T22: 0.3390 -REMARK 3 T33: 0.2732 T12: -0.1146 -REMARK 3 T13: 0.0131 T23: 0.0711 -REMARK 3 L TENSOR -REMARK 3 L11: 6.3478 L22: 9.3251 -REMARK 3 L33: 5.4894 L12: -1.6751 -REMARK 3 L13: -1.3368 L23: 2.9191 -REMARK 3 S TENSOR -REMARK 3 S11: 0.1374 S12: 0.4752 S13: 0.8809 -REMARK 3 S21: -0.2252 S22: 0.0174 S23: -0.9703 -REMARK 3 S31: -1.4878 S32: 0.5679 S33: -0.1024 -REMARK 3 TLS GROUP : 3 -REMARK 3 SELECTION: chain 'A' and (resid 38 through 86 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 12.0299 -4.8692 13.7308 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1921 T22: 0.2423 -REMARK 3 T33: 0.1793 T12: 0.0057 -REMARK 3 T13: 0.0041 T23: -0.0143 -REMARK 3 L TENSOR -REMARK 3 L11: 1.8229 L22: 3.0929 -REMARK 3 L33: 2.8758 L12: 1.0899 -REMARK 3 L13: 0.2587 L23: -0.0075 -REMARK 3 S TENSOR -REMARK 3 S11: 0.1555 S12: -0.0781 S13: 0.0165 -REMARK 3 S21: 0.1337 S22: -0.1202 S23: 0.0458 -REMARK 3 S31: 0.0627 S32: 0.1012 S33: -0.0399 -REMARK 3 TLS GROUP : 4 -REMARK 3 SELECTION: chain 'A' and (resid 87 through 100 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 10.8742 -4.6966 22.3544 -REMARK 3 T TENSOR -REMARK 3 T11: 0.4573 T22: 0.3327 -REMARK 3 T33: 0.2715 T12: -0.0363 -REMARK 3 T13: 0.0154 T23: -0.0229 -REMARK 3 L TENSOR -REMARK 3 L11: 9.3739 L22: 4.9720 -REMARK 3 L33: 0.0627 L12: 6.7926 -REMARK 3 L13: 0.7814 L23: 0.4067 -REMARK 3 S TENSOR -REMARK 3 S11: -0.1087 S12: 0.0667 S13: -0.3674 -REMARK 3 S21: -0.4185 S22: 0.1934 S23: -0.1040 -REMARK 3 S31: 0.0179 S32: 0.2954 S33: -0.0951 -REMARK 3 TLS GROUP : 5 -REMARK 3 SELECTION: chain 'A' and (resid 101 through 152 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 25.3619 -1.1903 21.8612 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2424 T22: 0.3030 -REMARK 3 T33: 0.1570 T12: -0.0124 -REMARK 3 T13: -0.0384 T23: -0.0567 -REMARK 3 L TENSOR -REMARK 3 L11: 2.9774 L22: 3.5114 -REMARK 3 L33: 8.1942 L12: 0.2834 -REMARK 3 L13: 2.3189 L23: -2.3631 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0385 S12: 0.0995 S13: 0.1632 -REMARK 3 S21: 0.0202 S22: -0.0321 S23: -0.3284 -REMARK 3 S31: 0.0388 S32: 0.4188 S33: 0.0812 -REMARK 3 TLS GROUP : 6 -REMARK 3 SELECTION: chain 'A' and (resid 153 through 216 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 23.1693 6.2682 7.3597 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2550 T22: 0.4224 -REMARK 3 T33: 0.2827 T12: -0.0986 -REMARK 3 T13: 0.0189 T23: -0.0221 -REMARK 3 L TENSOR -REMARK 3 L11: 2.0134 L22: 3.7565 -REMARK 3 L33: 3.6492 L12: -0.4347 -REMARK 3 L13: 0.0531 L23: -0.8514 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0897 S12: 0.0177 S13: 0.2839 -REMARK 3 S21: 0.0164 S22: -0.1132 S23: -0.6065 -REMARK 3 S31: -0.3736 S32: 0.7221 S33: 0.0633 -REMARK 3 TLS GROUP : 7 -REMARK 3 SELECTION: chain 'B' and (resid 4 through 37 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 11.7905 -9.3190 -7.9593 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2025 T22: 0.3236 -REMARK 3 T33: 0.2550 T12: 0.0481 -REMARK 3 T13: 0.0364 T23: -0.0647 -REMARK 3 L TENSOR -REMARK 3 L11: 3.6287 L22: 3.1423 -REMARK 3 L33: 3.0007 L12: 1.0484 -REMARK 3 L13: 0.3472 L23: -1.0446 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0960 S12: 0.3007 S13: -0.3171 -REMARK 3 S21: -0.1329 S22: -0.0124 S23: -0.3755 -REMARK 3 S31: 0.1412 S32: 0.4958 S33: -0.0539 -REMARK 3 TLS GROUP : 8 -REMARK 3 SELECTION: chain 'B' and (resid 38 through 56 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 0.1620 9.1215 -7.3183 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2348 T22: 0.2147 -REMARK 3 T33: 0.2739 T12: -0.0059 -REMARK 3 T13: -0.0091 T23: 0.0469 -REMARK 3 L TENSOR -REMARK 3 L11: 3.0545 L22: 6.2816 -REMARK 3 L33: 7.7011 L12: -4.0601 -REMARK 3 L13: 2.7727 L23: -2.8739 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0759 S12: -0.0991 S13: 0.3418 -REMARK 3 S21: -0.0425 S22: 0.2800 S23: 0.2201 -REMARK 3 S31: -0.6067 S32: -0.3073 S33: -0.1197 -REMARK 3 TLS GROUP : 9 -REMARK 3 SELECTION: chain 'B' and (resid 57 through 87 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -9.0721 5.0697 -6.7935 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1976 T22: 0.1806 -REMARK 3 T33: 0.2866 T12: 0.0082 -REMARK 3 T13: -0.0307 T23: 0.0345 -REMARK 3 L TENSOR -REMARK 3 L11: 2.2939 L22: 3.1853 -REMARK 3 L33: 4.5097 L12: 0.4367 -REMARK 3 L13: -0.1908 L23: 0.9722 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0591 S12: 0.0989 S13: 0.3597 -REMARK 3 S21: -0.1435 S22: -0.0041 S23: 0.5650 -REMARK 3 S31: -0.4725 S32: -0.0689 S33: -0.0009 -REMARK 3 TLS GROUP : 10 -REMARK 3 SELECTION: chain 'B' and (resid 88 through 100 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -13.6201 5.4722 -8.7300 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3285 T22: 0.2809 -REMARK 3 T33: 0.4418 T12: 0.0033 -REMARK 3 T13: -0.0756 T23: 0.0819 -REMARK 3 L TENSOR -REMARK 3 L11: 4.7080 L22: 6.5543 -REMARK 3 L33: 9.0136 L12: -0.2897 -REMARK 3 L13: 0.5454 L23: 2.9229 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0167 S12: 0.1832 S13: 0.6399 -REMARK 3 S21: 0.1989 S22: -0.1656 S23: 0.1336 -REMARK 3 S31: -0.4471 S32: -0.2982 S33: 0.0286 -REMARK 3 TLS GROUP : 11 -REMARK 3 SELECTION: chain 'B' and (resid 101 through 127 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -19.4581 1.0517 -17.8888 -REMARK 3 T TENSOR -REMARK 3 T11: 0.4451 T22: 0.5360 -REMARK 3 T33: 0.7020 T12: -0.0544 -REMARK 3 T13: -0.1737 T23: 0.0758 -REMARK 3 L TENSOR -REMARK 3 L11: 5.6249 L22: 4.2114 -REMARK 3 L33: 4.7536 L12: -2.4673 -REMARK 3 L13: -1.0265 L23: -1.0321 -REMARK 3 S TENSOR -REMARK 3 S11: 0.3066 S12: 0.1490 S13: -0.3129 -REMARK 3 S21: 0.3123 S22: 0.3331 S23: 1.8742 -REMARK 3 S31: 0.5098 S32: -1.0567 S33: -0.4721 -REMARK 3 TLS GROUP : 12 -REMARK 3 SELECTION: chain 'B' and (resid 128 through 165 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -8.0289 2.8212 -20.8366 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3105 T22: 0.2046 -REMARK 3 T33: 0.2996 T12: -0.0078 -REMARK 3 T13: -0.1292 T23: 0.0576 -REMARK 3 L TENSOR -REMARK 3 L11: 7.4033 L22: 3.3607 -REMARK 3 L33: 3.1928 L12: -3.0711 -REMARK 3 L13: -0.1955 L23: -0.2494 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0449 S12: 0.2226 S13: -0.2503 -REMARK 3 S21: -0.4713 S22: 0.0433 S23: 0.6805 -REMARK 3 S31: -0.1652 S32: 0.0517 S33: -0.0899 -REMARK 3 TLS GROUP : 13 -REMARK 3 SELECTION: chain 'B' and (resid 166 through 179 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 1.7217 3.5405 -22.9572 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3020 T22: 0.2842 -REMARK 3 T33: 0.2183 T12: -0.0475 -REMARK 3 T13: -0.0280 T23: 0.0484 -REMARK 3 L TENSOR -REMARK 3 L11: 1.8428 L22: 3.4867 -REMARK 3 L33: 2.6575 L12: -2.1537 -REMARK 3 L13: -1.8438 L23: 1.4901 -REMARK 3 S TENSOR -REMARK 3 S11: -0.1121 S12: 0.2952 S13: 0.1938 -REMARK 3 S21: -0.1234 S22: 0.1184 S23: 0.0988 -REMARK 3 S31: -0.1890 S32: 0.0746 S33: 0.0474 -REMARK 3 TLS GROUP : 14 -REMARK 3 SELECTION: chain 'B' and (resid 180 through 217 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 3.7454 -13.7514 -12.7741 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2674 T22: 0.2860 -REMARK 3 T33: 0.2342 T12: 0.0261 -REMARK 3 T13: 0.0026 T23: -0.0712 -REMARK 3 L TENSOR -REMARK 3 L11: 3.6259 L22: 6.6450 -REMARK 3 L33: 3.8025 L12: 1.7450 -REMARK 3 L13: 0.3382 L23: -0.8431 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0850 S12: 0.4215 S13: -0.4131 -REMARK 3 S21: -0.4885 S22: 0.1456 S23: -0.0432 -REMARK 3 S31: 0.5445 S32: 0.0073 S33: -0.0711 -REMARK 3 TLS GROUP : 15 -REMARK 3 SELECTION: chain 'C' and (resid 4 through 17 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -14.8002 5.2641 25.7419 -REMARK 3 T TENSOR -REMARK 3 T11: 0.4519 T22: 0.5025 -REMARK 3 T33: 0.5261 T12: -0.1123 -REMARK 3 T13: 0.2360 T23: -0.1521 -REMARK 3 L TENSOR -REMARK 3 L11: 2.4939 L22: 0.2716 -REMARK 3 L33: 4.0367 L12: -0.7858 -REMARK 3 L13: -1.2106 L23: 0.1507 -REMARK 3 S TENSOR -REMARK 3 S11: 0.2196 S12: -0.1074 S13: -0.3731 -REMARK 3 S21: 1.2339 S22: -0.6445 S23: 1.0583 -REMARK 3 S31: -0.1297 S32: -0.6932 S33: 0.3067 -REMARK 3 TLS GROUP : 16 -REMARK 3 SELECTION: chain 'C' and (resid 18 through 37 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -6.2078 -8.0140 25.2309 -REMARK 3 T TENSOR -REMARK 3 T11: 0.4199 T22: 0.2999 -REMARK 3 T33: 0.3372 T12: -0.1174 -REMARK 3 T13: 0.0404 T23: 0.0325 -REMARK 3 L TENSOR -REMARK 3 L11: 4.5958 L22: 2.0855 -REMARK 3 L33: 5.3145 L12: 1.4540 -REMARK 3 L13: 1.9488 L23: 0.0979 -REMARK 3 S TENSOR -REMARK 3 S11: 0.4184 S12: -0.3626 S13: -0.5220 -REMARK 3 S21: 0.4671 S22: -0.1381 S23: 0.1603 -REMARK 3 S31: 0.6002 S32: -0.2884 S33: -0.2772 -REMARK 3 TLS GROUP : 17 -REMARK 3 SELECTION: chain 'C' and (resid 38 through 56 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -4.5354 14.3474 13.8291 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3400 T22: 0.2063 -REMARK 3 T33: 0.3313 T12: -0.0001 -REMARK 3 T13: 0.1224 T23: -0.0235 -REMARK 3 L TENSOR -REMARK 3 L11: 5.7932 L22: 6.3044 -REMARK 3 L33: 3.8763 L12: 4.2064 -REMARK 3 L13: 0.0905 L23: -0.0663 -REMARK 3 S TENSOR -REMARK 3 S11: 0.1031 S12: 0.0624 S13: 0.7132 -REMARK 3 S21: -0.5421 S22: 0.0949 S23: 0.1644 -REMARK 3 S31: -0.6505 S32: -0.1254 S33: -0.1066 -REMARK 3 TLS GROUP : 18 -REMARK 3 SELECTION: chain 'C' and (resid 57 through 85 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 6.0027 13.8690 15.5492 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3351 T22: 0.2157 -REMARK 3 T33: 0.2640 T12: -0.1063 -REMARK 3 T13: 0.0809 T23: -0.0342 -REMARK 3 L TENSOR -REMARK 3 L11: 4.6491 L22: 0.5365 -REMARK 3 L33: 3.0010 L12: -0.6665 -REMARK 3 L13: 1.3498 L23: 0.8748 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0577 S12: 0.0339 S13: 0.4225 -REMARK 3 S21: 0.0477 S22: -0.1015 S23: 0.1085 -REMARK 3 S31: -0.5330 S32: 0.3055 S33: 0.0232 -REMARK 3 TLS GROUP : 19 -REMARK 3 SELECTION: chain 'C' and (resid 86 through 100 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 9.0002 17.3071 12.2154 -REMARK 3 T TENSOR -REMARK 3 T11: 0.5092 T22: 0.3385 -REMARK 3 T33: 0.4654 T12: -0.0712 -REMARK 3 T13: 0.0850 T23: -0.0447 -REMARK 3 L TENSOR -REMARK 3 L11: 3.7662 L22: 3.8053 -REMARK 3 L33: 3.8671 L12: 2.5060 -REMARK 3 L13: 0.2796 L23: 3.0611 -REMARK 3 S TENSOR -REMARK 3 S11: -0.3232 S12: -0.0318 S13: 0.7002 -REMARK 3 S21: -0.2447 S22: 0.1126 S23: 0.2700 -REMARK 3 S31: -1.6107 S32: -0.1009 S33: 0.3292 -REMARK 3 TLS GROUP : 20 -REMARK 3 SELECTION: chain 'C' and (resid 101 through 127 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 16.2858 21.2308 25.1680 -REMARK 3 T TENSOR -REMARK 3 T11: 0.5071 T22: 0.4735 -REMARK 3 T33: 0.5341 T12: -0.0457 -REMARK 3 T13: 0.1161 T23: 0.0398 -REMARK 3 L TENSOR -REMARK 3 L11: 5.1569 L22: 3.0106 -REMARK 3 L33: 9.6358 L12: -2.9825 -REMARK 3 L13: 3.6773 L23: -4.6960 -REMARK 3 S TENSOR -REMARK 3 S11: 0.2981 S12: -0.3220 S13: 0.7213 -REMARK 3 S21: 0.1061 S22: -0.8327 S23: -1.2978 -REMARK 3 S31: 0.4972 S32: 1.0513 S33: 0.3472 -REMARK 3 TLS GROUP : 21 -REMARK 3 SELECTION: chain 'C' and (resid 128 through 152 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 5.6286 19.9185 29.9169 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2659 T22: 0.2222 -REMARK 3 T33: 0.2617 T12: -0.0345 -REMARK 3 T13: 0.0677 T23: -0.0594 -REMARK 3 L TENSOR -REMARK 3 L11: 5.7029 L22: 7.0638 -REMARK 3 L33: 8.3276 L12: 2.4706 -REMARK 3 L13: -2.0266 L23: -2.9262 -REMARK 3 S TENSOR -REMARK 3 S11: -0.0218 S12: -0.4065 S13: 0.1586 -REMARK 3 S21: 0.2687 S22: -0.3832 S23: -0.2002 -REMARK 3 S31: -0.0449 S32: 0.0873 S33: 0.3842 -REMARK 3 TLS GROUP : 22 -REMARK 3 SELECTION: chain 'C' and (resid 153 through 165 ) -REMARK 3 ORIGIN FOR THE GROUP (A): 1.9947 20.8924 24.2281 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3617 T22: 0.2000 -REMARK 3 T33: 0.3001 T12: -0.0679 -REMARK 3 T13: 0.1359 T23: -0.0704 -REMARK 3 L TENSOR -REMARK 3 L11: 7.2222 L22: 7.6794 -REMARK 3 L33: 2.9007 L12: 4.8860 -REMARK 3 L13: 0.0328 L23: -0.2847 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0094 S12: 0.3612 S13: 0.2829 -REMARK 3 S21: 0.0456 S22: 0.0181 S23: -0.0041 -REMARK 3 S31: -0.3718 S32: -0.1961 S33: 0.0242 -REMARK 3 TLS GROUP : 23 -REMARK 3 SELECTION: chain 'C' and (resid 166 through 179 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -5.6439 17.6761 31.3303 -REMARK 3 T TENSOR -REMARK 3 T11: 0.5744 T22: 0.4890 -REMARK 3 T33: 0.4615 T12: -0.0777 -REMARK 3 T13: 0.2231 T23: -0.1319 -REMARK 3 L TENSOR -REMARK 3 L11: 0.2801 L22: 0.4819 -REMARK 3 L33: 6.0005 L12: 0.3319 -REMARK 3 L13: -1.2257 L23: -1.6367 -REMARK 3 S TENSOR -REMARK 3 S11: 0.3794 S12: -0.5828 S13: 0.4005 -REMARK 3 S21: 0.6050 S22: -0.0997 S23: 0.3705 -REMARK 3 S31: -1.4104 S32: -0.1493 S33: -0.3174 -REMARK 3 TLS GROUP : 24 -REMARK 3 SELECTION: chain 'C' and (resid 180 through 197 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -1.2843 2.6492 30.3826 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3827 T22: 0.3258 -REMARK 3 T33: 0.2227 T12: -0.1238 -REMARK 3 T13: 0.0693 T23: -0.0195 -REMARK 3 L TENSOR -REMARK 3 L11: 6.1945 L22: 5.2026 -REMARK 3 L33: 2.8929 L12: -2.5123 -REMARK 3 L13: 1.4510 L23: -1.7782 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0302 S12: -0.5840 S13: -0.0394 -REMARK 3 S21: 0.7396 S22: -0.0750 S23: 0.0436 -REMARK 3 S31: -0.1888 S32: 0.2572 S33: 0.0432 -REMARK 3 TLS GROUP : 25 -REMARK 3 SELECTION: chain 'C' and (resid 198 through 217 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -0.2277 -4.9589 31.0597 -REMARK 3 T TENSOR -REMARK 3 T11: 0.3256 T22: 0.3494 -REMARK 3 T33: 0.2430 T12: -0.1166 -REMARK 3 T13: 0.0292 T23: 0.0229 -REMARK 3 L TENSOR -REMARK 3 L11: 6.5854 L22: 7.0219 -REMARK 3 L33: 3.8471 L12: -0.9788 -REMARK 3 L13: -0.0121 L23: -1.6477 -REMARK 3 S TENSOR -REMARK 3 S11: 0.2853 S12: -1.1363 S13: -0.3380 -REMARK 3 S21: 0.7591 S22: -0.0161 S23: -0.1311 -REMARK 3 S31: -0.1604 S32: 0.0951 S33: -0.2664 -REMARK 3 TLS GROUP : 26 -REMARK 3 SELECTION: chain 'D' and (resid 4 through 37 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -19.7687 7.9262 12.3306 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2938 T22: 0.3022 -REMARK 3 T33: 0.5025 T12: 0.0628 -REMARK 3 T13: 0.1000 T23: -0.0411 -REMARK 3 L TENSOR -REMARK 3 L11: 2.0154 L22: 1.4706 -REMARK 3 L33: 4.9327 L12: 1.5759 -REMARK 3 L13: 0.6482 L23: 1.6684 -REMARK 3 S TENSOR -REMARK 3 S11: 0.2635 S12: -0.1958 S13: 0.3666 -REMARK 3 S21: 0.2279 S22: -0.2062 S23: 0.6715 -REMARK 3 S31: -0.6958 S32: -0.4394 S33: -0.1152 -REMARK 3 TLS GROUP : 27 -REMARK 3 SELECTION: chain 'D' and (resid 38 through 85 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -9.3180 -11.1190 4.8960 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2029 T22: 0.1682 -REMARK 3 T33: 0.2818 T12: -0.0174 -REMARK 3 T13: -0.0111 T23: 0.0018 -REMARK 3 L TENSOR -REMARK 3 L11: 2.6384 L22: 0.7363 -REMARK 3 L33: 3.0040 L12: -0.4053 -REMARK 3 L13: 0.0498 L23: 0.9104 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0868 S12: -0.0227 S13: -0.2157 -REMARK 3 S21: 0.0834 S22: 0.0141 S23: 0.1540 -REMARK 3 S31: 0.1725 S32: 0.1730 S33: -0.0901 -REMARK 3 TLS GROUP : 28 -REMARK 3 SELECTION: chain 'D' and (resid 86 through 102 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -7.3858 -15.3306 -2.4011 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2033 T22: 0.2437 -REMARK 3 T33: 0.2731 T12: -0.0290 -REMARK 3 T13: 0.0366 T23: -0.0046 -REMARK 3 L TENSOR -REMARK 3 L11: 5.8711 L22: 2.5353 -REMARK 3 L33: 6.1068 L12: 3.2149 -REMARK 3 L13: 3.3977 L23: 1.6686 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0517 S12: -0.1318 S13: -0.3811 -REMARK 3 S21: 0.0170 S22: 0.1104 S23: 0.0416 -REMARK 3 S31: 0.2354 S32: -0.2260 S33: -0.2115 -REMARK 3 TLS GROUP : 29 -REMARK 3 SELECTION: chain 'D' and (resid 103 through 127 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -21.1679 -17.6624 -10.5807 -REMARK 3 T TENSOR -REMARK 3 T11: 0.4050 T22: 0.4330 -REMARK 3 T33: 0.4386 T12: -0.0910 -REMARK 3 T13: -0.0558 T23: -0.0559 -REMARK 3 L TENSOR -REMARK 3 L11: 5.8089 L22: 4.6034 -REMARK 3 L33: 5.8075 L12: -4.9288 -REMARK 3 L13: 4.0693 L23: -4.6891 -REMARK 3 S TENSOR -REMARK 3 S11: 0.1487 S12: 0.7254 S13: 0.6893 -REMARK 3 S21: -1.1507 S22: -0.5453 S23: -0.6519 -REMARK 3 S31: 0.3356 S32: 0.0048 S33: 0.4885 -REMARK 3 TLS GROUP : 30 -REMARK 3 SELECTION: chain 'D' and (resid 128 through 165 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -22.0224 -16.9523 0.6254 -REMARK 3 T TENSOR -REMARK 3 T11: 0.1555 T22: 0.1799 -REMARK 3 T33: 0.2530 T12: -0.0535 -REMARK 3 T13: -0.0014 T23: 0.0325 -REMARK 3 L TENSOR -REMARK 3 L11: 3.1201 L22: 7.1702 -REMARK 3 L33: 3.9062 L12: -2.9147 -REMARK 3 L13: -2.0855 L23: 4.8093 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0171 S12: 0.1705 S13: 0.0210 -REMARK 3 S21: 0.1975 S22: -0.1344 S23: 0.1069 -REMARK 3 S31: 0.1501 S32: -0.2435 S33: 0.1238 -REMARK 3 TLS GROUP : 31 -REMARK 3 SELECTION: chain 'D' and (resid 166 through 217 ) -REMARK 3 ORIGIN FOR THE GROUP (A): -24.6784 0.8813 5.0001 -REMARK 3 T TENSOR -REMARK 3 T11: 0.2228 T22: 0.3741 -REMARK 3 T33: 0.4971 T12: 0.0658 -REMARK 3 T13: 0.0159 T23: -0.0067 -REMARK 3 L TENSOR -REMARK 3 L11: 1.1335 L22: 3.0594 -REMARK 3 L33: 3.5083 L12: 0.5127 -REMARK 3 L13: -0.4859 L23: -0.3460 -REMARK 3 S TENSOR -REMARK 3 S11: 0.0416 S12: 0.1868 S13: 0.2085 -REMARK 3 S21: 0.0127 S22: -0.0363 S23: 0.6115 -REMARK 3 S31: -0.3381 S32: -0.6544 S33: -0.0106 -REMARK 3 -REMARK 3 NCS DETAILS -REMARK 3 NUMBER OF NCS GROUPS : NULL -REMARK 3 -REMARK 3 OTHER REFINEMENT REMARKS: NULL -REMARK 4 -REMARK 4 4RAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14. -REMARK 100 THE RCSB ID CODE IS RCSB087110. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 05-AUG-13 -REMARK 200 TEMPERATURE (KELVIN) : 100 -REMARK 200 PH : NULL -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON -REMARK 200 BEAMLINE : MX1 -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369 -REMARK 200 MONOCHROMATOR : NULL -REMARK 200 OPTICS : NULL -REMARK 200 -REMARK 200 DETECTOR TYPE : CCD -REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270 -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS -REMARK 200 DATA SCALING SOFTWARE : SCALA -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68208 -REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870 -REMARK 200 RESOLUTION RANGE LOW (A) : 46.430 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 -REMARK 200 DATA REDUNDANCY : NULL -REMARK 200 R MERGE (I) : NULL -REMARK 200 R SYM (I) : NULL -REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT -REMARK 200 SOFTWARE USED: PHASES -REMARK 200 STARTING MODEL: NULL -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 41.02 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: NULL -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 38.30100 -REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.42450 -REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.42650 -REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.42450 -REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.30100 -REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.42650 -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: 11660 ANGSTROM**2 -REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2 -REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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 ASP A 89 -REMARK 465 SER A 103 -REMARK 465 TYR A 104 -REMARK 465 CYS A 105 -REMARK 465 ASN A 106 -REMARK 465 ASP A 107 -REMARK 465 GLN A 108 -REMARK 465 SER A 109 -REMARK 465 THR A 110 -REMARK 465 GLY A 111 -REMARK 465 ASP A 112 -REMARK 465 ILE A 113 -REMARK 465 LYS A 114 -REMARK 465 VAL A 115 -REMARK 465 ILE A 116 -REMARK 465 GLY A 117 -REMARK 465 GLY A 118 -REMARK 465 ASP A 119 -REMARK 465 ASP A 120 -REMARK 465 ALA A 217 -REMARK 465 ALA B 1 -REMARK 465 THR B 2 -REMARK 465 ARG B 3 -REMARK 465 SER B 103 -REMARK 465 TYR B 104 -REMARK 465 CYS B 105 -REMARK 465 ASN B 106 -REMARK 465 ASP B 107 -REMARK 465 GLN B 108 -REMARK 465 SER B 109 -REMARK 465 THR B 110 -REMARK 465 GLY B 111 -REMARK 465 ASP B 112 -REMARK 465 ILE B 113 -REMARK 465 LYS B 114 -REMARK 465 LEU B 121 -REMARK 465 SER B 122 -REMARK 465 VAL B 171 -REMARK 465 GLY B 172 -REMARK 465 ALA C 1 -REMARK 465 THR C 2 -REMARK 465 ARG C 3 -REMARK 465 SER C 103 -REMARK 465 TYR C 104 -REMARK 465 CYS C 105 -REMARK 465 ASN C 106 -REMARK 465 ASP C 107 -REMARK 465 GLN C 108 -REMARK 465 SER C 109 -REMARK 465 THR C 110 -REMARK 465 GLY C 111 -REMARK 465 ASP C 112 -REMARK 465 ILE C 113 -REMARK 465 ALA D 1 -REMARK 465 THR D 2 -REMARK 465 ARG D 3 -REMARK 465 CYS D 105 -REMARK 465 ASN D 106 -REMARK 465 ASP D 107 -REMARK 465 GLN D 108 -REMARK 465 SER D 109 -REMARK 465 THR D 110 -REMARK 465 GLY D 111 -REMARK 470 -REMARK 470 MISSING ATOM -REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; -REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; -REMARK 470 I=INSERTION CODE): -REMARK 470 M RES CSSEQI ATOMS -REMARK 470 CYS A 22 SG -REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2 -REMARK 470 LYS A 102 CG CD CE NZ -REMARK 470 CYS A 205 SG -REMARK 470 CYS B 22 SG -REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2 -REMARK 470 ILE B 92 CG1 CG2 CD1 -REMARK 470 LYS B 102 CG CD CE NZ -REMARK 470 ASP B 120 CG OD1 OD2 -REMARK 470 LYS B 174 CG CD CE NZ -REMARK 470 CYS B 205 SG -REMARK 470 CYS C 22 SG -REMARK 470 ILE C 92 CG1 CG2 CD1 -REMARK 470 LYS C 102 CG CD CE NZ -REMARK 470 LYS C 114 CG CD CE NZ -REMARK 470 CYS C 205 SG -REMARK 470 CYS D 22 SG -REMARK 470 ASP D 112 CG OD1 OD2 -REMARK 470 CYS D 205 SG -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 LYS B 165 NH2 ARG B 169 2.17 -REMARK 500 O HOH C 450 O HOH C 451 2.19 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: COVALENT BOND ANGLES -REMARK 500 -REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES -REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE -REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN -REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). -REMARK 500 -REMARK 500 STANDARD TABLE: -REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) -REMARK 500 -REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 -REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 -REMARK 500 -REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 -REMARK 500 PRO B 93 C - N - CA ANGL. DEV. = 20.8 DEGREES -REMARK 500 PRO B 93 C - N - CD ANGL. DEV. = -17.6 DEGREES -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: TORSION ANGLES -REMARK 500 -REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: -REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). -REMARK 500 -REMARK 500 STANDARD TABLE: -REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) -REMARK 500 -REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- -REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 -REMARK 500 -REMARK 500 M RES CSSEQI PSI PHI -REMARK 500 ASP A 137 -79.98 -119.09 -REMARK 500 ASN A 153 68.36 38.12 -REMARK 500 ALA A 191 -12.06 80.32 -REMARK 500 GLU A 196 -11.43 79.36 -REMARK 500 SER B 88 -162.73 -106.70 -REMARK 500 ILE B 92 -121.61 -71.69 -REMARK 500 ASP B 137 -83.44 -122.03 -REMARK 500 VAL B 149 -58.67 60.92 -REMARK 500 ALA B 191 -10.33 82.40 -REMARK 500 GLU B 196 -11.77 80.16 -REMARK 500 ASP B 200 46.15 -89.31 -REMARK 500 ASP C 12 33.68 -97.04 -REMARK 500 LEU C 121 0.11 -65.26 -REMARK 500 ASP C 137 -81.36 -118.99 -REMARK 500 ALA C 191 -8.59 79.91 -REMARK 500 GLU C 196 -12.94 75.85 -REMARK 500 PHE C 198 -0.28 77.73 -REMARK 500 ASP C 200 42.51 -89.00 -REMARK 500 ASP D 137 -85.06 -118.19 -REMARK 500 ALA D 191 -14.39 82.21 -REMARK 500 GLU D 196 -10.81 78.97 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS -REMARK 500 -REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH -REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED -REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND -REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. -REMARK 500 MODEL OMEGA -REMARK 500 GLY B 58 HIS B 59 145.45 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 620 -REMARK 620 METAL COORDINATION -REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG C 302 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 HOH C 450 O -REMARK 620 2 GLU C 133 OE1 133.0 -REMARK 620 3 HOH C 448 O 66.1 88.1 -REMARK 620 4 ASP C 134 OD1 126.1 81.1 167.6 -REMARK 620 5 HOH C 405 O 99.4 120.5 90.6 89.5 -REMARK 620 6 HOH C 411 O 63.6 79.1 90.8 93.2 160.4 -REMARK 620 7 HOH C 451 O 56.2 146.0 119.2 73.1 81.7 80.6 -REMARK 620 N 1 2 3 4 5 6 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG D 302 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 HOH D 447 O -REMARK 620 2 HOH D 445 O 93.6 -REMARK 620 3 GLU D 133 OE1 101.7 85.8 -REMARK 620 4 HOH D 410 O 86.5 163.2 110.7 -REMARK 620 5 HOH D 401 O 113.3 76.9 141.5 87.6 -REMARK 620 6 ASP D 134 OD1 171.0 94.4 74.8 87.0 72.6 -REMARK 620 N 1 2 3 4 5 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG B 303 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 HOH B 447 O -REMARK 620 2 ASP B 193 OD1 91.9 -REMARK 620 3 HOH B 448 O 90.0 171.7 -REMARK 620 4 3L7 B 301 OAE 84.5 83.8 104.4 -REMARK 620 5 HOH B 446 O 170.5 85.3 91.6 104.2 -REMARK 620 6 HOH B 421 O 90.8 81.0 90.9 164.0 79.8 -REMARK 620 N 1 2 3 4 5 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG B 302 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 GLU B 133 OE1 -REMARK 620 2 ASP B 134 OD1 81.8 -REMARK 620 3 3L7 B 301 OAU 137.1 136.3 -REMARK 620 4 GLU B 133 OE2 50.5 116.2 106.3 -REMARK 620 N 1 2 3 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG C 303 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 HOH C 452 O -REMARK 620 2 ASP C 193 OD1 97.6 -REMARK 620 3 HOH C 453 O 67.3 149.1 -REMARK 620 4 HOH C 421 O 159.3 99.0 102.9 -REMARK 620 5 HOH C 412 O 87.8 82.9 121.3 82.0 -REMARK 620 6 3L7 C 301 OAB 93.7 86.0 69.1 99.7 168.9 -REMARK 620 7 HOH C 438 O 78.0 154.4 52.1 81.7 71.7 119.3 -REMARK 620 N 1 2 3 4 5 6 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG D 303 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 ASP D 193 OD1 -REMARK 620 2 HOH D 425 O 82.9 -REMARK 620 3 HOH D 446 O 98.2 109.9 -REMARK 620 4 3L7 D 301 OAE 73.3 155.3 80.5 -REMARK 620 N 1 2 3 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG A 302 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 HOH A 449 O -REMARK 620 2 HOH A 450 O 96.0 -REMARK 620 3 HOH A 418 O 86.1 77.4 -REMARK 620 4 GLU A 133 OE1 109.5 145.7 81.8 -REMARK 620 5 ASP A 134 OD1 176.1 80.4 94.3 74.3 -REMARK 620 6 HOH A 426 O 94.9 80.7 158.1 118.1 83.3 -REMARK 620 7 GLU A 133 OE2 78.5 161.4 119.5 51.2 104.6 82.0 -REMARK 620 N 1 2 3 4 5 6 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 MG A 303 MG -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 ASP A 193 OD1 -REMARK 620 2 3L7 A 301 OAD 83.9 -REMARK 620 3 HOH A 451 O 79.1 157.1 -REMARK 620 4 HOH A 452 O 86.1 88.1 75.5 -REMARK 620 N 1 2 3 -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 A 301 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC4 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 B 301 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC5 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC6 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 303 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC7 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 C 301 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC8 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 302 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: AC9 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L7 D 301 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 302 -REMARK 800 -REMARK 800 SITE_IDENTIFIER: BC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 303 -REMARK 900 -REMARK 900 RELATED ENTRIES -REMARK 900 RELATED ID: 4RAB RELATED DB: PDB -REMARK 900 RELATED ID: 4RAC RELATED DB: PDB -REMARK 900 RELATED ID: 4RAD RELATED DB: PDB -REMARK 900 RELATED ID: 4RAN RELATED DB: PDB -REMARK 900 RELATED ID: 4RAQ RELATED DB: PDB -DBREF 4RAO A 1 217 UNP P00492 HPRT_HUMAN 2 218 -DBREF 4RAO B 1 217 UNP P00492 HPRT_HUMAN 2 218 -DBREF 4RAO C 1 217 UNP P00492 HPRT_HUMAN 2 218 -DBREF 4RAO D 1 217 UNP P00492 HPRT_HUMAN 2 218 -SEQRES 1 A 217 ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU -SEQRES 2 A 217 PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS -SEQRES 3 A 217 TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY -SEQRES 4 A 217 LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL -SEQRES 5 A 217 MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS -SEQRES 6 A 217 VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU -SEQRES 7 A 217 ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER -SEQRES 8 A 217 ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR -SEQRES 9 A 217 CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY -SEQRES 10 A 217 GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU -SEQRES 11 A 217 ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN -SEQRES 12 A 217 THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET -SEQRES 13 A 217 VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG -SEQRES 14 A 217 SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE -SEQRES 15 A 217 PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN -SEQRES 16 A 217 GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER -SEQRES 17 A 217 GLU THR GLY LYS ALA LYS TYR LYS ALA -SEQRES 1 B 217 ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU -SEQRES 2 B 217 PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS -SEQRES 3 B 217 TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY -SEQRES 4 B 217 LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL -SEQRES 5 B 217 MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS -SEQRES 6 B 217 VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU -SEQRES 7 B 217 ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER -SEQRES 8 B 217 ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR -SEQRES 9 B 217 CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY -SEQRES 10 B 217 GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU -SEQRES 11 B 217 ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN -SEQRES 12 B 217 THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET -SEQRES 13 B 217 VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG -SEQRES 14 B 217 SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE -SEQRES 15 B 217 PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN -SEQRES 16 B 217 GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER -SEQRES 17 B 217 GLU THR GLY LYS ALA LYS TYR LYS ALA -SEQRES 1 C 217 ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU -SEQRES 2 C 217 PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS -SEQRES 3 C 217 TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY -SEQRES 4 C 217 LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL -SEQRES 5 C 217 MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS -SEQRES 6 C 217 VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU -SEQRES 7 C 217 ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER -SEQRES 8 C 217 ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR -SEQRES 9 C 217 CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY -SEQRES 10 C 217 GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU -SEQRES 11 C 217 ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN -SEQRES 12 C 217 THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET -SEQRES 13 C 217 VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG -SEQRES 14 C 217 SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE -SEQRES 15 C 217 PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN -SEQRES 16 C 217 GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER -SEQRES 17 C 217 GLU THR GLY LYS ALA LYS TYR LYS ALA -SEQRES 1 D 217 ALA THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU -SEQRES 2 D 217 PRO GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS -SEQRES 3 D 217 TYR ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY -SEQRES 4 D 217 LEU ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL -SEQRES 5 D 217 MET LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS -SEQRES 6 D 217 VAL LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU -SEQRES 7 D 217 ASP TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER -SEQRES 8 D 217 ILE PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR -SEQRES 9 D 217 CYS ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY -SEQRES 10 D 217 GLY ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU -SEQRES 11 D 217 ILE VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN -SEQRES 12 D 217 THR LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET -SEQRES 13 D 217 VAL LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG -SEQRES 14 D 217 SER VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE -SEQRES 15 D 217 PRO ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN -SEQRES 16 D 217 GLU TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER -SEQRES 17 D 217 GLU THR GLY LYS ALA LYS TYR LYS ALA -HET 3L7 A 301 28 -HET MG A 302 1 -HET MG A 303 1 -HET 3L7 B 301 56 -HET MG B 302 1 -HET MG B 303 1 -HET 3L7 C 301 28 -HET MG C 302 1 -HET MG C 303 1 -HET 3L7 D 301 28 -HET MG D 302 1 -HET MG D 303 1 -HETNAM 3L7 (2-{[2-(6-OXO-1,6-DIHYDRO-9H-PURIN-9-YL)ETHYL](2-{[(E)- -HETNAM 2 3L7 2-PHOSPHONOETHENYL]OXY}ETHYL)AMINO}ETHYL)PHOSPHONIC -HETNAM 3 3L7 ACID -HETNAM MG MAGNESIUM ION -FORMUL 5 3L7 4(C13 H21 N5 O8 P2) -FORMUL 6 MG 8(MG 2+) -FORMUL 17 HOH *201(H2 O) -HELIX 1 1 ASP A 17 PHE A 21 5 5 -HELIX 2 2 PRO A 24 ALA A 28 5 5 -HELIX 3 3 PRO A 37 GLY A 57 1 21 -HELIX 4 4 GLY A 70 ASN A 87 1 18 -HELIX 5 5 LEU A 121 THR A 125 5 5 -HELIX 6 6 GLY A 139 ARG A 150 1 12 -HELIX 7 7 GLN A 151 ASN A 153 5 3 -HELIX 8 8 SER A 208 LYS A 216 1 9 -HELIX 9 9 ASP B 17 PHE B 21 5 5 -HELIX 10 10 PRO B 24 ALA B 28 5 5 -HELIX 11 11 PRO B 37 GLY B 57 1 21 -HELIX 12 12 GLY B 70 SER B 88 1 19 -HELIX 13 13 GLY B 139 GLN B 151 1 13 -HELIX 14 14 SER B 208 TYR B 215 1 8 -HELIX 15 15 ASP C 17 PHE C 21 5 5 -HELIX 16 16 PRO C 24 ALA C 28 5 5 -HELIX 17 17 PRO C 37 GLY C 57 1 21 -HELIX 18 18 GLY C 70 ARG C 86 1 17 -HELIX 19 19 ASP C 120 THR C 125 5 6 -HELIX 20 20 GLY C 139 GLN C 151 1 13 -HELIX 21 21 SER C 208 TYR C 215 1 8 -HELIX 22 22 ASP D 17 PHE D 21 5 5 -HELIX 23 23 PRO D 24 ALA D 28 5 5 -HELIX 24 24 PRO D 37 GLY D 57 1 21 -HELIX 25 25 GLY D 70 ARG D 86 1 17 -HELIX 26 26 ASP D 120 THR D 125 5 6 -HELIX 27 27 GLY D 139 ARG D 150 1 12 -HELIX 28 28 GLN D 151 ASN D 153 5 3 -HELIX 29 29 SER D 208 LYS D 216 1 9 -SHEET 1 A 6 VAL A 7 VAL A 8 0 -SHEET 2 A 6 PHE A 177 ILE A 182 1 O GLU A 181 N VAL A 7 -SHEET 3 A 6 MET A 156 LYS A 165 1 N SER A 161 O PHE A 177 -SHEET 4 A 6 ASN A 128 ILE A 136 1 N ILE A 131 O ALA A 160 -SHEET 5 A 6 ILE A 61 LEU A 67 1 N LEU A 64 O LEU A 130 -SHEET 6 A 6 MET A 94 ARG A 100 1 O ASP A 97 N CYS A 65 -SHEET 1 B 3 LEU A 31 ILE A 36 0 -SHEET 2 B 3 VAL A 204 ILE A 207 -1 O VAL A 206 N GLU A 32 -SHEET 3 B 3 VAL A 187 VAL A 188 -1 N VAL A 188 O CYS A 205 -SHEET 1 C 7 VAL B 7 VAL B 8 0 -SHEET 2 C 7 PHE B 177 ILE B 182 1 O GLU B 181 N VAL B 7 -SHEET 3 C 7 MET B 156 LYS B 165 1 N SER B 161 O PHE B 177 -SHEET 4 C 7 ASN B 128 ILE B 136 1 N ILE B 131 O ALA B 160 -SHEET 5 C 7 ILE B 61 LEU B 67 1 N LEU B 64 O LEU B 130 -SHEET 6 C 7 MET B 94 ARG B 100 1 O ILE B 99 N LEU B 67 -SHEET 7 C 7 ILE B 116 GLY B 117 -1 O ILE B 116 N ARG B 100 -SHEET 1 D 3 LEU B 31 ILE B 36 0 -SHEET 2 D 3 VAL B 204 ILE B 207 -1 O VAL B 206 N GLU B 32 -SHEET 3 D 3 VAL B 187 VAL B 188 -1 N VAL B 188 O CYS B 205 -SHEET 1 E 6 VAL C 7 VAL C 8 0 -SHEET 2 E 6 PHE C 177 ILE C 182 1 O GLU C 181 N VAL C 7 -SHEET 3 E 6 MET C 156 LYS C 165 1 N SER C 161 O PHE C 177 -SHEET 4 E 6 ASN C 128 ILE C 136 1 N VAL C 129 O MET C 156 -SHEET 5 E 6 ILE C 61 LEU C 67 1 N LEU C 64 O LEU C 130 -SHEET 6 E 6 MET C 94 ARG C 100 1 O ILE C 99 N LEU C 67 -SHEET 1 F 3 LEU C 31 ILE C 36 0 -SHEET 2 F 3 VAL C 204 ILE C 207 -1 O VAL C 206 N GLU C 32 -SHEET 3 F 3 VAL C 187 VAL C 188 -1 N VAL C 188 O CYS C 205 -SHEET 1 G 7 VAL D 7 VAL D 8 0 -SHEET 2 G 7 PHE D 177 ILE D 182 1 O GLU D 181 N VAL D 7 -SHEET 3 G 7 MET D 156 LYS D 165 1 N SER D 161 O PHE D 177 -SHEET 4 G 7 ASN D 128 ILE D 136 1 N VAL D 129 O MET D 156 -SHEET 5 G 7 ILE D 61 VAL D 66 1 N LEU D 64 O LEU D 130 -SHEET 6 G 7 MET D 94 LYS D 102 1 O ASP D 97 N CYS D 65 -SHEET 7 G 7 LYS D 114 ILE D 116 -1 O ILE D 116 N ARG D 100 -SHEET 1 H 3 LEU D 31 ILE D 36 0 -SHEET 2 H 3 VAL D 204 ILE D 207 -1 O VAL D 206 N GLU D 32 -SHEET 3 H 3 VAL D 187 VAL D 188 -1 N VAL D 188 O CYS D 205 -LINK MG MG C 302 O HOH C 450 1555 1555 1.80 -LINK MG MG D 302 O HOH D 447 1555 1555 1.91 -LINK MG MG B 303 O HOH B 447 1555 1555 1.96 -LINK OE1AGLU B 133 MG MG B 302 1555 1555 2.06 -LINK OD1 ASP B 134 MG MG B 302 1555 1555 2.10 -LINK MG MG C 303 O HOH C 452 1555 1555 2.11 -LINK MG MG D 302 O HOH D 445 1555 1555 2.14 -LINK OE1 GLU D 133 MG MG D 302 1555 1555 2.15 -LINK OD1 ASP B 193 MG MG B 303 1555 1555 2.16 -LINK OD1 ASP D 193 MG MG D 303 1555 1555 2.18 -LINK OE1BGLU B 133 MG MG B 302 1555 1555 2.18 -LINK OE1 GLU C 133 MG MG C 302 1555 1555 2.19 -LINK OD1 ASP C 193 MG MG C 303 1555 1555 2.21 -LINK MG MG A 302 O HOH A 449 1555 1555 2.21 -LINK MG MG C 302 O HOH C 448 1555 1555 2.25 -LINK MG MG C 303 O HOH C 453 1555 1555 2.25 -LINK OD1 ASP C 134 MG MG C 302 1555 1555 2.26 -LINK MG MG D 302 O HOH D 410 1555 1555 2.26 -LINK MG MG B 303 O HOH B 448 1555 1555 2.27 -LINK OD1 ASP A 193 MG MG A 303 1555 1555 2.27 -LINK MG MG C 303 O HOH C 421 1555 1555 2.28 -LINK OAEB3L7 B 301 MG MG B 303 1555 1555 2.28 -LINK MG MG A 302 O HOH A 450 1555 1555 2.28 -LINK MG MG A 302 O HOH A 418 1555 1555 2.29 -LINK MG MG D 303 O HOH D 425 1555 1555 2.30 -LINK MG MG C 302 O HOH C 405 1555 1555 2.31 -LINK OE1 GLU A 133 MG MG A 302 1555 1555 2.33 -LINK MG MG B 303 O HOH B 446 1555 1555 2.34 -LINK MG MG D 303 O HOH D 446 1555 1555 2.35 -LINK MG MG D 302 O HOH D 401 1555 1555 2.35 -LINK OD1 ASP A 134 MG MG A 302 1555 1555 2.35 -LINK OD1 ASP D 134 MG MG D 302 1555 1555 2.36 -LINK OAD 3L7 A 301 MG MG A 303 1555 1555 2.41 -LINK MG MG A 302 O HOH A 426 1555 1555 2.42 -LINK MG MG C 302 O HOH C 411 1555 1555 2.45 -LINK MG MG C 303 O HOH C 412 1555 1555 2.45 -LINK MG MG B 303 O HOH B 421 1555 1555 2.48 -LINK OAB 3L7 C 301 MG MG C 303 1555 1555 2.52 -LINK MG MG C 302 O HOH C 451 1555 1555 2.60 -LINK MG MG A 303 O HOH A 451 1555 1555 2.61 -LINK OAUB3L7 B 301 MG MG B 302 1555 1555 2.63 -LINK OE2 GLU A 133 MG MG A 302 1555 1555 2.69 -LINK MG MG C 303 O HOH C 438 1555 1555 2.70 -LINK MG MG A 303 O HOH A 452 1555 1555 2.74 -LINK OAE 3L7 D 301 MG MG D 303 1555 1555 2.75 -LINK OE2AGLU B 133 MG MG B 302 1555 1555 2.82 -CISPEP 1 LEU A 67 LYS A 68 0 -2.10 -CISPEP 2 GLY B 57 GLY B 58 0 9.27 -CISPEP 3 LEU B 67 LYS B 68 0 -4.05 -CISPEP 4 ILE B 92 PRO B 93 0 0.30 -CISPEP 5 LEU C 67 LYS C 68 0 -2.75 -CISPEP 6 LEU D 67 LYS D 68 0 -8.23 -SITE 1 AC1 19 LYS A 68 GLY A 69 ASP A 137 THR A 138 -SITE 2 AC1 19 GLY A 139 LYS A 140 THR A 141 LYS A 165 -SITE 3 AC1 19 LYS A 185 PHE A 186 VAL A 187 ASP A 193 -SITE 4 AC1 19 ARG A 199 MG A 303 HOH A 412 HOH A 418 -SITE 5 AC1 19 HOH A 426 HOH A 450 HOH A 452 -SITE 1 AC2 6 GLU A 133 ASP A 134 HOH A 418 HOH A 426 -SITE 2 AC2 6 HOH A 449 HOH A 450 -SITE 1 AC3 4 ASP A 193 3L7 A 301 HOH A 451 HOH A 452 -SITE 1 AC4 22 LYS B 68 GLY B 69 GLU B 133 ASP B 137 -SITE 2 AC4 22 THR B 138 GLY B 139 LYS B 140 THR B 141 -SITE 3 AC4 22 LYS B 165 LYS B 185 PHE B 186 VAL B 187 -SITE 4 AC4 22 ASP B 193 ARG B 199 MG B 302 MG B 303 -SITE 5 AC4 22 HOH B 401 HOH B 414 HOH B 430 HOH B 446 -SITE 6 AC4 22 HOH B 447 HOH B 448 -SITE 1 AC5 3 GLU B 133 ASP B 134 3L7 B 301 -SITE 1 AC6 6 ASP B 193 3L7 B 301 HOH B 421 HOH B 446 -SITE 2 AC6 6 HOH B 447 HOH B 448 -SITE 1 AC7 25 LYS C 68 GLY C 69 ARG C 100 ASP C 137 -SITE 2 AC7 25 THR C 138 GLY C 139 LYS C 140 THR C 141 -SITE 3 AC7 25 LYS C 165 LYS C 185 PHE C 186 VAL C 187 -SITE 4 AC7 25 ASP C 193 ARG C 199 MG C 303 HOH C 402 -SITE 5 AC7 25 HOH C 405 HOH C 411 HOH C 413 HOH C 418 -SITE 6 AC7 25 HOH C 421 HOH C 449 HOH C 450 HOH C 451 -SITE 7 AC7 25 HOH C 453 -SITE 1 AC8 7 GLU C 133 ASP C 134 HOH C 405 HOH C 411 -SITE 2 AC8 7 HOH C 448 HOH C 450 HOH C 451 -SITE 1 AC9 7 ASP C 193 3L7 C 301 HOH C 412 HOH C 421 -SITE 2 AC9 7 HOH C 438 HOH C 452 HOH C 453 -SITE 1 BC1 19 LYS D 68 GLY D 69 ASP D 137 THR D 138 -SITE 2 BC1 19 GLY D 139 LYS D 140 THR D 141 LYS D 165 -SITE 3 BC1 19 LYS D 185 PHE D 186 VAL D 187 ASP D 193 -SITE 4 BC1 19 ARG D 199 MG D 303 HOH D 401 HOH D 405 -SITE 5 BC1 19 HOH D 410 HOH D 432 HOH D 445 -SITE 1 BC2 6 GLU D 133 ASP D 134 HOH D 401 HOH D 410 -SITE 2 BC2 6 HOH D 445 HOH D 447 -SITE 1 BC3 4 ASP D 193 3L7 D 301 HOH D 425 HOH D 446 -CRYST1 76.602 92.853 114.849 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 0.013054 0.000000 0.000000 0.00000 -SCALE2 0.000000 0.010770 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.008707 0.00000 -ATOM 1 N ALA A 1 29.351 -15.299 10.549 1.00 74.92 N -ANISOU 1 N ALA A 1 7124 9614 11727 415 -2282 2479 N -ATOM 2 CA ALA A 1 28.468 -14.947 9.436 1.00 73.31 C -ANISOU 2 CA ALA A 1 7090 9292 11472 457 -2044 2081 C -ATOM 3 C ALA A 1 27.420 -13.904 9.827 1.00 70.93 C -ANISOU 3 C ALA A 1 7078 9180 10693 224 -1925 2028 C -ATOM 4 O ALA A 1 26.898 -13.915 10.943 1.00 70.22 O -ANISOU 4 O ALA A 1 7090 9184 10407 75 -2003 2318 O -ATOM 5 CB ALA A 1 27.789 -16.190 8.876 1.00 72.44 C -ANISOU 5 CB ALA A 1 6943 8763 11820 639 -2052 2026 C -ATOM 6 N THR A 2 27.118 -13.006 8.896 1.00 68.65 N -ANISOU 6 N THR A 2 6912 8955 10215 211 -1725 1667 N -ATOM 7 CA THR A 2 26.058 -12.025 9.086 1.00 67.59 C -ANISOU 7 CA THR A 2 7040 8946 9696 24 -1591 1568 C -ATOM 8 C THR A 2 24.709 -12.738 9.002 1.00 65.98 C -ANISOU 8 C THR A 2 6940 8476 9654 47 -1545 1596 C -ATOM 9 O THR A 2 24.376 -13.318 7.963 1.00 65.77 O -ANISOU 9 O THR A 2 6881 8188 9921 208 -1498 1377 O -ATOM 10 CB THR A 2 26.121 -10.925 8.005 1.00 67.81 C -ANISOU 10 CB THR A 2 7139 9079 9545 22 -1398 1203 C -ATOM 11 OG1 THR A 2 27.483 -10.518 7.811 1.00 70.55 O -ANISOU 11 OG1 THR A 2 7304 9595 9908 54 -1433 1186 O -ATOM 12 CG2 THR A 2 25.271 -9.717 8.403 1.00 64.90 C -ANISOU 12 CG2 THR A 2 7011 8877 8770 -192 -1293 1135 C -ATOM 13 N ARG A 3 23.943 -12.700 10.094 1.00 59.98 N -ANISOU 13 N ARG A 3 6293 7790 8707 -105 -1564 1865 N -ATOM 14 CA ARG A 3 22.657 -13.400 10.173 1.00 57.18 C -ANISOU 14 CA ARG A 3 5991 7188 8549 -107 -1525 1981 C -ATOM 15 C ARG A 3 21.689 -12.952 9.078 1.00 54.95 C -ANISOU 15 C ARG A 3 5835 6771 8272 -91 -1357 1618 C -ATOM 16 O ARG A 3 20.867 -13.734 8.585 1.00 54.27 O -ANISOU 16 O ARG A 3 5721 6371 8530 -18 -1370 1583 O -ATOM 17 CB ARG A 3 22.017 -13.199 11.553 1.00 54.82 C -ANISOU 17 CB ARG A 3 5798 7085 7946 -275 -1510 2338 C -ATOM 18 CG ARG A 3 20.755 -14.030 11.792 1.00 54.28 C -ANISOU 18 CG ARG A 3 5718 6766 8139 -284 -1468 2575 C -ATOM 19 CD ARG A 3 21.063 -15.516 11.680 1.00 62.24 C -ANISOU 19 CD ARG A 3 6498 7425 9728 -146 -1653 2800 C -ATOM 20 NE ARG A 3 19.883 -16.359 11.857 1.00 66.19 N -ANISOU 20 NE ARG A 3 6942 7630 10577 -166 -1638 3050 N -ATOM 21 CZ ARG A 3 18.925 -16.507 10.946 1.00 65.34 C -ANISOU 21 CZ ARG A 3 6854 7229 10744 -139 -1575 2799 C -ATOM 22 NH1 ARG A 3 18.997 -15.853 9.791 1.00 61.70 N -ANISOU 22 NH1 ARG A 3 6491 6763 10190 -78 -1509 2294 N -ATOM 23 NH2 ARG A 3 17.889 -17.302 11.190 1.00 66.44 N -ANISOU 23 NH2 ARG A 3 6901 7085 11258 -175 -1588 3075 N -ATOM 24 N SER A 4 21.789 -11.689 8.693 1.00 50.57 N -ANISOU 24 N SER A 4 5408 6441 7364 -162 -1225 1359 N -ATOM 25 CA SER A 4 20.893 -11.170 7.671 1.00 50.99 C -ANISOU 25 CA SER A 4 5584 6402 7389 -149 -1077 1044 C -ATOM 26 C SER A 4 21.570 -10.070 6.858 1.00 49.88 C -ANISOU 26 C SER A 4 5484 6454 7016 -138 -977 752 C -ATOM 27 O SER A 4 21.272 -8.888 7.053 1.00 43.16 O -ANISOU 27 O SER A 4 4768 5789 5841 -281 -866 681 O -ATOM 28 CB SER A 4 19.597 -10.666 8.315 1.00 48.54 C -ANISOU 28 CB SER A 4 5428 6135 6880 -308 -963 1149 C -ATOM 29 OG SER A 4 18.556 -10.565 7.364 1.00 50.34 O -ANISOU 29 OG SER A 4 5723 6177 7228 -275 -876 919 O -ATOM 30 N PRO A 5 22.484 -10.460 5.935 1.00 54.89 N -ANISOU 30 N PRO A 5 5985 7037 7836 43 -1004 591 N -ATOM 31 CA PRO A 5 23.197 -9.503 5.079 1.00 52.90 C -ANISOU 31 CA PRO A 5 5724 6973 7402 76 -886 367 C -ATOM 32 C PRO A 5 22.193 -8.758 4.215 1.00 51.34 C -ANISOU 32 C PRO A 5 5696 6760 7052 54 -737 127 C -ATOM 33 O PRO A 5 21.062 -9.227 4.042 1.00 54.58 O -ANISOU 33 O PRO A 5 6190 6968 7581 70 -750 80 O -ATOM 34 CB PRO A 5 24.098 -10.397 4.215 1.00 53.45 C -ANISOU 34 CB PRO A 5 5612 6940 7757 332 -921 253 C -ATOM 35 CG PRO A 5 23.392 -11.705 4.179 1.00 56.28 C -ANISOU 35 CG PRO A 5 5958 6970 8457 447 -1039 264 C -ATOM 36 CD PRO A 5 22.788 -11.852 5.552 1.00 57.48 C -ANISOU 36 CD PRO A 5 6156 7099 8585 250 -1129 597 C -ATOM 37 N GLY A 6 22.587 -7.614 3.674 1.00 42.12 N -ANISOU 37 N GLY A 6 4555 5789 5658 12 -609 2 N -ATOM 38 CA GLY A 6 21.591 -6.699 3.161 1.00 35.03 C -ANISOU 38 CA GLY A 6 3826 4906 4580 -64 -483 -145 C -ATOM 39 C GLY A 6 21.459 -6.620 1.659 1.00 30.98 C -ANISOU 39 C GLY A 6 3331 4377 4064 110 -386 -393 C -ATOM 40 O GLY A 6 22.131 -7.327 0.913 1.00 30.10 O -ANISOU 40 O GLY A 6 3112 4247 4079 323 -397 -496 O -ATOM 41 N VAL A 7 20.556 -5.746 1.230 1.00 26.95 N -ANISOU 41 N VAL A 7 2962 3884 3393 33 -292 -488 N -ATOM 42 CA VAL A 7 20.394 -5.398 -0.174 1.00 27.17 C -ANISOU 42 CA VAL A 7 3032 3964 3328 173 -194 -691 C -ATOM 43 C VAL A 7 21.639 -4.624 -0.584 1.00 27.34 C -ANISOU 43 C VAL A 7 2938 4232 3217 192 -68 -651 C -ATOM 44 O VAL A 7 21.919 -3.550 -0.038 1.00 28.85 O -ANISOU 44 O VAL A 7 3123 4540 3301 0 -17 -528 O -ATOM 45 CB VAL A 7 19.142 -4.513 -0.360 1.00 25.01 C -ANISOU 45 CB VAL A 7 2918 3656 2930 51 -137 -737 C -ATOM 46 CG1 VAL A 7 19.019 -4.013 -1.810 1.00 26.04 C -ANISOU 46 CG1 VAL A 7 3094 3886 2913 187 -43 -901 C -ATOM 47 CG2 VAL A 7 17.892 -5.277 0.059 1.00 27.68 C -ANISOU 47 CG2 VAL A 7 3325 3747 3445 24 -250 -740 C -ATOM 48 N VAL A 8 22.389 -5.164 -1.537 1.00 29.05 N -ANISOU 48 N VAL A 8 3053 4523 3463 431 -19 -757 N -ATOM 49 CA VAL A 8 23.618 -4.519 -1.977 1.00 34.59 C -ANISOU 49 CA VAL A 8 3596 5469 4078 472 129 -677 C -ATOM 50 C VAL A 8 23.278 -3.426 -2.989 1.00 36.07 C -ANISOU 50 C VAL A 8 3859 5806 4038 471 295 -716 C -ATOM 51 O VAL A 8 22.765 -3.710 -4.068 1.00 33.00 O -ANISOU 51 O VAL A 8 3564 5433 3542 663 336 -895 O -ATOM 52 CB VAL A 8 24.608 -5.530 -2.605 1.00 39.10 C -ANISOU 52 CB VAL A 8 4002 6089 4764 762 159 -761 C -ATOM 53 CG1 VAL A 8 25.800 -4.806 -3.208 1.00 42.06 C -ANISOU 53 CG1 VAL A 8 4189 6744 5049 822 361 -654 C -ATOM 54 CG2 VAL A 8 25.089 -6.547 -1.562 1.00 37.62 C -ANISOU 54 CG2 VAL A 8 3699 5750 4846 756 -14 -663 C -ATOM 55 N ILE A 9 23.552 -2.175 -2.636 1.00 31.74 N -ANISOU 55 N ILE A 9 3272 5361 3428 256 366 -548 N -ATOM 56 CA ILE A 9 23.335 -1.068 -3.561 1.00 32.85 C -ANISOU 56 CA ILE A 9 3446 5636 3397 242 526 -517 C -ATOM 57 C ILE A 9 24.676 -0.718 -4.215 1.00 37.50 C -ANISOU 57 C ILE A 9 3805 6470 3973 341 701 -376 C -ATOM 58 O ILE A 9 25.654 -0.412 -3.534 1.00 31.73 O -ANISOU 58 O ILE A 9 2888 5781 3386 213 686 -209 O -ATOM 59 CB ILE A 9 22.681 0.131 -2.840 1.00 34.84 C -ANISOU 59 CB ILE A 9 3794 5801 3643 -46 495 -427 C -ATOM 60 CG1 ILE A 9 21.286 -0.280 -2.352 1.00 33.10 C -ANISOU 60 CG1 ILE A 9 3779 5368 3429 -96 373 -555 C -ATOM 61 CG2 ILE A 9 22.611 1.351 -3.752 1.00 37.59 C -ANISOU 61 CG2 ILE A 9 4132 6269 3880 -76 653 -333 C -ATOM 62 CD1 ILE A 9 20.430 0.848 -1.871 1.00 37.12 C -ANISOU 62 CD1 ILE A 9 4402 5790 3911 -311 379 -518 C -ATOM 63 N SER A 10 24.742 -0.800 -5.541 1.00 32.59 N -ANISOU 63 N SER A 10 3181 6026 3177 583 865 -436 N -ATOM 64 CA SER A 10 26.027 -0.667 -6.224 1.00 38.67 C -ANISOU 64 CA SER A 10 3708 7058 3928 735 1074 -293 C -ATOM 65 C SER A 10 26.538 0.770 -6.236 1.00 35.77 C -ANISOU 65 C SER A 10 3187 6808 3596 523 1203 6 C -ATOM 66 O SER A 10 25.772 1.707 -6.025 1.00 35.31 O -ANISOU 66 O SER A 10 3252 6646 3517 312 1156 59 O -ATOM 67 CB SER A 10 25.930 -1.189 -7.660 1.00 47.07 C -ANISOU 67 CB SER A 10 4831 8321 4733 1091 1230 -455 C -ATOM 68 OG SER A 10 24.866 -0.538 -8.324 1.00 52.65 O -ANISOU 68 OG SER A 10 5740 9050 5216 1066 1244 -489 O -ATOM 69 N ASP A 11 27.833 0.927 -6.510 1.00 38.36 N -ANISOU 69 N ASP A 11 3224 7334 4016 588 1367 208 N -ATOM 70 CA ASP A 11 28.466 2.236 -6.557 1.00 42.68 C -ANISOU 70 CA ASP A 11 3562 7974 4679 388 1485 531 C -ATOM 71 C ASP A 11 27.835 3.139 -7.623 1.00 46.68 C -ANISOU 71 C ASP A 11 4166 8605 4966 417 1657 637 C -ATOM 72 O ASP A 11 27.788 4.357 -7.464 1.00 50.77 O -ANISOU 72 O ASP A 11 4635 9041 5613 171 1653 849 O -ATOM 73 CB ASP A 11 29.966 2.100 -6.838 1.00 43.26 C -ANISOU 73 CB ASP A 11 3267 8264 4906 505 1663 748 C -ATOM 74 CG ASP A 11 30.751 1.550 -5.652 1.00 45.72 C -ANISOU 74 CG ASP A 11 3413 8444 5515 397 1460 749 C -ATOM 75 OD1 ASP A 11 30.200 1.504 -4.533 1.00 45.38 O -ANISOU 75 OD1 ASP A 11 3534 8161 5549 183 1188 632 O -ATOM 76 OD2 ASP A 11 31.937 1.187 -5.848 1.00 48.95 O -ANISOU 76 OD2 ASP A 11 3514 9010 6076 535 1583 888 O -ATOM 77 N ASP A 12 27.345 2.536 -8.703 1.00 46.50 N -ANISOU 77 N ASP A 12 4347 8653 4670 695 1715 460 N -ATOM 78 CA AASP A 12 26.799 3.335 -9.800 0.59 46.31 C -ANISOU 78 CA AASP A 12 4472 8657 4468 719 1786 557 C -ATOM 79 CA BASP A 12 26.795 3.266 -9.842 0.41 46.48 C -ANISOU 79 CA BASP A 12 4501 8684 4477 737 1787 543 C -ATOM 80 C ASP A 12 25.283 3.452 -9.763 1.00 45.82 C -ANISOU 80 C ASP A 12 4691 8452 4264 662 1641 380 C -ATOM 81 O ASP A 12 24.665 3.874 -10.736 1.00 50.19 O -ANISOU 81 O ASP A 12 5389 9037 4643 730 1661 409 O -ATOM 82 CB AASP A 12 27.258 2.810 -11.159 0.59 49.62 C -ANISOU 82 CB AASP A 12 4917 9270 4667 1029 1925 524 C -ATOM 83 CB BASP A 12 27.121 2.528 -11.140 0.41 49.33 C -ANISOU 83 CB BASP A 12 4922 9222 4601 1070 1898 443 C -ATOM 84 CG AASP A 12 26.948 1.342 -11.359 0.59 50.57 C -ANISOU 84 CG AASP A 12 5190 9385 4640 1295 1840 155 C -ATOM 85 CG BASP A 12 28.592 2.194 -11.270 0.41 54.02 C -ANISOU 85 CG BASP A 12 5247 9965 5312 1186 2059 574 C -ATOM 86 OD1AASP A 12 26.046 0.807 -10.682 0.59 47.79 O -ANISOU 86 OD1AASP A 12 4990 8864 4306 1254 1655 -83 O -ATOM 87 OD1BASP A 12 29.433 3.056 -10.933 0.41 54.05 O -ANISOU 87 OD1BASP A 12 5007 9982 5548 1003 2139 881 O -ATOM 88 OD2AASP A 12 27.615 0.715 -12.210 0.59 58.64 O -ANISOU 88 OD2AASP A 12 6174 10562 5545 1549 1954 98 O -ATOM 89 OD2BASP A 12 28.912 1.067 -11.713 0.41 59.24 O -ANISOU 89 OD2BASP A 12 5935 10708 5866 1460 2093 363 O -ATOM 90 N GLU A 13 24.691 3.100 -8.626 1.00 40.11 N -ANISOU 90 N GLU A 13 4028 7589 3625 529 1491 213 N -ATOM 91 CA GLU A 13 23.244 3.239 -8.440 1.00 41.06 C -ANISOU 91 CA GLU A 13 4409 7505 3688 437 1326 52 C -ATOM 92 C GLU A 13 22.844 4.690 -8.662 1.00 39.88 C -ANISOU 92 C GLU A 13 4253 7334 3565 247 1389 294 C -ATOM 93 O GLU A 13 23.339 5.580 -7.977 1.00 40.63 O -ANISOU 93 O GLU A 13 4204 7331 3903 3 1393 487 O -ATOM 94 CB GLU A 13 22.828 2.795 -7.038 1.00 44.57 C -ANISOU 94 CB GLU A 13 4936 7648 4349 249 1100 -106 C -ATOM 95 CG GLU A 13 21.370 3.106 -6.688 1.00 47.84 C -ANISOU 95 CG GLU A 13 5572 7833 4771 115 959 -217 C -ATOM 96 CD GLU A 13 20.377 2.332 -7.537 1.00 53.92 C -ANISOU 96 CD GLU A 13 6526 8607 5357 334 893 -434 C -ATOM 97 OE1 GLU A 13 20.623 1.134 -7.792 1.00 60.41 O -ANISOU 97 OE1 GLU A 13 7358 9466 6130 546 848 -620 O -ATOM 98 OE2 GLU A 13 19.357 2.928 -7.949 1.00 52.41 O -ANISOU 98 OE2 GLU A 13 6457 8361 5097 296 865 -426 O -ATOM 99 N PRO A 14 21.965 4.937 -9.647 1.00 44.06 N -ANISOU 99 N PRO A 14 4951 7876 3913 354 1382 277 N -ATOM 100 CA PRO A 14 21.609 6.314 -10.006 1.00 43.53 C -ANISOU 100 CA PRO A 14 4867 7775 3900 207 1438 537 C -ATOM 101 C PRO A 14 20.482 6.857 -9.142 1.00 42.19 C -ANISOU 101 C PRO A 14 4809 7357 3865 -19 1306 471 C -ATOM 102 O PRO A 14 20.275 8.066 -9.107 1.00 47.99 O -ANISOU 102 O PRO A 14 5493 7990 4750 -194 1335 682 O -ATOM 103 CB PRO A 14 21.139 6.180 -11.458 1.00 45.41 C -ANISOU 103 CB PRO A 14 5239 8147 3869 443 1452 524 C -ATOM 104 CG PRO A 14 20.558 4.804 -11.523 1.00 50.07 C -ANISOU 104 CG PRO A 14 6006 8707 4311 629 1304 158 C -ATOM 105 CD PRO A 14 21.376 3.951 -10.571 1.00 48.12 C -ANISOU 105 CD PRO A 14 5654 8431 4198 621 1302 33 C -ATOM 106 N GLY A 15 19.771 5.977 -8.448 1.00 38.82 N -ANISOU 106 N GLY A 15 4539 6747 3462 -17 1131 175 N -ATOM 107 CA GLY A 15 18.619 6.393 -7.673 1.00 32.91 C -ANISOU 107 CA GLY A 15 3924 5709 2873 -199 992 83 C -ATOM 108 C GLY A 15 17.504 6.859 -8.594 1.00 36.41 C -ANISOU 108 C GLY A 15 4482 6154 3200 -128 976 121 C -ATOM 109 O GLY A 15 17.548 6.621 -9.808 1.00 41.10 O -ANISOU 109 O GLY A 15 5095 6987 3534 87 1032 163 O -ATOM 110 N TYR A 16 16.521 7.542 -8.017 1.00 32.48 N -ANISOU 110 N TYR A 16 4053 5403 2884 -294 898 110 N -ATOM 111 CA TYR A 16 15.303 7.914 -8.729 1.00 32.38 C -ANISOU 111 CA TYR A 16 4143 5339 2822 -239 838 130 C -ATOM 112 C TYR A 16 15.120 9.430 -8.774 1.00 35.84 C -ANISOU 112 C TYR A 16 4508 5664 3447 -398 905 385 C -ATOM 113 O TYR A 16 15.432 10.140 -7.804 1.00 33.88 O -ANISOU 113 O TYR A 16 4191 5229 3453 -602 927 417 O -ATOM 114 CB TYR A 16 14.085 7.271 -8.047 1.00 31.78 C -ANISOU 114 CB TYR A 16 4197 5027 2852 -265 678 -115 C -ATOM 115 CG TYR A 16 14.138 5.758 -7.960 1.00 32.53 C -ANISOU 115 CG TYR A 16 4352 5161 2848 -124 578 -354 C -ATOM 116 CD1 TYR A 16 13.722 4.962 -9.027 1.00 41.14 C -ANISOU 116 CD1 TYR A 16 5523 6369 3738 98 476 -480 C -ATOM 117 CD2 TYR A 16 14.610 5.127 -6.811 1.00 33.82 C -ANISOU 117 CD2 TYR A 16 4490 5231 3127 -207 563 -457 C -ATOM 118 CE1 TYR A 16 13.778 3.581 -8.947 1.00 41.90 C -ANISOU 118 CE1 TYR A 16 5663 6448 3807 229 362 -718 C -ATOM 119 CE2 TYR A 16 14.662 3.754 -6.720 1.00 32.38 C -ANISOU 119 CE2 TYR A 16 4341 5046 2914 -82 463 -643 C -ATOM 120 CZ TYR A 16 14.243 2.989 -7.778 1.00 36.73 C -ANISOU 120 CZ TYR A 16 4962 5671 3323 132 362 -781 C -ATOM 121 OH TYR A 16 14.308 1.622 -7.681 1.00 37.92 O -ANISOU 121 OH TYR A 16 5136 5769 3503 257 242 -985 O -ATOM 122 N ASP A 17 14.609 9.907 -9.907 1.00 32.85 N -ANISOU 122 N ASP A 17 4146 5391 2944 -295 914 556 N -ATOM 123 CA ASP A 17 14.235 11.302 -10.094 1.00 34.06 C -ANISOU 123 CA ASP A 17 4231 5407 3302 -418 951 820 C -ATOM 124 C ASP A 17 13.229 11.695 -9.022 1.00 30.20 C -ANISOU 124 C ASP A 17 3801 4552 3121 -579 857 659 C -ATOM 125 O ASP A 17 12.251 10.978 -8.789 1.00 28.08 O -ANISOU 125 O ASP A 17 3649 4195 2826 -521 742 436 O -ATOM 126 CB ASP A 17 13.615 11.474 -11.486 1.00 38.85 C -ANISOU 126 CB ASP A 17 4883 6204 3675 -241 925 995 C -ATOM 127 CG ASP A 17 13.383 12.926 -11.860 1.00 47.28 C -ANISOU 127 CG ASP A 17 5847 7165 4954 -345 977 1354 C -ATOM 128 OD1 ASP A 17 13.072 13.749 -10.975 1.00 45.32 O -ANISOU 128 OD1 ASP A 17 5551 6579 5089 -544 959 1352 O -ATOM 129 OD2 ASP A 17 13.506 13.245 -13.057 1.00 59.31 O -ANISOU 129 OD2 ASP A 17 7336 8945 6254 -213 1033 1643 O -ATOM 130 N LEU A 18 13.469 12.831 -8.364 1.00 32.50 N -ANISOU 130 N LEU A 18 4000 4625 3724 -773 906 768 N -ATOM 131 CA LEU A 18 12.600 13.270 -7.269 1.00 33.00 C -ANISOU 131 CA LEU A 18 4118 4355 4064 -904 848 587 C -ATOM 132 C LEU A 18 11.183 13.484 -7.768 1.00 27.01 C -ANISOU 132 C LEU A 18 3419 3482 3360 -827 779 607 C -ATOM 133 O LEU A 18 10.229 13.322 -7.016 1.00 30.63 O -ANISOU 133 O LEU A 18 3946 3742 3950 -852 732 406 O -ATOM 134 CB LEU A 18 13.113 14.581 -6.670 1.00 30.87 C -ANISOU 134 CB LEU A 18 3737 3860 4132 -1100 891 693 C -ATOM 135 CG LEU A 18 14.514 14.565 -6.077 1.00 35.64 C -ANISOU 135 CG LEU A 18 4246 4524 4770 -1216 921 686 C -ATOM 136 CD1 LEU A 18 15.013 15.989 -5.841 1.00 41.06 C -ANISOU 136 CD1 LEU A 18 4786 4976 5837 -1401 929 855 C -ATOM 137 CD2 LEU A 18 14.493 13.779 -4.783 1.00 35.34 C -ANISOU 137 CD2 LEU A 18 4320 4436 4673 -1258 860 348 C -ATOM 138 N ASP A 19 11.055 13.859 -9.047 1.00 28.84 N -ANISOU 138 N ASP A 19 3611 3858 3490 -725 775 875 N -ATOM 139 CA ASP A 19 9.756 14.207 -9.621 1.00 32.50 C -ANISOU 139 CA ASP A 19 4102 4215 4032 -656 681 951 C -ATOM 140 C ASP A 19 8.797 13.029 -9.743 1.00 30.19 C -ANISOU 140 C ASP A 19 3926 3971 3574 -524 541 713 C -ATOM 141 O ASP A 19 7.603 13.222 -10.008 1.00 30.01 O -ANISOU 141 O ASP A 19 3911 3815 3675 -484 434 730 O -ATOM 142 CB ASP A 19 9.930 14.889 -10.978 1.00 39.01 C -ANISOU 142 CB ASP A 19 4854 5223 4746 -572 697 1336 C -ATOM 143 CG ASP A 19 10.532 16.282 -10.858 1.00 49.12 C -ANISOU 143 CG ASP A 19 5977 6336 6349 -729 806 1632 C -ATOM 144 OD1 ASP A 19 10.018 17.078 -10.041 1.00 50.40 O -ANISOU 144 OD1 ASP A 19 6106 6135 6910 -862 791 1563 O -ATOM 145 OD2 ASP A 19 11.520 16.573 -11.573 1.00 55.44 O -ANISOU 145 OD2 ASP A 19 6677 7362 7028 -711 908 1932 O -ATOM 146 N LEU A 20 9.324 11.825 -9.529 1.00 27.04 N -ANISOU 146 N LEU A 20 3593 3732 2947 -464 527 503 N -ATOM 147 CA LEU A 20 8.550 10.584 -9.604 1.00 26.86 C -ANISOU 147 CA LEU A 20 3663 3728 2814 -349 374 266 C -ATOM 148 C LEU A 20 7.935 10.219 -8.244 1.00 28.66 C -ANISOU 148 C LEU A 20 3904 3696 3290 -459 374 50 C -ATOM 149 O LEU A 20 7.099 9.313 -8.139 1.00 27.12 O -ANISOU 149 O LEU A 20 3745 3434 3125 -401 251 -107 O -ATOM 150 CB LEU A 20 9.434 9.429 -10.124 1.00 29.63 C -ANISOU 150 CB LEU A 20 4069 4366 2823 -204 353 152 C -ATOM 151 CG LEU A 20 9.982 9.537 -11.553 1.00 36.15 C -ANISOU 151 CG LEU A 20 4903 5526 3305 -31 365 328 C -ATOM 152 CD1 LEU A 20 11.024 8.458 -11.827 1.00 41.31 C -ANISOU 152 CD1 LEU A 20 5592 6441 3664 113 403 181 C -ATOM 153 CD2 LEU A 20 8.869 9.441 -12.572 1.00 38.36 C -ANISOU 153 CD2 LEU A 20 5251 5854 3469 109 167 339 C -ATOM 154 N PHE A 21 8.340 10.941 -7.208 1.00 24.46 N -ANISOU 154 N PHE A 21 3335 3020 2941 -612 508 52 N -ATOM 155 CA PHE A 21 7.842 10.688 -5.860 1.00 25.87 C -ANISOU 155 CA PHE A 21 3534 3004 3293 -701 546 -135 C -ATOM 156 C PHE A 21 7.221 11.897 -5.182 1.00 26.99 C -ANISOU 156 C PHE A 21 3637 2890 3729 -802 632 -114 C -ATOM 157 O PHE A 21 7.301 13.019 -5.676 1.00 25.61 O -ANISOU 157 O PHE A 21 3405 2646 3679 -832 656 55 O -ATOM 158 CB PHE A 21 8.963 10.109 -4.996 1.00 29.32 C -ANISOU 158 CB PHE A 21 3996 3537 3608 -761 603 -249 C -ATOM 159 CG PHE A 21 9.461 8.803 -5.504 1.00 33.97 C -ANISOU 159 CG PHE A 21 4615 4327 3965 -643 522 -312 C -ATOM 160 CD1 PHE A 21 8.820 7.625 -5.149 1.00 38.92 C -ANISOU 160 CD1 PHE A 21 5278 4902 4606 -590 434 -460 C -ATOM 161 CD2 PHE A 21 10.528 8.746 -6.388 1.00 33.27 C -ANISOU 161 CD2 PHE A 21 4502 4468 3670 -570 538 -215 C -ATOM 162 CE1 PHE A 21 9.251 6.403 -5.648 1.00 39.47 C -ANISOU 162 CE1 PHE A 21 5374 5112 4512 -467 335 -546 C -ATOM 163 CE2 PHE A 21 10.961 7.529 -6.893 1.00 38.63 C -ANISOU 163 CE2 PHE A 21 5212 5324 4140 -425 469 -313 C -ATOM 164 CZ PHE A 21 10.324 6.357 -6.521 1.00 43.53 C -ANISOU 164 CZ PHE A 21 5882 5856 4801 -374 353 -497 C -ATOM 165 N CYS A 22 6.576 11.632 -4.050 1.00 28.80 N -ANISOU 165 N CYS A 22 3889 2979 4076 -839 684 -279 N -ATOM 166 CA CYS A 22 6.040 12.666 -3.185 1.00 30.99 C -ANISOU 166 CA CYS A 22 4147 3026 4604 -909 794 -336 C -ATOM 167 C CYS A 22 7.160 13.096 -2.248 1.00 31.10 C -ANISOU 167 C CYS A 22 4202 3050 4566 -1024 867 -441 C -ATOM 168 O CYS A 22 7.619 12.298 -1.427 1.00 34.81 O -ANISOU 168 O CYS A 22 4731 3629 4867 -1047 882 -571 O -ATOM 169 CB CYS A 22 4.877 12.111 -2.392 1.00 31.59 C -ANISOU 169 CB CYS A 22 4222 3000 4783 -871 844 -455 C -ATOM 170 N ILE A 23 7.601 14.343 -2.392 1.00 27.70 N -ANISOU 170 N ILE A 23 3726 2493 4304 -1099 887 -370 N -ATOM 171 CA ILE A 23 8.719 14.909 -1.633 1.00 32.34 C -ANISOU 171 CA ILE A 23 4327 3055 4906 -1225 903 -462 C -ATOM 172 C ILE A 23 8.238 16.171 -0.914 1.00 35.70 C -ANISOU 172 C ILE A 23 4746 3214 5606 -1248 936 -579 C -ATOM 173 O ILE A 23 7.518 16.975 -1.510 1.00 43.40 O -ANISOU 173 O ILE A 23 5650 4026 6814 -1199 931 -455 O -ATOM 174 CB ILE A 23 9.861 15.292 -2.599 1.00 36.18 C -ANISOU 174 CB ILE A 23 4721 3643 5384 -1275 855 -227 C -ATOM 175 CG1 ILE A 23 10.357 14.059 -3.357 1.00 39.08 C -ANISOU 175 CG1 ILE A 23 5093 4316 5441 -1184 820 -133 C -ATOM 176 CG2 ILE A 23 11.005 15.953 -1.869 1.00 41.27 C -ANISOU 176 CG2 ILE A 23 5336 4219 6127 -1426 836 -298 C -ATOM 177 CD1 ILE A 23 10.915 12.981 -2.448 1.00 39.84 C -ANISOU 177 CD1 ILE A 23 5258 4552 5327 -1196 807 -319 C -ATOM 178 N PRO A 24 8.642 16.369 0.359 1.00 37.87 N -ANISOU 178 N PRO A 24 5087 3484 5817 -1276 933 -806 N -ATOM 179 CA PRO A 24 8.285 17.639 1.015 1.00 41.16 C -ANISOU 179 CA PRO A 24 5498 3685 6458 -1254 929 -934 C -ATOM 180 C PRO A 24 8.841 18.851 0.262 1.00 41.55 C -ANISOU 180 C PRO A 24 5438 3562 6787 -1324 831 -754 C -ATOM 181 O PRO A 24 10.022 18.859 -0.110 1.00 37.51 O -ANISOU 181 O PRO A 24 4873 3118 6259 -1435 756 -630 O -ATOM 182 CB PRO A 24 8.939 17.520 2.399 1.00 42.30 C -ANISOU 182 CB PRO A 24 5745 3906 6423 -1296 908 -1194 C -ATOM 183 CG PRO A 24 9.990 16.453 2.245 1.00 40.80 C -ANISOU 183 CG PRO A 24 5568 3945 5988 -1377 857 -1128 C -ATOM 184 CD PRO A 24 9.435 15.494 1.241 1.00 34.59 C -ANISOU 184 CD PRO A 24 4757 3258 5128 -1327 920 -953 C -ATOM 185 N ASN A 25 7.995 19.863 0.060 1.00 50.72 N -ANISOU 185 N ASN A 25 9844 4248 5180 740 -103 514 N -ATOM 186 CA ASN A 25 8.343 21.058 -0.700 1.00 56.54 C -ANISOU 186 CA ASN A 25 10832 4687 5963 691 -73 757 C -ATOM 187 C ASN A 25 9.607 21.746 -0.213 1.00 56.00 C -ANISOU 187 C ASN A 25 10920 4332 6025 220 1 750 C -ATOM 188 O ASN A 25 10.417 22.210 -1.015 1.00 51.94 O -ANISOU 188 O ASN A 25 10441 3741 5554 -3 101 979 O -ATOM 189 CB ASN A 25 7.192 22.065 -0.651 1.00 66.10 C -ANISOU 189 CB ASN A 25 12196 5640 7281 1070 -101 711 C -ATOM 190 CG ASN A 25 6.743 22.503 -2.027 1.00 75.99 C -ANISOU 190 CG ASN A 25 13479 6938 8455 1350 -161 986 C -ATOM 191 OD1 ASN A 25 6.071 21.750 -2.734 1.00 77.48 O -ANISOU 191 OD1 ASN A 25 13454 7471 8514 1641 -281 998 O -ATOM 192 ND2 ASN A 25 7.098 23.730 -2.415 1.00 84.14 N -ANISOU 192 ND2 ASN A 25 14784 7620 9566 1271 -88 1191 N -ATOM 193 N HIS A 26 9.767 21.810 1.107 1.00 53.49 N -ANISOU 193 N HIS A 26 10672 3872 5778 73 -41 451 N -ATOM 194 CA HIS A 26 10.884 22.539 1.698 1.00 51.75 C -ANISOU 194 CA HIS A 26 10553 3384 5725 -353 -40 337 C -ATOM 195 C HIS A 26 12.248 21.890 1.429 1.00 48.55 C -ANISOU 195 C HIS A 26 9952 3142 5352 -790 -56 398 C -ATOM 196 O HIS A 26 13.282 22.476 1.727 1.00 51.15 O -ANISOU 196 O HIS A 26 10262 3278 5895 -1176 -58 295 O -ATOM 197 CB HIS A 26 10.654 22.806 3.202 1.00 52.50 C -ANISOU 197 CB HIS A 26 10742 3379 5827 -350 -126 -51 C -ATOM 198 CG HIS A 26 10.406 21.576 4.025 1.00 52.69 C -ANISOU 198 CG HIS A 26 10641 3748 5632 -263 -206 -252 C -ATOM 199 ND1 HIS A 26 9.152 21.022 4.188 1.00 48.64 N -ANISOU 199 ND1 HIS A 26 10064 3413 5004 123 -121 -299 N -ATOM 200 CD2 HIS A 26 11.250 20.810 4.760 1.00 51.50 C -ANISOU 200 CD2 HIS A 26 10381 3813 5374 -502 -354 -423 C -ATOM 201 CE1 HIS A 26 9.240 19.956 4.963 1.00 47.01 C -ANISOU 201 CE1 HIS A 26 9736 3504 4620 96 -148 -448 C -ATOM 202 NE2 HIS A 26 10.500 19.806 5.326 1.00 47.48 N -ANISOU 202 NE2 HIS A 26 9787 3604 4649 -249 -317 -512 N -ATOM 203 N TYR A 27 12.242 20.692 0.845 1.00 44.81 N -ANISOU 203 N TYR A 27 9175 3132 4719 -703 -60 516 N -ATOM 204 CA TYR A 27 13.478 19.983 0.501 1.00 44.35 C -ANISOU 204 CA TYR A 27 8768 3367 4718 -1043 -51 550 C -ATOM 205 C TYR A 27 13.623 19.748 -1.005 1.00 46.60 C -ANISOU 205 C TYR A 27 8969 3821 4916 -1014 144 891 C -ATOM 206 O TYR A 27 14.556 19.076 -1.435 1.00 47.45 O -ANISOU 206 O TYR A 27 8757 4208 5064 -1247 210 918 O -ATOM 207 CB TYR A 27 13.557 18.630 1.219 1.00 41.46 C -ANISOU 207 CB TYR A 27 8068 3445 4239 -982 -218 341 C -ATOM 208 CG TYR A 27 13.776 18.693 2.718 1.00 38.89 C -ANISOU 208 CG TYR A 27 7828 3036 3911 -1065 -426 13 C -ATOM 209 CD1 TYR A 27 14.600 19.655 3.284 1.00 41.25 C -ANISOU 209 CD1 TYR A 27 8257 3013 4401 -1390 -525 -167 C -ATOM 210 CD2 TYR A 27 13.163 17.775 3.560 1.00 36.36 C -ANISOU 210 CD2 TYR A 27 7481 2952 3381 -822 -510 -129 C -ATOM 211 CE1 TYR A 27 14.800 19.707 4.658 1.00 45.08 C -ANISOU 211 CE1 TYR A 27 8859 3461 4809 -1432 -773 -510 C -ATOM 212 CE2 TYR A 27 13.353 17.815 4.931 1.00 35.32 C -ANISOU 212 CE2 TYR A 27 7519 2766 3135 -855 -693 -405 C -ATOM 213 CZ TYR A 27 14.170 18.780 5.475 1.00 38.69 C -ANISOU 213 CZ TYR A 27 8088 2920 3692 -1141 -859 -609 C -ATOM 214 OH TYR A 27 14.359 18.817 6.842 1.00 40.74 O -ANISOU 214 OH TYR A 27 8463 3220 3798 -1106 -1064 -881 O -ATOM 215 N ALA A 28 12.706 20.294 -1.799 1.00 48.00 N -ANISOU 215 N ALA A 28 9413 3862 4961 -689 221 1120 N -ATOM 216 CA ALA A 28 12.686 20.044 -3.245 1.00 52.74 C -ANISOU 216 CA ALA A 28 9900 4740 5401 -547 351 1377 C -ATOM 217 C ALA A 28 14.002 20.387 -3.950 1.00 57.49 C -ANISOU 217 C ALA A 28 10447 5277 6118 -947 614 1556 C -ATOM 218 O ALA A 28 14.413 19.696 -4.885 1.00 58.65 O -ANISOU 218 O ALA A 28 10390 5766 6128 -968 743 1672 O -ATOM 219 CB ALA A 28 11.529 20.784 -3.901 1.00 54.14 C -ANISOU 219 CB ALA A 28 10290 4806 5477 -111 309 1515 C -ATOM 220 N GLU A 29 14.649 21.463 -3.509 1.00 60.50 N -ANISOU 220 N GLU A 29 10979 5222 6786 -1263 719 1538 N -ATOM 221 CA GLU A 29 15.904 21.903 -4.115 1.00 64.79 C -ANISOU 221 CA GLU A 29 11421 5652 7543 -1673 1020 1673 C -ATOM 222 C GLU A 29 17.134 21.314 -3.429 1.00 62.88 C -ANISOU 222 C GLU A 29 10798 5512 7581 -2163 1012 1409 C -ATOM 223 O GLU A 29 18.222 21.295 -4.006 1.00 64.62 O -ANISOU 223 O GLU A 29 10760 5796 7998 -2487 1274 1466 O -ATOM 224 CB GLU A 29 16.002 23.424 -4.078 1.00 74.42 C -ANISOU 224 CB GLU A 29 12929 6333 9015 -1778 1152 1769 C -ATOM 225 CG GLU A 29 15.484 24.054 -2.788 1.00 84.40 C -ANISOU 225 CG GLU A 29 14368 7257 10445 -1734 918 1491 C -ATOM 226 CD GLU A 29 16.045 25.446 -2.548 1.00100.40 C -ANISOU 226 CD GLU A 29 16537 8744 12866 -2021 1063 1471 C -ATOM 227 OE1 GLU A 29 15.390 26.245 -1.839 1.00104.96 O -ANISOU 227 OE1 GLU A 29 17356 8991 13533 -1864 934 1333 O -ATOM 228 OE2 GLU A 29 17.147 25.738 -3.061 1.00108.34 O -ANISOU 228 OE2 GLU A 29 17385 9656 14123 -2409 1322 1573 O -ATOM 229 N ASP A 30 16.956 20.840 -2.199 1.00 54.78 N -ANISOU 229 N ASP A 30 9713 4516 6584 -2196 692 1100 N -ATOM 230 CA ASP A 30 18.080 20.418 -1.370 1.00 52.43 C -ANISOU 230 CA ASP A 30 8983 4350 6588 -2572 529 755 C -ATOM 231 C ASP A 30 18.491 18.971 -1.604 1.00 50.31 C -ANISOU 231 C ASP A 30 8219 4666 6230 -2494 459 689 C -ATOM 232 O ASP A 30 19.574 18.556 -1.191 1.00 52.21 O -ANISOU 232 O ASP A 30 8017 5071 6751 -2768 350 446 O -ATOM 233 CB ASP A 30 17.748 20.632 0.110 1.00 52.79 C -ANISOU 233 CB ASP A 30 9132 4261 6665 -2501 147 395 C -ATOM 234 CG ASP A 30 17.343 22.060 0.409 1.00 58.61 C -ANISOU 234 CG ASP A 30 10305 4433 7530 -2524 210 385 C -ATOM 235 OD1 ASP A 30 17.810 22.962 -0.312 1.00 59.76 O -ANISOU 235 OD1 ASP A 30 10468 4321 7915 -2697 501 566 O -ATOM 236 OD2 ASP A 30 16.559 22.276 1.359 1.00 60.73 O -ANISOU 236 OD2 ASP A 30 10819 4587 7671 -2287 -9 186 O -ATOM 237 N LEU A 31 17.619 18.201 -2.248 1.00 41.71 N -ANISOU 237 N LEU A 31 7183 3877 4788 -2101 492 867 N -ATOM 238 CA LEU A 31 17.910 16.806 -2.545 1.00 38.73 C -ANISOU 238 CA LEU A 31 6377 4002 4335 -1997 456 798 C -ATOM 239 C LEU A 31 18.245 16.648 -4.019 1.00 44.86 C -ANISOU 239 C LEU A 31 7102 4937 5005 -2050 837 1052 C -ATOM 240 O LEU A 31 17.827 17.456 -4.851 1.00 47.71 O -ANISOU 240 O LEU A 31 7866 5076 5184 -1999 1076 1347 O -ATOM 241 CB LEU A 31 16.720 15.916 -2.178 1.00 35.22 C -ANISOU 241 CB LEU A 31 5980 3790 3612 -1550 236 736 C -ATOM 242 CG LEU A 31 16.263 16.041 -0.723 1.00 34.22 C -ANISOU 242 CG LEU A 31 5990 3516 3496 -1455 -61 511 C -ATOM 243 CD1 LEU A 31 15.022 15.201 -0.434 1.00 33.99 C -ANISOU 243 CD1 LEU A 31 6010 3670 3234 -1050 -151 472 C -ATOM 244 CD2 LEU A 31 17.396 15.670 0.217 1.00 35.88 C -ANISOU 244 CD2 LEU A 31 5897 3812 3922 -1693 -288 256 C -ATOM 245 N GLU A 32 19.013 15.614 -4.343 1.00 44.74 N -ANISOU 245 N GLU A 32 6625 5293 5079 -2125 903 941 N -ATOM 246 CA GLU A 32 19.406 15.393 -5.727 1.00 44.28 C -ANISOU 246 CA GLU A 32 6513 5423 4887 -2180 1310 1133 C -ATOM 247 C GLU A 32 18.601 14.245 -6.331 1.00 40.09 C -ANISOU 247 C GLU A 32 5945 5291 3996 -1766 1238 1126 C -ATOM 248 O GLU A 32 18.103 14.348 -7.453 1.00 44.22 O -ANISOU 248 O GLU A 32 6748 5900 4154 -1588 1438 1342 O -ATOM 249 CB GLU A 32 20.902 15.097 -5.837 1.00 50.98 C -ANISOU 249 CB GLU A 32 6832 6397 6141 -2572 1525 972 C -ATOM 250 CG GLU A 32 21.419 15.127 -7.272 1.00 59.39 C -ANISOU 250 CG GLU A 32 7882 7578 7108 -2610 2019 1165 C -ATOM 251 CD GLU A 32 21.208 16.480 -7.937 1.00 72.51 C -ANISOU 251 CD GLU A 32 10024 8868 8657 -2610 2256 1496 C -ATOM 252 OE1 GLU A 32 21.350 17.517 -7.250 1.00 75.16 O -ANISOU 252 OE1 GLU A 32 10498 8794 9266 -2841 2199 1495 O -ATOM 253 OE2 GLU A 32 20.894 16.505 -9.147 1.00 78.88 O -ANISOU 253 OE2 GLU A 32 11067 9804 9099 -2364 2463 1740 O -ATOM 254 N ARG A 33 18.497 13.151 -5.582 1.00 37.59 N -ANISOU 254 N ARG A 33 5301 5200 3783 -1613 944 867 N -ATOM 255 CA ARG A 33 17.800 11.947 -6.033 1.00 37.32 C -ANISOU 255 CA ARG A 33 5155 5501 3524 -1273 877 782 C -ATOM 256 C ARG A 33 17.254 11.205 -4.832 1.00 32.02 C -ANISOU 256 C ARG A 33 4370 4841 2955 -1087 530 581 C -ATOM 257 O ARG A 33 17.802 11.295 -3.738 1.00 30.58 O -ANISOU 257 O ARG A 33 4077 4534 3008 -1227 346 471 O -ATOM 258 CB ARG A 33 18.758 10.994 -6.766 1.00 41.98 C -ANISOU 258 CB ARG A 33 5329 6409 4212 -1362 1102 668 C -ATOM 259 CG ARG A 33 19.514 11.567 -7.941 1.00 46.99 C -ANISOU 259 CG ARG A 33 6023 7069 4762 -1593 1558 842 C -ATOM 260 CD ARG A 33 18.645 11.673 -9.177 1.00 52.69 C -ANISOU 260 CD ARG A 33 7133 7866 5020 -1259 1664 1011 C -ATOM 261 NE ARG A 33 18.485 10.386 -9.846 1.00 47.68 N -ANISOU 261 NE ARG A 33 6284 7558 4275 -999 1652 795 N -ATOM 262 CZ ARG A 33 17.968 10.244 -11.061 1.00 51.82 C -ANISOU 262 CZ ARG A 33 7071 8167 4451 -708 1734 833 C -ATOM 263 NH1 ARG A 33 17.562 11.312 -11.729 1.00 50.60 N -ANISOU 263 NH1 ARG A 33 7357 7876 3993 -566 1824 1142 N -ATOM 264 NH2 ARG A 33 17.864 9.039 -11.612 1.00 49.71 N -ANISOU 264 NH2 ARG A 33 6615 8128 4147 -542 1699 568 N -ATOM 265 N VAL A 34 16.182 10.449 -5.034 1.00 27.22 N -ANISOU 265 N VAL A 34 3795 4381 2166 -772 449 518 N -ATOM 266 CA VAL A 34 15.789 9.444 -4.056 1.00 26.06 C -ANISOU 266 CA VAL A 34 3493 4270 2140 -618 248 336 C -ATOM 267 C VAL A 34 16.747 8.263 -4.215 1.00 26.01 C -ANISOU 267 C VAL A 34 3073 4482 2330 -662 291 195 C -ATOM 268 O VAL A 34 16.980 7.782 -5.333 1.00 30.06 O -ANISOU 268 O VAL A 34 3424 5216 2782 -640 484 159 O -ATOM 269 CB VAL A 34 14.337 9.008 -4.263 1.00 28.90 C -ANISOU 269 CB VAL A 34 3955 4682 2342 -315 205 272 C -ATOM 270 CG1 VAL A 34 13.977 7.832 -3.349 1.00 29.16 C -ANISOU 270 CG1 VAL A 34 3825 4718 2535 -197 116 102 C -ATOM 271 CG2 VAL A 34 13.406 10.182 -3.984 1.00 35.08 C -ANISOU 271 CG2 VAL A 34 5102 5229 2999 -225 138 380 C -ATOM 272 N PHE A 35 17.320 7.808 -3.105 1.00 26.75 N -ANISOU 272 N PHE A 35 3016 4511 2636 -692 101 107 N -ATOM 273 CA PHE A 35 18.332 6.757 -3.167 1.00 26.42 C -ANISOU 273 CA PHE A 35 2566 4634 2837 -695 97 -24 C -ATOM 274 C PHE A 35 17.711 5.414 -2.788 1.00 30.97 C -ANISOU 274 C PHE A 35 3094 5228 3445 -427 29 -119 C -ATOM 275 O PHE A 35 17.842 4.427 -3.524 1.00 31.82 O -ANISOU 275 O PHE A 35 2956 5491 3644 -332 166 -236 O -ATOM 276 CB PHE A 35 19.498 7.100 -2.252 1.00 29.90 C -ANISOU 276 CB PHE A 35 2841 4999 3522 -865 -121 -72 C -ATOM 277 CG PHE A 35 20.752 6.359 -2.569 1.00 34.90 C -ANISOU 277 CG PHE A 35 2974 5813 4473 -906 -93 -214 C -ATOM 278 CD1 PHE A 35 21.340 6.461 -3.829 1.00 36.84 C -ANISOU 278 CD1 PHE A 35 2972 6228 4799 -1065 260 -237 C -ATOM 279 CD2 PHE A 35 21.365 5.571 -1.603 1.00 36.99 C -ANISOU 279 CD2 PHE A 35 3031 6076 4947 -759 -409 -322 C -ATOM 280 CE1 PHE A 35 22.515 5.786 -4.115 1.00 44.82 C -ANISOU 280 CE1 PHE A 35 3467 7406 6156 -1096 330 -410 C -ATOM 281 CE2 PHE A 35 22.545 4.890 -1.885 1.00 39.70 C -ANISOU 281 CE2 PHE A 35 2858 6579 5646 -749 -413 -481 C -ATOM 282 CZ PHE A 35 23.114 4.996 -3.143 1.00 44.53 C -ANISOU 282 CZ PHE A 35 3188 7339 6394 -916 -25 -536 C -ATOM 283 N ILE A 36 17.036 5.384 -1.641 1.00 30.70 N -ANISOU 283 N ILE A 36 3318 5005 3342 -318 -137 -80 N -ATOM 284 CA ILE A 36 16.247 4.216 -1.241 1.00 26.69 C -ANISOU 284 CA ILE A 36 2849 4430 2864 -97 -108 -131 C -ATOM 285 C ILE A 36 14.836 4.635 -0.865 1.00 28.05 C -ANISOU 285 C ILE A 36 3339 4456 2862 -26 -46 -97 C -ATOM 286 O ILE A 36 14.629 5.223 0.200 1.00 26.81 O -ANISOU 286 O ILE A 36 3466 4131 2590 -31 -153 -23 O -ATOM 287 CB ILE A 36 16.880 3.475 -0.045 1.00 25.56 C -ANISOU 287 CB ILE A 36 2712 4169 2829 14 -312 -106 C -ATOM 288 CG1 ILE A 36 18.368 3.225 -0.297 1.00 27.97 C -ANISOU 288 CG1 ILE A 36 2637 4618 3370 -37 -442 -174 C -ATOM 289 CG2 ILE A 36 16.167 2.144 0.201 1.00 26.13 C -ANISOU 289 CG2 ILE A 36 2824 4116 2986 219 -182 -128 C -ATOM 290 CD1 ILE A 36 19.150 2.864 0.987 1.00 32.00 C -ANISOU 290 CD1 ILE A 36 3183 5035 3942 98 -794 -142 C -ATOM 291 N PRO A 37 13.857 4.329 -1.732 1.00 23.86 N -ANISOU 291 N PRO A 37 2740 4003 2323 57 117 -197 N -ATOM 292 CA PRO A 37 12.462 4.688 -1.459 1.00 22.73 C -ANISOU 292 CA PRO A 37 2790 3743 2102 147 181 -225 C -ATOM 293 C PRO A 37 11.992 4.136 -0.128 1.00 24.94 C -ANISOU 293 C PRO A 37 3245 3793 2440 215 238 -203 C -ATOM 294 O PRO A 37 12.369 3.011 0.236 1.00 23.55 O -ANISOU 294 O PRO A 37 2989 3555 2404 261 280 -208 O -ATOM 295 CB PRO A 37 11.692 3.988 -2.582 1.00 22.78 C -ANISOU 295 CB PRO A 37 2559 3906 2192 245 292 -428 C -ATOM 296 CG PRO A 37 12.699 3.874 -3.712 1.00 26.92 C -ANISOU 296 CG PRO A 37 2892 4668 2667 183 287 -448 C -ATOM 297 CD PRO A 37 14.006 3.603 -3.008 1.00 26.13 C -ANISOU 297 CD PRO A 37 2736 4506 2685 87 232 -346 C -ATOM 298 N HIS A 38 11.181 4.921 0.576 1.00 24.19 N -ANISOU 298 N HIS A 38 3622 3048 2522 -96 -326 494 N -ATOM 299 CA HIS A 38 10.599 4.522 1.852 1.00 22.50 C -ANISOU 299 CA HIS A 38 3258 2823 2468 8 -307 407 C -ATOM 300 C HIS A 38 10.006 3.120 1.792 1.00 22.40 C -ANISOU 300 C HIS A 38 3166 2895 2451 61 -335 349 C -ATOM 301 O HIS A 38 10.228 2.288 2.674 1.00 21.00 O -ANISOU 301 O HIS A 38 2891 2780 2309 87 -257 260 O -ATOM 302 CB HIS A 38 9.482 5.496 2.251 1.00 23.79 C -ANISOU 302 CB HIS A 38 3407 2834 2798 98 -401 448 C -ATOM 303 CG HIS A 38 8.790 5.113 3.524 1.00 27.52 C -ANISOU 303 CG HIS A 38 3731 3303 3424 193 -360 352 C -ATOM 304 ND1 HIS A 38 7.515 4.586 3.551 1.00 26.71 N -ANISOU 304 ND1 HIS A 38 3526 3200 3424 283 -442 344 N -ATOM 305 CD2 HIS A 38 9.196 5.177 4.818 1.00 27.18 C -ANISOU 305 CD2 HIS A 38 3628 3265 3435 192 -243 262 C -ATOM 306 CE1 HIS A 38 7.167 4.341 4.802 1.00 27.64 C -ANISOU 306 CE1 HIS A 38 3528 3323 3649 332 -358 251 C -ATOM 307 NE2 HIS A 38 8.162 4.694 5.592 1.00 29.83 N -ANISOU 307 NE2 HIS A 38 3841 3601 3892 279 -241 200 N -ATOM 308 N GLY A 39 9.250 2.861 0.733 1.00 24.98 N -ANISOU 308 N GLY A 39 3552 3215 2725 63 -461 408 N -ATOM 309 CA GLY A 39 8.557 1.590 0.632 1.00 29.03 C -ANISOU 309 CA GLY A 39 4004 3787 3237 94 -509 358 C -ATOM 310 C GLY A 39 9.511 0.424 0.510 1.00 24.25 C -ANISOU 310 C GLY A 39 3418 3288 2509 53 -397 274 C -ATOM 311 O GLY A 39 9.235 -0.662 1.000 1.00 23.94 O -ANISOU 311 O GLY A 39 3308 3283 2505 86 -382 201 O -ATOM 312 N LEU A 40 10.636 0.640 -0.162 1.00 23.98 N -ANISOU 312 N LEU A 40 3480 3300 2332 -21 -314 284 N -ATOM 313 CA LEU A 40 11.657 -0.403 -0.245 1.00 26.06 C -ANISOU 313 CA LEU A 40 3738 3661 2502 -37 -185 193 C -ATOM 314 C LEU A 40 12.255 -0.672 1.146 1.00 23.61 C -ANISOU 314 C LEU A 40 3288 3375 2308 15 -87 124 C -ATOM 315 O LEU A 40 12.544 -1.817 1.525 1.00 21.19 O -ANISOU 315 O LEU A 40 2931 3110 2009 58 -39 45 O -ATOM 316 CB LEU A 40 12.723 -0.008 -1.274 1.00 27.57 C -ANISOU 316 CB LEU A 40 4040 3910 2524 -134 -96 217 C -ATOM 317 CG LEU A 40 13.958 -0.904 -1.385 1.00 33.10 C -ANISOU 317 CG LEU A 40 4709 4719 3149 -137 71 117 C -ATOM 318 CD1 LEU A 40 13.547 -2.349 -1.637 1.00 36.51 C -ANISOU 318 CD1 LEU A 40 5163 5161 3550 -79 53 30 C -ATOM 319 CD2 LEU A 40 14.907 -0.401 -2.463 1.00 26.13 C -ANISOU 319 CD2 LEU A 40 3928 3904 2095 -251 176 142 C -ATOM 320 N ILE A 41 12.407 0.390 1.924 1.00 21.18 N -ANISOU 320 N ILE A 41 2936 3025 2087 7 -73 156 N -ATOM 321 CA ILE A 41 12.903 0.257 3.289 1.00 20.06 C -ANISOU 321 CA ILE A 41 2682 2901 2038 35 -5 100 C -ATOM 322 C ILE A 41 11.943 -0.614 4.090 1.00 21.78 C -ANISOU 322 C ILE A 41 2835 3096 2346 107 -50 55 C -ATOM 323 O ILE A 41 12.371 -1.522 4.811 1.00 19.59 O -ANISOU 323 O ILE A 41 2499 2860 2083 133 -6 -2 O -ATOM 324 CB ILE A 41 13.089 1.634 3.961 1.00 23.66 C -ANISOU 324 CB ILE A 41 3136 3296 2559 -3 8 136 C -ATOM 325 CG1 ILE A 41 14.204 2.435 3.284 1.00 23.20 C -ANISOU 325 CG1 ILE A 41 3137 3269 2407 -107 68 180 C -ATOM 326 CG2 ILE A 41 13.403 1.477 5.465 1.00 21.49 C -ANISOU 326 CG2 ILE A 41 2765 3034 2365 13 55 75 C -ATOM 327 CD1 ILE A 41 14.307 3.895 3.788 1.00 25.30 C -ANISOU 327 CD1 ILE A 41 3444 3441 2728 -166 63 224 C -ATOM 328 N MET A 42 10.644 -0.350 3.942 1.00 20.09 N -ANISOU 328 N MET A 42 2624 2814 2194 134 -145 88 N -ATOM 329 CA MET A 42 9.611 -1.104 4.651 1.00 20.55 C -ANISOU 329 CA MET A 42 2609 2859 2342 179 -181 51 C -ATOM 330 C MET A 42 9.682 -2.583 4.278 1.00 20.08 C -ANISOU 330 C MET A 42 2570 2845 2214 178 -188 7 C -ATOM 331 O MET A 42 9.679 -3.452 5.157 1.00 19.55 O -ANISOU 331 O MET A 42 2458 2789 2183 194 -157 -41 O -ATOM 332 CB MET A 42 8.218 -0.577 4.301 1.00 21.82 C -ANISOU 332 CB MET A 42 2745 2956 2587 208 -289 100 C -ATOM 333 CG MET A 42 7.949 0.823 4.804 1.00 25.68 C -ANISOU 333 CG MET A 42 3211 3365 3181 239 -282 129 C -ATOM 334 SD MET A 42 8.244 0.981 6.578 1.00 34.50 S -ANISOU 334 SD MET A 42 4256 4478 4376 247 -153 46 S -ATOM 335 CE MET A 42 6.759 0.238 7.263 1.00 52.39 C -ANISOU 335 CE MET A 42 6396 6749 6759 290 -168 3 C -ATOM 336 N ASP A 43 9.748 -2.870 2.981 1.00 19.02 N -ANISOU 336 N ASP A 43 2528 2727 1972 153 -230 24 N -ATOM 337 CA ASP A 43 9.774 -4.276 2.543 1.00 19.87 C -ANISOU 337 CA ASP A 43 2686 2856 2009 150 -236 -33 C -ATOM 338 C ASP A 43 10.990 -5.025 3.061 1.00 23.61 C -ANISOU 338 C ASP A 43 3144 3364 2463 183 -124 -98 C -ATOM 339 O ASP A 43 10.900 -6.197 3.438 1.00 21.44 O -ANISOU 339 O ASP A 43 2872 3071 2203 209 -124 -148 O -ATOM 340 CB ASP A 43 9.732 -4.369 1.020 1.00 21.07 C -ANISOU 340 CB ASP A 43 2968 3019 2018 103 -287 -16 C -ATOM 341 CG ASP A 43 8.402 -3.946 0.455 1.00 26.75 C -ANISOU 341 CG ASP A 43 3701 3704 2760 73 -445 54 C -ATOM 342 OD1 ASP A 43 7.371 -4.102 1.155 1.00 29.97 O -ANISOU 342 OD1 ASP A 43 4005 4085 3297 95 -509 59 O -ATOM 343 OD2 ASP A 43 8.393 -3.447 -0.679 1.00 28.42 O -ANISOU 343 OD2 ASP A 43 4021 3918 2860 24 -505 109 O -ATOM 344 N ARG A 44 12.144 -4.362 3.062 1.00 22.17 N -ANISOU 344 N ARG A 44 2943 3227 2252 180 -37 -92 N -ATOM 345 CA ARG A 44 13.352 -4.997 3.577 1.00 20.08 C -ANISOU 345 CA ARG A 44 2628 3008 1995 223 56 -145 C -ATOM 346 C ARG A 44 13.216 -5.196 5.079 1.00 23.64 C -ANISOU 346 C ARG A 44 2994 3436 2552 249 40 -146 C -ATOM 347 O ARG A 44 13.563 -6.252 5.620 1.00 23.28 O -ANISOU 347 O ARG A 44 2932 3384 2530 298 48 -184 O -ATOM 348 CB ARG A 44 14.598 -4.157 3.236 1.00 19.96 C -ANISOU 348 CB ARG A 44 2583 3065 1934 190 150 -131 C -ATOM 349 CG ARG A 44 15.876 -4.699 3.830 1.00 21.29 C -ANISOU 349 CG ARG A 44 2652 3296 2141 241 231 -176 C -ATOM 350 CD ARG A 44 16.181 -6.117 3.358 1.00 25.89 C -ANISOU 350 CD ARG A 44 3265 3876 2698 323 267 -253 C -ATOM 351 NE ARG A 44 17.410 -6.611 3.991 1.00 28.49 N -ANISOU 351 NE ARG A 44 3472 4257 3096 397 328 -287 N -ATOM 352 CZ ARG A 44 17.604 -7.863 4.401 1.00 33.52 C -ANISOU 352 CZ ARG A 44 4098 4850 3787 500 313 -333 C -ATOM 353 NH1 ARG A 44 16.656 -8.779 4.230 1.00 29.37 N -ANISOU 353 NH1 ARG A 44 3690 4226 3244 523 253 -360 N -ATOM 354 NH2 ARG A 44 18.757 -8.202 4.968 1.00 34.74 N -ANISOU 354 NH2 ARG A 44 4124 5055 4020 577 347 -347 N -ATOM 355 N THR A 45 12.682 -4.186 5.760 1.00 20.09 N -ANISOU 355 N THR A 45 2508 2965 2162 216 16 -107 N -ATOM 356 CA THR A 45 12.536 -4.244 7.212 1.00 19.95 C -ANISOU 356 CA THR A 45 2431 2931 2216 218 15 -114 C -ATOM 357 C THR A 45 11.589 -5.374 7.612 1.00 23.89 C -ANISOU 357 C THR A 45 2945 3390 2743 231 -30 -133 C -ATOM 358 O THR A 45 11.783 -6.024 8.642 1.00 22.60 O -ANISOU 358 O THR A 45 2767 3220 2599 236 -25 -145 O -ATOM 359 CB THR A 45 12.057 -2.894 7.780 1.00 20.78 C -ANISOU 359 CB THR A 45 2516 3007 2374 181 18 -88 C -ATOM 360 OG1 THR A 45 13.015 -1.881 7.442 1.00 23.00 O -ANISOU 360 OG1 THR A 45 2802 3314 2624 146 56 -65 O -ATOM 361 CG2 THR A 45 11.904 -2.947 9.318 1.00 22.04 C -ANISOU 361 CG2 THR A 45 2640 3157 2580 165 37 -110 C -ATOM 362 N GLU A 46 10.578 -5.633 6.786 1.00 20.49 N -ANISOU 362 N GLU A 46 2550 2930 2304 223 -84 -130 N -ATOM 363 CA GLU A 46 9.669 -6.744 7.071 1.00 17.67 C -ANISOU 363 CA GLU A 46 2208 2536 1971 208 -129 -147 C -ATOM 364 C GLU A 46 10.423 -8.071 7.142 1.00 22.81 C -ANISOU 364 C GLU A 46 2917 3167 2581 240 -118 -182 C -ATOM 365 O GLU A 46 10.200 -8.872 8.056 1.00 20.73 O -ANISOU 365 O GLU A 46 2663 2870 2345 227 -130 -185 O -ATOM 366 CB GLU A 46 8.557 -6.858 6.019 1.00 21.19 C -ANISOU 366 CB GLU A 46 2681 2964 2407 179 -210 -136 C -ATOM 367 CG GLU A 46 7.571 -8.000 6.335 1.00 21.03 C -ANISOU 367 CG GLU A 46 2666 2909 2415 133 -260 -153 C -ATOM 368 CD GLU A 46 6.402 -8.072 5.357 1.00 32.29 C -ANISOU 368 CD GLU A 46 4094 4331 3843 84 -364 -137 C -ATOM 369 OE1 GLU A 46 5.548 -8.962 5.508 1.00 31.60 O -ANISOU 369 OE1 GLU A 46 4005 4222 3779 22 -414 -148 O -ATOM 370 OE2 GLU A 46 6.336 -7.241 4.428 1.00 36.92 O -ANISOU 370 OE2 GLU A 46 4689 4934 4403 95 -410 -104 O -ATOM 371 N ARG A 47 11.318 -8.296 6.183 1.00 21.89 N -ANISOU 371 N ARG A 47 2848 3068 2402 283 -91 -209 N -ATOM 372 CA ARG A 47 12.069 -9.550 6.142 1.00 24.30 C -ANISOU 372 CA ARG A 47 3206 3338 2689 344 -73 -255 C -ATOM 373 C ARG A 47 13.043 -9.550 7.304 1.00 25.52 C -ANISOU 373 C ARG A 47 3288 3515 2895 388 -46 -238 C -ATOM 374 O ARG A 47 13.244 -10.574 7.963 1.00 24.00 O -ANISOU 374 O ARG A 47 3125 3265 2730 425 -73 -242 O -ATOM 375 CB ARG A 47 12.816 -9.709 4.821 1.00 25.74 C -ANISOU 375 CB ARG A 47 3444 3543 2792 384 -19 -306 C -ATOM 376 CG ARG A 47 13.781 -10.896 4.812 1.00 28.90 C -ANISOU 376 CG ARG A 47 3876 3904 3200 483 26 -368 C -ATOM 377 CD ARG A 47 13.040 -12.195 5.065 1.00 32.91 C -ANISOU 377 CD ARG A 47 4489 4294 3723 480 -44 -391 C -ATOM 378 NE ARG A 47 13.950 -13.326 5.264 1.00 37.36 N -ANISOU 378 NE ARG A 47 5086 4786 4324 596 -18 -439 N -ATOM 379 CZ ARG A 47 14.142 -14.301 4.386 1.00 35.97 C -ANISOU 379 CZ ARG A 47 5029 4530 4106 651 12 -527 C -ATOM 380 NH1 ARG A 47 13.477 -14.305 3.229 1.00 32.81 N -ANISOU 380 NH1 ARG A 47 4741 4123 3601 577 12 -574 N -ATOM 381 NH2 ARG A 47 14.990 -15.289 4.666 1.00 34.61 N -ANISOU 381 NH2 ARG A 47 4876 4277 3997 782 34 -569 N -ATOM 382 N LEU A 48 13.634 -8.390 7.571 1.00 21.61 N -ANISOU 382 N LEU A 48 2709 3092 2409 374 -7 -211 N -ATOM 383 CA LEU A 48 14.561 -8.276 8.699 1.00 23.33 C -ANISOU 383 CA LEU A 48 2854 3344 2667 392 -4 -189 C -ATOM 384 C LEU A 48 13.910 -8.674 10.021 1.00 23.21 C -ANISOU 384 C LEU A 48 2863 3281 2677 351 -58 -160 C -ATOM 385 O LEU A 48 14.539 -9.324 10.853 1.00 24.60 O -ANISOU 385 O LEU A 48 3034 3443 2868 382 -93 -141 O -ATOM 386 CB LEU A 48 15.133 -6.861 8.818 1.00 28.00 C -ANISOU 386 CB LEU A 48 3369 4012 3257 344 36 -166 C -ATOM 387 CG LEU A 48 16.333 -6.513 7.954 1.00 35.63 C -ANISOU 387 CG LEU A 48 4278 5056 4203 370 104 -181 C -ATOM 388 CD1 LEU A 48 17.002 -5.248 8.450 1.00 31.23 C -ANISOU 388 CD1 LEU A 48 3645 4566 3656 298 124 -148 C -ATOM 389 CD2 LEU A 48 17.329 -7.654 7.932 1.00 36.55 C -ANISOU 389 CD2 LEU A 48 4350 5187 4351 474 116 -213 C -ATOM 390 N ALA A 49 12.662 -8.260 10.227 1.00 21.05 N -ANISOU 390 N ALA A 49 2608 2984 2404 280 -63 -153 N -ATOM 391 CA ALA A 49 11.957 -8.575 11.465 1.00 22.85 C -ANISOU 391 CA ALA A 49 2859 3181 2641 218 -83 -133 C -ATOM 392 C ALA A 49 11.815 -10.076 11.623 1.00 21.61 C -ANISOU 392 C ALA A 49 2784 2950 2478 232 -133 -128 C -ATOM 393 O ALA A 49 11.940 -10.612 12.727 1.00 21.96 O -ANISOU 393 O ALA A 49 2867 2966 2510 202 -164 -95 O -ATOM 394 CB ALA A 49 10.603 -7.911 11.482 1.00 24.59 C -ANISOU 394 CB ALA A 49 3058 3399 2887 154 -60 -140 C -ATOM 395 N ARG A 50 11.543 -10.768 10.519 1.00 21.68 N -ANISOU 395 N ARG A 50 2841 2914 2482 266 -149 -159 N -ATOM 396 CA ARG A 50 11.395 -12.212 10.598 1.00 24.36 C -ANISOU 396 CA ARG A 50 3284 3153 2816 275 -198 -161 C -ATOM 397 C ARG A 50 12.728 -12.875 10.948 1.00 28.01 C -ANISOU 397 C ARG A 50 3763 3583 3295 381 -222 -150 C -ATOM 398 O ARG A 50 12.773 -13.828 11.744 1.00 30.29 O -ANISOU 398 O ARG A 50 4130 3789 3589 378 -280 -113 O -ATOM 399 CB ARG A 50 10.853 -12.782 9.282 1.00 30.91 C -ANISOU 399 CB ARG A 50 4184 3935 3626 278 -212 -211 C -ATOM 400 CG ARG A 50 10.316 -14.202 9.436 1.00 38.70 C -ANISOU 400 CG ARG A 50 5299 4797 4607 240 -269 -215 C -ATOM 401 CD ARG A 50 9.586 -14.645 8.189 1.00 43.51 C -ANISOU 401 CD ARG A 50 5984 5365 5183 201 -295 -267 C -ATOM 402 NE ARG A 50 10.520 -14.969 7.121 1.00 45.92 N -ANISOU 402 NE ARG A 50 6349 5644 5453 311 -266 -334 N -ATOM 403 CZ ARG A 50 10.255 -14.844 5.825 1.00 47.01 C -ANISOU 403 CZ ARG A 50 6535 5798 5529 293 -262 -388 C -ATOM 404 NH1 ARG A 50 9.079 -14.386 5.421 1.00 46.12 N -ANISOU 404 NH1 ARG A 50 6401 5726 5397 179 -314 -369 N -ATOM 405 NH2 ARG A 50 11.173 -15.169 4.931 1.00 49.43 N -ANISOU 405 NH2 ARG A 50 6905 6084 5791 390 -206 -462 N -ATOM 406 N ASP A 51 13.809 -12.370 10.354 1.00 23.79 N -ANISOU 406 N ASP A 51 3150 3115 2773 470 -180 -176 N -ATOM 407 CA ASP A 51 15.152 -12.886 10.614 1.00 22.46 C -ANISOU 407 CA ASP A 51 2944 2941 2650 590 -199 -169 C -ATOM 408 C ASP A 51 15.511 -12.680 12.082 1.00 25.15 C -ANISOU 408 C ASP A 51 3250 3306 3001 552 -264 -92 C -ATOM 409 O ASP A 51 16.095 -13.553 12.718 1.00 25.18 O -ANISOU 409 O ASP A 51 3284 3245 3036 616 -341 -52 O -ATOM 410 CB ASP A 51 16.183 -12.178 9.716 1.00 25.87 C -ANISOU 410 CB ASP A 51 3262 3474 3093 661 -118 -212 C -ATOM 411 CG ASP A 51 16.028 -12.535 8.233 1.00 31.39 C -ANISOU 411 CG ASP A 51 4023 4147 3755 702 -50 -294 C -ATOM 412 OD1 ASP A 51 15.317 -13.506 7.921 1.00 28.96 O -ANISOU 412 OD1 ASP A 51 3847 3728 3430 702 -81 -324 O -ATOM 413 OD2 ASP A 51 16.642 -11.859 7.378 1.00 27.89 O -ANISOU 413 OD2 ASP A 51 3513 3794 3290 721 36 -330 O -ATOM 414 N VAL A 52 15.155 -11.516 12.611 1.00 25.09 N -ANISOU 414 N VAL A 52 3192 3380 2959 446 -239 -72 N -ATOM 415 CA VAL A 52 15.411 -11.218 14.020 1.00 23.93 C -ANISOU 415 CA VAL A 52 3041 3263 2790 378 -293 -11 C -ATOM 416 C VAL A 52 14.680 -12.219 14.895 1.00 27.83 C -ANISOU 416 C VAL A 52 3667 3658 3250 319 -356 35 C -ATOM 417 O VAL A 52 15.252 -12.812 15.804 1.00 25.44 O -ANISOU 417 O VAL A 52 3407 3321 2937 329 -449 101 O -ATOM 418 CB VAL A 52 14.955 -9.799 14.386 1.00 27.72 C -ANISOU 418 CB VAL A 52 3479 3821 3232 267 -234 -21 C -ATOM 419 CG1 VAL A 52 14.870 -9.640 15.902 1.00 26.10 C -ANISOU 419 CG1 VAL A 52 3324 3624 2967 162 -277 25 C -ATOM 420 CG2 VAL A 52 15.892 -8.751 13.772 1.00 29.09 C -ANISOU 420 CG2 VAL A 52 3537 4088 3429 297 -191 -43 C -ATOM 421 N MET A 53 13.411 -12.437 14.597 1.00 27.48 N -ANISOU 421 N MET A 53 3688 3567 3186 248 -314 10 N -ATOM 422 CA AMET A 53 12.607 -13.333 15.412 0.64 28.63 C -ANISOU 422 CA AMET A 53 3960 3628 3290 154 -353 54 C -ATOM 423 CA BMET A 53 12.599 -13.336 15.408 0.36 28.70 C -ANISOU 423 CA BMET A 53 3969 3637 3300 154 -353 54 C -ATOM 424 C MET A 53 13.095 -14.772 15.334 1.00 30.63 C -ANISOU 424 C MET A 53 4319 3750 3569 238 -446 89 C -ATOM 425 O MET A 53 13.069 -15.505 16.328 1.00 32.28 O -ANISOU 425 O MET A 53 4641 3886 3740 184 -522 163 O -ATOM 426 CB AMET A 53 11.127 -13.202 15.047 0.64 28.63 C -ANISOU 426 CB AMET A 53 3969 3626 3283 51 -285 16 C -ATOM 427 CB BMET A 53 11.115 -13.238 15.021 0.36 28.51 C -ANISOU 427 CB BMET A 53 3956 3607 3268 52 -286 16 C -ATOM 428 CG AMET A 53 10.511 -11.959 15.652 0.64 25.87 C -ANISOU 428 CG AMET A 53 3545 3372 2911 -44 -202 0 C -ATOM 429 CG BMET A 53 10.173 -14.095 15.872 0.36 30.65 C -ANISOU 429 CG BMET A 53 4343 3810 3493 -84 -301 59 C -ATOM 430 SD AMET A 53 10.681 -11.950 17.458 0.64 42.46 S -ANISOU 430 SD AMET A 53 5729 5488 4916 -163 -213 60 S -ATOM 431 SD BMET A 53 9.775 -13.512 17.547 0.36 53.46 S -ANISOU 431 SD BMET A 53 7257 6765 6292 -244 -251 100 S -ATOM 432 CE AMET A 53 9.694 -13.392 17.849 0.64 53.64 C -ANISOU 432 CE AMET A 53 7285 6800 6294 -274 -239 105 C -ATOM 433 CE BMET A 53 10.496 -11.866 17.615 0.36 42.00 C -ANISOU 433 CE BMET A 53 5674 5437 4849 -189 -198 58 C -ATOM 434 N LYS A 54 13.566 -15.175 14.161 1.00 28.38 N -ANISOU 434 N LYS A 54 4014 3426 3342 370 -439 33 N -ATOM 435 CA LYS A 54 14.128 -16.508 14.019 1.00 31.47 C -ANISOU 435 CA LYS A 54 4506 3673 3779 483 -516 47 C -ATOM 436 C LYS A 54 15.356 -16.674 14.917 1.00 34.25 C -ANISOU 436 C LYS A 54 4822 4025 4165 573 -613 124 C -ATOM 437 O LYS A 54 15.554 -17.717 15.540 1.00 33.83 O -ANISOU 437 O LYS A 54 4889 3840 4124 603 -721 194 O -ATOM 438 CB LYS A 54 14.498 -16.782 12.560 1.00 32.32 C -ANISOU 438 CB LYS A 54 4593 3753 3935 615 -460 -51 C -ATOM 439 CG LYS A 54 14.781 -18.248 12.277 1.00 44.31 C -ANISOU 439 CG LYS A 54 6252 5083 5500 724 -518 -66 C -ATOM 440 CD LYS A 54 13.521 -19.087 12.486 1.00 52.91 C -ANISOU 440 CD LYS A 54 7526 6039 6538 579 -559 -45 C -ATOM 441 CE LYS A 54 13.791 -20.573 12.276 1.00 58.88 C -ANISOU 441 CE LYS A 54 8460 6571 7339 677 -628 -56 C -ATOM 442 NZ LYS A 54 14.723 -21.115 13.298 1.00 64.93 N -ANISOU 442 NZ LYS A 54 9252 7254 8163 782 -739 42 N -ATOM 443 N GLU A 55 16.169 -15.628 15.006 1.00 32.10 N -ANISOU 443 N GLU A 55 4389 3899 3909 605 -589 120 N -ATOM 444 CA GLU A 55 17.415 -15.701 15.774 1.00 32.98 C -ANISOU 444 CA GLU A 55 4428 4038 4066 688 -697 193 C -ATOM 445 C GLU A 55 17.212 -15.439 17.272 1.00 32.76 C -ANISOU 445 C GLU A 55 4469 4036 3943 538 -787 294 C -ATOM 446 O GLU A 55 17.862 -16.061 18.115 1.00 35.55 O -ANISOU 446 O GLU A 55 4867 4334 4306 576 -933 390 O -ATOM 447 CB GLU A 55 18.435 -14.707 15.198 1.00 38.73 C -ANISOU 447 CB GLU A 55 4946 4920 4850 763 -635 144 C -ATOM 448 CG GLU A 55 19.751 -14.607 15.972 1.00 48.12 C -ANISOU 448 CG GLU A 55 6011 6175 6096 830 -754 218 C -ATOM 449 CD GLU A 55 20.746 -15.703 15.616 1.00 57.96 C -ANISOU 449 CD GLU A 55 7203 7338 7482 1052 -821 224 C -ATOM 450 OE1 GLU A 55 20.429 -16.554 14.754 1.00 59.45 O -ANISOU 450 OE1 GLU A 55 7474 7402 7710 1152 -762 157 O -ATOM 451 OE2 GLU A 55 21.854 -15.707 16.200 1.00 61.60 O -ANISOU 451 OE2 GLU A 55 7533 7853 8017 1128 -937 291 O -ATOM 452 N MET A 56 16.308 -14.522 17.603 1.00 35.13 N -ANISOU 452 N MET A 56 4784 4413 4149 370 -702 271 N -ATOM 453 CA MET A 56 16.251 -13.996 18.972 1.00 35.87 C -ANISOU 453 CA MET A 56 4928 4565 4136 220 -751 338 C -ATOM 454 C MET A 56 14.935 -14.239 19.700 1.00 38.83 C -ANISOU 454 C MET A 56 5464 4890 4398 43 -708 357 C -ATOM 455 O MET A 56 14.786 -13.827 20.851 1.00 40.34 O -ANISOU 455 O MET A 56 5723 5128 4475 -100 -724 399 O -ATOM 456 CB MET A 56 16.526 -12.486 18.973 1.00 32.64 C -ANISOU 456 CB MET A 56 4388 4308 3708 165 -675 286 C -ATOM 457 CG MET A 56 17.802 -12.067 18.279 1.00 34.54 C -ANISOU 457 CG MET A 56 4449 4627 4047 297 -693 264 C -ATOM 458 SD MET A 56 17.982 -10.281 18.260 1.00 33.35 S -ANISOU 458 SD MET A 56 4185 4625 3863 194 -599 207 S -ATOM 459 CE MET A 56 18.436 -9.990 19.970 1.00 38.79 C -ANISOU 459 CE MET A 56 4945 5358 4437 49 -731 289 C -ATOM 460 N GLY A 57 13.985 -14.890 19.039 1.00 37.47 N -ANISOU 460 N GLY A 57 5354 4633 4251 36 -649 322 N -ATOM 461 CA GLY A 57 12.645 -15.025 19.586 1.00 36.49 C -ANISOU 461 CA GLY A 57 5337 4489 4039 -145 -577 325 C -ATOM 462 C GLY A 57 12.447 -16.084 20.656 1.00 42.22 C -ANISOU 462 C GLY A 57 6259 5109 4672 -253 -671 433 C -ATOM 463 O GLY A 57 11.326 -16.308 21.107 1.00 47.31 O -ANISOU 463 O GLY A 57 6995 5739 5241 -421 -599 439 O -ATOM 464 N GLY A 58 13.525 -16.738 21.073 1.00 41.08 N -ANISOU 464 N GLY A 58 6177 4894 4538 -163 -833 526 N -ATOM 465 CA GLY A 58 13.425 -17.782 22.081 1.00 45.59 C -ANISOU 465 CA GLY A 58 6962 5343 5017 -260 -953 653 C -ATOM 466 C GLY A 58 13.445 -17.256 23.508 1.00 47.05 C -ANISOU 466 C GLY A 58 7233 5611 5032 -439 -979 723 C -ATOM 467 O GLY A 58 13.256 -18.006 24.467 1.00 45.66 O -ANISOU 467 O GLY A 58 7260 5351 4737 -567 -1067 837 O -ATOM 468 N HIS A 59 13.684 -15.960 23.660 1.00 44.90 N -ANISOU 468 N HIS A 59 6829 5498 4734 -461 -904 656 N -ATOM 469 CA HIS A 59 13.776 -15.372 24.989 1.00 44.18 C -ANISOU 469 CA HIS A 59 6830 5490 4467 -634 -923 701 C -ATOM 470 C HIS A 59 13.419 -13.892 24.923 1.00 42.30 C -ANISOU 470 C HIS A 59 6465 5400 4207 -693 -748 571 C -ATOM 471 O HIS A 59 13.522 -13.283 23.868 1.00 43.00 O -ANISOU 471 O HIS A 59 6376 5531 4431 -565 -674 479 O -ATOM 472 CB HIS A 59 15.188 -15.555 25.548 1.00 49.42 C -ANISOU 472 CB HIS A 59 7505 6149 5122 -557 -1154 814 C -ATOM 473 CG HIS A 59 15.350 -15.092 26.965 1.00 56.52 C -ANISOU 473 CG HIS A 59 8542 7121 5811 -755 -1216 878 C -ATOM 474 ND1 HIS A 59 14.929 -15.838 28.046 1.00 60.12 N -ANISOU 474 ND1 HIS A 59 9251 7506 6086 -933 -1284 993 N -ATOM 475 CD2 HIS A 59 15.899 -13.964 27.480 1.00 58.33 C -ANISOU 475 CD2 HIS A 59 8714 7484 5965 -821 -1223 842 C -ATOM 476 CE1 HIS A 59 15.207 -15.189 29.164 1.00 61.88 C -ANISOU 476 CE1 HIS A 59 9569 7822 6119 -1099 -1327 1022 C -ATOM 477 NE2 HIS A 59 15.797 -14.050 28.849 1.00 59.83 N -ANISOU 477 NE2 HIS A 59 9125 7685 5924 -1034 -1294 927 N -ATOM 478 N HIS A 60 12.989 -13.336 26.056 1.00 37.20 N -ANISOU 478 N HIS A 60 5930 4820 3384 -892 -679 563 N -ATOM 479 CA HIS A 60 12.658 -11.922 26.192 1.00 34.32 C -ANISOU 479 CA HIS A 60 5484 4571 2985 -958 -513 437 C -ATOM 480 C HIS A 60 13.660 -11.035 25.446 1.00 36.70 C -ANISOU 480 C HIS A 60 5602 4932 3410 -805 -558 388 C -ATOM 481 O HIS A 60 14.863 -11.095 25.703 1.00 36.61 O -ANISOU 481 O HIS A 60 5577 4937 3395 -759 -734 462 O -ATOM 482 CB HIS A 60 12.641 -11.577 27.683 1.00 38.63 C -ANISOU 482 CB HIS A 60 6214 5167 3296 -1174 -511 462 C -ATOM 483 CG HIS A 60 12.123 -10.209 28.002 1.00 47.66 C -ANISOU 483 CG HIS A 60 7327 6402 4380 -1267 -313 317 C -ATOM 484 ND1 HIS A 60 11.320 -9.962 29.100 1.00 51.86 N -ANISOU 484 ND1 HIS A 60 8017 6968 4718 -1478 -167 273 N -ATOM 485 CD2 HIS A 60 12.323 -9.009 27.405 1.00 46.42 C -ANISOU 485 CD2 HIS A 60 7016 6295 4325 -1180 -233 205 C -ATOM 486 CE1 HIS A 60 11.032 -8.675 29.147 1.00 52.15 C -ANISOU 486 CE1 HIS A 60 7992 7066 4756 -1497 0 127 C -ATOM 487 NE2 HIS A 60 11.623 -8.073 28.133 1.00 48.85 N -ANISOU 487 NE2 HIS A 60 7392 6650 4518 -1320 -47 91 N -ATOM 488 N ILE A 61 13.158 -10.234 24.511 1.00 32.61 N -ANISOU 488 N ILE A 61 4937 4445 3007 -734 -407 272 N -ATOM 489 CA ILE A 61 13.997 -9.311 23.742 1.00 32.47 C -ANISOU 489 CA ILE A 61 4758 4482 3097 -617 -421 223 C -ATOM 490 C ILE A 61 13.904 -7.899 24.330 1.00 37.20 C -ANISOU 490 C ILE A 61 5368 5151 3616 -728 -320 135 C -ATOM 491 O ILE A 61 12.806 -7.421 24.628 1.00 36.57 O -ANISOU 491 O ILE A 61 5331 5071 3492 -813 -152 53 O -ATOM 492 CB ILE A 61 13.563 -9.266 22.254 1.00 35.50 C -ANISOU 492 CB ILE A 61 4998 4844 3648 -471 -335 161 C -ATOM 493 CG1 ILE A 61 13.805 -10.615 21.571 1.00 36.90 C -ANISOU 493 CG1 ILE A 61 5173 4940 3906 -350 -435 227 C -ATOM 494 CG2 ILE A 61 14.306 -8.171 21.486 1.00 28.30 C -ANISOU 494 CG2 ILE A 61 3941 3991 2822 -388 -320 108 C -ATOM 495 CD1 ILE A 61 13.306 -10.661 20.132 1.00 39.37 C -ANISOU 495 CD1 ILE A 61 5382 5229 4347 -236 -356 163 C -ATOM 496 N VAL A 62 15.052 -7.250 24.524 1.00 34.71 N -ANISOU 496 N VAL A 62 5012 4889 3286 -732 -419 149 N -ATOM 497 CA VAL A 62 15.086 -5.817 24.812 1.00 37.92 C -ANISOU 497 CA VAL A 62 5420 5340 3647 -818 -328 52 C -ATOM 498 C VAL A 62 15.607 -5.120 23.572 1.00 34.07 C -ANISOU 498 C VAL A 62 4756 4869 3318 -690 -312 15 C -ATOM 499 O VAL A 62 16.746 -5.353 23.177 1.00 30.26 O -ANISOU 499 O VAL A 62 4173 4426 2899 -619 -444 78 O -ATOM 500 CB VAL A 62 16.041 -5.470 25.959 1.00 40.23 C -ANISOU 500 CB VAL A 62 5810 5686 3789 -959 -461 91 C -ATOM 501 CG1 VAL A 62 16.106 -3.966 26.159 1.00 40.75 C -ANISOU 501 CG1 VAL A 62 5891 5776 3817 -1050 -365 -22 C -ATOM 502 CG2 VAL A 62 15.579 -6.113 27.227 1.00 44.62 C -ANISOU 502 CG2 VAL A 62 6573 6228 4151 -1112 -483 137 C -ATOM 503 N ALA A 63 14.784 -4.271 22.962 1.00 28.57 N -ANISOU 503 N ALA A 63 4019 4146 2689 -661 -151 -82 N -ATOM 504 CA ALA A 63 15.208 -3.519 21.778 1.00 27.30 C -ANISOU 504 CA ALA A 63 3724 3992 2657 -564 -130 -109 C -ATOM 505 C ALA A 63 15.751 -2.162 22.221 1.00 29.13 C -ANISOU 505 C ALA A 63 3988 4243 2839 -669 -115 -164 C -ATOM 506 O ALA A 63 15.056 -1.382 22.877 1.00 29.59 O -ANISOU 506 O ALA A 63 4150 4262 2830 -758 -5 -249 O -ATOM 507 CB ALA A 63 14.055 -3.350 20.800 1.00 27.80 C -ANISOU 507 CB ALA A 63 3734 4003 2825 -473 0 -164 C -ATOM 508 N LEU A 64 17.008 -1.892 21.879 1.00 24.60 N -ANISOU 508 N LEU A 64 3324 3726 2298 -666 -220 -121 N -ATOM 509 CA LEU A 64 17.661 -0.653 22.278 1.00 27.28 C -ANISOU 509 CA LEU A 64 3694 4084 2588 -791 -230 -163 C -ATOM 510 C LEU A 64 17.797 0.285 21.065 1.00 27.80 C -ANISOU 510 C LEU A 64 3667 4126 2770 -734 -158 -194 C -ATOM 511 O LEU A 64 18.538 -0.004 20.126 1.00 26.63 O -ANISOU 511 O LEU A 64 3379 4032 2709 -655 -206 -140 O -ATOM 512 CB LEU A 64 19.026 -0.979 22.875 1.00 31.36 C -ANISOU 512 CB LEU A 64 4168 4695 3051 -865 -417 -81 C -ATOM 513 CG LEU A 64 19.883 0.141 23.457 1.00 36.03 C -ANISOU 513 CG LEU A 64 4794 5326 3571 -1036 -476 -108 C -ATOM 514 CD1 LEU A 64 19.158 0.868 24.593 1.00 38.00 C -ANISOU 514 CD1 LEU A 64 5266 5510 3662 -1192 -397 -203 C -ATOM 515 CD2 LEU A 64 21.202 -0.430 23.962 1.00 39.19 C -ANISOU 515 CD2 LEU A 64 5105 5839 3946 -1084 -693 -4 C -ATOM 516 N CYS A 65 17.076 1.405 21.084 1.00 27.57 N -ANISOU 516 N CYS A 65 3726 4009 2739 -774 -37 -283 N -ATOM 517 CA CYS A 65 17.091 2.352 19.975 1.00 25.75 C -ANISOU 517 CA CYS A 65 3447 3730 2608 -731 23 -301 C -ATOM 518 C CYS A 65 18.256 3.333 20.102 1.00 23.97 C -ANISOU 518 C CYS A 65 3225 3531 2352 -869 -34 -298 C -ATOM 519 O CYS A 65 18.387 4.000 21.123 1.00 25.94 O -ANISOU 519 O CYS A 65 3599 3753 2505 -1011 -41 -354 O -ATOM 520 CB CYS A 65 15.786 3.148 19.963 1.00 29.40 C -ANISOU 520 CB CYS A 65 4003 4063 3104 -698 164 -390 C -ATOM 521 SG CYS A 65 15.756 4.446 18.689 1.00 28.02 S -ANISOU 521 SG CYS A 65 3814 3791 3041 -655 214 -397 S -ATOM 522 N VAL A 66 19.101 3.436 19.076 1.00 25.02 N -ANISOU 522 N VAL A 66 3229 3720 2556 -845 -69 -241 N -ATOM 523 CA VAL A 66 20.176 4.433 19.121 1.00 25.41 C -ANISOU 523 CA VAL A 66 3270 3798 2585 -1000 -113 -236 C -ATOM 524 C VAL A 66 19.708 5.753 18.494 1.00 30.51 C -ANISOU 524 C VAL A 66 4014 4308 3270 -1027 -14 -282 C -ATOM 525 O VAL A 66 19.659 5.884 17.270 1.00 25.00 O -ANISOU 525 O VAL A 66 3253 3596 2648 -951 28 -243 O -ATOM 526 CB VAL A 66 21.469 3.953 18.416 1.00 30.32 C -ANISOU 526 CB VAL A 66 3688 4568 3263 -992 -191 -152 C -ATOM 527 CG1 VAL A 66 22.588 4.943 18.667 1.00 32.08 C -ANISOU 527 CG1 VAL A 66 3892 4840 3457 -1190 -247 -146 C -ATOM 528 CG2 VAL A 66 21.884 2.565 18.920 1.00 30.64 C -ANISOU 528 CG2 VAL A 66 3625 4717 3299 -918 -299 -98 C -ATOM 529 N LEU A 67 19.362 6.710 19.356 1.00 28.98 N -ANISOU 529 N LEU A 67 3992 4003 3015 -1137 21 -365 N -ATOM 530 CA LEU A 67 18.895 8.040 18.959 1.00 27.02 C -ANISOU 530 CA LEU A 67 3873 3586 2808 -1163 105 -417 C -ATOM 531 C LEU A 67 20.050 8.855 18.393 1.00 29.89 C -ANISOU 531 C LEU A 67 4208 3971 3177 -1309 58 -368 C -ATOM 532 O LEU A 67 21.204 8.576 18.732 1.00 31.73 O -ANISOU 532 O LEU A 67 4345 4350 3363 -1433 -40 -327 O -ATOM 533 CB LEU A 67 18.325 8.749 20.193 1.00 26.02 C -ANISOU 533 CB LEU A 67 3947 3337 2605 -1247 160 -539 C -ATOM 534 CG LEU A 67 17.074 8.087 20.745 1.00 28.51 C -ANISOU 534 CG LEU A 67 4294 3624 2915 -1120 246 -600 C -ATOM 535 CD1 LEU A 67 16.631 8.724 22.060 1.00 28.89 C -ANISOU 535 CD1 LEU A 67 4543 3576 2860 -1224 321 -736 C -ATOM 536 CD2 LEU A 67 15.961 8.120 19.709 1.00 26.56 C -ANISOU 536 CD2 LEU A 67 3996 3284 2810 -923 332 -592 C -ATOM 537 N LYS A 68 19.767 9.854 17.546 1.00 28.86 N -ANISOU 537 N LYS A 68 4157 3701 3107 -1305 116 -363 N -ATOM 538 CA LYS A 68 18.409 10.183 17.095 1.00 26.76 C -ANISOU 538 CA LYS A 68 3982 3266 2921 -1141 206 -397 C -ATOM 539 C LYS A 68 18.056 9.431 15.831 1.00 28.61 C -ANISOU 539 C LYS A 68 4083 3559 3227 -977 211 -311 C -ATOM 540 O LYS A 68 16.889 9.085 15.602 1.00 25.96 O -ANISOU 540 O LYS A 68 3748 3163 2954 -812 253 -328 O -ATOM 541 CB LYS A 68 18.296 11.679 16.800 1.00 27.05 C -ANISOU 541 CB LYS A 68 4192 3094 2990 -1215 240 -420 C -ATOM 542 CG LYS A 68 18.362 12.618 18.000 1.00 28.68 C -ANISOU 542 CG LYS A 68 4592 3173 3133 -1361 259 -537 C -ATOM 543 CD LYS A 68 18.368 14.049 17.463 1.00 31.53 C -ANISOU 543 CD LYS A 68 5123 3313 3542 -1429 280 -536 C -ATOM 544 CE LYS A 68 18.528 15.095 18.519 1.00 40.91 C -ANISOU 544 CE LYS A 68 6533 4345 4667 -1593 300 -657 C -ATOM 545 NZ LYS A 68 18.287 16.416 17.870 1.00 42.88 N -ANISOU 545 NZ LYS A 68 6963 4335 4996 -1605 325 -650 N -ATOM 546 N GLY A 69 19.074 9.181 15.008 1.00 26.17 N -ANISOU 546 N GLY A 69 3659 3377 2908 -1034 172 -225 N -ATOM 547 CA GLY A 69 18.892 8.680 13.654 1.00 23.46 C -ANISOU 547 CA GLY A 69 3229 3077 2607 -919 186 -148 C -ATOM 548 C GLY A 69 18.256 7.304 13.577 1.00 24.57 C -ANISOU 548 C GLY A 69 3266 3300 2769 -748 184 -149 C -ATOM 549 O GLY A 69 17.649 6.935 12.567 1.00 25.17 O -ANISOU 549 O GLY A 69 3320 3363 2880 -631 199 -110 O -ATOM 550 N GLY A 70 18.385 6.527 14.641 1.00 21.95 N -ANISOU 550 N GLY A 70 2887 3048 2404 -748 156 -187 N -ATOM 551 CA GLY A 70 17.788 5.200 14.625 1.00 22.42 C -ANISOU 551 CA GLY A 70 2870 3169 2480 -605 149 -184 C -ATOM 552 C GLY A 70 16.280 5.147 14.854 1.00 23.64 C -ANISOU 552 C GLY A 70 3095 3211 2676 -496 197 -233 C -ATOM 553 O GLY A 70 15.682 4.071 14.731 1.00 22.33 O -ANISOU 553 O GLY A 70 2871 3085 2527 -392 193 -225 O -ATOM 554 N TYR A 71 15.651 6.273 15.188 1.00 23.52 N -ANISOU 554 N TYR A 71 3196 3052 2687 -518 245 -286 N -ATOM 555 CA TYR A 71 14.288 6.210 15.738 1.00 25.86 C -ANISOU 555 CA TYR A 71 3532 3263 3029 -426 307 -355 C -ATOM 556 C TYR A 71 13.235 5.666 14.760 1.00 21.87 C -ANISOU 556 C TYR A 71 2954 2743 2613 -272 309 -318 C -ATOM 557 O TYR A 71 12.316 4.948 15.167 1.00 23.98 O -ANISOU 557 O TYR A 71 3180 3027 2905 -203 340 -352 O -ATOM 558 CB TYR A 71 13.854 7.556 16.350 1.00 26.17 C -ANISOU 558 CB TYR A 71 3710 3139 3094 -465 374 -440 C -ATOM 559 CG TYR A 71 12.933 8.398 15.486 1.00 27.52 C -ANISOU 559 CG TYR A 71 3914 3154 3390 -349 399 -430 C -ATOM 560 CD1 TYR A 71 11.559 8.173 15.466 1.00 26.33 C -ANISOU 560 CD1 TYR A 71 3714 2951 3340 -201 449 -466 C -ATOM 561 CD2 TYR A 71 13.436 9.440 14.717 1.00 25.96 C -ANISOU 561 CD2 TYR A 71 3794 2857 3211 -397 365 -378 C -ATOM 562 CE1 TYR A 71 10.722 8.937 14.682 1.00 27.90 C -ANISOU 562 CE1 TYR A 71 3924 3007 3670 -82 445 -445 C -ATOM 563 CE2 TYR A 71 12.611 10.209 13.923 1.00 29.00 C -ANISOU 563 CE2 TYR A 71 4225 3084 3710 -287 360 -350 C -ATOM 564 CZ TYR A 71 11.255 9.953 13.908 1.00 31.91 C -ANISOU 564 CZ TYR A 71 4528 3405 4191 -119 391 -382 C -ATOM 565 OH TYR A 71 10.428 10.722 13.119 1.00 32.79 O -ANISOU 565 OH TYR A 71 4669 3358 4433 3 361 -341 O -ATOM 566 N LYS A 72 13.352 6.013 13.481 1.00 22.38 N -ANISOU 566 N LYS A 72 3011 2780 2714 -237 271 -246 N -ATOM 567 CA LYS A 72 12.397 5.532 12.474 1.00 23.03 C -ANISOU 567 CA LYS A 72 3037 2852 2863 -112 245 -202 C -ATOM 568 C LYS A 72 12.523 4.034 12.210 1.00 25.35 C -ANISOU 568 C LYS A 72 3236 3280 3115 -79 214 -177 C -ATOM 569 O LYS A 72 11.534 3.302 12.258 1.00 25.33 O -ANISOU 569 O LYS A 72 3184 3284 3154 -3 214 -192 O -ATOM 570 CB LYS A 72 12.552 6.304 11.154 1.00 26.87 C -ANISOU 570 CB LYS A 72 3572 3273 3366 -107 199 -120 C -ATOM 571 CG LYS A 72 11.754 7.594 11.105 1.00 36.92 C -ANISOU 571 CG LYS A 72 4931 4361 4736 -59 204 -128 C -ATOM 572 CD LYS A 72 10.260 7.310 11.152 1.00 44.86 C -ANISOU 572 CD LYS A 72 5866 5319 5859 88 204 -156 C -ATOM 573 CE LYS A 72 9.778 6.692 9.852 1.00 49.93 C -ANISOU 573 CE LYS A 72 6452 6006 6513 157 112 -66 C -ATOM 574 NZ LYS A 72 8.423 6.081 9.989 1.00 51.61 N -ANISOU 574 NZ LYS A 72 6552 6229 6829 271 103 -94 N -ATOM 575 N PHE A 73 13.738 3.588 11.905 1.00 20.75 N -ANISOU 575 N PHE A 73 2625 2800 2460 -136 190 -141 N -ATOM 576 CA PHE A 73 14.013 2.174 11.703 1.00 19.77 C -ANISOU 576 CA PHE A 73 2426 2783 2303 -96 164 -127 C -ATOM 577 C PHE A 73 13.567 1.365 12.916 1.00 21.76 C -ANISOU 577 C PHE A 73 2664 3053 2550 -87 171 -172 C -ATOM 578 O PHE A 73 12.945 0.305 12.784 1.00 22.96 O -ANISOU 578 O PHE A 73 2786 3223 2713 -27 155 -169 O -ATOM 579 CB PHE A 73 15.511 1.977 11.408 1.00 22.76 C -ANISOU 579 CB PHE A 73 2756 3264 2626 -153 155 -98 C -ATOM 580 CG PHE A 73 15.899 0.556 11.085 1.00 22.83 C -ANISOU 580 CG PHE A 73 2692 3364 2618 -88 136 -90 C -ATOM 581 CD1 PHE A 73 15.189 -0.192 10.152 1.00 22.30 C -ANISOU 581 CD1 PHE A 73 2634 3284 2557 -4 128 -83 C -ATOM 582 CD2 PHE A 73 17.006 -0.018 11.684 1.00 21.49 C -ANISOU 582 CD2 PHE A 73 2450 3284 2430 -109 114 -89 C -ATOM 583 CE1 PHE A 73 15.579 -1.510 9.848 1.00 22.68 C -ANISOU 583 CE1 PHE A 73 2638 3390 2589 59 117 -89 C -ATOM 584 CE2 PHE A 73 17.395 -1.334 11.389 1.00 22.21 C -ANISOU 584 CE2 PHE A 73 2479 3435 2526 -25 96 -85 C -ATOM 585 CZ PHE A 73 16.687 -2.069 10.470 1.00 23.71 C -ANISOU 585 CZ PHE A 73 2697 3593 2717 59 106 -92 C -ATOM 586 N PHE A 74 13.860 1.887 14.098 1.00 19.78 N -ANISOU 586 N PHE A 74 2456 2791 2270 -167 192 -211 N -ATOM 587 CA PHE A 74 13.454 1.255 15.351 1.00 21.07 C -ANISOU 587 CA PHE A 74 2639 2968 2397 -191 206 -251 C -ATOM 588 C PHE A 74 11.931 1.110 15.443 1.00 23.55 C -ANISOU 588 C PHE A 74 2952 3224 2773 -129 264 -289 C -ATOM 589 O PHE A 74 11.441 0.019 15.694 1.00 21.64 O -ANISOU 589 O PHE A 74 2686 3016 2520 -111 257 -284 O -ATOM 590 CB PHE A 74 14.008 2.066 16.518 1.00 20.56 C -ANISOU 590 CB PHE A 74 2649 2892 2269 -309 222 -295 C -ATOM 591 CG PHE A 74 13.627 1.548 17.885 1.00 23.16 C -ANISOU 591 CG PHE A 74 3036 3237 2526 -365 244 -337 C -ATOM 592 CD1 PHE A 74 14.287 0.459 18.449 1.00 28.82 C -ANISOU 592 CD1 PHE A 74 3741 4040 3170 -399 164 -291 C -ATOM 593 CD2 PHE A 74 12.662 2.201 18.632 1.00 26.05 C -ANISOU 593 CD2 PHE A 74 3478 3528 2892 -389 347 -423 C -ATOM 594 CE1 PHE A 74 13.959 0.011 19.728 1.00 27.60 C -ANISOU 594 CE1 PHE A 74 3670 3895 2922 -476 176 -315 C -ATOM 595 CE2 PHE A 74 12.324 1.756 19.921 1.00 31.66 C -ANISOU 595 CE2 PHE A 74 4261 4262 3507 -467 389 -467 C -ATOM 596 CZ PHE A 74 12.979 0.659 20.461 1.00 28.03 C -ANISOU 596 CZ PHE A 74 3809 3889 2952 -522 296 -405 C -ATOM 597 N ALA A 75 11.185 2.196 15.221 1.00 22.14 N -ANISOU 597 N ALA A 75 2792 2952 2668 -96 316 -324 N -ATOM 598 CA ALA A 75 9.731 2.144 15.371 1.00 23.94 C -ANISOU 598 CA ALA A 75 2981 3134 2980 -30 377 -367 C -ATOM 599 C ALA A 75 9.153 1.134 14.384 1.00 25.15 C -ANISOU 599 C ALA A 75 3050 3327 3177 41 316 -311 C -ATOM 600 O ALA A 75 8.282 0.309 14.726 1.00 24.30 O -ANISOU 600 O ALA A 75 2895 3248 3089 47 341 -328 O -ATOM 601 CB ALA A 75 9.105 3.538 15.164 1.00 24.67 C -ANISOU 601 CB ALA A 75 3094 3103 3176 25 425 -405 C -ATOM 602 N ASP A 76 9.656 1.179 13.161 1.00 22.09 N -ANISOU 602 N ASP A 76 2658 2945 2790 73 241 -247 N -ATOM 603 CA ASP A 76 9.147 0.321 12.092 1.00 21.86 C -ANISOU 603 CA ASP A 76 2579 2943 2783 128 175 -201 C -ATOM 604 C ASP A 76 9.529 -1.143 12.256 1.00 25.29 C -ANISOU 604 C ASP A 76 3009 3451 3148 105 148 -191 C -ATOM 605 O ASP A 76 8.683 -2.041 12.113 1.00 22.70 O -ANISOU 605 O ASP A 76 2647 3133 2844 119 128 -191 O -ATOM 606 CB ASP A 76 9.613 0.851 10.732 1.00 24.06 C -ANISOU 606 CB ASP A 76 2885 3204 3051 151 113 -140 C -ATOM 607 CG ASP A 76 8.891 2.119 10.322 1.00 27.14 C -ANISOU 607 CG ASP A 76 3286 3494 3534 198 102 -125 C -ATOM 608 OD1 ASP A 76 7.837 2.415 10.915 1.00 29.23 O -ANISOU 608 OD1 ASP A 76 3501 3709 3897 243 139 -167 O -ATOM 609 OD2 ASP A 76 9.369 2.807 9.395 1.00 28.30 O -ANISOU 609 OD2 ASP A 76 3490 3606 3656 191 59 -68 O -ATOM 610 N LEU A 77 10.801 -1.392 12.556 1.00 20.51 N -ANISOU 610 N LEU A 77 2434 2891 2468 68 140 -181 N -ATOM 611 CA LEU A 77 11.246 -2.763 12.805 1.00 20.00 C -ANISOU 611 CA LEU A 77 2373 2873 2353 66 106 -169 C -ATOM 612 C LEU A 77 10.453 -3.364 13.976 1.00 19.10 C -ANISOU 612 C LEU A 77 2274 2751 2233 22 133 -193 C -ATOM 613 O LEU A 77 9.997 -4.513 13.904 1.00 19.88 O -ANISOU 613 O LEU A 77 2378 2848 2328 26 105 -181 O -ATOM 614 CB LEU A 77 12.757 -2.803 13.096 1.00 21.22 C -ANISOU 614 CB LEU A 77 2528 3080 2453 43 85 -152 C -ATOM 615 CG LEU A 77 13.390 -4.153 13.456 1.00 24.74 C -ANISOU 615 CG LEU A 77 2976 3559 2867 63 34 -131 C -ATOM 616 CD1 LEU A 77 13.288 -5.128 12.306 1.00 24.18 C -ANISOU 616 CD1 LEU A 77 2901 3477 2810 140 10 -125 C -ATOM 617 CD2 LEU A 77 14.858 -3.978 13.859 1.00 26.66 C -ANISOU 617 CD2 LEU A 77 3182 3864 3084 44 2 -111 C -ATOM 618 N LEU A 78 10.257 -2.597 15.041 1.00 18.84 N -ANISOU 618 N LEU A 78 2264 2706 2189 -34 197 -232 N -ATOM 619 CA ALEU A 78 9.499 -3.128 16.175 0.72 22.44 C -ANISOU 619 CA ALEU A 78 2745 3164 2615 -97 248 -259 C -ATOM 620 CA BLEU A 78 9.487 -3.085 16.187 0.28 22.37 C -ANISOU 620 CA BLEU A 78 2737 3155 2608 -97 251 -261 C -ATOM 621 C LEU A 78 8.045 -3.371 15.795 1.00 23.63 C -ANISOU 621 C LEU A 78 2828 3298 2851 -72 287 -278 C -ATOM 622 O LEU A 78 7.432 -4.332 16.264 1.00 22.55 O -ANISOU 622 O LEU A 78 2698 3176 2694 -123 301 -274 O -ATOM 623 CB ALEU A 78 9.590 -2.223 17.407 0.72 23.19 C -ANISOU 623 CB ALEU A 78 2899 3254 2660 -174 327 -315 C -ATOM 624 CB BLEU A 78 9.509 -2.083 17.342 0.28 23.73 C -ANISOU 624 CB BLEU A 78 2961 3316 2740 -167 335 -321 C -ATOM 625 CG ALEU A 78 10.559 -2.727 18.466 0.72 27.52 C -ANISOU 625 CG ALEU A 78 3533 3841 3081 -264 281 -290 C -ATOM 626 CG BLEU A 78 10.676 -2.162 18.315 0.28 27.68 C -ANISOU 626 CG BLEU A 78 3546 3850 3120 -254 294 -306 C -ATOM 627 CD1ALEU A 78 11.963 -2.773 17.875 0.72 27.08 C -ANISOU 627 CD1ALEU A 78 3456 3816 3018 -229 174 -234 C -ATOM 628 CD1BLEU A 78 10.323 -1.456 19.604 0.28 31.52 C -ANISOU 628 CD1BLEU A 78 4116 4323 3538 -352 394 -381 C -ATOM 629 CD2ALEU A 78 10.528 -1.834 19.691 0.72 32.44 C -ANISOU 629 CD2ALEU A 78 4241 4455 3629 -364 362 -358 C -ATOM 630 CD2BLEU A 78 11.032 -3.593 18.598 0.28 26.45 C -ANISOU 630 CD2BLEU A 78 3419 3729 2904 -273 211 -241 C -ATOM 631 N ASP A 79 7.491 -2.517 14.944 1.00 20.71 N -ANISOU 631 N ASP A 79 2393 2897 2579 -2 292 -288 N -ATOM 632 CA ASP A 79 6.105 -2.729 14.523 1.00 22.41 C -ANISOU 632 CA ASP A 79 2511 3108 2894 26 304 -297 C -ATOM 633 C ASP A 79 5.961 -4.042 13.759 1.00 20.98 C -ANISOU 633 C ASP A 79 2327 2949 2696 18 212 -248 C -ATOM 634 O ASP A 79 4.965 -4.760 13.911 1.00 21.90 O -ANISOU 634 O ASP A 79 2392 3082 2846 -24 223 -254 O -ATOM 635 CB ASP A 79 5.595 -1.557 13.680 1.00 27.90 C -ANISOU 635 CB ASP A 79 3141 3755 3706 117 290 -298 C -ATOM 636 CG ASP A 79 5.073 -0.420 14.526 1.00 32.20 C -ANISOU 636 CG ASP A 79 3660 4255 4321 136 407 -371 C -ATOM 637 OD1 ASP A 79 4.966 -0.592 15.757 1.00 32.13 O -ANISOU 637 OD1 ASP A 79 3679 4269 4260 65 515 -430 O -ATOM 638 OD2 ASP A 79 4.748 0.638 13.956 1.00 32.29 O -ANISOU 638 OD2 ASP A 79 3636 4198 4434 221 393 -370 O -ATOM 639 N TYR A 80 6.943 -4.355 12.925 1.00 19.31 N -ANISOU 639 N TYR A 80 2172 2736 2431 51 131 -209 N -ATOM 640 CA TYR A 80 6.911 -5.628 12.193 1.00 19.11 C -ANISOU 640 CA TYR A 80 2174 2711 2376 47 52 -181 C -ATOM 641 C TYR A 80 7.100 -6.820 13.121 1.00 23.96 C -ANISOU 641 C TYR A 80 2853 3324 2928 -18 59 -177 C -ATOM 642 O TYR A 80 6.465 -7.863 12.948 1.00 21.45 O -ANISOU 642 O TYR A 80 2550 2988 2611 -60 24 -167 O -ATOM 643 CB TYR A 80 7.967 -5.668 11.069 1.00 18.82 C -ANISOU 643 CB TYR A 80 2186 2673 2290 104 -7 -158 C -ATOM 644 CG TYR A 80 7.540 -4.928 9.812 1.00 21.36 C -ANISOU 644 CG TYR A 80 2480 2987 2648 144 -52 -140 C -ATOM 645 CD1 TYR A 80 6.532 -5.437 9.001 1.00 24.65 C -ANISOU 645 CD1 TYR A 80 2876 3397 3093 134 -124 -129 C -ATOM 646 CD2 TYR A 80 8.156 -3.738 9.429 1.00 20.33 C -ANISOU 646 CD2 TYR A 80 2357 2853 2515 174 -39 -125 C -ATOM 647 CE1 TYR A 80 6.132 -4.781 7.836 1.00 26.18 C -ANISOU 647 CE1 TYR A 80 3058 3584 3306 162 -195 -96 C -ATOM 648 CE2 TYR A 80 7.765 -3.070 8.266 1.00 24.00 C -ANISOU 648 CE2 TYR A 80 2823 3299 2999 201 -98 -89 C -ATOM 649 CZ TYR A 80 6.746 -3.599 7.487 1.00 24.30 C -ANISOU 649 CZ TYR A 80 2840 3332 3059 199 -181 -72 C -ATOM 650 OH TYR A 80 6.340 -2.963 6.338 1.00 23.37 O -ANISOU 650 OH TYR A 80 2735 3196 2947 218 -267 -22 O -ATOM 651 N ILE A 81 8.002 -6.687 14.083 1.00 21.07 N -ANISOU 651 N ILE A 81 2539 2967 2501 -37 86 -174 N -ATOM 652 CA ILE A 81 8.198 -7.744 15.079 1.00 20.77 C -ANISOU 652 CA ILE A 81 2581 2917 2394 -105 75 -151 C -ATOM 653 C ILE A 81 6.920 -7.999 15.866 1.00 24.27 C -ANISOU 653 C ILE A 81 3011 3365 2844 -207 146 -168 C -ATOM 654 O ILE A 81 6.542 -9.148 16.087 1.00 24.40 O -ANISOU 654 O ILE A 81 3083 3355 2832 -273 119 -141 O -ATOM 655 CB ILE A 81 9.360 -7.407 16.040 1.00 25.31 C -ANISOU 655 CB ILE A 81 3209 3512 2897 -120 71 -137 C -ATOM 656 CG1 ILE A 81 10.691 -7.494 15.291 1.00 26.29 C -ANISOU 656 CG1 ILE A 81 3325 3641 3021 -29 -2 -113 C -ATOM 657 CG2 ILE A 81 9.374 -8.382 17.220 1.00 24.76 C -ANISOU 657 CG2 ILE A 81 3239 3425 2745 -210 51 -100 C -ATOM 658 CD1 ILE A 81 11.890 -6.995 16.109 1.00 27.49 C -ANISOU 658 CD1 ILE A 81 3488 3832 3124 -47 -24 -96 C -ATOM 659 N LYS A 82 6.246 -6.923 16.274 1.00 21.37 N -ANISOU 659 N LYS A 82 2570 3028 2521 -222 246 -218 N -ATOM 660 CA LYS A 82 4.989 -7.031 17.006 1.00 19.32 C -ANISOU 660 CA LYS A 82 2263 2794 2285 -314 349 -252 C -ATOM 661 C LYS A 82 3.912 -7.753 16.199 1.00 23.63 C -ANISOU 661 C LYS A 82 2724 3341 2913 -330 312 -238 C -ATOM 662 O LYS A 82 3.143 -8.541 16.738 1.00 25.65 O -ANISOU 662 O LYS A 82 2981 3612 3153 -444 354 -234 O -ATOM 663 CB LYS A 82 4.504 -5.643 17.412 1.00 22.82 C -ANISOU 663 CB LYS A 82 2626 3256 2790 -287 472 -325 C -ATOM 664 CG LYS A 82 5.241 -5.097 18.635 1.00 28.24 C -ANISOU 664 CG LYS A 82 3421 3946 3364 -343 541 -357 C -ATOM 665 CD LYS A 82 5.355 -3.588 18.608 1.00 33.21 C -ANISOU 665 CD LYS A 82 4017 4552 4051 -272 605 -422 C -ATOM 666 CE LYS A 82 3.999 -2.922 18.620 1.00 39.23 C -ANISOU 666 CE LYS A 82 4647 5314 4947 -235 732 -497 C -ATOM 667 NZ LYS A 82 4.140 -1.425 18.588 1.00 40.92 N -ANISOU 667 NZ LYS A 82 4854 5468 5226 -150 787 -561 N -ATOM 668 N ALA A 83 3.854 -7.469 14.903 1.00 19.60 N -ANISOU 668 N ALA A 83 2149 2818 2479 -236 229 -229 N -ATOM 669 CA ALA A 83 2.902 -8.144 14.020 1.00 21.94 C -ANISOU 669 CA ALA A 83 2376 3118 2842 -262 160 -213 C -ATOM 670 C ALA A 83 3.159 -9.649 14.036 1.00 24.23 C -ANISOU 670 C ALA A 83 2793 3365 3047 -343 93 -176 C -ATOM 671 O ALA A 83 2.222 -10.457 14.086 1.00 27.44 O -ANISOU 671 O ALA A 83 3176 3776 3475 -451 87 -169 O -ATOM 672 CB ALA A 83 3.014 -7.601 12.610 1.00 21.61 C -ANISOU 672 CB ALA A 83 2294 3065 2853 -157 60 -199 C -ATOM 673 N LEU A 84 4.433 -10.032 13.987 1.00 20.28 N -ANISOU 673 N LEU A 84 2426 2816 2462 -292 41 -153 N -ATOM 674 CA LEU A 84 4.779 -11.449 14.045 1.00 22.74 C -ANISOU 674 CA LEU A 84 2877 3057 2707 -341 -27 -119 C -ATOM 675 C LEU A 84 4.365 -12.039 15.387 1.00 29.51 C -ANISOU 675 C LEU A 84 3792 3909 3510 -480 33 -96 C -ATOM 676 O LEU A 84 3.902 -13.177 15.470 1.00 27.67 O -ANISOU 676 O LEU A 84 3637 3622 3253 -582 -2 -67 O -ATOM 677 CB LEU A 84 6.281 -11.652 13.842 1.00 24.18 C -ANISOU 677 CB LEU A 84 3159 3195 2835 -234 -83 -103 C -ATOM 678 CG LEU A 84 6.857 -11.314 12.473 1.00 25.58 C -ANISOU 678 CG LEU A 84 3315 3372 3033 -116 -131 -125 C -ATOM 679 CD1 LEU A 84 8.360 -11.413 12.521 1.00 24.30 C -ANISOU 679 CD1 LEU A 84 3209 3192 2832 -19 -150 -115 C -ATOM 680 CD2 LEU A 84 6.303 -12.265 11.423 1.00 27.59 C -ANISOU 680 CD2 LEU A 84 3622 3571 3291 -140 -202 -137 C -ATOM 681 N ASN A 85 4.530 -11.261 16.447 1.00 25.75 N -ANISOU 681 N ASN A 85 3300 3484 3001 -501 126 -107 N -ATOM 682 CA ASN A 85 4.204 -11.758 17.775 1.00 25.30 C -ANISOU 682 CA ASN A 85 3325 3430 2857 -650 194 -84 C -ATOM 683 C ASN A 85 2.714 -11.939 18.040 1.00 33.11 C -ANISOU 683 C ASN A 85 4219 4469 3891 -789 294 -108 C -ATOM 684 O ASN A 85 2.336 -12.722 18.908 1.00 37.97 O -ANISOU 684 O ASN A 85 4926 5073 4426 -946 335 -74 O -ATOM 685 CB ASN A 85 4.844 -10.867 18.852 1.00 34.19 C -ANISOU 685 CB ASN A 85 4486 4599 3907 -650 266 -99 C -ATOM 686 CG ASN A 85 6.240 -11.332 19.235 1.00 45.52 C -ANISOU 686 CG ASN A 85 6068 5979 5247 -613 154 -35 C -ATOM 687 OD1 ASN A 85 6.400 -12.287 20.004 1.00 50.99 O -ANISOU 687 OD1 ASN A 85 6904 6625 5845 -708 110 31 O -ATOM 688 ND2 ASN A 85 7.254 -10.665 18.704 1.00 53.52 N -ANISOU 688 ND2 ASN A 85 7043 7002 6291 -479 100 -46 N -ATOM 689 N ARG A 86 1.851 -11.241 17.306 1.00 31.15 N -ANISOU 689 N ARG A 86 3784 4278 3772 -742 329 -158 N -ATOM 690 CA ARG A 86 0.416 -11.372 17.597 1.00 36.61 C -ANISOU 690 CA ARG A 86 4340 5040 4532 -871 431 -185 C -ATOM 691 C ARG A 86 -0.354 -12.236 16.590 1.00 39.78 C -ANISOU 691 C ARG A 86 4684 5425 5007 -928 327 -160 C -ATOM 692 O ARG A 86 -1.552 -12.501 16.758 1.00 43.62 O -ANISOU 692 O ARG A 86 5042 5975 5557 -1058 391 -172 O -ATOM 693 CB ARG A 86 -0.252 -10.001 17.766 1.00 35.67 C -ANISOU 693 CB ARG A 86 4022 5006 4526 -802 565 -263 C -ATOM 694 CG ARG A 86 -0.257 -9.171 16.501 1.00 31.24 C -ANISOU 694 CG ARG A 86 3335 4439 4095 -632 472 -277 C -ATOM 695 CD ARG A 86 -0.969 -7.834 16.646 1.00 31.78 C -ANISOU 695 CD ARG A 86 3211 4562 4301 -545 590 -348 C -ATOM 696 NE ARG A 86 -0.867 -7.095 15.392 1.00 29.74 N -ANISOU 696 NE ARG A 86 2874 4276 4148 -388 466 -333 N -ATOM 697 CZ ARG A 86 -0.010 -6.109 15.168 1.00 32.09 C -ANISOU 697 CZ ARG A 86 3230 4527 4436 -261 448 -342 C -ATOM 698 NH1 ARG A 86 0.805 -5.706 16.134 1.00 26.98 N -ANISOU 698 NH1 ARG A 86 2702 3861 3687 -269 541 -373 N -ATOM 699 NH2 ARG A 86 0.015 -5.514 13.981 1.00 31.77 N -ANISOU 699 NH2 ARG A 86 3135 4459 4477 -143 329 -313 N -ATOM 700 N ASN A 87 0.326 -12.682 15.547 1.00 44.19 N -ANISOU 700 N ASN A 87 7468 4672 4648 -1100 -470 -251 N -ATOM 701 CA ASN A 87 -0.333 -13.483 14.528 1.00 55.45 C -ANISOU 701 CA ASN A 87 8993 6158 5916 -1372 -453 -360 C -ATOM 702 C ASN A 87 0.308 -14.859 14.518 1.00 61.70 C -ANISOU 702 C ASN A 87 9626 6892 6923 -1284 -152 -781 C -ATOM 703 O ASN A 87 0.451 -15.498 13.478 1.00 71.73 O -ANISOU 703 O ASN A 87 10918 8292 8043 -1616 43 -1108 O -ATOM 704 CB ASN A 87 -0.229 -12.805 13.164 1.00 62.64 C -ANISOU 704 CB ASN A 87 10077 7349 6374 -1926 -505 -329 C -ATOM 705 CG ASN A 87 -0.963 -11.465 13.109 1.00 62.79 C -ANISOU 705 CG ASN A 87 10184 7338 6338 -2038 -887 168 C -ATOM 706 OD1 ASN A 87 -2.194 -11.408 13.183 1.00 61.69 O -ANISOU 706 OD1 ASN A 87 10069 7041 6329 -2004 -1147 458 O -ATOM 707 ND2 ASN A 87 -0.206 -10.386 12.957 1.00 59.76 N -ANISOU 707 ND2 ASN A 87 9807 7067 5832 -2183 -931 265 N -ATOM 708 N SER A 88 0.678 -15.298 15.717 1.00 62.36 N -ANISOU 708 N SER A 88 9513 6775 7405 -879 -129 -764 N -ATOM 709 CA ASER A 88 1.399 -16.547 15.895 0.47 64.86 C -ANISOU 709 CA ASER A 88 9577 6935 8131 -749 90 -1085 C -ATOM 710 CA BSER A 88 1.426 -16.532 15.911 0.53 64.20 C -ANISOU 710 CA BSER A 88 9491 6851 8050 -746 91 -1084 C -ATOM 711 C SER A 88 0.907 -17.306 17.123 1.00 65.33 C -ANISOU 711 C SER A 88 9476 6752 8593 -389 -74 -856 C -ATOM 712 O SER A 88 0.905 -16.786 18.242 1.00 64.37 O -ANISOU 712 O SER A 88 9327 6618 8511 -192 -240 -558 O -ATOM 713 CB ASER A 88 2.898 -16.273 15.999 0.47 63.72 C -ANISOU 713 CB ASER A 88 9271 6819 8121 -742 285 -1295 C -ATOM 714 CB BSER A 88 2.898 -16.199 16.116 0.53 61.35 C -ANISOU 714 CB BSER A 88 8971 6514 7823 -714 262 -1256 C -ATOM 715 OG ASER A 88 3.355 -15.577 14.849 0.47 62.96 O -ANISOU 715 OG ASER A 88 9326 6992 7604 -1138 441 -1512 O -ATOM 716 OG BSER A 88 3.047 -15.240 17.147 0.53 52.64 O -ANISOU 716 OG BSER A 88 7896 5434 6671 -514 77 -910 O -ATOM 717 N ARG A 90 2.346 -18.673 20.317 1.00 59.41 N -ANISOU 717 N ARG A 90 8019 5576 8976 204 -365 -369 N -ATOM 718 CA ARG A 90 3.792 -18.570 20.156 1.00 57.77 C -ANISOU 718 CA ARG A 90 7610 5316 9022 187 -207 -565 C -ATOM 719 C ARG A 90 4.271 -17.113 20.129 1.00 60.98 C -ANISOU 719 C ARG A 90 8225 5992 8951 105 -152 -540 C -ATOM 720 O ARG A 90 4.403 -16.518 19.049 1.00 61.54 O -ANISOU 720 O ARG A 90 8474 6204 8704 -69 37 -808 O -ATOM 721 CB ARG A 90 4.228 -19.286 18.893 1.00 59.64 C -ANISOU 721 CB ARG A 90 7717 5414 9530 68 102 -1088 C -ATOM 722 N SER A 91 4.538 -16.543 21.306 1.00 53.54 N -ANISOU 722 N SER A 91 7250 5143 7951 173 -325 -215 N -ATOM 723 CA SER A 91 5.064 -15.175 21.382 1.00 54.85 C -ANISOU 723 CA SER A 91 7563 5529 7748 108 -270 -203 C -ATOM 724 C SER A 91 6.028 -14.958 22.551 1.00 55.98 C -ANISOU 724 C SER A 91 7516 5714 8041 145 -377 26 C -ATOM 725 O SER A 91 6.104 -15.760 23.484 1.00 53.81 O -ANISOU 725 O SER A 91 7018 5343 8084 179 -572 289 O -ATOM 726 CB SER A 91 3.937 -14.139 21.426 1.00 52.42 C -ANISOU 726 CB SER A 91 7532 5392 6994 51 -344 -83 C -ATOM 727 OG SER A 91 3.358 -14.051 22.713 1.00 53.26 O -ANISOU 727 OG SER A 91 7596 5561 7077 87 -512 187 O -ATOM 728 N ILE A 92 6.759 -13.849 22.479 1.00 52.24 N -ANISOU 728 N ILE A 92 7125 5400 7324 92 -279 -37 N -ATOM 729 CA ILE A 92 7.872 -13.574 23.380 1.00 48.48 C -ANISOU 729 CA ILE A 92 6471 4979 6968 87 -343 127 C -ATOM 730 C ILE A 92 7.768 -12.120 23.846 1.00 44.97 C -ANISOU 730 C ILE A 92 6218 4804 6065 6 -331 194 C -ATOM 731 O ILE A 92 7.549 -11.217 23.032 1.00 43.48 O -ANISOU 731 O ILE A 92 6231 4685 5606 -29 -206 17 O -ATOM 732 CB ILE A 92 9.222 -13.886 22.656 1.00 75.81 C -ANISOU 732 CB ILE A 92 9738 8282 10786 109 -166 -135 C -ATOM 733 CG1 ILE A 92 10.153 -12.669 22.590 1.00 73.96 C -ANISOU 733 CG1 ILE A 92 9589 8232 10279 51 -50 -209 C -ATOM 734 CG2 ILE A 92 8.946 -14.415 21.243 1.00 76.69 C -ANISOU 734 CG2 ILE A 92 9900 8274 10964 72 63 -544 C -ATOM 735 CD1 ILE A 92 10.129 -11.935 21.248 1.00 71.75 C -ANISOU 735 CD1 ILE A 92 9545 8064 9654 -57 185 -548 C -ATOM 736 N PRO A 93 7.868 -11.885 25.162 1.00 41.28 N -ANISOU 736 N PRO A 93 5664 4496 5523 -80 -473 455 N -ATOM 737 CA PRO A 93 7.709 -10.488 25.583 1.00 43.58 C -ANISOU 737 CA PRO A 93 6096 5022 5442 -181 -401 418 C -ATOM 738 C PRO A 93 8.852 -9.610 25.073 1.00 38.45 C -ANISOU 738 C PRO A 93 5473 4410 4729 -166 -261 272 C -ATOM 739 O PRO A 93 9.954 -10.103 24.838 1.00 40.10 O -ANISOU 739 O PRO A 93 5537 4522 5178 -120 -243 259 O -ATOM 740 CB PRO A 93 7.716 -10.569 27.112 1.00 47.79 C -ANISOU 740 CB PRO A 93 6497 5774 5886 -376 -548 679 C -ATOM 741 CG PRO A 93 8.389 -11.866 27.436 1.00 53.60 C -ANISOU 741 CG PRO A 93 6993 6377 6995 -373 -753 947 C -ATOM 742 CD PRO A 93 8.073 -12.803 26.296 1.00 49.47 C -ANISOU 742 CD PRO A 93 6464 5534 6798 -162 -711 793 C -ATOM 743 N MET A 94 8.584 -8.325 24.881 1.00 34.61 N -ANISOU 743 N MET A 94 5132 4026 3992 -213 -167 157 N -ATOM 744 CA MET A 94 9.621 -7.411 24.423 1.00 31.90 C -ANISOU 744 CA MET A 94 4820 3737 3564 -224 -54 45 C -ATOM 745 C MET A 94 9.554 -6.089 25.186 1.00 34.71 C -ANISOU 745 C MET A 94 5188 4261 3740 -326 -16 38 C -ATOM 746 O MET A 94 8.467 -5.568 25.430 1.00 30.61 O -ANISOU 746 O MET A 94 4704 3739 3187 -375 -17 -4 O -ATOM 747 CB MET A 94 9.493 -7.182 22.914 1.00 37.65 C -ANISOU 747 CB MET A 94 5702 4371 4234 -221 25 -126 C -ATOM 748 CG MET A 94 10.504 -6.193 22.347 1.00 42.83 C -ANISOU 748 CG MET A 94 6405 5110 4758 -288 129 -228 C -ATOM 749 SD MET A 94 10.644 -6.313 20.548 1.00 51.02 S -ANISOU 749 SD MET A 94 7585 6131 5669 -436 225 -427 S -ATOM 750 CE MET A 94 8.914 -6.250 20.069 1.00 65.71 C -ANISOU 750 CE MET A 94 9596 7916 7454 -504 62 -305 C -ATOM 751 N THR A 95 10.713 -5.563 25.583 1.00 28.83 N -ANISOU 751 N THR A 95 4376 3639 2940 -372 35 45 N -ATOM 752 CA THR A 95 10.787 -4.259 26.225 1.00 31.06 C -ANISOU 752 CA THR A 95 4645 4075 3081 -488 115 -27 C -ATOM 753 C THR A 95 11.682 -3.348 25.395 1.00 33.18 C -ANISOU 753 C THR A 95 4975 4317 3313 -449 196 -122 C -ATOM 754 O THR A 95 12.426 -3.822 24.530 1.00 32.50 O -ANISOU 754 O THR A 95 4922 4161 3266 -378 212 -139 O -ATOM 755 CB THR A 95 11.306 -4.353 27.671 1.00 31.68 C -ANISOU 755 CB THR A 95 4581 4407 3050 -677 90 90 C -ATOM 756 OG1 THR A 95 12.507 -5.129 27.698 1.00 35.87 O -ANISOU 756 OG1 THR A 95 5015 4927 3687 -639 -4 271 O -ATOM 757 CG2 THR A 95 10.278 -5.022 28.556 1.00 34.70 C -ANISOU 757 CG2 THR A 95 4909 4889 3388 -826 13 175 C -ATOM 758 N VAL A 96 11.593 -2.043 25.636 1.00 31.74 N -ANISOU 758 N VAL A 96 4783 4184 3094 -524 265 -219 N -ATOM 759 CA VAL A 96 12.324 -1.084 24.808 1.00 33.36 C -ANISOU 759 CA VAL A 96 5045 4356 3274 -516 305 -270 C -ATOM 760 C VAL A 96 13.161 -0.174 25.681 1.00 36.58 C -ANISOU 760 C VAL A 96 5355 4928 3615 -599 401 -328 C -ATOM 761 O VAL A 96 12.816 0.084 26.834 1.00 35.41 O -ANISOU 761 O VAL A 96 5097 4908 3451 -723 462 -395 O -ATOM 762 CB VAL A 96 11.377 -0.218 23.932 1.00 36.92 C -ANISOU 762 CB VAL A 96 5551 4622 3855 -543 232 -281 C -ATOM 763 CG1 VAL A 96 10.407 -1.083 23.188 1.00 36.45 C -ANISOU 763 CG1 VAL A 96 5585 4432 3832 -514 124 -209 C -ATOM 764 CG2 VAL A 96 10.607 0.787 24.784 1.00 40.45 C -ANISOU 764 CG2 VAL A 96 5842 5010 4518 -610 279 -394 C -ATOM 765 N ASP A 97 14.279 0.295 25.141 1.00 27.36 N -ANISOU 765 N ASP A 97 4223 3792 2382 -582 437 -332 N -ATOM 766 CA ASP A 97 15.023 1.367 25.787 1.00 30.55 C -ANISOU 766 CA ASP A 97 4546 4325 2736 -663 528 -401 C -ATOM 767 C ASP A 97 15.704 2.219 24.723 1.00 31.26 C -ANISOU 767 C ASP A 97 4710 4353 2813 -649 528 -412 C -ATOM 768 O ASP A 97 15.747 1.842 23.541 1.00 31.60 O -ANISOU 768 O ASP A 97 4870 4320 2817 -632 471 -369 O -ATOM 769 CB ASP A 97 16.036 0.837 26.801 1.00 35.86 C -ANISOU 769 CB ASP A 97 5129 5212 3284 -725 551 -323 C -ATOM 770 CG ASP A 97 16.206 1.771 27.993 1.00 47.23 C -ANISOU 770 CG ASP A 97 6456 6863 4625 -923 656 -424 C -ATOM 771 OD1 ASP A 97 15.930 2.986 27.848 1.00 45.00 O -ANISOU 771 OD1 ASP A 97 6145 6514 4438 -951 751 -603 O -ATOM 772 OD2 ASP A 97 16.611 1.290 29.072 1.00 55.55 O -ANISOU 772 OD2 ASP A 97 7423 8151 5534 -1096 631 -317 O -ATOM 773 N PHE A 98 16.228 3.364 25.147 1.00 27.74 N -ANISOU 773 N PHE A 98 4189 3971 2379 -712 598 -482 N -ATOM 774 CA PHE A 98 16.791 4.328 24.212 1.00 31.51 C -ANISOU 774 CA PHE A 98 4717 4392 2864 -740 567 -460 C -ATOM 775 C PHE A 98 18.130 4.797 24.731 1.00 32.01 C -ANISOU 775 C PHE A 98 4733 4629 2801 -760 677 -507 C -ATOM 776 O PHE A 98 18.320 4.954 25.933 1.00 32.80 O -ANISOU 776 O PHE A 98 4720 4865 2878 -812 770 -581 O -ATOM 777 CB PHE A 98 15.848 5.529 24.056 1.00 32.19 C -ANISOU 777 CB PHE A 98 4701 4268 3260 -803 489 -474 C -ATOM 778 CG PHE A 98 14.484 5.155 23.574 1.00 29.26 C -ANISOU 778 CG PHE A 98 4344 3695 3080 -799 349 -395 C -ATOM 779 CD1 PHE A 98 13.510 4.730 24.474 1.00 29.24 C -ANISOU 779 CD1 PHE A 98 4240 3652 3216 -772 416 -516 C -ATOM 780 CD2 PHE A 98 14.173 5.215 22.227 1.00 30.02 C -ANISOU 780 CD2 PHE A 98 4552 3675 3181 -881 142 -190 C -ATOM 781 CE1 PHE A 98 12.249 4.374 24.035 1.00 29.62 C -ANISOU 781 CE1 PHE A 98 4291 3499 3464 -760 285 -443 C -ATOM 782 CE2 PHE A 98 12.909 4.851 21.772 1.00 31.07 C -ANISOU 782 CE2 PHE A 98 4695 3626 3486 -905 -17 -79 C -ATOM 783 CZ PHE A 98 11.947 4.424 22.678 1.00 30.22 C -ANISOU 783 CZ PHE A 98 4479 3432 3572 -810 58 -210 C -ATOM 784 N ILE A 99 19.066 5.024 23.822 1.00 29.93 N -ANISOU 784 N ILE A 99 4553 4394 2425 -772 671 -472 N -ATOM 785 CA ILE A 99 20.367 5.517 24.232 1.00 31.89 C -ANISOU 785 CA ILE A 99 4754 4789 2575 -785 769 -510 C -ATOM 786 C ILE A 99 20.847 6.490 23.184 1.00 33.39 C -ANISOU 786 C ILE A 99 5010 4952 2722 -868 727 -481 C -ATOM 787 O ILE A 99 20.481 6.381 22.008 1.00 32.08 O -ANISOU 787 O ILE A 99 4954 4727 2506 -959 626 -409 O -ATOM 788 CB ILE A 99 21.372 4.354 24.446 1.00 44.19 C -ANISOU 788 CB ILE A 99 6289 6445 4055 -723 826 -496 C -ATOM 789 CG1 ILE A 99 22.585 4.834 25.244 1.00 50.99 C -ANISOU 789 CG1 ILE A 99 7056 7460 4859 -752 896 -492 C -ATOM 790 CG2 ILE A 99 21.765 3.707 23.124 1.00 44.46 C -ANISOU 790 CG2 ILE A 99 6410 6427 4054 -726 852 -551 C -ATOM 791 CD1 ILE A 99 23.579 3.744 25.556 1.00 55.84 C -ANISOU 791 CD1 ILE A 99 7565 8103 5546 -708 894 -417 C -ATOM 792 N ARG A 100 21.627 7.476 23.604 1.00 31.75 N -ANISOU 792 N ARG A 100 4734 4815 2516 -896 786 -517 N -ATOM 793 CA ARG A 100 22.166 8.424 22.645 1.00 34.54 C -ANISOU 793 CA ARG A 100 5139 5161 2824 -1006 721 -452 C -ATOM 794 C ARG A 100 23.667 8.569 22.866 1.00 41.23 C -ANISOU 794 C ARG A 100 5979 6185 3502 -994 856 -520 C -ATOM 795 O ARG A 100 24.118 8.661 24.008 1.00 38.56 O -ANISOU 795 O ARG A 100 5538 5930 3182 -934 955 -584 O -ATOM 796 CB ARG A 100 21.475 9.784 22.772 1.00 42.29 C -ANISOU 796 CB ARG A 100 5991 5957 4121 -1068 609 -403 C -ATOM 797 CG ARG A 100 22.191 10.880 22.001 1.00 47.33 C -ANISOU 797 CG ARG A 100 6637 6597 4749 -1204 509 -285 C -ATOM 798 CD ARG A 100 21.260 11.625 21.091 1.00 54.64 C -ANISOU 798 CD ARG A 100 7514 7289 5957 -1370 215 -37 C -ATOM 799 NE ARG A 100 20.665 12.784 21.739 1.00 59.61 N -ANISOU 799 NE ARG A 100 7868 7633 7147 -1340 160 -69 N -ATOM 800 CZ ARG A 100 20.895 14.040 21.372 1.00 62.72 C -ANISOU 800 CZ ARG A 100 8119 7869 7843 -1461 -10 84 C -ATOM 801 NH1 ARG A 100 21.703 14.302 20.356 1.00 61.58 N -ANISOU 801 NH1 ARG A 100 8122 7882 7393 -1653 -161 319 N -ATOM 802 NH2 ARG A 100 20.311 15.037 22.018 1.00 68.74 N -ANISOU 802 NH2 ARG A 100 8556 8308 9254 -1426 -19 -22 N -ATOM 803 N LEU A 101 24.418 8.554 21.765 1.00 45.55 N -ANISOU 803 N LEU A 101 6927 5196 5183 -621 -1167 -462 N -ATOM 804 CA LEU A 101 25.864 8.751 21.768 1.00 49.37 C -ANISOU 804 CA LEU A 101 7348 5720 5691 -978 -1304 -337 C -ATOM 805 C LEU A 101 26.201 10.015 20.975 1.00 56.85 C -ANISOU 805 C LEU A 101 8493 6446 6662 -1239 -1505 -171 C -ATOM 806 O LEU A 101 25.604 10.271 19.926 1.00 57.98 O -ANISOU 806 O LEU A 101 8642 6563 6826 -1188 -1454 -88 O -ATOM 807 CB LEU A 101 26.567 7.547 21.130 1.00 45.67 C -ANISOU 807 CB LEU A 101 6470 5636 5246 -1058 -1124 -231 C -ATOM 808 CG LEU A 101 27.033 6.384 22.004 1.00 51.17 C -ANISOU 808 CG LEU A 101 6974 6540 5926 -976 -1040 -310 C -ATOM 809 CD1 LEU A 101 25.899 5.817 22.842 1.00 48.44 C -ANISOU 809 CD1 LEU A 101 6730 6143 5532 -682 -949 -497 C -ATOM 810 CD2 LEU A 101 27.650 5.291 21.141 1.00 51.11 C -ANISOU 810 CD2 LEU A 101 6631 6862 5926 -975 -864 -210 C -ATOM 811 N LYS A 102 27.152 10.799 21.476 1.00 63.96 N -ANISOU 811 N LYS A 102 9570 7185 7548 -1552 -1763 -100 N -ATOM 812 CA LYS A 102 27.630 11.985 20.761 1.00 72.44 C -ANISOU 812 CA LYS A 102 10847 8047 8630 -1905 -2007 111 C -ATOM 813 C LYS A 102 29.132 12.190 20.961 1.00 77.93 C -ANISOU 813 C LYS A 102 11375 8913 9321 -2326 -2142 336 C -ATOM 814 O LYS A 102 29.915 12.083 20.017 1.00 82.23 O -ANISOU 814 O LYS A 102 11607 9760 9877 -2607 -2096 596 O -ATOM 815 CB LYS A 102 26.864 13.223 21.198 1.00 73.98 C -ANISOU 815 CB LYS A 102 11615 7709 8786 -1756 -2233 -11 C -ATOM 816 N LEU A 121 19.760 0.952 32.614 1.00 58.91 N -ANISOU 816 N LEU A 121 8208 8523 5654 434 -277 -985 N -ATOM 817 CA LEU A 121 20.020 -0.059 31.586 1.00 51.73 C -ANISOU 817 CA LEU A 121 7140 7634 4882 266 -330 -865 C -ATOM 818 C LEU A 121 20.154 -1.469 32.159 1.00 50.31 C -ANISOU 818 C LEU A 121 6915 7548 4653 93 -372 -730 C -ATOM 819 O LEU A 121 20.531 -2.412 31.454 1.00 48.06 O -ANISOU 819 O LEU A 121 6576 7209 4476 -36 -446 -641 O -ATOM 820 CB LEU A 121 21.251 0.298 30.751 1.00 53.09 C -ANISOU 820 CB LEU A 121 7363 7561 5246 174 -462 -914 C -ATOM 821 CG LEU A 121 21.037 1.212 29.539 1.00 52.91 C -ANISOU 821 CG LEU A 121 7330 7446 5326 257 -449 -956 C -ATOM 822 CD1 LEU A 121 22.275 1.229 28.651 1.00 52.58 C -ANISOU 822 CD1 LEU A 121 7264 7244 5471 99 -558 -925 C -ATOM 823 CD2 LEU A 121 19.810 0.789 28.743 1.00 51.69 C -ANISOU 823 CD2 LEU A 121 6994 7466 5178 306 -325 -841 C -ATOM 824 N SER A 122 19.823 -1.616 33.438 1.00 49.91 N -ANISOU 824 N SER A 122 6921 7617 4423 108 -333 -713 N -ATOM 825 CA SER A 122 19.655 -2.932 34.039 1.00 48.94 C -ANISOU 825 CA SER A 122 6765 7610 4218 -47 -371 -553 C -ATOM 826 C SER A 122 18.493 -3.635 33.348 1.00 51.14 C -ANISOU 826 C SER A 122 6845 8107 4479 -129 -296 -382 C -ATOM 827 O SER A 122 18.259 -4.819 33.557 1.00 53.31 O -ANISOU 827 O SER A 122 7098 8436 4722 -315 -358 -212 O -ATOM 828 CB SER A 122 19.380 -2.801 35.537 1.00 52.00 C -ANISOU 828 CB SER A 122 7246 8128 4384 -8 -319 -561 C -ATOM 829 OG SER A 122 18.375 -1.833 35.775 1.00 54.23 O -ANISOU 829 OG SER A 122 7474 8598 4532 200 -130 -633 O -ATOM 830 N THR A 123 17.774 -2.884 32.517 1.00 57.73 N -ANISOU 830 N THR A 123 7550 9049 5335 -5 -190 -412 N -ATOM 831 CA THR A 123 16.712 -3.411 31.671 1.00 66.59 C -ANISOU 831 CA THR A 123 8466 10381 6454 -110 -151 -232 C -ATOM 832 C THR A 123 17.238 -4.459 30.679 1.00 67.01 C -ANISOU 832 C THR A 123 8591 10205 6663 -333 -312 -152 C -ATOM 833 O THR A 123 16.454 -5.170 30.049 1.00 71.13 O -ANISOU 833 O THR A 123 9020 10821 7187 -509 -344 24 O -ATOM 834 CB THR A 123 16.020 -2.264 30.891 1.00 72.44 C -ANISOU 834 CB THR A 123 9075 11249 7200 117 -34 -293 C -ATOM 835 OG1 THR A 123 16.971 -1.614 30.036 1.00 74.29 O -ANISOU 835 OG1 THR A 123 9452 11148 7628 182 -111 -454 O -ATOM 836 CG2 THR A 123 15.440 -1.237 31.854 1.00 75.96 C -ANISOU 836 CG2 THR A 123 9497 11867 7497 423 131 -387 C -ATOM 837 N LEU A 124 18.562 -4.550 30.551 1.00 59.07 N -ANISOU 837 N LEU A 124 7759 8898 5786 -313 -417 -276 N -ATOM 838 CA LEU A 124 19.205 -5.439 29.579 1.00 47.60 C -ANISOU 838 CA LEU A 124 6402 7213 4471 -412 -541 -248 C -ATOM 839 C LEU A 124 19.637 -6.783 30.168 1.00 41.86 C -ANISOU 839 C LEU A 124 5813 6362 3729 -523 -672 -157 C -ATOM 840 O LEU A 124 19.760 -7.773 29.445 1.00 37.78 O -ANISOU 840 O LEU A 124 5402 5684 3269 -606 -768 -97 O -ATOM 841 CB LEU A 124 20.445 -4.769 28.985 1.00 46.09 C -ANISOU 841 CB LEU A 124 6258 6835 4417 -288 -563 -413 C -ATOM 842 CG LEU A 124 20.356 -3.375 28.378 1.00 43.58 C -ANISOU 842 CG LEU A 124 5862 6538 4158 -167 -474 -522 C -ATOM 843 CD1 LEU A 124 21.733 -2.919 27.928 1.00 44.05 C -ANISOU 843 CD1 LEU A 124 5959 6414 4364 -120 -526 -620 C -ATOM 844 CD2 LEU A 124 19.405 -3.366 27.204 1.00 43.50 C -ANISOU 844 CD2 LEU A 124 5764 6585 4180 -201 -424 -439 C -ATOM 845 N THR A 125 19.889 -6.814 31.475 1.00 39.49 N -ANISOU 845 N THR A 125 5545 6120 3341 -509 -684 -154 N -ATOM 846 CA THR A 125 20.520 -7.981 32.102 1.00 39.99 C -ANISOU 846 CA THR A 125 5745 6050 3399 -580 -826 -81 C -ATOM 847 C THR A 125 19.745 -9.292 31.886 1.00 46.17 C -ANISOU 847 C THR A 125 6605 6789 4148 -801 -908 115 C -ATOM 848 O THR A 125 18.526 -9.350 32.082 1.00 45.49 O -ANISOU 848 O THR A 125 6408 6914 3963 -965 -845 259 O -ATOM 849 CB THR A 125 20.779 -7.725 33.593 1.00 47.34 C -ANISOU 849 CB THR A 125 6693 7082 4212 -552 -826 -93 C -ATOM 850 OG1 THR A 125 21.515 -6.500 33.723 1.00 50.73 O -ANISOU 850 OG1 THR A 125 7107 7490 4678 -388 -792 -273 O -ATOM 851 CG2 THR A 125 21.584 -8.856 34.204 1.00 46.72 C -ANISOU 851 CG2 THR A 125 6750 6858 4142 -606 -991 -16 C -ATOM 852 N GLY A 126 20.459 -10.328 31.443 1.00 44.86 N -ANISOU 852 N GLY A 126 6635 6352 4056 -809 -1057 128 N -ATOM 853 CA GLY A 126 19.866 -11.632 31.215 1.00 41.60 C -ANISOU 853 CA GLY A 126 6401 5790 3616 -1036 -1188 301 C -ATOM 854 C GLY A 126 18.877 -11.702 30.061 1.00 45.74 C -ANISOU 854 C GLY A 126 6898 6322 4159 -1181 -1167 365 C -ATOM 855 O GLY A 126 18.120 -12.671 29.950 1.00 47.63 O -ANISOU 855 O GLY A 126 7261 6482 4356 -1456 -1283 543 O -ATOM 856 N LYS A 127 18.867 -10.694 29.190 1.00 41.59 N -ANISOU 856 N LYS A 127 6226 5881 3694 -1036 -1046 238 N -ATOM 857 CA LYS A 127 17.906 -10.694 28.088 1.00 42.50 C -ANISOU 857 CA LYS A 127 6298 6029 3821 -1178 -1036 313 C -ATOM 858 C LYS A 127 18.602 -10.668 26.731 1.00 37.14 C -ANISOU 858 C LYS A 127 5759 5120 3232 -1024 -1054 163 C -ATOM 859 O LYS A 127 19.805 -10.431 26.652 1.00 41.22 O -ANISOU 859 O LYS A 127 6331 5530 3801 -790 -1037 1 O -ATOM 860 CB LYS A 127 16.912 -9.530 28.224 1.00 42.45 C -ANISOU 860 CB LYS A 127 5969 6394 3765 -1186 -875 356 C -ATOM 861 CG LYS A 127 16.090 -9.585 29.533 1.00 50.36 C -ANISOU 861 CG LYS A 127 6801 7707 4627 -1329 -825 521 C -ATOM 862 CD LYS A 127 15.066 -8.457 29.632 1.00 52.49 C -ANISOU 862 CD LYS A 127 6733 8399 4810 -1267 -649 567 C -ATOM 863 CE LYS A 127 14.411 -8.390 31.010 1.00 55.73 C -ANISOU 863 CE LYS A 127 6956 9170 5049 -1312 -552 689 C -ATOM 864 NZ LYS A 127 15.403 -8.079 32.067 1.00 54.31 N -ANISOU 864 NZ LYS A 127 6919 8886 4831 -1117 -517 521 N -ATOM 865 N ASN A 128 17.839 -10.943 25.680 1.00 35.79 N -ANISOU 865 N ASN A 128 5638 4900 3061 -1175 -1093 237 N -ATOM 866 CA ASN A 128 18.340 -10.849 24.316 1.00 35.73 C -ANISOU 866 CA ASN A 128 5755 4720 3102 -1039 -1087 105 C -ATOM 867 C ASN A 128 18.262 -9.409 23.821 1.00 36.80 C -ANISOU 867 C ASN A 128 5626 5072 3285 -910 -930 18 C -ATOM 868 O ASN A 128 17.187 -8.932 23.450 1.00 41.65 O -ANISOU 868 O ASN A 128 6076 5865 3885 -1041 -900 126 O -ATOM 869 CB ASN A 128 17.546 -11.775 23.396 1.00 39.22 C -ANISOU 869 CB ASN A 128 6412 4987 3502 -1279 -1222 228 C -ATOM 870 CG ASN A 128 17.820 -13.242 23.680 1.00 46.40 C -ANISOU 870 CG ASN A 128 7714 5560 4358 -1381 -1420 288 C -ATOM 871 OD1 ASN A 128 18.592 -13.576 24.584 1.00 46.70 O -ANISOU 871 OD1 ASN A 128 7836 5516 4394 -1260 -1455 246 O -ATOM 872 ND2 ASN A 128 17.184 -14.125 22.913 1.00 49.03 N -ANISOU 872 ND2 ASN A 128 8323 5672 4636 -1614 -1577 399 N -ATOM 873 N VAL A 129 19.408 -8.731 23.812 1.00 37.52 N -ANISOU 873 N VAL A 129 5683 5147 3426 -671 -851 -154 N -ATOM 874 CA VAL A 129 19.476 -7.312 23.472 1.00 31.83 C -ANISOU 874 CA VAL A 129 4762 4583 2747 -569 -727 -233 C -ATOM 875 C VAL A 129 19.636 -7.104 21.971 1.00 35.30 C -ANISOU 875 C VAL A 129 5263 4946 3205 -533 -703 -286 C -ATOM 876 O VAL A 129 20.574 -7.636 21.358 1.00 33.27 O -ANISOU 876 O VAL A 129 5174 4530 2937 -420 -714 -381 O -ATOM 877 CB VAL A 129 20.626 -6.627 24.224 1.00 32.36 C -ANISOU 877 CB VAL A 129 4770 4674 2851 -404 -677 -361 C -ATOM 878 CG1 VAL A 129 20.701 -5.135 23.872 1.00 31.47 C -ANISOU 878 CG1 VAL A 129 4477 4659 2821 -316 -557 -426 C -ATOM 879 CG2 VAL A 129 20.435 -6.790 25.724 1.00 37.99 C -ANISOU 879 CG2 VAL A 129 5441 5474 3522 -438 -699 -310 C -ATOM 880 N LEU A 130 18.701 -6.366 21.370 1.00 28.68 N -ANISOU 880 N LEU A 130 4293 4240 2366 -616 -671 -214 N -ATOM 881 CA LEU A 130 18.818 -6.000 19.968 1.00 26.57 C -ANISOU 881 CA LEU A 130 4070 3926 2100 -595 -647 -249 C -ATOM 882 C LEU A 130 19.120 -4.510 19.900 1.00 28.39 C -ANISOU 882 C LEU A 130 4116 4272 2397 -489 -539 -303 C -ATOM 883 O LEU A 130 18.287 -3.688 20.272 1.00 30.28 O -ANISOU 883 O LEU A 130 4178 4657 2670 -488 -508 -233 O -ATOM 884 CB LEU A 130 17.533 -6.321 19.192 1.00 27.07 C -ANISOU 884 CB LEU A 130 4136 4022 2127 -788 -724 -95 C -ATOM 885 CG LEU A 130 17.474 -5.884 17.724 1.00 33.40 C -ANISOU 885 CG LEU A 130 4981 4799 2911 -794 -715 -103 C -ATOM 886 CD1 LEU A 130 18.530 -6.606 16.895 1.00 32.31 C -ANISOU 886 CD1 LEU A 130 5098 4458 2720 -688 -703 -237 C -ATOM 887 CD2 LEU A 130 16.096 -6.098 17.132 1.00 37.37 C -ANISOU 887 CD2 LEU A 130 5439 5375 3385 -1013 -814 80 C -ATOM 888 N ILE A 131 20.322 -4.164 19.457 1.00 26.27 N -ANISOU 888 N ILE A 131 3869 3928 2185 -360 -466 -406 N -ATOM 889 CA ILE A 131 20.681 -2.759 19.269 1.00 28.27 C -ANISOU 889 CA ILE A 131 3973 4226 2542 -292 -385 -421 C -ATOM 890 C ILE A 131 20.207 -2.340 17.874 1.00 24.32 C -ANISOU 890 C ILE A 131 3490 3742 2009 -357 -383 -357 C -ATOM 891 O ILE A 131 20.472 -3.029 16.892 1.00 25.31 O -ANISOU 891 O ILE A 131 3754 3826 2035 -385 -387 -371 O -ATOM 892 CB ILE A 131 22.204 -2.539 19.428 1.00 31.05 C -ANISOU 892 CB ILE A 131 4289 4555 2954 -193 -331 -499 C -ATOM 893 CG1 ILE A 131 22.657 -2.914 20.836 1.00 27.97 C -ANISOU 893 CG1 ILE A 131 3883 4155 2591 -143 -366 -544 C -ATOM 894 CG2 ILE A 131 22.582 -1.103 19.161 1.00 31.29 C -ANISOU 894 CG2 ILE A 131 4211 4604 3072 -208 -300 -476 C -ATOM 895 CD1 ILE A 131 24.168 -2.846 21.041 1.00 31.06 C -ANISOU 895 CD1 ILE A 131 4195 4572 3035 -60 -344 -581 C -ATOM 896 N VAL A 132 19.470 -1.234 17.788 1.00 25.72 N -ANISOU 896 N VAL A 132 3557 3970 2244 -358 -387 -287 N -ATOM 897 CA VAL A 132 18.915 -0.812 16.495 1.00 23.71 C -ANISOU 897 CA VAL A 132 3317 3738 1956 -429 -416 -193 C -ATOM 898 C VAL A 132 19.539 0.516 16.060 1.00 27.67 C -ANISOU 898 C VAL A 132 3785 4190 2540 -389 -382 -184 C -ATOM 899 O VAL A 132 19.346 1.536 16.716 1.00 28.78 O -ANISOU 899 O VAL A 132 3872 4290 2773 -305 -397 -182 O -ATOM 900 CB VAL A 132 17.386 -0.689 16.522 1.00 23.91 C -ANISOU 900 CB VAL A 132 3240 3882 1961 -471 -490 -59 C -ATOM 901 CG1 VAL A 132 16.865 -0.375 15.112 1.00 21.87 C -ANISOU 901 CG1 VAL A 132 3009 3647 1652 -567 -556 57 C -ATOM 902 CG2 VAL A 132 16.745 -1.986 17.044 1.00 28.31 C -ANISOU 902 CG2 VAL A 132 3819 4515 2424 -593 -557 -14 C -ATOM 903 N GLU A 133 20.261 0.493 14.946 1.00 27.49 N -ANISOU 903 N GLU A 133 3823 4165 2456 -453 -347 -170 N -ATOM 904 CA GLU A 133 21.042 1.645 14.489 1.00 28.58 C -ANISOU 904 CA GLU A 133 3931 4280 2646 -487 -327 -120 C -ATOM 905 C GLU A 133 20.633 2.089 13.085 1.00 24.78 C -ANISOU 905 C GLU A 133 3504 3823 2087 -587 -360 3 C -ATOM 906 O GLU A 133 20.085 1.305 12.312 1.00 26.27 O -ANISOU 906 O GLU A 133 3772 4063 2146 -634 -374 21 O -ATOM 907 CB GLU A 133 22.540 1.294 14.534 1.00 37.50 C -ANISOU 907 CB GLU A 133 5017 5478 3753 -482 -231 -175 C -ATOM 908 CG GLU A 133 23.524 2.384 14.082 1.00 40.47 C -ANISOU 908 CG GLU A 133 5320 5897 4160 -594 -219 -74 C -ATOM 909 CD GLU A 133 23.566 3.588 15.011 1.00 42.18 C -ANISOU 909 CD GLU A 133 5540 5967 4521 -639 -335 -51 C -ATOM 910 OE1 GLU A 133 22.512 4.225 15.214 1.00 40.89 O -ANISOU 910 OE1 GLU A 133 5468 5659 4409 -590 -426 -43 O -ATOM 911 OE2 GLU A 133 24.657 3.908 15.529 1.00 44.72 O -ANISOU 911 OE2 GLU A 133 5783 6320 4887 -714 -349 -36 O -ATOM 912 N ASP A 134 20.908 3.347 12.743 1.00 23.62 N -ANISOU 912 N ASP A 134 3355 3621 2001 -648 -402 102 N -ATOM 913 CA ASP A 134 20.605 3.830 11.406 1.00 27.25 C -ANISOU 913 CA ASP A 134 3876 4103 2374 -762 -447 246 C -ATOM 914 C ASP A 134 21.706 3.468 10.393 1.00 26.28 C -ANISOU 914 C ASP A 134 3763 4133 2090 -870 -328 272 C -ATOM 915 O ASP A 134 21.424 2.974 9.291 1.00 28.00 O -ANISOU 915 O ASP A 134 4072 4436 2131 -922 -308 306 O -ATOM 916 CB ASP A 134 20.344 5.351 11.402 1.00 29.50 C -ANISOU 916 CB ASP A 134 4205 4230 2772 -784 -578 370 C -ATOM 917 CG ASP A 134 21.471 6.163 12.045 1.00 29.83 C -ANISOU 917 CG ASP A 134 4256 4175 2904 -853 -594 365 C -ATOM 918 OD1 ASP A 134 22.337 5.602 12.752 1.00 28.74 O -ANISOU 918 OD1 ASP A 134 4032 4112 2778 -845 -507 262 O -ATOM 919 OD2 ASP A 134 21.484 7.397 11.834 1.00 37.95 O -ANISOU 919 OD2 ASP A 134 5398 5035 3987 -933 -730 486 O -ATOM 920 N ILE A 135 22.958 3.726 10.763 1.00 27.06 N -ANISOU 920 N ILE A 135 3762 4297 2224 -901 -251 267 N -ATOM 921 CA ILE A 135 24.049 3.512 9.811 1.00 27.98 C -ANISOU 921 CA ILE A 135 3817 4646 2169 -976 -108 331 C -ATOM 922 C ILE A 135 25.358 3.132 10.508 1.00 26.32 C -ANISOU 922 C ILE A 135 3423 4592 1985 -911 10 276 C -ATOM 923 O ILE A 135 25.695 3.648 11.581 1.00 26.27 O -ANISOU 923 O ILE A 135 3337 4499 2147 -945 -71 276 O -ATOM 924 CB ILE A 135 24.225 4.737 8.866 1.00 31.80 C -ANISOU 924 CB ILE A 135 4315 5159 2610 -1208 -172 559 C -ATOM 925 CG1 ILE A 135 25.254 4.446 7.755 1.00 30.21 C -ANISOU 925 CG1 ILE A 135 4024 5288 2168 -1282 13 649 C -ATOM 926 CG2 ILE A 135 24.567 5.980 9.670 1.00 30.78 C -ANISOU 926 CG2 ILE A 135 4156 4866 2671 -1341 -320 656 C -ATOM 927 CD1 ILE A 135 25.244 5.456 6.599 1.00 32.44 C -ANISOU 927 CD1 ILE A 135 4360 5630 2337 -1539 -48 897 C -ATOM 928 N ILE A 136 26.060 2.178 9.914 1.00 29.20 N -ANISOU 928 N ILE A 136 3742 5190 2164 -785 192 222 N -ATOM 929 CA ILE A 136 27.414 1.855 10.321 1.00 33.38 C -ANISOU 929 CA ILE A 136 4036 5964 2682 -694 325 224 C -ATOM 930 C ILE A 136 28.347 2.310 9.218 1.00 34.16 C -ANISOU 930 C ILE A 136 3966 6412 2600 -814 467 414 C -ATOM 931 O ILE A 136 28.135 2.001 8.038 1.00 34.46 O -ANISOU 931 O ILE A 136 4124 6561 2407 -776 574 417 O -ATOM 932 CB ILE A 136 27.572 0.366 10.613 1.00 36.65 C -ANISOU 932 CB ILE A 136 4517 6396 3012 -375 432 17 C -ATOM 933 CG1 ILE A 136 26.754 0.019 11.856 1.00 39.64 C -ANISOU 933 CG1 ILE A 136 5013 6477 3573 -328 278 -113 C -ATOM 934 CG2 ILE A 136 29.051 0.004 10.822 1.00 36.22 C -ANISOU 934 CG2 ILE A 136 4179 6673 2911 -214 595 48 C -ATOM 935 CD1 ILE A 136 26.707 -1.438 12.168 1.00 45.61 C -ANISOU 935 CD1 ILE A 136 5918 7163 4248 -70 315 -294 C -ATOM 936 N ASP A 137 29.356 3.090 9.591 1.00 33.33 N -ANISOU 936 N ASP A 137 3590 6496 2579 -999 450 598 N -ATOM 937 CA ASP A 137 30.325 3.583 8.622 1.00 36.81 C -ANISOU 937 CA ASP A 137 3799 7348 2840 -1170 583 843 C -ATOM 938 C ASP A 137 31.708 3.068 9.003 1.00 47.48 C -ANISOU 938 C ASP A 137 4769 9123 4150 -1024 752 894 C -ATOM 939 O ASP A 137 32.177 2.090 8.437 1.00 48.20 O -ANISOU 939 O ASP A 137 4779 9511 4026 -699 1003 807 O -ATOM 940 CB ASP A 137 30.272 5.117 8.532 1.00 39.84 C -ANISOU 940 CB ASP A 137 4195 7616 3325 -1616 366 1109 C -ATOM 941 CG ASP A 137 31.287 5.697 7.565 1.00 45.85 C -ANISOU 941 CG ASP A 137 4696 8834 3891 -1884 476 1427 C -ATOM 942 OD1 ASP A 137 31.810 4.965 6.694 1.00 51.06 O -ANISOU 942 OD1 ASP A 137 5231 9814 4357 -1641 711 1380 O -ATOM 943 OD2 ASP A 137 31.542 6.913 7.656 1.00 50.08 O -ANISOU 943 OD2 ASP A 137 5217 9284 4528 -2276 258 1669 O -ATOM 944 N THR A 138 32.357 3.709 9.972 1.00 42.43 N -ANISOU 944 N THR A 138 3912 8510 3698 -1238 603 1033 N -ATOM 945 CA THR A 138 33.682 3.253 10.382 1.00 47.94 C -ANISOU 945 CA THR A 138 4188 9655 4370 -1115 732 1126 C -ATOM 946 C THR A 138 33.518 2.054 11.306 1.00 45.26 C -ANISOU 946 C THR A 138 3934 9144 4119 -697 757 838 C -ATOM 947 O THR A 138 34.352 1.146 11.327 1.00 48.78 O -ANISOU 947 O THR A 138 4141 9927 4466 -358 946 806 O -ATOM 948 CB THR A 138 34.491 4.351 11.103 1.00 43.92 C -ANISOU 948 CB THR A 138 3419 9255 4014 -1556 513 1412 C -ATOM 949 OG1 THR A 138 33.798 4.754 12.295 1.00 42.95 O -ANISOU 949 OG1 THR A 138 3581 8606 4134 -1664 225 1273 O -ATOM 950 CG2 THR A 138 34.695 5.549 10.189 1.00 46.62 C -ANISOU 950 CG2 THR A 138 3788 9633 4293 -1949 394 1679 C -ATOM 951 N GLY A 139 32.426 2.050 12.057 1.00 36.31 N -ANISOU 951 N GLY A 139 3143 7499 3154 -704 566 644 N -ATOM 952 CA GLY A 139 32.173 0.994 13.018 1.00 35.51 C -ANISOU 952 CA GLY A 139 3157 7199 3136 -389 544 407 C -ATOM 953 C GLY A 139 32.553 1.416 14.427 1.00 36.36 C -ANISOU 953 C GLY A 139 3146 7215 3453 -542 339 453 C -ATOM 954 O GLY A 139 32.266 0.702 15.391 1.00 36.51 O -ANISOU 954 O GLY A 139 3281 7033 3557 -350 274 282 O -ATOM 955 N LYS A 140 33.197 2.576 14.554 1.00 39.98 N -ANISOU 955 N LYS A 140 3406 7811 3973 -920 212 697 N -ATOM 956 CA LYS A 140 33.651 3.065 15.869 1.00 44.31 C -ANISOU 956 CA LYS A 140 3876 8276 4684 -1120 -23 758 C -ATOM 957 C LYS A 140 32.529 3.218 16.877 1.00 41.86 C -ANISOU 957 C LYS A 140 3951 7451 4502 -1112 -209 541 C -ATOM 958 O LYS A 140 32.654 2.796 18.029 1.00 44.41 O -ANISOU 958 O LYS A 140 4282 7690 4901 -1016 -302 445 O -ATOM 959 CB LYS A 140 34.359 4.416 15.751 1.00 53.22 C -ANISOU 959 CB LYS A 140 4844 9542 5834 -1617 -199 1068 C -ATOM 960 CG LYS A 140 35.770 4.376 15.206 1.00 64.17 C -ANISOU 960 CG LYS A 140 5709 11561 7114 -1715 -72 1371 C -ATOM 961 CD LYS A 140 36.456 5.715 15.469 1.00 71.76 C -ANISOU 961 CD LYS A 140 6663 12489 8115 -2224 -358 1657 C -ATOM 962 CE LYS A 140 37.709 5.906 14.626 1.00 81.08 C -ANISOU 962 CE LYS A 140 7512 14160 9135 -2289 -256 1954 C -ATOM 963 NZ LYS A 140 37.386 6.239 13.205 1.00 83.31 N -ANISOU 963 NZ LYS A 140 7850 14536 9267 -2344 -117 2031 N -ATOM 964 N THR A 141 31.442 3.851 16.449 1.00 36.66 N -ANISOU 964 N THR A 141 3595 6484 3850 -1204 -263 485 N -ATOM 965 CA THR A 141 30.300 4.081 17.321 1.00 36.59 C -ANISOU 965 CA THR A 141 3918 6051 3932 -1156 -406 299 C -ATOM 966 C THR A 141 29.743 2.772 17.871 1.00 38.62 C -ANISOU 966 C THR A 141 4244 6247 4183 -821 -309 83 C -ATOM 967 O THR A 141 29.479 2.644 19.073 1.00 39.36 O -ANISOU 967 O THR A 141 4440 6177 4340 -773 -416 -27 O -ATOM 968 CB THR A 141 29.176 4.820 16.592 1.00 35.38 C -ANISOU 968 CB THR A 141 4025 5647 3770 -1219 -442 292 C -ATOM 969 OG1 THR A 141 29.671 6.061 16.080 1.00 43.75 O -ANISOU 969 OG1 THR A 141 5083 6711 4830 -1557 -572 514 O -ATOM 970 CG2 THR A 141 28.012 5.083 17.539 1.00 39.63 C -ANISOU 970 CG2 THR A 141 4850 5824 4384 -1110 -563 117 C -ATOM 971 N MET A 142 29.559 1.798 16.988 1.00 29.73 N -ANISOU 971 N MET A 142 3100 5241 2953 -609 -123 29 N -ATOM 972 CA MET A 142 28.990 0.521 17.415 1.00 29.74 C -ANISOU 972 CA MET A 142 3232 5139 2928 -339 -74 -152 C -ATOM 973 C MET A 142 29.921 -0.238 18.374 1.00 26.77 C -ANISOU 973 C MET A 142 2704 4884 2582 -195 -89 -173 C -ATOM 974 O MET A 142 29.474 -0.761 19.399 1.00 30.25 O -ANISOU 974 O MET A 142 3274 5156 3064 -114 -172 -281 O -ATOM 975 CB MET A 142 28.599 -0.338 16.203 1.00 36.09 C -ANISOU 975 CB MET A 142 4141 5989 3581 -170 80 -210 C -ATOM 976 CG MET A 142 27.653 -1.470 16.567 1.00 42.16 C -ANISOU 976 CG MET A 142 5155 6547 4316 -5 52 -371 C -ATOM 977 SD MET A 142 26.391 -1.006 17.790 1.00 47.20 S -ANISOU 977 SD MET A 142 5929 6927 5079 -130 -115 -417 S -ATOM 978 CE MET A 142 25.471 0.251 16.902 1.00 25.99 C -ANISOU 978 CE MET A 142 3301 4169 2403 -306 -144 -333 C -ATOM 979 N GLN A 143 31.211 -0.269 18.064 1.00 33.22 N -ANISOU 979 N GLN A 143 3222 6029 3370 -168 -15 -41 N -ATOM 980 CA GLN A 143 32.179 -0.899 18.965 1.00 36.66 C -ANISOU 980 CA GLN A 143 3461 6624 3844 -23 -52 -18 C -ATOM 981 C GLN A 143 32.168 -0.238 20.336 1.00 39.87 C -ANISOU 981 C GLN A 143 3901 6876 4371 -249 -282 -2 C -ATOM 982 O GLN A 143 32.273 -0.904 21.371 1.00 40.08 O -ANISOU 982 O GLN A 143 3960 6841 4428 -125 -364 -68 O -ATOM 983 CB GLN A 143 33.581 -0.881 18.355 1.00 43.96 C -ANISOU 983 CB GLN A 143 3974 8019 4710 31 70 175 C -ATOM 984 CG GLN A 143 33.747 -1.848 17.183 1.00 49.71 C -ANISOU 984 CG GLN A 143 4694 8931 5264 398 326 110 C -ATOM 985 CD GLN A 143 35.192 -2.004 16.744 1.00 59.79 C -ANISOU 985 CD GLN A 143 5507 10757 6455 565 485 299 C -ATOM 986 OE1 GLN A 143 36.013 -1.102 16.931 1.00 61.63 O -ANISOU 986 OE1 GLN A 143 5380 11291 6746 266 414 548 O -ATOM 987 NE2 GLN A 143 35.513 -3.156 16.159 1.00 64.76 N -ANISOU 987 NE2 GLN A 143 6150 11531 6927 1048 690 192 N -ATOM 988 N THR A 144 32.023 1.081 20.337 1.00 38.85 N -ANISOU 988 N THR A 144 3815 6658 4287 -578 -403 84 N -ATOM 989 CA THR A 144 31.944 1.838 21.577 1.00 42.90 C -ANISOU 989 CA THR A 144 4459 6972 4870 -792 -638 70 C -ATOM 990 C THR A 144 30.702 1.418 22.343 1.00 37.80 C -ANISOU 990 C THR A 144 4127 6017 4218 -636 -655 -145 C -ATOM 991 O THR A 144 30.767 1.107 23.537 1.00 35.44 O -ANISOU 991 O THR A 144 3887 5654 3925 -604 -763 -207 O -ATOM 992 CB THR A 144 31.878 3.343 21.302 1.00 44.07 C -ANISOU 992 CB THR A 144 4713 6991 5040 -1141 -782 179 C -ATOM 993 OG1 THR A 144 33.133 3.782 20.764 1.00 45.13 O -ANISOU 993 OG1 THR A 144 4519 7462 5166 -1379 -809 440 O -ATOM 994 CG2 THR A 144 31.575 4.106 22.577 1.00 49.99 C -ANISOU 994 CG2 THR A 144 5738 7440 5816 -1296 -1027 96 C -ATOM 995 N LEU A 145 29.571 1.389 21.646 1.00 34.17 N -ANISOU 995 N LEU A 145 3845 5407 3730 -553 -552 -232 N -ATOM 996 CA LEU A 145 28.307 1.044 22.279 1.00 31.40 C -ANISOU 996 CA LEU A 145 3732 4842 3357 -434 -556 -386 C -ATOM 997 C LEU A 145 28.302 -0.402 22.776 1.00 37.48 C -ANISOU 997 C LEU A 145 4497 5656 4089 -234 -511 -452 C -ATOM 998 O LEU A 145 27.857 -0.681 23.898 1.00 38.58 O -ANISOU 998 O LEU A 145 4752 5701 4207 -207 -584 -523 O -ATOM 999 CB LEU A 145 27.130 1.306 21.344 1.00 33.60 C -ANISOU 999 CB LEU A 145 4141 5015 3612 -408 -475 -413 C -ATOM 1000 CG LEU A 145 25.770 1.014 21.981 1.00 39.41 C -ANISOU 1000 CG LEU A 145 5047 5616 4313 -304 -475 -520 C -ATOM 1001 CD1 LEU A 145 25.620 1.774 23.291 1.00 40.65 C -ANISOU 1001 CD1 LEU A 145 5319 5656 4470 -331 -591 -584 C -ATOM 1002 CD2 LEU A 145 24.636 1.361 21.033 1.00 40.83 C -ANISOU 1002 CD2 LEU A 145 5298 5739 4475 -290 -423 -502 C -ATOM 1003 N LEU A 146 28.811 -1.315 21.954 1.00 31.28 N -ANISOU 1003 N LEU A 146 3609 5007 3269 -83 -399 -427 N -ATOM 1004 CA LEU A 146 28.896 -2.716 22.355 1.00 32.83 C -ANISOU 1004 CA LEU A 146 3867 5188 3421 128 -393 -484 C -ATOM 1005 C LEU A 146 29.702 -2.866 23.652 1.00 34.31 C -ANISOU 1005 C LEU A 146 3958 5429 3649 131 -523 -451 C -ATOM 1006 O LEU A 146 29.315 -3.620 24.544 1.00 34.58 O -ANISOU 1006 O LEU A 146 4136 5351 3652 194 -597 -502 O -ATOM 1007 CB LEU A 146 29.511 -3.563 21.236 1.00 32.90 C -ANISOU 1007 CB LEU A 146 3815 5326 3360 351 -257 -477 C -ATOM 1008 CG LEU A 146 28.544 -3.914 20.109 1.00 33.18 C -ANISOU 1008 CG LEU A 146 4063 5244 3298 382 -169 -544 C -ATOM 1009 CD1 LEU A 146 29.288 -4.384 18.867 1.00 29.06 C -ANISOU 1009 CD1 LEU A 146 3485 4891 2668 590 -13 -541 C -ATOM 1010 CD2 LEU A 146 27.565 -4.980 20.575 1.00 34.59 C -ANISOU 1010 CD2 LEU A 146 4530 5191 3420 428 -253 -628 C -ATOM 1011 N SER A 147 30.801 -2.130 23.770 1.00 36.31 N -ANISOU 1011 N SER A 147 3970 5869 3958 20 -577 -338 N -ATOM 1012 CA SER A 147 31.669 -2.260 24.945 1.00 38.98 C -ANISOU 1012 CA SER A 147 4189 6296 4326 -3 -733 -275 C -ATOM 1013 C SER A 147 30.982 -1.841 26.248 1.00 43.49 C -ANISOU 1013 C SER A 147 4987 6663 4874 -157 -886 -354 C -ATOM 1014 O SER A 147 31.412 -2.243 27.334 1.00 43.57 O -ANISOU 1014 O SER A 147 4993 6693 4867 -146 -1020 -334 O -ATOM 1015 CB SER A 147 32.976 -1.490 24.762 1.00 45.84 C -ANISOU 1015 CB SER A 147 4723 7448 5245 -163 -793 -90 C -ATOM 1016 OG SER A 147 32.800 -0.109 25.004 1.00 52.25 O -ANISOU 1016 OG SER A 147 5620 8154 6078 -503 -924 -60 O -ATOM 1017 N LEU A 148 29.924 -1.040 26.134 1.00 42.09 N -ANISOU 1017 N LEU A 148 5009 6310 4675 -268 -861 -439 N -ATOM 1018 CA LEU A 148 29.121 -0.630 27.288 1.00 41.66 C -ANISOU 1018 CA LEU A 148 5188 6090 4550 -337 -952 -538 C -ATOM 1019 C LEU A 148 28.014 -1.637 27.587 1.00 40.79 C -ANISOU 1019 C LEU A 148 5224 5912 4362 -194 -871 -612 C -ATOM 1020 O LEU A 148 27.832 -2.066 28.731 1.00 41.52 O -ANISOU 1020 O LEU A 148 5416 5987 4373 -187 -946 -636 O -ATOM 1021 CB LEU A 148 28.496 0.752 27.055 1.00 41.44 C -ANISOU 1021 CB LEU A 148 5311 5917 4518 -460 -966 -589 C -ATOM 1022 CG LEU A 148 27.493 1.198 28.128 1.00 45.09 C -ANISOU 1022 CG LEU A 148 6038 6229 4866 -429 -1003 -722 C -ATOM 1023 CD1 LEU A 148 28.156 1.344 29.498 1.00 43.81 C -ANISOU 1023 CD1 LEU A 148 5967 6056 4624 -526 -1188 -742 C -ATOM 1024 CD2 LEU A 148 26.782 2.492 27.742 1.00 51.11 C -ANISOU 1024 CD2 LEU A 148 6978 6822 5620 -445 -1000 -783 C -ATOM 1025 N VAL A 149 27.275 -2.003 26.545 1.00 34.42 N -ANISOU 1025 N VAL A 149 4435 5082 3562 -118 -736 -623 N -ATOM 1026 CA VAL A 149 26.139 -2.915 26.658 1.00 34.60 C -ANISOU 1026 CA VAL A 149 4589 5055 3503 -59 -687 -647 C -ATOM 1027 C VAL A 149 26.534 -4.260 27.277 1.00 43.81 C -ANISOU 1027 C VAL A 149 5805 6216 4627 15 -763 -613 C -ATOM 1028 O VAL A 149 25.775 -4.846 28.063 1.00 40.99 O -ANISOU 1028 O VAL A 149 5572 5829 4171 -22 -802 -602 O -ATOM 1029 CB VAL A 149 25.469 -3.117 25.289 1.00 36.53 C -ANISOU 1029 CB VAL A 149 4846 5278 3756 -33 -578 -638 C -ATOM 1030 CG1 VAL A 149 24.448 -4.268 25.329 1.00 37.53 C -ANISOU 1030 CG1 VAL A 149 5111 5361 3790 -35 -583 -616 C -ATOM 1031 CG2 VAL A 149 24.805 -1.832 24.863 1.00 34.69 C -ANISOU 1031 CG2 VAL A 149 4604 5029 3547 -96 -531 -653 C -ATOM 1032 N ARG A 150 27.734 -4.730 26.945 1.00 39.44 N -ANISOU 1032 N ARG A 150 5143 5710 4133 129 -789 -576 N -ATOM 1033 CA ARG A 150 28.213 -6.001 27.474 1.00 40.59 C -ANISOU 1033 CA ARG A 150 5358 5818 4247 262 -883 -539 C -ATOM 1034 C ARG A 150 28.378 -5.964 28.995 1.00 42.90 C -ANISOU 1034 C ARG A 150 5681 6127 4492 173 -1029 -508 C -ATOM 1035 O ARG A 150 28.298 -6.999 29.657 1.00 41.03 O -ANISOU 1035 O ARG A 150 5583 5817 4189 217 -1130 -465 O -ATOM 1036 CB ARG A 150 29.521 -6.413 26.794 1.00 41.73 C -ANISOU 1036 CB ARG A 150 5335 6065 4455 483 -860 -501 C -ATOM 1037 CG ARG A 150 29.332 -6.675 25.301 1.00 44.65 C -ANISOU 1037 CG ARG A 150 5744 6414 4807 609 -709 -547 C -ATOM 1038 CD ARG A 150 30.389 -7.589 24.715 1.00 49.34 C -ANISOU 1038 CD ARG A 150 6285 7076 5387 944 -670 -537 C -ATOM 1039 NE ARG A 150 30.080 -7.908 23.321 1.00 54.90 N -ANISOU 1039 NE ARG A 150 7116 7730 6013 1071 -529 -610 N -ATOM 1040 CZ ARG A 150 30.696 -7.373 22.268 1.00 59.78 C -ANISOU 1040 CZ ARG A 150 7520 8567 6627 1154 -366 -594 C -ATOM 1041 NH1 ARG A 150 31.676 -6.490 22.443 1.00 60.40 N -ANISOU 1041 NH1 ARG A 150 7220 8940 6791 1093 -338 -481 N -ATOM 1042 NH2 ARG A 150 30.338 -7.727 21.036 1.00 57.07 N -ANISOU 1042 NH2 ARG A 150 7352 8162 6170 1265 -249 -672 N -ATOM 1043 N GLN A 151 28.594 -4.773 29.545 1.00 39.84 N -ANISOU 1043 N GLN A 151 5212 5811 4114 33 -1064 -526 N -ATOM 1044 CA GLN A 151 28.791 -4.636 30.985 1.00 42.55 C -ANISOU 1044 CA GLN A 151 5621 6173 4373 -63 -1214 -512 C -ATOM 1045 C GLN A 151 27.504 -4.848 31.783 1.00 44.87 C -ANISOU 1045 C GLN A 151 6122 6420 4505 -130 -1187 -550 C -ATOM 1046 O GLN A 151 27.552 -5.042 32.992 1.00 42.42 O -ANISOU 1046 O GLN A 151 5881 6136 4100 -194 -1260 -514 O -ATOM 1047 CB GLN A 151 29.429 -3.290 31.315 1.00 41.61 C -ANISOU 1047 CB GLN A 151 5427 6105 4276 -214 -1298 -528 C -ATOM 1048 CG GLN A 151 30.806 -3.116 30.696 1.00 42.44 C -ANISOU 1048 CG GLN A 151 5258 6350 4516 -209 -1353 -420 C -ATOM 1049 CD GLN A 151 31.401 -1.748 30.942 1.00 42.66 C -ANISOU 1049 CD GLN A 151 5242 6410 4558 -450 -1484 -395 C -ATOM 1050 OE1 GLN A 151 31.470 -1.283 32.079 1.00 41.81 O -ANISOU 1050 OE1 GLN A 151 5285 6249 4350 -597 -1654 -423 O -ATOM 1051 NE2 GLN A 151 31.838 -1.092 29.867 1.00 40.48 N -ANISOU 1051 NE2 GLN A 151 4790 6209 4380 -518 -1426 -333 N -ATOM 1052 N TYR A 152 26.356 -4.812 31.107 1.00 43.32 N -ANISOU 1052 N TYR A 152 5973 6199 4288 -129 -1042 -582 N -ATOM 1053 CA TYR A 152 25.072 -5.123 31.757 1.00 45.96 C -ANISOU 1053 CA TYR A 152 6396 6579 4486 -202 -963 -549 C -ATOM 1054 C TYR A 152 24.739 -6.622 31.685 1.00 41.51 C -ANISOU 1054 C TYR A 152 5916 5964 3890 -212 -1013 -439 C -ATOM 1055 O TYR A 152 23.619 -7.037 32.002 1.00 44.73 O -ANISOU 1055 O TYR A 152 6363 6425 4209 -285 -961 -368 O -ATOM 1056 CB TYR A 152 23.934 -4.256 31.183 1.00 42.72 C -ANISOU 1056 CB TYR A 152 5984 6186 4063 -196 -818 -595 C -ATOM 1057 CG TYR A 152 24.065 -2.811 31.602 1.00 42.73 C -ANISOU 1057 CG TYR A 152 6004 6174 4056 -175 -788 -696 C -ATOM 1058 CD1 TYR A 152 23.449 -2.346 32.762 1.00 39.32 C -ANISOU 1058 CD1 TYR A 152 5678 5794 3467 -165 -747 -726 C -ATOM 1059 CD2 TYR A 152 24.843 -1.922 30.866 1.00 42.70 C -ANISOU 1059 CD2 TYR A 152 5950 6101 4173 -168 -825 -761 C -ATOM 1060 CE1 TYR A 152 23.587 -1.037 33.167 1.00 41.24 C -ANISOU 1060 CE1 TYR A 152 6008 5988 3674 -135 -739 -845 C -ATOM 1061 CE2 TYR A 152 24.984 -0.608 31.260 1.00 40.51 C -ANISOU 1061 CE2 TYR A 152 5764 5756 3873 -185 -852 -847 C -ATOM 1062 CZ TYR A 152 24.350 -0.171 32.415 1.00 45.00 C -ANISOU 1062 CZ TYR A 152 6468 6342 4287 -153 -807 -903 C -ATOM 1063 OH TYR A 152 24.485 1.135 32.828 1.00 46.03 O -ANISOU 1063 OH TYR A 152 6747 6361 4382 -136 -846 -1013 O -ATOM 1064 N ASN A 153 25.742 -7.408 31.296 1.00 63.94 N -ANISOU 1064 N ASN A 153 9290 9908 5097 505 -2450 561 N -ATOM 1065 CA ASN A 153 25.635 -8.857 31.123 1.00 59.88 C -ANISOU 1065 CA ASN A 153 8810 9296 4644 701 -2406 748 C -ATOM 1066 C ASN A 153 24.318 -9.370 30.527 1.00 54.75 C -ANISOU 1066 C ASN A 153 8312 8461 4030 749 -2112 786 C -ATOM 1067 O ASN A 153 23.514 -10.016 31.200 1.00 56.46 O -ANISOU 1067 O ASN A 153 8773 8573 4104 796 -1972 899 O -ATOM 1068 CB ASN A 153 26.010 -9.585 32.410 1.00 64.90 C -ANISOU 1068 CB ASN A 153 9600 9971 5090 793 -2539 895 C -ATOM 1069 CG ASN A 153 27.491 -9.428 32.749 1.00 71.94 C -ANISOU 1069 CG ASN A 153 10265 11054 6014 793 -2863 910 C -ATOM 1070 OD1 ASN A 153 28.359 -9.668 31.906 1.00 71.94 O -ANISOU 1070 OD1 ASN A 153 9976 11103 6255 853 -2979 935 O -ATOM 1071 ND2 ASN A 153 27.784 -9.002 33.978 1.00 77.57 N -ANISOU 1071 ND2 ASN A 153 11100 11884 6489 731 -3004 894 N -ATOM 1072 N PRO A 154 24.094 -9.060 29.249 1.00 46.22 N -ANISOU 1072 N PRO A 154 7072 7347 3141 726 -2015 696 N -ATOM 1073 CA PRO A 154 22.950 -9.608 28.517 1.00 44.35 C -ANISOU 1073 CA PRO A 154 6935 6951 2967 773 -1766 741 C -ATOM 1074 C PRO A 154 23.184 -11.084 28.238 1.00 43.88 C -ANISOU 1074 C PRO A 154 6876 6793 3003 968 -1781 910 C -ATOM 1075 O PRO A 154 24.318 -11.544 28.327 1.00 49.94 O -ANISOU 1075 O PRO A 154 7500 7636 3840 1083 -1977 963 O -ATOM 1076 CB PRO A 154 22.999 -8.844 27.195 1.00 43.82 C -ANISOU 1076 CB PRO A 154 6610 6905 3133 680 -1693 589 C -ATOM 1077 CG PRO A 154 24.455 -8.526 27.034 1.00 42.45 C -ANISOU 1077 CG PRO A 154 6182 6906 3040 709 -1958 542 C -ATOM 1078 CD PRO A 154 24.935 -8.201 28.397 1.00 45.42 C -ANISOU 1078 CD PRO A 154 6678 7365 3215 649 -2138 559 C -ATOM 1079 N LYS A 155 22.122 -11.807 27.899 1.00 48.24 N -ANISOU 1079 N LYS A 155 7565 7161 3602 977 -1556 992 N -ATOM 1080 CA LYS A 155 22.240 -13.197 27.492 1.00 52.73 C -ANISOU 1080 CA LYS A 155 8158 7581 4297 1136 -1540 1132 C -ATOM 1081 C LYS A 155 22.903 -13.213 26.119 1.00 48.86 C -ANISOU 1081 C LYS A 155 7372 7106 4087 1185 -1555 1032 C -ATOM 1082 O LYS A 155 23.766 -14.039 25.821 1.00 51.53 O -ANISOU 1082 O LYS A 155 7626 7430 4521 1378 -1667 1099 O -ATOM 1083 CB LYS A 155 20.844 -13.816 27.410 1.00 59.69 C -ANISOU 1083 CB LYS A 155 9235 8248 5198 1056 -1279 1221 C -ATOM 1084 CG LYS A 155 20.794 -15.331 27.270 1.00 67.43 C -ANISOU 1084 CG LYS A 155 10347 9019 6254 1194 -1260 1392 C -ATOM 1085 CD LYS A 155 19.755 -15.912 28.229 1.00 72.51 C -ANISOU 1085 CD LYS A 155 11297 9527 6726 1138 -1115 1570 C -ATOM 1086 CE LYS A 155 19.507 -17.394 27.984 1.00 75.52 C -ANISOU 1086 CE LYS A 155 11832 9646 7214 1222 -1062 1738 C -ATOM 1087 NZ LYS A 155 18.843 -17.627 26.670 1.00 74.59 N -ANISOU 1087 NZ LYS A 155 11600 9372 7369 1111 -913 1651 N -ATOM 1088 N MET A 156 22.492 -12.262 25.292 1.00 41.91 N -ANISOU 1088 N MET A 156 6342 6257 3325 1023 -1431 874 N -ATOM 1089 CA MET A 156 22.893 -12.213 23.899 1.00 40.64 C -ANISOU 1089 CA MET A 156 5938 6094 3408 1044 -1386 777 C -ATOM 1090 C MET A 156 22.803 -10.747 23.456 1.00 42.92 C -ANISOU 1090 C MET A 156 6066 6505 3738 857 -1343 609 C -ATOM 1091 O MET A 156 21.939 -10.009 23.942 1.00 41.24 O -ANISOU 1091 O MET A 156 5976 6283 3411 709 -1255 567 O -ATOM 1092 CB MET A 156 21.926 -13.087 23.088 1.00 43.14 C -ANISOU 1092 CB MET A 156 6358 6180 3851 1039 -1192 811 C -ATOM 1093 CG MET A 156 22.048 -12.977 21.593 1.00 44.49 C -ANISOU 1093 CG MET A 156 6345 6323 4234 1034 -1108 695 C -ATOM 1094 SD MET A 156 20.578 -13.602 20.721 1.00 54.41 S -ANISOU 1094 SD MET A 156 7747 7326 5601 925 -897 693 S -ATOM 1095 CE MET A 156 20.441 -15.256 21.417 1.00 40.68 C -ANISOU 1095 CE MET A 156 6278 5369 3811 1066 -928 886 C -ATOM 1096 N VAL A 157 23.703 -10.322 22.564 1.00 39.46 N -ANISOU 1096 N VAL A 157 5362 6175 3456 875 -1394 523 N -ATOM 1097 CA VAL A 157 23.621 -9.001 21.934 1.00 35.38 C -ANISOU 1097 CA VAL A 157 4696 5736 3010 698 -1332 376 C -ATOM 1098 C VAL A 157 23.711 -9.162 20.431 1.00 34.38 C -ANISOU 1098 C VAL A 157 4406 5566 3092 729 -1205 323 C -ATOM 1099 O VAL A 157 24.623 -9.826 19.939 1.00 39.10 O -ANISOU 1099 O VAL A 157 4864 6202 3792 892 -1255 360 O -ATOM 1100 CB VAL A 157 24.784 -8.072 22.316 1.00 41.07 C -ANISOU 1100 CB VAL A 157 5231 6664 3710 643 -1530 318 C -ATOM 1101 CG1 VAL A 157 24.452 -6.632 21.908 1.00 39.14 C -ANISOU 1101 CG1 VAL A 157 4928 6447 3495 427 -1453 177 C -ATOM 1102 CG2 VAL A 157 25.057 -8.124 23.756 1.00 45.83 C -ANISOU 1102 CG2 VAL A 157 5980 7335 4098 664 -1723 378 C -ATOM 1103 N LYS A 158 22.772 -8.552 19.711 1.00 30.40 N -ANISOU 1103 N LYS A 158 3926 4986 2639 590 -1041 242 N -ATOM 1104 CA LYS A 158 22.785 -8.533 18.261 1.00 29.14 C -ANISOU 1104 CA LYS A 158 3640 4791 2639 598 -924 180 C -ATOM 1105 C LYS A 158 22.617 -7.091 17.852 1.00 31.00 C -ANISOU 1105 C LYS A 158 3781 5097 2901 418 -871 74 C -ATOM 1106 O LYS A 158 22.030 -6.300 18.594 1.00 31.33 O -ANISOU 1106 O LYS A 158 3923 5140 2842 293 -872 45 O -ATOM 1107 CB LYS A 158 21.618 -9.340 17.689 1.00 32.68 C -ANISOU 1107 CB LYS A 158 4252 5041 3124 604 -786 202 C -ATOM 1108 CG LYS A 158 21.647 -10.822 18.021 1.00 36.87 C -ANISOU 1108 CG LYS A 158 4926 5444 3640 764 -821 311 C -ATOM 1109 CD LYS A 158 22.869 -11.508 17.434 1.00 45.04 C -ANISOU 1109 CD LYS A 158 5838 6514 4759 971 -875 321 C -ATOM 1110 CE LYS A 158 22.811 -13.011 17.683 1.00 47.96 C -ANISOU 1110 CE LYS A 158 6394 6706 5120 1144 -898 426 C -ATOM 1111 NZ LYS A 158 24.085 -13.669 17.317 1.00 47.29 N -ANISOU 1111 NZ LYS A 158 6193 6670 5107 1393 -957 450 N -ATOM 1112 N VAL A 159 23.130 -6.750 16.677 1.00 27.40 N -ANISOU 1112 N VAL A 159 3154 4689 2570 418 -812 20 N -ATOM 1113 CA VAL A 159 22.976 -5.401 16.145 1.00 26.35 C -ANISOU 1113 CA VAL A 159 2943 4595 2471 251 -748 -66 C -ATOM 1114 C VAL A 159 22.286 -5.441 14.792 1.00 26.09 C -ANISOU 1114 C VAL A 159 2931 4465 2517 245 -589 -101 C -ATOM 1115 O VAL A 159 22.710 -6.160 13.889 1.00 30.21 O -ANISOU 1115 O VAL A 159 3394 4976 3107 367 -543 -91 O -ATOM 1116 CB VAL A 159 24.346 -4.700 15.997 1.00 27.67 C -ANISOU 1116 CB VAL A 159 2869 4937 2709 215 -832 -86 C -ATOM 1117 CG1 VAL A 159 24.199 -3.327 15.322 1.00 28.04 C -ANISOU 1117 CG1 VAL A 159 2857 4993 2805 35 -750 -162 C -ATOM 1118 CG2 VAL A 159 25.006 -4.566 17.352 1.00 29.47 C -ANISOU 1118 CG2 VAL A 159 3080 5269 2848 194 -1033 -61 C -ATOM 1119 N ALA A 160 21.206 -4.664 14.668 1.00 26.46 N -ANISOU 1119 N ALA A 160 3071 4439 2542 118 -510 -141 N -ATOM 1120 CA ALA A 160 20.547 -4.424 13.398 1.00 25.25 C -ANISOU 1120 CA ALA A 160 2928 4216 2451 86 -391 -177 C -ATOM 1121 C ALA A 160 20.865 -2.999 12.946 1.00 25.28 C -ANISOU 1121 C ALA A 160 2836 4283 2485 -36 -356 -230 C -ATOM 1122 O ALA A 160 20.638 -2.053 13.685 1.00 26.37 O -ANISOU 1122 O ALA A 160 3014 4427 2579 -144 -382 -257 O -ATOM 1123 CB ALA A 160 19.043 -4.611 13.536 1.00 22.00 C -ANISOU 1123 CB ALA A 160 2669 3676 2014 43 -334 -162 C -ATOM 1124 N SER A 161 21.374 -2.839 11.730 1.00 23.59 N -ANISOU 1124 N SER A 161 2524 4103 2336 -18 -287 -243 N -ATOM 1125 CA SER A 161 21.627 -1.501 11.202 1.00 23.23 C -ANISOU 1125 CA SER A 161 2408 4095 2324 -145 -237 -273 C -ATOM 1126 C SER A 161 20.937 -1.388 9.879 1.00 26.29 C -ANISOU 1126 C SER A 161 2857 4409 2725 -135 -124 -282 C -ATOM 1127 O SER A 161 21.074 -2.278 9.035 1.00 24.14 O -ANISOU 1127 O SER A 161 2589 4127 2456 -20 -80 -274 O -ATOM 1128 CB SER A 161 23.128 -1.250 11.038 1.00 28.63 C -ANISOU 1128 CB SER A 161 2881 4925 3072 -155 -259 -258 C -ATOM 1129 OG SER A 161 23.385 0.076 10.611 1.00 26.62 O -ANISOU 1129 OG SER A 161 2569 4689 2857 -311 -211 -274 O -ATOM 1130 N LEU A 162 20.173 -0.312 9.699 1.00 22.74 N -ANISOU 1130 N LEU A 162 2475 3896 2267 -240 -84 -299 N -ATOM 1131 CA LEU A 162 19.447 -0.104 8.446 1.00 23.76 C -ANISOU 1131 CA LEU A 162 2672 3959 2396 -231 -2 -296 C -ATOM 1132 C LEU A 162 20.440 -0.047 7.296 1.00 22.85 C -ANISOU 1132 C LEU A 162 2469 3917 2296 -201 77 -283 C -ATOM 1133 O LEU A 162 20.250 -0.680 6.255 1.00 25.75 O -ANISOU 1133 O LEU A 162 2892 4260 2632 -111 127 -284 O -ATOM 1134 CB LEU A 162 18.660 1.211 8.483 1.00 25.38 C -ANISOU 1134 CB LEU A 162 2946 4095 2601 -334 27 -302 C -ATOM 1135 CG LEU A 162 18.029 1.540 7.119 1.00 26.52 C -ANISOU 1135 CG LEU A 162 3151 4187 2737 -319 92 -283 C -ATOM 1136 CD1 LEU A 162 16.947 0.530 6.750 1.00 24.81 C -ANISOU 1136 CD1 LEU A 162 3009 3913 2503 -241 59 -278 C -ATOM 1137 CD2 LEU A 162 17.479 2.958 7.113 1.00 25.51 C -ANISOU 1137 CD2 LEU A 162 3082 3989 2620 -402 125 -275 C -ATOM 1138 N LEU A 163 21.510 0.719 7.492 1.00 22.11 N -ANISOU 1138 N LEU A 163 2242 3912 2247 -285 90 -271 N -ATOM 1139 CA LEU A 163 22.512 0.884 6.444 1.00 24.22 C -ANISOU 1139 CA LEU A 163 2394 4267 2540 -271 198 -238 C -ATOM 1140 C LEU A 163 23.893 0.503 6.939 1.00 26.13 C -ANISOU 1140 C LEU A 163 2421 4658 2849 -243 171 -215 C -ATOM 1141 O LEU A 163 24.215 0.684 8.111 1.00 26.30 O -ANISOU 1141 O LEU A 163 2375 4716 2901 -314 49 -224 O -ATOM 1142 CB LEU A 163 22.555 2.334 5.978 1.00 23.99 C -ANISOU 1142 CB LEU A 163 2371 4213 2532 -427 266 -213 C -ATOM 1143 CG LEU A 163 21.230 2.966 5.551 1.00 27.47 C -ANISOU 1143 CG LEU A 163 3004 4512 2921 -454 281 -219 C -ATOM 1144 CD1 LEU A 163 21.420 4.456 5.289 1.00 28.57 C -ANISOU 1144 CD1 LEU A 163 3158 4606 3092 -608 337 -185 C -ATOM 1145 CD2 LEU A 163 20.650 2.275 4.314 1.00 25.68 C -ANISOU 1145 CD2 LEU A 163 2882 4257 2619 -328 340 -209 C -ATOM 1146 N VAL A 164 24.709 -0.014 6.022 1.00 25.42 N -ANISOU 1146 N VAL A 164 2226 4658 2774 -130 285 -182 N -ATOM 1147 CA VAL A 164 26.137 -0.241 6.257 1.00 27.43 C -ANISOU 1147 CA VAL A 164 2217 5085 3120 -94 293 -136 C -ATOM 1148 C VAL A 164 26.878 0.300 5.053 1.00 28.91 C -ANISOU 1148 C VAL A 164 2287 5362 3338 -116 485 -78 C -ATOM 1149 O VAL A 164 26.579 -0.076 3.917 1.00 28.83 O -ANISOU 1149 O VAL A 164 2399 5311 3243 4 625 -81 O -ATOM 1150 CB VAL A 164 26.483 -1.735 6.406 1.00 28.01 C -ANISOU 1150 CB VAL A 164 2263 5194 3184 146 273 -138 C -ATOM 1151 CG1 VAL A 164 27.997 -1.921 6.474 1.00 30.51 C -ANISOU 1151 CG1 VAL A 164 2269 5712 3611 216 305 -72 C -ATOM 1152 CG2 VAL A 164 25.807 -2.310 7.641 1.00 26.87 C -ANISOU 1152 CG2 VAL A 164 2239 4965 3006 163 94 -171 C -ATOM 1153 N LYS A 165 27.833 1.188 5.294 1.00 30.54 N -ANISOU 1153 N LYS A 165 2266 5684 3656 -281 489 -22 N -ATOM 1154 CA LYS A 165 28.599 1.787 4.213 1.00 32.64 C -ANISOU 1154 CA LYS A 165 2394 6043 3965 -333 692 59 C -ATOM 1155 C LYS A 165 29.769 0.914 3.836 1.00 39.41 C -ANISOU 1155 C LYS A 165 3000 7088 4885 -144 809 117 C -ATOM 1156 O LYS A 165 30.469 0.388 4.715 1.00 36.03 O -ANISOU 1156 O LYS A 165 2365 6774 4550 -88 686 127 O -ATOM 1157 CB LYS A 165 29.129 3.159 4.615 1.00 40.03 C -ANISOU 1157 CB LYS A 165 3186 7009 5017 -625 649 106 C -ATOM 1158 CG LYS A 165 28.123 4.286 4.521 1.00 42.69 C -ANISOU 1158 CG LYS A 165 3776 7152 5294 -801 631 78 C -ATOM 1159 CD LYS A 165 28.830 5.592 4.135 1.00 43.52 C -ANISOU 1159 CD LYS A 165 3760 7278 5499 -1051 722 165 C -ATOM 1160 CE LYS A 165 27.829 6.718 4.163 1.00 39.09 C -ANISOU 1160 CE LYS A 165 3472 6497 4883 -1204 686 135 C -ATOM 1161 NZ LYS A 165 28.438 8.055 4.224 1.00 35.03 N -ANISOU 1161 NZ LYS A 165 2884 5946 4482 -1493 698 195 N -ATOM 1162 N ARG A 166 29.991 0.772 2.529 1.00 38.92 N -ANISOU 1162 N ARG A 166 2963 7062 4762 -29 1052 159 N -ATOM 1163 CA ARG A 166 31.211 0.162 2.026 1.00 44.24 C -ANISOU 1163 CA ARG A 166 3373 7932 5504 149 1229 233 C -ATOM 1164 C ARG A 166 32.330 1.178 2.076 1.00 50.28 C -ANISOU 1164 C ARG A 166 3789 8872 6444 -69 1298 353 C -ATOM 1165 O ARG A 166 32.350 2.145 1.312 1.00 53.45 O -ANISOU 1165 O ARG A 166 4217 9258 6833 -233 1453 418 O -ATOM 1166 CB ARG A 166 31.041 -0.304 0.582 1.00 43.64 C -ANISOU 1166 CB ARG A 166 3482 7829 5271 351 1487 232 C -ATOM 1167 CG ARG A 166 30.252 -1.582 0.439 1.00 40.39 C -ANISOU 1167 CG ARG A 166 3359 7277 4711 604 1434 119 C -ATOM 1168 CD ARG A 166 30.468 -2.167 -0.954 1.00 45.33 C -ANISOU 1168 CD ARG A 166 4116 7919 5188 841 1701 117 C -ATOM 1169 NE ARG A 166 30.036 -1.226 -1.979 1.00 39.17 N -ANISOU 1169 NE ARG A 166 3505 7093 4286 707 1837 152 N -ATOM 1170 CZ ARG A 166 28.764 -0.983 -2.271 1.00 36.98 C -ANISOU 1170 CZ ARG A 166 3557 6628 3866 629 1730 85 C -ATOM 1171 NH1 ARG A 166 27.806 -1.620 -1.617 1.00 34.75 N -ANISOU 1171 NH1 ARG A 166 3451 6195 3558 657 1502 -20 N -ATOM 1172 NH2 ARG A 166 28.452 -0.114 -3.222 1.00 45.44 N -ANISOU 1172 NH2 ARG A 166 4773 7667 4824 528 1851 136 N -ATOM 1173 N THR A 167 33.270 0.964 2.978 1.00 53.89 N -ANISOU 1173 N THR A 167 3915 9492 7067 -81 1173 392 N -ATOM 1174 CA THR A 167 34.372 1.889 3.090 1.00 61.36 C -ANISOU 1174 CA THR A 167 4557 10547 8211 -311 1186 495 C -ATOM 1175 C THR A 167 35.630 1.116 3.456 1.00 67.97 C -ANISOU 1175 C THR A 167 5087 11530 9210 -143 1152 544 C -ATOM 1176 O THR A 167 35.583 0.200 4.279 1.00 68.48 O -ANISOU 1176 O THR A 167 5122 11632 9266 27 978 500 O -ATOM 1177 CB THR A 167 34.043 3.030 4.104 1.00 64.29 C -ANISOU 1177 CB THR A 167 4940 10847 8639 -665 938 466 C -ATOM 1178 OG1 THR A 167 35.081 4.016 4.094 1.00 60.12 O -ANISOU 1178 OG1 THR A 167 4196 10343 8304 -907 947 552 O -ATOM 1179 CG2 THR A 167 33.853 2.489 5.519 1.00 62.71 C -ANISOU 1179 CG2 THR A 167 4720 10665 8441 -635 628 386 C -ATOM 1180 N PRO A 168 36.756 1.454 2.810 1.00 74.81 N -ANISOU 1180 N PRO A 168 5728 12477 10220 -178 1331 638 N -ATOM 1181 CA PRO A 168 38.057 0.945 3.255 1.00 80.25 C -ANISOU 1181 CA PRO A 168 6069 13319 11102 -78 1276 692 C -ATOM 1182 C PRO A 168 38.340 1.429 4.679 1.00 83.00 C -ANISOU 1182 C PRO A 168 6254 13697 11585 -308 926 681 C -ATOM 1183 O PRO A 168 39.174 0.853 5.381 1.00 84.16 O -ANISOU 1183 O PRO A 168 6161 13960 11858 -205 779 704 O -ATOM 1184 CB PRO A 168 39.047 1.571 2.257 1.00 83.41 C -ANISOU 1184 CB PRO A 168 6277 13789 11627 -170 1543 789 C -ATOM 1185 CG PRO A 168 38.300 2.694 1.598 1.00 80.57 C -ANISOU 1185 CG PRO A 168 6151 13292 11170 -410 1657 796 C -ATOM 1186 CD PRO A 168 36.867 2.264 1.584 1.00 76.96 C -ANISOU 1186 CD PRO A 168 6064 12706 10472 -292 1608 701 C -ATOM 1187 N ARG A 169 37.622 2.477 5.087 1.00 80.97 N -ANISOU 1187 N ARG A 169 6159 13322 11284 -608 790 640 N -ATOM 1188 CA ARG A 169 37.713 3.058 6.427 1.00 80.44 C -ANISOU 1188 CA ARG A 169 6040 13234 11291 -850 450 598 C -ATOM 1189 C ARG A 169 37.097 2.178 7.520 1.00 77.06 C -ANISOU 1189 C ARG A 169 5736 12800 10743 -696 196 515 C -ATOM 1190 O ARG A 169 37.248 2.468 8.708 1.00 75.38 O -ANISOU 1190 O ARG A 169 5497 12579 10565 -845 -100 475 O -ATOM 1191 CB ARG A 169 37.039 4.440 6.452 1.00 79.63 C -ANISOU 1191 CB ARG A 169 6142 12965 11149 -1194 409 563 C -ATOM 1192 CG ARG A 169 37.992 5.627 6.576 1.00 82.91 C -ANISOU 1192 CG ARG A 169 6362 13371 11769 -1512 361 615 C -ATOM 1193 CD ARG A 169 37.342 6.938 6.120 1.00 81.36 C -ANISOU 1193 CD ARG A 169 6402 12982 11529 -1790 443 611 C -ATOM 1194 NE ARG A 169 36.492 7.561 7.136 1.00 78.57 N -ANISOU 1194 NE ARG A 169 6309 12465 11080 -1981 179 496 N -ATOM 1195 CZ ARG A 169 35.172 7.702 7.033 1.00 78.12 C -ANISOU 1195 CZ ARG A 169 6589 12265 10829 -1973 202 425 C -ATOM 1196 NH1 ARG A 169 34.529 7.257 5.959 1.00 75.90 N -ANISOU 1196 NH1 ARG A 169 6425 11988 10425 -1791 458 458 N -ATOM 1197 NH2 ARG A 169 34.487 8.288 8.008 1.00 78.34 N -ANISOU 1197 NH2 ARG A 169 6848 12140 10777 -2140 -28 312 N -ATOM 1198 N SER A 170 36.397 1.117 7.124 1.00 77.02 N -ANISOU 1198 N SER A 170 5893 12786 10587 -401 309 485 N -ATOM 1199 CA SER A 170 35.765 0.219 8.090 1.00 75.31 C -ANISOU 1199 CA SER A 170 5811 12552 10251 -238 96 416 C -ATOM 1200 C SER A 170 36.803 -0.457 8.974 1.00 77.12 C -ANISOU 1200 C SER A 170 5803 12896 10603 -113 -100 463 C -ATOM 1201 O SER A 170 37.749 -1.069 8.476 1.00 78.31 O -ANISOU 1201 O SER A 170 5734 13150 10870 88 35 538 O -ATOM 1202 CB SER A 170 34.916 -0.843 7.387 1.00 73.77 C -ANISOU 1202 CB SER A 170 5824 12313 9894 71 274 377 C -ATOM 1203 OG SER A 170 34.597 -1.906 8.273 1.00 71.07 O -ANISOU 1203 OG SER A 170 5587 11937 9478 278 87 336 O -ATOM 1204 N VAL A 171 36.615 -0.345 10.288 1.00 77.07 N -ANISOU 1204 N VAL A 171 5862 12865 10558 -222 -416 415 N -ATOM 1205 CA VAL A 171 37.514 -0.972 11.259 1.00 80.05 C -ANISOU 1205 CA VAL A 171 6054 13338 11024 -109 -646 457 C -ATOM 1206 C VAL A 171 37.277 -2.486 11.238 1.00 75.62 C -ANISOU 1206 C VAL A 171 5571 12784 10377 286 -602 476 C -ATOM 1207 O VAL A 171 37.998 -3.267 11.870 1.00 75.49 O -ANISOU 1207 O VAL A 171 5419 12838 10425 467 -746 529 O -ATOM 1208 CB VAL A 171 37.328 -0.371 12.682 1.00 88.36 C -ANISOU 1208 CB VAL A 171 7220 14335 12019 -342 -999 391 C -ATOM 1209 CG1 VAL A 171 38.440 -0.817 13.616 1.00 91.70 C -ANISOU 1209 CG1 VAL A 171 7416 14870 12557 -267 -1246 443 C -ATOM 1210 CG2 VAL A 171 37.314 1.148 12.615 1.00 87.42 C -ANISOU 1210 CG2 VAL A 171 7123 14143 11951 -724 -1017 346 C -ATOM 1211 N GLY A 172 36.262 -2.890 10.482 1.00 69.75 N -ANISOU 1211 N GLY A 172 5059 11953 9489 422 -404 430 N -ATOM 1212 CA GLY A 172 36.001 -4.294 10.249 1.00 69.66 C -ANISOU 1212 CA GLY A 172 5160 11907 9400 800 -319 436 C -ATOM 1213 C GLY A 172 34.777 -4.820 10.967 1.00 68.25 C -ANISOU 1213 C GLY A 172 5322 11581 9030 860 -466 361 C -ATOM 1214 O GLY A 172 34.461 -6.003 10.838 1.00 67.85 O -ANISOU 1214 O GLY A 172 5452 11419 8909 1149 -411 356 O -ATOM 1215 N TYR A 173 34.086 -3.959 11.717 1.00 65.29 N -ANISOU 1215 N TYR A 173 5126 11111 8571 573 -634 293 N -ATOM 1216 CA TYR A 173 32.894 -4.403 12.442 1.00 56.37 C -ANISOU 1216 CA TYR A 173 4394 9764 7261 596 -743 222 C -ATOM 1217 C TYR A 173 31.699 -4.654 11.517 1.00 53.22 C -ANISOU 1217 C TYR A 173 4326 9140 6756 647 -525 148 C -ATOM 1218 O TYR A 173 31.380 -3.828 10.662 1.00 48.58 O -ANISOU 1218 O TYR A 173 3770 8513 6174 495 -368 110 O -ATOM 1219 CB TYR A 173 32.487 -3.446 13.575 1.00 52.69 C -ANISOU 1219 CB TYR A 173 4042 9264 6716 308 -971 167 C -ATOM 1220 CG TYR A 173 31.163 -3.874 14.159 1.00 46.60 C -ANISOU 1220 CG TYR A 173 3678 8270 5759 341 -1008 105 C -ATOM 1221 CD1 TYR A 173 31.093 -4.935 15.053 1.00 45.05 C -ANISOU 1221 CD1 TYR A 173 3590 8047 5480 530 -1151 148 C -ATOM 1222 CD2 TYR A 173 29.973 -3.265 13.763 1.00 41.64 C -ANISOU 1222 CD2 TYR A 173 3315 7460 5047 198 -883 21 C -ATOM 1223 CE1 TYR A 173 29.877 -5.365 15.553 1.00 41.80 C -ANISOU 1223 CE1 TYR A 173 3536 7436 4911 551 -1154 113 C -ATOM 1224 CE2 TYR A 173 28.756 -3.685 14.263 1.00 37.58 C -ANISOU 1224 CE2 TYR A 173 3128 6763 4388 230 -895 -18 C -ATOM 1225 CZ TYR A 173 28.715 -4.735 15.152 1.00 40.28 C -ANISOU 1225 CZ TYR A 173 3566 7084 4654 396 -1021 30 C -ATOM 1226 OH TYR A 173 27.499 -5.151 15.642 1.00 45.55 O -ANISOU 1226 OH TYR A 173 4545 7574 5188 410 -1010 10 O -ATOM 1227 N LYS A 174 31.037 -5.793 11.726 1.00 53.07 N -ANISOU 1227 N LYS A 174 4557 8967 6640 849 -536 136 N -ATOM 1228 CA LYS A 174 29.872 -6.206 10.946 1.00 48.95 C -ANISOU 1228 CA LYS A 174 4352 8225 6020 899 -378 68 C -ATOM 1229 C LYS A 174 28.657 -6.437 11.841 1.00 39.40 C -ANISOU 1229 C LYS A 174 3451 6833 4684 828 -499 32 C -ATOM 1230 O LYS A 174 28.698 -7.269 12.743 1.00 38.31 O -ANISOU 1230 O LYS A 174 3381 6667 4506 951 -633 77 O -ATOM 1231 CB LYS A 174 30.175 -7.504 10.195 1.00 55.61 C -ANISOU 1231 CB LYS A 174 5230 9023 6877 1218 -246 88 C -ATOM 1232 CG LYS A 174 30.881 -7.331 8.859 1.00 62.76 C -ANISOU 1232 CG LYS A 174 5963 10032 7851 1308 -12 93 C -ATOM 1233 CD LYS A 174 32.075 -8.278 8.736 1.00 71.44 C -ANISOU 1233 CD LYS A 174 6841 11260 9044 1626 38 169 C -ATOM 1234 CE LYS A 174 31.848 -9.618 9.451 1.00 74.90 C -ANISOU 1234 CE LYS A 174 7470 11554 9432 1863 -88 186 C -ATOM 1235 NZ LYS A 174 30.915 -10.542 8.737 1.00 76.25 N -ANISOU 1235 NZ LYS A 174 8023 11458 9491 1998 27 106 N -ATOM 1236 N PRO A 175 27.560 -5.714 11.582 1.00 36.46 N -ANISOU 1236 N PRO A 175 3266 6339 4247 641 -441 -35 N -ATOM 1237 CA PRO A 175 26.360 -5.974 12.382 1.00 29.62 C -ANISOU 1237 CA PRO A 175 2670 5312 3273 587 -518 -56 C -ATOM 1238 C PRO A 175 25.743 -7.324 11.995 1.00 33.91 C -ANISOU 1238 C PRO A 175 3416 5685 3781 772 -458 -49 C -ATOM 1239 O PRO A 175 26.179 -7.946 11.021 1.00 36.38 O -ANISOU 1239 O PRO A 175 3698 5991 4136 936 -350 -54 O -ATOM 1240 CB PRO A 175 25.434 -4.821 11.998 1.00 31.57 C -ANISOU 1240 CB PRO A 175 3014 5489 3491 372 -444 -120 C -ATOM 1241 CG PRO A 175 25.860 -4.458 10.601 1.00 32.55 C -ANISOU 1241 CG PRO A 175 3025 5661 3683 382 -283 -135 C -ATOM 1242 CD PRO A 175 27.340 -4.674 10.560 1.00 33.23 C -ANISOU 1242 CD PRO A 175 2832 5932 3863 489 -296 -79 C -ATOM 1243 N ASP A 176 24.746 -7.764 12.753 1.00 28.48 N -ANISOU 1243 N ASP A 176 2947 4859 3015 739 -520 -38 N -ATOM 1244 CA ASP A 176 24.135 -9.077 12.561 1.00 31.94 C -ANISOU 1244 CA ASP A 176 3594 5112 3429 876 -493 -20 C -ATOM 1245 C ASP A 176 22.995 -9.055 11.548 1.00 31.41 C -ANISOU 1245 C ASP A 176 3687 4896 3353 794 -383 -85 C -ATOM 1246 O ASP A 176 22.763 -10.032 10.822 1.00 31.64 O -ANISOU 1246 O ASP A 176 3852 4786 3385 909 -334 -103 O -ATOM 1247 CB ASP A 176 23.617 -9.579 13.908 1.00 30.36 C -ANISOU 1247 CB ASP A 176 3543 4839 3153 862 -607 48 C -ATOM 1248 CG ASP A 176 24.693 -9.606 14.953 1.00 34.14 C -ANISOU 1248 CG ASP A 176 3890 5467 3615 942 -754 116 C -ATOM 1249 OD1 ASP A 176 25.486 -10.569 14.931 1.00 36.16 O -ANISOU 1249 OD1 ASP A 176 4105 5728 3907 1161 -790 173 O -ATOM 1250 OD2 ASP A 176 24.765 -8.667 15.782 1.00 33.82 O -ANISOU 1250 OD2 ASP A 176 3792 5536 3521 798 -841 110 O -ATOM 1251 N PHE A 177 22.282 -7.935 11.518 1.00 25.46 N -ANISOU 1251 N PHE A 177 2927 4162 2583 598 -358 -121 N -ATOM 1252 CA PHE A 177 21.162 -7.733 10.614 1.00 25.54 C -ANISOU 1252 CA PHE A 177 3057 4060 2588 506 -281 -171 C -ATOM 1253 C PHE A 177 21.413 -6.438 9.864 1.00 28.30 C -ANISOU 1253 C PHE A 177 3283 4515 2955 408 -209 -214 C -ATOM 1254 O PHE A 177 21.668 -5.410 10.484 1.00 31.47 O -ANISOU 1254 O PHE A 177 3584 5013 3361 298 -238 -209 O -ATOM 1255 CB PHE A 177 19.862 -7.625 11.414 1.00 23.23 C -ANISOU 1255 CB PHE A 177 2887 3676 2265 374 -314 -145 C -ATOM 1256 CG PHE A 177 19.611 -8.805 12.325 1.00 25.63 C -ANISOU 1256 CG PHE A 177 3317 3879 2545 440 -375 -75 C -ATOM 1257 CD1 PHE A 177 19.111 -9.996 11.811 1.00 26.99 C -ANISOU 1257 CD1 PHE A 177 3641 3879 2736 499 -370 -68 C -ATOM 1258 CD2 PHE A 177 19.882 -8.720 13.691 1.00 26.22 C -ANISOU 1258 CD2 PHE A 177 3382 4016 2565 437 -445 -14 C -ATOM 1259 CE1 PHE A 177 18.888 -11.093 12.655 1.00 31.56 C -ANISOU 1259 CE1 PHE A 177 4354 4338 3299 549 -420 14 C -ATOM 1260 CE2 PHE A 177 19.658 -9.801 14.534 1.00 30.87 C -ANISOU 1260 CE2 PHE A 177 4107 4506 3116 502 -493 71 C -ATOM 1261 CZ PHE A 177 19.159 -10.992 14.004 1.00 32.94 C -ANISOU 1261 CZ PHE A 177 4514 4585 3417 555 -473 92 C -ATOM 1262 N VAL A 178 21.369 -6.495 8.533 1.00 23.98 N -ANISOU 1262 N VAL A 178 2769 3936 2406 448 -120 -255 N -ATOM 1263 CA VAL A 178 21.648 -5.323 7.714 1.00 23.58 C -ANISOU 1263 CA VAL A 178 2624 3975 2363 367 -34 -276 C -ATOM 1264 C VAL A 178 20.530 -5.061 6.710 1.00 24.30 C -ANISOU 1264 C VAL A 178 2859 3963 2412 302 7 -312 C -ATOM 1265 O VAL A 178 20.153 -5.952 5.935 1.00 22.50 O -ANISOU 1265 O VAL A 178 2771 3635 2145 386 15 -343 O -ATOM 1266 CB VAL A 178 22.961 -5.497 6.930 1.00 29.74 C -ANISOU 1266 CB VAL A 178 3270 4866 3163 500 63 -272 C -ATOM 1267 CG1 VAL A 178 23.193 -4.319 5.980 1.00 30.18 C -ANISOU 1267 CG1 VAL A 178 3252 4997 3217 404 176 -275 C -ATOM 1268 CG2 VAL A 178 24.124 -5.650 7.890 1.00 32.28 C -ANISOU 1268 CG2 VAL A 178 3396 5321 3547 560 1 -223 C -ATOM 1269 N GLY A 179 20.014 -3.836 6.683 1.00 22.89 N -ANISOU 1269 N GLY A 179 2659 3801 2237 159 20 -308 N -ATOM 1270 CA GLY A 179 19.026 -3.507 5.667 1.00 22.95 C -ANISOU 1270 CA GLY A 179 2782 3732 2206 115 44 -326 C -ATOM 1271 C GLY A 179 19.638 -3.391 4.284 1.00 22.82 C -ANISOU 1271 C GLY A 179 2781 3755 2136 181 146 -342 C -ATOM 1272 O GLY A 179 19.316 -4.160 3.364 1.00 25.21 O -ANISOU 1272 O GLY A 179 3224 3984 2370 263 149 -378 O -ATOM 1273 N PHE A 180 20.549 -2.428 4.124 1.00 21.68 N -ANISOU 1273 N PHE A 180 2504 3721 2013 139 233 -313 N -ATOM 1274 CA PHE A 180 21.103 -2.123 2.814 1.00 23.52 C -ANISOU 1274 CA PHE A 180 2747 4003 2185 184 365 -304 C -ATOM 1275 C PHE A 180 22.586 -1.859 2.969 1.00 24.33 C -ANISOU 1275 C PHE A 180 2636 4257 2351 204 462 -263 C -ATOM 1276 O PHE A 180 22.994 -1.205 3.929 1.00 26.24 O -ANISOU 1276 O PHE A 180 2729 4558 2681 93 413 -236 O -ATOM 1277 CB PHE A 180 20.434 -0.864 2.247 1.00 24.14 C -ANISOU 1277 CB PHE A 180 2888 4049 2235 60 389 -275 C -ATOM 1278 CG PHE A 180 18.950 -1.002 2.075 1.00 25.08 C -ANISOU 1278 CG PHE A 180 3170 4047 2314 37 282 -297 C -ATOM 1279 CD1 PHE A 180 18.083 -0.808 3.146 1.00 24.49 C -ANISOU 1279 CD1 PHE A 180 3078 3918 2308 -40 182 -294 C -ATOM 1280 CD2 PHE A 180 18.426 -1.346 0.835 1.00 26.45 C -ANISOU 1280 CD2 PHE A 180 3507 4168 2375 97 282 -316 C -ATOM 1281 CE1 PHE A 180 16.711 -0.964 2.978 1.00 19.50 C -ANISOU 1281 CE1 PHE A 180 2547 3195 1665 -60 92 -297 C -ATOM 1282 CE2 PHE A 180 17.061 -1.500 0.662 1.00 28.30 C -ANISOU 1282 CE2 PHE A 180 3856 4306 2590 63 156 -328 C -ATOM 1283 CZ PHE A 180 16.211 -1.316 1.733 1.00 20.07 C -ANISOU 1283 CZ PHE A 180 2752 3225 1649 -16 66 -311 C -ATOM 1284 N GLU A 181 23.378 -2.332 2.017 1.00 25.63 N -ANISOU 1284 N GLU A 181 2785 4486 2468 342 599 -259 N -ATOM 1285 CA GLU A 181 24.801 -2.016 1.996 1.00 29.81 C -ANISOU 1285 CA GLU A 181 3069 5184 3074 360 722 -198 C -ATOM 1286 C GLU A 181 25.012 -0.991 0.885 1.00 33.15 C -ANISOU 1286 C GLU A 181 3499 5650 3447 281 886 -145 C -ATOM 1287 O GLU A 181 24.702 -1.253 -0.284 1.00 30.28 O -ANISOU 1287 O GLU A 181 3318 5243 2946 378 986 -162 O -ATOM 1288 CB GLU A 181 25.644 -3.265 1.733 1.00 29.07 C -ANISOU 1288 CB GLU A 181 2925 5150 2971 603 802 -211 C -ATOM 1289 CG GLU A 181 27.141 -3.011 1.858 1.00 36.13 C -ANISOU 1289 CG GLU A 181 3498 6248 3980 634 917 -132 C -ATOM 1290 CD GLU A 181 27.981 -4.135 1.291 1.00 40.25 C -ANISOU 1290 CD GLU A 181 3979 6835 4479 918 1060 -135 C -ATOM 1291 OE1 GLU A 181 28.121 -4.196 0.053 1.00 39.74 O -ANISOU 1291 OE1 GLU A 181 4018 6779 4303 1022 1257 -139 O -ATOM 1292 OE2 GLU A 181 28.493 -4.949 2.087 1.00 41.33 O -ANISOU 1292 OE2 GLU A 181 3997 7010 4697 1051 980 -129 O -ATOM 1293 N ILE A 182 25.537 0.177 1.247 1.00 30.53 N -ANISOU 1293 N ILE A 182 2992 5393 3216 98 907 -78 N -ATOM 1294 CA ILE A 182 25.526 1.320 0.341 1.00 29.29 C -ANISOU 1294 CA ILE A 182 2881 5231 3019 -24 1038 -11 C -ATOM 1295 C ILE A 182 26.936 1.797 0.010 1.00 31.78 C -ANISOU 1295 C ILE A 182 2936 5717 3422 -72 1218 88 C -ATOM 1296 O ILE A 182 27.881 1.521 0.754 1.00 34.33 O -ANISOU 1296 O ILE A 182 2997 6168 3878 -68 1189 107 O -ATOM 1297 CB ILE A 182 24.677 2.482 0.925 1.00 27.83 C -ANISOU 1297 CB ILE A 182 2779 4926 2870 -231 913 -10 C -ATOM 1298 CG1 ILE A 182 25.302 3.032 2.206 1.00 29.10 C -ANISOU 1298 CG1 ILE A 182 2734 5139 3184 -391 811 -2 C -ATOM 1299 CG2 ILE A 182 23.243 2.040 1.189 1.00 26.19 C -ANISOU 1299 CG2 ILE A 182 2790 4571 2589 -180 762 -86 C -ATOM 1300 CD1 ILE A 182 24.749 4.398 2.624 1.00 31.72 C -ANISOU 1300 CD1 ILE A 182 3152 5351 3550 -602 745 7 C -ATOM 1301 N PRO A 183 27.100 2.499 -1.128 1.00 33.06 N -ANISOU 1301 N PRO A 183 3158 5892 3510 -115 1408 167 N -ATOM 1302 CA PRO A 183 28.432 3.033 -1.416 1.00 35.74 C -ANISOU 1302 CA PRO A 183 3223 6400 3957 -195 1599 285 C -ATOM 1303 C PRO A 183 28.793 4.180 -0.477 1.00 35.98 C -ANISOU 1303 C PRO A 183 3069 6433 4168 -483 1491 333 C -ATOM 1304 O PRO A 183 27.956 4.616 0.329 1.00 34.02 O -ANISOU 1304 O PRO A 183 2951 6043 3935 -598 1290 268 O -ATOM 1305 CB PRO A 183 28.314 3.537 -2.867 1.00 36.99 C -ANISOU 1305 CB PRO A 183 3560 6537 3957 -179 1826 365 C -ATOM 1306 CG PRO A 183 26.861 3.719 -3.104 1.00 34.75 C -ANISOU 1306 CG PRO A 183 3621 6055 3527 -180 1687 299 C -ATOM 1307 CD PRO A 183 26.151 2.719 -2.238 1.00 33.50 C -ANISOU 1307 CD PRO A 183 3523 5828 3377 -73 1463 165 C -ATOM 1308 N ASP A 184 30.032 4.655 -0.582 1.00 39.18 N -ANISOU 1308 N ASP A 184 3178 6998 4712 -598 1627 445 N -ATOM 1309 CA ASP A 184 30.516 5.756 0.250 1.00 46.78 C -ANISOU 1309 CA ASP A 184 3957 7961 5855 -903 1517 491 C -ATOM 1310 C ASP A 184 29.966 7.098 -0.245 1.00 46.05 C -ANISOU 1310 C ASP A 184 4078 7696 5723 -1117 1569 548 C -ATOM 1311 O ASP A 184 30.694 7.894 -0.833 1.00 45.03 O -ANISOU 1311 O ASP A 184 3829 7618 5663 -1280 1745 681 O -ATOM 1312 CB ASP A 184 32.051 5.787 0.250 1.00 51.42 C -ANISOU 1312 CB ASP A 184 4120 8789 6628 -974 1640 608 C -ATOM 1313 CG ASP A 184 32.628 6.638 1.380 1.00 57.53 C -ANISOU 1313 CG ASP A 184 4686 9563 7609 -1273 1433 618 C -ATOM 1314 OD1 ASP A 184 31.856 7.351 2.056 1.00 58.07 O -ANISOU 1314 OD1 ASP A 184 4951 9458 7654 -1450 1248 546 O -ATOM 1315 OD2 ASP A 184 33.862 6.593 1.582 1.00 62.45 O -ANISOU 1315 OD2 ASP A 184 5009 10297 8420 -1302 1436 677 O -ATOM 1316 N LYS A 185 28.677 7.328 -0.015 1.00 41.29 N -ANISOU 1316 N LYS A 185 3786 6888 5013 -1106 1426 460 N -ATOM 1317 CA LYS A 185 28.019 8.577 -0.400 1.00 43.00 C -ANISOU 1317 CA LYS A 185 4237 6913 5189 -1268 1448 509 C -ATOM 1318 C LYS A 185 27.292 9.055 0.834 1.00 35.18 C -ANISOU 1318 C LYS A 185 3355 5763 4249 -1379 1201 402 C -ATOM 1319 O LYS A 185 26.854 8.237 1.628 1.00 33.38 O -ANISOU 1319 O LYS A 185 3134 5547 4000 -1255 1045 290 O -ATOM 1320 CB LYS A 185 26.952 8.323 -1.470 1.00 40.46 C -ANISOU 1320 CB LYS A 185 4226 6494 4655 -1078 1522 507 C -ATOM 1321 CG LYS A 185 27.452 7.909 -2.834 1.00 51.80 C -ANISOU 1321 CG LYS A 185 5664 8048 5968 -941 1778 600 C -ATOM 1322 CD LYS A 185 26.258 7.556 -3.722 1.00 54.33 C -ANISOU 1322 CD LYS A 185 6324 8261 6058 -752 1768 564 C -ATOM 1323 CE LYS A 185 26.280 8.326 -5.028 1.00 56.44 C -ANISOU 1323 CE LYS A 185 6764 8492 6189 -781 1973 707 C -ATOM 1324 NZ LYS A 185 27.507 8.034 -5.800 1.00 57.55 N -ANISOU 1324 NZ LYS A 185 6735 8823 6310 -736 2254 808 N -ATOM 1325 N PHE A 186 27.130 10.364 0.994 1.00 35.93 N -ANISOU 1325 N PHE A 186 3563 5693 4397 -1600 1177 438 N -ATOM 1326 CA PHE A 186 26.379 10.858 2.154 1.00 34.58 C -ANISOU 1326 CA PHE A 186 3539 5352 4247 -1677 965 325 C -ATOM 1327 C PHE A 186 24.881 10.810 1.888 1.00 34.20 C -ANISOU 1327 C PHE A 186 3792 5146 4058 -1502 933 278 C -ATOM 1328 O PHE A 186 24.404 11.370 0.893 1.00 38.75 O -ANISOU 1328 O PHE A 186 4544 5620 4557 -1479 1044 362 O -ATOM 1329 CB PHE A 186 26.800 12.283 2.516 1.00 40.20 C -ANISOU 1329 CB PHE A 186 4280 5919 5076 -1980 938 364 C -ATOM 1330 CG PHE A 186 26.398 12.684 3.902 1.00 44.06 C -ANISOU 1330 CG PHE A 186 4870 6276 5596 -2071 717 228 C -ATOM 1331 CD1 PHE A 186 25.172 13.290 4.134 1.00 46.58 C -ANISOU 1331 CD1 PHE A 186 5500 6363 5835 -2016 665 168 C -ATOM 1332 CD2 PHE A 186 27.242 12.437 4.977 1.00 49.37 C -ANISOU 1332 CD2 PHE A 186 5328 7063 6366 -2193 560 163 C -ATOM 1333 CE1 PHE A 186 24.789 13.650 5.424 1.00 51.71 C -ANISOU 1333 CE1 PHE A 186 6268 6890 6489 -2075 490 37 C -ATOM 1334 CE2 PHE A 186 26.872 12.789 6.270 1.00 53.33 C -ANISOU 1334 CE2 PHE A 186 5962 7443 6857 -2268 355 30 C -ATOM 1335 CZ PHE A 186 25.644 13.401 6.493 1.00 53.47 C -ANISOU 1335 CZ PHE A 186 6312 7222 6782 -2206 335 -38 C -ATOM 1336 N VAL A 187 24.143 10.133 2.766 1.00 30.30 N -ANISOU 1336 N VAL A 187 3343 4639 3529 -1379 780 160 N -ATOM 1337 CA VAL A 187 22.707 9.994 2.588 1.00 29.57 C -ANISOU 1337 CA VAL A 187 3479 4426 3329 -1215 739 122 C -ATOM 1338 C VAL A 187 21.943 10.568 3.771 1.00 33.30 C -ANISOU 1338 C VAL A 187 4078 4747 3825 -1259 603 32 C -ATOM 1339 O VAL A 187 22.462 10.632 4.892 1.00 28.59 O -ANISOU 1339 O VAL A 187 3398 4171 3292 -1366 502 -38 O -ATOM 1340 CB VAL A 187 22.281 8.520 2.372 1.00 29.53 C -ANISOU 1340 CB VAL A 187 3442 4535 3241 -993 714 76 C -ATOM 1341 CG1 VAL A 187 22.867 7.975 1.080 1.00 27.75 C -ANISOU 1341 CG1 VAL A 187 3165 4429 2950 -907 868 151 C -ATOM 1342 CG2 VAL A 187 22.685 7.667 3.559 1.00 32.33 C -ANISOU 1342 CG2 VAL A 187 3645 4991 3650 -975 596 -9 C -ATOM 1343 N VAL A 188 20.707 10.985 3.514 1.00 26.83 N -ANISOU 1343 N VAL A 188 3466 3782 2948 -1162 600 38 N -ATOM 1344 CA VAL A 188 19.864 11.582 4.547 1.00 26.41 C -ANISOU 1344 CA VAL A 188 3554 3575 2905 -1161 512 -39 C -ATOM 1345 C VAL A 188 18.463 11.030 4.386 1.00 26.00 C -ANISOU 1345 C VAL A 188 3586 3505 2788 -951 485 -49 C -ATOM 1346 O VAL A 188 18.184 10.353 3.408 1.00 25.74 O -ANISOU 1346 O VAL A 188 3531 3548 2699 -842 515 2 O -ATOM 1347 CB VAL A 188 19.831 13.127 4.429 1.00 29.19 C -ANISOU 1347 CB VAL A 188 4084 3713 3294 -1291 555 1 C -ATOM 1348 CG1 VAL A 188 21.189 13.741 4.769 1.00 30.08 C -ANISOU 1348 CG1 VAL A 188 4107 3824 3496 -1550 552 3 C -ATOM 1349 CG2 VAL A 188 19.367 13.546 3.023 1.00 28.52 C -ANISOU 1349 CG2 VAL A 188 4114 3563 3160 -1217 660 130 C -ATOM 1350 N GLY A 189 17.582 11.318 5.340 1.00 27.04 N -ANISOU 1350 N GLY A 189 3814 3537 2923 -898 431 -115 N -ATOM 1351 CA GLY A 189 16.218 10.833 5.251 1.00 23.20 C -ANISOU 1351 CA GLY A 189 3366 3045 2404 -714 409 -109 C -ATOM 1352 C GLY A 189 15.965 9.611 6.109 1.00 23.91 C -ANISOU 1352 C GLY A 189 3351 3251 2483 -647 344 -176 C -ATOM 1353 O GLY A 189 16.911 8.978 6.607 1.00 26.16 O -ANISOU 1353 O GLY A 189 3528 3640 2770 -716 310 -220 O -ATOM 1354 N TYR A 190 14.687 9.283 6.288 1.00 23.12 N -ANISOU 1354 N TYR A 190 3271 3134 2378 -513 327 -171 N -ATOM 1355 CA TYR A 190 14.277 8.205 7.191 1.00 23.21 C -ANISOU 1355 CA TYR A 190 3207 3228 2384 -456 282 -217 C -ATOM 1356 C TYR A 190 14.968 8.355 8.551 1.00 25.77 C -ANISOU 1356 C TYR A 190 3549 3551 2691 -538 263 -300 C -ATOM 1357 O TYR A 190 15.516 7.390 9.094 1.00 24.90 O -ANISOU 1357 O TYR A 190 3354 3547 2562 -555 212 -330 O -ATOM 1358 CB TYR A 190 14.577 6.846 6.532 1.00 20.79 C -ANISOU 1358 CB TYR A 190 2792 3048 2061 -431 240 -199 C -ATOM 1359 CG TYR A 190 13.847 5.672 7.170 1.00 24.09 C -ANISOU 1359 CG TYR A 190 3153 3518 2482 -362 194 -213 C -ATOM 1360 CD1 TYR A 190 12.460 5.557 7.087 1.00 25.57 C -ANISOU 1360 CD1 TYR A 190 3339 3677 2701 -280 187 -172 C -ATOM 1361 CD2 TYR A 190 14.546 4.685 7.855 1.00 21.10 C -ANISOU 1361 CD2 TYR A 190 2713 3217 2087 -382 157 -251 C -ATOM 1362 CE1 TYR A 190 11.782 4.482 7.685 1.00 26.04 C -ANISOU 1362 CE1 TYR A 190 3335 3778 2779 -246 156 -166 C -ATOM 1363 CE2 TYR A 190 13.883 3.607 8.446 1.00 23.74 C -ANISOU 1363 CE2 TYR A 190 3018 3577 2424 -331 124 -246 C -ATOM 1364 CZ TYR A 190 12.504 3.511 8.360 1.00 26.20 C -ANISOU 1364 CZ TYR A 190 3328 3854 2772 -277 130 -203 C -ATOM 1365 OH TYR A 190 11.855 2.428 8.952 1.00 25.94 O -ANISOU 1365 OH TYR A 190 3256 3843 2758 -254 108 -182 O -ATOM 1366 N ALA A 191 14.927 9.586 9.080 1.00 25.25 N -ANISOU 1366 N ALA A 191 3618 3353 2623 -582 293 -337 N -ATOM 1367 CA ALA A 191 15.532 10.001 10.355 1.00 26.20 C -ANISOU 1367 CA ALA A 191 3815 3436 2703 -674 256 -432 C -ATOM 1368 C ALA A 191 17.036 10.290 10.313 1.00 26.44 C -ANISOU 1368 C ALA A 191 3794 3499 2753 -863 193 -457 C -ATOM 1369 O ALA A 191 17.565 10.863 11.253 1.00 28.80 O -ANISOU 1369 O ALA A 191 4178 3742 3022 -972 135 -537 O -ATOM 1370 CB ALA A 191 15.181 9.043 11.531 1.00 23.22 C -ANISOU 1370 CB ALA A 191 3414 3145 2263 -605 225 -475 C -ATOM 1371 N LEU A 192 17.716 9.917 9.228 1.00 28.65 N -ANISOU 1371 N LEU A 192 3936 3870 3080 -903 206 -387 N -ATOM 1372 CA LEU A 192 19.131 10.273 9.082 1.00 30.24 C -ANISOU 1372 CA LEU A 192 4048 4115 3329 -1085 174 -384 C -ATOM 1373 C LEU A 192 19.285 11.756 8.746 1.00 28.22 C -ANISOU 1373 C LEU A 192 3931 3679 3111 -1218 219 -369 C -ATOM 1374 O LEU A 192 18.588 12.282 7.878 1.00 28.14 O -ANISOU 1374 O LEU A 192 4021 3565 3105 -1150 305 -304 O -ATOM 1375 CB LEU A 192 19.821 9.407 8.020 1.00 30.48 C -ANISOU 1375 CB LEU A 192 3888 4304 3390 -1063 213 -306 C -ATOM 1376 CG LEU A 192 20.159 7.971 8.435 1.00 33.74 C -ANISOU 1376 CG LEU A 192 4151 4885 3784 -975 151 -325 C -ATOM 1377 CD1 LEU A 192 18.968 7.040 8.312 1.00 31.86 C -ANISOU 1377 CD1 LEU A 192 3962 4647 3496 -795 162 -320 C -ATOM 1378 CD2 LEU A 192 21.327 7.437 7.610 1.00 37.07 C -ANISOU 1378 CD2 LEU A 192 4378 5454 4252 -997 192 -267 C -ATOM 1379 N ASP A 193 20.200 12.443 9.416 1.00 27.87 N -ANISOU 1379 N ASP A 193 3905 3589 3096 -1416 146 -425 N -ATOM 1380 CA ASP A 193 20.266 13.883 9.259 1.00 29.67 C -ANISOU 1380 CA ASP A 193 4315 3598 3360 -1556 176 -424 C -ATOM 1381 C ASP A 193 21.532 14.400 8.586 1.00 37.88 C -ANISOU 1381 C ASP A 193 5234 4656 4500 -1791 192 -350 C -ATOM 1382 O ASP A 193 22.554 13.711 8.504 1.00 36.08 O -ANISOU 1382 O ASP A 193 4757 4630 4321 -1868 156 -321 O -ATOM 1383 CB ASP A 193 20.174 14.564 10.619 1.00 30.97 C -ANISOU 1383 CB ASP A 193 4677 3617 3474 -1632 78 -562 C -ATOM 1384 CG ASP A 193 21.463 14.454 11.398 1.00 32.45 C -ANISOU 1384 CG ASP A 193 4744 3904 3684 -1849 -78 -625 C -ATOM 1385 OD1 ASP A 193 21.968 13.326 11.547 1.00 37.53 O -ANISOU 1385 OD1 ASP A 193 5157 4776 4327 -1810 -137 -608 O -ATOM 1386 OD2 ASP A 193 21.966 15.495 11.844 1.00 35.67 O -ANISOU 1386 OD2 ASP A 193 5288 4152 4114 -2058 -153 -688 O -ATOM 1387 N TYR A 194 21.436 15.638 8.123 1.00 32.99 N -ANISOU 1387 N TYR A 194 4796 3820 3918 -1895 255 -308 N -ATOM 1388 CA TYR A 194 22.597 16.457 7.833 1.00 35.49 C -ANISOU 1388 CA TYR A 194 5063 4082 4340 -2183 254 -256 C -ATOM 1389 C TYR A 194 22.475 17.688 8.702 1.00 37.50 C -ANISOU 1389 C TYR A 194 5597 4057 4596 -2332 171 -362 C -ATOM 1390 O TYR A 194 21.656 18.574 8.433 1.00 39.52 O -ANISOU 1390 O TYR A 194 6122 4065 4828 -2261 247 -348 O -ATOM 1391 CB TYR A 194 22.627 16.839 6.365 1.00 35.95 C -ANISOU 1391 CB TYR A 194 5122 4103 4433 -2185 423 -88 C -ATOM 1392 CG TYR A 194 23.852 17.618 5.983 1.00 43.18 C -ANISOU 1392 CG TYR A 194 5954 4981 5471 -2496 455 -2 C -ATOM 1393 CD1 TYR A 194 25.099 17.008 5.948 1.00 47.77 C -ANISOU 1393 CD1 TYR A 194 6203 5808 6139 -2638 436 38 C -ATOM 1394 CD2 TYR A 194 23.765 18.954 5.649 1.00 52.49 C -ANISOU 1394 CD2 TYR A 194 7375 5877 6691 -2644 510 54 C -ATOM 1395 CE1 TYR A 194 26.227 17.711 5.589 1.00 54.96 C -ANISOU 1395 CE1 TYR A 194 6993 6705 7185 -2939 477 136 C -ATOM 1396 CE2 TYR A 194 24.887 19.675 5.293 1.00 57.72 C -ANISOU 1396 CE2 TYR A 194 7954 6495 7481 -2960 547 150 C -ATOM 1397 CZ TYR A 194 26.114 19.045 5.265 1.00 61.08 C -ANISOU 1397 CZ TYR A 194 8016 7190 8002 -3115 532 193 C -ATOM 1398 OH TYR A 194 27.235 19.748 4.905 1.00 72.43 O -ANISOU 1398 OH TYR A 194 9325 8608 9589 -3415 575 306 O -ATOM 1399 N ASN A 195 23.279 17.738 9.760 1.00 46.34 N -ANISOU 1399 N ASN A 195 6666 5208 5733 -2526 3 -471 N -ATOM 1400 CA ASN A 195 23.187 18.798 10.755 1.00 44.37 C -ANISOU 1400 CA ASN A 195 6716 4693 5451 -2667 -108 -611 C -ATOM 1401 C ASN A 195 21.750 19.094 11.220 1.00 40.11 C -ANISOU 1401 C ASN A 195 6500 3958 4781 -2402 -49 -701 C -ATOM 1402 O ASN A 195 21.299 20.246 11.225 1.00 41.75 O -ANISOU 1402 O ASN A 195 7018 3862 4985 -2425 -6 -731 O -ATOM 1403 CB ASN A 195 23.926 20.045 10.279 1.00 56.36 C -ANISOU 1403 CB ASN A 195 8322 5998 7094 -2979 -99 -551 C -ATOM 1404 CG ASN A 195 25.413 19.791 10.110 1.00 66.95 C -ANISOU 1404 CG ASN A 195 9316 7547 8576 -3271 -180 -480 C -ATOM 1405 OD1 ASN A 195 26.001 18.982 10.831 1.00 69.37 O -ANISOU 1405 OD1 ASN A 195 9397 8086 8873 -3287 -329 -542 O -ATOM 1406 ND2 ASN A 195 26.025 20.466 9.151 1.00 73.26 N -ANISOU 1406 ND2 ASN A 195 10041 8288 9509 -3428 -74 -328 N -ATOM 1407 N GLU A 196 21.065 18.011 11.592 1.00 37.65 N -ANISOU 1407 N GLU A 196 6101 3829 4376 -2149 -39 -730 N -ATOM 1408 CA GLU A 196 19.711 17.997 12.169 1.00 43.39 C -ANISOU 1408 CA GLU A 196 7046 4456 4983 -1875 24 -805 C -ATOM 1409 C GLU A 196 18.577 18.153 11.156 1.00 43.14 C -ANISOU 1409 C GLU A 196 7069 4350 4974 -1640 196 -690 C -ATOM 1410 O GLU A 196 17.414 17.906 11.485 1.00 40.74 O -ANISOU 1410 O GLU A 196 6847 4034 4600 -1387 263 -715 O -ATOM 1411 CB GLU A 196 19.564 18.969 13.350 1.00 39.03 C -ANISOU 1411 CB GLU A 196 6839 3650 4339 -1939 -49 -976 C -ATOM 1412 CG GLU A 196 20.406 18.591 14.568 1.00 43.83 C -ANISOU 1412 CG GLU A 196 7417 4369 4867 -2101 -250 -1110 C -ATOM 1413 CD GLU A 196 20.157 17.170 15.077 1.00 47.98 C -ANISOU 1413 CD GLU A 196 7744 5180 5305 -1919 -273 -1109 C -ATOM 1414 OE1 GLU A 196 19.007 16.677 15.022 1.00 42.37 O -ANISOU 1414 OE1 GLU A 196 7056 4505 4540 -1643 -136 -1077 O -ATOM 1415 OE2 GLU A 196 21.125 16.540 15.547 1.00 54.64 O -ANISOU 1415 OE2 GLU A 196 8405 6213 6143 -2058 -435 -1130 O -ATOM 1416 N TYR A 197 18.920 18.516 9.920 1.00 37.68 N -ANISOU 1416 N TYR A 197 6313 3627 4376 -1723 266 -551 N -ATOM 1417 CA TYR A 197 17.928 18.568 8.845 1.00 37.17 C -ANISOU 1417 CA TYR A 197 6276 3527 4319 -1504 397 -423 C -ATOM 1418 C TYR A 197 17.761 17.230 8.142 1.00 33.80 C -ANISOU 1418 C TYR A 197 5572 3387 3884 -1370 420 -336 C -ATOM 1419 O TYR A 197 18.627 16.360 8.244 1.00 31.51 O -ANISOU 1419 O TYR A 197 5059 3309 3605 -1470 362 -345 O -ATOM 1420 CB TYR A 197 18.284 19.643 7.824 1.00 43.64 C -ANISOU 1420 CB TYR A 197 7217 4154 5212 -1636 467 -303 C -ATOM 1421 CG TYR A 197 18.072 21.022 8.370 1.00 53.64 C -ANISOU 1421 CG TYR A 197 8828 5069 6482 -1695 466 -377 C -ATOM 1422 CD1 TYR A 197 16.813 21.604 8.353 1.00 55.73 C -ANISOU 1422 CD1 TYR A 197 9324 5137 6712 -1436 546 -371 C -ATOM 1423 CD2 TYR A 197 19.118 21.727 8.941 1.00 60.92 C -ANISOU 1423 CD2 TYR A 197 9846 5852 7448 -2006 377 -457 C -ATOM 1424 CE1 TYR A 197 16.605 22.859 8.870 1.00 62.99 C -ANISOU 1424 CE1 TYR A 197 10593 5711 7629 -1459 558 -448 C -ATOM 1425 CE2 TYR A 197 18.925 22.987 9.455 1.00 67.00 C -ANISOU 1425 CE2 TYR A 197 10976 6266 8213 -2067 367 -542 C -ATOM 1426 CZ TYR A 197 17.666 23.549 9.420 1.00 69.14 C -ANISOU 1426 CZ TYR A 197 11505 6328 8438 -1780 468 -541 C -ATOM 1427 OH TYR A 197 17.471 24.808 9.938 1.00 75.64 O -ANISOU 1427 OH TYR A 197 12719 6770 9249 -1813 470 -634 O -ATOM 1428 N PHE A 198 16.639 17.098 7.430 1.00 31.21 N -ANISOU 1428 N PHE A 198 5270 3052 3538 -1140 494 -252 N -ATOM 1429 CA PHE A 198 16.292 15.921 6.634 1.00 29.21 C -ANISOU 1429 CA PHE A 198 4810 3022 3264 -1004 507 -171 C -ATOM 1430 C PHE A 198 15.816 14.709 7.431 1.00 27.99 C -ANISOU 1430 C PHE A 198 4519 3044 3070 -881 455 -247 C -ATOM 1431 O PHE A 198 15.629 13.633 6.855 1.00 28.06 O -ANISOU 1431 O PHE A 198 4365 3230 3067 -797 446 -197 O -ATOM 1432 CB PHE A 198 17.433 15.511 5.699 1.00 29.22 C -ANISOU 1432 CB PHE A 198 4647 3168 3288 -1152 523 -89 C -ATOM 1433 CG PHE A 198 17.914 16.616 4.802 1.00 34.54 C -ANISOU 1433 CG PHE A 198 5441 3686 3996 -1283 599 19 C -ATOM 1434 CD1 PHE A 198 17.143 17.048 3.729 1.00 35.09 C -ANISOU 1434 CD1 PHE A 198 5634 3664 4035 -1146 666 143 C -ATOM 1435 CD2 PHE A 198 19.148 17.208 5.017 1.00 40.17 C -ANISOU 1435 CD2 PHE A 198 6138 4349 4776 -1552 596 12 C -ATOM 1436 CE1 PHE A 198 17.593 18.071 2.885 1.00 33.49 C -ANISOU 1436 CE1 PHE A 198 5567 3306 3852 -1266 748 265 C -ATOM 1437 CE2 PHE A 198 19.610 18.223 4.184 1.00 40.65 C -ANISOU 1437 CE2 PHE A 198 6309 4257 4878 -1697 682 132 C -ATOM 1438 CZ PHE A 198 18.829 18.655 3.117 1.00 41.88 C -ANISOU 1438 CZ PHE A 198 6617 4307 4987 -1548 767 262 C -ATOM 1439 N ARG A 199 15.616 14.857 8.740 1.00 28.06 N -ANISOU 1439 N ARG A 199 4616 2996 3048 -872 424 -365 N -ATOM 1440 CA ARG A 199 15.050 13.732 9.492 1.00 28.52 C -ANISOU 1440 CA ARG A 199 4567 3208 3060 -745 398 -411 C -ATOM 1441 C ARG A 199 13.576 13.518 9.148 1.00 35.23 C -ANISOU 1441 C ARG A 199 5408 4057 3920 -513 462 -346 C -ATOM 1442 O ARG A 199 13.079 12.381 9.154 1.00 34.38 O -ANISOU 1442 O ARG A 199 5147 4108 3808 -423 445 -321 O -ATOM 1443 CB ARG A 199 15.233 13.916 11.000 1.00 27.19 C -ANISOU 1443 CB ARG A 199 4514 2992 2823 -789 357 -546 C -ATOM 1444 CG ARG A 199 16.699 14.002 11.461 1.00 28.33 C -ANISOU 1444 CG ARG A 199 4630 3171 2963 -1031 245 -614 C -ATOM 1445 CD ARG A 199 16.819 13.709 12.968 1.00 29.79 C -ANISOU 1445 CD ARG A 199 4890 3387 3042 -1042 165 -739 C -ATOM 1446 NE ARG A 199 18.091 14.125 13.563 1.00 32.29 N -ANISOU 1446 NE ARG A 199 5237 3686 3346 -1281 27 -822 N -ATOM 1447 CZ ARG A 199 19.192 13.373 13.635 1.00 30.18 C -ANISOU 1447 CZ ARG A 199 4755 3608 3105 -1406 -90 -809 C -ATOM 1448 NH1 ARG A 199 19.206 12.143 13.128 1.00 28.33 N -ANISOU 1448 NH1 ARG A 199 4289 3575 2900 -1304 -71 -724 N -ATOM 1449 NH2 ARG A 199 20.287 13.871 14.209 1.00 32.20 N -ANISOU 1449 NH2 ARG A 199 5030 3842 3362 -1633 -235 -881 N -ATOM 1450 N ASP A 200 12.901 14.620 8.823 1.00 29.39 N -ANISOU 1450 N ASP A 200 4829 3134 3206 -423 527 -308 N -ATOM 1451 CA ASP A 200 11.468 14.645 8.540 1.00 29.16 C -ANISOU 1451 CA ASP A 200 4785 3091 3206 -191 582 -236 C -ATOM 1452 C ASP A 200 11.229 14.365 7.067 1.00 31.15 C -ANISOU 1452 C ASP A 200 4933 3412 3491 -152 551 -103 C -ATOM 1453 O ASP A 200 10.627 15.165 6.352 1.00 37.29 O -ANISOU 1453 O ASP A 200 5801 4071 4295 -46 578 -15 O -ATOM 1454 CB ASP A 200 10.881 16.024 8.902 1.00 31.52 C -ANISOU 1454 CB ASP A 200 5320 3142 3512 -81 666 -256 C -ATOM 1455 CG ASP A 200 11.604 17.172 8.210 1.00 35.96 C -ANISOU 1455 CG ASP A 200 6064 3507 4093 -206 666 -223 C -ATOM 1456 OD1 ASP A 200 12.811 17.033 7.911 1.00 33.25 O -ANISOU 1456 OD1 ASP A 200 5681 3208 3746 -431 613 -231 O -ATOM 1457 OD2 ASP A 200 10.960 18.213 7.961 1.00 38.62 O -ANISOU 1457 OD2 ASP A 200 6575 3641 4457 -75 728 -177 O -ATOM 1458 N LEU A 201 11.724 13.217 6.631 1.00 29.67 N -ANISOU 1458 N LEU A 201 4578 3410 3287 -227 489 -90 N -ATOM 1459 CA LEU A 201 11.702 12.789 5.238 1.00 28.76 C -ANISOU 1459 CA LEU A 201 4390 3377 3162 -213 449 12 C -ATOM 1460 C LEU A 201 11.626 11.270 5.280 1.00 26.56 C -ANISOU 1460 C LEU A 201 3929 3292 2869 -206 385 -10 C -ATOM 1461 O LEU A 201 12.407 10.640 5.993 1.00 27.52 O -ANISOU 1461 O LEU A 201 3991 3489 2975 -300 374 -87 O -ATOM 1462 CB LEU A 201 12.988 13.246 4.547 1.00 32.38 C -ANISOU 1462 CB LEU A 201 4908 3800 3593 -379 471 37 C -ATOM 1463 CG LEU A 201 13.338 12.771 3.134 1.00 32.66 C -ANISOU 1463 CG LEU A 201 4898 3934 3578 -392 460 128 C -ATOM 1464 CD1 LEU A 201 12.336 13.291 2.122 1.00 33.85 C -ANISOU 1464 CD1 LEU A 201 5141 4014 3707 -250 444 244 C -ATOM 1465 CD2 LEU A 201 14.764 13.221 2.761 1.00 28.81 C -ANISOU 1465 CD2 LEU A 201 4437 3430 3080 -579 524 146 C -ATOM 1466 N ASN A 202 10.685 10.682 4.538 1.00 30.34 N -ANISOU 1466 N ASN A 202 4330 3842 3356 -98 328 59 N -ATOM 1467 CA AASN A 202 10.434 9.236 4.569 0.58 31.00 C -ANISOU 1467 CA AASN A 202 4269 4074 3438 -94 256 41 C -ATOM 1468 CA BASN A 202 10.467 9.234 4.606 0.42 30.36 C -ANISOU 1468 CA BASN A 202 4188 3992 3356 -97 258 37 C -ATOM 1469 C ASN A 202 11.419 8.409 3.732 1.00 28.06 C -ANISOU 1469 C ASN A 202 3874 3791 2997 -176 219 30 C -ATOM 1470 O ASN A 202 11.682 7.250 4.032 1.00 29.29 O -ANISOU 1470 O ASN A 202 3946 4038 3145 -202 182 -18 O -ATOM 1471 CB AASN A 202 9.012 8.947 4.074 0.58 33.61 C -ANISOU 1471 CB AASN A 202 4520 4437 3814 30 185 118 C -ATOM 1472 CB BASN A 202 8.995 8.857 4.330 0.42 33.20 C -ANISOU 1472 CB BASN A 202 4454 4391 3771 27 193 105 C -ATOM 1473 CG AASN A 202 8.089 8.456 5.173 0.58 38.22 C -ANISOU 1473 CG AASN A 202 4985 5062 4474 86 203 104 C -ATOM 1474 CG BASN A 202 8.554 9.166 2.898 0.42 34.37 C -ANISOU 1474 CG BASN A 202 4642 4528 3889 86 116 200 C -ATOM 1475 OD1AASN A 202 8.435 8.477 6.362 0.58 36.32 O -ANISOU 1475 OD1AASN A 202 4763 4807 4230 57 281 35 O -ATOM 1476 OD1BASN A 202 9.159 9.994 2.218 0.42 38.68 O -ANISOU 1476 OD1BASN A 202 5319 5000 4378 66 151 233 O -ATOM 1477 ND2AASN A 202 6.896 8.008 4.777 0.58 42.53 N -ANISOU 1477 ND2AASN A 202 5407 5667 5086 161 127 178 N -ATOM 1478 ND2BASN A 202 7.484 8.506 2.442 0.42 27.81 N -ANISOU 1478 ND2BASN A 202 3701 3771 3093 150 3 253 N -ATOM 1479 N HIS A 203 11.943 9.008 2.668 1.00 24.12 N -ANISOU 1479 N HIS A 203 3464 3257 2443 -200 242 83 N -ATOM 1480 CA HIS A 203 12.860 8.306 1.758 1.00 23.55 C -ANISOU 1480 CA HIS A 203 3387 3273 2290 -248 243 82 C -ATOM 1481 C HIS A 203 14.308 8.534 2.193 1.00 28.48 C -ANISOU 1481 C HIS A 203 3986 3913 2921 -373 330 42 C -ATOM 1482 O HIS A 203 14.613 9.552 2.800 1.00 29.88 O -ANISOU 1482 O HIS A 203 4208 4000 3146 -444 379 36 O -ATOM 1483 CB HIS A 203 12.722 8.843 0.328 1.00 24.44 C -ANISOU 1483 CB HIS A 203 3617 3353 2315 -209 245 178 C -ATOM 1484 CG HIS A 203 11.322 8.838 -0.202 1.00 26.39 C -ANISOU 1484 CG HIS A 203 3886 3584 2557 -91 132 238 C -ATOM 1485 ND1 HIS A 203 10.617 7.678 -0.444 1.00 27.62 N -ANISOU 1485 ND1 HIS A 203 3972 3823 2698 -47 7 214 N -ATOM 1486 CD2 HIS A 203 10.498 9.859 -0.551 1.00 27.39 C -ANISOU 1486 CD2 HIS A 203 4089 3619 2700 -8 111 330 C -ATOM 1487 CE1 HIS A 203 9.424 7.984 -0.923 1.00 30.69 C -ANISOU 1487 CE1 HIS A 203 4368 4192 3102 43 -98 289 C -ATOM 1488 NE2 HIS A 203 9.324 9.299 -0.988 1.00 27.96 N -ANISOU 1488 NE2 HIS A 203 4104 3745 2773 86 -34 364 N -ATOM 1489 N VAL A 204 15.206 7.608 1.861 1.00 26.81 N -ANISOU 1489 N VAL A 204 3706 3812 2667 -397 346 15 N -ATOM 1490 CA VAL A 204 16.634 7.890 1.992 1.00 27.41 C -ANISOU 1490 CA VAL A 204 3724 3930 2761 -510 432 10 C -ATOM 1491 C VAL A 204 17.092 8.532 0.690 1.00 30.83 C -ANISOU 1491 C VAL A 204 4240 4349 3127 -534 530 104 C -ATOM 1492 O VAL A 204 16.791 8.030 -0.393 1.00 30.05 O -ANISOU 1492 O VAL A 204 4206 4288 2925 -443 529 138 O -ATOM 1493 CB VAL A 204 17.467 6.635 2.335 1.00 25.15 C -ANISOU 1493 CB VAL A 204 3302 3777 2475 -500 422 -50 C -ATOM 1494 CG1 VAL A 204 18.972 6.909 2.149 1.00 27.71 C -ANISOU 1494 CG1 VAL A 204 3526 4178 2824 -600 521 -24 C -ATOM 1495 CG2 VAL A 204 17.195 6.202 3.763 1.00 24.36 C -ANISOU 1495 CG2 VAL A 204 3140 3679 2435 -503 339 -123 C -ATOM 1496 N CYS A 205 17.794 9.659 0.793 1.00 27.55 N -ANISOU 1496 N CYS A 205 3842 3866 2759 -665 610 148 N -ATOM 1497 CA CYS A 205 18.139 10.426 -0.389 1.00 29.68 C -ANISOU 1497 CA CYS A 205 4214 4095 2968 -702 720 264 C -ATOM 1498 C CYS A 205 19.585 10.902 -0.354 1.00 29.44 C -ANISOU 1498 C CYS A 205 4082 4105 3000 -877 840 303 C -ATOM 1499 O CYS A 205 20.216 10.966 0.703 1.00 28.21 O -ANISOU 1499 O CYS A 205 3800 3968 2951 -993 805 239 O -ATOM 1500 CB CYS A 205 17.191 11.613 -0.551 1.00 30.02 C -ANISOU 1500 CB CYS A 205 4439 3955 3014 -681 699 329 C -ATOM 1501 N VAL A 206 20.102 11.237 -1.519 1.00 29.13 N -ANISOU 1501 N VAL A 206 4095 4085 2889 -901 978 417 N -ATOM 1502 CA VAL A 206 21.401 11.882 -1.609 1.00 32.67 C -ANISOU 1502 CA VAL A 206 4442 4558 3413 -1093 1114 493 C -ATOM 1503 C VAL A 206 21.166 13.389 -1.682 1.00 37.50 C -ANISOU 1503 C VAL A 206 5230 4953 4065 -1223 1141 580 C -ATOM 1504 O VAL A 206 20.229 13.859 -2.334 1.00 41.21 O -ANISOU 1504 O VAL A 206 5913 5300 4444 -1121 1131 645 O -ATOM 1505 CB VAL A 206 22.219 11.369 -2.821 1.00 41.24 C -ANISOU 1505 CB VAL A 206 5472 5799 4397 -1048 1295 584 C -ATOM 1506 CG1 VAL A 206 23.452 12.220 -3.042 1.00 46.05 C -ANISOU 1506 CG1 VAL A 206 5976 6424 5098 -1264 1464 703 C -ATOM 1507 CG2 VAL A 206 22.636 9.925 -2.601 1.00 41.62 C -ANISOU 1507 CG2 VAL A 206 5341 6038 4433 -926 1278 488 C -ATOM 1508 N ILE A 207 22.017 14.143 -1.002 1.00 40.04 N -ANISOU 1508 N ILE A 207 5469 5218 4527 -1449 1159 583 N -ATOM 1509 CA ILE A 207 21.818 15.573 -0.833 1.00 42.59 C -ANISOU 1509 CA ILE A 207 5981 5291 4910 -1592 1161 637 C -ATOM 1510 C ILE A 207 22.460 16.352 -1.972 1.00 52.15 C -ANISOU 1510 C ILE A 207 7263 6453 6099 -1717 1347 824 C -ATOM 1511 O ILE A 207 23.563 16.024 -2.406 1.00 57.74 O -ANISOU 1511 O ILE A 207 7779 7330 6831 -1817 1479 893 O -ATOM 1512 CB ILE A 207 22.345 15.996 0.565 1.00 70.88 C -ANISOU 1512 CB ILE A 207 9478 8809 8645 -1792 1052 524 C -ATOM 1513 CG1 ILE A 207 22.405 17.512 0.737 1.00 73.04 C -ANISOU 1513 CG1 ILE A 207 9955 8802 8994 -1990 1065 574 C -ATOM 1514 CG2 ILE A 207 23.698 15.353 0.846 1.00 70.08 C -ANISOU 1514 CG2 ILE A 207 9063 8932 8631 -1932 1074 511 C -ATOM 1515 CD1 ILE A 207 22.622 17.916 2.195 1.00 72.83 C -ANISOU 1515 CD1 ILE A 207 9929 8672 9072 -2146 914 423 C -ATOM 1516 N SER A 208 21.763 17.366 -2.480 1.00 53.98 N -ANISOU 1516 N SER A 208 7768 6458 6282 -1696 1370 921 N -ATOM 1517 CA SER A 208 22.286 18.149 -3.593 1.00 56.09 C -ANISOU 1517 CA SER A 208 8147 6655 6508 -1808 1554 1123 C -ATOM 1518 C SER A 208 23.466 18.999 -3.139 1.00 61.53 C -ANISOU 1518 C SER A 208 8740 7262 7376 -2147 1624 1170 C -ATOM 1519 O SER A 208 23.766 19.077 -1.942 1.00 62.26 O -ANISOU 1519 O SER A 208 8720 7326 7611 -2285 1495 1034 O -ATOM 1520 CB SER A 208 21.206 19.034 -4.224 1.00 56.07 C -ANISOU 1520 CB SER A 208 8483 6413 6407 -1683 1543 1228 C -ATOM 1521 OG SER A 208 20.877 20.135 -3.399 1.00 59.74 O -ANISOU 1521 OG SER A 208 9109 6597 6995 -1784 1462 1191 O -ATOM 1522 N GLU A 209 24.141 19.624 -4.097 1.00 59.98 N -ANISOU 1522 N GLU A 209 8590 7031 7168 -2293 1821 1369 N -ATOM 1523 CA GLU A 209 25.239 20.519 -3.768 1.00 67.32 C -ANISOU 1523 CA GLU A 209 9403 7877 8299 -2597 1854 1427 C -ATOM 1524 C GLU A 209 24.720 21.734 -3.015 1.00 69.00 C -ANISOU 1524 C GLU A 209 9873 7737 8604 -2713 1719 1375 C -ATOM 1525 O GLU A 209 25.397 22.252 -2.125 1.00 73.77 O -ANISOU 1525 O GLU A 209 10377 8262 9388 -2946 1623 1300 O -ATOM 1526 CB GLU A 209 26.008 20.947 -5.026 1.00 77.33 C -ANISOU 1526 CB GLU A 209 10626 9199 9555 -2630 2054 1652 C -ATOM 1527 CG GLU A 209 26.824 19.827 -5.654 1.00 83.61 C -ANISOU 1527 CG GLU A 209 11126 10343 10298 -2539 2207 1699 C -ATOM 1528 CD GLU A 209 27.611 19.033 -4.620 1.00 88.42 C -ANISOU 1528 CD GLU A 209 11378 11152 11065 -2635 2130 1555 C -ATOM 1529 OE1 GLU A 209 27.541 17.785 -4.644 1.00 87.67 O -ANISOU 1529 OE1 GLU A 209 11149 11291 10872 -2456 2146 1470 O -ATOM 1530 OE2 GLU A 209 28.298 19.656 -3.780 1.00 92.35 O -ANISOU 1530 OE2 GLU A 209 11737 11569 11782 -2882 2037 1524 O -ATOM 1531 N THR A 210 23.513 22.175 -3.363 1.00 65.96 N -ANISOU 1531 N THR A 210 9826 7142 8094 -2528 1699 1409 N -ATOM 1532 CA THR A 210 22.930 23.365 -2.751 1.00 68.66 C -ANISOU 1532 CA THR A 210 10452 7126 8509 -2573 1593 1366 C -ATOM 1533 C THR A 210 22.465 23.095 -1.314 1.00 66.57 C -ANISOU 1533 C THR A 210 10187 6807 8298 -2561 1412 1130 C -ATOM 1534 O THR A 210 22.565 23.970 -0.455 1.00 70.49 O -ANISOU 1534 O THR A 210 10819 7058 8904 -2721 1322 1044 O -ATOM 1535 CB THR A 210 21.778 23.967 -3.612 1.00 79.80 C -ANISOU 1535 CB THR A 210 12205 8336 9782 -2329 1622 1494 C -ATOM 1536 OG1 THR A 210 21.760 25.393 -3.470 1.00 84.73 O -ANISOU 1536 OG1 THR A 210 13057 8629 10508 -2429 1596 1540 O -ATOM 1537 CG2 THR A 210 20.420 23.404 -3.211 1.00 74.21 C -ANISOU 1537 CG2 THR A 210 11597 7626 8975 -2025 1496 1374 C -ATOM 1538 N GLY A 211 21.987 21.879 -1.055 1.00 57.27 N -ANISOU 1538 N GLY A 211 8833 5883 7043 -2326 1332 1009 N -ATOM 1539 CA GLY A 211 21.515 21.515 0.268 1.00 53.08 C -ANISOU 1539 CA GLY A 211 8266 5355 6547 -2249 1158 788 C -ATOM 1540 C GLY A 211 22.683 21.246 1.197 1.00 57.04 C -ANISOU 1540 C GLY A 211 8522 5978 7172 -2515 1087 680 C -ATOM 1541 O GLY A 211 22.605 21.514 2.394 1.00 58.67 O -ANISOU 1541 O GLY A 211 8789 6073 7431 -2586 946 519 O -ATOM 1542 N LYS A 212 23.769 20.713 0.640 1.00 57.66 N -ANISOU 1542 N LYS A 212 8325 6296 7289 -2649 1184 774 N -ATOM 1543 CA LYS A 212 24.980 20.439 1.412 1.00 59.20 C -ANISOU 1543 CA LYS A 212 8232 6642 7620 -2903 1113 704 C -ATOM 1544 C LYS A 212 25.609 21.729 1.929 1.00 59.82 C -ANISOU 1544 C LYS A 212 8418 6467 7845 -3230 1053 704 C -ATOM 1545 O LYS A 212 25.969 21.829 3.103 1.00 59.30 O -ANISOU 1545 O LYS A 212 8296 6377 7857 -3361 869 548 O -ATOM 1546 CB LYS A 212 25.996 19.643 0.582 1.00 64.27 C -ANISOU 1546 CB LYS A 212 8541 7597 8281 -2940 1265 832 C -ATOM 1547 CG LYS A 212 25.967 18.142 0.841 1.00 67.10 C -ANISOU 1547 CG LYS A 212 8653 8264 8578 -2712 1211 730 C -ATOM 1548 CD LYS A 212 27.154 17.426 0.211 1.00 72.34 C -ANISOU 1548 CD LYS A 212 8971 9224 9291 -2764 1360 838 C -ATOM 1549 CE LYS A 212 26.898 17.073 -1.244 1.00 74.01 C -ANISOU 1549 CE LYS A 212 9253 9517 9349 -2567 1581 983 C -ATOM 1550 NZ LYS A 212 28.099 16.462 -1.882 1.00 77.00 N -ANISOU 1550 NZ LYS A 212 9312 10173 9773 -2599 1766 1094 N -ATOM 1551 N ALA A 213 25.734 22.714 1.047 1.00 62.71 N -ANISOU 1551 N ALA A 213 8927 6657 8243 -3282 1172 868 N -ATOM 1552 CA ALA A 213 26.310 24.006 1.412 1.00 63.81 C -ANISOU 1552 CA ALA A 213 9163 6548 8532 -3517 1101 873 C -ATOM 1553 C ALA A 213 25.364 24.796 2.315 1.00 68.60 C -ANISOU 1553 C ALA A 213 10144 6821 9101 -3471 960 715 C -ATOM 1554 O ALA A 213 25.805 25.570 3.167 1.00 73.58 O -ANISOU 1554 O ALA A 213 10838 7284 9835 -3655 820 612 O -ATOM 1555 CB ALA A 213 26.656 24.813 0.161 1.00 63.70 C -ANISOU 1555 CB ALA A 213 9209 6437 8557 -3572 1284 1110 C -ATOM 1556 N LYS A 214 24.064 24.596 2.121 1.00 67.16 N -ANISOU 1556 N LYS A 214 10209 6542 8768 -3205 1001 698 N -ATOM 1557 CA LYS A 214 23.046 25.341 2.860 1.00 74.94 C -ANISOU 1557 CA LYS A 214 11560 7204 9708 -3086 911 569 C -ATOM 1558 C LYS A 214 22.935 24.899 4.325 1.00 78.07 C -ANISOU 1558 C LYS A 214 11938 7635 10092 -3098 733 321 C -ATOM 1559 O LYS A 214 22.488 25.667 5.181 1.00 77.91 O -ANISOU 1559 O LYS A 214 12187 7356 10061 -3069 637 182 O -ATOM 1560 CB LYS A 214 21.679 25.198 2.178 1.00 74.44 C -ANISOU 1560 CB LYS A 214 11727 7050 9506 -2762 1012 648 C -ATOM 1561 CG LYS A 214 20.762 26.401 2.343 1.00 77.99 C -ANISOU 1561 CG LYS A 214 12569 7120 9943 -2614 996 632 C -ATOM 1562 CD LYS A 214 19.284 26.019 2.221 1.00 73.45 C -ANISOU 1562 CD LYS A 214 12133 6525 9248 -2220 1014 625 C -ATOM 1563 CE LYS A 214 18.904 25.620 0.804 1.00 68.91 C -ANISOU 1563 CE LYS A 214 11491 6104 8586 -2033 1121 837 C -ATOM 1564 NZ LYS A 214 17.460 25.255 0.687 1.00 61.68 N -ANISOU 1564 NZ LYS A 214 10628 5230 7577 -1626 1086 826 N -ATOM 1565 N TYR A 215 23.346 23.665 4.610 1.00 78.81 N -ANISOU 1565 N TYR A 215 11723 8052 10171 -3122 693 268 N -ATOM 1566 CA TYR A 215 23.140 23.089 5.935 1.00 79.54 C -ANISOU 1566 CA TYR A 215 11774 8232 10216 -3049 521 48 C -ATOM 1567 C TYR A 215 24.413 22.600 6.644 1.00 81.66 C -ANISOU 1567 C TYR A 215 11732 8726 10570 -3306 378 -25 C -ATOM 1568 O TYR A 215 24.321 22.006 7.719 1.00 78.74 O -ANISOU 1568 O TYR A 215 11317 8457 10142 -3259 230 -192 O -ATOM 1569 CB TYR A 215 22.120 21.941 5.872 1.00 78.90 C -ANISOU 1569 CB TYR A 215 11597 8371 10011 -2662 547 17 C -ATOM 1570 CG TYR A 215 20.731 22.308 5.377 1.00 79.68 C -ANISOU 1570 CG TYR A 215 11954 8294 10026 -2356 638 66 C -ATOM 1571 CD1 TYR A 215 19.922 23.187 6.090 1.00 82.47 C -ANISOU 1571 CD1 TYR A 215 12641 8342 10350 -2263 606 -39 C -ATOM 1572 CD2 TYR A 215 20.219 21.746 4.214 1.00 76.75 C -ANISOU 1572 CD2 TYR A 215 11490 8070 9600 -2144 748 214 C -ATOM 1573 CE1 TYR A 215 18.648 23.508 5.645 1.00 80.57 C -ANISOU 1573 CE1 TYR A 215 12597 7962 10053 -1958 687 21 C -ATOM 1574 CE2 TYR A 215 18.953 22.063 3.760 1.00 75.26 C -ANISOU 1574 CE2 TYR A 215 11505 7744 9345 -1865 799 269 C -ATOM 1575 CZ TYR A 215 18.171 22.941 4.479 1.00 76.09 C -ANISOU 1575 CZ TYR A 215 11901 7563 9448 -1767 771 181 C -ATOM 1576 OH TYR A 215 16.910 23.249 4.026 1.00 74.45 O -ANISOU 1576 OH TYR A 215 11858 7237 9193 -1467 821 251 O -ATOM 1577 N LYS A 216 25.589 22.828 6.059 1.00 87.18 N -ANISOU 1577 N LYS A 216 12185 9533 11406 -3506 413 109 N -ATOM 1578 CA LYS A 216 26.839 22.416 6.713 1.00 90.63 C -ANISOU 1578 CA LYS A 216 12282 10201 11952 -3689 264 60 C -ATOM 1579 C LYS A 216 27.074 23.162 8.024 1.00 91.29 C -ANISOU 1579 C LYS A 216 12524 10103 12057 -3822 36 -121 C -ATOM 1580 O LYS A 216 27.251 24.378 8.032 1.00 93.74 O -ANISOU 1580 O LYS A 216 13033 10146 12440 -3964 19 -112 O -ATOM 1581 CB LYS A 216 28.059 22.592 5.801 1.00 96.07 C -ANISOU 1581 CB LYS A 216 12669 11023 12809 -3865 372 252 C -ATOM 1582 CG LYS A 216 29.382 22.317 6.514 1.00 99.39 C -ANISOU 1582 CG LYS A 216 12739 11646 13378 -4051 206 209 C -ATOM 1583 CD LYS A 216 30.558 22.275 5.549 1.00102.24 C -ANISOU 1583 CD LYS A 216 12747 12185 13914 -4175 357 411 C -ATOM 1584 CE LYS A 216 30.464 21.088 4.597 1.00 99.28 C -ANISOU 1584 CE LYS A 216 12154 12101 13468 -3962 557 530 C -ATOM 1585 NZ LYS A 216 31.698 20.931 3.772 1.00101.80 N -ANISOU 1585 NZ LYS A 216 12102 12623 13953 -4047 715 712 N -TER 1586 LYS A 216 -ATOM 1587 N SER B 4 4.774 12.235 -18.959 1.00 73.09 N -ANISOU 1587 N SER B 4 9298 8729 9745 -849 92 2826 N -ATOM 1588 CA SER B 4 5.720 11.466 -18.152 1.00 70.21 C -ANISOU 1588 CA SER B 4 8940 8481 9258 -874 219 2478 C -ATOM 1589 C SER B 4 5.600 9.958 -18.381 1.00 63.04 C -ANISOU 1589 C SER B 4 7957 7913 8081 -816 236 2287 C -ATOM 1590 O SER B 4 4.499 9.398 -18.341 1.00 61.71 O -ANISOU 1590 O SER B 4 7751 7750 7944 -665 181 2266 O -ATOM 1591 CB SER B 4 5.551 11.789 -16.668 1.00 70.21 C -ANISOU 1591 CB SER B 4 9010 8142 9526 -740 293 2246 C -ATOM 1592 OG SER B 4 6.314 10.905 -15.865 1.00 70.46 O -ANISOU 1592 OG SER B 4 9033 8310 9427 -749 384 1929 O -ATOM 1593 N PRO B 5 6.747 9.294 -18.612 1.00 57.72 N -ANISOU 1593 N PRO B 5 7254 7516 7161 -937 314 2148 N -ATOM 1594 CA PRO B 5 6.781 7.858 -18.901 1.00 54.58 C -ANISOU 1594 CA PRO B 5 6802 7423 6511 -891 340 1952 C -ATOM 1595 C PRO B 5 6.747 7.024 -17.629 1.00 47.99 C -ANISOU 1595 C PRO B 5 5964 6506 5766 -742 402 1634 C -ATOM 1596 O PRO B 5 6.649 5.796 -17.709 1.00 50.63 O -ANISOU 1596 O PRO B 5 6264 7027 5948 -678 413 1461 O -ATOM 1597 CB PRO B 5 8.121 7.677 -19.626 1.00 58.54 C -ANISOU 1597 CB PRO B 5 7264 8216 6761 -1070 426 1950 C -ATOM 1598 CG PRO B 5 8.966 8.880 -19.237 1.00 58.45 C -ANISOU 1598 CG PRO B 5 7272 8024 6912 -1205 461 2060 C -ATOM 1599 CD PRO B 5 8.101 9.861 -18.487 1.00 57.34 C -ANISOU 1599 CD PRO B 5 7213 7476 7097 -1115 389 2147 C -ATOM 1600 N GLY B 6 6.809 7.675 -16.469 1.00 35.78 N -ANISOU 1600 N GLY B 6 4465 4675 4456 -697 435 1559 N -ATOM 1601 CA GLY B 6 6.798 6.945 -15.213 1.00 29.93 C -ANISOU 1601 CA GLY B 6 3731 3866 3776 -578 489 1280 C -ATOM 1602 C GLY B 6 8.204 6.578 -14.776 1.00 29.30 C -ANISOU 1602 C GLY B 6 3623 3911 3601 -674 560 1111 C -ATOM 1603 O GLY B 6 9.180 7.070 -15.339 1.00 30.66 O -ANISOU 1603 O GLY B 6 3767 4183 3701 -834 583 1212 O -ATOM 1604 N VAL B 7 8.310 5.720 -13.762 1.00 27.81 N -ANISOU 1604 N VAL B 7 3427 3722 3418 -582 591 877 N -ATOM 1605 CA VAL B 7 9.614 5.255 -13.301 1.00 28.52 C -ANISOU 1605 CA VAL B 7 3461 3942 3434 -653 637 728 C -ATOM 1606 C VAL B 7 10.172 4.301 -14.344 1.00 27.97 C -ANISOU 1606 C VAL B 7 3290 4186 3153 -670 669 714 C -ATOM 1607 O VAL B 7 9.600 3.239 -14.586 1.00 28.08 O -ANISOU 1607 O VAL B 7 3290 4296 3082 -557 657 625 O -ATOM 1608 CB VAL B 7 9.516 4.501 -11.979 1.00 29.40 C -ANISOU 1608 CB VAL B 7 3591 3984 3596 -547 641 511 C -ATOM 1609 CG1 VAL B 7 10.882 3.930 -11.597 1.00 29.24 C -ANISOU 1609 CG1 VAL B 7 3481 4123 3505 -613 664 391 C -ATOM 1610 CG2 VAL B 7 8.995 5.423 -10.871 1.00 32.18 C -ANISOU 1610 CG2 VAL B 7 4063 4040 4126 -530 639 482 C -ATOM 1611 N VAL B 8 11.296 4.667 -14.943 1.00 29.40 N -ANISOU 1611 N VAL B 8 3398 4523 3250 -816 719 791 N -ATOM 1612 CA VAL B 8 11.890 3.824 -15.973 1.00 37.66 C -ANISOU 1612 CA VAL B 8 4346 5880 4082 -828 788 761 C -ATOM 1613 C VAL B 8 12.774 2.725 -15.364 1.00 38.07 C -ANISOU 1613 C VAL B 8 4295 6050 4118 -751 844 541 C -ATOM 1614 O VAL B 8 13.825 2.993 -14.788 1.00 37.29 O -ANISOU 1614 O VAL B 8 4112 5968 4089 -828 869 521 O -ATOM 1615 CB VAL B 8 12.644 4.669 -17.021 1.00 38.87 C -ANISOU 1615 CB VAL B 8 4448 6190 4131 -1018 841 966 C -ATOM 1616 CG1 VAL B 8 13.337 3.785 -18.064 1.00 36.46 C -ANISOU 1616 CG1 VAL B 8 4039 6234 3579 -1025 954 905 C -ATOM 1617 CG2 VAL B 8 11.674 5.623 -17.710 1.00 43.32 C -ANISOU 1617 CG2 VAL B 8 5114 6637 4708 -1076 762 1211 C -ATOM 1618 N ILE B 9 12.314 1.484 -15.476 1.00 31.22 N -ANISOU 1618 N ILE B 9 3432 5250 3178 -604 845 389 N -ATOM 1619 CA ILE B 9 13.104 0.329 -15.072 1.00 31.59 C -ANISOU 1619 CA ILE B 9 3379 5405 3219 -507 895 197 C -ATOM 1620 C ILE B 9 13.837 -0.184 -16.303 1.00 35.38 C -ANISOU 1620 C ILE B 9 3765 6169 3508 -521 1017 166 C -ATOM 1621 O ILE B 9 13.209 -0.640 -17.268 1.00 37.29 O -ANISOU 1621 O ILE B 9 4074 6504 3589 -492 1029 146 O -ATOM 1622 CB ILE B 9 12.211 -0.764 -14.469 1.00 34.12 C -ANISOU 1622 CB ILE B 9 3767 5610 3587 -344 828 48 C -ATOM 1623 CG1 ILE B 9 11.561 -0.260 -13.185 1.00 38.68 C -ANISOU 1623 CG1 ILE B 9 4426 5939 4332 -332 742 67 C -ATOM 1624 CG2 ILE B 9 13.006 -2.020 -14.183 1.00 35.95 C -ANISOU 1624 CG2 ILE B 9 3900 5934 3824 -232 872 -131 C -ATOM 1625 CD1 ILE B 9 10.686 -1.279 -12.529 1.00 40.40 C -ANISOU 1625 CD1 ILE B 9 4697 6055 4597 -196 684 -48 C -ATOM 1626 N SER B 10 15.162 -0.080 -16.290 1.00 35.08 N -ANISOU 1626 N SER B 10 3569 6282 3480 -576 1112 165 N -ATOM 1627 CA SER B 10 15.942 -0.352 -17.500 1.00 41.28 C -ANISOU 1627 CA SER B 10 4246 7362 4075 -608 1269 157 C -ATOM 1628 C SER B 10 15.867 -1.817 -17.902 1.00 41.46 C -ANISOU 1628 C SER B 10 4268 7481 4005 -425 1338 -74 C -ATOM 1629 O SER B 10 15.547 -2.686 -17.080 1.00 37.27 O -ANISOU 1629 O SER B 10 3765 6795 3600 -276 1266 -220 O -ATOM 1630 CB SER B 10 17.401 0.062 -17.329 1.00 48.32 C -ANISOU 1630 CB SER B 10 4927 8404 5028 -703 1364 217 C -ATOM 1631 OG SER B 10 18.055 -0.764 -16.394 1.00 53.73 O -ANISOU 1631 OG SER B 10 5486 9062 5866 -571 1358 68 O -ATOM 1632 N ASP B 11 16.150 -2.078 -19.173 1.00 40.47 N -ANISOU 1632 N ASP B 11 4162 7512 3703 -429 1432 -102 N -ATOM 1633 CA ASP B 11 16.164 -3.433 -19.698 1.00 45.20 C -ANISOU 1633 CA ASP B 11 4805 8137 4234 -264 1488 -331 C -ATOM 1634 C ASP B 11 17.116 -4.353 -18.916 1.00 47.40 C -ANISOU 1634 C ASP B 11 4938 8365 4707 -96 1536 -485 C -ATOM 1635 O ASP B 11 16.836 -5.539 -18.753 1.00 50.21 O -ANISOU 1635 O ASP B 11 5347 8625 5107 66 1521 -673 O -ATOM 1636 CB ASP B 11 16.532 -3.423 -21.190 1.00 44.91 C -ANISOU 1636 CB ASP B 11 4804 8285 3975 -320 1602 -326 C -ATOM 1637 CG ASP B 11 15.473 -2.745 -22.061 1.00 46.41 C -ANISOU 1637 CG ASP B 11 5154 8527 3953 -469 1524 -180 C -ATOM 1638 OD1 ASP B 11 14.281 -2.774 -21.695 1.00 42.08 O -ANISOU 1638 OD1 ASP B 11 4716 7867 3407 -470 1390 -161 O -ATOM 1639 OD2 ASP B 11 15.838 -2.196 -23.125 1.00 51.77 O -ANISOU 1639 OD2 ASP B 11 5839 9367 4465 -586 1592 -69 O -ATOM 1640 N ASP B 12 18.224 -3.803 -18.421 1.00 44.45 N -ANISOU 1640 N ASP B 12 4378 8048 4462 -145 1578 -389 N -ATOM 1641 CA ASP B 12 19.231 -4.600 -17.714 1.00 48.83 C -ANISOU 1641 CA ASP B 12 4760 8584 5211 3 1613 -490 C -ATOM 1642 C ASP B 12 19.040 -4.669 -16.187 1.00 50.12 C -ANISOU 1642 C ASP B 12 4870 8603 5571 39 1473 -485 C -ATOM 1643 O ASP B 12 19.905 -5.184 -15.475 1.00 48.78 O -ANISOU 1643 O ASP B 12 4532 8427 5575 135 1469 -521 O -ATOM 1644 CB ASP B 12 20.652 -4.121 -18.045 1.00 55.80 C -ANISOU 1644 CB ASP B 12 5434 9635 6132 -62 1735 -393 C -ATOM 1645 CG ASP B 12 20.878 -2.649 -17.713 1.00 59.74 C -ANISOU 1645 CG ASP B 12 5872 10177 6650 -297 1677 -163 C -ATOM 1646 OD1 ASP B 12 20.031 -2.045 -17.020 1.00 56.74 O -ANISOU 1646 OD1 ASP B 12 5592 9676 6292 -388 1547 -90 O -ATOM 1647 OD2 ASP B 12 21.914 -2.094 -18.141 1.00 63.33 O -ANISOU 1647 OD2 ASP B 12 6180 10775 7107 -395 1767 -55 O -ATOM 1648 N GLU B 13 17.915 -4.150 -15.697 1.00 46.31 N -ANISOU 1648 N GLU B 13 4522 8015 5058 -41 1363 -433 N -ATOM 1649 CA GLU B 13 17.582 -4.196 -14.268 1.00 48.97 C -ANISOU 1649 CA GLU B 13 4893 8137 5576 -17 1197 -421 C -ATOM 1650 C GLU B 13 17.582 -5.630 -13.727 1.00 42.70 C -ANISOU 1650 C GLU B 13 4079 7250 4896 196 1162 -587 C -ATOM 1651 O GLU B 13 16.816 -6.476 -14.180 1.00 40.46 O -ANISOU 1651 O GLU B 13 3922 6900 4550 303 1166 -713 O -ATOM 1652 CB GLU B 13 16.221 -3.541 -14.019 1.00 53.62 C -ANISOU 1652 CB GLU B 13 5706 8531 6134 -98 1074 -343 C -ATOM 1653 CG GLU B 13 15.598 -3.866 -12.662 1.00 59.04 C -ANISOU 1653 CG GLU B 13 6480 8989 6965 -39 924 -374 C -ATOM 1654 CD GLU B 13 16.327 -3.202 -11.512 1.00 64.89 C -ANISOU 1654 CD GLU B 13 7142 9685 7829 -135 851 -295 C -ATOM 1655 OE1 GLU B 13 16.526 -3.871 -10.472 1.00 66.45 O -ANISOU 1655 OE1 GLU B 13 7306 9808 8133 -59 766 -347 O -ATOM 1656 OE2 GLU B 13 16.695 -2.013 -11.651 1.00 66.92 O -ANISOU 1656 OE2 GLU B 13 7379 9977 8070 -303 866 -174 O -ATOM 1657 N PRO B 14 18.455 -5.907 -12.753 1.00 46.99 N -ANISOU 1657 N PRO B 14 4461 7779 5613 244 1109 -572 N -ATOM 1658 CA PRO B 14 18.590 -7.275 -12.242 1.00 46.79 C -ANISOU 1658 CA PRO B 14 4392 7661 5725 450 1069 -696 C -ATOM 1659 C PRO B 14 17.513 -7.658 -11.228 1.00 40.95 C -ANISOU 1659 C PRO B 14 3836 6675 5047 473 892 -697 C -ATOM 1660 O PRO B 14 17.355 -8.846 -10.955 1.00 43.54 O -ANISOU 1660 O PRO B 14 4182 6893 5470 632 851 -793 O -ATOM 1661 CB PRO B 14 19.962 -7.254 -11.566 1.00 49.99 C -ANISOU 1661 CB PRO B 14 4531 8169 6294 462 1055 -621 C -ATOM 1662 CG PRO B 14 20.107 -5.838 -11.093 1.00 52.62 C -ANISOU 1662 CG PRO B 14 4866 8532 6597 219 981 -453 C -ATOM 1663 CD PRO B 14 19.435 -4.987 -12.150 1.00 51.51 C -ANISOU 1663 CD PRO B 14 4869 8434 6266 98 1075 -427 C -ATOM 1664 N GLY B 15 16.783 -6.688 -10.685 1.00 33.46 N -ANISOU 1664 N GLY B 15 3022 5637 4055 320 799 -593 N -ATOM 1665 CA GLY B 15 15.821 -6.985 -9.634 1.00 33.35 C -ANISOU 1665 CA GLY B 15 3157 5421 4093 332 657 -584 C -ATOM 1666 C GLY B 15 16.541 -7.396 -8.354 1.00 36.70 C -ANISOU 1666 C GLY B 15 3478 5811 4657 360 543 -543 C -ATOM 1667 O GLY B 15 17.753 -7.212 -8.244 1.00 39.26 O -ANISOU 1667 O GLY B 15 3609 6264 5043 340 557 -499 O -ATOM 1668 N TYR B 16 15.806 -7.956 -7.394 1.00 29.04 N -ANISOU 1668 N TYR B 16 2621 4683 3730 394 424 -538 N -ATOM 1669 CA TYR B 16 16.388 -8.315 -6.092 1.00 31.79 C -ANISOU 1669 CA TYR B 16 2897 5003 4178 393 288 -469 C -ATOM 1670 C TYR B 16 16.286 -9.798 -5.760 1.00 32.43 C -ANISOU 1670 C TYR B 16 2966 4978 4379 563 218 -501 C -ATOM 1671 O TYR B 16 15.330 -10.463 -6.172 1.00 30.18 O -ANISOU 1671 O TYR B 16 2809 4578 4081 638 238 -574 O -ATOM 1672 CB TYR B 16 15.665 -7.548 -5.001 1.00 30.60 C -ANISOU 1672 CB TYR B 16 2905 4765 3955 245 198 -405 C -ATOM 1673 CG TYR B 16 15.703 -6.054 -5.164 1.00 30.58 C -ANISOU 1673 CG TYR B 16 2947 4806 3866 75 247 -373 C -ATOM 1674 CD1 TYR B 16 16.765 -5.323 -4.674 1.00 33.60 C -ANISOU 1674 CD1 TYR B 16 3225 5280 4262 -59 195 -310 C -ATOM 1675 CD2 TYR B 16 14.677 -5.380 -5.803 1.00 27.51 C -ANISOU 1675 CD2 TYR B 16 2700 4353 3400 41 328 -392 C -ATOM 1676 CE1 TYR B 16 16.814 -3.959 -4.805 1.00 32.78 C -ANISOU 1676 CE1 TYR B 16 3177 5178 4098 -229 228 -281 C -ATOM 1677 CE2 TYR B 16 14.712 -3.995 -5.941 1.00 30.97 C -ANISOU 1677 CE2 TYR B 16 3187 4792 3790 -109 365 -348 C -ATOM 1678 CZ TYR B 16 15.790 -3.300 -5.437 1.00 32.60 C -ANISOU 1678 CZ TYR B 16 3307 5066 4014 -246 317 -300 C -ATOM 1679 OH TYR B 16 15.859 -1.935 -5.562 1.00 36.23 O -ANISOU 1679 OH TYR B 16 3827 5493 4445 -409 343 -257 O -ATOM 1680 N ASP B 17 17.261 -10.309 -5.002 1.00 35.39 N -ANISOU 1680 N ASP B 17 3184 5382 4881 612 118 -430 N -ATOM 1681 CA ASP B 17 17.229 -11.701 -4.524 1.00 35.39 C -ANISOU 1681 CA ASP B 17 3168 5251 5027 768 21 -419 C -ATOM 1682 C ASP B 17 15.969 -11.889 -3.678 1.00 28.89 C -ANISOU 1682 C ASP B 17 2564 4279 4135 696 -79 -374 C -ATOM 1683 O ASP B 17 15.658 -11.051 -2.835 1.00 27.24 O -ANISOU 1683 O ASP B 17 2440 4098 3813 534 -136 -300 O -ATOM 1684 CB ASP B 17 18.492 -12.026 -3.698 1.00 39.53 C -ANISOU 1684 CB ASP B 17 3474 5846 5700 804 -105 -294 C -ATOM 1685 CG ASP B 17 18.628 -13.522 -3.364 1.00 49.10 C -ANISOU 1685 CG ASP B 17 4635 6907 7112 1001 -200 -266 C -ATOM 1686 OD1 ASP B 17 17.641 -14.140 -2.908 1.00 48.92 O -ANISOU 1686 OD1 ASP B 17 4793 6714 7078 1003 -278 -250 O -ATOM 1687 OD2 ASP B 17 19.733 -14.083 -3.553 1.00 57.87 O -ANISOU 1687 OD2 ASP B 17 5513 8064 8413 1156 -195 -247 O -ATOM 1688 N LEU B 18 15.247 -12.981 -3.901 1.00 26.73 N -ANISOU 1688 N LEU B 18 2380 3847 3928 809 -92 -424 N -ATOM 1689 CA LEU B 18 14.010 -13.266 -3.157 1.00 26.80 C -ANISOU 1689 CA LEU B 18 2571 3726 3885 738 -174 -366 C -ATOM 1690 C LEU B 18 14.274 -13.354 -1.649 1.00 27.19 C -ANISOU 1690 C LEU B 18 2613 3781 3938 659 -335 -200 C -ATOM 1691 O LEU B 18 13.393 -13.066 -0.834 1.00 29.54 O -ANISOU 1691 O LEU B 18 3050 4053 4119 538 -373 -136 O -ATOM 1692 CB LEU B 18 13.428 -14.599 -3.619 1.00 27.44 C -ANISOU 1692 CB LEU B 18 2717 3626 4082 868 -191 -429 C -ATOM 1693 CG LEU B 18 13.071 -14.749 -5.088 1.00 32.26 C -ANISOU 1693 CG LEU B 18 3371 4218 4667 937 -59 -607 C -ATOM 1694 CD1 LEU B 18 12.716 -16.187 -5.385 1.00 35.76 C -ANISOU 1694 CD1 LEU B 18 3878 4455 5254 1060 -107 -677 C -ATOM 1695 CD2 LEU B 18 11.914 -13.858 -5.422 1.00 32.46 C -ANISOU 1695 CD2 LEU B 18 3529 4284 4521 800 -1 -619 C -ATOM 1696 N ASP B 19 15.480 -13.780 -1.291 1.00 26.52 N -ANISOU 1696 N ASP B 19 2354 3739 3982 730 -426 -124 N -ATOM 1697 CA ASP B 19 15.816 -14.068 0.102 1.00 27.59 C -ANISOU 1697 CA ASP B 19 2470 3885 4129 662 -615 58 C -ATOM 1698 C ASP B 19 15.988 -12.804 0.937 1.00 31.67 C -ANISOU 1698 C ASP B 19 3026 4556 4452 447 -653 113 C -ATOM 1699 O ASP B 19 16.163 -12.875 2.157 1.00 31.24 O -ANISOU 1699 O ASP B 19 2994 4540 4335 341 -811 255 O -ATOM 1700 CB ASP B 19 17.091 -14.917 0.178 1.00 37.67 C -ANISOU 1700 CB ASP B 19 3517 5161 5633 816 -719 143 C -ATOM 1701 CG ASP B 19 16.934 -16.269 -0.509 1.00 50.95 C -ANISOU 1701 CG ASP B 19 5187 6641 7531 1041 -692 78 C -ATOM 1702 OD1 ASP B 19 15.896 -16.931 -0.271 1.00 51.72 O -ANISOU 1702 OD1 ASP B 19 5457 6571 7622 1029 -734 96 O -ATOM 1703 OD2 ASP B 19 17.839 -16.655 -1.292 1.00 55.36 O -ANISOU 1703 OD2 ASP B 19 5565 7206 8265 1222 -620 1 O -ATOM 1704 N LEU B 20 15.940 -11.650 0.282 1.00 26.05 N -ANISOU 1704 N LEU B 20 2335 3925 3638 371 -516 1 N -ATOM 1705 CA LEU B 20 16.081 -10.387 0.999 1.00 25.90 C -ANISOU 1705 CA LEU B 20 2380 4013 3448 162 -542 22 C -ATOM 1706 C LEU B 20 14.715 -9.818 1.365 1.00 26.67 C -ANISOU 1706 C LEU B 20 2717 4040 3377 63 -466 -29 C -ATOM 1707 O LEU B 20 14.625 -8.836 2.108 1.00 24.42 O -ANISOU 1707 O LEU B 20 2537 3804 2938 -104 -477 -35 O -ATOM 1708 CB LEU B 20 16.898 -9.390 0.173 1.00 26.26 C -ANISOU 1708 CB LEU B 20 2303 4171 3502 118 -451 -42 C -ATOM 1709 CG LEU B 20 18.344 -9.829 -0.011 1.00 28.11 C -ANISOU 1709 CG LEU B 20 2263 4517 3900 195 -522 29 C -ATOM 1710 CD1 LEU B 20 19.057 -9.009 -1.085 1.00 40.05 C -ANISOU 1710 CD1 LEU B 20 3634 6148 5436 175 -387 -34 C -ATOM 1711 CD2 LEU B 20 19.081 -9.715 1.301 1.00 34.54 C -ANISOU 1711 CD2 LEU B 20 3018 5422 4682 53 -735 176 C -ATOM 1712 N PHE B 21 13.660 -10.461 0.863 1.00 25.34 N -ANISOU 1712 N PHE B 21 2628 3754 3246 166 -391 -69 N -ATOM 1713 CA PHE B 21 12.281 -10.023 1.094 1.00 25.78 C -ANISOU 1713 CA PHE B 21 2867 3748 3180 103 -302 -104 C -ATOM 1714 C PHE B 21 11.421 -11.112 1.695 1.00 24.45 C -ANISOU 1714 C PHE B 21 2771 3492 3026 133 -360 -21 C -ATOM 1715 O PHE B 21 11.851 -12.274 1.809 1.00 24.22 O -ANISOU 1715 O PHE B 21 2666 3414 3121 217 -474 59 O -ATOM 1716 CB PHE B 21 11.663 -9.545 -0.229 1.00 27.39 C -ANISOU 1716 CB PHE B 21 3086 3913 3406 161 -149 -213 C -ATOM 1717 CG PHE B 21 12.360 -8.357 -0.795 1.00 28.60 C -ANISOU 1717 CG PHE B 21 3191 4147 3529 101 -82 -269 C -ATOM 1718 CD1 PHE B 21 11.959 -7.076 -0.444 1.00 32.57 C -ANISOU 1718 CD1 PHE B 21 3806 4646 3924 -21 -19 -297 C -ATOM 1719 CD2 PHE B 21 13.466 -8.512 -1.611 1.00 31.44 C -ANISOU 1719 CD2 PHE B 21 3387 4581 3977 162 -78 -286 C -ATOM 1720 CE1 PHE B 21 12.622 -5.968 -0.935 1.00 37.49 C -ANISOU 1720 CE1 PHE B 21 4393 5317 4535 -98 27 -329 C -ATOM 1721 CE2 PHE B 21 14.135 -7.412 -2.097 1.00 38.21 C -ANISOU 1721 CE2 PHE B 21 4189 5524 4806 80 -20 -309 C -ATOM 1722 CZ PHE B 21 13.713 -6.139 -1.771 1.00 39.59 C -ANISOU 1722 CZ PHE B 21 4489 5675 4881 -59 22 -323 C -ATOM 1723 N CYS B 22 10.212 -10.731 2.110 1.00 23.98 N -ANISOU 1723 N CYS B 22 2850 3408 2855 65 -279 -27 N -ATOM 1724 CA CYS B 22 9.232 -11.697 2.593 1.00 26.88 C -ANISOU 1724 CA CYS B 22 3278 3702 3232 72 -308 63 C -ATOM 1725 C CYS B 22 8.403 -12.131 1.402 1.00 27.60 C -ANISOU 1725 C CYS B 22 3357 3693 3438 169 -235 2 C -ATOM 1726 O CYS B 22 7.807 -11.302 0.716 1.00 26.51 O -ANISOU 1726 O CYS B 22 3243 3563 3268 169 -112 -83 O -ATOM 1727 CB CYS B 22 8.338 -11.089 3.682 1.00 26.00 C -ANISOU 1727 CB CYS B 22 3300 3643 2936 -54 -238 91 C -ATOM 1728 N ILE B 23 8.370 -13.436 1.162 1.00 24.77 N -ANISOU 1728 N ILE B 23 2967 3229 3216 245 -326 52 N -ATOM 1729 CA ILE B 23 7.694 -14.016 0.002 1.00 25.62 C -ANISOU 1729 CA ILE B 23 3074 3231 3431 321 -292 -19 C -ATOM 1730 C ILE B 23 6.943 -15.252 0.490 1.00 27.20 C -ANISOU 1730 C ILE B 23 3319 3309 3709 301 -385 98 C -ATOM 1731 O ILE B 23 7.476 -15.997 1.308 1.00 29.03 O -ANISOU 1731 O ILE B 23 3539 3501 3990 301 -506 215 O -ATOM 1732 CB ILE B 23 8.746 -14.438 -1.062 1.00 35.58 C -ANISOU 1732 CB ILE B 23 4246 4459 4815 453 -308 -127 C -ATOM 1733 CG1 ILE B 23 9.092 -13.262 -1.971 1.00 36.40 C -ANISOU 1733 CG1 ILE B 23 4313 4675 4842 457 -185 -245 C -ATOM 1734 CG2 ILE B 23 8.269 -15.596 -1.911 1.00 33.84 C -ANISOU 1734 CG2 ILE B 23 4051 4083 4724 531 -340 -183 C -ATOM 1735 CD1 ILE B 23 10.360 -12.600 -1.593 1.00 43.77 C -ANISOU 1735 CD1 ILE B 23 5160 5722 5749 443 -195 -236 C -ATOM 1736 N PRO B 24 5.722 -15.493 -0.022 1.00 28.54 N -ANISOU 1736 N PRO B 24 3528 3416 3900 273 -345 88 N -ATOM 1737 CA PRO B 24 4.986 -16.703 0.392 1.00 29.21 C -ANISOU 1737 CA PRO B 24 3651 3373 4076 228 -443 213 C -ATOM 1738 C PRO B 24 5.790 -17.958 0.082 1.00 30.46 C -ANISOU 1738 C PRO B 24 3797 3360 4418 328 -577 203 C -ATOM 1739 O PRO B 24 6.249 -18.081 -1.062 1.00 28.91 O -ANISOU 1739 O PRO B 24 3579 3111 4296 434 -554 39 O -ATOM 1740 CB PRO B 24 3.753 -16.697 -0.517 1.00 32.72 C -ANISOU 1740 CB PRO B 24 4109 3781 4542 194 -390 162 C -ATOM 1741 CG PRO B 24 3.644 -15.329 -1.073 1.00 30.28 C -ANISOU 1741 CG PRO B 24 3776 3607 4123 205 -254 61 C -ATOM 1742 CD PRO B 24 5.006 -14.713 -1.048 1.00 27.95 C -ANISOU 1742 CD PRO B 24 3454 3382 3783 272 -233 -16 C -ATOM 1743 N ASN B 25 5.936 -18.879 1.039 1.00 30.03 N -ANISOU 1743 N ASN B 25 3758 3215 4438 300 -706 373 N -ATOM 1744 CA ASN B 25 6.733 -20.081 0.797 1.00 38.07 C -ANISOU 1744 CA ASN B 25 4758 4034 5672 420 -837 375 C -ATOM 1745 C ASN B 25 6.239 -20.899 -0.396 1.00 33.57 C -ANISOU 1745 C ASN B 25 4240 3264 5250 473 -848 233 C -ATOM 1746 O ASN B 25 7.037 -21.553 -1.063 1.00 32.98 O -ANISOU 1746 O ASN B 25 4149 3046 5335 623 -881 113 O -ATOM 1747 CB ASN B 25 6.859 -20.963 2.054 1.00 43.35 C -ANISOU 1747 CB ASN B 25 5443 4619 6409 366 -997 627 C -ATOM 1748 CG ASN B 25 7.614 -22.270 1.782 1.00 56.05 C -ANISOU 1748 CG ASN B 25 7033 5969 8295 513 -1140 642 C -ATOM 1749 OD1 ASN B 25 7.012 -23.347 1.713 1.00 61.77 O -ANISOU 1749 OD1 ASN B 25 7829 6466 9173 486 -1233 707 O -ATOM 1750 ND2 ASN B 25 8.934 -22.174 1.615 1.00 52.48 N -ANISOU 1750 ND2 ASN B 25 6475 5539 7924 670 -1155 582 N -ATOM 1751 N HIS B 26 4.940 -20.845 -0.690 1.00 33.29 N -ANISOU 1751 N HIS B 26 4262 3225 5160 351 -815 236 N -ATOM 1752 CA HIS B 26 4.402 -21.653 -1.789 1.00 33.65 C -ANISOU 1752 CA HIS B 26 4374 3084 5326 359 -856 105 C -ATOM 1753 C HIS B 26 4.876 -21.186 -3.171 1.00 32.45 C -ANISOU 1753 C HIS B 26 4216 2981 5131 469 -757 -157 C -ATOM 1754 O HIS B 26 4.717 -21.896 -4.163 1.00 39.71 O -ANISOU 1754 O HIS B 26 5208 3747 6134 499 -789 -314 O -ATOM 1755 CB HIS B 26 2.865 -21.787 -1.732 1.00 32.62 C -ANISOU 1755 CB HIS B 26 4283 2948 5165 176 -876 206 C -ATOM 1756 CG HIS B 26 2.121 -20.496 -1.880 1.00 32.42 C -ANISOU 1756 CG HIS B 26 4205 3160 4953 104 -739 198 C -ATOM 1757 ND1 HIS B 26 1.798 -19.690 -0.808 1.00 34.77 N -ANISOU 1757 ND1 HIS B 26 4455 3636 5121 35 -658 348 N -ATOM 1758 CD2 HIS B 26 1.577 -19.899 -2.971 1.00 33.25 C -ANISOU 1758 CD2 HIS B 26 4302 3343 4989 89 -675 68 C -ATOM 1759 CE1 HIS B 26 1.130 -18.634 -1.237 1.00 33.57 C -ANISOU 1759 CE1 HIS B 26 4260 3637 4857 7 -538 299 C -ATOM 1760 NE2 HIS B 26 0.979 -18.738 -2.543 1.00 36.09 N -ANISOU 1760 NE2 HIS B 26 4595 3904 5214 35 -557 149 N -ATOM 1761 N TYR B 27 5.470 -20.003 -3.231 1.00 27.55 N -ANISOU 1761 N TYR B 27 3522 2576 4371 513 -638 -206 N -ATOM 1762 CA TYR B 27 6.057 -19.519 -4.481 1.00 27.72 C -ANISOU 1762 CA TYR B 27 3524 2673 4336 609 -535 -423 C -ATOM 1763 C TYR B 27 7.594 -19.467 -4.444 1.00 32.26 C -ANISOU 1763 C TYR B 27 4006 3281 4969 769 -499 -485 C -ATOM 1764 O TYR B 27 8.213 -18.881 -5.331 1.00 32.86 O -ANISOU 1764 O TYR B 27 4036 3475 4974 839 -387 -634 O -ATOM 1765 CB TYR B 27 5.518 -18.131 -4.821 1.00 23.31 C -ANISOU 1765 CB TYR B 27 2942 2332 3585 526 -421 -431 C -ATOM 1766 CG TYR B 27 4.058 -18.081 -5.221 1.00 24.33 C -ANISOU 1766 CG TYR B 27 3122 2456 3666 395 -440 -400 C -ATOM 1767 CD1 TYR B 27 3.485 -19.083 -5.989 1.00 25.36 C -ANISOU 1767 CD1 TYR B 27 3333 2433 3870 362 -527 -481 C -ATOM 1768 CD2 TYR B 27 3.263 -17.021 -4.827 1.00 24.06 C -ANISOU 1768 CD2 TYR B 27 3049 2569 3524 306 -374 -290 C -ATOM 1769 CE1 TYR B 27 2.141 -19.025 -6.352 1.00 24.26 C -ANISOU 1769 CE1 TYR B 27 3215 2310 3694 221 -568 -429 C -ATOM 1770 CE2 TYR B 27 1.927 -16.949 -5.185 1.00 23.85 C -ANISOU 1770 CE2 TYR B 27 3028 2555 3480 198 -392 -235 C -ATOM 1771 CZ TYR B 27 1.373 -17.956 -5.944 1.00 24.06 C -ANISOU 1771 CZ TYR B 27 3115 2451 3577 146 -500 -293 C -ATOM 1772 OH TYR B 27 0.035 -17.885 -6.304 1.00 25.02 O -ANISOU 1772 OH TYR B 27 3217 2603 3688 19 -543 -218 O -ATOM 1773 N ALA B 28 8.207 -20.080 -3.436 1.00 32.20 N -ANISOU 1773 N ALA B 28 3956 3186 5094 820 -598 -349 N -ATOM 1774 CA ALA B 28 9.664 -19.981 -3.253 1.00 37.43 C -ANISOU 1774 CA ALA B 28 4487 3905 5829 963 -585 -359 C -ATOM 1775 C ALA B 28 10.496 -20.414 -4.469 1.00 39.73 C -ANISOU 1775 C ALA B 28 4735 4136 6223 1146 -499 -586 C -ATOM 1776 O ALA B 28 11.576 -19.871 -4.715 1.00 41.19 O -ANISOU 1776 O ALA B 28 4785 4467 6396 1239 -412 -640 O -ATOM 1777 CB ALA B 28 10.105 -20.764 -2.019 1.00 38.29 C -ANISOU 1777 CB ALA B 28 4558 3901 6090 988 -744 -149 C -ATOM 1778 N GLU B 29 10.006 -21.404 -5.211 1.00 35.94 N -ANISOU 1778 N GLU B 29 4370 3443 5842 1190 -518 -722 N -ATOM 1779 CA GLU B 29 10.760 -21.966 -6.335 1.00 40.82 C -ANISOU 1779 CA GLU B 29 4977 3978 6557 1375 -423 -969 C -ATOM 1780 C GLU B 29 10.231 -21.465 -7.680 1.00 39.91 C -ANISOU 1780 C GLU B 29 4952 3975 6236 1312 -294 -1186 C -ATOM 1781 O GLU B 29 10.793 -21.757 -8.736 1.00 42.71 O -ANISOU 1781 O GLU B 29 5314 4318 6595 1439 -178 -1418 O -ATOM 1782 CB GLU B 29 10.729 -23.497 -6.288 1.00 48.79 C -ANISOU 1782 CB GLU B 29 6073 4635 7830 1484 -534 -1009 C -ATOM 1783 CG GLU B 29 11.745 -24.135 -5.330 1.00 59.92 C -ANISOU 1783 CG GLU B 29 7349 5921 9497 1643 -631 -847 C -ATOM 1784 CD GLU B 29 11.168 -24.480 -3.960 1.00 69.21 C -ANISOU 1784 CD GLU B 29 8560 7000 10736 1508 -831 -540 C -ATOM 1785 OE1 GLU B 29 10.044 -25.028 -3.893 1.00 72.64 O -ANISOU 1785 OE1 GLU B 29 9154 7269 11178 1371 -920 -502 O -ATOM 1786 OE2 GLU B 29 11.851 -24.212 -2.948 1.00 70.59 O -ANISOU 1786 OE2 GLU B 29 8600 7279 10944 1524 -903 -327 O -ATOM 1787 N ASP B 30 9.159 -20.687 -7.623 1.00 36.58 N -ANISOU 1787 N ASP B 30 4591 3676 5631 1118 -311 -1099 N -ATOM 1788 CA ASP B 30 8.426 -20.272 -8.813 1.00 36.02 C -ANISOU 1788 CA ASP B 30 4617 3699 5370 1023 -243 -1246 C -ATOM 1789 C ASP B 30 8.783 -18.867 -9.286 1.00 37.09 C -ANISOU 1789 C ASP B 30 4665 4126 5300 991 -104 -1252 C -ATOM 1790 O ASP B 30 8.342 -18.439 -10.355 1.00 36.65 O -ANISOU 1790 O ASP B 30 4673 4179 5072 921 -42 -1359 O -ATOM 1791 CB ASP B 30 6.929 -20.359 -8.528 1.00 34.44 C -ANISOU 1791 CB ASP B 30 4519 3435 5132 833 -364 -1126 C -ATOM 1792 CG ASP B 30 6.518 -21.732 -8.032 1.00 41.97 C -ANISOU 1792 CG ASP B 30 5562 4093 6292 828 -515 -1088 C -ATOM 1793 OD1 ASP B 30 7.111 -22.720 -8.504 1.00 44.41 O -ANISOU 1793 OD1 ASP B 30 5928 4208 6740 961 -519 -1259 O -ATOM 1794 OD2 ASP B 30 5.614 -21.820 -7.171 1.00 43.35 O -ANISOU 1794 OD2 ASP B 30 5750 4225 6497 693 -619 -886 O -ATOM 1795 N LEU B 31 9.571 -18.150 -8.481 1.00 34.07 N -ANISOU 1795 N LEU B 31 4143 3867 4934 1021 -71 -1122 N -ATOM 1796 CA LEU B 31 9.985 -16.782 -8.809 1.00 33.14 C -ANISOU 1796 CA LEU B 31 3940 3999 4651 974 48 -1104 C -ATOM 1797 C LEU B 31 11.497 -16.726 -8.986 1.00 36.06 C -ANISOU 1797 C LEU B 31 4155 4463 5082 1118 149 -1169 C -ATOM 1798 O LEU B 31 12.229 -17.490 -8.358 1.00 39.99 O -ANISOU 1798 O LEU B 31 4573 4852 5769 1242 97 -1143 O -ATOM 1799 CB LEU B 31 9.557 -15.798 -7.720 1.00 29.34 C -ANISOU 1799 CB LEU B 31 3432 3597 4118 849 3 -899 C -ATOM 1800 CG LEU B 31 8.077 -15.812 -7.380 1.00 29.67 C -ANISOU 1800 CG LEU B 31 3582 3567 4125 721 -76 -805 C -ATOM 1801 CD1 LEU B 31 7.776 -14.842 -6.250 1.00 27.15 C -ANISOU 1801 CD1 LEU B 31 3235 3327 3755 627 -81 -635 C -ATOM 1802 CD2 LEU B 31 7.289 -15.473 -8.636 1.00 29.68 C -ANISOU 1802 CD2 LEU B 31 3654 3629 3994 655 -33 -894 C -ATOM 1803 N GLU B 32 11.959 -15.836 -9.858 1.00 35.89 N -ANISOU 1803 N GLU B 32 4078 4647 4912 1097 289 -1235 N -ATOM 1804 CA GLU B 32 13.384 -15.716 -10.120 1.00 38.01 C -ANISOU 1804 CA GLU B 32 4170 5043 5230 1218 408 -1289 C -ATOM 1805 C GLU B 32 13.954 -14.578 -9.276 1.00 35.23 C -ANISOU 1805 C GLU B 32 3682 4840 4862 1129 392 -1105 C -ATOM 1806 O GLU B 32 14.986 -14.733 -8.620 1.00 39.65 O -ANISOU 1806 O GLU B 32 4079 5423 5561 1208 368 -1039 O -ATOM 1807 CB GLU B 32 13.634 -15.449 -11.606 1.00 39.54 C -ANISOU 1807 CB GLU B 32 4374 5395 5254 1231 586 -1463 C -ATOM 1808 CG GLU B 32 15.078 -15.618 -12.034 1.00 45.32 C -ANISOU 1808 CG GLU B 32 4918 6246 6056 1385 742 -1552 C -ATOM 1809 CD GLU B 32 15.560 -17.055 -11.934 1.00 55.76 C -ANISOU 1809 CD GLU B 32 6242 7352 7593 1568 728 -1634 C -ATOM 1810 OE1 GLU B 32 14.714 -17.974 -11.962 1.00 58.10 O -ANISOU 1810 OE1 GLU B 32 6712 7427 7938 1589 638 -1723 O -ATOM 1811 OE2 GLU B 32 16.787 -17.267 -11.833 1.00 61.45 O -ANISOU 1811 OE2 GLU B 32 6785 8117 8447 1689 806 -1599 O -ATOM 1812 N ARG B 33 13.273 -13.437 -9.306 1.00 30.91 N -ANISOU 1812 N ARG B 33 3205 4385 4153 961 396 -1023 N -ATOM 1813 CA ARG B 33 13.726 -12.222 -8.620 1.00 31.71 C -ANISOU 1813 CA ARG B 33 3221 4611 4218 848 389 -879 C -ATOM 1814 C ARG B 33 12.528 -11.387 -8.214 1.00 29.55 C -ANISOU 1814 C ARG B 33 3085 4300 3841 698 337 -785 C -ATOM 1815 O ARG B 33 11.485 -11.437 -8.869 1.00 32.15 O -ANISOU 1815 O ARG B 33 3534 4590 4092 666 347 -824 O -ATOM 1816 CB ARG B 33 14.573 -11.368 -9.573 1.00 33.79 C -ANISOU 1816 CB ARG B 33 3372 5083 4384 819 537 -911 C -ATOM 1817 CG ARG B 33 15.711 -12.081 -10.265 1.00 41.51 C -ANISOU 1817 CG ARG B 33 4195 6140 5435 977 653 -1030 C -ATOM 1818 CD ARG B 33 16.838 -12.359 -9.300 1.00 46.91 C -ANISOU 1818 CD ARG B 33 4681 6834 6308 1054 591 -945 C -ATOM 1819 NE ARG B 33 17.565 -11.141 -8.957 1.00 47.46 N -ANISOU 1819 NE ARG B 33 4619 7075 6338 913 597 -813 N -ATOM 1820 CZ ARG B 33 18.613 -11.105 -8.144 1.00 50.45 C -ANISOU 1820 CZ ARG B 33 4803 7515 6850 922 527 -708 C -ATOM 1821 NH1 ARG B 33 19.055 -12.226 -7.590 1.00 53.13 N -ANISOU 1821 NH1 ARG B 33 5048 7758 7382 1087 446 -703 N -ATOM 1822 NH2 ARG B 33 19.218 -9.951 -7.891 1.00 48.89 N -ANISOU 1822 NH2 ARG B 33 4506 7467 6605 758 522 -596 N -ATOM 1823 N VAL B 34 12.665 -10.592 -7.156 1.00 24.70 N -ANISOU 1823 N VAL B 34 2454 3705 3227 602 284 -665 N -ATOM 1824 CA VAL B 34 11.712 -9.496 -6.946 1.00 23.27 C -ANISOU 1824 CA VAL B 34 2381 3514 2945 472 291 -597 C -ATOM 1825 C VAL B 34 12.082 -8.389 -7.944 1.00 25.92 C -ANISOU 1825 C VAL B 34 2680 3980 3187 405 397 -601 C -ATOM 1826 O VAL B 34 13.258 -8.048 -8.074 1.00 25.92 O -ANISOU 1826 O VAL B 34 2553 4094 3199 392 439 -595 O -ATOM 1827 CB VAL B 34 11.786 -8.944 -5.533 1.00 25.11 C -ANISOU 1827 CB VAL B 34 2633 3722 3185 384 220 -503 C -ATOM 1828 CG1 VAL B 34 10.873 -7.724 -5.397 1.00 26.94 C -ANISOU 1828 CG1 VAL B 34 2974 3928 3332 276 262 -462 C -ATOM 1829 CG2 VAL B 34 11.383 -10.014 -4.550 1.00 27.19 C -ANISOU 1829 CG2 VAL B 34 2938 3878 3515 428 114 -467 C -ATOM 1830 N PHE B 35 11.092 -7.843 -8.654 1.00 25.73 N -ANISOU 1830 N PHE B 35 2752 3946 3079 354 433 -586 N -ATOM 1831 CA PHE B 35 11.359 -6.883 -9.724 1.00 27.87 C -ANISOU 1831 CA PHE B 35 2999 4337 3253 285 522 -562 C -ATOM 1832 C PHE B 35 10.979 -5.475 -9.274 1.00 29.01 C -ANISOU 1832 C PHE B 35 3197 4438 3388 167 520 -450 C -ATOM 1833 O PHE B 35 11.754 -4.525 -9.415 1.00 29.12 O -ANISOU 1833 O PHE B 35 3158 4522 3385 80 563 -398 O -ATOM 1834 CB PHE B 35 10.588 -7.289 -10.988 1.00 29.53 C -ANISOU 1834 CB PHE B 35 3276 4577 3367 308 547 -611 C -ATOM 1835 CG PHE B 35 11.120 -6.675 -12.256 1.00 31.87 C -ANISOU 1835 CG PHE B 35 3533 5044 3533 253 647 -603 C -ATOM 1836 CD1 PHE B 35 12.412 -6.938 -12.679 1.00 32.26 C -ANISOU 1836 CD1 PHE B 35 3460 5235 3564 292 744 -673 C -ATOM 1837 CD2 PHE B 35 10.306 -5.865 -13.043 1.00 36.14 C -ANISOU 1837 CD2 PHE B 35 4147 5614 3970 163 647 -509 C -ATOM 1838 CE1 PHE B 35 12.908 -6.383 -13.864 1.00 37.45 C -ANISOU 1838 CE1 PHE B 35 4075 6078 4076 227 857 -656 C -ATOM 1839 CE2 PHE B 35 10.783 -5.304 -14.223 1.00 35.31 C -ANISOU 1839 CE2 PHE B 35 4014 5682 3720 92 732 -473 C -ATOM 1840 CZ PHE B 35 12.088 -5.562 -14.634 1.00 39.83 C -ANISOU 1840 CZ PHE B 35 4473 6413 4249 117 847 -551 C -ATOM 1841 N ILE B 36 9.778 -5.346 -8.723 1.00 24.48 N -ANISOU 1841 N ILE B 36 2725 3738 2840 165 476 -413 N -ATOM 1842 CA ILE B 36 9.322 -4.082 -8.141 1.00 25.32 C -ANISOU 1842 CA ILE B 36 2896 3759 2966 86 488 -334 C -ATOM 1843 C ILE B 36 8.748 -4.366 -6.773 1.00 27.19 C -ANISOU 1843 C ILE B 36 3194 3886 3251 106 446 -347 C -ATOM 1844 O ILE B 36 7.647 -4.922 -6.660 1.00 25.26 O -ANISOU 1844 O ILE B 36 2989 3582 3026 158 428 -338 O -ATOM 1845 CB ILE B 36 8.232 -3.414 -8.996 1.00 24.09 C -ANISOU 1845 CB ILE B 36 2792 3569 2791 72 510 -253 C -ATOM 1846 CG1 ILE B 36 8.646 -3.381 -10.463 1.00 28.11 C -ANISOU 1846 CG1 ILE B 36 3258 4219 3205 47 541 -234 C -ATOM 1847 CG2 ILE B 36 7.910 -1.999 -8.474 1.00 24.04 C -ANISOU 1847 CG2 ILE B 36 2848 3446 2840 10 540 -177 C -ATOM 1848 CD1 ILE B 36 7.561 -2.838 -11.406 1.00 27.78 C -ANISOU 1848 CD1 ILE B 36 3259 4168 3127 24 527 -124 C -ATOM 1849 N PRO B 37 9.495 -4.002 -5.714 1.00 27.00 N -ANISOU 1849 N PRO B 37 3175 3851 3234 46 427 -360 N -ATOM 1850 CA PRO B 37 8.998 -4.286 -4.370 1.00 21.64 C -ANISOU 1850 CA PRO B 37 2567 3098 2558 47 394 -371 C -ATOM 1851 C PRO B 37 7.668 -3.589 -4.114 1.00 22.23 C -ANISOU 1851 C PRO B 37 2738 3064 2643 53 459 -347 C -ATOM 1852 O PRO B 37 7.466 -2.454 -4.564 1.00 21.25 O -ANISOU 1852 O PRO B 37 2646 2888 2540 22 516 -322 O -ATOM 1853 CB PRO B 37 10.071 -3.672 -3.465 1.00 23.15 C -ANISOU 1853 CB PRO B 37 2764 3313 2721 -60 359 -387 C -ATOM 1854 CG PRO B 37 11.341 -3.790 -4.267 1.00 24.13 C -ANISOU 1854 CG PRO B 37 2749 3555 2862 -73 342 -380 C -ATOM 1855 CD PRO B 37 10.888 -3.518 -5.705 1.00 26.27 C -ANISOU 1855 CD PRO B 37 3005 3843 3134 -34 420 -361 C -ATOM 1856 N HIS B 38 6.797 -4.257 -3.368 1.00 24.77 N -ANISOU 1856 N HIS B 38 3967 3332 2111 323 -687 -261 N -ATOM 1857 CA HIS B 38 5.488 -3.712 -3.015 1.00 26.09 C -ANISOU 1857 CA HIS B 38 4063 3420 2429 122 -721 -114 C -ATOM 1858 C HIS B 38 5.541 -2.261 -2.541 1.00 20.45 C -ANISOU 1858 C HIS B 38 3049 2851 1871 92 -499 -149 C -ATOM 1859 O HIS B 38 4.764 -1.416 -2.996 1.00 21.01 O -ANISOU 1859 O HIS B 38 2971 2891 2121 -33 -457 -42 O -ATOM 1860 CB HIS B 38 4.849 -4.532 -1.899 1.00 27.22 C -ANISOU 1860 CB HIS B 38 4287 3463 2594 67 -738 12 C -ATOM 1861 CG HIS B 38 3.534 -3.978 -1.447 1.00 28.37 C -ANISOU 1861 CG HIS B 38 4183 3599 2996 -114 -623 257 C -ATOM 1862 ND1 HIS B 38 3.383 -3.290 -0.260 1.00 28.88 N -ANISOU 1862 ND1 HIS B 38 4083 3803 3089 -12 -376 277 N -ATOM 1863 CD2 HIS B 38 2.316 -3.982 -2.041 1.00 26.09 C -ANISOU 1863 CD2 HIS B 38 3777 3206 2931 -339 -730 504 C -ATOM 1864 CE1 HIS B 38 2.124 -2.918 -0.131 1.00 32.98 C -ANISOU 1864 CE1 HIS B 38 4385 4337 3810 -127 -286 548 C -ATOM 1865 NE2 HIS B 38 1.454 -3.322 -1.196 1.00 29.84 N -ANISOU 1865 NE2 HIS B 38 3970 3806 3563 -355 -500 700 N -ATOM 1866 N GLY B 39 6.445 -1.989 -1.606 1.00 22.31 N -ANISOU 1866 N GLY B 39 3238 3212 2027 226 -406 -308 N -ATOM 1867 CA GLY B 39 6.566 -0.663 -1.019 1.00 22.10 C -ANISOU 1867 CA GLY B 39 3027 3247 2124 217 -290 -374 C -ATOM 1868 C GLY B 39 6.923 0.399 -2.056 1.00 22.95 C -ANISOU 1868 C GLY B 39 2984 3383 2353 111 -273 -376 C -ATOM 1869 O GLY B 39 6.502 1.556 -1.939 1.00 23.52 O -ANISOU 1869 O GLY B 39 2961 3400 2576 39 -219 -353 O -ATOM 1870 N LEU B 40 7.701 0.015 -3.061 1.00 21.25 N -ANISOU 1870 N LEU B 40 2778 3254 2043 145 -309 -383 N -ATOM 1871 CA LEU B 40 8.060 0.937 -4.131 1.00 23.76 C -ANISOU 1871 CA LEU B 40 2955 3621 2452 65 -252 -315 C -ATOM 1872 C LEU B 40 6.828 1.235 -4.991 1.00 24.08 C -ANISOU 1872 C LEU B 40 3053 3512 2584 -33 -263 -173 C -ATOM 1873 O LEU B 40 6.633 2.365 -5.456 1.00 19.69 O -ANISOU 1873 O LEU B 40 2395 2916 2169 -134 -200 -107 O -ATOM 1874 CB LEU B 40 9.223 0.376 -4.967 1.00 22.11 C -ANISOU 1874 CB LEU B 40 2736 3609 2057 226 -234 -308 C -ATOM 1875 CG LEU B 40 9.597 1.153 -6.233 1.00 30.80 C -ANISOU 1875 CG LEU B 40 3705 4799 3198 198 -124 -157 C -ATOM 1876 CD1 LEU B 40 9.784 2.648 -5.949 1.00 29.12 C -ANISOU 1876 CD1 LEU B 40 3243 4551 3270 -45 -63 -110 C -ATOM 1877 CD2 LEU B 40 10.852 0.577 -6.885 1.00 30.93 C -ANISOU 1877 CD2 LEU B 40 3665 5101 2986 451 -46 -106 C -ATOM 1878 N ILE B 41 5.978 0.231 -5.194 1.00 20.13 N -ANISOU 1878 N ILE B 41 2726 2906 2018 -18 -383 -113 N -ATOM 1879 CA ILE B 41 4.711 0.464 -5.896 1.00 21.13 C -ANISOU 1879 CA ILE B 41 2866 2895 2268 -128 -456 33 C -ATOM 1880 C ILE B 41 3.866 1.489 -5.135 1.00 22.31 C -ANISOU 1880 C ILE B 41 2834 3024 2619 -214 -343 94 C -ATOM 1881 O ILE B 41 3.255 2.382 -5.739 1.00 20.89 O -ANISOU 1881 O ILE B 41 2588 2798 2551 -262 -321 176 O -ATOM 1882 CB ILE B 41 3.917 -0.842 -6.067 1.00 23.71 C -ANISOU 1882 CB ILE B 41 3382 3076 2553 -162 -684 115 C -ATOM 1883 CG1 ILE B 41 4.705 -1.809 -6.954 1.00 24.57 C -ANISOU 1883 CG1 ILE B 41 3790 3156 2391 15 -844 30 C -ATOM 1884 CG2 ILE B 41 2.561 -0.568 -6.695 1.00 21.33 C -ANISOU 1884 CG2 ILE B 41 3018 2652 2435 -308 -809 288 C -ATOM 1885 CD1 ILE B 41 4.111 -3.225 -7.024 1.00 29.83 C -ANISOU 1885 CD1 ILE B 41 4725 3593 3016 -17 -1124 72 C -ATOM 1886 N AMET B 42 3.838 1.364 -3.814 0.29 19.85 N -ANISOU 1886 N AMET B 42 2486 2750 2307 -168 -271 54 N -ATOM 1887 N BMET B 42 3.830 1.361 -3.814 0.71 19.67 N -ANISOU 1887 N BMET B 42 2463 2726 2284 -168 -271 56 N -ATOM 1888 CA AMET B 42 3.065 2.278 -2.978 0.29 19.81 C -ANISOU 1888 CA AMET B 42 2375 2747 2407 -126 -151 110 C -ATOM 1889 CA BMET B 42 3.064 2.296 -2.981 0.71 19.31 C -ANISOU 1889 CA BMET B 42 2310 2683 2344 -126 -150 109 C -ATOM 1890 C AMET B 42 3.578 3.703 -3.081 0.29 20.72 C -ANISOU 1890 C AMET B 42 2471 2827 2573 -112 -103 2 C -ATOM 1891 C BMET B 42 3.579 3.712 -3.095 0.71 21.41 C -ANISOU 1891 C BMET B 42 2559 2914 2661 -113 -103 2 C -ATOM 1892 O AMET B 42 2.795 4.645 -3.225 0.29 21.11 O -ANISOU 1892 O AMET B 42 2489 2822 2710 -89 -60 78 O -ATOM 1893 O BMET B 42 2.801 4.665 -3.259 0.71 20.73 O -ANISOU 1893 O BMET B 42 2441 2772 2664 -92 -61 78 O -ATOM 1894 CB AMET B 42 3.081 1.808 -1.522 0.29 20.54 C -ANISOU 1894 CB AMET B 42 2502 2894 2408 10 -74 82 C -ATOM 1895 CB BMET B 42 3.072 1.848 -1.511 0.71 19.74 C -ANISOU 1895 CB BMET B 42 2399 2793 2309 13 -71 82 C -ATOM 1896 CG AMET B 42 2.595 0.387 -1.369 0.29 22.66 C -ANISOU 1896 CG AMET B 42 2806 3155 2647 -44 -132 236 C -ATOM 1897 CG BMET B 42 2.444 0.486 -1.247 0.71 24.43 C -ANISOU 1897 CG BMET B 42 3010 3387 2884 -32 -108 259 C -ATOM 1898 SD AMET B 42 1.019 0.161 -2.200 0.29 37.14 S -ANISOU 1898 SD AMET B 42 4476 4939 4696 -234 -216 560 S -ATOM 1899 SD BMET B 42 0.692 0.413 -1.660 0.71 29.67 S -ANISOU 1899 SD BMET B 42 3458 4049 3766 -168 -112 622 S -ATOM 1900 CE AMET B 42 -0.100 0.576 -0.857 0.29 30.48 C -ANISOU 1900 CE AMET B 42 3420 4250 3909 -75 43 808 C -ATOM 1901 CE BMET B 42 0.826 -0.216 -3.341 0.71 40.65 C -ANISOU 1901 CE BMET B 42 4966 5283 5197 -378 -415 602 C -ATOM 1902 N ASP B 43 4.895 3.856 -3.022 1.00 19.86 N -ANISOU 1902 N ASP B 43 2380 2745 2421 -132 -134 -152 N -ATOM 1903 CA ASP B 43 5.512 5.178 -3.100 1.00 20.09 C -ANISOU 1903 CA ASP B 43 2386 2697 2551 -198 -150 -218 C -ATOM 1904 C ASP B 43 5.201 5.843 -4.433 1.00 22.69 C -ANISOU 1904 C ASP B 43 2687 2964 2969 -305 -123 -81 C -ATOM 1905 O ASP B 43 4.925 7.046 -4.487 1.00 20.99 O -ANISOU 1905 O ASP B 43 2515 2610 2852 -335 -128 -64 O -ATOM 1906 CB ASP B 43 7.027 5.075 -2.969 1.00 22.09 C -ANISOU 1906 CB ASP B 43 2563 3037 2795 -257 -212 -328 C -ATOM 1907 CG ASP B 43 7.485 4.756 -1.548 1.00 30.44 C -ANISOU 1907 CG ASP B 43 3682 4116 3769 -131 -290 -507 C -ATOM 1908 OD1 ASP B 43 6.766 5.087 -0.576 1.00 28.70 O -ANISOU 1908 OD1 ASP B 43 3599 3796 3508 12 -293 -562 O -ATOM 1909 OD2 ASP B 43 8.583 4.179 -1.423 1.00 29.88 O -ANISOU 1909 OD2 ASP B 43 3528 4182 3643 -124 -344 -582 O -ATOM 1910 N ARG B 44 5.279 5.071 -5.510 1.00 18.05 N -ANISOU 1910 N ARG B 44 2090 2457 2312 -322 -117 7 N -ATOM 1911 CA ARG B 44 5.011 5.635 -6.833 1.00 18.67 C -ANISOU 1911 CA ARG B 44 2188 2484 2422 -364 -93 140 C -ATOM 1912 C ARG B 44 3.517 5.964 -6.959 1.00 21.26 C -ANISOU 1912 C ARG B 44 2555 2709 2816 -331 -123 223 C -ATOM 1913 O ARG B 44 3.141 7.024 -7.470 1.00 22.18 O -ANISOU 1913 O ARG B 44 2701 2724 3002 -343 -99 290 O -ATOM 1914 CB ARG B 44 5.440 4.658 -7.929 1.00 18.42 C -ANISOU 1914 CB ARG B 44 2219 2556 2222 -286 -109 196 C -ATOM 1915 CG ARG B 44 5.094 5.130 -9.340 1.00 21.68 C -ANISOU 1915 CG ARG B 44 2718 2917 2603 -253 -92 337 C -ATOM 1916 CD ARG B 44 5.686 6.511 -9.641 1.00 20.43 C -ANISOU 1916 CD ARG B 44 2470 2728 2565 -359 42 433 C -ATOM 1917 NE ARG B 44 5.392 6.922 -11.022 1.00 22.80 N -ANISOU 1917 NE ARG B 44 2887 2986 2791 -283 86 592 N -ATOM 1918 CZ ARG B 44 5.280 8.187 -11.417 1.00 28.74 C -ANISOU 1918 CZ ARG B 44 3651 3612 3656 -369 157 710 C -ATOM 1919 NH1 ARG B 44 5.468 9.166 -10.533 1.00 27.79 N -ANISOU 1919 NH1 ARG B 44 3455 3366 3736 -547 152 672 N -ATOM 1920 NH2 ARG B 44 4.998 8.479 -12.695 1.00 26.75 N -ANISOU 1920 NH2 ARG B 44 3543 3327 3294 -252 203 860 N -ATOM 1921 N THR B 45 2.681 5.065 -6.440 1.00 20.88 N -ANISOU 1921 N THR B 45 2484 2696 2754 -289 -177 249 N -ATOM 1922 CA THR B 45 1.226 5.246 -6.452 1.00 21.15 C -ANISOU 1922 CA THR B 45 2448 2706 2880 -256 -203 389 C -ATOM 1923 C THR B 45 0.796 6.478 -5.662 1.00 22.83 C -ANISOU 1923 C THR B 45 2640 2890 3143 -138 -92 379 C -ATOM 1924 O THR B 45 -0.123 7.204 -6.073 1.00 22.44 O -ANISOU 1924 O THR B 45 2565 2810 3149 -65 -87 484 O -ATOM 1925 CB THR B 45 0.497 3.969 -5.978 1.00 25.19 C -ANISOU 1925 CB THR B 45 2881 3277 3413 -287 -284 495 C -ATOM 1926 OG1 THR B 45 0.863 2.883 -6.840 1.00 24.16 O -ANISOU 1926 OG1 THR B 45 2883 3095 3203 -360 -467 480 O -ATOM 1927 CG2 THR B 45 -1.034 4.132 -6.040 1.00 21.86 C -ANISOU 1927 CG2 THR B 45 2274 2892 3140 -280 -316 721 C -ATOM 1928 N GLU B 46 1.471 6.746 -4.552 1.00 19.62 N -ANISOU 1928 N GLU B 46 2291 2476 2687 -72 -36 239 N -ATOM 1929 CA GLU B 46 1.192 7.971 -3.812 1.00 23.03 C -ANISOU 1929 CA GLU B 46 2828 2815 3106 103 6 185 C -ATOM 1930 C GLU B 46 1.371 9.200 -4.690 1.00 23.47 C -ANISOU 1930 C GLU B 46 3000 2692 3225 38 -43 181 C -ATOM 1931 O GLU B 46 0.544 10.115 -4.661 1.00 21.14 O -ANISOU 1931 O GLU B 46 2793 2320 2920 211 -27 228 O -ATOM 1932 CB GLU B 46 2.111 8.105 -2.598 1.00 18.88 C -ANISOU 1932 CB GLU B 46 2429 2242 2501 175 -26 -12 C -ATOM 1933 CG GLU B 46 1.803 9.348 -1.774 1.00 24.79 C -ANISOU 1933 CG GLU B 46 3403 2836 3180 427 -54 -102 C -ATOM 1934 CD GLU B 46 2.705 9.472 -0.553 1.00 30.85 C -ANISOU 1934 CD GLU B 46 4360 3513 3850 526 -171 -326 C -ATOM 1935 OE1 GLU B 46 2.514 10.415 0.226 1.00 30.47 O -ANISOU 1935 OE1 GLU B 46 4590 3296 3691 790 -255 -438 O -ATOM 1936 OE2 GLU B 46 3.591 8.616 -0.372 1.00 33.64 O -ANISOU 1936 OE2 GLU B 46 4617 3953 4211 382 -209 -400 O -ATOM 1937 N ARG B 47 2.457 9.240 -5.461 1.00 22.42 N -ANISOU 1937 N ARG B 47 2872 2505 3141 -179 -86 156 N -ATOM 1938 CA ARG B 47 2.693 10.398 -6.327 1.00 22.64 C -ANISOU 1938 CA ARG B 47 3009 2353 3241 -272 -111 214 C -ATOM 1939 C ARG B 47 1.680 10.422 -7.462 1.00 23.15 C -ANISOU 1939 C ARG B 47 3065 2440 3289 -204 -81 368 C -ATOM 1940 O ARG B 47 1.242 11.489 -7.895 1.00 26.52 O -ANISOU 1940 O ARG B 47 3630 2711 3735 -144 -93 423 O -ATOM 1941 CB ARG B 47 4.128 10.396 -6.880 1.00 24.24 C -ANISOU 1941 CB ARG B 47 3143 2558 3508 -510 -114 239 C -ATOM 1942 CG ARG B 47 4.417 11.504 -7.913 1.00 26.47 C -ANISOU 1942 CG ARG B 47 3507 2672 3877 -642 -99 392 C -ATOM 1943 CD ARG B 47 4.158 12.908 -7.363 1.00 29.19 C -ANISOU 1943 CD ARG B 47 4089 2699 4302 -636 -226 340 C -ATOM 1944 NE ARG B 47 4.267 13.936 -8.410 1.00 30.90 N -ANISOU 1944 NE ARG B 47 4427 2720 4595 -757 -213 523 N -ATOM 1945 CZ ARG B 47 5.298 14.769 -8.547 1.00 38.01 C -ANISOU 1945 CZ ARG B 47 5350 3425 5669 -1041 -290 629 C -ATOM 1946 NH1 ARG B 47 6.325 14.720 -7.707 1.00 40.40 N -ANISOU 1946 NH1 ARG B 47 5539 3706 6106 -1240 -429 548 N -ATOM 1947 NH2 ARG B 47 5.303 15.668 -9.523 1.00 39.80 N -ANISOU 1947 NH2 ARG B 47 5703 3466 5953 -1141 -252 843 N -ATOM 1948 N LEU B 48 1.298 9.251 -7.954 1.00 20.59 N -ANISOU 1948 N LEU B 48 2621 2279 2925 -204 -90 431 N -ATOM 1949 CA LEU B 48 0.304 9.222 -9.034 1.00 24.66 C -ANISOU 1949 CA LEU B 48 3141 2797 3434 -138 -147 562 C -ATOM 1950 C LEU B 48 -1.020 9.789 -8.567 1.00 24.91 C -ANISOU 1950 C LEU B 48 3119 2838 3506 42 -147 627 C -ATOM 1951 O LEU B 48 -1.693 10.473 -9.331 1.00 26.83 O -ANISOU 1951 O LEU B 48 3424 3019 3751 138 -183 710 O -ATOM 1952 CB LEU B 48 0.091 7.811 -9.601 1.00 22.92 C -ANISOU 1952 CB LEU B 48 2858 2682 3168 -177 -264 605 C -ATOM 1953 CG LEU B 48 1.217 7.263 -10.483 1.00 28.61 C -ANISOU 1953 CG LEU B 48 3694 3417 3759 -218 -267 580 C -ATOM 1954 CD1 LEU B 48 0.926 5.845 -10.915 1.00 30.39 C -ANISOU 1954 CD1 LEU B 48 3971 3678 3896 -196 -458 584 C -ATOM 1955 CD2 LEU B 48 1.445 8.136 -11.694 1.00 32.47 C -ANISOU 1955 CD2 LEU B 48 4324 3825 4188 -167 -214 672 C -ATOM 1956 N ALA B 49 -1.399 9.516 -7.317 1.00 21.19 N -ANISOU 1956 N ALA B 49 2536 2473 3041 142 -89 610 N -ATOM 1957 CA ALA B 49 -2.678 10.038 -6.804 1.00 22.15 C -ANISOU 1957 CA ALA B 49 2567 2685 3164 404 -34 725 C -ATOM 1958 C ALA B 49 -2.670 11.549 -6.851 1.00 25.94 C -ANISOU 1958 C ALA B 49 3308 2970 3576 585 -18 656 C -ATOM 1959 O ALA B 49 -3.673 12.200 -7.201 1.00 25.32 O -ANISOU 1959 O ALA B 49 3227 2915 3479 804 -18 764 O -ATOM 1960 CB ALA B 49 -2.925 9.549 -5.372 1.00 23.29 C -ANISOU 1960 CB ALA B 49 2588 2993 3266 549 85 745 C -ATOM 1961 N ARG B 50 -1.536 12.126 -6.473 1.00 24.79 N -ANISOU 1961 N ARG B 50 3402 2617 3402 497 -39 486 N -ATOM 1962 CA ARG B 50 -1.434 13.577 -6.497 1.00 28.34 C -ANISOU 1962 CA ARG B 50 4175 2788 3804 618 -97 422 C -ATOM 1963 C ARG B 50 -1.492 14.102 -7.925 1.00 29.91 C -ANISOU 1963 C ARG B 50 4455 2862 4048 509 -134 529 C -ATOM 1964 O ARG B 50 -2.117 15.127 -8.180 1.00 31.29 O -ANISOU 1964 O ARG B 50 4836 2891 4161 720 -165 563 O -ATOM 1965 CB ARG B 50 -0.180 14.068 -5.775 1.00 33.01 C -ANISOU 1965 CB ARG B 50 4994 3139 4412 477 -199 242 C -ATOM 1966 CG ARG B 50 -0.288 15.527 -5.339 1.00 48.99 C -ANISOU 1966 CG ARG B 50 7437 4822 6355 686 -336 149 C -ATOM 1967 CD ARG B 50 0.951 15.962 -4.587 1.00 57.12 C -ANISOU 1967 CD ARG B 50 8690 5570 7442 499 -542 -29 C -ATOM 1968 NE ARG B 50 2.087 16.140 -5.486 1.00 63.99 N -ANISOU 1968 NE ARG B 50 9488 6298 8528 30 -610 59 N -ATOM 1969 CZ ARG B 50 3.361 16.039 -5.121 1.00 66.17 C -ANISOU 1969 CZ ARG B 50 9704 6489 8950 -283 -748 -4 C -ATOM 1970 NH1 ARG B 50 3.679 15.744 -3.869 1.00 65.25 N -ANISOU 1970 NH1 ARG B 50 9646 6375 8770 -174 -873 -206 N -ATOM 1971 NH2 ARG B 50 4.320 16.226 -6.014 1.00 66.02 N -ANISOU 1971 NH2 ARG B 50 9545 6408 9131 -678 -754 164 N -ATOM 1972 N ASP B 51 -0.867 13.398 -8.868 1.00 27.52 N -ANISOU 1972 N ASP B 51 4032 2620 3806 246 -127 588 N -ATOM 1973 CA ASP B 51 -0.943 13.816 -10.278 1.00 27.47 C -ANISOU 1973 CA ASP B 51 4130 2521 3787 210 -139 713 C -ATOM 1974 C ASP B 51 -2.375 13.739 -10.816 1.00 26.16 C -ANISOU 1974 C ASP B 51 3890 2473 3577 452 -188 810 C -ATOM 1975 O ASP B 51 -2.811 14.599 -11.579 1.00 30.98 O -ANISOU 1975 O ASP B 51 4684 2951 4137 584 -218 880 O -ATOM 1976 CB ASP B 51 -0.042 12.941 -11.163 1.00 32.95 C -ANISOU 1976 CB ASP B 51 4732 3311 4478 -1 -104 770 C -ATOM 1977 CG ASP B 51 1.435 13.053 -10.813 1.00 36.27 C -ANISOU 1977 CG ASP B 51 5143 3672 4965 -243 -47 741 C -ATOM 1978 OD1 ASP B 51 1.838 14.048 -10.177 1.00 38.90 O -ANISOU 1978 OD1 ASP B 51 5611 3789 5380 -319 -89 697 O -ATOM 1979 OD2 ASP B 51 2.190 12.124 -11.183 1.00 37.95 O -ANISOU 1979 OD2 ASP B 51 5224 4052 5144 -340 7 768 O -ATOM 1980 N VAL B 52 -3.103 12.693 -10.434 1.00 27.27 N -ANISOU 1980 N VAL B 52 3745 2862 3755 496 -217 841 N -ATOM 1981 CA VAL B 52 -4.497 12.551 -10.875 1.00 30.10 C -ANISOU 1981 CA VAL B 52 3931 3370 4136 681 -311 979 C -ATOM 1982 C VAL B 52 -5.336 13.707 -10.370 1.00 30.95 C -ANISOU 1982 C VAL B 52 4113 3465 4181 1021 -251 1011 C -ATOM 1983 O VAL B 52 -6.105 14.329 -11.122 1.00 33.42 O -ANISOU 1983 O VAL B 52 4488 3755 4453 1217 -321 1093 O -ATOM 1984 CB VAL B 52 -5.101 11.221 -10.364 1.00 32.56 C -ANISOU 1984 CB VAL B 52 3874 3939 4560 601 -368 1069 C -ATOM 1985 CG1 VAL B 52 -6.616 11.218 -10.516 1.00 28.57 C -ANISOU 1985 CG1 VAL B 52 3082 3631 4140 786 -462 1272 C -ATOM 1986 CG2 VAL B 52 -4.477 10.043 -11.093 1.00 36.27 C -ANISOU 1986 CG2 VAL B 52 4356 4381 5045 341 -511 1038 C -ATOM 1987 N AMET B 53 -5.173 13.998 -9.084 0.48 31.13 N -ANISOU 1987 N AMET B 53 4175 3497 4155 1152 -136 934 N -ATOM 1988 N BMET B 53 -5.199 14.025 -9.092 0.52 31.35 N -ANISOU 1988 N BMET B 53 4205 3524 4181 1160 -136 936 N -ATOM 1989 CA AMET B 53 -5.864 15.116 -8.438 0.48 37.00 C -ANISOU 1989 CA AMET B 53 5089 4209 4759 1578 -78 933 C -ATOM 1990 CA BMET B 53 -5.983 15.131 -8.546 0.52 36.59 C -ANISOU 1990 CA BMET B 53 5021 4172 4709 1595 -84 951 C -ATOM 1991 C AMET B 53 -5.572 16.446 -9.123 0.48 37.86 C -ANISOU 1991 C AMET B 53 5648 3959 4776 1652 -159 862 C -ATOM 1992 C BMET B 53 -5.580 16.491 -9.119 0.52 37.93 C -ANISOU 1992 C BMET B 53 5670 3961 4781 1663 -160 861 C -ATOM 1993 O AMET B 53 -6.466 17.270 -9.323 0.48 39.64 O -ANISOU 1993 O AMET B 53 5997 4177 4889 2018 -175 924 O -ATOM 1994 O BMET B 53 -6.420 17.381 -9.255 0.52 39.82 O -ANISOU 1994 O BMET B 53 6065 4169 4897 2036 -175 909 O -ATOM 1995 CB AMET B 53 -5.458 15.201 -6.962 0.48 39.68 C -ANISOU 1995 CB AMET B 53 5538 4539 5000 1723 16 810 C -ATOM 1996 CB BMET B 53 -5.968 15.125 -7.014 0.52 38.59 C -ANISOU 1996 CB BMET B 53 5283 4518 4860 1828 41 889 C -ATOM 1997 CG AMET B 53 -5.883 16.492 -6.275 0.48 46.98 C -ANISOU 1997 CG AMET B 53 6836 5318 5698 2220 26 740 C -ATOM 1998 CG BMET B 53 -6.761 13.967 -6.406 0.52 37.79 C -ANISOU 1998 CG BMET B 53 4684 4839 4834 1881 163 1089 C -ATOM 1999 SD AMET B 53 -7.613 16.507 -5.768 0.48 45.73 S -ANISOU 1999 SD AMET B 53 6355 5618 5402 2836 207 992 S -ATOM 2000 SD BMET B 53 -8.491 13.876 -6.948 0.52 43.35 S -ANISOU 2000 SD BMET B 53 4934 5920 5618 2145 175 1427 S -ATOM 2001 CE AMET B 53 -7.514 15.668 -4.188 0.48 38.40 C -ANISOU 2001 CE AMET B 53 5237 4961 4392 2933 401 999 C -ATOM 2002 CE BMET B 53 -9.216 15.237 -6.046 0.52 62.25 C -ANISOU 2002 CE BMET B 53 7584 8369 7698 2781 341 1395 C -ATOM 2003 N LYS B 54 -4.309 16.651 -9.475 1.00 36.31 N -ANISOU 2003 N LYS B 54 5684 3476 4634 1310 -206 768 N -ATOM 2004 CA LYS B 54 -3.879 17.893 -10.129 1.00 39.15 C -ANISOU 2004 CA LYS B 54 6475 3451 4951 1286 -284 759 C -ATOM 2005 C LYS B 54 -4.577 18.052 -11.475 1.00 42.41 C -ANISOU 2005 C LYS B 54 6886 3900 5328 1384 -307 904 C -ATOM 2006 O LYS B 54 -4.918 19.156 -11.885 1.00 42.57 O -ANISOU 2006 O LYS B 54 7245 3686 5242 1597 -361 932 O -ATOM 2007 CB LYS B 54 -2.355 17.919 -10.326 1.00 39.27 C -ANISOU 2007 CB LYS B 54 6596 3233 5091 834 -306 730 C -ATOM 2008 CG LYS B 54 -1.813 19.129 -11.114 1.00 50.72 C -ANISOU 2008 CG LYS B 54 8437 4280 6556 707 -374 817 C -ATOM 2009 CD LYS B 54 -1.216 20.186 -10.193 1.00 59.46 C -ANISOU 2009 CD LYS B 54 9931 4974 7688 659 -547 700 C -ATOM 2010 CE LYS B 54 -0.028 20.914 -10.831 1.00 65.70 C -ANISOU 2010 CE LYS B 54 10888 5426 8647 223 -611 842 C -ATOM 2011 NZ LYS B 54 -0.390 21.708 -12.034 1.00 70.36 N -ANISOU 2011 NZ LYS B 54 11620 5936 9178 283 -553 1002 N -ATOM 2012 N GLU B 55 -4.829 16.936 -12.146 1.00 40.19 N -ANISOU 2012 N GLU B 55 6270 3887 5113 1263 -307 985 N -ATOM 2013 CA AGLU B 55 -5.354 16.978 -13.503 0.51 44.42 C -ANISOU 2013 CA AGLU B 55 6847 4432 5599 1343 -387 1098 C -ATOM 2014 CA BGLU B 55 -5.355 16.969 -13.509 0.49 44.40 C -ANISOU 2014 CA BGLU B 55 6842 4431 5597 1342 -388 1099 C -ATOM 2015 C GLU B 55 -6.874 16.791 -13.589 1.00 45.27 C -ANISOU 2015 C GLU B 55 6696 4807 5696 1668 -486 1184 C -ATOM 2016 O GLU B 55 -7.534 17.408 -14.428 1.00 47.22 O -ANISOU 2016 O GLU B 55 7092 4999 5851 1904 -576 1251 O -ATOM 2017 CB AGLU B 55 -4.629 15.936 -14.356 0.51 44.31 C -ANISOU 2017 CB AGLU B 55 6731 4485 5622 1055 -403 1130 C -ATOM 2018 CB BGLU B 55 -4.647 15.914 -14.370 0.49 44.33 C -ANISOU 2018 CB BGLU B 55 6727 4492 5624 1057 -406 1131 C -ATOM 2019 CG AGLU B 55 -4.882 16.052 -15.845 0.51 49.27 C -ANISOU 2019 CG AGLU B 55 7536 5051 6134 1161 -492 1229 C -ATOM 2020 CG BGLU B 55 -5.244 15.720 -15.760 0.49 47.97 C -ANISOU 2020 CG BGLU B 55 7250 4982 5994 1192 -547 1224 C -ATOM 2021 CD AGLU B 55 -3.838 15.316 -16.668 0.51 53.07 C -ANISOU 2021 CD AGLU B 55 8078 5530 6556 962 -448 1265 C -ATOM 2022 CD BGLU B 55 -5.079 16.938 -16.652 0.49 50.01 C -ANISOU 2022 CD BGLU B 55 7920 4970 6111 1330 -504 1302 C -ATOM 2023 OE1AGLU B 55 -2.747 15.031 -16.130 0.51 49.67 O -ANISOU 2023 OE1AGLU B 55 7583 5101 6189 718 -309 1234 O -ATOM 2024 OE1BGLU B 55 -3.962 17.496 -16.694 0.49 48.96 O -ANISOU 2024 OE1BGLU B 55 8007 4622 5973 1140 -353 1341 O -ATOM 2025 OE2AGLU B 55 -4.108 15.032 -17.855 0.51 59.46 O -ANISOU 2025 OE2AGLU B 55 9016 6347 7229 1101 -560 1325 O -ATOM 2026 OE2BGLU B 55 -6.065 17.334 -17.314 0.49 53.65 O -ANISOU 2026 OE2BGLU B 55 8442 5452 6489 1593 -628 1336 O -ATOM 2027 N MET B 56 -7.432 15.958 -12.714 1.00 43.11 N -ANISOU 2027 N MET B 56 6015 4838 5525 1684 -469 1217 N -ATOM 2028 CA MET B 56 -8.850 15.591 -12.811 1.00 48.45 C -ANISOU 2028 CA MET B 56 6301 5838 6269 1909 -575 1383 C -ATOM 2029 C MET B 56 -9.778 16.099 -11.708 1.00 55.58 C -ANISOU 2029 C MET B 56 7022 6977 7120 2320 -437 1474 C -ATOM 2030 O MET B 56 -10.991 15.888 -11.775 1.00 61.17 O -ANISOU 2030 O MET B 56 7344 7995 7904 2456 -491 1625 O -ATOM 2031 CB MET B 56 -8.996 14.070 -12.898 1.00 47.64 C -ANISOU 2031 CB MET B 56 5785 5950 6365 1597 -709 1466 C -ATOM 2032 CG MET B 56 -8.129 13.412 -13.939 1.00 46.63 C -ANISOU 2032 CG MET B 56 5860 5632 6227 1294 -854 1377 C -ATOM 2033 SD MET B 56 -8.517 11.668 -14.032 1.00 44.96 S -ANISOU 2033 SD MET B 56 5259 5604 6221 1001 -1121 1470 S -ATOM 2034 CE MET B 56 -10.153 11.728 -14.776 1.00 46.19 C -ANISOU 2034 CE MET B 56 5117 5933 6500 1191 -1449 1674 C -ATOM 2035 N GLY B 57 -9.223 16.749 -10.693 1.00 59.09 N -ANISOU 2035 N GLY B 57 9238 5007 8205 227 -904 1087 N -ATOM 2036 CA GLY B 57 -10.034 17.286 -9.614 1.00 66.33 C -ANISOU 2036 CA GLY B 57 10101 5758 9343 451 -851 949 C -ATOM 2037 C GLY B 57 -9.962 18.800 -9.542 1.00 75.36 C -ANISOU 2037 C GLY B 57 11523 6606 10504 458 -796 964 C -ATOM 2038 O GLY B 57 -8.872 19.375 -9.565 1.00 80.02 O -ANISOU 2038 O GLY B 57 12327 7119 10957 177 -704 981 O -ATOM 2039 N GLY B 58 -11.117 19.448 -9.414 1.00 78.08 N -ANISOU 2039 N GLY B 58 11842 6799 11027 771 -842 945 N -ATOM 2040 CA GLY B 58 -12.351 18.737 -9.149 1.00 73.74 C -ANISOU 2040 CA GLY B 58 10977 6394 10648 1066 -904 871 C -ATOM 2041 C GLY B 58 -13.558 18.960 -10.048 1.00 71.13 C -ANISOU 2041 C GLY B 58 10561 6077 10387 1359 -1075 975 C -ATOM 2042 O GLY B 58 -14.225 20.002 -9.996 1.00 70.21 O -ANISOU 2042 O GLY B 58 10538 5754 10383 1569 -1084 984 O -ATOM 2043 N HIS B 59 -13.807 17.969 -10.900 1.00 63.82 N -ANISOU 2043 N HIS B 59 9462 5400 9387 1360 -1217 1051 N -ATOM 2044 CA HIS B 59 -15.155 17.598 -11.281 1.00 64.21 C -ANISOU 2044 CA HIS B 59 9241 5602 9554 1637 -1355 1043 C -ATOM 2045 C HIS B 59 -15.303 16.197 -10.691 1.00 56.47 C -ANISOU 2045 C HIS B 59 7923 4897 8637 1584 -1306 906 C -ATOM 2046 O HIS B 59 -14.332 15.629 -10.194 1.00 52.40 O -ANISOU 2046 O HIS B 59 7432 4423 8057 1357 -1200 863 O -ATOM 2047 CB HIS B 59 -15.352 17.575 -12.798 1.00 77.68 C -ANISOU 2047 CB HIS B 59 11025 7380 11111 1653 -1565 1229 C -ATOM 2048 CG HIS B 59 -16.765 17.295 -13.219 1.00 90.88 C -ANISOU 2048 CG HIS B 59 12421 9210 12899 1929 -1723 1217 C -ATOM 2049 ND1 HIS B 59 -17.857 17.783 -12.528 1.00 96.89 N -ANISOU 2049 ND1 HIS B 59 13011 9922 13883 2212 -1692 1113 N -ATOM 2050 CD2 HIS B 59 -17.267 16.575 -14.250 1.00 94.74 C -ANISOU 2050 CD2 HIS B 59 12766 9924 13308 1953 -1906 1281 C -ATOM 2051 CE1 HIS B 59 -18.968 17.376 -13.118 1.00 99.83 C -ANISOU 2051 CE1 HIS B 59 13128 10492 14311 2392 -1854 1120 C -ATOM 2052 NE2 HIS B 59 -18.639 16.645 -14.166 1.00 98.76 N -ANISOU 2052 NE2 HIS B 59 13010 10520 13994 2236 -1992 1219 N -ATOM 2053 N HIS B 60 -16.511 15.657 -10.716 1.00 53.49 N -ANISOU 2053 N HIS B 60 7226 4706 8391 1780 -1375 836 N -ATOM 2054 CA HIS B 60 -16.760 14.300 -10.267 1.00 50.20 C -ANISOU 2054 CA HIS B 60 6477 4557 8039 1713 -1328 714 C -ATOM 2055 C HIS B 60 -15.969 13.330 -11.146 1.00 37.34 C -ANISOU 2055 C HIS B 60 4884 3078 6225 1482 -1419 816 C -ATOM 2056 O HIS B 60 -15.945 13.479 -12.366 1.00 51.42 O -ANISOU 2056 O HIS B 60 6797 4878 7864 1470 -1582 958 O -ATOM 2057 CB HIS B 60 -18.261 14.020 -10.384 1.00 57.94 C -ANISOU 2057 CB HIS B 60 7129 5717 9168 1936 -1404 639 C -ATOM 2058 CG HIS B 60 -18.664 12.653 -9.936 1.00 61.38 C -ANISOU 2058 CG HIS B 60 7218 6424 9679 1848 -1335 506 C -ATOM 2059 ND1 HIS B 60 -18.265 11.504 -10.586 1.00 60.61 N -ANISOU 2059 ND1 HIS B 60 7057 6504 9468 1657 -1410 551 N -ATOM 2060 CD2 HIS B 60 -19.448 12.247 -8.906 1.00 63.78 C -ANISOU 2060 CD2 HIS B 60 7233 6849 10151 1910 -1180 328 C -ATOM 2061 CE1 HIS B 60 -18.771 10.452 -9.969 1.00 56.28 C -ANISOU 2061 CE1 HIS B 60 6207 6153 9023 1600 -1306 412 C -ATOM 2062 NE2 HIS B 60 -19.491 10.875 -8.949 1.00 60.98 N -ANISOU 2062 NE2 HIS B 60 6659 6725 9784 1740 -1160 279 N -ATOM 2063 N AILE B 61 -15.298 12.359 -10.545 0.36 34.25 N -ANISOU 2063 N AILE B 61 4395 2794 5825 1303 -1306 748 N -ATOM 2064 N BILE B 61 -15.345 12.333 -10.513 0.64 34.25 N -ANISOU 2064 N BILE B 61 4380 2801 5834 1308 -1303 741 N -ATOM 2065 CA AILE B 61 -14.674 11.345 -11.373 0.36 32.60 C -ANISOU 2065 CA AILE B 61 4187 2751 5450 1114 -1386 831 C -ATOM 2066 CA BILE B 61 -14.572 11.299 -11.200 0.64 33.75 C -ANISOU 2066 CA BILE B 61 4327 2892 5604 1098 -1359 818 C -ATOM 2067 C AILE B 61 -15.293 9.982 -11.122 0.36 35.42 C -ANISOU 2067 C AILE B 61 4203 3359 5896 1099 -1360 717 C -ATOM 2068 C BILE B 61 -15.264 9.942 -11.082 0.64 36.52 C -ANISOU 2068 C BILE B 61 4338 3504 6033 1091 -1350 712 C -ATOM 2069 O AILE B 61 -15.713 9.655 -10.008 0.36 35.83 O -ANISOU 2069 O AILE B 61 4055 3465 6093 1130 -1193 567 O -ATOM 2070 O BILE B 61 -15.688 9.559 -9.989 0.64 35.81 O -ANISOU 2070 O BILE B 61 4043 3478 6085 1116 -1184 562 O -ATOM 2071 CB AILE B 61 -13.125 11.301 -11.253 0.36 37.56 C -ANISOU 2071 CB AILE B 61 5040 3364 5868 838 -1245 870 C -ATOM 2072 CB BILE B 61 -13.151 11.164 -10.589 0.64 35.54 C -ANISOU 2072 CB BILE B 61 4705 3128 5670 837 -1146 788 C -ATOM 2073 CG1AILE B 61 -12.668 10.151 -10.354 0.36 34.08 C -ANISOU 2073 CG1AILE B 61 4412 3131 5403 688 -1044 730 C -ATOM 2074 CG1BILE B 61 -12.318 12.416 -10.870 0.64 42.56 C -ANISOU 2074 CG1BILE B 61 5947 3776 6447 761 -1154 900 C -ATOM 2075 CG2AILE B 61 -12.566 12.663 -10.809 0.36 43.41 C -ANISOU 2075 CG2AILE B 61 6062 3829 6605 825 -1174 899 C -ATOM 2076 CG2BILE B 61 -12.431 9.945 -11.133 0.64 34.27 C -ANISOU 2076 CG2BILE B 61 4495 3203 5323 631 -1127 806 C -ATOM 2077 CD1AILE B 61 -11.172 9.915 -10.373 0.36 32.74 C -ANISOU 2077 CD1AILE B 61 4396 3030 5014 434 -928 753 C -ATOM 2078 CD1BILE B 61 -11.055 12.512 -10.028 0.64 41.25 C -ANISOU 2078 CD1BILE B 61 5886 3616 6172 526 -940 827 C -ATOM 2079 N VAL B 62 -15.381 9.210 -12.193 1.00 35.18 N -ANISOU 2079 N VAL B 62 4132 3491 5745 1027 -1502 775 N -ATOM 2080 CA VAL B 62 -15.786 7.810 -12.115 1.00 29.59 C -ANISOU 2080 CA VAL B 62 3159 3009 5073 947 -1474 675 C -ATOM 2081 C VAL B 62 -14.521 7.015 -12.343 1.00 28.62 C -ANISOU 2081 C VAL B 62 3180 2977 4719 702 -1369 697 C -ATOM 2082 O VAL B 62 -13.870 7.164 -13.373 1.00 31.09 O -ANISOU 2082 O VAL B 62 3693 3284 4837 621 -1472 814 O -ATOM 2083 CB VAL B 62 -16.842 7.444 -13.171 1.00 31.59 C -ANISOU 2083 CB VAL B 62 3279 3414 5311 1007 -1660 673 C -ATOM 2084 CG1 VAL B 62 -17.212 5.961 -13.061 1.00 36.97 C -ANISOU 2084 CG1 VAL B 62 3716 4301 6030 880 -1619 557 C -ATOM 2085 CG2 VAL B 62 -18.075 8.313 -12.988 1.00 36.27 C -ANISOU 2085 CG2 VAL B 62 3746 3970 6066 1239 -1706 630 C -ATOM 2086 N ALA B 63 -14.144 6.198 -11.369 1.00 25.55 N -ANISOU 2086 N ALA B 63 2700 2670 4340 592 -1157 587 N -ATOM 2087 CA ALA B 63 -12.943 5.408 -11.498 1.00 24.20 C -ANISOU 2087 CA ALA B 63 2638 2588 3967 403 -1057 593 C -ATOM 2088 C ALA B 63 -13.362 4.038 -11.956 1.00 33.94 C -ANISOU 2088 C ALA B 63 3732 3978 5184 340 -1095 537 C -ATOM 2089 O ALA B 63 -14.202 3.389 -11.324 1.00 31.02 O -ANISOU 2089 O ALA B 63 3163 3661 4963 360 -1034 436 O -ATOM 2090 CB ALA B 63 -12.193 5.321 -10.194 1.00 25.49 C -ANISOU 2090 CB ALA B 63 2820 2739 4124 337 -832 518 C -ATOM 2091 N LEU B 64 -12.765 3.607 -13.064 1.00 26.55 N -ANISOU 2091 N LEU B 64 2919 3113 4057 245 -1182 594 N -ATOM 2092 CA ALEU B 64 -13.133 2.355 -13.693 0.65 26.32 C -ANISOU 2092 CA ALEU B 64 2804 3211 3987 175 -1241 535 C -ATOM 2093 CA BLEU B 64 -13.114 2.344 -13.708 0.35 26.89 C -ANISOU 2093 CA BLEU B 64 2879 3284 4055 173 -1241 536 C -ATOM 2094 C LEU B 64 -12.012 1.339 -13.486 1.00 25.73 C -ANISOU 2094 C LEU B 64 2811 3199 3767 49 -1078 487 C -ATOM 2095 O LEU B 64 -10.901 1.516 -13.981 1.00 26.95 O -ANISOU 2095 O LEU B 64 3128 3374 3739 -13 -1052 539 O -ATOM 2096 CB ALEU B 64 -13.400 2.621 -15.180 0.65 30.41 C -ANISOU 2096 CB ALEU B 64 3409 3763 4381 185 -1480 622 C -ATOM 2097 CB BLEU B 64 -13.261 2.530 -15.217 0.35 30.53 C -ANISOU 2097 CB BLEU B 64 3441 3787 4372 167 -1467 621 C -ATOM 2098 CG ALEU B 64 -13.967 1.565 -16.114 0.65 33.03 C -ANISOU 2098 CG ALEU B 64 3672 4224 4654 119 -1615 564 C -ATOM 2099 CG BLEU B 64 -14.491 3.159 -15.850 0.35 32.84 C -ANISOU 2099 CG BLEU B 64 3645 4069 4765 303 -1715 669 C -ATOM 2100 CD1ALEU B 64 -15.052 0.782 -15.410 0.65 32.63 C -ANISOU 2100 CD1ALEU B 64 3358 4221 4819 121 -1579 432 C -ATOM 2101 CD1BLEU B 64 -14.638 2.639 -17.275 0.35 36.66 C -ANISOU 2101 CD1BLEU B 64 4200 4665 5066 236 -1910 694 C -ATOM 2102 CD2ALEU B 64 -14.532 2.249 -17.355 0.65 37.64 C -ANISOU 2102 CD2ALEU B 64 4320 4822 5158 190 -1894 667 C -ATOM 2103 CD2BLEU B 64 -15.725 2.859 -15.034 0.35 33.80 C -ANISOU 2103 CD2BLEU B 64 3468 4222 5152 384 -1700 553 C -ATOM 2104 N CYS B 65 -12.308 0.275 -12.747 1.00 25.64 N -ANISOU 2104 N CYS B 65 2687 3216 3837 14 -962 385 N -ATOM 2105 CA CYS B 65 -11.306 -0.753 -12.474 1.00 27.57 C -ANISOU 2105 CA CYS B 65 3017 3498 3961 -62 -819 339 C -ATOM 2106 C CYS B 65 -11.305 -1.856 -13.534 1.00 29.12 C -ANISOU 2106 C CYS B 65 3259 3760 4044 -138 -890 293 C -ATOM 2107 O CYS B 65 -12.324 -2.518 -13.752 1.00 27.12 O -ANISOU 2107 O CYS B 65 2906 3519 3879 -175 -955 229 O -ATOM 2108 CB CYS B 65 -11.558 -1.383 -11.108 1.00 27.07 C -ANISOU 2108 CB CYS B 65 2873 3400 4012 -62 -652 268 C -ATOM 2109 SG CYS B 65 -10.352 -2.674 -10.721 1.00 27.87 S -ANISOU 2109 SG CYS B 65 3101 3520 3967 -103 -505 227 S -ATOM 2110 N VAL B 66 -10.174 -2.053 -14.209 1.00 27.16 N -ANISOU 2110 N VAL B 66 3155 3563 3599 -172 -870 309 N -ATOM 2111 CA VAL B 66 -10.106 -3.149 -15.169 1.00 24.80 C -ANISOU 2111 CA VAL B 66 2925 3318 3182 -237 -911 240 C -ATOM 2112 C VAL B 66 -9.673 -4.426 -14.458 1.00 24.80 C -ANISOU 2112 C VAL B 66 2949 3283 3189 -242 -754 149 C -ATOM 2113 O VAL B 66 -8.496 -4.580 -14.093 1.00 24.35 O -ANISOU 2113 O VAL B 66 2961 3248 3042 -200 -634 149 O -ATOM 2114 CB VAL B 66 -9.176 -2.856 -16.355 1.00 31.59 C -ANISOU 2114 CB VAL B 66 3931 4260 3810 -271 -953 279 C -ATOM 2115 CG1 VAL B 66 -9.308 -3.966 -17.373 1.00 30.33 C -ANISOU 2115 CG1 VAL B 66 3844 4149 3531 -335 -1006 185 C -ATOM 2116 CG2 VAL B 66 -9.533 -1.516 -17.003 1.00 30.36 C -ANISOU 2116 CG2 VAL B 66 3807 4103 3625 -263 -1107 401 C -ATOM 2117 N LEU B 67 -10.640 -5.326 -14.259 1.00 24.25 N -ANISOU 2117 N LEU B 67 2824 3161 3229 -294 -760 73 N -ATOM 2118 CA LEU B 67 -10.440 -6.588 -13.542 1.00 25.13 C -ANISOU 2118 CA LEU B 67 2997 3190 3361 -308 -616 0 C -ATOM 2119 C LEU B 67 -9.775 -7.612 -14.468 1.00 28.79 C -ANISOU 2119 C LEU B 67 3618 3657 3663 -328 -614 -79 C -ATOM 2120 O LEU B 67 -9.836 -7.452 -15.689 1.00 27.39 O -ANISOU 2120 O LEU B 67 3475 3557 3377 -373 -734 -98 O -ATOM 2121 CB LEU B 67 -11.789 -7.108 -13.036 1.00 21.10 C -ANISOU 2121 CB LEU B 67 2378 2612 3025 -401 -610 -54 C -ATOM 2122 CG LEU B 67 -12.481 -6.285 -11.945 1.00 26.60 C -ANISOU 2122 CG LEU B 67 2913 3300 3893 -372 -561 -9 C -ATOM 2123 CD1 LEU B 67 -13.867 -6.835 -11.664 1.00 28.30 C -ANISOU 2123 CD1 LEU B 67 2986 3494 4275 -493 -551 -86 C -ATOM 2124 CD2 LEU B 67 -11.646 -6.258 -10.666 1.00 27.32 C -ANISOU 2124 CD2 LEU B 67 3079 3337 3964 -296 -389 33 C -ATOM 2125 N LYS B 68 -9.128 -8.646 -13.920 1.00 24.05 N -ANISOU 2125 N LYS B 68 3134 2973 3032 -281 -480 -127 N -ATOM 2126 CA LYS B 68 -8.931 -8.835 -12.482 1.00 26.70 C -ANISOU 2126 CA LYS B 68 3470 3225 3450 -216 -348 -88 C -ATOM 2127 C LYS B 68 -7.671 -8.140 -12.014 1.00 24.04 C -ANISOU 2127 C LYS B 68 3126 2976 3034 -87 -295 -25 C -ATOM 2128 O LYS B 68 -7.582 -7.696 -10.870 1.00 25.15 O -ANISOU 2128 O LYS B 68 3219 3103 3233 -43 -232 31 O -ATOM 2129 CB LYS B 68 -8.774 -10.325 -12.170 1.00 25.18 C -ANISOU 2129 CB LYS B 68 3448 2881 3239 -208 -251 -157 C -ATOM 2130 CG LYS B 68 -9.941 -11.213 -12.531 1.00 27.53 C -ANISOU 2130 CG LYS B 68 3782 3067 3612 -375 -275 -242 C -ATOM 2131 CD LYS B 68 -9.768 -12.550 -11.808 1.00 32.88 C -ANISOU 2131 CD LYS B 68 4664 3540 4290 -364 -142 -273 C -ATOM 2132 CE LYS B 68 -10.414 -13.685 -12.535 1.00 33.59 C -ANISOU 2132 CE LYS B 68 4882 3498 4382 -518 -159 -395 C -ATOM 2133 NZ LYS B 68 -10.104 -14.982 -11.847 1.00 33.18 N -ANISOU 2133 NZ LYS B 68 5090 3201 4314 -484 -24 -412 N -ATOM 2134 N GLY B 69 -6.687 -8.069 -12.901 1.00 23.57 N -ANISOU 2134 N GLY B 69 3109 3018 2827 -40 -313 -48 N -ATOM 2135 CA GLY B 69 -5.360 -7.593 -12.546 1.00 26.89 C -ANISOU 2135 CA GLY B 69 3507 3549 3162 64 -253 -19 C -ATOM 2136 C GLY B 69 -5.253 -6.174 -12.010 1.00 27.06 C -ANISOU 2136 C GLY B 69 3418 3643 3222 42 -268 69 C -ATOM 2137 O GLY B 69 -4.309 -5.842 -11.281 1.00 30.11 O -ANISOU 2137 O GLY B 69 3767 4099 3573 110 -209 87 O -ATOM 2138 N GLY B 70 -6.201 -5.318 -12.366 1.00 24.85 N -ANISOU 2138 N GLY B 70 3086 3344 3013 -46 -356 117 N -ATOM 2139 CA GLY B 70 -6.100 -3.934 -11.936 1.00 22.35 C -ANISOU 2139 CA GLY B 70 2703 3059 2731 -61 -369 193 C -ATOM 2140 C GLY B 70 -6.595 -3.714 -10.516 1.00 23.35 C -ANISOU 2140 C GLY B 70 2775 3105 2992 -30 -311 210 C -ATOM 2141 O GLY B 70 -6.468 -2.605 -9.998 1.00 23.37 O -ANISOU 2141 O GLY B 70 2740 3115 3026 -34 -305 253 O -ATOM 2142 N TYR B 71 -7.136 -4.751 -9.877 1.00 22.29 N -ANISOU 2142 N TYR B 71 2659 2887 2922 -12 -255 173 N -ATOM 2143 CA TYR B 71 -7.856 -4.541 -8.611 1.00 21.75 C -ANISOU 2143 CA TYR B 71 2545 2745 2976 -12 -187 185 C -ATOM 2144 C TYR B 71 -6.977 -3.974 -7.490 1.00 21.30 C -ANISOU 2144 C TYR B 71 2496 2728 2868 45 -116 210 C -ATOM 2145 O TYR B 71 -7.435 -3.155 -6.688 1.00 22.21 O -ANISOU 2145 O TYR B 71 2563 2815 3060 35 -83 222 O -ATOM 2146 CB TYR B 71 -8.620 -5.814 -8.159 1.00 25.98 C -ANISOU 2146 CB TYR B 71 3125 3175 3571 -45 -118 146 C -ATOM 2147 CG TYR B 71 -7.966 -6.603 -7.028 1.00 25.96 C -ANISOU 2147 CG TYR B 71 3239 3125 3501 23 -6 156 C -ATOM 2148 CD1 TYR B 71 -8.144 -6.240 -5.699 1.00 25.04 C -ANISOU 2148 CD1 TYR B 71 3117 2986 3412 33 83 184 C -ATOM 2149 CD2 TYR B 71 -7.195 -7.729 -7.301 1.00 25.80 C -ANISOU 2149 CD2 TYR B 71 3351 3073 3378 91 5 135 C -ATOM 2150 CE1 TYR B 71 -7.545 -6.966 -4.671 1.00 26.76 C -ANISOU 2150 CE1 TYR B 71 3468 3162 3536 102 162 209 C -ATOM 2151 CE2 TYR B 71 -6.591 -8.454 -6.287 1.00 26.53 C -ANISOU 2151 CE2 TYR B 71 3570 3111 3400 188 80 160 C -ATOM 2152 CZ TYR B 71 -6.765 -8.058 -4.975 1.00 27.36 C -ANISOU 2152 CZ TYR B 71 3676 3204 3515 189 149 206 C -ATOM 2153 OH TYR B 71 -6.176 -8.784 -3.958 1.00 27.76 O -ANISOU 2153 OH TYR B 71 3878 3201 3467 291 202 246 O -ATOM 2154 N LYS B 72 -5.730 -4.423 -7.397 1.00 20.45 N -ANISOU 2154 N LYS B 72 2443 2695 2633 112 -94 201 N -ATOM 2155 CA LYS B 72 -4.871 -3.954 -6.302 1.00 23.82 C -ANISOU 2155 CA LYS B 72 2864 3188 3000 161 -51 212 C -ATOM 2156 C LYS B 72 -4.443 -2.504 -6.523 1.00 23.97 C -ANISOU 2156 C LYS B 72 2817 3284 3007 98 -88 225 C -ATOM 2157 O LYS B 72 -4.584 -1.651 -5.639 1.00 21.95 O -ANISOU 2157 O LYS B 72 2546 3007 2786 74 -61 229 O -ATOM 2158 CB LYS B 72 -3.642 -4.849 -6.147 1.00 25.14 C -ANISOU 2158 CB LYS B 72 3074 3438 3040 274 -40 191 C -ATOM 2159 CG LYS B 72 -3.868 -6.050 -5.265 1.00 35.91 C -ANISOU 2159 CG LYS B 72 4556 4694 4393 359 12 202 C -ATOM 2160 CD LYS B 72 -4.199 -5.613 -3.859 1.00 41.63 C -ANISOU 2160 CD LYS B 72 5302 5388 5128 344 64 232 C -ATOM 2161 CE LYS B 72 -2.965 -5.140 -3.130 1.00 44.58 C -ANISOU 2161 CE LYS B 72 5640 5913 5384 417 34 228 C -ATOM 2162 NZ LYS B 72 -3.312 -4.725 -1.747 1.00 41.71 N -ANISOU 2162 NZ LYS B 72 5325 5521 5003 393 85 246 N -ATOM 2163 N PHE B 73 -3.918 -2.225 -7.708 1.00 20.94 N -ANISOU 2163 N PHE B 73 2417 2977 2562 58 -138 228 N -ATOM 2164 CA PHE B 73 -3.519 -0.870 -8.056 1.00 21.91 C -ANISOU 2164 CA PHE B 73 2519 3146 2662 -34 -165 254 C -ATOM 2165 C PHE B 73 -4.711 0.087 -7.903 1.00 24.16 C -ANISOU 2165 C PHE B 73 2813 3286 3079 -69 -196 292 C -ATOM 2166 O PHE B 73 -4.580 1.199 -7.380 1.00 20.07 O -ANISOU 2166 O PHE B 73 2305 2736 2583 -112 -184 299 O -ATOM 2167 CB PHE B 73 -2.976 -0.864 -9.490 1.00 20.29 C -ANISOU 2167 CB PHE B 73 2325 3028 2355 -89 -199 261 C -ATOM 2168 CG PHE B 73 -2.518 0.474 -9.968 1.00 22.61 C -ANISOU 2168 CG PHE B 73 2638 3354 2601 -214 -213 303 C -ATOM 2169 CD1 PHE B 73 -1.641 1.248 -9.211 1.00 21.49 C -ANISOU 2169 CD1 PHE B 73 2460 3279 2425 -277 -166 283 C -ATOM 2170 CD2 PHE B 73 -2.942 0.953 -11.204 1.00 26.22 C -ANISOU 2170 CD2 PHE B 73 3168 3768 3027 -285 -279 364 C -ATOM 2171 CE1 PHE B 73 -1.206 2.491 -9.679 1.00 23.55 C -ANISOU 2171 CE1 PHE B 73 2768 3543 2637 -430 -165 321 C -ATOM 2172 CE2 PHE B 73 -2.505 2.190 -11.684 1.00 29.85 C -ANISOU 2172 CE2 PHE B 73 3694 4225 3422 -417 -284 422 C -ATOM 2173 CZ PHE B 73 -1.633 2.955 -10.921 1.00 26.12 C -ANISOU 2173 CZ PHE B 73 3195 3799 2930 -499 -217 399 C -ATOM 2174 N PHE B 74 -5.883 -0.361 -8.330 1.00 20.86 N -ANISOU 2174 N PHE B 74 2386 2782 2756 -46 -238 301 N -ATOM 2175 CA PHE B 74 -7.098 0.445 -8.221 1.00 21.42 C -ANISOU 2175 CA PHE B 74 2426 2739 2974 -40 -278 322 C -ATOM 2176 C PHE B 74 -7.403 0.763 -6.749 1.00 20.98 C -ANISOU 2176 C PHE B 74 2345 2628 2998 -8 -180 285 C -ATOM 2177 O PHE B 74 -7.646 1.914 -6.392 1.00 22.73 O -ANISOU 2177 O PHE B 74 2574 2779 3282 -6 -179 289 O -ATOM 2178 CB PHE B 74 -8.249 -0.315 -8.894 1.00 19.99 C -ANISOU 2178 CB PHE B 74 2195 2524 2877 -28 -343 313 C -ATOM 2179 CG PHE B 74 -9.603 0.363 -8.788 1.00 23.04 C -ANISOU 2179 CG PHE B 74 2493 2826 3437 8 -394 317 C -ATOM 2180 CD1 PHE B 74 -9.992 1.319 -9.718 1.00 25.15 C -ANISOU 2180 CD1 PHE B 74 2770 3058 3729 27 -531 376 C -ATOM 2181 CD2 PHE B 74 -10.497 0.003 -7.792 1.00 23.02 C -ANISOU 2181 CD2 PHE B 74 2396 2784 3564 30 -303 260 C -ATOM 2182 CE1 PHE B 74 -11.249 1.926 -9.639 1.00 26.94 C -ANISOU 2182 CE1 PHE B 74 2892 3216 4129 105 -597 372 C -ATOM 2183 CE2 PHE B 74 -11.745 0.609 -7.705 1.00 28.46 C -ANISOU 2183 CE2 PHE B 74 2961 3426 4427 80 -340 241 C -ATOM 2184 CZ PHE B 74 -12.124 1.561 -8.640 1.00 26.71 C -ANISOU 2184 CZ PHE B 74 2727 3174 4248 135 -497 294 C -ATOM 2185 N ALA B 75 -7.380 -0.252 -5.889 1.00 18.66 N -ANISOU 2185 N ALA B 75 2051 2353 2687 17 -93 249 N -ATOM 2186 CA ALA B 75 -7.754 -0.042 -4.485 1.00 20.42 C -ANISOU 2186 CA ALA B 75 2272 2533 2956 35 13 213 C -ATOM 2187 C ALA B 75 -6.762 0.894 -3.801 1.00 21.43 C -ANISOU 2187 C ALA B 75 2447 2700 2995 18 33 199 C -ATOM 2188 O ALA B 75 -7.148 1.788 -3.048 1.00 22.43 O -ANISOU 2188 O ALA B 75 2580 2763 3179 16 82 164 O -ATOM 2189 CB ALA B 75 -7.847 -1.374 -3.745 1.00 22.27 C -ANISOU 2189 CB ALA B 75 2545 2768 3149 51 101 200 C -ATOM 2190 N ASP B 76 -5.484 0.694 -4.080 1.00 19.42 N -ANISOU 2190 N ASP B 76 2217 2559 2604 1 -2 209 N -ATOM 2191 CA ASP B 76 -4.433 1.493 -3.464 1.00 20.25 C -ANISOU 2191 CA ASP B 76 2342 2739 2613 -46 7 179 C -ATOM 2192 C ASP B 76 -4.418 2.909 -4.027 1.00 20.66 C -ANISOU 2192 C ASP B 76 2416 2725 2708 -132 -31 190 C -ATOM 2193 O ASP B 76 -4.289 3.870 -3.274 1.00 22.12 O -ANISOU 2193 O ASP B 76 2643 2866 2896 -179 1 147 O -ATOM 2194 CB ASP B 76 -3.064 0.832 -3.669 1.00 22.85 C -ANISOU 2194 CB ASP B 76 2643 3242 2795 -35 -22 172 C -ATOM 2195 CG ASP B 76 -2.902 -0.450 -2.875 1.00 27.00 C -ANISOU 2195 CG ASP B 76 3193 3808 3257 76 6 167 C -ATOM 2196 OD1 ASP B 76 -3.637 -0.633 -1.895 1.00 27.83 O -ANISOU 2196 OD1 ASP B 76 3353 3828 3393 101 66 164 O -ATOM 2197 OD2 ASP B 76 -2.013 -1.272 -3.217 1.00 26.04 O -ANISOU 2197 OD2 ASP B 76 3047 3801 3046 144 -26 165 O -ATOM 2198 N LEU B 77 -4.563 3.052 -5.347 1.00 18.48 N -ANISOU 2198 N LEU B 77 2142 2427 2451 -157 -100 247 N -ATOM 2199 CA LEU B 77 -4.565 4.378 -5.932 1.00 21.66 C -ANISOU 2199 CA LEU B 77 2616 2736 2879 -236 -142 283 C -ATOM 2200 C LEU B 77 -5.734 5.155 -5.369 1.00 25.16 C -ANISOU 2200 C LEU B 77 3086 2998 3475 -171 -130 269 C -ATOM 2201 O LEU B 77 -5.584 6.315 -4.969 1.00 23.70 O -ANISOU 2201 O LEU B 77 2986 2712 3308 -220 -111 247 O -ATOM 2202 CB LEU B 77 -4.649 4.330 -7.459 1.00 21.68 C -ANISOU 2202 CB LEU B 77 2645 2740 2853 -263 -226 363 C -ATOM 2203 CG LEU B 77 -4.758 5.682 -8.175 1.00 22.41 C -ANISOU 2203 CG LEU B 77 2862 2698 2955 -336 -283 435 C -ATOM 2204 CD1 LEU B 77 -3.463 6.504 -8.086 1.00 21.36 C -ANISOU 2204 CD1 LEU B 77 2797 2615 2702 -509 -231 423 C -ATOM 2205 CD2 LEU B 77 -5.109 5.426 -9.628 1.00 24.93 C -ANISOU 2205 CD2 LEU B 77 3217 3021 3233 -331 -383 521 C -ATOM 2206 N LEU B 78 -6.899 4.511 -5.310 1.00 21.83 N -ANISOU 2206 N LEU B 78 2590 2536 3169 -66 -130 265 N -ATOM 2207 CA LEU B 78 -8.068 5.179 -4.752 1.00 23.63 C -ANISOU 2207 CA LEU B 78 2797 2622 3557 19 -102 229 C -ATOM 2208 C LEU B 78 -7.880 5.503 -3.261 1.00 25.07 C -ANISOU 2208 C LEU B 78 3010 2792 3724 11 25 136 C -ATOM 2209 O LEU B 78 -8.361 6.527 -2.782 1.00 20.85 O -ANISOU 2209 O LEU B 78 2519 2125 3278 49 60 88 O -ATOM 2210 CB LEU B 78 -9.328 4.366 -4.990 1.00 21.32 C -ANISOU 2210 CB LEU B 78 2376 2333 3392 104 -117 225 C -ATOM 2211 CG LEU B 78 -10.127 4.820 -6.210 1.00 30.47 C -ANISOU 2211 CG LEU B 78 3505 3422 4648 166 -264 289 C -ATOM 2212 CD1 LEU B 78 -9.311 4.792 -7.500 1.00 34.75 C -ANISOU 2212 CD1 LEU B 78 4141 4011 5050 90 -378 381 C -ATOM 2213 CD2 LEU B 78 -11.401 4.004 -6.366 1.00 30.01 C -ANISOU 2213 CD2 LEU B 78 3278 3400 4725 228 -283 257 C -ATOM 2214 N ASP B 79 -7.161 4.659 -2.526 1.00 21.62 N -ANISOU 2214 N ASP B 79 2569 2484 3161 -28 87 106 N -ATOM 2215 CA ASP B 79 -6.915 4.977 -1.113 1.00 21.34 C -ANISOU 2215 CA ASP B 79 2586 2454 3068 -46 189 19 C -ATOM 2216 C ASP B 79 -6.052 6.225 -0.960 1.00 20.99 C -ANISOU 2216 C ASP B 79 2640 2373 2962 -142 169 -18 C -ATOM 2217 O ASP B 79 -6.298 7.047 -0.073 1.00 23.37 O -ANISOU 2217 O ASP B 79 3011 2583 3287 -147 239 -104 O -ATOM 2218 CB ASP B 79 -6.295 3.798 -0.359 1.00 22.86 C -ANISOU 2218 CB ASP B 79 2777 2794 3115 -50 231 12 C -ATOM 2219 CG ASP B 79 -7.333 2.823 0.130 1.00 29.48 C -ANISOU 2219 CG ASP B 79 3579 3610 4010 12 321 10 C -ATOM 2220 OD1 ASP B 79 -8.521 3.200 0.148 1.00 35.30 O -ANISOU 2220 OD1 ASP B 79 4262 4247 4902 49 376 -21 O -ATOM 2221 OD2 ASP B 79 -6.962 1.690 0.498 1.00 32.04 O -ANISOU 2221 OD2 ASP B 79 3933 4014 4228 24 341 38 O -ATOM 2222 N TYR B 80 -5.055 6.368 -1.825 1.00 22.27 N -ANISOU 2222 N TYR B 80 2816 2605 3042 -235 88 34 N -ATOM 2223 CA TYR B 80 -4.210 7.555 -1.794 1.00 21.32 C -ANISOU 2223 CA TYR B 80 2791 2446 2862 -376 75 0 C -ATOM 2224 C TYR B 80 -4.976 8.794 -2.223 1.00 22.64 C -ANISOU 2224 C TYR B 80 3073 2367 3164 -359 61 18 C -ATOM 2225 O TYR B 80 -4.756 9.861 -1.668 1.00 22.70 O -ANISOU 2225 O TYR B 80 3200 2255 3168 -435 97 -52 O -ATOM 2226 CB TYR B 80 -2.948 7.385 -2.652 1.00 21.64 C -ANISOU 2226 CB TYR B 80 2798 2645 2777 -504 17 45 C -ATOM 2227 CG TYR B 80 -1.849 6.591 -1.974 1.00 23.05 C -ANISOU 2227 CG TYR B 80 2882 3068 2809 -532 23 -12 C -ATOM 2228 CD1 TYR B 80 -1.185 7.099 -0.865 1.00 24.88 C -ANISOU 2228 CD1 TYR B 80 3137 3363 2952 -622 44 -115 C -ATOM 2229 CD2 TYR B 80 -1.476 5.330 -2.449 1.00 26.43 C -ANISOU 2229 CD2 TYR B 80 3202 3660 3179 -455 -6 30 C -ATOM 2230 CE1 TYR B 80 -0.173 6.378 -0.236 1.00 26.33 C -ANISOU 2230 CE1 TYR B 80 3222 3790 2993 -623 16 -163 C -ATOM 2231 CE2 TYR B 80 -0.462 4.606 -1.831 1.00 23.48 C -ANISOU 2231 CE2 TYR B 80 2742 3503 2677 -436 -21 -17 C -ATOM 2232 CZ TYR B 80 0.184 5.138 -0.730 1.00 26.41 C -ANISOU 2232 CZ TYR B 80 3120 3955 2961 -514 -21 -108 C -ATOM 2233 OH TYR B 80 1.193 4.432 -0.110 1.00 28.03 O -ANISOU 2233 OH TYR B 80 3226 4393 3030 -472 -67 -152 O -ATOM 2234 N ILE B 81 -5.867 8.660 -3.208 1.00 20.01 N -ANISOU 2234 N ILE B 81 2713 1948 2943 -254 -2 108 N -ATOM 2235 CA ILE B 81 -6.729 9.788 -3.592 1.00 20.74 C -ANISOU 2235 CA ILE B 81 2910 1795 3176 -176 -40 135 C -ATOM 2236 C ILE B 81 -7.675 10.163 -2.441 1.00 21.60 C -ANISOU 2236 C ILE B 81 3007 1788 3412 -48 56 20 C -ATOM 2237 O ILE B 81 -7.869 11.332 -2.138 1.00 25.43 O -ANISOU 2237 O ILE B 81 3629 2071 3961 -30 78 -30 O -ATOM 2238 CB ILE B 81 -7.545 9.495 -4.876 1.00 29.93 C -ANISOU 2238 CB ILE B 81 4024 2924 4422 -66 -159 253 C -ATOM 2239 CG1 ILE B 81 -6.620 9.433 -6.091 1.00 24.83 C -ANISOU 2239 CG1 ILE B 81 3449 2351 3634 -206 -239 362 C -ATOM 2240 CG2 ILE B 81 -8.595 10.585 -5.111 1.00 31.86 C -ANISOU 2240 CG2 ILE B 81 4352 2920 4832 82 -216 275 C -ATOM 2241 CD1 ILE B 81 -7.252 8.740 -7.307 1.00 27.18 C -ANISOU 2241 CD1 ILE B 81 3679 2699 3950 -123 -356 461 C -ATOM 2242 N LYS B 82 -8.279 9.173 -1.805 1.00 22.02 N -ANISOU 2242 N LYS B 82 2911 1958 3496 36 126 -29 N -ATOM 2243 CA LYS B 82 -9.116 9.468 -0.641 1.00 25.34 C -ANISOU 2243 CA LYS B 82 3313 2305 4010 133 254 -155 C -ATOM 2244 C LYS B 82 -8.351 10.189 0.472 1.00 27.29 C -ANISOU 2244 C LYS B 82 3707 2519 4144 27 343 -271 C -ATOM 2245 O LYS B 82 -8.888 11.083 1.104 1.00 26.17 O -ANISOU 2245 O LYS B 82 3643 2217 4085 93 422 -375 O -ATOM 2246 CB LYS B 82 -9.771 8.183 -0.132 1.00 27.94 C -ANISOU 2246 CB LYS B 82 3478 2785 4354 186 338 -179 C -ATOM 2247 CG LYS B 82 -10.827 7.667 -1.092 1.00 30.53 C -ANISOU 2247 CG LYS B 82 3648 3117 4836 294 263 -111 C -ATOM 2248 CD LYS B 82 -10.979 6.154 -0.974 1.00 38.55 C -ANISOU 2248 CD LYS B 82 4545 4299 5802 255 307 -92 C -ATOM 2249 CE LYS B 82 -11.103 5.727 0.469 1.00 43.21 C -ANISOU 2249 CE LYS B 82 5143 4945 6329 229 490 -187 C -ATOM 2250 NZ LYS B 82 -11.112 4.241 0.600 1.00 48.43 N -ANISOU 2250 NZ LYS B 82 5755 5731 6915 174 533 -147 N -ATOM 2251 N ALA B 83 -7.085 9.833 0.681 1.00 26.25 N -ANISOU 2251 N ALA B 83 3609 2541 3823 -134 323 -264 N -ATOM 2252 CA ALA B 83 -6.266 10.508 1.698 1.00 23.76 C -ANISOU 2252 CA ALA B 83 3422 2226 3380 -265 378 -384 C -ATOM 2253 C ALA B 83 -6.124 11.989 1.392 1.00 26.99 C -ANISOU 2253 C ALA B 83 4009 2397 3848 -330 356 -416 C -ATOM 2254 O ALA B 83 -6.163 12.833 2.290 1.00 27.31 O -ANISOU 2254 O ALA B 83 4182 2315 3880 -360 436 -553 O -ATOM 2255 CB ALA B 83 -4.893 9.858 1.802 1.00 26.59 C -ANISOU 2255 CB ALA B 83 3742 2825 3538 -413 322 -366 C -ATOM 2256 N LEU B 84 -5.928 12.305 0.115 1.00 25.37 N -ANISOU 2256 N LEU B 84 3839 2115 3685 -365 253 -289 N -ATOM 2257 CA LEU B 84 -5.836 13.697 -0.313 1.00 27.46 C -ANISOU 2257 CA LEU B 84 4319 2111 4004 -429 226 -285 C -ATOM 2258 C LEU B 84 -7.177 14.406 -0.115 1.00 30.97 C -ANISOU 2258 C LEU B 84 4828 2291 4648 -199 263 -330 C -ATOM 2259 O LEU B 84 -7.222 15.580 0.288 1.00 31.89 O -ANISOU 2259 O LEU B 84 5150 2162 4807 -215 307 -420 O -ATOM 2260 CB LEU B 84 -5.437 13.769 -1.795 1.00 30.26 C -ANISOU 2260 CB LEU B 84 4710 2448 4339 -504 111 -113 C -ATOM 2261 CG LEU B 84 -4.070 13.251 -2.212 1.00 29.18 C -ANISOU 2261 CG LEU B 84 4510 2557 4021 -732 83 -72 C -ATOM 2262 CD1 LEU B 84 -3.924 13.214 -3.748 1.00 28.38 C -ANISOU 2262 CD1 LEU B 84 4439 2442 3901 -772 -8 100 C -ATOM 2263 CD2 LEU B 84 -2.981 14.134 -1.600 1.00 27.27 C -ANISOU 2263 CD2 LEU B 84 4400 2292 3668 -990 132 -182 C -ATOM 2264 N ASN B 85 -8.267 13.704 -0.421 1.00 28.81 N -ANISOU 2264 N ASN B 85 4376 2068 4503 14 245 -280 N -ATOM 2265 CA ASN B 85 -9.606 14.296 -0.314 1.00 31.84 C -ANISOU 2265 CA ASN B 85 4754 2246 5099 266 270 -329 C -ATOM 2266 C ASN B 85 -9.998 14.693 1.104 1.00 34.97 C -ANISOU 2266 C ASN B 85 5182 2581 5523 323 443 -533 C -ATOM 2267 O ASN B 85 -10.838 15.568 1.291 1.00 38.52 O -ANISOU 2267 O ASN B 85 5699 2803 6133 507 483 -612 O -ATOM 2268 CB ASN B 85 -10.672 13.344 -0.872 1.00 33.44 C -ANISOU 2268 CB ASN B 85 4703 2577 5427 449 218 -257 C -ATOM 2269 CG ASN B 85 -10.721 13.341 -2.374 1.00 40.29 C -ANISOU 2269 CG ASN B 85 5581 3408 6320 478 30 -74 C -ATOM 2270 OD1 ASN B 85 -10.331 14.308 -3.017 1.00 45.08 O -ANISOU 2270 OD1 ASN B 85 6406 3813 6909 439 -55 5 O -ATOM 2271 ND2 ASN B 85 -11.219 12.257 -2.945 1.00 47.93 N -ANISOU 2271 ND2 ASN B 85 6335 4559 7316 534 -33 -6 N -ATOM 2272 N ARG B 86 -9.408 14.047 2.104 1.00 33.64 N -ANISOU 2272 N ARG B 86 4973 2618 5192 184 544 -623 N -ATOM 2273 CA ARG B 86 -9.775 14.360 3.491 1.00 33.66 C -ANISOU 2273 CA ARG B 86 5021 2587 5179 222 720 -823 C -ATOM 2274 C ARG B 86 -8.716 15.173 4.242 1.00 38.28 C -ANISOU 2274 C ARG B 86 5843 3103 5599 15 755 -945 C -ATOM 2275 O ARG B 86 -8.973 15.677 5.339 1.00 37.44 O -ANISOU 2275 O ARG B 86 5836 2921 5469 36 894 -1130 O -ATOM 2276 CB ARG B 86 -10.152 13.088 4.266 1.00 31.86 C -ANISOU 2276 CB ARG B 86 4603 2620 4883 243 831 -857 C -ATOM 2277 CG ARG B 86 -8.990 12.147 4.509 1.00 27.44 C -ANISOU 2277 CG ARG B 86 4031 2307 4087 47 787 -799 C -ATOM 2278 CD ARG B 86 -9.410 10.852 5.184 1.00 34.31 C -ANISOU 2278 CD ARG B 86 4760 3389 4888 78 888 -799 C -ATOM 2279 NE ARG B 86 -8.234 9.994 5.310 1.00 33.13 N -ANISOU 2279 NE ARG B 86 4619 3448 4520 -68 810 -727 N -ATOM 2280 CZ ARG B 86 -8.000 8.897 4.598 1.00 31.53 C -ANISOU 2280 CZ ARG B 86 4299 3383 4298 -69 722 -585 C -ATOM 2281 NH1 ARG B 86 -8.884 8.457 3.704 1.00 27.51 N -ANISOU 2281 NH1 ARG B 86 3652 2839 3960 38 698 -499 N -ATOM 2282 NH2 ARG B 86 -6.868 8.232 4.792 1.00 29.51 N -ANISOU 2282 NH2 ARG B 86 4059 3306 3846 -171 651 -542 N -ATOM 2283 N ASN B 87 -7.539 15.330 3.638 1.00 37.91 N -ANISOU 2283 N ASN B 87 5881 3087 5435 -197 636 -857 N -ATOM 2284 CA ASN B 87 -6.449 16.067 4.286 1.00 42.03 C -ANISOU 2284 CA ASN B 87 6596 3576 5795 -440 653 -979 C -ATOM 2285 C ASN B 87 -6.007 17.343 3.570 1.00 47.68 C -ANISOU 2285 C ASN B 87 7553 4004 6560 -563 590 -954 C -ATOM 2286 O ASN B 87 -5.392 18.224 4.185 1.00 51.99 O -ANISOU 2286 O ASN B 87 8303 4430 7020 -748 631 -1097 O -ATOM 2287 CB ASN B 87 -5.240 15.149 4.505 1.00 43.55 C -ANISOU 2287 CB ASN B 87 6672 4108 5766 -643 593 -949 C -ATOM 2288 CG ASN B 87 -5.455 14.164 5.644 1.00 45.14 C -ANISOU 2288 CG ASN B 87 6759 4541 5851 -578 676 -1024 C -ATOM 2289 OD1 ASN B 87 -5.824 14.557 6.755 1.00 44.50 O -ANISOU 2289 OD1 ASN B 87 6780 4400 5727 -554 796 -1192 O -ATOM 2290 ND2 ASN B 87 -5.234 12.880 5.369 1.00 42.56 N -ANISOU 2290 ND2 ASN B 87 6246 4464 5460 -549 620 -901 N -ATOM 2291 N SER B 88 -6.316 17.458 2.283 1.00 76.44 N -ANISOU 2291 N SER B 88 11509 5930 11604 -1609 -2172 -1899 N -ATOM 2292 CA SER B 88 -5.822 18.607 1.522 1.00 78.38 C -ANISOU 2292 CA SER B 88 11796 5840 12144 -1934 -2039 -1787 C -ATOM 2293 C SER B 88 -6.876 19.661 1.182 1.00 80.01 C -ANISOU 2293 C SER B 88 12394 5554 12452 -1702 -1840 -1705 C -ATOM 2294 O SER B 88 -7.960 19.706 1.770 1.00 74.01 O -ANISOU 2294 O SER B 88 11853 4714 11554 -1290 -1814 -1852 O -ATOM 2295 CB SER B 88 -5.093 18.161 0.247 1.00 73.22 C -ANISOU 2295 CB SER B 88 10793 5364 11663 -2215 -1950 -1438 C -ATOM 2296 OG SER B 88 -6.008 17.733 -0.743 1.00 68.57 O -ANISOU 2296 OG SER B 88 10235 4734 11084 -1950 -1787 -1068 O -ATOM 2297 N ASP B 89 -6.524 20.496 0.210 1.00 88.39 N -ANISOU 2297 N ASP B 89 13534 6311 13739 -1960 -1688 -1477 N -ATOM 2298 CA ASP B 89 -7.279 21.691 -0.137 1.00 96.01 C -ANISOU 2298 CA ASP B 89 14907 6750 14824 -1780 -1539 -1407 C -ATOM 2299 C ASP B 89 -8.150 21.493 -1.375 1.00 93.13 C -ANISOU 2299 C ASP B 89 14583 6326 14477 -1475 -1397 -974 C -ATOM 2300 O ASP B 89 -8.626 22.462 -1.965 1.00 95.80 O -ANISOU 2300 O ASP B 89 15232 6245 14921 -1343 -1287 -820 O -ATOM 2301 CB ASP B 89 -6.302 22.840 -0.388 1.00104.94 C -ANISOU 2301 CB ASP B 89 16176 7522 16176 -2280 -1456 -1443 C -ATOM 2302 CG ASP B 89 -5.189 22.456 -1.353 1.00108.47 C -ANISOU 2302 CG ASP B 89 16293 8197 16724 -2767 -1357 -1189 C -ATOM 2303 OD1 ASP B 89 -4.822 23.288 -2.212 1.00113.81 O -ANISOU 2303 OD1 ASP B 89 17119 8538 17586 -3054 -1159 -986 O -ATOM 2304 OD2 ASP B 89 -4.683 21.316 -1.253 1.00107.22 O -ANISOU 2304 OD2 ASP B 89 15719 8558 16462 -2844 -1468 -1201 O -ATOM 2305 N ARG B 90 -8.351 20.241 -1.772 1.00 86.89 N -ANISOU 2305 N ARG B 90 13485 5953 13577 -1349 -1419 -786 N -ATOM 2306 CA ARG B 90 -9.145 19.939 -2.960 1.00 83.80 C -ANISOU 2306 CA ARG B 90 13085 5585 13171 -1069 -1312 -396 C -ATOM 2307 C ARG B 90 -9.911 18.644 -2.769 1.00 74.51 C -ANISOU 2307 C ARG B 90 11654 4802 11855 -732 -1371 -404 C -ATOM 2308 O ARG B 90 -9.550 17.826 -1.924 1.00 71.68 O -ANISOU 2308 O ARG B 90 11090 4764 11382 -812 -1457 -617 O -ATOM 2309 CB ARG B 90 -8.252 19.853 -4.188 1.00 86.14 C -ANISOU 2309 CB ARG B 90 13256 5949 13525 -1462 -1191 -37 C -ATOM 2310 N SER B 91 -10.961 18.451 -3.559 1.00 72.81 N -ANISOU 2310 N SER B 91 11440 4608 11614 -351 -1310 -177 N -ATOM 2311 CA SER B 91 -11.794 17.260 -3.419 1.00 71.20 C -ANISOU 2311 CA SER B 91 10921 4907 11227 -41 -1256 -197 C -ATOM 2312 C SER B 91 -12.144 16.563 -4.730 1.00 73.71 C -ANISOU 2312 C SER B 91 11026 5494 11488 58 -1186 174 C -ATOM 2313 O SER B 91 -12.137 17.174 -5.802 1.00 79.00 O -ANISOU 2313 O SER B 91 11884 5885 12249 59 -1200 462 O -ATOM 2314 CB SER B 91 -13.090 17.600 -2.678 1.00 70.64 C -ANISOU 2314 CB SER B 91 10948 4776 11116 436 -1229 -487 C -ATOM 2315 OG SER B 91 -13.008 17.240 -1.309 1.00 68.34 O -ANISOU 2315 OG SER B 91 10618 4691 10659 398 -1210 -848 O -ATOM 2316 N ILE B 92 -12.448 15.272 -4.619 1.00 69.14 N -ANISOU 2316 N ILE B 92 10106 5437 10727 130 -1116 163 N -ATOM 2317 CA ILE B 92 -13.169 14.540 -5.654 1.00 63.79 C -ANISOU 2317 CA ILE B 92 9216 5054 9965 326 -1062 394 C -ATOM 2318 C ILE B 92 -14.639 15.057 -5.606 1.00 61.66 C -ANISOU 2318 C ILE B 92 8990 4703 9736 810 -1072 269 C -ATOM 2319 O ILE B 92 -14.818 16.262 -5.753 1.00 61.62 O -ANISOU 2319 O ILE B 92 9295 4240 9878 977 -1160 274 O -ATOM 2320 CB ILE B 92 -13.008 13.068 -5.441 1.00 52.29 C -ANISOU 2320 CB ILE B 92 7451 4090 8326 217 -993 372 C -ATOM 2321 N PRO B 93 -15.698 14.232 -5.385 1.00 54.91 N -ANISOU 2321 N PRO B 93 7836 4257 8769 1041 -985 129 N -ATOM 2322 CA PRO B 93 -16.179 12.865 -5.126 1.00 52.30 C -ANISOU 2322 CA PRO B 93 7169 4436 8265 995 -853 49 C -ATOM 2323 C PRO B 93 -15.846 11.910 -6.246 1.00 43.54 C -ANISOU 2323 C PRO B 93 5889 3575 7078 839 -870 333 C -ATOM 2324 O PRO B 93 -15.618 12.332 -7.383 1.00 40.69 O -ANISOU 2324 O PRO B 93 5613 3075 6774 872 -969 590 O -ATOM 2325 CB PRO B 93 -17.705 13.029 -5.069 1.00 56.39 C -ANISOU 2325 CB PRO B 93 7485 5124 8818 1400 -799 -156 C -ATOM 2326 CG PRO B 93 -17.974 14.249 -5.836 1.00 61.76 C -ANISOU 2326 CG PRO B 93 8361 5434 9672 1724 -979 -48 C -ATOM 2327 CD PRO B 93 -16.850 15.150 -5.444 1.00 60.64 C -ANISOU 2327 CD PRO B 93 8631 4798 9613 1510 -1041 -7 C -ATOM 2328 N MET B 94 -15.793 10.635 -5.897 1.00 37.28 N -ANISOU 2328 N MET B 94 4919 3119 6129 665 -768 283 N -ATOM 2329 CA MET B 94 -15.562 9.588 -6.853 1.00 38.58 C -ANISOU 2329 CA MET B 94 4927 3529 6203 542 -774 480 C -ATOM 2330 C MET B 94 -16.686 8.584 -6.746 1.00 37.40 C -ANISOU 2330 C MET B 94 4532 3725 5955 592 -661 346 C -ATOM 2331 O MET B 94 -17.156 8.290 -5.647 1.00 34.86 O -ANISOU 2331 O MET B 94 4192 3495 5558 556 -519 128 O -ATOM 2332 CB MET B 94 -14.264 8.860 -6.530 1.00 36.37 C -ANISOU 2332 CB MET B 94 4706 3281 5834 253 -778 533 C -ATOM 2333 CG MET B 94 -13.017 9.706 -6.600 1.00 41.37 C -ANISOU 2333 CG MET B 94 5489 3654 6577 98 -866 620 C -ATOM 2334 SD MET B 94 -11.600 8.602 -6.514 1.00 49.54 S -ANISOU 2334 SD MET B 94 6428 4882 7513 -151 -903 653 S -ATOM 2335 CE MET B 94 -12.210 7.329 -7.566 1.00 46.48 C -ANISOU 2335 CE MET B 94 5873 4790 6995 -70 -838 780 C -ATOM 2336 N THR B 95 -17.112 8.060 -7.887 1.00 33.85 N -ANISOU 2336 N THR B 95 3906 3473 5482 639 -710 464 N -ATOM 2337 CA THR B 95 -17.875 6.816 -7.904 1.00 33.18 C -ANISOU 2337 CA THR B 95 3595 3717 5294 536 -605 353 C -ATOM 2338 C THR B 95 -17.010 5.760 -8.575 1.00 30.74 C -ANISOU 2338 C THR B 95 3342 3469 4869 329 -640 521 C -ATOM 2339 O THR B 95 -15.996 6.087 -9.205 1.00 29.98 O -ANISOU 2339 O THR B 95 3368 3241 4781 315 -735 712 O -ATOM 2340 CB THR B 95 -19.209 6.968 -8.627 1.00 35.48 C -ANISOU 2340 CB THR B 95 3584 4243 5654 768 -661 255 C -ATOM 2341 OG1 THR B 95 -18.991 7.550 -9.918 1.00 36.06 O -ANISOU 2341 OG1 THR B 95 3717 4235 5750 958 -877 478 O -ATOM 2342 CG2 THR B 95 -20.138 7.872 -7.822 1.00 38.55 C -ANISOU 2342 CG2 THR B 95 3858 4627 6161 1018 -597 6 C -ATOM 2343 N VAL B 96 -17.381 4.493 -8.439 1.00 30.10 N -ANISOU 2343 N VAL B 96 3185 3575 4677 155 -543 434 N -ATOM 2344 CA VAL B 96 -16.539 3.429 -8.981 1.00 30.25 C -ANISOU 2344 CA VAL B 96 3301 3607 4584 6 -583 548 C -ATOM 2345 C VAL B 96 -17.349 2.445 -9.801 1.00 33.35 C -ANISOU 2345 C VAL B 96 3529 4225 4919 -68 -579 482 C -ATOM 2346 O VAL B 96 -18.552 2.264 -9.580 1.00 32.66 O -ANISOU 2346 O VAL B 96 3241 4308 4860 -114 -493 308 O -ATOM 2347 CB VAL B 96 -15.783 2.666 -7.867 1.00 33.94 C -ANISOU 2347 CB VAL B 96 4008 3951 4936 -159 -516 519 C -ATOM 2348 CG1 VAL B 96 -15.032 3.633 -6.969 1.00 38.04 C -ANISOU 2348 CG1 VAL B 96 4667 4285 5500 -105 -554 521 C -ATOM 2349 CG2 VAL B 96 -16.742 1.847 -7.039 1.00 34.22 C -ANISOU 2349 CG2 VAL B 96 4074 4062 4867 -332 -335 368 C -ATOM 2350 N ASP B 97 -16.698 1.821 -10.773 1.00 29.65 N -ANISOU 2350 N ASP B 97 3113 3782 4369 -89 -667 583 N -ATOM 2351 CA ASP B 97 -17.294 0.668 -11.429 1.00 32.38 C -ANISOU 2351 CA ASP B 97 3380 4290 4632 -213 -672 480 C -ATOM 2352 C ASP B 97 -16.157 -0.256 -11.811 1.00 27.90 C -ANISOU 2352 C ASP B 97 3022 3626 3951 -261 -705 548 C -ATOM 2353 O ASP B 97 -14.986 0.115 -11.720 1.00 26.71 O -ANISOU 2353 O ASP B 97 2979 3365 3803 -175 -733 669 O -ATOM 2354 CB ASP B 97 -18.119 1.074 -12.657 1.00 37.82 C -ANISOU 2354 CB ASP B 97 3825 5215 5330 -64 -814 459 C -ATOM 2355 CG ASP B 97 -19.132 -0.010 -13.085 1.00 46.45 C -ANISOU 2355 CG ASP B 97 4744 6526 6380 -244 -821 244 C -ATOM 2356 OD1 ASP B 97 -19.326 -1.018 -12.360 1.00 41.18 O -ANISOU 2356 OD1 ASP B 97 4162 5790 5695 -526 -668 119 O -ATOM 2357 OD2 ASP B 97 -19.743 0.163 -14.161 1.00 54.75 O -ANISOU 2357 OD2 ASP B 97 5598 7805 7397 -116 -995 197 O -ATOM 2358 N PHE B 98 -16.508 -1.460 -12.226 1.00 28.14 N -ANISOU 2358 N PHE B 98 3092 3703 3895 -400 -702 432 N -ATOM 2359 CA PHE B 98 -15.523 -2.495 -12.452 1.00 27.71 C -ANISOU 2359 CA PHE B 98 3274 3519 3736 -407 -731 437 C -ATOM 2360 C PHE B 98 -15.895 -3.132 -13.765 1.00 29.12 C -ANISOU 2360 C PHE B 98 3382 3857 3824 -419 -812 336 C -ATOM 2361 O PHE B 98 -17.054 -3.478 -13.982 1.00 30.80 O -ANISOU 2361 O PHE B 98 3466 4190 4047 -579 -814 187 O -ATOM 2362 CB PHE B 98 -15.606 -3.549 -11.345 1.00 28.40 C -ANISOU 2362 CB PHE B 98 3646 3372 3773 -599 -641 365 C -ATOM 2363 CG PHE B 98 -15.301 -3.018 -9.981 1.00 27.81 C -ANISOU 2363 CG PHE B 98 3694 3157 3715 -593 -575 439 C -ATOM 2364 CD1 PHE B 98 -16.298 -2.418 -9.211 1.00 28.51 C -ANISOU 2364 CD1 PHE B 98 3666 3314 3854 -716 -437 389 C -ATOM 2365 CD2 PHE B 98 -14.019 -3.120 -9.460 1.00 28.86 C -ANISOU 2365 CD2 PHE B 98 4037 3126 3803 -441 -665 518 C -ATOM 2366 CE1 PHE B 98 -16.015 -1.912 -7.939 1.00 29.54 C -ANISOU 2366 CE1 PHE B 98 3946 3325 3953 -702 -375 427 C -ATOM 2367 CE2 PHE B 98 -13.720 -2.625 -8.186 1.00 30.00 C -ANISOU 2367 CE2 PHE B 98 4314 3159 3926 -428 -650 558 C -ATOM 2368 CZ PHE B 98 -14.728 -2.021 -7.423 1.00 30.52 C -ANISOU 2368 CZ PHE B 98 4322 3269 4006 -568 -497 517 C -ATOM 2369 N ILE B 99 -14.928 -3.266 -14.658 1.00 28.72 N -ANISOU 2369 N ILE B 99 3385 3849 3676 -259 -873 384 N -ATOM 2370 CA ILE B 99 -15.215 -3.954 -15.898 1.00 30.32 C -ANISOU 2370 CA ILE B 99 3578 4202 3738 -259 -952 254 C -ATOM 2371 C ILE B 99 -14.218 -5.072 -16.098 1.00 30.79 C -ANISOU 2371 C ILE B 99 3881 4116 3703 -192 -949 161 C -ATOM 2372 O ILE B 99 -13.087 -5.038 -15.602 1.00 30.68 O -ANISOU 2372 O ILE B 99 3952 3985 3721 -55 -917 235 O -ATOM 2373 CB ILE B 99 -15.244 -3.001 -17.132 1.00 43.70 C -ANISOU 2373 CB ILE B 99 5109 6171 5325 -90 -1033 364 C -ATOM 2374 CG1 ILE B 99 -14.003 -2.129 -17.173 1.00 47.41 C -ANISOU 2374 CG1 ILE B 99 5598 6623 5793 54 -956 578 C -ATOM 2375 CG2 ILE B 99 -16.489 -2.123 -17.137 1.00 42.69 C -ANISOU 2375 CG2 ILE B 99 4759 6190 5271 -86 -1117 383 C -ATOM 2376 CD1 ILE B 99 -12.856 -2.756 -17.921 1.00 58.22 C -ANISOU 2376 CD1 ILE B 99 7054 8060 7008 147 -902 530 C -ATOM 2377 N ARG B 100 -14.629 -6.090 -16.816 1.00 32.74 N -ANISOU 2377 N ARG B 100 4230 4369 3841 -268 -1007 -41 N -ATOM 2378 CA AARG B 100 -13.702 -7.139 -17.174 0.60 36.31 C -ANISOU 2378 CA AARG B 100 4927 4680 4190 -131 -1022 -172 C -ATOM 2379 CA BARG B 100 -13.680 -7.120 -17.187 0.40 36.48 C -ANISOU 2379 CA BARG B 100 4944 4706 4210 -125 -1022 -169 C -ATOM 2380 C ARG B 100 -13.841 -7.449 -18.651 1.00 37.84 C -ANISOU 2380 C ARG B 100 5085 5111 4182 -66 -1091 -334 C -ATOM 2381 O ARG B 100 -14.947 -7.400 -19.199 1.00 41.23 O -ANISOU 2381 O ARG B 100 5401 5704 4560 -225 -1177 -428 O -ATOM 2382 CB AARG B 100 -13.972 -8.375 -16.334 0.60 38.68 C -ANISOU 2382 CB AARG B 100 5573 4589 4536 -303 -1024 -299 C -ATOM 2383 CB BARG B 100 -13.828 -8.376 -16.335 0.40 39.15 C -ANISOU 2383 CB BARG B 100 5642 4643 4592 -269 -1025 -293 C -ATOM 2384 CG AARG B 100 -12.923 -9.440 -16.471 0.60 42.47 C -ANISOU 2384 CG AARG B 100 6371 4826 4940 -70 -1073 -427 C -ATOM 2385 CG BARG B 100 -12.622 -9.302 -16.440 0.40 42.50 C -ANISOU 2385 CG BARG B 100 6346 4854 4947 9 -1071 -398 C -ATOM 2386 CD AARG B 100 -13.221 -10.607 -15.573 0.60 42.98 C -ANISOU 2386 CD AARG B 100 6894 4409 5027 -242 -1088 -497 C -ATOM 2387 CD BARG B 100 -13.004 -10.751 -16.222 0.40 44.51 C -ANISOU 2387 CD BARG B 100 7053 4692 5167 -137 -1120 -588 C -ATOM 2388 NE AARG B 100 -12.367 -11.734 -15.911 0.60 46.37 N -ANISOU 2388 NE AARG B 100 7677 4568 5374 30 -1184 -674 N -ATOM 2389 NE BARG B 100 -13.753 -10.916 -14.986 0.40 44.13 N -ANISOU 2389 NE BARG B 100 7203 4362 5200 -459 -1054 -481 N -ATOM 2390 CZ AARG B 100 -12.542 -12.963 -15.446 0.60 49.88 C -ANISOU 2390 CZ AARG B 100 8650 4510 5794 -70 -1231 -774 C -ATOM 2391 CZ BARG B 100 -13.909 -12.073 -14.354 0.40 46.65 C -ANISOU 2391 CZ BARG B 100 8035 4201 5490 -612 -1059 -539 C -ATOM 2392 NH1AARG B 100 -13.542 -13.220 -14.615 0.60 50.71 N -ANISOU 2392 NH1AARG B 100 8971 4362 5934 -510 -1147 -697 N -ATOM 2393 NH1BARG B 100 -13.360 -13.177 -14.839 0.40 50.60 N -ANISOU 2393 NH1BARG B 100 8907 4406 5913 -423 -1167 -722 N -ATOM 2394 NH2AARG B 100 -11.716 -13.932 -15.812 0.60 51.79 N -ANISOU 2394 NH2AARG B 100 9221 4490 5966 266 -1347 -958 N -ATOM 2395 NH2BARG B 100 -14.607 -12.124 -13.230 0.40 45.64 N -ANISOU 2395 NH2BARG B 100 8086 3866 5389 -951 -939 -414 N -ATOM 2396 N LEU B 101 -12.723 -7.749 -19.290 1.00 42.82 N -ANISOU 2396 N LEU B 101 7214 4006 5050 -566 -3073 -353 N -ATOM 2397 CA LEU B 101 -12.746 -8.114 -20.697 1.00 53.55 C -ANISOU 2397 CA LEU B 101 8465 5410 6471 -490 -3165 -465 C -ATOM 2398 C LEU B 101 -12.469 -9.600 -20.829 1.00 61.18 C -ANISOU 2398 C LEU B 101 9746 6068 7432 -522 -3342 -528 C -ATOM 2399 O LEU B 101 -11.401 -10.078 -20.435 1.00 63.83 O -ANISOU 2399 O LEU B 101 10375 6342 7536 -328 -3223 -515 O -ATOM 2400 CB LEU B 101 -11.719 -7.300 -21.475 1.00 57.18 C -ANISOU 2400 CB LEU B 101 8816 6188 6720 -185 -2870 -513 C -ATOM 2401 CG LEU B 101 -12.171 -5.958 -22.055 1.00 60.71 C -ANISOU 2401 CG LEU B 101 8932 6917 7217 -163 -2776 -496 C -ATOM 2402 CD1 LEU B 101 -13.061 -5.178 -21.104 1.00 63.78 C -ANISOU 2402 CD1 LEU B 101 9176 7309 7750 -319 -2822 -396 C -ATOM 2403 CD2 LEU B 101 -10.953 -5.148 -22.402 1.00 56.42 C -ANISOU 2403 CD2 LEU B 101 8349 6592 6496 61 -2466 -496 C -ATOM 2404 N LYS B 102 -13.443 -10.325 -21.368 1.00 67.90 N -ANISOU 2404 N LYS B 102 10509 6723 8566 -772 -3617 -598 N -ATOM 2405 CA LYS B 102 -13.359 -11.778 -21.472 1.00 74.46 C -ANISOU 2405 CA LYS B 102 11626 7198 9467 -866 -3800 -681 C -ATOM 2406 C LYS B 102 -13.856 -12.266 -22.825 1.00 79.25 C -ANISOU 2406 C LYS B 102 12098 7816 10198 -908 -4017 -871 C -ATOM 2407 O LYS B 102 -13.647 -13.420 -23.189 1.00 87.37 O -ANISOU 2407 O LYS B 102 13366 8594 11237 -920 -4167 -998 O -ATOM 2408 CB LYS B 102 -14.151 -12.433 -20.347 1.00 77.82 C -ANISOU 2408 CB LYS B 102 12112 7208 10246 -1269 -3841 -563 C -ATOM 2409 N VAL B 115 -17.576 -8.235 -22.326 1.00 69.72 N -ANISOU 2409 N VAL B 115 9285 7368 9837 -1460 -3937 -450 N -ATOM 2410 CA VAL B 115 -17.431 -7.178 -21.326 1.00 68.85 C -ANISOU 2410 CA VAL B 115 9092 7364 9704 -1419 -3734 -267 C -ATOM 2411 C VAL B 115 -18.389 -7.415 -20.166 1.00 72.29 C -ANISOU 2411 C VAL B 115 9275 7543 10649 -1842 -3701 -33 C -ATOM 2412 O VAL B 115 -19.535 -6.968 -20.210 1.00 74.91 O -ANISOU 2412 O VAL B 115 9107 7975 11382 -2029 -3702 119 O -ATOM 2413 CB VAL B 115 -17.726 -5.774 -21.923 1.00 60.23 C -ANISOU 2413 CB VAL B 115 7683 6654 8548 -1223 -3659 -227 C -ATOM 2414 CG1 VAL B 115 -17.489 -4.683 -20.878 1.00 57.20 C -ANISOU 2414 CG1 VAL B 115 7239 6361 8133 -1159 -3462 -67 C -ATOM 2415 CG2 VAL B 115 -16.862 -5.517 -23.131 1.00 56.27 C -ANISOU 2415 CG2 VAL B 115 7360 6380 7640 -880 -3579 -393 C -ATOM 2416 N ILE B 116 -17.943 -8.120 -19.131 1.00 69.60 N -ANISOU 2416 N ILE B 116 9251 6907 10286 -1923 -3496 64 N -ATOM 2417 CA ILE B 116 -18.841 -8.383 -18.007 1.00 73.92 C -ANISOU 2417 CA ILE B 116 9559 7290 11235 -2148 -3079 402 C -ATOM 2418 C ILE B 116 -18.875 -7.204 -17.046 1.00 70.96 C -ANISOU 2418 C ILE B 116 9043 7200 10719 -1916 -2583 621 C -ATOM 2419 O ILE B 116 -17.871 -6.504 -16.863 1.00 62.31 O -ANISOU 2419 O ILE B 116 8217 6304 9155 -1591 -2483 514 O -ATOM 2420 CB ILE B 116 -18.526 -9.712 -17.259 1.00 79.00 C -ANISOU 2420 CB ILE B 116 10577 7508 11933 -2276 -2923 500 C -ATOM 2421 CG1 ILE B 116 -18.460 -9.492 -15.741 1.00 80.70 C -ANISOU 2421 CG1 ILE B 116 10857 7756 12047 -2139 -2307 839 C -ATOM 2422 CG2 ILE B 116 -17.267 -10.368 -17.809 1.00 76.51 C -ANISOU 2422 CG2 ILE B 116 10815 7059 11195 -2090 -3226 201 C -ATOM 2423 CD1 ILE B 116 -17.097 -9.169 -15.178 1.00 78.21 C -ANISOU 2423 CD1 ILE B 116 11009 7606 11102 -1735 -2139 759 C -ATOM 2424 N GLY B 117 -20.030 -6.989 -16.429 1.00 75.63 N -ANISOU 2424 N GLY B 117 9204 7805 11727 -2082 -2270 919 N -ATOM 2425 CA GLY B 117 -20.164 -5.893 -15.500 1.00 74.42 C -ANISOU 2425 CA GLY B 117 8922 7898 11455 -1848 -1783 1111 C -ATOM 2426 C GLY B 117 -20.198 -4.598 -16.270 1.00 76.14 C -ANISOU 2426 C GLY B 117 8913 8436 11580 -1653 -1930 979 C -ATOM 2427 O GLY B 117 -20.598 -4.564 -17.435 1.00 78.29 O -ANISOU 2427 O GLY B 117 8941 8775 12031 -1761 -2350 862 O -ATOM 2428 N GLY B 118 -19.755 -3.526 -15.629 1.00 74.23 N -ANISOU 2428 N GLY B 118 8768 8389 11047 -1351 -1590 991 N -ATOM 2429 CA GLY B 118 -20.081 -2.207 -16.117 1.00 76.21 C -ANISOU 2429 CA GLY B 118 8723 8891 11342 -1177 -1578 978 C -ATOM 2430 C GLY B 118 -21.496 -1.933 -15.642 1.00 81.67 C -ANISOU 2430 C GLY B 118 8899 9633 12497 -1280 -1266 1292 C -ATOM 2431 O GLY B 118 -22.226 -2.854 -15.267 1.00 84.58 O -ANISOU 2431 O GLY B 118 9094 9845 13197 -1549 -1190 1490 O -ATOM 2432 N ASP B 119 -21.886 -0.666 -15.641 1.00 82.25 N -ANISOU 2432 N ASP B 119 8720 9911 12620 -1060 -1058 1361 N -ATOM 2433 CA ASP B 119 -23.212 -0.281 -15.174 1.00 86.09 C -ANISOU 2433 CA ASP B 119 8698 10486 13524 -1085 -717 1676 C -ATOM 2434 C ASP B 119 -24.055 0.171 -16.349 1.00 85.55 C -ANISOU 2434 C ASP B 119 8125 10595 13786 -1123 -1038 1730 C -ATOM 2435 O ASP B 119 -25.241 0.470 -16.191 1.00 90.35 O -ANISOU 2435 O ASP B 119 8216 11318 14793 -1151 -839 2003 O -ATOM 2436 CB ASP B 119 -23.104 0.880 -14.181 1.00 88.30 C -ANISOU 2436 CB ASP B 119 9069 10866 13615 -744 -178 1727 C -ATOM 2437 CG ASP B 119 -22.841 0.421 -12.756 1.00 90.71 C -ANISOU 2437 CG ASP B 119 9674 11077 13716 -706 263 1811 C -ATOM 2438 OD1 ASP B 119 -23.141 -0.751 -12.433 1.00 93.31 O -ANISOU 2438 OD1 ASP B 119 9983 11265 14206 -957 271 1975 O -ATOM 2439 OD2 ASP B 119 -22.349 1.248 -11.957 1.00 88.75 O -ANISOU 2439 OD2 ASP B 119 9680 10893 13148 -415 606 1715 O -ATOM 2440 N ASP B 120 -23.423 0.168 -17.523 1.00 81.49 N -ANISOU 2440 N ASP B 120 7759 10124 13078 -1102 -1535 1483 N -ATOM 2441 CA ASP B 120 -23.783 1.007 -18.669 1.00 78.92 C -ANISOU 2441 CA ASP B 120 7118 10034 12834 -950 -1808 1480 C -ATOM 2442 C ASP B 120 -23.436 2.458 -18.359 1.00 73.23 C -ANISOU 2442 C ASP B 120 6486 9406 11931 -562 -1437 1508 C -ATOM 2443 O ASP B 120 -22.271 2.788 -18.136 1.00 71.52 O -ANISOU 2443 O ASP B 120 6735 9109 11329 -405 -1359 1309 O -ATOM 2444 CB ASP B 120 -25.255 0.862 -19.069 1.00 85.72 C -ANISOU 2444 CB ASP B 120 7309 11046 14214 -1128 -1931 1720 C -ATOM 2445 N THR B 123 -23.758 5.863 -17.505 1.00 55.59 N -ANISOU 2445 N THR B 123 4092 7293 9737 263 -438 1737 N -ATOM 2446 CA THR B 123 -23.279 6.493 -16.273 1.00 63.62 C -ANISOU 2446 CA THR B 123 5438 8165 10569 440 69 1643 C -ATOM 2447 C THR B 123 -22.110 7.437 -16.527 1.00 60.69 C -ANISOU 2447 C THR B 123 5452 7698 9911 647 69 1401 C -ATOM 2448 O THR B 123 -21.860 8.359 -15.750 1.00 63.26 O -ANISOU 2448 O THR B 123 5960 7911 10165 856 471 1316 O -ATOM 2449 CB THR B 123 -22.783 5.456 -15.243 1.00 66.73 C -ANISOU 2449 CB THR B 123 6170 8444 10739 241 169 1528 C -ATOM 2450 OG1 THR B 123 -23.075 4.128 -15.697 1.00 74.33 O -ANISOU 2450 OG1 THR B 123 6998 9417 11828 -87 -199 1592 O -ATOM 2451 CG2 THR B 123 -23.430 5.701 -13.889 1.00 66.14 C -ANISOU 2451 CG2 THR B 123 6032 8357 10743 358 745 1680 C -ATOM 2452 N LEU B 124 -21.387 7.194 -17.613 1.00 58.22 N -ANISOU 2452 N LEU B 124 5258 7422 9440 587 -378 1284 N -ATOM 2453 CA LEU B 124 -20.127 7.886 -17.857 1.00 53.28 C -ANISOU 2453 CA LEU B 124 5005 6701 8538 723 -403 1063 C -ATOM 2454 C LEU B 124 -20.285 9.265 -18.510 1.00 56.23 C -ANISOU 2454 C LEU B 124 5222 7068 9077 1010 -275 1185 C -ATOM 2455 O LEU B 124 -19.357 10.076 -18.492 1.00 54.58 O -ANISOU 2455 O LEU B 124 5285 6717 8734 1133 -156 1033 O -ATOM 2456 CB LEU B 124 -19.210 7.001 -18.695 1.00 48.57 C -ANISOU 2456 CB LEU B 124 4629 6155 7671 571 -887 905 C -ATOM 2457 CG LEU B 124 -18.959 5.620 -18.092 1.00 45.29 C -ANISOU 2457 CG LEU B 124 4418 5696 7095 312 -1010 791 C -ATOM 2458 CD1 LEU B 124 -17.896 4.871 -18.877 1.00 40.55 C -ANISOU 2458 CD1 LEU B 124 4101 5115 6190 232 -1440 603 C -ATOM 2459 CD2 LEU B 124 -18.561 5.752 -16.627 1.00 44.80 C -ANISOU 2459 CD2 LEU B 124 4634 5514 6876 337 -600 676 C -ATOM 2460 N THR B 125 -21.463 9.523 -19.072 1.00 55.63 N -ANISOU 2460 N THR B 125 4688 7138 9312 1115 -293 1473 N -ATOM 2461 CA THR B 125 -21.715 10.748 -19.828 1.00 51.16 C -ANISOU 2461 CA THR B 125 3935 6589 8915 1425 -199 1661 C -ATOM 2462 C THR B 125 -21.510 12.031 -19.021 1.00 53.75 C -ANISOU 2462 C THR B 125 4440 6656 9326 1661 329 1609 C -ATOM 2463 O THR B 125 -22.097 12.211 -17.952 1.00 52.98 O -ANISOU 2463 O THR B 125 4299 6481 9350 1707 714 1617 O -ATOM 2464 CB THR B 125 -23.122 10.736 -20.442 1.00 56.26 C -ANISOU 2464 CB THR B 125 4010 7484 9880 1515 -302 1999 C -ATOM 2465 OG1 THR B 125 -23.285 9.543 -21.220 1.00 55.75 O -ANISOU 2465 OG1 THR B 125 3799 7640 9744 1268 -839 1983 O -ATOM 2466 CG2 THR B 125 -23.332 11.953 -21.346 1.00 55.81 C -ANISOU 2466 CG2 THR B 125 3795 7472 9937 1869 -239 2218 C -ATOM 2467 N GLY B 126 -20.671 12.921 -19.545 1.00 51.32 N -ANISOU 2467 N GLY B 126 4337 6202 8961 1814 355 1553 N -ATOM 2468 CA GLY B 126 -20.433 14.204 -18.912 1.00 52.30 C -ANISOU 2468 CA GLY B 126 4641 6019 9213 2023 823 1476 C -ATOM 2469 C GLY B 126 -19.627 14.100 -17.636 1.00 53.55 C -ANISOU 2469 C GLY B 126 5211 5978 9157 1871 1025 1090 C -ATOM 2470 O GLY B 126 -19.570 15.053 -16.854 1.00 59.03 O -ANISOU 2470 O GLY B 126 6065 6415 9949 2019 1430 955 O -ATOM 2471 N LYS B 127 -19.007 12.938 -17.426 1.00 49.15 N -ANISOU 2471 N LYS B 127 4835 5543 8296 1597 734 903 N -ATOM 2472 CA LYS B 127 -18.197 12.695 -16.239 1.00 49.95 C -ANISOU 2472 CA LYS B 127 5318 5532 8127 1464 863 551 C -ATOM 2473 C LYS B 127 -16.722 12.635 -16.613 1.00 45.51 C -ANISOU 2473 C LYS B 127 5061 4918 7312 1338 608 309 C -ATOM 2474 O LYS B 127 -16.379 12.369 -17.765 1.00 44.23 O -ANISOU 2474 O LYS B 127 4823 4866 7118 1308 280 430 O -ATOM 2475 CB LYS B 127 -18.599 11.368 -15.592 1.00 51.18 C -ANISOU 2475 CB LYS B 127 5453 5867 8127 1277 772 559 C -ATOM 2476 CG LYS B 127 -20.008 11.342 -15.025 1.00 56.80 C -ANISOU 2476 CG LYS B 127 5852 6645 9085 1375 1077 801 C -ATOM 2477 CD LYS B 127 -20.050 11.899 -13.605 1.00 64.10 C -ANISOU 2477 CD LYS B 127 6996 7436 9924 1517 1559 618 C -ATOM 2478 CE LYS B 127 -21.482 11.965 -13.074 1.00 70.36 C -ANISOU 2478 CE LYS B 127 7447 8313 10974 1671 1922 903 C -ATOM 2479 NZ LYS B 127 -22.175 10.649 -13.177 1.00 72.23 N -ANISOU 2479 NZ LYS B 127 7403 8768 11274 1449 1731 1152 N -ATOM 2480 N ASN B 128 -15.853 12.889 -15.640 1.00 39.13 N -ANISOU 2480 N ASN B 128 5047 3532 6288 1074 -1037 668 N -ATOM 2481 CA ASN B 128 -14.429 12.641 -15.813 1.00 37.97 C -ANISOU 2481 CA ASN B 128 5038 3392 5998 859 -1021 581 C -ATOM 2482 C ASN B 128 -14.145 11.193 -15.491 1.00 36.58 C -ANISOU 2482 C ASN B 128 4729 3469 5701 785 -969 631 C -ATOM 2483 O ASN B 128 -14.282 10.782 -14.347 1.00 39.43 O -ANISOU 2483 O ASN B 128 4943 4032 6005 907 -843 587 O -ATOM 2484 CB ASN B 128 -13.609 13.521 -14.872 1.00 43.20 C -ANISOU 2484 CB ASN B 128 5775 4008 6630 885 -936 312 C -ATOM 2485 CG ASN B 128 -13.722 14.992 -15.200 1.00 51.07 C -ANISOU 2485 CG ASN B 128 6915 4665 7826 929 -980 245 C -ATOM 2486 OD1 ASN B 128 -14.451 15.384 -16.111 1.00 49.34 O -ANISOU 2486 OD1 ASN B 128 6743 4270 7733 974 -1056 443 O -ATOM 2487 ND2 ASN B 128 -12.998 15.818 -14.451 1.00 58.16 N -ANISOU 2487 ND2 ASN B 128 7868 5460 8772 930 -942 -43 N -ATOM 2488 N VAL B 129 -13.725 10.419 -16.485 1.00 31.47 N -ANISOU 2488 N VAL B 129 4131 2817 5008 614 -1055 729 N -ATOM 2489 CA VAL B 129 -13.523 8.989 -16.291 1.00 27.24 C -ANISOU 2489 CA VAL B 129 3468 2455 4426 549 -1019 785 C -ATOM 2490 C VAL B 129 -12.042 8.659 -16.203 1.00 26.16 C -ANISOU 2490 C VAL B 129 3439 2400 4101 410 -960 688 C -ATOM 2491 O VAL B 129 -11.261 9.094 -17.052 1.00 28.10 O -ANISOU 2491 O VAL B 129 3853 2548 4274 284 -1020 659 O -ATOM 2492 CB VAL B 129 -14.147 8.184 -17.444 1.00 27.75 C -ANISOU 2492 CB VAL B 129 3478 2468 4595 481 -1183 905 C -ATOM 2493 CG1 VAL B 129 -13.945 6.689 -17.236 1.00 25.35 C -ANISOU 2493 CG1 VAL B 129 3035 2267 4330 408 -1147 945 C -ATOM 2494 CG2 VAL B 129 -15.633 8.525 -17.578 1.00 32.79 C -ANISOU 2494 CG2 VAL B 129 3972 3049 5438 618 -1265 997 C -ATOM 2495 N LEU B 130 -11.666 7.916 -15.161 1.00 24.59 N -ANISOU 2495 N LEU B 130 3122 2402 3820 459 -828 668 N -ATOM 2496 CA LEU B 130 -10.312 7.407 -14.992 1.00 23.23 C -ANISOU 2496 CA LEU B 130 3003 2356 3469 360 -772 593 C -ATOM 2497 C LEU B 130 -10.327 5.890 -15.143 1.00 26.45 C -ANISOU 2497 C LEU B 130 3301 2835 3914 330 -752 734 C -ATOM 2498 O LEU B 130 -10.836 5.170 -14.278 1.00 30.58 O -ANISOU 2498 O LEU B 130 3642 3474 4503 451 -636 853 O -ATOM 2499 CB LEU B 130 -9.754 7.765 -13.605 1.00 23.87 C -ANISOU 2499 CB LEU B 130 3028 2647 3395 485 -646 442 C -ATOM 2500 CG LEU B 130 -8.338 7.266 -13.331 1.00 33.52 C -ANISOU 2500 CG LEU B 130 4267 4047 4423 411 -598 354 C -ATOM 2501 CD1 LEU B 130 -7.335 7.902 -14.290 1.00 26.07 C -ANISOU 2501 CD1 LEU B 130 3487 2953 3466 198 -684 250 C -ATOM 2502 CD2 LEU B 130 -7.936 7.508 -11.880 1.00 29.90 C -ANISOU 2502 CD2 LEU B 130 3711 3873 3778 595 -500 193 C -ATOM 2503 N ILE B 131 -9.744 5.408 -16.233 1.00 25.12 N -ANISOU 2503 N ILE B 131 3236 2594 3714 187 -849 728 N -ATOM 2504 CA ILE B 131 -9.568 3.979 -16.437 1.00 21.83 C -ANISOU 2504 CA ILE B 131 2739 2201 3354 155 -845 800 C -ATOM 2505 C ILE B 131 -8.299 3.533 -15.729 1.00 22.17 C -ANISOU 2505 C ILE B 131 2784 2433 3208 167 -710 765 C -ATOM 2506 O ILE B 131 -7.235 4.110 -15.928 1.00 25.00 O -ANISOU 2506 O ILE B 131 3265 2854 3378 95 -712 644 O -ATOM 2507 CB ILE B 131 -9.458 3.635 -17.937 1.00 26.02 C -ANISOU 2507 CB ILE B 131 3383 2612 3891 47 -1024 755 C -ATOM 2508 CG1 ILE B 131 -10.760 3.989 -18.658 1.00 31.35 C -ANISOU 2508 CG1 ILE B 131 4026 3147 4737 68 -1190 785 C -ATOM 2509 CG2 ILE B 131 -9.096 2.153 -18.122 1.00 24.99 C -ANISOU 2509 CG2 ILE B 131 3186 2479 3832 23 -1026 762 C -ATOM 2510 CD1 ILE B 131 -10.626 4.132 -20.172 1.00 33.06 C -ANISOU 2510 CD1 ILE B 131 4395 3323 4844 23 -1383 720 C -ATOM 2511 N VAL B 132 -8.421 2.506 -14.895 1.00 23.51 N -ANISOU 2511 N VAL B 132 2792 2696 3446 266 -584 897 N -ATOM 2512 CA VAL B 132 -7.301 2.053 -14.071 1.00 20.76 C -ANISOU 2512 CA VAL B 132 2414 2577 2898 339 -447 897 C -ATOM 2513 C VAL B 132 -6.893 0.646 -14.479 1.00 25.71 C -ANISOU 2513 C VAL B 132 3006 3140 3624 312 -434 990 C -ATOM 2514 O VAL B 132 -7.662 -0.310 -14.291 1.00 24.44 O -ANISOU 2514 O VAL B 132 2696 2861 3729 360 -383 1173 O -ATOM 2515 CB VAL B 132 -7.670 2.073 -12.582 1.00 21.94 C -ANISOU 2515 CB VAL B 132 2397 2953 2985 557 -271 1012 C -ATOM 2516 CG1 VAL B 132 -6.489 1.602 -11.734 1.00 23.13 C -ANISOU 2516 CG1 VAL B 132 2507 3399 2883 675 -150 1014 C -ATOM 2517 CG2 VAL B 132 -8.127 3.478 -12.169 1.00 23.32 C -ANISOU 2517 CG2 VAL B 132 2607 3173 3079 617 -299 863 C -ATOM 2518 N AGLU B 133 -5.674 0.519 -14.997 0.46 25.22 N -ANISOU 2518 N AGLU B 133 3060 3143 3380 243 -466 870 N -ATOM 2519 N BGLU B 133 -5.670 0.526 -14.990 0.08 25.28 N -ANISOU 2519 N BGLU B 133 3068 3152 3387 243 -465 870 N -ATOM 2520 N CGLU B 133 -5.695 0.514 -15.047 0.46 25.27 N -ANISOU 2520 N CGLU B 133 3069 3138 3393 237 -472 868 N -ATOM 2521 CA AGLU B 133 -5.208 -0.730 -15.592 0.46 25.69 C -ANISOU 2521 CA AGLU B 133 3123 3115 3524 226 -481 897 C -ATOM 2522 CA BGLU B 133 -5.177 -0.709 -15.585 0.08 25.84 C -ANISOU 2522 CA BGLU B 133 3144 3140 3534 226 -480 893 C -ATOM 2523 CA CGLU B 133 -5.220 -0.765 -15.577 0.46 25.29 C -ANISOU 2523 CA CGLU B 133 3067 3062 3479 229 -479 902 C -ATOM 2524 C AGLU B 133 -3.907 -1.228 -14.964 0.46 24.86 C -ANISOU 2524 C AGLU B 133 2990 3244 3210 319 -352 914 C -ATOM 2525 C BGLU B 133 -3.937 -1.235 -14.870 0.08 25.18 C -ANISOU 2525 C BGLU B 133 3020 3294 3253 329 -342 926 C -ATOM 2526 C CGLU B 133 -3.957 -1.240 -14.884 0.46 24.97 C -ANISOU 2526 C CGLU B 133 2994 3263 3232 328 -344 926 C -ATOM 2527 O AGLU B 133 -3.084 -0.439 -14.510 0.46 25.60 O -ANISOU 2527 O AGLU B 133 3109 3573 3046 327 -318 813 O -ATOM 2528 O BGLU B 133 -3.183 -0.470 -14.272 0.08 25.38 O -ANISOU 2528 O BGLU B 133 3053 3566 3023 357 -295 841 O -ATOM 2529 O CGLU B 133 -3.199 -0.447 -14.337 0.46 26.00 O -ANISOU 2529 O CGLU B 133 3139 3633 3106 348 -303 835 O -ATOM 2530 CB AGLU B 133 -5.022 -0.539 -17.106 0.46 27.51 C -ANISOU 2530 CB AGLU B 133 3518 3214 3721 92 -663 731 C -ATOM 2531 CB BGLU B 133 -4.850 -0.461 -17.058 0.08 26.81 C -ANISOU 2531 CB BGLU B 133 3438 3157 3591 92 -650 722 C -ATOM 2532 CB CGLU B 133 -4.915 -0.648 -17.075 0.46 27.30 C -ANISOU 2532 CB CGLU B 133 3487 3197 3687 99 -652 733 C -ATOM 2533 CG AGLU B 133 -4.536 -1.767 -17.864 0.46 28.95 C -ANISOU 2533 CG AGLU B 133 3725 3308 3966 101 -712 677 C -ATOM 2534 CG BGLU B 133 -5.933 -0.882 -18.032 0.08 29.23 C -ANISOU 2534 CG BGLU B 133 3746 3212 4149 45 -821 694 C -ATOM 2535 CG CGLU B 133 -6.094 -0.798 -18.005 0.46 29.90 C -ANISOU 2535 CG CGLU B 133 3823 3284 4254 43 -827 702 C -ATOM 2536 CD AGLU B 133 -5.571 -2.870 -17.905 0.46 31.52 C -ANISOU 2536 CD AGLU B 133 3918 3371 4686 123 -761 749 C -ATOM 2537 CD BGLU B 133 -5.624 -2.215 -18.689 0.08 31.48 C -ANISOU 2537 CD BGLU B 133 4027 3378 4557 61 -883 627 C -ATOM 2538 CD CGLU B 133 -5.690 -0.660 -19.463 0.46 30.68 C -ANISOU 2538 CD CGLU B 133 4090 3363 4203 -17 -992 534 C -ATOM 2539 OE1AGLU B 133 -5.835 -3.478 -16.848 0.46 35.94 O -ANISOU 2539 OE1AGLU B 133 4315 3911 5430 206 -604 952 O -ATOM 2540 OE1BGLU B 133 -5.594 -3.236 -17.974 0.08 33.19 O -ANISOU 2540 OE1BGLU B 133 4110 3530 4970 131 -768 749 O -ATOM 2541 OE1CGLU B 133 -5.231 -1.658 -20.061 0.46 30.31 O -ANISOU 2541 OE1CGLU B 133 4065 3279 4171 9 -1042 444 O -ATOM 2542 OE2AGLU B 133 -6.130 -3.122 -18.992 0.46 35.00 O -ANISOU 2542 OE2AGLU B 133 4399 3632 5265 66 -958 606 O -ATOM 2543 OE2BGLU B 133 -5.395 -2.237 -19.917 0.08 31.97 O -ANISOU 2543 OE2BGLU B 133 4216 3415 4514 30 -1039 455 O -ATOM 2544 OE2CGLU B 133 -5.824 0.454 -20.001 0.46 34.35 O -ANISOU 2544 OE2CGLU B 133 4662 3859 4530 -63 -1059 505 O -ATOM 2545 N ASP B 134 -3.718 -2.542 -14.941 1.00 22.86 N -ANISOU 2545 N ASP B 134 2669 2916 3102 394 -291 1030 N -ATOM 2546 CA ASP B 134 -2.513 -3.123 -14.362 1.00 22.99 C -ANISOU 2546 CA ASP B 134 2644 3160 2933 522 -167 1078 C -ATOM 2547 C ASP B 134 -1.311 -2.981 -15.297 1.00 26.91 C -ANISOU 2547 C ASP B 134 3272 3733 3219 436 -247 873 C -ATOM 2548 O ASP B 134 -0.221 -2.578 -14.869 1.00 28.13 O -ANISOU 2548 O ASP B 134 3410 4174 3105 471 -192 810 O -ATOM 2549 CB ASP B 134 -2.736 -4.588 -13.943 1.00 30.78 C -ANISOU 2549 CB ASP B 134 3499 4007 4190 663 -43 1324 C -ATOM 2550 CG ASP B 134 -3.235 -5.474 -15.087 1.00 31.66 C -ANISOU 2550 CG ASP B 134 3649 3721 4658 560 -172 1254 C -ATOM 2551 OD1 ASP B 134 -3.650 -4.944 -16.140 1.00 31.82 O -ANISOU 2551 OD1 ASP B 134 3783 3610 4695 408 -362 1045 O -ATOM 2552 OD2 ASP B 134 -3.217 -6.712 -14.917 1.00 41.44 O -ANISOU 2552 OD2 ASP B 134 4795 4780 6171 654 -89 1405 O -ATOM 2553 N ILE B 135 -1.508 -3.290 -16.574 1.00 27.17 N -ANISOU 2553 N ILE B 135 3414 3542 3366 340 -379 759 N -ATOM 2554 CA ILE B 135 -0.391 -3.311 -17.508 1.00 24.11 C -ANISOU 2554 CA ILE B 135 3135 3257 2770 308 -422 603 C -ATOM 2555 C ILE B 135 -0.815 -3.075 -18.945 1.00 31.77 C -ANISOU 2555 C ILE B 135 4247 4069 3754 210 -593 453 C -ATOM 2556 O ILE B 135 -1.860 -3.561 -19.387 1.00 31.10 O -ANISOU 2556 O ILE B 135 4162 3733 3920 203 -711 428 O -ATOM 2557 CB ILE B 135 0.414 -4.643 -17.384 1.00 35.70 C -ANISOU 2557 CB ILE B 135 4550 4746 4269 463 -337 644 C -ATOM 2558 CG1 ILE B 135 1.654 -4.624 -18.285 1.00 34.41 C -ANISOU 2558 CG1 ILE B 135 4473 4752 3848 464 -353 488 C -ATOM 2559 CG2 ILE B 135 -0.466 -5.849 -17.708 1.00 38.80 C -ANISOU 2559 CG2 ILE B 135 4915 4780 5046 509 -393 676 C -ATOM 2560 CD1 ILE B 135 2.618 -5.774 -18.008 1.00 35.41 C -ANISOU 2560 CD1 ILE B 135 4533 4963 3957 648 -247 529 C -ATOM 2561 N ILE B 136 -0.008 -2.288 -19.655 1.00 29.79 N -ANISOU 2561 N ILE B 136 4095 3988 3237 145 -604 366 N -ATOM 2562 CA AILE B 136 -0.177 -2.057 -21.083 0.49 30.20 C -ANISOU 2562 CA AILE B 136 4286 3994 3196 114 -737 257 C -ATOM 2563 CA BILE B 136 -0.200 -2.088 -21.083 0.51 30.38 C -ANISOU 2563 CA BILE B 136 4307 4010 3225 116 -739 256 C -ATOM 2564 C ILE B 136 0.936 -2.793 -21.816 1.00 32.80 C -ANISOU 2564 C ILE B 136 4657 4467 3338 216 -706 159 C -ATOM 2565 O ILE B 136 2.112 -2.550 -21.549 1.00 32.56 O -ANISOU 2565 O ILE B 136 4583 4667 3120 216 -570 196 O -ATOM 2566 CB AILE B 136 -0.057 -0.566 -21.432 0.49 28.88 C -ANISOU 2566 CB AILE B 136 4189 3920 2865 -9 -728 299 C -ATOM 2567 CB BILE B 136 -0.251 -0.592 -21.456 0.51 29.31 C -ANISOU 2567 CB BILE B 136 4246 3942 2948 -7 -748 297 C -ATOM 2568 CG1AILE B 136 -1.093 0.246 -20.655 0.49 26.70 C -ANISOU 2568 CG1AILE B 136 3872 3509 2762 -81 -750 371 C -ATOM 2569 CG1BILE B 136 -1.515 0.046 -20.870 0.51 26.43 C -ANISOU 2569 CG1BILE B 136 3851 3404 2786 -65 -805 361 C -ATOM 2570 CG2AILE B 136 -0.223 -0.363 -22.944 0.49 31.05 C -ANISOU 2570 CG2AILE B 136 4604 4206 2989 18 -843 245 C -ATOM 2571 CG2BILE B 136 -0.233 -0.404 -22.977 0.51 31.28 C -ANISOU 2571 CG2BILE B 136 4635 4233 3017 23 -848 240 C -ATOM 2572 CD1AILE B 136 -2.520 -0.128 -21.008 0.49 25.71 C -ANISOU 2572 CD1AILE B 136 3754 3159 2853 -51 -905 358 C -ATOM 2573 CD1BILE B 136 -1.562 1.564 -20.961 0.51 24.47 C -ANISOU 2573 CD1BILE B 136 3658 3168 2470 -173 -790 414 C -ATOM 2574 N ASP B 137 0.569 -3.693 -22.720 1.00 31.01 N -ANISOU 2574 N ASP B 137 4493 4114 3174 316 -841 8 N -ATOM 2575 CA ASP B 137 1.545 -4.444 -23.490 1.00 33.07 C -ANISOU 2575 CA ASP B 137 4804 4512 3250 463 -824 -127 C -ATOM 2576 C ASP B 137 1.276 -4.177 -24.969 1.00 35.90 C -ANISOU 2576 C ASP B 137 5302 4942 3395 523 -978 -277 C -ATOM 2577 O ASP B 137 1.900 -3.290 -25.561 1.00 37.05 O -ANISOU 2577 O ASP B 137 5507 5341 3229 510 -900 -196 O -ATOM 2578 CB ASP B 137 1.450 -5.931 -23.140 1.00 34.72 C -ANISOU 2578 CB ASP B 137 4947 4502 3742 590 -845 -214 C -ATOM 2579 CG ASP B 137 2.381 -6.797 -23.974 1.00 39.36 C -ANISOU 2579 CG ASP B 137 5593 5195 4166 782 -848 -406 C -ATOM 2580 OD1 ASP B 137 3.378 -6.266 -24.505 1.00 41.79 O -ANISOU 2580 OD1 ASP B 137 5946 5827 4106 822 -756 -398 O -ATOM 2581 OD2 ASP B 137 2.106 -8.011 -24.091 1.00 38.10 O -ANISOU 2581 OD2 ASP B 137 5419 4781 4278 899 -935 -562 O -ATOM 2582 N THR B 138 0.332 -4.906 -25.567 1.00 36.27 N -ANISOU 2582 N THR B 138 5382 4782 3618 598 -1198 -485 N -ATOM 2583 CA THR B 138 -0.056 -4.597 -26.952 1.00 38.97 C -ANISOU 2583 CA THR B 138 5848 5247 3713 696 -1382 -645 C -ATOM 2584 C THR B 138 -0.884 -3.316 -27.041 1.00 39.79 C -ANISOU 2584 C THR B 138 5981 5360 3777 571 -1430 -476 C -ATOM 2585 O THR B 138 -1.022 -2.739 -28.114 1.00 44.30 O -ANISOU 2585 O THR B 138 6655 6119 4057 661 -1517 -493 O -ATOM 2586 CB THR B 138 -0.872 -5.722 -27.627 1.00 41.37 C -ANISOU 2586 CB THR B 138 6155 5339 4225 823 -1663 -995 C -ATOM 2587 OG1 THR B 138 -2.131 -5.884 -26.955 1.00 44.08 O -ANISOU 2587 OG1 THR B 138 6380 5337 5030 678 -1780 -971 O -ATOM 2588 CG2 THR B 138 -0.097 -7.025 -27.627 1.00 45.55 C -ANISOU 2588 CG2 THR B 138 6667 5801 4838 976 -1632 -1194 C -ATOM 2589 N GLY B 139 -1.460 -2.888 -25.924 1.00 34.32 N -ANISOU 2589 N GLY B 139 5195 4480 3366 401 -1370 -306 N -ATOM 2590 CA GLY B 139 -2.332 -1.725 -25.930 1.00 34.75 C -ANISOU 2590 CA GLY B 139 5268 4497 3439 303 -1421 -164 C -ATOM 2591 C GLY B 139 -3.760 -2.057 -26.344 1.00 40.54 C -ANISOU 2591 C GLY B 139 5967 5039 4397 333 -1689 -311 C -ATOM 2592 O GLY B 139 -4.607 -1.173 -26.413 1.00 41.62 O -ANISOU 2592 O GLY B 139 6108 5143 4565 286 -1759 -208 O -ATOM 2593 N LYS B 140 -4.041 -3.338 -26.590 1.00 39.88 N -ANISOU 2593 N LYS B 140 5828 4810 4516 409 -1846 -563 N -ATOM 2594 CA LYS B 140 -5.352 -3.739 -27.093 1.00 40.37 C -ANISOU 2594 CA LYS B 140 5818 4694 4829 431 -2141 -766 C -ATOM 2595 C LYS B 140 -6.512 -3.647 -26.087 1.00 44.28 C -ANISOU 2595 C LYS B 140 6132 4912 5780 277 -2145 -623 C -ATOM 2596 O LYS B 140 -7.594 -3.179 -26.451 1.00 44.34 O -ANISOU 2596 O LYS B 140 6093 4887 5869 267 -2329 -647 O -ATOM 2597 CB LYS B 140 -5.279 -5.083 -27.837 1.00 48.32 C -ANISOU 2597 CB LYS B 140 6813 5615 5932 568 -2348 -1149 C -ATOM 2598 CG LYS B 140 -4.493 -4.943 -29.150 1.00 60.15 C -ANISOU 2598 CG LYS B 140 8482 7474 6898 784 -2382 -1306 C -ATOM 2599 CD LYS B 140 -4.188 -6.260 -29.855 1.00 70.33 C -ANISOU 2599 CD LYS B 140 9762 8715 8246 957 -2498 -1683 C -ATOM 2600 CE LYS B 140 -3.336 -6.004 -31.101 1.00 75.37 C -ANISOU 2600 CE LYS B 140 10521 9766 8351 1174 -2387 -1716 C -ATOM 2601 NZ LYS B 140 -2.764 -7.248 -31.684 1.00 80.84 N -ANISOU 2601 NZ LYS B 140 11220 10452 9045 1377 -2457 -2061 N -ATOM 2602 N THR B 141 -6.321 -4.066 -24.836 1.00 45.04 N -ANISOU 2602 N THR B 141 6113 4849 6151 189 -1937 -453 N -ATOM 2603 CA ATHR B 141 -7.424 -3.854 -23.898 0.35 44.40 C -ANISOU 2603 CA ATHR B 141 5854 4578 6439 82 -1903 -271 C -ATOM 2604 CA BTHR B 141 -7.302 -3.866 -23.775 0.65 43.16 C -ANISOU 2604 CA BTHR B 141 5698 4427 6272 80 -1868 -248 C -ATOM 2605 C THR B 141 -7.611 -2.371 -23.627 1.00 45.33 C -ANISOU 2605 C THR B 141 6038 4856 6329 44 -1815 -71 C -ATOM 2606 O THR B 141 -8.749 -1.950 -23.394 1.00 46.25 O -ANISOU 2606 O THR B 141 6045 4874 6654 6 -1888 2 O -ATOM 2607 CB ATHR B 141 -7.381 -4.658 -22.553 0.35 41.22 C -ANISOU 2607 CB ATHR B 141 5277 3988 6398 39 -1688 -80 C -ATOM 2608 CB BTHR B 141 -6.751 -4.413 -22.432 0.65 39.89 C -ANISOU 2608 CB BTHR B 141 5183 3945 6029 59 -1593 -38 C -ATOM 2609 OG1ATHR B 141 -7.072 -3.781 -21.462 0.35 39.76 O -ANISOU 2609 OG1ATHR B 141 5094 3962 6052 17 -1442 188 O -ATOM 2610 OG1BTHR B 141 -6.493 -5.817 -22.556 0.65 40.36 O -ANISOU 2610 OG1BTHR B 141 5178 3804 6355 106 -1628 -170 O -ATOM 2611 CG2ATHR B 141 -6.412 -5.809 -22.597 0.35 40.98 C -ANISOU 2611 CG2ATHR B 141 5269 3897 6404 112 -1626 -178 C -ATOM 2612 CG2BTHR B 141 -7.725 -4.176 -21.294 0.65 39.91 C -ANISOU 2612 CG2BTHR B 141 4997 3830 6338 -3 -1481 208 C -ATOM 2613 N MET B 142 -6.550 -1.566 -23.726 1.00 38.18 N -ANISOU 2613 N MET B 142 5294 4176 5037 57 -1674 5 N -ATOM 2614 CA AMET B 142 -6.701 -0.120 -23.523 0.72 34.21 C -ANISOU 2614 CA AMET B 142 4854 3761 4384 15 -1599 173 C -ATOM 2615 CA BMET B 142 -6.672 -0.125 -23.560 0.28 33.03 C -ANISOU 2615 CA BMET B 142 4709 3617 4224 17 -1601 169 C -ATOM 2616 C MET B 142 -7.497 0.535 -24.658 1.00 35.08 C -ANISOU 2616 C MET B 142 5036 3903 4388 73 -1812 131 C -ATOM 2617 O MET B 142 -8.386 1.344 -24.393 1.00 35.02 O -ANISOU 2617 O MET B 142 4986 3827 4493 56 -1839 241 O -ATOM 2618 CB AMET B 142 -5.352 0.596 -23.297 0.72 27.64 C -ANISOU 2618 CB AMET B 142 4130 3115 3259 -18 -1392 268 C -ATOM 2619 CB BMET B 142 -5.298 0.539 -23.473 0.28 28.47 C -ANISOU 2619 CB BMET B 142 4249 3232 3335 -8 -1408 251 C -ATOM 2620 CG AMET B 142 -5.489 2.099 -23.048 0.72 28.23 C -ANISOU 2620 CG AMET B 142 4256 3201 3270 -77 -1318 416 C -ATOM 2621 CG BMET B 142 -5.336 1.796 -22.657 0.28 27.61 C -ANISOU 2621 CG BMET B 142 4135 3119 3235 -85 -1275 406 C -ATOM 2622 SD AMET B 142 -3.912 2.998 -23.064 0.72 40.15 S -ANISOU 2622 SD AMET B 142 5857 4884 4515 -151 -1117 499 S -ATOM 2623 SD BMET B 142 -6.204 1.425 -21.130 0.28 44.71 S -ANISOU 2623 SD BMET B 142 6108 5151 5729 -92 -1204 467 S -ATOM 2624 CE AMET B 142 -3.236 2.437 -24.631 0.72 40.95 C -ANISOU 2624 CE AMET B 142 6075 5171 4312 -46 -1183 442 C -ATOM 2625 CE BMET B 142 -7.763 2.246 -21.400 0.28 21.74 C -ANISOU 2625 CE BMET B 142 3171 2103 2988 -76 -1351 518 C -ATOM 2626 N GLN B 143 -7.190 0.188 -25.903 1.00 45.09 N -ANISOU 2626 N GLN B 143 6408 5306 5419 180 -1961 -26 N -ATOM 2627 CA GLN B 143 -7.963 0.672 -27.050 1.00 49.11 C -ANISOU 2627 CA GLN B 143 6972 5909 5778 296 -2192 -77 C -ATOM 2628 C GLN B 143 -9.445 0.314 -26.905 1.00 51.90 C -ANISOU 2628 C GLN B 143 7142 6075 6503 282 -2416 -178 C -ATOM 2629 O GLN B 143 -10.327 1.117 -27.214 1.00 54.03 O -ANISOU 2629 O GLN B 143 7392 6367 6769 325 -2486 -96 O -ATOM 2630 CB GLN B 143 -7.424 0.067 -28.349 1.00 60.35 C -ANISOU 2630 CB GLN B 143 8483 7549 6900 455 -2275 -288 C -ATOM 2631 CG GLN B 143 -8.471 -0.063 -29.457 1.00 71.00 C -ANISOU 2631 CG GLN B 143 9776 8972 8230 587 -2488 -466 C -ATOM 2632 CD GLN B 143 -8.266 -1.300 -30.323 1.00 79.39 C -ANISOU 2632 CD GLN B 143 10822 10100 9242 712 -2620 -812 C -ATOM 2633 OE1 GLN B 143 -9.117 -2.192 -30.367 1.00 83.49 O -ANISOU 2633 OE1 GLN B 143 11201 10433 10089 706 -2826 -1065 O -ATOM 2634 NE2 GLN B 143 -7.134 -1.356 -31.016 1.00 81.22 N -ANISOU 2634 NE2 GLN B 143 11178 10585 9096 828 -2492 -820 N -ATOM 2635 N THR B 144 -9.702 -0.898 -26.420 1.00 51.31 N -ANISOU 2635 N THR B 144 6906 5803 6787 217 -2465 -331 N -ATOM 2636 CA THR B 144 -11.057 -1.413 -26.237 1.00 51.65 C -ANISOU 2636 CA THR B 144 6713 5634 7279 171 -2661 -424 C -ATOM 2637 C THR B 144 -11.803 -0.650 -25.147 1.00 49.51 C -ANISOU 2637 C THR B 144 6317 5263 7231 89 -2504 -147 C -ATOM 2638 O THR B 144 -12.976 -0.295 -25.308 1.00 48.22 O -ANISOU 2638 O THR B 144 6021 5060 7241 106 -2665 -138 O -ATOM 2639 CB THR B 144 -11.023 -2.917 -25.875 1.00 50.76 C -ANISOU 2639 CB THR B 144 6439 5273 7576 103 -2688 -595 C -ATOM 2640 OG1 THR B 144 -10.498 -3.660 -26.984 1.00 50.51 O -ANISOU 2640 OG1 THR B 144 6511 5322 7358 222 -2839 -914 O -ATOM 2641 CG2 THR B 144 -12.417 -3.429 -25.532 1.00 50.40 C -ANISOU 2641 CG2 THR B 144 6094 4965 8090 17 -2820 -621 C -ATOM 2642 N LEU B 145 -11.113 -0.397 -24.042 1.00 41.95 N -ANISOU 2642 N LEU B 145 5391 4299 6249 27 -2200 58 N -ATOM 2643 CA LEU B 145 -11.692 0.362 -22.947 1.00 42.68 C -ANISOU 2643 CA LEU B 145 5385 4347 6485 -4 -2032 288 C -ATOM 2644 C LEU B 145 -11.943 1.803 -23.376 1.00 47.33 C -ANISOU 2644 C LEU B 145 6107 5042 6832 57 -2067 374 C -ATOM 2645 O LEU B 145 -12.931 2.420 -22.955 1.00 46.61 O -ANISOU 2645 O LEU B 145 5906 4897 6909 82 -2072 482 O -ATOM 2646 CB LEU B 145 -10.771 0.335 -21.738 1.00 44.07 C -ANISOU 2646 CB LEU B 145 5580 4559 6607 -38 -1730 431 C -ATOM 2647 CG LEU B 145 -11.257 -0.526 -20.584 1.00 48.59 C -ANISOU 2647 CG LEU B 145 5911 5003 7549 -58 -1590 560 C -ATOM 2648 CD1 LEU B 145 -12.646 -0.076 -20.178 1.00 57.22 C -ANISOU 2648 CD1 LEU B 145 6813 6026 8903 -42 -1617 678 C -ATOM 2649 CD2 LEU B 145 -11.284 -1.961 -21.014 1.00 45.35 C -ANISOU 2649 CD2 LEU B 145 5395 4419 7416 -93 -1704 432 C -ATOM 2650 N LEU B 146 -11.047 2.329 -24.214 1.00 43.36 N -ANISOU 2650 N LEU B 146 5830 4688 5958 98 -2073 352 N -ATOM 2651 CA LEU B 146 -11.142 3.718 -24.688 1.00 42.16 C -ANISOU 2651 CA LEU B 146 5818 4606 5596 164 -2072 489 C -ATOM 2652 C LEU B 146 -12.230 3.976 -25.741 1.00 46.06 C -ANISOU 2652 C LEU B 146 6282 5150 6069 289 -2320 448 C -ATOM 2653 O LEU B 146 -12.722 5.096 -25.837 1.00 48.63 O -ANISOU 2653 O LEU B 146 6644 5473 6359 350 -2277 593 O -ATOM 2654 CB LEU B 146 -9.796 4.210 -25.215 1.00 38.62 C -ANISOU 2654 CB LEU B 146 5581 4297 4794 163 -1944 548 C -ATOM 2655 CG LEU B 146 -8.751 4.610 -24.188 1.00 36.57 C -ANISOU 2655 CG LEU B 146 5356 4014 4524 47 -1673 630 C -ATOM 2656 CD1 LEU B 146 -7.461 4.946 -24.900 1.00 40.03 C -ANISOU 2656 CD1 LEU B 146 5951 4601 4659 37 -1572 684 C -ATOM 2657 CD2 LEU B 146 -9.240 5.808 -23.381 1.00 34.05 C -ANISOU 2657 CD2 LEU B 146 5018 3567 4352 29 -1576 755 C -ATOM 2658 N SER B 147 -12.597 2.964 -26.528 1.00 52.44 N -ANISOU 2658 N SER B 147 7011 6009 6905 330 -2521 218 N -ATOM 2659 CA SER B 147 -13.702 3.091 -27.497 1.00 55.33 C -ANISOU 2659 CA SER B 147 7301 6464 7257 450 -2716 120 C -ATOM 2660 C SER B 147 -15.037 2.853 -26.799 1.00 54.49 C -ANISOU 2660 C SER B 147 6933 6181 7590 392 -2800 109 C -ATOM 2661 O SER B 147 -16.046 3.517 -27.063 1.00 58.23 O -ANISOU 2661 O SER B 147 7331 6696 8097 474 -2871 167 O -ATOM 2662 CB SER B 147 -13.513 2.129 -28.658 1.00 62.39 C -ANISOU 2662 CB SER B 147 8211 7505 7989 535 -2884 -164 C -ATOM 2663 OG SER B 147 -12.300 2.420 -29.327 1.00 69.73 O -ANISOU 2663 OG SER B 147 9354 8647 8491 615 -2765 -111 O -ATOM 2664 N LEU B 148 -15.019 1.904 -25.878 1.00 55.49 N -ANISOU 2664 N LEU B 148 6899 6122 8062 260 -2765 70 N -ATOM 2665 CA LEU B 148 -15.950 1.914 -24.769 1.00 62.47 C -ANISOU 2665 CA LEU B 148 7538 6845 9352 192 -2689 209 C -ATOM 2666 C LEU B 148 -15.649 3.222 -24.023 1.00 68.14 C -ANISOU 2666 C LEU B 148 8384 7602 9904 230 -2461 458 C -ATOM 2667 O LEU B 148 -14.696 3.927 -24.354 1.00 70.16 O -ANISOU 2667 O LEU B 148 8889 7950 9819 265 -2382 510 O -ATOM 2668 CB LEU B 148 -15.681 0.709 -23.874 1.00 65.39 C -ANISOU 2668 CB LEU B 148 7729 7038 10078 67 -2614 207 C -ATOM 2669 CG LEU B 148 -16.868 0.003 -23.236 1.00 68.30 C -ANISOU 2669 CG LEU B 148 7749 7220 10983 -11 -2607 252 C -ATOM 2670 CD1 LEU B 148 -17.877 -0.297 -24.305 1.00 72.65 C -ANISOU 2670 CD1 LEU B 148 8208 7756 11641 13 -2862 19 C -ATOM 2671 CD2 LEU B 148 -16.421 -1.281 -22.547 1.00 68.97 C -ANISOU 2671 CD2 LEU B 148 7675 7117 11414 -121 -2509 275 C -ATOM 2672 N VAL B 149 -16.439 3.560 -23.016 1.00 65.43 N -ANISOU 2672 N VAL B 149 7868 7186 9807 229 -2326 601 N -ATOM 2673 CA VAL B 149 -16.316 4.873 -22.384 1.00 56.55 C -ANISOU 2673 CA VAL B 149 6861 6089 8535 296 -2122 758 C -ATOM 2674 C VAL B 149 -16.579 6.032 -23.365 1.00 50.05 C -ANISOU 2674 C VAL B 149 6197 5337 7482 410 -2209 782 C -ATOM 2675 O VAL B 149 -17.472 6.833 -23.125 1.00 51.02 O -ANISOU 2675 O VAL B 149 6248 5447 7688 501 -2173 863 O -ATOM 2676 CB VAL B 149 -14.955 5.107 -21.701 1.00 51.36 C -ANISOU 2676 CB VAL B 149 6384 5437 7692 251 -1918 809 C -ATOM 2677 CG1 VAL B 149 -14.980 6.437 -21.001 1.00 48.78 C -ANISOU 2677 CG1 VAL B 149 6137 5096 7300 321 -1744 902 C -ATOM 2678 CG2 VAL B 149 -14.621 3.981 -20.719 1.00 50.86 C -ANISOU 2678 CG2 VAL B 149 6174 5348 7800 177 -1780 820 C -ATOM 2679 N ARG B 150 -15.808 6.124 -24.452 1.00 43.75 N -ANISOU 2679 N ARG B 150 5604 4631 6389 433 -2298 737 N -ATOM 2680 CA ARG B 150 -15.949 7.238 -25.396 1.00 50.57 C -ANISOU 2680 CA ARG B 150 6613 5582 7019 569 -2328 834 C -ATOM 2681 C ARG B 150 -17.293 7.230 -26.106 1.00 51.94 C -ANISOU 2681 C ARG B 150 6631 5843 7261 694 -2530 788 C -ATOM 2682 O ARG B 150 -17.748 8.260 -26.619 1.00 47.15 O -ANISOU 2682 O ARG B 150 6079 5295 6539 844 -2531 921 O -ATOM 2683 CB ARG B 150 -14.798 7.279 -26.407 1.00 52.80 C -ANISOU 2683 CB ARG B 150 7117 5998 6948 592 -2328 844 C -ATOM 2684 CG ARG B 150 -13.643 8.138 -25.924 1.00 52.89 C -ANISOU 2684 CG ARG B 150 7312 5923 6863 525 -2089 1002 C -ATOM 2685 CD ARG B 150 -12.451 8.143 -26.846 1.00 53.79 C -ANISOU 2685 CD ARG B 150 7606 6180 6653 535 -2043 1054 C -ATOM 2686 NE ARG B 150 -11.368 8.899 -26.227 1.00 55.88 N -ANISOU 2686 NE ARG B 150 7993 6318 6921 422 -1816 1189 N -ATOM 2687 CZ ARG B 150 -10.081 8.734 -26.500 1.00 55.87 C -ANISOU 2687 CZ ARG B 150 8106 6396 6726 350 -1715 1225 C -ATOM 2688 NH1 ARG B 150 -9.701 7.831 -27.396 1.00 54.46 N -ANISOU 2688 NH1 ARG B 150 7950 6444 6299 410 -1804 1128 N -ATOM 2689 NH2 ARG B 150 -9.175 9.474 -25.872 1.00 54.24 N -ANISOU 2689 NH2 ARG B 150 7973 6048 6588 222 -1525 1334 N -ATOM 2690 N GLN B 151 -17.936 6.068 -26.112 1.00 52.68 N -ANISOU 2690 N GLN B 151 6510 5931 7575 632 -2697 607 N -ATOM 2691 CA GLN B 151 -19.255 5.940 -26.716 1.00 55.77 C -ANISOU 2691 CA GLN B 151 6704 6404 8082 724 -2905 522 C -ATOM 2692 C GLN B 151 -20.318 6.575 -25.825 1.00 53.36 C -ANISOU 2692 C GLN B 151 6221 6013 8039 757 -2807 665 C -ATOM 2693 O GLN B 151 -21.414 6.886 -26.289 1.00 58.96 O -ANISOU 2693 O GLN B 151 6792 6814 8796 875 -2938 666 O -ATOM 2694 CB GLN B 151 -19.595 4.465 -26.972 1.00 62.41 C -ANISOU 2694 CB GLN B 151 7349 7210 9154 620 -3101 256 C -ATOM 2695 CG GLN B 151 -20.196 3.739 -25.765 1.00 65.48 C -ANISOU 2695 CG GLN B 151 7462 7385 10034 466 -3020 278 C -ATOM 2696 CD GLN B 151 -20.465 2.260 -26.031 1.00 70.74 C -ANISOU 2696 CD GLN B 151 7935 7937 11007 348 -3186 30 C -ATOM 2697 OE1 GLN B 151 -19.631 1.562 -26.611 1.00 72.51 O -ANISOU 2697 OE1 GLN B 151 8290 8170 11090 328 -3264 -156 O -ATOM 2698 NE2 GLN B 151 -21.632 1.779 -25.606 1.00 71.18 N -ANISOU 2698 NE2 GLN B 151 7674 7870 11500 279 -3221 28 N -ATOM 2699 N TYR B 152 -19.998 6.758 -24.547 1.00 49.88 N -ANISOU 2699 N TYR B 152 5774 5436 7744 678 -2569 777 N -ATOM 2700 CA TYR B 152 -20.941 7.367 -23.618 1.00 53.56 C -ANISOU 2700 CA TYR B 152 6078 5857 8415 744 -2433 900 C -ATOM 2701 C TYR B 152 -20.677 8.856 -23.433 1.00 51.73 C -ANISOU 2701 C TYR B 152 6057 5604 7996 882 -2273 1041 C -ATOM 2702 O TYR B 152 -21.212 9.463 -22.516 1.00 53.59 O -ANISOU 2702 O TYR B 152 6213 5792 8357 959 -2120 1117 O -ATOM 2703 CB TYR B 152 -20.941 6.634 -22.268 1.00 54.27 C -ANISOU 2703 CB TYR B 152 5984 5857 8779 628 -2248 934 C -ATOM 2704 CG TYR B 152 -21.515 5.237 -22.373 1.00 62.63 C -ANISOU 2704 CG TYR B 152 6765 6868 10162 498 -2382 841 C -ATOM 2705 CD1 TYR B 152 -22.889 5.038 -22.457 1.00 65.17 C -ANISOU 2705 CD1 TYR B 152 6801 7202 10760 521 -2479 840 C -ATOM 2706 CD2 TYR B 152 -20.685 4.121 -22.413 1.00 64.36 C -ANISOU 2706 CD2 TYR B 152 7003 7008 10444 355 -2413 749 C -ATOM 2707 CE1 TYR B 152 -23.422 3.769 -22.571 1.00 68.29 C -ANISOU 2707 CE1 TYR B 152 6931 7497 11518 380 -2596 744 C -ATOM 2708 CE2 TYR B 152 -21.208 2.843 -22.526 1.00 66.70 C -ANISOU 2708 CE2 TYR B 152 7047 7191 11107 233 -2531 650 C -ATOM 2709 CZ TYR B 152 -22.582 2.675 -22.607 1.00 70.74 C -ANISOU 2709 CZ TYR B 152 7275 7682 11921 235 -2619 646 C -ATOM 2710 OH TYR B 152 -23.130 1.413 -22.723 1.00 72.28 O -ANISOU 2710 OH TYR B 152 7215 7712 12537 100 -2723 541 O -ATOM 2711 N ASN B 153 -19.858 9.433 -24.310 1.00 48.32 N -ANISOU 2711 N ASN B 153 5881 5198 7281 923 -2298 1078 N -ATOM 2712 CA ASN B 153 -19.530 10.863 -24.256 1.00 48.67 C -ANISOU 2712 CA ASN B 153 6125 5158 7209 1036 -2143 1228 C -ATOM 2713 C ASN B 153 -19.172 11.410 -22.871 1.00 48.26 C -ANISOU 2713 C ASN B 153 6105 4947 7284 1002 -1910 1237 C -ATOM 2714 O ASN B 153 -19.887 12.245 -22.318 1.00 51.21 O -ANISOU 2714 O ASN B 153 6431 5253 7773 1138 -1828 1286 O -ATOM 2715 CB ASN B 153 -20.662 11.693 -24.855 1.00 53.03 C -ANISOU 2715 CB ASN B 153 6620 5769 7761 1253 -2223 1335 C -ATOM 2716 CG ASN B 153 -20.958 11.316 -26.291 1.00 58.72 C -ANISOU 2716 CG ASN B 153 7319 6703 8288 1341 -2459 1324 C -ATOM 2717 OD1 ASN B 153 -20.105 11.456 -27.171 1.00 61.18 O -ANISOU 2717 OD1 ASN B 153 7818 7092 8336 1364 -2469 1387 O -ATOM 2718 ND2 ASN B 153 -22.181 10.854 -26.543 1.00 63.02 N -ANISOU 2718 ND2 ASN B 153 7616 7373 8954 1408 -2646 1246 N -ATOM 2719 N PRO B 154 -18.058 10.939 -22.308 1.00 42.72 N -ANISOU 2719 N PRO B 154 5482 4205 6547 850 -1814 1173 N -ATOM 2720 CA PRO B 154 -17.580 11.480 -21.031 1.00 41.75 C -ANISOU 2720 CA PRO B 154 5399 3963 6500 846 -1623 1149 C -ATOM 2721 C PRO B 154 -17.057 12.894 -21.241 1.00 42.02 C -ANISOU 2721 C PRO B 154 5651 3822 6493 900 -1542 1212 C -ATOM 2722 O PRO B 154 -16.805 13.283 -22.386 1.00 41.52 O -ANISOU 2722 O PRO B 154 5717 3756 6302 910 -1591 1320 O -ATOM 2723 CB PRO B 154 -16.425 10.550 -20.679 1.00 39.06 C -ANISOU 2723 CB PRO B 154 5096 3659 6087 677 -1583 1076 C -ATOM 2724 CG PRO B 154 -15.943 10.075 -22.015 1.00 39.56 C -ANISOU 2724 CG PRO B 154 5262 3794 5973 603 -1720 1087 C -ATOM 2725 CD PRO B 154 -17.143 9.929 -22.865 1.00 40.93 C -ANISOU 2725 CD PRO B 154 5317 4052 6184 706 -1893 1108 C -ATOM 2726 N LYS B 155 -16.907 13.659 -20.165 1.00 45.90 N -ANISOU 2726 N LYS B 155 6170 4161 7108 956 -1419 1150 N -ATOM 2727 CA LYS B 155 -16.326 14.992 -20.280 1.00 49.04 C -ANISOU 2727 CA LYS B 155 6760 4314 7558 973 -1340 1177 C -ATOM 2728 C LYS B 155 -14.840 14.874 -20.630 1.00 44.06 C -ANISOU 2728 C LYS B 155 6284 3630 6826 769 -1303 1178 C -ATOM 2729 O LYS B 155 -14.321 15.639 -21.454 1.00 42.44 O -ANISOU 2729 O LYS B 155 6222 3303 6602 735 -1255 1310 O -ATOM 2730 CB LYS B 155 -16.529 15.794 -18.992 1.00 52.49 C -ANISOU 2730 CB LYS B 155 7177 4578 8190 1100 -1255 1029 C -ATOM 2731 CG LYS B 155 -16.100 17.246 -19.095 1.00 57.32 C -ANISOU 2731 CG LYS B 155 7961 4870 8949 1121 -1179 1020 C -ATOM 2732 CD LYS B 155 -16.617 18.063 -17.928 1.00 64.12 C -ANISOU 2732 CD LYS B 155 8781 5571 10011 1319 -1129 824 C -ATOM 2733 CE LYS B 155 -15.600 18.147 -16.812 1.00 66.95 C -ANISOU 2733 CE LYS B 155 9172 5814 10453 1257 -1103 525 C -ATOM 2734 NZ LYS B 155 -16.011 19.153 -15.786 1.00 74.42 N -ANISOU 2734 NZ LYS B 155 10103 6586 11586 1482 -1059 257 N -ATOM 2735 N MET B 156 -14.172 13.914 -19.998 1.00 38.72 N -ANISOU 2735 N MET B 156 5563 3056 6092 651 -1307 1064 N -ATOM 2736 CA MET B 156 -12.781 13.590 -20.301 1.00 41.49 C -ANISOU 2736 CA MET B 156 6030 3410 6323 458 -1280 1062 C -ATOM 2737 C MET B 156 -12.487 12.131 -19.924 1.00 39.14 C -ANISOU 2737 C MET B 156 5619 3366 5886 376 -1288 967 C -ATOM 2738 O MET B 156 -13.150 11.556 -19.044 1.00 36.10 O -ANISOU 2738 O MET B 156 5070 3089 5559 453 -1270 891 O -ATOM 2739 CB MET B 156 -11.815 14.549 -19.571 1.00 48.68 C -ANISOU 2739 CB MET B 156 7019 4119 7358 367 -1155 922 C -ATOM 2740 CG MET B 156 -11.597 14.235 -18.080 1.00 53.22 C -ANISOU 2740 CG MET B 156 7475 4824 7925 377 -1078 639 C -ATOM 2741 SD MET B 156 -10.185 15.045 -17.244 1.00 53.77 S -ANISOU 2741 SD MET B 156 7584 4769 8077 230 -981 359 S -ATOM 2742 CE MET B 156 -10.449 16.763 -17.645 1.00 46.10 C -ANISOU 2742 CE MET B 156 6737 3324 7456 268 -984 406 C -ATOM 2743 N VAL B 157 -11.523 11.516 -20.614 1.00 35.27 N -ANISOU 2743 N VAL B 157 5202 2979 5221 240 -1293 995 N -ATOM 2744 CA AVAL B 157 -11.039 10.186 -20.243 0.69 35.14 C -ANISOU 2744 CA AVAL B 157 5094 3164 5093 160 -1271 896 C -ATOM 2745 CA BVAL B 157 -11.037 10.193 -20.250 0.31 35.34 C -ANISOU 2745 CA BVAL B 157 5121 3189 5119 160 -1271 897 C -ATOM 2746 C VAL B 157 -9.536 10.221 -20.055 1.00 35.58 C -ANISOU 2746 C VAL B 157 5223 3266 5029 10 -1152 822 C -ATOM 2747 O VAL B 157 -8.811 10.809 -20.863 1.00 36.50 O -ANISOU 2747 O VAL B 157 5466 3316 5088 -67 -1129 912 O -ATOM 2748 CB AVAL B 157 -11.322 9.105 -21.310 0.69 36.62 C -ANISOU 2748 CB AVAL B 157 5262 3472 5179 164 -1422 948 C -ATOM 2749 CB BVAL B 157 -11.382 9.135 -21.313 0.31 36.16 C -ANISOU 2749 CB BVAL B 157 5202 3409 5128 170 -1426 952 C -ATOM 2750 CG1AVAL B 157 -11.333 7.731 -20.667 0.69 28.89 C -ANISOU 2750 CG1AVAL B 157 4128 2612 4236 131 -1405 855 C -ATOM 2751 CG1BVAL B 157 -12.843 8.982 -21.392 0.31 38.11 C -ANISOU 2751 CG1BVAL B 157 5312 3635 5533 296 -1558 988 C -ATOM 2752 CG2AVAL B 157 -12.621 9.364 -22.000 0.69 40.94 C -ANISOU 2752 CG2AVAL B 157 5764 3986 5806 297 -1575 1029 C -ATOM 2753 CG2BVAL B 157 -10.843 9.535 -22.681 0.31 36.19 C -ANISOU 2753 CG2BVAL B 157 5377 3426 4948 162 -1482 1069 C -ATOM 2754 N LYS B 158 -9.080 9.598 -18.977 1.00 29.38 N -ANISOU 2754 N LYS B 158 4336 2614 4212 -14 -1065 684 N -ATOM 2755 CA LYS B 158 -7.662 9.499 -18.707 1.00 34.54 C -ANISOU 2755 CA LYS B 158 5012 3362 4748 -140 -970 591 C -ATOM 2756 C LYS B 158 -7.412 8.043 -18.391 1.00 32.52 C -ANISOU 2756 C LYS B 158 4658 3317 4381 -128 -950 568 C -ATOM 2757 O LYS B 158 -8.324 7.335 -17.942 1.00 30.39 O -ANISOU 2757 O LYS B 158 4273 3085 4187 -27 -968 599 O -ATOM 2758 CB LYS B 158 -7.265 10.368 -17.511 1.00 36.13 C -ANISOU 2758 CB LYS B 158 5171 3533 5026 -139 -890 405 C -ATOM 2759 CG LYS B 158 -7.535 11.854 -17.684 1.00 43.70 C -ANISOU 2759 CG LYS B 158 6214 4207 6184 -143 -904 395 C -ATOM 2760 CD LYS B 158 -6.586 12.481 -18.685 1.00 46.36 C -ANISOU 2760 CD LYS B 158 6658 4398 6559 -314 -874 508 C -ATOM 2761 CE LYS B 158 -6.898 13.962 -18.891 1.00 50.64 C -ANISOU 2761 CE LYS B 158 7278 4588 7373 -313 -870 552 C -ATOM 2762 NZ LYS B 158 -5.784 14.622 -19.612 1.00 50.49 N -ANISOU 2762 NZ LYS B 158 7313 4416 7457 -504 -788 673 N -ATOM 2763 N VAL B 159 -6.183 7.589 -18.623 1.00 26.05 N -ANISOU 2763 N VAL B 159 3865 2618 3415 -224 -900 537 N -ATOM 2764 CA VAL B 159 -5.825 6.210 -18.309 1.00 23.41 C -ANISOU 2764 CA VAL B 159 3443 2456 2993 -195 -867 522 C -ATOM 2765 C VAL B 159 -4.661 6.214 -17.330 1.00 27.20 C -ANISOU 2765 C VAL B 159 3856 3113 3366 -219 -753 407 C -ATOM 2766 O VAL B 159 -3.682 6.935 -17.530 1.00 28.12 O -ANISOU 2766 O VAL B 159 4015 3236 3433 -332 -724 343 O -ATOM 2767 CB VAL B 159 -5.421 5.436 -19.573 1.00 25.07 C -ANISOU 2767 CB VAL B 159 3732 2698 3096 -233 -932 569 C -ATOM 2768 CG1 VAL B 159 -5.007 4.016 -19.225 1.00 23.82 C -ANISOU 2768 CG1 VAL B 159 3486 2663 2901 -192 -894 540 C -ATOM 2769 CG2 VAL B 159 -6.567 5.429 -20.590 1.00 30.38 C -ANISOU 2769 CG2 VAL B 159 4454 3248 3839 -181 -1090 636 C -ATOM 2770 N ALA B 160 -4.783 5.430 -16.261 1.00 20.02 N -ANISOU 2770 N ALA B 160 2817 2358 2433 -101 -687 398 N -ATOM 2771 CA ALA B 160 -3.678 5.208 -15.336 1.00 21.80 C -ANISOU 2771 CA ALA B 160 2956 2826 2503 -71 -597 298 C -ATOM 2772 C ALA B 160 -3.318 3.743 -15.482 1.00 29.12 C -ANISOU 2772 C ALA B 160 3836 3857 3373 -20 -554 405 C -ATOM 2773 O ALA B 160 -4.196 2.890 -15.402 1.00 30.42 O -ANISOU 2773 O ALA B 160 3944 3954 3661 67 -546 536 O -ATOM 2774 CB ALA B 160 -4.105 5.478 -13.915 1.00 22.56 C -ANISOU 2774 CB ALA B 160 2933 3068 2570 98 -539 229 C -ATOM 2775 N SER B 161 -2.036 3.446 -15.672 1.00 25.22 N -ANISOU 2775 N SER B 161 3341 3509 2732 -70 -521 352 N -ATOM 2776 CA SER B 161 -1.604 2.061 -15.756 1.00 22.46 C -ANISOU 2776 CA SER B 161 2948 3249 2339 9 -471 438 C -ATOM 2777 C SER B 161 -0.394 1.877 -14.857 1.00 24.34 C -ANISOU 2777 C SER B 161 3074 3788 2387 82 -384 375 C -ATOM 2778 O SER B 161 0.568 2.657 -14.938 1.00 25.57 O -ANISOU 2778 O SER B 161 3224 4051 2442 -25 -397 235 O -ATOM 2779 CB SER B 161 -1.303 1.670 -17.219 1.00 26.19 C -ANISOU 2779 CB SER B 161 3540 3607 2803 -81 -539 441 C -ATOM 2780 OG SER B 161 -0.997 0.288 -17.315 1.00 26.60 O -ANISOU 2780 OG SER B 161 3554 3688 2863 17 -507 488 O -ATOM 2781 N LEU B 162 -0.459 0.900 -13.952 1.00 22.23 N -ANISOU 2781 N LEU B 162 2691 3665 2092 272 -293 492 N -ATOM 2782 CA LEU B 162 0.693 0.603 -13.100 1.00 24.36 C -ANISOU 2782 CA LEU B 162 2839 4273 2145 395 -220 453 C -ATOM 2783 C LEU B 162 1.948 0.360 -13.932 1.00 24.69 C -ANISOU 2783 C LEU B 162 2908 4375 2097 297 -232 383 C -ATOM 2784 O LEU B 162 3.018 0.913 -13.651 1.00 26.80 O -ANISOU 2784 O LEU B 162 3096 4873 2215 255 -240 235 O -ATOM 2785 CB LEU B 162 0.444 -0.626 -12.214 1.00 25.27 C -ANISOU 2785 CB LEU B 162 2835 4508 2257 648 -91 684 C -ATOM 2786 CG LEU B 162 1.619 -0.892 -11.276 1.00 29.84 C -ANISOU 2786 CG LEU B 162 3277 5497 2565 829 -26 658 C -ATOM 2787 CD1 LEU B 162 1.770 0.245 -10.258 1.00 30.11 C -ANISOU 2787 CD1 LEU B 162 3224 5822 2393 890 -72 447 C -ATOM 2788 CD2 LEU B 162 1.464 -2.219 -10.543 1.00 33.65 C -ANISOU 2788 CD2 LEU B 162 3651 6077 3058 1104 131 965 C -ATOM 2789 N LEU B 163 1.818 -0.483 -14.946 1.00 23.75 N -ANISOU 2789 N LEU B 163 2881 4065 2079 275 -239 469 N -ATOM 2790 CA LEU B 163 2.964 -0.860 -15.773 1.00 24.70 C -ANISOU 2790 CA LEU B 163 3024 4269 2090 239 -228 418 C -ATOM 2791 C LEU B 163 2.705 -0.618 -17.251 1.00 22.85 C -ANISOU 2791 C LEU B 163 2950 3824 1908 100 -306 381 C -ATOM 2792 O LEU B 163 1.583 -0.793 -17.739 1.00 25.89 O -ANISOU 2792 O LEU B 163 3426 3961 2450 88 -383 416 O -ATOM 2793 CB LEU B 163 3.298 -2.334 -15.582 1.00 26.73 C -ANISOU 2793 CB LEU B 163 3227 4568 2360 438 -151 532 C -ATOM 2794 CG LEU B 163 3.431 -2.858 -14.161 1.00 31.13 C -ANISOU 2794 CG LEU B 163 3626 5343 2859 655 -48 662 C -ATOM 2795 CD1 LEU B 163 3.677 -4.374 -14.174 1.00 32.44 C -ANISOU 2795 CD1 LEU B 163 3760 5447 3119 851 40 825 C -ATOM 2796 CD2 LEU B 163 4.545 -2.138 -13.397 1.00 27.96 C -ANISOU 2796 CD2 LEU B 163 3090 5338 2194 677 -40 535 C -ATOM 2797 N VAL B 164 3.755 -0.221 -17.961 1.00 23.15 N -ANISOU 2797 N VAL B 164 2999 3994 1803 14 -284 321 N -ATOM 2798 CA VAL B 164 3.732 -0.122 -19.410 1.00 24.85 C -ANISOU 2798 CA VAL B 164 3353 4113 1976 -45 -324 318 C -ATOM 2799 C VAL B 164 4.978 -0.834 -19.896 1.00 27.01 C -ANISOU 2799 C VAL B 164 3583 4598 2079 43 -244 297 C -ATOM 2800 O VAL B 164 6.073 -0.492 -19.468 1.00 25.56 O -ANISOU 2800 O VAL B 164 3262 4649 1799 5 -159 285 O -ATOM 2801 CB VAL B 164 3.796 1.340 -19.884 1.00 27.11 C -ANISOU 2801 CB VAL B 164 3678 4367 2257 -235 -328 332 C -ATOM 2802 CG1 VAL B 164 3.907 1.393 -21.422 1.00 32.15 C -ANISOU 2802 CG1 VAL B 164 4446 4995 2773 -235 -335 386 C -ATOM 2803 CG2 VAL B 164 2.556 2.085 -19.453 1.00 25.73 C -ANISOU 2803 CG2 VAL B 164 3551 3973 2252 -294 -408 341 C -ATOM 2804 N LYS B 165 4.820 -1.830 -20.765 1.00 25.55 N -ANISOU 2804 N LYS B 165 3496 4340 1870 174 -282 264 N -ATOM 2805 CA LYS B 165 5.979 -2.558 -21.305 1.00 28.28 C -ANISOU 2805 CA LYS B 165 3811 4893 2042 305 -202 224 C -ATOM 2806 C LYS B 165 6.591 -1.815 -22.487 1.00 27.58 C -ANISOU 2806 C LYS B 165 3771 4963 1746 241 -153 245 C -ATOM 2807 O LYS B 165 5.868 -1.262 -23.308 1.00 30.59 O -ANISOU 2807 O LYS B 165 4283 5231 2109 188 -227 265 O -ATOM 2808 CB LYS B 165 5.571 -3.957 -21.772 1.00 31.15 C -ANISOU 2808 CB LYS B 165 4257 5092 2486 502 -273 132 C -ATOM 2809 CG LYS B 165 5.379 -4.961 -20.654 1.00 33.44 C -ANISOU 2809 CG LYS B 165 4454 5267 2986 620 -244 182 C -ATOM 2810 CD LYS B 165 5.405 -6.396 -21.213 1.00 36.50 C -ANISOU 2810 CD LYS B 165 4893 5495 3481 825 -282 74 C -ATOM 2811 CE LYS B 165 5.449 -7.391 -20.071 1.00 34.31 C -ANISOU 2811 CE LYS B 165 4496 5120 3420 966 -195 204 C -ATOM 2812 NZ LYS B 165 5.377 -8.787 -20.552 1.00 27.66 N -ANISOU 2812 NZ LYS B 165 3695 4020 2793 1154 -235 98 N -ATOM 2813 N ARG B 166 7.919 -1.818 -22.591 1.00 28.88 N -ANISOU 2813 N ARG B 166 3911 4311 2749 -304 -42 69 N -ATOM 2814 CA ARG B 166 8.569 -1.302 -23.798 1.00 27.52 C -ANISOU 2814 CA ARG B 166 3671 4199 2588 -448 -42 102 C -ATOM 2815 C ARG B 166 8.510 -2.375 -24.868 1.00 35.26 C -ANISOU 2815 C ARG B 166 4696 5228 3472 -473 21 134 C -ATOM 2816 O ARG B 166 9.372 -3.260 -24.943 1.00 35.52 O -ANISOU 2816 O ARG B 166 4722 5343 3430 -417 73 84 O -ATOM 2817 CB ARG B 166 10.018 -0.866 -23.531 1.00 26.56 C -ANISOU 2817 CB ARG B 166 3431 4161 2498 -453 -52 5 C -ATOM 2818 CG ARG B 166 10.123 0.514 -22.875 1.00 30.83 C -ANISOU 2818 CG ARG B 166 3905 4643 3168 -499 -111 -39 C -ATOM 2819 CD ARG B 166 11.566 1.001 -22.724 1.00 33.61 C -ANISOU 2819 CD ARG B 166 4093 5077 3602 -541 -114 -181 C -ATOM 2820 NE ARG B 166 12.372 0.062 -21.946 1.00 35.90 N -ANISOU 2820 NE ARG B 166 4330 5502 3810 -366 -160 -319 N -ATOM 2821 CZ ARG B 166 12.366 -0.017 -20.619 1.00 37.15 C -ANISOU 2821 CZ ARG B 166 4499 5684 3932 -184 -255 -429 C -ATOM 2822 NH1 ARG B 166 11.600 0.802 -19.901 1.00 31.22 N -ANISOU 2822 NH1 ARG B 166 3801 4823 3238 -178 -310 -418 N -ATOM 2823 NH2 ARG B 166 13.131 -0.918 -20.008 1.00 37.84 N -ANISOU 2823 NH2 ARG B 166 4563 5907 3906 20 -291 -546 N -ATOM 2824 N THR B 167 7.470 -2.295 -25.686 1.00 32.83 N -ANISOU 2824 N THR B 167 4434 4876 3163 -539 6 202 N -ATOM 2825 CA THR B 167 7.186 -3.319 -26.678 1.00 36.92 C -ANISOU 2825 CA THR B 167 4999 5434 3595 -557 43 202 C -ATOM 2826 C THR B 167 6.412 -2.664 -27.834 1.00 41.35 C -ANISOU 2826 C THR B 167 5580 5991 4140 -628 -20 271 C -ATOM 2827 O THR B 167 5.703 -1.669 -27.617 1.00 42.74 O -ANISOU 2827 O THR B 167 5748 6109 4383 -637 -82 316 O -ATOM 2828 CB THR B 167 6.382 -4.457 -26.019 1.00 39.25 C -ANISOU 2828 CB THR B 167 5341 5669 3904 -487 96 141 C -ATOM 2829 OG1 THR B 167 6.238 -5.552 -26.930 1.00 46.99 O -ANISOU 2829 OG1 THR B 167 6360 6680 4814 -514 148 104 O -ATOM 2830 CG2 THR B 167 5.020 -3.955 -25.592 1.00 32.65 C -ANISOU 2830 CG2 THR B 167 4494 4735 3175 -497 50 150 C -ATOM 2831 N PRO B 168 6.565 -3.193 -29.068 1.00 40.15 N -ANISOU 2831 N PRO B 168 5470 5906 3878 -650 -5 278 N -ATOM 2832 CA PRO B 168 5.899 -2.540 -30.202 1.00 39.88 C -ANISOU 2832 CA PRO B 168 5483 5888 3783 -660 -78 339 C -ATOM 2833 C PRO B 168 4.392 -2.421 -29.995 1.00 40.78 C -ANISOU 2833 C PRO B 168 5569 5967 3960 -636 -182 301 C -ATOM 2834 O PRO B 168 3.762 -3.377 -29.545 1.00 38.81 O -ANISOU 2834 O PRO B 168 5280 5698 3770 -636 -173 198 O -ATOM 2835 CB PRO B 168 6.191 -3.487 -31.371 1.00 40.36 C -ANISOU 2835 CB PRO B 168 5604 6032 3701 -654 -53 309 C -ATOM 2836 CG PRO B 168 7.469 -4.165 -31.003 1.00 37.53 C -ANISOU 2836 CG PRO B 168 5229 5697 3332 -663 64 288 C -ATOM 2837 CD PRO B 168 7.372 -4.352 -29.497 1.00 38.30 C -ANISOU 2837 CD PRO B 168 5263 5738 3550 -638 76 233 C -ATOM 2838 N ARG B 169 3.824 -1.267 -30.339 1.00 42.66 N -ANISOU 2838 N ARG B 169 5828 6188 4193 -610 -257 379 N -ATOM 2839 CA ARG B 169 2.428 -0.996 -30.021 1.00 52.65 C -ANISOU 2839 CA ARG B 169 7040 7425 5540 -573 -359 342 C -ATOM 2840 C ARG B 169 1.726 -0.238 -31.155 1.00 60.95 C -ANISOU 2840 C ARG B 169 8144 8535 6479 -489 -474 393 C -ATOM 2841 O ARG B 169 1.909 0.971 -31.313 1.00 65.24 O -ANISOU 2841 O ARG B 169 8764 9036 6987 -450 -462 522 O -ATOM 2842 CB ARG B 169 2.357 -0.213 -28.705 1.00 55.52 C -ANISOU 2842 CB ARG B 169 7372 7681 6042 -580 -330 385 C -ATOM 2843 CG ARG B 169 1.123 -0.484 -27.861 1.00 55.70 C -ANISOU 2843 CG ARG B 169 7316 7645 6201 -560 -362 310 C -ATOM 2844 CD ARG B 169 1.272 0.091 -26.459 1.00 52.27 C -ANISOU 2844 CD ARG B 169 6882 7101 5876 -549 -308 346 C -ATOM 2845 NE ARG B 169 2.123 -0.747 -25.622 1.00 57.82 N -ANISOU 2845 NE ARG B 169 7599 7783 6588 -549 -206 296 N -ATOM 2846 CZ ARG B 169 3.236 -0.335 -25.025 1.00 53.00 C -ANISOU 2846 CZ ARG B 169 7010 7164 5963 -542 -173 319 C -ATOM 2847 NH1 ARG B 169 3.641 0.918 -25.155 1.00 50.81 N -ANISOU 2847 NH1 ARG B 169 6740 6871 5695 -572 -205 388 N -ATOM 2848 NH2 ARG B 169 3.936 -1.179 -24.287 1.00 55.78 N -ANISOU 2848 NH2 ARG B 169 7377 7522 6296 -493 -100 258 N -ATOM 2849 N SER B 170 0.922 -0.955 -31.936 1.00 64.47 N -ANISOU 2849 N SER B 170 8555 9076 6865 -446 -580 276 N -ATOM 2850 CA SER B 170 0.235 -0.364 -33.086 1.00 73.04 C -ANISOU 2850 CA SER B 170 9698 10255 7800 -311 -722 294 C -ATOM 2851 C SER B 170 -0.759 0.719 -32.664 1.00 77.30 C -ANISOU 2851 C SER B 170 10200 10759 8411 -230 -807 342 C -ATOM 2852 O SER B 170 -0.451 1.911 -32.705 1.00 79.34 O -ANISOU 2852 O SER B 170 10575 10955 8616 -173 -763 507 O -ATOM 2853 CB SER B 170 -0.480 -1.444 -33.909 1.00 73.89 C -ANISOU 2853 CB SER B 170 9735 10489 7849 -278 -849 97 C -ATOM 2854 OG SER B 170 -1.573 -1.989 -33.196 1.00 74.96 O -ANISOU 2854 OG SER B 170 9684 10607 8189 -331 -900 -74 O -ATOM 2855 N TYR B 173 -2.807 5.660 -28.378 1.00 56.17 N -ANISOU 2855 N TYR B 173 7515 7558 6269 -125 -713 739 N -ATOM 2856 CA TYR B 173 -2.956 6.376 -27.112 1.00 57.31 C -ANISOU 2856 CA TYR B 173 7659 7559 6558 -150 -649 786 C -ATOM 2857 C TYR B 173 -1.842 6.021 -26.131 1.00 57.01 C -ANISOU 2857 C TYR B 173 7623 7437 6601 -285 -531 758 C -ATOM 2858 O TYR B 173 -1.600 4.846 -25.854 1.00 57.55 O -ANISOU 2858 O TYR B 173 7616 7546 6704 -344 -513 654 O -ATOM 2859 CB TYR B 173 -4.314 6.058 -26.479 1.00 58.66 C -ANISOU 2859 CB TYR B 173 7685 7735 6869 -100 -718 694 C -ATOM 2860 CG TYR B 173 -4.727 6.999 -25.366 1.00 58.77 C -ANISOU 2860 CG TYR B 173 7726 7606 6996 -69 -668 765 C -ATOM 2861 CD1 TYR B 173 -5.375 8.196 -25.657 1.00 62.61 C -ANISOU 2861 CD1 TYR B 173 8282 8071 7437 62 -714 871 C -ATOM 2862 CD2 TYR B 173 -4.487 6.689 -24.029 1.00 56.87 C -ANISOU 2862 CD2 TYR B 173 7467 7254 6888 -140 -572 727 C -ATOM 2863 CE1 TYR B 173 -5.769 9.066 -24.656 1.00 61.14 C -ANISOU 2863 CE1 TYR B 173 8132 7747 7351 96 -662 936 C -ATOM 2864 CE2 TYR B 173 -4.880 7.558 -23.012 1.00 58.02 C -ANISOU 2864 CE2 TYR B 173 7654 7267 7122 -95 -529 786 C -ATOM 2865 CZ TYR B 173 -5.522 8.746 -23.337 1.00 58.25 C -ANISOU 2865 CZ TYR B 173 7741 7271 7122 10 -573 889 C -ATOM 2866 OH TYR B 173 -5.920 9.628 -22.353 1.00 56.64 O -ANISOU 2866 OH TYR B 173 7591 6929 7001 59 -524 949 O -ATOM 2867 N LYS B 174 -1.162 7.042 -25.615 1.00 54.72 N -ANISOU 2867 N LYS B 174 7420 7030 6340 -318 -449 838 N -ATOM 2868 CA LYS B 174 -0.208 6.860 -24.524 1.00 50.58 C -ANISOU 2868 CA LYS B 174 6878 6440 5901 -407 -375 778 C -ATOM 2869 C LYS B 174 -0.940 7.119 -23.208 1.00 39.28 C -ANISOU 2869 C LYS B 174 5427 4912 4587 -359 -380 756 C -ATOM 2870 O LYS B 174 -1.697 8.086 -23.100 1.00 37.32 O -ANISOU 2870 O LYS B 174 5222 4590 4367 -296 -395 832 O -ATOM 2871 CB LYS B 174 0.970 7.812 -24.678 1.00 53.47 C -ANISOU 2871 CB LYS B 174 7320 6734 6263 -483 -282 827 C -ATOM 2872 N PRO B 175 -0.735 6.253 -22.204 1.00 37.21 N -ANISOU 2872 N PRO B 175 5122 4640 4378 -362 -352 662 N -ATOM 2873 CA PRO B 175 -1.488 6.464 -20.956 1.00 31.10 C -ANISOU 2873 CA PRO B 175 4359 3759 3699 -287 -333 652 C -ATOM 2874 C PRO B 175 -1.107 7.767 -20.270 1.00 32.04 C -ANISOU 2874 C PRO B 175 4557 3767 3851 -283 -320 689 C -ATOM 2875 O PRO B 175 0.034 8.203 -20.368 1.00 32.25 O -ANISOU 2875 O PRO B 175 4604 3793 3856 -356 -304 665 O -ATOM 2876 CB PRO B 175 -1.098 5.259 -20.088 1.00 36.29 C -ANISOU 2876 CB PRO B 175 5004 4421 4362 -261 -274 553 C -ATOM 2877 CG PRO B 175 0.143 4.693 -20.724 1.00 40.32 C -ANISOU 2877 CG PRO B 175 5499 5038 4784 -332 -277 509 C -ATOM 2878 CD PRO B 175 0.063 5.016 -22.186 1.00 39.81 C -ANISOU 2878 CD PRO B 175 5414 5046 4665 -397 -322 573 C -ATOM 2879 N ASP B 176 -2.056 8.377 -19.573 1.00 32.06 N -ANISOU 2879 N ASP B 176 4593 3669 3921 -205 -315 731 N -ATOM 2880 CA ASP B 176 -1.819 9.666 -18.932 1.00 33.79 C -ANISOU 2880 CA ASP B 176 4899 3764 4175 -198 -298 760 C -ATOM 2881 C ASP B 176 -1.030 9.576 -17.630 1.00 32.66 C -ANISOU 2881 C ASP B 176 4788 3572 4048 -175 -284 649 C -ATOM 2882 O ASP B 176 -0.289 10.492 -17.271 1.00 34.18 O -ANISOU 2882 O ASP B 176 5021 3702 4266 -219 -283 607 O -ATOM 2883 CB ASP B 176 -3.159 10.338 -18.674 1.00 36.98 C -ANISOU 2883 CB ASP B 176 5335 4081 4634 -100 -296 847 C -ATOM 2884 CG ASP B 176 -4.008 10.406 -19.920 1.00 35.76 C -ANISOU 2884 CG ASP B 176 5137 4006 4446 -71 -343 929 C -ATOM 2885 OD1 ASP B 176 -4.761 9.446 -20.195 1.00 29.70 O -ANISOU 2885 OD1 ASP B 176 4260 3325 3700 -40 -375 886 O -ATOM 2886 OD2 ASP B 176 -3.887 11.411 -20.636 1.00 35.00 O -ANISOU 2886 OD2 ASP B 176 5118 3881 4297 -68 -340 1021 O -ATOM 2887 N PHE B 177 -1.206 8.476 -16.910 1.00 25.26 N -ANISOU 2887 N PHE B 177 3841 2660 3098 -91 -266 588 N -ATOM 2888 CA PHE B 177 -0.498 8.280 -15.654 1.00 25.81 C -ANISOU 2888 CA PHE B 177 3967 2704 3136 -3 -266 478 C -ATOM 2889 C PHE B 177 0.124 6.889 -15.659 1.00 29.54 C -ANISOU 2889 C PHE B 177 4408 3284 3532 30 -248 402 C -ATOM 2890 O PHE B 177 -0.583 5.886 -15.774 1.00 32.14 O -ANISOU 2890 O PHE B 177 4732 3615 3865 71 -177 432 O -ATOM 2891 CB PHE B 177 -1.472 8.405 -14.476 1.00 26.65 C -ANISOU 2891 CB PHE B 177 4171 2682 3274 151 -213 504 C -ATOM 2892 CG PHE B 177 -2.324 9.642 -14.522 1.00 30.07 C -ANISOU 2892 CG PHE B 177 4637 3004 3782 141 -212 600 C -ATOM 2893 CD1 PHE B 177 -1.791 10.885 -14.190 1.00 28.63 C -ANISOU 2893 CD1 PHE B 177 4513 2751 3614 109 -249 572 C -ATOM 2894 CD2 PHE B 177 -3.663 9.566 -14.893 1.00 27.71 C -ANISOU 2894 CD2 PHE B 177 4304 2673 3553 167 -169 701 C -ATOM 2895 CE1 PHE B 177 -2.579 12.030 -14.236 1.00 30.85 C -ANISOU 2895 CE1 PHE B 177 4851 2914 3955 115 -227 671 C -ATOM 2896 CE2 PHE B 177 -4.457 10.709 -14.931 1.00 27.53 C -ANISOU 2896 CE2 PHE B 177 4316 2559 3585 191 -170 794 C -ATOM 2897 CZ PHE B 177 -3.914 11.941 -14.606 1.00 28.58 C -ANISOU 2897 CZ PHE B 177 4542 2607 3710 170 -191 793 C -ATOM 2898 N VAL B 178 1.444 6.819 -15.536 1.00 24.54 N -ANISOU 2898 N VAL B 178 3747 2736 2843 12 -300 289 N -ATOM 2899 CA VAL B 178 2.133 5.528 -15.605 1.00 23.46 C -ANISOU 2899 CA VAL B 178 3586 2712 2617 61 -283 221 C -ATOM 2900 C VAL B 178 2.948 5.284 -14.348 1.00 24.40 C -ANISOU 2900 C VAL B 178 3765 2859 2645 240 -321 83 C -ATOM 2901 O VAL B 178 3.708 6.163 -13.936 1.00 26.68 O -ANISOU 2901 O VAL B 178 4021 3166 2952 228 -413 -27 O -ATOM 2902 CB VAL B 178 3.087 5.497 -16.810 1.00 31.07 C -ANISOU 2902 CB VAL B 178 4437 3795 3574 -102 -315 201 C -ATOM 2903 CG1 VAL B 178 3.938 4.217 -16.805 1.00 28.41 C -ANISOU 2903 CG1 VAL B 178 4078 3581 3137 -35 -301 119 C -ATOM 2904 CG2 VAL B 178 2.315 5.627 -18.096 1.00 31.02 C -ANISOU 2904 CG2 VAL B 178 4399 3781 3605 -225 -289 329 C -ATOM 2905 N GLY B 179 2.797 4.112 -13.723 1.00 21.70 N -ANISOU 2905 N GLY B 179 3520 2518 2207 423 -243 74 N -ATOM 2906 CA GLY B 179 3.618 3.817 -12.565 1.00 23.39 C -ANISOU 2906 CA GLY B 179 3817 2782 2287 654 -290 -59 C -ATOM 2907 C GLY B 179 5.061 3.599 -12.996 1.00 30.08 C -ANISOU 2907 C GLY B 179 4533 3813 3083 612 -393 -196 C -ATOM 2908 O GLY B 179 5.949 4.395 -12.658 1.00 26.87 O -ANISOU 2908 O GLY B 179 4041 3475 2692 603 -526 -349 O -ATOM 2909 N PHE B 180 5.287 2.520 -13.748 1.00 24.44 N -ANISOU 2909 N PHE B 180 3006 3302 2978 40 -295 559 N -ATOM 2910 CA PHE B 180 6.631 2.055 -14.082 1.00 22.23 C -ANISOU 2910 CA PHE B 180 2715 3183 2549 -86 -193 530 C -ATOM 2911 C PHE B 180 6.669 1.637 -15.539 1.00 26.88 C -ANISOU 2911 C PHE B 180 3354 3929 2931 -177 -191 611 C -ATOM 2912 O PHE B 180 5.755 0.972 -16.011 1.00 25.49 O -ANISOU 2912 O PHE B 180 3190 3801 2694 -128 -261 599 O -ATOM 2913 CB PHE B 180 6.959 0.827 -13.237 1.00 22.97 C -ANISOU 2913 CB PHE B 180 2716 3364 2649 -17 -103 353 C -ATOM 2914 CG PHE B 180 6.938 1.083 -11.755 1.00 21.86 C -ANISOU 2914 CG PHE B 180 2579 3092 2635 40 -106 264 C -ATOM 2915 CD1 PHE B 180 5.745 1.018 -11.033 1.00 22.53 C -ANISOU 2915 CD1 PHE B 180 2680 3071 2808 162 -113 204 C -ATOM 2916 CD2 PHE B 180 8.113 1.374 -11.088 1.00 22.89 C -ANISOU 2916 CD2 PHE B 180 2701 3211 2787 -48 -97 240 C -ATOM 2917 CE1 PHE B 180 5.734 1.245 -9.653 1.00 25.39 C -ANISOU 2917 CE1 PHE B 180 3105 3317 3226 192 -76 102 C -ATOM 2918 CE2 PHE B 180 8.113 1.619 -9.718 1.00 24.55 C -ANISOU 2918 CE2 PHE B 180 2978 3298 3053 -33 -126 153 C -ATOM 2919 CZ PHE B 180 6.927 1.554 -9.002 1.00 23.57 C -ANISOU 2919 CZ PHE B 180 2925 3068 2962 85 -98 74 C -ATOM 2920 N GLU B 181 7.727 2.013 -16.244 1.00 24.64 N -ANISOU 2920 N GLU B 181 3111 3726 2527 -332 -103 691 N -ATOM 2921 CA GLU B 181 7.935 1.530 -17.603 1.00 26.13 C -ANISOU 2921 CA GLU B 181 3391 4084 2455 -444 -32 732 C -ATOM 2922 C GLU B 181 8.974 0.417 -17.552 1.00 29.24 C -ANISOU 2922 C GLU B 181 3675 4636 2800 -437 197 559 C -ATOM 2923 O GLU B 181 10.114 0.633 -17.136 1.00 30.01 O -ANISOU 2923 O GLU B 181 3646 4757 2998 -483 322 547 O -ATOM 2924 CB GLU B 181 8.405 2.661 -18.497 1.00 28.58 C -ANISOU 2924 CB GLU B 181 3831 4382 2647 -635 -36 946 C -ATOM 2925 CG GLU B 181 8.337 2.347 -19.982 1.00 35.62 C -ANISOU 2925 CG GLU B 181 4908 5426 3200 -780 0 1024 C -ATOM 2926 CD GLU B 181 9.092 3.350 -20.780 1.00 39.99 C -ANISOU 2926 CD GLU B 181 5588 5997 3611 -1006 73 1229 C -ATOM 2927 OE1 GLU B 181 10.342 3.345 -20.674 1.00 42.81 O -ANISOU 2927 OE1 GLU B 181 5831 6444 3990 -1095 322 1182 O -ATOM 2928 OE2 GLU B 181 8.440 4.150 -21.491 1.00 42.21 O -ANISOU 2928 OE2 GLU B 181 6064 6191 3781 -1099 -131 1457 O -ATOM 2929 N ILE B 182 8.582 -0.779 -17.977 1.00 27.79 N -ANISOU 2929 N ILE B 182 3528 4541 2491 -381 239 430 N -ATOM 2930 CA ILE B 182 9.392 -1.967 -17.715 1.00 25.21 C -ANISOU 2930 CA ILE B 182 3081 4298 2199 -305 436 241 C -ATOM 2931 C ILE B 182 9.854 -2.626 -19.007 1.00 27.50 C -ANISOU 2931 C ILE B 182 3486 4732 2229 -391 647 167 C -ATOM 2932 O ILE B 182 9.310 -2.339 -20.077 1.00 30.12 O -ANISOU 2932 O ILE B 182 4038 5108 2298 -519 590 250 O -ATOM 2933 CB ILE B 182 8.594 -2.980 -16.884 1.00 23.95 C -ANISOU 2933 CB ILE B 182 2877 4068 2154 -146 340 107 C -ATOM 2934 CG1 ILE B 182 7.372 -3.476 -17.655 1.00 27.52 C -ANISOU 2934 CG1 ILE B 182 3490 4528 2440 -168 216 94 C -ATOM 2935 CG2 ILE B 182 8.216 -2.382 -15.520 1.00 25.09 C -ANISOU 2935 CG2 ILE B 182 2933 4078 2524 -68 199 149 C -ATOM 2936 CD1 ILE B 182 6.676 -4.663 -16.950 1.00 28.59 C -ANISOU 2936 CD1 ILE B 182 3578 4603 2682 -49 162 -46 C -ATOM 2937 N PRO B 183 10.866 -3.510 -18.920 1.00 28.52 N -ANISOU 2937 N PRO B 183 3480 4926 2431 -320 892 10 N -ATOM 2938 CA PRO B 183 11.264 -4.222 -20.140 1.00 33.05 C -ANISOU 2938 CA PRO B 183 4192 5614 2750 -381 1153 -113 C -ATOM 2939 C PRO B 183 10.195 -5.234 -20.539 1.00 31.77 C -ANISOU 2939 C PRO B 183 4244 5413 2413 -346 1045 -249 C -ATOM 2940 O PRO B 183 9.258 -5.482 -19.785 1.00 34.04 O -ANISOU 2940 O PRO B 183 4503 5596 2834 -257 801 -247 O -ATOM 2941 CB PRO B 183 12.534 -4.976 -19.723 1.00 38.29 C -ANISOU 2941 CB PRO B 183 4594 6306 3650 -250 1426 -257 C -ATOM 2942 CG PRO B 183 12.890 -4.483 -18.337 1.00 31.46 C -ANISOU 2942 CG PRO B 183 3462 5362 3128 -174 1258 -159 C -ATOM 2943 CD PRO B 183 11.653 -3.922 -17.739 1.00 29.87 C -ANISOU 2943 CD PRO B 183 3384 5052 2914 -180 933 -60 C -ATOM 2944 N ASP B 184 10.365 -5.840 -21.702 1.00 37.58 N -ANISOU 2944 N ASP B 184 5198 6229 2851 -430 1247 -379 N -ATOM 2945 CA ASP B 184 9.451 -6.867 -22.170 1.00 42.28 C -ANISOU 2945 CA ASP B 184 6029 6777 3257 -437 1146 -535 C -ATOM 2946 C ASP B 184 9.797 -8.198 -21.503 1.00 38.31 C -ANISOU 2946 C ASP B 184 5393 6170 2992 -231 1278 -767 C -ATOM 2947 O ASP B 184 10.306 -9.113 -22.145 1.00 45.55 O -ANISOU 2947 O ASP B 184 6429 7086 3792 -204 1550 -987 O -ATOM 2948 CB ASP B 184 9.545 -6.983 -23.695 1.00 47.16 C -ANISOU 2948 CB ASP B 184 6999 7501 3418 -633 1311 -601 C -ATOM 2949 CG ASP B 184 8.445 -7.846 -24.296 1.00 54.55 C -ANISOU 2949 CG ASP B 184 8219 8359 4151 -690 1090 -708 C -ATOM 2950 OD1 ASP B 184 7.536 -8.281 -23.557 1.00 55.72 O -ANISOU 2950 OD1 ASP B 184 8304 8425 4444 -634 838 -731 O -ATOM 2951 OD2 ASP B 184 8.495 -8.069 -25.526 1.00 61.97 O -ANISOU 2951 OD2 ASP B 184 9419 9310 4816 -794 1150 -755 O -ATOM 2952 N LYS B 185 9.532 -8.274 -20.208 1.00 35.33 N -ANISOU 2952 N LYS B 185 4791 5689 2944 -87 1095 -713 N -ATOM 2953 CA LYS B 185 9.710 -9.492 -19.425 1.00 39.51 C -ANISOU 2953 CA LYS B 185 5208 6085 3717 98 1136 -873 C -ATOM 2954 C LYS B 185 8.360 -9.863 -18.833 1.00 35.50 C -ANISOU 2954 C LYS B 185 4763 5471 3256 96 828 -844 C -ATOM 2955 O LYS B 185 7.558 -8.986 -18.538 1.00 35.42 O -ANISOU 2955 O LYS B 185 4730 5482 3248 27 604 -671 O -ATOM 2956 CB LYS B 185 10.698 -9.249 -18.280 1.00 42.91 C -ANISOU 2956 CB LYS B 185 5311 6494 4499 244 1184 -801 C -ATOM 2957 CG LYS B 185 12.155 -9.279 -18.687 1.00 56.46 C -ANISOU 2957 CG LYS B 185 6862 8286 6303 296 1518 -864 C -ATOM 2958 CD LYS B 185 13.052 -8.972 -17.498 1.00 60.63 C -ANISOU 2958 CD LYS B 185 7045 8792 7199 405 1467 -752 C -ATOM 2959 CE LYS B 185 14.520 -9.047 -17.902 1.00 68.06 C -ANISOU 2959 CE LYS B 185 7741 9813 8304 463 1801 -800 C -ATOM 2960 NZ LYS B 185 15.320 -7.930 -17.314 1.00 70.27 N -ANISOU 2960 NZ LYS B 185 7746 10175 8777 389 1738 -601 N -ATOM 2961 N PHE B 186 8.107 -11.149 -18.619 1.00 37.04 N -ANISOU 2961 N PHE B 186 5020 5533 3523 174 831 -1006 N -ATOM 2962 CA PHE B 186 6.840 -11.536 -18.001 1.00 34.14 C -ANISOU 2962 CA PHE B 186 4678 5066 3228 147 564 -963 C -ATOM 2963 C PHE B 186 6.888 -11.376 -16.485 1.00 32.85 C -ANISOU 2963 C PHE B 186 4285 4836 3360 269 477 -849 C -ATOM 2964 O PHE B 186 7.686 -12.014 -15.808 1.00 31.62 O -ANISOU 2964 O PHE B 186 4026 4593 3396 409 571 -903 O -ATOM 2965 CB PHE B 186 6.436 -12.961 -18.382 1.00 38.18 C -ANISOU 2965 CB PHE B 186 5385 5438 3683 133 571 -1165 C -ATOM 2966 CG PHE B 186 4.973 -13.243 -18.170 1.00 39.76 C -ANISOU 2966 CG PHE B 186 5645 5579 3883 12 287 -1108 C -ATOM 2967 CD1 PHE B 186 4.502 -13.648 -16.935 1.00 37.24 C -ANISOU 2967 CD1 PHE B 186 5183 5149 3819 80 183 -1042 C -ATOM 2968 CD2 PHE B 186 4.070 -13.106 -19.222 1.00 45.93 C -ANISOU 2968 CD2 PHE B 186 6623 6421 4405 -191 119 -1106 C -ATOM 2969 CE1 PHE B 186 3.149 -13.906 -16.739 1.00 38.48 C -ANISOU 2969 CE1 PHE B 186 5349 5263 4009 -45 -39 -981 C -ATOM 2970 CE2 PHE B 186 2.722 -13.362 -19.037 1.00 46.72 C -ANISOU 2970 CE2 PHE B 186 6715 6475 4561 -311 -157 -1034 C -ATOM 2971 CZ PHE B 186 2.261 -13.766 -17.791 1.00 40.84 C -ANISOU 2971 CZ PHE B 186 5785 5625 4108 -235 -212 -977 C -ATOM 2972 N VAL B 187 6.032 -10.518 -15.951 1.00 24.47 N -ANISOU 2972 N VAL B 187 3157 3803 2336 215 294 -689 N -ATOM 2973 CA VAL B 187 6.052 -10.240 -14.524 1.00 23.23 C -ANISOU 2973 CA VAL B 187 2843 3592 2392 300 237 -594 C -ATOM 2974 C VAL B 187 4.729 -10.685 -13.905 1.00 26.99 C -ANISOU 2974 C VAL B 187 3332 3987 2936 263 93 -565 C -ATOM 2975 O VAL B 187 3.714 -10.779 -14.590 1.00 25.75 O -ANISOU 2975 O VAL B 187 3243 3846 2694 159 -14 -563 O -ATOM 2976 CB VAL B 187 6.301 -8.736 -14.241 1.00 28.50 C -ANISOU 2976 CB VAL B 187 3415 4337 3078 281 212 -449 C -ATOM 2977 CG1 VAL B 187 7.692 -8.321 -14.706 1.00 28.21 C -ANISOU 2977 CG1 VAL B 187 3322 4379 3019 292 368 -456 C -ATOM 2978 CG2 VAL B 187 5.247 -7.891 -14.925 1.00 31.05 C -ANISOU 2978 CG2 VAL B 187 3797 4707 3294 179 86 -353 C -ATOM 2979 N VAL B 188 4.745 -10.977 -12.614 1.00 25.71 N -ANISOU 2979 N VAL B 188 3103 3742 2924 327 83 -531 N -ATOM 2980 CA VAL B 188 3.553 -11.429 -11.914 1.00 25.26 C -ANISOU 2980 CA VAL B 188 3045 3613 2940 278 3 -495 C -ATOM 2981 C VAL B 188 3.557 -10.765 -10.551 1.00 23.10 C -ANISOU 2981 C VAL B 188 2702 3325 2750 317 17 -401 C -ATOM 2982 O VAL B 188 4.569 -10.194 -10.152 1.00 25.10 O -ANISOU 2982 O VAL B 188 2929 3600 3008 374 47 -377 O -ATOM 2983 CB VAL B 188 3.561 -12.958 -11.722 1.00 22.90 C -ANISOU 2983 CB VAL B 188 2836 3175 2691 282 8 -581 C -ATOM 2984 CG1 VAL B 188 3.437 -13.682 -13.062 1.00 24.80 C -ANISOU 2984 CG1 VAL B 188 3204 3396 2822 220 0 -715 C -ATOM 2985 CG2 VAL B 188 4.828 -13.406 -10.981 1.00 27.27 C -ANISOU 2985 CG2 VAL B 188 3377 3649 3334 410 67 -589 C -ATOM 2986 N GLY B 189 2.441 -10.829 -9.835 1.00 19.13 N -ANISOU 2986 N GLY B 189 2175 2786 2309 269 5 -353 N -ATOM 2987 CA GLY B 189 2.405 -10.276 -8.490 1.00 19.35 C -ANISOU 2987 CA GLY B 189 2197 2788 2366 288 60 -294 C -ATOM 2988 C GLY B 189 1.637 -8.964 -8.468 1.00 21.24 C -ANISOU 2988 C GLY B 189 2353 3072 2646 291 90 -248 C -ATOM 2989 O GLY B 189 1.380 -8.399 -9.529 1.00 21.35 O -ANISOU 2989 O GLY B 189 2305 3141 2666 289 28 -230 O -ATOM 2990 N TYR B 190 1.288 -8.482 -7.272 1.00 20.46 N -ANISOU 2990 N TYR B 190 2274 2932 2567 296 186 -229 N -ATOM 2991 CA TYR B 190 0.429 -7.290 -7.108 1.00 22.77 C -ANISOU 2991 CA TYR B 190 2482 3219 2952 329 261 -206 C -ATOM 2992 C TYR B 190 -0.817 -7.408 -8.001 1.00 26.08 C -ANISOU 2992 C TYR B 190 2723 3669 3517 313 209 -163 C -ATOM 2993 O TYR B 190 -1.197 -6.465 -8.712 1.00 22.84 O -ANISOU 2993 O TYR B 190 2212 3271 3195 357 145 -113 O -ATOM 2994 CB TYR B 190 1.228 -6.008 -7.387 1.00 16.97 C -ANISOU 2994 CB TYR B 190 1780 2483 2185 378 223 -199 C -ATOM 2995 CG TYR B 190 0.594 -4.728 -6.892 1.00 22.70 C -ANISOU 2995 CG TYR B 190 2485 3134 3008 435 322 -199 C -ATOM 2996 CD1 TYR B 190 0.481 -4.452 -5.527 1.00 20.68 C -ANISOU 2996 CD1 TYR B 190 2346 2801 2709 434 480 -261 C -ATOM 2997 CD2 TYR B 190 0.125 -3.787 -7.787 1.00 23.20 C -ANISOU 2997 CD2 TYR B 190 2439 3181 3195 488 258 -137 C -ATOM 2998 CE1 TYR B 190 -0.098 -3.270 -5.082 1.00 20.76 C -ANISOU 2998 CE1 TYR B 190 2361 2710 2819 503 614 -299 C -ATOM 2999 CE2 TYR B 190 -0.450 -2.599 -7.355 1.00 20.49 C -ANISOU 2999 CE2 TYR B 190 2071 2722 2992 573 354 -141 C -ATOM 3000 CZ TYR B 190 -0.556 -2.348 -6.001 1.00 21.24 C -ANISOU 3000 CZ TYR B 190 2279 2729 3060 589 553 -240 C -ATOM 3001 OH TYR B 190 -1.126 -1.164 -5.580 1.00 22.23 O -ANISOU 3001 OH TYR B 190 2403 2708 3335 690 689 -280 O -ATOM 3002 N ALA B 191 -1.431 -8.599 -7.958 1.00 22.12 N -ANISOU 3002 N ALA B 191 2189 3166 3050 232 205 -164 N -ATOM 3003 CA ALA B 191 -2.660 -8.950 -8.701 1.00 22.07 C -ANISOU 3003 CA ALA B 191 2002 3188 3196 166 117 -115 C -ATOM 3004 C ALA B 191 -2.480 -9.374 -10.167 1.00 22.19 C -ANISOU 3004 C ALA B 191 2048 3250 3134 102 -103 -118 C -ATOM 3005 O ALA B 191 -3.430 -9.868 -10.776 1.00 23.13 O -ANISOU 3005 O ALA B 191 2058 3385 3346 1 -229 -82 O -ATOM 3006 CB ALA B 191 -3.774 -7.862 -8.565 1.00 24.68 C -ANISOU 3006 CB ALA B 191 2104 3516 3756 234 179 -46 C -ATOM 3007 N LEU B 192 -1.279 -9.193 -10.715 1.00 23.16 N -ANISOU 3007 N LEU B 192 2322 3395 3083 140 -140 -164 N -ATOM 3008 CA LEU B 192 -0.962 -9.684 -12.060 1.00 26.05 C -ANISOU 3008 CA LEU B 192 2787 3802 3309 68 -282 -204 C -ATOM 3009 C LEU B 192 -0.706 -11.185 -11.986 1.00 26.30 C -ANISOU 3009 C LEU B 192 2940 3765 3288 7 -265 -308 C -ATOM 3010 O LEU B 192 0.018 -11.651 -11.093 1.00 23.77 O -ANISOU 3010 O LEU B 192 2685 3379 2966 67 -152 -346 O -ATOM 3011 CB LEU B 192 0.279 -8.989 -12.629 1.00 23.91 C -ANISOU 3011 CB LEU B 192 2621 3581 2882 125 -257 -222 C -ATOM 3012 CG LEU B 192 0.120 -7.556 -13.134 1.00 33.81 C -ANISOU 3012 CG LEU B 192 3819 4880 4148 148 -326 -109 C -ATOM 3013 CD1 LEU B 192 0.161 -6.560 -11.986 1.00 31.13 C -ANISOU 3013 CD1 LEU B 192 3402 4484 3944 252 -215 -68 C -ATOM 3014 CD2 LEU B 192 1.176 -7.220 -14.185 1.00 40.18 C -ANISOU 3014 CD2 LEU B 192 4764 5755 4747 117 -333 -120 C -ATOM 3015 N ASP B 193 -1.256 -11.934 -12.934 1.00 26.67 N -ANISOU 3015 N ASP B 193 3039 3805 3290 -120 -404 -347 N -ATOM 3016 CA ASP B 193 -1.239 -13.389 -12.829 1.00 22.36 C -ANISOU 3016 CA ASP B 193 2616 3143 2738 -195 -401 -446 C -ATOM 3017 C ASP B 193 -0.471 -14.112 -13.933 1.00 25.69 C -ANISOU 3017 C ASP B 193 3265 3525 2969 -222 -423 -601 C -ATOM 3018 O ASP B 193 -0.162 -13.554 -14.990 1.00 25.56 O -ANISOU 3018 O ASP B 193 3325 3602 2785 -239 -466 -627 O -ATOM 3019 CB ASP B 193 -2.667 -13.941 -12.824 1.00 24.05 C -ANISOU 3019 CB ASP B 193 2719 3327 3092 -365 -529 -390 C -ATOM 3020 CG ASP B 193 -3.308 -13.903 -14.198 1.00 30.63 C -ANISOU 3020 CG ASP B 193 3578 4219 3842 -515 -768 -392 C -ATOM 3021 OD1 ASP B 193 -3.293 -12.829 -14.826 1.00 29.75 O -ANISOU 3021 OD1 ASP B 193 3417 4218 3667 -478 -849 -320 O -ATOM 3022 OD2 ASP B 193 -3.814 -14.949 -14.655 1.00 29.45 O -ANISOU 3022 OD2 ASP B 193 3522 3989 3677 -689 -899 -456 O -ATOM 3023 N TYR B 194 -0.195 -15.384 -13.669 1.00 24.08 N -ANISOU 3023 N TYR B 194 3192 3163 2793 -233 -379 -705 N -ATOM 3024 CA TYR B 194 0.192 -16.332 -14.708 1.00 27.17 C -ANISOU 3024 CA TYR B 194 3823 3459 3042 -290 -394 -890 C -ATOM 3025 C TYR B 194 -0.773 -17.480 -14.514 1.00 28.75 C -ANISOU 3025 C TYR B 194 4079 3502 3343 -458 -512 -909 C -ATOM 3026 O TYR B 194 -0.709 -18.188 -13.506 1.00 29.28 O -ANISOU 3026 O TYR B 194 4137 3424 3562 -423 -449 -878 O -ATOM 3027 CB TYR B 194 1.633 -16.797 -14.507 1.00 29.27 C -ANISOU 3027 CB TYR B 194 4183 3626 3312 -100 -200 -1005 C -ATOM 3028 CG TYR B 194 2.059 -17.891 -15.469 1.00 30.13 C -ANISOU 3028 CG TYR B 194 4551 3584 3313 -122 -148 -1234 C -ATOM 3029 CD1 TYR B 194 2.248 -17.618 -16.812 1.00 32.36 C -ANISOU 3029 CD1 TYR B 194 4996 3959 3341 -192 -124 -1362 C -ATOM 3030 CD2 TYR B 194 2.261 -19.194 -15.029 1.00 30.49 C -ANISOU 3030 CD2 TYR B 194 4712 3373 3500 -80 -114 -1325 C -ATOM 3031 CE1 TYR B 194 2.634 -18.606 -17.696 1.00 41.41 C -ANISOU 3031 CE1 TYR B 194 6425 4954 4356 -217 -32 -1610 C -ATOM 3032 CE2 TYR B 194 2.654 -20.187 -15.902 1.00 35.50 C -ANISOU 3032 CE2 TYR B 194 5607 3827 4055 -81 -38 -1565 C -ATOM 3033 CZ TYR B 194 2.837 -19.890 -17.234 1.00 41.52 C -ANISOU 3033 CZ TYR B 194 6539 4692 4544 -149 19 -1725 C -ATOM 3034 OH TYR B 194 3.224 -20.882 -18.112 1.00 46.25 O -ANISOU 3034 OH TYR B 194 7443 5098 5032 -156 137 -2003 O -ATOM 3035 N ASN B 195 -1.699 -17.628 -15.457 1.00 29.57 N -ANISOU 3035 N ASN B 195 4242 3634 3360 -669 -711 -934 N -ATOM 3036 CA AASN B 195 -2.763 -18.626 -15.362 0.59 31.58 C -ANISOU 3036 CA AASN B 195 4518 3754 3729 -888 -868 -931 C -ATOM 3037 CA BASN B 195 -2.747 -18.642 -15.356 0.41 31.58 C -ANISOU 3037 CA BASN B 195 4521 3751 3729 -887 -865 -933 C -ATOM 3038 C ASN B 195 -3.486 -18.620 -14.011 1.00 30.68 C -ANISOU 3038 C ASN B 195 4147 3628 3881 -902 -824 -747 C -ATOM 3039 O ASN B 195 -3.729 -19.668 -13.408 1.00 31.70 O -ANISOU 3039 O ASN B 195 4340 3576 4130 -990 -807 -751 O -ATOM 3040 CB AASN B 195 -2.230 -20.014 -15.716 0.59 38.31 C -ANISOU 3040 CB AASN B 195 5691 4351 4513 -923 -829 -1149 C -ATOM 3041 CB BASN B 195 -2.181 -20.038 -15.617 0.41 37.61 C -ANISOU 3041 CB BASN B 195 5596 4254 4439 -908 -813 -1145 C -ATOM 3042 CG AASN B 195 -1.780 -20.104 -17.162 0.59 42.10 C -ANISOU 3042 CG AASN B 195 6462 4839 4696 -975 -859 -1361 C -ATOM 3043 CG BASN B 195 -3.266 -21.076 -15.779 0.41 42.66 C -ANISOU 3043 CG BASN B 195 6319 4733 5157 -1191 -1014 -1167 C -ATOM 3044 OD1AASN B 195 -2.300 -19.400 -18.027 0.59 45.33 O -ANISOU 3044 OD1AASN B 195 6865 5421 4935 -1111 -1031 -1318 O -ATOM 3045 OD1BASN B 195 -4.305 -20.806 -16.378 0.41 46.02 O -ANISOU 3045 OD1BASN B 195 6662 5266 5557 -1415 -1252 -1102 O -ATOM 3046 ND2AASN B 195 -0.812 -20.971 -17.432 0.59 45.95 N -ANISOU 3046 ND2AASN B 195 7213 5127 5118 -866 -685 -1586 N -ATOM 3047 ND2BASN B 195 -3.049 -22.258 -15.213 0.41 45.58 N -ANISOU 3047 ND2BASN B 195 6837 4833 5650 -1194 -946 -1232 N -ATOM 3048 N GLU B 196 -3.815 -17.413 -13.545 1.00 29.11 N -ANISOU 3048 N GLU B 196 3684 3611 3766 -819 -785 -589 N -ATOM 3049 CA GLU B 196 -4.563 -17.174 -12.297 1.00 28.66 C -ANISOU 3049 CA GLU B 196 3375 3579 3934 -827 -685 -426 C -ATOM 3050 C GLU B 196 -3.728 -17.251 -11.024 1.00 34.27 C -ANISOU 3050 C GLU B 196 4145 4223 4653 -666 -457 -405 C -ATOM 3051 O GLU B 196 -4.181 -16.832 -9.962 1.00 32.68 O -ANISOU 3051 O GLU B 196 3786 4067 4563 -651 -325 -286 O -ATOM 3052 CB GLU B 196 -5.822 -18.042 -12.184 1.00 31.21 C -ANISOU 3052 CB GLU B 196 3596 3824 4436 -1084 -799 -365 C -ATOM 3053 CG GLU B 196 -6.874 -17.750 -13.246 1.00 39.08 C -ANISOU 3053 CG GLU B 196 4437 4923 5488 -1266 -1075 -318 C -ATOM 3054 CD GLU B 196 -7.302 -16.289 -13.258 1.00 39.74 C -ANISOU 3054 CD GLU B 196 4219 5202 5679 -1143 -1081 -178 C -ATOM 3055 OE1 GLU B 196 -7.288 -15.652 -12.185 1.00 36.66 O -ANISOU 3055 OE1 GLU B 196 3661 4855 5413 -990 -843 -100 O -ATOM 3056 OE2 GLU B 196 -7.655 -15.777 -14.339 1.00 42.92 O -ANISOU 3056 OE2 GLU B 196 4580 5697 6033 -1206 -1333 -146 O -ATOM 3057 N TYR B 197 -2.499 -17.752 -11.130 1.00 26.29 N -ANISOU 3057 N TYR B 197 3361 3105 3525 -545 -409 -519 N -ATOM 3058 CA TYR B 197 -1.611 -17.787 -9.982 1.00 25.03 C -ANISOU 3058 CA TYR B 197 3254 2885 3374 -395 -264 -473 C -ATOM 3059 C TYR B 197 -0.806 -16.497 -9.837 1.00 23.42 C -ANISOU 3059 C TYR B 197 2971 2834 3094 -214 -184 -454 C -ATOM 3060 O TYR B 197 -0.692 -15.714 -10.791 1.00 22.73 O -ANISOU 3060 O TYR B 197 2837 2870 2930 -181 -227 -498 O -ATOM 3061 CB TYR B 197 -0.680 -19.000 -10.049 1.00 25.98 C -ANISOU 3061 CB TYR B 197 3603 2781 3486 -335 -269 -574 C -ATOM 3062 CG TYR B 197 -1.396 -20.297 -9.777 1.00 32.75 C -ANISOU 3062 CG TYR B 197 4570 3429 4444 -517 -330 -555 C -ATOM 3063 CD1 TYR B 197 -1.512 -20.785 -8.484 1.00 32.21 C -ANISOU 3063 CD1 TYR B 197 4534 3249 4453 -556 -274 -408 C -ATOM 3064 CD2 TYR B 197 -1.979 -21.025 -10.809 1.00 37.69 C -ANISOU 3064 CD2 TYR B 197 5296 3959 5066 -683 -455 -674 C -ATOM 3065 CE1 TYR B 197 -2.176 -21.968 -8.224 1.00 39.84 C -ANISOU 3065 CE1 TYR B 197 5612 4008 5518 -751 -326 -365 C -ATOM 3066 CE2 TYR B 197 -2.645 -22.218 -10.560 1.00 42.97 C -ANISOU 3066 CE2 TYR B 197 6074 4409 5844 -882 -525 -652 C -ATOM 3067 CZ TYR B 197 -2.743 -22.680 -9.264 1.00 45.07 C -ANISOU 3067 CZ TYR B 197 6349 4562 6212 -913 -452 -489 C -ATOM 3068 OH TYR B 197 -3.401 -23.855 -9.000 1.00 51.65 O -ANISOU 3068 OH TYR B 197 7300 5165 7159 -1135 -516 -442 O -ATOM 3069 N PHE B 198 -0.263 -16.302 -8.637 1.00 22.13 N -ANISOU 3069 N PHE B 198 2821 2650 2937 -127 -89 -376 N -ATOM 3070 CA PHE B 198 0.589 -15.167 -8.270 1.00 20.55 C -ANISOU 3070 CA PHE B 198 2576 2558 2675 15 -30 -352 C -ATOM 3071 C PHE B 198 -0.159 -13.868 -8.015 1.00 23.18 C -ANISOU 3071 C PHE B 198 2757 3031 3019 3 30 -289 C -ATOM 3072 O PHE B 198 0.480 -12.836 -7.818 1.00 24.02 O -ANISOU 3072 O PHE B 198 2843 3209 3075 100 65 -281 O -ATOM 3073 CB PHE B 198 1.692 -14.898 -9.311 1.00 20.09 C -ANISOU 3073 CB PHE B 198 2539 2541 2551 130 -54 -453 C -ATOM 3074 CG PHE B 198 2.588 -16.069 -9.580 1.00 24.91 C -ANISOU 3074 CG PHE B 198 3275 2997 3191 199 -63 -542 C -ATOM 3075 CD1 PHE B 198 3.602 -16.405 -8.698 1.00 21.28 C -ANISOU 3075 CD1 PHE B 198 2846 2445 2796 313 -59 -491 C -ATOM 3076 CD2 PHE B 198 2.443 -16.809 -10.745 1.00 27.29 C -ANISOU 3076 CD2 PHE B 198 3674 3233 3463 155 -86 -680 C -ATOM 3077 CE1 PHE B 198 4.437 -17.485 -8.957 1.00 25.95 C -ANISOU 3077 CE1 PHE B 198 3516 2861 3482 416 -64 -566 C -ATOM 3078 CE2 PHE B 198 3.275 -17.889 -11.013 1.00 34.75 C -ANISOU 3078 CE2 PHE B 198 4743 3997 4463 248 -54 -793 C -ATOM 3079 CZ PHE B 198 4.280 -18.222 -10.116 1.00 31.39 C -ANISOU 3079 CZ PHE B 198 4300 3465 4163 399 -35 -731 C -ATOM 3080 N ARG B 199 -1.490 -13.886 -8.051 1.00 20.89 N -ANISOU 3080 N ARG B 199 2343 2766 2830 -110 40 -246 N -ATOM 3081 CA ARG B 199 -2.212 -12.658 -7.727 1.00 21.56 C -ANISOU 3081 CA ARG B 199 2256 2949 2988 -80 129 -189 C -ATOM 3082 C ARG B 199 -2.048 -12.364 -6.251 1.00 27.26 C -ANISOU 3082 C ARG B 199 3050 3644 3662 -55 309 -154 C -ATOM 3083 O ARG B 199 -2.104 -11.201 -5.833 1.00 25.31 O -ANISOU 3083 O ARG B 199 2756 3444 3417 21 412 -152 O -ATOM 3084 CB ARG B 199 -3.691 -12.737 -8.097 1.00 22.54 C -ANISOU 3084 CB ARG B 199 2163 3107 3294 -193 100 -135 C -ATOM 3085 CG ARG B 199 -3.961 -12.898 -9.615 1.00 23.17 C -ANISOU 3085 CG ARG B 199 2198 3224 3382 -257 -135 -157 C -ATOM 3086 CD ARG B 199 -5.399 -12.521 -9.956 1.00 25.11 C -ANISOU 3086 CD ARG B 199 2156 3531 3855 -338 -212 -61 C -ATOM 3087 NE ARG B 199 -5.880 -13.028 -11.245 1.00 26.64 N -ANISOU 3087 NE ARG B 199 2335 3740 4047 -486 -488 -61 N -ATOM 3088 CZ ARG B 199 -5.714 -12.397 -12.408 1.00 28.24 C -ANISOU 3088 CZ ARG B 199 2565 4011 4155 -468 -685 -52 C -ATOM 3089 NH1 ARG B 199 -5.070 -11.242 -12.445 1.00 25.38 N -ANISOU 3089 NH1 ARG B 199 2221 3696 3725 -302 -625 -34 N -ATOM 3090 NH2 ARG B 199 -6.191 -12.923 -13.532 1.00 29.82 N -ANISOU 3090 NH2 ARG B 199 2802 4220 4306 -642 -954 -55 N -ATOM 3091 N ASP B 200 -1.824 -13.429 -5.481 1.00 22.69 N -ANISOU 3091 N ASP B 200 2625 2969 3025 -130 334 -126 N -ATOM 3092 CA ASP B 200 -1.678 -13.358 -4.024 1.00 23.98 C -ANISOU 3092 CA ASP B 200 2933 3099 3079 -159 481 -73 C -ATOM 3093 C ASP B 200 -0.228 -13.128 -3.620 1.00 27.14 C -ANISOU 3093 C ASP B 200 3511 3472 3328 -66 388 -81 C -ATOM 3094 O ASP B 200 0.311 -13.802 -2.741 1.00 28.86 O -ANISOU 3094 O ASP B 200 3918 3605 3444 -110 352 -15 O -ATOM 3095 CB ASP B 200 -2.183 -14.648 -3.370 1.00 25.16 C -ANISOU 3095 CB ASP B 200 3183 3146 3231 -320 523 7 C -ATOM 3096 CG ASP B 200 -1.503 -15.893 -3.916 1.00 26.85 C -ANISOU 3096 CG ASP B 200 3515 3225 3460 -326 328 3 C -ATOM 3097 OD1 ASP B 200 -1.106 -15.895 -5.102 1.00 24.46 O -ANISOU 3097 OD1 ASP B 200 3150 2934 3211 -243 199 -86 O -ATOM 3098 OD2 ASP B 200 -1.387 -16.882 -3.154 1.00 29.55 O -ANISOU 3098 OD2 ASP B 200 4034 3433 3759 -418 317 91 O -ATOM 3099 N LEU B 201 0.407 -12.185 -4.295 1.00 27.58 N -ANISOU 3099 N LEU B 201 3495 3597 3386 48 326 -139 N -ATOM 3100 CA LEU B 201 1.802 -11.836 -4.045 1.00 27.54 C -ANISOU 3100 CA LEU B 201 3588 3586 3288 124 225 -140 C -ATOM 3101 C LEU B 201 1.853 -10.315 -4.051 1.00 26.34 C -ANISOU 3101 C LEU B 201 3387 3510 3112 172 283 -178 C -ATOM 3102 O LEU B 201 1.286 -9.693 -4.943 1.00 29.62 O -ANISOU 3102 O LEU B 201 3654 3980 3621 209 308 -208 O -ATOM 3103 CB LEU B 201 2.681 -12.440 -5.136 1.00 27.16 C -ANISOU 3103 CB LEU B 201 3489 3522 3308 203 92 -178 C -ATOM 3104 CG LEU B 201 4.141 -12.021 -5.267 1.00 27.30 C -ANISOU 3104 CG LEU B 201 3495 3562 3314 297 0 -184 C -ATOM 3105 CD1 LEU B 201 4.902 -12.429 -4.037 1.00 29.43 C -ANISOU 3105 CD1 LEU B 201 3895 3752 3536 284 -95 -95 C -ATOM 3106 CD2 LEU B 201 4.736 -12.681 -6.510 1.00 27.04 C -ANISOU 3106 CD2 LEU B 201 3389 3518 3368 376 -35 -254 C -ATOM 3107 N ASN B 202 2.482 -9.710 -3.044 1.00 22.40 N -ANISOU 3107 N ASN B 202 3032 2992 2485 156 282 -168 N -ATOM 3108 CA ASN B 202 2.437 -8.247 -2.926 1.00 23.34 C -ANISOU 3108 CA ASN B 202 3151 3135 2584 183 353 -220 C -ATOM 3109 C ASN B 202 3.464 -7.532 -3.816 1.00 22.55 C -ANISOU 3109 C ASN B 202 2964 3074 2529 245 220 -228 C -ATOM 3110 O ASN B 202 3.237 -6.399 -4.245 1.00 26.65 O -ANISOU 3110 O ASN B 202 3426 3602 3098 279 263 -256 O -ATOM 3111 CB ASN B 202 2.520 -7.791 -1.453 1.00 28.22 C -ANISOU 3111 CB ASN B 202 4010 3699 3011 101 433 -235 C -ATOM 3112 CG ASN B 202 3.876 -8.109 -0.794 1.00 34.59 C -ANISOU 3112 CG ASN B 202 4983 4482 3677 43 216 -175 C -ATOM 3113 OD1 ASN B 202 4.602 -9.002 -1.233 1.00 41.12 O -ANISOU 3113 OD1 ASN B 202 5732 5313 4580 77 50 -108 O -ATOM 3114 ND2 ASN B 202 4.207 -7.373 0.277 1.00 33.70 N -ANISOU 3114 ND2 ASN B 202 5103 4332 3371 -47 211 -202 N -ATOM 3115 N HIS B 203 4.577 -8.210 -4.105 1.00 20.73 N -ANISOU 3115 N HIS B 203 2713 2857 2306 260 74 -195 N -ATOM 3116 CA HIS B 203 5.642 -7.635 -4.931 1.00 20.56 C -ANISOU 3116 CA HIS B 203 2586 2888 2338 299 -11 -194 C -ATOM 3117 C HIS B 203 5.386 -7.976 -6.392 1.00 25.36 C -ANISOU 3117 C HIS B 203 3057 3553 3024 352 19 -220 C -ATOM 3118 O HIS B 203 4.747 -8.988 -6.692 1.00 26.59 O -ANISOU 3118 O HIS B 203 3208 3691 3206 358 41 -239 O -ATOM 3119 CB HIS B 203 7.002 -8.248 -4.532 1.00 19.42 C -ANISOU 3119 CB HIS B 203 2438 2729 2212 305 -161 -142 C -ATOM 3120 CG HIS B 203 7.317 -8.135 -3.070 1.00 18.53 C -ANISOU 3120 CG HIS B 203 2503 2558 1979 218 -262 -92 C -ATOM 3121 ND1 HIS B 203 7.437 -6.927 -2.429 1.00 23.88 N -ANISOU 3121 ND1 HIS B 203 3297 3224 2551 134 -276 -112 N -ATOM 3122 CD2 HIS B 203 7.526 -9.093 -2.136 1.00 19.68 C -ANISOU 3122 CD2 HIS B 203 2772 2637 2069 185 -369 -17 C -ATOM 3123 CE1 HIS B 203 7.713 -7.139 -1.148 1.00 24.16 C -ANISOU 3123 CE1 HIS B 203 3538 3205 2436 36 -388 -66 C -ATOM 3124 NE2 HIS B 203 7.782 -8.439 -0.952 1.00 22.34 N -ANISOU 3124 NE2 HIS B 203 3310 2947 2233 65 -457 10 N -ATOM 3125 N VAL B 204 5.897 -7.162 -7.314 1.00 20.30 N -ANISOU 3125 N VAL B 204 2337 2976 2401 361 13 -219 N -ATOM 3126 CA VAL B 204 5.949 -7.591 -8.710 1.00 21.67 C -ANISOU 3126 CA VAL B 204 2437 3212 2584 384 35 -247 C -ATOM 3127 C VAL B 204 7.265 -8.343 -8.896 1.00 24.39 C -ANISOU 3127 C VAL B 204 2724 3568 2975 431 31 -269 C -ATOM 3128 O VAL B 204 8.318 -7.857 -8.494 1.00 24.78 O -ANISOU 3128 O VAL B 204 2714 3634 3069 427 -8 -227 O -ATOM 3129 CB VAL B 204 5.844 -6.414 -9.690 1.00 22.06 C -ANISOU 3129 CB VAL B 204 2454 3322 2604 353 45 -213 C -ATOM 3130 CG1 VAL B 204 6.105 -6.887 -11.127 1.00 23.10 C -ANISOU 3130 CG1 VAL B 204 2571 3534 2672 343 77 -246 C -ATOM 3131 CG2 VAL B 204 4.459 -5.770 -9.574 1.00 22.94 C -ANISOU 3131 CG2 VAL B 204 2577 3395 2744 348 39 -182 C -ATOM 3132 N CYS B 205 7.194 -9.536 -9.485 1.00 20.55 N -ANISOU 3132 N CYS B 205 2246 3057 2506 475 66 -336 N -ATOM 3133 CA CYS B 205 8.349 -10.417 -9.552 1.00 22.24 C -ANISOU 3133 CA CYS B 205 2392 3234 2825 564 87 -369 C -ATOM 3134 C CYS B 205 8.412 -11.018 -10.935 1.00 28.29 C -ANISOU 3134 C CYS B 205 3172 4023 3555 593 211 -487 C -ATOM 3135 O CYS B 205 7.416 -11.024 -11.669 1.00 23.31 O -ANISOU 3135 O CYS B 205 2641 3415 2800 521 220 -530 O -ATOM 3136 CB CYS B 205 8.235 -11.526 -8.511 1.00 26.75 C -ANISOU 3136 CB CYS B 205 3025 3666 3472 605 0 -343 C -ATOM 3137 N VAL B 206 9.588 -11.527 -11.274 1.00 29.99 N -ANISOU 3137 N VAL B 206 3284 4225 3885 692 306 -539 N -ATOM 3138 CA VAL B 206 9.785 -12.229 -12.525 1.00 35.05 C -ANISOU 3138 CA VAL B 206 3975 4861 4482 733 479 -692 C -ATOM 3139 C VAL B 206 9.640 -13.713 -12.244 1.00 36.74 C -ANISOU 3139 C VAL B 206 4267 4881 4811 831 461 -777 C -ATOM 3140 O VAL B 206 10.254 -14.262 -11.318 1.00 36.90 O -ANISOU 3140 O VAL B 206 4194 4786 5039 941 385 -715 O -ATOM 3141 CB VAL B 206 11.161 -11.928 -13.145 1.00 38.46 C -ANISOU 3141 CB VAL B 206 4232 5381 5000 798 668 -723 C -ATOM 3142 CG1 VAL B 206 11.420 -12.838 -14.339 1.00 40.61 C -ANISOU 3142 CG1 VAL B 206 4591 5616 5225 862 905 -923 C -ATOM 3143 CG2 VAL B 206 11.232 -10.466 -13.564 1.00 40.89 C -ANISOU 3143 CG2 VAL B 206 4505 5860 5170 661 688 -630 C -ATOM 3144 N ILE B 207 8.800 -14.351 -13.047 1.00 36.81 N -ANISOU 3144 N ILE B 207 4465 4837 4682 770 498 -904 N -ATOM 3145 CA ILE B 207 8.502 -15.763 -12.901 1.00 33.94 C -ANISOU 3145 CA ILE B 207 4229 4257 4410 823 476 -998 C -ATOM 3146 C ILE B 207 9.683 -16.600 -13.386 1.00 40.04 C -ANISOU 3146 C ILE B 207 4955 4909 5349 1010 667 -1145 C -ATOM 3147 O ILE B 207 10.361 -16.227 -14.344 1.00 44.93 O -ANISOU 3147 O ILE B 207 5529 5639 5902 1037 880 -1248 O -ATOM 3148 CB ILE B 207 7.184 -16.084 -13.658 1.00 52.09 C -ANISOU 3148 CB ILE B 207 6747 6540 6504 654 424 -1088 C -ATOM 3149 CG1 ILE B 207 6.684 -17.491 -13.354 1.00 53.03 C -ANISOU 3149 CG1 ILE B 207 7015 6411 6723 654 357 -1157 C -ATOM 3150 CG2 ILE B 207 7.332 -15.835 -15.168 1.00 56.32 C -ANISOU 3150 CG2 ILE B 207 7401 7183 6815 592 574 -1242 C -ATOM 3151 CD1 ILE B 207 5.309 -17.754 -13.933 1.00 49.87 C -ANISOU 3151 CD1 ILE B 207 6790 6002 6156 443 246 -1207 C -ATOM 3152 N SER B 208 9.952 -17.714 -12.707 1.00 37.28 N -ANISOU 3152 N SER B 208 4609 4323 5233 1142 609 -1143 N -ATOM 3153 CA SER B 208 11.049 -18.588 -13.079 1.00 46.72 C -ANISOU 3153 CA SER B 208 5732 5353 6669 1365 792 -1280 C -ATOM 3154 C SER B 208 10.573 -19.633 -14.095 1.00 47.59 C -ANISOU 3154 C SER B 208 6124 5280 6676 1352 935 -1541 C -ATOM 3155 O SER B 208 9.377 -19.729 -14.382 1.00 42.85 O -ANISOU 3155 O SER B 208 5758 4683 5841 1149 828 -1578 O -ATOM 3156 CB SER B 208 11.622 -19.293 -11.851 1.00 48.70 C -ANISOU 3156 CB SER B 208 5853 5394 7255 1531 621 -1127 C -ATOM 3157 OG SER B 208 10.717 -20.257 -11.346 1.00 48.06 O -ANISOU 3157 OG SER B 208 6004 5086 7172 1469 460 -1105 O -ATOM 3158 N GLU B 209 11.507 -20.406 -14.639 1.00 53.64 N -ANISOU 3158 N GLU B 209 6867 5884 7631 1559 1173 -1721 N -ATOM 3159 CA GLU B 209 11.153 -21.444 -15.599 1.00 56.01 C -ANISOU 3159 CA GLU B 209 7491 6004 7786 1533 1285 -1948 C -ATOM 3160 C GLU B 209 10.337 -22.543 -14.931 1.00 55.98 C -ANISOU 3160 C GLU B 209 7682 5673 7916 1506 1084 -1958 C -ATOM 3161 O GLU B 209 9.330 -23.000 -15.480 1.00 52.29 O -ANISOU 3161 O GLU B 209 7520 5110 7238 1317 1040 -2109 O -ATOM 3162 CB GLU B 209 12.401 -22.018 -16.275 1.00 67.05 C -ANISOU 3162 CB GLU B 209 8821 7356 9299 1752 1523 -2048 C -ATOM 3163 CG GLU B 209 13.089 -21.038 -17.217 1.00 72.10 C -ANISOU 3163 CG GLU B 209 9338 8306 9749 1718 1759 -2080 C -ATOM 3164 CD GLU B 209 12.144 -20.492 -18.272 1.00 76.41 C -ANISOU 3164 CD GLU B 209 10174 9019 9842 1449 1792 -2203 C -ATOM 3165 OE1 GLU B 209 12.259 -19.298 -18.620 1.00 76.72 O -ANISOU 3165 OE1 GLU B 209 10119 9333 9699 1331 1855 -2116 O -ATOM 3166 OE2 GLU B 209 11.283 -21.259 -18.754 1.00 79.78 O -ANISOU 3166 OE2 GLU B 209 10926 9292 10095 1337 1724 -2368 O -ATOM 3167 N THR B 210 10.770 -22.956 -13.743 1.00 56.40 N -ANISOU 3167 N THR B 210 7566 5555 8307 1665 929 -1770 N -ATOM 3168 CA THR B 210 10.045 -23.952 -12.956 1.00 59.63 C -ANISOU 3168 CA THR B 210 8156 5662 8840 1615 699 -1693 C -ATOM 3169 C THR B 210 8.641 -23.457 -12.571 1.00 52.31 C -ANISOU 3169 C THR B 210 7347 4900 7627 1293 478 -1548 C -ATOM 3170 O THR B 210 7.695 -24.244 -12.475 1.00 51.79 O -ANISOU 3170 O THR B 210 7514 4640 7522 1135 358 -1566 O -ATOM 3171 CB THR B 210 10.848 -24.364 -11.701 1.00 65.37 C -ANISOU 3171 CB THR B 210 8683 6211 9943 1825 531 -1447 C -ATOM 3172 OG1 THR B 210 9.966 -24.507 -10.580 1.00 62.12 O -ANISOU 3172 OG1 THR B 210 8379 5745 9478 1645 237 -1205 O -ATOM 3173 CG2 THR B 210 11.899 -23.309 -11.375 1.00 68.90 C -ANISOU 3173 CG2 THR B 210 8766 6938 10477 1940 553 -1291 C -ATOM 3174 N GLY B 211 8.508 -22.150 -12.364 1.00 43.44 N -ANISOU 3174 N GLY B 211 6050 4119 6335 1195 437 -1406 N -ATOM 3175 CA GLY B 211 7.208 -21.545 -12.117 1.00 42.78 C -ANISOU 3175 CA GLY B 211 6027 4209 6016 926 283 -1291 C -ATOM 3176 C GLY B 211 6.333 -21.580 -13.365 1.00 43.24 C -ANISOU 3176 C GLY B 211 6287 4322 5821 735 329 -1486 C -ATOM 3177 O GLY B 211 5.125 -21.835 -13.285 1.00 38.40 O -ANISOU 3177 O GLY B 211 5793 3677 5119 516 180 -1449 O -ATOM 3178 N LYS B 212 6.941 -21.341 -14.527 1.00 44.41 N -ANISOU 3178 N LYS B 212 6474 4551 5846 797 531 -1687 N -ATOM 3179 CA LYS B 212 6.199 -21.380 -15.782 1.00 46.87 C -ANISOU 3179 CA LYS B 212 7032 4913 5862 594 550 -1875 C -ATOM 3180 C LYS B 212 5.687 -22.786 -16.058 1.00 48.33 C -ANISOU 3180 C LYS B 212 7512 4768 6082 518 503 -2053 C -ATOM 3181 O LYS B 212 4.562 -22.965 -16.522 1.00 49.74 O -ANISOU 3181 O LYS B 212 7874 4948 6079 256 341 -2093 O -ATOM 3182 CB LYS B 212 7.052 -20.884 -16.959 1.00 54.51 C -ANISOU 3182 CB LYS B 212 8035 6027 6649 663 817 -2057 C -ATOM 3183 CG LYS B 212 7.054 -19.366 -17.145 1.00 56.96 C -ANISOU 3183 CG LYS B 212 8175 6689 6779 583 804 -1898 C -ATOM 3184 CD LYS B 212 7.843 -18.945 -18.386 1.00 64.41 C -ANISOU 3184 CD LYS B 212 9202 7770 7500 600 1087 -2069 C -ATOM 3185 CE LYS B 212 7.221 -19.491 -19.668 1.00 68.64 C -ANISOU 3185 CE LYS B 212 10122 8257 7702 407 1092 -2286 C -ATOM 3186 NZ LYS B 212 7.976 -19.088 -20.899 1.00 73.82 N -ANISOU 3186 NZ LYS B 212 10839 9086 8123 415 1308 -2349 N -ATOM 3187 N ALA B 213 6.521 -23.781 -15.768 1.00 49.92 N -ANISOU 3187 N ALA B 213 7748 4669 6549 744 624 -2150 N -ATOM 3188 CA ALA B 213 6.177 -25.176 -16.020 1.00 53.45 C -ANISOU 3188 CA ALA B 213 8504 4734 7072 701 601 -2339 C -ATOM 3189 C ALA B 213 5.115 -25.688 -15.041 1.00 50.05 C -ANISOU 3189 C ALA B 213 8104 4163 6751 513 313 -2130 C -ATOM 3190 O ALA B 213 4.191 -26.402 -15.429 1.00 51.63 O -ANISOU 3190 O ALA B 213 8560 4194 6864 279 190 -2232 O -ATOM 3191 CB ALA B 213 7.428 -26.052 -15.970 1.00 60.22 C -ANISOU 3191 CB ALA B 213 9316 5346 8217 1036 764 -2430 C -ATOM 3192 N LYS B 214 5.258 -25.325 -13.772 1.00 44.33 N -ANISOU 3192 N LYS B 214 7132 3508 6203 593 211 -1837 N -ATOM 3193 CA LYS B 214 4.345 -25.784 -12.729 1.00 46.91 C -ANISOU 3193 CA LYS B 214 7484 3715 6625 419 -6 -1616 C -ATOM 3194 C LYS B 214 2.903 -25.327 -12.966 1.00 43.47 C -ANISOU 3194 C LYS B 214 7059 3482 5977 77 -149 -1559 C -ATOM 3195 O LYS B 214 1.967 -26.124 -12.869 1.00 43.01 O -ANISOU 3195 O LYS B 214 7153 3237 5952 -150 -283 -1546 O -ATOM 3196 CB LYS B 214 4.826 -25.312 -11.350 1.00 45.95 C -ANISOU 3196 CB LYS B 214 7127 3680 6652 549 -67 -1318 C -ATOM 3197 CG LYS B 214 4.087 -25.950 -10.177 1.00 50.30 C -ANISOU 3197 CG LYS B 214 7753 4058 7302 391 -241 -1084 C -ATOM 3198 CD LYS B 214 4.477 -25.309 -8.837 1.00 50.45 C -ANISOU 3198 CD LYS B 214 7590 4218 7359 465 -308 -794 C -ATOM 3199 CE LYS B 214 5.902 -25.673 -8.429 1.00 54.09 C -ANISOU 3199 CE LYS B 214 7992 4500 8061 776 -317 -746 C -ATOM 3200 NZ LYS B 214 6.286 -25.017 -7.136 1.00 55.39 N -ANISOU 3200 NZ LYS B 214 8018 4810 8218 804 -437 -461 N -ATOM 3201 N TYR B 215 2.730 -24.050 -13.291 1.00 40.42 N -ANISOU 3201 N TYR B 215 6493 3459 5405 39 -131 -1513 N -ATOM 3202 CA TYR B 215 1.392 -23.472 -13.418 1.00 41.02 C -ANISOU 3202 CA TYR B 215 6495 3743 5349 -241 -282 -1412 C -ATOM 3203 C TYR B 215 0.920 -23.332 -14.870 1.00 46.66 C -ANISOU 3203 C TYR B 215 7361 4544 5822 -411 -335 -1608 C -ATOM 3204 O TYR B 215 -0.043 -22.619 -15.148 1.00 50.22 O -ANISOU 3204 O TYR B 215 7701 5213 6169 -603 -478 -1512 O -ATOM 3205 CB TYR B 215 1.323 -22.122 -12.690 1.00 37.15 C -ANISOU 3205 CB TYR B 215 5711 3562 4841 -190 -269 -1192 C -ATOM 3206 CG TYR B 215 1.717 -22.212 -11.230 1.00 34.38 C -ANISOU 3206 CG TYR B 215 5264 3142 4657 -75 -246 -994 C -ATOM 3207 CD1 TYR B 215 0.950 -22.937 -10.322 1.00 38.10 C -ANISOU 3207 CD1 TYR B 215 5781 3459 5237 -229 -325 -851 C -ATOM 3208 CD2 TYR B 215 2.852 -21.567 -10.757 1.00 36.47 C -ANISOU 3208 CD2 TYR B 215 5405 3499 4952 153 -160 -935 C -ATOM 3209 CE1 TYR B 215 1.312 -23.024 -8.979 1.00 39.65 C -ANISOU 3209 CE1 TYR B 215 5948 3593 5523 -156 -317 -654 C -ATOM 3210 CE2 TYR B 215 3.220 -21.641 -9.420 1.00 36.07 C -ANISOU 3210 CE2 TYR B 215 5306 3388 5012 226 -190 -743 C -ATOM 3211 CZ TYR B 215 2.453 -22.370 -8.537 1.00 39.12 C -ANISOU 3211 CZ TYR B 215 5784 3620 5459 72 -268 -604 C -ATOM 3212 OH TYR B 215 2.843 -22.450 -7.215 1.00 36.51 O -ANISOU 3212 OH TYR B 215 5462 3230 5180 118 -309 -401 O -ATOM 3213 N LYS B 216 1.600 -24.010 -15.790 1.00 49.94 N -ANISOU 3213 N LYS B 216 8042 4780 6152 -339 -222 -1879 N -ATOM 3214 CA LYS B 216 1.224 -23.957 -17.199 1.00 56.65 C -ANISOU 3214 CA LYS B 216 9127 5695 6704 -528 -271 -2087 C -ATOM 3215 C LYS B 216 -0.142 -24.601 -17.409 1.00 62.54 C -ANISOU 3215 C LYS B 216 10005 6329 7427 -878 -551 -2081 C -ATOM 3216 O LYS B 216 -0.441 -25.638 -16.819 1.00 61.34 O -ANISOU 3216 O LYS B 216 9937 5892 7478 -942 -610 -2072 O -ATOM 3217 CB LYS B 216 2.284 -24.646 -18.070 1.00 65.11 C -ANISOU 3217 CB LYS B 216 10494 6562 7683 -371 -25 -2417 C -ATOM 3218 CG LYS B 216 1.839 -24.949 -19.496 1.00 71.30 C -ANISOU 3218 CG LYS B 216 11509 7401 8181 -576 -94 -2599 C -ATOM 3219 CD LYS B 216 3.009 -24.968 -20.474 1.00 75.78 C -ANISOU 3219 CD LYS B 216 12161 8023 8610 -367 200 -2806 C -ATOM 3220 CE LYS B 216 2.547 -25.361 -21.872 1.00 81.97 C -ANISOU 3220 CE LYS B 216 13222 8836 9085 -580 124 -2977 C -ATOM 3221 NZ LYS B 216 1.341 -24.589 -22.297 1.00 82.45 N -ANISOU 3221 NZ LYS B 216 13285 9136 8907 -901 -189 -2816 N -ATOM 3222 N ALA B 217 -0.973 -23.975 -18.239 1.00 70.42 N -ANISOU 3222 N ALA B 217 11012 7547 8197 -1120 -748 -2061 N -ATOM 3223 CA ALA B 217 -2.298 -24.510 -18.546 1.00 77.12 C -ANISOU 3223 CA ALA B 217 11933 8327 9041 -1481 -1058 -2036 C -ATOM 3224 C ALA B 217 -2.284 -25.326 -19.834 1.00 85.78 C -ANISOU 3224 C ALA B 217 13314 9337 9944 -1565 -1065 -2262 C -ATOM 3225 O ALA B 217 -1.439 -25.115 -20.708 1.00 87.22 O -ANISOU 3225 O ALA B 217 13650 9592 9899 -1422 -882 -2430 O -ATOM 3226 CB ALA B 217 -3.318 -23.386 -18.637 1.00 74.92 C -ANISOU 3226 CB ALA B 217 11362 8372 8731 -1653 -1299 -1794 C -ATOM 3227 OXT ALA B 217 -3.122 -26.207 -20.034 1.00 91.27 O -ANISOU 3227 OXT ALA B 217 14090 9888 10702 -1791 -1246 -2278 O -TER 3228 ALA B 217 -ATOM 3229 N SER C 4 -10.278 20.758 20.620 1.00 70.62 N -ANISOU 3229 N SER C 4 10395 8353 8083 905 1012 -910 N -ATOM 3230 CA SER C 4 -11.254 19.868 21.243 1.00 70.28 C -ANISOU 3230 CA SER C 4 10158 8404 8143 889 1223 -1085 C -ATOM 3231 C SER C 4 -10.692 19.225 22.509 1.00 72.47 C -ANISOU 3231 C SER C 4 10718 8611 8207 441 1242 -1071 C -ATOM 3232 O SER C 4 -9.473 19.119 22.667 1.00 74.64 O -ANISOU 3232 O SER C 4 11191 8882 8285 161 1006 -908 O -ATOM 3233 CB SER C 4 -11.731 18.792 20.245 1.00 66.17 C -ANISOU 3233 CB SER C 4 9033 8223 7888 1102 1085 -1111 C -ATOM 3234 OG SER C 4 -10.654 18.105 19.622 1.00 57.40 O -ANISOU 3234 OG SER C 4 7774 7279 6757 973 718 -932 O -ATOM 3235 N PRO C 5 -11.582 18.802 23.425 1.00 71.80 N -ANISOU 3235 N PRO C 5 10644 8496 8142 381 1531 -1234 N -ATOM 3236 CA PRO C 5 -11.166 17.954 24.551 1.00 67.57 C -ANISOU 3236 CA PRO C 5 10287 7954 7433 0 1558 -1209 C -ATOM 3237 C PRO C 5 -10.775 16.569 24.042 1.00 54.93 C -ANISOU 3237 C PRO C 5 8329 6597 5943 -75 1318 -1105 C -ATOM 3238 O PRO C 5 -10.283 15.737 24.809 1.00 52.63 O -ANISOU 3238 O PRO C 5 8157 6330 5512 -363 1293 -1034 O -ATOM 3239 CB PRO C 5 -12.437 17.850 25.400 1.00 73.77 C -ANISOU 3239 CB PRO C 5 11071 8682 8277 48 1946 -1415 C -ATOM 3240 CG PRO C 5 -13.552 18.059 24.428 1.00 75.57 C -ANISOU 3240 CG PRO C 5 10897 9028 8789 464 2043 -1541 C -ATOM 3241 CD PRO C 5 -13.028 19.083 23.456 1.00 74.63 C -ANISOU 3241 CD PRO C 5 10835 8852 8670 680 1856 -1440 C -ATOM 3242 N GLY C 6 -11.005 16.338 22.751 1.00 42.40 N -ANISOU 3242 N GLY C 6 6316 5194 4599 204 1154 -1097 N -ATOM 3243 CA GLY C 6 -10.634 15.095 22.105 1.00 36.14 C -ANISOU 3243 CA GLY C 6 5175 4627 3931 174 912 -1015 C -ATOM 3244 C GLY C 6 -11.792 14.125 22.014 1.00 32.48 C -ANISOU 3244 C GLY C 6 4322 4291 3727 265 1096 -1193 C -ATOM 3245 O GLY C 6 -12.941 14.485 22.263 1.00 36.09 O -ANISOU 3245 O GLY C 6 4708 4716 4289 409 1390 -1378 O -ATOM 3246 N VAL C 7 -11.486 12.883 21.658 1.00 30.81 N -ANISOU 3246 N VAL C 7 3861 4232 3615 178 930 -1140 N -ATOM 3247 CA VAL C 7 -12.492 11.837 21.672 1.00 32.24 C -ANISOU 3247 CA VAL C 7 3708 4511 4032 181 1114 -1311 C -ATOM 3248 C VAL C 7 -12.777 11.485 23.123 1.00 35.99 C -ANISOU 3248 C VAL C 7 4484 4815 4376 -102 1410 -1342 C -ATOM 3249 O VAL C 7 -11.886 11.046 23.854 1.00 32.91 O -ANISOU 3249 O VAL C 7 4391 4340 3773 -365 1338 -1178 O -ATOM 3250 CB VAL C 7 -12.012 10.589 20.926 1.00 29.61 C -ANISOU 3250 CB VAL C 7 3077 4342 3830 146 863 -1245 C -ATOM 3251 CG1 VAL C 7 -13.048 9.478 21.045 1.00 35.74 C -ANISOU 3251 CG1 VAL C 7 3552 5180 4848 87 1088 -1437 C -ATOM 3252 CG2 VAL C 7 -11.725 10.910 19.457 1.00 36.78 C -ANISOU 3252 CG2 VAL C 7 3661 5455 4859 442 561 -1214 C -ATOM 3253 N VAL C 8 -14.018 11.701 23.551 1.00 35.93 N -ANISOU 3253 N VAL C 8 4393 4785 4473 -30 1747 -1546 N -ATOM 3254 CA VAL C 8 -14.393 11.423 24.927 1.00 41.06 C -ANISOU 3254 CA VAL C 8 5309 5291 5000 -275 2055 -1583 C -ATOM 3255 C VAL C 8 -14.773 9.957 25.084 1.00 45.04 C -ANISOU 3255 C VAL C 8 5585 5859 5670 -446 2154 -1623 C -ATOM 3256 O VAL C 8 -15.745 9.481 24.486 1.00 45.74 O -ANISOU 3256 O VAL C 8 5250 6094 6034 -329 2256 -1806 O -ATOM 3257 CB VAL C 8 -15.554 12.307 25.385 1.00 46.21 C -ANISOU 3257 CB VAL C 8 5991 5898 5668 -125 2391 -1779 C -ATOM 3258 CG1 VAL C 8 -16.025 11.880 26.759 1.00 46.04 C -ANISOU 3258 CG1 VAL C 8 6183 5770 5540 -371 2718 -1826 C -ATOM 3259 CG2 VAL C 8 -15.126 13.764 25.407 1.00 40.94 C -ANISOU 3259 CG2 VAL C 8 5650 5094 4810 8 2336 -1731 C -ATOM 3260 N ILE C 9 -13.981 9.233 25.869 1.00 38.43 N -ANISOU 3260 N ILE C 9 5026 4920 4656 -722 2124 -1450 N -ATOM 3261 CA ILE C 9 -14.321 7.859 26.217 1.00 40.56 C -ANISOU 3261 CA ILE C 9 5173 5183 5054 -911 2274 -1463 C -ATOM 3262 C ILE C 9 -14.986 7.922 27.586 1.00 41.36 C -ANISOU 3262 C ILE C 9 5519 5163 5035 -1079 2660 -1520 C -ATOM 3263 O ILE C 9 -14.375 8.364 28.564 1.00 41.77 O -ANISOU 3263 O ILE C 9 5992 5099 4780 -1212 2693 -1390 O -ATOM 3264 CB ILE C 9 -13.080 6.957 26.204 1.00 38.90 C -ANISOU 3264 CB ILE C 9 5108 4949 4722 -1064 2024 -1221 C -ATOM 3265 CG1 ILE C 9 -12.474 6.932 24.796 1.00 37.20 C -ANISOU 3265 CG1 ILE C 9 4623 4883 4628 -872 1643 -1179 C -ATOM 3266 CG2 ILE C 9 -13.425 5.541 26.653 1.00 39.54 C -ANISOU 3266 CG2 ILE C 9 5130 4970 4925 -1261 2222 -1217 C -ATOM 3267 CD1 ILE C 9 -11.264 6.056 24.664 1.00 34.40 C -ANISOU 3267 CD1 ILE C 9 4376 4539 4156 -975 1380 -946 C -ATOM 3268 N SER C 10 -16.260 7.546 27.652 1.00 49.43 N -ANISOU 3268 N SER C 10 6261 6236 6282 -1069 2955 -1726 N -ATOM 3269 CA SER C 10 -17.021 7.750 28.881 1.00 53.27 C -ANISOU 3269 CA SER C 10 6939 6634 6668 -1177 3287 -1779 C -ATOM 3270 C SER C 10 -16.710 6.680 29.918 1.00 52.71 C -ANISOU 3270 C SER C 10 7102 6440 6486 -1475 3436 -1630 C -ATOM 3271 O SER C 10 -16.142 5.636 29.592 1.00 48.06 O -ANISOU 3271 O SER C 10 6458 5842 5960 -1594 3348 -1525 O -ATOM 3272 CB SER C 10 -18.526 7.845 28.603 1.00 58.50 C -ANISOU 3272 CB SER C 10 7231 7407 7591 -1020 3376 -1961 C -ATOM 3273 OG SER C 10 -18.898 7.035 27.504 1.00 63.79 O -ANISOU 3273 OG SER C 10 7473 8214 8551 -963 3232 -2042 O -ATOM 3274 N ASP C 11 -17.078 6.959 31.166 1.00 49.89 N -ANISOU 3274 N ASP C 11 7007 5985 5965 -1565 3628 -1600 N -ATOM 3275 CA ASP C 11 -16.749 6.091 32.297 1.00 55.02 C -ANISOU 3275 CA ASP C 11 7925 6514 6466 -1799 3735 -1426 C -ATOM 3276 C ASP C 11 -17.328 4.692 32.137 1.00 55.65 C -ANISOU 3276 C ASP C 11 7757 6575 6814 -1911 3842 -1449 C -ATOM 3277 O ASP C 11 -16.749 3.714 32.607 1.00 57.47 O -ANISOU 3277 O ASP C 11 8159 6708 6970 -2058 3830 -1268 O -ATOM 3278 CB ASP C 11 -17.250 6.702 33.611 1.00 56.15 C -ANISOU 3278 CB ASP C 11 8313 6591 6429 -1830 3924 -1437 C -ATOM 3279 CG ASP C 11 -16.368 7.833 34.114 1.00 59.97 C -ANISOU 3279 CG ASP C 11 9170 7034 6583 -1804 3793 -1351 C -ATOM 3280 OD1 ASP C 11 -15.689 8.482 33.296 1.00 59.01 O -ANISOU 3280 OD1 ASP C 11 9066 6948 6407 -1707 3586 -1349 O -ATOM 3281 OD2 ASP C 11 -16.366 8.074 35.342 1.00 66.34 O -ANISOU 3281 OD2 ASP C 11 10242 7776 7186 -1884 3889 -1295 O -ATOM 3282 N ASP C 12 -18.473 4.608 31.468 1.00 55.53 N -ANISOU 3282 N ASP C 12 7344 6657 7099 -1821 3913 -1667 N -ATOM 3283 CA ASP C 12 -19.132 3.330 31.240 1.00 63.27 C -ANISOU 3283 CA ASP C 12 8075 7617 8346 -1937 4000 -1731 C -ATOM 3284 C ASP C 12 -18.809 2.748 29.862 1.00 61.20 C -ANISOU 3284 C ASP C 12 7508 7430 8314 -1881 3781 -1787 C -ATOM 3285 O ASP C 12 -19.647 2.094 29.239 1.00 63.89 O -ANISOU 3285 O ASP C 12 7514 7832 8929 -1883 3785 -1949 O -ATOM 3286 CB ASP C 12 -20.648 3.450 31.454 1.00 70.20 C -ANISOU 3286 CB ASP C 12 8708 8579 9385 -1909 4191 -1929 C -ATOM 3287 CG ASP C 12 -21.333 4.293 30.394 1.00 73.82 C -ANISOU 3287 CG ASP C 12 8810 9248 9993 -1655 4050 -2116 C -ATOM 3288 OD1 ASP C 12 -20.637 5.033 29.660 1.00 70.21 O -ANISOU 3288 OD1 ASP C 12 8347 8848 9480 -1479 3833 -2093 O -ATOM 3289 OD2 ASP C 12 -22.578 4.214 30.300 1.00 78.78 O -ANISOU 3289 OD2 ASP C 12 9168 9995 10770 -1618 4143 -2269 O -ATOM 3290 N GLU C 13 -17.592 2.995 29.388 1.00 56.75 N -ANISOU 3290 N GLU C 13 7065 6879 7620 -1831 3571 -1654 N -ATOM 3291 CA GLU C 13 -17.127 2.388 28.146 1.00 57.52 C -ANISOU 3291 CA GLU C 13 6897 7048 7910 -1779 3345 -1675 C -ATOM 3292 C GLU C 13 -16.751 0.931 28.385 1.00 58.04 C -ANISOU 3292 C GLU C 13 7068 6953 8031 -1973 3381 -1538 C -ATOM 3293 O GLU C 13 -15.837 0.640 29.161 1.00 56.18 O -ANISOU 3293 O GLU C 13 7212 6589 7544 -2078 3380 -1281 O -ATOM 3294 CB GLU C 13 -15.927 3.153 27.583 1.00 60.42 C -ANISOU 3294 CB GLU C 13 7373 7488 8094 -1638 3047 -1546 C -ATOM 3295 CG GLU C 13 -15.283 2.516 26.345 1.00 67.17 C -ANISOU 3295 CG GLU C 13 7997 8416 9109 -1545 2707 -1511 C -ATOM 3296 CD GLU C 13 -16.104 2.695 25.072 1.00 74.83 C -ANISOU 3296 CD GLU C 13 8443 9595 10394 -1349 2631 -1788 C -ATOM 3297 OE1 GLU C 13 -17.184 3.323 25.134 1.00 80.25 O -ANISOU 3297 OE1 GLU C 13 8994 10351 11146 -1243 2736 -1951 O -ATOM 3298 OE2 GLU C 13 -15.663 2.212 24.003 1.00 75.97 O -ANISOU 3298 OE2 GLU C 13 8360 9828 10677 -1254 2356 -1792 O -ATOM 3299 N PRO C 14 -17.464 0.003 27.724 1.00 66.67 N -ANISOU 3299 N PRO C 14 7851 8052 9428 -1994 3383 -1702 N -ATOM 3300 CA PRO C 14 -17.124 -1.417 27.857 1.00 67.63 C -ANISOU 3300 CA PRO C 14 8085 7994 9618 -2148 3420 -1587 C -ATOM 3301 C PRO C 14 -15.808 -1.759 27.170 1.00 59.78 C -ANISOU 3301 C PRO C 14 7147 6994 8572 -2106 3158 -1410 C -ATOM 3302 O PRO C 14 -15.208 -2.777 27.501 1.00 65.21 O -ANISOU 3302 O PRO C 14 8061 7511 9205 -2203 3171 -1219 O -ATOM 3303 CB PRO C 14 -18.284 -2.128 27.146 1.00 70.35 C -ANISOU 3303 CB PRO C 14 8059 8381 10292 -2162 3462 -1862 C -ATOM 3304 CG PRO C 14 -18.826 -1.119 26.195 1.00 70.12 C -ANISOU 3304 CG PRO C 14 7680 8605 10357 -1947 3280 -2070 C -ATOM 3305 CD PRO C 14 -18.642 0.216 26.863 1.00 69.70 C -ANISOU 3305 CD PRO C 14 7809 8606 10067 -1864 3332 -1987 C -ATOM 3306 N GLY C 15 -15.356 -0.925 26.240 1.00 54.32 N -ANISOU 3306 N GLY C 15 6258 6496 7887 -1944 2914 -1459 N -ATOM 3307 CA GLY C 15 -14.221 -1.303 25.413 1.00 51.71 C -ANISOU 3307 CA GLY C 15 5925 6193 7529 -1842 2563 -1313 C -ATOM 3308 C GLY C 15 -14.556 -2.585 24.665 1.00 52.04 C -ANISOU 3308 C GLY C 15 5703 6179 7892 -1911 2585 -1451 C -ATOM 3309 O GLY C 15 -15.731 -2.862 24.406 1.00 55.29 O -ANISOU 3309 O GLY C 15 5873 6617 8517 -1899 2687 -1702 O -ATOM 3310 N TYR C 16 -13.541 -3.387 24.354 1.00 45.39 N -ANISOU 3310 N TYR C 16 4999 5249 7000 -1895 2387 -1261 N -ATOM 3311 CA TYR C 16 -13.741 -4.576 23.528 1.00 45.27 C -ANISOU 3311 CA TYR C 16 4753 5170 7276 -1930 2364 -1400 C -ATOM 3312 C TYR C 16 -13.114 -5.847 24.109 1.00 47.74 C -ANISOU 3312 C TYR C 16 5421 5194 7526 -2076 2487 -1164 C -ATOM 3313 O TYR C 16 -12.015 -5.807 24.666 1.00 45.36 O -ANISOU 3313 O TYR C 16 5494 4835 6906 -2026 2371 -836 O -ATOM 3314 CB TYR C 16 -13.173 -4.328 22.129 1.00 39.71 C -ANISOU 3314 CB TYR C 16 3749 4694 6646 -1683 1941 -1465 C -ATOM 3315 CG TYR C 16 -13.735 -3.107 21.446 1.00 42.36 C -ANISOU 3315 CG TYR C 16 3757 5317 7021 -1471 1788 -1662 C -ATOM 3316 CD1 TYR C 16 -14.902 -3.190 20.696 1.00 50.05 C -ANISOU 3316 CD1 TYR C 16 4462 6393 8161 -1342 1751 -1928 C -ATOM 3317 CD2 TYR C 16 -13.110 -1.869 21.562 1.00 37.01 C -ANISOU 3317 CD2 TYR C 16 3202 4768 6090 -1317 1597 -1510 C -ATOM 3318 CE1 TYR C 16 -15.427 -2.082 20.074 1.00 50.41 C -ANISOU 3318 CE1 TYR C 16 4339 6656 8159 -1105 1573 -2025 C -ATOM 3319 CE2 TYR C 16 -13.632 -0.745 20.941 1.00 42.82 C -ANISOU 3319 CE2 TYR C 16 3648 5740 6880 -1118 1501 -1681 C -ATOM 3320 CZ TYR C 16 -14.791 -0.867 20.196 1.00 46.07 C -ANISOU 3320 CZ TYR C 16 3849 6220 7435 -977 1449 -1892 C -ATOM 3321 OH TYR C 16 -15.324 0.233 19.574 1.00 46.25 O -ANISOU 3321 OH TYR C 16 3760 6415 7400 -737 1286 -1948 O -ATOM 3322 N ASP C 17 -13.819 -6.969 23.963 1.00 45.63 N -ANISOU 3322 N ASP C 17 5075 4779 7482 -2156 2642 -1314 N -ATOM 3323 CA ASP C 17 -13.307 -8.283 24.352 1.00 50.26 C -ANISOU 3323 CA ASP C 17 5968 5079 8051 -2254 2760 -1119 C -ATOM 3324 C ASP C 17 -12.020 -8.552 23.569 1.00 47.97 C -ANISOU 3324 C ASP C 17 5710 4788 7728 -2152 2469 -958 C -ATOM 3325 O ASP C 17 -11.966 -8.308 22.366 1.00 42.67 O -ANISOU 3325 O ASP C 17 4682 4327 7203 -1993 2173 -1144 O -ATOM 3326 CB ASP C 17 -14.353 -9.371 24.054 1.00 55.20 C -ANISOU 3326 CB ASP C 17 6425 5582 8968 -2356 2952 -1378 C -ATOM 3327 CG ASP C 17 -13.954 -10.755 24.581 1.00 64.66 C -ANISOU 3327 CG ASP C 17 7967 6449 10150 -2459 3133 -1181 C -ATOM 3328 OD1 ASP C 17 -12.780 -11.155 24.425 1.00 64.08 O -ANISOU 3328 OD1 ASP C 17 8112 6271 9965 -2384 2987 -934 O -ATOM 3329 OD2 ASP C 17 -14.826 -11.455 25.148 1.00 71.76 O -ANISOU 3329 OD2 ASP C 17 8927 7195 11144 -2603 3425 -1269 O -ATOM 3330 N LEU C 18 -10.997 -9.056 24.262 1.00 37.47 N -ANISOU 3330 N LEU C 18 5055 4461 4720 -1712 610 451 N -ATOM 3331 CA LEU C 18 -9.696 -9.344 23.656 1.00 35.61 C -ANISOU 3331 CA LEU C 18 4957 4011 4564 -1526 447 371 C -ATOM 3332 C LEU C 18 -9.836 -10.296 22.470 1.00 32.17 C -ANISOU 3332 C LEU C 18 4548 3408 4266 -1529 280 309 C -ATOM 3333 O LEU C 18 -9.084 -10.210 21.509 1.00 33.38 O -ANISOU 3333 O LEU C 18 4697 3503 4482 -1337 208 164 O -ATOM 3334 CB LEU C 18 -8.759 -9.974 24.692 1.00 36.63 C -ANISOU 3334 CB LEU C 18 5294 3991 4633 -1564 332 482 C -ATOM 3335 CG LEU C 18 -8.378 -9.149 25.921 1.00 38.45 C -ANISOU 3335 CG LEU C 18 5541 4373 4694 -1573 461 531 C -ATOM 3336 CD1 LEU C 18 -7.632 -9.999 26.946 1.00 40.82 C -ANISOU 3336 CD1 LEU C 18 6049 4533 4927 -1670 303 695 C -ATOM 3337 CD2 LEU C 18 -7.530 -7.977 25.506 1.00 34.31 C -ANISOU 3337 CD2 LEU C 18 4953 3917 4168 -1337 526 378 C -ATOM 3338 N ASP C 19 -10.816 -11.191 22.544 1.00 32.65 N -ANISOU 3338 N ASP C 19 4630 3421 4356 -1771 220 412 N -ATOM 3339 CA ASP C 19 -10.961 -12.246 21.538 1.00 37.36 C -ANISOU 3339 CA ASP C 19 5304 3812 5079 -1815 29 346 C -ATOM 3340 C ASP C 19 -11.410 -11.763 20.165 1.00 32.76 C -ANISOU 3340 C ASP C 19 4538 3366 4543 -1725 68 189 C -ATOM 3341 O ASP C 19 -11.478 -12.553 19.222 1.00 33.72 O -ANISOU 3341 O ASP C 19 4716 3348 4747 -1747 -84 88 O -ATOM 3342 CB ASP C 19 -11.928 -13.317 22.029 1.00 43.62 C -ANISOU 3342 CB ASP C 19 6184 4512 5878 -2160 -65 525 C -ATOM 3343 CG ASP C 19 -11.290 -14.255 23.008 1.00 60.83 C -ANISOU 3343 CG ASP C 19 8634 6419 8059 -2255 -237 680 C -ATOM 3344 OD1 ASP C 19 -10.510 -13.781 23.861 1.00 66.38 O -ANISOU 3344 OD1 ASP C 19 9379 7165 8678 -2144 -180 729 O -ATOM 3345 OD2 ASP C 19 -11.556 -15.470 22.916 1.00 72.93 O -ANISOU 3345 OD2 ASP C 19 10350 7679 9680 -2448 -455 760 O -ATOM 3346 N LEU C 20 -11.732 -10.481 20.060 1.00 31.19 N -ANISOU 3346 N LEU C 20 4133 3430 4289 -1630 251 167 N -ATOM 3347 CA LEU C 20 -12.203 -9.926 18.794 1.00 30.51 C -ANISOU 3347 CA LEU C 20 3865 3492 4234 -1558 270 64 C -ATOM 3348 C LEU C 20 -11.043 -9.331 18.015 1.00 30.72 C -ANISOU 3348 C LEU C 20 3904 3518 4252 -1313 247 -77 C -ATOM 3349 O LEU C 20 -11.199 -8.922 16.859 1.00 28.31 O -ANISOU 3349 O LEU C 20 3478 3330 3947 -1256 230 -158 O -ATOM 3350 CB LEU C 20 -13.275 -8.858 19.039 1.00 36.04 C -ANISOU 3350 CB LEU C 20 4327 4462 4905 -1578 446 131 C -ATOM 3351 CG LEU C 20 -14.584 -9.376 19.627 1.00 35.52 C -ANISOU 3351 CG LEU C 20 4158 4514 4823 -1841 491 256 C -ATOM 3352 CD1 LEU C 20 -15.457 -8.228 20.109 1.00 41.49 C -ANISOU 3352 CD1 LEU C 20 4662 5559 5543 -1784 692 282 C -ATOM 3353 CD2 LEU C 20 -15.346 -10.212 18.624 1.00 36.66 C -ANISOU 3353 CD2 LEU C 20 4251 4652 5027 -2015 354 247 C -ATOM 3354 N PHE C 21 -9.881 -9.297 18.664 1.00 28.01 N -ANISOU 3354 N PHE C 21 3692 3074 3879 -1196 239 -88 N -ATOM 3355 CA PHE C 21 -8.679 -8.690 18.102 1.00 28.75 C -ANISOU 3355 CA PHE C 21 3774 3216 3933 -993 230 -202 C -ATOM 3356 C PHE C 21 -7.482 -9.636 18.105 1.00 30.67 C -ANISOU 3356 C PHE C 21 4167 3287 4200 -884 89 -300 C -ATOM 3357 O PHE C 21 -7.538 -10.718 18.688 1.00 30.35 O -ANISOU 3357 O PHE C 21 4278 3030 4222 -955 -20 -255 O -ATOM 3358 CB PHE C 21 -8.340 -7.415 18.864 1.00 27.51 C -ANISOU 3358 CB PHE C 21 3580 3167 3707 -927 367 -135 C -ATOM 3359 CG PHE C 21 -9.387 -6.355 18.730 1.00 35.65 C -ANISOU 3359 CG PHE C 21 4455 4351 4742 -952 486 -85 C -ATOM 3360 CD1 PHE C 21 -9.357 -5.473 17.662 1.00 37.49 C -ANISOU 3360 CD1 PHE C 21 4573 4699 4971 -873 481 -123 C -ATOM 3361 CD2 PHE C 21 -10.426 -6.266 19.645 1.00 40.74 C -ANISOU 3361 CD2 PHE C 21 5052 5039 5388 -1056 591 2 C -ATOM 3362 CE1 PHE C 21 -10.325 -4.496 17.516 1.00 45.16 C -ANISOU 3362 CE1 PHE C 21 5405 5775 5978 -860 553 -69 C -ATOM 3363 CE2 PHE C 21 -11.402 -5.293 19.504 1.00 47.34 C -ANISOU 3363 CE2 PHE C 21 5715 6023 6251 -1025 692 18 C -ATOM 3364 CZ PHE C 21 -11.349 -4.403 18.436 1.00 48.36 C -ANISOU 3364 CZ PHE C 21 5749 6212 6413 -910 659 -15 C -ATOM 3365 N CYS C 22 -6.413 -9.225 17.420 1.00 28.63 N -ANISOU 3365 N CYS C 22 3852 3134 3891 -716 77 -429 N -ATOM 3366 CA CYS C 22 -5.175 -9.992 17.401 1.00 32.72 C -ANISOU 3366 CA CYS C 22 4454 3550 4429 -554 -45 -554 C -ATOM 3367 C CYS C 22 -4.338 -9.454 18.555 1.00 31.66 C -ANISOU 3367 C CYS C 22 4358 3430 4241 -503 -2 -445 C -ATOM 3368 O CYS C 22 -4.003 -8.277 18.582 1.00 31.66 O -ANISOU 3368 O CYS C 22 4263 3620 4147 -491 106 -413 O -ATOM 3369 CB CYS C 22 -4.447 -9.815 16.062 1.00 33.74 C -ANISOU 3369 CB CYS C 22 4454 3876 4491 -418 -61 -762 C -ATOM 3370 N ILE C 23 -4.047 -10.312 19.528 1.00 31.09 N -ANISOU 3370 N ILE C 23 4442 3144 4225 -499 -109 -372 N -ATOM 3371 CA ILE C 23 -3.347 -9.910 20.748 1.00 34.60 C -ANISOU 3371 CA ILE C 23 4940 3604 4603 -489 -90 -245 C -ATOM 3372 C ILE C 23 -2.175 -10.857 20.986 1.00 33.89 C -ANISOU 3372 C ILE C 23 4933 3367 4575 -310 -280 -300 C -ATOM 3373 O ILE C 23 -2.341 -12.068 20.867 1.00 36.92 O -ANISOU 3373 O ILE C 23 5443 3496 5088 -280 -445 -332 O -ATOM 3374 CB ILE C 23 -4.294 -10.051 21.963 1.00 36.66 C -ANISOU 3374 CB ILE C 23 5315 3768 4844 -706 -49 -36 C -ATOM 3375 CG1 ILE C 23 -5.492 -9.112 21.817 1.00 38.25 C -ANISOU 3375 CG1 ILE C 23 5401 4133 4997 -840 141 -2 C -ATOM 3376 CG2 ILE C 23 -3.539 -9.845 23.279 1.00 36.14 C -ANISOU 3376 CG2 ILE C 23 5335 3709 4687 -715 -64 93 C -ATOM 3377 CD1 ILE C 23 -5.146 -7.660 21.905 1.00 34.75 C -ANISOU 3377 CD1 ILE C 23 4858 3889 4457 -785 284 -24 C -ATOM 3378 N PRO C 24 -0.998 -10.324 21.355 1.00 30.76 N -ANISOU 3378 N PRO C 24 4471 3118 4100 -193 -279 -305 N -ATOM 3379 CA PRO C 24 0.128 -11.247 21.569 1.00 34.06 C -ANISOU 3379 CA PRO C 24 4931 3416 4595 18 -478 -363 C -ATOM 3380 C PRO C 24 -0.153 -12.243 22.695 1.00 38.56 C -ANISOU 3380 C PRO C 24 5731 3671 5251 -61 -645 -170 C -ATOM 3381 O PRO C 24 -0.650 -11.847 23.755 1.00 37.85 O -ANISOU 3381 O PRO C 24 5722 3594 5063 -275 -575 44 O -ATOM 3382 CB PRO C 24 1.289 -10.308 21.919 1.00 30.51 C -ANISOU 3382 CB PRO C 24 4345 3239 4010 85 -425 -353 C -ATOM 3383 CG PRO C 24 0.654 -9.011 22.322 1.00 35.26 C -ANISOU 3383 CG PRO C 24 4932 3989 4475 -139 -227 -231 C -ATOM 3384 CD PRO C 24 -0.613 -8.916 21.544 1.00 27.04 C -ANISOU 3384 CD PRO C 24 3884 2911 3479 -240 -126 -270 C -ATOM 3385 N ASN C 25 0.143 -13.521 22.449 1.00 39.15 N -ANISOU 3385 N ASN C 25 5915 3464 5496 101 -874 -250 N -ATOM 3386 CA ASN C 25 -0.185 -14.602 23.380 1.00 45.97 C -ANISOU 3386 CA ASN C 25 7034 3966 6465 1 -1087 -43 C -ATOM 3387 C ASN C 25 0.399 -14.423 24.782 1.00 43.19 C -ANISOU 3387 C ASN C 25 6752 3641 6017 -60 -1154 208 C -ATOM 3388 O ASN C 25 -0.155 -14.944 25.757 1.00 44.17 O -ANISOU 3388 O ASN C 25 7076 3574 6131 -283 -1254 467 O -ATOM 3389 CB ASN C 25 0.243 -15.956 22.787 1.00 54.82 C -ANISOU 3389 CB ASN C 25 8269 4743 7818 252 -1363 -213 C -ATOM 3390 CG ASN C 25 -0.120 -17.138 23.677 1.00 68.27 C -ANISOU 3390 CG ASN C 25 10279 6003 9655 125 -1637 29 C -ATOM 3391 OD1 ASN C 25 -1.298 -17.431 23.890 1.00 73.29 O -ANISOU 3391 OD1 ASN C 25 11062 6498 10287 -190 -1625 189 O -ATOM 3392 ND2 ASN C 25 0.894 -17.842 24.175 1.00 71.52 N -ANISOU 3392 ND2 ASN C 25 10782 6204 10189 362 -1904 67 N -ATOM 3393 N HIS C 26 1.509 -13.692 24.891 1.00 40.98 N -ANISOU 3393 N HIS C 26 6304 3626 5643 101 -1107 145 N -ATOM 3394 CA HIS C 26 2.189 -13.570 26.184 1.00 43.87 C -ANISOU 3394 CA HIS C 26 6727 4034 5909 55 -1203 367 C -ATOM 3395 C HIS C 26 1.483 -12.620 27.148 1.00 43.78 C -ANISOU 3395 C HIS C 26 6754 4208 5674 -277 -1001 561 C -ATOM 3396 O HIS C 26 1.841 -12.553 28.321 1.00 45.44 O -ANISOU 3396 O HIS C 26 7045 4456 5762 -387 -1073 765 O -ATOM 3397 CB HIS C 26 3.692 -13.236 26.041 1.00 41.78 C -ANISOU 3397 CB HIS C 26 6260 3993 5620 333 -1265 242 C -ATOM 3398 CG HIS C 26 3.988 -11.967 25.299 1.00 42.12 C -ANISOU 3398 CG HIS C 26 6058 4423 5525 339 -1018 65 C -ATOM 3399 ND1 HIS C 26 4.248 -11.933 23.942 1.00 44.99 N -ANISOU 3399 ND1 HIS C 26 6238 4909 5947 531 -958 -210 N -ATOM 3400 CD2 HIS C 26 4.119 -10.688 25.734 1.00 40.19 C -ANISOU 3400 CD2 HIS C 26 5731 4464 5076 164 -840 130 C -ATOM 3401 CE1 HIS C 26 4.502 -10.689 23.573 1.00 43.07 C -ANISOU 3401 CE1 HIS C 26 5815 5013 5539 447 -761 -268 C -ATOM 3402 NE2 HIS C 26 4.432 -9.915 24.641 1.00 40.10 N -ANISOU 3402 NE2 HIS C 26 5506 4711 5018 233 -695 -70 N -ATOM 3403 N TYR C 27 0.477 -11.904 26.642 1.00 41.44 N -ANISOU 3403 N TYR C 27 6393 4032 5321 -425 -758 485 N -ATOM 3404 CA TYR C 27 -0.352 -11.015 27.456 1.00 41.42 C -ANISOU 3404 CA TYR C 27 6409 4199 5129 -701 -549 609 C -ATOM 3405 C TYR C 27 -1.805 -11.492 27.584 1.00 45.09 C -ANISOU 3405 C TYR C 27 6972 4547 5613 -939 -492 714 C -ATOM 3406 O TYR C 27 -2.657 -10.752 28.065 1.00 44.42 O -ANISOU 3406 O TYR C 27 6853 4640 5386 -1137 -286 760 O -ATOM 3407 CB TYR C 27 -0.341 -9.596 26.869 1.00 33.82 C -ANISOU 3407 CB TYR C 27 5265 3506 4078 -673 -312 442 C -ATOM 3408 CG TYR C 27 0.987 -8.879 26.974 1.00 33.05 C -ANISOU 3408 CG TYR C 27 5067 3598 3893 -551 -332 384 C -ATOM 3409 CD1 TYR C 27 1.794 -9.022 28.100 1.00 32.12 C -ANISOU 3409 CD1 TYR C 27 5021 3509 3674 -582 -459 527 C -ATOM 3410 CD2 TYR C 27 1.429 -8.051 25.947 1.00 33.91 C -ANISOU 3410 CD2 TYR C 27 5002 3883 4000 -442 -238 209 C -ATOM 3411 CE1 TYR C 27 3.012 -8.358 28.200 1.00 34.82 C -ANISOU 3411 CE1 TYR C 27 5249 4057 3925 -500 -487 480 C -ATOM 3412 CE2 TYR C 27 2.634 -7.380 26.034 1.00 31.59 C -ANISOU 3412 CE2 TYR C 27 4600 3795 3608 -383 -261 173 C -ATOM 3413 CZ TYR C 27 3.426 -7.537 27.151 1.00 34.80 C -ANISOU 3413 CZ TYR C 27 5064 4233 3925 -407 -383 299 C -ATOM 3414 OH TYR C 27 4.633 -6.864 27.216 1.00 33.16 O -ANISOU 3414 OH TYR C 27 4726 4261 3611 -373 -415 266 O -ATOM 3415 N ALA C 28 -2.088 -12.720 27.153 1.00 48.66 N -ANISOU 3415 N ALA C 28 7537 4712 6240 -920 -680 737 N -ATOM 3416 CA ALA C 28 -3.474 -13.196 27.062 1.00 51.79 C -ANISOU 3416 CA ALA C 28 7996 5016 6664 -1167 -637 821 C -ATOM 3417 C ALA C 28 -4.257 -13.162 28.385 1.00 52.23 C -ANISOU 3417 C ALA C 28 8139 5176 6531 -1511 -566 1084 C -ATOM 3418 O ALA C 28 -5.475 -12.976 28.380 1.00 57.23 O -ANISOU 3418 O ALA C 28 8710 5932 7104 -1730 -404 1115 O -ATOM 3419 CB ALA C 28 -3.526 -14.600 26.437 1.00 55.14 C -ANISOU 3419 CB ALA C 28 8573 5062 7314 -1109 -903 804 C -ATOM 3420 N GLU C 29 -3.552 -13.345 29.501 1.00 51.35 N -ANISOU 3420 N GLU C 29 8148 5054 6310 -1562 -689 1268 N -ATOM 3421 CA GLU C 29 -4.142 -13.345 30.841 1.00 52.51 C -ANISOU 3421 CA GLU C 29 8381 5346 6223 -1906 -636 1526 C -ATOM 3422 C GLU C 29 -4.091 -11.989 31.550 1.00 49.62 C -ANISOU 3422 C GLU C 29 7888 5360 5604 -1952 -369 1459 C -ATOM 3423 O GLU C 29 -4.767 -11.774 32.560 1.00 49.60 O -ANISOU 3423 O GLU C 29 7902 5576 5370 -2235 -242 1595 O -ATOM 3424 CB GLU C 29 -3.376 -14.330 31.715 1.00 60.47 C -ANISOU 3424 CB GLU C 29 9613 6132 7229 -1960 -956 1791 C -ATOM 3425 CG GLU C 29 -3.223 -15.699 31.114 1.00 67.46 C -ANISOU 3425 CG GLU C 29 10673 6566 8394 -1865 -1281 1845 C -ATOM 3426 CD GLU C 29 -3.950 -16.751 31.918 1.00 74.55 C -ANISOU 3426 CD GLU C 29 11716 7368 9243 -2169 -1432 2109 C -ATOM 3427 OE1 GLU C 29 -3.782 -16.781 33.159 1.00 72.00 O -ANISOU 3427 OE1 GLU C 29 11426 7216 8714 -2330 -1467 2305 O -ATOM 3428 OE2 GLU C 29 -4.695 -17.543 31.303 1.00 80.46 O -ANISOU 3428 OE2 GLU C 29 12500 7931 10142 -2226 -1502 2072 O -ATOM 3429 N ASP C 30 -3.269 -11.089 31.026 1.00 44.22 N -ANISOU 3429 N ASP C 30 7083 4763 4954 -1687 -295 1243 N -ATOM 3430 CA ASP C 30 -2.854 -9.886 31.750 1.00 41.20 C -ANISOU 3430 CA ASP C 30 6641 4657 4355 -1703 -131 1181 C -ATOM 3431 C ASP C 30 -3.671 -8.645 31.399 1.00 39.35 C -ANISOU 3431 C ASP C 30 6248 4636 4067 -1700 173 976 C -ATOM 3432 O ASP C 30 -3.461 -7.565 31.961 1.00 40.26 O -ANISOU 3432 O ASP C 30 6330 4951 4016 -1715 318 886 O -ATOM 3433 CB ASP C 30 -1.371 -9.625 31.458 1.00 40.99 C -ANISOU 3433 CB ASP C 30 6584 4603 4387 -1450 -266 1095 C -ATOM 3434 CG ASP C 30 -0.505 -10.843 31.737 1.00 46.49 C -ANISOU 3434 CG ASP C 30 7410 5075 5178 -1376 -594 1272 C -ATOM 3435 OD1 ASP C 30 -0.758 -11.516 32.757 1.00 46.79 O -ANISOU 3435 OD1 ASP C 30 7607 5063 5108 -1597 -713 1525 O -ATOM 3436 OD2 ASP C 30 0.411 -11.131 30.937 1.00 50.58 O -ANISOU 3436 OD2 ASP C 30 7864 5480 5875 -1096 -739 1159 O -ATOM 3437 N LEU C 31 -4.590 -8.788 30.454 1.00 34.91 N -ANISOU 3437 N LEU C 31 5593 4016 3654 -1673 248 896 N -ATOM 3438 CA LEU C 31 -5.370 -7.645 30.004 1.00 39.30 C -ANISOU 3438 CA LEU C 31 5986 4742 4202 -1626 496 710 C -ATOM 3439 C LEU C 31 -6.837 -7.927 30.252 1.00 41.74 C -ANISOU 3439 C LEU C 31 6229 5165 4465 -1833 628 772 C -ATOM 3440 O LEU C 31 -7.283 -9.062 30.107 1.00 42.89 O -ANISOU 3440 O LEU C 31 6430 5184 4681 -1969 504 917 O -ATOM 3441 CB LEU C 31 -5.130 -7.381 28.517 1.00 29.78 C -ANISOU 3441 CB LEU C 31 4675 3435 3204 -1394 469 548 C -ATOM 3442 CG LEU C 31 -3.694 -7.114 28.086 1.00 30.91 C -ANISOU 3442 CG LEU C 31 4828 3528 3388 -1198 350 473 C -ATOM 3443 CD1 LEU C 31 -3.587 -6.927 26.578 1.00 29.88 C -ANISOU 3443 CD1 LEU C 31 4576 3357 3419 -1020 338 324 C -ATOM 3444 CD2 LEU C 31 -3.192 -5.872 28.807 1.00 34.22 C -ANISOU 3444 CD2 LEU C 31 5248 4111 3642 -1210 459 417 C -ATOM 3445 N GLU C 32 -7.596 -6.908 30.635 1.00 39.78 N -ANISOU 3445 N GLU C 32 5857 5159 4098 -1860 869 655 N -ATOM 3446 CA AGLU C 32 -9.012 -7.145 30.834 0.54 43.74 C -ANISOU 3446 CA AGLU C 32 6233 5839 4548 -2044 1011 695 C -ATOM 3447 CA BGLU C 32 -9.028 -7.051 30.860 0.46 43.91 C -ANISOU 3447 CA BGLU C 32 6247 5876 4562 -2037 1027 682 C -ATOM 3448 C GLU C 32 -9.788 -6.892 29.545 1.00 43.29 C -ANISOU 3448 C GLU C 32 5997 5752 4698 -1905 1064 572 C -ATOM 3449 O GLU C 32 -10.637 -7.708 29.185 1.00 43.57 O -ANISOU 3449 O GLU C 32 5973 5784 4796 -2052 1028 667 O -ATOM 3450 CB AGLU C 32 -9.575 -6.367 32.031 0.54 47.32 C -ANISOU 3450 CB AGLU C 32 6615 6624 4741 -2160 1246 629 C -ATOM 3451 CB BGLU C 32 -9.500 -5.992 31.860 0.46 46.35 C -ANISOU 3451 CB BGLU C 32 6468 6495 4648 -2075 1276 556 C -ATOM 3452 CG AGLU C 32 -10.680 -7.114 32.818 0.54 51.58 C -ANISOU 3452 CG AGLU C 32 7069 7378 5153 -2401 1278 762 C -ATOM 3453 CG BGLU C 32 -10.880 -6.248 32.447 0.46 51.70 C -ANISOU 3453 CG BGLU C 32 6981 7458 5206 -2261 1421 590 C -ATOM 3454 CD AGLU C 32 -10.187 -8.347 33.594 0.54 50.54 C -ANISOU 3454 CD AGLU C 32 7129 7137 4937 -2605 1042 1025 C -ATOM 3455 CD BGLU C 32 -11.876 -5.143 32.137 0.46 56.41 C -ANISOU 3455 CD BGLU C 32 7331 8267 5836 -2105 1667 351 C -ATOM 3456 OE1AGLU C 32 -9.649 -9.292 32.980 0.54 47.38 O -ANISOU 3456 OE1AGLU C 32 6874 6430 4697 -2620 814 1173 O -ATOM 3457 OE1BGLU C 32 -11.487 -3.957 32.157 0.46 58.29 O -ANISOU 3457 OE1BGLU C 32 7574 8506 6067 -1906 1775 139 O -ATOM 3458 OE2AGLU C 32 -10.357 -8.376 34.829 0.54 52.59 O -ANISOU 3458 OE2AGLU C 32 7393 7615 4973 -2746 1075 1074 O -ATOM 3459 OE2BGLU C 32 -13.053 -5.468 31.872 0.46 59.78 O -ANISOU 3459 OE2BGLU C 32 7560 8840 6314 -2161 1721 372 O -ATOM 3460 N ARG C 33 -9.470 -5.808 28.832 1.00 38.05 N -ANISOU 3460 N ARG C 33 5263 5060 4135 -1652 1118 385 N -ATOM 3461 CA ARG C 33 -10.181 -5.431 27.617 1.00 37.00 C -ANISOU 3461 CA ARG C 33 4958 4920 4180 -1518 1154 284 C -ATOM 3462 C ARG C 33 -9.305 -4.586 26.716 1.00 34.39 C -ANISOU 3462 C ARG C 33 4644 4461 3961 -1280 1094 163 C -ATOM 3463 O ARG C 33 -8.367 -3.937 27.182 1.00 31.78 O -ANISOU 3463 O ARG C 33 4415 4107 3555 -1213 1092 115 O -ATOM 3464 CB ARG C 33 -11.407 -4.579 27.958 1.00 46.03 C -ANISOU 3464 CB ARG C 33 5897 6319 5273 -1503 1379 177 C -ATOM 3465 CG ARG C 33 -12.449 -5.243 28.834 1.00 60.35 C -ANISOU 3465 CG ARG C 33 7618 8375 6936 -1764 1487 279 C -ATOM 3466 CD ARG C 33 -13.235 -6.306 28.084 1.00 66.93 C -ANISOU 3466 CD ARG C 33 8366 9184 7879 -1920 1393 408 C -ATOM 3467 NE ARG C 33 -14.445 -5.747 27.492 1.00 73.47 N -ANISOU 3467 NE ARG C 33 8910 10211 8794 -1838 1520 307 N -ATOM 3468 CZ ARG C 33 -15.454 -6.474 27.028 1.00 77.63 C -ANISOU 3468 CZ ARG C 33 9284 10842 9370 -2012 1495 398 C -ATOM 3469 NH1 ARG C 33 -15.396 -7.798 27.081 1.00 78.60 N -ANISOU 3469 NH1 ARG C 33 9547 10845 9471 -2291 1340 590 N -ATOM 3470 NH2 ARG C 33 -16.521 -5.877 26.512 1.00 79.10 N -ANISOU 3470 NH2 ARG C 33 9182 11241 9634 -1910 1603 303 N -ATOM 3471 N VAL C 34 -9.632 -4.556 25.427 1.00 32.21 N -ANISOU 3471 N VAL C 34 4263 4130 3844 -1183 1043 123 N -ATOM 3472 CA VAL C 34 -9.056 -3.541 24.550 1.00 28.12 C -ANISOU 3472 CA VAL C 34 3722 3558 3405 -995 1014 24 C -ATOM 3473 C VAL C 34 -9.832 -2.250 24.830 1.00 29.40 C -ANISOU 3473 C VAL C 34 3778 3823 3571 -901 1168 -76 C -ATOM 3474 O VAL C 34 -11.060 -2.257 24.861 1.00 32.67 O -ANISOU 3474 O VAL C 34 4032 4364 4017 -917 1265 -88 O -ATOM 3475 CB VAL C 34 -9.143 -3.932 23.068 1.00 31.84 C -ANISOU 3475 CB VAL C 34 4117 3972 4009 -944 898 20 C -ATOM 3476 CG1 VAL C 34 -8.674 -2.779 22.183 1.00 32.33 C -ANISOU 3476 CG1 VAL C 34 4142 4026 4118 -798 873 -45 C -ATOM 3477 CG2 VAL C 34 -8.311 -5.169 22.804 1.00 34.55 C -ANISOU 3477 CG2 VAL C 34 4574 4192 4361 -984 741 59 C -ATOM 3478 N PHE C 35 -9.124 -1.152 25.069 1.00 30.75 N -ANISOU 3478 N PHE C 35 4033 3940 3711 -801 1180 -155 N -ATOM 3479 CA PHE C 35 -9.780 0.083 25.498 1.00 31.57 C -ANISOU 3479 CA PHE C 35 4082 4087 3827 -686 1307 -284 C -ATOM 3480 C PHE C 35 -9.838 1.065 24.323 1.00 33.36 C -ANISOU 3480 C PHE C 35 4258 4201 4216 -528 1225 -312 C -ATOM 3481 O PHE C 35 -10.870 1.684 24.053 1.00 34.59 O -ANISOU 3481 O PHE C 35 4273 4386 4482 -401 1276 -371 O -ATOM 3482 CB PHE C 35 -9.019 0.683 26.681 1.00 35.32 C -ANISOU 3482 CB PHE C 35 4722 4550 4149 -712 1359 -366 C -ATOM 3483 CG PHE C 35 -9.814 1.678 27.478 1.00 39.94 C -ANISOU 3483 CG PHE C 35 5262 5212 4703 -612 1522 -546 C -ATOM 3484 CD1 PHE C 35 -10.977 1.296 28.124 1.00 43.76 C -ANISOU 3484 CD1 PHE C 35 5586 5921 5120 -649 1688 -591 C -ATOM 3485 CD2 PHE C 35 -9.383 2.992 27.594 1.00 42.45 C -ANISOU 3485 CD2 PHE C 35 5695 5384 5050 -489 1504 -685 C -ATOM 3486 CE1 PHE C 35 -11.711 2.212 28.862 1.00 48.32 C -ANISOU 3486 CE1 PHE C 35 6090 6612 5659 -522 1855 -806 C -ATOM 3487 CE2 PHE C 35 -10.105 3.914 28.330 1.00 46.12 C -ANISOU 3487 CE2 PHE C 35 6131 5892 5501 -357 1644 -902 C -ATOM 3488 CZ PHE C 35 -11.274 3.524 28.965 1.00 47.20 C -ANISOU 3488 CZ PHE C 35 6078 6288 5569 -352 1831 -981 C -ATOM 3489 N ILE C 36 -8.721 1.197 23.619 1.00 28.56 N -ANISOU 3489 N ILE C 36 3752 3486 3615 -541 1085 -256 N -ATOM 3490 CA ILE C 36 -8.670 2.001 22.407 1.00 28.88 C -ANISOU 3490 CA ILE C 36 3757 3443 3772 -456 974 -226 C -ATOM 3491 C ILE C 36 -7.909 1.219 21.353 1.00 29.20 C -ANISOU 3491 C ILE C 36 3785 3515 3793 -534 848 -134 C -ATOM 3492 O ILE C 36 -6.686 1.107 21.426 1.00 25.96 O -ANISOU 3492 O ILE C 36 3475 3099 3291 -595 788 -119 O -ATOM 3493 CB ILE C 36 -7.966 3.362 22.640 1.00 26.04 C -ANISOU 3493 CB ILE C 36 3548 2938 3407 -414 928 -274 C -ATOM 3494 CG1 ILE C 36 -8.412 3.999 23.951 1.00 29.29 C -ANISOU 3494 CG1 ILE C 36 4022 3321 3786 -345 1062 -428 C -ATOM 3495 CG2 ILE C 36 -8.202 4.315 21.463 1.00 32.18 C -ANISOU 3495 CG2 ILE C 36 4294 3611 4323 -335 801 -213 C -ATOM 3496 CD1 ILE C 36 -7.712 5.315 24.288 1.00 31.32 C -ANISOU 3496 CD1 ILE C 36 4471 3393 4037 -323 1000 -505 C -ATOM 3497 N PRO C 37 -8.634 0.646 20.377 1.00 25.76 N -ANISOU 3497 N PRO C 37 3211 3144 3433 -531 809 -91 N -ATOM 3498 CA PRO C 37 -8.015 -0.087 19.267 1.00 25.19 C -ANISOU 3498 CA PRO C 37 3113 3126 3333 -588 696 -52 C -ATOM 3499 C PRO C 37 -6.953 0.747 18.557 1.00 27.29 C -ANISOU 3499 C PRO C 37 3427 3395 3545 -600 598 -17 C -ATOM 3500 O PRO C 37 -7.135 1.960 18.378 1.00 26.06 O -ANISOU 3500 O PRO C 37 3292 3172 3438 -566 567 22 O -ATOM 3501 CB PRO C 37 -9.204 -0.335 18.334 1.00 24.02 C -ANISOU 3501 CB PRO C 37 2804 3045 3278 -578 669 -21 C -ATOM 3502 CG PRO C 37 -10.366 -0.467 19.278 1.00 29.92 C -ANISOU 3502 CG PRO C 37 3483 3809 4078 -560 793 -45 C -ATOM 3503 CD PRO C 37 -10.109 0.600 20.313 1.00 26.67 C -ANISOU 3503 CD PRO C 37 3165 3320 3647 -481 874 -97 C -ATOM 3504 N HIS C 38 -5.859 0.102 18.160 1.00 24.69 N -ANISOU 3504 N HIS C 38 2727 3031 3624 -648 -266 159 N -ATOM 3505 CA HIS C 38 -4.760 0.770 17.454 1.00 23.67 C -ANISOU 3505 CA HIS C 38 2575 2761 3656 -496 -73 36 C -ATOM 3506 C HIS C 38 -5.257 1.623 16.298 1.00 24.12 C -ANISOU 3506 C HIS C 38 2770 2866 3528 -396 143 -110 C -ATOM 3507 O HIS C 38 -4.851 2.775 16.140 1.00 23.47 O -ANISOU 3507 O HIS C 38 2696 2811 3410 -341 286 -169 O -ATOM 3508 CB HIS C 38 -3.761 -0.269 16.926 1.00 25.85 C -ANISOU 3508 CB HIS C 38 2784 2737 4301 -416 -65 7 C -ATOM 3509 CG HIS C 38 -2.626 0.325 16.147 1.00 28.07 C -ANISOU 3509 CG HIS C 38 3014 2889 4763 -291 184 -150 C -ATOM 3510 ND1 HIS C 38 -2.575 0.294 14.769 1.00 29.11 N -ANISOU 3510 ND1 HIS C 38 3275 2917 4867 -223 444 -355 N -ATOM 3511 CD2 HIS C 38 -1.512 0.978 16.552 1.00 27.48 C -ANISOU 3511 CD2 HIS C 38 2778 2797 4868 -270 220 -135 C -ATOM 3512 CE1 HIS C 38 -1.469 0.891 14.361 1.00 29.32 C -ANISOU 3512 CE1 HIS C 38 3219 2867 5055 -163 657 -467 C -ATOM 3513 NE2 HIS C 38 -0.806 1.316 15.420 1.00 30.21 N -ANISOU 3513 NE2 HIS C 38 3138 3024 5317 -177 521 -334 N -ATOM 3514 N GLY C 39 -6.146 1.056 15.486 1.00 23.57 N -ANISOU 3514 N GLY C 39 2820 2800 3337 -405 137 -143 N -ATOM 3515 CA GLY C 39 -6.601 1.760 14.304 1.00 27.30 C -ANISOU 3515 CA GLY C 39 3438 3311 3622 -354 274 -225 C -ATOM 3516 C GLY C 39 -7.369 3.033 14.624 1.00 23.77 C -ANISOU 3516 C GLY C 39 2968 3045 3018 -317 270 -172 C -ATOM 3517 O GLY C 39 -7.311 4.014 13.873 1.00 25.10 O -ANISOU 3517 O GLY C 39 3225 3194 3116 -251 381 -195 O -ATOM 3518 N LEU C 40 -8.101 3.019 15.728 1.00 26.12 N -ANISOU 3518 N LEU C 40 3149 3500 3276 -375 157 -106 N -ATOM 3519 CA LEU C 40 -8.814 4.208 16.188 1.00 29.51 C -ANISOU 3519 CA LEU C 40 3509 4066 3635 -329 204 -112 C -ATOM 3520 C LEU C 40 -7.828 5.303 16.588 1.00 26.72 C -ANISOU 3520 C LEU C 40 3150 3639 3363 -283 342 -174 C -ATOM 3521 O LEU C 40 -8.055 6.493 16.325 1.00 24.16 O -ANISOU 3521 O LEU C 40 2849 3288 3042 -187 445 -208 O -ATOM 3522 CB LEU C 40 -9.729 3.861 17.367 1.00 30.41 C -ANISOU 3522 CB LEU C 40 3491 4381 3681 -456 119 -84 C -ATOM 3523 CG LEU C 40 -10.489 5.066 17.927 1.00 33.64 C -ANISOU 3523 CG LEU C 40 3791 4912 4078 -407 237 -161 C -ATOM 3524 CD1 LEU C 40 -11.244 5.783 16.799 1.00 35.35 C -ANISOU 3524 CD1 LEU C 40 4008 5080 4342 -226 249 -137 C -ATOM 3525 CD2 LEU C 40 -11.429 4.660 19.044 1.00 38.62 C -ANISOU 3525 CD2 LEU C 40 4285 5774 4616 -582 216 -178 C -ATOM 3526 N ILE C 41 -6.735 4.895 17.229 1.00 18.85 N -ANISOU 3526 N ILE C 41 2113 2589 2461 -364 320 -171 N -ATOM 3527 CA ILE C 41 -5.648 5.820 17.554 1.00 22.03 C -ANISOU 3527 CA ILE C 41 2501 2922 2948 -364 428 -224 C -ATOM 3528 C ILE C 41 -5.084 6.444 16.283 1.00 22.34 C -ANISOU 3528 C ILE C 41 2648 2806 3035 -249 586 -272 C -ATOM 3529 O ILE C 41 -4.794 7.644 16.239 1.00 23.14 O -ANISOU 3529 O ILE C 41 2791 2859 3142 -221 708 -317 O -ATOM 3530 CB ILE C 41 -4.517 5.103 18.323 1.00 21.02 C -ANISOU 3530 CB ILE C 41 2268 2758 2960 -480 311 -162 C -ATOM 3531 CG1 ILE C 41 -5.023 4.623 19.677 1.00 23.31 C -ANISOU 3531 CG1 ILE C 41 2497 3227 3133 -676 133 -75 C -ATOM 3532 CG2 ILE C 41 -3.319 6.028 18.520 1.00 21.91 C -ANISOU 3532 CG2 ILE C 41 2343 2806 3176 -502 410 -212 C -ATOM 3533 CD1 ILE C 41 -3.967 3.912 20.529 1.00 27.23 C -ANISOU 3533 CD1 ILE C 41 2888 3692 3768 -829 -76 69 C -ATOM 3534 N MET C 42 -4.900 5.619 15.252 1.00 20.54 N -ANISOU 3534 N MET C 42 2485 2489 2829 -220 601 -275 N -ATOM 3535 CA MET C 42 -4.381 6.103 13.990 1.00 24.52 C -ANISOU 3535 CA MET C 42 3127 2880 3311 -185 774 -329 C -ATOM 3536 C MET C 42 -5.311 7.138 13.374 1.00 23.77 C -ANISOU 3536 C MET C 42 3168 2817 3048 -138 778 -269 C -ATOM 3537 O MET C 42 -4.860 8.190 12.895 1.00 23.81 O -ANISOU 3537 O MET C 42 3268 2737 3041 -131 900 -266 O -ATOM 3538 CB MET C 42 -4.143 4.937 13.022 1.00 26.44 C -ANISOU 3538 CB MET C 42 3438 3038 3569 -213 823 -396 C -ATOM 3539 CG MET C 42 -3.082 3.957 13.479 1.00 28.26 C -ANISOU 3539 CG MET C 42 3499 3148 4089 -215 835 -453 C -ATOM 3540 SD MET C 42 -1.470 4.728 13.708 1.00 35.42 S -ANISOU 3540 SD MET C 42 4256 3967 5235 -211 1007 -513 S -ATOM 3541 CE MET C 42 -1.541 5.070 15.468 1.00 46.73 C -ANISOU 3541 CE MET C 42 5521 5523 6710 -258 759 -368 C -ATOM 3542 N ASP C 43 -6.604 6.844 13.386 1.00 22.90 N -ANISOU 3542 N ASP C 43 3047 2814 2839 -115 627 -198 N -ATOM 3543 CA ASP C 43 -7.576 7.743 12.779 1.00 24.57 C -ANISOU 3543 CA ASP C 43 3330 3038 2968 -49 570 -95 C -ATOM 3544 C ASP C 43 -7.596 9.085 13.499 1.00 23.14 C -ANISOU 3544 C ASP C 43 3079 2798 2916 40 640 -106 C -ATOM 3545 O ASP C 43 -7.666 10.138 12.860 1.00 24.25 O -ANISOU 3545 O ASP C 43 3323 2818 3074 96 665 -28 O -ATOM 3546 CB ASP C 43 -8.977 7.146 12.842 1.00 24.51 C -ANISOU 3546 CB ASP C 43 3236 3178 2900 -42 383 -20 C -ATOM 3547 CG ASP C 43 -9.168 5.972 11.881 1.00 31.81 C -ANISOU 3547 CG ASP C 43 4287 4136 3662 -160 298 -4 C -ATOM 3548 OD1 ASP C 43 -8.472 5.895 10.837 1.00 29.41 O -ANISOU 3548 OD1 ASP C 43 4181 3744 3249 -238 393 -36 O -ATOM 3549 OD2 ASP C 43 -10.037 5.133 12.177 1.00 32.79 O -ANISOU 3549 OD2 ASP C 43 4322 4380 3755 -207 159 19 O -ATOM 3550 N ARG C 44 -7.571 9.046 14.825 1.00 22.46 N -ANISOU 3550 N ARG C 44 2839 2785 2910 23 666 -201 N -ATOM 3551 CA ARG C 44 -7.611 10.272 15.618 1.00 22.99 C -ANISOU 3551 CA ARG C 44 2852 2791 3090 66 775 -281 C -ATOM 3552 C ARG C 44 -6.316 11.042 15.393 1.00 25.06 C -ANISOU 3552 C ARG C 44 3231 2893 3399 25 910 -317 C -ATOM 3553 O ARG C 44 -6.312 12.269 15.275 1.00 27.16 O -ANISOU 3553 O ARG C 44 3562 3002 3757 82 997 -325 O -ATOM 3554 CB ARG C 44 -7.798 9.936 17.107 1.00 23.44 C -ANISOU 3554 CB ARG C 44 2762 3010 3135 -41 789 -400 C -ATOM 3555 CG ARG C 44 -7.812 11.149 18.057 1.00 25.43 C -ANISOU 3555 CG ARG C 44 2980 3212 3470 -59 955 -562 C -ATOM 3556 CD ARG C 44 -8.782 12.244 17.595 1.00 26.00 C -ANISOU 3556 CD ARG C 44 3025 3133 3722 143 1022 -569 C -ATOM 3557 NE ARG C 44 -8.790 13.380 18.520 1.00 27.18 N -ANISOU 3557 NE ARG C 44 3148 3183 3998 126 1229 -783 N -ATOM 3558 CZ ARG C 44 -9.108 14.621 18.169 1.00 28.96 C -ANISOU 3558 CZ ARG C 44 3391 3146 4465 295 1327 -810 C -ATOM 3559 NH1 ARG C 44 -9.463 14.877 16.915 1.00 27.78 N -ANISOU 3559 NH1 ARG C 44 3287 2839 4430 478 1187 -581 N -ATOM 3560 NH2 ARG C 44 -9.075 15.597 19.065 1.00 29.15 N -ANISOU 3560 NH2 ARG C 44 3405 3053 4618 256 1551 -1059 N -ATOM 3561 N THR C 45 -5.210 10.309 15.322 1.00 22.89 N -ANISOU 3561 N THR C 45 2962 2634 3102 -77 928 -336 N -ATOM 3562 CA THR C 45 -3.895 10.932 15.144 1.00 25.73 C -ANISOU 3562 CA THR C 45 3376 2872 3527 -148 1066 -379 C -ATOM 3563 C THR C 45 -3.780 11.608 13.768 1.00 26.40 C -ANISOU 3563 C THR C 45 3655 2815 3561 -122 1151 -300 C -ATOM 3564 O THR C 45 -3.159 12.669 13.639 1.00 24.62 O -ANISOU 3564 O THR C 45 3514 2455 3387 -167 1269 -309 O -ATOM 3565 CB THR C 45 -2.754 9.908 15.363 1.00 23.48 C -ANISOU 3565 CB THR C 45 2976 2629 3316 -242 1059 -412 C -ATOM 3566 OG1 THR C 45 -2.838 9.386 16.696 1.00 20.70 O -ANISOU 3566 OG1 THR C 45 2475 2404 2987 -317 925 -421 O -ATOM 3567 CG2 THR C 45 -1.380 10.551 15.160 1.00 26.41 C -ANISOU 3567 CG2 THR C 45 3344 2898 3795 -328 1214 -462 C -ATOM 3568 N GLU C 46 -4.379 10.998 12.745 1.00 23.42 N -ANISOU 3568 N GLU C 46 3372 2472 3053 -98 1078 -211 N -ATOM 3569 CA GLU C 46 -4.436 11.617 11.428 1.00 24.52 C -ANISOU 3569 CA GLU C 46 3736 2513 3066 -138 1107 -90 C -ATOM 3570 C GLU C 46 -5.057 13.006 11.505 1.00 25.98 C -ANISOU 3570 C GLU C 46 3978 2551 3344 -45 1053 27 C -ATOM 3571 O GLU C 46 -4.552 13.959 10.912 1.00 25.66 O -ANISOU 3571 O GLU C 46 4104 2352 3295 -112 1131 105 O -ATOM 3572 CB GLU C 46 -5.238 10.749 10.441 1.00 22.65 C -ANISOU 3572 CB GLU C 46 3602 2375 2631 -169 977 0 C -ATOM 3573 CG GLU C 46 -5.344 11.384 9.059 1.00 29.61 C -ANISOU 3573 CG GLU C 46 4755 3189 3307 -284 959 169 C -ATOM 3574 CD GLU C 46 -6.163 10.540 8.086 1.00 34.78 C -ANISOU 3574 CD GLU C 46 5537 3969 3708 -383 800 258 C -ATOM 3575 OE1 GLU C 46 -6.843 9.603 8.531 1.00 45.60 O -ANISOU 3575 OE1 GLU C 46 6764 5455 5107 -320 683 208 O -ATOM 3576 OE2 GLU C 46 -6.110 10.817 6.879 1.00 35.50 O -ANISOU 3576 OE2 GLU C 46 5892 4053 3544 -570 790 381 O -ATOM 3577 N ARG C 47 -6.144 13.118 12.258 1.00 23.29 N -ANISOU 3577 N ARG C 47 3484 2240 3125 102 937 29 N -ATOM 3578 CA ARG C 47 -6.836 14.394 12.396 1.00 25.20 C -ANISOU 3578 CA ARG C 47 3721 2292 3561 237 903 106 C -ATOM 3579 C ARG C 47 -6.022 15.368 13.253 1.00 29.90 C -ANISOU 3579 C ARG C 47 4318 2731 4311 204 1096 -55 C -ATOM 3580 O ARG C 47 -5.988 16.563 12.965 1.00 30.32 O -ANISOU 3580 O ARG C 47 4486 2531 4505 241 1128 20 O -ATOM 3581 CB ARG C 47 -8.232 14.173 12.991 1.00 26.33 C -ANISOU 3581 CB ARG C 47 3642 2525 3838 399 783 96 C -ATOM 3582 CG ARG C 47 -8.956 15.467 13.360 1.00 27.98 C -ANISOU 3582 CG ARG C 47 3762 2500 4370 581 805 100 C -ATOM 3583 CD ARG C 47 -8.963 16.448 12.210 1.00 50.43 C -ANISOU 3583 CD ARG C 47 6793 5075 7291 624 688 369 C -ATOM 3584 NE ARG C 47 -10.313 16.691 11.731 1.00 57.42 N -ANISOU 3584 NE ARG C 47 7543 5893 8380 809 445 592 N -ATOM 3585 CZ ARG C 47 -11.032 17.767 12.012 1.00 50.59 C -ANISOU 3585 CZ ARG C 47 6533 4751 7937 1030 432 624 C -ATOM 3586 NH1 ARG C 47 -10.532 18.741 12.756 1.00 57.85 N -ANISOU 3586 NH1 ARG C 47 7477 5418 9085 1071 672 419 N -ATOM 3587 NH2 ARG C 47 -12.255 17.868 11.527 1.00 52.69 N -ANISOU 3587 NH2 ARG C 47 6616 4975 8429 1203 169 860 N -ATOM 3588 N LEU C 48 -5.341 14.869 14.284 1.00 26.83 N -ANISOU 3588 N LEU C 48 3819 2479 3896 104 1198 -254 N -ATOM 3589 CA LEU C 48 -4.501 15.762 15.104 1.00 30.48 C -ANISOU 3589 CA LEU C 48 4297 2824 4459 3 1360 -411 C -ATOM 3590 C LEU C 48 -3.348 16.358 14.298 1.00 28.59 C -ANISOU 3590 C LEU C 48 4233 2434 4195 -123 1455 -341 C -ATOM 3591 O LEU C 48 -2.953 17.503 14.513 1.00 30.72 O -ANISOU 3591 O LEU C 48 4593 2495 4583 -177 1562 -389 O -ATOM 3592 CB LEU C 48 -3.943 15.046 16.334 1.00 30.66 C -ANISOU 3592 CB LEU C 48 4172 3058 4418 -142 1382 -581 C -ATOM 3593 CG LEU C 48 -4.897 14.690 17.474 1.00 33.68 C -ANISOU 3593 CG LEU C 48 4408 3599 4790 -126 1353 -705 C -ATOM 3594 CD1 LEU C 48 -4.134 14.020 18.609 1.00 29.70 C -ANISOU 3594 CD1 LEU C 48 3814 3299 4170 -353 1325 -802 C -ATOM 3595 CD2 LEU C 48 -5.660 15.909 17.991 1.00 33.44 C -ANISOU 3595 CD2 LEU C 48 4381 3395 4928 -44 1492 -853 C -ATOM 3596 N ALA C 49 -2.787 15.576 13.391 1.00 27.05 N -ANISOU 3596 N ALA C 49 4086 2339 3852 -200 1448 -256 N -ATOM 3597 CA ALA C 49 -1.695 16.069 12.555 1.00 25.92 C -ANISOU 3597 CA ALA C 49 4097 2092 3660 -362 1586 -207 C -ATOM 3598 C ALA C 49 -2.177 17.263 11.744 1.00 29.35 C -ANISOU 3598 C ALA C 49 4764 2276 4110 -340 1553 -17 C -ATOM 3599 O ALA C 49 -1.449 18.243 11.557 1.00 30.16 O -ANISOU 3599 O ALA C 49 5001 2197 4260 -472 1670 4 O -ATOM 3600 CB ALA C 49 -1.193 14.979 11.643 1.00 25.49 C -ANISOU 3600 CB ALA C 49 4053 2185 3446 -449 1632 -193 C -ATOM 3601 N ARG C 50 -3.415 17.186 11.263 1.00 29.54 N -ANISOU 3601 N ARG C 50 4827 2281 4118 -186 1364 151 N -ATOM 3602 CA ARG C 50 -3.972 18.295 10.486 1.00 31.91 C -ANISOU 3602 CA ARG C 50 5322 2313 4488 -147 1251 405 C -ATOM 3603 C ARG C 50 -4.191 19.523 11.376 1.00 33.39 C -ANISOU 3603 C ARG C 50 5466 2210 5011 -25 1304 323 C -ATOM 3604 O ARG C 50 -3.896 20.657 10.978 1.00 36.03 O -ANISOU 3604 O ARG C 50 5991 2246 5454 -88 1327 451 O -ATOM 3605 CB ARG C 50 -5.280 17.869 9.805 1.00 34.31 C -ANISOU 3605 CB ARG C 50 5620 2681 4736 -15 981 630 C -ATOM 3606 CG ARG C 50 -5.647 18.740 8.594 1.00 45.23 C -ANISOU 3606 CG ARG C 50 7257 3845 6084 -72 788 1001 C -ATOM 3607 CD ARG C 50 -6.891 18.216 7.894 1.00 53.49 C -ANISOU 3607 CD ARG C 50 8275 5005 7045 7 469 1249 C -ATOM 3608 NE ARG C 50 -8.115 18.557 8.616 1.00 56.55 N -ANISOU 3608 NE ARG C 50 8383 5272 7830 325 315 1268 N -ATOM 3609 CZ ARG C 50 -9.304 17.999 8.397 1.00 58.28 C -ANISOU 3609 CZ ARG C 50 8437 5629 8078 445 57 1406 C -ATOM 3610 NH1 ARG C 50 -9.441 17.051 7.482 1.00 55.03 N -ANISOU 3610 NH1 ARG C 50 8151 5477 7281 254 -98 1538 N -ATOM 3611 NH2 ARG C 50 -10.357 18.386 9.101 1.00 60.65 N -ANISOU 3611 NH2 ARG C 50 8434 5809 8802 735 -24 1385 N -ATOM 3612 N ASP C 51 -4.699 19.293 12.586 1.00 35.03 N -ANISOU 3612 N ASP C 51 5442 2493 5375 115 1343 93 N -ATOM 3613 CA ASP C 51 -4.912 20.394 13.538 1.00 40.75 C -ANISOU 3613 CA ASP C 51 6123 2952 6409 200 1463 -82 C -ATOM 3614 C ASP C 51 -3.582 21.076 13.897 1.00 34.39 C -ANISOU 3614 C ASP C 51 5450 2031 5585 -38 1660 -224 C -ATOM 3615 O ASP C 51 -3.505 22.298 13.989 1.00 37.13 O -ANISOU 3615 O ASP C 51 5922 2027 6159 -41 1738 -239 O -ATOM 3616 CB ASP C 51 -5.575 19.888 14.825 1.00 40.02 C -ANISOU 3616 CB ASP C 51 5778 3042 6387 294 1528 -358 C -ATOM 3617 CG ASP C 51 -6.979 19.322 14.607 1.00 43.09 C -ANISOU 3617 CG ASP C 51 5986 3533 6852 521 1358 -248 C -ATOM 3618 OD1 ASP C 51 -7.612 19.606 13.568 1.00 41.54 O -ANISOU 3618 OD1 ASP C 51 5843 3188 6755 653 1164 44 O -ATOM 3619 OD2 ASP C 51 -7.459 18.606 15.516 1.00 41.69 O -ANISOU 3619 OD2 ASP C 51 5609 3598 6634 535 1403 -441 O -ATOM 3620 N VAL C 52 -2.542 20.273 14.112 1.00 34.16 N -ANISOU 3620 N VAL C 52 5371 2280 5329 -238 1730 -326 N -ATOM 3621 CA VAL C 52 -1.201 20.796 14.414 1.00 37.38 C -ANISOU 3621 CA VAL C 52 5848 2636 5718 -497 1890 -441 C -ATOM 3622 C VAL C 52 -0.681 21.666 13.284 1.00 37.61 C -ANISOU 3622 C VAL C 52 6128 2415 5748 -615 1926 -230 C -ATOM 3623 O VAL C 52 -0.171 22.766 13.510 1.00 41.85 O -ANISOU 3623 O VAL C 52 6766 2741 6393 -733 2009 -280 O -ATOM 3624 CB VAL C 52 -0.181 19.650 14.658 1.00 34.29 C -ANISOU 3624 CB VAL C 52 5292 2586 5149 -662 1913 -524 C -ATOM 3625 CG1 VAL C 52 1.240 20.212 14.766 1.00 34.95 C -ANISOU 3625 CG1 VAL C 52 5406 2623 5248 -941 2055 -595 C -ATOM 3626 CG2 VAL C 52 -0.540 18.868 15.903 1.00 32.41 C -ANISOU 3626 CG2 VAL C 52 4841 2582 4893 -626 1850 -699 C -ATOM 3627 N MET C 53 -0.811 21.175 12.058 1.00 37.03 N -ANISOU 3627 N MET C 53 6152 2422 5497 -615 1838 8 N -ATOM 3628 CA MET C 53 -0.335 21.934 10.905 1.00 41.41 C -ANISOU 3628 CA MET C 53 6983 2781 5971 -797 1865 243 C -ATOM 3629 C MET C 53 -1.132 23.208 10.675 1.00 40.99 C -ANISOU 3629 C MET C 53 7098 2328 6149 -672 1726 442 C -ATOM 3630 O MET C 53 -0.567 24.241 10.328 1.00 43.78 O -ANISOU 3630 O MET C 53 7592 2514 6527 -820 1728 528 O -ATOM 3631 CB MET C 53 -0.333 21.066 9.649 1.00 43.15 C -ANISOU 3631 CB MET C 53 7296 3219 5879 -887 1814 426 C -ATOM 3632 CG MET C 53 0.865 20.133 9.539 1.00 45.05 C -ANISOU 3632 CG MET C 53 7417 3755 5946 -1088 2027 242 C -ATOM 3633 SD MET C 53 2.389 20.964 9.019 1.00 77.05 S -ANISOU 3633 SD MET C 53 11547 7808 9921 -1400 2211 208 S -ATOM 3634 CE MET C 53 3.173 21.248 10.597 1.00 63.11 C -ANISOU 3634 CE MET C 53 9512 6052 8416 -1395 2293 -74 C -ATOM 3635 N LYS C 54 -2.444 23.138 10.865 1.00 43.84 N -ANISOU 3635 N LYS C 54 7369 2588 6700 -378 1559 509 N -ATOM 3636 CA LYS C 54 -3.293 24.324 10.755 1.00 49.07 C -ANISOU 3636 CA LYS C 54 8091 2851 7701 -192 1398 678 C -ATOM 3637 C LYS C 54 -2.844 25.412 11.733 1.00 49.03 C -ANISOU 3637 C LYS C 54 8038 2670 7923 -220 1532 407 C -ATOM 3638 O LYS C 54 -2.911 26.609 11.438 1.00 50.41 O -ANISOU 3638 O LYS C 54 8341 2513 8300 -216 1434 543 O -ATOM 3639 CB LYS C 54 -4.758 23.951 11.008 1.00 55.65 C -ANISOU 3639 CB LYS C 54 8720 3650 8775 154 1242 718 C -ATOM 3640 CG LYS C 54 -5.761 25.053 10.670 1.00 67.91 C -ANISOU 3640 CG LYS C 54 10262 4827 10712 379 991 952 C -ATOM 3641 CD LYS C 54 -7.201 24.542 10.723 1.00 77.52 C -ANISOU 3641 CD LYS C 54 11214 6089 12151 703 802 1037 C -ATOM 3642 CE LYS C 54 -7.763 24.533 12.144 1.00 82.35 C -ANISOU 3642 CE LYS C 54 11499 6770 13020 904 1002 590 C -ATOM 3643 NZ LYS C 54 -9.052 23.773 12.245 1.00 83.87 N -ANISOU 3643 NZ LYS C 54 11385 7125 13356 1158 869 625 N -ATOM 3644 N GLU C 55 -2.357 24.978 12.891 1.00 46.14 N -ANISOU 3644 N GLU C 55 7506 2532 7495 -284 1735 41 N -ATOM 3645 CA GLU C 55 -2.014 25.878 13.990 1.00 48.79 C -ANISOU 3645 CA GLU C 55 7791 2771 7976 -344 1872 -252 C -ATOM 3646 C GLU C 55 -0.530 26.291 14.009 1.00 47.69 C -ANISOU 3646 C GLU C 55 7764 2690 7665 -678 1993 -311 C -ATOM 3647 O GLU C 55 -0.200 27.426 14.349 1.00 49.04 O -ANISOU 3647 O GLU C 55 8020 2641 7973 -762 2042 -394 O -ATOM 3648 CB GLU C 55 -2.405 25.200 15.306 1.00 51.33 C -ANISOU 3648 CB GLU C 55 7873 3347 8282 -281 1983 -586 C -ATOM 3649 CG GLU C 55 -2.115 25.996 16.540 1.00 57.26 C -ANISOU 3649 CG GLU C 55 8586 4068 9103 -399 2140 -903 C -ATOM 3650 CD GLU C 55 -3.337 26.142 17.427 1.00 65.91 C -ANISOU 3650 CD GLU C 55 9508 5140 10397 -194 2191 -1115 C -ATOM 3651 OE1 GLU C 55 -4.225 25.256 17.377 1.00 62.12 O -ANISOU 3651 OE1 GLU C 55 8870 4817 9917 -11 2122 -1079 O -ATOM 3652 OE2 GLU C 55 -3.400 27.151 18.162 1.00 72.07 O -ANISOU 3652 OE2 GLU C 55 10306 5746 11330 -234 2318 -1327 O -ATOM 3653 N MET C 56 0.357 25.376 13.625 1.00 43.47 N -ANISOU 3653 N MET C 56 7210 2450 6857 -864 2044 -274 N -ATOM 3654 CA MET C 56 1.802 25.608 13.722 1.00 52.06 C -ANISOU 3654 CA MET C 56 8310 3667 7804 -1170 2162 -357 C -ATOM 3655 C MET C 56 2.532 25.624 12.367 1.00 53.14 C -ANISOU 3655 C MET C 56 8592 3833 7765 -1348 2160 -108 C -ATOM 3656 O MET C 56 3.748 25.833 12.311 1.00 55.58 O -ANISOU 3656 O MET C 56 8881 4259 7977 -1595 2263 -167 O -ATOM 3657 CB MET C 56 2.443 24.554 14.638 1.00 52.42 C -ANISOU 3657 CB MET C 56 8118 4078 7722 -1276 2236 -587 C -ATOM 3658 CG MET C 56 1.821 24.449 16.027 1.00 52.13 C -ANISOU 3658 CG MET C 56 7949 4095 7762 -1194 2244 -840 C -ATOM 3659 SD MET C 56 2.662 23.261 17.098 1.00 47.68 S -ANISOU 3659 SD MET C 56 7133 3950 7034 -1393 2241 -1030 S -ATOM 3660 CE MET C 56 4.179 24.168 17.420 1.00 48.71 C -ANISOU 3660 CE MET C 56 7281 4098 7127 -1716 2294 -1104 C -ATOM 3661 N GLY C 57 1.792 25.417 11.280 1.00 51.08 N -ANISOU 3661 N GLY C 57 8345 3436 7628 -842 184 349 N -ATOM 3662 CA GLY C 57 2.394 25.222 9.969 1.00 54.55 C -ANISOU 3662 CA GLY C 57 8746 4042 7940 -946 217 698 C -ATOM 3663 C GLY C 57 3.144 26.406 9.378 1.00 64.85 C -ANISOU 3663 C GLY C 57 10172 5088 9379 -1157 133 1003 C -ATOM 3664 O GLY C 57 3.819 26.273 8.357 1.00 67.97 O -ANISOU 3664 O GLY C 57 10515 5669 9640 -1293 171 1313 O -ATOM 3665 N GLY C 58 3.038 27.565 10.017 1.00 66.23 N -ANISOU 3665 N GLY C 58 10397 4949 9818 -1144 31 893 N -ATOM 3666 CA GLY C 58 3.625 28.773 9.471 1.00 72.11 C -ANISOU 3666 CA GLY C 58 11186 5491 10721 -1280 -14 1146 C -ATOM 3667 C GLY C 58 5.065 29.027 9.875 1.00 71.95 C -ANISOU 3667 C GLY C 58 11068 5536 10735 -1572 40 1171 C -ATOM 3668 O GLY C 58 5.615 30.092 9.576 1.00 74.30 O -ANISOU 3668 O GLY C 58 11418 5639 11172 -1709 18 1337 O -ATOM 3669 N HIS C 59 5.680 28.058 10.549 1.00 65.23 N -ANISOU 3669 N HIS C 59 10085 4959 9741 -1664 110 1004 N -ATOM 3670 CA HIS C 59 7.067 28.207 10.978 1.00 66.22 C -ANISOU 3670 CA HIS C 59 10095 5187 9878 -1917 151 999 C -ATOM 3671 C HIS C 59 7.756 26.859 11.199 1.00 58.45 C -ANISOU 3671 C HIS C 59 8962 4626 8620 -1993 248 929 C -ATOM 3672 O HIS C 59 7.107 25.815 11.242 1.00 57.78 O -ANISOU 3672 O HIS C 59 8876 4712 8367 -1852 297 826 O -ATOM 3673 CB HIS C 59 7.148 29.043 12.259 1.00 71.59 C -ANISOU 3673 CB HIS C 59 10796 5590 10814 -1932 77 704 C -ATOM 3674 CG HIS C 59 8.451 29.758 12.436 1.00 77.50 C -ANISOU 3674 CG HIS C 59 11483 6289 11674 -2191 90 761 C -ATOM 3675 ND1 HIS C 59 8.705 30.993 11.872 1.00 84.49 N -ANISOU 3675 ND1 HIS C 59 12472 6894 12737 -2303 70 955 N -ATOM 3676 CD2 HIS C 59 9.574 29.421 13.115 1.00 77.65 C -ANISOU 3676 CD2 HIS C 59 11361 6506 11638 -2361 115 648 C -ATOM 3677 CE1 HIS C 59 9.925 31.379 12.193 1.00 85.28 C -ANISOU 3677 CE1 HIS C 59 12485 7014 12904 -2544 92 951 C -ATOM 3678 NE2 HIS C 59 10.475 30.443 12.947 1.00 81.02 N -ANISOU 3678 NE2 HIS C 59 11785 6768 12232 -2574 115 762 N -ATOM 3679 N HIS C 60 9.081 26.904 11.319 1.00 55.74 N -ANISOU 3679 N HIS C 60 8498 4445 8236 -2211 288 975 N -ATOM 3680 CA HIS C 60 9.877 25.748 11.697 1.00 48.89 C -ANISOU 3680 CA HIS C 60 7485 3961 7130 -2278 371 865 C -ATOM 3681 C HIS C 60 9.348 25.213 13.021 1.00 44.82 C -ANISOU 3681 C HIS C 60 6991 3426 6613 -2152 363 517 C -ATOM 3682 O HIS C 60 9.030 25.984 13.924 1.00 47.94 O -ANISOU 3682 O HIS C 60 7449 3554 7210 -2115 278 328 O -ATOM 3683 CB HIS C 60 11.342 26.164 11.861 1.00 55.32 C -ANISOU 3683 CB HIS C 60 8183 4876 7959 -2514 383 909 C -ATOM 3684 CG HIS C 60 12.273 25.025 12.146 1.00 63.34 C -ANISOU 3684 CG HIS C 60 9043 6305 8719 -2574 460 810 C -ATOM 3685 ND1 HIS C 60 13.287 24.658 11.281 1.00 70.54 N -ANISOU 3685 ND1 HIS C 60 9814 7549 9439 -2694 520 990 N -ATOM 3686 CD2 HIS C 60 12.357 24.176 13.198 1.00 61.10 C -ANISOU 3686 CD2 HIS C 60 8716 6169 8330 -2515 485 542 C -ATOM 3687 CE1 HIS C 60 13.942 23.628 11.786 1.00 66.28 C -ANISOU 3687 CE1 HIS C 60 9154 7325 8703 -2695 566 824 C -ATOM 3688 NE2 HIS C 60 13.396 23.312 12.947 1.00 59.40 N -ANISOU 3688 NE2 HIS C 60 8346 6341 7882 -2593 552 565 N -ATOM 3689 N ILE C 61 9.271 23.893 13.132 1.00 39.19 N -ANISOU 3689 N ILE C 61 6209 3010 5672 -2081 455 428 N -ATOM 3690 CA ILE C 61 8.802 23.244 14.339 1.00 45.06 C -ANISOU 3690 CA ILE C 61 6950 3793 6376 -1963 483 130 C -ATOM 3691 C ILE C 61 9.907 22.344 14.870 1.00 44.74 C -ANISOU 3691 C ILE C 61 6767 4080 6153 -2063 552 44 C -ATOM 3692 O ILE C 61 10.531 21.611 14.103 1.00 40.99 O -ANISOU 3692 O ILE C 61 6192 3873 5510 -2118 606 182 O -ATOM 3693 CB ILE C 61 7.569 22.396 14.012 1.00 50.57 C -ANISOU 3693 CB ILE C 61 7694 4524 6997 -1764 541 101 C -ATOM 3694 CG1 ILE C 61 6.379 23.307 13.713 1.00 57.19 C -ANISOU 3694 CG1 ILE C 61 8682 5032 8015 -1621 461 121 C -ATOM 3695 CG2 ILE C 61 7.244 21.416 15.132 1.00 45.54 C -ANISOU 3695 CG2 ILE C 61 7001 4033 6269 -1668 606 -155 C -ATOM 3696 CD1 ILE C 61 5.311 22.630 12.893 1.00 58.67 C -ANISOU 3696 CD1 ILE C 61 8871 5301 8118 -1413 498 188 C -ATOM 3697 N VAL C 62 10.179 22.421 16.168 1.00 38.23 N -ANISOU 3697 N VAL C 62 5921 3254 5352 -2077 540 -192 N -ATOM 3698 CA VAL C 62 10.954 21.369 16.813 1.00 34.69 C -ANISOU 3698 CA VAL C 62 5352 3118 4711 -2113 609 -305 C -ATOM 3699 C VAL C 62 9.967 20.473 17.548 1.00 35.00 C -ANISOU 3699 C VAL C 62 5404 3208 4688 -1942 663 -475 C -ATOM 3700 O VAL C 62 9.323 20.911 18.497 1.00 32.80 O -ANISOU 3700 O VAL C 62 5174 2793 4494 -1862 637 -663 O -ATOM 3701 CB VAL C 62 11.992 21.913 17.803 1.00 39.37 C -ANISOU 3701 CB VAL C 62 5891 3738 5330 -2246 574 -452 C -ATOM 3702 CG1 VAL C 62 12.792 20.757 18.416 1.00 38.28 C -ANISOU 3702 CG1 VAL C 62 5628 3944 4973 -2268 642 -556 C -ATOM 3703 CG2 VAL C 62 12.915 22.897 17.124 1.00 42.46 C -ANISOU 3703 CG2 VAL C 62 6263 4046 5823 -2430 517 -284 C -ATOM 3704 N ALA C 63 9.827 19.230 17.094 1.00 32.84 N -ANISOU 3704 N ALA C 63 5069 3138 4272 -1880 729 -411 N -ATOM 3705 CA ALA C 63 8.973 18.256 17.772 1.00 32.03 C -ANISOU 3705 CA ALA C 63 4928 3136 4106 -1686 762 -526 C -ATOM 3706 C ALA C 63 9.764 17.538 18.868 1.00 34.89 C -ANISOU 3706 C ALA C 63 5192 3729 4336 -1721 785 -648 C -ATOM 3707 O ALA C 63 10.774 16.881 18.576 1.00 30.48 O -ANISOU 3707 O ALA C 63 4542 3380 3658 -1788 793 -587 O -ATOM 3708 CB ALA C 63 8.424 17.266 16.788 1.00 31.12 C -ANISOU 3708 CB ALA C 63 4765 3127 3931 -1550 781 -400 C -ATOM 3709 N LEU C 64 9.297 17.657 20.115 1.00 28.32 N -ANISOU 3709 N LEU C 64 4367 2887 3507 -1659 792 -826 N -ATOM 3710 CA LEU C 64 10.004 17.132 21.289 1.00 28.12 C -ANISOU 3710 CA LEU C 64 4252 3087 3346 -1683 807 -945 C -ATOM 3711 C LEU C 64 9.285 15.894 21.850 1.00 31.45 C -ANISOU 3711 C LEU C 64 4614 3671 3664 -1524 847 -936 C -ATOM 3712 O LEU C 64 8.190 16.000 22.403 1.00 32.73 O -ANISOU 3712 O LEU C 64 4794 3787 3854 -1418 865 -1010 O -ATOM 3713 CB LEU C 64 10.070 18.221 22.359 1.00 29.31 C -ANISOU 3713 CB LEU C 64 4427 3153 3557 -1734 778 -1163 C -ATOM 3714 CG LEU C 64 10.969 18.088 23.596 1.00 37.20 C -ANISOU 3714 CG LEU C 64 5330 4378 4424 -1787 778 -1326 C -ATOM 3715 CD1 LEU C 64 12.399 17.755 23.219 1.00 38.26 C -ANISOU 3715 CD1 LEU C 64 5396 4671 4471 -1933 774 -1251 C -ATOM 3716 CD2 LEU C 64 10.953 19.374 24.402 1.00 34.01 C -ANISOU 3716 CD2 LEU C 64 4953 3839 4129 -1836 726 -1569 C -ATOM 3717 N CYS C 65 9.904 14.726 21.707 1.00 26.63 N -ANISOU 3717 N CYS C 65 3926 3251 2939 -1510 851 -843 N -ATOM 3718 CA CYS C 65 9.305 13.472 22.163 1.00 23.83 C -ANISOU 3718 CA CYS C 65 3520 3017 2517 -1384 871 -790 C -ATOM 3719 C CYS C 65 9.625 13.226 23.633 1.00 29.51 C -ANISOU 3719 C CYS C 65 4180 3929 3102 -1380 885 -881 C -ATOM 3720 O CYS C 65 10.796 13.225 24.026 1.00 29.73 O -ANISOU 3720 O CYS C 65 4162 4101 3033 -1450 863 -929 O -ATOM 3721 CB CYS C 65 9.840 12.311 21.313 1.00 25.32 C -ANISOU 3721 CB CYS C 65 3654 3294 2672 -1353 838 -661 C -ATOM 3722 SG CYS C 65 9.247 10.693 21.840 1.00 30.66 S -ANISOU 3722 SG CYS C 65 4274 4064 3313 -1223 832 -571 S -ATOM 3723 N VAL C 66 8.594 13.044 24.457 1.00 29.07 N -ANISOU 3723 N VAL C 66 4111 3913 3022 -1295 923 -908 N -ATOM 3724 CA VAL C 66 8.817 12.695 25.855 1.00 28.96 C -ANISOU 3724 CA VAL C 66 4020 4139 2845 -1275 940 -960 C -ATOM 3725 C VAL C 66 8.903 11.172 26.004 1.00 31.51 C -ANISOU 3725 C VAL C 66 4291 4591 3089 -1221 933 -772 C -ATOM 3726 O VAL C 66 7.882 10.484 26.061 1.00 28.36 O -ANISOU 3726 O VAL C 66 3880 4177 2720 -1160 960 -661 O -ATOM 3727 CB VAL C 66 7.720 13.262 26.779 1.00 31.65 C -ANISOU 3727 CB VAL C 66 4338 4529 3158 -1213 984 -1085 C -ATOM 3728 CG1 VAL C 66 8.087 13.025 28.250 1.00 34.48 C -ANISOU 3728 CG1 VAL C 66 4594 5197 3308 -1195 1001 -1152 C -ATOM 3729 CG2 VAL C 66 7.520 14.770 26.529 1.00 31.49 C -ANISOU 3729 CG2 VAL C 66 4385 4312 3268 -1240 959 -1282 C -ATOM 3730 N LEU C 67 10.132 10.657 26.041 1.00 34.03 N -ANISOU 3730 N LEU C 67 4577 5027 3325 -1246 885 -741 N -ATOM 3731 CA LEU C 67 10.380 9.220 26.199 1.00 31.73 C -ANISOU 3731 CA LEU C 67 4246 4832 2979 -1181 844 -572 C -ATOM 3732 C LEU C 67 9.978 8.773 27.606 1.00 30.69 C -ANISOU 3732 C LEU C 67 4058 4900 2701 -1141 877 -513 C -ATOM 3733 O LEU C 67 9.949 9.602 28.526 1.00 29.58 O -ANISOU 3733 O LEU C 67 3884 4905 2450 -1158 920 -655 O -ATOM 3734 CB LEU C 67 11.869 8.940 25.973 1.00 36.27 C -ANISOU 3734 CB LEU C 67 4786 5515 3479 -1199 773 -598 C -ATOM 3735 CG LEU C 67 12.387 9.238 24.576 1.00 37.92 C -ANISOU 3735 CG LEU C 67 5015 5607 3788 -1243 739 -628 C -ATOM 3736 CD1 LEU C 67 13.869 8.947 24.485 1.00 41.86 C -ANISOU 3736 CD1 LEU C 67 5445 6283 4177 -1258 672 -675 C -ATOM 3737 CD2 LEU C 67 11.616 8.412 23.578 1.00 31.74 C -ANISOU 3737 CD2 LEU C 67 4252 4663 3143 -1166 712 -505 C -ATOM 3738 N LYS C 68 9.657 7.489 27.799 1.00 29.63 N -ANISOU 3738 N LYS C 68 3906 4785 2568 -1087 851 -306 N -ATOM 3739 CA LYS C 68 9.611 6.486 26.721 1.00 31.78 C -ANISOU 3739 CA LYS C 68 4207 4866 3001 -1050 779 -176 C -ATOM 3740 C LYS C 68 8.214 6.340 26.134 1.00 30.08 C -ANISOU 3740 C LYS C 68 4013 4467 2949 -1047 819 -112 C -ATOM 3741 O LYS C 68 8.055 6.084 24.928 1.00 31.10 O -ANISOU 3741 O LYS C 68 4167 4412 3235 -1024 776 -110 O -ATOM 3742 CB LYS C 68 10.055 5.120 27.258 1.00 34.31 C -ANISOU 3742 CB LYS C 68 4499 5264 3274 -991 697 10 C -ATOM 3743 CG LYS C 68 11.473 5.096 27.813 1.00 38.43 C -ANISOU 3743 CG LYS C 68 4988 5990 3625 -964 639 -49 C -ATOM 3744 CD LYS C 68 12.033 3.678 27.871 1.00 41.39 C -ANISOU 3744 CD LYS C 68 5356 6355 4018 -871 510 120 C -ATOM 3745 CE LYS C 68 12.141 3.178 29.291 1.00 47.87 C -ANISOU 3745 CE LYS C 68 6142 7389 4659 -842 508 276 C -ATOM 3746 NZ LYS C 68 12.695 1.790 29.338 1.00 48.92 N -ANISOU 3746 NZ LYS C 68 6283 7469 4834 -738 357 459 N -ATOM 3747 N GLY C 69 7.206 6.492 26.990 1.00 26.01 N -ANISOU 3747 N GLY C 69 3465 4039 2378 -1063 899 -72 N -ATOM 3748 CA GLY C 69 5.823 6.241 26.604 1.00 29.92 C -ANISOU 3748 CA GLY C 69 3952 4410 3006 -1063 940 -3 C -ATOM 3749 C GLY C 69 5.361 7.075 25.419 1.00 25.59 C -ANISOU 3749 C GLY C 69 3454 3672 2598 -1050 953 -147 C -ATOM 3750 O GLY C 69 4.441 6.695 24.688 1.00 29.62 O -ANISOU 3750 O GLY C 69 3960 4040 3254 -1029 952 -101 O -ATOM 3751 N GLY C 70 6.003 8.214 25.207 1.00 24.72 N -ANISOU 3751 N GLY C 70 3387 3555 2450 -1065 957 -314 N -ATOM 3752 CA GLY C 70 5.632 9.056 24.081 1.00 28.08 C -ANISOU 3752 CA GLY C 70 3870 3798 3002 -1055 960 -414 C -ATOM 3753 C GLY C 70 6.060 8.565 22.710 1.00 30.61 C -ANISOU 3753 C GLY C 70 4210 3984 3435 -1033 891 -364 C -ATOM 3754 O GLY C 70 5.596 9.097 21.701 1.00 23.99 O -ANISOU 3754 O GLY C 70 3406 3014 2696 -1010 892 -406 O -ATOM 3755 N TYR C 71 6.923 7.551 22.650 1.00 26.50 N -ANISOU 3755 N TYR C 71 3658 3517 2894 -1020 821 -284 N -ATOM 3756 CA TYR C 71 7.604 7.252 21.387 1.00 24.48 C -ANISOU 3756 CA TYR C 71 3395 3205 2701 -989 745 -294 C -ATOM 3757 C TYR C 71 6.694 6.820 20.235 1.00 22.85 C -ANISOU 3757 C TYR C 71 3176 2857 2651 -920 719 -272 C -ATOM 3758 O TYR C 71 6.931 7.209 19.087 1.00 24.33 O -ANISOU 3758 O TYR C 71 3363 3014 2868 -899 696 -320 O -ATOM 3759 CB TYR C 71 8.777 6.269 21.576 1.00 32.31 C -ANISOU 3759 CB TYR C 71 4342 4302 3632 -960 653 -254 C -ATOM 3760 CG TYR C 71 8.506 4.847 21.112 1.00 32.88 C -ANISOU 3760 CG TYR C 71 4375 4287 3833 -869 556 -169 C -ATOM 3761 CD1 TYR C 71 8.693 4.472 19.782 1.00 33.45 C -ANISOU 3761 CD1 TYR C 71 4407 4305 3997 -795 476 -225 C -ATOM 3762 CD2 TYR C 71 8.094 3.875 22.019 1.00 29.80 C -ANISOU 3762 CD2 TYR C 71 3975 3875 3473 -858 533 -35 C -ATOM 3763 CE1 TYR C 71 8.437 3.166 19.364 1.00 34.98 C -ANISOU 3763 CE1 TYR C 71 4554 4398 4338 -700 362 -189 C -ATOM 3764 CE2 TYR C 71 7.843 2.574 21.619 1.00 29.36 C -ANISOU 3764 CE2 TYR C 71 3889 3689 3578 -788 422 44 C -ATOM 3765 CZ TYR C 71 8.015 2.229 20.288 1.00 28.83 C -ANISOU 3765 CZ TYR C 71 3784 3543 3627 -703 330 -55 C -ATOM 3766 OH TYR C 71 7.762 0.932 19.887 1.00 27.58 O -ANISOU 3766 OH TYR C 71 3586 3236 3658 -621 198 -17 O -ATOM 3767 N LYS C 72 5.670 6.018 20.516 1.00 23.95 N -ANISOU 3767 N LYS C 72 3288 2930 2881 -890 722 -197 N -ATOM 3768 CA LYS C 72 4.790 5.553 19.428 1.00 26.98 C -ANISOU 3768 CA LYS C 72 3638 3189 3423 -821 688 -204 C -ATOM 3769 C LYS C 72 3.913 6.666 18.865 1.00 27.23 C -ANISOU 3769 C LYS C 72 3704 3166 3478 -808 758 -280 C -ATOM 3770 O LYS C 72 3.828 6.854 17.647 1.00 24.24 O -ANISOU 3770 O LYS C 72 3315 2743 3153 -748 725 -326 O -ATOM 3771 CB LYS C 72 3.912 4.384 19.885 1.00 25.93 C -ANISOU 3771 CB LYS C 72 3456 2989 3407 -820 667 -100 C -ATOM 3772 CG LYS C 72 4.571 3.029 19.760 1.00 39.63 C -ANISOU 3772 CG LYS C 72 5153 4677 5228 -778 535 -36 C -ATOM 3773 CD LYS C 72 5.033 2.780 18.344 1.00 43.15 C -ANISOU 3773 CD LYS C 72 5559 5085 5750 -676 433 -152 C -ATOM 3774 CE LYS C 72 3.864 2.513 17.429 1.00 50.35 C -ANISOU 3774 CE LYS C 72 6419 5883 6829 -624 419 -204 C -ATOM 3775 NZ LYS C 72 4.318 2.210 16.041 1.00 53.92 N -ANISOU 3775 NZ LYS C 72 6804 6348 7334 -503 310 -334 N -ATOM 3776 N PHE C 73 3.229 7.375 19.754 1.00 25.28 N -ANISOU 3776 N PHE C 73 3484 2940 3182 -848 845 -297 N -ATOM 3777 CA PHE C 73 2.447 8.547 19.366 1.00 26.72 C -ANISOU 3777 CA PHE C 73 3709 3061 3382 -818 895 -386 C -ATOM 3778 C PHE C 73 3.286 9.537 18.563 1.00 25.98 C -ANISOU 3778 C PHE C 73 3683 2928 3262 -828 872 -429 C -ATOM 3779 O PHE C 73 2.842 10.070 17.535 1.00 23.62 O -ANISOU 3779 O PHE C 73 3408 2547 3021 -771 862 -449 O -ATOM 3780 CB PHE C 73 1.871 9.216 20.613 1.00 25.54 C -ANISOU 3780 CB PHE C 73 3568 2981 3156 -847 972 -438 C -ATOM 3781 CG PHE C 73 0.906 10.330 20.321 1.00 25.85 C -ANISOU 3781 CG PHE C 73 3643 2947 3233 -786 1004 -551 C -ATOM 3782 CD1 PHE C 73 -0.121 10.165 19.387 1.00 25.45 C -ANISOU 3782 CD1 PHE C 73 3564 2817 3287 -701 995 -560 C -ATOM 3783 CD2 PHE C 73 1.009 11.537 20.998 1.00 24.20 C -ANISOU 3783 CD2 PHE C 73 3487 2746 2963 -796 1027 -668 C -ATOM 3784 CE1 PHE C 73 -1.029 11.204 19.136 1.00 24.69 C -ANISOU 3784 CE1 PHE C 73 3503 2658 3222 -618 1010 -669 C -ATOM 3785 CE2 PHE C 73 0.111 12.583 20.753 1.00 26.70 C -ANISOU 3785 CE2 PHE C 73 3843 2970 3334 -714 1030 -787 C -ATOM 3786 CZ PHE C 73 -0.910 12.411 19.821 1.00 24.75 C -ANISOU 3786 CZ PHE C 73 3575 2650 3178 -620 1023 -779 C -ATOM 3787 N PHE C 74 4.504 9.781 19.037 1.00 23.85 N -ANISOU 3787 N PHE C 74 3435 2730 2897 -906 863 -430 N -ATOM 3788 CA PHE C 74 5.400 10.725 18.394 1.00 20.84 C -ANISOU 3788 CA PHE C 74 3102 2329 2485 -960 845 -449 C -ATOM 3789 C PHE C 74 5.716 10.294 16.973 1.00 25.28 C -ANISOU 3789 C PHE C 74 3623 2909 3075 -912 791 -399 C -ATOM 3790 O PHE C 74 5.602 11.090 16.042 1.00 24.14 O -ANISOU 3790 O PHE C 74 3513 2708 2952 -907 789 -381 O -ATOM 3791 CB PHE C 74 6.663 10.859 19.241 1.00 23.47 C -ANISOU 3791 CB PHE C 74 3432 2777 2707 -1060 842 -472 C -ATOM 3792 CG PHE C 74 7.736 11.713 18.634 1.00 28.68 C -ANISOU 3792 CG PHE C 74 4117 3447 3334 -1154 823 -478 C -ATOM 3793 CD1 PHE C 74 7.728 13.091 18.803 1.00 29.61 C -ANISOU 3793 CD1 PHE C 74 4314 3451 3485 -1234 844 -532 C -ATOM 3794 CD2 PHE C 74 8.781 11.131 17.943 1.00 24.96 C -ANISOU 3794 CD2 PHE C 74 3577 3106 2802 -1170 776 -437 C -ATOM 3795 CE1 PHE C 74 8.739 13.878 18.284 1.00 31.58 C -ANISOU 3795 CE1 PHE C 74 4579 3699 3719 -1359 826 -510 C -ATOM 3796 CE2 PHE C 74 9.793 11.911 17.403 1.00 28.31 C -ANISOU 3796 CE2 PHE C 74 3998 3582 3176 -1284 768 -426 C -ATOM 3797 CZ PHE C 74 9.772 13.283 17.580 1.00 29.57 C -ANISOU 3797 CZ PHE C 74 4243 3612 3381 -1395 797 -445 C -ATOM 3798 N ALA C 75 6.115 9.033 16.805 1.00 21.87 N -ANISOU 3798 N ALA C 75 3108 2564 2639 -867 734 -377 N -ATOM 3799 CA ALA C 75 6.519 8.527 15.497 1.00 22.34 C -ANISOU 3799 CA ALA C 75 3093 2693 2703 -798 665 -373 C -ATOM 3800 C ALA C 75 5.352 8.604 14.524 1.00 24.69 C -ANISOU 3800 C ALA C 75 3378 2910 3092 -698 665 -379 C -ATOM 3801 O ALA C 75 5.506 9.059 13.379 1.00 22.67 O -ANISOU 3801 O ALA C 75 3101 2708 2804 -666 648 -364 O -ATOM 3802 CB ALA C 75 7.015 7.091 15.608 1.00 26.19 C -ANISOU 3802 CB ALA C 75 3492 3253 3205 -736 579 -386 C -ATOM 3803 N ASP C 76 4.192 8.151 14.979 1.00 20.82 N -ANISOU 3803 N ASP C 76 2885 2323 2701 -652 684 -394 N -ATOM 3804 CA ASP C 76 2.981 8.162 14.162 1.00 26.00 C -ANISOU 3804 CA ASP C 76 3514 2917 3448 -549 683 -424 C -ATOM 3805 C ASP C 76 2.473 9.559 13.844 1.00 22.75 C -ANISOU 3805 C ASP C 76 3189 2440 3016 -544 735 -418 C -ATOM 3806 O ASP C 76 2.131 9.833 12.697 1.00 24.47 O -ANISOU 3806 O ASP C 76 3385 2671 3241 -458 710 -415 O -ATOM 3807 CB ASP C 76 1.872 7.318 14.810 1.00 26.96 C -ANISOU 3807 CB ASP C 76 3593 2970 3682 -527 694 -440 C -ATOM 3808 CG ASP C 76 2.184 5.835 14.779 1.00 31.59 C -ANISOU 3808 CG ASP C 76 4089 3564 4349 -504 606 -436 C -ATOM 3809 OD1 ASP C 76 2.978 5.442 13.905 1.00 31.97 O -ANISOU 3809 OD1 ASP C 76 4082 3682 4382 -444 522 -473 O -ATOM 3810 OD2 ASP C 76 1.642 5.063 15.609 1.00 26.68 O -ANISOU 3810 OD2 ASP C 76 3443 2886 3809 -543 610 -394 O -ATOM 3811 N LEU C 77 2.400 10.432 14.848 1.00 21.00 N -ANISOU 3811 N LEU C 77 3059 2150 2772 -621 793 -425 N -ATOM 3812 CA LEU C 77 1.967 11.809 14.634 1.00 22.82 C -ANISOU 3812 CA LEU C 77 3386 2272 3013 -609 815 -433 C -ATOM 3813 C LEU C 77 2.869 12.471 13.607 1.00 25.20 C -ANISOU 3813 C LEU C 77 3719 2590 3265 -648 783 -346 C -ATOM 3814 O LEU C 77 2.393 13.125 12.679 1.00 25.93 O -ANISOU 3814 O LEU C 77 3844 2630 3379 -579 766 -301 O -ATOM 3815 CB LEU C 77 1.998 12.610 15.932 1.00 24.48 C -ANISOU 3815 CB LEU C 77 3673 2420 3208 -686 857 -492 C -ATOM 3816 CG LEU C 77 1.599 14.087 15.824 1.00 27.55 C -ANISOU 3816 CG LEU C 77 4174 2651 3645 -666 850 -527 C -ATOM 3817 CD1 LEU C 77 0.135 14.232 15.420 1.00 24.64 C -ANISOU 3817 CD1 LEU C 77 3797 2221 3344 -511 849 -581 C -ATOM 3818 CD2 LEU C 77 1.855 14.818 17.150 1.00 29.47 C -ANISOU 3818 CD2 LEU C 77 4469 2855 3872 -742 869 -630 C -ATOM 3819 N LEU C 78 4.179 12.300 13.769 1.00 23.75 N -ANISOU 3819 N LEU C 78 3515 2506 3002 -760 773 -310 N -ATOM 3820 CA LEU C 78 5.120 12.873 12.810 1.00 23.82 C -ANISOU 3820 CA LEU C 78 3524 2586 2942 -827 751 -210 C -ATOM 3821 C LEU C 78 4.957 12.280 11.406 1.00 24.22 C -ANISOU 3821 C LEU C 78 3469 2779 2956 -707 709 -171 C -ATOM 3822 O LEU C 78 5.104 12.985 10.418 1.00 23.98 O -ANISOU 3822 O LEU C 78 3447 2784 2879 -712 699 -64 O -ATOM 3823 CB LEU C 78 6.557 12.725 13.299 1.00 26.34 C -ANISOU 3823 CB LEU C 78 3810 3030 3169 -968 748 -206 C -ATOM 3824 CG LEU C 78 7.075 13.995 13.968 1.00 35.30 C -ANISOU 3824 CG LEU C 78 5049 4046 4317 -1127 774 -194 C -ATOM 3825 CD1 LEU C 78 6.275 14.344 15.216 1.00 36.84 C -ANISOU 3825 CD1 LEU C 78 5325 4081 4591 -1106 801 -305 C -ATOM 3826 CD2 LEU C 78 8.541 13.860 14.294 1.00 40.91 C -ANISOU 3826 CD2 LEU C 78 5700 4920 4922 -1269 769 -196 C -ATOM 3827 N ASP C 79 4.669 10.982 11.319 1.00 24.02 N -ANISOU 3827 N ASP C 79 3335 2840 2952 -601 675 -254 N -ATOM 3828 CA ASP C 79 4.434 10.378 10.016 1.00 22.78 C -ANISOU 3828 CA ASP C 79 3055 2828 2771 -462 620 -270 C -ATOM 3829 C ASP C 79 3.221 10.995 9.306 1.00 23.07 C -ANISOU 3829 C ASP C 79 3126 2785 2854 -351 629 -246 C -ATOM 3830 O ASP C 79 3.254 11.201 8.101 1.00 22.00 O -ANISOU 3830 O ASP C 79 2928 2787 2642 -276 601 -191 O -ATOM 3831 CB ASP C 79 4.304 8.846 10.118 1.00 28.50 C -ANISOU 3831 CB ASP C 79 3659 3609 3560 -368 556 -392 C -ATOM 3832 CG ASP C 79 5.655 8.149 10.145 1.00 32.90 C -ANISOU 3832 CG ASP C 79 4131 4336 4033 -402 500 -420 C -ATOM 3833 OD1 ASP C 79 6.671 8.813 9.847 1.00 35.99 O -ANISOU 3833 OD1 ASP C 79 4520 4864 4290 -492 517 -350 O -ATOM 3834 OD2 ASP C 79 5.698 6.936 10.441 1.00 38.65 O -ANISOU 3834 OD2 ASP C 79 4787 5061 4836 -339 431 -511 O -ATOM 3835 N TYR C 80 2.158 11.279 10.047 1.00 21.90 N -ANISOU 3835 N TYR C 80 3060 2451 2811 -329 666 -292 N -ATOM 3836 CA TYR C 80 0.994 11.943 9.463 1.00 22.07 C -ANISOU 3836 CA TYR C 80 3119 2394 2874 -209 667 -287 C -ATOM 3837 C TYR C 80 1.293 13.396 9.062 1.00 23.12 C -ANISOU 3837 C TYR C 80 3375 2445 2963 -260 673 -142 C -ATOM 3838 O TYR C 80 0.846 13.862 8.004 1.00 23.66 O -ANISOU 3838 O TYR C 80 3439 2549 3001 -154 645 -67 O -ATOM 3839 CB TYR C 80 -0.210 11.870 10.416 1.00 23.94 C -ANISOU 3839 CB TYR C 80 3388 2489 3220 -169 702 -395 C -ATOM 3840 CG TYR C 80 -0.931 10.533 10.386 1.00 26.29 C -ANISOU 3840 CG TYR C 80 3547 2851 3590 -88 683 -507 C -ATOM 3841 CD1 TYR C 80 -1.609 10.118 9.246 1.00 27.01 C -ANISOU 3841 CD1 TYR C 80 3530 3033 3700 65 636 -562 C -ATOM 3842 CD2 TYR C 80 -0.938 9.690 11.496 1.00 24.30 C -ANISOU 3842 CD2 TYR C 80 3267 2572 3395 -169 705 -550 C -ATOM 3843 CE1 TYR C 80 -2.284 8.895 9.206 1.00 31.03 C -ANISOU 3843 CE1 TYR C 80 3904 3575 4311 124 604 -681 C -ATOM 3844 CE2 TYR C 80 -1.612 8.452 11.468 1.00 26.49 C -ANISOU 3844 CE2 TYR C 80 3420 2871 3774 -122 675 -628 C -ATOM 3845 CZ TYR C 80 -2.276 8.069 10.316 1.00 28.49 C -ANISOU 3845 CZ TYR C 80 3566 3185 4072 19 622 -704 C -ATOM 3846 OH TYR C 80 -2.952 6.866 10.278 1.00 29.31 O -ANISOU 3846 OH TYR C 80 3540 3286 4309 51 580 -797 O -ATOM 3847 N ILE C 81 2.065 14.112 9.882 1.00 23.48 N -ANISOU 3847 N ILE C 81 3527 2383 3012 -424 698 -94 N -ATOM 3848 CA ILE C 81 2.515 15.469 9.490 1.00 24.67 C -ANISOU 3848 CA ILE C 81 3794 2426 3153 -513 687 65 C -ATOM 3849 C ILE C 81 3.356 15.441 8.212 1.00 26.24 C -ANISOU 3849 C ILE C 81 3909 2844 3217 -545 666 229 C -ATOM 3850 O ILE C 81 3.191 16.275 7.304 1.00 26.05 O -ANISOU 3850 O ILE C 81 3931 2800 3169 -520 642 394 O -ATOM 3851 CB ILE C 81 3.295 16.158 10.636 1.00 27.14 C -ANISOU 3851 CB ILE C 81 4209 2593 3508 -702 707 52 C -ATOM 3852 CG1 ILE C 81 2.355 16.428 11.808 1.00 26.11 C -ANISOU 3852 CG1 ILE C 81 4155 2277 3489 -645 720 -110 C -ATOM 3853 CG2 ILE C 81 3.928 17.465 10.163 1.00 29.01 C -ANISOU 3853 CG2 ILE C 81 4551 2710 3761 -835 681 233 C -ATOM 3854 CD1 ILE C 81 3.074 16.912 13.108 1.00 26.40 C -ANISOU 3854 CD1 ILE C 81 4256 2223 3554 -803 736 -187 C -ATOM 3855 N LYS C 82 4.263 14.476 8.135 1.00 25.36 N -ANISOU 3855 N LYS C 82 3664 2966 3008 -590 668 189 N -ATOM 3856 CA LYS C 82 5.100 14.328 6.954 1.00 27.26 C -ANISOU 3856 CA LYS C 82 3778 3494 3086 -606 648 308 C -ATOM 3857 C LYS C 82 4.261 14.044 5.712 1.00 27.84 C -ANISOU 3857 C LYS C 82 3757 3715 3105 -399 612 320 C -ATOM 3858 O LYS C 82 4.547 14.556 4.633 1.00 26.44 O -ANISOU 3858 O LYS C 82 3536 3707 2802 -398 600 494 O -ATOM 3859 CB LYS C 82 6.143 13.233 7.177 1.00 29.21 C -ANISOU 3859 CB LYS C 82 3882 3973 3245 -647 637 202 C -ATOM 3860 CG LYS C 82 7.304 13.686 8.051 1.00 33.92 C -ANISOU 3860 CG LYS C 82 4533 4533 3822 -870 668 238 C -ATOM 3861 CD LYS C 82 7.896 12.533 8.826 1.00 39.18 C -ANISOU 3861 CD LYS C 82 5115 5298 4474 -863 651 72 C -ATOM 3862 CE LYS C 82 8.384 11.443 7.894 1.00 43.63 C -ANISOU 3862 CE LYS C 82 5477 6188 4915 -743 591 4 C -ATOM 3863 NZ LYS C 82 8.748 10.225 8.670 1.00 48.59 N -ANISOU 3863 NZ LYS C 82 6041 6844 5576 -693 546 -165 N -ATOM 3864 N ALA C 83 3.200 13.255 5.880 1.00 23.76 N -ANISOU 3864 N ALA C 83 3200 3146 2681 -230 594 143 N -ATOM 3865 CA ALA C 83 2.314 12.929 4.750 1.00 27.27 C -ANISOU 3865 CA ALA C 83 3537 3737 3087 -17 553 108 C -ATOM 3866 C ALA C 83 1.637 14.202 4.254 1.00 28.17 C -ANISOU 3866 C ALA C 83 3776 3723 3203 28 555 278 C -ATOM 3867 O ALA C 83 1.514 14.427 3.056 1.00 29.15 O -ANISOU 3867 O ALA C 83 3826 4044 3204 133 525 389 O -ATOM 3868 CB ALA C 83 1.276 11.881 5.158 1.00 22.82 C -ANISOU 3868 CB ALA C 83 2910 3106 2656 121 533 -121 C -ATOM 3869 N LEU C 84 1.216 15.043 5.190 1.00 25.71 N -ANISOU 3869 N LEU C 84 3649 3091 3028 -41 578 295 N -ATOM 3870 CA LEU C 84 0.696 16.361 4.842 1.00 29.27 C -ANISOU 3870 CA LEU C 84 4248 3358 3514 -9 557 461 C -ATOM 3871 C LEU C 84 1.728 17.199 4.093 1.00 33.67 C -ANISOU 3871 C LEU C 84 4836 3998 3960 -154 549 747 C -ATOM 3872 O LEU C 84 1.431 17.815 3.058 1.00 31.93 O -ANISOU 3872 O LEU C 84 4627 3839 3667 -70 514 939 O -ATOM 3873 CB LEU C 84 0.260 17.093 6.101 1.00 29.23 C -ANISOU 3873 CB LEU C 84 4421 3001 3683 -68 566 385 C -ATOM 3874 CG LEU C 84 -0.958 16.474 6.784 1.00 32.66 C -ANISOU 3874 CG LEU C 84 4824 3373 4214 80 577 139 C -ATOM 3875 CD1 LEU C 84 -1.297 17.262 8.043 1.00 33.48 C -ANISOU 3875 CD1 LEU C 84 5078 3190 4454 26 584 52 C -ATOM 3876 CD2 LEU C 84 -2.150 16.450 5.833 1.00 34.10 C -ANISOU 3876 CD2 LEU C 84 4950 3628 4379 320 537 113 C -ATOM 3877 N ASN C 85 2.944 17.217 4.622 1.00 29.29 N -ANISOU 3877 N ASN C 85 4284 3462 3382 -379 582 789 N -ATOM 3878 CA ASN C 85 4.006 18.048 4.067 1.00 31.36 C -ANISOU 3878 CA ASN C 85 4568 3795 3552 -573 584 1067 C -ATOM 3879 C ASN C 85 4.399 17.694 2.642 1.00 32.42 C -ANISOU 3879 C ASN C 85 4516 4351 3451 -513 577 1217 C -ATOM 3880 O ASN C 85 4.883 18.550 1.897 1.00 40.08 O -ANISOU 3880 O ASN C 85 5507 5392 4331 -625 571 1513 O -ATOM 3881 CB ASN C 85 5.247 17.970 4.955 1.00 34.94 C -ANISOU 3881 CB ASN C 85 5019 4244 4013 -818 622 1029 C -ATOM 3882 CG ASN C 85 5.127 18.819 6.199 1.00 42.46 C -ANISOU 3882 CG ASN C 85 6169 4791 5173 -937 619 973 C -ATOM 3883 OD1 ASN C 85 4.406 19.811 6.212 1.00 44.86 O -ANISOU 3883 OD1 ASN C 85 6632 4803 5612 -896 577 1051 O -ATOM 3884 ND2 ASN C 85 5.847 18.441 7.249 1.00 43.53 N -ANISOU 3884 ND2 ASN C 85 6287 4922 5331 -1068 651 825 N -ATOM 3885 N ARG C 86 4.246 16.430 2.269 1.00 42.90 N -ANISOU 3885 N ARG C 86 6441 4762 5095 -504 -183 746 N -ATOM 3886 CA ARG C 86 4.704 16.006 0.945 1.00 43.25 C -ANISOU 3886 CA ARG C 86 6542 5003 4889 -956 -142 898 C -ATOM 3887 C ARG C 86 3.578 15.913 -0.064 1.00 45.49 C -ANISOU 3887 C ARG C 86 6809 5402 5072 -751 -403 1013 C -ATOM 3888 O ARG C 86 3.805 15.534 -1.213 1.00 46.14 O -ANISOU 3888 O ARG C 86 6925 5687 4919 -1118 -383 1131 O -ATOM 3889 CB ARG C 86 5.471 14.684 1.009 1.00 39.20 C -ANISOU 3889 CB ARG C 86 5563 4905 4428 -1292 262 733 C -ATOM 3890 CG ARG C 86 4.661 13.525 1.542 1.00 36.20 C -ANISOU 3890 CG ARG C 86 4613 4869 4271 -967 426 533 C -ATOM 3891 CD ARG C 86 5.404 12.217 1.389 1.00 32.98 C -ANISOU 3891 CD ARG C 86 3791 4822 3917 -1314 778 403 C -ATOM 3892 NE ARG C 86 4.562 11.131 1.853 1.00 30.60 N -ANISOU 3892 NE ARG C 86 3005 4812 3811 -1020 926 234 N -ATOM 3893 CZ ARG C 86 4.638 10.604 3.069 1.00 32.14 C -ANISOU 3893 CZ ARG C 86 2954 5047 4210 -858 1097 82 C -ATOM 3894 NH1 ARG C 86 5.549 11.047 3.924 1.00 28.61 N -ANISOU 3894 NH1 ARG C 86 2670 4394 3807 -951 1128 72 N -ATOM 3895 NH2 ARG C 86 3.820 9.627 3.421 1.00 28.43 N -ANISOU 3895 NH2 ARG C 86 2134 4784 3883 -609 1205 -45 N -ATOM 3896 N ASN C 87 2.371 16.273 0.356 1.00 47.02 N -ANISOU 3896 N ASN C 87 6937 5484 5443 -180 -650 950 N -ATOM 3897 CA ASN C 87 1.231 16.298 -0.553 1.00 49.84 C -ANISOU 3897 CA ASN C 87 7276 5929 5731 82 -969 1039 C -ATOM 3898 C ASN C 87 0.544 17.654 -0.609 1.00 56.34 C -ANISOU 3898 C ASN C 87 8552 6264 6590 482 -1466 1183 C -ATOM 3899 O ASN C 87 -0.543 17.789 -1.173 1.00 60.31 O -ANISOU 3899 O ASN C 87 9015 6792 7108 833 -1807 1219 O -ATOM 3900 CB ASN C 87 0.226 15.199 -0.196 1.00 51.08 C -ANISOU 3900 CB ASN C 87 6790 6518 6100 417 -807 760 C -ATOM 3901 CG ASN C 87 0.781 13.806 -0.438 1.00 45.84 C -ANISOU 3901 CG ASN C 87 5709 6320 5388 21 -381 659 C -ATOM 3902 OD1 ASN C 87 0.983 13.405 -1.582 1.00 43.75 O -ANISOU 3902 OD1 ASN C 87 5458 6267 4898 -321 -372 778 O -ATOM 3903 ND2 ASN C 87 1.028 13.065 0.636 1.00 43.57 N -ANISOU 3903 ND2 ASN C 87 5061 6182 5311 55 -36 433 N -ATOM 3904 N SER C 88 1.190 18.660 -0.034 1.00 56.27 N -ANISOU 3904 N SER C 88 8969 5801 6611 433 -1523 1252 N -ATOM 3905 CA SER C 88 0.640 20.010 -0.033 1.00 64.65 C -ANISOU 3905 CA SER C 88 10504 6317 7745 802 -1993 1382 C -ATOM 3906 C SER C 88 1.621 20.971 -0.689 1.00 68.25 C -ANISOU 3906 C SER C 88 11682 6350 7902 340 -2143 1722 C -ATOM 3907 O SER C 88 2.809 20.666 -0.794 1.00 65.25 O -ANISOU 3907 O SER C 88 11377 6090 7325 -235 -1811 1759 O -ATOM 3908 CB SER C 88 0.328 20.458 1.396 1.00 65.62 C -ANISOU 3908 CB SER C 88 10481 6223 8229 1233 -1935 1092 C -ATOM 3909 OG SER C 88 -0.502 19.513 2.055 1.00 62.70 O -ANISOU 3909 OG SER C 88 9455 6273 8095 1566 -1730 754 O -ATOM 3910 N ASP C 89 1.117 22.115 -1.141 1.00 76.90 N -ANISOU 3910 N ASP C 89 13305 6945 8968 584 -2648 1953 N -ATOM 3911 CA ASP C 89 1.961 23.149 -1.724 1.00 87.63 C -ANISOU 3911 CA ASP C 89 15438 7821 10037 156 -2823 2290 C -ATOM 3912 C ASP C 89 2.996 23.584 -0.702 1.00 91.38 C -ANISOU 3912 C ASP C 89 16043 8069 10609 -72 -2503 2148 C -ATOM 3913 O ASP C 89 4.196 23.422 -0.903 1.00 92.80 O -ANISOU 3913 O ASP C 89 16377 8342 10541 -700 -2192 2201 O -ATOM 3914 CB ASP C 89 1.122 24.357 -2.143 1.00 94.03 C -ANISOU 3914 CB ASP C 89 16784 8046 10897 584 -3464 2533 C -ATOM 3915 CG ASP C 89 0.047 23.999 -3.144 1.00 98.17 C -ANISOU 3915 CG ASP C 89 17184 8785 11331 854 -3855 2670 C -ATOM 3916 OD1 ASP C 89 0.261 23.053 -3.930 1.00 95.98 O -ANISOU 3916 OD1 ASP C 89 16692 9013 10763 457 -3660 2731 O -ATOM 3917 OD2 ASP C 89 -1.014 24.662 -3.144 1.00103.30 O -ANISOU 3917 OD2 ASP C 89 17868 9156 12226 1447 -4310 2650 O -ATOM 3918 N ARG C 90 2.516 24.123 0.410 1.00 92.34 N -ANISOU 3918 N ARG C 90 16069 7919 11099 435 -2571 1925 N -ATOM 3919 CA ARG C 90 3.401 24.597 1.458 1.00 92.41 C -ANISOU 3919 CA ARG C 90 16190 7708 11211 264 -2298 1764 C -ATOM 3920 C ARG C 90 3.740 23.503 2.457 1.00 85.49 C -ANISOU 3920 C ARG C 90 14650 7350 10481 218 -1805 1421 C -ATOM 3921 O ARG C 90 2.950 22.588 2.702 1.00 83.65 O -ANISOU 3921 O ARG C 90 13849 7525 10409 538 -1721 1230 O -ATOM 3922 CB ARG C 90 2.773 25.775 2.194 1.00 98.77 C -ANISOU 3922 CB ARG C 90 17248 7943 12336 790 -2601 1668 C -ATOM 3923 CG ARG C 90 3.151 27.137 1.660 1.00106.53 C -ANISOU 3923 CG ARG C 90 18969 8332 13174 603 -2891 1940 C -ATOM 3924 CD ARG C 90 2.237 28.183 2.264 1.00112.99 C -ANISOU 3924 CD ARG C 90 19785 8776 14370 1206 -3172 1761 C -ATOM 3925 NE ARG C 90 2.829 29.516 2.298 1.00120.27 N -ANISOU 3925 NE ARG C 90 21187 9270 15240 988 -3217 1838 N -ATOM 3926 CZ ARG C 90 2.885 30.342 1.258 1.00127.42 C -ANISOU 3926 CZ ARG C 90 22569 9923 15922 807 -3502 2134 C -ATOM 3927 NH1 ARG C 90 2.399 29.974 0.078 1.00129.69 N -ANISOU 3927 NH1 ARG C 90 22920 10358 15998 791 -3771 2385 N -ATOM 3928 NH2 ARG C 90 3.432 31.540 1.403 1.00131.56 N -ANISOU 3928 NH2 ARG C 90 23511 10051 16425 629 -3518 2170 N -ATOM 3929 N SER C 91 4.933 23.617 3.024 1.00 81.45 N -ANISOU 3929 N SER C 91 14237 6809 9903 -200 -1494 1346 N -ATOM 3930 CA SER C 91 5.378 22.766 4.114 1.00 71.84 C -ANISOU 3930 CA SER C 91 12489 5980 8826 -246 -1083 1043 C -ATOM 3931 C SER C 91 6.462 23.549 4.832 1.00 70.13 C -ANISOU 3931 C SER C 91 12588 5468 8589 -544 -938 975 C -ATOM 3932 O SER C 91 7.103 24.420 4.238 1.00 70.00 O -ANISOU 3932 O SER C 91 13138 5084 8374 -894 -1047 1177 O -ATOM 3933 CB SER C 91 5.939 21.448 3.585 1.00 65.92 C -ANISOU 3933 CB SER C 91 11351 5779 7916 -638 -785 1046 C -ATOM 3934 OG SER C 91 7.016 21.682 2.695 1.00 67.96 O -ANISOU 3934 OG SER C 91 11982 5968 7873 -1250 -725 1236 O -ATOM 3935 N ILE C 92 6.647 23.263 6.115 1.00 68.18 N -ANISOU 3935 N ILE C 92 11999 5378 8527 -426 -698 688 N -ATOM 3936 CA ILE C 92 7.720 23.874 6.886 1.00 67.67 C -ANISOU 3936 CA ILE C 92 12147 5123 8441 -726 -529 577 C -ATOM 3937 C ILE C 92 8.527 22.751 7.508 1.00 62.73 C -ANISOU 3937 C ILE C 92 11033 4997 7806 -981 -170 397 C -ATOM 3938 O ILE C 92 7.971 21.715 7.884 1.00 57.42 O -ANISOU 3938 O ILE C 92 9859 4709 7249 -739 -65 280 O -ATOM 3939 CB ILE C 92 7.158 24.790 7.957 1.00 71.47 C -ANISOU 3939 CB ILE C 92 12741 5252 9164 -316 -637 383 C -ATOM 3940 N PRO C 93 9.846 22.933 7.603 1.00 59.92 N -ANISOU 3940 N PRO C 93 10820 4630 7316 -1478 9 365 N -ATOM 3941 CA PRO C 93 10.629 21.813 8.129 1.00 57.23 C -ANISOU 3941 CA PRO C 93 9992 4757 6995 -1693 295 197 C -ATOM 3942 C PRO C 93 10.371 21.518 9.609 1.00 45.48 C -ANISOU 3942 C PRO C 93 8174 3414 5691 -1384 390 -42 C -ATOM 3943 O PRO C 93 9.844 22.337 10.360 1.00 47.41 O -ANISOU 3943 O PRO C 93 8590 3385 6038 -1101 295 -142 O -ATOM 3944 CB PRO C 93 12.079 22.267 7.919 1.00 59.01 C -ANISOU 3944 CB PRO C 93 10469 4895 7056 -2279 429 172 C -ATOM 3945 CG PRO C 93 12.009 23.761 7.816 1.00 64.84 C -ANISOU 3945 CG PRO C 93 11834 5075 7728 -2303 252 263 C -ATOM 3946 CD PRO C 93 10.691 24.052 7.157 1.00 64.66 C -ANISOU 3946 CD PRO C 93 12000 4826 7740 -1892 -38 472 C -ATOM 3947 N MET C 94 10.742 20.316 10.012 1.00 41.95 N -ANISOU 3947 N MET C 94 7258 3397 5285 -1456 575 -142 N -ATOM 3948 CA MET C 94 10.677 19.936 11.406 1.00 42.91 C -ANISOU 3948 CA MET C 94 7098 3690 5514 -1270 673 -342 C -ATOM 3949 C MET C 94 12.023 19.356 11.794 1.00 42.41 C -ANISOU 3949 C MET C 94 6831 3869 5413 -1645 831 -435 C -ATOM 3950 O MET C 94 12.627 18.617 11.018 1.00 39.64 O -ANISOU 3950 O MET C 94 6300 3726 5036 -1908 908 -380 O -ATOM 3951 CB MET C 94 9.603 18.875 11.614 1.00 39.65 C -ANISOU 3951 CB MET C 94 6284 3574 5207 -918 705 -366 C -ATOM 3952 CG MET C 94 8.164 19.345 11.431 1.00 43.82 C -ANISOU 3952 CG MET C 94 6899 3928 5822 -481 548 -361 C -ATOM 3953 SD MET C 94 7.047 18.004 11.914 1.00 60.74 S -ANISOU 3953 SD MET C 94 8515 6490 8074 -153 666 -477 S -ATOM 3954 CE MET C 94 8.092 17.244 13.130 1.00 34.66 C -ANISOU 3954 CE MET C 94 4989 3448 4733 -403 870 -587 C -ATOM 3955 N THR C 95 12.509 19.700 12.979 1.00 39.00 N -ANISOU 3955 N THR C 95 6412 3417 4989 -1675 869 -602 N -ATOM 3956 CA THR C 95 13.618 18.954 13.550 1.00 37.37 C -ANISOU 3956 CA THR C 95 5916 3498 4784 -1924 971 -711 C -ATOM 3957 C THR C 95 13.043 18.169 14.718 1.00 39.43 C -ANISOU 3957 C THR C 95 5881 3995 5106 -1636 991 -785 C -ATOM 3958 O THR C 95 11.956 18.494 15.196 1.00 36.30 O -ANISOU 3958 O THR C 95 5558 3504 4730 -1319 963 -819 O -ATOM 3959 CB THR C 95 14.774 19.857 13.978 1.00 39.44 C -ANISOU 3959 CB THR C 95 6403 3612 4969 -2255 990 -850 C -ATOM 3960 OG1 THR C 95 14.262 20.971 14.708 1.00 41.68 O -ANISOU 3960 OG1 THR C 95 6999 3602 5234 -2082 937 -928 O -ATOM 3961 CG2 THR C 95 15.521 20.382 12.742 1.00 47.54 C -ANISOU 3961 CG2 THR C 95 7660 4502 5901 -2621 1008 -779 C -ATOM 3962 N VAL C 96 13.741 17.129 15.157 1.00 33.90 N -ANISOU 3962 N VAL C 96 4851 3591 4438 -1751 1034 -822 N -ATOM 3963 CA VAL C 96 13.231 16.309 16.261 1.00 33.27 C -ANISOU 3963 CA VAL C 96 4540 3728 4373 -1530 1045 -857 C -ATOM 3964 C VAL C 96 14.218 16.274 17.417 1.00 34.82 C -ANISOU 3964 C VAL C 96 4684 4034 4511 -1696 1007 -977 C -ATOM 3965 O VAL C 96 15.418 16.498 17.235 1.00 36.90 O -ANISOU 3965 O VAL C 96 4946 4297 4778 -1983 983 -1042 O -ATOM 3966 CB VAL C 96 12.903 14.875 15.808 1.00 39.24 C -ANISOU 3966 CB VAL C 96 4946 4737 5227 -1442 1090 -749 C -ATOM 3967 CG1 VAL C 96 11.908 14.891 14.653 1.00 38.85 C -ANISOU 3967 CG1 VAL C 96 4927 4619 5216 -1288 1117 -645 C -ATOM 3968 CG2 VAL C 96 14.171 14.137 15.404 1.00 37.52 C -ANISOU 3968 CG2 VAL C 96 4490 4670 5096 -1718 1087 -752 C -ATOM 3969 N ASP C 97 13.709 16.034 18.621 1.00 35.60 N -ANISOU 3969 N ASP C 97 4748 4242 4538 -1539 1002 -1030 N -ATOM 3970 CA ASP C 97 14.581 15.803 19.768 1.00 37.77 C -ANISOU 3970 CA ASP C 97 4952 4673 4727 -1686 929 -1112 C -ATOM 3971 C ASP C 97 13.838 14.902 20.740 1.00 33.63 C -ANISOU 3971 C ASP C 97 4304 4348 4126 -1517 934 -1071 C -ATOM 3972 O ASP C 97 12.646 14.645 20.562 1.00 32.86 O -ANISOU 3972 O ASP C 97 4188 4253 4044 -1302 1028 -1035 O -ATOM 3973 CB ASP C 97 15.017 17.112 20.434 1.00 41.03 C -ANISOU 3973 CB ASP C 97 5639 4927 5023 -1824 916 -1290 C -ATOM 3974 CG ASP C 97 16.297 16.956 21.268 1.00 50.24 C -ANISOU 3974 CG ASP C 97 6711 6262 6117 -2063 807 -1384 C -ATOM 3975 OD1 ASP C 97 16.950 15.888 21.202 1.00 48.99 O -ANISOU 3975 OD1 ASP C 97 6274 6304 6036 -2117 713 -1309 O -ATOM 3976 OD2 ASP C 97 16.660 17.915 21.982 1.00 57.52 O -ANISOU 3976 OD2 ASP C 97 7825 7108 6921 -2192 802 -1553 O -ATOM 3977 N PHE C 98 14.552 14.409 21.742 1.00 34.33 N -ANISOU 3977 N PHE C 98 4314 4609 4122 -1633 825 -1081 N -ATOM 3978 CA PHE C 98 14.008 13.400 22.638 1.00 34.14 C -ANISOU 3978 CA PHE C 98 4203 4777 3992 -1543 808 -998 C -ATOM 3979 C PHE C 98 14.484 13.729 24.034 1.00 38.13 C -ANISOU 3979 C PHE C 98 4839 5380 4268 -1685 707 -1095 C -ATOM 3980 O PHE C 98 15.620 14.150 24.216 1.00 39.93 O -ANISOU 3980 O PHE C 98 5075 5607 4490 -1860 579 -1168 O -ATOM 3981 CB PHE C 98 14.522 12.020 22.250 1.00 32.72 C -ANISOU 3981 CB PHE C 98 3748 4722 3961 -1548 708 -827 C -ATOM 3982 CG PHE C 98 14.113 11.582 20.870 1.00 32.68 C -ANISOU 3982 CG PHE C 98 3584 4664 4170 -1448 818 -748 C -ATOM 3983 CD1 PHE C 98 14.881 11.929 19.759 1.00 32.59 C -ANISOU 3983 CD1 PHE C 98 3499 4564 4319 -1569 814 -784 C -ATOM 3984 CD2 PHE C 98 12.969 10.826 20.682 1.00 34.79 C -ANISOU 3984 CD2 PHE C 98 3775 4991 4454 -1275 938 -661 C -ATOM 3985 CE1 PHE C 98 14.506 11.528 18.484 1.00 28.38 C -ANISOU 3985 CE1 PHE C 98 2832 4010 3943 -1519 917 -717 C -ATOM 3986 CE2 PHE C 98 12.583 10.424 19.402 1.00 27.45 C -ANISOU 3986 CE2 PHE C 98 2687 4038 3703 -1200 1037 -602 C -ATOM 3987 CZ PHE C 98 13.356 10.781 18.312 1.00 27.03 C -ANISOU 3987 CZ PHE C 98 2576 3904 3791 -1323 1018 -623 C -ATOM 3988 N ILE C 99 13.620 13.550 25.018 1.00 37.42 N -ANISOU 3988 N ILE C 99 4849 5395 3975 -1639 774 -1122 N -ATOM 3989 CA ILE C 99 14.000 13.780 26.406 1.00 39.96 C -ANISOU 3989 CA ILE C 99 5311 5850 4023 -1811 681 -1208 C -ATOM 3990 C ILE C 99 13.291 12.783 27.305 1.00 40.59 C -ANISOU 3990 C ILE C 99 5413 6120 3889 -1814 696 -1103 C -ATOM 3991 O ILE C 99 12.254 12.245 26.926 1.00 39.28 O -ANISOU 3991 O ILE C 99 5188 5959 3778 -1672 855 -1054 O -ATOM 3992 CB ILE C 99 13.614 15.191 26.881 1.00 47.63 C -ANISOU 3992 CB ILE C 99 6502 6716 4878 -1853 819 -1483 C -ATOM 3993 CG1 ILE C 99 12.131 15.460 26.617 1.00 43.37 C -ANISOU 3993 CG1 ILE C 99 6002 6090 4387 -1647 1052 -1590 C -ATOM 3994 CG2 ILE C 99 14.502 16.257 26.241 1.00 55.05 C -ANISOU 3994 CG2 ILE C 99 7500 7457 5960 -1937 782 -1590 C -ATOM 3995 CD1 ILE C 99 11.635 16.759 27.224 1.00 48.36 C -ANISOU 3995 CD1 ILE C 99 6826 6614 4935 -1662 1186 -1903 C -ATOM 3996 N ARG C 100 13.874 12.533 28.478 1.00 42.88 N -ANISOU 3996 N ARG C 100 5801 6573 3920 -2001 521 -1070 N -ATOM 3997 CA AARG C 100 13.229 11.750 29.522 0.51 45.58 C -ANISOU 3997 CA AARG C 100 6263 7095 3962 -2092 536 -983 C -ATOM 3998 CA BARG C 100 13.230 11.746 29.520 0.49 45.62 C -ANISOU 3998 CA BARG C 100 6267 7099 3967 -2091 535 -983 C -ATOM 3999 C ARG C 100 13.113 12.646 30.738 1.00 48.30 C -ANISOU 3999 C ARG C 100 6833 7552 3967 -2298 593 -1216 C -ATOM 4000 O ARG C 100 13.956 13.521 30.943 1.00 49.65 O -ANISOU 4000 O ARG C 100 7045 7698 4122 -2399 493 -1353 O -ATOM 4001 CB AARG C 100 14.086 10.554 29.930 0.51 49.09 C -ANISOU 4001 CB AARG C 100 6667 7633 4351 -2166 215 -698 C -ATOM 4002 CB BARG C 100 14.069 10.517 29.896 0.49 49.67 C -ANISOU 4002 CB BARG C 100 6734 7703 4433 -2159 217 -691 C -ATOM 4003 CG AARG C 100 14.278 9.450 28.914 0.51 49.90 C -ANISOU 4003 CG AARG C 100 6535 7642 4782 -1994 132 -471 C -ATOM 4004 CG BARG C 100 14.493 9.620 28.739 0.49 50.49 C -ANISOU 4004 CG BARG C 100 6574 7693 4916 -1983 114 -497 C -ATOM 4005 CD AARG C 100 15.452 8.601 29.389 0.51 53.46 C -ANISOU 4005 CD AARG C 100 6937 8140 5235 -2057 -268 -262 C -ATOM 4006 CD BARG C 100 15.085 8.299 29.241 0.49 52.74 C -ANISOU 4006 CD BARG C 100 6839 8034 5166 -2018 -200 -215 C -ATOM 4007 NE AARG C 100 15.387 7.208 28.968 0.51 52.65 N -ANISOU 4007 NE AARG C 100 6705 7976 5324 -1940 -367 -7 N -ATOM 4008 NE BARG C 100 14.053 7.381 29.716 0.49 53.81 N -ANISOU 4008 NE BARG C 100 7123 8221 5100 -2047 -87 -57 N -ATOM 4009 CZ AARG C 100 16.182 6.670 28.052 0.51 51.02 C -ANISOU 4009 CZ AARG C 100 6209 7667 5508 -1811 -519 54 C -ATOM 4010 CZ BARG C 100 13.830 7.085 30.993 0.49 56.17 C -ANISOU 4010 CZ BARG C 100 7703 8653 4988 -2249 -172 32 C -ATOM 4011 NH1AARG C 100 17.105 7.411 27.455 0.51 48.11 N -ANISOU 4011 NH1AARG C 100 5657 7269 5353 -1810 -578 -124 N -ATOM 4012 NH1BARG C 100 14.577 7.623 31.945 0.49 62.77 N -ANISOU 4012 NH1BARG C 100 8686 9597 5567 -2422 -397 -13 N -ATOM 4013 NH2AARG C 100 16.053 5.391 27.734 0.51 52.42 N -ANISOU 4013 NH2AARG C 100 6280 7771 5866 -1709 -592 265 N -ATOM 4014 NH2BARG C 100 12.862 6.242 31.316 0.49 54.39 N -ANISOU 4014 NH2BARG C 100 7619 8463 4583 -2314 -25 159 N -ATOM 4015 N LEU C 101 12.086 12.430 31.551 1.00 48.17 N -ANISOU 4015 N LEU C 101 8370 6164 3767 -1427 -484 879 N -ATOM 4016 CA LEU C 101 11.965 13.175 32.804 1.00 53.23 C -ANISOU 4016 CA LEU C 101 8567 7346 4313 -1570 -519 782 C -ATOM 4017 C LEU C 101 12.251 12.298 34.024 1.00 58.59 C -ANISOU 4017 C LEU C 101 9225 8238 4799 -1637 -764 1026 C -ATOM 4018 O LEU C 101 11.904 11.120 34.039 1.00 62.71 O -ANISOU 4018 O LEU C 101 10086 8570 5172 -1767 -957 1337 O -ATOM 4019 CB LEU C 101 10.588 13.830 32.924 1.00 57.57 C -ANISOU 4019 CB LEU C 101 8990 8234 4650 -1827 -474 718 C -ATOM 4020 CG LEU C 101 10.371 15.139 32.164 1.00 58.84 C -ANISOU 4020 CG LEU C 101 9004 8371 4983 -1732 -227 398 C -ATOM 4021 CD1 LEU C 101 11.698 15.750 31.751 1.00 58.31 C -ANISOU 4021 CD1 LEU C 101 8803 8057 5294 -1466 -110 207 C -ATOM 4022 CD2 LEU C 101 9.476 14.962 30.954 1.00 59.00 C -ANISOU 4022 CD2 LEU C 101 9286 8146 4985 -1832 -124 467 C -ATOM 4023 N LYS C 102 12.897 12.880 35.034 1.00 62.56 N -ANISOU 4023 N LYS C 102 9357 9104 5307 -1557 -797 896 N -ATOM 4024 CA LYS C 102 13.150 12.190 36.303 1.00 73.03 C -ANISOU 4024 CA LYS C 102 10592 10738 6417 -1602 -1016 1113 C -ATOM 4025 C LYS C 102 12.713 13.037 37.497 1.00 77.21 C -ANISOU 4025 C LYS C 102 10754 11889 6692 -1677 -1076 952 C -ATOM 4026 O LYS C 102 12.690 14.268 37.427 1.00 78.63 O -ANISOU 4026 O LYS C 102 10748 12177 6949 -1607 -983 595 O -ATOM 4027 CB LYS C 102 14.620 11.817 36.429 1.00 74.38 C -ANISOU 4027 CB LYS C 102 10722 10752 6787 -1325 -1052 1163 C -ATOM 4028 N LYS C 114 14.093 16.116 36.809 1.00 65.63 N -ANISOU 4028 N LYS C 114 8845 10228 5866 -1407 -902 59 N -ATOM 4029 CA LYS C 114 15.060 16.789 35.940 1.00 67.09 C -ANISOU 4029 CA LYS C 114 8924 10068 6499 -1328 -816 -47 C -ATOM 4030 C LYS C 114 15.074 16.220 34.512 1.00 63.98 C -ANISOU 4030 C LYS C 114 8741 9265 6304 -1235 -565 142 C -ATOM 4031 O LYS C 114 14.900 15.017 34.316 1.00 64.68 O -ANISOU 4031 O LYS C 114 9088 9235 6254 -1191 -552 397 O -ATOM 4032 CB LYS C 114 16.451 16.715 36.550 1.00 69.81 C -ANISOU 4032 CB LYS C 114 9018 10495 7011 -1265 -1002 41 C -ATOM 4033 N VAL C 115 15.287 17.092 33.527 1.00 63.71 N -ANISOU 4033 N VAL C 115 8631 9000 6577 -1189 -403 20 N -ATOM 4034 CA VAL C 115 15.380 16.690 32.120 1.00 64.02 C -ANISOU 4034 CA VAL C 115 8848 8695 6780 -1020 -154 173 C -ATOM 4035 C VAL C 115 16.695 15.967 31.839 1.00 68.65 C -ANISOU 4035 C VAL C 115 9368 9197 7517 -738 -126 457 C -ATOM 4036 O VAL C 115 17.771 16.504 32.104 1.00 72.60 O -ANISOU 4036 O VAL C 115 9495 9837 8254 -702 -189 520 O -ATOM 4037 CB VAL C 115 15.270 17.905 31.164 1.00 75.15 C -ANISOU 4037 CB VAL C 115 10135 9949 8469 -1028 24 9 C -ATOM 4038 CG1 VAL C 115 15.609 17.506 29.726 1.00 75.00 C -ANISOU 4038 CG1 VAL C 115 10241 9650 8607 -763 286 202 C -ATOM 4039 CG2 VAL C 115 13.883 18.523 31.229 1.00 72.59 C -ANISOU 4039 CG2 VAL C 115 9938 9697 7946 -1198 52 -240 C -ATOM 4040 N ILE C 116 16.605 14.751 31.303 1.00 66.32 N -ANISOU 4040 N ILE C 116 9451 8681 7065 -522 -64 651 N -ATOM 4041 CA ILE C 116 17.797 13.975 30.964 1.00 65.70 C -ANISOU 4041 CA ILE C 116 9389 8533 7041 -108 -11 928 C -ATOM 4042 C ILE C 116 17.876 13.694 29.460 1.00 63.53 C -ANISOU 4042 C ILE C 116 9388 7951 6800 275 237 1009 C -ATOM 4043 O ILE C 116 16.851 13.542 28.781 1.00 55.49 O -ANISOU 4043 O ILE C 116 8751 6668 5664 195 283 884 O -ATOM 4044 CB ILE C 116 17.904 12.677 31.819 1.00 58.90 C -ANISOU 4044 CB ILE C 116 8795 7674 5909 -43 -226 1106 C -ATOM 4045 CG1 ILE C 116 18.488 11.511 31.021 1.00 57.94 C -ANISOU 4045 CG1 ILE C 116 9087 7245 5683 480 -157 1339 C -ATOM 4046 CG2 ILE C 116 16.552 12.304 32.408 1.00 62.61 C -ANISOU 4046 CG2 ILE C 116 9552 8121 6115 -431 -404 1024 C -ATOM 4047 CD1 ILE C 116 18.576 10.211 31.802 1.00 63.07 C -ANISOU 4047 CD1 ILE C 116 10083 7803 6077 558 -403 1532 C -ATOM 4048 N GLY C 117 19.100 13.662 28.941 1.00 68.38 N -ANISOU 4048 N GLY C 117 9771 8662 7547 714 392 1247 N -ATOM 4049 CA GLY C 117 19.320 13.481 27.521 1.00 69.63 C -ANISOU 4049 CA GLY C 117 10124 8639 7694 1198 656 1352 C -ATOM 4050 C GLY C 117 18.858 14.711 26.773 1.00 70.55 C -ANISOU 4050 C GLY C 117 9995 8762 8049 985 840 1210 C -ATOM 4051 O GLY C 117 18.625 15.763 27.373 1.00 72.71 O -ANISOU 4051 O GLY C 117 9904 9188 8536 524 755 1064 O -ATOM 4052 N GLY C 118 18.719 14.583 25.460 1.00 69.82 N -ANISOU 4052 N GLY C 118 10146 8489 7892 1360 1072 1243 N -ATOM 4053 CA GLY C 118 18.256 15.694 24.651 1.00 66.94 C -ANISOU 4053 CA GLY C 118 9577 8121 7738 1201 1267 1142 C -ATOM 4054 C GLY C 118 19.356 16.682 24.325 1.00 65.88 C -ANISOU 4054 C GLY C 118 8760 8320 7951 1307 1440 1434 C -ATOM 4055 O GLY C 118 20.401 16.716 24.980 1.00 63.54 O -ANISOU 4055 O GLY C 118 8046 8314 7781 1331 1351 1686 O -ATOM 4056 N ASP C 119 19.123 17.481 23.292 1.00 66.22 N -ANISOU 4056 N ASP C 119 8666 8343 8150 1346 1668 1456 N -ATOM 4057 CA ASP C 119 20.073 18.510 22.913 1.00 69.85 C -ANISOU 4057 CA ASP C 119 8448 9112 8980 1355 1801 1810 C -ATOM 4058 C ASP C 119 20.078 19.600 23.967 1.00 70.76 C -ANISOU 4058 C ASP C 119 8184 9265 9436 690 1513 1693 C -ATOM 4059 O ASP C 119 19.159 19.682 24.785 1.00 67.92 O -ANISOU 4059 O ASP C 119 8112 8713 8983 306 1300 1288 O -ATOM 4060 CB ASP C 119 19.706 19.106 21.551 1.00 67.06 C -ANISOU 4060 CB ASP C 119 8076 8707 8698 1538 2102 1867 C -ATOM 4061 CG ASP C 119 19.891 18.122 20.416 1.00 70.40 C -ANISOU 4061 CG ASP C 119 8848 9144 8759 2308 2374 2016 C -ATOM 4062 OD1 ASP C 119 20.610 17.123 20.612 1.00 72.15 O -ANISOU 4062 OD1 ASP C 119 9194 9483 8736 2772 2358 2188 O -ATOM 4063 OD2 ASP C 119 19.326 18.359 19.327 1.00 72.25 O -ANISOU 4063 OD2 ASP C 119 9260 9271 8922 2495 2590 1953 O -ATOM 4064 N ASP C 120 21.130 20.412 23.958 1.00 76.77 N -ANISOU 4064 N ASP C 120 8309 10299 10562 577 1474 2082 N -ATOM 4065 CA ASP C 120 21.148 21.636 24.735 1.00 80.64 C -ANISOU 4065 CA ASP C 120 8499 10728 11414 -52 1143 1972 C -ATOM 4066 C ASP C 120 19.836 22.335 24.411 1.00 78.10 C -ANISOU 4066 C ASP C 120 8528 10052 11093 -283 1184 1541 C -ATOM 4067 O ASP C 120 19.549 22.605 23.246 1.00 78.51 O -ANISOU 4067 O ASP C 120 8593 10046 11192 -85 1476 1643 O -ATOM 4068 CB ASP C 120 22.327 22.508 24.302 1.00 86.95 C -ANISOU 4068 CB ASP C 120 8588 11803 12647 -154 1122 2551 C -ATOM 4069 CG ASP C 120 22.727 23.525 25.354 1.00 90.53 C -ANISOU 4069 CG ASP C 120 8737 12201 13458 -802 620 2525 C -ATOM 4070 OD1 ASP C 120 21.908 24.416 25.671 1.00 88.38 O -ANISOU 4070 OD1 ASP C 120 8719 11560 13300 -1199 401 2099 O -ATOM 4071 OD2 ASP C 120 23.872 23.440 25.848 1.00 95.52 O -ANISOU 4071 OD2 ASP C 120 8893 13167 14233 -883 420 2940 O -ATOM 4072 N LEU C 121 19.022 22.600 25.428 1.00 74.55 N -ANISOU 4072 N LEU C 121 8360 9424 10542 -638 911 1079 N -ATOM 4073 CA LEU C 121 17.693 23.161 25.193 1.00 67.56 C -ANISOU 4073 CA LEU C 121 7821 8285 9563 -774 969 680 C -ATOM 4074 C LEU C 121 17.728 24.572 24.595 1.00 63.61 C -ANISOU 4074 C LEU C 121 7086 7625 9457 -980 957 748 C -ATOM 4075 O LEU C 121 16.685 25.171 24.336 1.00 60.05 O -ANISOU 4075 O LEU C 121 6889 6975 8951 -1054 1016 451 O -ATOM 4076 CB LEU C 121 16.843 23.113 26.465 1.00 65.03 C -ANISOU 4076 CB LEU C 121 7808 7931 8970 -1009 696 233 C -ATOM 4077 CG LEU C 121 16.421 21.718 26.926 1.00 65.00 C -ANISOU 4077 CG LEU C 121 8121 8036 8539 -850 727 167 C -ATOM 4078 CD1 LEU C 121 15.325 21.803 27.974 1.00 65.10 C -ANISOU 4078 CD1 LEU C 121 8393 8099 8243 -1055 534 -210 C -ATOM 4079 CD2 LEU C 121 15.970 20.869 25.747 1.00 62.24 C -ANISOU 4079 CD2 LEU C 121 8050 7591 8005 -533 1052 278 C -ATOM 4080 N SER C 122 18.934 25.089 24.371 1.00 63.20 N -ANISOU 4080 N SER C 122 6530 7684 9799 -1077 868 1196 N -ATOM 4081 CA SER C 122 19.116 26.335 23.640 1.00 64.75 C -ANISOU 4081 CA SER C 122 6454 7733 10415 -1275 856 1417 C -ATOM 4082 C SER C 122 18.753 26.126 22.167 1.00 60.78 C -ANISOU 4082 C SER C 122 5971 7284 9838 -881 1354 1610 C -ATOM 4083 O SER C 122 18.569 27.084 21.420 1.00 58.62 O -ANISOU 4083 O SER C 122 5575 6869 9829 -982 1429 1733 O -ATOM 4084 CB SER C 122 20.556 26.837 23.779 1.00 69.08 C -ANISOU 4084 CB SER C 122 6382 8462 11401 -1529 596 1982 C -ATOM 4085 OG SER C 122 21.475 25.767 23.697 1.00 69.35 O -ANISOU 4085 OG SER C 122 6125 8932 11294 -1186 775 2390 O -ATOM 4086 N THR C 123 18.651 24.861 21.761 1.00 56.35 N -ANISOU 4086 N THR C 123 5611 6904 8897 -416 1655 1631 N -ATOM 4087 CA THR C 123 18.187 24.514 20.423 1.00 55.69 C -ANISOU 4087 CA THR C 123 5686 6844 8628 18 2080 1713 C -ATOM 4088 C THR C 123 16.715 24.873 20.268 1.00 50.29 C -ANISOU 4088 C THR C 123 5454 5868 7787 -119 2124 1232 C -ATOM 4089 O THR C 123 16.216 25.015 19.154 1.00 48.00 O -ANISOU 4089 O THR C 123 5249 5549 7438 105 2415 1277 O -ATOM 4090 CB THR C 123 18.380 23.021 20.121 1.00 57.50 C -ANISOU 4090 CB THR C 123 6178 7237 8434 564 2282 1775 C -ATOM 4091 OG1 THR C 123 17.695 22.238 21.104 1.00 57.15 O -ANISOU 4091 OG1 THR C 123 6601 7032 8083 427 2072 1350 O -ATOM 4092 CG2 THR C 123 19.851 22.663 20.137 1.00 64.31 C -ANISOU 4092 CG2 THR C 123 6557 8485 9393 838 2310 2317 C -ATOM 4093 N LEU C 124 16.023 25.013 21.396 1.00 44.32 N -ANISOU 4093 N LEU C 124 4958 4958 6922 -445 1839 803 N -ATOM 4094 CA LEU C 124 14.625 25.429 21.392 1.00 38.84 C -ANISOU 4094 CA LEU C 124 4622 4090 6045 -560 1863 395 C -ATOM 4095 C LEU C 124 14.495 26.947 21.329 1.00 39.94 C -ANISOU 4095 C LEU C 124 4613 4028 6535 -814 1745 346 C -ATOM 4096 O LEU C 124 13.406 27.472 21.095 1.00 42.07 O -ANISOU 4096 O LEU C 124 5122 4178 6685 -823 1824 83 O -ATOM 4097 CB LEU C 124 13.899 24.916 22.641 1.00 36.35 C -ANISOU 4097 CB LEU C 124 4623 3802 5387 -716 1629 14 C -ATOM 4098 CG LEU C 124 14.076 23.441 23.001 1.00 36.63 C -ANISOU 4098 CG LEU C 124 4838 3971 5109 -563 1617 66 C -ATOM 4099 CD1 LEU C 124 13.227 23.076 24.210 1.00 34.10 C -ANISOU 4099 CD1 LEU C 124 4773 3728 4456 -760 1391 -243 C -ATOM 4100 CD2 LEU C 124 13.719 22.574 21.818 1.00 37.06 C -ANISOU 4100 CD2 LEU C 124 5143 3995 4943 -236 1903 180 C -ATOM 4101 N THR C 125 15.599 27.657 21.551 1.00 41.98 N -ANISOU 4101 N THR C 125 4489 4240 7220 -1030 1517 628 N -ATOM 4102 CA THR C 125 15.511 29.107 21.690 1.00 45.44 C -ANISOU 4102 CA THR C 125 4887 4371 8005 -1340 1255 554 C -ATOM 4103 C THR C 125 14.990 29.743 20.410 1.00 48.26 C -ANISOU 4103 C THR C 125 5228 4626 8485 -1205 1569 690 C -ATOM 4104 O THR C 125 15.552 29.536 19.333 1.00 50.86 O -ANISOU 4104 O THR C 125 5237 5137 8950 -1009 1869 1153 O -ATOM 4105 CB THR C 125 16.849 29.738 22.099 1.00 52.47 C -ANISOU 4105 CB THR C 125 5356 5204 9376 -1687 869 925 C -ATOM 4106 OG1 THR C 125 17.273 29.183 23.352 1.00 54.74 O -ANISOU 4106 OG1 THR C 125 5681 5598 9519 -1809 553 760 O -ATOM 4107 CG2 THR C 125 16.701 31.237 22.247 1.00 56.61 C -ANISOU 4107 CG2 THR C 125 5967 5285 10257 -2035 498 822 C -ATOM 4108 N GLY C 126 13.897 30.493 20.530 1.00 47.69 N -ANISOU 4108 N GLY C 126 5498 4314 8308 -1244 1518 299 N -ATOM 4109 CA GLY C 126 13.314 31.185 19.395 1.00 48.72 C -ANISOU 4109 CA GLY C 126 5639 4333 8540 -1120 1791 398 C -ATOM 4110 C GLY C 126 12.634 30.262 18.399 1.00 50.41 C -ANISOU 4110 C GLY C 126 5945 4818 8391 -750 2276 428 C -ATOM 4111 O GLY C 126 12.357 30.661 17.271 1.00 54.02 O -ANISOU 4111 O GLY C 126 6335 5295 8894 -569 2511 599 O -ATOM 4112 N LYS C 127 12.356 29.028 18.810 1.00 48.38 N -ANISOU 4112 N LYS C 127 5884 4771 7728 -620 2331 252 N -ATOM 4113 CA ALYS C 127 11.727 28.066 17.913 0.73 45.38 C -ANISOU 4113 CA ALYS C 127 5691 4579 6971 -298 2631 256 C -ATOM 4114 CA BLYS C 127 11.737 28.042 17.931 0.27 46.01 C -ANISOU 4114 CA BLYS C 127 5772 4661 7049 -300 2630 256 C -ATOM 4115 C LYS C 127 10.284 27.769 18.312 1.00 42.07 C -ANISOU 4115 C LYS C 127 5663 4206 6114 -318 2560 -138 C -ATOM 4116 O LYS C 127 9.857 28.072 19.429 1.00 42.69 O -ANISOU 4116 O LYS C 127 5855 4266 6097 -515 2421 -418 O -ATOM 4117 CB ALYS C 127 12.536 26.763 17.868 0.73 47.94 C -ANISOU 4117 CB ALYS C 127 5984 5079 7150 -97 2656 450 C -ATOM 4118 CB BLYS C 127 12.529 26.732 17.980 0.27 47.86 C -ANISOU 4118 CB BLYS C 127 5983 5067 7135 -119 2653 433 C -ATOM 4119 CG ALYS C 127 13.956 26.919 17.339 0.73 53.12 C -ANISOU 4119 CG ALYS C 127 6199 5854 8128 44 2697 931 C -ATOM 4120 CG BLYS C 127 14.022 26.887 17.723 0.27 52.31 C -ANISOU 4120 CG BLYS C 127 6083 5731 8062 -50 2678 904 C -ATOM 4121 CD ALYS C 127 13.967 27.268 15.854 0.73 55.06 C -ANISOU 4121 CD ALYS C 127 6389 6179 8352 349 2741 1127 C -ATOM 4122 CD BLYS C 127 14.317 27.500 16.355 0.27 55.35 C -ANISOU 4122 CD BLYS C 127 6275 6197 8559 194 2714 1188 C -ATOM 4123 CE ALYS C 127 15.381 27.488 15.348 0.73 58.93 C -ANISOU 4123 CE ALYS C 127 6408 6878 9104 495 2766 1653 C -ATOM 4124 CE BLYS C 127 13.812 26.625 15.212 0.27 54.54 C -ANISOU 4124 CE BLYS C 127 6497 6182 8043 602 2765 1123 C -ATOM 4125 NZ ALYS C 127 15.526 28.812 14.672 0.73 60.95 N -ANISOU 4125 NZ ALYS C 127 6399 7087 9674 383 2716 1878 N -ATOM 4126 NZ BLYS C 127 12.397 26.933 14.843 0.27 51.11 N -ANISOU 4126 NZ BLYS C 127 6387 5614 7417 522 2674 799 N -ATOM 4127 N ASN C 128 9.529 27.187 17.386 1.00 39.58 N -ANISOU 4127 N ASN C 128 5747 4127 5165 -599 830 949 N -ATOM 4128 CA ASN C 128 8.181 26.708 17.687 1.00 41.56 C -ANISOU 4128 CA ASN C 128 6015 4432 5342 -472 655 773 C -ATOM 4129 C ASN C 128 8.278 25.266 18.163 1.00 38.41 C -ANISOU 4129 C ASN C 128 5557 4167 4872 -440 812 549 C -ATOM 4130 O ASN C 128 8.647 24.382 17.394 1.00 43.02 O -ANISOU 4130 O ASN C 128 6261 4849 5238 -487 1036 536 O -ATOM 4131 CB ASN C 128 7.289 26.756 16.447 1.00 48.67 C -ANISOU 4131 CB ASN C 128 7092 5448 5953 -498 536 908 C -ATOM 4132 CG ASN C 128 6.635 28.106 16.236 1.00 53.55 C -ANISOU 4132 CG ASN C 128 7732 5915 6700 -418 291 1143 C -ATOM 4133 OD1 ASN C 128 7.146 29.141 16.669 1.00 53.52 O -ANISOU 4133 OD1 ASN C 128 7724 5654 6957 -404 295 1233 O -ATOM 4134 ND2 ASN C 128 5.486 28.100 15.560 1.00 56.50 N -ANISOU 4134 ND2 ASN C 128 8132 6440 6894 -378 71 1267 N -ATOM 4135 N VAL C 129 7.946 25.025 19.424 1.00 32.32 N -ANISOU 4135 N VAL C 129 4645 3368 4268 -361 730 376 N -ATOM 4136 CA VAL C 129 8.171 23.714 20.023 1.00 29.69 C -ANISOU 4136 CA VAL C 129 4257 3113 3913 -324 882 222 C -ATOM 4137 C VAL C 129 6.854 22.965 20.165 1.00 32.56 C -ANISOU 4137 C VAL C 129 4677 3552 4142 -307 791 45 C -ATOM 4138 O VAL C 129 5.871 23.513 20.679 1.00 26.87 O -ANISOU 4138 O VAL C 129 3876 2830 3501 -259 591 -5 O -ATOM 4139 CB VAL C 129 8.886 23.822 21.390 1.00 31.63 C -ANISOU 4139 CB VAL C 129 4303 3326 4388 -309 859 199 C -ATOM 4140 CG1 VAL C 129 9.146 22.443 21.983 1.00 30.53 C -ANISOU 4140 CG1 VAL C 129 4105 3258 4237 -237 1011 124 C -ATOM 4141 CG2 VAL C 129 10.201 24.554 21.231 1.00 35.89 C -ANISOU 4141 CG2 VAL C 129 4732 3843 5061 -407 916 403 C -ATOM 4142 N LEU C 130 6.838 21.726 19.679 1.00 29.33 N -ANISOU 4142 N LEU C 130 4416 3191 3537 -356 971 -45 N -ATOM 4143 CA LEU C 130 5.701 20.830 19.878 1.00 29.48 C -ANISOU 4143 CA LEU C 130 4496 3280 3425 -424 907 -218 C -ATOM 4144 C LEU C 130 6.146 19.722 20.826 1.00 25.00 C -ANISOU 4144 C LEU C 130 3915 2633 2951 -361 1101 -321 C -ATOM 4145 O LEU C 130 6.998 18.903 20.479 1.00 28.47 O -ANISOU 4145 O LEU C 130 4489 2977 3353 -324 1387 -311 O -ATOM 4146 CB LEU C 130 5.265 20.226 18.535 1.00 32.74 C -ANISOU 4146 CB LEU C 130 5191 3768 3482 -617 955 -257 C -ATOM 4147 CG LEU C 130 3.835 19.701 18.272 1.00 36.91 C -ANISOU 4147 CG LEU C 130 5775 4458 3791 -826 751 -363 C -ATOM 4148 CD1 LEU C 130 3.838 18.313 17.586 1.00 36.37 C -ANISOU 4148 CD1 LEU C 130 6089 4335 3395 -1065 975 -552 C -ATOM 4149 CD2 LEU C 130 2.942 19.725 19.493 1.00 34.77 C -ANISOU 4149 CD2 LEU C 130 5224 4249 3738 -757 589 -424 C -ATOM 4150 N ILE C 131 5.599 19.706 22.035 1.00 26.01 N -ANISOU 4150 N ILE C 131 3888 2789 3208 -325 977 -392 N -ATOM 4151 CA ILE C 131 5.938 18.662 22.991 1.00 28.11 C -ANISOU 4151 CA ILE C 131 4150 2991 3538 -277 1123 -435 C -ATOM 4152 C ILE C 131 4.948 17.530 22.815 1.00 27.12 C -ANISOU 4152 C ILE C 131 4206 2859 3240 -424 1179 -586 C -ATOM 4153 O ILE C 131 3.736 17.761 22.803 1.00 29.25 O -ANISOU 4153 O ILE C 131 4412 3265 3436 -548 993 -663 O -ATOM 4154 CB ILE C 131 5.851 19.173 24.433 1.00 27.45 C -ANISOU 4154 CB ILE C 131 3867 2959 3604 -226 975 -437 C -ATOM 4155 CG1 ILE C 131 6.913 20.242 24.672 1.00 29.15 C -ANISOU 4155 CG1 ILE C 131 3946 3164 3966 -176 905 -304 C -ATOM 4156 CG2 ILE C 131 6.053 18.028 25.415 1.00 30.11 C -ANISOU 4156 CG2 ILE C 131 4221 3265 3956 -203 1089 -433 C -ATOM 4157 CD1 ILE C 131 6.763 20.959 25.997 1.00 27.69 C -ANISOU 4157 CD1 ILE C 131 3660 3012 3850 -203 744 -362 C -ATOM 4158 N VAL C 132 5.453 16.308 22.674 1.00 24.92 N -ANISOU 4158 N VAL C 132 4142 2410 2916 -416 1451 -610 N -ATOM 4159 CA VAL C 132 4.568 15.174 22.428 1.00 30.54 C -ANISOU 4159 CA VAL C 132 5115 3049 3441 -632 1532 -774 C -ATOM 4160 C VAL C 132 4.640 14.173 23.579 1.00 31.91 C -ANISOU 4160 C VAL C 132 5315 3082 3728 -577 1665 -759 C -ATOM 4161 O VAL C 132 5.694 13.595 23.845 1.00 30.74 O -ANISOU 4161 O VAL C 132 5216 2746 3719 -368 1892 -626 O -ATOM 4162 CB VAL C 132 4.907 14.462 21.113 1.00 28.43 C -ANISOU 4162 CB VAL C 132 5203 2620 2978 -733 1755 -831 C -ATOM 4163 CG1 VAL C 132 3.929 13.330 20.850 1.00 28.94 C -ANISOU 4163 CG1 VAL C 132 5508 2625 2864 -1040 1745 -955 C -ATOM 4164 CG2 VAL C 132 4.895 15.435 19.932 1.00 29.18 C -ANISOU 4164 CG2 VAL C 132 5350 2864 2874 -817 1668 -838 C -ATOM 4165 N GLU C 133 3.496 13.944 24.217 1.00 29.15 N -ANISOU 4165 N GLU C 133 4906 2842 3327 -764 1523 -844 N -ATOM 4166 CA GLU C 133 3.407 13.148 25.434 1.00 30.66 C -ANISOU 4166 CA GLU C 133 5102 2949 3597 -751 1605 -796 C -ATOM 4167 C GLU C 133 2.420 11.994 25.243 1.00 30.46 C -ANISOU 4167 C GLU C 133 5347 2814 3411 -1076 1698 -940 C -ATOM 4168 O GLU C 133 1.545 12.064 24.372 1.00 30.17 O -ANISOU 4168 O GLU C 133 5349 2911 3203 -1350 1571 -1059 O -ATOM 4169 CB GLU C 133 2.958 14.079 26.573 1.00 30.91 C -ANISOU 4169 CB GLU C 133 4796 3241 3707 -704 1380 -759 C -ATOM 4170 CG GLU C 133 2.854 13.472 27.951 1.00 41.25 C -ANISOU 4170 CG GLU C 133 6091 4542 5039 -711 1431 -685 C -ATOM 4171 CD GLU C 133 4.185 13.001 28.499 1.00 43.93 C -ANISOU 4171 CD GLU C 133 6480 4720 5490 -486 1546 -461 C -ATOM 4172 OE1 GLU C 133 4.697 11.987 27.987 1.00 39.33 O -ANISOU 4172 OE1 GLU C 133 6136 3862 4947 -421 1778 -396 O -ATOM 4173 OE2 GLU C 133 4.705 13.630 29.453 1.00 43.28 O -ANISOU 4173 OE2 GLU C 133 6206 4788 5452 -384 1410 -338 O -ATOM 4174 N ASP C 134 2.566 10.913 26.012 1.00 29.14 N -ANISOU 4174 N ASP C 134 5358 2419 3294 -1076 1890 -876 N -ATOM 4175 CA ASP C 134 1.582 9.831 25.954 1.00 30.17 C -ANISOU 4175 CA ASP C 134 5697 2487 3280 -1419 1944 -952 C -ATOM 4176 C ASP C 134 0.320 10.124 26.786 1.00 32.56 C -ANISOU 4176 C ASP C 134 5759 3063 3550 -1687 1767 -1020 C -ATOM 4177 O ASP C 134 -0.808 9.867 26.338 1.00 34.82 O -ANISOU 4177 O ASP C 134 6023 3519 3686 -2040 1661 -1122 O -ATOM 4178 CB ASP C 134 2.195 8.470 26.341 1.00 32.74 C -ANISOU 4178 CB ASP C 134 6335 2450 3654 -1304 2245 -828 C -ATOM 4179 CG ASP C 134 2.875 8.485 27.711 1.00 34.93 C -ANISOU 4179 CG ASP C 134 6519 2609 4142 -1042 2306 -613 C -ATOM 4180 OD1 ASP C 134 3.125 9.571 28.272 1.00 33.66 O -ANISOU 4180 OD1 ASP C 134 5996 2745 4050 -884 2092 -527 O -ATOM 4181 OD2 ASP C 134 3.181 7.387 28.219 1.00 39.77 O -ANISOU 4181 OD2 ASP C 134 7329 2978 4803 -944 2489 -466 O -ATOM 4182 N ILE C 135 0.505 10.654 27.986 1.00 33.26 N -ANISOU 4182 N ILE C 135 5575 3311 3753 -1473 1703 -883 N -ATOM 4183 CA ILE C 135 -0.631 10.813 28.895 1.00 30.70 C -ANISOU 4183 CA ILE C 135 5003 3269 3392 -1661 1621 -897 C -ATOM 4184 C ILE C 135 -0.450 11.948 29.890 1.00 31.34 C -ANISOU 4184 C ILE C 135 4770 3595 3543 -1406 1515 -836 C -ATOM 4185 O ILE C 135 0.643 12.167 30.426 1.00 32.13 O -ANISOU 4185 O ILE C 135 4905 3606 3697 -1156 1522 -712 O -ATOM 4186 CB ILE C 135 -0.954 9.467 29.602 1.00 38.94 C -ANISOU 4186 CB ILE C 135 6305 4111 4381 -1899 1816 -829 C -ATOM 4187 CG1 ILE C 135 -2.203 9.584 30.481 1.00 36.70 C -ANISOU 4187 CG1 ILE C 135 5748 4157 4041 -2142 1783 -839 C -ATOM 4188 CG2 ILE C 135 0.247 8.969 30.405 1.00 40.31 C -ANISOU 4188 CG2 ILE C 135 6666 4016 4636 -1607 1959 -604 C -ATOM 4189 CD1 ILE C 135 -2.730 8.232 30.918 1.00 39.27 C -ANISOU 4189 CD1 ILE C 135 6313 4325 4284 -2388 1889 -791 C -ATOM 4190 N ILE C 136 -1.523 12.701 30.112 1.00 30.01 N -ANISOU 4190 N ILE C 136 4288 3740 3373 -1480 1424 -920 N -ATOM 4191 CA ILE C 136 -1.529 13.685 31.180 1.00 30.34 C -ANISOU 4191 CA ILE C 136 4124 3963 3442 -1289 1410 -922 C -ATOM 4192 C ILE C 136 -2.469 13.141 32.239 1.00 31.08 C -ANISOU 4192 C ILE C 136 4154 4213 3442 -1493 1561 -914 C -ATOM 4193 O ILE C 136 -3.587 12.709 31.917 1.00 34.74 O -ANISOU 4193 O ILE C 136 4478 4819 3902 -1752 1593 -947 O -ATOM 4194 CB ILE C 136 -2.035 15.068 30.713 1.00 29.53 C -ANISOU 4194 CB ILE C 136 3722 4050 3449 -1131 1286 -1011 C -ATOM 4195 CG1 ILE C 136 -1.199 15.614 29.543 1.00 31.29 C -ANISOU 4195 CG1 ILE C 136 4015 4134 3741 -982 1140 -992 C -ATOM 4196 CG2 ILE C 136 -2.079 16.056 31.915 1.00 31.56 C -ANISOU 4196 CG2 ILE C 136 3868 4413 3710 -952 1356 -1072 C -ATOM 4197 CD1 ILE C 136 0.246 15.901 29.877 1.00 32.78 C -ANISOU 4197 CD1 ILE C 136 4360 4145 3952 -791 1133 -925 C -ATOM 4198 N ASP C 137 -2.023 13.129 33.495 1.00 33.92 N -ANISOU 4198 N ASP C 137 4612 4578 3697 -1428 1644 -847 N -ATOM 4199 CA ASP C 137 -2.853 12.641 34.587 1.00 38.66 C -ANISOU 4199 CA ASP C 137 5189 5340 4160 -1630 1827 -821 C -ATOM 4200 C ASP C 137 -3.081 13.769 35.590 1.00 36.66 C -ANISOU 4200 C ASP C 137 4797 5287 3845 -1461 1856 -920 C -ATOM 4201 O ASP C 137 -4.112 14.431 35.564 1.00 38.69 O -ANISOU 4201 O ASP C 137 4777 5730 4194 -1409 1917 -1031 O -ATOM 4202 CB ASP C 137 -2.202 11.418 35.249 1.00 37.74 C -ANISOU 4202 CB ASP C 137 5403 5012 3923 -1729 1883 -606 C -ATOM 4203 CG ASP C 137 -3.045 10.825 36.363 1.00 43.20 C -ANISOU 4203 CG ASP C 137 6100 5828 4484 -1906 1985 -536 C -ATOM 4204 OD1 ASP C 137 -4.262 11.118 36.441 1.00 43.26 O -ANISOU 4204 OD1 ASP C 137 5847 6067 4524 -2000 2043 -650 O -ATOM 4205 OD2 ASP C 137 -2.480 10.046 37.165 1.00 46.82 O -ANISOU 4205 OD2 ASP C 137 6810 6165 4815 -1940 2019 -323 O -ATOM 4206 N THR C 138 -2.117 13.999 36.468 1.00 34.15 N -ANISOU 4206 N THR C 138 4684 4928 3364 -1384 1825 -867 N -ATOM 4207 CA THR C 138 -2.249 15.078 37.441 1.00 39.15 C -ANISOU 4207 CA THR C 138 5299 5692 3886 -1280 1858 -1001 C -ATOM 4208 C THR C 138 -1.912 16.381 36.736 1.00 38.70 C -ANISOU 4208 C THR C 138 5145 5570 3989 -1059 1763 -1163 C -ATOM 4209 O THR C 138 -2.377 17.447 37.124 1.00 40.41 O -ANISOU 4209 O THR C 138 5298 5822 4235 -926 1832 -1317 O -ATOM 4210 CB THR C 138 -1.280 14.905 38.613 1.00 40.09 C -ANISOU 4210 CB THR C 138 5702 5833 3698 -1367 1810 -886 C -ATOM 4211 OG1 THR C 138 0.068 14.914 38.113 1.00 35.67 O -ANISOU 4211 OG1 THR C 138 5238 5143 3172 -1295 1602 -757 O -ATOM 4212 CG2 THR C 138 -1.552 13.599 39.337 1.00 43.94 C -ANISOU 4212 CG2 THR C 138 6317 6349 4028 -1564 1894 -664 C -ATOM 4213 N GLY C 139 -1.100 16.279 35.689 1.00 32.93 N -ANISOU 4213 N GLY C 139 4430 4693 3390 -997 1603 -1096 N -ATOM 4214 CA GLY C 139 -0.625 17.450 34.972 1.00 34.91 C -ANISOU 4214 CA GLY C 139 4621 4839 3803 -803 1464 -1187 C -ATOM 4215 C GLY C 139 0.680 18.010 35.514 1.00 38.21 C -ANISOU 4215 C GLY C 139 5225 5184 4109 -793 1309 -1157 C -ATOM 4216 O GLY C 139 1.244 18.955 34.961 1.00 31.79 O -ANISOU 4216 O GLY C 139 4399 4258 3421 -686 1185 -1205 O -ATOM 4217 N LYS C 140 1.182 17.429 36.597 1.00 38.36 N -ANISOU 4217 N LYS C 140 5409 5287 3877 -943 1291 -1041 N -ATOM 4218 CA ALYS C 140 2.415 17.915 37.210 0.72 41.25 C -ANISOU 4218 CA ALYS C 140 5912 5670 4091 -1014 1084 -966 C -ATOM 4219 CA BLYS C 140 2.409 17.935 37.201 0.28 41.37 C -ANISOU 4219 CA BLYS C 140 5926 5684 4109 -1012 1084 -970 C -ATOM 4220 C LYS C 140 3.628 17.776 36.295 1.00 39.16 C -ANISOU 4220 C LYS C 140 5548 5293 4037 -916 869 -743 C -ATOM 4221 O LYS C 140 4.463 18.677 36.219 1.00 45.54 O -ANISOU 4221 O LYS C 140 6352 6082 4869 -937 700 -757 O -ATOM 4222 CB ALYS C 140 2.668 17.202 38.534 0.72 45.38 C -ANISOU 4222 CB ALYS C 140 6606 6366 4270 -1215 1064 -804 C -ATOM 4223 CB BLYS C 140 2.656 17.306 38.574 0.28 45.93 C -ANISOU 4223 CB BLYS C 140 6684 6440 4329 -1220 1065 -827 C -ATOM 4224 CG ALYS C 140 1.564 17.407 39.549 0.72 50.78 C -ANISOU 4224 CG ALYS C 140 7424 7189 4682 -1342 1326 -1032 C -ATOM 4225 CG BLYS C 140 1.927 18.013 39.708 0.28 51.33 C -ANISOU 4225 CG BLYS C 140 7558 7252 4693 -1367 1249 -1109 C -ATOM 4226 CD ALYS C 140 1.687 16.407 40.691 0.72 55.77 C -ANISOU 4226 CD ALYS C 140 8229 7996 4966 -1553 1329 -795 C -ATOM 4227 CD BLYS C 140 0.963 17.078 40.424 0.28 55.25 C -ANISOU 4227 CD BLYS C 140 8087 7876 5027 -1459 1482 -1050 C -ATOM 4228 CE ALYS C 140 0.542 16.539 41.679 0.72 59.79 C -ANISOU 4228 CE ALYS C 140 8803 8597 5318 -1621 1570 -964 C -ATOM 4229 CE BLYS C 140 1.696 15.947 41.130 0.28 57.04 C -ANISOU 4229 CE BLYS C 140 8457 8223 4992 -1636 1337 -681 C -ATOM 4230 NZ ALYS C 140 0.679 17.750 42.532 0.72 65.41 N -ANISOU 4230 NZ ALYS C 140 9693 9330 5831 -1683 1548 -1199 N -ATOM 4231 NZ BLYS C 140 0.778 14.873 41.603 0.28 59.25 N -ANISOU 4231 NZ BLYS C 140 8754 8548 5211 -1713 1549 -560 N -ATOM 4232 N THR C 141 3.730 16.648 35.596 1.00 34.12 N -ANISOU 4232 N THR C 141 4851 4565 3550 -828 914 -545 N -ATOM 4233 CA THR C 141 4.870 16.447 34.699 1.00 33.60 C -ANISOU 4233 CA THR C 141 4693 4383 3692 -692 808 -334 C -ATOM 4234 C THR C 141 4.892 17.541 33.634 1.00 35.31 C -ANISOU 4234 C THR C 141 4819 4513 4084 -607 770 -503 C -ATOM 4235 O THR C 141 5.933 18.168 33.394 1.00 33.95 O -ANISOU 4235 O THR C 141 4573 4336 3991 -590 627 -406 O -ATOM 4236 CB THR C 141 4.865 15.047 34.054 1.00 39.30 C -ANISOU 4236 CB THR C 141 5457 4935 4539 -597 961 -159 C -ATOM 4237 OG1 THR C 141 4.972 14.060 35.086 1.00 44.03 O -ANISOU 4237 OG1 THR C 141 6160 5572 4997 -658 986 69 O -ATOM 4238 CG2 THR C 141 6.033 14.888 33.083 1.00 40.49 C -ANISOU 4238 CG2 THR C 141 5523 4950 4913 -408 949 31 C -ATOM 4239 N MET C 142 3.738 17.813 33.026 1.00 30.64 N -ANISOU 4239 N MET C 142 4210 3880 3551 -575 883 -714 N -ATOM 4240 CA MET C 142 3.703 18.810 31.952 1.00 29.22 C -ANISOU 4240 CA MET C 142 3956 3613 3534 -478 834 -807 C -ATOM 4241 C MET C 142 3.924 20.223 32.487 1.00 31.59 C -ANISOU 4241 C MET C 142 4291 3897 3815 -501 750 -939 C -ATOM 4242 O MET C 142 4.611 21.022 31.855 1.00 30.53 O -ANISOU 4242 O MET C 142 4138 3664 3798 -472 651 -902 O -ATOM 4243 CB MET C 142 2.412 18.719 31.137 1.00 30.65 C -ANISOU 4243 CB MET C 142 4062 3802 3781 -444 922 -921 C -ATOM 4244 CG MET C 142 2.483 19.440 29.783 1.00 38.20 C -ANISOU 4244 CG MET C 142 4959 4676 4878 -347 844 -908 C -ATOM 4245 SD MET C 142 3.987 19.141 28.821 1.00 45.35 S -ANISOU 4245 SD MET C 142 5931 5459 5840 -314 810 -719 S -ATOM 4246 CE MET C 142 3.882 17.379 28.529 1.00 30.69 C -ANISOU 4246 CE MET C 142 4199 3555 3908 -376 971 -659 C -ATOM 4247 N GLN C 143 3.351 20.522 33.653 1.00 29.69 N -ANISOU 4247 N GLN C 143 4145 3728 3407 -581 823 -1102 N -ATOM 4248 CA GLN C 143 3.639 21.771 34.348 1.00 33.99 C -ANISOU 4248 CA GLN C 143 4843 4207 3865 -664 783 -1273 C -ATOM 4249 C GLN C 143 5.148 21.981 34.453 1.00 39.60 C -ANISOU 4249 C GLN C 143 5579 4932 4536 -827 540 -1103 C -ATOM 4250 O GLN C 143 5.670 23.057 34.137 1.00 44.45 O -ANISOU 4250 O GLN C 143 6246 5407 5236 -880 449 -1157 O -ATOM 4251 CB GLN C 143 3.079 21.705 35.770 1.00 44.66 C -ANISOU 4251 CB GLN C 143 6365 5676 4927 -796 919 -1441 C -ATOM 4252 CG GLN C 143 1.953 22.662 36.085 1.00 51.56 C -ANISOU 4252 CG GLN C 143 7322 6444 5825 -677 1175 -1738 C -ATOM 4253 CD GLN C 143 1.562 22.604 37.564 1.00 58.57 C -ANISOU 4253 CD GLN C 143 8388 7454 6412 -809 1293 -1823 C -ATOM 4254 OE1 GLN C 143 2.212 21.922 38.366 1.00 59.42 O -ANISOU 4254 OE1 GLN C 143 8630 7736 6211 -1063 1189 -1743 O -ATOM 4255 NE2 GLN C 143 0.499 23.313 37.925 1.00 57.89 N -ANISOU 4255 NE2 GLN C 143 8308 7288 6398 -635 1520 -1965 N -ATOM 4256 N THR C 144 5.840 20.939 34.902 1.00 40.20 N -ANISOU 4256 N THR C 144 5592 5180 4502 -910 437 -857 N -ATOM 4257 CA THR C 144 7.278 21.008 35.152 1.00 49.90 C -ANISOU 4257 CA THR C 144 6741 6520 5698 -1069 184 -610 C -ATOM 4258 C THR C 144 8.064 21.174 33.853 1.00 48.03 C -ANISOU 4258 C THR C 144 6303 6186 5760 -942 145 -437 C -ATOM 4259 O THR C 144 8.954 22.015 33.766 1.00 52.03 O -ANISOU 4259 O THR C 144 6761 6699 6309 -1098 -20 -380 O -ATOM 4260 CB THR C 144 7.776 19.768 35.933 1.00 58.17 C -ANISOU 4260 CB THR C 144 7720 7783 6600 -1113 95 -298 C -ATOM 4261 OG1 THR C 144 6.956 19.571 37.094 1.00 59.87 O -ANISOU 4261 OG1 THR C 144 8153 8097 6497 -1249 171 -452 O -ATOM 4262 CG2 THR C 144 9.225 19.948 36.372 1.00 63.77 C -ANISOU 4262 CG2 THR C 144 8275 8697 7258 -1305 -219 6 C -ATOM 4263 N LEU C 145 7.721 20.382 32.841 1.00 44.08 N -ANISOU 4263 N LEU C 145 5716 5598 5435 -705 313 -364 N -ATOM 4264 CA LEU C 145 8.413 20.449 31.554 1.00 42.53 C -ANISOU 4264 CA LEU C 145 5378 5315 5467 -582 347 -215 C -ATOM 4265 C LEU C 145 8.227 21.813 30.888 1.00 40.79 C -ANISOU 4265 C LEU C 145 5217 4952 5331 -622 318 -381 C -ATOM 4266 O LEU C 145 9.192 22.419 30.408 1.00 42.39 O -ANISOU 4266 O LEU C 145 5322 5140 5645 -693 237 -245 O -ATOM 4267 CB LEU C 145 7.932 19.337 30.629 1.00 40.31 C -ANISOU 4267 CB LEU C 145 5110 4938 5267 -381 563 -180 C -ATOM 4268 CG LEU C 145 8.605 19.248 29.264 1.00 44.83 C -ANISOU 4268 CG LEU C 145 5607 5420 6008 -255 676 -50 C -ATOM 4269 CD1 LEU C 145 10.121 19.352 29.396 1.00 47.76 C -ANISOU 4269 CD1 LEU C 145 5745 5898 6503 -257 604 252 C -ATOM 4270 CD2 LEU C 145 8.218 17.953 28.556 1.00 43.99 C -ANISOU 4270 CD2 LEU C 145 5614 5195 5905 -120 915 -42 C -ATOM 4271 N LEU C 146 6.987 22.297 30.870 1.00 33.99 N -ANISOU 4271 N LEU C 146 4494 3982 4438 -567 398 -635 N -ATOM 4272 CA LEU C 146 6.701 23.615 30.310 1.00 32.66 C -ANISOU 4272 CA LEU C 146 4407 3625 4377 -549 388 -756 C -ATOM 4273 C LEU C 146 7.536 24.706 30.959 1.00 38.61 C -ANISOU 4273 C LEU C 146 5267 4305 5096 -787 249 -796 C -ATOM 4274 O LEU C 146 8.067 25.587 30.274 1.00 38.00 O -ANISOU 4274 O LEU C 146 5206 4082 5151 -845 199 -731 O -ATOM 4275 CB LEU C 146 5.221 23.946 30.432 1.00 33.90 C -ANISOU 4275 CB LEU C 146 4640 3704 4537 -407 513 -976 C -ATOM 4276 CG LEU C 146 4.319 23.283 29.407 1.00 34.96 C -ANISOU 4276 CG LEU C 146 4652 3892 4738 -240 587 -921 C -ATOM 4277 CD1 LEU C 146 2.884 23.586 29.713 1.00 39.38 C -ANISOU 4277 CD1 LEU C 146 5177 4459 5327 -112 694 -1080 C -ATOM 4278 CD2 LEU C 146 4.683 23.805 28.028 1.00 32.23 C -ANISOU 4278 CD2 LEU C 146 4285 3445 4517 -182 530 -776 C -ATOM 4279 N SER C 147 7.660 24.650 32.283 1.00 44.68 N -ANISOU 4279 N SER C 147 6142 5180 5653 -981 180 -897 N -ATOM 4280 CA SER C 147 8.482 25.620 32.998 1.00 46.62 C -ANISOU 4280 CA SER C 147 6539 5386 5787 -1320 9 -958 C -ATOM 4281 C SER C 147 9.953 25.514 32.588 1.00 49.95 C -ANISOU 4281 C SER C 147 6705 5968 6305 -1496 -195 -625 C -ATOM 4282 O SER C 147 10.628 26.522 32.415 1.00 52.67 O -ANISOU 4282 O SER C 147 7106 6200 6705 -1740 -307 -617 O -ATOM 4283 CB SER C 147 8.339 25.446 34.512 1.00 52.34 C -ANISOU 4283 CB SER C 147 7455 6260 6173 -1547 -44 -1115 C -ATOM 4284 OG SER C 147 9.175 26.358 35.196 1.00 56.18 O -ANISOU 4284 OG SER C 147 8129 6730 6486 -1970 -248 -1188 O -ATOM 4285 N LEU C 148 10.440 24.288 32.429 1.00 50.72 N -ANISOU 4285 N LEU C 148 6516 6308 6446 -1364 -209 -335 N -ATOM 4286 CA LEU C 148 11.821 24.054 32.016 1.00 56.12 C -ANISOU 4286 CA LEU C 148 6866 7180 7278 -1441 -332 37 C -ATOM 4287 C LEU C 148 12.097 24.617 30.620 1.00 56.49 C -ANISOU 4287 C LEU C 148 6839 7056 7567 -1347 -209 105 C -ATOM 4288 O LEU C 148 13.033 25.398 30.421 1.00 55.74 O -ANISOU 4288 O LEU C 148 6635 6987 7556 -1600 -332 240 O -ATOM 4289 CB LEU C 148 12.121 22.558 32.030 1.00 60.69 C -ANISOU 4289 CB LEU C 148 7193 7958 7909 -1195 -261 330 C -ATOM 4290 CG LEU C 148 13.263 22.123 32.934 1.00 67.50 C -ANISOU 4290 CG LEU C 148 7771 9160 8715 -1371 -516 690 C -ATOM 4291 CD1 LEU C 148 12.881 20.856 33.689 1.00 70.95 C -ANISOU 4291 CD1 LEU C 148 8226 9705 9028 -1199 -482 804 C -ATOM 4292 CD2 LEU C 148 14.542 21.928 32.128 1.00 66.67 C -ANISOU 4292 CD2 LEU C 148 7229 9196 8906 -1279 -493 1097 C -ATOM 4293 N VAL C 149 11.271 24.204 29.663 1.00 51.81 N -ANISOU 4293 N VAL C 149 6315 6314 7055 -1033 22 28 N -ATOM 4294 CA VAL C 149 11.408 24.616 28.273 1.00 45.32 C -ANISOU 4294 CA VAL C 149 5473 5357 6390 -935 154 106 C -ATOM 4295 C VAL C 149 11.394 26.134 28.138 1.00 46.47 C -ANISOU 4295 C VAL C 149 5803 5279 6574 -1146 62 -2 C -ATOM 4296 O VAL C 149 12.195 26.716 27.401 1.00 47.50 O -ANISOU 4296 O VAL C 149 5846 5378 6825 -1269 65 179 O -ATOM 4297 CB VAL C 149 10.290 23.998 27.415 1.00 40.25 C -ANISOU 4297 CB VAL C 149 4952 4613 5728 -649 349 -7 C -ATOM 4298 CG1 VAL C 149 10.234 24.653 26.045 1.00 42.08 C -ANISOU 4298 CG1 VAL C 149 5249 4706 6034 -603 433 50 C -ATOM 4299 CG2 VAL C 149 10.499 22.501 27.287 1.00 38.30 C -ANISOU 4299 CG2 VAL C 149 4584 4495 5472 -472 501 121 C -ATOM 4300 N ARG C 150 10.500 26.775 28.877 1.00 46.36 N -ANISOU 4300 N ARG C 150 6062 5086 6467 -1189 22 -290 N -ATOM 4301 CA ARG C 150 10.354 28.221 28.791 1.00 50.75 C -ANISOU 4301 CA ARG C 150 6882 5318 7084 -1337 -4 -422 C -ATOM 4302 C ARG C 150 11.587 28.987 29.270 1.00 56.67 C -ANISOU 4302 C ARG C 150 7636 6077 7820 -1792 -191 -344 C -ATOM 4303 O ARG C 150 11.768 30.153 28.912 1.00 56.97 O -ANISOU 4303 O ARG C 150 7875 5819 7953 -1969 -197 -367 O -ATOM 4304 CB ARG C 150 9.092 28.682 29.518 1.00 49.48 C -ANISOU 4304 CB ARG C 150 7018 4931 6850 -1218 82 -758 C -ATOM 4305 CG ARG C 150 7.830 28.377 28.733 1.00 48.29 C -ANISOU 4305 CG ARG C 150 6833 4722 6793 -815 241 -776 C -ATOM 4306 CD ARG C 150 6.565 28.850 29.435 1.00 56.12 C -ANISOU 4306 CD ARG C 150 8025 5523 7776 -642 379 -1058 C -ATOM 4307 NE ARG C 150 5.395 28.602 28.595 1.00 59.49 N -ANISOU 4307 NE ARG C 150 8317 5963 8323 -286 478 -991 N -ATOM 4308 CZ ARG C 150 4.234 28.122 29.031 1.00 58.35 C -ANISOU 4308 CZ ARG C 150 8093 5926 8152 -85 598 -1120 C -ATOM 4309 NH1 ARG C 150 4.067 27.838 30.314 1.00 59.24 N -ANISOU 4309 NH1 ARG C 150 8296 6113 8100 -180 681 -1343 N -ATOM 4310 NH2 ARG C 150 3.238 27.932 28.176 1.00 58.46 N -ANISOU 4310 NH2 ARG C 150 7924 6009 8278 174 625 -1000 N -ATOM 4311 N GLN C 151 12.439 28.327 30.056 1.00 58.84 N -ANISOU 4311 N GLN C 151 7678 6697 7982 -2004 -359 -211 N -ATOM 4312 CA GLN C 151 13.691 28.938 30.518 1.00 63.51 C -ANISOU 4312 CA GLN C 151 8172 7415 8544 -2508 -604 -68 C -ATOM 4313 C GLN C 151 14.666 29.117 29.357 1.00 62.14 C -ANISOU 4313 C GLN C 151 7689 7310 8612 -2555 -561 278 C -ATOM 4314 O GLN C 151 15.688 29.781 29.493 1.00 64.02 O -ANISOU 4314 O GLN C 151 7814 7631 8879 -2975 -730 427 O -ATOM 4315 CB GLN C 151 14.361 28.080 31.596 1.00 66.19 C -ANISOU 4315 CB GLN C 151 8243 8195 8709 -2688 -836 94 C -ATOM 4316 CG GLN C 151 13.471 27.701 32.768 1.00 68.25 C -ANISOU 4316 CG GLN C 151 8782 8470 8680 -2651 -855 -192 C -ATOM 4317 CD GLN C 151 13.442 28.750 33.862 1.00 77.54 C -ANISOU 4317 CD GLN C 151 10375 9513 9576 -3075 -997 -499 C -ATOM 4318 OE1 GLN C 151 14.385 29.527 34.026 1.00 81.26 O -ANISOU 4318 OE1 GLN C 151 10820 10032 10025 -3381 -1159 -404 O -ATOM 4319 NE2 GLN C 151 12.353 28.773 34.625 1.00 80.32 N -ANISOU 4319 NE2 GLN C 151 11096 9711 9710 -2951 -850 -851 N -ATOM 4320 N TYR C 152 14.351 28.505 28.221 1.00 59.99 N -ANISOU 4320 N TYR C 152 7290 7027 8476 -2137 -316 401 N -ATOM 4321 CA TYR C 152 15.217 28.572 27.053 1.00 57.20 C -ANISOU 4321 CA TYR C 152 6671 6754 8308 -2140 -190 722 C -ATOM 4322 C TYR C 152 14.618 29.437 25.950 1.00 52.34 C -ANISOU 4322 C TYR C 152 6358 5774 7756 -2049 -36 657 C -ATOM 4323 O TYR C 152 15.099 29.443 24.814 1.00 47.97 O -ANISOU 4323 O TYR C 152 5668 5261 7298 -1996 131 898 O -ATOM 4324 CB TYR C 152 15.550 27.164 26.564 1.00 55.53 C -ANISOU 4324 CB TYR C 152 6101 6833 8163 -1784 5 955 C -ATOM 4325 CG TYR C 152 16.530 26.475 27.484 1.00 62.92 C -ANISOU 4325 CG TYR C 152 6624 8156 9127 -1900 -159 1204 C -ATOM 4326 CD1 TYR C 152 17.898 26.679 27.345 1.00 65.83 C -ANISOU 4326 CD1 TYR C 152 6545 8805 9663 -2148 -221 1580 C -ATOM 4327 CD2 TYR C 152 16.088 25.652 28.519 1.00 65.30 C -ANISOU 4327 CD2 TYR C 152 6951 8572 9289 -1783 -269 1111 C -ATOM 4328 CE1 TYR C 152 18.805 26.065 28.195 1.00 71.69 C -ANISOU 4328 CE1 TYR C 152 6895 9931 10412 -2176 -409 1839 C -ATOM 4329 CE2 TYR C 152 16.991 25.028 29.373 1.00 69.57 C -ANISOU 4329 CE2 TYR C 152 7100 9488 9845 -1881 -462 1416 C -ATOM 4330 CZ TYR C 152 18.349 25.242 29.206 1.00 73.00 C -ANISOU 4330 CZ TYR C 152 7050 10220 10466 -2097 -554 1819 C -ATOM 4331 OH TYR C 152 19.250 24.630 30.050 1.00 77.01 O -ANISOU 4331 OH TYR C 152 7198 11105 10958 -2094 -765 2135 O -ATOM 4332 N ASN C 153 13.566 30.168 26.309 1.00 47.90 N -ANISOU 4332 N ASN C 153 7026 4058 7115 -1805 733 -179 N -ATOM 4333 CA ASN C 153 12.991 31.199 25.452 1.00 45.58 C -ANISOU 4333 CA ASN C 153 6855 3667 6797 -1755 876 -108 C -ATOM 4334 C ASN C 153 12.521 30.731 24.075 1.00 42.07 C -ANISOU 4334 C ASN C 153 6359 3339 6287 -1697 1064 -20 C -ATOM 4335 O ASN C 153 12.899 31.312 23.055 1.00 41.40 O -ANISOU 4335 O ASN C 153 6258 3253 6219 -1800 1149 126 O -ATOM 4336 CB ASN C 153 13.976 32.364 25.319 1.00 53.70 C -ANISOU 4336 CB ASN C 153 7878 4564 7961 -1920 820 -13 C -ATOM 4337 CG ASN C 153 14.472 32.856 26.667 1.00 62.74 C -ANISOU 4337 CG ASN C 153 9086 5597 9157 -2030 634 -113 C -ATOM 4338 OD1 ASN C 153 15.646 32.693 27.008 1.00 70.49 O -ANISOU 4338 OD1 ASN C 153 9917 6602 10264 -2192 495 -78 O -ATOM 4339 ND2 ASN C 153 13.575 33.453 27.447 1.00 57.44 N -ANISOU 4339 ND2 ASN C 153 8620 4797 8406 -1964 647 -250 N -ATOM 4340 N PRO C 154 11.664 29.699 24.040 1.00 43.13 N -ANISOU 4340 N PRO C 154 6484 3584 6320 -1570 1126 -97 N -ATOM 4341 CA PRO C 154 11.132 29.297 22.738 1.00 42.28 C -ANISOU 4341 CA PRO C 154 6361 3594 6109 -1565 1297 -18 C -ATOM 4342 C PRO C 154 10.181 30.378 22.254 1.00 43.34 C -ANISOU 4342 C PRO C 154 6672 3573 6222 -1524 1291 157 C -ATOM 4343 O PRO C 154 9.732 31.203 23.051 1.00 48.09 O -ANISOU 4343 O PRO C 154 7376 3962 6934 -1429 1203 130 O -ATOM 4344 CB PRO C 154 10.355 28.021 23.059 1.00 35.47 C -ANISOU 4344 CB PRO C 154 5463 2837 5178 -1441 1322 -154 C -ATOM 4345 CG PRO C 154 9.911 28.215 24.484 1.00 36.41 C -ANISOU 4345 CG PRO C 154 5679 2847 5309 -1343 1176 -251 C -ATOM 4346 CD PRO C 154 10.980 29.022 25.159 1.00 41.10 C -ANISOU 4346 CD PRO C 154 6274 3343 5999 -1462 1044 -238 C -ATOM 4347 N LYS C 155 9.888 30.389 20.964 1.00 44.50 N -ANISOU 4347 N LYS C 155 6843 3825 6239 -1616 1375 344 N -ATOM 4348 CA LYS C 155 8.987 31.388 20.424 1.00 50.45 C -ANISOU 4348 CA LYS C 155 7736 4404 7027 -1593 1296 614 C -ATOM 4349 C LYS C 155 7.567 31.023 20.819 1.00 48.05 C -ANISOU 4349 C LYS C 155 7451 4037 6768 -1358 1254 569 C -ATOM 4350 O LYS C 155 6.764 31.877 21.201 1.00 50.60 O -ANISOU 4350 O LYS C 155 7827 4070 7329 -1208 1180 642 O -ATOM 4351 CB LYS C 155 9.108 31.421 18.905 1.00 55.86 C -ANISOU 4351 CB LYS C 155 8448 5311 7468 -1822 1330 880 C -ATOM 4352 CG LYS C 155 8.299 32.512 18.233 1.00 66.16 C -ANISOU 4352 CG LYS C 155 9882 6430 8826 -1848 1152 1283 C -ATOM 4353 CD LYS C 155 8.199 32.249 16.741 1.00 70.60 C -ANISOU 4353 CD LYS C 155 10480 7341 9002 -2108 1125 1543 C -ATOM 4354 CE LYS C 155 7.305 33.261 16.054 1.00 76.58 C -ANISOU 4354 CE LYS C 155 11329 7935 9832 -2132 837 2030 C -ATOM 4355 NZ LYS C 155 6.994 32.845 14.659 1.00 80.55 N -ANISOU 4355 NZ LYS C 155 11868 8858 9881 -2379 747 2253 N -ATOM 4356 N MET C 156 7.278 29.731 20.732 1.00 44.37 N -ANISOU 4356 N MET C 156 6887 3854 6119 -1307 1301 418 N -ATOM 4357 CA MET C 156 5.944 29.187 20.978 1.00 42.98 C -ANISOU 4357 CA MET C 156 6664 3726 5942 -1095 1247 367 C -ATOM 4358 C MET C 156 6.091 27.759 21.504 1.00 41.32 C -ANISOU 4358 C MET C 156 6364 3718 5619 -1066 1326 94 C -ATOM 4359 O MET C 156 7.004 27.043 21.088 1.00 39.65 O -ANISOU 4359 O MET C 156 6082 3680 5302 -1206 1411 15 O -ATOM 4360 CB MET C 156 5.132 29.203 19.672 1.00 44.48 C -ANISOU 4360 CB MET C 156 6834 4087 5981 -1136 1133 652 C -ATOM 4361 CG MET C 156 3.937 28.253 19.632 1.00 48.68 C -ANISOU 4361 CG MET C 156 7264 4797 6436 -997 1082 588 C -ATOM 4362 SD MET C 156 3.233 28.071 17.976 1.00 65.42 S -ANISOU 4362 SD MET C 156 9382 7219 8257 -1182 900 922 S -ATOM 4363 CE MET C 156 2.588 29.719 17.693 1.00 69.12 C -ANISOU 4363 CE MET C 156 9863 7344 9056 -1110 636 1383 C -ATOM 4364 N VAL C 157 5.225 27.357 22.437 1.00 36.17 N -ANISOU 4364 N VAL C 157 5698 3015 5032 -899 1317 -54 N -ATOM 4365 CA VAL C 157 5.174 25.963 22.886 1.00 35.17 C -ANISOU 4365 CA VAL C 157 5492 3062 4809 -881 1350 -246 C -ATOM 4366 C VAL C 157 3.747 25.454 22.896 1.00 38.13 C -ANISOU 4366 C VAL C 157 5811 3523 5153 -735 1331 -262 C -ATOM 4367 O VAL C 157 2.872 26.039 23.543 1.00 37.28 O -ANISOU 4367 O VAL C 157 5723 3254 5187 -608 1341 -283 O -ATOM 4368 CB VAL C 157 5.719 25.751 24.316 1.00 41.75 C -ANISOU 4368 CB VAL C 157 6377 3775 5710 -915 1342 -422 C -ATOM 4369 CG1 VAL C 157 5.910 24.257 24.584 1.00 37.35 C -ANISOU 4369 CG1 VAL C 157 5714 3375 5104 -937 1322 -531 C -ATOM 4370 CG2 VAL C 157 7.020 26.471 24.521 1.00 45.40 C -ANISOU 4370 CG2 VAL C 157 6883 4108 6258 -1062 1315 -395 C -ATOM 4371 N LYS C 158 3.516 24.341 22.212 1.00 32.49 N -ANISOU 4371 N LYS C 158 5008 3048 4290 -768 1333 -289 N -ATOM 4372 CA LYS C 158 2.233 23.662 22.296 1.00 30.91 C -ANISOU 4372 CA LYS C 158 4731 2949 4064 -665 1306 -324 C -ATOM 4373 C LYS C 158 2.482 22.219 22.737 1.00 29.14 C -ANISOU 4373 C LYS C 158 4456 2832 3784 -706 1352 -517 C -ATOM 4374 O LYS C 158 3.567 21.672 22.497 1.00 27.90 O -ANISOU 4374 O LYS C 158 4272 2707 3623 -811 1396 -590 O -ATOM 4375 CB LYS C 158 1.531 23.676 20.935 1.00 33.44 C -ANISOU 4375 CB LYS C 158 4998 3453 4255 -711 1212 -137 C -ATOM 4376 CG LYS C 158 1.390 25.045 20.298 1.00 39.64 C -ANISOU 4376 CG LYS C 158 5823 4123 5116 -716 1096 152 C -ATOM 4377 CD LYS C 158 0.132 25.745 20.731 1.00 49.31 C -ANISOU 4377 CD LYS C 158 6946 5156 6635 -507 1008 262 C -ATOM 4378 CE LYS C 158 -0.342 26.670 19.620 1.00 55.13 C -ANISOU 4378 CE LYS C 158 7646 5861 7439 -546 779 656 C -ATOM 4379 NZ LYS C 158 -0.946 27.917 20.140 1.00 61.73 N -ANISOU 4379 NZ LYS C 158 8395 6312 8747 -334 735 781 N -ATOM 4380 N VAL C 159 1.483 21.611 23.368 1.00 27.65 N -ANISOU 4380 N VAL C 159 4226 2671 3608 -631 1349 -591 N -ATOM 4381 CA VAL C 159 1.578 20.226 23.817 1.00 30.72 C -ANISOU 4381 CA VAL C 159 4571 3124 3979 -681 1358 -725 C -ATOM 4382 C VAL C 159 0.526 19.359 23.132 1.00 28.36 C -ANISOU 4382 C VAL C 159 4172 3003 3602 -677 1347 -745 C -ATOM 4383 O VAL C 159 -0.644 19.737 23.079 1.00 30.32 O -ANISOU 4383 O VAL C 159 4370 3291 3860 -599 1320 -676 O -ATOM 4384 CB VAL C 159 1.379 20.149 25.341 1.00 26.24 C -ANISOU 4384 CB VAL C 159 4082 2443 3444 -685 1362 -792 C -ATOM 4385 CG1 VAL C 159 1.463 18.721 25.840 1.00 28.68 C -ANISOU 4385 CG1 VAL C 159 4352 2788 3756 -765 1315 -851 C -ATOM 4386 CG2 VAL C 159 2.407 21.030 26.054 1.00 30.10 C -ANISOU 4386 CG2 VAL C 159 4696 2770 3971 -749 1342 -782 C -ATOM 4387 N ALA C 160 0.950 18.210 22.597 1.00 27.62 N -ANISOU 4387 N ALA C 160 4022 2991 3481 -771 1374 -853 N -ATOM 4388 CA ALA C 160 0.026 17.191 22.120 1.00 27.17 C -ANISOU 4388 CA ALA C 160 3889 3079 3355 -815 1364 -923 C -ATOM 4389 C ALA C 160 0.143 15.999 23.069 1.00 30.85 C -ANISOU 4389 C ALA C 160 4324 3440 3959 -830 1367 -1029 C -ATOM 4390 O ALA C 160 1.246 15.511 23.325 1.00 30.37 O -ANISOU 4390 O ALA C 160 4243 3243 4053 -864 1381 -1088 O -ATOM 4391 CB ALA C 160 0.366 16.772 20.677 1.00 26.78 C -ANISOU 4391 CB ALA C 160 3828 3190 3159 -971 1423 -1008 C -ATOM 4392 N SER C 161 -0.979 15.523 23.592 1.00 27.11 N -ANISOU 4392 N SER C 161 3820 3010 3471 -820 1339 -1025 N -ATOM 4393 CA SER C 161 -0.955 14.310 24.418 1.00 23.96 C -ANISOU 4393 CA SER C 161 3406 2514 3184 -885 1314 -1076 C -ATOM 4394 C SER C 161 -1.960 13.331 23.867 1.00 24.14 C -ANISOU 4394 C SER C 161 3340 2653 3178 -949 1318 -1153 C -ATOM 4395 O SER C 161 -3.112 13.706 23.618 1.00 28.51 O -ANISOU 4395 O SER C 161 3842 3359 3632 -927 1310 -1109 O -ATOM 4396 CB SER C 161 -1.285 14.649 25.881 1.00 27.29 C -ANISOU 4396 CB SER C 161 3922 2871 3577 -896 1296 -995 C -ATOM 4397 OG SER C 161 -1.221 13.501 26.705 1.00 28.64 O -ANISOU 4397 OG SER C 161 4109 2953 3820 -1016 1223 -971 O -ATOM 4398 N LEU C 162 -1.533 12.088 23.649 1.00 23.62 N -ANISOU 4398 N LEU C 162 3227 2491 3258 -1033 1325 -1270 N -ATOM 4399 CA LEU C 162 -2.438 11.077 23.147 1.00 25.44 C -ANISOU 4399 CA LEU C 162 3389 2804 3475 -1134 1331 -1374 C -ATOM 4400 C LEU C 162 -3.647 10.982 24.066 1.00 27.15 C -ANISOU 4400 C LEU C 162 3591 3079 3646 -1148 1285 -1264 C -ATOM 4401 O LEU C 162 -4.789 10.945 23.595 1.00 25.29 O -ANISOU 4401 O LEU C 162 3273 3021 3315 -1186 1275 -1273 O -ATOM 4402 CB LEU C 162 -1.763 9.708 23.054 1.00 27.17 C -ANISOU 4402 CB LEU C 162 3542 2825 3956 -1194 1350 -1498 C -ATOM 4403 CG LEU C 162 -2.711 8.577 22.644 1.00 30.78 C -ANISOU 4403 CG LEU C 162 3940 3337 4417 -1310 1351 -1604 C -ATOM 4404 CD1 LEU C 162 -3.308 8.815 21.243 1.00 30.85 C -ANISOU 4404 CD1 LEU C 162 3956 3603 4162 -1439 1412 -1766 C -ATOM 4405 CD2 LEU C 162 -2.017 7.216 22.678 1.00 33.70 C -ANISOU 4405 CD2 LEU C 162 4215 3488 5100 -1275 1346 -1647 C -ATOM 4406 N LEU C 163 -3.390 10.941 25.374 1.00 25.88 N -ANISOU 4406 N LEU C 163 3504 2785 3546 -1158 1256 -1155 N -ATOM 4407 CA LEU C 163 -4.451 10.723 26.359 1.00 26.53 C -ANISOU 4407 CA LEU C 163 3594 2923 3563 -1243 1275 -1084 C -ATOM 4408 C LEU C 163 -4.476 11.799 27.424 1.00 26.05 C -ANISOU 4408 C LEU C 163 3644 2876 3378 -1223 1342 -1009 C -ATOM 4409 O LEU C 163 -3.436 12.314 27.836 1.00 31.26 O -ANISOU 4409 O LEU C 163 4422 3428 4028 -1206 1295 -960 O -ATOM 4410 CB LEU C 163 -4.287 9.365 27.053 1.00 26.90 C -ANISOU 4410 CB LEU C 163 3672 2803 3746 -1408 1187 -1026 C -ATOM 4411 CG LEU C 163 -4.179 8.112 26.198 1.00 28.25 C -ANISOU 4411 CG LEU C 163 3744 2862 4130 -1460 1150 -1143 C -ATOM 4412 CD1 LEU C 163 -3.952 6.881 27.083 1.00 28.19 C -ANISOU 4412 CD1 LEU C 163 3757 2654 4300 -1543 992 -976 C -ATOM 4413 CD2 LEU C 163 -5.415 7.919 25.302 1.00 28.07 C -ANISOU 4413 CD2 LEU C 163 3609 3052 4003 -1502 1213 -1270 C -ATOM 4414 N VAL C 164 -5.679 12.140 27.873 1.00 28.18 N -ANISOU 4414 N VAL C 164 3860 3272 3577 -1246 1475 -1031 N -ATOM 4415 CA VAL C 164 -5.844 13.008 29.034 1.00 25.95 C -ANISOU 4415 CA VAL C 164 3694 2989 3176 -1294 1625 -1043 C -ATOM 4416 C VAL C 164 -6.832 12.327 29.958 1.00 27.79 C -ANISOU 4416 C VAL C 164 3928 3302 3328 -1509 1750 -1054 C -ATOM 4417 O VAL C 164 -7.904 11.918 29.531 1.00 30.92 O -ANISOU 4417 O VAL C 164 4124 3804 3820 -1499 1811 -1093 O -ATOM 4418 CB VAL C 164 -6.335 14.422 28.654 1.00 32.31 C -ANISOU 4418 CB VAL C 164 4392 3829 4055 -1092 1766 -1117 C -ATOM 4419 CG1 VAL C 164 -6.675 15.234 29.913 1.00 32.09 C -ANISOU 4419 CG1 VAL C 164 4470 3774 3948 -1175 2009 -1224 C -ATOM 4420 CG2 VAL C 164 -5.283 15.145 27.833 1.00 35.33 C -ANISOU 4420 CG2 VAL C 164 4819 4133 4474 -941 1643 -1070 C -ATOM 4421 N LYS C 165 -6.467 12.176 31.226 1.00 29.34 N -ANISOU 4421 N LYS C 165 4356 3466 3326 -1753 1771 -1001 N -ATOM 4422 CA LYS C 165 -7.347 11.510 32.174 1.00 34.33 C -ANISOU 4422 CA LYS C 165 5034 4194 3815 -2026 1895 -993 C -ATOM 4423 C LYS C 165 -8.278 12.495 32.865 1.00 33.48 C -ANISOU 4423 C LYS C 165 4902 4165 3653 -1994 2145 -1185 C -ATOM 4424 O LYS C 165 -7.866 13.608 33.195 1.00 36.79 O -ANISOU 4424 O LYS C 165 5419 4520 4039 -1933 2213 -1275 O -ATOM 4425 CB LYS C 165 -6.538 10.774 33.239 1.00 37.83 C -ANISOU 4425 CB LYS C 165 5756 4569 4049 -2310 1668 -789 C -ATOM 4426 CG LYS C 165 -6.031 9.418 32.805 1.00 39.29 C -ANISOU 4426 CG LYS C 165 5885 4609 4434 -2319 1356 -580 C -ATOM 4427 CD LYS C 165 -5.468 8.651 33.987 1.00 43.95 C -ANISOU 4427 CD LYS C 165 6684 5144 4869 -2571 1084 -306 C -ATOM 4428 CE LYS C 165 -5.237 7.204 33.630 1.00 42.67 C -ANISOU 4428 CE LYS C 165 6399 4794 5020 -2552 815 -106 C -ATOM 4429 NZ LYS C 165 -4.615 6.460 34.753 1.00 37.94 N -ANISOU 4429 NZ LYS C 165 5955 4101 4360 -2777 498 225 N -ATOM 4430 N ARG C 166 -9.532 12.099 33.064 1.00 36.47 N -ANISOU 4430 N ARG C 166 3841 5674 4343 -440 2120 -755 N -ATOM 4431 CA ARG C 166 -10.418 12.861 33.934 1.00 38.94 C -ANISOU 4431 CA ARG C 166 4232 5998 4566 -264 2327 -835 C -ATOM 4432 C ARG C 166 -10.100 12.426 35.357 1.00 47.64 C -ANISOU 4432 C ARG C 166 5369 7227 5505 -430 2349 -915 C -ATOM 4433 O ARG C 166 -10.265 11.257 35.697 1.00 48.59 O -ANISOU 4433 O ARG C 166 5293 7561 5608 -529 2270 -827 O -ATOM 4434 CB ARG C 166 -11.892 12.587 33.610 1.00 40.20 C -ANISOU 4434 CB ARG C 166 4142 6348 4783 -35 2400 -693 C -ATOM 4435 CG ARG C 166 -12.339 13.126 32.247 1.00 40.65 C -ANISOU 4435 CG ARG C 166 4150 6314 4981 164 2404 -603 C -ATOM 4436 CD ARG C 166 -13.835 12.959 32.051 1.00 43.68 C -ANISOU 4436 CD ARG C 166 4263 6962 5370 391 2495 -445 C -ATOM 4437 NE ARG C 166 -14.226 11.551 32.096 1.00 43.33 N -ANISOU 4437 NE ARG C 166 3944 7205 5316 200 2364 -312 N -ATOM 4438 CZ ARG C 166 -14.128 10.717 31.065 1.00 40.72 C -ANISOU 4438 CZ ARG C 166 3494 6893 5084 58 2178 -178 C -ATOM 4439 NH1 ARG C 166 -13.652 11.144 29.905 1.00 39.93 N -ANISOU 4439 NH1 ARG C 166 3446 6620 5106 93 2124 -175 N -ATOM 4440 NH2 ARG C 166 -14.503 9.452 31.192 1.00 46.63 N -ANISOU 4440 NH2 ARG C 166 4152 7750 5814 -122 2025 -54 N -ATOM 4441 N THR C 167 -9.620 13.356 36.176 1.00 43.99 N -ANISOU 4441 N THR C 167 5183 6625 4906 -480 2458 -1080 N -ATOM 4442 CA THR C 167 -9.247 13.036 37.557 1.00 43.45 C -ANISOU 4442 CA THR C 167 5167 6677 4666 -657 2481 -1165 C -ATOM 4443 C THR C 167 -9.338 14.253 38.471 1.00 46.42 C -ANISOU 4443 C THR C 167 5870 6889 4877 -614 2683 -1339 C -ATOM 4444 O THR C 167 -9.063 15.376 38.041 1.00 47.07 O -ANISOU 4444 O THR C 167 6235 6711 4938 -574 2760 -1428 O -ATOM 4445 CB THR C 167 -7.813 12.451 37.625 1.00 46.02 C -ANISOU 4445 CB THR C 167 5490 7062 4933 -962 2298 -1164 C -ATOM 4446 OG1 THR C 167 -7.354 12.446 38.983 1.00 49.26 O -ANISOU 4446 OG1 THR C 167 6001 7571 5144 -1141 2341 -1266 O -ATOM 4447 CG2 THR C 167 -6.861 13.279 36.786 1.00 44.86 C -ANISOU 4447 CG2 THR C 167 5530 6707 4807 -1054 2237 -1214 C -ATOM 4448 N PRO C 168 -9.725 14.034 39.739 1.00 48.46 N -ANISOU 4448 N PRO C 168 6128 7283 5000 -629 2781 -1389 N -ATOM 4449 CA PRO C 168 -9.773 15.139 40.707 1.00 50.75 C -ANISOU 4449 CA PRO C 168 6776 7399 5106 -604 2965 -1548 C -ATOM 4450 C PRO C 168 -8.379 15.643 41.073 1.00 52.00 C -ANISOU 4450 C PRO C 168 7222 7436 5101 -958 2909 -1693 C -ATOM 4451 O PRO C 168 -8.254 16.702 41.688 1.00 54.26 O -ANISOU 4451 O PRO C 168 7882 7509 5226 -994 3031 -1825 O -ATOM 4452 CB PRO C 168 -10.452 14.511 41.936 1.00 50.38 C -ANISOU 4452 CB PRO C 168 6586 7562 4995 -551 2977 -1504 C -ATOM 4453 CG PRO C 168 -10.297 13.040 41.764 1.00 48.90 C -ANISOU 4453 CG PRO C 168 6036 7631 4912 -673 2762 -1357 C -ATOM 4454 CD PRO C 168 -10.304 12.794 40.287 1.00 48.67 C -ANISOU 4454 CD PRO C 168 5853 7583 5058 -615 2684 -1256 C -ATOM 4455 N ARG C 169 -7.347 14.896 40.697 1.00 48.76 N -ANISOU 4455 N ARG C 169 6637 7167 4721 -1212 2699 -1635 N -ATOM 4456 CA ARG C 169 -5.974 15.282 41.007 1.00 53.54 C -ANISOU 4456 CA ARG C 169 7441 7755 5148 -1574 2614 -1727 C -ATOM 4457 C ARG C 169 -5.381 16.278 40.017 1.00 52.67 C -ANISOU 4457 C ARG C 169 7576 7387 5049 -1641 2597 -1778 C -ATOM 4458 O ARG C 169 -4.312 16.831 40.267 1.00 56.51 O -ANISOU 4458 O ARG C 169 8284 7842 5344 -1966 2554 -1868 O -ATOM 4459 CB ARG C 169 -5.072 14.053 41.071 1.00 51.67 C -ANISOU 4459 CB ARG C 169 6899 7822 4912 -1778 2392 -1600 C -ATOM 4460 CG ARG C 169 -5.418 13.084 42.180 1.00 54.71 C -ANISOU 4460 CG ARG C 169 7090 8415 5281 -1747 2334 -1529 C -ATOM 4461 CD ARG C 169 -4.264 12.134 42.410 1.00 56.59 C -ANISOU 4461 CD ARG C 169 7144 8892 5465 -1948 2110 -1413 C -ATOM 4462 NE ARG C 169 -3.904 11.410 41.193 1.00 54.94 N -ANISOU 4462 NE ARG C 169 6742 8730 5402 -1881 1969 -1257 N -ATOM 4463 CZ ARG C 169 -2.831 10.634 41.073 1.00 53.67 C -ANISOU 4463 CZ ARG C 169 6445 8740 5206 -1977 1774 -1123 C -ATOM 4464 NH1 ARG C 169 -2.007 10.473 42.099 1.00 52.47 N -ANISOU 4464 NH1 ARG C 169 6291 8762 4882 -2152 1691 -1122 N -ATOM 4465 NH2 ARG C 169 -2.580 10.019 39.926 1.00 49.21 N -ANISOU 4465 NH2 ARG C 169 5753 8172 4772 -1875 1664 -978 N -ATOM 4466 N SER C 170 -6.071 16.486 38.896 1.00 52.59 N -ANISOU 4466 N SER C 170 7517 7221 5245 -1353 2626 -1710 N -ATOM 4467 CA SER C 170 -5.633 17.422 37.856 1.00 56.05 C -ANISOU 4467 CA SER C 170 8184 7394 5718 -1370 2621 -1748 C -ATOM 4468 C SER C 170 -5.359 18.813 38.419 1.00 61.75 C -ANISOU 4468 C SER C 170 9435 7834 6195 -1507 2798 -1945 C -ATOM 4469 O SER C 170 -6.178 19.361 39.161 1.00 63.06 O -ANISOU 4469 O SER C 170 9832 7870 6259 -1330 3019 -2030 O -ATOM 4470 CB SER C 170 -6.679 17.501 36.738 1.00 58.09 C -ANISOU 4470 CB SER C 170 8322 7536 6214 -981 2676 -1647 C -ATOM 4471 OG SER C 170 -6.557 18.698 35.997 1.00 63.60 O -ANISOU 4471 OG SER C 170 9352 7910 6901 -918 2766 -1721 O -ATOM 4472 N VAL C 171 -4.198 19.375 38.088 1.00 64.91 N -ANISOU 4472 N VAL C 171 10047 8145 6472 -1837 2706 -2008 N -ATOM 4473 CA VAL C 171 -3.859 20.714 38.571 1.00 71.45 C -ANISOU 4473 CA VAL C 171 11411 8677 7059 -2026 2833 -2165 C -ATOM 4474 C VAL C 171 -4.536 21.782 37.716 1.00 72.52 C -ANISOU 4474 C VAL C 171 11846 8418 7290 -1711 2982 -2176 C -ATOM 4475 O VAL C 171 -4.488 22.972 38.031 1.00 75.58 O -ANISOU 4475 O VAL C 171 12679 8502 7536 -1758 3081 -2235 O -ATOM 4476 CB VAL C 171 -2.326 20.962 38.654 1.00 70.51 C -ANISOU 4476 CB VAL C 171 11391 8653 6745 -2553 2651 -2190 C -ATOM 4477 CG1 VAL C 171 -1.738 20.304 39.900 1.00 70.95 C -ANISOU 4477 CG1 VAL C 171 11275 9045 6639 -2850 2548 -2174 C -ATOM 4478 CG2 VAL C 171 -1.621 20.489 37.397 1.00 67.66 C -ANISOU 4478 CG2 VAL C 171 10782 8427 6499 -2631 2476 -2107 C -ATOM 4479 N GLY C 172 -5.181 21.344 36.640 1.00 69.40 N -ANISOU 4479 N GLY C 172 11197 8043 7130 -1383 2999 -2092 N -ATOM 4480 CA GLY C 172 -5.924 22.249 35.787 1.00 69.22 C -ANISOU 4480 CA GLY C 172 11379 7704 7219 -1020 3128 -2057 C -ATOM 4481 C GLY C 172 -5.192 22.546 34.499 1.00 67.22 C -ANISOU 4481 C GLY C 172 11174 7320 7048 -1138 3018 -2050 C -ATOM 4482 O GLY C 172 -5.573 23.447 33.752 1.00 67.34 O -ANISOU 4482 O GLY C 172 11409 7051 7126 -905 3097 -2018 O -ATOM 4483 N TYR C 173 -4.130 21.794 34.235 1.00 64.61 N -ANISOU 4483 N TYR C 173 10572 7231 6747 -1475 2770 -2006 N -ATOM 4484 CA TYR C 173 -3.418 21.953 32.977 1.00 63.34 C -ANISOU 4484 CA TYR C 173 10373 6997 6697 -1573 2616 -1952 C -ATOM 4485 C TYR C 173 -4.135 21.217 31.837 1.00 57.67 C -ANISOU 4485 C TYR C 173 9238 6359 6315 -1208 2532 -1771 C -ATOM 4486 O TYR C 173 -4.533 20.068 32.007 1.00 60.37 O -ANISOU 4486 O TYR C 173 9167 6980 6789 -1104 2441 -1649 O -ATOM 4487 CB TYR C 173 -1.973 21.453 33.073 1.00 61.09 C -ANISOU 4487 CB TYR C 173 9931 6979 6301 -2042 2372 -1924 C -ATOM 4488 CG TYR C 173 -1.356 21.477 31.710 1.00 58.32 C -ANISOU 4488 CG TYR C 173 9472 6591 6097 -2077 2211 -1836 C -ATOM 4489 CD1 TYR C 173 -0.939 22.677 31.152 1.00 59.00 C -ANISOU 4489 CD1 TYR C 173 9977 6368 6073 -2213 2274 -1941 C -ATOM 4490 CD2 TYR C 173 -1.262 20.317 30.944 1.00 56.27 C -ANISOU 4490 CD2 TYR C 173 8729 6571 6078 -1954 2016 -1647 C -ATOM 4491 CE1 TYR C 173 -0.418 22.723 29.889 1.00 56.50 C -ANISOU 4491 CE1 TYR C 173 9562 6011 5895 -2231 2133 -1860 C -ATOM 4492 CE2 TYR C 173 -0.739 20.352 29.667 1.00 53.81 C -ANISOU 4492 CE2 TYR C 173 8333 6209 5902 -1961 1882 -1563 C -ATOM 4493 CZ TYR C 173 -0.318 21.562 29.153 1.00 54.21 C -ANISOU 4493 CZ TYR C 173 8766 5977 5853 -2099 1936 -1670 C -ATOM 4494 OH TYR C 173 0.201 21.625 27.893 1.00 49.23 O -ANISOU 4494 OH TYR C 173 8055 5296 5354 -2109 1804 -1589 O -ATOM 4495 N LYS C 174 -4.275 21.864 30.677 1.00 52.27 N -ANISOU 4495 N LYS C 174 8680 5432 5748 -1041 2561 -1753 N -ATOM 4496 CA LYS C 174 -4.873 21.213 29.505 1.00 49.39 C -ANISOU 4496 CA LYS C 174 7935 5148 5682 -744 2467 -1579 C -ATOM 4497 C LYS C 174 -4.037 21.382 28.236 1.00 44.55 C -ANISOU 4497 C LYS C 174 7311 4440 5174 -869 2304 -1535 C -ATOM 4498 O LYS C 174 -3.676 22.499 27.875 1.00 45.63 O -ANISOU 4498 O LYS C 174 7838 4287 5214 -937 2387 -1639 O -ATOM 4499 CB LYS C 174 -6.304 21.703 29.263 1.00 56.81 C -ANISOU 4499 CB LYS C 174 8931 5948 6705 -269 2693 -1543 C -ATOM 4500 CG LYS C 174 -7.334 21.048 30.175 1.00 64.48 C -ANISOU 4500 CG LYS C 174 9673 7154 7673 -69 2786 -1487 C -ATOM 4501 CD LYS C 174 -8.670 20.831 29.466 1.00 67.89 C -ANISOU 4501 CD LYS C 174 9829 7679 8286 370 2863 -1323 C -ATOM 4502 CE LYS C 174 -9.668 20.089 30.360 1.00 71.71 C -ANISOU 4502 CE LYS C 174 10040 8457 8750 523 2932 -1247 C -ATOM 4503 NZ LYS C 174 -10.975 19.832 29.683 1.00 72.78 N -ANISOU 4503 NZ LYS C 174 9860 8770 9024 905 2993 -1059 N -ATOM 4504 N PRO C 175 -3.738 20.264 27.549 1.00 40.72 N -ANISOU 4504 N PRO C 175 6408 4189 4874 -895 2084 -1377 N -ATOM 4505 CA PRO C 175 -2.897 20.310 26.345 1.00 40.61 C -ANISOU 4505 CA PRO C 175 6350 4120 4961 -1008 1918 -1317 C -ATOM 4506 C PRO C 175 -3.601 21.000 25.175 1.00 40.08 C -ANISOU 4506 C PRO C 175 6378 3790 5061 -703 2004 -1291 C -ATOM 4507 O PRO C 175 -4.827 21.107 25.172 1.00 38.92 O -ANISOU 4507 O PRO C 175 6192 3602 4994 -360 2157 -1257 O -ATOM 4508 CB PRO C 175 -2.670 18.827 26.003 1.00 37.75 C -ANISOU 4508 CB PRO C 175 5535 4064 4744 -1023 1709 -1137 C -ATOM 4509 CG PRO C 175 -3.172 18.036 27.168 1.00 39.34 C -ANISOU 4509 CG PRO C 175 5580 4489 4878 -1005 1751 -1124 C -ATOM 4510 CD PRO C 175 -4.189 18.898 27.864 1.00 40.07 C -ANISOU 4510 CD PRO C 175 5913 4417 4896 -818 1993 -1244 C -ATOM 4511 N ASP C 176 -2.830 21.456 24.193 1.00 37.57 N -ANISOU 4511 N ASP C 176 6164 3330 4782 -820 1909 -1291 N -ATOM 4512 CA ASP C 176 -3.404 22.088 23.016 1.00 40.41 C -ANISOU 4512 CA ASP C 176 6605 3448 5300 -539 1978 -1256 C -ATOM 4513 C ASP C 176 -4.056 21.062 22.098 1.00 37.82 C -ANISOU 4513 C ASP C 176 5838 3293 5240 -303 1861 -1064 C -ATOM 4514 O ASP C 176 -5.110 21.317 21.522 1.00 40.31 O -ANISOU 4514 O ASP C 176 6108 3531 5678 33 1970 -1001 O -ATOM 4515 CB ASP C 176 -2.325 22.871 22.270 1.00 38.73 C -ANISOU 4515 CB ASP C 176 6647 3036 5031 -774 1903 -1318 C -ATOM 4516 CG ASP C 176 -1.604 23.837 23.175 1.00 44.83 C -ANISOU 4516 CG ASP C 176 7878 3662 5493 -1100 2001 -1505 C -ATOM 4517 OD1 ASP C 176 -2.113 24.956 23.368 1.00 45.71 O -ANISOU 4517 OD1 ASP C 176 8320 3560 5488 -944 2165 -1540 O -ATOM 4518 OD2 ASP C 176 -0.553 23.461 23.727 1.00 40.34 O -ANISOU 4518 OD2 ASP C 176 7244 3312 4772 -1484 1857 -1518 O -ATOM 4519 N PHE C 177 -3.426 19.898 21.975 1.00 32.62 N -ANISOU 4519 N PHE C 177 4873 2881 4640 -481 1650 -958 N -ATOM 4520 CA PHE C 177 -3.945 18.834 21.134 1.00 30.31 C -ANISOU 4520 CA PHE C 177 4220 2739 4558 -324 1534 -778 C -ATOM 4521 C PHE C 177 -4.107 17.577 21.977 1.00 35.65 C -ANISOU 4521 C PHE C 177 4646 3706 5194 -394 1475 -706 C -ATOM 4522 O PHE C 177 -3.170 17.150 22.660 1.00 33.65 O -ANISOU 4522 O PHE C 177 4389 3588 4808 -637 1392 -727 O -ATOM 4523 CB PHE C 177 -3.001 18.572 19.959 1.00 28.27 C -ANISOU 4523 CB PHE C 177 3886 2452 4405 -440 1344 -694 C -ATOM 4524 CG PHE C 177 -2.572 19.832 19.245 1.00 34.80 C -ANISOU 4524 CG PHE C 177 4997 2996 5228 -453 1385 -783 C -ATOM 4525 CD1 PHE C 177 -3.430 20.469 18.357 1.00 37.28 C -ANISOU 4525 CD1 PHE C 177 5368 3115 5681 -170 1483 -763 C -ATOM 4526 CD2 PHE C 177 -1.325 20.398 19.491 1.00 35.05 C -ANISOU 4526 CD2 PHE C 177 5247 2979 5090 -761 1334 -879 C -ATOM 4527 CE1 PHE C 177 -3.042 21.646 17.708 1.00 38.55 C -ANISOU 4527 CE1 PHE C 177 5831 2989 5825 -173 1536 -847 C -ATOM 4528 CE2 PHE C 177 -0.928 21.564 18.845 1.00 33.23 C -ANISOU 4528 CE2 PHE C 177 5316 2478 4831 -811 1375 -966 C -ATOM 4529 CZ PHE C 177 -1.790 22.188 17.955 1.00 35.92 C -ANISOU 4529 CZ PHE C 177 5745 2579 5323 -506 1482 -956 C -ATOM 4530 N VAL C 178 -5.301 16.996 21.937 1.00 29.26 N -ANISOU 4530 N VAL C 178 3627 3015 4477 -187 1523 -611 N -ATOM 4531 CA VAL C 178 -5.602 15.828 22.755 1.00 28.71 C -ANISOU 4531 CA VAL C 178 3351 3203 4354 -249 1489 -547 C -ATOM 4532 C VAL C 178 -6.220 14.731 21.905 1.00 29.72 C -ANISOU 4532 C VAL C 178 3208 3464 4621 -176 1387 -366 C -ATOM 4533 O VAL C 178 -7.215 14.970 21.220 1.00 28.21 O -ANISOU 4533 O VAL C 178 2926 3259 4534 22 1442 -299 O -ATOM 4534 CB VAL C 178 -6.606 16.169 23.862 1.00 33.24 C -ANISOU 4534 CB VAL C 178 3960 3839 4829 -116 1678 -617 C -ATOM 4535 CG1 VAL C 178 -6.981 14.916 24.645 1.00 32.35 C -ANISOU 4535 CG1 VAL C 178 3625 4000 4667 -187 1638 -541 C -ATOM 4536 CG2 VAL C 178 -6.045 17.228 24.802 1.00 38.92 C -ANISOU 4536 CG2 VAL C 178 5007 4409 5372 -215 1798 -804 C -ATOM 4537 N GLY C 179 -5.656 13.531 21.965 1.00 27.62 N -ANISOU 4537 N GLY C 179 2830 3336 4327 -335 1252 -276 N -ATOM 4538 CA GLY C 179 -6.250 12.408 21.261 1.00 27.27 C -ANISOU 4538 CA GLY C 179 2598 3401 4364 -313 1170 -110 C -ATOM 4539 C GLY C 179 -7.556 11.957 21.879 1.00 25.84 C -ANISOU 4539 C GLY C 179 2266 3411 4140 -248 1259 -67 C -ATOM 4540 O GLY C 179 -8.618 12.064 21.266 1.00 28.11 O -ANISOU 4540 O GLY C 179 2425 3751 4503 -118 1296 13 O -ATOM 4541 N PHE C 180 -7.481 11.459 23.115 1.00 25.11 N -ANISOU 4541 N PHE C 180 3554 2353 3634 -937 1144 -443 N -ATOM 4542 CA PHE C 180 -8.625 10.872 23.790 1.00 26.83 C -ANISOU 4542 CA PHE C 180 3789 2547 3857 -881 1246 -555 C -ATOM 4543 C PHE C 180 -8.694 11.340 25.235 1.00 30.27 C -ANISOU 4543 C PHE C 180 4375 2893 4234 -923 1341 -707 C -ATOM 4544 O PHE C 180 -7.668 11.479 25.896 1.00 28.88 O -ANISOU 4544 O PHE C 180 4304 2734 3935 -1021 1271 -760 O -ATOM 4545 CB PHE C 180 -8.525 9.343 23.763 1.00 28.62 C -ANISOU 4545 CB PHE C 180 3969 2925 3981 -871 1204 -536 C -ATOM 4546 CG PHE C 180 -8.454 8.768 22.374 1.00 27.04 C -ANISOU 4546 CG PHE C 180 3663 2823 3787 -779 1079 -454 C -ATOM 4547 CD1 PHE C 180 -7.262 8.762 21.662 1.00 22.86 C -ANISOU 4547 CD1 PHE C 180 3126 2424 3137 -769 998 -364 C -ATOM 4548 CD2 PHE C 180 -9.582 8.229 21.782 1.00 27.42 C -ANISOU 4548 CD2 PHE C 180 3613 2844 3960 -681 1034 -469 C -ATOM 4549 CE1 PHE C 180 -7.214 8.234 20.371 1.00 21.54 C -ANISOU 4549 CE1 PHE C 180 2893 2387 2905 -619 897 -313 C -ATOM 4550 CE2 PHE C 180 -9.543 7.704 20.503 1.00 24.87 C -ANISOU 4550 CE2 PHE C 180 3232 2616 3600 -559 874 -448 C -ATOM 4551 CZ PHE C 180 -8.361 7.704 19.797 1.00 24.48 C -ANISOU 4551 CZ PHE C 180 3215 2725 3361 -506 816 -382 C -ATOM 4552 N GLU C 181 -9.907 11.596 25.721 1.00 29.88 N -ANISOU 4552 N GLU C 181 4329 2762 4262 -825 1494 -779 N -ATOM 4553 CA GLU C 181 -10.099 11.947 27.122 1.00 30.56 C -ANISOU 4553 CA GLU C 181 4578 2812 4221 -791 1621 -939 C -ATOM 4554 C GLU C 181 -10.714 10.717 27.769 1.00 33.95 C -ANISOU 4554 C GLU C 181 4955 3392 4551 -745 1765 -878 C -ATOM 4555 O GLU C 181 -11.769 10.234 27.331 1.00 36.30 O -ANISOU 4555 O GLU C 181 5076 3690 5027 -680 1851 -773 O -ATOM 4556 CB GLU C 181 -11.032 13.152 27.284 1.00 30.58 C -ANISOU 4556 CB GLU C 181 4615 2627 4376 -663 1739 -1046 C -ATOM 4557 CG GLU C 181 -11.150 13.625 28.732 1.00 32.77 C -ANISOU 4557 CG GLU C 181 5110 2878 4462 -568 1861 -1266 C -ATOM 4558 CD GLU C 181 -12.367 14.489 28.971 1.00 39.19 C -ANISOU 4558 CD GLU C 181 5925 3553 5413 -365 2054 -1363 C -ATOM 4559 OE1 GLU C 181 -13.472 13.927 29.092 1.00 40.24 O -ANISOU 4559 OE1 GLU C 181 5910 3786 5592 -244 2272 -1257 O -ATOM 4560 OE2 GLU C 181 -12.218 15.722 29.032 1.00 46.77 O -ANISOU 4560 OE2 GLU C 181 7011 4286 6473 -324 1981 -1530 O -ATOM 4561 N ILE C 182 -10.042 10.189 28.788 1.00 31.50 N -ANISOU 4561 N ILE C 182 4777 3201 3989 -785 1770 -914 N -ATOM 4562 CA ILE C 182 -10.369 8.870 29.319 1.00 31.73 C -ANISOU 4562 CA ILE C 182 4738 3377 3942 -773 1875 -779 C -ATOM 4563 C ILE C 182 -10.666 8.948 30.810 1.00 32.28 C -ANISOU 4563 C ILE C 182 4964 3548 3753 -663 2079 -835 C -ATOM 4564 O ILE C 182 -10.301 9.929 31.467 1.00 36.02 O -ANISOU 4564 O ILE C 182 5653 3990 4044 -612 2063 -1042 O -ATOM 4565 CB ILE C 182 -9.216 7.851 29.067 1.00 32.59 C -ANISOU 4565 CB ILE C 182 4833 3585 3964 -895 1685 -693 C -ATOM 4566 CG1 ILE C 182 -7.940 8.279 29.806 1.00 34.42 C -ANISOU 4566 CG1 ILE C 182 5264 3872 3944 -963 1561 -806 C -ATOM 4567 CG2 ILE C 182 -8.951 7.678 27.563 1.00 33.28 C -ANISOU 4567 CG2 ILE C 182 4777 3624 4245 -938 1512 -638 C -ATOM 4568 CD1 ILE C 182 -6.845 7.196 29.838 1.00 32.03 C -ANISOU 4568 CD1 ILE C 182 4940 3693 3536 -1051 1412 -700 C -ATOM 4569 N PRO C 183 -11.357 7.927 31.349 1.00 36.46 N -ANISOU 4569 N PRO C 183 5385 4195 4274 -609 2268 -645 N -ATOM 4570 CA PRO C 183 -11.547 7.849 32.805 1.00 37.91 C -ANISOU 4570 CA PRO C 183 5721 4548 4133 -472 2490 -636 C -ATOM 4571 C PRO C 183 -10.226 7.529 33.513 1.00 38.81 C -ANISOU 4571 C PRO C 183 6048 4791 3905 -541 2317 -692 C -ATOM 4572 O PRO C 183 -9.231 7.198 32.859 1.00 37.66 O -ANISOU 4572 O PRO C 183 5874 4603 3830 -703 2056 -688 O -ATOM 4573 CB PRO C 183 -12.562 6.703 32.980 1.00 42.86 C -ANISOU 4573 CB PRO C 183 6085 5248 4952 -427 2652 -308 C -ATOM 4574 CG PRO C 183 -12.483 5.907 31.730 1.00 39.04 C -ANISOU 4574 CG PRO C 183 5390 4631 4813 -603 2497 -202 C -ATOM 4575 CD PRO C 183 -12.106 6.879 30.630 1.00 33.80 C -ANISOU 4575 CD PRO C 183 4767 3821 4254 -652 2285 -418 C -ATOM 4576 N ASP C 184 -10.199 7.636 34.834 1.00 42.64 N -ANISOU 4576 N ASP C 184 6708 5451 4041 -384 2394 -722 N -ATOM 4577 CA ASP C 184 -8.976 7.300 35.550 1.00 49.44 C -ANISOU 4577 CA ASP C 184 7762 6450 4572 -436 2207 -764 C -ATOM 4578 C ASP C 184 -8.887 5.799 35.782 1.00 47.65 C -ANISOU 4578 C ASP C 184 7394 6364 4347 -482 2256 -426 C -ATOM 4579 O ASP C 184 -9.055 5.332 36.908 1.00 45.24 O -ANISOU 4579 O ASP C 184 7132 6275 3784 -334 2359 -276 O -ATOM 4580 CB ASP C 184 -8.855 8.054 36.880 1.00 54.93 C -ANISOU 4580 CB ASP C 184 8714 7292 4864 -223 2184 -965 C -ATOM 4581 CG ASP C 184 -7.443 7.982 37.460 1.00 53.54 C -ANISOU 4581 CG ASP C 184 8749 7206 4387 -302 1887 -1087 C -ATOM 4582 OD1 ASP C 184 -6.545 7.443 36.776 1.00 56.41 O -ANISOU 4582 OD1 ASP C 184 9054 7509 4871 -533 1715 -1017 O -ATOM 4583 OD2 ASP C 184 -7.223 8.471 38.583 1.00 51.79 O -ANISOU 4583 OD2 ASP C 184 8735 7130 3814 -124 1805 -1262 O -ATOM 4584 N LYS C 185 -8.646 5.062 34.698 1.00 46.14 N -ANISOU 4584 N LYS C 185 7020 6048 4464 -665 2165 -304 N -ATOM 4585 CA LYS C 185 -8.315 3.638 34.748 1.00 45.99 C -ANISOU 4585 CA LYS C 185 6875 6082 4515 -738 2118 -23 C -ATOM 4586 C LYS C 185 -6.865 3.499 34.320 1.00 38.61 C -ANISOU 4586 C LYS C 185 5996 5130 3544 -870 1787 -119 C -ATOM 4587 O LYS C 185 -6.362 4.329 33.556 1.00 35.87 O -ANISOU 4587 O LYS C 185 5669 4679 3283 -941 1617 -326 O -ATOM 4588 CB LYS C 185 -9.164 2.852 33.759 1.00 46.76 C -ANISOU 4588 CB LYS C 185 6675 6012 5080 -800 2161 162 C -ATOM 4589 CG LYS C 185 -10.630 2.704 34.129 1.00 54.25 C -ANISOU 4589 CG LYS C 185 7439 6970 6204 -676 2404 355 C -ATOM 4590 CD LYS C 185 -11.357 2.027 32.973 1.00 55.62 C -ANISOU 4590 CD LYS C 185 7320 6926 6888 -772 2332 470 C -ATOM 4591 CE LYS C 185 -12.861 2.059 33.146 1.00 59.97 C -ANISOU 4591 CE LYS C 185 7645 7458 7682 -672 2511 633 C -ATOM 4592 NZ LYS C 185 -13.352 0.820 33.799 1.00 63.54 N -ANISOU 4592 NZ LYS C 185 7911 7953 8277 -674 2565 984 N -ATOM 4593 N PHE C 186 -6.191 2.452 34.790 1.00 39.62 N -ANISOU 4593 N PHE C 186 6122 5358 3574 -894 1705 69 N -ATOM 4594 CA PHE C 186 -4.801 2.243 34.401 1.00 38.84 C -ANISOU 4594 CA PHE C 186 6034 5258 3465 -997 1407 12 C -ATOM 4595 C PHE C 186 -4.725 1.560 33.047 1.00 35.58 C -ANISOU 4595 C PHE C 186 5404 4682 3432 -1066 1303 68 C -ATOM 4596 O PHE C 186 -5.126 0.406 32.901 1.00 39.09 O -ANISOU 4596 O PHE C 186 5713 5062 4078 -1056 1342 269 O -ATOM 4597 CB PHE C 186 -4.025 1.442 35.453 1.00 42.71 C -ANISOU 4597 CB PHE C 186 6615 5925 3688 -970 1332 183 C -ATOM 4598 CG PHE C 186 -2.542 1.585 35.309 1.00 42.63 C -ANISOU 4598 CG PHE C 186 6642 5952 3604 -1054 1022 82 C -ATOM 4599 CD1 PHE C 186 -1.856 0.868 34.338 1.00 43.15 C -ANISOU 4599 CD1 PHE C 186 6528 5929 3939 -1119 872 158 C -ATOM 4600 CD2 PHE C 186 -1.841 2.479 36.101 1.00 45.98 C -ANISOU 4600 CD2 PHE C 186 7268 6491 3713 -1054 866 -105 C -ATOM 4601 CE1 PHE C 186 -0.490 1.022 34.172 1.00 44.47 C -ANISOU 4601 CE1 PHE C 186 6677 6147 4073 -1183 619 104 C -ATOM 4602 CE2 PHE C 186 -0.474 2.639 35.945 1.00 49.50 C -ANISOU 4602 CE2 PHE C 186 7690 6953 4164 -1154 560 -169 C -ATOM 4603 CZ PHE C 186 0.205 1.906 34.980 1.00 43.62 C -ANISOU 4603 CZ PHE C 186 6726 6145 3702 -1218 459 -38 C -ATOM 4604 N VAL C 187 -4.209 2.274 32.054 1.00 29.79 N -ANISOU 4604 N VAL C 187 4641 3876 2801 -1120 1160 -106 N -ATOM 4605 CA VAL C 187 -4.173 1.755 30.694 1.00 25.65 C -ANISOU 4605 CA VAL C 187 3945 3238 2562 -1126 1070 -94 C -ATOM 4606 C VAL C 187 -2.727 1.531 30.249 1.00 29.34 C -ANISOU 4606 C VAL C 187 4382 3769 2996 -1152 863 -98 C -ATOM 4607 O VAL C 187 -1.801 2.191 30.731 1.00 32.22 O -ANISOU 4607 O VAL C 187 4826 4226 3190 -1207 766 -150 O -ATOM 4608 CB VAL C 187 -4.908 2.695 29.727 1.00 29.56 C -ANISOU 4608 CB VAL C 187 4392 3627 3212 -1116 1119 -228 C -ATOM 4609 CG1 VAL C 187 -6.381 2.818 30.147 1.00 30.59 C -ANISOU 4609 CG1 VAL C 187 4502 3696 3425 -1071 1335 -192 C -ATOM 4610 CG2 VAL C 187 -4.245 4.065 29.733 1.00 32.83 C -ANISOU 4610 CG2 VAL C 187 4905 4066 3504 -1166 1057 -374 C -ATOM 4611 N VAL C 188 -2.538 0.574 29.347 1.00 25.02 N -ANISOU 4611 N VAL C 188 3710 3167 2631 -1096 783 -48 N -ATOM 4612 CA VAL C 188 -1.205 0.206 28.873 1.00 25.14 C -ANISOU 4612 CA VAL C 188 3664 3261 2629 -1067 626 -24 C -ATOM 4613 C VAL C 188 -1.295 -0.037 27.390 1.00 26.30 C -ANISOU 4613 C VAL C 188 3705 3351 2936 -958 585 -94 C -ATOM 4614 O VAL C 188 -2.399 -0.143 26.841 1.00 24.84 O -ANISOU 4614 O VAL C 188 3499 3045 2894 -920 628 -155 O -ATOM 4615 CB VAL C 188 -0.695 -1.093 29.560 1.00 24.23 C -ANISOU 4615 CB VAL C 188 3535 3164 2506 -1033 555 131 C -ATOM 4616 CG1 VAL C 188 -0.502 -0.870 31.042 1.00 25.77 C -ANISOU 4616 CG1 VAL C 188 3856 3472 2465 -1103 576 215 C -ATOM 4617 CG2 VAL C 188 -1.669 -2.252 29.321 1.00 24.55 C -ANISOU 4617 CG2 VAL C 188 3516 3026 2785 -973 585 197 C -ATOM 4618 N GLY C 189 -0.144 -0.151 26.734 1.00 24.31 N -ANISOU 4618 N GLY C 189 3378 3203 2655 -885 496 -79 N -ATOM 4619 CA GLY C 189 -0.150 -0.436 25.316 1.00 24.27 C -ANISOU 4619 CA GLY C 189 3300 3198 2723 -716 465 -151 C -ATOM 4620 C GLY C 189 0.136 0.822 24.519 1.00 23.50 C -ANISOU 4620 C GLY C 189 3159 3207 2562 -716 519 -159 C -ATOM 4621 O GLY C 189 0.107 1.925 25.073 1.00 26.96 O -ANISOU 4621 O GLY C 189 3630 3644 2970 -872 566 -139 O -ATOM 4622 N TYR C 190 0.385 0.656 23.224 1.00 24.76 N -ANISOU 4622 N TYR C 190 3254 3451 2702 -522 509 -184 N -ATOM 4623 CA TYR C 190 0.814 1.755 22.345 1.00 24.63 C -ANISOU 4623 CA TYR C 190 3161 3575 2624 -485 582 -106 C -ATOM 4624 C TYR C 190 1.939 2.572 23.009 1.00 26.89 C -ANISOU 4624 C TYR C 190 3359 3945 2913 -655 595 56 C -ATOM 4625 O TYR C 190 1.906 3.805 23.037 1.00 28.29 O -ANISOU 4625 O TYR C 190 3515 4096 3140 -790 633 114 O -ATOM 4626 CB TYR C 190 -0.382 2.632 21.961 1.00 21.91 C -ANISOU 4626 CB TYR C 190 2873 3131 2322 -527 632 -173 C -ATOM 4627 CG TYR C 190 -0.130 3.548 20.773 1.00 24.45 C -ANISOU 4627 CG TYR C 190 3116 3589 2584 -420 702 -69 C -ATOM 4628 CD1 TYR C 190 -0.014 3.045 19.487 1.00 24.06 C -ANISOU 4628 CD1 TYR C 190 3043 3695 2406 -137 694 -86 C -ATOM 4629 CD2 TYR C 190 -0.042 4.932 20.950 1.00 21.98 C -ANISOU 4629 CD2 TYR C 190 2765 3243 2343 -584 767 50 C -ATOM 4630 CE1 TYR C 190 0.213 3.906 18.384 1.00 27.25 C -ANISOU 4630 CE1 TYR C 190 3373 4270 2710 -7 788 68 C -ATOM 4631 CE2 TYR C 190 0.166 5.783 19.890 1.00 22.98 C -ANISOU 4631 CE2 TYR C 190 2800 3480 2451 -494 843 212 C -ATOM 4632 CZ TYR C 190 0.298 5.280 18.608 1.00 23.92 C -ANISOU 4632 CZ TYR C 190 2883 3803 2401 -203 872 248 C -ATOM 4633 OH TYR C 190 0.510 6.156 17.563 1.00 25.38 O -ANISOU 4633 OH TYR C 190 2974 4139 2531 -90 975 466 O -ATOM 4634 N ALA C 191 2.931 1.843 23.522 1.00 27.52 N -ANISOU 4634 N ALA C 191 3377 4101 2979 -643 531 126 N -ATOM 4635 CA ALA C 191 4.111 2.373 24.216 1.00 28.10 C -ANISOU 4635 CA ALA C 191 3336 4252 3087 -798 473 277 C -ATOM 4636 C ALA C 191 3.890 2.765 25.682 1.00 26.96 C -ANISOU 4636 C ALA C 191 3320 3987 2935 -1034 376 213 C -ATOM 4637 O ALA C 191 4.849 3.065 26.387 1.00 30.00 O -ANISOU 4637 O ALA C 191 3635 4419 3342 -1160 257 297 O -ATOM 4638 CB ALA C 191 4.793 3.512 23.430 1.00 25.76 C -ANISOU 4638 CB ALA C 191 2860 4062 2867 -823 538 456 C -ATOM 4639 N LEU C 192 2.641 2.762 26.143 1.00 25.23 N -ANISOU 4639 N LEU C 192 3280 3629 2678 -1072 419 68 N -ATOM 4640 CA LEU C 192 2.381 2.998 27.562 1.00 25.67 C -ANISOU 4640 CA LEU C 192 3485 3620 2649 -1221 362 3 C -ATOM 4641 C LEU C 192 2.672 1.731 28.339 1.00 30.22 C -ANISOU 4641 C LEU C 192 4091 4244 3147 -1173 299 62 C -ATOM 4642 O LEU C 192 2.307 0.642 27.908 1.00 29.88 O -ANISOU 4642 O LEU C 192 4028 4170 3157 -1040 340 80 O -ATOM 4643 CB LEU C 192 0.936 3.435 27.809 1.00 27.92 C -ANISOU 4643 CB LEU C 192 3921 3770 2917 -1241 479 -130 C -ATOM 4644 CG LEU C 192 0.691 4.917 27.514 1.00 36.16 C -ANISOU 4644 CG LEU C 192 4978 4728 4031 -1326 503 -198 C -ATOM 4645 CD1 LEU C 192 0.419 5.152 26.036 1.00 32.10 C -ANISOU 4645 CD1 LEU C 192 4346 4213 3637 -1227 584 -148 C -ATOM 4646 CD2 LEU C 192 -0.443 5.476 28.385 1.00 38.77 C -ANISOU 4646 CD2 LEU C 192 5491 4944 4296 -1362 584 -346 C -ATOM 4647 N ASP C 193 3.314 1.868 29.492 1.00 29.54 N -ANISOU 4647 N ASP C 193 4060 4216 2948 -1275 171 91 N -ATOM 4648 CA ASP C 193 3.775 0.693 30.207 1.00 30.24 C -ANISOU 4648 CA ASP C 193 4152 4372 2965 -1219 92 204 C -ATOM 4649 C ASP C 193 3.148 0.496 31.575 1.00 32.55 C -ANISOU 4649 C ASP C 193 4644 4668 3058 -1254 103 197 C -ATOM 4650 O ASP C 193 2.585 1.420 32.169 1.00 32.80 O -ANISOU 4650 O ASP C 193 4826 4679 2957 -1323 137 72 O -ATOM 4651 CB ASP C 193 5.282 0.765 30.405 1.00 30.57 C -ANISOU 4651 CB ASP C 193 4049 4541 3024 -1262 -100 313 C -ATOM 4652 CG ASP C 193 5.666 1.768 31.453 1.00 33.38 C -ANISOU 4652 CG ASP C 193 4500 4923 3261 -1428 -274 243 C -ATOM 4653 OD1 ASP C 193 5.237 2.933 31.334 1.00 33.11 O -ANISOU 4653 OD1 ASP C 193 4532 4797 3250 -1524 -253 105 O -ATOM 4654 OD2 ASP C 193 6.385 1.384 32.395 1.00 32.03 O -ANISOU 4654 OD2 ASP C 193 4346 4848 2974 -1449 -458 314 O -ATOM 4655 N TYR C 194 3.276 -0.730 32.068 1.00 30.98 N -ANISOU 4655 N TYR C 194 4441 4498 2831 -1176 81 349 N -ATOM 4656 CA TYR C 194 3.173 -1.002 33.491 1.00 35.11 C -ANISOU 4656 CA TYR C 194 5120 5110 3110 -1185 47 435 C -ATOM 4657 C TYR C 194 4.468 -1.709 33.877 1.00 38.49 C -ANISOU 4657 C TYR C 194 5456 5650 3518 -1157 -162 595 C -ATOM 4658 O TYR C 194 4.715 -2.844 33.450 1.00 34.28 O -ANISOU 4658 O TYR C 194 4800 5066 3158 -1057 -161 738 O -ATOM 4659 CB TYR C 194 1.965 -1.873 33.789 1.00 30.61 C -ANISOU 4659 CB TYR C 194 4605 4459 2568 -1114 243 555 C -ATOM 4660 CG TYR C 194 1.904 -2.321 35.216 1.00 34.15 C -ANISOU 4660 CG TYR C 194 5190 5039 2747 -1079 248 732 C -ATOM 4661 CD1 TYR C 194 1.352 -1.504 36.191 1.00 38.14 C -ANISOU 4661 CD1 TYR C 194 5897 5661 2932 -1080 333 650 C -ATOM 4662 CD2 TYR C 194 2.398 -3.560 35.597 1.00 38.11 C -ANISOU 4662 CD2 TYR C 194 5627 5559 3293 -1013 171 987 C -ATOM 4663 CE1 TYR C 194 1.288 -1.908 37.499 1.00 40.56 C -ANISOU 4663 CE1 TYR C 194 6349 6143 2919 -1000 357 828 C -ATOM 4664 CE2 TYR C 194 2.337 -3.974 36.910 1.00 44.61 C -ANISOU 4664 CE2 TYR C 194 6577 6533 3840 -961 185 1200 C -ATOM 4665 CZ TYR C 194 1.789 -3.142 37.855 1.00 45.64 C -ANISOU 4665 CZ TYR C 194 6916 6822 3601 -948 284 1124 C -ATOM 4666 OH TYR C 194 1.724 -3.557 39.164 1.00 52.86 O -ANISOU 4666 OH TYR C 194 7975 7939 4171 -849 317 1353 O -ATOM 4667 N ASN C 195 5.294 -1.023 34.668 1.00 34.92 N -ANISOU 4667 N ASN C 195 5060 5331 2878 -1237 -369 555 N -ATOM 4668 CA AASN C 195 6.618 -1.523 35.023 0.45 38.04 C -ANISOU 4668 CA AASN C 195 5333 5844 3276 -1225 -612 705 C -ATOM 4669 CA BASN C 195 6.636 -1.493 35.009 0.55 35.68 C -ANISOU 4669 CA BASN C 195 5031 5546 2980 -1228 -615 700 C -ATOM 4670 C ASN C 195 7.442 -2.010 33.821 1.00 39.18 C -ANISOU 4670 C ASN C 195 5196 5955 3737 -1164 -624 791 C -ATOM 4671 O ASN C 195 8.015 -3.103 33.864 1.00 39.04 O -ANISOU 4671 O ASN C 195 5070 5965 3798 -1049 -682 972 O -ATOM 4672 CB AASN C 195 6.493 -2.635 36.060 0.45 41.70 C -ANISOU 4672 CB AASN C 195 5898 6387 3560 -1124 -625 919 C -ATOM 4673 CB BASN C 195 6.594 -2.514 36.142 0.55 42.81 C -ANISOU 4673 CB BASN C 195 6045 6545 3676 -1136 -656 906 C -ATOM 4674 CG AASN C 195 7.784 -2.888 36.797 0.45 42.21 C -ANISOU 4674 CG AASN C 195 5900 6612 3524 -1120 -928 1051 C -ATOM 4675 CG BASN C 195 6.628 -1.856 37.499 0.55 46.48 C -ANISOU 4675 CG BASN C 195 6745 7172 3742 -1172 -806 834 C -ATOM 4676 OD1AASN C 195 8.708 -2.071 36.760 0.45 41.54 O -ANISOU 4676 OD1AASN C 195 5726 6589 3470 -1223 -1158 951 O -ATOM 4677 OD1BASN C 195 7.212 -0.783 37.658 0.55 49.08 O -ANISOU 4677 OD1BASN C 195 7097 7539 4011 -1280 -1022 643 O -ATOM 4678 ND2AASN C 195 7.858 -4.024 37.474 0.45 42.73 N -ANISOU 4678 ND2AASN C 195 5992 6735 3509 -1007 -947 1305 N -ATOM 4679 ND2BASN C 195 6.010 -2.490 38.488 0.55 52.88 N -ANISOU 4679 ND2BASN C 195 7731 8079 4282 -1067 -705 993 N -ATOM 4680 N GLU C 196 7.479 -1.193 32.764 1.00 36.95 N -ANISOU 4680 N GLU C 196 4801 5621 3619 -1211 -554 676 N -ATOM 4681 CA GLU C 196 8.223 -1.454 31.519 1.00 38.68 C -ANISOU 4681 CA GLU C 196 4758 5858 4082 -1113 -513 752 C -ATOM 4682 C GLU C 196 7.581 -2.481 30.583 1.00 37.40 C -ANISOU 4682 C GLU C 196 4584 5595 4031 -916 -327 745 C -ATOM 4683 O GLU C 196 7.959 -2.578 29.415 1.00 37.13 O -ANISOU 4683 O GLU C 196 4388 5586 4134 -786 -250 747 O -ATOM 4684 CB GLU C 196 9.699 -1.784 31.787 1.00 42.66 C -ANISOU 4684 CB GLU C 196 5041 6501 4665 -1093 -722 934 C -ATOM 4685 CG GLU C 196 10.442 -0.675 32.523 1.00 46.46 C -ANISOU 4685 CG GLU C 196 5484 7054 5116 -1303 -977 918 C -ATOM 4686 CD GLU C 196 10.317 0.687 31.834 1.00 51.83 C -ANISOU 4686 CD GLU C 196 6100 7664 5927 -1445 -927 811 C -ATOM 4687 OE1 GLU C 196 10.362 0.744 30.584 1.00 44.44 O -ANISOU 4687 OE1 GLU C 196 4991 6729 5164 -1358 -734 870 O -ATOM 4688 OE2 GLU C 196 10.174 1.703 32.552 1.00 55.55 O -ANISOU 4688 OE2 GLU C 196 6708 8079 6321 -1625 -1090 668 O -ATOM 4689 N TYR C 197 6.592 -3.220 31.074 1.00 33.74 N -ANISOU 4689 N TYR C 197 4287 5015 3515 -883 -260 739 N -ATOM 4690 CA TYR C 197 5.874 -4.166 30.219 1.00 34.04 C -ANISOU 4690 CA TYR C 197 4321 4894 3718 -723 -145 698 C -ATOM 4691 C TYR C 197 4.722 -3.514 29.465 1.00 29.76 C -ANISOU 4691 C TYR C 197 3853 4253 3202 -754 4 520 C -ATOM 4692 O TYR C 197 4.299 -2.406 29.811 1.00 29.24 O -ANISOU 4692 O TYR C 197 3873 4217 3021 -903 50 447 O -ATOM 4693 CB TYR C 197 5.360 -5.357 31.032 1.00 38.51 C -ANISOU 4693 CB TYR C 197 4973 5338 4323 -683 -163 833 C -ATOM 4694 CG TYR C 197 6.475 -6.277 31.459 1.00 47.07 C -ANISOU 4694 CG TYR C 197 5956 6476 5452 -581 -313 1022 C -ATOM 4695 CD1 TYR C 197 6.884 -7.324 30.644 1.00 49.14 C -ANISOU 4695 CD1 TYR C 197 6101 6630 5942 -368 -346 1028 C -ATOM 4696 CD2 TYR C 197 7.143 -6.079 32.664 1.00 48.01 C -ANISOU 4696 CD2 TYR C 197 6103 6758 5381 -669 -445 1175 C -ATOM 4697 CE1 TYR C 197 7.914 -8.158 31.019 1.00 52.02 C -ANISOU 4697 CE1 TYR C 197 6357 7033 6376 -250 -479 1207 C -ATOM 4698 CE2 TYR C 197 8.172 -6.908 33.050 1.00 50.75 C -ANISOU 4698 CE2 TYR C 197 6338 7161 5783 -568 -601 1368 C -ATOM 4699 CZ TYR C 197 8.555 -7.944 32.222 1.00 54.24 C -ANISOU 4699 CZ TYR C 197 6641 7480 6486 -360 -605 1396 C -ATOM 4700 OH TYR C 197 9.583 -8.772 32.601 1.00 61.07 O -ANISOU 4700 OH TYR C 197 7381 8388 7434 -235 -756 1596 O -ATOM 4701 N PHE C 198 4.238 -4.219 28.439 1.00 26.82 N -ANISOU 4701 N PHE C 198 3229 3465 3496 -1125 71 -96 N -ATOM 4702 CA PHE C 198 3.059 -3.848 27.648 1.00 25.69 C -ANISOU 4702 CA PHE C 198 3235 3204 3322 -1049 275 -174 C -ATOM 4703 C PHE C 198 3.331 -2.741 26.620 1.00 26.27 C -ANISOU 4703 C PHE C 198 3336 3146 3499 -1023 464 -322 C -ATOM 4704 O PHE C 198 2.430 -2.332 25.899 1.00 27.98 O -ANISOU 4704 O PHE C 198 3669 3270 3691 -946 611 -366 O -ATOM 4705 CB PHE C 198 1.869 -3.446 28.537 1.00 27.05 C -ANISOU 4705 CB PHE C 198 3542 3487 3251 -1109 327 -198 C -ATOM 4706 CG PHE C 198 1.413 -4.524 29.502 1.00 28.17 C -ANISOU 4706 CG PHE C 198 3668 3764 3272 -1126 205 13 C -ATOM 4707 CD1 PHE C 198 0.658 -5.598 29.058 1.00 29.30 C -ANISOU 4707 CD1 PHE C 198 3778 3803 3551 -1048 195 182 C -ATOM 4708 CD2 PHE C 198 1.717 -4.435 30.857 1.00 32.51 C -ANISOU 4708 CD2 PHE C 198 4249 4538 3564 -1229 93 49 C -ATOM 4709 CE1 PHE C 198 0.219 -6.589 29.948 1.00 28.54 C -ANISOU 4709 CE1 PHE C 198 3648 3797 3398 -1079 109 433 C -ATOM 4710 CE2 PHE C 198 1.290 -5.415 31.761 1.00 32.08 C -ANISOU 4710 CE2 PHE C 198 4193 4626 3369 -1234 12 309 C -ATOM 4711 CZ PHE C 198 0.545 -6.497 31.307 1.00 34.03 C -ANISOU 4711 CZ PHE C 198 4375 4741 3814 -1162 38 525 C -ATOM 4712 N ARG C 199 4.563 -2.249 26.562 1.00 24.00 N -ANISOU 4712 N ARG C 199 2919 2849 3352 -1092 455 -362 N -ATOM 4713 CA ARG C 199 4.903 -1.240 25.561 1.00 26.48 C -ANISOU 4713 CA ARG C 199 3236 3022 3805 -1074 667 -434 C -ATOM 4714 C ARG C 199 4.783 -1.840 24.157 1.00 31.40 C -ANISOU 4714 C ARG C 199 3894 3545 4491 -862 814 -358 C -ATOM 4715 O ARG C 199 4.461 -1.137 23.199 1.00 36.07 O -ANISOU 4715 O ARG C 199 4591 4039 5076 -787 1009 -378 O -ATOM 4716 CB ARG C 199 6.314 -0.685 25.777 1.00 28.32 C -ANISOU 4716 CB ARG C 199 3258 3252 4251 -1213 626 -450 C -ATOM 4717 CG ARG C 199 6.552 0.040 27.114 1.00 27.25 C -ANISOU 4717 CG ARG C 199 3117 3202 4035 -1447 429 -590 C -ATOM 4718 CD ARG C 199 7.631 1.083 26.967 1.00 29.58 C -ANISOU 4718 CD ARG C 199 3245 3386 4610 -1615 454 -658 C -ATOM 4719 NE ARG C 199 8.198 1.574 28.233 1.00 32.71 N -ANISOU 4719 NE ARG C 199 3585 3869 4974 -1863 162 -810 N -ATOM 4720 CZ ARG C 199 7.736 2.623 28.907 1.00 33.33 C -ANISOU 4720 CZ ARG C 199 3864 3884 4914 -2009 134 -1059 C -ATOM 4721 NH1 ARG C 199 6.671 3.279 28.462 1.00 36.20 N -ANISOU 4721 NH1 ARG C 199 4463 4097 5194 -1898 395 -1133 N -ATOM 4722 NH2 ARG C 199 8.313 2.996 30.042 1.00 35.48 N -ANISOU 4722 NH2 ARG C 199 4119 4249 5112 -2203 -178 -1215 N -ATOM 4723 N ASP C 200 5.026 -3.146 24.065 1.00 30.00 N -ANISOU 4723 N ASP C 200 3652 3387 4359 -756 707 -273 N -ATOM 4724 CA ASP C 200 5.054 -3.900 22.813 1.00 32.92 C -ANISOU 4724 CA ASP C 200 4081 3657 4769 -542 813 -256 C -ATOM 4725 C ASP C 200 3.671 -4.438 22.447 1.00 34.97 C -ANISOU 4725 C ASP C 200 4541 3864 4882 -465 744 -288 C -ATOM 4726 O ASP C 200 3.517 -5.590 22.031 1.00 42.89 O -ANISOU 4726 O ASP C 200 5587 4787 5922 -345 659 -287 O -ATOM 4727 CB ASP C 200 6.013 -5.079 22.950 1.00 34.94 C -ANISOU 4727 CB ASP C 200 4166 3905 5207 -454 722 -174 C -ATOM 4728 CG ASP C 200 5.598 -6.033 24.050 1.00 38.18 C -ANISOU 4728 CG ASP C 200 4547 4356 5603 -518 459 -88 C -ATOM 4729 OD1 ASP C 200 5.100 -5.551 25.090 1.00 33.29 O -ANISOU 4729 OD1 ASP C 200 3949 3855 4845 -689 351 -75 O -ATOM 4730 OD2 ASP C 200 5.744 -7.261 23.859 1.00 40.02 O -ANISOU 4730 OD2 ASP C 200 4756 4490 5961 -386 382 -28 O -ATOM 4731 N LEU C 201 2.668 -3.597 22.627 1.00 37.07 N -ANISOU 4731 N LEU C 201 4908 4151 5024 -538 770 -321 N -ATOM 4732 CA LEU C 201 1.279 -3.947 22.380 1.00 33.86 C -ANISOU 4732 CA LEU C 201 4622 3712 4531 -496 687 -324 C -ATOM 4733 C LEU C 201 0.756 -2.789 21.537 1.00 31.25 C -ANISOU 4733 C LEU C 201 4410 3348 4115 -436 841 -359 C -ATOM 4734 O LEU C 201 1.020 -1.640 21.863 1.00 27.01 O -ANISOU 4734 O LEU C 201 3853 2818 3590 -510 974 -373 O -ATOM 4735 CB LEU C 201 0.546 -4.066 23.718 1.00 33.63 C -ANISOU 4735 CB LEU C 201 4534 3773 4469 -635 581 -264 C -ATOM 4736 CG LEU C 201 -0.967 -4.226 23.820 1.00 35.13 C -ANISOU 4736 CG LEU C 201 4757 3960 4632 -641 530 -218 C -ATOM 4737 CD1 LEU C 201 -1.420 -5.521 23.153 1.00 40.10 C -ANISOU 4737 CD1 LEU C 201 5398 4473 5365 -577 358 -184 C -ATOM 4738 CD2 LEU C 201 -1.410 -4.183 25.307 1.00 27.37 C -ANISOU 4738 CD2 LEU C 201 3705 3114 3580 -768 527 -136 C -ATOM 4739 N ASN C 202 0.057 -3.073 20.438 1.00 30.30 N -ANISOU 4739 N ASN C 202 4421 3175 3917 -301 801 -373 N -ATOM 4740 CA AASN C 202 -0.351 -1.987 19.546 0.47 28.64 C -ANISOU 4740 CA AASN C 202 4328 2944 3609 -213 933 -352 C -ATOM 4741 CA BASN C 202 -0.393 -2.036 19.500 0.53 28.83 C -ANISOU 4741 CA BASN C 202 4359 2968 3629 -206 924 -353 C -ATOM 4742 C ASN C 202 -1.611 -1.254 20.005 1.00 28.14 C -ANISOU 4742 C ASN C 202 4245 2886 3562 -258 908 -311 C -ATOM 4743 O ASN C 202 -1.756 -0.061 19.752 1.00 31.82 O -ANISOU 4743 O ASN C 202 4753 3311 4027 -226 1061 -271 O -ATOM 4744 CB AASN C 202 -0.441 -2.435 18.073 0.47 30.27 C -ANISOU 4744 CB AASN C 202 4718 3129 3656 -23 903 -379 C -ATOM 4745 CB BASN C 202 -0.716 -2.677 18.142 0.53 30.22 C -ANISOU 4745 CB BASN C 202 4709 3118 3654 -31 832 -390 C -ATOM 4746 CG AASN C 202 -1.472 -3.527 17.845 0.47 29.89 C -ANISOU 4746 CG AASN C 202 4722 3052 3585 0 611 -441 C -ATOM 4747 CG BASN C 202 -0.046 -1.970 16.977 0.53 37.42 C -ANISOU 4747 CG BASN C 202 5763 4040 4415 119 1057 -351 C -ATOM 4748 OD1AASN C 202 -1.819 -4.267 18.762 0.47 26.79 O -ANISOU 4748 OD1AASN C 202 4200 2637 3341 -120 463 -438 O -ATOM 4749 OD1BASN C 202 0.882 -1.176 17.159 0.53 45.70 O -ANISOU 4749 OD1BASN C 202 6734 5083 5548 77 1295 -284 O -ATOM 4750 ND2AASN C 202 -1.963 -3.635 16.609 0.47 28.92 N -ANISOU 4750 ND2AASN C 202 4791 2925 3274 145 513 -485 N -ATOM 4751 ND2BASN C 202 -0.512 -2.263 15.766 0.53 43.97 N -ANISOU 4751 ND2BASN C 202 6804 4886 5016 288 974 -381 N -ATOM 4752 N HIS C 203 -2.502 -1.944 20.712 1.00 28.46 N -ANISOU 4752 N HIS C 203 4200 2958 3655 -326 746 -297 N -ATOM 4753 CA HIS C 203 -3.714 -1.298 21.210 1.00 24.60 C -ANISOU 4753 CA HIS C 203 3646 2487 3215 -344 771 -242 C -ATOM 4754 C HIS C 203 -3.491 -0.729 22.611 1.00 28.07 C -ANISOU 4754 C HIS C 203 4017 2978 3670 -463 913 -276 C -ATOM 4755 O HIS C 203 -2.619 -1.206 23.343 1.00 28.75 O -ANISOU 4755 O HIS C 203 4072 3120 3731 -565 885 -310 O -ATOM 4756 CB HIS C 203 -4.855 -2.306 21.319 1.00 23.83 C -ANISOU 4756 CB HIS C 203 3447 2405 3201 -367 559 -176 C -ATOM 4757 CG HIS C 203 -5.041 -3.162 20.112 1.00 24.07 C -ANISOU 4757 CG HIS C 203 3563 2375 3209 -291 329 -207 C -ATOM 4758 ND1 HIS C 203 -5.518 -2.670 18.918 1.00 27.24 N -ANISOU 4758 ND1 HIS C 203 4071 2761 3517 -157 262 -201 N -ATOM 4759 CD2 HIS C 203 -4.827 -4.486 19.921 1.00 25.93 C -ANISOU 4759 CD2 HIS C 203 3817 2546 3489 -321 132 -260 C -ATOM 4760 CE1 HIS C 203 -5.593 -3.656 18.040 1.00 28.38 C -ANISOU 4760 CE1 HIS C 203 4320 2860 3603 -115 18 -284 C -ATOM 4761 NE2 HIS C 203 -5.180 -4.764 18.623 1.00 26.26 N -ANISOU 4761 NE2 HIS C 203 4000 2535 3443 -213 -54 -337 N -ATOM 4762 N VAL C 204 -4.308 0.252 23.005 1.00 22.87 N -ANISOU 4762 N VAL C 204 3340 2305 3044 -436 1051 -271 N -ATOM 4763 CA VAL C 204 -4.388 0.637 24.414 1.00 22.09 C -ANISOU 4763 CA VAL C 204 3213 2277 2904 -526 1174 -338 C -ATOM 4764 C VAL C 204 -5.388 -0.282 25.096 1.00 28.53 C -ANISOU 4764 C VAL C 204 3899 3209 3730 -550 1111 -220 C -ATOM 4765 O VAL C 204 -6.476 -0.521 24.572 1.00 31.15 O -ANISOU 4765 O VAL C 204 4129 3520 4186 -476 1056 -104 O -ATOM 4766 CB VAL C 204 -4.780 2.105 24.591 1.00 21.26 C -ANISOU 4766 CB VAL C 204 3165 2068 2846 -460 1396 -419 C -ATOM 4767 CG1 VAL C 204 -5.140 2.400 26.048 1.00 25.93 C -ANISOU 4767 CG1 VAL C 204 3761 2750 3342 -511 1536 -520 C -ATOM 4768 CG2 VAL C 204 -3.641 3.017 24.131 1.00 25.47 C -ANISOU 4768 CG2 VAL C 204 3806 2455 3416 -493 1472 -513 C -ATOM 4769 N CYS C 205 -5.010 -0.819 26.252 1.00 28.39 N -ANISOU 4769 N CYS C 205 3870 3322 3597 -662 1103 -218 N -ATOM 4770 CA CYS C 205 -5.813 -1.824 26.941 1.00 30.76 C -ANISOU 4770 CA CYS C 205 4040 3734 3915 -704 1064 -41 C -ATOM 4771 C CYS C 205 -5.815 -1.546 28.419 1.00 31.14 C -ANISOU 4771 C CYS C 205 4130 3955 3746 -757 1230 -63 C -ATOM 4772 O CYS C 205 -4.888 -0.932 28.941 1.00 30.75 O -ANISOU 4772 O CYS C 205 4221 3944 3519 -807 1256 -237 O -ATOM 4773 CB CYS C 205 -5.252 -3.230 26.682 1.00 31.35 C -ANISOU 4773 CB CYS C 205 4074 3785 4055 -775 821 63 C -ATOM 4774 N VAL C 206 -6.859 -2.002 29.098 1.00 29.70 N -ANISOU 4774 N VAL C 206 3825 3886 3573 -750 1339 119 N -ATOM 4775 CA VAL C 206 -6.888 -1.940 30.545 1.00 38.94 C -ANISOU 4775 CA VAL C 206 5064 5272 4458 -784 1510 138 C -ATOM 4776 C VAL C 206 -6.224 -3.211 31.055 1.00 38.56 C -ANISOU 4776 C VAL C 206 4999 5326 4328 -904 1307 328 C -ATOM 4777 O VAL C 206 -6.557 -4.316 30.627 1.00 36.73 O -ANISOU 4777 O VAL C 206 4611 5013 4332 -942 1165 554 O -ATOM 4778 CB VAL C 206 -8.325 -1.833 31.084 1.00 40.21 C -ANISOU 4778 CB VAL C 206 5081 5531 4665 -695 1798 297 C -ATOM 4779 CG1 VAL C 206 -8.322 -1.665 32.598 1.00 38.97 C -ANISOU 4779 CG1 VAL C 206 5048 5629 4129 -672 1982 291 C -ATOM 4780 CG2 VAL C 206 -9.040 -0.658 30.436 1.00 43.77 C -ANISOU 4780 CG2 VAL C 206 5498 5840 5293 -539 1968 157 C -ATOM 4781 N ILE C 207 -5.259 -3.042 31.950 1.00 38.91 N -ANISOU 4781 N ILE C 207 5204 5520 4059 -966 1263 230 N -ATOM 4782 CA ILE C 207 -4.552 -4.162 32.560 1.00 38.52 C -ANISOU 4782 CA ILE C 207 5143 5587 3907 -1058 1060 440 C -ATOM 4783 C ILE C 207 -5.453 -4.810 33.612 1.00 44.14 C -ANISOU 4783 C ILE C 207 5801 6499 4469 -1061 1228 750 C -ATOM 4784 O ILE C 207 -6.204 -4.112 34.294 1.00 47.76 O -ANISOU 4784 O ILE C 207 6325 7111 4709 -996 1522 698 O -ATOM 4785 CB ILE C 207 -3.222 -3.663 33.194 1.00 49.00 C -ANISOU 4785 CB ILE C 207 6639 7037 4942 -1125 913 239 C -ATOM 4786 CG1 ILE C 207 -2.355 -4.826 33.688 1.00 47.24 C -ANISOU 4786 CG1 ILE C 207 6368 6914 4669 -1195 646 484 C -ATOM 4787 CG2 ILE C 207 -3.497 -2.645 34.317 1.00 52.18 C -ANISOU 4787 CG2 ILE C 207 7247 7648 4931 -1111 1117 41 C -ATOM 4788 CD1 ILE C 207 -0.964 -4.389 34.167 1.00 48.76 C -ANISOU 4788 CD1 ILE C 207 6653 7216 4658 -1273 419 306 C -ATOM 4789 N SER C 208 -5.399 -6.139 33.726 1.00 37.79 N -ANISOU 4789 N SER C 208 4874 5676 3809 -1123 1075 1087 N -ATOM 4790 CA SER C 208 -6.170 -6.859 34.731 1.00 48.00 C -ANISOU 4790 CA SER C 208 6098 7146 4994 -1141 1240 1463 C -ATOM 4791 C SER C 208 -5.460 -6.864 36.092 1.00 53.33 C -ANISOU 4791 C SER C 208 6979 8120 5165 -1139 1215 1519 C -ATOM 4792 O SER C 208 -4.319 -6.420 36.208 1.00 52.00 O -ANISOU 4792 O SER C 208 6964 8035 4760 -1183 1017 1301 O -ATOM 4793 CB SER C 208 -6.420 -8.302 34.289 1.00 49.86 C -ANISOU 4793 CB SER C 208 6132 7139 5674 -1184 1053 1769 C -ATOM 4794 OG SER C 208 -5.219 -9.044 34.222 1.00 47.37 O -ANISOU 4794 OG SER C 208 5849 6775 5376 -1252 759 1873 O -ATOM 4795 N GLU C 209 -6.138 -7.366 37.122 1.00 54.80 N -ANISOU 4795 N GLU C 209 7177 8419 5225 -1071 1385 1773 N -ATOM 4796 CA GLU C 209 -5.503 -7.511 38.433 1.00 58.95 C -ANISOU 4796 CA GLU C 209 7913 9230 5257 -1052 1326 1871 C -ATOM 4797 C GLU C 209 -4.422 -8.595 38.372 1.00 58.01 C -ANISOU 4797 C GLU C 209 7724 9081 5237 -1146 945 2129 C -ATOM 4798 O GLU C 209 -3.357 -8.448 38.964 1.00 60.47 O -ANISOU 4798 O GLU C 209 8186 9601 5187 -1175 718 2084 O -ATOM 4799 CB GLU C 209 -6.534 -7.817 39.528 1.00 68.09 C -ANISOU 4799 CB GLU C 209 9123 10497 6249 -967 1639 2099 C -ATOM 4800 CG GLU C 209 -7.792 -6.941 39.486 1.00 75.23 C -ANISOU 4800 CG GLU C 209 10024 11360 7198 -886 2046 1913 C -ATOM 4801 CD GLU C 209 -7.516 -5.453 39.696 1.00 82.16 C -ANISOU 4801 CD GLU C 209 11162 12346 7708 -762 2177 1474 C -ATOM 4802 OE1 GLU C 209 -8.334 -4.628 39.230 1.00 83.44 O -ANISOU 4802 OE1 GLU C 209 11273 12380 8050 -688 2440 1272 O -ATOM 4803 OE2 GLU C 209 -6.496 -5.106 40.333 1.00 86.20 O -ANISOU 4803 OE2 GLU C 209 11909 13063 7780 -742 1982 1318 O -ATOM 4804 N THR C 210 -4.695 -9.670 37.635 1.00 58.90 N -ANISOU 4804 N THR C 210 7604 8901 5874 -1183 848 2373 N -ATOM 4805 CA THR C 210 -3.711 -10.734 37.427 1.00 62.15 C -ANISOU 4805 CA THR C 210 7930 9185 6499 -1232 508 2604 C -ATOM 4806 C THR C 210 -2.430 -10.195 36.782 1.00 59.69 C -ANISOU 4806 C THR C 210 7669 8872 6138 -1292 248 2365 C -ATOM 4807 O THR C 210 -1.320 -10.555 37.184 1.00 60.41 O -ANISOU 4807 O THR C 210 7784 9046 6124 -1290 -30 2461 O -ATOM 4808 CB THR C 210 -4.293 -11.879 36.571 1.00 68.99 C -ANISOU 4808 CB THR C 210 8566 9652 7995 -1244 452 2776 C -ATOM 4809 OG1 THR C 210 -5.381 -12.492 37.275 1.00 74.86 O -ANISOU 4809 OG1 THR C 210 9238 10406 8798 -1222 651 3032 O -ATOM 4810 CG2 THR C 210 -3.230 -12.935 36.278 1.00 72.27 C -ANISOU 4810 CG2 THR C 210 8909 9868 8683 -1251 123 2957 C -ATOM 4811 N GLY C 211 -2.591 -9.319 35.791 1.00 51.45 N -ANISOU 4811 N GLY C 211 6621 7667 5259 -1274 324 1952 N -ATOM 4812 CA GLY C 211 -1.458 -8.690 35.141 1.00 45.15 C -ANISOU 4812 CA GLY C 211 5856 6784 4514 -1263 130 1592 C -ATOM 4813 C GLY C 211 -0.698 -7.764 36.076 1.00 47.57 C -ANISOU 4813 C GLY C 211 6341 7399 4333 -1299 54 1392 C -ATOM 4814 O GLY C 211 0.531 -7.707 36.038 1.00 49.82 O -ANISOU 4814 O GLY C 211 6600 7695 4637 -1324 -218 1300 O -ATOM 4815 N LYS C 212 -1.429 -7.037 36.916 1.00 50.21 N -ANISOU 4815 N LYS C 212 6851 7979 4249 -1297 290 1312 N -ATOM 4816 CA LYS C 212 -0.818 -6.110 37.861 1.00 56.39 C -ANISOU 4816 CA LYS C 212 7862 9046 4519 -1338 209 1055 C -ATOM 4817 C LYS C 212 0.085 -6.839 38.851 1.00 58.69 C -ANISOU 4817 C LYS C 212 8189 9595 4516 -1378 -115 1335 C -ATOM 4818 O LYS C 212 1.110 -6.308 39.279 1.00 57.80 O -ANISOU 4818 O LYS C 212 8166 9628 4166 -1446 -397 1121 O -ATOM 4819 CB LYS C 212 -1.896 -5.329 38.615 1.00 64.20 C -ANISOU 4819 CB LYS C 212 9060 10241 5091 -1285 579 930 C -ATOM 4820 CG LYS C 212 -2.388 -4.089 37.887 1.00 67.49 C -ANISOU 4820 CG LYS C 212 9517 10457 5670 -1245 813 503 C -ATOM 4821 CD LYS C 212 -3.611 -3.483 38.573 1.00 74.20 C -ANISOU 4821 CD LYS C 212 10484 11383 6326 -1069 1206 430 C -ATOM 4822 CE LYS C 212 -4.026 -2.180 37.893 1.00 72.16 C -ANISOU 4822 CE LYS C 212 10258 10905 6256 -1001 1402 26 C -ATOM 4823 NZ LYS C 212 -5.204 -1.549 38.552 1.00 75.14 N -ANISOU 4823 NZ LYS C 212 10702 11338 6511 -767 1765 -26 N -ATOM 4824 N ALA C 213 -0.305 -8.061 39.201 1.00 58.49 N -ANISOU 4824 N ALA C 213 8073 9607 4543 -1342 -97 1836 N -ATOM 4825 CA ALA C 213 0.416 -8.853 40.191 1.00 62.18 C -ANISOU 4825 CA ALA C 213 8559 10274 4794 -1321 -377 2162 C -ATOM 4826 C ALA C 213 1.624 -9.589 39.609 1.00 61.14 C -ANISOU 4826 C ALA C 213 8207 9981 5041 -1351 -774 2334 C -ATOM 4827 O ALA C 213 2.639 -9.748 40.288 1.00 65.31 O -ANISOU 4827 O ALA C 213 8742 10705 5369 -1360 -1119 2428 O -ATOM 4828 CB ALA C 213 -0.528 -9.832 40.874 1.00 63.51 C -ANISOU 4828 CB ALA C 213 8709 10430 4992 -1211 -150 2571 C -ATOM 4829 N LYS C 214 1.508 -10.053 38.367 1.00 53.91 N -ANISOU 4829 N LYS C 214 7081 8659 4743 -1314 -713 2318 N -ATOM 4830 CA LYS C 214 2.610 -10.753 37.707 1.00 58.28 C -ANISOU 4830 CA LYS C 214 7412 8974 5758 -1268 -1002 2402 C -ATOM 4831 C LYS C 214 3.780 -9.807 37.436 1.00 55.12 C -ANISOU 4831 C LYS C 214 6972 8625 5347 -1312 -1211 2015 C -ATOM 4832 O LYS C 214 4.948 -10.195 37.542 1.00 56.91 O -ANISOU 4832 O LYS C 214 7034 8870 5720 -1290 -1529 2138 O -ATOM 4833 CB LYS C 214 2.146 -11.384 36.384 1.00 58.17 C -ANISOU 4833 CB LYS C 214 7245 8511 6345 -1205 -857 2390 C -ATOM 4834 CG LYS C 214 3.220 -12.220 35.674 1.00 61.80 C -ANISOU 4834 CG LYS C 214 7495 8693 7293 -1107 -1086 2474 C -ATOM 4835 CD LYS C 214 2.839 -12.551 34.231 1.00 60.35 C -ANISOU 4835 CD LYS C 214 7240 8086 7604 -1038 -939 2288 C -ATOM 4836 CE LYS C 214 1.510 -13.289 34.153 1.00 64.29 C -ANISOU 4836 CE LYS C 214 7765 8403 8259 -1067 -778 2503 C -ATOM 4837 NZ LYS C 214 1.096 -13.526 32.741 1.00 63.01 N -ANISOU 4837 NZ LYS C 214 7571 7855 8516 -1019 -696 2260 N -ATOM 4838 N TYR C 215 3.456 -8.562 37.097 1.00 49.39 N -ANISOU 4838 N TYR C 215 6368 7903 4495 -1374 -1027 1576 N -ATOM 4839 CA TYR C 215 4.456 -7.606 36.624 1.00 47.86 C -ANISOU 4839 CA TYR C 215 6105 7663 4418 -1439 -1163 1204 C -ATOM 4840 C TYR C 215 4.845 -6.530 37.631 1.00 54.62 C -ANISOU 4840 C TYR C 215 7144 8825 4785 -1573 -1325 941 C -ATOM 4841 O TYR C 215 5.664 -5.665 37.326 1.00 60.09 O -ANISOU 4841 O TYR C 215 7768 9462 5600 -1669 -1456 632 O -ATOM 4842 CB TYR C 215 3.986 -6.953 35.324 1.00 45.94 C -ANISOU 4842 CB TYR C 215 5846 7121 4489 -1413 -874 896 C -ATOM 4843 CG TYR C 215 3.847 -7.936 34.195 1.00 49.03 C -ANISOU 4843 CG TYR C 215 6072 7197 5359 -1288 -792 1057 C -ATOM 4844 CD1 TYR C 215 4.962 -8.583 33.674 1.00 48.16 C -ANISOU 4844 CD1 TYR C 215 5740 6947 5612 -1216 -974 1158 C -ATOM 4845 CD2 TYR C 215 2.601 -8.221 33.647 1.00 50.73 C -ANISOU 4845 CD2 TYR C 215 6347 7248 5679 -1236 -543 1092 C -ATOM 4846 CE1 TYR C 215 4.836 -9.492 32.638 1.00 49.29 C -ANISOU 4846 CE1 TYR C 215 5784 6781 6161 -1079 -888 1247 C -ATOM 4847 CE2 TYR C 215 2.468 -9.123 32.609 1.00 50.82 C -ANISOU 4847 CE2 TYR C 215 6248 6957 6105 -1136 -517 1181 C -ATOM 4848 CZ TYR C 215 3.587 -9.755 32.110 1.00 51.73 C -ANISOU 4848 CZ TYR C 215 6203 6925 6529 -1051 -680 1236 C -ATOM 4849 OH TYR C 215 3.447 -10.654 31.076 1.00 54.61 O -ANISOU 4849 OH TYR C 215 6508 6968 7271 -931 -641 1267 O -ATOM 4850 N LYS C 216 4.272 -6.577 38.828 1.00 52.59 N -ANISOU 4850 N LYS C 216 7125 8881 3975 -1584 -1312 1059 N -ATOM 4851 CA LYS C 216 4.647 -5.611 39.856 1.00 64.12 C -ANISOU 4851 CA LYS C 216 8821 10647 4896 -1702 -1503 768 C -ATOM 4852 C LYS C 216 6.092 -5.833 40.295 1.00 71.37 C -ANISOU 4852 C LYS C 216 9574 11718 5826 -1788 -2038 856 C -ATOM 4853 O LYS C 216 6.592 -6.959 40.281 1.00 71.90 O -ANISOU 4853 O LYS C 216 9416 11782 6120 -1711 -2238 1285 O -ATOM 4854 CB LYS C 216 3.707 -5.685 41.060 1.00 67.35 C -ANISOU 4854 CB LYS C 216 9535 11340 4714 -1620 -1308 877 C -ATOM 4855 CG LYS C 216 4.229 -6.504 42.226 1.00 75.36 C -ANISOU 4855 CG LYS C 216 10572 12591 5470 -1539 -1586 1216 C -ATOM 4856 CD LYS C 216 3.229 -6.480 43.361 1.00 82.63 C -ANISOU 4856 CD LYS C 216 11802 13712 5881 -1394 -1294 1274 C -ATOM 4857 CE LYS C 216 2.787 -5.052 43.649 1.00 85.85 C -ANISOU 4857 CE LYS C 216 12500 14141 5980 -1387 -1093 718 C -ATOM 4858 NZ LYS C 216 1.475 -5.002 44.353 1.00 90.15 N -ANISOU 4858 NZ LYS C 216 13292 14781 6179 -1200 -635 784 N -ATOM 4859 N ALA C 217 6.764 -4.750 40.669 1.00 78.12 N -ANISOU 4859 N ALA C 217 10503 12605 6573 -1897 -2229 437 N -ATOM 4860 CA ALA C 217 8.163 -4.827 41.064 1.00 87.35 C -ANISOU 4860 CA ALA C 217 11459 13836 7892 -1946 -2699 466 C -ATOM 4861 C ALA C 217 8.296 -4.931 42.577 1.00 98.36 C -ANISOU 4861 C ALA C 217 13093 15541 8738 -1873 -2922 514 C -ATOM 4862 O ALA C 217 7.671 -4.174 43.320 1.00102.33 O -ANISOU 4862 O ALA C 217 13956 16158 8767 -1851 -2781 215 O -ATOM 4863 CB ALA C 217 8.928 -3.622 40.540 1.00 86.57 C -ANISOU 4863 CB ALA C 217 11244 13540 8109 -2110 -2807 12 C -ATOM 4864 OXT ALA C 217 9.038 -5.771 43.090 1.00104.60 O -ANISOU 4864 OXT ALA C 217 13727 16465 9551 -1809 -3241 850 O -TER 4865 ALA C 217 -ATOM 4866 N SER D 4 -19.172 -16.669 17.512 1.00 59.28 N -ANISOU 4866 N SER D 4 9750 5310 7462 -1899 -1688 880 N -ATOM 4867 CA SER D 4 -18.826 -15.245 17.570 1.00 59.00 C -ANISOU 4867 CA SER D 4 9325 5571 7522 -1711 -1497 792 C -ATOM 4868 C SER D 4 -19.710 -14.397 16.655 1.00 58.71 C -ANISOU 4868 C SER D 4 8828 5837 7641 -1705 -1201 668 C -ATOM 4869 O SER D 4 -19.670 -14.540 15.428 1.00 58.39 O -ANISOU 4869 O SER D 4 8596 5810 7780 -1509 -1242 585 O -ATOM 4870 CB SER D 4 -17.351 -15.031 17.218 1.00 56.05 C -ANISOU 4870 CB SER D 4 8882 5137 7279 -1269 -1723 730 C -ATOM 4871 OG SER D 4 -17.012 -13.654 17.222 1.00 56.21 O -ANISOU 4871 OG SER D 4 8555 5432 7372 -1123 -1534 642 O -ATOM 4872 N PRO D 5 -20.515 -13.504 17.252 1.00 54.28 N -ANISOU 4872 N PRO D 5 8089 5527 7009 -1912 -909 646 N -ATOM 4873 CA PRO D 5 -21.354 -12.624 16.435 1.00 50.89 C -ANISOU 4873 CA PRO D 5 7224 5384 6730 -1862 -651 526 C -ATOM 4874 C PRO D 5 -20.563 -11.418 15.944 1.00 46.84 C -ANISOU 4874 C PRO D 5 6419 4991 6388 -1501 -611 441 C -ATOM 4875 O PRO D 5 -21.144 -10.538 15.297 1.00 43.86 O -ANISOU 4875 O PRO D 5 5702 4827 6136 -1416 -420 352 O -ATOM 4876 CB PRO D 5 -22.430 -12.172 17.420 1.00 52.28 C -ANISOU 4876 CB PRO D 5 7356 5765 6743 -2206 -379 514 C -ATOM 4877 CG PRO D 5 -21.717 -12.158 18.740 1.00 49.94 C -ANISOU 4877 CG PRO D 5 7359 5353 6265 -2303 -456 603 C -ATOM 4878 CD PRO D 5 -20.754 -13.318 18.696 1.00 50.10 C -ANISOU 4878 CD PRO D 5 7758 5032 6247 -2211 -810 719 C -ATOM 4879 N GLY D 6 -19.266 -11.376 16.258 1.00 39.33 N -ANISOU 4879 N GLY D 6 5608 3911 5426 -1303 -798 465 N -ATOM 4880 CA GLY D 6 -18.413 -10.258 15.891 1.00 32.34 C -ANISOU 4880 CA GLY D 6 4488 3143 4655 -1016 -765 381 C -ATOM 4881 C GLY D 6 -18.439 -9.127 16.905 1.00 32.16 C -ANISOU 4881 C GLY D 6 4417 3261 4542 -1099 -563 368 C -ATOM 4882 O GLY D 6 -18.930 -9.294 18.020 1.00 33.86 O -ANISOU 4882 O GLY D 6 4805 3472 4587 -1368 -481 428 O -ATOM 4883 N VAL D 7 -17.890 -7.980 16.530 1.00 30.33 N -ANISOU 4883 N VAL D 7 3969 3151 4405 -891 -481 284 N -ATOM 4884 CA VAL D 7 -17.969 -6.794 17.377 1.00 30.82 C -ANISOU 4884 CA VAL D 7 3970 3340 4399 -957 -264 247 C -ATOM 4885 C VAL D 7 -19.417 -6.300 17.367 1.00 35.29 C -ANISOU 4885 C VAL D 7 4356 4052 5002 -1097 3 200 C -ATOM 4886 O VAL D 7 -19.941 -5.905 16.324 1.00 29.67 O -ANISOU 4886 O VAL D 7 3404 3422 4447 -964 73 142 O -ATOM 4887 CB VAL D 7 -17.056 -5.678 16.891 1.00 30.17 C -ANISOU 4887 CB VAL D 7 3729 3334 4399 -723 -241 163 C -ATOM 4888 CG1 VAL D 7 -17.229 -4.442 17.771 1.00 31.66 C -ANISOU 4888 CG1 VAL D 7 3883 3629 4518 -807 -3 114 C -ATOM 4889 CG2 VAL D 7 -15.607 -6.128 16.909 1.00 28.64 C -ANISOU 4889 CG2 VAL D 7 3660 3065 4157 -582 -497 168 C -ATOM 4890 N VAL D 8 -20.066 -6.344 18.525 1.00 36.39 N -ANISOU 4890 N VAL D 8 4601 4240 4984 -1370 142 214 N -ATOM 4891 CA VAL D 8 -21.473 -5.961 18.616 1.00 34.80 C -ANISOU 4891 CA VAL D 8 4207 4220 4796 -1517 395 134 C -ATOM 4892 C VAL D 8 -21.599 -4.457 18.844 1.00 36.70 C -ANISOU 4892 C VAL D 8 4253 4595 5098 -1397 622 14 C -ATOM 4893 O VAL D 8 -21.069 -3.919 19.815 1.00 36.95 O -ANISOU 4893 O VAL D 8 4399 4622 5017 -1461 685 1 O -ATOM 4894 CB VAL D 8 -22.186 -6.729 19.735 1.00 37.79 C -ANISOU 4894 CB VAL D 8 4777 4626 4954 -1910 459 174 C -ATOM 4895 CG1 VAL D 8 -23.615 -6.232 19.897 1.00 42.17 C -ANISOU 4895 CG1 VAL D 8 5079 5437 5508 -2063 744 39 C -ATOM 4896 CG2 VAL D 8 -22.186 -8.220 19.434 1.00 38.62 C -ANISOU 4896 CG2 VAL D 8 5112 4564 4998 -2041 235 293 C -ATOM 4897 N ILE D 9 -22.277 -3.777 17.926 1.00 34.72 N -ANISOU 4897 N ILE D 9 3723 4449 5020 -1215 728 -74 N -ATOM 4898 CA ILE D 9 -22.562 -2.355 18.078 1.00 34.94 C -ANISOU 4898 CA ILE D 9 3583 4574 5119 -1080 935 -197 C -ATOM 4899 C ILE D 9 -24.022 -2.217 18.516 1.00 36.33 C -ANISOU 4899 C ILE D 9 3572 4958 5273 -1230 1159 -318 C -ATOM 4900 O ILE D 9 -24.935 -2.717 17.851 1.00 36.60 O -ANISOU 4900 O ILE D 9 3437 5101 5370 -1246 1158 -338 O -ATOM 4901 CB ILE D 9 -22.261 -1.606 16.782 1.00 34.54 C -ANISOU 4901 CB ILE D 9 3379 4483 5263 -757 875 -212 C -ATOM 4902 CG1 ILE D 9 -20.769 -1.717 16.486 1.00 38.06 C -ANISOU 4902 CG1 ILE D 9 3991 4779 5690 -658 678 -133 C -ATOM 4903 CG2 ILE D 9 -22.684 -0.137 16.871 1.00 35.11 C -ANISOU 4903 CG2 ILE D 9 3311 4614 5416 -600 1071 -337 C -ATOM 4904 CD1 ILE D 9 -20.341 -1.040 15.228 1.00 41.61 C -ANISOU 4904 CD1 ILE D 9 4328 5197 6284 -404 610 -145 C -ATOM 4905 N SER D 10 -24.243 -1.589 19.666 1.00 35.75 N -ANISOU 4905 N SER D 10 3522 4970 5093 -1362 1354 -418 N -ATOM 4906 CA SER D 10 -25.569 -1.577 20.271 1.00 40.25 C -ANISOU 4906 CA SER D 10 3919 5779 5595 -1561 1575 -565 C -ATOM 4907 C SER D 10 -26.498 -0.624 19.533 1.00 38.78 C -ANISOU 4907 C SER D 10 3392 5736 5607 -1282 1703 -726 C -ATOM 4908 O SER D 10 -26.042 0.233 18.772 1.00 37.48 O -ANISOU 4908 O SER D 10 3182 5450 5608 -955 1645 -718 O -ATOM 4909 CB SER D 10 -25.492 -1.184 21.744 1.00 45.76 C -ANISOU 4909 CB SER D 10 4739 6541 6105 -1799 1752 -646 C -ATOM 4910 OG SER D 10 -24.960 0.116 21.866 1.00 50.33 O -ANISOU 4910 OG SER D 10 5303 7050 6770 -1566 1837 -726 O -ATOM 4911 N ASP D 11 -27.795 -0.787 19.770 1.00 42.46 N -ANISOU 4911 N ASP D 11 3625 6468 6038 -1423 1865 -876 N -ATOM 4912 CA ASP D 11 -28.821 0.059 19.174 1.00 49.43 C -ANISOU 4912 CA ASP D 11 4151 7533 7095 -1153 1980 -1058 C -ATOM 4913 C ASP D 11 -28.616 1.539 19.500 1.00 54.89 C -ANISOU 4913 C ASP D 11 4813 8157 7886 -883 2105 -1191 C -ATOM 4914 O ASP D 11 -28.920 2.414 18.689 1.00 58.40 O -ANISOU 4914 O ASP D 11 5091 8577 8523 -519 2083 -1253 O -ATOM 4915 CB ASP D 11 -30.200 -0.385 19.660 1.00 51.42 C -ANISOU 4915 CB ASP D 11 4226 8094 7217 -1369 2097 -1203 C -ATOM 4916 CG ASP D 11 -30.644 -1.687 19.035 1.00 54.82 C -ANISOU 4916 CG ASP D 11 4636 8604 7589 -1566 1977 -1102 C -ATOM 4917 OD1 ASP D 11 -29.994 -2.135 18.069 1.00 55.27 O -ANISOU 4917 OD1 ASP D 11 4733 8510 7759 -1486 1823 -954 O -ATOM 4918 OD2 ASP D 11 -31.645 -2.253 19.501 1.00 55.10 O -ANISOU 4918 OD2 ASP D 11 4622 8852 7461 -1807 2036 -1186 O -ATOM 4919 N ASP D 12 -28.078 1.809 20.683 1.00 52.39 N -ANISOU 4919 N ASP D 12 4694 7790 7424 -1069 2217 -1222 N -ATOM 4920 CA ASP D 12 -27.983 3.172 21.173 1.00 54.22 C -ANISOU 4920 CA ASP D 12 4912 7974 7715 -878 2374 -1384 C -ATOM 4921 C ASP D 12 -26.589 3.796 21.020 1.00 52.18 C -ANISOU 4921 C ASP D 12 4934 7407 7486 -730 2261 -1248 C -ATOM 4922 O ASP D 12 -26.328 4.874 21.552 1.00 53.40 O -ANISOU 4922 O ASP D 12 5156 7484 7648 -637 2390 -1364 O -ATOM 4923 CB ASP D 12 -28.487 3.246 22.620 1.00 59.22 C -ANISOU 4923 CB ASP D 12 5586 8775 8142 -1153 2543 -1533 C -ATOM 4924 CG ASP D 12 -29.956 2.825 22.752 1.00 68.69 C -ANISOU 4924 CG ASP D 12 6553 10262 9284 -1241 2579 -1665 C -ATOM 4925 OD1 ASP D 12 -30.822 3.517 22.180 1.00 72.87 O -ANISOU 4925 OD1 ASP D 12 6844 10877 9968 -926 2581 -1791 O -ATOM 4926 OD2 ASP D 12 -30.250 1.810 23.429 1.00 70.92 O -ANISOU 4926 OD2 ASP D 12 6913 10681 9352 -1627 2591 -1638 O -ATOM 4927 N GLU D 13 -25.702 3.129 20.284 1.00 47.37 N -ANISOU 4927 N GLU D 13 4480 6636 6884 -717 2027 -1025 N -ATOM 4928 CA GLU D 13 -24.374 3.683 20.008 1.00 46.17 C -ANISOU 4928 CA GLU D 13 4553 6241 6748 -588 1911 -916 C -ATOM 4929 C GLU D 13 -24.493 4.995 19.234 1.00 50.20 C -ANISOU 4929 C GLU D 13 4990 6641 7442 -231 1935 -994 C -ATOM 4930 O GLU D 13 -25.084 5.034 18.154 1.00 53.60 O -ANISOU 4930 O GLU D 13 5247 7089 8030 -10 1851 -981 O -ATOM 4931 CB GLU D 13 -23.510 2.691 19.223 1.00 46.82 C -ANISOU 4931 CB GLU D 13 4752 6216 6820 -608 1651 -705 C -ATOM 4932 CG GLU D 13 -22.308 3.319 18.496 1.00 52.17 C -ANISOU 4932 CG GLU D 13 5566 6703 7555 -416 1517 -624 C -ATOM 4933 CD GLU D 13 -21.184 3.752 19.431 1.00 58.03 C -ANISOU 4933 CD GLU D 13 6541 7366 8144 -542 1553 -624 C -ATOM 4934 OE1 GLU D 13 -20.842 2.984 20.357 1.00 65.03 O -ANISOU 4934 OE1 GLU D 13 7550 8296 8863 -789 1534 -577 O -ATOM 4935 OE2 GLU D 13 -20.638 4.860 19.235 1.00 58.35 O -ANISOU 4935 OE2 GLU D 13 6657 7299 8216 -408 1592 -668 O -ATOM 4936 N PRO D 14 -23.935 6.079 19.797 1.00 52.49 N -ANISOU 4936 N PRO D 14 5435 6807 7700 -188 2043 -1071 N -ATOM 4937 CA PRO D 14 -23.954 7.432 19.222 1.00 53.65 C -ANISOU 4937 CA PRO D 14 5604 6790 7989 121 2069 -1146 C -ATOM 4938 C PRO D 14 -22.959 7.649 18.072 1.00 48.11 C -ANISOU 4938 C PRO D 14 5053 5891 7334 256 1863 -980 C -ATOM 4939 O PRO D 14 -23.084 8.648 17.357 1.00 51.35 O -ANISOU 4939 O PRO D 14 5492 6154 7864 511 1840 -1006 O -ATOM 4940 CB PRO D 14 -23.572 8.318 20.417 1.00 51.33 C -ANISOU 4940 CB PRO D 14 5480 6438 7586 16 2266 -1284 C -ATOM 4941 CG PRO D 14 -22.689 7.441 21.247 1.00 51.69 C -ANISOU 4941 CG PRO D 14 5679 6543 7418 -329 2237 -1180 C -ATOM 4942 CD PRO D 14 -23.274 6.049 21.116 1.00 52.76 C -ANISOU 4942 CD PRO D 14 5661 6853 7533 -468 2149 -1096 C -ATOM 4943 N GLY D 15 -22.001 6.742 17.886 1.00 42.41 N -ANISOU 4943 N GLY D 15 4431 5169 6514 89 1708 -823 N -ATOM 4944 CA GLY D 15 -20.959 6.954 16.898 1.00 38.66 C -ANISOU 4944 CA GLY D 15 4087 4555 6049 170 1535 -705 C -ATOM 4945 C GLY D 15 -20.038 8.080 17.340 1.00 42.57 C -ANISOU 4945 C GLY D 15 4820 4906 6449 137 1616 -755 C -ATOM 4946 O GLY D 15 -20.003 8.425 18.525 1.00 44.58 O -ANISOU 4946 O GLY D 15 5154 5181 6604 4 1783 -857 O -ATOM 4947 N TYR D 16 -19.303 8.670 16.399 1.00 41.01 N -ANISOU 4947 N TYR D 16 4744 4575 6261 226 1507 -694 N -ATOM 4948 CA TYR D 16 -18.401 9.773 16.733 1.00 39.17 C -ANISOU 4948 CA TYR D 16 4762 4205 5915 159 1583 -746 C -ATOM 4949 C TYR D 16 -18.696 11.043 15.944 1.00 40.46 C -ANISOU 4949 C TYR D 16 5042 4155 6174 370 1590 -771 C -ATOM 4950 O TYR D 16 -19.025 10.982 14.752 1.00 35.14 O -ANISOU 4950 O TYR D 16 4298 3443 5612 535 1446 -686 O -ATOM 4951 CB TYR D 16 -16.951 9.374 16.475 1.00 38.94 C -ANISOU 4951 CB TYR D 16 4840 4224 5732 -15 1448 -665 C -ATOM 4952 CG TYR D 16 -16.475 8.165 17.239 1.00 36.98 C -ANISOU 4952 CG TYR D 16 4532 4147 5373 -199 1395 -631 C -ATOM 4953 CD1 TYR D 16 -16.701 6.886 16.758 1.00 34.75 C -ANISOU 4953 CD1 TYR D 16 4089 3961 5152 -173 1237 -540 C -ATOM 4954 CD2 TYR D 16 -15.779 8.306 18.432 1.00 44.52 C -ANISOU 4954 CD2 TYR D 16 5615 5152 6149 -400 1487 -686 C -ATOM 4955 CE1 TYR D 16 -16.255 5.779 17.448 1.00 37.89 C -ANISOU 4955 CE1 TYR D 16 4484 4469 5444 -325 1159 -498 C -ATOM 4956 CE2 TYR D 16 -15.330 7.204 19.131 1.00 42.03 C -ANISOU 4956 CE2 TYR D 16 5276 4974 5721 -554 1404 -637 C -ATOM 4957 CZ TYR D 16 -15.569 5.946 18.630 1.00 38.21 C -ANISOU 4957 CZ TYR D 16 4660 4550 5308 -506 1232 -540 C -ATOM 4958 OH TYR D 16 -15.134 4.840 19.316 1.00 39.68 O -ANISOU 4958 OH TYR D 16 4869 4827 5379 -641 1121 -482 O -ATOM 4959 N ASP D 17 -18.561 12.182 16.627 1.00 39.37 N -ANISOU 4959 N ASP D 17 5108 3870 5980 352 1749 -885 N -ATOM 4960 CA ASP D 17 -18.590 13.513 16.019 1.00 42.56 C -ANISOU 4960 CA ASP D 17 5737 4008 6426 510 1749 -907 C -ATOM 4961 C ASP D 17 -17.614 13.550 14.845 1.00 40.17 C -ANISOU 4961 C ASP D 17 5568 3654 6042 435 1567 -769 C -ATOM 4962 O ASP D 17 -16.450 13.187 14.998 1.00 33.77 O -ANISOU 4962 O ASP D 17 4819 2955 5057 186 1537 -740 O -ATOM 4963 CB ASP D 17 -18.169 14.548 17.071 1.00 47.71 C -ANISOU 4963 CB ASP D 17 6644 4526 6956 387 1947 -1047 C -ATOM 4964 CG ASP D 17 -18.356 15.986 16.616 1.00 54.33 C -ANISOU 4964 CG ASP D 17 7764 5036 7843 563 1966 -1095 C -ATOM 4965 OD1 ASP D 17 -18.270 16.276 15.405 1.00 55.62 O -ANISOU 4965 OD1 ASP D 17 8026 5062 8046 675 1797 -976 O -ATOM 4966 OD2 ASP D 17 -18.570 16.851 17.492 1.00 60.89 O -ANISOU 4966 OD2 ASP D 17 8745 5731 8659 578 2147 -1254 O -ATOM 4967 N LEU D 18 -18.083 14.015 13.688 1.00 41.80 N -ANISOU 4967 N LEU D 18 5815 3709 6359 644 1441 -696 N -ATOM 4968 CA LEU D 18 -17.263 14.082 12.473 1.00 39.97 C -ANISOU 4968 CA LEU D 18 5707 3441 6039 556 1268 -570 C -ATOM 4969 C LEU D 18 -16.022 14.962 12.669 1.00 35.94 C -ANISOU 4969 C LEU D 18 5536 2819 5302 300 1326 -603 C -ATOM 4970 O LEU D 18 -14.983 14.735 12.049 1.00 35.39 O -ANISOU 4970 O LEU D 18 5517 2849 5079 92 1229 -548 O -ATOM 4971 CB LEU D 18 -18.097 14.626 11.303 1.00 42.98 C -ANISOU 4971 CB LEU D 18 6125 3642 6563 827 1131 -489 C -ATOM 4972 CG LEU D 18 -19.328 13.827 10.855 1.00 46.00 C -ANISOU 4972 CG LEU D 18 6164 4160 7154 1078 1045 -452 C -ATOM 4973 CD1 LEU D 18 -20.208 14.652 9.911 1.00 46.14 C -ANISOU 4973 CD1 LEU D 18 6260 3967 7304 1385 923 -399 C -ATOM 4974 CD2 LEU D 18 -18.923 12.520 10.197 1.00 40.94 C -ANISOU 4974 CD2 LEU D 18 5299 3769 6487 944 913 -354 C -ATOM 4975 N ASP D 19 -16.131 15.956 13.545 1.00 36.78 N -ANISOU 4975 N ASP D 19 5862 2737 5374 298 1495 -717 N -ATOM 4976 CA ASP D 19 -15.041 16.906 13.752 1.00 42.66 C -ANISOU 4976 CA ASP D 19 6963 3354 5892 38 1569 -762 C -ATOM 4977 C ASP D 19 -13.793 16.302 14.401 1.00 39.82 C -ANISOU 4977 C ASP D 19 6544 3270 5315 -300 1618 -804 C -ATOM 4978 O ASP D 19 -12.732 16.926 14.422 1.00 43.18 O -ANISOU 4978 O ASP D 19 7214 3676 5516 -568 1655 -841 O -ATOM 4979 CB ASP D 19 -15.539 18.097 14.574 1.00 46.88 C -ANISOU 4979 CB ASP D 19 7751 3607 6456 133 1745 -893 C -ATOM 4980 CG ASP D 19 -16.561 18.914 13.830 1.00 57.46 C -ANISOU 4980 CG ASP D 19 9230 4628 7974 475 1662 -860 C -ATOM 4981 OD1 ASP D 19 -16.350 19.149 12.622 1.00 58.12 O -ANISOU 4981 OD1 ASP D 19 9457 4599 8026 484 1484 -723 O -ATOM 4982 OD2 ASP D 19 -17.577 19.307 14.445 1.00 63.88 O -ANISOU 4982 OD2 ASP D 19 10000 5319 8952 736 1764 -979 O -ATOM 4983 N LEU D 20 -13.938 15.090 14.920 1.00 36.89 N -ANISOU 4983 N LEU D 20 5858 3157 5002 -289 1605 -802 N -ATOM 4984 CA LEU D 20 -12.872 14.396 15.623 1.00 39.18 C -ANISOU 4984 CA LEU D 20 6065 3712 5110 -548 1618 -839 C -ATOM 4985 C LEU D 20 -12.010 13.633 14.632 1.00 43.28 C -ANISOU 4985 C LEU D 20 6461 4429 5555 -639 1424 -765 C -ATOM 4986 O LEU D 20 -10.939 13.144 14.978 1.00 29.96 O -ANISOU 4986 O LEU D 20 4717 2971 3697 -841 1393 -807 O -ATOM 4987 CB LEU D 20 -13.464 13.416 16.637 1.00 40.11 C -ANISOU 4987 CB LEU D 20 5943 3986 5313 -494 1670 -859 C -ATOM 4988 CG LEU D 20 -14.263 14.080 17.756 1.00 45.50 C -ANISOU 4988 CG LEU D 20 6703 4543 6042 -446 1885 -974 C -ATOM 4989 CD1 LEU D 20 -15.074 13.056 18.541 1.00 44.96 C -ANISOU 4989 CD1 LEU D 20 6380 4636 6067 -394 1921 -982 C -ATOM 4990 CD2 LEU D 20 -13.323 14.835 18.676 1.00 47.89 C -ANISOU 4990 CD2 LEU D 20 7238 4842 6114 -713 2033 -1082 C -ATOM 4991 N PHE D 21 -12.484 13.547 13.395 1.00 30.62 N -ANISOU 4991 N PHE D 21 4807 2751 4075 -482 1289 -670 N -ATOM 4992 CA PHE D 21 -11.816 12.757 12.379 1.00 29.09 C -ANISOU 4992 CA PHE D 21 4464 2754 3837 -546 1108 -618 C -ATOM 4993 C PHE D 21 -11.553 13.544 11.099 1.00 33.35 C -ANISOU 4993 C PHE D 21 5191 3175 4305 -604 1028 -569 C -ATOM 4994 O PHE D 21 -12.049 14.656 10.923 1.00 32.29 O -ANISOU 4994 O PHE D 21 5316 2761 4192 -542 1083 -545 O -ATOM 4995 CB PHE D 21 -12.649 11.515 12.072 1.00 27.99 C -ANISOU 4995 CB PHE D 21 4021 2710 3905 -335 996 -542 C -ATOM 4996 CG PHE D 21 -12.752 10.570 13.221 1.00 33.74 C -ANISOU 4996 CG PHE D 21 4587 3578 4655 -340 1037 -574 C -ATOM 4997 CD1 PHE D 21 -11.816 9.564 13.384 1.00 37.64 C -ANISOU 4997 CD1 PHE D 21 4951 4301 5048 -453 930 -594 C -ATOM 4998 CD2 PHE D 21 -13.772 10.692 14.152 1.00 39.89 C -ANISOU 4998 CD2 PHE D 21 5353 4263 5541 -237 1174 -595 C -ATOM 4999 CE1 PHE D 21 -11.894 8.686 14.463 1.00 40.29 C -ANISOU 4999 CE1 PHE D 21 5188 4736 5383 -468 941 -601 C -ATOM 5000 CE2 PHE D 21 -13.859 9.823 15.229 1.00 46.07 C -ANISOU 5000 CE2 PHE D 21 6020 5176 6308 -292 1210 -615 C -ATOM 5001 CZ PHE D 21 -12.920 8.814 15.382 1.00 45.58 C -ANISOU 5001 CZ PHE D 21 5872 5308 6138 -410 1084 -601 C -ATOM 5002 N CYS D 22 -10.740 12.965 10.218 1.00 34.50 N -ANISOU 5002 N CYS D 22 5219 3535 4353 -732 891 -564 N -ATOM 5003 CA CYS D 22 -10.502 13.549 8.907 1.00 34.41 C -ANISOU 5003 CA CYS D 22 5360 3459 4256 -824 797 -511 C -ATOM 5004 C CYS D 22 -11.587 13.011 7.987 1.00 33.11 C -ANISOU 5004 C CYS D 22 5027 3233 4318 -559 664 -387 C -ATOM 5005 O CYS D 22 -11.686 11.804 7.788 1.00 32.40 O -ANISOU 5005 O CYS D 22 4636 3345 4331 -475 573 -381 O -ATOM 5006 CB CYS D 22 -9.124 13.165 8.387 1.00 36.87 C -ANISOU 5006 CB CYS D 22 5588 4082 4339 -1106 726 -601 C -ATOM 5007 N ILE D 23 -12.397 13.911 7.432 1.00 30.82 N -ANISOU 5007 N ILE D 23 4946 2663 4102 -426 642 -293 N -ATOM 5008 CA ILE D 23 -13.550 13.538 6.603 1.00 31.65 C -ANISOU 5008 CA ILE D 23 4899 2706 4423 -153 516 -176 C -ATOM 5009 C ILE D 23 -13.434 14.237 5.249 1.00 32.18 C -ANISOU 5009 C ILE D 23 5185 2654 4388 -234 382 -75 C -ATOM 5010 O ILE D 23 -13.027 15.391 5.196 1.00 38.42 O -ANISOU 5010 O ILE D 23 6344 3239 5016 -383 419 -70 O -ATOM 5011 CB ILE D 23 -14.874 13.992 7.288 1.00 40.78 C -ANISOU 5011 CB ILE D 23 6077 3628 5790 158 596 -162 C -ATOM 5012 CG1 ILE D 23 -15.028 13.336 8.668 1.00 35.64 C -ANISOU 5012 CG1 ILE D 23 5232 3102 5209 190 740 -264 C -ATOM 5013 CG2 ILE D 23 -16.093 13.707 6.410 1.00 38.33 C -ANISOU 5013 CG2 ILE D 23 5600 3279 5686 445 459 -55 C -ATOM 5014 CD1 ILE D 23 -15.066 11.813 8.637 1.00 32.06 C -ANISOU 5014 CD1 ILE D 23 4420 2930 4833 201 670 -257 C -ATOM 5015 N PRO D 24 -13.788 13.544 4.151 1.00 32.74 N -ANISOU 5015 N PRO D 24 5055 2848 4535 -162 225 8 N -ATOM 5016 CA PRO D 24 -13.736 14.238 2.855 1.00 35.47 C -ANISOU 5016 CA PRO D 24 5632 3078 4766 -255 87 119 C -ATOM 5017 C PRO D 24 -14.676 15.435 2.831 1.00 37.25 C -ANISOU 5017 C PRO D 24 6169 2912 5073 -30 62 222 C -ATOM 5018 O PRO D 24 -15.842 15.305 3.208 1.00 37.80 O -ANISOU 5018 O PRO D 24 6089 2889 5383 315 65 243 O -ATOM 5019 CB PRO D 24 -14.190 13.167 1.848 1.00 33.29 C -ANISOU 5019 CB PRO D 24 5031 3013 4605 -161 -64 182 C -ATOM 5020 CG PRO D 24 -14.783 12.054 2.655 1.00 32.79 C -ANISOU 5020 CG PRO D 24 4610 3091 4759 50 -6 125 C -ATOM 5021 CD PRO D 24 -14.133 12.119 4.014 1.00 33.68 C -ANISOU 5021 CD PRO D 24 4768 3221 4808 -47 164 -1 C -ATOM 5022 N ASN D 25 -14.160 16.590 2.411 1.00 45.17 N -ANISOU 5022 N ASN D 25 7607 3692 5866 -230 35 270 N -ATOM 5023 CA ASN D 25 -14.918 17.833 2.414 1.00 54.25 C -ANISOU 5023 CA ASN D 25 9134 4411 7066 -21 -6 359 C -ATOM 5024 C ASN D 25 -16.246 17.751 1.680 1.00 51.87 C -ANISOU 5024 C ASN D 25 8717 4001 6989 365 -187 494 C -ATOM 5025 O ASN D 25 -17.219 18.407 2.059 1.00 55.38 O -ANISOU 5025 O ASN D 25 9272 4165 7603 711 -199 509 O -ATOM 5026 CB ASN D 25 -14.092 18.962 1.787 1.00 68.58 C -ANISOU 5026 CB ASN D 25 11470 6012 8576 -360 -56 421 C -ATOM 5027 CG ASN D 25 -12.768 19.185 2.495 1.00 78.77 C -ANISOU 5027 CG ASN D 25 12898 7422 9610 -770 126 271 C -ATOM 5028 OD1 ASN D 25 -11.802 18.451 2.272 1.00 82.24 O -ANISOU 5028 OD1 ASN D 25 13118 8234 9894 -1069 152 188 O -ATOM 5029 ND2 ASN D 25 -12.713 20.208 3.343 1.00 80.85 N -ANISOU 5029 ND2 ASN D 25 13519 7381 9821 -780 250 219 N -ATOM 5030 N HIS D 26 -16.283 16.967 0.611 1.00 43.39 N -ANISOU 5030 N HIS D 26 7414 3164 5909 309 -333 575 N -ATOM 5031 CA HIS D 26 -17.470 16.936 -0.231 1.00 45.02 C -ANISOU 5031 CA HIS D 26 7526 3294 6283 631 -528 715 C -ATOM 5032 C HIS D 26 -18.631 16.160 0.402 1.00 43.49 C -ANISOU 5032 C HIS D 26 6897 3231 6397 1013 -479 650 C -ATOM 5033 O HIS D 26 -19.769 16.257 -0.058 1.00 49.25 O -ANISOU 5033 O HIS D 26 7529 3891 7291 1342 -618 731 O -ATOM 5034 CB HIS D 26 -17.131 16.406 -1.631 1.00 42.57 C -ANISOU 5034 CB HIS D 26 7135 3200 5840 410 -698 820 C -ATOM 5035 CG HIS D 26 -16.587 15.010 -1.641 1.00 38.45 C -ANISOU 5035 CG HIS D 26 6182 3105 5322 233 -628 711 C -ATOM 5036 ND1 HIS D 26 -15.244 14.729 -1.505 1.00 36.92 N -ANISOU 5036 ND1 HIS D 26 6000 3112 4915 -151 -527 593 N -ATOM 5037 CD2 HIS D 26 -17.208 13.815 -1.793 1.00 36.61 C -ANISOU 5037 CD2 HIS D 26 5505 3130 5276 394 -657 691 C -ATOM 5038 CE1 HIS D 26 -15.062 13.421 -1.564 1.00 34.35 C -ANISOU 5038 CE1 HIS D 26 5263 3126 4661 -182 -510 506 C -ATOM 5039 NE2 HIS D 26 -16.236 12.844 -1.741 1.00 37.94 N -ANISOU 5039 NE2 HIS D 26 5456 3606 5352 129 -583 570 N -ATOM 5040 N TYR D 27 -18.337 15.399 1.456 1.00 40.66 N -ANISOU 5040 N TYR D 27 6282 3075 6093 951 -289 502 N -ATOM 5041 CA TYR D 27 -19.370 14.684 2.201 1.00 38.38 C -ANISOU 5041 CA TYR D 27 5616 2916 6051 1240 -212 422 C -ATOM 5042 C TYR D 27 -19.661 15.336 3.558 1.00 48.71 C -ANISOU 5042 C TYR D 27 7030 4041 7436 1388 -30 296 C -ATOM 5043 O TYR D 27 -20.472 14.825 4.326 1.00 46.29 O -ANISOU 5043 O TYR D 27 6432 3852 7305 1584 67 201 O -ATOM 5044 CB TYR D 27 -18.982 13.211 2.406 1.00 35.12 C -ANISOU 5044 CB TYR D 27 4826 2867 5651 1073 -149 353 C -ATOM 5045 CG TYR D 27 -19.008 12.381 1.143 1.00 38.60 C -ANISOU 5045 CG TYR D 27 5066 3522 6079 1001 -315 441 C -ATOM 5046 CD1 TYR D 27 -19.959 12.609 0.153 1.00 38.28 C -ANISOU 5046 CD1 TYR D 27 4991 3431 6122 1209 -489 562 C -ATOM 5047 CD2 TYR D 27 -18.082 11.372 0.943 1.00 34.33 C -ANISOU 5047 CD2 TYR D 27 4367 3238 5439 736 -305 389 C -ATOM 5048 CE1 TYR D 27 -19.982 11.842 -0.996 1.00 35.65 C -ANISOU 5048 CE1 TYR D 27 4472 3309 5764 1118 -632 635 C -ATOM 5049 CE2 TYR D 27 -18.092 10.613 -0.196 1.00 30.88 C -ANISOU 5049 CE2 TYR D 27 3748 2997 4989 663 -443 443 C -ATOM 5050 CZ TYR D 27 -19.039 10.854 -1.161 1.00 32.89 C -ANISOU 5050 CZ TYR D 27 3975 3205 5316 836 -598 568 C -ATOM 5051 OH TYR D 27 -19.034 10.086 -2.293 1.00 31.76 O -ANISOU 5051 OH TYR D 27 3649 3273 5145 736 -727 613 O -ATOM 5052 N ALA D 28 -19.013 16.468 3.831 1.00 52.51 N -ANISOU 5052 N ALA D 28 7936 4243 7770 1268 21 285 N -ATOM 5053 CA ALA D 28 -19.091 17.140 5.140 1.00 56.66 C -ANISOU 5053 CA ALA D 28 8606 4591 8329 1344 214 145 C -ATOM 5054 C ALA D 28 -20.483 17.233 5.783 1.00 53.97 C -ANISOU 5054 C ALA D 28 8058 4203 8248 1763 264 52 C -ATOM 5055 O ALA D 28 -20.673 16.790 6.912 1.00 54.51 O -ANISOU 5055 O ALA D 28 7912 4415 8386 1772 449 -92 O -ATOM 5056 CB ALA D 28 -18.451 18.522 5.071 1.00 59.61 C -ANISOU 5056 CB ALA D 28 9528 4599 8523 1213 213 171 C -ATOM 5057 N GLU D 29 -21.451 17.816 5.083 1.00 55.87 N -ANISOU 5057 N GLU D 29 8355 4259 8615 2103 95 122 N -ATOM 5058 CA GLU D 29 -22.792 17.943 5.654 1.00 58.92 C -ANISOU 5058 CA GLU D 29 8501 4643 9241 2516 134 -4 C -ATOM 5059 C GLU D 29 -23.755 16.849 5.194 1.00 52.03 C -ANISOU 5059 C GLU D 29 7121 4125 8525 2664 44 10 C -ATOM 5060 O GLU D 29 -24.963 16.941 5.407 1.00 56.14 O -ANISOU 5060 O GLU D 29 7348 4753 9231 2883 50 -75 O -ATOM 5061 CB GLU D 29 -23.383 19.338 5.409 1.00 71.11 C -ANISOU 5061 CB GLU D 29 10275 5890 10854 2713 11 4 C -ATOM 5062 CG GLU D 29 -22.797 20.413 6.327 1.00 81.64 C -ANISOU 5062 CG GLU D 29 11991 6936 12093 2609 151 -109 C -ATOM 5063 CD GLU D 29 -23.793 21.506 6.691 1.00 92.90 C -ANISOU 5063 CD GLU D 29 13427 8176 13695 2907 129 -219 C -ATOM 5064 OE1 GLU D 29 -24.612 21.893 5.829 1.00 98.37 O -ANISOU 5064 OE1 GLU D 29 14069 8808 14498 3143 -48 -113 O -ATOM 5065 OE2 GLU D 29 -23.758 21.980 7.847 1.00 95.97 O -ANISOU 5065 OE2 GLU D 29 13877 8487 14102 2906 299 -415 O -ATOM 5066 N ASP D 30 -23.210 15.805 4.579 1.00 49.20 N -ANISOU 5066 N ASP D 30 6605 4008 8081 2420 -4 116 N -ATOM 5067 CA ASP D 30 -24.021 14.704 4.072 1.00 47.34 C -ANISOU 5067 CA ASP D 30 5928 4096 7963 2515 -82 139 C -ATOM 5068 C ASP D 30 -24.015 13.539 5.056 1.00 50.49 C -ANISOU 5068 C ASP D 30 5997 4798 8389 2351 113 13 C -ATOM 5069 O ASP D 30 -24.771 12.577 4.906 1.00 50.45 O -ANISOU 5069 O ASP D 30 5660 5120 8389 2360 88 -12 O -ATOM 5070 CB ASP D 30 -23.490 14.231 2.710 1.00 45.91 C -ANISOU 5070 CB ASP D 30 5768 4005 7670 2323 -276 320 C -ATOM 5071 CG ASP D 30 -23.606 15.300 1.628 1.00 51.09 C -ANISOU 5071 CG ASP D 30 6751 4382 8280 2465 -503 473 C -ATOM 5072 OD1 ASP D 30 -24.606 16.055 1.630 1.00 52.25 O -ANISOU 5072 OD1 ASP D 30 6904 4429 8518 2758 -524 473 O -ATOM 5073 OD2 ASP D 30 -22.692 15.382 0.776 1.00 50.94 O -ANISOU 5073 OD2 ASP D 30 6962 4318 8075 2190 -606 602 O -ATOM 5074 N LEU D 31 -23.146 13.623 6.057 1.00 48.21 N -ANISOU 5074 N LEU D 31 5865 4455 7995 2127 290 -67 N -ATOM 5075 CA LEU D 31 -23.019 12.555 7.041 1.00 38.51 C -ANISOU 5075 CA LEU D 31 4394 3478 6759 1942 455 -166 C -ATOM 5076 C LEU D 31 -23.452 13.094 8.395 1.00 43.32 C -ANISOU 5076 C LEU D 31 5020 4021 7419 2040 663 -344 C -ATOM 5077 O LEU D 31 -23.461 14.305 8.609 1.00 51.47 O -ANISOU 5077 O LEU D 31 6320 4782 8456 2181 692 -391 O -ATOM 5078 CB LEU D 31 -21.582 12.054 7.101 1.00 38.64 C -ANISOU 5078 CB LEU D 31 4545 3544 6591 1580 473 -118 C -ATOM 5079 CG LEU D 31 -21.022 11.468 5.801 1.00 37.60 C -ANISOU 5079 CG LEU D 31 4385 3512 6390 1445 288 18 C -ATOM 5080 CD1 LEU D 31 -19.519 11.262 5.910 1.00 33.20 C -ANISOU 5080 CD1 LEU D 31 3991 2988 5637 1119 311 17 C -ATOM 5081 CD2 LEU D 31 -21.714 10.157 5.476 1.00 39.39 C -ANISOU 5081 CD2 LEU D 31 4240 4008 6719 1475 234 31 C -ATOM 5082 N GLU D 32 -23.828 12.199 9.301 1.00 42.49 N -ANISOU 5082 N GLU D 32 4647 4157 7340 1951 804 -448 N -ATOM 5083 CA AGLU D 32 -24.267 12.622 10.627 0.58 47.68 C -ANISOU 5083 CA AGLU D 32 5287 4805 8023 2000 1017 -638 C -ATOM 5084 CA BGLU D 32 -24.288 12.584 10.631 0.42 47.97 C -ANISOU 5084 CA BGLU D 32 5313 4853 8061 1997 1017 -638 C -ATOM 5085 C GLU D 32 -23.208 12.292 11.676 1.00 45.10 C -ANISOU 5085 C GLU D 32 5094 4506 7534 1664 1167 -669 C -ATOM 5086 O GLU D 32 -22.857 13.146 12.491 1.00 44.52 O -ANISOU 5086 O GLU D 32 5240 4272 7402 1632 1304 -768 O -ATOM 5087 CB AGLU D 32 -25.603 11.973 11.004 0.58 51.08 C -ANISOU 5087 CB AGLU D 32 5370 5564 8474 2075 1040 -740 C -ATOM 5088 CB BGLU D 32 -25.556 11.798 10.970 0.42 50.63 C -ANISOU 5088 CB BGLU D 32 5291 5532 8415 2044 1036 -727 C -ATOM 5089 CG AGLU D 32 -26.369 12.707 12.103 0.58 57.10 C -ANISOU 5089 CG AGLU D 32 6113 6343 9239 2206 1198 -947 C -ATOM 5090 CG BGLU D 32 -26.595 12.558 11.767 0.42 57.32 C -ANISOU 5090 CG BGLU D 32 6081 6422 9275 2246 1139 -915 C -ATOM 5091 CD AGLU D 32 -27.214 13.855 11.571 0.58 62.65 C -ANISOU 5091 CD AGLU D 32 6893 6931 9981 2582 1076 -982 C -ATOM 5092 CD BGLU D 32 -27.986 11.970 11.594 0.42 62.19 C -ANISOU 5092 CD BGLU D 32 6361 7372 9896 2363 1103 -956 C -ATOM 5093 OE1AGLU D 32 -26.669 14.962 11.387 0.58 63.21 O -ANISOU 5093 OE1AGLU D 32 7293 6668 10057 2689 1028 -970 O -ATOM 5094 OE1BGLU D 32 -28.945 12.754 11.429 0.42 68.16 O -ANISOU 5094 OE1BGLU D 32 7082 8135 10679 2664 1071 -1014 O -ATOM 5095 OE2AGLU D 32 -28.425 13.650 11.335 0.58 69.27 O -ANISOU 5095 OE2AGLU D 32 7482 8005 10833 2766 1037 -1009 O -ATOM 5096 OE2BGLU D 32 -28.117 10.726 11.614 0.42 60.57 O -ANISOU 5096 OE2BGLU D 32 5942 7411 9660 2148 1117 -917 O -ATOM 5097 N ARG D 33 -22.697 11.062 11.646 1.00 41.49 N -ANISOU 5097 N ARG D 33 4517 4248 6999 1422 1126 -589 N -ATOM 5098 CA ARG D 33 -21.700 10.596 12.612 1.00 41.35 C -ANISOU 5098 CA ARG D 33 4601 4288 6821 1120 1225 -607 C -ATOM 5099 C ARG D 33 -20.781 9.585 11.950 1.00 37.23 C -ANISOU 5099 C ARG D 33 4062 3868 6215 935 1070 -472 C -ATOM 5100 O ARG D 33 -21.172 8.936 10.981 1.00 40.49 O -ANISOU 5100 O ARG D 33 4307 4371 6705 1006 930 -391 O -ATOM 5101 CB ARG D 33 -22.378 9.885 13.794 1.00 44.47 C -ANISOU 5101 CB ARG D 33 4798 4881 7219 1028 1382 -720 C -ATOM 5102 CG ARG D 33 -23.529 10.624 14.461 1.00 51.56 C -ANISOU 5102 CG ARG D 33 5595 5777 8218 1218 1548 -903 C -ATOM 5103 CD ARG D 33 -23.027 11.753 15.339 1.00 55.25 C -ANISOU 5103 CD ARG D 33 6326 6056 8611 1188 1703 -1015 C -ATOM 5104 NE ARG D 33 -22.411 11.245 16.561 1.00 57.19 N -ANISOU 5104 NE ARG D 33 6624 6415 8692 874 1838 -1056 N -ATOM 5105 CZ ARG D 33 -21.957 12.012 17.547 1.00 56.97 C -ANISOU 5105 CZ ARG D 33 6794 6290 8562 768 2002 -1169 C -ATOM 5106 NH1 ARG D 33 -22.038 13.331 17.454 1.00 55.82 N -ANISOU 5106 NH1 ARG D 33 6835 5905 8469 952 2058 -1259 N -ATOM 5107 NH2 ARG D 33 -21.415 11.454 18.622 1.00 55.27 N -ANISOU 5107 NH2 ARG D 33 6611 6205 8183 472 2099 -1188 N -ATOM 5108 N VAL D 34 -19.567 9.433 12.477 1.00 30.92 N -ANISOU 5108 N VAL D 34 3421 3074 5254 703 1091 -467 N -ATOM 5109 CA VAL D 34 -18.752 8.282 12.125 1.00 31.63 C -ANISOU 5109 CA VAL D 34 3446 3303 5269 542 958 -389 C -ATOM 5110 C VAL D 34 -19.268 7.135 12.992 1.00 35.34 C -ANISOU 5110 C VAL D 34 3750 3929 5749 457 1006 -410 C -ATOM 5111 O VAL D 34 -19.467 7.303 14.194 1.00 33.23 O -ANISOU 5111 O VAL D 34 3520 3675 5431 378 1162 -492 O -ATOM 5112 CB VAL D 34 -17.252 8.519 12.390 1.00 33.59 C -ANISOU 5112 CB VAL D 34 3895 3538 5330 342 946 -398 C -ATOM 5113 CG1 VAL D 34 -16.480 7.223 12.241 1.00 30.32 C -ANISOU 5113 CG1 VAL D 34 3381 3289 4851 216 808 -357 C -ATOM 5114 CG2 VAL D 34 -16.699 9.539 11.423 1.00 33.67 C -ANISOU 5114 CG2 VAL D 34 4085 3416 5292 358 887 -371 C -ATOM 5115 N PHE D 35 -19.503 5.976 12.386 1.00 35.37 N -ANISOU 5115 N PHE D 35 3589 4047 5803 450 876 -342 N -ATOM 5116 CA PHE D 35 -20.148 4.873 13.090 1.00 33.52 C -ANISOU 5116 CA PHE D 35 3225 3940 5571 352 911 -351 C -ATOM 5117 C PHE D 35 -19.123 3.801 13.431 1.00 33.09 C -ANISOU 5117 C PHE D 35 3249 3927 5395 172 800 -300 C -ATOM 5118 O PHE D 35 -19.085 3.277 14.543 1.00 32.74 O -ANISOU 5118 O PHE D 35 3260 3923 5258 19 857 -314 O -ATOM 5119 CB PHE D 35 -21.251 4.303 12.202 1.00 34.43 C -ANISOU 5119 CB PHE D 35 3115 4146 5821 462 844 -320 C -ATOM 5120 CG PHE D 35 -22.293 3.533 12.942 1.00 37.71 C -ANISOU 5120 CG PHE D 35 3386 4701 6241 366 938 -367 C -ATOM 5121 CD1 PHE D 35 -23.046 4.137 13.938 1.00 38.52 C -ANISOU 5121 CD1 PHE D 35 3449 4846 6339 366 1136 -487 C -ATOM 5122 CD2 PHE D 35 -22.549 2.210 12.611 1.00 41.28 C -ANISOU 5122 CD2 PHE D 35 3744 5251 6691 258 836 -308 C -ATOM 5123 CE1 PHE D 35 -24.025 3.429 14.609 1.00 43.93 C -ANISOU 5123 CE1 PHE D 35 3989 5703 6999 231 1236 -552 C -ATOM 5124 CE2 PHE D 35 -23.525 1.493 13.277 1.00 40.41 C -ANISOU 5124 CE2 PHE D 35 3524 5279 6552 116 928 -353 C -ATOM 5125 CZ PHE D 35 -24.264 2.102 14.278 1.00 43.21 C -ANISOU 5125 CZ PHE D 35 3824 5709 6884 89 1132 -477 C -ATOM 5126 N ILE D 36 -18.287 3.469 12.460 1.00 27.44 N -ANISOU 5126 N ILE D 36 2543 3208 4675 195 630 -248 N -ATOM 5127 CA ILE D 36 -17.184 2.552 12.689 1.00 23.52 C -ANISOU 5127 CA ILE D 36 2116 2747 4072 82 497 -228 C -ATOM 5128 C ILE D 36 -15.955 3.149 12.032 1.00 31.13 C -ANISOU 5128 C ILE D 36 3152 3708 4968 94 420 -254 C -ATOM 5129 O ILE D 36 -15.864 3.192 10.805 1.00 33.06 O -ANISOU 5129 O ILE D 36 3324 3968 5270 167 324 -237 O -ATOM 5130 CB ILE D 36 -17.463 1.157 12.092 1.00 25.84 C -ANISOU 5130 CB ILE D 36 2302 3088 4427 83 342 -175 C -ATOM 5131 CG1 ILE D 36 -18.843 0.648 12.493 1.00 27.32 C -ANISOU 5131 CG1 ILE D 36 2397 3308 4675 44 430 -158 C -ATOM 5132 CG2 ILE D 36 -16.389 0.154 12.494 1.00 24.30 C -ANISOU 5132 CG2 ILE D 36 2201 2901 4129 3 188 -167 C -ATOM 5133 CD1 ILE D 36 -19.226 -0.678 11.824 1.00 32.22 C -ANISOU 5133 CD1 ILE D 36 2930 3964 5350 20 290 -109 C -ATOM 5134 N PRO D 37 -15.011 3.642 12.848 1.00 30.69 N -ANISOU 5134 N PRO D 37 3236 3657 4769 -7 470 -304 N -ATOM 5135 CA PRO D 37 -13.806 4.250 12.282 1.00 29.09 C -ANISOU 5135 CA PRO D 37 3096 3493 4463 -46 415 -354 C -ATOM 5136 C PRO D 37 -13.033 3.248 11.426 1.00 28.00 C -ANISOU 5136 C PRO D 37 2851 3469 4319 -27 208 -366 C -ATOM 5137 O PRO D 37 -13.012 2.055 11.732 1.00 27.43 O -ANISOU 5137 O PRO D 37 2728 3428 4266 -13 98 -348 O -ATOM 5138 CB PRO D 37 -13.000 4.644 13.526 1.00 30.47 C -ANISOU 5138 CB PRO D 37 3411 3697 4469 -183 498 -413 C -ATOM 5139 CG PRO D 37 -14.044 4.871 14.588 1.00 31.38 C -ANISOU 5139 CG PRO D 37 3569 3730 4623 -196 668 -399 C -ATOM 5140 CD PRO D 37 -15.088 3.814 14.311 1.00 30.80 C -ANISOU 5140 CD PRO D 37 3354 3658 4691 -116 604 -330 C -ATOM 5141 N HIS D 38 -12.422 3.737 10.355 1.00 28.06 N -ANISOU 5141 N HIS D 38 3701 2642 4319 -361 344 -438 N -ATOM 5142 CA HIS D 38 -11.639 2.903 9.454 1.00 25.26 C -ANISOU 5142 CA HIS D 38 3340 2329 3930 -421 329 -340 C -ATOM 5143 C HIS D 38 -10.650 2.008 10.197 1.00 23.49 C -ANISOU 5143 C HIS D 38 3028 2269 3628 -492 336 -366 C -ATOM 5144 O HIS D 38 -10.544 0.815 9.922 1.00 23.85 O -ANISOU 5144 O HIS D 38 3022 2404 3635 -478 310 -297 O -ATOM 5145 CB HIS D 38 -10.859 3.788 8.477 1.00 28.04 C -ANISOU 5145 CB HIS D 38 3800 2542 4311 -497 345 -308 C -ATOM 5146 CG HIS D 38 -10.025 3.009 7.509 1.00 27.59 C -ANISOU 5146 CG HIS D 38 3724 2553 4206 -555 333 -223 C -ATOM 5147 ND1 HIS D 38 -8.652 2.936 7.597 1.00 31.10 N -ANISOU 5147 ND1 HIS D 38 4142 3073 4602 -679 357 -257 N -ATOM 5148 CD2 HIS D 38 -10.374 2.250 6.441 1.00 26.07 C -ANISOU 5148 CD2 HIS D 38 3521 2386 3998 -498 296 -125 C -ATOM 5149 CE1 HIS D 38 -8.188 2.178 6.619 1.00 29.32 C -ANISOU 5149 CE1 HIS D 38 3892 2915 4333 -688 337 -181 C -ATOM 5150 NE2 HIS D 38 -9.212 1.746 5.907 1.00 31.38 N -ANISOU 5150 NE2 HIS D 38 4166 3143 4614 -581 298 -102 N -ATOM 5151 N GLY D 39 -9.922 2.604 11.133 1.00 29.37 N -ANISOU 5151 N GLY D 39 3759 3051 4349 -559 366 -475 N -ATOM 5152 CA GLY D 39 -8.885 1.893 11.863 1.00 29.14 C -ANISOU 5152 CA GLY D 39 3645 3196 4231 -612 367 -512 C -ATOM 5153 C GLY D 39 -9.431 0.719 12.657 1.00 29.59 C -ANISOU 5153 C GLY D 39 3622 3393 4227 -535 350 -472 C -ATOM 5154 O GLY D 39 -8.783 -0.327 12.781 1.00 28.07 O -ANISOU 5154 O GLY D 39 3382 3318 3967 -535 330 -428 O -ATOM 5155 N LEU D 40 -10.637 0.882 13.191 1.00 25.89 N -ANISOU 5155 N LEU D 40 3142 2915 3781 -467 360 -485 N -ATOM 5156 CA ALEU D 40 -11.304 -0.192 13.925 0.07 27.03 C -ANISOU 5156 CA ALEU D 40 3216 3184 3870 -414 358 -431 C -ATOM 5157 CA BLEU D 40 -11.282 -0.202 13.927 0.93 26.29 C -ANISOU 5157 CA BLEU D 40 3122 3092 3775 -415 358 -431 C -ATOM 5158 C LEU D 40 -11.639 -1.332 12.965 1.00 27.36 C -ANISOU 5158 C LEU D 40 3267 3192 3939 -394 327 -301 C -ATOM 5159 O LEU D 40 -11.520 -2.512 13.305 1.00 24.40 O -ANISOU 5159 O LEU D 40 2857 2900 3514 -387 317 -231 O -ATOM 5160 CB ALEU D 40 -12.582 0.326 14.588 0.07 28.70 C -ANISOU 5160 CB ALEU D 40 3399 3407 4098 -354 382 -485 C -ATOM 5161 CB BLEU D 40 -12.527 0.309 14.664 0.93 27.68 C -ANISOU 5161 CB BLEU D 40 3266 3288 3963 -356 383 -488 C -ATOM 5162 CG ALEU D 40 -13.017 -0.213 15.952 0.07 30.59 C -ANISOU 5162 CG ALEU D 40 3549 3828 4244 -330 410 -498 C -ATOM 5163 CG BLEU D 40 -13.331 -0.711 15.461 0.93 29.62 C -ANISOU 5163 CG BLEU D 40 3434 3674 4146 -324 399 -428 C -ATOM 5164 CD1ALEU D 40 -14.529 -0.102 16.100 0.07 31.65 C -ANISOU 5164 CD1ALEU D 40 3643 3976 4407 -269 428 -503 C -ATOM 5165 CD1BLEU D 40 -12.404 -1.484 16.373 0.93 31.66 C -ANISOU 5165 CD1BLEU D 40 3655 4084 4292 -350 404 -402 C -ATOM 5166 CD2ALEU D 40 -12.554 -1.642 16.193 0.07 30.49 C -ANISOU 5166 CD2ALEU D 40 3510 3918 4157 -348 401 -379 C -ATOM 5167 CD2BLEU D 40 -14.427 -0.016 16.272 0.93 32.96 C -ANISOU 5167 CD2BLEU D 40 3805 4156 4561 -271 431 -520 C -ATOM 5168 N ILE D 41 -12.071 -0.970 11.761 1.00 23.49 N -ANISOU 5168 N ILE D 41 2828 2573 3526 -378 309 -271 N -ATOM 5169 CA ILE D 41 -12.355 -1.960 10.738 1.00 24.02 C -ANISOU 5169 CA ILE D 41 2897 2611 3619 -361 274 -176 C -ATOM 5170 C ILE D 41 -11.074 -2.735 10.443 1.00 24.87 C -ANISOU 5170 C ILE D 41 3005 2764 3682 -398 251 -144 C -ATOM 5171 O ILE D 41 -11.092 -3.958 10.354 1.00 22.49 O -ANISOU 5171 O ILE D 41 2682 2496 3368 -381 226 -82 O -ATOM 5172 CB ILE D 41 -12.886 -1.304 9.453 1.00 23.94 C -ANISOU 5172 CB ILE D 41 2940 2480 3676 -328 254 -158 C -ATOM 5173 CG1 ILE D 41 -14.249 -0.664 9.712 1.00 22.02 C -ANISOU 5173 CG1 ILE D 41 2684 2210 3472 -257 264 -194 C -ATOM 5174 CG2 ILE D 41 -13.008 -2.324 8.344 1.00 21.50 C -ANISOU 5174 CG2 ILE D 41 2621 2166 3381 -313 213 -84 C -ATOM 5175 CD1 ILE D 41 -14.704 0.255 8.572 1.00 26.57 C -ANISOU 5175 CD1 ILE D 41 3331 2664 4102 -198 242 -182 C -ATOM 5176 N MET D 42 -9.958 -2.021 10.315 1.00 23.97 N -ANISOU 5176 N MET D 42 2913 2652 3544 -449 260 -195 N -ATOM 5177 CA MET D 42 -8.662 -2.669 10.068 1.00 27.55 C -ANISOU 5177 CA MET D 42 3346 3185 3939 -477 238 -190 C -ATOM 5178 C MET D 42 -8.279 -3.656 11.177 1.00 23.79 C -ANISOU 5178 C MET D 42 2817 2836 3386 -445 227 -183 C -ATOM 5179 O MET D 42 -7.913 -4.798 10.899 1.00 22.25 O -ANISOU 5179 O MET D 42 2613 2674 3167 -406 189 -129 O -ATOM 5180 CB MET D 42 -7.553 -1.621 9.869 1.00 25.89 C -ANISOU 5180 CB MET D 42 3148 2980 3709 -562 263 -265 C -ATOM 5181 CG MET D 42 -7.726 -0.707 8.661 1.00 29.40 C -ANISOU 5181 CG MET D 42 3666 3291 4214 -600 276 -241 C -ATOM 5182 SD MET D 42 -7.778 -1.611 7.095 1.00 33.38 S -ANISOU 5182 SD MET D 42 4177 3787 4721 -558 230 -145 S -ATOM 5183 CE MET D 42 -9.560 -1.776 6.933 1.00 41.72 C -ANISOU 5183 CE MET D 42 5255 4745 5850 -462 211 -91 C -ATOM 5184 N ASP D 43 -8.367 -3.224 12.429 1.00 21.27 N -ANISOU 5184 N ASP D 43 2469 2590 3022 -449 258 -237 N -ATOM 5185 CA ASP D 43 -8.002 -4.095 13.544 1.00 24.73 C -ANISOU 5185 CA ASP D 43 2864 3168 3365 -408 250 -217 C -ATOM 5186 C ASP D 43 -8.858 -5.356 13.588 1.00 24.51 C -ANISOU 5186 C ASP D 43 2851 3107 3353 -357 236 -95 C -ATOM 5187 O ASP D 43 -8.343 -6.450 13.829 1.00 25.47 O -ANISOU 5187 O ASP D 43 2975 3280 3423 -312 206 -32 O -ATOM 5188 CB ASP D 43 -8.114 -3.363 14.896 1.00 21.91 C -ANISOU 5188 CB ASP D 43 2465 2915 2946 -416 288 -302 C -ATOM 5189 CG ASP D 43 -7.102 -2.233 15.043 1.00 28.74 C -ANISOU 5189 CG ASP D 43 3306 3826 3787 -481 301 -443 C -ATOM 5190 OD1 ASP D 43 -5.995 -2.341 14.485 1.00 28.77 O -ANISOU 5190 OD1 ASP D 43 3298 3864 3769 -513 279 -465 O -ATOM 5191 OD2 ASP D 43 -7.416 -1.251 15.741 1.00 32.41 O -ANISOU 5191 OD2 ASP D 43 3757 4301 4255 -505 335 -544 O -ATOM 5192 N ARG D 44 -10.165 -5.199 13.386 1.00 21.75 N -ANISOU 5192 N ARG D 44 2511 2675 3076 -363 258 -67 N -ATOM 5193 CA ARG D 44 -11.063 -6.357 13.360 1.00 20.73 C -ANISOU 5193 CA ARG D 44 2390 2509 2978 -348 254 37 C -ATOM 5194 C ARG D 44 -10.759 -7.267 12.171 1.00 23.26 C -ANISOU 5194 C ARG D 44 2746 2739 3353 -335 203 86 C -ATOM 5195 O ARG D 44 -10.782 -8.492 12.291 1.00 23.37 O -ANISOU 5195 O ARG D 44 2781 2732 3366 -316 183 166 O -ATOM 5196 CB ARG D 44 -12.530 -5.913 13.320 1.00 22.67 C -ANISOU 5196 CB ARG D 44 2612 2716 3286 -363 288 29 C -ATOM 5197 CG ARG D 44 -13.517 -7.063 13.271 1.00 23.11 C -ANISOU 5197 CG ARG D 44 2659 2742 3379 -379 295 120 C -ATOM 5198 CD ARG D 44 -13.469 -7.924 14.523 1.00 21.39 C -ANISOU 5198 CD ARG D 44 2437 2613 3078 -388 326 203 C -ATOM 5199 NE ARG D 44 -14.478 -8.986 14.437 1.00 24.89 N -ANISOU 5199 NE ARG D 44 2880 3006 3572 -435 344 294 N -ATOM 5200 CZ ARG D 44 -14.300 -10.223 14.871 1.00 28.81 C -ANISOU 5200 CZ ARG D 44 3422 3478 4045 -450 346 410 C -ATOM 5201 NH1 ARG D 44 -13.146 -10.576 15.426 1.00 28.54 N -ANISOU 5201 NH1 ARG D 44 3435 3484 3925 -394 323 452 N -ATOM 5202 NH2 ARG D 44 -15.277 -11.109 14.741 1.00 26.23 N -ANISOU 5202 NH2 ARG D 44 3098 3088 3782 -521 371 481 N -ATOM 5203 N THR D 45 -10.465 -6.660 11.025 1.00 21.74 N -ANISOU 5203 N THR D 45 2566 2490 3206 -343 181 38 N -ATOM 5204 CA THR D 45 -10.148 -7.413 9.810 1.00 22.29 C -ANISOU 5204 CA THR D 45 2655 2500 3315 -324 130 61 C -ATOM 5205 C THR D 45 -8.858 -8.218 9.985 1.00 24.87 C -ANISOU 5205 C THR D 45 2985 2889 3575 -284 93 67 C -ATOM 5206 O THR D 45 -8.748 -9.357 9.498 1.00 25.43 O -ANISOU 5206 O THR D 45 3077 2915 3672 -243 48 103 O -ATOM 5207 CB THR D 45 -10.068 -6.458 8.599 1.00 24.56 C -ANISOU 5207 CB THR D 45 2951 2744 3636 -340 124 16 C -ATOM 5208 OG1 THR D 45 -11.362 -5.870 8.383 1.00 23.58 O -ANISOU 5208 OG1 THR D 45 2828 2561 3572 -342 144 18 O -ATOM 5209 CG2 THR D 45 -9.640 -7.195 7.338 1.00 23.54 C -ANISOU 5209 CG2 THR D 45 2828 2594 3523 -315 72 24 C -ATOM 5210 N GLU D 46 -7.892 -7.655 10.712 1.00 22.30 N -ANISOU 5210 N GLU D 46 2635 2674 3165 -287 106 17 N -ATOM 5211 CA GLU D 46 -6.657 -8.386 10.998 1.00 22.17 C -ANISOU 5211 CA GLU D 46 2605 2754 3066 -227 65 11 C -ATOM 5212 C GLU D 46 -6.970 -9.678 11.756 1.00 23.09 C -ANISOU 5212 C GLU D 46 2758 2849 3167 -161 47 109 C -ATOM 5213 O GLU D 46 -6.418 -10.739 11.460 1.00 22.67 O -ANISOU 5213 O GLU D 46 2731 2777 3106 -85 -8 138 O -ATOM 5214 CB GLU D 46 -5.667 -7.528 11.811 1.00 24.23 C -ANISOU 5214 CB GLU D 46 2812 3166 3227 -247 86 -75 C -ATOM 5215 CG GLU D 46 -4.377 -8.281 12.100 1.00 22.79 C -ANISOU 5215 CG GLU D 46 2596 3119 2944 -165 36 -95 C -ATOM 5216 CD GLU D 46 -3.409 -7.498 12.968 1.00 34.51 C -ANISOU 5216 CD GLU D 46 4005 4787 4319 -187 52 -199 C -ATOM 5217 OE1 GLU D 46 -2.352 -8.059 13.314 1.00 34.51 O -ANISOU 5217 OE1 GLU D 46 3960 4934 4218 -105 8 -228 O -ATOM 5218 OE2 GLU D 46 -3.700 -6.329 13.295 1.00 44.03 O -ANISOU 5218 OE2 GLU D 46 5194 5994 5541 -278 105 -263 O -ATOM 5219 N ARG D 47 -7.857 -9.603 12.742 1.00 21.69 N -ANISOU 5219 N ARG D 47 2588 2672 2982 -186 93 162 N -ATOM 5220 CA ARG D 47 -8.220 -10.807 13.480 1.00 24.38 C -ANISOU 5220 CA ARG D 47 2977 2982 3305 -145 90 281 C -ATOM 5221 C ARG D 47 -8.985 -11.776 12.576 1.00 26.55 C -ANISOU 5221 C ARG D 47 3304 3085 3700 -160 68 340 C -ATOM 5222 O ARG D 47 -8.760 -12.999 12.621 1.00 24.74 O -ANISOU 5222 O ARG D 47 3138 2782 3480 -105 31 415 O -ATOM 5223 CB ARG D 47 -9.027 -10.452 14.734 1.00 23.87 C -ANISOU 5223 CB ARG D 47 2893 2989 3189 -184 157 323 C -ATOM 5224 CG ARG D 47 -9.806 -11.615 15.350 1.00 30.56 C -ANISOU 5224 CG ARG D 47 3796 3775 4041 -189 179 470 C -ATOM 5225 CD ARG D 47 -8.942 -12.857 15.601 1.00 43.95 C -ANISOU 5225 CD ARG D 47 5567 5445 5685 -90 125 564 C -ATOM 5226 NE ARG D 47 -8.394 -12.896 16.938 1.00 52.35 N -ANISOU 5226 NE ARG D 47 6626 6670 6592 -24 137 615 N -ATOM 5227 CZ ARG D 47 -8.790 -13.730 17.891 1.00 49.02 C -ANISOU 5227 CZ ARG D 47 6266 6247 6110 -9 166 770 C -ATOM 5228 NH1 ARG D 47 -9.733 -14.633 17.658 1.00 56.72 N -ANISOU 5228 NH1 ARG D 47 7317 7048 7185 -76 192 887 N -ATOM 5229 NH2 ARG D 47 -8.222 -13.664 19.079 1.00 39.98 N -ANISOU 5229 NH2 ARG D 47 5107 5286 4800 67 171 807 N -ATOM 5230 N LEU D 48 -9.893 -11.248 11.763 1.00 25.42 N -ANISOU 5230 N LEU D 48 3137 2874 3648 -228 87 299 N -ATOM 5231 CA LEU D 48 -10.660 -12.127 10.872 1.00 27.59 C -ANISOU 5231 CA LEU D 48 3440 3008 4035 -251 65 327 C -ATOM 5232 C LEU D 48 -9.732 -12.899 9.934 1.00 25.49 C -ANISOU 5232 C LEU D 48 3205 2691 3789 -179 -11 297 C -ATOM 5233 O LEU D 48 -9.955 -14.074 9.676 1.00 22.44 O -ANISOU 5233 O LEU D 48 2872 2187 3467 -164 -42 339 O -ATOM 5234 CB LEU D 48 -11.719 -11.363 10.069 1.00 27.76 C -ANISOU 5234 CB LEU D 48 3413 3001 4131 -312 86 271 C -ATOM 5235 CG LEU D 48 -12.908 -10.804 10.850 1.00 27.04 C -ANISOU 5235 CG LEU D 48 3282 2950 4042 -372 154 288 C -ATOM 5236 CD1 LEU D 48 -13.870 -10.039 9.943 1.00 27.31 C -ANISOU 5236 CD1 LEU D 48 3267 2967 4143 -394 157 221 C -ATOM 5237 CD2 LEU D 48 -13.632 -11.914 11.594 1.00 25.43 C -ANISOU 5237 CD2 LEU D 48 3099 2706 3856 -422 186 387 C -ATOM 5238 N ALA D 49 -8.693 -12.249 9.423 1.00 20.67 N -ANISOU 5238 N ALA D 49 2560 2168 3124 -140 -38 217 N -ATOM 5239 CA ALA D 49 -7.754 -12.943 8.519 1.00 21.56 C -ANISOU 5239 CA ALA D 49 2681 2272 3237 -61 -110 169 C -ATOM 5240 C ALA D 49 -7.150 -14.156 9.216 1.00 22.78 C -ANISOU 5240 C ALA D 49 2898 2399 3360 35 -151 229 C -ATOM 5241 O ALA D 49 -6.967 -15.223 8.621 1.00 24.37 O -ANISOU 5241 O ALA D 49 3144 2503 3614 101 -210 222 O -ATOM 5242 CB ALA D 49 -6.653 -11.992 8.054 1.00 23.03 C -ANISOU 5242 CB ALA D 49 2807 2600 3345 -51 -116 78 C -ATOM 5243 N ARG D 50 -6.835 -13.989 10.494 1.00 24.10 N -ANISOU 5243 N ARG D 50 3071 2652 3434 56 -124 284 N -ATOM 5244 CA ARG D 50 -6.255 -15.087 11.257 1.00 26.52 C -ANISOU 5244 CA ARG D 50 3446 2941 3688 169 -164 362 C -ATOM 5245 C ARG D 50 -7.278 -16.198 11.482 1.00 27.99 C -ANISOU 5245 C ARG D 50 3735 2930 3971 138 -152 484 C -ATOM 5246 O ARG D 50 -6.952 -17.385 11.367 1.00 24.85 O -ANISOU 5246 O ARG D 50 3425 2412 3606 228 -209 528 O -ATOM 5247 CB ARG D 50 -5.685 -14.576 12.585 1.00 31.62 C -ANISOU 5247 CB ARG D 50 4062 3762 4189 203 -137 388 C -ATOM 5248 CG ARG D 50 -4.519 -15.409 13.108 1.00 38.31 C -ANISOU 5248 CG ARG D 50 4943 4680 4934 371 -206 415 C -ATOM 5249 CD ARG D 50 -3.965 -14.842 14.407 1.00 43.24 C -ANISOU 5249 CD ARG D 50 5517 5516 5397 409 -184 422 C -ATOM 5250 NE ARG D 50 -4.921 -14.969 15.504 1.00 49.52 N -ANISOU 5250 NE ARG D 50 6364 6279 6172 357 -120 558 N -ATOM 5251 CZ ARG D 50 -4.795 -14.374 16.689 1.00 56.43 C -ANISOU 5251 CZ ARG D 50 7190 7338 6914 359 -82 567 C -ATOM 5252 NH1 ARG D 50 -3.753 -13.590 16.941 1.00 57.19 N -ANISOU 5252 NH1 ARG D 50 7182 7650 6896 402 -102 438 N -ATOM 5253 NH2 ARG D 50 -5.717 -14.557 17.626 1.00 55.59 N -ANISOU 5253 NH2 ARG D 50 7126 7213 6782 310 -19 696 N -ATOM 5254 N ASP D 51 -8.519 -15.822 11.778 1.00 29.59 N -ANISOU 5254 N ASP D 51 3925 3095 4223 8 -78 530 N -ATOM 5255 CA ASP D 51 -9.585 -16.808 11.932 1.00 28.40 C -ANISOU 5255 CA ASP D 51 3852 2768 4171 -64 -52 635 C -ATOM 5256 C ASP D 51 -9.802 -17.564 10.611 1.00 26.42 C -ANISOU 5256 C ASP D 51 3629 2351 4058 -68 -108 567 C -ATOM 5257 O ASP D 51 -10.018 -18.774 10.596 1.00 28.88 O -ANISOU 5257 O ASP D 51 4039 2485 4449 -63 -130 632 O -ATOM 5258 CB ASP D 51 -10.893 -16.107 12.335 1.00 31.07 C -ANISOU 5258 CB ASP D 51 4131 3145 4530 -207 38 656 C -ATOM 5259 CG ASP D 51 -10.815 -15.435 13.700 1.00 34.24 C -ANISOU 5259 CG ASP D 51 4502 3711 4795 -206 97 713 C -ATOM 5260 OD1 ASP D 51 -9.885 -15.742 14.469 1.00 32.45 O -ANISOU 5260 OD1 ASP D 51 4319 3551 4461 -106 73 770 O -ATOM 5261 OD2 ASP D 51 -11.705 -14.612 14.012 1.00 38.03 O -ANISOU 5261 OD2 ASP D 51 4911 4268 5272 -295 163 691 O -ATOM 5262 N VAL D 52 -9.776 -16.828 9.504 1.00 24.84 N -ANISOU 5262 N VAL D 52 3344 2210 3886 -81 -128 437 N -ATOM 5263 CA VAL D 52 -9.983 -17.435 8.191 1.00 28.36 C -ANISOU 5263 CA VAL D 52 3791 2541 4442 -79 -184 350 C -ATOM 5264 C VAL D 52 -8.910 -18.469 7.895 1.00 30.36 C -ANISOU 5264 C VAL D 52 4116 2725 4697 61 -270 326 C -ATOM 5265 O VAL D 52 -9.213 -19.609 7.514 1.00 29.68 O -ANISOU 5265 O VAL D 52 4105 2455 4719 66 -307 326 O -ATOM 5266 CB VAL D 52 -10.024 -16.383 7.083 1.00 26.53 C -ANISOU 5266 CB VAL D 52 3456 2419 4203 -98 -191 229 C -ATOM 5267 CG1 VAL D 52 -9.842 -17.030 5.723 1.00 29.86 C -ANISOU 5267 CG1 VAL D 52 3871 2779 4694 -51 -265 122 C -ATOM 5268 CG2 VAL D 52 -11.343 -15.614 7.140 1.00 27.37 C -ANISOU 5268 CG2 VAL D 52 3505 2545 4347 -219 -124 237 C -ATOM 5269 N MET D 53 -7.652 -18.093 8.099 1.00 25.98 N -ANISOU 5269 N MET D 53 3535 2315 4022 177 -302 296 N -ATOM 5270 CA AMET D 53 -6.564 -19.034 7.833 0.63 27.95 C -ANISOU 5270 CA AMET D 53 3835 2531 4255 340 -391 257 C -ATOM 5271 CA BMET D 53 -6.531 -19.012 7.869 0.37 29.00 C -ANISOU 5271 CA BMET D 53 3967 2670 4382 342 -391 258 C -ATOM 5272 C MET D 53 -6.616 -20.265 8.731 1.00 32.28 C -ANISOU 5272 C MET D 53 4529 2902 4833 403 -409 389 C -ATOM 5273 O MET D 53 -6.250 -21.368 8.300 1.00 32.57 O -ANISOU 5273 O MET D 53 4648 2793 4935 510 -484 361 O -ATOM 5274 CB AMET D 53 -5.203 -18.335 7.897 0.63 30.86 C -ANISOU 5274 CB AMET D 53 4119 3130 4475 444 -418 184 C -ATOM 5275 CB BMET D 53 -5.190 -18.311 8.121 0.37 31.42 C -ANISOU 5275 CB BMET D 53 4197 3209 4534 444 -412 203 C -ATOM 5276 CG AMET D 53 -4.957 -17.420 6.707 0.63 30.55 C -ANISOU 5276 CG AMET D 53 3963 3226 4419 400 -419 48 C -ATOM 5277 CG BMET D 53 -4.617 -17.532 6.941 0.37 30.84 C -ANISOU 5277 CG BMET D 53 4005 3287 4425 441 -430 53 C -ATOM 5278 SD AMET D 53 -4.967 -18.347 5.154 0.63 37.40 S -ANISOU 5278 SD AMET D 53 4833 3993 5385 463 -500 -75 S -ATOM 5279 SD BMET D 53 -4.052 -18.558 5.562 0.37 37.70 S -ANISOU 5279 SD BMET D 53 4873 4104 5347 569 -533 -81 S -ATOM 5280 CE AMET D 53 -3.524 -19.380 5.395 0.63 41.22 C -ANISOU 5280 CE AMET D 53 5353 4509 5798 689 -598 -118 C -ATOM 5281 CE BMET D 53 -5.520 -18.510 4.541 0.37 39.37 C -ANISOU 5281 CE BMET D 53 5081 4174 5704 422 -505 -106 C -ATOM 5282 N LYS D 54 -7.088 -20.098 9.964 1.00 32.14 N -ANISOU 5282 N LYS D 54 4551 2891 4769 339 -339 534 N -ATOM 5283 CA LYS D 54 -7.193 -21.240 10.876 1.00 34.51 C -ANISOU 5283 CA LYS D 54 5006 3023 5086 387 -342 695 C -ATOM 5284 C LYS D 54 -8.193 -22.261 10.347 1.00 33.68 C -ANISOU 5284 C LYS D 54 4995 2639 5163 286 -339 720 C -ATOM 5285 O LYS D 54 -7.981 -23.466 10.461 1.00 31.34 O -ANISOU 5285 O LYS D 54 4845 2135 4929 368 -387 785 O -ATOM 5286 CB LYS D 54 -7.581 -20.790 12.295 1.00 40.69 C -ANISOU 5286 CB LYS D 54 5796 3903 5763 322 -256 848 C -ATOM 5287 CG LYS D 54 -7.232 -21.791 13.392 1.00 49.40 C -ANISOU 5287 CG LYS D 54 7051 4915 6804 431 -270 1029 C -ATOM 5288 CD LYS D 54 -7.736 -21.353 14.767 1.00 56.04 C -ANISOU 5288 CD LYS D 54 7888 5876 7529 354 -176 1181 C -ATOM 5289 CE LYS D 54 -9.261 -21.264 14.816 1.00 58.83 C -ANISOU 5289 CE LYS D 54 8231 6137 7986 121 -72 1238 C -ATOM 5290 NZ LYS D 54 -9.729 -19.869 15.095 1.00 58.23 N -ANISOU 5290 NZ LYS D 54 7996 6292 7838 19 0 1167 N -ATOM 5291 N GLU D 55 -9.280 -21.789 9.754 1.00 31.68 N -ANISOU 5291 N GLU D 55 4661 2378 4998 113 -286 658 N -ATOM 5292 CA GLU D 55 -10.307 -22.717 9.284 1.00 36.31 C -ANISOU 5292 CA GLU D 55 5314 2725 5758 -10 -275 662 C -ATOM 5293 C GLU D 55 -10.084 -23.205 7.849 1.00 34.65 C -ANISOU 5293 C GLU D 55 5085 2424 5655 45 -364 482 C -ATOM 5294 O GLU D 55 -10.440 -24.335 7.512 1.00 36.71 O -ANISOU 5294 O GLU D 55 5448 2444 6058 17 -394 471 O -ATOM 5295 CB GLU D 55 -11.697 -22.091 9.406 1.00 39.04 C -ANISOU 5295 CB GLU D 55 5570 3120 6143 -223 -176 678 C -ATOM 5296 CG GLU D 55 -12.167 -21.892 10.831 1.00 54.47 C -ANISOU 5296 CG GLU D 55 7553 5127 8015 -304 -79 858 C -ATOM 5297 CD GLU D 55 -13.639 -21.516 10.909 1.00 65.29 C -ANISOU 5297 CD GLU D 55 8836 6528 9443 -514 16 862 C -ATOM 5298 OE1 GLU D 55 -13.959 -20.524 11.606 1.00 67.90 O -ANISOU 5298 OE1 GLU D 55 9079 7052 9670 -555 84 893 O -ATOM 5299 OE2 GLU D 55 -14.467 -22.216 10.279 1.00 68.82 O -ANISOU 5299 OE2 GLU D 55 9295 6817 10038 -635 20 817 O -ATOM 5300 N MET D 56 -9.491 -22.348 7.021 1.00 30.48 N -ANISOU 5300 N MET D 56 4430 2093 5058 116 -403 338 N -ATOM 5301 CA MET D 56 -9.456 -22.550 5.573 1.00 30.18 C -ANISOU 5301 CA MET D 56 4332 2039 5095 143 -472 154 C -ATOM 5302 C MET D 56 -8.056 -22.697 4.993 1.00 33.88 C -ANISOU 5302 C MET D 56 4786 2598 5490 346 -566 44 C -ATOM 5303 O MET D 56 -7.907 -23.017 3.814 1.00 32.12 O -ANISOU 5303 O MET D 56 4520 2366 5317 394 -631 -114 O -ATOM 5304 CB MET D 56 -10.149 -21.371 4.883 1.00 32.79 C -ANISOU 5304 CB MET D 56 4511 2542 5405 33 -428 73 C -ATOM 5305 CG MET D 56 -11.580 -21.160 5.340 1.00 33.96 C -ANISOU 5305 CG MET D 56 4640 2644 5619 -156 -340 146 C -ATOM 5306 SD MET D 56 -12.372 -19.892 4.356 1.00 31.20 S -ANISOU 5306 SD MET D 56 4122 2483 5250 -234 -316 32 S -ATOM 5307 CE MET D 56 -12.676 -20.783 2.823 1.00 27.12 C -ANISOU 5307 CE MET D 56 3577 1872 4855 -226 -399 -151 C -ATOM 5308 N GLY D 57 -7.032 -22.477 5.814 1.00 36.44 N -ANISOU 5308 N GLY D 57 5129 3031 5684 469 -576 114 N -ATOM 5309 CA GLY D 57 -5.663 -22.480 5.321 1.00 35.01 C -ANISOU 5309 CA GLY D 57 4899 2995 5407 657 -658 -1 C -ATOM 5310 C GLY D 57 -5.064 -23.818 4.934 1.00 37.18 C -ANISOU 5310 C GLY D 57 5273 3105 5748 832 -763 -71 C -ATOM 5311 O GLY D 57 -3.881 -23.893 4.589 1.00 38.27 O -ANISOU 5311 O GLY D 57 5363 3382 5795 1011 -836 -174 O -ATOM 5312 N GLY D 58 -5.858 -24.885 4.980 1.00 34.71 N -ANISOU 5312 N GLY D 58 5095 2496 5595 781 -771 -25 N -ATOM 5313 CA GLY D 58 -5.330 -26.213 4.744 1.00 40.19 C -ANISOU 5313 CA GLY D 58 5918 2981 6371 953 -871 -79 C -ATOM 5314 C GLY D 58 -5.332 -26.627 3.284 1.00 36.82 C -ANISOU 5314 C GLY D 58 5430 2525 6033 990 -945 -308 C -ATOM 5315 O GLY D 58 -4.761 -27.647 2.922 1.00 40.66 O -ANISOU 5315 O GLY D 58 5999 2871 6578 1161 -1043 -403 O -ATOM 5316 N HIS D 59 -5.974 -25.833 2.440 1.00 34.02 N -ANISOU 5316 N HIS D 59 4931 2311 5683 842 -904 -402 N -ATOM 5317 CA HIS D 59 -6.086 -26.193 1.035 1.00 34.21 C -ANISOU 5317 CA HIS D 59 4884 2337 5779 866 -970 -621 C -ATOM 5318 C HIS D 59 -6.247 -24.920 0.223 1.00 29.99 C -ANISOU 5318 C HIS D 59 4158 2097 5139 779 -928 -698 C -ATOM 5319 O HIS D 59 -6.643 -23.905 0.757 1.00 32.09 O -ANISOU 5319 O HIS D 59 4378 2476 5340 657 -841 -578 O -ATOM 5320 CB HIS D 59 -7.294 -27.104 0.826 1.00 37.22 C -ANISOU 5320 CB HIS D 59 5359 2417 6367 725 -964 -642 C -ATOM 5321 CG HIS D 59 -7.410 -27.655 -0.562 1.00 46.19 C -ANISOU 5321 CG HIS D 59 6434 3530 7587 762 -1045 -888 C -ATOM 5322 ND1 HIS D 59 -6.567 -28.633 -1.048 1.00 56.01 N -ANISOU 5322 ND1 HIS D 59 7719 4741 8822 942 -1128 -1010 N -ATOM 5323 CD2 HIS D 59 -8.287 -27.386 -1.561 1.00 48.00 C -ANISOU 5323 CD2 HIS D 59 6543 3831 7865 633 -1034 -1023 C -ATOM 5324 CE1 HIS D 59 -6.913 -28.935 -2.288 1.00 57.18 C -ANISOU 5324 CE1 HIS D 59 7775 4934 9015 918 -1168 -1213 C -ATOM 5325 NE2 HIS D 59 -7.953 -28.193 -2.624 1.00 51.82 N -ANISOU 5325 NE2 HIS D 59 6999 4321 8371 736 -1116 -1227 N -ATOM 5326 N HIS D 60 -5.930 -24.986 -1.066 1.00 35.75 N -ANISOU 5326 N HIS D 60 4785 2950 5848 853 -992 -898 N -ATOM 5327 CA HIS D 60 -6.096 -23.849 -1.978 1.00 30.02 C -ANISOU 5327 CA HIS D 60 3891 2496 5019 780 -957 -966 C -ATOM 5328 C HIS D 60 -7.412 -23.104 -1.741 1.00 30.01 C -ANISOU 5328 C HIS D 60 3867 2474 5061 570 -865 -860 C -ATOM 5329 O HIS D 60 -8.494 -23.694 -1.777 1.00 32.32 O -ANISOU 5329 O HIS D 60 4206 2577 5499 463 -859 -871 O -ATOM 5330 CB HIS D 60 -6.025 -24.351 -3.425 1.00 33.12 C -ANISOU 5330 CB HIS D 60 4201 2951 5432 855 -1039 -1197 C -ATOM 5331 CG HIS D 60 -6.078 -23.267 -4.457 1.00 40.20 C -ANISOU 5331 CG HIS D 60 4933 4141 6199 810 -1012 -1262 C -ATOM 5332 ND1 HIS D 60 -5.237 -23.244 -5.548 1.00 45.00 N -ANISOU 5332 ND1 HIS D 60 5429 4975 6695 936 -1069 -1428 N -ATOM 5333 CD2 HIS D 60 -6.880 -22.183 -4.578 1.00 39.65 C -ANISOU 5333 CD2 HIS D 60 4799 4177 6090 663 -935 -1178 C -ATOM 5334 CE1 HIS D 60 -5.508 -22.184 -6.285 1.00 42.33 C -ANISOU 5334 CE1 HIS D 60 4973 4863 6247 857 -1023 -1424 C -ATOM 5335 NE2 HIS D 60 -6.508 -21.529 -5.728 1.00 37.23 N -ANISOU 5335 NE2 HIS D 60 4359 4137 5648 701 -946 -1276 N -ATOM 5336 N ILE D 61 -7.302 -21.798 -1.515 1.00 27.68 N -ANISOU 5336 N ILE D 61 3496 2380 4641 513 -796 -771 N -ATOM 5337 CA ILE D 61 -8.454 -20.950 -1.287 1.00 29.24 C -ANISOU 5337 CA ILE D 61 3663 2590 4858 347 -714 -679 C -ATOM 5338 C ILE D 61 -8.767 -20.155 -2.540 1.00 31.01 C -ANISOU 5338 C ILE D 61 3759 3009 5017 322 -715 -774 C -ATOM 5339 O ILE D 61 -7.869 -19.595 -3.174 1.00 30.25 O -ANISOU 5339 O ILE D 61 3590 3113 4791 399 -730 -824 O -ATOM 5340 CB ILE D 61 -8.189 -19.985 -0.135 1.00 26.53 C -ANISOU 5340 CB ILE D 61 3336 2319 4425 305 -636 -516 C -ATOM 5341 CG1 ILE D 61 -8.143 -20.755 1.177 1.00 30.71 C -ANISOU 5341 CG1 ILE D 61 3994 2660 5013 314 -624 -396 C -ATOM 5342 CG2 ILE D 61 -9.265 -18.894 -0.025 1.00 28.21 C -ANISOU 5342 CG2 ILE D 61 3497 2589 4633 164 -556 -445 C -ATOM 5343 CD1 ILE D 61 -7.735 -19.892 2.329 1.00 31.93 C -ANISOU 5343 CD1 ILE D 61 4156 2914 5062 299 -560 -261 C -ATOM 5344 N VAL D 62 -10.039 -20.135 -2.914 1.00 24.75 N -ANISOU 5344 N VAL D 62 2933 2169 4304 218 -700 -799 N -ATOM 5345 CA VAL D 62 -10.510 -19.182 -3.908 1.00 26.37 C -ANISOU 5345 CA VAL D 62 3025 2565 4430 193 -689 -844 C -ATOM 5346 C VAL D 62 -11.314 -18.114 -3.175 1.00 28.16 C -ANISOU 5346 C VAL D 62 3250 2807 4642 85 -603 -701 C -ATOM 5347 O VAL D 62 -12.340 -18.401 -2.563 1.00 29.93 O -ANISOU 5347 O VAL D 62 3498 2904 4969 -12 -571 -660 O -ATOM 5348 CB VAL D 62 -11.364 -19.850 -4.993 1.00 25.18 C -ANISOU 5348 CB VAL D 62 2809 2403 4356 180 -747 -1007 C -ATOM 5349 CG1 VAL D 62 -11.902 -18.793 -5.969 1.00 32.82 C -ANISOU 5349 CG1 VAL D 62 3663 3589 5219 173 -737 -1029 C -ATOM 5350 CG2 VAL D 62 -10.560 -20.912 -5.728 1.00 29.81 C -ANISOU 5350 CG2 VAL D 62 3396 2973 4959 300 -839 -1173 C -ATOM 5351 N ALA D 63 -10.838 -16.878 -3.225 1.00 22.81 N -ANISOU 5351 N ALA D 63 2542 2285 3837 100 -562 -631 N -ATOM 5352 CA ALA D 63 -11.523 -15.772 -2.569 1.00 21.50 C -ANISOU 5352 CA ALA D 63 2380 2135 3654 21 -487 -512 C -ATOM 5353 C ALA D 63 -12.394 -15.059 -3.592 1.00 29.64 C -ANISOU 5353 C ALA D 63 3331 3281 4650 16 -492 -550 C -ATOM 5354 O ALA D 63 -11.894 -14.551 -4.606 1.00 29.45 O -ANISOU 5354 O ALA D 63 3263 3405 4520 76 -514 -584 O -ATOM 5355 CB ALA D 63 -10.520 -14.816 -1.976 1.00 22.11 C -ANISOU 5355 CB ALA D 63 2484 2289 3628 33 -439 -420 C -ATOM 5356 N LEU D 64 -13.693 -15.020 -3.311 1.00 26.29 N -ANISOU 5356 N LEU D 64 2883 2805 4300 -52 -471 -540 N -ATOM 5357 CA LEU D 64 -14.692 -14.483 -4.225 1.00 24.57 C -ANISOU 5357 CA LEU D 64 2581 2699 4055 -41 -488 -589 C -ATOM 5358 C LEU D 64 -15.193 -13.130 -3.705 1.00 25.36 C -ANISOU 5358 C LEU D 64 2690 2838 4108 -55 -425 -475 C -ATOM 5359 O LEU D 64 -15.847 -13.069 -2.671 1.00 27.17 O -ANISOU 5359 O LEU D 64 2933 2989 4399 -122 -378 -424 O -ATOM 5360 CB LEU D 64 -15.865 -15.464 -4.308 1.00 30.42 C -ANISOU 5360 CB LEU D 64 3268 3373 4919 -106 -514 -690 C -ATOM 5361 CG LEU D 64 -16.468 -15.810 -5.660 1.00 40.97 C -ANISOU 5361 CG LEU D 64 4497 4824 6246 -66 -585 -845 C -ATOM 5362 CD1 LEU D 64 -15.390 -16.435 -6.524 1.00 43.89 C -ANISOU 5362 CD1 LEU D 64 4872 5231 6575 16 -649 -940 C -ATOM 5363 CD2 LEU D 64 -17.645 -16.781 -5.497 1.00 39.79 C -ANISOU 5363 CD2 LEU D 64 4292 4589 6237 -171 -596 -949 C -ATOM 5364 N CYS D 65 -14.895 -12.052 -4.424 1.00 23.61 N -ANISOU 5364 N CYS D 65 2463 2734 3772 10 -424 -437 N -ATOM 5365 CA CYS D 65 -15.330 -10.723 -4.013 1.00 24.96 C -ANISOU 5365 CA CYS D 65 2661 2918 3904 14 -373 -337 C -ATOM 5366 C CYS D 65 -16.727 -10.432 -4.554 1.00 24.97 C -ANISOU 5366 C CYS D 65 2586 2992 3911 52 -398 -379 C -ATOM 5367 O CYS D 65 -16.960 -10.503 -5.770 1.00 25.16 O -ANISOU 5367 O CYS D 65 2549 3133 3877 121 -454 -443 O -ATOM 5368 CB CYS D 65 -14.351 -9.682 -4.539 1.00 27.62 C -ANISOU 5368 CB CYS D 65 3048 3323 4122 57 -355 -263 C -ATOM 5369 SG CYS D 65 -14.791 -7.979 -4.165 1.00 27.18 S -ANISOU 5369 SG CYS D 65 3055 3246 4026 73 -298 -144 S -ATOM 5370 N VAL D 66 -17.662 -10.127 -3.658 1.00 25.38 N -ANISOU 5370 N VAL D 66 2624 2998 4019 16 -360 -355 N -ATOM 5371 CA VAL D 66 -18.988 -9.690 -4.074 1.00 22.69 C -ANISOU 5371 CA VAL D 66 2200 2752 3670 70 -382 -397 C -ATOM 5372 C VAL D 66 -19.013 -8.175 -4.332 1.00 23.63 C -ANISOU 5372 C VAL D 66 2372 2910 3695 173 -369 -304 C -ATOM 5373 O VAL D 66 -19.139 -7.377 -3.402 1.00 22.26 O -ANISOU 5373 O VAL D 66 2252 2670 3537 165 -317 -236 O -ATOM 5374 CB VAL D 66 -20.048 -10.073 -3.043 1.00 26.16 C -ANISOU 5374 CB VAL D 66 2581 3155 4204 -12 -346 -429 C -ATOM 5375 CG1 VAL D 66 -21.430 -9.733 -3.581 1.00 31.08 C -ANISOU 5375 CG1 VAL D 66 3084 3914 4809 52 -380 -505 C -ATOM 5376 CG2 VAL D 66 -19.971 -11.566 -2.745 1.00 25.01 C -ANISOU 5376 CG2 VAL D 66 2415 2929 4159 -129 -350 -496 C -ATOM 5377 N LEU D 67 -18.874 -7.793 -5.601 1.00 26.38 N -ANISOU 5377 N LEU D 67 2715 3363 3946 271 -417 -300 N -ATOM 5378 CA LEU D 67 -18.854 -6.383 -6.023 1.00 23.96 C -ANISOU 5378 CA LEU D 67 2484 3077 3545 376 -409 -193 C -ATOM 5379 C LEU D 67 -20.234 -5.762 -5.863 1.00 28.54 C -ANISOU 5379 C LEU D 67 3013 3701 4132 467 -425 -210 C -ATOM 5380 O LEU D 67 -21.211 -6.503 -5.780 1.00 27.29 O -ANISOU 5380 O LEU D 67 2728 3616 4027 452 -453 -325 O -ATOM 5381 CB LEU D 67 -18.437 -6.316 -7.497 1.00 26.83 C -ANISOU 5381 CB LEU D 67 2840 3569 3785 459 -459 -183 C -ATOM 5382 CG LEU D 67 -16.991 -6.666 -7.817 1.00 30.76 C -ANISOU 5382 CG LEU D 67 3385 4063 4239 396 -442 -158 C -ATOM 5383 CD1 LEU D 67 -16.807 -6.704 -9.329 1.00 37.05 C -ANISOU 5383 CD1 LEU D 67 4141 5036 4900 486 -496 -172 C -ATOM 5384 CD2 LEU D 67 -16.057 -5.655 -7.171 1.00 31.46 C -ANISOU 5384 CD2 LEU D 67 3607 4034 4312 344 -366 -25 C -ATOM 5385 N LYS D 68 -20.335 -4.427 -5.802 1.00 25.84 N -ANISOU 5385 N LYS D 68 2763 3312 3741 560 -406 -108 N -ATOM 5386 CA LYS D 68 -19.178 -3.531 -5.706 1.00 27.27 C -ANISOU 5386 CA LYS D 68 3101 3377 3885 536 -355 23 C -ATOM 5387 C LYS D 68 -18.803 -3.314 -4.250 1.00 27.90 C -ANISOU 5387 C LYS D 68 3238 3310 4052 431 -284 39 C -ATOM 5388 O LYS D 68 -17.647 -3.082 -3.938 1.00 27.36 O -ANISOU 5388 O LYS D 68 3257 3158 3979 347 -237 98 O -ATOM 5389 CB LYS D 68 -19.486 -2.154 -6.308 1.00 24.17 C -ANISOU 5389 CB LYS D 68 2805 2968 3410 681 -367 131 C -ATOM 5390 CG LYS D 68 -19.882 -2.120 -7.768 1.00 26.56 C -ANISOU 5390 CG LYS D 68 3068 3431 3591 819 -438 144 C -ATOM 5391 CD LYS D 68 -20.290 -0.680 -8.108 1.00 30.06 C -ANISOU 5391 CD LYS D 68 3636 3819 3969 978 -445 271 C -ATOM 5392 CE LYS D 68 -20.774 -0.522 -9.525 1.00 33.59 C -ANISOU 5392 CE LYS D 68 4052 4438 4272 1147 -520 305 C -ATOM 5393 NZ LYS D 68 -21.028 0.916 -9.761 1.00 34.56 N -ANISOU 5393 NZ LYS D 68 4335 4461 4337 1300 -520 458 N -ATOM 5394 N GLY D 69 -19.795 -3.382 -3.364 1.00 26.41 N -ANISOU 5394 N GLY D 69 2984 3117 3932 438 -276 -23 N -ATOM 5395 CA GLY D 69 -19.610 -2.983 -1.981 1.00 26.77 C -ANISOU 5395 CA GLY D 69 3079 3053 4039 370 -212 -11 C -ATOM 5396 C GLY D 69 -18.592 -3.818 -1.228 1.00 23.69 C -ANISOU 5396 C GLY D 69 2699 2613 3689 221 -170 -15 C -ATOM 5397 O GLY D 69 -18.011 -3.359 -0.228 1.00 25.11 O -ANISOU 5397 O GLY D 69 2944 2707 3888 162 -115 13 O -ATOM 5398 N GLY D 70 -18.380 -5.050 -1.688 1.00 21.45 N -ANISOU 5398 N GLY D 70 2350 2387 3414 170 -200 -61 N -ATOM 5399 CA GLY D 70 -17.409 -5.925 -1.051 1.00 21.26 C -ANISOU 5399 CA GLY D 70 2341 2316 3421 58 -174 -63 C -ATOM 5400 C GLY D 70 -15.948 -5.585 -1.300 1.00 24.46 C -ANISOU 5400 C GLY D 70 2832 2691 3771 30 -156 -7 C -ATOM 5401 O GLY D 70 -15.078 -6.149 -0.640 1.00 24.67 O -ANISOU 5401 O GLY D 70 2874 2689 3813 -43 -134 -9 O -ATOM 5402 N TYR D 71 -15.666 -4.664 -2.222 1.00 24.47 N -ANISOU 5402 N TYR D 71 2887 2709 3701 86 -163 47 N -ATOM 5403 CA TYR D 71 -14.303 -4.546 -2.757 1.00 25.04 C -ANISOU 5403 CA TYR D 71 3009 2801 3706 45 -150 87 C -ATOM 5404 C TYR D 71 -13.246 -4.106 -1.745 1.00 23.50 C -ANISOU 5404 C TYR D 71 2875 2535 3517 -48 -88 114 C -ATOM 5405 O TYR D 71 -12.116 -4.589 -1.777 1.00 22.55 O -ANISOU 5405 O TYR D 71 2746 2458 3365 -103 -81 100 O -ATOM 5406 CB TYR D 71 -14.256 -3.677 -4.038 1.00 24.98 C -ANISOU 5406 CB TYR D 71 3048 2837 3604 113 -163 158 C -ATOM 5407 CG TYR D 71 -13.756 -2.254 -3.845 1.00 28.06 C -ANISOU 5407 CG TYR D 71 3563 3129 3969 86 -103 257 C -ATOM 5408 CD1 TYR D 71 -12.391 -1.961 -3.856 1.00 26.18 C -ANISOU 5408 CD1 TYR D 71 3374 2888 3686 -17 -54 294 C -ATOM 5409 CD2 TYR D 71 -14.649 -1.200 -3.680 1.00 27.90 C -ANISOU 5409 CD2 TYR D 71 3610 3021 3972 163 -98 303 C -ATOM 5410 CE1 TYR D 71 -11.934 -0.667 -3.674 1.00 29.87 C -ANISOU 5410 CE1 TYR D 71 3957 3248 4143 -70 7 375 C -ATOM 5411 CE2 TYR D 71 -14.197 0.108 -3.503 1.00 29.51 C -ANISOU 5411 CE2 TYR D 71 3946 3096 4169 135 -45 388 C -ATOM 5412 CZ TYR D 71 -12.839 0.360 -3.503 1.00 31.44 C -ANISOU 5412 CZ TYR D 71 4241 3324 4379 4 11 425 C -ATOM 5413 OH TYR D 71 -12.378 1.644 -3.348 1.00 31.95 O -ANISOU 5413 OH TYR D 71 4441 3251 4449 -52 70 501 O -ATOM 5414 N LYS D 72 -13.592 -3.186 -0.859 1.00 20.37 N -ANISOU 5414 N LYS D 72 2533 2050 3159 -57 -46 136 N -ATOM 5415 CA LYS D 72 -12.610 -2.690 0.103 1.00 24.33 C -ANISOU 5415 CA LYS D 72 3082 2499 3661 -147 11 141 C -ATOM 5416 C LYS D 72 -12.324 -3.732 1.161 1.00 24.05 C -ANISOU 5416 C LYS D 72 2988 2492 3656 -193 13 88 C -ATOM 5417 O LYS D 72 -11.169 -3.994 1.492 1.00 21.99 O -ANISOU 5417 O LYS D 72 2726 2266 3364 -253 29 74 O -ATOM 5418 CB LYS D 72 -13.077 -1.383 0.773 1.00 25.32 C -ANISOU 5418 CB LYS D 72 3283 2516 3822 -136 51 158 C -ATOM 5419 CG LYS D 72 -12.435 -0.146 0.205 1.00 39.02 C -ANISOU 5419 CG LYS D 72 5127 4177 5523 -167 85 224 C -ATOM 5420 CD LYS D 72 -10.925 -0.321 0.143 1.00 47.38 C -ANISOU 5420 CD LYS D 72 6182 5290 6530 -288 119 222 C -ATOM 5421 CE LYS D 72 -10.212 0.681 1.010 1.00 54.18 C -ANISOU 5421 CE LYS D 72 7108 6066 7413 -390 182 203 C -ATOM 5422 NZ LYS D 72 -8.780 0.299 1.159 1.00 58.24 N -ANISOU 5422 NZ LYS D 72 7574 6681 7873 -506 209 167 N -ATOM 5423 N PHE D 73 -13.378 -4.313 1.711 1.00 22.24 N -ANISOU 5423 N PHE D 73 2710 2257 3481 -163 -1 61 N -ATOM 5424 CA PHE D 73 -13.202 -5.347 2.726 1.00 23.13 C -ANISOU 5424 CA PHE D 73 2784 2385 3619 -205 5 36 C -ATOM 5425 C PHE D 73 -12.406 -6.500 2.123 1.00 25.57 C -ANISOU 5425 C PHE D 73 3069 2736 3909 -209 -36 21 C -ATOM 5426 O PHE D 73 -11.523 -7.067 2.772 1.00 23.64 O -ANISOU 5426 O PHE D 73 2827 2508 3648 -237 -31 15 O -ATOM 5427 CB PHE D 73 -14.569 -5.808 3.232 1.00 21.95 C -ANISOU 5427 CB PHE D 73 2581 2231 3527 -190 4 19 C -ATOM 5428 CG PHE D 73 -14.498 -6.851 4.314 1.00 22.72 C -ANISOU 5428 CG PHE D 73 2656 2332 3646 -241 21 21 C -ATOM 5429 CD1 PHE D 73 -13.674 -6.676 5.429 1.00 19.85 C -ANISOU 5429 CD1 PHE D 73 2320 1975 3245 -275 58 36 C -ATOM 5430 CD2 PHE D 73 -15.273 -7.998 4.230 1.00 21.59 C -ANISOU 5430 CD2 PHE D 73 2463 2184 3554 -258 0 11 C -ATOM 5431 CE1 PHE D 73 -13.632 -7.633 6.425 1.00 23.04 C -ANISOU 5431 CE1 PHE D 73 2714 2389 3653 -306 71 60 C -ATOM 5432 CE2 PHE D 73 -15.233 -8.958 5.222 1.00 23.44 C -ANISOU 5432 CE2 PHE D 73 2698 2400 3808 -310 22 38 C -ATOM 5433 CZ PHE D 73 -14.410 -8.776 6.321 1.00 22.92 C -ANISOU 5433 CZ PHE D 73 2669 2346 3691 -324 56 73 C -ATOM 5434 N PHE D 74 -12.710 -6.829 0.864 1.00 22.17 N -ANISOU 5434 N PHE D 74 2614 2337 3475 -166 -82 5 N -ATOM 5435 CA PHE D 74 -12.006 -7.883 0.139 1.00 19.50 C -ANISOU 5435 CA PHE D 74 2247 2046 3116 -152 -129 -34 C -ATOM 5436 C PHE D 74 -10.516 -7.565 0.011 1.00 22.99 C -ANISOU 5436 C PHE D 74 2710 2546 3480 -173 -114 -28 C -ATOM 5437 O PHE D 74 -9.673 -8.412 0.323 1.00 23.18 O -ANISOU 5437 O PHE D 74 2719 2597 3493 -171 -132 -61 O -ATOM 5438 CB PHE D 74 -12.666 -8.101 -1.247 1.00 17.41 C -ANISOU 5438 CB PHE D 74 1939 1831 2844 -95 -181 -67 C -ATOM 5439 CG PHE D 74 -11.968 -9.128 -2.134 1.00 24.03 C -ANISOU 5439 CG PHE D 74 2740 2734 3656 -66 -236 -132 C -ATOM 5440 CD1 PHE D 74 -12.249 -10.490 -2.019 1.00 23.02 C -ANISOU 5440 CD1 PHE D 74 2580 2563 3601 -62 -279 -200 C -ATOM 5441 CD2 PHE D 74 -11.083 -8.713 -3.127 1.00 24.09 C -ANISOU 5441 CD2 PHE D 74 2745 2844 3565 -43 -243 -130 C -ATOM 5442 CE1 PHE D 74 -11.637 -11.429 -2.866 1.00 25.49 C -ANISOU 5442 CE1 PHE D 74 2861 2926 3897 -18 -338 -283 C -ATOM 5443 CE2 PHE D 74 -10.459 -9.638 -3.971 1.00 27.71 C -ANISOU 5443 CE2 PHE D 74 3154 3387 3987 -2 -296 -210 C -ATOM 5444 CZ PHE D 74 -10.742 -10.998 -3.847 1.00 24.66 C -ANISOU 5444 CZ PHE D 74 2737 2949 3682 21 -349 -296 C -ATOM 5445 N ALA D 75 -10.180 -6.360 -0.447 1.00 22.51 N -ANISOU 5445 N ALA D 75 2683 2507 3363 -194 -80 11 N -ATOM 5446 CA ALA D 75 -8.770 -6.031 -0.684 1.00 23.42 C -ANISOU 5446 CA ALA D 75 2800 2701 3396 -240 -57 8 C -ATOM 5447 C ALA D 75 -8.007 -6.102 0.626 1.00 24.57 C -ANISOU 5447 C ALA D 75 2946 2845 3546 -288 -27 -14 C -ATOM 5448 O ALA D 75 -6.885 -6.610 0.682 1.00 20.32 O -ANISOU 5448 O ALA D 75 2368 2398 2953 -293 -38 -57 O -ATOM 5449 CB ALA D 75 -8.619 -4.650 -1.288 1.00 21.64 C -ANISOU 5449 CB ALA D 75 2631 2470 3123 -282 -10 71 C -ATOM 5450 N ASP D 76 -8.613 -5.571 1.680 1.00 21.08 N -ANISOU 5450 N ASP D 76 2538 2320 3153 -311 7 6 N -ATOM 5451 CA ASP D 76 -7.938 -5.477 2.977 1.00 21.72 C -ANISOU 5451 CA ASP D 76 2614 2420 3219 -354 38 -18 C -ATOM 5452 C ASP D 76 -7.814 -6.824 3.671 1.00 20.66 C -ANISOU 5452 C ASP D 76 2448 2309 3095 -306 0 -36 C -ATOM 5453 O ASP D 76 -6.752 -7.157 4.207 1.00 21.49 O -ANISOU 5453 O ASP D 76 2527 2493 3144 -305 -4 -68 O -ATOM 5454 CB ASP D 76 -8.667 -4.476 3.883 1.00 24.64 C -ANISOU 5454 CB ASP D 76 3025 2708 3631 -383 85 -5 C -ATOM 5455 CG ASP D 76 -8.477 -3.048 3.439 1.00 28.69 C -ANISOU 5455 CG ASP D 76 3594 3173 4134 -439 128 9 C -ATOM 5456 OD1 ASP D 76 -7.526 -2.779 2.676 1.00 31.13 O -ANISOU 5456 OD1 ASP D 76 3905 3535 4389 -488 139 12 O -ATOM 5457 OD2 ASP D 76 -9.279 -2.191 3.856 1.00 28.14 O -ANISOU 5457 OD2 ASP D 76 3570 3011 4110 -433 153 17 O -ATOM 5458 N LEU D 77 -8.902 -7.588 3.676 1.00 21.63 N -ANISOU 5458 N LEU D 77 2572 2361 3283 -266 -26 -16 N -ATOM 5459 CA LEU D 77 -8.887 -8.931 4.252 1.00 22.05 C -ANISOU 5459 CA LEU D 77 2620 2397 3360 -228 -59 -13 C -ATOM 5460 C LEU D 77 -7.838 -9.778 3.551 1.00 21.20 C -ANISOU 5460 C LEU D 77 2493 2349 3215 -175 -113 -57 C -ATOM 5461 O LEU D 77 -7.054 -10.481 4.205 1.00 22.69 O -ANISOU 5461 O LEU D 77 2681 2569 3370 -133 -134 -65 O -ATOM 5462 CB LEU D 77 -10.260 -9.608 4.125 1.00 22.36 C -ANISOU 5462 CB LEU D 77 2660 2348 3488 -223 -73 7 C -ATOM 5463 CG LEU D 77 -10.371 -11.018 4.729 1.00 25.38 C -ANISOU 5463 CG LEU D 77 3061 2671 3912 -205 -98 29 C -ATOM 5464 CD1 LEU D 77 -10.102 -11.008 6.237 1.00 25.94 C -ANISOU 5464 CD1 LEU D 77 3156 2757 3944 -218 -58 82 C -ATOM 5465 CD2 LEU D 77 -11.744 -11.625 4.440 1.00 25.00 C -ANISOU 5465 CD2 LEU D 77 3001 2541 3958 -234 -104 32 C -ATOM 5466 N LEU D 78 -7.804 -9.721 2.222 1.00 21.07 N -ANISOU 5466 N LEU D 78 2453 2364 3189 -159 -140 -90 N -ATOM 5467 CA LEU D 78 -6.783 -10.479 1.499 1.00 21.47 C -ANISOU 5467 CA LEU D 78 2468 2498 3190 -99 -192 -153 C -ATOM 5468 C LEU D 78 -5.361 -10.008 1.804 1.00 22.48 C -ANISOU 5468 C LEU D 78 2564 2761 3217 -112 -172 -183 C -ATOM 5469 O LEU D 78 -4.432 -10.831 1.880 1.00 24.30 O -ANISOU 5469 O LEU D 78 2764 3064 3406 -40 -216 -236 O -ATOM 5470 CB LEU D 78 -7.034 -10.503 -0.020 1.00 20.48 C -ANISOU 5470 CB LEU D 78 2312 2415 3055 -76 -224 -192 C -ATOM 5471 CG LEU D 78 -7.721 -11.758 -0.530 1.00 28.25 C -ANISOU 5471 CG LEU D 78 3289 3328 4116 -16 -289 -240 C -ATOM 5472 CD1 LEU D 78 -9.067 -11.911 0.163 1.00 24.85 C -ANISOU 5472 CD1 LEU D 78 2894 2761 3788 -56 -271 -191 C -ATOM 5473 CD2 LEU D 78 -7.886 -11.702 -2.050 1.00 31.23 C -ANISOU 5473 CD2 LEU D 78 3618 3791 4457 15 -323 -296 C -ATOM 5474 N ASP D 79 -5.171 -8.705 1.989 1.00 20.89 N -ANISOU 5474 N ASP D 79 2366 2594 2979 -201 -108 -159 N -ATOM 5475 CA ASP D 79 -3.834 -8.204 2.307 1.00 18.87 C -ANISOU 5475 CA ASP D 79 2063 2477 2629 -243 -81 -204 C -ATOM 5476 C ASP D 79 -3.372 -8.723 3.663 1.00 23.17 C -ANISOU 5476 C ASP D 79 2600 3048 3157 -201 -94 -221 C -ATOM 5477 O ASP D 79 -2.203 -9.039 3.851 1.00 19.72 O -ANISOU 5477 O ASP D 79 2102 2752 2638 -164 -115 -284 O -ATOM 5478 CB ASP D 79 -3.797 -6.674 2.293 1.00 24.95 C -ANISOU 5478 CB ASP D 79 2855 3242 3383 -367 -4 -179 C -ATOM 5479 CG ASP D 79 -3.603 -6.107 0.892 1.00 31.78 C -ANISOU 5479 CG ASP D 79 3714 4157 4205 -411 14 -164 C -ATOM 5480 OD1 ASP D 79 -3.402 -6.905 -0.050 1.00 32.71 O -ANISOU 5480 OD1 ASP D 79 3789 4351 4290 -343 -34 -194 O -ATOM 5481 OD2 ASP D 79 -3.636 -4.862 0.742 1.00 29.00 O -ANISOU 5481 OD2 ASP D 79 3405 3767 3849 -513 77 -124 O -ATOM 5482 N TYR D 80 -4.288 -8.803 4.621 1.00 21.37 N -ANISOU 5482 N TYR D 80 2423 2706 2991 -199 -81 -164 N -ATOM 5483 CA TYR D 80 -3.923 -9.353 5.922 1.00 20.85 C -ANISOU 5483 CA TYR D 80 2357 2673 2892 -148 -93 -160 C -ATOM 5484 C TYR D 80 -3.627 -10.847 5.809 1.00 21.72 C -ANISOU 5484 C TYR D 80 2477 2771 3005 -21 -168 -161 C -ATOM 5485 O TYR D 80 -2.703 -11.362 6.447 1.00 21.96 O -ANISOU 5485 O TYR D 80 2484 2898 2962 59 -201 -187 O -ATOM 5486 CB TYR D 80 -5.030 -9.099 6.953 1.00 20.81 C -ANISOU 5486 CB TYR D 80 2401 2567 2940 -181 -54 -93 C -ATOM 5487 CG TYR D 80 -4.985 -7.722 7.572 1.00 22.03 C -ANISOU 5487 CG TYR D 80 2543 2760 3069 -272 11 -119 C -ATOM 5488 CD1 TYR D 80 -3.936 -7.358 8.410 1.00 23.60 C -ANISOU 5488 CD1 TYR D 80 2693 3098 3178 -286 23 -180 C -ATOM 5489 CD2 TYR D 80 -5.983 -6.778 7.315 1.00 24.51 C -ANISOU 5489 CD2 TYR D 80 2890 2974 3449 -337 54 -98 C -ATOM 5490 CE1 TYR D 80 -3.877 -6.092 8.988 1.00 28.03 C -ANISOU 5490 CE1 TYR D 80 3241 3683 3725 -379 81 -228 C -ATOM 5491 CE2 TYR D 80 -5.934 -5.507 7.898 1.00 23.76 C -ANISOU 5491 CE2 TYR D 80 2797 2888 3342 -412 108 -136 C -ATOM 5492 CZ TYR D 80 -4.876 -5.177 8.729 1.00 26.33 C -ANISOU 5492 CZ TYR D 80 3077 3339 3589 -441 123 -206 C -ATOM 5493 OH TYR D 80 -4.814 -3.929 9.317 1.00 26.92 O -ANISOU 5493 OH TYR D 80 3153 3414 3663 -524 176 -266 O -ATOM 5494 N ILE D 81 -4.402 -11.553 4.999 1.00 20.69 N -ANISOU 5494 N ILE D 81 2382 2523 2958 7 -201 -143 N -ATOM 5495 CA ILE D 81 -4.125 -12.983 4.762 1.00 22.17 C -ANISOU 5495 CA ILE D 81 2591 2665 3167 127 -278 -162 C -ATOM 5496 C ILE D 81 -2.769 -13.180 4.070 1.00 21.27 C -ANISOU 5496 C ILE D 81 2404 2715 2962 206 -325 -265 C -ATOM 5497 O ILE D 81 -1.988 -14.055 4.460 1.00 25.44 O -ANISOU 5497 O ILE D 81 2933 3283 3449 329 -381 -293 O -ATOM 5498 CB ILE D 81 -5.258 -13.646 3.942 1.00 27.76 C -ANISOU 5498 CB ILE D 81 3338 3217 3990 121 -303 -152 C -ATOM 5499 CG1 ILE D 81 -6.503 -13.822 4.813 1.00 28.68 C -ANISOU 5499 CG1 ILE D 81 3519 3188 4191 62 -265 -56 C -ATOM 5500 CG2 ILE D 81 -4.813 -14.998 3.383 1.00 27.65 C -ANISOU 5500 CG2 ILE D 81 3341 3161 4004 243 -387 -212 C -ATOM 5501 CD1 ILE D 81 -7.772 -14.101 4.008 1.00 31.99 C -ANISOU 5501 CD1 ILE D 81 3946 3492 4719 14 -270 -62 C -ATOM 5502 N LYS D 82 -2.466 -12.364 3.056 1.00 22.80 N -ANISOU 5502 N LYS D 82 2533 3016 3113 141 -300 -319 N -ATOM 5503 CA LYS D 82 -1.141 -12.427 2.410 1.00 24.62 C -ANISOU 5503 CA LYS D 82 2670 3447 3237 193 -328 -423 C -ATOM 5504 C LYS D 82 0.002 -12.171 3.392 1.00 24.59 C -ANISOU 5504 C LYS D 82 2609 3605 3130 211 -320 -460 C -ATOM 5505 O LYS D 82 1.055 -12.823 3.341 1.00 26.43 O -ANISOU 5505 O LYS D 82 2778 3980 3284 330 -377 -545 O -ATOM 5506 CB LYS D 82 -1.057 -11.441 1.243 1.00 26.32 C -ANISOU 5506 CB LYS D 82 2832 3759 3411 88 -282 -446 C -ATOM 5507 CG LYS D 82 -1.746 -11.968 -0.023 1.00 31.15 C -ANISOU 5507 CG LYS D 82 3453 4310 4072 128 -321 -464 C -ATOM 5508 CD LYS D 82 -2.476 -10.862 -0.771 1.00 35.22 C -ANISOU 5508 CD LYS D 82 3984 4804 4595 12 -261 -404 C -ATOM 5509 CE LYS D 82 -1.525 -9.769 -1.194 1.00 36.77 C -ANISOU 5509 CE LYS D 82 4119 5176 4677 -86 -199 -415 C -ATOM 5510 NZ LYS D 82 -2.260 -8.673 -1.894 1.00 38.77 N -ANISOU 5510 NZ LYS D 82 4415 5377 4937 -186 -141 -332 N -ATOM 5511 N ALA D 83 -0.207 -11.219 4.296 1.00 20.74 N -ANISOU 5511 N ALA D 83 2135 3109 2636 105 -254 -412 N -ATOM 5512 CA ALA D 83 0.804 -10.917 5.301 1.00 23.17 C -ANISOU 5512 CA ALA D 83 2378 3583 2843 112 -245 -461 C -ATOM 5513 C ALA D 83 1.081 -12.147 6.180 1.00 28.87 C -ANISOU 5513 C ALA D 83 3129 4299 3541 290 -320 -446 C -ATOM 5514 O ALA D 83 2.237 -12.435 6.522 1.00 28.51 O -ANISOU 5514 O ALA D 83 3003 4444 3386 387 -361 -526 O -ATOM 5515 CB ALA D 83 0.381 -9.719 6.146 1.00 26.31 C -ANISOU 5515 CB ALA D 83 2794 3949 3253 -29 -165 -423 C -ATOM 5516 N LEU D 84 0.024 -12.867 6.548 1.00 25.21 N -ANISOU 5516 N LEU D 84 2780 3623 3175 334 -337 -341 N -ATOM 5517 CA LEU D 84 0.195 -14.097 7.326 1.00 26.22 C -ANISOU 5517 CA LEU D 84 2970 3701 3292 501 -405 -296 C -ATOM 5518 C LEU D 84 0.973 -15.121 6.505 1.00 29.72 C -ANISOU 5518 C LEU D 84 3390 4187 3716 661 -495 -381 C -ATOM 5519 O LEU D 84 1.880 -15.805 7.009 1.00 31.14 O -ANISOU 5519 O LEU D 84 3553 4466 3812 828 -561 -414 O -ATOM 5520 CB LEU D 84 -1.174 -14.676 7.716 1.00 26.80 C -ANISOU 5520 CB LEU D 84 3174 3520 3487 480 -392 -162 C -ATOM 5521 CG LEU D 84 -1.979 -13.900 8.752 1.00 28.61 C -ANISOU 5521 CG LEU D 84 3430 3718 3723 364 -314 -75 C -ATOM 5522 CD1 LEU D 84 -3.326 -14.539 8.978 1.00 28.11 C -ANISOU 5522 CD1 LEU D 84 3474 3430 3776 332 -297 44 C -ATOM 5523 CD2 LEU D 84 -1.217 -13.875 10.046 1.00 27.53 C -ANISOU 5523 CD2 LEU D 84 3269 3730 3460 438 -320 -63 C -ATOM 5524 N ASN D 85 0.628 -15.219 5.228 1.00 28.34 N -ANISOU 5524 N ASN D 85 3207 3951 3608 627 -503 -427 N -ATOM 5525 CA ASN D 85 1.197 -16.257 4.372 1.00 28.75 C -ANISOU 5525 CA ASN D 85 3243 4021 3658 784 -592 -522 C -ATOM 5526 C ASN D 85 2.661 -16.064 4.002 1.00 34.25 C -ANISOU 5526 C ASN D 85 3793 5012 4209 861 -621 -666 C -ATOM 5527 O ASN D 85 3.335 -17.024 3.623 1.00 39.83 O -ANISOU 5527 O ASN D 85 4477 5768 4886 1044 -709 -757 O -ATOM 5528 CB ASN D 85 0.365 -16.397 3.089 1.00 29.97 C -ANISOU 5528 CB ASN D 85 3416 4055 3915 725 -592 -547 C -ATOM 5529 CG ASN D 85 -0.732 -17.443 3.203 1.00 43.89 C -ANISOU 5529 CG ASN D 85 5316 5532 5828 759 -626 -474 C -ATOM 5530 OD1 ASN D 85 -0.533 -18.609 2.867 1.00 52.33 O -ANISOU 5530 OD1 ASN D 85 6430 6512 6942 902 -709 -530 O -ATOM 5531 ND2 ASN D 85 -1.902 -17.027 3.658 1.00 45.79 N -ANISOU 5531 ND2 ASN D 85 5620 5628 6149 622 -561 -361 N -ATOM 5532 N ARG D 86 3.156 -14.831 4.060 1.00 30.35 N -ANISOU 5532 N ARG D 86 3201 4183 4147 102 -70 -31 N -ATOM 5533 CA ARG D 86 4.558 -14.601 3.724 1.00 31.74 C -ANISOU 5533 CA ARG D 86 3200 4523 4337 181 -81 -222 C -ATOM 5534 C ARG D 86 5.406 -14.481 4.981 1.00 33.93 C -ANISOU 5534 C ARG D 86 3440 4894 4557 154 -207 -90 C -ATOM 5535 O ARG D 86 6.599 -14.194 4.914 1.00 35.90 O -ANISOU 5535 O ARG D 86 3522 5334 4784 191 -222 -228 O -ATOM 5536 CB ARG D 86 4.735 -13.377 2.812 1.00 31.92 C -ANISOU 5536 CB ARG D 86 3208 4759 4161 59 133 -386 C -ATOM 5537 CG ARG D 86 4.333 -12.059 3.451 1.00 32.58 C -ANISOU 5537 CG ARG D 86 3453 4915 4011 -121 237 -262 C -ATOM 5538 CD ARG D 86 4.654 -10.858 2.565 1.00 30.91 C -ANISOU 5538 CD ARG D 86 3270 4853 3621 -277 355 -383 C -ATOM 5539 NE ARG D 86 4.185 -9.641 3.209 1.00 31.24 N -ANISOU 5539 NE ARG D 86 3496 4868 3505 -405 395 -289 N -ATOM 5540 CZ ARG D 86 3.017 -9.067 2.952 1.00 31.82 C -ANISOU 5540 CZ ARG D 86 3723 4798 3570 -423 431 -259 C -ATOM 5541 NH1 ARG D 86 2.221 -9.589 2.030 1.00 28.63 N -ANISOU 5541 NH1 ARG D 86 3316 4292 3271 -362 443 -277 N -ATOM 5542 NH2 ARG D 86 2.656 -7.972 3.613 1.00 27.98 N -ANISOU 5542 NH2 ARG D 86 3377 4271 2982 -489 436 -241 N -ATOM 5543 N ASN D 87 4.791 -14.716 6.134 1.00 31.18 N -ANISOU 5543 N ASN D 87 3231 4460 4158 52 -303 176 N -ATOM 5544 CA ASN D 87 5.536 -14.654 7.384 1.00 37.60 C -ANISOU 5544 CA ASN D 87 4024 5377 4887 -21 -448 336 C -ATOM 5545 C ASN D 87 5.401 -15.923 8.221 1.00 39.65 C -ANISOU 5545 C ASN D 87 4345 5423 5299 -18 -770 599 C -ATOM 5546 O ASN D 87 5.863 -15.978 9.351 1.00 41.51 O -ANISOU 5546 O ASN D 87 4596 5733 5443 -131 -938 800 O -ATOM 5547 CB ASN D 87 5.151 -13.403 8.173 1.00 35.80 C -ANISOU 5547 CB ASN D 87 3905 5356 4341 -250 -263 401 C -ATOM 5548 CG ASN D 87 5.721 -12.133 7.550 1.00 36.62 C -ANISOU 5548 CG ASN D 87 3968 5635 4310 -280 -70 187 C -ATOM 5549 OD1 ASN D 87 6.938 -11.948 7.517 1.00 36.66 O -ANISOU 5549 OD1 ASN D 87 3836 5789 4303 -262 -119 104 O -ATOM 5550 ND2 ASN D 87 4.847 -11.263 7.044 1.00 32.10 N -ANISOU 5550 ND2 ASN D 87 3512 5045 3640 -344 115 105 N -ATOM 5551 N SER D 88 4.780 -16.945 7.637 1.00 41.42 N -ANISOU 5551 N SER D 88 4621 5371 5747 81 -887 610 N -ATOM 5552 CA SER D 88 4.671 -18.253 8.279 1.00 45.64 C -ANISOU 5552 CA SER D 88 5254 5616 6470 69 -1269 873 C -ATOM 5553 C SER D 88 5.500 -19.308 7.541 1.00 46.45 C -ANISOU 5553 C SER D 88 5228 5432 6990 412 -1550 681 C -ATOM 5554 O SER D 88 5.862 -19.125 6.375 1.00 44.23 O -ANISOU 5554 O SER D 88 4776 5209 6818 622 -1380 316 O -ATOM 5555 CB SER D 88 3.213 -18.694 8.344 1.00 48.32 C -ANISOU 5555 CB SER D 88 5787 5837 6736 -140 -1245 1063 C -ATOM 5556 OG SER D 88 2.706 -18.940 7.045 1.00 55.38 O -ANISOU 5556 OG SER D 88 6660 6588 7793 15 -1121 834 O -ATOM 5557 N ASP D 89 5.787 -20.409 8.231 1.00 43.69 N -ANISOU 5557 N ASP D 89 4955 4778 6866 450 -2003 914 N -ATOM 5558 CA ASP D 89 6.631 -21.483 7.700 1.00 54.49 C -ANISOU 5558 CA ASP D 89 6192 5814 8698 828 -2364 707 C -ATOM 5559 C ASP D 89 6.064 -22.117 6.431 1.00 60.49 C -ANISOU 5559 C ASP D 89 6959 6331 9694 1003 -2308 429 C -ATOM 5560 O ASP D 89 6.791 -22.355 5.461 1.00 63.81 O -ANISOU 5560 O ASP D 89 7137 6741 10368 1338 -2300 -9 O -ATOM 5561 CB ASP D 89 6.832 -22.570 8.759 1.00 55.60 C -ANISOU 5561 CB ASP D 89 6499 5578 9047 788 -2948 1092 C -ATOM 5562 CG ASP D 89 7.609 -22.073 9.964 1.00 62.50 C -ANISOU 5562 CG ASP D 89 7325 6693 9730 650 -3074 1335 C -ATOM 5563 OD1 ASP D 89 8.220 -20.985 9.868 1.00 56.57 O -ANISOU 5563 OD1 ASP D 89 6365 6361 8769 677 -2740 1122 O -ATOM 5564 OD2 ASP D 89 7.612 -22.772 11.002 1.00 69.34 O -ANISOU 5564 OD2 ASP D 89 8389 7353 10607 455 -3455 1715 O -ATOM 5565 N ARG D 90 4.769 -22.408 6.452 1.00 57.51 N -ANISOU 5565 N ARG D 90 6837 5804 9212 752 -2271 660 N -ATOM 5566 CA ARG D 90 4.112 -22.997 5.295 1.00 59.88 C -ANISOU 5566 CA ARG D 90 7173 5884 9695 858 -2216 432 C -ATOM 5567 C ARG D 90 2.884 -22.169 4.938 1.00 56.45 C -ANISOU 5567 C ARG D 90 6823 5718 8906 580 -1782 483 C -ATOM 5568 O ARG D 90 2.293 -21.510 5.796 1.00 61.18 O -ANISOU 5568 O ARG D 90 7523 6542 9179 281 -1642 768 O -ATOM 5569 CB ARG D 90 3.748 -24.462 5.556 1.00 66.96 C -ANISOU 5569 CB ARG D 90 8303 6222 10916 858 -2726 648 C -ATOM 5570 CG ARG D 90 4.911 -25.297 6.098 1.00 77.46 C -ANISOU 5570 CG ARG D 90 9587 7304 12539 1067 -3161 622 C -ATOM 5571 CD ARG D 90 5.274 -26.457 5.175 1.00 86.08 C -ANISOU 5571 CD ARG D 90 10630 8086 13991 1341 -3334 213 C -ATOM 5572 NE ARG D 90 5.806 -26.008 3.890 1.00 85.92 N -ANISOU 5572 NE ARG D 90 10292 8318 14033 1648 -3005 -355 N -ATOM 5573 CZ ARG D 90 5.968 -26.796 2.828 1.00 87.87 C -ANISOU 5573 CZ ARG D 90 10453 8434 14499 1847 -3031 -783 C -ATOM 5574 NH1 ARG D 90 5.635 -28.078 2.889 1.00 87.51 N -ANISOU 5574 NH1 ARG D 90 10615 7953 14683 1821 -3402 -712 N -ATOM 5575 NH2 ARG D 90 6.456 -26.297 1.700 1.00 88.89 N -ANISOU 5575 NH2 ARG D 90 10283 8909 14581 2025 -2693 -1280 N -ATOM 5576 N SER D 91 2.515 -22.190 3.665 1.00 48.42 N -ANISOU 5576 N SER D 91 5743 4701 7955 686 -1579 175 N -ATOM 5577 CA SER D 91 1.455 -21.329 3.165 1.00 41.06 C -ANISOU 5577 CA SER D 91 4848 4027 6727 482 -1193 174 C -ATOM 5578 C SER D 91 0.696 -22.067 2.071 1.00 42.71 C -ANISOU 5578 C SER D 91 5115 4026 7088 511 -1198 19 C -ATOM 5579 O SER D 91 1.159 -23.104 1.593 1.00 43.99 O -ANISOU 5579 O SER D 91 5253 3879 7580 727 -1452 -177 O -ATOM 5580 CB SER D 91 2.065 -20.055 2.591 1.00 36.60 C -ANISOU 5580 CB SER D 91 4089 3842 5975 546 -856 -88 C -ATOM 5581 OG SER D 91 2.927 -20.366 1.517 1.00 46.05 O -ANISOU 5581 OG SER D 91 5085 5044 7367 792 -856 -490 O -ATOM 5582 N ILE D 92 -0.457 -21.530 1.670 1.00 35.41 N -ANISOU 5582 N ILE D 92 4250 3267 5938 311 -938 77 N -ATOM 5583 CA ILE D 92 -1.248 -22.132 0.590 1.00 34.46 C -ANISOU 5583 CA ILE D 92 4178 3003 5914 296 -917 -63 C -ATOM 5584 C ILE D 92 -1.545 -21.127 -0.518 1.00 28.93 C -ANISOU 5584 C ILE D 92 3361 2610 5021 279 -566 -286 C -ATOM 5585 O ILE D 92 -1.692 -19.936 -0.259 1.00 27.75 O -ANISOU 5585 O ILE D 92 3177 2741 4626 187 -351 -209 O -ATOM 5586 CB ILE D 92 -2.588 -22.735 1.093 1.00 54.22 C -ANISOU 5586 CB ILE D 92 6887 5367 8348 10 -1030 270 C -ATOM 5587 CG1 ILE D 92 -3.120 -21.943 2.286 1.00 55.10 C -ANISOU 5587 CG1 ILE D 92 7028 5759 8148 -237 -914 580 C -ATOM 5588 CG2 ILE D 92 -2.432 -24.216 1.438 1.00 58.19 C -ANISOU 5588 CG2 ILE D 92 7562 5396 9151 21 -1475 394 C -ATOM 5589 CD1 ILE D 92 -3.874 -20.697 1.908 1.00 53.85 C -ANISOU 5589 CD1 ILE D 92 6769 5962 7728 -307 -551 501 C -ATOM 5590 N PRO D 93 -1.629 -21.607 -1.767 1.00 34.49 N -ANISOU 5590 N PRO D 93 4018 3249 5838 351 -540 -569 N -ATOM 5591 CA PRO D 93 -1.971 -20.644 -2.816 1.00 34.29 C -ANISOU 5591 CA PRO D 93 3910 3525 5593 264 -251 -718 C -ATOM 5592 C PRO D 93 -3.400 -20.130 -2.668 1.00 28.17 C -ANISOU 5592 C PRO D 93 3245 2832 4624 45 -142 -455 C -ATOM 5593 O PRO D 93 -4.272 -20.822 -2.133 1.00 28.06 O -ANISOU 5593 O PRO D 93 3351 2657 4653 -69 -267 -242 O -ATOM 5594 CB PRO D 93 -1.810 -21.451 -4.113 1.00 40.62 C -ANISOU 5594 CB PRO D 93 4641 4249 6544 346 -277 -1077 C -ATOM 5595 CG PRO D 93 -1.806 -22.898 -3.686 1.00 44.46 C -ANISOU 5595 CG PRO D 93 5234 4303 7356 461 -600 -1062 C -ATOM 5596 CD PRO D 93 -1.208 -22.909 -2.310 1.00 41.41 C -ANISOU 5596 CD PRO D 93 4886 3806 7041 533 -778 -820 C -ATOM 5597 N MET D 94 -3.619 -18.904 -3.121 1.00 24.96 N -ANISOU 5597 N MET D 94 2791 2689 4006 -25 61 -475 N -ATOM 5598 CA MET D 94 -4.943 -18.312 -3.131 1.00 24.76 C -ANISOU 5598 CA MET D 94 2814 2761 3832 -171 148 -305 C -ATOM 5599 C MET D 94 -5.169 -17.708 -4.507 1.00 29.52 C -ANISOU 5599 C MET D 94 3379 3507 4331 -231 255 -452 C -ATOM 5600 O MET D 94 -4.288 -17.039 -5.046 1.00 25.66 O -ANISOU 5600 O MET D 94 2834 3158 3757 -222 324 -595 O -ATOM 5601 CB MET D 94 -5.045 -17.215 -2.064 1.00 26.15 C -ANISOU 5601 CB MET D 94 2989 3081 3865 -186 219 -146 C -ATOM 5602 CG MET D 94 -6.405 -16.496 -2.037 1.00 30.55 C -ANISOU 5602 CG MET D 94 3539 3767 4303 -274 295 -48 C -ATOM 5603 SD MET D 94 -6.622 -15.514 -0.540 1.00 42.31 S -ANISOU 5603 SD MET D 94 5000 5416 5662 -274 355 61 S -ATOM 5604 CE MET D 94 -4.992 -14.769 -0.372 1.00 45.58 C -ANISOU 5604 CE MET D 94 5434 5830 6054 -177 371 -26 C -ATOM 5605 N THR D 95 -6.330 -17.968 -5.092 1.00 26.31 N -ANISOU 5605 N THR D 95 3000 3092 3906 -338 250 -404 N -ATOM 5606 CA THR D 95 -6.681 -17.322 -6.349 1.00 26.25 C -ANISOU 5606 CA THR D 95 2972 3230 3772 -439 311 -482 C -ATOM 5607 C THR D 95 -7.876 -16.430 -6.066 1.00 27.39 C -ANISOU 5607 C THR D 95 3123 3451 3833 -481 315 -292 C -ATOM 5608 O THR D 95 -8.515 -16.552 -5.010 1.00 24.48 O -ANISOU 5608 O THR D 95 2741 3066 3494 -455 304 -158 O -ATOM 5609 CB THR D 95 -7.014 -18.326 -7.463 1.00 28.82 C -ANISOU 5609 CB THR D 95 3297 3512 4144 -527 280 -634 C -ATOM 5610 OG1 THR D 95 -7.942 -19.297 -6.968 1.00 32.36 O -ANISOU 5610 OG1 THR D 95 3798 3794 4703 -561 192 -510 O -ATOM 5611 CG2 THR D 95 -5.734 -19.033 -7.963 1.00 31.98 C -ANISOU 5611 CG2 THR D 95 3633 3889 4629 -448 282 -945 C -ATOM 5612 N VAL D 96 -8.185 -15.527 -6.993 1.00 28.25 N -ANISOU 5612 N VAL D 96 3238 3664 3832 -559 308 -291 N -ATOM 5613 CA VAL D 96 -9.289 -14.597 -6.749 1.00 28.36 C -ANISOU 5613 CA VAL D 96 3234 3720 3824 -534 259 -157 C -ATOM 5614 C VAL D 96 -10.271 -14.543 -7.916 1.00 30.72 C -ANISOU 5614 C VAL D 96 3519 4073 4080 -653 180 -126 C -ATOM 5615 O VAL D 96 -9.909 -14.810 -9.061 1.00 30.70 O -ANISOU 5615 O VAL D 96 3553 4113 3998 -801 171 -201 O -ATOM 5616 CB VAL D 96 -8.791 -13.166 -6.423 1.00 32.88 C -ANISOU 5616 CB VAL D 96 3854 4294 4344 -466 229 -127 C -ATOM 5617 CG1 VAL D 96 -7.803 -13.187 -5.287 1.00 33.61 C -ANISOU 5617 CG1 VAL D 96 3953 4365 4453 -375 304 -156 C -ATOM 5618 CG2 VAL D 96 -8.162 -12.523 -7.640 1.00 36.44 C -ANISOU 5618 CG2 VAL D 96 4390 4786 4668 -624 167 -145 C -ATOM 5619 N ASP D 97 -11.524 -14.217 -7.607 1.00 26.05 N -ANISOU 5619 N ASP D 97 2845 3524 3530 -599 122 -42 N -ATOM 5620 CA ASP D 97 -12.507 -13.932 -8.638 1.00 27.97 C -ANISOU 5620 CA ASP D 97 3055 3825 3745 -684 -1 12 C -ATOM 5621 C ASP D 97 -13.465 -12.867 -8.108 1.00 27.35 C -ANISOU 5621 C ASP D 97 2872 3774 3747 -510 -110 55 C -ATOM 5622 O ASP D 97 -13.476 -12.554 -6.905 1.00 30.51 O -ANISOU 5622 O ASP D 97 3201 4191 4201 -351 -45 9 O -ATOM 5623 CB ASP D 97 -13.259 -15.194 -9.068 1.00 31.91 C -ANISOU 5623 CB ASP D 97 3498 4383 4244 -825 24 2 C -ATOM 5624 CG ASP D 97 -13.837 -15.082 -10.483 1.00 41.10 C -ANISOU 5624 CG ASP D 97 4671 5618 5326 -993 -96 36 C -ATOM 5625 OD1 ASP D 97 -13.579 -14.056 -11.175 1.00 34.19 O -ANISOU 5625 OD1 ASP D 97 3867 4740 4383 -1030 -218 91 O -ATOM 5626 OD2 ASP D 97 -14.546 -16.023 -10.902 1.00 44.77 O -ANISOU 5626 OD2 ASP D 97 5090 6141 5778 -1128 -93 26 O -ATOM 5627 N PHE D 98 -14.239 -12.303 -9.021 1.00 25.49 N -ANISOU 5627 N PHE D 98 2616 3550 3519 -540 -296 119 N -ATOM 5628 CA PHE D 98 -15.162 -11.223 -8.711 1.00 29.60 C -ANISOU 5628 CA PHE D 98 3020 4059 4169 -326 -474 115 C -ATOM 5629 C PHE D 98 -16.503 -11.521 -9.338 1.00 37.22 C -ANISOU 5629 C PHE D 98 3815 5161 5165 -362 -589 148 C -ATOM 5630 O PHE D 98 -16.593 -11.829 -10.530 1.00 38.63 O -ANISOU 5630 O PHE D 98 4074 5349 5254 -575 -683 248 O -ATOM 5631 CB PHE D 98 -14.629 -9.907 -9.271 1.00 26.67 C -ANISOU 5631 CB PHE D 98 2837 3483 3815 -308 -714 197 C -ATOM 5632 CG PHE D 98 -13.274 -9.555 -8.769 1.00 27.35 C -ANISOU 5632 CG PHE D 98 3089 3464 3840 -324 -615 174 C -ATOM 5633 CD1 PHE D 98 -12.134 -10.090 -9.368 1.00 24.13 C -ANISOU 5633 CD1 PHE D 98 2818 3094 3255 -572 -499 200 C -ATOM 5634 CD2 PHE D 98 -13.125 -8.686 -7.689 1.00 26.21 C -ANISOU 5634 CD2 PHE D 98 2935 3217 3806 -91 -637 85 C -ATOM 5635 CE1 PHE D 98 -10.880 -9.779 -8.899 1.00 23.16 C -ANISOU 5635 CE1 PHE D 98 2804 2926 3068 -591 -410 165 C -ATOM 5636 CE2 PHE D 98 -11.876 -8.376 -7.211 1.00 26.08 C -ANISOU 5636 CE2 PHE D 98 3066 3126 3718 -131 -550 71 C -ATOM 5637 CZ PHE D 98 -10.745 -8.920 -7.812 1.00 25.31 C -ANISOU 5637 CZ PHE D 98 3090 3083 3443 -383 -439 124 C -ATOM 5638 N ILE D 99 -17.554 -11.430 -8.540 1.00 28.85 N -ANISOU 5638 N ILE D 99 2494 4262 4207 -178 -579 43 N -ATOM 5639 CA ILE D 99 -18.893 -11.597 -9.070 1.00 36.44 C -ANISOU 5639 CA ILE D 99 3237 5402 5209 -188 -708 51 C -ATOM 5640 C ILE D 99 -19.784 -10.452 -8.624 1.00 33.66 C -ANISOU 5640 C ILE D 99 2645 5084 5059 154 -907 -92 C -ATOM 5641 O ILE D 99 -19.476 -9.734 -7.674 1.00 33.85 O -ANISOU 5641 O ILE D 99 2639 5045 5176 385 -877 -242 O -ATOM 5642 CB ILE D 99 -19.504 -12.926 -8.630 1.00 44.10 C -ANISOU 5642 CB ILE D 99 4035 6647 6073 -366 -491 19 C -ATOM 5643 CG1 ILE D 99 -19.623 -12.970 -7.109 1.00 44.05 C -ANISOU 5643 CG1 ILE D 99 3848 6825 6065 -250 -302 -129 C -ATOM 5644 CG2 ILE D 99 -18.669 -14.100 -9.157 1.00 39.89 C -ANISOU 5644 CG2 ILE D 99 3745 6011 5401 -661 -360 117 C -ATOM 5645 CD1 ILE D 99 -20.203 -14.255 -6.593 1.00 49.69 C -ANISOU 5645 CD1 ILE D 99 4427 7817 6637 -506 -128 -111 C -ATOM 5646 N ARG D 100 -20.883 -10.265 -9.330 1.00 36.14 N -ANISOU 5646 N ARG D 100 2781 5495 5458 198 -1135 -72 N -ATOM 5647 CA ARG D 100 -21.874 -9.316 -8.885 1.00 45.80 C -ANISOU 5647 CA ARG D 100 3693 6793 6915 569 -1339 -279 C -ATOM 5648 C ARG D 100 -23.196 -10.044 -8.950 1.00 47.27 C -ANISOU 5648 C ARG D 100 3502 7396 7064 505 -1290 -354 C -ATOM 5649 O ARG D 100 -23.383 -10.907 -9.805 1.00 47.52 O -ANISOU 5649 O ARG D 100 3604 7506 6946 194 -1273 -167 O -ATOM 5650 CB ARG D 100 -21.874 -8.070 -9.766 1.00 52.77 C -ANISOU 5650 CB ARG D 100 4738 7310 8002 741 -1802 -169 C -ATOM 5651 CG ARG D 100 -22.826 -6.989 -9.290 1.00 64.62 C -ANISOU 5651 CG ARG D 100 5928 8796 9830 1211 -2086 -438 C -ATOM 5652 CD ARG D 100 -22.336 -5.614 -9.687 1.00 70.05 C -ANISOU 5652 CD ARG D 100 6907 8964 10745 1408 -2530 -350 C -ATOM 5653 NE ARG D 100 -23.361 -4.606 -9.451 1.00 78.10 N -ANISOU 5653 NE ARG D 100 7733 9904 12038 1806 -2771 -588 N -ATOM 5654 CZ ARG D 100 -23.496 -3.500 -10.172 1.00 84.43 C -ANISOU 5654 CZ ARG D 100 8782 10278 13017 1902 -3206 -460 C -ATOM 5655 NH1 ARG D 100 -22.662 -3.255 -11.175 1.00 84.71 N -ANISOU 5655 NH1 ARG D 100 9246 9972 12970 1606 -3472 -76 N -ATOM 5656 NH2 ARG D 100 -24.465 -2.638 -9.893 1.00 89.73 N -ANISOU 5656 NH2 ARG D 100 9279 10882 13931 2248 -3377 -721 N -ATOM 5657 N LEU D 101 -24.087 -9.734 -8.017 1.00 44.13 N -ANISOU 5657 N LEU D 101 2685 7308 6774 769 -1248 -659 N -ATOM 5658 CA LEU D 101 -25.410 -10.335 -8.011 1.00 52.93 C -ANISOU 5658 CA LEU D 101 3371 8904 7837 700 -1206 -769 C -ATOM 5659 C LEU D 101 -26.381 -9.270 -8.470 1.00 59.29 C -ANISOU 5659 C LEU D 101 4005 9614 8907 1050 -1557 -868 C -ATOM 5660 O LEU D 101 -26.382 -8.162 -7.932 1.00 65.40 O -ANISOU 5660 O LEU D 101 4787 10188 9874 1407 -1656 -1066 O -ATOM 5661 CB LEU D 101 -25.777 -10.847 -6.616 1.00 53.76 C -ANISOU 5661 CB LEU D 101 3271 9391 7763 621 -824 -979 C -ATOM 5662 CG LEU D 101 -24.991 -12.028 -6.040 1.00 55.75 C -ANISOU 5662 CG LEU D 101 3687 9758 7738 229 -499 -845 C -ATOM 5663 CD1 LEU D 101 -24.249 -12.785 -7.107 1.00 55.95 C -ANISOU 5663 CD1 LEU D 101 4097 9483 7678 -69 -539 -514 C -ATOM 5664 CD2 LEU D 101 -24.010 -11.558 -5.018 1.00 54.34 C -ANISOU 5664 CD2 LEU D 101 3630 9453 7565 365 -359 -960 C -ATOM 5665 N LYS D 102 -27.192 -9.591 -9.472 1.00 55.26 N -ANISOU 5665 N LYS D 102 3391 9214 8393 922 -1747 -716 N -ATOM 5666 CA LYS D 102 -28.083 -8.603 -10.061 1.00 60.79 C -ANISOU 5666 CA LYS D 102 3986 9779 9334 1220 -2117 -735 C -ATOM 5667 C LYS D 102 -29.533 -8.889 -9.714 1.00 68.07 C -ANISOU 5667 C LYS D 102 4488 11137 10238 1255 -2001 -928 C -ATOM 5668 O LYS D 102 -29.999 -10.025 -9.809 1.00 61.91 O -ANISOU 5668 O LYS D 102 3578 10703 9242 909 -1800 -860 O -ATOM 5669 CB LYS D 102 -27.900 -8.557 -11.578 1.00 56.71 C -ANISOU 5669 CB LYS D 102 3706 9017 8826 1049 -2502 -385 C -ATOM 5670 CG LYS D 102 -28.797 -7.572 -12.314 1.00 68.97 C -ANISOU 5670 CG LYS D 102 5207 10412 10585 1304 -2917 -336 C -ATOM 5671 CD LYS D 102 -28.330 -7.428 -13.758 1.00 71.06 C -ANISOU 5671 CD LYS D 102 5856 10361 10784 1057 -3277 46 C -ATOM 5672 CE LYS D 102 -29.348 -6.701 -14.622 1.00 78.94 C -ANISOU 5672 CE LYS D 102 6787 11283 11924 1215 -3679 134 C -ATOM 5673 NZ LYS D 102 -28.912 -6.663 -16.050 1.00 79.82 N -ANISOU 5673 NZ LYS D 102 7308 11128 11892 863 -3976 525 N -ATOM 5674 N SER D 103 -30.237 -7.842 -9.308 1.00 56.51 N -ANISOU 5674 N SER D 103 6625 7855 6992 282 -2705 -865 N -ATOM 5675 CA SER D 103 -31.639 -7.952 -8.946 1.00 66.62 C -ANISOU 5675 CA SER D 103 7849 9554 7910 432 -2590 -799 C -ATOM 5676 C SER D 103 -32.506 -7.563 -10.134 1.00 71.74 C -ANISOU 5676 C SER D 103 8544 10372 8343 414 -2636 -656 C -ATOM 5677 O SER D 103 -32.274 -6.539 -10.778 1.00 76.91 O -ANISOU 5677 O SER D 103 9313 10795 9116 528 -2834 -656 O -ATOM 5678 CB SER D 103 -31.946 -7.053 -7.747 1.00 72.20 C -ANISOU 5678 CB SER D 103 8600 10200 8634 841 -2691 -924 C -ATOM 5679 OG SER D 103 -32.713 -7.739 -6.775 1.00 75.18 O -ANISOU 5679 OG SER D 103 8847 10919 8799 938 -2515 -859 O -ATOM 5680 N TYR D 104 -33.492 -8.403 -10.434 1.00 71.72 N -ANISOU 5680 N TYR D 104 8469 10699 8081 245 -2507 -488 N -ATOM 5681 CA TYR D 104 -34.487 -8.089 -11.447 1.00 73.41 C -ANISOU 5681 CA TYR D 104 8731 11080 8080 234 -2553 -335 C -ATOM 5682 C TYR D 104 -35.852 -7.981 -10.777 1.00 76.56 C -ANISOU 5682 C TYR D 104 9028 11698 8364 403 -2530 -197 C -ATOM 5683 O TYR D 104 -36.291 -8.911 -10.092 1.00 74.79 O -ANISOU 5683 O TYR D 104 8691 11565 8160 340 -2467 -124 O -ATOM 5684 CB TYR D 104 -34.538 -9.174 -12.525 1.00 69.79 C -ANISOU 5684 CB TYR D 104 8370 10642 7504 -81 -2539 -267 C -ATOM 5685 CG TYR D 104 -33.220 -9.470 -13.212 1.00 66.64 C -ANISOU 5685 CG TYR D 104 8072 10104 7145 -194 -2525 -403 C -ATOM 5686 CD1 TYR D 104 -32.272 -10.300 -12.614 1.00 65.13 C -ANISOU 5686 CD1 TYR D 104 7850 9769 7127 -328 -2442 -520 C -ATOM 5687 CD2 TYR D 104 -32.937 -8.949 -14.471 1.00 65.27 C -ANISOU 5687 CD2 TYR D 104 8089 9788 6922 -168 -2466 -303 C -ATOM 5688 CE1 TYR D 104 -31.075 -10.586 -13.240 1.00 62.21 C -ANISOU 5688 CE1 TYR D 104 7641 9099 6897 -437 -2258 -501 C -ATOM 5689 CE2 TYR D 104 -31.744 -9.234 -15.112 1.00 64.78 C -ANISOU 5689 CE2 TYR D 104 8172 9449 6993 -261 -2237 -236 C -ATOM 5690 CZ TYR D 104 -30.815 -10.052 -14.490 1.00 61.79 C -ANISOU 5690 CZ TYR D 104 7761 8928 6790 -387 -2132 -331 C -ATOM 5691 OH TYR D 104 -29.622 -10.341 -15.115 1.00 58.32 O -ANISOU 5691 OH TYR D 104 7434 8274 6449 -418 -1877 -211 O -ATOM 5692 N ASP D 112 -35.993 -11.721 -7.689 1.00 83.13 N -ANISOU 5692 N ASP D 112 9413 12696 9478 186 -2265 -69 N -ATOM 5693 CA ASP D 112 -35.160 -12.550 -8.559 1.00 82.98 C -ANISOU 5693 CA ASP D 112 9545 12413 9571 -117 -2306 -177 C -ATOM 5694 C ASP D 112 -33.715 -12.056 -8.594 1.00 82.62 C -ANISOU 5694 C ASP D 112 9627 12160 9604 -182 -2269 -330 C -ATOM 5695 O ASP D 112 -33.459 -10.877 -8.841 1.00 86.73 O -ANISOU 5695 O ASP D 112 10189 12687 10076 -52 -2293 -396 O -ATOM 5696 CB ASP D 112 -35.738 -12.597 -9.962 1.00 83.88 C -ANISOU 5696 CB ASP D 112 9771 12526 9573 -218 -2402 -171 C -ATOM 5697 N ILE D 113 -32.775 -12.970 -8.369 1.00 76.01 N -ANISOU 5697 N ILE D 113 8817 11159 8904 -348 -2204 -408 N -ATOM 5698 CA ILE D 113 -31.376 -12.601 -8.188 1.00 69.28 C -ANISOU 5698 CA ILE D 113 7991 10184 8147 -391 -2110 -557 C -ATOM 5699 C ILE D 113 -30.417 -13.588 -8.874 1.00 60.99 C -ANISOU 5699 C ILE D 113 7064 8949 7162 -655 -2047 -626 C -ATOM 5700 O ILE D 113 -30.508 -14.800 -8.665 1.00 62.99 O -ANISOU 5700 O ILE D 113 7337 9096 7498 -685 -2023 -637 O -ATOM 5701 CB ILE D 113 -31.065 -12.452 -6.677 1.00 71.52 C -ANISOU 5701 CB ILE D 113 8154 10492 8527 -165 -2043 -623 C -ATOM 5702 CG1 ILE D 113 -29.577 -12.204 -6.438 1.00 68.14 C -ANISOU 5702 CG1 ILE D 113 7770 9796 8323 -163 -2005 -828 C -ATOM 5703 CG2 ILE D 113 -31.598 -13.641 -5.893 1.00 74.29 C -ANISOU 5703 CG2 ILE D 113 8392 10948 8886 -203 -1992 -481 C -ATOM 5704 CD1 ILE D 113 -29.200 -10.772 -6.690 1.00 70.96 C -ANISOU 5704 CD1 ILE D 113 8208 9916 8836 41 -2186 -967 C -ATOM 5705 N LYS D 114 -29.511 -13.063 -9.702 1.00 51.90 N -ANISOU 5705 N LYS D 114 5964 7715 6042 -684 -2029 -775 N -ATOM 5706 CA LYS D 114 -28.611 -13.902 -10.508 1.00 46.95 C -ANISOU 5706 CA LYS D 114 5479 6935 5425 -849 -1981 -864 C -ATOM 5707 C LYS D 114 -27.147 -13.444 -10.461 1.00 45.25 C -ANISOU 5707 C LYS D 114 5276 6378 5538 -816 -1813 -822 C -ATOM 5708 O LYS D 114 -26.859 -12.274 -10.213 1.00 46.99 O -ANISOU 5708 O LYS D 114 5417 6428 6009 -694 -1899 -777 O -ATOM 5709 CB LYS D 114 -29.094 -13.960 -11.969 1.00 47.49 C -ANISOU 5709 CB LYS D 114 5793 7037 5213 -882 -1980 -767 C -ATOM 5710 CG LYS D 114 -30.478 -14.595 -12.163 1.00 52.40 C -ANISOU 5710 CG LYS D 114 6406 7860 5646 -866 -2087 -766 C -ATOM 5711 CD LYS D 114 -30.408 -16.115 -12.088 1.00 54.11 C -ANISOU 5711 CD LYS D 114 6692 7992 5875 -967 -2044 -823 C -ATOM 5712 CE LYS D 114 -31.784 -16.734 -11.960 1.00 60.22 C -ANISOU 5712 CE LYS D 114 7346 8880 6654 -948 -2156 -750 C -ATOM 5713 NZ LYS D 114 -31.737 -18.218 -12.132 1.00 64.45 N -ANISOU 5713 NZ LYS D 114 7981 9312 7195 -1095 -2194 -786 N -ATOM 5714 N VAL D 115 -26.228 -14.376 -10.708 1.00 45.07 N -ANISOU 5714 N VAL D 115 5349 6244 5530 -914 -1601 -802 N -ATOM 5715 CA VAL D 115 -24.796 -14.071 -10.721 1.00 46.43 C -ANISOU 5715 CA VAL D 115 5471 6151 6018 -891 -1400 -656 C -ATOM 5716 C VAL D 115 -24.324 -13.505 -12.063 1.00 51.06 C -ANISOU 5716 C VAL D 115 6174 6653 6575 -797 -1203 -354 C -ATOM 5717 O VAL D 115 -24.561 -14.104 -13.114 1.00 53.43 O -ANISOU 5717 O VAL D 115 6717 7079 6503 -730 -1075 -316 O -ATOM 5718 CB VAL D 115 -23.957 -15.322 -10.380 1.00 50.69 C -ANISOU 5718 CB VAL D 115 6040 6660 6559 -970 -1216 -715 C -ATOM 5719 CG1 VAL D 115 -22.480 -15.103 -10.713 1.00 52.34 C -ANISOU 5719 CG1 VAL D 115 6192 6670 7025 -920 -948 -448 C -ATOM 5720 CG2 VAL D 115 -24.127 -15.679 -8.920 1.00 49.88 C -ANISOU 5720 CG2 VAL D 115 5740 6617 6594 -1030 -1373 -926 C -ATOM 5721 N ILE D 116 -23.661 -12.349 -12.019 1.00 53.53 N -ANISOU 5721 N ILE D 116 6313 6744 7283 -767 -1222 -117 N -ATOM 5722 CA ILE D 116 -23.103 -11.730 -13.221 1.00 58.38 C -ANISOU 5722 CA ILE D 116 6932 7302 7948 -668 -1012 304 C -ATOM 5723 C ILE D 116 -21.577 -11.761 -13.171 1.00 62.33 C -ANISOU 5723 C ILE D 116 7229 7637 8816 -687 -784 660 C -ATOM 5724 O ILE D 116 -20.962 -11.412 -12.154 1.00 60.03 O -ANISOU 5724 O ILE D 116 6717 7103 8990 -816 -959 651 O -ATOM 5725 CB ILE D 116 -23.608 -10.275 -13.429 1.00 59.86 C -ANISOU 5725 CB ILE D 116 7039 7355 8349 -634 -1245 448 C -ATOM 5726 CG1 ILE D 116 -24.959 -10.268 -14.136 1.00 59.89 C -ANISOU 5726 CG1 ILE D 116 7256 7618 7880 -540 -1307 303 C -ATOM 5727 CG2 ILE D 116 -22.629 -9.470 -14.268 1.00 64.45 C -ANISOU 5727 CG2 ILE D 116 7457 7776 9254 -592 -1070 1018 C -ATOM 5728 CD1 ILE D 116 -26.070 -10.916 -13.356 1.00 59.46 C -ANISOU 5728 CD1 ILE D 116 7269 7764 7559 -593 -1521 -116 C -ATOM 5729 N GLY D 117 -20.973 -12.207 -14.267 1.00 67.82 N -ANISOU 5729 N GLY D 117 8005 8493 9273 -511 -408 988 N -ATOM 5730 CA GLY D 117 -19.531 -12.270 -14.370 1.00 70.43 C -ANISOU 5730 CA GLY D 117 8095 8770 9896 -465 -125 1452 C -ATOM 5731 C GLY D 117 -18.904 -13.396 -13.584 1.00 70.06 C -ANISOU 5731 C GLY D 117 8057 8731 9830 -515 -22 1237 C -ATOM 5732 O GLY D 117 -19.552 -14.405 -13.287 1.00 68.89 O -ANISOU 5732 O GLY D 117 8180 8688 9307 -520 -80 769 O -ATOM 5733 N GLY D 118 -17.634 -13.215 -13.237 1.00 67.16 N -ANISOU 5733 N GLY D 118 7362 8241 9913 -570 100 1628 N -ATOM 5734 CA GLY D 118 -16.879 -14.260 -12.580 1.00 58.68 C -ANISOU 5734 CA GLY D 118 6268 7199 8829 -580 254 1510 C -ATOM 5735 C GLY D 118 -16.279 -15.193 -13.612 1.00 58.01 C -ANISOU 5735 C GLY D 118 6362 7419 8260 -216 734 1768 C -ATOM 5736 O GLY D 118 -16.600 -15.117 -14.807 1.00 56.14 O -ANISOU 5736 O GLY D 118 6327 7391 7614 72 916 1945 O -ATOM 5737 N ASP D 119 -15.382 -16.060 -13.158 1.00 54.34 N -ANISOU 5737 N ASP D 119 5843 6996 7807 -163 934 1795 N -ATOM 5738 CA ASP D 119 -14.888 -17.133 -13.997 1.00 57.84 C -ANISOU 5738 CA ASP D 119 6563 7727 7687 271 1346 1910 C -ATOM 5739 C ASP D 119 -16.008 -18.162 -14.114 1.00 55.24 C -ANISOU 5739 C ASP D 119 6796 7415 6779 336 1164 1242 C -ATOM 5740 O ASP D 119 -16.987 -18.114 -13.359 1.00 45.25 O -ANISOU 5740 O ASP D 119 5577 5984 5632 2 786 784 O -ATOM 5741 CB ASP D 119 -13.637 -17.780 -13.380 1.00 58.96 C -ANISOU 5741 CB ASP D 119 6487 7895 8020 309 1581 2111 C -ATOM 5742 CG ASP D 119 -12.452 -16.820 -13.297 1.00 63.31 C -ANISOU 5742 CG ASP D 119 6425 8425 9203 219 1717 2880 C -ATOM 5743 OD1 ASP D 119 -12.499 -15.752 -13.940 1.00 66.86 O -ANISOU 5743 OD1 ASP D 119 6650 8881 9870 216 1705 3342 O -ATOM 5744 OD2 ASP D 119 -11.469 -17.143 -12.597 1.00 64.20 O -ANISOU 5744 OD2 ASP D 119 6261 8508 9624 140 1811 3063 O -ATOM 5745 N ASP D 120 -15.879 -19.070 -15.076 1.00 58.99 N -ANISOU 5745 N ASP D 120 7693 8092 6629 798 1396 1226 N -ATOM 5746 CA ASP D 120 -16.714 -20.255 -15.082 1.00 59.09 C -ANISOU 5746 CA ASP D 120 8246 8031 6174 837 1148 622 C -ATOM 5747 C ASP D 120 -16.560 -20.866 -13.695 1.00 52.76 C -ANISOU 5747 C ASP D 120 7291 7041 5713 475 995 327 C -ATOM 5748 O ASP D 120 -15.439 -21.075 -13.224 1.00 54.49 O -ANISOU 5748 O ASP D 120 7272 7287 6147 527 1253 564 O -ATOM 5749 CB ASP D 120 -16.239 -21.240 -16.147 1.00 68.49 C -ANISOU 5749 CB ASP D 120 9934 9405 6684 1472 1399 656 C -ATOM 5750 CG ASP D 120 -17.130 -22.460 -16.245 1.00 69.99 C -ANISOU 5750 CG ASP D 120 10745 9418 6430 1504 1009 35 C -ATOM 5751 OD1 ASP D 120 -17.114 -23.286 -15.308 1.00 62.33 O -ANISOU 5751 OD1 ASP D 120 9802 8257 5624 1247 840 -266 O -ATOM 5752 OD2 ASP D 120 -17.845 -22.591 -17.261 1.00 74.07 O -ANISOU 5752 OD2 ASP D 120 11715 9970 6458 1783 832 -127 O -ATOM 5753 N LEU D 121 -17.680 -21.128 -13.031 1.00 50.66 N -ANISOU 5753 N LEU D 121 7117 6627 5504 125 587 -127 N -ATOM 5754 CA LEU D 121 -17.653 -21.514 -11.624 1.00 50.50 C -ANISOU 5754 CA LEU D 121 6866 6482 5842 -217 433 -350 C -ATOM 5755 C LEU D 121 -17.104 -22.919 -11.384 1.00 46.96 C -ANISOU 5755 C LEU D 121 6668 5986 5187 -84 522 -514 C -ATOM 5756 O LEU D 121 -16.993 -23.350 -10.239 1.00 45.10 O -ANISOU 5756 O LEU D 121 6245 5672 5219 -325 435 -666 O -ATOM 5757 CB LEU D 121 -19.038 -21.359 -10.997 1.00 55.14 C -ANISOU 5757 CB LEU D 121 7411 7016 6523 -558 9 -673 C -ATOM 5758 CG LEU D 121 -19.578 -19.932 -10.900 1.00 58.51 C -ANISOU 5758 CG LEU D 121 7551 7466 7214 -695 -121 -560 C -ATOM 5759 CD1 LEU D 121 -21.009 -19.970 -10.418 1.00 61.71 C -ANISOU 5759 CD1 LEU D 121 7961 7911 7573 -917 -500 -842 C -ATOM 5760 CD2 LEU D 121 -18.736 -19.055 -9.980 1.00 56.39 C -ANISOU 5760 CD2 LEU D 121 6841 7110 7474 -805 -62 -372 C -ATOM 5761 N SER D 122 -16.747 -23.623 -12.455 1.00 45.82 N -ANISOU 5761 N SER D 122 6970 5897 4542 357 685 -482 N -ATOM 5762 CA SER D 122 -16.078 -24.915 -12.322 1.00 48.03 C -ANISOU 5762 CA SER D 122 7540 6118 4593 586 786 -609 C -ATOM 5763 C SER D 122 -14.680 -24.730 -11.726 1.00 47.15 C -ANISOU 5763 C SER D 122 7005 6117 4794 652 1199 -248 C -ATOM 5764 O SER D 122 -14.050 -25.697 -11.303 1.00 46.95 O -ANISOU 5764 O SER D 122 7088 6049 4700 766 1303 -330 O -ATOM 5765 CB SER D 122 -16.011 -25.657 -13.667 1.00 55.32 C -ANISOU 5765 CB SER D 122 9119 7077 4825 1178 824 -680 C -ATOM 5766 OG SER D 122 -15.295 -24.914 -14.640 1.00 58.61 O -ANISOU 5766 OG SER D 122 9454 7782 5035 1638 1246 -221 O -ATOM 5767 N THR D 123 -14.206 -23.484 -11.682 1.00 42.89 N -ANISOU 5767 N THR D 123 5974 5689 4632 560 1387 173 N -ATOM 5768 CA THR D 123 -12.933 -23.168 -11.044 1.00 42.94 C -ANISOU 5768 CA THR D 123 5493 5759 5061 524 1674 573 C -ATOM 5769 C THR D 123 -13.034 -23.338 -9.531 1.00 38.81 C -ANISOU 5769 C THR D 123 4708 5056 4983 81 1431 284 C -ATOM 5770 O THR D 123 -12.020 -23.420 -8.842 1.00 42.88 O -ANISOU 5770 O THR D 123 4908 5583 5800 46 1599 488 O -ATOM 5771 CB THR D 123 -12.494 -21.732 -11.324 1.00 48.01 C -ANISOU 5771 CB THR D 123 5655 6475 6111 454 1788 1122 C -ATOM 5772 OG1 THR D 123 -13.537 -20.836 -10.925 1.00 45.87 O -ANISOU 5772 OG1 THR D 123 5272 6028 6129 62 1392 887 O -ATOM 5773 CG2 THR D 123 -12.186 -21.539 -12.804 1.00 49.34 C -ANISOU 5773 CG2 THR D 123 5979 6917 5849 971 2128 1563 C -ATOM 5774 N LEU D 124 -14.261 -23.387 -9.022 1.00 35.96 N -ANISOU 5774 N LEU D 124 4453 4566 4642 -218 1041 -148 N -ATOM 5775 CA LEU D 124 -14.487 -23.536 -7.583 1.00 32.51 C -ANISOU 5775 CA LEU D 124 3767 4034 4551 -552 813 -403 C -ATOM 5776 C LEU D 124 -14.410 -24.995 -7.131 1.00 34.64 C -ANISOU 5776 C LEU D 124 4276 4265 4621 -517 818 -655 C -ATOM 5777 O LEU D 124 -14.216 -25.264 -5.946 1.00 29.95 O -ANISOU 5777 O LEU D 124 3438 3647 4295 -698 755 -761 O -ATOM 5778 CB LEU D 124 -15.855 -22.973 -7.190 1.00 30.83 C -ANISOU 5778 CB LEU D 124 3508 3788 4417 -814 424 -664 C -ATOM 5779 CG LEU D 124 -16.016 -21.516 -6.759 1.00 36.79 C -ANISOU 5779 CG LEU D 124 3908 4505 5565 -961 253 -561 C -ATOM 5780 CD1 LEU D 124 -14.969 -20.614 -7.366 1.00 35.69 C -ANISOU 5780 CD1 LEU D 124 3567 4330 5665 -858 465 -109 C -ATOM 5781 CD2 LEU D 124 -17.423 -21.024 -7.092 1.00 34.78 C -ANISOU 5781 CD2 LEU D 124 3777 4291 5147 -1037 -25 -733 C -ATOM 5782 N THR D 125 -14.568 -25.924 -8.070 1.00 34.14 N -ANISOU 5782 N THR D 125 4713 4176 4082 -255 851 -757 N -ATOM 5783 CA THR D 125 -14.617 -27.348 -7.734 1.00 34.19 C -ANISOU 5783 CA THR D 125 5027 4060 3903 -227 748 -1016 C -ATOM 5784 C THR D 125 -13.359 -27.801 -6.995 1.00 34.62 C -ANISOU 5784 C THR D 125 4867 4157 4131 -136 1050 -877 C -ATOM 5785 O THR D 125 -12.242 -27.660 -7.501 1.00 36.01 O -ANISOU 5785 O THR D 125 5005 4460 4218 194 1429 -564 O -ATOM 5786 CB THR D 125 -14.829 -28.219 -8.979 1.00 42.02 C -ANISOU 5786 CB THR D 125 6682 4953 4329 144 675 -1154 C -ATOM 5787 OG1 THR D 125 -16.025 -27.802 -9.650 1.00 38.51 O -ANISOU 5787 OG1 THR D 125 6425 4467 3741 37 352 -1282 O -ATOM 5788 CG2 THR D 125 -14.943 -29.696 -8.599 1.00 43.65 C -ANISOU 5788 CG2 THR D 125 7244 4932 4409 137 447 -1436 C -ATOM 5789 N GLY D 126 -13.552 -28.331 -5.789 1.00 34.47 N -ANISOU 5789 N GLY D 126 4666 4073 4356 -409 893 -1056 N -ATOM 5790 CA GLY D 126 -12.464 -28.899 -5.012 1.00 34.63 C -ANISOU 5790 CA GLY D 126 4511 4122 4524 -338 1134 -971 C -ATOM 5791 C GLY D 126 -11.623 -27.893 -4.246 1.00 36.37 C -ANISOU 5791 C GLY D 126 4164 4462 5191 -447 1303 -717 C -ATOM 5792 O GLY D 126 -10.550 -28.248 -3.748 1.00 35.79 O -ANISOU 5792 O GLY D 126 3916 4439 5244 -351 1540 -567 O -ATOM 5793 N LYS D 127 -12.095 -26.647 -4.146 1.00 29.62 N -ANISOU 5793 N LYS D 127 3041 3624 4591 -638 1134 -667 N -ATOM 5794 CA LYS D 127 -11.314 -25.587 -3.504 1.00 30.38 C -ANISOU 5794 CA LYS D 127 2653 3735 5156 -742 1159 -429 C -ATOM 5795 C LYS D 127 -12.018 -25.127 -2.235 1.00 25.24 C -ANISOU 5795 C LYS D 127 1849 3056 4683 -922 754 -660 C -ATOM 5796 O LYS D 127 -13.211 -25.376 -2.065 1.00 26.71 O -ANISOU 5796 O LYS D 127 2195 3272 4681 -979 539 -896 O -ATOM 5797 CB LYS D 127 -11.157 -24.383 -4.440 1.00 32.94 C -ANISOU 5797 CB LYS D 127 2872 4060 5584 -695 1203 -98 C -ATOM 5798 CG LYS D 127 -10.585 -24.707 -5.808 1.00 39.83 C -ANISOU 5798 CG LYS D 127 3981 5057 6095 -340 1575 227 C -ATOM 5799 CD LYS D 127 -9.193 -25.281 -5.711 1.00 44.11 C -ANISOU 5799 CD LYS D 127 4377 5718 6667 -115 1945 558 C -ATOM 5800 CE LYS D 127 -8.583 -25.403 -7.106 1.00 54.08 C -ANISOU 5800 CE LYS D 127 5815 7195 7537 359 2348 986 C -ATOM 5801 NZ LYS D 127 -8.840 -24.163 -7.893 1.00 61.16 N -ANISOU 5801 NZ LYS D 127 6546 8128 8563 328 2311 1311 N -ATOM 5802 N ASN D 128 -11.279 -24.464 -1.351 1.00 26.96 N -ANISOU 5802 N ASN D 128 2890 2900 4454 69 -782 -550 N -ATOM 5803 CA ASN D 128 -11.874 -23.798 -0.198 1.00 27.20 C -ANISOU 5803 CA ASN D 128 3063 2910 4360 136 -847 -476 C -ATOM 5804 C ASN D 128 -12.328 -22.414 -0.631 1.00 27.84 C -ANISOU 5804 C ASN D 128 2971 3056 4552 -58 -657 -404 C -ATOM 5805 O ASN D 128 -11.506 -21.519 -0.810 1.00 32.19 O -ANISOU 5805 O ASN D 128 3275 3613 5343 -89 -623 -586 O -ATOM 5806 CB ASN D 128 -10.868 -23.669 0.950 1.00 26.63 C -ANISOU 5806 CB ASN D 128 2981 2808 4329 422 -1145 -744 C -ATOM 5807 CG ASN D 128 -10.606 -24.993 1.653 1.00 31.72 C -ANISOU 5807 CG ASN D 128 3954 3350 4748 721 -1364 -768 C -ATOM 5808 OD1 ASN D 128 -11.201 -26.009 1.310 1.00 31.08 O -ANISOU 5808 OD1 ASN D 128 4104 3190 4516 664 -1237 -571 O -ATOM 5809 ND2 ASN D 128 -9.700 -24.986 2.633 1.00 34.52 N -ANISOU 5809 ND2 ASN D 128 4343 3691 5082 1072 -1698 -1042 N -ATOM 5810 N VAL D 129 -13.629 -22.233 -0.799 1.00 23.40 N -ANISOU 5810 N VAL D 129 2533 2520 3838 -179 -515 -173 N -ATOM 5811 CA VAL D 129 -14.134 -20.973 -1.343 1.00 21.24 C -ANISOU 5811 CA VAL D 129 2147 2297 3627 -313 -345 -88 C -ATOM 5812 C VAL D 129 -14.500 -20.007 -0.217 1.00 26.84 C -ANISOU 5812 C VAL D 129 2888 2989 4322 -275 -397 -83 C -ATOM 5813 O VAL D 129 -15.304 -20.344 0.665 1.00 26.89 O -ANISOU 5813 O VAL D 129 3086 2976 4154 -228 -451 2 O -ATOM 5814 CB VAL D 129 -15.361 -21.207 -2.236 1.00 24.09 C -ANISOU 5814 CB VAL D 129 2579 2727 3848 -412 -214 85 C -ATOM 5815 CG1 VAL D 129 -15.888 -19.881 -2.792 1.00 22.99 C -ANISOU 5815 CG1 VAL D 129 2391 2627 3717 -462 -78 174 C -ATOM 5816 CG2 VAL D 129 -15.009 -22.159 -3.380 1.00 26.23 C -ANISOU 5816 CG2 VAL D 129 2819 3027 4119 -434 -174 56 C -ATOM 5817 N LEU D 130 -13.890 -18.823 -0.240 1.00 24.17 N -ANISOU 5817 N LEU D 130 2369 2629 4185 -304 -339 -195 N -ATOM 5818 CA LEU D 130 -14.195 -17.743 0.706 1.00 22.80 C -ANISOU 5818 CA LEU D 130 2184 2438 4038 -282 -368 -218 C -ATOM 5819 C LEU D 130 -14.961 -16.644 -0.032 1.00 21.49 C -ANISOU 5819 C LEU D 130 2004 2270 3891 -408 -139 -54 C -ATOM 5820 O LEU D 130 -14.395 -15.955 -0.890 1.00 26.12 O -ANISOU 5820 O LEU D 130 2486 2790 4649 -483 61 -88 O -ATOM 5821 CB LEU D 130 -12.901 -17.138 1.255 1.00 26.38 C -ANISOU 5821 CB LEU D 130 2412 2844 4766 -212 -462 -539 C -ATOM 5822 CG LEU D 130 -12.826 -16.490 2.652 1.00 35.13 C -ANISOU 5822 CG LEU D 130 3508 3952 5887 -75 -653 -705 C -ATOM 5823 CD1 LEU D 130 -11.962 -15.236 2.630 1.00 33.33 C -ANISOU 5823 CD1 LEU D 130 2960 3658 6046 -148 -553 -993 C -ATOM 5824 CD2 LEU D 130 -14.176 -16.234 3.275 1.00 34.29 C -ANISOU 5824 CD2 LEU D 130 3636 3870 5524 -81 -633 -459 C -ATOM 5825 N ILE D 131 -16.237 -16.486 0.301 1.00 20.67 N -ANISOU 5825 N ILE D 131 2029 2213 3610 -413 -144 105 N -ATOM 5826 CA ILE D 131 -17.053 -15.418 -0.273 1.00 23.39 C -ANISOU 5826 CA ILE D 131 2385 2561 3939 -456 8 235 C -ATOM 5827 C ILE D 131 -16.920 -14.207 0.635 1.00 22.11 C -ANISOU 5827 C ILE D 131 2160 2334 3907 -451 14 160 C -ATOM 5828 O ILE D 131 -17.090 -14.324 1.850 1.00 23.71 O -ANISOU 5828 O ILE D 131 2392 2557 4061 -399 -134 93 O -ATOM 5829 CB ILE D 131 -18.537 -15.839 -0.352 1.00 21.67 C -ANISOU 5829 CB ILE D 131 2268 2442 3525 -451 -23 353 C -ATOM 5830 CG1 ILE D 131 -18.695 -17.024 -1.309 1.00 24.86 C -ANISOU 5830 CG1 ILE D 131 2698 2912 3837 -459 -27 372 C -ATOM 5831 CG2 ILE D 131 -19.400 -14.679 -0.818 1.00 26.91 C -ANISOU 5831 CG2 ILE D 131 2945 3121 4159 -418 61 440 C -ATOM 5832 CD1 ILE D 131 -20.073 -17.706 -1.267 1.00 28.61 C -ANISOU 5832 CD1 ILE D 131 3198 3469 4204 -480 -53 368 C -ATOM 5833 N VAL D 132 -16.601 -13.052 0.067 1.00 20.36 N -ANISOU 5833 N VAL D 132 1887 2008 3840 -492 212 164 N -ATOM 5834 CA VAL D 132 -16.397 -11.861 0.870 1.00 22.55 C -ANISOU 5834 CA VAL D 132 2074 2197 4299 -506 251 54 C -ATOM 5835 C VAL D 132 -17.447 -10.801 0.533 1.00 29.76 C -ANISOU 5835 C VAL D 132 3105 3071 5132 -489 386 234 C -ATOM 5836 O VAL D 132 -17.518 -10.334 -0.609 1.00 26.63 O -ANISOU 5836 O VAL D 132 2827 2585 4708 -474 601 365 O -ATOM 5837 CB VAL D 132 -14.992 -11.302 0.652 1.00 23.82 C -ANISOU 5837 CB VAL D 132 2049 2202 4799 -579 423 -177 C -ATOM 5838 CG1 VAL D 132 -14.760 -10.052 1.500 1.00 22.30 C -ANISOU 5838 CG1 VAL D 132 1761 1931 4780 -567 460 -348 C -ATOM 5839 CG2 VAL D 132 -13.928 -12.376 0.974 1.00 25.08 C -ANISOU 5839 CG2 VAL D 132 2060 2419 5049 -541 233 -418 C -ATOM 5840 N GLU D 133 -18.222 -10.397 1.543 1.00 24.71 N -ANISOU 5840 N GLU D 133 2467 2484 4440 -457 266 226 N -ATOM 5841 CA GLU D 133 -19.396 -9.542 1.358 1.00 25.25 C -ANISOU 5841 CA GLU D 133 2631 2551 4411 -404 323 365 C -ATOM 5842 C GLU D 133 -19.268 -8.294 2.228 1.00 30.01 C -ANISOU 5842 C GLU D 133 3160 3046 5198 -422 376 265 C -ATOM 5843 O GLU D 133 -18.560 -8.321 3.244 1.00 25.74 O -ANISOU 5843 O GLU D 133 2487 2501 4793 -452 277 64 O -ATOM 5844 CB GLU D 133 -20.663 -10.355 1.700 1.00 27.31 C -ANISOU 5844 CB GLU D 133 2934 2986 4455 -367 157 413 C -ATOM 5845 CG GLU D 133 -22.000 -9.648 1.551 1.00 34.50 C -ANISOU 5845 CG GLU D 133 3883 3942 5283 -285 156 475 C -ATOM 5846 CD GLU D 133 -22.307 -9.251 0.123 1.00 31.27 C -ANISOU 5846 CD GLU D 133 3595 3511 4776 -147 228 592 C -ATOM 5847 OE1 GLU D 133 -21.672 -8.303 -0.369 1.00 29.40 O -ANISOU 5847 OE1 GLU D 133 3461 3099 4611 -110 408 666 O -ATOM 5848 OE2 GLU D 133 -23.192 -9.873 -0.506 1.00 32.71 O -ANISOU 5848 OE2 GLU D 133 3788 3833 4806 -55 121 586 O -ATOM 5849 N ASP D 134 -19.903 -7.190 1.823 1.00 28.09 N -ANISOU 5849 N ASP D 134 3010 2708 4954 -367 514 374 N -ATOM 5850 CA ASP D 134 -19.949 -5.994 2.679 1.00 21.88 C -ANISOU 5850 CA ASP D 134 2155 1816 4341 -383 564 276 C -ATOM 5851 C ASP D 134 -20.973 -6.126 3.820 1.00 25.12 C -ANISOU 5851 C ASP D 134 2529 2389 4626 -347 351 235 C -ATOM 5852 O ASP D 134 -20.665 -5.858 4.987 1.00 28.81 O -ANISOU 5852 O ASP D 134 2894 2859 5194 -374 270 64 O -ATOM 5853 CB ASP D 134 -20.152 -4.698 1.876 1.00 25.85 C -ANISOU 5853 CB ASP D 134 2818 2098 4907 -320 833 405 C -ATOM 5854 CG ASP D 134 -21.390 -4.729 1.001 1.00 30.59 C -ANISOU 5854 CG ASP D 134 3635 2779 5209 -125 774 615 C -ATOM 5855 OD1 ASP D 134 -21.950 -5.824 0.778 1.00 29.07 O -ANISOU 5855 OD1 ASP D 134 3425 2803 4818 -84 575 638 O -ATOM 5856 OD2 ASP D 134 -21.796 -3.650 0.524 1.00 33.55 O -ANISOU 5856 OD2 ASP D 134 4200 2989 5558 12 924 725 O -ATOM 5857 N ILE D 135 -22.183 -6.562 3.501 1.00 28.80 N -ANISOU 5857 N ILE D 135 3073 2988 4882 -277 270 347 N -ATOM 5858 CA ILE D 135 -23.216 -6.609 4.520 1.00 26.02 C -ANISOU 5858 CA ILE D 135 2684 2748 4456 -272 162 283 C -ATOM 5859 C ILE D 135 -24.260 -7.679 4.250 1.00 27.70 C -ANISOU 5859 C ILE D 135 2906 3117 4501 -264 90 301 C -ATOM 5860 O ILE D 135 -24.646 -7.907 3.098 1.00 29.97 O -ANISOU 5860 O ILE D 135 3221 3450 4718 -185 80 365 O -ATOM 5861 CB ILE D 135 -23.855 -5.198 4.688 1.00 35.17 C -ANISOU 5861 CB ILE D 135 3837 3827 5700 -200 220 280 C -ATOM 5862 CG1 ILE D 135 -24.944 -5.202 5.763 1.00 32.50 C -ANISOU 5862 CG1 ILE D 135 3440 3599 5309 -209 143 181 C -ATOM 5863 CG2 ILE D 135 -24.378 -4.669 3.347 1.00 34.53 C -ANISOU 5863 CG2 ILE D 135 3878 3693 5549 -43 281 419 C -ATOM 5864 CD1 ILE D 135 -25.277 -3.793 6.247 1.00 33.57 C -ANISOU 5864 CD1 ILE D 135 3543 3641 5570 -157 188 130 C -ATOM 5865 N ILE D 136 -24.685 -8.344 5.327 1.00 24.96 N -ANISOU 5865 N ILE D 136 2558 2831 4095 -335 64 216 N -ATOM 5866 CA ILE D 136 -25.822 -9.260 5.318 1.00 26.49 C -ANISOU 5866 CA ILE D 136 2729 3123 4212 -379 87 160 C -ATOM 5867 C ILE D 136 -26.973 -8.528 5.995 1.00 30.57 C -ANISOU 5867 C ILE D 136 3170 3665 4782 -373 128 51 C -ATOM 5868 O ILE D 136 -26.808 -8.021 7.104 1.00 28.41 O -ANISOU 5868 O ILE D 136 2945 3338 4513 -393 160 19 O -ATOM 5869 CB ILE D 136 -25.552 -10.512 6.185 1.00 28.97 C -ANISOU 5869 CB ILE D 136 3173 3413 4423 -471 140 138 C -ATOM 5870 CG1 ILE D 136 -24.254 -11.213 5.782 1.00 31.36 C -ANISOU 5870 CG1 ILE D 136 3550 3682 4684 -454 69 209 C -ATOM 5871 CG2 ILE D 136 -26.735 -11.498 6.116 1.00 28.35 C -ANISOU 5871 CG2 ILE D 136 3062 3373 4335 -568 267 44 C -ATOM 5872 CD1 ILE D 136 -24.179 -11.525 4.333 1.00 30.80 C -ANISOU 5872 CD1 ILE D 136 3403 3662 4639 -442 46 265 C -ATOM 5873 N ASP D 137 -28.133 -8.487 5.348 1.00 30.82 N -ANISOU 5873 N ASP D 137 3065 3786 4857 -323 110 -51 N -ATOM 5874 CA ASP D 137 -29.313 -7.873 5.943 1.00 33.24 C -ANISOU 5874 CA ASP D 137 3247 4127 5254 -317 150 -217 C -ATOM 5875 C ASP D 137 -30.395 -8.937 6.095 1.00 35.41 C -ANISOU 5875 C ASP D 137 3391 4467 5596 -444 273 -435 C -ATOM 5876 O ASP D 137 -30.521 -9.558 7.147 1.00 35.11 O -ANISOU 5876 O ASP D 137 3445 4353 5543 -609 481 -477 O -ATOM 5877 CB ASP D 137 -29.776 -6.695 5.075 1.00 36.59 C -ANISOU 5877 CB ASP D 137 3597 4584 5720 -93 9 -229 C -ATOM 5878 CG ASP D 137 -30.913 -5.910 5.695 1.00 40.06 C -ANISOU 5878 CG ASP D 137 3890 5056 6275 -52 18 -421 C -ATOM 5879 OD1 ASP D 137 -31.196 -6.089 6.901 1.00 43.43 O -ANISOU 5879 OD1 ASP D 137 4295 5458 6750 -221 171 -514 O -ATOM 5880 OD2 ASP D 137 -31.509 -5.099 4.962 1.00 40.00 O -ANISOU 5880 OD2 ASP D 137 3823 5087 6288 181 -126 -482 O -ATOM 5881 N THR D 138 -31.169 -9.171 5.044 1.00 36.18 N -ANISOU 5881 N THR D 138 3294 4683 5769 -351 167 -603 N -ATOM 5882 CA THR D 138 -32.163 -10.241 5.094 1.00 36.51 C -ANISOU 5882 CA THR D 138 3143 4770 5960 -501 314 -894 C -ATOM 5883 C THR D 138 -31.481 -11.603 4.979 1.00 36.28 C -ANISOU 5883 C THR D 138 3255 4673 5857 -651 433 -792 C -ATOM 5884 O THR D 138 -31.971 -12.598 5.512 1.00 39.29 O -ANISOU 5884 O THR D 138 3619 4972 6337 -860 703 -945 O -ATOM 5885 CB THR D 138 -33.210 -10.118 3.981 1.00 39.63 C -ANISOU 5885 CB THR D 138 3229 5340 6487 -312 108 -1208 C -ATOM 5886 OG1 THR D 138 -32.583 -10.274 2.699 1.00 39.56 O -ANISOU 5886 OG1 THR D 138 3308 5403 6320 -114 -122 -1070 O -ATOM 5887 CG2 THR D 138 -33.888 -8.774 4.053 1.00 42.63 C -ANISOU 5887 CG2 THR D 138 3498 5777 6923 -104 -41 -1317 C -ATOM 5888 N GLY D 139 -30.351 -11.642 4.278 1.00 31.55 N -ANISOU 5888 N GLY D 139 2811 4078 5100 -548 272 -545 N -ATOM 5889 CA GLY D 139 -29.649 -12.902 4.057 1.00 30.02 C -ANISOU 5889 CA GLY D 139 2740 3829 4837 -653 342 -457 C -ATOM 5890 C GLY D 139 -30.033 -13.572 2.750 1.00 30.21 C -ANISOU 5890 C GLY D 139 2584 3979 4918 -590 227 -619 C -ATOM 5891 O GLY D 139 -29.474 -14.607 2.386 1.00 34.21 O -ANISOU 5891 O GLY D 139 3166 4451 5380 -660 264 -564 O -ATOM 5892 N LYS D 140 -30.985 -12.986 2.031 1.00 33.28 N -ANISOU 5892 N LYS D 140 2737 4517 5391 -418 57 -848 N -ATOM 5893 CA LYS D 140 -31.454 -13.573 0.772 1.00 38.01 C -ANISOU 5893 CA LYS D 140 3147 5269 6028 -286 -114 -1082 C -ATOM 5894 C LYS D 140 -30.377 -13.616 -0.312 1.00 38.12 C -ANISOU 5894 C LYS D 140 3366 5310 5808 -113 -283 -824 C -ATOM 5895 O LYS D 140 -30.286 -14.582 -1.073 1.00 40.69 O -ANISOU 5895 O LYS D 140 3637 5696 6128 -116 -324 -923 O -ATOM 5896 CB LYS D 140 -32.689 -12.829 0.257 1.00 45.73 C -ANISOU 5896 CB LYS D 140 3849 6418 7109 -38 -334 -1427 C -ATOM 5897 CG LYS D 140 -33.979 -13.152 1.013 1.00 54.79 C -ANISOU 5897 CG LYS D 140 4849 7502 8467 -203 -127 -1766 C -ATOM 5898 CD LYS D 140 -35.197 -12.562 0.309 1.00 60.61 C -ANISOU 5898 CD LYS D 140 5400 8379 9252 84 -380 -2138 C -ATOM 5899 CE LYS D 140 -35.610 -11.231 0.914 1.00 63.14 C -ANISOU 5899 CE LYS D 140 5700 8700 9591 193 -437 -2128 C -ATOM 5900 NZ LYS D 140 -36.542 -11.439 2.058 1.00 67.11 N -ANISOU 5900 NZ LYS D 140 6096 9080 10322 -64 -135 -2375 N -ATOM 5901 N THR D 141 -29.564 -12.569 -0.387 1.00 38.38 N -ANISOU 5901 N THR D 141 3631 5278 5675 23 -339 -521 N -ATOM 5902 CA THR D 141 -28.516 -12.514 -1.400 1.00 38.09 C -ANISOU 5902 CA THR D 141 3811 5220 5441 166 -410 -286 C -ATOM 5903 C THR D 141 -27.536 -13.660 -1.200 1.00 36.65 C -ANISOU 5903 C THR D 141 3697 4960 5267 -60 -279 -174 C -ATOM 5904 O THR D 141 -27.161 -14.346 -2.148 1.00 36.36 O -ANISOU 5904 O THR D 141 3693 4974 5148 -3 -334 -172 O -ATOM 5905 CB THR D 141 -27.766 -11.166 -1.372 1.00 36.54 C -ANISOU 5905 CB THR D 141 3848 4892 5144 286 -376 -12 C -ATOM 5906 OG1 THR D 141 -28.714 -10.098 -1.494 1.00 42.89 O -ANISOU 5906 OG1 THR D 141 4624 5741 5931 523 -497 -109 O -ATOM 5907 CG2 THR D 141 -26.759 -11.081 -2.511 1.00 39.77 C -ANISOU 5907 CG2 THR D 141 4497 5239 5375 426 -361 195 C -ATOM 5908 N MET D 142 -27.135 -13.888 0.043 1.00 29.59 N -ANISOU 5908 N MET D 142 2851 3945 4449 -279 -121 -99 N -ATOM 5909 CA AMET D 142 -26.148 -14.919 0.345 0.49 28.73 C -ANISOU 5909 CA AMET D 142 2855 3742 4318 -428 -29 5 C -ATOM 5910 CA BMET D 142 -26.145 -14.923 0.305 0.51 28.31 C -ANISOU 5910 CA BMET D 142 2801 3692 4263 -424 -33 5 C -ATOM 5911 C MET D 142 -26.712 -16.330 0.189 1.00 26.36 C -ANISOU 5911 C MET D 142 2460 3464 4093 -552 46 -180 C -ATOM 5912 O MET D 142 -26.034 -17.226 -0.308 1.00 29.17 O -ANISOU 5912 O MET D 142 2875 3800 4406 -579 44 -134 O -ATOM 5913 CB AMET D 142 -25.575 -14.722 1.753 0.49 29.73 C -ANISOU 5913 CB AMET D 142 3116 3732 4447 -532 71 109 C -ATOM 5914 CB BMET D 142 -25.454 -14.732 1.659 0.51 29.75 C -ANISOU 5914 CB BMET D 142 3126 3735 4443 -524 62 123 C -ATOM 5915 CG AMET D 142 -24.242 -15.408 1.973 0.49 29.14 C -ANISOU 5915 CG AMET D 142 3194 3565 4313 -563 73 225 C -ATOM 5916 CG BMET D 142 -24.401 -13.631 1.687 0.51 30.52 C -ANISOU 5916 CG BMET D 142 3298 3775 4522 -440 8 272 C -ATOM 5917 SD AMET D 142 -23.111 -15.161 0.584 0.49 37.02 S -ANISOU 5917 SD AMET D 142 4183 4593 5289 -462 -17 326 S -ATOM 5918 SD BMET D 142 -22.979 -13.795 0.575 0.51 33.39 S -ANISOU 5918 SD BMET D 142 3720 4105 4860 -387 -18 384 S -ATOM 5919 CE AMET D 142 -22.850 -13.389 0.626 0.49 34.97 C -ANISOU 5919 CE AMET D 142 3927 4284 5077 -370 -10 404 C -ATOM 5920 CE BMET D 142 -22.777 -15.568 0.485 0.51 40.51 C -ANISOU 5920 CE BMET D 142 4646 5024 5724 -477 -18 333 C -ATOM 5921 N GLN D 143 -27.948 -16.537 0.629 1.00 29.92 N -ANISOU 5921 N GLN D 143 2747 3931 4689 -644 149 -421 N -ATOM 5922 CA GLN D 143 -28.547 -17.863 0.465 1.00 30.53 C -ANISOU 5922 CA GLN D 143 2701 3986 4913 -796 292 -660 C -ATOM 5923 C GLN D 143 -28.610 -18.207 -1.019 1.00 36.28 C -ANISOU 5923 C GLN D 143 3275 4886 5625 -646 81 -799 C -ATOM 5924 O GLN D 143 -28.359 -19.345 -1.416 1.00 38.28 O -ANISOU 5924 O GLN D 143 3523 5107 5916 -733 141 -862 O -ATOM 5925 CB GLN D 143 -29.922 -17.937 1.124 1.00 42.52 C -ANISOU 5925 CB GLN D 143 4053 5471 6632 -913 484 -954 C -ATOM 5926 CG GLN D 143 -29.855 -18.387 2.585 1.00 48.58 C -ANISOU 5926 CG GLN D 143 5101 5995 7360 -1081 809 -833 C -ATOM 5927 CD GLN D 143 -31.213 -18.416 3.255 1.00 56.48 C -ANISOU 5927 CD GLN D 143 6018 6932 8510 -1147 1033 -1102 C -ATOM 5928 OE1 GLN D 143 -32.210 -17.970 2.683 1.00 58.43 O -ANISOU 5928 OE1 GLN D 143 5974 7320 8909 -1066 916 -1393 O -ATOM 5929 NE2 GLN D 143 -31.259 -18.940 4.475 1.00 56.83 N -ANISOU 5929 NE2 GLN D 143 6340 6748 8503 -1266 1360 -1033 N -ATOM 5930 N THR D 144 -28.902 -17.196 -1.835 1.00 40.70 N -ANISOU 5930 N THR D 144 3759 5611 6094 -383 -168 -835 N -ATOM 5931 CA THR D 144 -28.947 -17.349 -3.287 1.00 43.68 C -ANISOU 5931 CA THR D 144 4075 6159 6361 -139 -406 -951 C -ATOM 5932 C THR D 144 -27.574 -17.711 -3.851 1.00 40.53 C -ANISOU 5932 C THR D 144 3923 5701 5776 -124 -400 -656 C -ATOM 5933 O THR D 144 -27.431 -18.652 -4.635 1.00 39.92 O -ANISOU 5933 O THR D 144 3797 5683 5687 -113 -444 -768 O -ATOM 5934 CB THR D 144 -29.417 -16.056 -3.963 1.00 45.09 C -ANISOU 5934 CB THR D 144 4272 6472 6386 220 -657 -977 C -ATOM 5935 OG1 THR D 144 -30.797 -15.834 -3.658 1.00 49.15 O -ANISOU 5935 OG1 THR D 144 4479 7090 7106 257 -725 -1365 O -ATOM 5936 CG2 THR D 144 -29.248 -16.149 -5.477 1.00 47.87 C -ANISOU 5936 CG2 THR D 144 4714 6968 6505 548 -893 -1019 C -ATOM 5937 N LEU D 145 -26.564 -16.950 -3.456 1.00 34.03 N -ANISOU 5937 N LEU D 145 3329 4758 4841 -126 -338 -326 N -ATOM 5938 CA LEU D 145 -25.208 -17.195 -3.927 1.00 34.02 C -ANISOU 5938 CA LEU D 145 3518 4685 4725 -128 -300 -98 C -ATOM 5939 C LEU D 145 -24.704 -18.569 -3.484 1.00 35.60 C -ANISOU 5939 C LEU D 145 3706 4801 5020 -348 -189 -119 C -ATOM 5940 O LEU D 145 -24.070 -19.285 -4.261 1.00 37.06 O -ANISOU 5940 O LEU D 145 3928 5003 5152 -329 -209 -105 O -ATOM 5941 CB LEU D 145 -24.263 -16.096 -3.440 1.00 32.22 C -ANISOU 5941 CB LEU D 145 3459 4322 4459 -124 -219 158 C -ATOM 5942 CG LEU D 145 -22.825 -16.274 -3.917 1.00 37.00 C -ANISOU 5942 CG LEU D 145 4201 4836 5022 -144 -140 318 C -ATOM 5943 CD1 LEU D 145 -22.787 -16.409 -5.449 1.00 39.54 C -ANISOU 5943 CD1 LEU D 145 4613 5241 5170 50 -187 314 C -ATOM 5944 CD2 LEU D 145 -21.965 -15.112 -3.439 1.00 35.93 C -ANISOU 5944 CD2 LEU D 145 4161 4552 4937 -158 -29 470 C -ATOM 5945 N LEU D 146 -25.002 -18.944 -2.243 1.00 26.47 N -ANISOU 5945 N LEU D 146 2540 3534 3982 -530 -55 -152 N -ATOM 5946 CA LEU D 146 -24.532 -20.223 -1.715 1.00 27.97 C -ANISOU 5946 CA LEU D 146 2821 3587 4218 -689 78 -143 C -ATOM 5947 C LEU D 146 -25.121 -21.389 -2.509 1.00 32.42 C -ANISOU 5947 C LEU D 146 3237 4204 4877 -744 103 -378 C -ATOM 5948 O LEU D 146 -24.415 -22.334 -2.858 1.00 31.11 O -ANISOU 5948 O LEU D 146 3143 3984 4694 -777 122 -345 O -ATOM 5949 CB LEU D 146 -24.862 -20.353 -0.215 1.00 27.45 C -ANISOU 5949 CB LEU D 146 2877 3355 4200 -823 265 -125 C -ATOM 5950 CG LEU D 146 -23.940 -19.531 0.685 1.00 26.92 C -ANISOU 5950 CG LEU D 146 2991 3213 4026 -756 217 81 C -ATOM 5951 CD1 LEU D 146 -24.414 -19.528 2.119 1.00 28.55 C -ANISOU 5951 CD1 LEU D 146 3353 3277 4217 -828 386 84 C -ATOM 5952 CD2 LEU D 146 -22.514 -20.065 0.606 1.00 29.65 C -ANISOU 5952 CD2 LEU D 146 3478 3492 4297 -698 140 197 C -ATOM 5953 N SER D 147 -26.413 -21.306 -2.804 1.00 34.40 N -ANISOU 5953 N SER D 147 3248 4564 5258 -742 89 -664 N -ATOM 5954 CA SER D 147 -27.099 -22.333 -3.582 1.00 41.28 C -ANISOU 5954 CA SER D 147 3894 5507 6282 -784 93 -998 C -ATOM 5955 C SER D 147 -26.457 -22.545 -4.963 1.00 40.90 C -ANISOU 5955 C SER D 147 3856 5609 6076 -594 -124 -978 C -ATOM 5956 O SER D 147 -26.379 -23.669 -5.457 1.00 41.90 O -ANISOU 5956 O SER D 147 3913 5723 6284 -665 -86 -1131 O -ATOM 5957 CB SER D 147 -28.579 -21.982 -3.734 1.00 48.10 C -ANISOU 5957 CB SER D 147 4502 6487 7287 -712 47 -1351 C -ATOM 5958 OG SER D 147 -28.756 -20.903 -4.634 1.00 55.46 O -ANISOU 5958 OG SER D 147 5316 7665 8091 -423 -279 -1411 O -ATOM 5959 N LEU D 148 -25.991 -21.469 -5.583 1.00 37.22 N -ANISOU 5959 N LEU D 148 3508 5253 5382 -355 -309 -790 N -ATOM 5960 CA LEU D 148 -25.283 -21.595 -6.855 1.00 40.79 C -ANISOU 5960 CA LEU D 148 4058 5804 5638 -167 -442 -727 C -ATOM 5961 C LEU D 148 -23.912 -22.241 -6.656 1.00 41.74 C -ANISOU 5961 C LEU D 148 4349 5770 5739 -308 -310 -492 C -ATOM 5962 O LEU D 148 -23.553 -23.202 -7.344 1.00 44.16 O -ANISOU 5962 O LEU D 148 4636 6100 6044 -317 -321 -575 O -ATOM 5963 CB LEU D 148 -25.113 -20.234 -7.529 1.00 43.65 C -ANISOU 5963 CB LEU D 148 4594 6245 5744 129 -573 -561 C -ATOM 5964 CG LEU D 148 -24.348 -20.342 -8.846 1.00 45.40 C -ANISOU 5964 CG LEU D 148 5001 6523 5725 332 -629 -473 C -ATOM 5965 CD1 LEU D 148 -25.052 -21.324 -9.763 1.00 46.00 C -ANISOU 5965 CD1 LEU D 148 4895 6782 5800 448 -802 -829 C -ATOM 5966 CD2 LEU D 148 -24.251 -19.007 -9.518 1.00 51.14 C -ANISOU 5966 CD2 LEU D 148 5996 7262 6173 646 -675 -297 C -ATOM 5967 N VAL D 149 -23.151 -21.718 -5.702 1.00 33.87 N -ANISOU 5967 N VAL D 149 3499 4626 4745 -395 -210 -246 N -ATOM 5968 CA VAL D 149 -21.782 -22.175 -5.486 1.00 30.08 C -ANISOU 5968 CA VAL D 149 3152 4018 4259 -467 -141 -80 C -ATOM 5969 C VAL D 149 -21.690 -23.662 -5.138 1.00 30.54 C -ANISOU 5969 C VAL D 149 3205 3974 4426 -611 -64 -176 C -ATOM 5970 O VAL D 149 -20.820 -24.374 -5.648 1.00 34.43 O -ANISOU 5970 O VAL D 149 3738 4441 4903 -604 -72 -160 O -ATOM 5971 CB VAL D 149 -21.079 -21.321 -4.418 1.00 30.60 C -ANISOU 5971 CB VAL D 149 3325 3962 4341 -497 -95 101 C -ATOM 5972 CG1 VAL D 149 -19.774 -21.970 -3.977 1.00 30.34 C -ANISOU 5972 CG1 VAL D 149 3377 3802 4349 -544 -74 162 C -ATOM 5973 CG2 VAL D 149 -20.817 -19.912 -4.975 1.00 33.19 C -ANISOU 5973 CG2 VAL D 149 3698 4329 4585 -364 -104 215 C -ATOM 5974 N ARG D 150 -22.593 -24.129 -4.285 1.00 29.26 N -ANISOU 5974 N ARG D 150 3013 3722 4381 -742 53 -286 N -ATOM 5975 CA ARG D 150 -22.568 -25.517 -3.837 1.00 32.24 C -ANISOU 5975 CA ARG D 150 3470 3920 4859 -881 213 -356 C -ATOM 5976 C ARG D 150 -22.700 -26.524 -4.974 1.00 36.65 C -ANISOU 5976 C ARG D 150 3885 4551 5491 -895 191 -560 C -ATOM 5977 O ARG D 150 -22.273 -27.675 -4.859 1.00 35.39 O -ANISOU 5977 O ARG D 150 3825 4235 5386 -970 298 -574 O -ATOM 5978 CB ARG D 150 -23.659 -25.764 -2.800 1.00 33.18 C -ANISOU 5978 CB ARG D 150 3608 3888 5110 -1039 447 -464 C -ATOM 5979 CG ARG D 150 -23.326 -25.178 -1.441 1.00 36.79 C -ANISOU 5979 CG ARG D 150 4317 4201 5462 -1022 514 -248 C -ATOM 5980 CD ARG D 150 -24.033 -25.915 -0.314 1.00 43.40 C -ANISOU 5980 CD ARG D 150 5350 4768 6372 -1176 853 -297 C -ATOM 5981 NE ARG D 150 -23.590 -25.409 0.980 1.00 49.30 N -ANISOU 5981 NE ARG D 150 6411 5380 6941 -1090 882 -83 N -ATOM 5982 CZ ARG D 150 -24.182 -24.408 1.623 1.00 55.33 C -ANISOU 5982 CZ ARG D 150 7141 6186 7697 -1102 912 -76 C -ATOM 5983 NH1 ARG D 150 -25.251 -23.828 1.090 1.00 49.64 N -ANISOU 5983 NH1 ARG D 150 6087 5637 7139 -1175 903 -270 N -ATOM 5984 NH2 ARG D 150 -23.715 -23.991 2.798 1.00 57.56 N -ANISOU 5984 NH2 ARG D 150 7722 6354 7794 -992 914 94 N -ATOM 5985 N GLN D 151 -23.290 -26.091 -6.077 1.00 37.71 N -ANISOU 5985 N GLN D 151 3809 4917 5602 -783 35 -732 N -ATOM 5986 CA GLN D 151 -23.506 -26.993 -7.202 1.00 41.22 C -ANISOU 5986 CA GLN D 151 4095 5465 6100 -756 -26 -987 C -ATOM 5987 C GLN D 151 -22.201 -27.349 -7.899 1.00 39.86 C -ANISOU 5987 C GLN D 151 4057 5300 5789 -674 -91 -829 C -ATOM 5988 O GLN D 151 -22.150 -28.287 -8.695 1.00 43.22 O -ANISOU 5988 O GLN D 151 4397 5765 6258 -673 -112 -1008 O -ATOM 5989 CB GLN D 151 -24.500 -26.383 -8.187 1.00 47.29 C -ANISOU 5989 CB GLN D 151 4640 6501 6826 -564 -235 -1254 C -ATOM 5990 CG GLN D 151 -25.886 -26.193 -7.591 1.00 53.84 C -ANISOU 5990 CG GLN D 151 5258 7334 7867 -645 -170 -1524 C -ATOM 5991 CD GLN D 151 -26.916 -25.797 -8.625 1.00 67.27 C -ANISOU 5991 CD GLN D 151 6764 9280 9515 -372 -412 -1851 C -ATOM 5992 OE1 GLN D 151 -26.770 -24.780 -9.306 1.00 70.97 O -ANISOU 5992 OE1 GLN D 151 7263 9958 9745 -96 -680 -1795 O -ATOM 5993 NE2 GLN D 151 -27.965 -26.605 -8.756 1.00 72.98 N -ANISOU 5993 NE2 GLN D 151 7317 9965 10446 -400 -309 -2211 N -ATOM 5994 N TYR D 152 -21.147 -26.601 -7.587 1.00 33.64 N -ANISOU 5994 N TYR D 152 3446 4464 4870 -614 -107 -540 N -ATOM 5995 CA TYR D 152 -19.851 -26.796 -8.222 1.00 34.85 C -ANISOU 5995 CA TYR D 152 3690 4615 4939 -548 -133 -430 C -ATOM 5996 C TYR D 152 -18.922 -27.608 -7.345 1.00 30.99 C -ANISOU 5996 C TYR D 152 3317 3917 4541 -640 -60 -345 C -ATOM 5997 O TYR D 152 -17.736 -27.738 -7.641 1.00 32.07 O -ANISOU 5997 O TYR D 152 3498 4028 4660 -591 -83 -285 O -ATOM 5998 CB TYR D 152 -19.234 -25.450 -8.619 1.00 36.62 C -ANISOU 5998 CB TYR D 152 4000 4902 5011 -415 -157 -252 C -ATOM 5999 CG TYR D 152 -20.029 -24.814 -9.735 1.00 44.76 C -ANISOU 5999 CG TYR D 152 5018 6123 5865 -223 -247 -332 C -ATOM 6000 CD1 TYR D 152 -21.099 -23.970 -9.458 1.00 52.31 C -ANISOU 6000 CD1 TYR D 152 5934 7152 6788 -148 -318 -367 C -ATOM 6001 CD2 TYR D 152 -19.754 -25.111 -11.067 1.00 47.75 C -ANISOU 6001 CD2 TYR D 152 5445 6612 6088 -74 -283 -404 C -ATOM 6002 CE1 TYR D 152 -21.856 -23.414 -10.478 1.00 58.16 C -ANISOU 6002 CE1 TYR D 152 6694 8072 7332 113 -461 -478 C -ATOM 6003 CE2 TYR D 152 -20.501 -24.556 -12.095 1.00 53.10 C -ANISOU 6003 CE2 TYR D 152 6183 7464 6530 195 -409 -495 C -ATOM 6004 CZ TYR D 152 -21.549 -23.705 -11.795 1.00 58.12 C -ANISOU 6004 CZ TYR D 152 6787 8172 7124 308 -517 -537 C -ATOM 6005 OH TYR D 152 -22.303 -23.150 -12.812 1.00 59.63 O -ANISOU 6005 OH TYR D 152 7068 8542 7046 658 -699 -659 O -ATOM 6006 N ASN D 153 -19.488 -28.155 -6.274 1.00 29.37 N -ANISOU 6006 N ASN D 153 3183 3549 4430 -749 43 -364 N -ATOM 6007 CA AASN D 153 -18.753 -29.026 -5.359 0.72 29.75 C -ANISOU 6007 CA AASN D 153 3440 3361 4502 -762 107 -287 C -ATOM 6008 CA BASN D 153 -18.765 -29.032 -5.355 0.28 30.02 C -ANISOU 6008 CA BASN D 153 3474 3394 4537 -763 108 -288 C -ATOM 6009 C ASN D 153 -17.437 -28.452 -4.871 1.00 31.06 C -ANISOU 6009 C ASN D 153 3705 3498 4599 -633 -16 -145 C -ATOM 6010 O ASN D 153 -16.382 -29.060 -5.078 1.00 27.70 O -ANISOU 6010 O ASN D 153 3312 3022 4190 -559 -83 -169 O -ATOM 6011 CB AASN D 153 -18.511 -30.388 -6.001 0.72 30.66 C -ANISOU 6011 CB AASN D 153 3547 3410 4694 -794 150 -416 C -ATOM 6012 CB BASN D 153 -18.530 -30.397 -6.005 0.28 31.23 C -ANISOU 6012 CB BASN D 153 3617 3481 4767 -796 152 -419 C -ATOM 6013 CG AASN D 153 -19.792 -31.131 -6.240 0.72 33.52 C -ANISOU 6013 CG AASN D 153 3798 3734 5204 -945 313 -635 C -ATOM 6014 CG BASN D 153 -18.396 -31.518 -4.988 0.28 34.99 C -ANISOU 6014 CG BASN D 153 4372 3646 5277 -820 304 -382 C -ATOM 6015 OD1AASN D 153 -20.805 -30.833 -5.608 0.72 38.47 O -ANISOU 6015 OD1AASN D 153 4410 4308 5897 -1043 445 -681 O -ATOM 6016 OD1BASN D 153 -18.573 -31.316 -3.785 0.28 38.84 O -ANISOU 6016 OD1BASN D 153 5092 3966 5701 -801 391 -261 O -ATOM 6017 ND2AASN D 153 -19.770 -32.094 -7.151 0.72 35.26 N -ANISOU 6017 ND2AASN D 153 3906 3978 5514 -976 322 -819 N -ATOM 6018 ND2BASN D 153 -18.100 -32.715 -5.474 0.28 38.16 N -ANISOU 6018 ND2BASN D 153 4799 3947 5753 -836 354 -483 N -ATOM 6019 N PRO D 154 -17.485 -27.270 -4.218 1.00 26.76 N -ANISOU 6019 N PRO D 154 3172 2985 4010 -601 -53 -49 N -ATOM 6020 CA PRO D 154 -16.239 -26.793 -3.618 1.00 25.68 C -ANISOU 6020 CA PRO D 154 3086 2803 3868 -477 -174 -5 C -ATOM 6021 C PRO D 154 -15.871 -27.730 -2.476 1.00 26.75 C -ANISOU 6021 C PRO D 154 3489 2730 3945 -367 -209 5 C -ATOM 6022 O PRO D 154 -16.733 -28.466 -1.989 1.00 28.16 O -ANISOU 6022 O PRO D 154 3860 2764 4075 -425 -59 38 O -ATOM 6023 CB PRO D 154 -16.615 -25.420 -3.070 1.00 25.72 C -ANISOU 6023 CB PRO D 154 3058 2862 3852 -481 -178 67 C -ATOM 6024 CG PRO D 154 -18.095 -25.509 -2.784 1.00 26.54 C -ANISOU 6024 CG PRO D 154 3205 2958 3923 -584 -57 85 C -ATOM 6025 CD PRO D 154 -18.649 -26.444 -3.840 1.00 26.88 C -ANISOU 6025 CD PRO D 154 3151 3052 4011 -664 9 -25 C -ATOM 6026 N LYS D 155 -14.616 -27.714 -2.047 1.00 29.98 N -ANISOU 6026 N LYS D 155 3929 3100 4361 -188 -386 -54 N -ATOM 6027 CA LYS D 155 -14.226 -28.532 -0.895 1.00 33.75 C -ANISOU 6027 CA LYS D 155 4742 3376 4707 27 -477 -50 C -ATOM 6028 C LYS D 155 -14.923 -28.016 0.363 1.00 32.06 C -ANISOU 6028 C LYS D 155 4774 3072 4337 77 -428 59 C -ATOM 6029 O LYS D 155 -15.319 -28.781 1.244 1.00 32.03 O -ANISOU 6029 O LYS D 155 5167 2845 4158 176 -325 144 O -ATOM 6030 CB LYS D 155 -12.710 -28.497 -0.713 1.00 36.56 C -ANISOU 6030 CB LYS D 155 5015 3752 5124 268 -751 -228 C -ATOM 6031 CG LYS D 155 -12.191 -29.238 0.504 1.00 38.38 C -ANISOU 6031 CG LYS D 155 5630 3792 5160 614 -938 -260 C -ATOM 6032 CD LYS D 155 -10.679 -29.361 0.438 1.00 47.02 C -ANISOU 6032 CD LYS D 155 6546 4939 6378 869 -1249 -539 C -ATOM 6033 CE LYS D 155 -10.132 -30.152 1.614 1.00 53.47 C -ANISOU 6033 CE LYS D 155 7795 5573 6949 1321 -1508 -603 C -ATOM 6034 NZ LYS D 155 -10.719 -31.514 1.643 1.00 58.34 N -ANISOU 6034 NZ LYS D 155 8855 5940 7371 1346 -1314 -402 N -ATOM 6035 N MET D 156 -15.045 -26.698 0.446 1.00 29.03 N -ANISOU 6035 N MET D 156 4187 2834 4010 18 -468 56 N -ATOM 6036 CA MET D 156 -15.804 -26.050 1.510 1.00 31.43 C -ANISOU 6036 CA MET D 156 4664 3088 4191 30 -404 145 C -ATOM 6037 C MET D 156 -16.155 -24.660 1.010 1.00 31.44 C -ANISOU 6037 C MET D 156 4342 3277 4328 -128 -382 144 C -ATOM 6038 O MET D 156 -15.512 -24.130 0.093 1.00 27.89 O -ANISOU 6038 O MET D 156 3614 2952 4032 -172 -438 70 O -ATOM 6039 CB MET D 156 -15.005 -25.964 2.823 1.00 34.10 C -ANISOU 6039 CB MET D 156 5264 3332 4359 355 -629 89 C -ATOM 6040 CG MET D 156 -13.961 -24.858 2.859 1.00 36.91 C -ANISOU 6040 CG MET D 156 5310 3846 4869 460 -885 -103 C -ATOM 6041 SD MET D 156 -13.208 -24.590 4.491 1.00 38.55 S -ANISOU 6041 SD MET D 156 5780 3992 4873 890 -1210 -261 S -ATOM 6042 CE MET D 156 -12.393 -26.151 4.743 1.00 35.69 C -ANISOU 6042 CE MET D 156 5772 3467 4323 1244 -1398 -328 C -ATOM 6043 N VAL D 157 -17.200 -24.080 1.578 1.00 27.31 N -ANISOU 6043 N VAL D 157 3886 2744 3746 -209 -258 223 N -ATOM 6044 CA VAL D 157 -17.546 -22.711 1.241 1.00 24.40 C -ANISOU 6044 CA VAL D 157 3270 2522 3479 -306 -252 228 C -ATOM 6045 C VAL D 157 -17.903 -21.981 2.528 1.00 28.08 C -ANISOU 6045 C VAL D 157 3879 2940 3850 -237 -261 254 C -ATOM 6046 O VAL D 157 -18.671 -22.488 3.349 1.00 28.18 O -ANISOU 6046 O VAL D 157 4156 2826 3725 -238 -124 314 O -ATOM 6047 CB VAL D 157 -18.657 -22.620 0.139 1.00 31.87 C -ANISOU 6047 CB VAL D 157 4042 3575 4493 -487 -104 250 C -ATOM 6048 CG1 VAL D 157 -19.895 -23.421 0.522 1.00 38.83 C -ANISOU 6048 CG1 VAL D 157 5051 4361 5340 -595 87 243 C -ATOM 6049 CG2 VAL D 157 -19.002 -21.159 -0.169 1.00 24.38 C -ANISOU 6049 CG2 VAL D 157 2919 2745 3599 -513 -110 272 C -ATOM 6050 N LYS D 158 -17.278 -20.820 2.728 1.00 24.35 N -ANISOU 6050 N LYS D 158 3248 2539 3464 -175 -390 187 N -ATOM 6051 CA LYS D 158 -17.469 -20.020 3.927 1.00 23.12 C -ANISOU 6051 CA LYS D 158 3192 2359 3233 -86 -439 170 C -ATOM 6052 C LYS D 158 -17.718 -18.593 3.499 1.00 26.38 C -ANISOU 6052 C LYS D 158 3342 2870 3813 -199 -395 164 C -ATOM 6053 O LYS D 158 -17.260 -18.174 2.434 1.00 26.14 O -ANISOU 6053 O LYS D 158 3093 2892 3945 -271 -367 141 O -ATOM 6054 CB LYS D 158 -16.222 -20.037 4.820 1.00 24.88 C -ANISOU 6054 CB LYS D 158 3496 2546 3412 183 -700 1 C -ATOM 6055 CG LYS D 158 -15.776 -21.402 5.313 1.00 34.82 C -ANISOU 6055 CG LYS D 158 5088 3684 4460 403 -800 -6 C -ATOM 6056 CD LYS D 158 -16.747 -21.963 6.319 1.00 40.65 C -ANISOU 6056 CD LYS D 158 6282 4262 4902 463 -632 152 C -ATOM 6057 CE LYS D 158 -16.160 -23.171 7.028 1.00 46.07 C -ANISOU 6057 CE LYS D 158 7421 4771 5312 786 -742 148 C -ATOM 6058 NZ LYS D 158 -17.121 -23.676 8.033 1.00 50.21 N -ANISOU 6058 NZ LYS D 158 8476 5072 5529 839 -473 322 N -ATOM 6059 N VAL D 159 -18.436 -17.847 4.330 1.00 21.97 N -ANISOU 6059 N VAL D 159 2843 2305 3200 -201 -355 188 N -ATOM 6060 CA VAL D 159 -18.748 -16.462 4.009 1.00 21.23 C -ANISOU 6060 CA VAL D 159 2543 2272 3251 -284 -304 190 C -ATOM 6061 C VAL D 159 -18.198 -15.550 5.087 1.00 24.35 C -ANISOU 6061 C VAL D 159 2920 2644 3686 -170 -424 60 C -ATOM 6062 O VAL D 159 -18.433 -15.793 6.278 1.00 23.25 O -ANISOU 6062 O VAL D 159 3001 2467 3367 -51 -484 39 O -ATOM 6063 CB VAL D 159 -20.266 -16.247 3.898 1.00 25.28 C -ANISOU 6063 CB VAL D 159 3069 2819 3716 -396 -150 286 C -ATOM 6064 CG1 VAL D 159 -20.587 -14.776 3.642 1.00 22.93 C -ANISOU 6064 CG1 VAL D 159 2612 2564 3537 -419 -122 291 C -ATOM 6065 CG2 VAL D 159 -20.831 -17.130 2.794 1.00 26.70 C -ANISOU 6065 CG2 VAL D 159 3209 3044 3892 -484 -67 326 C -ATOM 6066 N ALA D 160 -17.455 -14.515 4.673 1.00 21.14 N -ANISOU 6066 N ALA D 160 2276 2238 3517 -198 -429 -50 N -ATOM 6067 CA ALA D 160 -17.029 -13.458 5.586 1.00 23.29 C -ANISOU 6067 CA ALA D 160 2455 2491 3905 -123 -516 -230 C -ATOM 6068 C ALA D 160 -17.800 -12.210 5.192 1.00 27.05 C -ANISOU 6068 C ALA D 160 2837 2950 4492 -252 -334 -130 C -ATOM 6069 O ALA D 160 -17.828 -11.826 4.016 1.00 25.00 O -ANISOU 6069 O ALA D 160 2495 2660 4346 -353 -168 -36 O -ATOM 6070 CB ALA D 160 -15.529 -13.207 5.501 1.00 23.59 C -ANISOU 6070 CB ALA D 160 2256 2497 4211 -65 -620 -522 C -ATOM 6071 N SER D 161 -18.441 -11.577 6.164 1.00 24.19 N -ANISOU 6071 N SER D 161 2530 2594 4065 -214 -360 -147 N -ATOM 6072 CA SER D 161 -19.184 -10.358 5.885 1.00 22.99 C -ANISOU 6072 CA SER D 161 2301 2417 4017 -298 -212 -72 C -ATOM 6073 C SER D 161 -18.714 -9.296 6.850 1.00 26.97 C -ANISOU 6073 C SER D 161 2698 2874 4675 -246 -275 -281 C -ATOM 6074 O SER D 161 -18.646 -9.543 8.060 1.00 26.68 O -ANISOU 6074 O SER D 161 2756 2879 4502 -117 -443 -405 O -ATOM 6075 CB SER D 161 -20.699 -10.584 6.043 1.00 23.52 C -ANISOU 6075 CB SER D 161 2499 2546 3891 -327 -152 83 C -ATOM 6076 OG SER D 161 -21.416 -9.402 5.721 1.00 27.01 O -ANISOU 6076 OG SER D 161 2865 2970 4429 -356 -52 131 O -ATOM 6077 N LEU D 162 -18.368 -8.118 6.338 1.00 23.13 N -ANISOU 6077 N LEU D 162 2046 2280 4462 -324 -123 -338 N -ATOM 6078 CA LEU D 162 -17.889 -7.070 7.225 1.00 22.73 C -ANISOU 6078 CA LEU D 162 1844 2168 4623 -295 -162 -595 C -ATOM 6079 C LEU D 162 -18.945 -6.754 8.273 1.00 26.75 C -ANISOU 6079 C LEU D 162 2476 2748 4940 -228 -242 -552 C -ATOM 6080 O LEU D 162 -18.628 -6.625 9.461 1.00 23.59 O -ANISOU 6080 O LEU D 162 2067 2387 4509 -105 -421 -775 O -ATOM 6081 CB LEU D 162 -17.562 -5.785 6.473 1.00 22.71 C -ANISOU 6081 CB LEU D 162 1699 1973 4957 -420 119 -628 C -ATOM 6082 CG LEU D 162 -17.177 -4.647 7.423 1.00 25.91 C -ANISOU 6082 CG LEU D 162 1920 2299 5626 -412 104 -930 C -ATOM 6083 CD1 LEU D 162 -15.872 -4.953 8.161 1.00 28.10 C -ANISOU 6083 CD1 LEU D 162 2016 2636 6025 -291 -100 -1330 C -ATOM 6084 CD2 LEU D 162 -17.086 -3.315 6.696 1.00 29.45 C -ANISOU 6084 CD2 LEU D 162 2377 2551 6260 -472 457 -874 C -ATOM 6085 N LEU D 163 -20.193 -6.633 7.818 1.00 23.81 N -ANISOU 6085 N LEU D 163 2213 2395 4438 -283 -117 -305 N -ATOM 6086 CA LEU D 163 -21.294 -6.203 8.676 1.00 24.32 C -ANISOU 6086 CA LEU D 163 2353 2506 4381 -254 -124 -284 C -ATOM 6087 C LEU D 163 -22.440 -7.196 8.609 1.00 24.37 C -ANISOU 6087 C LEU D 163 2519 2607 4135 -272 -95 -119 C -ATOM 6088 O LEU D 163 -22.719 -7.771 7.553 1.00 23.32 O -ANISOU 6088 O LEU D 163 2391 2497 3972 -319 -39 15 O -ATOM 6089 CB LEU D 163 -21.810 -4.818 8.253 1.00 26.47 C -ANISOU 6089 CB LEU D 163 2537 2682 4837 -294 25 -243 C -ATOM 6090 CG LEU D 163 -20.815 -3.661 8.126 1.00 27.28 C -ANISOU 6090 CG LEU D 163 2481 2612 5273 -329 126 -405 C -ATOM 6091 CD1 LEU D 163 -21.507 -2.395 7.628 1.00 29.78 C -ANISOU 6091 CD1 LEU D 163 2818 2790 5706 -337 317 -297 C -ATOM 6092 CD2 LEU D 163 -20.104 -3.376 9.441 1.00 29.82 C -ANISOU 6092 CD2 LEU D 163 2680 2953 5697 -273 -33 -725 C -ATOM 6093 N VAL D 164 -23.099 -7.404 9.740 1.00 23.39 N -ANISOU 6093 N VAL D 164 2526 2520 3842 -235 -103 -163 N -ATOM 6094 CA VAL D 164 -24.334 -8.185 9.770 1.00 24.91 C -ANISOU 6094 CA VAL D 164 2831 2754 3880 -300 24 -72 C -ATOM 6095 C VAL D 164 -25.345 -7.339 10.507 1.00 29.82 C -ANISOU 6095 C VAL D 164 3428 3382 4522 -312 110 -141 C -ATOM 6096 O VAL D 164 -25.066 -6.876 11.615 1.00 28.62 O -ANISOU 6096 O VAL D 164 3357 3207 4309 -233 63 -245 O -ATOM 6097 CB VAL D 164 -24.170 -9.511 10.527 1.00 30.33 C -ANISOU 6097 CB VAL D 164 3796 3415 4314 -256 43 -61 C -ATOM 6098 CG1 VAL D 164 -25.543 -10.135 10.847 1.00 33.54 C -ANISOU 6098 CG1 VAL D 164 4323 3799 4623 -364 290 -36 C -ATOM 6099 CG2 VAL D 164 -23.329 -10.474 9.739 1.00 25.74 C -ANISOU 6099 CG2 VAL D 164 3233 2831 3717 -246 -34 1 C -ATOM 6100 N LYS D 165 -26.506 -7.125 9.888 1.00 31.35 N -ANISOU 6100 N LYS D 165 3495 3615 4803 -380 209 -124 N -ATOM 6101 CA LYS D 165 -27.560 -6.301 10.488 1.00 36.99 C -ANISOU 6101 CA LYS D 165 4136 4340 5577 -390 292 -225 C -ATOM 6102 C LYS D 165 -28.484 -7.118 11.379 1.00 37.80 C -ANISOU 6102 C LYS D 165 4372 4434 5558 -478 500 -301 C -ATOM 6103 O LYS D 165 -28.925 -8.210 10.995 1.00 36.80 O -ANISOU 6103 O LYS D 165 4272 4306 5404 -570 625 -296 O -ATOM 6104 CB LYS D 165 -28.397 -5.614 9.401 1.00 38.93 C -ANISOU 6104 CB LYS D 165 4173 4633 5986 -360 268 -234 C -ATOM 6105 CG LYS D 165 -28.050 -4.162 9.195 1.00 43.58 C -ANISOU 6105 CG LYS D 165 4696 5156 6708 -260 195 -216 C -ATOM 6106 CD LYS D 165 -29.056 -3.448 8.291 1.00 41.18 C -ANISOU 6106 CD LYS D 165 4273 4879 6494 -144 161 -236 C -ATOM 6107 CE LYS D 165 -28.443 -2.163 7.782 1.00 35.99 C -ANISOU 6107 CE LYS D 165 3660 4078 5936 -25 145 -141 C -ATOM 6108 NZ LYS D 165 -29.331 -1.388 6.882 1.00 31.94 N -ANISOU 6108 NZ LYS D 165 3135 3554 5445 182 89 -135 N -ATOM 6109 N ARG D 166 -28.770 -6.601 12.573 1.00 42.83 N -ANISOU 6109 N ARG D 166 3679 5755 6841 -359 1166 -489 N -ATOM 6110 CA ARG D 166 -29.837 -7.167 13.391 1.00 44.72 C -ANISOU 6110 CA ARG D 166 3812 6062 7118 -479 1350 -530 C -ATOM 6111 C ARG D 166 -31.164 -6.665 12.840 1.00 48.16 C -ANISOU 6111 C ARG D 166 3897 6692 7710 -406 1362 -536 C -ATOM 6112 O ARG D 166 -31.457 -5.471 12.916 1.00 48.36 O -ANISOU 6112 O ARG D 166 3836 6736 7802 -203 1403 -524 O -ATOM 6113 CB ARG D 166 -29.704 -6.738 14.853 1.00 44.84 C -ANISOU 6113 CB ARG D 166 4002 5968 7068 -447 1549 -549 C -ATOM 6114 CG ARG D 166 -28.471 -7.271 15.583 1.00 38.86 C -ANISOU 6114 CG ARG D 166 3580 5035 6149 -529 1535 -533 C -ATOM 6115 CD ARG D 166 -28.603 -6.997 17.091 1.00 38.13 C -ANISOU 6115 CD ARG D 166 3655 4857 5975 -543 1746 -559 C -ATOM 6116 NE ARG D 166 -28.558 -5.566 17.380 1.00 36.61 N -ANISOU 6116 NE ARG D 166 3486 4628 5795 -356 1794 -569 N -ATOM 6117 CZ ARG D 166 -27.438 -4.855 17.431 1.00 39.27 C -ANISOU 6117 CZ ARG D 166 4022 4849 6052 -273 1685 -544 C -ATOM 6118 NH1 ARG D 166 -26.271 -5.449 17.213 1.00 31.49 N -ANISOU 6118 NH1 ARG D 166 3190 3794 4980 -343 1523 -502 N -ATOM 6119 NH2 ARG D 166 -27.483 -3.556 17.700 1.00 43.71 N -ANISOU 6119 NH2 ARG D 166 4626 5361 6620 -120 1744 -560 N -ATOM 6120 N THR D 167 -31.962 -7.567 12.278 1.00 53.47 N -ANISOU 6120 N THR D 167 4371 7504 8440 -570 1321 -552 N -ATOM 6121 CA THR D 167 -33.249 -7.191 11.692 1.00 56.75 C -ANISOU 6121 CA THR D 167 4411 8139 9012 -518 1300 -548 C -ATOM 6122 C THR D 167 -34.275 -8.305 11.856 1.00 59.12 C -ANISOU 6122 C THR D 167 4563 8568 9331 -759 1360 -568 C -ATOM 6123 O THR D 167 -33.930 -9.485 11.804 1.00 57.73 O -ANISOU 6123 O THR D 167 4526 8330 9080 -990 1342 -599 O -ATOM 6124 CB THR D 167 -33.114 -6.819 10.191 1.00 58.58 C -ANISOU 6124 CB THR D 167 4538 8449 9271 -426 1033 -504 C -ATOM 6125 OG1 THR D 167 -34.412 -6.775 9.579 1.00 60.31 O -ANISOU 6125 OG1 THR D 167 4421 8898 9597 -428 960 -478 O -ATOM 6126 CG2 THR D 167 -32.259 -7.841 9.460 1.00 56.47 C -ANISOU 6126 CG2 THR D 167 4472 8102 8883 -596 877 -510 C -ATOM 6127 N PRO D 168 -35.546 -7.931 12.073 1.00 63.70 N -ANISOU 6127 N PRO D 168 4895 9316 9991 -696 1428 -536 N -ATOM 6128 CA PRO D 168 -36.619 -8.931 12.110 1.00 65.66 C -ANISOU 6128 CA PRO D 168 4986 9705 10254 -922 1451 -527 C -ATOM 6129 C PRO D 168 -36.875 -9.565 10.731 1.00 65.51 C -ANISOU 6129 C PRO D 168 4837 9805 10250 -1060 1195 -504 C -ATOM 6130 O PRO D 168 -37.408 -10.675 10.657 1.00 62.82 O -ANISOU 6130 O PRO D 168 4468 9510 9890 -1316 1185 -513 O -ATOM 6131 CB PRO D 168 -37.839 -8.122 12.578 1.00 70.12 C -ANISOU 6131 CB PRO D 168 5284 10437 10922 -761 1575 -482 C -ATOM 6132 CG PRO D 168 -37.515 -6.694 12.236 1.00 68.57 C -ANISOU 6132 CG PRO D 168 5057 10224 10771 -439 1516 -455 C -ATOM 6133 CD PRO D 168 -36.030 -6.577 12.401 1.00 64.28 C -ANISOU 6133 CD PRO D 168 4843 9440 10141 -415 1511 -504 C -ATOM 6134 N ARG D 169 -36.488 -8.868 9.661 1.00 67.32 N -ANISOU 6134 N ARG D 169 5013 10063 10502 -902 992 -476 N -ATOM 6135 CA ARG D 169 -36.649 -9.367 8.293 1.00 69.27 C -ANISOU 6135 CA ARG D 169 5170 10410 10742 -1022 736 -459 C -ATOM 6136 C ARG D 169 -35.625 -10.445 7.928 1.00 68.91 C -ANISOU 6136 C ARG D 169 5403 10206 10572 -1235 673 -531 C -ATOM 6137 O ARG D 169 -35.570 -10.890 6.779 1.00 68.61 O -ANISOU 6137 O ARG D 169 5359 10215 10495 -1343 468 -538 O -ATOM 6138 CB ARG D 169 -36.524 -8.226 7.278 1.00 71.26 C -ANISOU 6138 CB ARG D 169 5307 10732 11037 -773 543 -402 C -ATOM 6139 CG ARG D 169 -37.765 -7.368 7.070 1.00 78.90 C -ANISOU 6139 CG ARG D 169 5943 11910 12125 -598 503 -303 C -ATOM 6140 CD ARG D 169 -37.417 -6.180 6.181 1.00 81.75 C -ANISOU 6140 CD ARG D 169 6279 12284 12498 -325 333 -247 C -ATOM 6141 NE ARG D 169 -36.144 -5.591 6.590 1.00 81.19 N -ANISOU 6141 NE ARG D 169 6483 11990 12375 -179 418 -297 N -ATOM 6142 CZ ARG D 169 -35.210 -5.153 5.752 1.00 79.25 C -ANISOU 6142 CZ ARG D 169 6375 11649 12086 -83 261 -293 C -ATOM 6143 NH1 ARG D 169 -35.407 -5.228 4.442 1.00 79.38 N -ANISOU 6143 NH1 ARG D 169 6298 11780 12083 -110 8 -253 N -ATOM 6144 NH2 ARG D 169 -34.077 -4.641 6.227 1.00 75.33 N -ANISOU 6144 NH2 ARG D 169 6123 10940 11558 30 353 -320 N -ATOM 6145 N SER D 170 -34.803 -10.847 8.894 1.00 67.13 N -ANISOU 6145 N SER D 170 5438 9791 10278 -1287 848 -580 N -ATOM 6146 CA SER D 170 -33.782 -11.870 8.662 1.00 65.24 C -ANISOU 6146 CA SER D 170 5482 9383 9923 -1464 818 -636 C -ATOM 6147 C SER D 170 -34.403 -13.247 8.411 1.00 64.09 C -ANISOU 6147 C SER D 170 5369 9262 9721 -1768 790 -661 C -ATOM 6148 O SER D 170 -35.295 -13.675 9.144 1.00 63.35 O -ANISOU 6148 O SER D 170 5200 9219 9652 -1884 916 -651 O -ATOM 6149 CB SER D 170 -32.822 -11.939 9.852 1.00 65.70 C -ANISOU 6149 CB SER D 170 5844 9221 9898 -1411 994 -637 C -ATOM 6150 OG SER D 170 -31.903 -13.005 9.712 1.00 67.56 O -ANISOU 6150 OG SER D 170 6397 9275 9998 -1540 959 -651 O -ATOM 6151 N VAL D 171 -33.931 -13.933 7.370 1.00 63.25 N -ANISOU 6151 N VAL D 171 5391 9109 9533 -1899 632 -697 N -ATOM 6152 CA VAL D 171 -34.407 -15.286 7.069 1.00 64.82 C -ANISOU 6152 CA VAL D 171 5686 9286 9657 -2195 600 -731 C -ATOM 6153 C VAL D 171 -33.654 -16.295 7.926 1.00 60.63 C -ANISOU 6153 C VAL D 171 5502 8514 9021 -2324 770 -766 C -ATOM 6154 O VAL D 171 -33.947 -17.494 7.907 1.00 62.43 O -ANISOU 6154 O VAL D 171 5881 8666 9172 -2561 789 -794 O -ATOM 6155 CB VAL D 171 -34.230 -15.660 5.580 1.00 65.16 C -ANISOU 6155 CB VAL D 171 5774 9356 9626 -2295 367 -762 C -ATOM 6156 CG1 VAL D 171 -34.945 -14.658 4.677 1.00 67.06 C -ANISOU 6156 CG1 VAL D 171 5694 9829 9956 -2159 171 -711 C -ATOM 6157 CG2 VAL D 171 -32.742 -15.777 5.224 1.00 62.11 C -ANISOU 6157 CG2 VAL D 171 5720 8757 9123 -2200 344 -782 C -ATOM 6158 N GLY D 172 -32.669 -15.798 8.666 1.00 55.67 N -ANISOU 6158 N GLY D 172 5023 7748 8380 -2150 880 -752 N -ATOM 6159 CA GLY D 172 -31.939 -16.626 9.601 1.00 55.62 C -ANISOU 6159 CA GLY D 172 5356 7508 8269 -2213 1028 -751 C -ATOM 6160 C GLY D 172 -30.550 -17.033 9.148 1.00 53.96 C -ANISOU 6160 C GLY D 172 5481 7083 7936 -2113 943 -734 C -ATOM 6161 O GLY D 172 -29.916 -17.855 9.815 1.00 56.08 O -ANISOU 6161 O GLY D 172 6043 7150 8114 -2163 1041 -725 O -ATOM 6162 N TYR D 173 -30.067 -16.481 8.031 1.00 44.64 N -ANISOU 6162 N TYR D 173 4264 5944 6752 -1968 770 -724 N -ATOM 6163 CA TYR D 173 -28.695 -16.788 7.594 1.00 42.40 C -ANISOU 6163 CA TYR D 173 4274 5471 6366 -1849 713 -705 C -ATOM 6164 C TYR D 173 -27.632 -16.055 8.408 1.00 43.47 C -ANISOU 6164 C TYR D 173 4509 5510 6497 -1605 766 -640 C -ATOM 6165 O TYR D 173 -27.670 -14.835 8.530 1.00 48.86 O -ANISOU 6165 O TYR D 173 5021 6296 7248 -1437 741 -609 O -ATOM 6166 CB TYR D 173 -28.445 -16.499 6.101 1.00 40.16 C -ANISOU 6166 CB TYR D 173 3955 5248 6055 -1789 529 -716 C -ATOM 6167 CG TYR D 173 -26.992 -16.770 5.763 1.00 38.30 C -ANISOU 6167 CG TYR D 173 4004 4823 5726 -1648 514 -693 C -ATOM 6168 CD1 TYR D 173 -26.535 -18.073 5.611 1.00 42.05 C -ANISOU 6168 CD1 TYR D 173 4764 5112 6102 -1764 560 -727 C -ATOM 6169 CD2 TYR D 173 -26.070 -15.740 5.656 1.00 38.61 C -ANISOU 6169 CD2 TYR D 173 4027 4860 5782 -1398 472 -636 C -ATOM 6170 CE1 TYR D 173 -25.206 -18.343 5.347 1.00 37.94 C -ANISOU 6170 CE1 TYR D 173 4479 4424 5513 -1610 567 -701 C -ATOM 6171 CE2 TYR D 173 -24.734 -16.001 5.389 1.00 36.86 C -ANISOU 6171 CE2 TYR D 173 4028 4486 5492 -1273 473 -610 C -ATOM 6172 CZ TYR D 173 -24.320 -17.309 5.234 1.00 37.51 C -ANISOU 6172 CZ TYR D 173 4365 4401 5489 -1368 523 -642 C -ATOM 6173 OH TYR D 173 -23.009 -17.588 4.973 1.00 37.01 O -ANISOU 6173 OH TYR D 173 4496 4193 5372 -1221 540 -612 O -ATOM 6174 N LYS D 174 -26.657 -16.798 8.922 1.00 44.68 N -ANISOU 6174 N LYS D 174 4948 5462 6565 -1585 827 -617 N -ATOM 6175 CA LYS D 174 -25.513 -16.193 9.600 1.00 44.28 C -ANISOU 6175 CA LYS D 174 5003 5324 6498 -1371 841 -550 C -ATOM 6176 C LYS D 174 -24.214 -16.573 8.891 1.00 33.44 C -ANISOU 6176 C LYS D 174 3821 3823 5062 -1254 767 -525 C -ATOM 6177 O LYS D 174 -23.994 -17.742 8.569 1.00 36.12 O -ANISOU 6177 O LYS D 174 4356 4033 5336 -1346 786 -547 O -ATOM 6178 CB LYS D 174 -25.460 -16.622 11.068 1.00 52.13 C -ANISOU 6178 CB LYS D 174 6148 6209 7449 -1419 982 -523 C -ATOM 6179 CG LYS D 174 -26.646 -16.152 11.902 1.00 57.70 C -ANISOU 6179 CG LYS D 174 6675 7036 8214 -1510 1097 -544 C -ATOM 6180 CD LYS D 174 -26.646 -16.794 13.287 1.00 62.66 C -ANISOU 6180 CD LYS D 174 7505 7536 8766 -1602 1252 -522 C -ATOM 6181 CE LYS D 174 -27.880 -16.395 14.094 1.00 67.02 C -ANISOU 6181 CE LYS D 174 7881 8211 9372 -1707 1404 -552 C -ATOM 6182 NZ LYS D 174 -28.158 -17.344 15.221 1.00 70.68 N -ANISOU 6182 NZ LYS D 174 8552 8554 9748 -1885 1573 -545 N -ATOM 6183 N PRO D 175 -23.345 -15.583 8.641 1.00 30.94 N -ANISOU 6183 N PRO D 175 3452 3536 4766 -1053 695 -480 N -ATOM 6184 CA PRO D 175 -22.102 -15.885 7.925 1.00 28.15 C -ANISOU 6184 CA PRO D 175 3243 3085 4368 -936 643 -454 C -ATOM 6185 C PRO D 175 -21.095 -16.550 8.857 1.00 30.53 C -ANISOU 6185 C PRO D 175 3754 3222 4623 -868 702 -396 C -ATOM 6186 O PRO D 175 -21.293 -16.568 10.067 1.00 33.16 O -ANISOU 6186 O PRO D 175 4125 3527 4948 -900 764 -370 O -ATOM 6187 CB PRO D 175 -21.605 -14.503 7.491 1.00 28.92 C -ANISOU 6187 CB PRO D 175 3192 3285 4511 -770 561 -418 C -ATOM 6188 CG PRO D 175 -22.171 -13.567 8.482 1.00 29.79 C -ANISOU 6188 CG PRO D 175 3173 3474 4673 -754 594 -403 C -ATOM 6189 CD PRO D 175 -23.494 -14.144 8.916 1.00 29.54 C -ANISOU 6189 CD PRO D 175 3087 3480 4656 -933 669 -454 C -ATOM 6190 N ASP D 176 -20.028 -17.094 8.293 1.00 29.78 N -ANISOU 6190 N ASP D 176 3796 3024 4494 -767 684 -372 N -ATOM 6191 CA ASP D 176 -19.054 -17.822 9.083 1.00 30.98 C -ANISOU 6191 CA ASP D 176 4141 3023 4609 -679 724 -306 C -ATOM 6192 C ASP D 176 -18.103 -16.876 9.796 1.00 31.55 C -ANISOU 6192 C ASP D 176 4137 3141 4710 -519 674 -223 C -ATOM 6193 O ASP D 176 -17.651 -17.156 10.902 1.00 30.86 O -ANISOU 6193 O ASP D 176 4157 2976 4591 -483 688 -159 O -ATOM 6194 CB ASP D 176 -18.287 -18.778 8.176 1.00 30.19 C -ANISOU 6194 CB ASP D 176 4204 2795 4472 -610 740 -312 C -ATOM 6195 CG ASP D 176 -19.203 -19.719 7.442 1.00 35.94 C -ANISOU 6195 CG ASP D 176 5043 3463 5151 -795 782 -404 C -ATOM 6196 OD1 ASP D 176 -19.575 -20.744 8.038 1.00 36.61 O -ANISOU 6196 OD1 ASP D 176 5312 3411 5187 -909 856 -413 O -ATOM 6197 OD2 ASP D 176 -19.568 -19.421 6.284 1.00 30.96 O -ANISOU 6197 OD2 ASP D 176 4327 2919 4517 -842 736 -466 O -ATOM 6198 N PHE D 177 -17.819 -15.743 9.160 1.00 25.92 N -ANISOU 6198 N PHE D 177 3254 2550 4045 -438 607 -221 N -ATOM 6199 CA PHE D 177 -16.926 -14.747 9.738 1.00 25.05 C -ANISOU 6199 CA PHE D 177 3068 2490 3960 -318 551 -151 C -ATOM 6200 C PHE D 177 -17.630 -13.396 9.695 1.00 29.51 C -ANISOU 6200 C PHE D 177 3463 3187 4565 -347 522 -180 C -ATOM 6201 O PHE D 177 -18.157 -13.016 8.647 1.00 28.89 O -ANISOU 6201 O PHE D 177 3283 3183 4511 -366 500 -226 O -ATOM 6202 CB PHE D 177 -15.628 -14.695 8.928 1.00 25.79 C -ANISOU 6202 CB PHE D 177 3144 2581 4076 -173 511 -107 C -ATOM 6203 CG PHE D 177 -14.948 -16.034 8.785 1.00 28.11 C -ANISOU 6203 CG PHE D 177 3600 2738 4343 -107 556 -81 C -ATOM 6204 CD1 PHE D 177 -14.245 -16.584 9.857 1.00 27.20 C -ANISOU 6204 CD1 PHE D 177 3589 2536 4209 -36 550 0 C -ATOM 6205 CD2 PHE D 177 -15.031 -16.750 7.600 1.00 26.34 C -ANISOU 6205 CD2 PHE D 177 3447 2461 4100 -112 605 -136 C -ATOM 6206 CE1 PHE D 177 -13.631 -17.815 9.746 1.00 28.69 C -ANISOU 6206 CE1 PHE D 177 3939 2584 4379 54 596 34 C -ATOM 6207 CE2 PHE D 177 -14.410 -17.983 7.476 1.00 30.13 C -ANISOU 6207 CE2 PHE D 177 4105 2788 4553 -33 667 -117 C -ATOM 6208 CZ PHE D 177 -13.709 -18.516 8.558 1.00 29.20 C -ANISOU 6208 CZ PHE D 177 4080 2581 4435 62 665 -28 C -ATOM 6209 N VAL D 178 -17.645 -12.669 10.814 1.00 24.12 N -ANISOU 6209 N VAL D 178 2766 2522 3876 -345 521 -153 N -ATOM 6210 CA VAL D 178 -18.398 -11.422 10.894 1.00 25.77 C -ANISOU 6210 CA VAL D 178 2845 2828 4120 -358 521 -184 C -ATOM 6211 C VAL D 178 -17.541 -10.331 11.491 1.00 25.88 C -ANISOU 6211 C VAL D 178 2854 2853 4128 -284 469 -134 C -ATOM 6212 O VAL D 178 -17.002 -10.509 12.582 1.00 25.87 O -ANISOU 6212 O VAL D 178 2959 2796 4075 -288 465 -92 O -ATOM 6213 CB VAL D 178 -19.605 -11.575 11.833 1.00 29.45 C -ANISOU 6213 CB VAL D 178 3321 3295 4573 -465 615 -225 C -ATOM 6214 CG1 VAL D 178 -20.422 -10.296 11.852 1.00 28.92 C -ANISOU 6214 CG1 VAL D 178 3109 3323 4556 -445 633 -258 C -ATOM 6215 CG2 VAL D 178 -20.461 -12.730 11.422 1.00 38.01 C -ANISOU 6215 CG2 VAL D 178 4422 4363 5656 -583 669 -273 C -ATOM 6216 N GLY D 179 -17.434 -9.191 10.817 1.00 22.96 N -ANISOU 6216 N GLY D 179 2379 2548 3796 -230 424 -136 N -ATOM 6217 CA GLY D 179 -16.699 -8.080 11.385 1.00 23.47 C -ANISOU 6217 CA GLY D 179 2456 2614 3849 -192 379 -98 C -ATOM 6218 C GLY D 179 -17.466 -7.448 12.533 1.00 28.13 C -ANISOU 6218 C GLY D 179 3090 3189 4410 -233 440 -128 C -ATOM 6219 O GLY D 179 -17.025 -7.497 13.690 1.00 24.79 O -ANISOU 6219 O GLY D 179 2783 2715 3920 -264 439 -103 O -ATOM 6220 N PHE D 180 -18.628 -6.870 12.207 1.00 24.50 N -ANISOU 6220 N PHE D 180 2539 2775 3996 -226 496 -180 N -ATOM 6221 CA PHE D 180 -19.420 -6.105 13.157 1.00 24.05 C -ANISOU 6221 CA PHE D 180 2506 2706 3926 -234 583 -215 C -ATOM 6222 C PHE D 180 -20.892 -6.468 13.048 1.00 28.53 C -ANISOU 6222 C PHE D 180 2964 3331 4547 -263 682 -270 C -ATOM 6223 O PHE D 180 -21.405 -6.695 11.949 1.00 30.33 O -ANISOU 6223 O PHE D 180 3058 3630 4836 -252 648 -283 O -ATOM 6224 CB PHE D 180 -19.230 -4.604 12.895 1.00 23.77 C -ANISOU 6224 CB PHE D 180 2454 2669 3909 -157 552 -211 C -ATOM 6225 CG PHE D 180 -17.805 -4.156 12.993 1.00 23.06 C -ANISOU 6225 CG PHE D 180 2451 2538 3773 -160 455 -159 C -ATOM 6226 CD1 PHE D 180 -16.921 -4.337 11.934 1.00 22.39 C -ANISOU 6226 CD1 PHE D 180 2306 2486 3716 -136 364 -115 C -ATOM 6227 CD2 PHE D 180 -17.338 -3.562 14.166 1.00 24.14 C -ANISOU 6227 CD2 PHE D 180 2730 2610 3831 -201 458 -154 C -ATOM 6228 CE1 PHE D 180 -15.595 -3.935 12.044 1.00 22.91 C -ANISOU 6228 CE1 PHE D 180 2416 2537 3754 -151 282 -62 C -ATOM 6229 CE2 PHE D 180 -16.023 -3.160 14.290 1.00 23.37 C -ANISOU 6229 CE2 PHE D 180 2692 2495 3693 -231 351 -104 C -ATOM 6230 CZ PHE D 180 -15.144 -3.336 13.231 1.00 24.21 C -ANISOU 6230 CZ PHE D 180 2700 2650 3848 -206 265 -54 C -ATOM 6231 N GLU D 181 -21.571 -6.544 14.186 1.00 26.98 N -ANISOU 6231 N GLU D 181 2823 3110 4318 -313 805 -302 N -ATOM 6232 CA GLU D 181 -23.013 -6.727 14.169 1.00 27.52 C -ANISOU 6232 CA GLU D 181 2751 3254 4452 -343 919 -353 C -ATOM 6233 C GLU D 181 -23.650 -5.389 14.527 1.00 32.04 C -ANISOU 6233 C GLU D 181 3271 3840 5062 -243 1002 -380 C -ATOM 6234 O GLU D 181 -23.386 -4.825 15.595 1.00 32.32 O -ANISOU 6234 O GLU D 181 3461 3794 5023 -236 1074 -388 O -ATOM 6235 CB GLU D 181 -23.447 -7.816 15.150 1.00 29.13 C -ANISOU 6235 CB GLU D 181 3045 3424 4600 -475 1037 -371 C -ATOM 6236 CG GLU D 181 -24.912 -8.225 14.986 1.00 30.83 C -ANISOU 6236 CG GLU D 181 3079 3740 4896 -546 1151 -421 C -ATOM 6237 CD GLU D 181 -25.436 -8.944 16.193 1.00 39.17 C -ANISOU 6237 CD GLU D 181 4240 4753 5888 -675 1317 -442 C -ATOM 6238 OE1 GLU D 181 -25.675 -8.265 17.209 1.00 40.98 O -ANISOU 6238 OE1 GLU D 181 4541 4953 6078 -646 1442 -460 O -ATOM 6239 OE2 GLU D 181 -25.605 -10.177 16.125 1.00 42.52 O -ANISOU 6239 OE2 GLU D 181 4702 5162 6291 -812 1332 -443 O -ATOM 6240 N ILE D 182 -24.482 -4.871 13.630 1.00 32.28 N -ANISOU 6240 N ILE D 182 3100 3967 5198 -161 989 -391 N -ATOM 6241 CA ILE D 182 -24.952 -3.494 13.744 1.00 30.63 C -ANISOU 6241 CA ILE D 182 2849 3754 5036 -18 1046 -402 C -ATOM 6242 C ILE D 182 -26.466 -3.405 13.856 1.00 33.43 C -ANISOU 6242 C ILE D 182 2992 4214 5494 22 1180 -440 C -ATOM 6243 O ILE D 182 -27.176 -4.343 13.484 1.00 34.28 O -ANISOU 6243 O ILE D 182 2938 4431 5655 -71 1182 -452 O -ATOM 6244 CB ILE D 182 -24.462 -2.652 12.538 1.00 31.17 C -ANISOU 6244 CB ILE D 182 2876 3827 5138 96 896 -359 C -ATOM 6245 CG1 ILE D 182 -24.972 -3.235 11.218 1.00 37.42 C -ANISOU 6245 CG1 ILE D 182 3470 4745 6002 87 790 -345 C -ATOM 6246 CG2 ILE D 182 -22.946 -2.567 12.523 1.00 30.13 C -ANISOU 6246 CG2 ILE D 182 2933 3600 4916 59 792 -321 C -ATOM 6247 CD1 ILE D 182 -24.776 -2.291 10.023 1.00 35.27 C -ANISOU 6247 CD1 ILE D 182 3152 4489 5761 214 663 -299 C -ATOM 6248 N PRO D 183 -26.971 -2.271 14.373 1.00 31.59 N -ANISOU 6248 N PRO D 183 2760 3950 5291 157 1300 -459 N -ATOM 6249 CA PRO D 183 -28.418 -2.043 14.433 1.00 33.69 C -ANISOU 6249 CA PRO D 183 2787 4333 5682 238 1437 -487 C -ATOM 6250 C PRO D 183 -29.013 -1.917 13.029 1.00 36.12 C -ANISOU 6250 C PRO D 183 2826 4784 6112 324 1291 -448 C -ATOM 6251 O PRO D 183 -28.271 -1.835 12.053 1.00 36.11 O -ANISOU 6251 O PRO D 183 2870 4766 6084 337 1104 -405 O -ATOM 6252 CB PRO D 183 -28.528 -0.689 15.142 1.00 41.54 C -ANISOU 6252 CB PRO D 183 3899 5218 6666 407 1573 -507 C -ATOM 6253 CG PRO D 183 -27.213 -0.481 15.830 1.00 39.00 C -ANISOU 6253 CG PRO D 183 3912 4722 6184 335 1541 -509 C -ATOM 6254 CD PRO D 183 -26.203 -1.166 14.983 1.00 33.65 C -ANISOU 6254 CD PRO D 183 3257 4058 5469 235 1324 -460 C -ATOM 6255 N ASP D 184 -30.336 -1.881 12.940 1.00 38.25 N -ANISOU 6255 N ASP D 184 2819 5202 6512 382 1375 -460 N -ATOM 6256 CA ASP D 184 -31.018 -1.684 11.665 1.00 45.49 C -ANISOU 6256 CA ASP D 184 3465 6275 7546 475 1223 -416 C -ATOM 6257 C ASP D 184 -31.014 -0.198 11.305 1.00 43.91 C -ANISOU 6257 C ASP D 184 3284 6013 7389 740 1193 -372 C -ATOM 6258 O ASP D 184 -32.053 0.463 11.349 1.00 44.21 O -ANISOU 6258 O ASP D 184 3116 6131 7549 916 1279 -362 O -ATOM 6259 CB ASP D 184 -32.452 -2.219 11.739 1.00 49.25 C -ANISOU 6259 CB ASP D 184 3603 6954 8155 428 1314 -437 C -ATOM 6260 CG ASP D 184 -33.134 -2.283 10.377 1.00 58.20 C -ANISOU 6260 CG ASP D 184 4446 8278 9390 464 1109 -388 C -ATOM 6261 OD1 ASP D 184 -32.463 -2.056 9.347 1.00 60.50 O -ANISOU 6261 OD1 ASP D 184 4826 8533 9626 503 900 -341 O -ATOM 6262 OD2 ASP D 184 -34.349 -2.575 10.343 1.00 65.52 O -ANISOU 6262 OD2 ASP D 184 5102 9397 10395 437 1137 -381 O -ATOM 6263 N LYS D 185 -29.826 0.311 10.983 1.00 37.82 N -ANISOU 6263 N LYS D 185 2765 5090 6514 765 1083 -343 N -ATOM 6264 CA LYS D 185 -29.625 1.691 10.544 1.00 43.85 C -ANISOU 6264 CA LYS D 185 3613 5758 7290 984 1036 -295 C -ATOM 6265 C LYS D 185 -28.976 1.639 9.165 1.00 40.90 C -ANISOU 6265 C LYS D 185 3259 5405 6877 963 795 -231 C -ATOM 6266 O LYS D 185 -28.251 0.692 8.866 1.00 35.92 O -ANISOU 6266 O LYS D 185 2694 4786 6169 779 705 -239 O -ATOM 6267 CB LYS D 185 -28.666 2.419 11.491 1.00 47.34 C -ANISOU 6267 CB LYS D 185 4388 5979 7621 993 1140 -323 C -ATOM 6268 CG LYS D 185 -29.219 2.767 12.863 1.00 55.01 C -ANISOU 6268 CG LYS D 185 5420 6884 8598 1045 1394 -388 C -ATOM 6269 CD LYS D 185 -28.143 3.475 13.697 1.00 54.16 C -ANISOU 6269 CD LYS D 185 5681 6550 8346 1016 1452 -416 C -ATOM 6270 CE LYS D 185 -28.741 4.196 14.903 1.00 58.48 C -ANISOU 6270 CE LYS D 185 6338 6994 8888 1126 1709 -480 C -ATOM 6271 NZ LYS D 185 -28.314 3.592 16.198 1.00 58.66 N -ANISOU 6271 NZ LYS D 185 6562 6949 8777 937 1832 -545 N -ATOM 6272 N PHE D 186 -29.217 2.643 8.323 1.00 40.56 N -ANISOU 6272 N PHE D 186 3180 5356 6876 1157 701 -165 N -ATOM 6273 CA PHE D 186 -28.575 2.648 7.011 1.00 38.57 C -ANISOU 6273 CA PHE D 186 2981 5110 6562 1132 487 -102 C -ATOM 6274 C PHE D 186 -27.183 3.252 7.107 1.00 34.03 C -ANISOU 6274 C PHE D 186 2723 4337 5868 1102 480 -90 C -ATOM 6275 O PHE D 186 -27.025 4.400 7.528 1.00 39.59 O -ANISOU 6275 O PHE D 186 3583 4894 6565 1235 559 -78 O -ATOM 6276 CB PHE D 186 -29.404 3.389 5.951 1.00 42.34 C -ANISOU 6276 CB PHE D 186 3297 5675 7117 1336 359 -19 C -ATOM 6277 CG PHE D 186 -28.998 3.043 4.542 1.00 42.90 C -ANISOU 6277 CG PHE D 186 3377 5810 7115 1265 134 37 C -ATOM 6278 CD1 PHE D 186 -27.914 3.670 3.943 1.00 40.52 C -ANISOU 6278 CD1 PHE D 186 3328 5364 6705 1277 61 85 C -ATOM 6279 CD2 PHE D 186 -29.684 2.064 3.830 1.00 46.16 C -ANISOU 6279 CD2 PHE D 186 3560 6424 7555 1161 6 37 C -ATOM 6280 CE1 PHE D 186 -27.517 3.332 2.646 1.00 39.75 C -ANISOU 6280 CE1 PHE D 186 3261 5318 6523 1204 -121 133 C -ATOM 6281 CE2 PHE D 186 -29.303 1.721 2.544 1.00 46.86 C -ANISOU 6281 CE2 PHE D 186 3695 6560 7552 1083 -190 78 C -ATOM 6282 CZ PHE D 186 -28.212 2.356 1.947 1.00 43.24 C -ANISOU 6282 CZ PHE D 186 3497 5953 6980 1113 -246 127 C -ATOM 6283 N VAL D 187 -26.178 2.477 6.713 1.00 31.39 N -ANISOU 6283 N VAL D 187 2484 3999 5444 925 393 -92 N -ATOM 6284 CA VAL D 187 -24.789 2.925 6.807 1.00 30.77 C -ANISOU 6284 CA VAL D 187 2665 3765 5263 865 383 -79 C -ATOM 6285 C VAL D 187 -24.122 2.990 5.444 1.00 35.07 C -ANISOU 6285 C VAL D 187 3259 4319 5748 845 227 -15 C -ATOM 6286 O VAL D 187 -24.526 2.303 4.514 1.00 32.45 O -ANISOU 6286 O VAL D 187 2791 4114 5423 816 121 0 O -ATOM 6287 CB VAL D 187 -23.969 2.025 7.750 1.00 30.90 C -ANISOU 6287 CB VAL D 187 2775 3746 5218 682 448 -134 C -ATOM 6288 CG1 VAL D 187 -24.538 2.096 9.160 1.00 33.61 C -ANISOU 6288 CG1 VAL D 187 3131 4053 5587 695 617 -194 C -ATOM 6289 CG2 VAL D 187 -23.971 0.584 7.248 1.00 31.00 C -ANISOU 6289 CG2 VAL D 187 2671 3882 5225 545 379 -149 C -ATOM 6290 N VAL D 188 -23.095 3.820 5.329 1.00 32.17 N -ANISOU 6290 N VAL D 188 3098 3813 5311 844 219 19 N -ATOM 6291 CA VAL D 188 -22.363 3.963 4.075 1.00 28.37 C -ANISOU 6291 CA VAL D 188 2691 3327 4761 815 102 82 C -ATOM 6292 C VAL D 188 -20.890 4.098 4.410 1.00 28.11 C -ANISOU 6292 C VAL D 188 2840 3188 4653 684 134 80 C -ATOM 6293 O VAL D 188 -20.538 4.200 5.584 1.00 27.00 O -ANISOU 6293 O VAL D 188 2774 2976 4510 632 222 38 O -ATOM 6294 CB VAL D 188 -22.822 5.226 3.295 1.00 29.94 C -ANISOU 6294 CB VAL D 188 2946 3466 4963 991 46 160 C -ATOM 6295 CG1 VAL D 188 -24.262 5.093 2.818 1.00 31.53 C -ANISOU 6295 CG1 VAL D 188 2930 3804 5246 1132 -22 180 C -ATOM 6296 CG2 VAL D 188 -22.657 6.485 4.161 1.00 30.68 C -ANISOU 6296 CG2 VAL D 188 3220 3377 5060 1076 154 159 C -ATOM 6297 N GLY D 189 -20.033 4.094 3.391 1.00 27.24 N -ANISOU 6297 N GLY D 189 2797 3076 4477 624 64 129 N -ATOM 6298 CA GLY D 189 -18.599 4.229 3.598 1.00 26.42 C -ANISOU 6298 CA GLY D 189 2823 2899 4315 496 90 138 C -ATOM 6299 C GLY D 189 -17.877 2.894 3.530 1.00 25.21 C -ANISOU 6299 C GLY D 189 2596 2835 4147 372 84 112 C -ATOM 6300 O GLY D 189 -18.519 1.842 3.614 1.00 26.70 O -ANISOU 6300 O GLY D 189 2663 3115 4367 368 78 71 O -ATOM 6301 N TYR D 190 -16.553 2.932 3.397 1.00 27.77 N -ANISOU 6301 N TYR D 190 2991 3132 4429 271 92 139 N -ATOM 6302 CA TYR D 190 -15.752 1.711 3.233 1.00 28.09 C -ANISOU 6302 CA TYR D 190 2965 3247 4462 185 95 127 C -ATOM 6303 C TYR D 190 -16.352 0.850 2.118 1.00 27.05 C -ANISOU 6303 C TYR D 190 2764 3201 4313 217 57 118 C -ATOM 6304 O TYR D 190 -16.522 -0.366 2.265 1.00 25.72 O -ANISOU 6304 O TYR D 190 2524 3090 4158 187 65 75 O -ATOM 6305 CB TYR D 190 -15.676 0.936 4.548 1.00 22.66 C -ANISOU 6305 CB TYR D 190 2234 2569 3807 138 129 79 C -ATOM 6306 CG TYR D 190 -14.580 -0.114 4.591 1.00 23.68 C -ANISOU 6306 CG TYR D 190 2324 2742 3930 65 136 85 C -ATOM 6307 CD1 TYR D 190 -13.238 0.255 4.576 1.00 28.32 C -ANISOU 6307 CD1 TYR D 190 2936 3319 4504 -2 137 130 C -ATOM 6308 CD2 TYR D 190 -14.885 -1.467 4.652 1.00 22.03 C -ANISOU 6308 CD2 TYR D 190 2052 2583 3735 64 146 50 C -ATOM 6309 CE1 TYR D 190 -12.225 -0.703 4.621 1.00 27.89 C -ANISOU 6309 CE1 TYR D 190 2819 3316 4463 -38 147 146 C -ATOM 6310 CE2 TYR D 190 -13.880 -2.429 4.711 1.00 21.92 C -ANISOU 6310 CE2 TYR D 190 2016 2592 3721 30 162 62 C -ATOM 6311 CZ TYR D 190 -12.557 -2.042 4.692 1.00 25.72 C -ANISOU 6311 CZ TYR D 190 2497 3074 4202 -6 161 113 C -ATOM 6312 OH TYR D 190 -11.542 -2.987 4.749 1.00 25.65 O -ANISOU 6312 OH TYR D 190 2438 3097 4209 -11 179 136 O -ATOM 6313 N ALA D 191 -16.674 1.519 1.005 1.00 25.56 N -ANISOU 6313 N ALA D 191 2622 3008 4080 271 9 162 N -ATOM 6314 CA ALA D 191 -17.222 0.915 -0.222 1.00 24.51 C -ANISOU 6314 CA ALA D 191 2463 2952 3899 289 -52 163 C -ATOM 6315 C ALA D 191 -18.721 0.660 -0.214 1.00 25.99 C -ANISOU 6315 C ALA D 191 2541 3208 4124 355 -120 135 C -ATOM 6316 O ALA D 191 -19.304 0.439 -1.266 1.00 29.13 O -ANISOU 6316 O ALA D 191 2926 3671 4473 371 -204 148 O -ATOM 6317 CB ALA D 191 -16.428 -0.352 -0.661 1.00 23.96 C -ANISOU 6317 CB ALA D 191 2387 2926 3791 205 -15 134 C -ATOM 6318 N LEU D 192 -19.357 0.715 0.954 1.00 26.27 N -ANISOU 6318 N LEU D 192 2499 3239 4244 385 -83 99 N -ATOM 6319 CA LEU D 192 -20.824 0.673 0.992 1.00 26.06 C -ANISOU 6319 CA LEU D 192 2338 3291 4274 460 -133 83 C -ATOM 6320 C LEU D 192 -21.441 1.992 0.503 1.00 31.93 C -ANISOU 6320 C LEU D 192 3103 4007 5024 608 -193 151 C -ATOM 6321 O LEU D 192 -20.973 3.081 0.870 1.00 29.98 O -ANISOU 6321 O LEU D 192 2976 3640 4774 662 -145 185 O -ATOM 6322 CB LEU D 192 -21.343 0.343 2.388 1.00 27.85 C -ANISOU 6322 CB LEU D 192 2477 3520 4584 451 -46 25 C -ATOM 6323 CG LEU D 192 -21.181 -1.112 2.842 1.00 32.39 C -ANISOU 6323 CG LEU D 192 3009 4139 5160 322 -5 -37 C -ATOM 6324 CD1 LEU D 192 -19.792 -1.359 3.380 1.00 31.99 C -ANISOU 6324 CD1 LEU D 192 3077 4006 5073 251 55 -38 C -ATOM 6325 CD2 LEU D 192 -22.233 -1.495 3.883 1.00 34.71 C -ANISOU 6325 CD2 LEU D 192 3181 4476 5530 316 59 -89 C -ATOM 6326 N ASP D 193 -22.507 1.898 -0.294 1.00 28.72 N -ANISOU 6326 N ASP D 193 2585 3704 4622 670 -305 173 N -ATOM 6327 CA ASP D 193 -23.041 3.077 -0.974 1.00 30.29 C -ANISOU 6327 CA ASP D 193 2817 3880 4811 829 -390 259 C -ATOM 6328 C ASP D 193 -24.474 3.454 -0.623 1.00 33.28 C -ANISOU 6328 C ASP D 193 3009 4335 5303 984 -423 271 C -ATOM 6329 O ASP D 193 -25.230 2.681 -0.038 1.00 34.08 O -ANISOU 6329 O ASP D 193 2919 4543 5485 946 -397 210 O -ATOM 6330 CB ASP D 193 -22.983 2.905 -2.491 1.00 31.01 C -ANISOU 6330 CB ASP D 193 2968 4030 4786 802 -531 312 C -ATOM 6331 CG ASP D 193 -24.043 1.952 -3.002 1.00 33.15 C -ANISOU 6331 CG ASP D 193 3056 4474 5064 762 -653 284 C -ATOM 6332 OD1 ASP D 193 -24.086 0.813 -2.504 1.00 33.85 O -ANISOU 6332 OD1 ASP D 193 3054 4622 5184 633 -602 199 O -ATOM 6333 OD2 ASP D 193 -24.837 2.338 -3.890 1.00 35.68 O -ANISOU 6333 OD2 ASP D 193 3330 4872 5356 851 -808 351 O -ATOM 6334 N TYR D 194 -24.825 4.670 -1.012 1.00 33.46 N -ANISOU 6334 N TYR D 194 3091 4294 5329 1163 -473 356 N -ATOM 6335 CA TYR D 194 -26.202 5.093 -1.116 1.00 35.68 C -ANISOU 6335 CA TYR D 194 3182 4670 5705 1350 -550 401 C -ATOM 6336 C TYR D 194 -26.296 5.666 -2.515 1.00 38.78 C -ANISOU 6336 C TYR D 194 3664 5069 6001 1437 -728 512 C -ATOM 6337 O TYR D 194 -25.660 6.678 -2.804 1.00 39.47 O -ANISOU 6337 O TYR D 194 3985 4993 6020 1509 -711 579 O -ATOM 6338 CB TYR D 194 -26.503 6.163 -0.074 1.00 36.46 C -ANISOU 6338 CB TYR D 194 3310 4641 5902 1530 -412 405 C -ATOM 6339 CG TYR D 194 -27.865 6.790 -0.205 1.00 39.16 C -ANISOU 6339 CG TYR D 194 3463 5060 6355 1778 -472 469 C -ATOM 6340 CD1 TYR D 194 -29.008 6.089 0.146 1.00 44.10 C -ANISOU 6340 CD1 TYR D 194 3769 5883 7105 1794 -478 430 C -ATOM 6341 CD2 TYR D 194 -28.003 8.091 -0.649 1.00 40.89 C -ANISOU 6341 CD2 TYR D 194 3821 5153 6563 2001 -514 573 C -ATOM 6342 CE1 TYR D 194 -30.256 6.667 0.038 1.00 47.94 C -ANISOU 6342 CE1 TYR D 194 4039 6462 7712 2035 -530 495 C -ATOM 6343 CE2 TYR D 194 -29.243 8.680 -0.760 1.00 49.88 C -ANISOU 6343 CE2 TYR D 194 4774 6362 7815 2264 -569 643 C -ATOM 6344 CZ TYR D 194 -30.367 7.963 -0.413 1.00 51.60 C -ANISOU 6344 CZ TYR D 194 4636 6801 8170 2285 -578 605 C -ATOM 6345 OH TYR D 194 -31.608 8.550 -0.522 1.00 58.57 O -ANISOU 6345 OH TYR D 194 5293 7777 9186 2560 -632 682 O -ATOM 6346 N ASN D 195 -27.062 5.005 -3.380 1.00 38.31 N -ANISOU 6346 N ASN D 195 3441 5195 5922 1409 -901 531 N -ATOM 6347 CA ASN D 195 -27.146 5.374 -4.793 1.00 39.82 C -ANISOU 6347 CA ASN D 195 3732 5411 5986 1458 -1096 635 C -ATOM 6348 C ASN D 195 -25.790 5.644 -5.448 1.00 38.59 C -ANISOU 6348 C ASN D 195 3899 5101 5661 1357 -1062 662 C -ATOM 6349 O ASN D 195 -25.621 6.650 -6.149 1.00 39.86 O -ANISOU 6349 O ASN D 195 4245 5161 5739 1472 -1125 770 O -ATOM 6350 CB ASN D 195 -28.086 6.565 -4.993 1.00 53.04 C -ANISOU 6350 CB ASN D 195 5346 7077 7728 1743 -1191 754 C -ATOM 6351 CG ASN D 195 -29.505 6.247 -4.598 1.00 60.79 C -ANISOU 6351 CG ASN D 195 5963 8260 8875 1846 -1253 745 C -ATOM 6352 OD1 ASN D 195 -29.982 5.140 -4.829 1.00 62.94 O -ANISOU 6352 OD1 ASN D 195 6037 8726 9152 1688 -1344 690 O -ATOM 6353 ND2 ASN D 195 -30.189 7.213 -3.988 1.00 63.15 N -ANISOU 6353 ND2 ASN D 195 6171 8510 9312 2107 -1191 795 N -ATOM 6354 N GLU D 196 -24.841 4.746 -5.185 1.00 37.03 N -ANISOU 6354 N GLU D 196 3763 4887 5421 1148 -950 569 N -ATOM 6355 CA GLU D 196 -23.493 4.765 -5.772 1.00 35.25 C -ANISOU 6355 CA GLU D 196 3793 4551 5051 1023 -890 578 C -ATOM 6356 C GLU D 196 -22.545 5.771 -5.110 1.00 36.49 C -ANISOU 6356 C GLU D 196 4126 4512 5225 1053 -737 599 C -ATOM 6357 O GLU D 196 -21.336 5.744 -5.345 1.00 34.96 O -ANISOU 6357 O GLU D 196 4100 4239 4946 927 -651 594 O -ATOM 6358 CB GLU D 196 -23.543 4.950 -7.295 1.00 37.82 C -ANISOU 6358 CB GLU D 196 4260 4904 5205 1026 -1051 665 C -ATOM 6359 CG GLU D 196 -24.234 3.792 -8.023 1.00 37.58 C -ANISOU 6359 CG GLU D 196 4105 5060 5115 925 -1202 625 C -ATOM 6360 CD GLU D 196 -23.543 2.463 -7.782 1.00 38.66 C -ANISOU 6360 CD GLU D 196 4236 5222 5230 716 -1089 502 C -ATOM 6361 OE1 GLU D 196 -22.325 2.465 -7.552 1.00 37.10 O -ANISOU 6361 OE1 GLU D 196 4184 4909 5003 645 -929 477 O -ATOM 6362 OE2 GLU D 196 -24.217 1.416 -7.828 1.00 47.68 O -ANISOU 6362 OE2 GLU D 196 5230 6499 6387 623 -1162 435 O -ATOM 6363 N TYR D 197 -23.095 6.638 -4.267 1.00 35.09 N -ANISOU 6363 N TYR D 197 3908 4264 5161 1211 -694 617 N -ATOM 6364 CA TYR D 197 -22.282 7.595 -3.534 1.00 34.56 C -ANISOU 6364 CA TYR D 197 4022 4003 5107 1220 -551 624 C -ATOM 6365 C TYR D 197 -21.771 7.037 -2.206 1.00 32.70 C -ANISOU 6365 C TYR D 197 3718 3755 4952 1103 -403 515 C -ATOM 6366 O TYR D 197 -22.272 6.021 -1.722 1.00 32.04 O -ANISOU 6366 O TYR D 197 3436 3800 4938 1060 -399 441 O -ATOM 6367 CB TYR D 197 -23.073 8.871 -3.298 1.00 36.52 C -ANISOU 6367 CB TYR D 197 4318 4142 5414 1456 -563 697 C -ATOM 6368 CG TYR D 197 -23.252 9.676 -4.553 1.00 47.33 C -ANISOU 6368 CG TYR D 197 5848 5459 6678 1570 -695 828 C -ATOM 6369 CD1 TYR D 197 -22.315 10.629 -4.921 1.00 48.27 C -ANISOU 6369 CD1 TYR D 197 6268 5383 6689 1534 -642 894 C -ATOM 6370 CD2 TYR D 197 -24.351 9.477 -5.380 1.00 51.73 C -ANISOU 6370 CD2 TYR D 197 6260 6165 7232 1699 -881 892 C -ATOM 6371 CE1 TYR D 197 -22.470 11.371 -6.073 1.00 54.19 C -ANISOU 6371 CE1 TYR D 197 7198 6069 7323 1635 -757 1024 C -ATOM 6372 CE2 TYR D 197 -24.514 10.213 -6.538 1.00 55.10 C -ANISOU 6372 CE2 TYR D 197 6853 6541 7542 1808 -1020 1025 C -ATOM 6373 CZ TYR D 197 -23.571 11.158 -6.878 1.00 56.75 C -ANISOU 6373 CZ TYR D 197 7388 6537 7636 1780 -951 1092 C -ATOM 6374 OH TYR D 197 -23.727 11.895 -8.029 1.00 60.78 O -ANISOU 6374 OH TYR D 197 8097 6984 8015 1885 -1084 1233 O -ATOM 6375 N PHE D 198 -20.765 7.707 -1.644 1.00 32.08 N -ANISOU 6375 N PHE D 198 3818 3520 4852 1037 -291 512 N -ATOM 6376 CA PHE D 198 -20.170 7.360 -0.345 1.00 30.63 C -ANISOU 6376 CA PHE D 198 3611 3305 4723 924 -167 424 C -ATOM 6377 C PHE D 198 -19.248 6.162 -0.361 1.00 28.92 C -ANISOU 6377 C PHE D 198 3334 3179 4477 735 -144 371 C -ATOM 6378 O PHE D 198 -18.789 5.725 0.695 1.00 27.84 O -ANISOU 6378 O PHE D 198 3160 3036 4381 646 -66 307 O -ATOM 6379 CB PHE D 198 -21.236 7.185 0.746 1.00 30.91 C -ANISOU 6379 CB PHE D 198 3490 3378 4875 1027 -121 363 C -ATOM 6380 CG PHE D 198 -22.070 8.405 0.968 1.00 32.78 C -ANISOU 6380 CG PHE D 198 3791 3506 5159 1239 -102 406 C -ATOM 6381 CD1 PHE D 198 -21.556 9.492 1.658 1.00 35.64 C -ANISOU 6381 CD1 PHE D 198 4373 3666 5502 1251 0 406 C -ATOM 6382 CD2 PHE D 198 -23.368 8.467 0.488 1.00 42.25 C -ANISOU 6382 CD2 PHE D 198 4830 4802 6421 1427 -187 448 C -ATOM 6383 CE1 PHE D 198 -22.325 10.634 1.869 1.00 39.76 C -ANISOU 6383 CE1 PHE D 198 4986 4057 6064 1468 37 444 C -ATOM 6384 CE2 PHE D 198 -24.146 9.598 0.688 1.00 47.82 C -ANISOU 6384 CE2 PHE D 198 5585 5403 7183 1660 -161 497 C -ATOM 6385 CZ PHE D 198 -23.621 10.686 1.380 1.00 46.96 C -ANISOU 6385 CZ PHE D 198 5726 5064 7051 1690 -38 493 C -ATOM 6386 N ARG D 199 -18.969 5.605 -1.538 1.00 28.87 N -ANISOU 6386 N ARG D 199 3328 3249 4392 679 -209 399 N -ATOM 6387 CA ARG D 199 -18.018 4.502 -1.555 1.00 27.51 C -ANISOU 6387 CA ARG D 199 3117 3141 4196 524 -162 351 C -ATOM 6388 C ARG D 199 -16.607 5.007 -1.264 1.00 30.61 C -ANISOU 6388 C ARG D 199 3630 3438 4560 412 -73 369 C -ATOM 6389 O ARG D 199 -15.791 4.272 -0.700 1.00 27.77 O -ANISOU 6389 O ARG D 199 3212 3114 4227 307 -14 326 O -ATOM 6390 CB ARG D 199 -18.034 3.748 -2.878 1.00 29.54 C -ANISOU 6390 CB ARG D 199 3371 3489 4362 488 -229 364 C -ATOM 6391 CG ARG D 199 -19.354 3.059 -3.198 1.00 31.91 C -ANISOU 6391 CG ARG D 199 3532 3910 4681 547 -336 338 C -ATOM 6392 CD ARG D 199 -19.147 1.990 -4.254 1.00 28.43 C -ANISOU 6392 CD ARG D 199 3107 3553 4141 454 -376 315 C -ATOM 6393 NE ARG D 199 -20.384 1.641 -4.949 1.00 29.69 N -ANISOU 6393 NE ARG D 199 3186 3822 4273 493 -522 318 N -ATOM 6394 CZ ARG D 199 -21.224 0.695 -4.538 1.00 31.80 C -ANISOU 6394 CZ ARG D 199 3288 4191 4605 459 -558 249 C -ATOM 6395 NH1 ARG D 199 -20.957 0.010 -3.433 1.00 30.30 N -ANISOU 6395 NH1 ARG D 199 3022 3989 4502 399 -448 177 N -ATOM 6396 NH2 ARG D 199 -22.319 0.429 -5.239 1.00 31.13 N -ANISOU 6396 NH2 ARG D 199 3118 4220 4490 472 -709 258 N -ATOM 6397 N ASP D 200 -16.347 6.259 -1.645 1.00 28.09 N -ANISOU 6397 N ASP D 200 3479 3002 4190 434 -69 439 N -ATOM 6398 CA ASP D 200 -15.028 6.884 -1.518 1.00 29.69 C -ANISOU 6398 CA ASP D 200 3805 3117 4358 301 8 468 C -ATOM 6399 C ASP D 200 -14.860 7.536 -0.144 1.00 32.01 C -ANISOU 6399 C ASP D 200 4142 3310 4710 273 57 435 C -ATOM 6400 O ASP D 200 -14.601 8.733 -0.029 1.00 33.84 O -ANISOU 6400 O ASP D 200 4551 3397 4910 255 83 474 O -ATOM 6401 CB ASP D 200 -14.817 7.931 -2.623 1.00 29.55 C -ANISOU 6401 CB ASP D 200 3986 3003 4240 310 -2 562 C -ATOM 6402 CG ASP D 200 -15.955 8.941 -2.697 1.00 33.67 C -ANISOU 6402 CG ASP D 200 4612 3421 4761 487 -65 609 C -ATOM 6403 OD1 ASP D 200 -17.111 8.536 -2.460 1.00 31.07 O -ANISOU 6403 OD1 ASP D 200 4149 3162 4494 625 -129 579 O -ATOM 6404 OD2 ASP D 200 -15.695 10.137 -2.986 1.00 32.20 O -ANISOU 6404 OD2 ASP D 200 4639 3080 4515 490 -45 680 O -ATOM 6405 N LEU D 201 -15.025 6.731 0.895 1.00 28.78 N -ANISOU 6405 N LEU D 201 3597 2966 4371 260 70 361 N -ATOM 6406 CA LEU D 201 -14.994 7.197 2.278 1.00 32.31 C -ANISOU 6406 CA LEU D 201 4092 3329 4856 233 112 317 C -ATOM 6407 C LEU D 201 -14.443 6.031 3.060 1.00 32.42 C -ANISOU 6407 C LEU D 201 3966 3445 4905 135 125 263 C -ATOM 6408 O LEU D 201 -14.897 4.906 2.863 1.00 32.25 O -ANISOU 6408 O LEU D 201 3804 3536 4913 176 106 235 O -ATOM 6409 CB LEU D 201 -16.410 7.549 2.733 1.00 33.72 C -ANISOU 6409 CB LEU D 201 4267 3464 5080 407 112 291 C -ATOM 6410 CG LEU D 201 -16.702 7.848 4.196 1.00 35.44 C -ANISOU 6410 CG LEU D 201 4530 3605 5332 414 177 227 C -ATOM 6411 CD1 LEU D 201 -15.941 9.086 4.641 1.00 32.50 C -ANISOU 6411 CD1 LEU D 201 4389 3056 4903 325 217 241 C -ATOM 6412 CD2 LEU D 201 -18.205 8.052 4.377 1.00 35.57 C -ANISOU 6412 CD2 LEU D 201 4490 3615 5408 617 195 210 C -ATOM 6413 N ASN D 202 -13.454 6.271 3.923 1.00 30.75 N -ANISOU 6413 N ASN D 202 3802 3196 4686 -1 146 254 N -ATOM 6414 CA AASN D 202 -12.766 5.179 4.613 0.51 30.41 C -ANISOU 6414 CA AASN D 202 3632 3252 4670 -89 140 224 C -ATOM 6415 CA BASN D 202 -12.776 5.165 4.600 0.49 30.37 C -ANISOU 6415 CA BASN D 202 3625 3249 4666 -87 140 224 C -ATOM 6416 C ASN D 202 -13.515 4.645 5.833 1.00 29.49 C -ANISOU 6416 C ASN D 202 3482 3141 4583 -47 149 159 C -ATOM 6417 O ASN D 202 -13.378 3.471 6.199 1.00 29.84 O -ANISOU 6417 O ASN D 202 3413 3274 4651 -64 141 137 O -ATOM 6418 CB AASN D 202 -11.354 5.610 5.019 0.51 33.37 C -ANISOU 6418 CB AASN D 202 4043 3613 5024 -262 135 253 C -ATOM 6419 CB BASN D 202 -11.309 5.506 4.932 0.49 33.25 C -ANISOU 6419 CB BASN D 202 4013 3611 5011 -261 134 256 C -ATOM 6420 CG AASN D 202 -10.271 4.775 4.360 0.51 37.07 C -ANISOU 6420 CG AASN D 202 4367 4206 5512 -326 136 292 C -ATOM 6421 CG BASN D 202 -11.175 6.640 5.940 0.49 32.61 C -ANISOU 6421 CG BASN D 202 4099 3399 4892 -348 134 238 C -ATOM 6422 OD1AASN D 202 -10.542 3.957 3.474 0.51 41.01 O -ANISOU 6422 OD1AASN D 202 4783 4778 6022 -243 152 295 O -ATOM 6423 OD1BASN D 202 -12.082 7.459 6.093 0.49 33.05 O -ANISOU 6423 OD1BASN D 202 4297 3333 4929 -262 161 218 O -ATOM 6424 ND2AASN D 202 -9.028 4.979 4.793 0.51 40.05 N -ANISOU 6424 ND2AASN D 202 4713 4612 5892 -476 122 320 N -ATOM 6425 ND2BASN D 202 -10.030 6.696 6.628 0.49 28.51 N -ANISOU 6425 ND2BASN D 202 3570 2904 4360 -518 101 248 N -ATOM 6426 N HIS D 203 -14.305 5.508 6.465 1.00 27.61 N -ANISOU 6426 N HIS D 203 3359 2795 4336 12 180 130 N -ATOM 6427 CA HIS D 203 -15.069 5.111 7.644 1.00 27.00 C -ANISOU 6427 CA HIS D 203 3272 2713 4276 49 219 65 C -ATOM 6428 C HIS D 203 -16.456 4.634 7.249 1.00 29.41 C -ANISOU 6428 C HIS D 203 3462 3077 4637 201 241 44 C -ATOM 6429 O HIS D 203 -16.988 5.034 6.206 1.00 31.08 O -ANISOU 6429 O HIS D 203 3654 3293 4864 301 218 79 O -ATOM 6430 CB HIS D 203 -15.263 6.300 8.594 1.00 27.42 C -ANISOU 6430 CB HIS D 203 3521 2611 4286 42 271 34 C -ATOM 6431 CG HIS D 203 -14.011 7.052 8.913 1.00 27.01 C -ANISOU 6431 CG HIS D 203 3614 2482 4169 -127 239 54 C -ATOM 6432 ND1 HIS D 203 -12.963 6.499 9.623 1.00 26.39 N -ANISOU 6432 ND1 HIS D 203 3502 2465 4061 -287 186 54 N -ATOM 6433 CD2 HIS D 203 -13.649 8.330 8.641 1.00 27.83 C -ANISOU 6433 CD2 HIS D 203 3897 2449 4227 -173 248 79 C -ATOM 6434 CE1 HIS D 203 -12.005 7.400 9.757 1.00 27.33 C -ANISOU 6434 CE1 HIS D 203 3749 2510 4125 -438 154 75 C -ATOM 6435 NE2 HIS D 203 -12.396 8.517 9.176 1.00 28.18 N -ANISOU 6435 NE2 HIS D 203 4000 2488 4219 -382 199 87 N -ATOM 6436 N VAL D 204 -17.070 3.824 8.102 1.00 25.16 N -ANISOU 6436 N VAL D 204 2853 2585 4123 210 281 -9 N -ATOM 6437 CA VAL D 204 -18.497 3.538 7.962 1.00 29.15 C -ANISOU 6437 CA VAL D 204 3243 3144 4688 336 318 -37 C -ATOM 6438 C VAL D 204 -19.257 4.604 8.736 1.00 31.40 C -ANISOU 6438 C VAL D 204 3630 3320 4982 433 408 -67 C -ATOM 6439 O VAL D 204 -18.963 4.876 9.901 1.00 28.10 O -ANISOU 6439 O VAL D 204 3343 2818 4516 370 471 -107 O -ATOM 6440 CB VAL D 204 -18.859 2.122 8.450 1.00 27.28 C -ANISOU 6440 CB VAL D 204 2884 3007 4475 286 339 -79 C -ATOM 6441 CG1 VAL D 204 -20.377 1.944 8.552 1.00 30.71 C -ANISOU 6441 CG1 VAL D 204 3192 3499 4977 387 398 -114 C -ATOM 6442 CG2 VAL D 204 -18.273 1.093 7.506 1.00 23.54 C -ANISOU 6442 CG2 VAL D 204 2324 2623 3997 228 264 -52 C -ATOM 6443 N CYS D 205 -20.216 5.239 8.081 1.00 29.65 N -ANISOU 6443 N CYS D 205 3361 3093 4811 593 414 -45 N -ATOM 6444 CA CYS D 205 -20.871 6.383 8.681 1.00 30.16 C -ANISOU 6444 CA CYS D 205 3541 3030 4887 722 512 -64 C -ATOM 6445 C CYS D 205 -22.377 6.264 8.540 1.00 34.96 C -ANISOU 6445 C CYS D 205 3961 3724 5597 900 559 -73 C -ATOM 6446 O CYS D 205 -22.869 5.472 7.742 1.00 32.68 O -ANISOU 6446 O CYS D 205 3467 3588 5359 914 481 -51 O -ATOM 6447 CB CYS D 205 -20.373 7.667 8.034 1.00 31.68 C -ANISOU 6447 CB CYS D 205 3916 3082 5039 767 477 -7 C -ATOM 6448 N VAL D 206 -23.108 7.052 9.316 1.00 34.64 N -ANISOU 6448 N VAL D 206 3988 3588 5585 1032 691 -107 N -ATOM 6449 CA VAL D 206 -24.537 7.203 9.080 1.00 41.30 C -ANISOU 6449 CA VAL D 206 4637 4511 6544 1242 739 -98 C -ATOM 6450 C VAL D 206 -24.747 8.483 8.272 1.00 39.58 C -ANISOU 6450 C VAL D 206 4513 4184 6343 1438 698 -24 C -ATOM 6451 O VAL D 206 -24.123 9.509 8.545 1.00 42.07 O -ANISOU 6451 O VAL D 206 5100 4297 6586 1444 741 -21 O -ATOM 6452 CB VAL D 206 -25.347 7.223 10.396 1.00 45.73 C -ANISOU 6452 CB VAL D 206 5185 5048 7143 1301 939 -177 C -ATOM 6453 CG1 VAL D 206 -25.288 5.872 11.076 1.00 42.65 C -ANISOU 6453 CG1 VAL D 206 4691 4778 6736 1115 972 -234 C -ATOM 6454 CG2 VAL D 206 -24.805 8.278 11.336 1.00 51.70 C -ANISOU 6454 CG2 VAL D 206 6265 5572 7806 1303 1059 -218 C -ATOM 6455 N ILE D 207 -25.611 8.421 7.266 1.00 48.19 N -ANISOU 6455 N ILE D 207 5392 5400 7517 1587 602 41 N -ATOM 6456 CA ILE D 207 -25.821 9.555 6.358 1.00 50.11 C -ANISOU 6456 CA ILE D 207 5722 5548 7767 1785 532 134 C -ATOM 6457 C ILE D 207 -26.881 10.543 6.879 1.00 58.08 C -ANISOU 6457 C ILE D 207 6736 6464 8868 2065 671 136 C -ATOM 6458 O ILE D 207 -27.867 10.134 7.488 1.00 65.64 O -ANISOU 6458 O ILE D 207 7474 7536 9929 2149 775 90 O -ATOM 6459 CB ILE D 207 -26.123 9.033 4.925 1.00 67.82 C -ANISOU 6459 CB ILE D 207 7769 7969 10029 1802 330 216 C -ATOM 6460 CG1 ILE D 207 -26.883 10.060 4.089 1.00 70.84 C -ANISOU 6460 CG1 ILE D 207 8146 8314 10458 2074 256 321 C -ATOM 6461 CG2 ILE D 207 -26.891 7.714 4.980 1.00 66.95 C -ANISOU 6461 CG2 ILE D 207 7337 8104 9998 1731 302 173 C -ATOM 6462 CD1 ILE D 207 -27.193 9.567 2.692 1.00 72.62 C -ANISOU 6462 CD1 ILE D 207 8203 8716 10674 2078 39 404 C -ATOM 6463 N SER D 208 -26.658 11.842 6.668 1.00 55.99 N -ANISOU 6463 N SER D 208 6731 5980 8564 2208 691 187 N -ATOM 6464 CA SER D 208 -27.537 12.877 7.216 1.00 61.45 C -ANISOU 6464 CA SER D 208 7488 6530 9329 2492 850 186 C -ATOM 6465 C SER D 208 -28.819 13.042 6.406 1.00 65.54 C -ANISOU 6465 C SER D 208 7725 7190 9989 2788 771 281 C -ATOM 6466 O SER D 208 -28.989 12.414 5.360 1.00 65.97 O -ANISOU 6466 O SER D 208 7564 7440 10061 2751 572 349 O -ATOM 6467 CB SER D 208 -26.809 14.222 7.301 1.00 61.51 C -ANISOU 6467 CB SER D 208 7919 6221 9233 2531 906 206 C -ATOM 6468 OG SER D 208 -26.704 14.841 6.033 1.00 61.86 O -ANISOU 6468 OG SER D 208 8038 6213 9254 2639 748 333 O -ATOM 6469 N GLU D 209 -29.723 13.885 6.900 1.00 71.30 N -ANISOU 6469 N GLU D 209 8463 7836 10792 3038 903 270 N -ATOM 6470 CA GLU D 209 -30.948 14.206 6.176 1.00 72.80 C -ANISOU 6470 CA GLU D 209 8405 8171 11084 3260 780 338 C -ATOM 6471 C GLU D 209 -30.632 14.969 4.896 1.00 72.47 C -ANISOU 6471 C GLU D 209 8522 8027 10986 3358 586 475 C -ATOM 6472 O GLU D 209 -31.163 14.655 3.830 1.00 75.03 O -ANISOU 6472 O GLU D 209 8614 8537 11356 3420 378 564 O -ATOM 6473 CB GLU D 209 -31.911 15.009 7.059 1.00 80.02 C -ANISOU 6473 CB GLU D 209 9325 9014 12067 3451 958 274 C -ATOM 6474 CG GLU D 209 -32.477 14.215 8.226 1.00 82.66 C -ANISOU 6474 CG GLU D 209 9455 9494 12459 3375 1143 152 C -ATOM 6475 CD GLU D 209 -33.098 12.889 7.796 1.00 84.78 C -ANISOU 6475 CD GLU D 209 9289 10104 12820 3280 1021 157 C -ATOM 6476 OE1 GLU D 209 -32.975 11.901 8.552 1.00 81.38 O -ANISOU 6476 OE1 GLU D 209 8763 9776 12384 3091 1132 75 O -ATOM 6477 OE2 GLU D 209 -33.717 12.835 6.710 1.00 88.87 O -ANISOU 6477 OE2 GLU D 209 9578 10781 13407 3377 812 243 O -ATOM 6478 N THR D 210 -29.763 15.969 5.019 1.00 70.85 N -ANISOU 6478 N THR D 210 8731 7522 10666 3348 653 487 N -ATOM 6479 CA THR D 210 -29.237 16.698 3.871 1.00 75.72 C -ANISOU 6479 CA THR D 210 9574 8002 11192 3387 496 615 C -ATOM 6480 C THR D 210 -28.691 15.731 2.820 1.00 74.44 C -ANISOU 6480 C THR D 210 9288 8013 10984 3250 302 692 C -ATOM 6481 O THR D 210 -28.882 15.929 1.620 1.00 76.77 O -ANISOU 6481 O THR D 210 9557 8360 11250 3331 107 813 O -ATOM 6482 CB THR D 210 -28.115 17.662 4.302 1.00 77.98 C -ANISOU 6482 CB THR D 210 10342 7951 11338 3283 618 590 C -ATOM 6483 OG1 THR D 210 -28.671 18.707 5.107 1.00 82.90 O -ANISOU 6483 OG1 THR D 210 11115 8400 11984 3431 778 536 O -ATOM 6484 CG2 THR D 210 -27.417 18.274 3.090 1.00 78.69 C -ANISOU 6484 CG2 THR D 210 10679 7908 11313 3260 464 721 C -ATOM 6485 N GLY D 211 -28.038 14.671 3.287 1.00 68.99 N -ANISOU 6485 N GLY D 211 8521 7432 10261 2974 336 598 N -ATOM 6486 CA GLY D 211 -27.394 13.704 2.413 1.00 66.02 C -ANISOU 6486 CA GLY D 211 8054 7228 9804 2721 157 616 C -ATOM 6487 C GLY D 211 -28.318 12.753 1.668 1.00 61.78 C -ANISOU 6487 C GLY D 211 7131 6996 9347 2764 -12 655 C -ATOM 6488 O GLY D 211 -28.136 12.519 0.468 1.00 57.56 O -ANISOU 6488 O GLY D 211 6585 6548 8736 2712 -207 738 O -ATOM 6489 N LYS D 212 -29.294 12.189 2.377 1.00 61.94 N -ANISOU 6489 N LYS D 212 6845 7181 9509 2835 67 594 N -ATOM 6490 CA LYS D 212 -30.244 11.262 1.767 1.00 63.66 C -ANISOU 6490 CA LYS D 212 6674 7701 9813 2848 -88 622 C -ATOM 6491 C LYS D 212 -31.054 11.967 0.693 1.00 61.49 C -ANISOU 6491 C LYS D 212 6320 7471 9574 3118 -272 768 C -ATOM 6492 O LYS D 212 -31.357 11.391 -0.346 1.00 61.37 O -ANISOU 6492 O LYS D 212 6130 7653 9534 3076 -494 835 O -ATOM 6493 CB LYS D 212 -31.179 10.664 2.821 1.00 66.77 C -ANISOU 6493 CB LYS D 212 6763 8246 10361 2877 64 531 C -ATOM 6494 CG LYS D 212 -30.903 9.200 3.139 1.00 68.15 C -ANISOU 6494 CG LYS D 212 6788 8592 10514 2559 67 428 C -ATOM 6495 CD LYS D 212 -31.931 8.638 4.117 1.00 72.95 C -ANISOU 6495 CD LYS D 212 7091 9355 11272 2587 222 352 C -ATOM 6496 CE LYS D 212 -33.358 8.937 3.670 1.00 77.72 C -ANISOU 6496 CE LYS D 212 7424 10137 11968 2774 117 380 C -ATOM 6497 NZ LYS D 212 -34.379 8.236 4.506 1.00 80.62 N -ANISOU 6497 NZ LYS D 212 7502 10700 12430 2714 239 277 N -ATOM 6498 N ALA D 213 -31.387 13.223 0.958 1.00 61.16 N -ANISOU 6498 N ALA D 213 6449 7232 9559 3324 -196 785 N -ATOM 6499 CA ALA D 213 -32.150 14.045 0.029 1.00 65.01 C -ANISOU 6499 CA ALA D 213 6916 7712 10072 3534 -368 900 C -ATOM 6500 C ALA D 213 -31.334 14.371 -1.219 1.00 68.45 C -ANISOU 6500 C ALA D 213 7611 8054 10344 3505 -547 1035 C -ATOM 6501 O ALA D 213 -31.832 14.314 -2.345 1.00 71.00 O -ANISOU 6501 O ALA D 213 7823 8507 10649 3560 -783 1143 O -ATOM 6502 CB ALA D 213 -32.578 15.334 0.722 1.00 63.23 C -ANISOU 6502 CB ALA D 213 6852 7262 9911 3750 -207 883 C -ATOM 6503 N LYS D 214 -30.075 14.724 -0.984 1.00 64.91 N -ANISOU 6503 N LYS D 214 7523 7373 9767 3406 -430 1026 N -ATOM 6504 CA LYS D 214 -29.154 15.202 -2.003 1.00 64.38 C -ANISOU 6504 CA LYS D 214 7783 7156 9522 3365 -540 1138 C -ATOM 6505 C LYS D 214 -28.841 14.111 -3.018 1.00 63.15 C -ANISOU 6505 C LYS D 214 7504 7225 9264 3133 -739 1152 C -ATOM 6506 O LYS D 214 -28.725 14.378 -4.217 1.00 64.68 O -ANISOU 6506 O LYS D 214 7824 7413 9337 3159 -920 1273 O -ATOM 6507 CB LYS D 214 -27.868 15.639 -1.303 1.00 65.00 C -ANISOU 6507 CB LYS D 214 8225 6968 9502 3175 -346 1060 C -ATOM 6508 CG LYS D 214 -26.880 16.470 -2.098 1.00 67.25 C -ANISOU 6508 CG LYS D 214 8916 7025 9613 3100 -389 1150 C -ATOM 6509 CD LYS D 214 -25.909 17.104 -1.107 1.00 68.85 C -ANISOU 6509 CD LYS D 214 9436 6957 9768 2960 -171 1063 C -ATOM 6510 CE LYS D 214 -24.672 17.689 -1.752 1.00 69.16 C -ANISOU 6510 CE LYS D 214 9848 6799 9630 2765 -183 1119 C -ATOM 6511 NZ LYS D 214 -23.704 18.120 -0.698 1.00 67.81 N -ANISOU 6511 NZ LYS D 214 9929 6416 9420 2568 10 1015 N -ATOM 6512 N TYR D 215 -28.707 12.880 -2.531 1.00 58.99 N -ANISOU 6512 N TYR D 215 6758 6882 8774 2898 -697 1025 N -ATOM 6513 CA TYR D 215 -28.277 11.769 -3.373 1.00 55.57 C -ANISOU 6513 CA TYR D 215 6254 6629 8233 2640 -844 1007 C -ATOM 6514 C TYR D 215 -29.407 10.822 -3.766 1.00 55.94 C -ANISOU 6514 C TYR D 215 5912 6981 8361 2659 -1011 1010 C -ATOM 6515 O TYR D 215 -29.201 9.891 -4.539 1.00 56.76 O -ANISOU 6515 O TYR D 215 5962 7236 8369 2458 -1149 996 O -ATOM 6516 CB TYR D 215 -27.115 11.024 -2.709 1.00 53.53 C -ANISOU 6516 CB TYR D 215 6085 6331 7923 2332 -694 874 C -ATOM 6517 CG TYR D 215 -25.905 11.914 -2.540 1.00 53.02 C -ANISOU 6517 CG TYR D 215 6394 5995 7754 2262 -574 884 C -ATOM 6518 CD1 TYR D 215 -25.230 12.404 -3.652 1.00 56.21 C -ANISOU 6518 CD1 TYR D 215 7051 6302 8003 2218 -666 982 C -ATOM 6519 CD2 TYR D 215 -25.455 12.289 -1.277 1.00 50.15 C -ANISOU 6519 CD2 TYR D 215 6143 5474 7439 2226 -371 798 C -ATOM 6520 CE1 TYR D 215 -24.135 13.234 -3.520 1.00 55.95 C -ANISOU 6520 CE1 TYR D 215 7350 6030 7880 2128 -553 996 C -ATOM 6521 CE2 TYR D 215 -24.350 13.118 -1.130 1.00 50.60 C -ANISOU 6521 CE2 TYR D 215 6538 5291 7397 2131 -277 807 C -ATOM 6522 CZ TYR D 215 -23.698 13.589 -2.259 1.00 52.95 C -ANISOU 6522 CZ TYR D 215 7059 5503 7555 2079 -366 907 C -ATOM 6523 OH TYR D 215 -22.607 14.417 -2.138 1.00 50.48 O -ANISOU 6523 OH TYR D 215 7072 4961 7148 1958 -268 919 O -ATOM 6524 N LYS D 216 -30.594 11.083 -3.231 1.00 62.01 N -ANISOU 6524 N LYS D 216 6418 7837 9306 2896 -990 1026 N -ATOM 6525 CA LYS D 216 -31.803 10.330 -3.552 1.00 71.40 C -ANISOU 6525 CA LYS D 216 7199 9330 10599 2934 -1152 1042 C -ATOM 6526 C LYS D 216 -32.000 10.209 -5.057 1.00 77.34 C -ANISOU 6526 C LYS D 216 7956 10207 11223 2925 -1454 1161 C -ATOM 6527 O LYS D 216 -31.826 11.184 -5.791 1.00 79.09 O -ANISOU 6527 O LYS D 216 8413 10286 11351 3091 -1550 1291 O -ATOM 6528 CB LYS D 216 -33.023 11.036 -2.950 1.00 77.33 C -ANISOU 6528 CB LYS D 216 7760 10079 11543 3172 -1090 1034 C -ATOM 6529 CG LYS D 216 -34.351 10.306 -3.113 1.00 82.46 C -ANISOU 6529 CG LYS D 216 7991 11017 12323 3144 -1227 998 C -ATOM 6530 CD LYS D 216 -34.555 9.256 -2.030 1.00 83.20 C -ANISOU 6530 CD LYS D 216 7853 11252 12507 2968 -1051 840 C -ATOM 6531 CE LYS D 216 -35.909 8.577 -2.172 1.00 86.38 C -ANISOU 6531 CE LYS D 216 7854 11934 13034 2928 -1173 794 C -ATOM 6532 NZ LYS D 216 -37.035 9.553 -2.143 1.00 90.53 N -ANISOU 6532 NZ LYS D 216 8247 12443 13709 3201 -1199 834 N -ATOM 6533 N ALA D 217 -32.360 9.010 -5.508 1.00 80.59 N -ANISOU 6533 N ALA D 217 8135 10871 11615 2719 -1601 1115 N -ATOM 6534 CA ALA D 217 -32.677 8.768 -6.913 1.00 84.79 C -ANISOU 6534 CA ALA D 217 8648 11554 12013 2684 -1906 1215 C -ATOM 6535 C ALA D 217 -33.687 9.784 -7.438 1.00 91.06 C -ANISOU 6535 C ALA D 217 9373 12340 12884 2954 -2069 1354 C -ATOM 6536 O ALA D 217 -34.549 10.258 -6.698 1.00 94.64 O -ANISOU 6536 O ALA D 217 9643 12772 13546 3108 -1973 1323 O -ATOM 6537 CB ALA D 217 -33.204 7.358 -7.095 1.00 84.21 C -ANISOU 6537 CB ALA D 217 8282 11761 11953 2434 -2023 1129 C -ATOM 6538 OXT ALA D 217 -33.663 10.157 -8.610 1.00 93.91 O -ANISOU 6538 OXT ALA D 217 9890 12693 13099 2993 -2287 1487 O -TER 6539 ALA D 217 -HETATM 6540 OAD 3L7 A 301 22.653 12.169 14.376 1.00 60.75 O -HETATM 6541 PBA 3L7 A 301 22.534 11.057 15.525 1.00 66.65 P -HETATM 6542 OAE 3L7 A 301 21.468 10.018 15.123 1.00 61.34 O -HETATM 6543 OAB 3L7 A 301 22.136 11.700 16.830 1.00 58.23 O -HETATM 6544 CAP 3L7 A 301 24.163 10.139 15.725 1.00 73.28 C -HETATM 6545 CAK 3L7 A 301 25.461 10.764 15.216 1.00 72.85 C -HETATM 6546 OAU 3L7 A 301 26.627 10.207 15.682 1.00 69.45 O -HETATM 6547 CAJ 3L7 A 301 27.165 9.126 15.052 1.00 59.88 C -HETATM 6548 CAL 3L7 A 301 27.517 9.287 13.579 1.00 49.95 C -HETATM 6549 NAY 3L7 A 301 27.521 8.046 12.781 1.00 42.66 N -HETATM 6550 CAN 3L7 A 301 28.860 7.450 12.701 1.00 39.28 C -HETATM 6551 CAQ 3L7 A 301 28.877 5.945 12.648 1.00 37.42 C -HETATM 6552 PBB 3L7 A 301 30.472 5.138 12.617 1.00 45.66 P -HETATM 6553 OAF 3L7 A 301 31.444 5.868 11.684 1.00 46.18 O -HETATM 6554 OAG 3L7 A 301 31.063 5.124 14.091 1.00 51.22 O -HETATM 6555 OAC 3L7 A 301 30.306 3.744 12.188 1.00 42.01 O -HETATM 6556 CAM 3L7 A 301 27.017 8.334 11.416 1.00 39.77 C -HETATM 6557 CAO 3L7 A 301 27.744 9.349 10.621 1.00 38.15 C -HETATM 6558 N9 3L7 A 301 27.558 9.108 9.137 1.00 42.15 N -HETATM 6559 C4 3L7 A 301 26.435 9.513 8.408 1.00 39.09 C -HETATM 6560 N3 3L7 A 301 25.257 10.231 8.767 1.00 36.41 N -HETATM 6561 C2 3L7 A 301 24.329 10.487 7.820 1.00 40.80 C -HETATM 6562 N1 3L7 A 301 24.520 10.071 6.534 1.00 39.93 N -HETATM 6563 C6 3L7 A 301 25.627 9.382 6.116 1.00 42.00 C -HETATM 6564 O6 3L7 A 301 25.771 8.997 4.853 1.00 42.39 O -HETATM 6565 C5 3L7 A 301 26.645 9.085 7.113 1.00 42.28 C -HETATM 6566 N7 3L7 A 301 27.882 8.418 7.071 1.00 45.38 N -HETATM 6567 C8 3L7 A 301 28.403 8.442 8.315 1.00 43.08 C -HETATM 6568 MG MG A 302 23.579 6.214 14.654 1.00 28.55 MG -HETATM 6569 MG MG A 303 23.966 13.164 12.618 1.00 45.81 MG -HETATM 6570 OADA3L7 B 301 -7.444 -14.766 -20.104 0.35 62.45 O -HETATM 6571 OADB3L7 B 301 -5.877 -9.820 -14.863 0.55 31.21 O -HETATM 6572 PBAA3L7 B 301 -8.048 -13.499 -19.456 0.35 62.55 P -HETATM 6573 PBAB3L7 B 301 -6.583 -10.638 -15.957 0.55 31.96 P -HETATM 6574 OAEA3L7 B 301 -9.602 -13.726 -19.163 0.35 51.89 O -HETATM 6575 OAEB3L7 B 301 -5.851 -12.043 -16.110 0.55 27.34 O -HETATM 6576 OABA3L7 B 301 -7.334 -13.212 -18.170 0.35 60.85 O -HETATM 6577 OABB3L7 B 301 -8.017 -10.850 -15.568 0.55 26.80 O -HETATM 6578 CAPA3L7 B 301 -7.846 -12.053 -20.635 0.35 43.17 C -HETATM 6579 CAPB3L7 B 301 -6.516 -9.708 -17.589 0.55 35.50 C -HETATM 6580 CAKA3L7 B 301 -6.430 -11.544 -20.876 0.35 42.94 C -HETATM 6581 CAKB3L7 B 301 -5.877 -8.323 -17.600 0.55 39.18 C -HETATM 6582 OAUA3L7 B 301 -5.986 -10.517 -20.087 0.35 43.07 O -HETATM 6583 OAUB3L7 B 301 -6.301 -7.458 -18.576 0.55 42.73 O -HETATM 6584 CAJA3L7 B 301 -4.772 -9.960 -20.340 0.35 40.10 C -HETATM 6585 CAJB3L7 B 301 -5.369 -6.713 -19.234 0.55 42.67 C -HETATM 6586 CALA3L7 B 301 -4.538 -8.558 -19.802 0.35 40.88 C -HETATM 6587 CALB3L7 B 301 -3.936 -7.213 -19.143 0.55 41.21 C -HETATM 6588 NAYA3L7 B 301 -3.223 -7.935 -20.077 0.35 40.19 N -HETATM 6589 NAYB3L7 B 301 -3.467 -8.156 -20.185 0.55 40.45 N -HETATM 6590 CANA3L7 B 301 -3.043 -7.637 -21.512 0.35 38.92 C -HETATM 6591 CANB3L7 B 301 -3.605 -7.510 -21.490 0.55 38.42 C -HETATM 6592 CAQA3L7 B 301 -2.829 -6.174 -21.874 0.35 38.79 C -HETATM 6593 CAQB3L7 B 301 -2.627 -6.398 -21.801 0.55 38.50 C -HETATM 6594 PBBA3L7 B 301 -2.669 -5.630 -23.586 0.35 35.23 P -HETATM 6595 PBBB3L7 B 301 -2.795 -5.672 -23.428 0.55 36.74 P -HETATM 6596 OAFA3L7 B 301 -1.673 -6.490 -24.362 0.35 32.70 O -HETATM 6597 OAFB3L7 B 301 -1.938 -6.460 -24.422 0.55 33.00 O -HETATM 6598 OAGA3L7 B 301 -4.047 -5.660 -24.359 0.35 40.07 O -HETATM 6599 OAGB3L7 B 301 -4.311 -5.728 -23.872 0.55 37.73 O -HETATM 6600 OACA3L7 B 301 -2.166 -4.254 -23.590 0.35 32.06 O -HETATM 6601 OACB3L7 B 301 -2.322 -4.285 -23.400 0.55 33.25 O -HETATM 6602 CAMA3L7 B 301 -2.168 -8.840 -19.551 0.35 38.93 C -HETATM 6603 CAMB3L7 B 301 -2.025 -8.377 -19.946 0.55 38.94 C -HETATM 6604 CAOA3L7 B 301 -1.288 -9.538 -20.520 0.35 37.75 C -HETATM 6605 CAOB3L7 B 301 -1.352 -9.612 -20.420 0.55 37.66 C -HETATM 6606 N9 A3L7 B 301 0.191 -9.435 -20.198 0.35 36.62 N -HETATM 6607 N9 B3L7 B 301 0.134 -9.508 -20.140 0.55 36.82 N -HETATM 6608 C4 A3L7 B 301 0.767 -9.824 -18.978 0.35 35.52 C -HETATM 6609 C4 B3L7 B 301 0.738 -9.871 -18.924 0.55 35.64 C -HETATM 6610 N3 A3L7 B 301 0.220 -10.399 -17.797 0.35 33.86 N -HETATM 6611 N3 B3L7 B 301 0.222 -10.440 -17.727 0.55 33.86 N -HETATM 6612 C2 A3L7 B 301 1.044 -10.679 -16.758 0.35 33.32 C -HETATM 6613 C2 B3L7 B 301 1.074 -10.701 -16.703 0.55 33.35 C -HETATM 6614 N1 A3L7 B 301 2.377 -10.423 -16.835 0.35 31.94 N -HETATM 6615 N1 B3L7 B 301 2.403 -10.432 -16.814 0.55 31.38 N -HETATM 6616 C6 A3L7 B 301 2.974 -9.873 -17.938 0.35 33.16 C -HETATM 6617 C6 B3L7 B 301 2.969 -9.886 -17.935 0.55 33.20 C -HETATM 6618 O6 A3L7 B 301 4.284 -9.633 -17.976 0.35 32.91 O -HETATM 6619 O6 B3L7 B 301 4.274 -9.630 -18.012 0.55 32.82 O -HETATM 6620 C5 A3L7 B 301 2.115 -9.557 -19.074 0.35 34.73 C -HETATM 6621 C5 B3L7 B 301 2.080 -9.591 -19.053 0.55 34.33 C -HETATM 6622 N7 A3L7 B 301 2.345 -9.002 -20.342 0.35 37.28 N -HETATM 6623 N7 B3L7 B 301 2.278 -9.046 -20.332 0.55 37.76 N -HETATM 6624 C8 A3L7 B 301 1.164 -8.941 -20.992 0.35 37.40 C -HETATM 6625 C8 B3L7 B 301 1.082 -9.002 -20.957 0.55 37.38 C -HETATM 6626 MG MG B 302 -5.210 -5.329 -17.495 1.00 75.02 MG -HETATM 6627 MG MG B 303 -3.838 -12.735 -16.918 1.00 36.82 MG -HETATM 6628 OAD 3L7 C 301 7.098 7.277 29.693 0.76 32.84 O -HETATM 6629 PBA 3L7 C 301 8.003 6.646 30.843 0.76 42.99 P -HETATM 6630 OAE 3L7 C 301 9.433 6.342 30.358 0.76 39.61 O -HETATM 6631 OAB 3L7 C 301 7.368 5.365 31.307 0.76 45.48 O -HETATM 6632 CAP 3L7 C 301 8.121 7.875 32.272 0.76 51.46 C -HETATM 6633 CAK 3L7 C 301 6.815 8.492 32.781 0.76 53.49 C -HETATM 6634 OAU 3L7 C 301 6.778 9.137 33.991 0.76 52.28 O -HETATM 6635 CAJ 3L7 C 301 5.689 9.889 34.322 0.76 46.21 C -HETATM 6636 CAL 3L7 C 301 4.344 9.192 34.486 0.76 38.41 C -HETATM 6637 NAY 3L7 C 301 3.165 9.912 33.952 0.76 38.50 N -HETATM 6638 CAN 3L7 C 301 2.703 10.972 34.866 0.76 38.99 C -HETATM 6639 CAQ 3L7 C 301 1.721 11.988 34.315 0.76 37.56 C -HETATM 6640 PBB 3L7 C 301 1.206 13.332 35.388 0.76 29.00 P -HETATM 6641 OAF 3L7 C 301 0.301 14.203 34.646 0.76 23.38 O -HETATM 6642 OAG 3L7 C 301 2.459 14.134 35.895 0.76 30.40 O -HETATM 6643 OAC 3L7 C 301 0.461 12.792 36.618 0.76 32.35 O -HETATM 6644 CAM 3L7 C 301 2.064 8.943 33.723 0.76 38.34 C -HETATM 6645 CAO 3L7 C 301 1.745 7.929 34.768 0.76 32.21 C -HETATM 6646 N9 3L7 C 301 0.362 7.355 34.526 0.76 32.63 N -HETATM 6647 C4 3L7 C 301 0.091 6.254 33.709 0.76 31.75 C -HETATM 6648 N3 3L7 C 301 0.940 5.393 32.973 0.76 30.79 N -HETATM 6649 C2 3L7 C 301 0.377 4.376 32.279 0.76 28.89 C -HETATM 6650 N1 3L7 C 301 -0.969 4.183 32.269 0.76 27.45 N -HETATM 6651 C6 3L7 C 301 -1.851 4.972 32.963 0.76 29.01 C -HETATM 6652 O6 3L7 C 301 -3.171 4.753 32.937 0.76 28.01 O -HETATM 6653 C5 3L7 C 301 -1.274 6.072 33.721 0.76 32.09 C -HETATM 6654 N7 3L7 C 301 -1.823 7.074 34.529 0.76 33.26 N -HETATM 6655 C8 3L7 C 301 -0.813 7.834 34.991 0.76 33.04 C -HETATM 6656 MG MG C 302 4.650 10.536 29.631 1.00 27.57 MG -HETATM 6657 MG MG C 303 5.548 4.520 32.837 1.00 41.66 MG -HETATM 6658 OAD 3L7 D 301 -23.450 -3.557 -5.767 1.00 80.13 O -HETATM 6659 PBA 3L7 D 301 -23.548 -3.063 -4.356 1.00 81.70 P -HETATM 6660 OAE 3L7 D 301 -23.594 -1.466 -4.354 1.00115.71 O -HETATM 6661 OAB 3L7 D 301 -22.311 -3.544 -3.571 1.00 79.26 O -HETATM 6662 CAP 3L7 D 301 -25.105 -3.719 -3.525 1.00 78.09 C -HETATM 6663 CAK 3L7 D 301 -25.603 -5.119 -3.877 1.00 76.52 C -HETATM 6664 OAU 3L7 D 301 -26.950 -5.349 -3.762 1.00 74.40 O -HETATM 6665 CAJ 3L7 D 301 -27.439 -6.041 -2.691 1.00 68.27 C -HETATM 6666 CAL 3L7 D 301 -27.919 -5.258 -1.476 1.00 60.41 C -HETATM 6667 NAY 3L7 D 301 -27.586 -5.819 -0.145 1.00 54.55 N -HETATM 6668 CAN 3L7 D 301 -28.666 -6.675 0.377 1.00 52.51 C -HETATM 6669 CAQ 3L7 D 301 -28.264 -7.882 1.198 1.00 50.36 C -HETATM 6670 PBB 3L7 D 301 -29.549 -8.981 1.821 1.00 45.20 P -HETATM 6671 OAF 3L7 D 301 -29.977 -9.959 0.648 1.00 40.70 O -HETATM 6672 OAG 3L7 D 301 -30.756 -8.181 2.323 1.00 41.87 O -HETATM 6673 OAC 3L7 D 301 -28.994 -9.755 2.951 1.00 37.63 O -HETATM 6674 CAM 3L7 D 301 -27.324 -4.709 0.805 1.00 52.48 C -HETATM 6675 CAO 3L7 D 301 -28.260 -3.555 0.847 1.00 48.58 C -HETATM 6676 N9 3L7 D 301 -28.212 -2.863 2.197 1.00 43.31 N -HETATM 6677 C4 3L7 D 301 -27.370 -1.791 2.508 1.00 42.40 C -HETATM 6678 N3 3L7 D 301 -26.423 -1.071 1.739 1.00 39.74 N -HETATM 6679 C2 3L7 D 301 -25.747 -0.053 2.331 1.00 41.42 C -HETATM 6680 N1 3L7 D 301 -25.962 0.280 3.630 1.00 37.89 N -HETATM 6681 C6 3L7 D 301 -26.863 -0.375 4.431 1.00 40.68 C -HETATM 6682 O6 3L7 D 301 -27.071 -0.031 5.698 1.00 37.04 O -HETATM 6683 C5 3L7 D 301 -27.607 -1.472 3.827 1.00 42.29 C -HETATM 6684 N7 3L7 D 301 -28.586 -2.351 4.305 1.00 41.39 N -HETATM 6685 C8 3L7 D 301 -28.925 -3.180 3.298 1.00 40.50 C -HETATM 6686 MG MG D 302 -23.121 -6.852 -1.000 1.00 26.21 MG -HETATM 6687 MG MG D 303 -25.740 -0.547 -2.907 1.00 45.21 MG -HETATM 6688 O HOH A 401 8.285 12.435 3.609 1.00 26.92 O -HETATM 6689 O HOH A 402 15.858 5.506 11.235 1.00 26.44 O -HETATM 6690 O HOH A 403 7.968 -9.955 9.122 1.00 31.00 O -HETATM 6691 O HOH A 404 15.153 17.070 10.439 1.00 37.46 O -HETATM 6692 O HOH A 405 8.043 9.541 12.387 1.00 31.36 O -HETATM 6693 O HOH A 406 9.452 -7.993 2.006 1.00 28.91 O -HETATM 6694 O HOH A 407 5.285 -2.739 1.644 1.00 34.85 O -HETATM 6695 O HOH A 408 2.520 -3.775 14.955 1.00 34.48 O -HETATM 6696 O HOH A 409 21.818 -7.596 -3.050 1.00 36.85 O -HETATM 6697 O HOH A 410 7.847 4.557 8.277 1.00 39.70 O -HETATM 6698 O HOH A 411 26.827 3.052 14.226 1.00 40.20 O -HETATM 6699 O HOH A 412 29.274 2.203 14.147 1.00 35.93 O -HETATM 6700 O HOH A 413 17.013 3.268 30.713 1.00 55.05 O -HETATM 6701 O HOH A 414 16.313 16.919 13.791 1.00 38.84 O -HETATM 6702 O HOH A 415 7.180 0.493 17.200 1.00 35.11 O -HETATM 6703 O HOH A 416 31.129 -0.010 7.421 1.00 45.01 O -HETATM 6704 O HOH A 417 2.613 -8.212 19.409 1.00 38.95 O -HETATM 6705 O HOH A 418 21.781 7.104 15.752 1.00 34.65 O -HETATM 6706 O HOH A 419 6.589 -6.816 1.984 1.00 40.18 O -HETATM 6707 O HOH A 420 10.213 -15.289 2.395 1.00 37.44 O -HETATM 6708 O HOH A 421 13.357 15.745 -12.744 1.00 48.12 O -HETATM 6709 O HOH A 422 5.914 -8.693 10.295 1.00 28.72 O -HETATM 6710 O HOH A 423 5.084 -0.291 20.682 1.00 39.43 O -HETATM 6711 O HOH A 424 31.852 -2.928 34.185 1.00 41.21 O -HETATM 6712 O HOH A 425 17.140 -11.431 4.702 1.00 39.12 O -HETATM 6713 O HOH A 426 25.446 6.113 13.118 1.00 42.19 O -HETATM 6714 O HOH A 427 15.894 14.239 -9.052 1.00 43.14 O -HETATM 6715 O HOH A 428 4.949 -4.655 4.467 1.00 41.01 O -HETATM 6716 O HOH A 429 6.155 18.339 -2.900 1.00 46.46 O -HETATM 6717 O HOH A 430 19.572 -11.545 4.541 1.00 46.34 O -HETATM 6718 O HOH A 431 20.186 -4.324 -5.176 1.00 56.18 O -HETATM 6719 O HOH A 432 33.206 -3.142 21.297 1.00 47.60 O -HETATM 6720 O HOH A 433 27.421 -7.322 8.447 1.00 52.95 O -HETATM 6721 O HOH A 434 27.635 -7.378 16.483 1.00 49.57 O -HETATM 6722 O HOH A 435 18.166 0.252 -8.440 1.00 48.88 O -HETATM 6723 O HOH A 436 7.555 17.406 -9.004 1.00 51.35 O -HETATM 6724 O HOH A 437 13.530 0.212 -9.954 1.00 46.42 O -HETATM 6725 O HOH A 438 10.765 -15.830 12.300 1.00 43.22 O -HETATM 6726 O HOH A 439 20.020 -2.143 -5.767 1.00 43.23 O -HETATM 6727 O HOH A 440 8.457 16.597 5.965 1.00 38.55 O -HETATM 6728 O HOH A 441 28.295 12.437 -1.042 1.00 46.97 O -HETATM 6729 O HOH A 442 23.608 -8.043 -5.331 1.00 57.06 O -HETATM 6730 O HOH A 443 9.737 -11.251 30.633 1.00 53.54 O -HETATM 6731 O HOH A 444 23.721 8.443 19.042 1.00 48.84 O -HETATM 6732 O HOH A 445 35.050 2.827 19.371 1.00 54.81 O -HETATM 6733 O HOH A 446 17.138 -17.212 22.969 1.00 38.19 O -HETATM 6734 O HOH A 447 16.555 -17.159 20.348 1.00 40.45 O -HETATM 6735 O HOH A 448 21.574 10.133 11.630 1.00 40.78 O -HETATM 6736 O HOH A 449 24.783 6.915 16.371 1.00 42.43 O -HETATM 6737 O HOH A 450 23.355 8.260 13.669 1.00 40.58 O -HETATM 6738 O HOH A 451 24.751 13.628 10.173 1.00 49.38 O -HETATM 6739 O HOH A 452 24.162 10.678 11.479 1.00 50.24 O -HETATM 6740 O HOH A 453 4.747 -0.719 5.120 1.00 72.45 O -HETATM 6741 O HOH B 401 -3.756 -2.392 -23.030 1.00 38.23 O -HETATM 6742 O HOH B 402 -9.729 1.810 -2.340 1.00 32.81 O -HETATM 6743 O HOH B 403 2.823 -11.238 -0.455 1.00 26.30 O -HETATM 6744 O HOH B 404 -1.231 -3.104 -1.421 1.00 32.12 O -HETATM 6745 O HOH B 405 -3.512 -15.975 -7.485 1.00 32.23 O -HETATM 6746 O HOH B 406 12.191 -14.926 0.735 1.00 31.05 O -HETATM 6747 O HOH B 407 14.259 -16.922 1.917 1.00 32.08 O -HETATM 6748 O HOH B 408 2.453 -5.878 1.347 1.00 44.12 O -HETATM 6749 O HOH B 409 -3.066 -4.242 -9.497 1.00 28.32 O -HETATM 6750 O HOH B 410 12.831 7.003 -14.408 1.00 35.79 O -HETATM 6751 O HOH B 411 19.476 -8.130 -4.396 1.00 40.84 O -HETATM 6752 O HOH B 412 1.545 11.184 -13.507 1.00 39.76 O -HETATM 6753 O HOH B 413 -2.326 10.455 -0.829 1.00 31.18 O -HETATM 6754 O HOH B 414 -3.151 -9.335 -14.781 1.00 48.25 O -HETATM 6755 O HOH B 415 8.639 15.702 -6.127 1.00 35.93 O -HETATM 6756 O HOH B 416 0.227 -15.213 -0.342 1.00 36.38 O -HETATM 6757 O HOH B 417 5.824 3.873 1.367 1.00 39.14 O -HETATM 6758 O HOH B 418 6.192 8.869 -3.008 1.00 38.33 O -HETATM 6759 O HOH B 419 6.677 16.070 -4.487 1.00 37.09 O -HETATM 6760 O HOH B 420 -11.778 10.939 1.622 1.00 39.84 O -HETATM 6761 O HOH B 421 -1.571 -13.722 -17.150 1.00 37.71 O -HETATM 6762 O HOH B 422 4.799 11.651 -11.555 1.00 41.31 O -HETATM 6763 O HOH B 423 -7.575 6.340 2.416 1.00 37.62 O -HETATM 6764 O HOH B 424 7.615 -22.814 -5.182 1.00 54.16 O -HETATM 6765 O HOH B 425 5.071 -11.366 -0.776 1.00 39.89 O -HETATM 6766 O HOH B 426 -3.118 -24.925 -6.408 1.00 55.77 O -HETATM 6767 O HOH B 427 4.804 -23.843 1.242 1.00 49.16 O -HETATM 6768 O HOH B 428 -3.239 5.472 1.876 1.00 48.08 O -HETATM 6769 O HOH B 429 -0.614 -13.446 -19.983 1.00 44.52 O -HETATM 6770 O HOH B 430 -0.661 -8.881 -24.121 1.00 46.32 O -HETATM 6771 O HOH B 431 -2.867 3.446 0.941 1.00 57.86 O -HETATM 6772 O HOH B 432 -1.913 -16.951 -0.407 1.00 47.25 O -HETATM 6773 O HOH B 433 2.771 7.918 -20.720 1.00 53.73 O -HETATM 6774 O HOH B 434 -1.660 -11.369 -24.025 1.00 57.55 O -HETATM 6775 O HOH B 435 12.561 -4.765 -23.088 1.00 47.25 O -HETATM 6776 O HOH B 436 -16.157 -10.593 -12.696 1.00 66.01 O -HETATM 6777 O HOH B 437 11.168 8.860 -15.647 1.00 47.90 O -HETATM 6778 O HOH B 438 5.787 7.417 -0.077 1.00 61.28 O -HETATM 6779 O HOH B 439 2.854 9.225 -15.411 1.00 42.17 O -HETATM 6780 O HOH B 440 12.353 9.221 -18.555 1.00 52.30 O -HETATM 6781 O HOH B 441 -1.525 -16.322 -17.882 1.00 44.43 O -HETATM 6782 O HOH B 442 -12.228 -7.454 -27.862 1.00 68.46 O -HETATM 6783 O HOH B 443 16.218 0.437 -20.785 1.00 52.72 O -HETATM 6784 O HOH B 444 16.255 0.046 -13.476 1.00 38.85 O -HETATM 6785 O HOH B 445 11.320 -22.724 0.362 1.00 62.53 O -HETATM 6786 O HOH B 446 -2.539 -10.786 -16.969 1.00 37.23 O -HETATM 6787 O HOH B 447 -4.640 -14.523 -16.855 1.00 41.20 O -HETATM 6788 O HOH B 448 -4.091 -12.701 -19.169 1.00 44.51 O -HETATM 6789 O HOH C 401 -0.720 11.582 -2.648 1.00 35.45 O -HETATM 6790 O HOH C 402 1.635 15.962 33.011 1.00 34.96 O -HETATM 6791 O HOH C 403 2.813 6.511 22.406 1.00 34.91 O -HETATM 6792 O HOH C 404 -5.163 10.541 38.929 1.00 44.85 O -HETATM 6793 O HOH C 405 3.050 10.694 31.284 1.00 32.10 O -HETATM 6794 O HOH C 406 4.693 9.655 6.385 1.00 38.94 O -HETATM 6795 O HOH C 407 2.570 14.206 31.073 1.00 38.56 O -HETATM 6796 O HOH C 408 -3.653 14.581 8.560 1.00 37.52 O -HETATM 6797 O HOH C 409 -14.122 16.562 10.177 1.00 34.83 O -HETATM 6798 O HOH C 410 -7.275 -12.382 21.429 1.00 38.57 O -HETATM 6799 O HOH C 411 6.548 9.696 28.325 1.00 35.13 O -HETATM 6800 O HOH C 412 3.720 3.362 33.995 1.00 41.27 O -HETATM 6801 O HOH C 413 -0.163 10.390 37.550 1.00 44.89 O -HETATM 6802 O HOH C 414 7.056 14.930 4.000 1.00 36.81 O -HETATM 6803 O HOH C 415 2.481 4.827 35.892 1.00 46.81 O -HETATM 6804 O HOH C 416 -14.101 19.608 11.498 1.00 48.24 O -HETATM 6805 O HOH C 417 -6.981 4.232 9.656 1.00 39.96 O -HETATM 6806 O HOH C 418 3.169 13.347 38.128 1.00 45.87 O -HETATM 6807 O HOH C 419 -7.308 18.439 20.543 1.00 39.67 O -HETATM 6808 O HOH C 420 -4.916 6.929 8.288 1.00 43.07 O -HETATM 6809 O HOH C 421 3.857 5.917 32.232 1.00 38.33 O -HETATM 6810 O HOH C 422 -9.222 9.218 39.865 1.00 42.85 O -HETATM 6811 O HOH C 423 0.677 -14.588 20.041 1.00 46.44 O -HETATM 6812 O HOH C 424 4.464 -8.197 21.195 1.00 38.98 O -HETATM 6813 O HOH C 425 -12.387 16.686 8.286 1.00 45.27 O -HETATM 6814 O HOH C 426 -9.396 10.443 10.624 1.00 36.27 O -HETATM 6815 O HOH C 427 -6.860 19.362 17.887 1.00 38.18 O -HETATM 6816 O HOH C 428 -17.161 6.029 25.009 1.00 55.16 O -HETATM 6817 O HOH C 429 0.573 -5.969 19.114 1.00 36.33 O -HETATM 6818 O HOH C 430 -19.731 7.780 24.217 1.00 56.89 O -HETATM 6819 O HOH C 431 -16.141 12.919 21.751 1.00 42.49 O -HETATM 6820 O HOH C 432 10.873 2.374 34.640 1.00 61.69 O -HETATM 6821 O HOH C 433 11.619 33.828 22.456 1.00 54.18 O -HETATM 6822 O HOH C 434 1.579 2.478 15.064 1.00 33.13 O -HETATM 6823 O HOH C 435 -1.854 -6.265 19.906 1.00 39.76 O -HETATM 6824 O HOH C 436 4.295 1.589 35.741 1.00 47.42 O -HETATM 6825 O HOH C 437 -1.529 13.027 7.233 1.00 41.62 O -HETATM 6826 O HOH C 438 5.162 5.721 35.219 1.00 57.38 O -HETATM 6827 O HOH C 439 3.332 -16.913 24.752 1.00 53.04 O -HETATM 6828 O HOH C 440 10.201 10.638 30.798 1.00 46.98 O -HETATM 6829 O HOH C 441 4.486 25.097 34.091 1.00 50.52 O -HETATM 6830 O HOH C 442 0.645 23.994 3.676 1.00 64.08 O -HETATM 6831 O HOH C 443 -9.780 17.547 16.498 1.00 48.77 O -HETATM 6832 O HOH C 444 -2.493 -14.174 19.509 1.00 44.26 O -HETATM 6833 O HOH C 445 9.887 -1.063 28.028 1.00 46.58 O -HETATM 6834 O HOH C 446 4.872 20.001 -0.319 1.00 75.11 O -HETATM 6835 O HOH C 447 18.298 12.100 23.921 1.00 55.46 O -HETATM 6836 O HOH C 448 6.007 11.907 30.780 1.00 43.65 O -HETATM 6837 O HOH C 449 8.209 11.052 31.886 1.00 58.64 O -HETATM 6838 O HOH C 450 5.937 9.684 30.549 1.00 57.32 O -HETATM 6839 O HOH C 451 4.537 8.021 30.284 1.00 38.58 O -HETATM 6840 O HOH C 452 6.895 3.469 34.081 1.00 60.93 O -HETATM 6841 O HOH C 453 6.953 5.881 33.941 1.00 81.26 O -HETATM 6842 O HOH D 401 -23.433 -4.534 -1.203 1.00 37.81 O -HETATM 6843 O HOH D 402 -18.933 6.530 -4.292 1.00 33.33 O -HETATM 6844 O HOH D 403 -15.950 -3.272 1.572 1.00 29.54 O -HETATM 6845 O HOH D 404 -5.664 -7.416 -1.515 1.00 29.90 O -HETATM 6846 O HOH D 405 -27.223 -11.794 2.109 1.00 30.50 O -HETATM 6847 O HOH D 406 -19.911 3.947 -6.880 1.00 33.94 O -HETATM 6848 O HOH D 407 -8.761 -27.419 4.266 1.00 35.75 O -HETATM 6849 O HOH D 408 -4.755 -0.751 12.922 1.00 37.43 O -HETATM 6850 O HOH D 409 1.831 -13.506 0.831 1.00 37.34 O -HETATM 6851 O HOH D 410 -24.925 -6.879 0.361 1.00 43.00 O -HETATM 6852 O HOH D 411 -6.541 -6.758 15.826 1.00 36.26 O -HETATM 6853 O HOH D 412 -11.917 9.022 3.464 1.00 29.81 O -HETATM 6854 O HOH D 413 -16.675 -14.010 13.222 1.00 35.07 O -HETATM 6855 O HOH D 414 5.445 -18.660 3.707 1.00 38.79 O -HETATM 6856 O HOH D 415 -18.451 -25.781 3.562 1.00 41.71 O -HETATM 6857 O HOH D 416 -2.247 -10.334 9.034 1.00 31.96 O -HETATM 6858 O HOH D 417 -8.564 0.450 3.729 1.00 43.74 O -HETATM 6859 O HOH D 418 -12.764 -13.000 16.178 1.00 46.54 O -HETATM 6860 O HOH D 419 -6.726 -15.625 -9.362 1.00 35.98 O -HETATM 6861 O HOH D 420 -8.489 -25.785 6.150 1.00 39.61 O -HETATM 6862 O HOH D 421 -25.324 -10.073 1.328 1.00 38.09 O -HETATM 6863 O HOH D 422 -0.145 -8.007 2.246 1.00 37.08 O -HETATM 6864 O HOH D 423 -18.973 -7.216 20.875 1.00 40.13 O -HETATM 6865 O HOH D 424 -3.845 -11.568 10.929 1.00 34.88 O -HETATM 6866 O HOH D 425 -26.783 0.697 -1.277 1.00 42.87 O -HETATM 6867 O HOH D 426 4.283 -20.579 10.894 1.00 52.54 O -HETATM 6868 O HOH D 427 -3.620 -3.940 11.752 1.00 45.34 O -HETATM 6869 O HOH D 428 -14.152 -15.122 13.142 1.00 38.76 O -HETATM 6870 O HOH D 429 -26.789 -19.632 8.406 1.00 47.29 O -HETATM 6871 O HOH D 430 -5.281 -13.132 19.782 1.00 47.94 O -HETATM 6872 O HOH D 431 -28.672 2.806 -2.242 1.00 47.44 O -HETATM 6873 O HOH D 432 -32.010 -8.850 -0.845 1.00 47.67 O -HETATM 6874 O HOH D 433 -13.025 10.720 -0.588 1.00 38.55 O -HETATM 6875 O HOH D 434 -28.803 -21.421 0.040 1.00 45.18 O -HETATM 6876 O HOH D 435 -28.145 -3.223 21.441 1.00 58.47 O -HETATM 6877 O HOH D 436 -22.403 -15.423 12.456 1.00 51.31 O -HETATM 6878 O HOH D 437 -31.748 -2.602 5.676 1.00 56.07 O -HETATM 6879 O HOH D 438 -22.188 -20.045 5.413 1.00 47.48 O -HETATM 6880 O HOH D 439 -31.600 4.619 8.440 1.00 52.41 O -HETATM 6881 O HOH D 440 -4.673 -23.669 8.606 1.00 55.66 O -HETATM 6882 O HOH D 441 -19.172 18.673 15.915 1.00 49.55 O -HETATM 6883 O HOH D 442 -24.281 -21.451 -13.546 1.00 55.78 O -HETATM 6884 O HOH D 443 -0.294 -5.429 1.187 1.00 51.06 O -HETATM 6885 O HOH D 444 -23.913 -13.482 12.955 1.00 53.07 O -HETATM 6886 O HOH D 445 -21.686 -6.298 -2.486 1.00 36.64 O -HETATM 6887 O HOH D 446 -26.329 0.263 -5.030 1.00 53.49 O -HETATM 6888 O HOH D 447 -24.178 -7.868 -2.229 1.00 49.33 O -CONECT 910 6568 -CONECT 911 6568 -CONECT 918 6568 -CONECT 1385 6569 -CONECT 2539 6626 -CONECT 2540 6626 -CONECT 2542 6626 -CONECT 2551 6626 -CONECT 3021 6627 -CONECT 4172 6656 -CONECT 4180 6656 -CONECT 4653 6657 -CONECT 5847 6686 -CONECT 5855 6686 -CONECT 6332 6687 -CONECT 6540 6541 6569 -CONECT 6541 6540 6542 6543 6544 -CONECT 6542 6541 -CONECT 6543 6541 -CONECT 6544 6541 6545 -CONECT 6545 6544 6546 -CONECT 6546 6545 6547 -CONECT 6547 6546 6548 -CONECT 6548 6547 6549 -CONECT 6549 6548 6550 6556 -CONECT 6550 6549 6551 -CONECT 6551 6550 6552 -CONECT 6552 6551 6553 6554 6555 -CONECT 6553 6552 -CONECT 6554 6552 -CONECT 6555 6552 -CONECT 6556 6549 6557 -CONECT 6557 6556 6558 -CONECT 6558 6557 6559 6567 -CONECT 6559 6558 6560 6565 -CONECT 6560 6559 6561 -CONECT 6561 6560 6562 -CONECT 6562 6561 6563 -CONECT 6563 6562 6564 6565 -CONECT 6564 6563 -CONECT 6565 6559 6563 6566 -CONECT 6566 6565 6567 -CONECT 6567 6558 6566 -CONECT 6568 910 911 918 6705 -CONECT 6568 6713 6736 6737 -CONECT 6569 1385 6540 6738 6739 -CONECT 6570 6572 -CONECT 6571 6573 -CONECT 6572 6570 6574 6576 6578 -CONECT 6573 6571 6575 6577 6579 -CONECT 6574 6572 -CONECT 6575 6573 6627 -CONECT 6576 6572 -CONECT 6577 6573 -CONECT 6578 6572 6580 -CONECT 6579 6573 6581 -CONECT 6580 6578 6582 -CONECT 6581 6579 6583 -CONECT 6582 6580 6584 -CONECT 6583 6581 6585 6626 -CONECT 6584 6582 6586 -CONECT 6585 6583 6587 -CONECT 6586 6584 6588 -CONECT 6587 6585 6589 -CONECT 6588 6586 6590 6602 -CONECT 6589 6587 6591 6603 -CONECT 6590 6588 6592 -CONECT 6591 6589 6593 -CONECT 6592 6590 6594 -CONECT 6593 6591 6595 -CONECT 6594 6592 6596 6598 6600 -CONECT 6595 6593 6597 6599 6601 -CONECT 6596 6594 -CONECT 6597 6595 -CONECT 6598 6594 -CONECT 6599 6595 -CONECT 6600 6594 -CONECT 6601 6595 -CONECT 6602 6588 6604 -CONECT 6603 6589 6605 -CONECT 6604 6602 6606 -CONECT 6605 6603 6607 -CONECT 6606 6604 6608 6624 -CONECT 6607 6605 6609 6625 -CONECT 6608 6606 6610 6620 -CONECT 6609 6607 6611 6621 -CONECT 6610 6608 6612 -CONECT 6611 6609 6613 -CONECT 6612 6610 6614 -CONECT 6613 6611 6615 -CONECT 6614 6612 6616 -CONECT 6615 6613 6617 -CONECT 6616 6614 6618 6620 -CONECT 6617 6615 6619 6621 -CONECT 6618 6616 -CONECT 6619 6617 -CONECT 6620 6608 6616 6622 -CONECT 6621 6609 6617 6623 -CONECT 6622 6620 6624 -CONECT 6623 6621 6625 -CONECT 6624 6606 6622 -CONECT 6625 6607 6623 -CONECT 6626 2539 2540 2542 2551 -CONECT 6626 6583 -CONECT 6627 3021 6575 6761 6786 -CONECT 6627 6787 6788 -CONECT 6628 6629 -CONECT 6629 6628 6630 6631 6632 -CONECT 6630 6629 -CONECT 6631 6629 6657 -CONECT 6632 6629 6633 -CONECT 6633 6632 6634 -CONECT 6634 6633 6635 -CONECT 6635 6634 6636 -CONECT 6636 6635 6637 -CONECT 6637 6636 6638 6644 -CONECT 6638 6637 6639 -CONECT 6639 6638 6640 -CONECT 6640 6639 6641 6642 6643 -CONECT 6641 6640 -CONECT 6642 6640 -CONECT 6643 6640 -CONECT 6644 6637 6645 -CONECT 6645 6644 6646 -CONECT 6646 6645 6647 6655 -CONECT 6647 6646 6648 6653 -CONECT 6648 6647 6649 -CONECT 6649 6648 6650 -CONECT 6650 6649 6651 -CONECT 6651 6650 6652 6653 -CONECT 6652 6651 -CONECT 6653 6647 6651 6654 -CONECT 6654 6653 6655 -CONECT 6655 6646 6654 -CONECT 6656 4172 4180 6793 6799 -CONECT 6656 6836 6838 6839 -CONECT 6657 4653 6631 6800 6809 -CONECT 6657 6826 6840 6841 -CONECT 6658 6659 -CONECT 6659 6658 6660 6661 6662 -CONECT 6660 6659 6687 -CONECT 6661 6659 -CONECT 6662 6659 6663 -CONECT 6663 6662 6664 -CONECT 6664 6663 6665 -CONECT 6665 6664 6666 -CONECT 6666 6665 6667 -CONECT 6667 6666 6668 6674 -CONECT 6668 6667 6669 -CONECT 6669 6668 6670 -CONECT 6670 6669 6671 6672 6673 -CONECT 6671 6670 -CONECT 6672 6670 -CONECT 6673 6670 -CONECT 6674 6667 6675 -CONECT 6675 6674 6676 -CONECT 6676 6675 6677 6685 -CONECT 6677 6676 6678 6683 -CONECT 6678 6677 6679 -CONECT 6679 6678 6680 -CONECT 6680 6679 6681 -CONECT 6681 6680 6682 6683 -CONECT 6682 6681 -CONECT 6683 6677 6681 6684 -CONECT 6684 6683 6685 -CONECT 6685 6676 6684 -CONECT 6686 5847 5855 6842 6851 -CONECT 6686 6886 6888 -CONECT 6687 6332 6660 6866 6887 -CONECT 6705 6568 -CONECT 6713 6568 -CONECT 6736 6568 -CONECT 6737 6568 -CONECT 6738 6569 -CONECT 6739 6569 -CONECT 6761 6627 -CONECT 6786 6627 -CONECT 6787 6627 -CONECT 6788 6627 -CONECT 6793 6656 -CONECT 6799 6656 -CONECT 6800 6657 -CONECT 6809 6657 -CONECT 6826 6657 -CONECT 6836 6656 -CONECT 6838 6656 -CONECT 6839 6656 -CONECT 6840 6657 -CONECT 6841 6657 -CONECT 6842 6686 -CONECT 6851 6686 -CONECT 6866 6687 -CONECT 6886 6686 -CONECT 6887 6687 -CONECT 6888 6686 -MASTER 991 0 12 29 38 0 36 6 6682 4 195 68 -END |