Browse entries in the PDBbind-CN Database
HEADER HYDROLASE/HYDROLASE INHIBITOR 28-AUG-18 6MAV TITLE COMPLEX OF TISSUE INHIBITOR OF METALLOPROTEINASE-1 (TIMP-1) MUTANT TITLE 2 L34G WITH MATRIX METALLOPROTEINASE-3 CATALYTIC DOMAIN (MMP-3CD) COMPND MOL_ID: 1; COMPND 2 MOLECULE: STROMELYSIN-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SL-1,MATRIX METALLOPROTEINASE-3,MMP-3,TRANSIN-1; COMPND 5 EC: 3.4.24.17; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: METALLOPROTEINASE INHIBITOR 1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: ERYTHROID-POTENTIATING ACTIVITY,EPA,FIBROBLAST COLLAGENASE COMPND 11 INHIBITOR,COLLAGENASE INHIBITOR,TISSUE INHIBITOR OF COMPND 12 METALLOPROTEINASES 1,TIMP-1; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: MMP3, STMY1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: TIMP1, CLGI, TIMP; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS PROTEASE INHIBITOR, MATRIX METALLOPROTEINASE-3 (MMP-3), TISSUE KEYWDS 2 INHIBITOR OF METALLOPROTEINASE-1 (TIMP-1), HYDROLASE-HYDROLASE KEYWDS 3 INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.RAEESZADEH-SARMAZDEH,E.RADISKY REVDAT 3 27-NOV-19 6MAV 1 REMARK REVDAT 2 26-JUN-19 6MAV 1 JRNL REVDAT 1 15-MAY-19 6MAV 0 JRNL AUTH M.RAEESZADEH-SARMAZDEH,K.A.GREENE,B.SANKARAN,G.P.DOWNEY, JRNL AUTH 2 D.C.RADISKY,E.S.RADISKY JRNL TITL DIRECTED EVOLUTION OF THE METALLOPROTEINASE INHIBITOR TIMP-1 JRNL TITL 2 REVEALS THAT ITS N- AND C-TERMINAL DOMAINS COOPERATE IN JRNL TITL 3 MATRIX METALLOPROTEINASE RECOGNITION. JRNL REF J.BIOL.CHEM. V. 294 9476 2019 JRNL REFN ESSN 1083-351X JRNL PMID 31040180 JRNL DOI 10.1074/JBC.RA119.008321 REMARK 2 REMARK 2 RESOLUTION. 2.37 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.59 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 19361 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.298 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 940 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 52.6007 - 4.5330 0.99 2946 158 0.1539 0.2286 REMARK 3 2 4.5330 - 3.5982 0.99 2693 156 0.1882 0.2713 REMARK 3 3 3.5982 - 3.1434 0.98 2634 131 0.2628 0.3562 REMARK 3 4 3.1434 - 2.8561 0.97 2602 134 0.2974 0.3877 REMARK 3 5 2.8561 - 2.6514 0.97 2580 107 0.3223 0.4230 REMARK 3 6 2.6514 - 2.4950 0.94 2463 120 0.3350 0.4036 REMARK 3 7 2.4950 - 2.3701 0.95 2503 134 0.3610 0.4444 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.890 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.47 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 : 0.010 2724 REMARK 3 ANGLE : 1.349 3697 REMARK 3 CHIRALITY : 0.051 401 REMARK 3 PLANARITY : 0.008 477 REMARK 3 DIHEDRAL : 16.369 968 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.1213 36.4216 13.5715 REMARK 3 T TENSOR REMARK 3 T11: 0.6927 T22: 0.5472 REMARK 3 T33: 0.8082 T12: -0.1281 REMARK 3 T13: -0.0502 T23: -0.1825 REMARK 3 L TENSOR REMARK 3 L11: 7.9948 L22: 4.7825 REMARK 3 L33: 3.8298 L12: -3.3463 REMARK 3 L13: 2.3663 L23: -0.8041 REMARK 3 S TENSOR REMARK 3 S11: -0.1619 S12: -0.4766 S13: 0.4742 REMARK 3 S21: 0.0574 S22: 0.1510 S23: -0.6436 REMARK 3 S31: -0.5691 S32: -0.1390 S33: -0.0286 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.3157 24.0632 9.5945 REMARK 3 T TENSOR REMARK 3 T11: 0.7075 T22: 0.7253 REMARK 3 T33: 0.7085 T12: 0.0823 REMARK 3 T13: -0.0602 T23: -0.2019 REMARK 3 L TENSOR REMARK 3 L11: 2.6625 L22: 7.8571 REMARK 3 L33: 4.2633 L12: 1.3607 REMARK 3 L13: 0.0617 L23: -0.0443 REMARK 3 S TENSOR REMARK 3 S11: 0.2350 S12: 0.3190 S13: -0.4877 REMARK 3 S21: -0.9635 S22: -0.3668 S23: -1.1668 REMARK 3 S31: 0.6041 S32: 1.5385 S33: 0.0666 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 181 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.0082 22.2508 19.5879 REMARK 3 T TENSOR REMARK 3 T11: 0.9607 T22: 0.4478 REMARK 3 T33: 0.4418 T12: -0.2000 REMARK 3 T13: -0.2045 T23: -0.1226 REMARK 3 L TENSOR REMARK 3 L11: 4.1940 L22: 5.4901 REMARK 3 L33: 2.0710 L12: 0.7272 REMARK 3 L13: -0.3378 L23: 2.4644 REMARK 3 S TENSOR REMARK 3 S11: 0.1064 S12: -1.0313 S13: -0.7692 REMARK 3 S21: 0.9218 S22: -0.2564 S23: 0.3345 REMARK 3 S31: 0.2612 S32: 0.4299 S33: 0.0271 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 217 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.9849 21.6407 6.5202 REMARK 3 T TENSOR REMARK 3 T11: 0.7590 T22: 0.4232 REMARK 3 T33: 0.6401 T12: -0.0222 REMARK 3 T13: -0.0671 T23: -0.2116 REMARK 3 L TENSOR REMARK 3 L11: 4.0189 L22: 3.4099 REMARK 3 L33: 1.5778 L12: -0.6934 REMARK 3 L13: -0.0189 L23: -2.0917 REMARK 3 S TENSOR REMARK 3 S11: -0.0458 S12: 0.2073 S13: -0.4014 REMARK 3 S21: -0.1943 S22: -0.1916 S23: 0.2156 REMARK 3 S31: -0.0928 S32: -0.1547 S33: 0.2055 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 218 THROUGH 235 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.9835 22.6199 -1.5860 REMARK 3 T TENSOR REMARK 3 T11: 1.0323 T22: 0.7378 REMARK 3 T33: 0.6215 T12: 0.0134 REMARK 3 T13: 0.0221 T23: -0.1813 REMARK 3 L TENSOR REMARK 3 L11: 2.6329 L22: 4.3586 REMARK 3 L33: 0.9525 L12: 0.1028 REMARK 3 L13: 0.4940 L23: 0.8730 REMARK 3 S TENSOR REMARK 3 S11: -0.1159 S12: 0.6430 S13: 0.0338 REMARK 3 S21: -0.2722 S22: 0.3854 S23: -0.5807 REMARK 3 S31: 0.6840 S32: 0.7760 S33: -0.0182 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 236 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3693 38.3403 1.5545 REMARK 3 T TENSOR REMARK 3 T11: 1.1277 T22: 0.3618 REMARK 3 T33: 0.6930 T12: -0.0277 REMARK 3 T13: 0.0602 T23: -0.2101 REMARK 3 L TENSOR REMARK 3 L11: 3.3960 L22: 2.0101 REMARK 3 L33: 3.8994 L12: 0.4781 REMARK 3 L13: -1.9920 L23: 0.4713 REMARK 3 S TENSOR REMARK 3 S11: 0.2019 S12: 0.5415 S13: -0.0713 REMARK 3 S21: -0.8792 S22: 0.0116 S23: 1.1008 REMARK 3 S31: -1.6412 S32: -0.1241 S33: 1.2447 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.4306 16.3791 15.5044 REMARK 3 T TENSOR REMARK 3 T11: 0.9424 T22: 0.5022 REMARK 3 T33: 0.5941 T12: -0.1185 REMARK 3 T13: 0.0970 T23: -0.1194 REMARK 3 L TENSOR REMARK 3 L11: 0.5454 L22: 4.5394 REMARK 3 L33: 3.6138 L12: 0.7464 REMARK 3 L13: 0.2857 L23: 2.3760 REMARK 3 S TENSOR REMARK 3 S11: 0.0321 S12: -0.5283 S13: 0.1458 REMARK 3 S21: 1.0554 S22: -0.2512 S23: 0.3108 REMARK 3 S31: 0.4093 S32: -0.1586 S33: 0.0920 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 42 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.2221 31.0704 25.9830 REMARK 3 T TENSOR REMARK 3 T11: 1.0805 T22: 0.6014 REMARK 3 T33: 0.6207 T12: -0.1095 REMARK 3 T13: 0.0909 T23: -0.2100 REMARK 3 L TENSOR REMARK 3 L11: 6.6004 L22: 3.0855 REMARK 3 L33: 5.1912 L12: -1.9514 REMARK 3 L13: 0.9335 L23: 1.8165 REMARK 3 S TENSOR REMARK 3 S11: -0.7906 S12: -0.2429 S13: 0.2598 REMARK 3 S21: 0.8497 S22: 0.4493 S23: -0.1942 REMARK 3 S31: -0.0003 S32: 0.2445 S33: 0.2456 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 43 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.4541 16.7835 25.7378 REMARK 3 T TENSOR REMARK 3 T11: 1.0414 T22: 0.7862 REMARK 3 T33: 0.9466 T12: -0.2852 REMARK 3 T13: 0.3718 T23: -0.1485 REMARK 3 L TENSOR REMARK 3 L11: 2.8770 L22: 1.4526 REMARK 3 L33: 7.3896 L12: 0.8407 REMARK 3 L13: -2.6129 L23: 1.6176 REMARK 3 S TENSOR REMARK 3 S11: 0.9753 S12: -0.2990 S13: 0.4002 REMARK 3 S21: 2.0443 S22: -0.9549 S23: 0.6791 REMARK 3 S31: 0.1882 S32: -2.4681 S33: -0.0190 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.1622 29.9125 17.5890 REMARK 3 T TENSOR REMARK 3 T11: 0.9776 T22: 0.4319 REMARK 3 T33: 0.6695 T12: -0.0428 REMARK 3 T13: 0.0673 T23: -0.1304 REMARK 3 L TENSOR REMARK 3 L11: 5.4774 L22: 1.7672 REMARK 3 L33: 3.1156 L12: -0.2279 REMARK 3 L13: -2.0906 L23: -0.3019 REMARK 3 S TENSOR REMARK 3 S11: 0.2266 S12: -0.0800 S13: 1.2657 REMARK 3 S21: 0.5252 S22: 0.0033 S23: 0.2348 REMARK 3 S31: -0.6206 S32: 0.0591 S33: -0.4212 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.2114 20.1575 21.0685 REMARK 3 T TENSOR REMARK 3 T11: 0.9989 T22: 0.3634 REMARK 3 T33: 0.4670 T12: -0.0582 REMARK 3 T13: 0.0237 T23: -0.0778 REMARK 3 L TENSOR REMARK 3 L11: 2.5417 L22: 5.6924 REMARK 3 L33: 3.4261 L12: 1.8831 REMARK 3 L13: -0.8110 L23: 2.8243 REMARK 3 S TENSOR REMARK 3 S11: -0.0449 S12: -0.9225 S13: 0.0529 REMARK 3 S21: 0.7649 S22: -0.3051 S23: -1.1821 REMARK 3 S31: 0.1331 S32: 0.4094 S33: -0.3207 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.7768 13.9806 10.7595 REMARK 3 T TENSOR REMARK 3 T11: 0.8138 T22: 0.6161 REMARK 3 T33: 0.7852 T12: -0.1155 REMARK 3 T13: 0.2173 T23: -0.2282 REMARK 3 L TENSOR REMARK 3 L11: 2.6542 L22: 6.3704 REMARK 3 L33: 3.7034 L12: 1.0017 REMARK 3 L13: -0.0977 L23: 0.1768 REMARK 3 S TENSOR REMARK 3 S11: 0.1335 S12: 0.3278 S13: -0.4465 REMARK 3 S21: 0.5573 S22: -0.9506 S23: 1.6966 REMARK 3 S31: 0.5794 S32: -2.0742 S33: 0.6536 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 124 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.1315 2.8640 11.7344 REMARK 3 T TENSOR REMARK 3 T11: 1.4000 T22: 0.4825 REMARK 3 T33: 0.7444 T12: -0.0013 REMARK 3 T13: 0.1350 T23: -0.1502 REMARK 3 L TENSOR REMARK 3 L11: 2.8228 L22: 8.4205 REMARK 3 L33: 6.7273 L12: 2.6203 REMARK 3 L13: 0.9868 L23: -1.5495 REMARK 3 S TENSOR REMARK 3 S11: 1.1423 S12: -1.1093 S13: -0.1732 REMARK 3 S21: 1.8756 S22: -0.7815 S23: 1.2280 REMARK 3 S31: 0.2417 S32: 1.4496 S33: -0.5046 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 132 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1329 2.6774 2.8208 REMARK 3 T TENSOR REMARK 3 T11: 1.1211 T22: 0.4700 REMARK 3 T33: 0.7487 T12: 0.0875 REMARK 3 T13: -0.1434 T23: -0.1260 REMARK 3 L TENSOR REMARK 3 L11: 2.3837 L22: 1.5954 REMARK 3 L33: 1.9619 L12: -1.9527 REMARK 3 L13: 2.1662 L23: -1.7695 REMARK 3 S TENSOR REMARK 3 S11: -0.4968 S12: 0.0281 S13: 1.0855 REMARK 3 S21: 0.4166 S22: 0.0830 S23: 0.0398 REMARK 3 S31: -0.0539 S32: 0.4802 S33: 0.1746 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 144 THROUGH 158 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.7160 11.3868 0.6616 REMARK 3 T TENSOR REMARK 3 T11: 1.0829 T22: 0.5631 REMARK 3 T33: 0.5628 T12: -0.1940 REMARK 3 T13: 0.0792 T23: -0.0622 REMARK 3 L TENSOR REMARK 3 L11: 6.6708 L22: 5.5958 REMARK 3 L33: 1.6612 L12: 1.3319 REMARK 3 L13: -0.5534 L23: 0.9600 REMARK 3 S TENSOR REMARK 3 S11: -0.1019 S12: 1.0898 S13: -0.0124 REMARK 3 S21: -0.9289 S22: 0.6273 S23: 0.0355 REMARK 3 S31: 0.4259 S32: 0.2774 S33: -0.5684 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.2772 2.6299 4.5834 REMARK 3 T TENSOR REMARK 3 T11: 1.0645 T22: 0.4377 REMARK 3 T33: 0.6315 T12: -0.0609 REMARK 3 T13: -0.0082 T23: -0.1337 REMARK 3 L TENSOR REMARK 3 L11: 4.0266 L22: 2.4215 REMARK 3 L33: 3.9411 L12: 1.2332 REMARK 3 L13: -0.5076 L23: 0.1385 REMARK 3 S TENSOR REMARK 3 S11: -0.3209 S12: -0.0583 S13: -0.0705 REMARK 3 S21: 0.0498 S22: -0.1535 S23: 0.1270 REMARK 3 S31: 0.6160 S32: -0.5327 S33: 0.4747 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 6MAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-18. REMARK 100 THE DEPOSITION ID IS D_1000236143. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-NOV-17 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 5.5-6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19911 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370 REMARK 200 RESOLUTION RANGE LOW (A) : 52.590 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.10 REMARK 200 R MERGE (I) : 0.06602 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 12.70 REMARK 200 R MERGE FOR SHELL (I) : 0.79070 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.090 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1UEA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE 0.1 M BIS-TRIS: REMARK 280 HCL, PH 5.5, 17 % (W/V) PEG 10,000, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 214.21733 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 107.10867 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 160.66300 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.55433 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 267.77167 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 214.21733 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 107.10867 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 53.55433 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 160.66300 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 267.77167 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 210 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 218 LIES ON A SPECIAL POSITION. 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 PHE A 83 REMARK 465 ARG A 84 REMARK 465 THR A 85 REMARK 465 PHE A 86 REMARK 465 PRO A 248 REMARK 465 PRO A 249 REMARK 465 PRO A 250 REMARK 465 LEU B 52 REMARK 465 GLY B 53 REMARK 465 ASP B 54 REMARK 465 ALA B 55 REMARK 465 ALA B 56 REMARK 465 ARG B 180 REMARK 465 SER B 181 REMARK 465 GLN B 182 REMARK 465 ILE B 183 REMARK 465 ALA B 184 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS B 41 CG CD CE NZ REMARK 470 ARG B 59 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 75 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 79 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 118 CG CD CE NZ REMARK 470 LYS B 138 CG CD CE NZ REMARK 470 GLN B 153 CG CD OE1 NE2 REMARK 470 LYS B 157 CG CD CE NZ 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 NH2 ARG B 20 OH TYR B 46 2.07 REMARK 500 ND2 ASN A 103 O PHE A 146 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 411 O HOH A 411 10665 2.14 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 ARG A 149 -125.47 55.19 REMARK 500 HIS A 151 51.40 -152.80 REMARK 500 ASN A 162 -104.83 47.35 REMARK 500 THR A 191 38.05 -148.72 REMARK 500 SER A 225 96.19 68.01 REMARK 500 ARG A 231 40.91 -107.16 REMARK 500 THR B 32 -22.77 129.19 REMARK 500 PHE B 49 -2.63 -55.92 REMARK 500 CYS B 70 28.98 85.36 REMARK 500 SER B 76 151.05 -45.26 REMARK 500 ASN B 78 101.96 60.86 REMARK 500 SER B 80 36.58 71.32 REMARK 500 CYS B 137 -52.80 73.58 REMARK 500 LYS B 138 105.74 64.91 REMARK 500 GLU B 156 -8.65 -53.37 REMARK 500 HIS B 163 -6.04 -146.18 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 GLU B 125 GLU B 126 135.77 REMARK 500 ILE B 135 PRO B 136 146.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 415 DISTANCE = 6.35 ANGSTROMS REMARK 525 HOH B 218 DISTANCE = 6.75 ANGSTROMS 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 CA A 302 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 107 OD1 REMARK 620 2 ASP A 107 OD2 57.8 REMARK 620 3 ASP A 182 O 155.7 144.2 REMARK 620 4 ASP A 182 OD1 86.7 112.8 74.6 REMARK 620 5 GLU A 184 O 121.6 69.8 82.5 139.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 303 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 141 O REMARK 620 2 GLY A 173 O 162.0 REMARK 620 3 ASN A 175 O 104.4 93.5 REMARK 620 4 ASP A 177 OD1 91.9 84.4 96.4 REMARK 620 5 HOH A 402 O 84.3 99.2 84.7 176.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 305 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 151 NE2 REMARK 620 2 ASP A 153 OD2 107.4 REMARK 620 3 HIS A 166 NE2 120.0 109.9 REMARK 620 4 HIS A 179 ND1 96.0 108.5 113.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 158 OD1 REMARK 620 2 GLY A 159 O 85.5 REMARK 620 3 GLY A 161 O 80.7 95.3 REMARK 620 4 VAL A 163 O 98.2 169.3 75.5 REMARK 620 5 ASP A 181 OD2 112.0 73.4 161.7 113.9 REMARK 620 6 GLU A 184 OE2 165.7 91.1 85.8 82.9 80.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 304 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 201 NE2 REMARK 620 2 HIS A 205 NE2 93.5 REMARK 620 3 HIS A 211 NE2 121.1 98.1 REMARK 620 4 CYS B 1 N 102.7 87.9 135.2 REMARK 620 5 CYS B 1 O 86.1 170.9 89.8 83.3 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 305 DBREF 6MAV A 83 250 UNP P08254 MMP3_HUMAN 100 267 DBREF 6MAV B 1 184 UNP P01033 TIMP1_HUMAN 24 207 SEQADV 6MAV GLY B 34 UNP P01033 LEU 57 ENGINEERED MUTATION SEQRES 1 A 168 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR SEQRES 2 A 168 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU SEQRES 3 A 168 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU SEQRES 4 A 168 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG SEQRES 5 A 168 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA SEQRES 6 A 168 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO SEQRES 7 A 168 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY SEQRES 8 A 168 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP SEQRES 9 A 168 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA SEQRES 10 A 168 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER SEQRES 11 A 168 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER SEQRES 12 A 168 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP SEQRES 13 A 168 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO SEQRES 1 B 184 CYS THR CYS VAL PRO PRO HIS PRO GLN THR ALA PHE CYS SEQRES 2 B 184 ASN SER ASP LEU VAL ILE ARG ALA LYS PHE VAL GLY THR SEQRES 3 B 184 PRO GLU VAL ASN GLN THR THR GLY TYR GLN ARG TYR GLU SEQRES 4 B 184 ILE LYS MET THR LYS MET TYR LYS GLY PHE GLN ALA LEU SEQRES 5 B 184 GLY ASP ALA ALA ASP ILE ARG PHE VAL TYR THR PRO ALA SEQRES 6 B 184 MET GLU SER VAL CYS GLY TYR PHE HIS ARG SER HIS ASN SEQRES 7 B 184 ARG SER GLU GLU PHE LEU ILE ALA GLY LYS LEU GLN ASP SEQRES 8 B 184 GLY LEU LEU HIS ILE THR THR CYS SER PHE VAL ALA PRO SEQRES 9 B 184 TRP ASN SER LEU SER LEU ALA GLN ARG ARG GLY PHE THR SEQRES 10 B 184 LYS THR TYR THR VAL GLY CYS GLU GLU CYS THR VAL PHE SEQRES 11 B 184 PRO CYS LEU SER ILE PRO CYS LYS LEU GLN SER GLY THR SEQRES 12 B 184 HIS CYS LEU TRP THR ASP GLN LEU LEU GLN GLY SER GLU SEQRES 13 B 184 LYS GLY PHE GLN SER ARG HIS LEU ALA CYS LEU PRO ARG SEQRES 14 B 184 GLU PRO GLY LEU CYS THR TRP GLN SER LEU ARG SER GLN SEQRES 15 B 184 ILE ALA HET CA A 301 1 HET CA A 302 1 HET CA A 303 1 HET ZN A 304 1 HET ZN A 305 1 HETNAM CA CALCIUM ION HETNAM ZN ZINC ION FORMUL 3 CA 3(CA 2+) FORMUL 6 ZN 2(ZN 2+) FORMUL 8 HOH *33(H2 O) HELIX 1 AA1 PRO A 109 GLU A 126 1 18 HELIX 2 AA2 LEU A 195 GLY A 208 1 14 HELIX 3 AA3 ASP A 228 PHE A 232 5 5 HELIX 4 AA4 SER A 235 GLY A 247 1 13 HELIX 5 AA5 HIS B 7 SER B 15 1 9 HELIX 6 AA6 MET B 66 CYS B 70 5 5 HELIX 7 AA7 ASN B 106 LEU B 108 5 3 HELIX 8 AA8 SER B 109 THR B 117 1 9 HELIX 9 AA9 THR B 119 CYS B 124 5 6 HELIX 10 AB1 THR B 148 GLY B 154 1 7 HELIX 11 AB2 GLY B 158 HIS B 163 1 6 SHEET 1 AA1 6 THR A 131 LEU A 135 0 SHEET 2 AA1 6 HIS A 96 ILE A 101 1 N TYR A 99 O LEU A 135 SHEET 3 AA1 6 ILE A 142 ALA A 147 1 O ILE A 144 N ARG A 100 SHEET 4 AA1 6 ALA A 178 ASP A 181 1 O PHE A 180 N ALA A 147 SHEET 5 AA1 6 VAL A 163 ALA A 167 -1 N HIS A 166 O HIS A 179 SHEET 6 AA1 6 THR B 2 CYS B 3 -1 O THR B 2 N LEU A 164 SHEET 1 AA2 2 TRP A 186 THR A 187 0 SHEET 2 AA2 2 THR A 193 ASN A 194 1 O THR A 193 N THR A 187 SHEET 1 AA3 5 GLU B 28 VAL B 29 0 SHEET 2 AA3 5 TYR B 35 LYS B 47 -1 O ARG B 37 N GLU B 28 SHEET 3 AA3 5 LEU B 17 PHE B 23 -1 N VAL B 18 O TYR B 46 SHEET 4 AA3 5 PHE B 83 GLN B 90 -1 O PHE B 83 N ALA B 21 SHEET 5 AA3 5 VAL B 102 PRO B 104 -1 O ALA B 103 N LEU B 84 SHEET 1 AA4 6 GLU B 28 VAL B 29 0 SHEET 2 AA4 6 TYR B 35 LYS B 47 -1 O ARG B 37 N GLU B 28 SHEET 3 AA4 6 PHE B 60 PRO B 64 -1 O VAL B 61 N TYR B 38 SHEET 4 AA4 6 LEU B 93 HIS B 95 1 O LEU B 94 N TYR B 62 SHEET 5 AA4 6 PHE B 83 GLN B 90 -1 N LYS B 88 O HIS B 95 SHEET 6 AA4 6 VAL B 102 PRO B 104 -1 O ALA B 103 N LEU B 84 SHEET 1 AA5 2 THR B 128 PRO B 131 0 SHEET 2 AA5 2 HIS B 144 TRP B 147 1 O CYS B 145 N PHE B 130 SHEET 1 AA6 2 LEU B 164 GLU B 170 0 SHEET 2 AA6 2 LEU B 173 SER B 178 -1 O THR B 175 N LEU B 167 SSBOND 1 CYS B 1 CYS B 70 1555 1555 2.06 SSBOND 2 CYS B 3 CYS B 99 1555 1555 2.02 SSBOND 3 CYS B 13 CYS B 124 1555 1555 2.05 SSBOND 4 CYS B 127 CYS B 174 1555 1555 2.05 SSBOND 5 CYS B 132 CYS B 137 1555 1555 2.04 SSBOND 6 CYS B 145 CYS B 166 1555 1555 2.07 LINK OD1 ASP A 107 CA CA A 302 1555 1555 2.32 LINK OD2 ASP A 107 CA CA A 302 1555 1555 2.21 LINK O ASP A 141 CA CA A 303 1555 1555 2.32 LINK NE2 HIS A 151 ZN ZN A 305 1555 1555 2.08 LINK OD2 ASP A 153 ZN ZN A 305 1555 1555 1.99 LINK OD1 ASP A 158 CA CA A 301 1555 1555 2.38 LINK O GLY A 159 CA CA A 301 1555 1555 2.35 LINK O GLY A 161 CA CA A 301 1555 1555 2.38 LINK O VAL A 163 CA CA A 301 1555 1555 2.20 LINK NE2 HIS A 166 ZN ZN A 305 1555 1555 2.10 LINK O GLY A 173 CA CA A 303 1555 1555 2.19 LINK O ASN A 175 CA CA A 303 1555 1555 2.19 LINK OD1 ASP A 177 CA CA A 303 1555 1555 2.67 LINK ND1 HIS A 179 ZN ZN A 305 1555 1555 1.93 LINK OD2 ASP A 181 CA CA A 301 1555 1555 2.21 LINK O ASP A 182 CA CA A 302 1555 1555 2.20 LINK OD1 ASP A 182 CA CA A 302 1555 1555 2.45 LINK O GLU A 184 CA CA A 302 1555 1555 2.43 LINK OE2 GLU A 184 CA CA A 301 1555 1555 2.39 LINK NE2 HIS A 201 ZN ZN A 304 1555 1555 2.15 LINK NE2 HIS A 205 ZN ZN A 304 1555 1555 2.25 LINK NE2 HIS A 211 ZN ZN A 304 1555 1555 1.87 LINK N CYS B 1 ZN ZN A 304 1555 1555 1.98 LINK O CYS B 1 ZN ZN A 304 1555 1555 2.28 LINK CA CA A 303 O HOH A 402 1555 1555 2.65 SITE 1 AC1 6 ASP A 158 GLY A 159 GLY A 161 VAL A 163 SITE 2 AC1 6 ASP A 181 GLU A 184 SITE 1 AC2 3 ASP A 107 ASP A 182 GLU A 184 SITE 1 AC3 5 ASP A 141 GLY A 173 ASN A 175 ASP A 177 SITE 2 AC3 5 HOH A 402 SITE 1 AC4 4 HIS A 201 HIS A 205 HIS A 211 CYS B 1 SITE 1 AC5 4 HIS A 151 ASP A 153 HIS A 166 HIS A 179 CRYST1 69.703 69.703 321.326 90.00 90.00 120.00 P 65 2 2 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014347 0.008283 0.000000 0.00000 SCALE2 0.000000 0.016566 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003112 0.00000 ATOM 1 N PRO A 87 4.990 46.266 18.419 1.00 84.35 N ANISOU 1 N PRO A 87 10686 12303 9060 3679 -734 -3439 N ATOM 2 CA PRO A 87 6.189 46.210 17.581 1.00 91.60 C ANISOU 2 CA PRO A 87 11878 12568 10357 3181 -866 -3389 C ATOM 3 C PRO A 87 7.011 44.942 17.788 1.00 92.67 C ANISOU 3 C PRO A 87 11898 12834 10479 2755 -727 -3108 C ATOM 4 O PRO A 87 6.494 43.949 18.314 1.00 84.87 O ANISOU 4 O PRO A 87 10589 12393 9265 2754 -510 -2825 O ATOM 5 CB PRO A 87 6.975 47.447 18.032 1.00 83.28 C ANISOU 5 CB PRO A 87 11155 11084 9402 3406 -1168 -3892 C ATOM 6 CG PRO A 87 5.898 48.408 18.586 1.00 96.47 C ANISOU 6 CG PRO A 87 12802 13006 10847 4053 -1251 -4232 C ATOM 7 CD PRO A 87 4.577 47.659 18.632 1.00 98.15 C ANISOU 7 CD PRO A 87 12621 13895 10776 4199 -947 -3897 C ATOM 8 N GLY A 88 8.274 44.992 17.364 1.00106.55 N ANISOU 8 N GLY A 88 13891 14080 12513 2404 -853 -3155 N ATOM 9 CA GLY A 88 9.235 43.922 17.591 1.00107.12 C ANISOU 9 CA GLY A 88 13895 14202 12606 2037 -772 -2963 C ATOM 10 C GLY A 88 9.515 43.047 16.378 1.00 94.68 C ANISOU 10 C GLY A 88 12292 12381 11303 1561 -677 -2605 C ATOM 11 O GLY A 88 8.966 41.959 16.268 1.00 89.81 O ANISOU 11 O GLY A 88 11422 12071 10630 1426 -518 -2291 O ATOM 12 N ILE A 89 10.373 43.511 15.471 1.00103.44 N ANISOU 12 N ILE A 89 13642 12942 12717 1322 -782 -2648 N ATOM 13 CA ILE A 89 10.713 42.751 14.254 1.00101.47 C ANISOU 13 CA ILE A 89 13398 12486 12671 941 -698 -2357 C ATOM 14 C ILE A 89 12.119 42.173 14.347 1.00 96.29 C ANISOU 14 C ILE A 89 12777 11656 12153 623 -692 -2322 C ATOM 15 O ILE A 89 13.100 42.846 14.027 1.00 98.33 O ANISOU 15 O ILE A 89 13219 11507 12636 506 -782 -2425 O ATOM 16 CB ILE A 89 10.629 43.620 12.985 1.00 97.09 C ANISOU 16 CB ILE A 89 13061 11511 12318 925 -764 -2333 C ATOM 17 CG1 ILE A 89 9.246 44.258 12.864 1.00107.94 C ANISOU 17 CG1 ILE A 89 14404 13031 13578 1270 -802 -2383 C ATOM 18 CG2 ILE A 89 10.938 42.802 11.749 1.00 89.73 C ANISOU 18 CG2 ILE A 89 12133 10466 11493 618 -675 -2064 C ATOM 19 CD1 ILE A 89 9.128 45.233 11.715 1.00108.41 C ANISOU 19 CD1 ILE A 89 14696 12679 13818 1316 -893 -2346 C ATOM 20 N PRO A 90 12.224 40.923 14.799 1.00 80.82 N ANISOU 20 N PRO A 90 10614 9994 10099 483 -593 -2151 N ATOM 21 CA PRO A 90 13.557 40.406 15.102 1.00 70.82 C ANISOU 21 CA PRO A 90 9362 8607 8941 248 -610 -2155 C ATOM 22 C PRO A 90 14.395 40.139 13.851 1.00 73.16 C ANISOU 22 C PRO A 90 9756 8540 9500 -59 -577 -2033 C ATOM 23 O PRO A 90 13.930 39.514 12.894 1.00 67.13 O ANISOU 23 O PRO A 90 8953 7788 8765 -157 -504 -1850 O ATOM 24 CB PRO A 90 13.264 39.112 15.868 1.00 76.12 C ANISOU 24 CB PRO A 90 9776 9698 9448 216 -513 -1945 C ATOM 25 CG PRO A 90 11.901 38.715 15.443 1.00 85.49 C ANISOU 25 CG PRO A 90 10797 11103 10581 279 -425 -1744 C ATOM 26 CD PRO A 90 11.154 39.987 15.177 1.00 85.17 C ANISOU 26 CD PRO A 90 10886 10996 10478 550 -478 -1934 C ATOM 27 N LYS A 91 15.624 40.649 13.878 1.00 68.06 N ANISOU 27 N LYS A 91 9220 7593 9044 -180 -645 -2149 N ATOM 28 CA LYS A 91 16.607 40.415 12.843 1.00 62.86 C ANISOU 28 CA LYS A 91 8614 6657 8615 -444 -575 -2017 C ATOM 29 C LYS A 91 18.002 40.536 13.439 1.00 61.42 C ANISOU 29 C LYS A 91 8406 6310 8622 -586 -653 -2129 C ATOM 30 O LYS A 91 18.223 41.304 14.361 1.00 63.28 O ANISOU 30 O LYS A 91 8675 6486 8884 -468 -819 -2364 O ATOM 31 CB LYS A 91 16.438 41.404 11.682 1.00 64.99 C ANISOU 31 CB LYS A 91 9057 6626 9011 -426 -553 -1950 C ATOM 32 CG LYS A 91 16.428 42.879 12.083 1.00 75.73 C ANISOU 32 CG LYS A 91 10552 7711 10511 -278 -709 -2138 C ATOM 33 CD LYS A 91 16.657 43.803 10.871 1.00 73.02 C ANISOU 33 CD LYS A 91 10365 6983 10398 -341 -672 -1965 C ATOM 34 CE LYS A 91 18.077 43.656 10.317 1.00 70.29 C ANISOU 34 CE LYS A 91 9977 6414 10316 -634 -571 -1790 C ATOM 35 NZ LYS A 91 18.436 44.745 9.365 1.00 78.20 N ANISOU 35 NZ LYS A 91 11094 7021 11596 -695 -537 -1573 N ATOM 36 N TRP A 92 18.947 39.772 12.915 1.00 65.31 N ANISOU 36 N TRP A 92 8828 6738 9249 -812 -560 -1992 N ATOM 37 CA TRP A 92 20.323 39.915 13.339 1.00 64.25 C ANISOU 37 CA TRP A 92 8632 6431 9350 -963 -634 -2074 C ATOM 38 C TRP A 92 20.807 41.295 12.987 1.00 59.68 C ANISOU 38 C TRP A 92 8151 5456 9066 -1008 -708 -2131 C ATOM 39 O TRP A 92 20.568 41.781 11.893 1.00 71.67 O ANISOU 39 O TRP A 92 9765 6803 10661 -1033 -592 -1956 O ATOM 40 CB TRP A 92 21.191 38.860 12.679 1.00 62.88 C ANISOU 40 CB TRP A 92 8348 6270 9272 -1161 -493 -1901 C ATOM 41 CG TRP A 92 20.849 37.481 13.128 1.00 69.36 C ANISOU 41 CG TRP A 92 9055 7389 9909 -1140 -480 -1846 C ATOM 42 CD1 TRP A 92 20.075 36.572 12.477 1.00 60.93 C ANISOU 42 CD1 TRP A 92 7971 6455 8723 -1124 -394 -1708 C ATOM 43 CD2 TRP A 92 21.276 36.855 14.351 1.00 70.09 C ANISOU 43 CD2 TRP A 92 9022 7657 9953 -1129 -589 -1908 C ATOM 44 NE1 TRP A 92 19.995 35.411 13.215 1.00 60.40 N ANISOU 44 NE1 TRP A 92 7762 6589 8600 -1136 -438 -1650 N ATOM 45 CE2 TRP A 92 20.726 35.560 14.360 1.00 65.86 C ANISOU 45 CE2 TRP A 92 8391 7331 9303 -1130 -536 -1743 C ATOM 46 CE3 TRP A 92 22.075 37.267 15.427 1.00 67.57 C ANISOU 46 CE3 TRP A 92 8658 7328 9689 -1107 -755 -2086 C ATOM 47 CZ2 TRP A 92 20.950 34.667 15.419 1.00 55.00 C ANISOU 47 CZ2 TRP A 92 6879 6161 7860 -1113 -608 -1684 C ATOM 48 CZ3 TRP A 92 22.297 36.374 16.480 1.00 59.56 C ANISOU 48 CZ3 TRP A 92 7521 6570 8537 -1056 -835 -2068 C ATOM 49 CH2 TRP A 92 21.729 35.088 16.463 1.00 54.92 C ANISOU 49 CH2 TRP A 92 6843 6194 7830 -1062 -741 -1834 C ATOM 50 N ARG A 93 21.489 41.942 13.907 1.00 72.09 N ANISOU 50 N ARG A 93 9694 6867 10829 -1010 -927 -2364 N ATOM 51 CA ARG A 93 21.981 43.267 13.591 1.00 82.34 C ANISOU 51 CA ARG A 93 11056 7704 12527 -1087 -1046 -2403 C ATOM 52 C ARG A 93 23.345 43.161 12.956 1.00 82.95 C ANISOU 52 C ARG A 93 10979 7559 12980 -1393 -943 -2193 C ATOM 53 O ARG A 93 23.856 44.118 12.393 1.00 90.08 O ANISOU 53 O ARG A 93 11877 8068 14282 -1532 -957 -2065 O ATOM 54 CB ARG A 93 22.012 44.132 14.831 1.00 81.31 C ANISOU 54 CB ARG A 93 10966 7446 12483 -917 -1398 -2809 C ATOM 55 CG ARG A 93 20.647 44.264 15.461 1.00 91.71 C ANISOU 55 CG ARG A 93 12407 9053 13385 -556 -1461 -3008 C ATOM 56 CD ARG A 93 20.751 44.701 16.901 1.00110.70 C ANISOU 56 CD ARG A 93 14824 11539 15700 -307 -1793 -3458 C ATOM 57 NE ARG A 93 19.484 44.525 17.598 1.00123.39 N ANISOU 57 NE ARG A 93 16482 13601 16798 74 -1771 -3591 N ATOM 58 CZ ARG A 93 19.356 43.872 18.748 1.00131.08 C ANISOU 58 CZ ARG A 93 17376 15054 17376 284 -1815 -3729 C ATOM 59 NH1 ARG A 93 20.421 43.332 19.330 1.00133.98 N ANISOU 59 NH1 ARG A 93 17633 15478 17793 156 -1919 -3782 N ATOM 60 NH2 ARG A 93 18.165 43.754 19.318 1.00130.82 N ANISOU 60 NH2 ARG A 93 17348 15469 16888 638 -1744 -3779 N ATOM 61 N LYS A 94 23.918 41.971 13.033 1.00 80.76 N ANISOU 61 N LYS A 94 10553 7540 12591 -1486 -829 -2124 N ATOM 62 CA LYS A 94 25.199 41.694 12.407 1.00 79.70 C ANISOU 62 CA LYS A 94 10232 7292 12760 -1733 -686 -1917 C ATOM 63 C LYS A 94 24.954 40.948 11.091 1.00 89.53 C ANISOU 63 C LYS A 94 11501 8718 13797 -1738 -351 -1609 C ATOM 64 O LYS A 94 24.127 40.030 11.032 1.00 80.22 O ANISOU 64 O LYS A 94 10394 7830 12254 -1603 -290 -1627 O ATOM 65 CB LYS A 94 26.073 40.873 13.353 1.00 70.89 C ANISOU 65 CB LYS A 94 8929 6335 11671 -1787 -815 -2077 C ATOM 66 CG LYS A 94 25.262 40.165 14.453 1.00 70.06 C ANISOU 66 CG LYS A 94 8895 6577 11148 -1566 -949 -2286 C ATOM 67 CD LYS A 94 26.095 39.150 15.243 1.00 79.52 C ANISOU 67 CD LYS A 94 9915 7977 12322 -1599 -1035 -2350 C ATOM 68 CE LYS A 94 25.590 39.018 16.672 1.00 87.56 C ANISOU 68 CE LYS A 94 10980 9256 13032 -1368 -1273 -2594 C ATOM 69 NZ LYS A 94 25.738 40.307 17.424 1.00 85.20 N ANISOU 69 NZ LYS A 94 10740 8749 12881 -1274 -1587 -2929 N ATOM 70 N THR A 95 25.645 41.343 10.027 1.00 91.00 N ANISOU 70 N THR A 95 11615 8744 14215 -1874 -145 -1320 N ATOM 71 CA THR A 95 25.514 40.609 8.772 1.00 79.91 C ANISOU 71 CA THR A 95 10237 7572 12555 -1814 158 -1073 C ATOM 72 C THR A 95 26.303 39.325 8.849 1.00 80.34 C ANISOU 72 C THR A 95 10110 7861 12555 -1848 236 -1113 C ATOM 73 O THR A 95 25.797 38.255 8.518 1.00 97.93 O ANISOU 73 O THR A 95 12397 10342 14470 -1717 298 -1153 O ATOM 74 CB THR A 95 26.022 41.394 7.579 1.00 81.96 C ANISOU 74 CB THR A 95 10462 7677 13002 -1892 401 -697 C ATOM 75 OG1 THR A 95 27.442 41.501 7.682 1.00 88.86 O ANISOU 75 OG1 THR A 95 11049 8432 14281 -2108 462 -578 O ATOM 76 CG2 THR A 95 25.401 42.782 7.533 1.00 85.10 C ANISOU 76 CG2 THR A 95 11019 7742 13574 -1882 289 -621 C ATOM 77 N HIS A 96 27.556 39.433 9.275 1.00 73.70 N ANISOU 77 N HIS A 96 9031 6905 12068 -2021 202 -1110 N ATOM 78 CA HIS A 96 28.392 38.251 9.418 1.00 76.67 C ANISOU 78 CA HIS A 96 9213 7484 12435 -2035 251 -1157 C ATOM 79 C HIS A 96 27.935 37.391 10.604 1.00 74.96 C ANISOU 79 C HIS A 96 9040 7409 12034 -1951 4 -1433 C ATOM 80 O HIS A 96 28.004 37.812 11.757 1.00 74.39 O ANISOU 80 O HIS A 96 8947 7245 12074 -1984 -252 -1621 O ATOM 81 CB HIS A 96 29.854 38.646 9.578 1.00 87.30 C ANISOU 81 CB HIS A 96 10249 8678 14244 -2239 265 -1067 C ATOM 82 CG HIS A 96 30.789 37.479 9.572 1.00104.42 C ANISOU 82 CG HIS A 96 12191 11061 16422 -2224 346 -1088 C ATOM 83 ND1 HIS A 96 32.133 37.599 9.854 1.00112.23 N ANISOU 83 ND1 HIS A 96 12845 11974 17824 -2387 328 -1044 N ATOM 84 CD2 HIS A 96 30.570 36.165 9.321 1.00100.20 C ANISOU 84 CD2 HIS A 96 11704 10789 15579 -2053 415 -1160 C ATOM 85 CE1 HIS A 96 32.704 36.408 9.777 1.00105.33 C ANISOU 85 CE1 HIS A 96 11828 11334 16857 -2292 403 -1088 C ATOM 86 NE2 HIS A 96 31.776 35.522 9.458 1.00 99.39 N ANISOU 86 NE2 HIS A 96 11316 10768 15680 -2088 447 -1166 N ATOM 87 N LEU A 97 27.460 36.187 10.304 1.00 69.24 N ANISOU 87 N LEU A 97 8370 6909 11029 -1823 68 -1446 N ATOM 88 CA LEU A 97 26.925 35.283 11.320 1.00 74.62 C ANISOU 88 CA LEU A 97 9075 7731 11547 -1748 -127 -1597 C ATOM 89 C LEU A 97 27.806 34.067 11.524 1.00 79.06 C ANISOU 89 C LEU A 97 9456 8392 12192 -1752 -145 -1615 C ATOM 90 O LEU A 97 28.633 33.733 10.672 1.00 79.85 O ANISOU 90 O LEU A 97 9439 8505 12396 -1759 26 -1541 O ATOM 91 CB LEU A 97 25.521 34.815 10.945 1.00 61.10 C ANISOU 91 CB LEU A 97 7542 6137 9536 -1614 -111 -1580 C ATOM 92 CG LEU A 97 24.310 35.544 11.522 1.00 70.72 C ANISOU 92 CG LEU A 97 8908 7366 10596 -1542 -221 -1636 C ATOM 93 CD1 LEU A 97 24.606 37.002 11.801 1.00 74.75 C ANISOU 93 CD1 LEU A 97 9457 7675 11270 -1592 -277 -1692 C ATOM 94 CD2 LEU A 97 23.159 35.423 10.555 1.00 68.22 C ANISOU 94 CD2 LEU A 97 8735 7107 10077 -1438 -133 -1564 C ATOM 95 N THR A 98 27.594 33.392 12.651 1.00 71.68 N ANISOU 95 N THR A 98 8496 7552 11188 -1713 -343 -1694 N ATOM 96 CA THR A 98 28.376 32.222 13.014 1.00 62.73 C ANISOU 96 CA THR A 98 7198 6486 10152 -1699 -411 -1698 C ATOM 97 C THR A 98 27.437 31.077 13.379 1.00 69.12 C ANISOU 97 C THR A 98 8071 7399 10791 -1607 -504 -1645 C ATOM 98 O THR A 98 26.283 31.307 13.782 1.00 65.40 O ANISOU 98 O THR A 98 7720 7000 10131 -1568 -551 -1613 O ATOM 99 CB THR A 98 29.339 32.535 14.192 1.00 74.38 C ANISOU 99 CB THR A 98 8514 7955 11792 -1755 -608 -1791 C ATOM 100 OG1 THR A 98 30.174 31.409 14.449 1.00 81.60 O ANISOU 100 OG1 THR A 98 9257 8926 12821 -1724 -671 -1775 O ATOM 101 CG2 THR A 98 28.570 32.833 15.436 1.00 73.32 C ANISOU 101 CG2 THR A 98 8482 7929 11448 -1679 -811 -1863 C ATOM 102 N TYR A 99 27.924 29.846 13.207 1.00 71.56 N ANISOU 102 N TYR A 99 8278 7703 11209 -1567 -533 -1619 N ATOM 103 CA TYR A 99 27.128 28.647 13.474 1.00 62.39 C ANISOU 103 CA TYR A 99 7136 6560 10011 -1511 -648 -1525 C ATOM 104 C TYR A 99 27.988 27.455 13.897 1.00 74.20 C ANISOU 104 C TYR A 99 8475 8017 11702 -1474 -776 -1493 C ATOM 105 O TYR A 99 29.194 27.410 13.643 1.00 88.06 O ANISOU 105 O TYR A 99 10106 9741 13611 -1460 -739 -1581 O ATOM 106 CB TYR A 99 26.276 28.263 12.244 1.00 71.87 C ANISOU 106 CB TYR A 99 8452 7690 11164 -1459 -575 -1548 C ATOM 107 CG TYR A 99 27.028 27.537 11.134 1.00 73.26 C ANISOU 107 CG TYR A 99 8588 7788 11460 -1362 -518 -1665 C ATOM 108 CD1 TYR A 99 27.715 28.244 10.154 1.00 77.27 C ANISOU 108 CD1 TYR A 99 9102 8338 11918 -1320 -304 -1738 C ATOM 109 CD2 TYR A 99 27.032 26.147 11.059 1.00 83.98 C ANISOU 109 CD2 TYR A 99 9890 9034 12984 -1285 -680 -1690 C ATOM 110 CE1 TYR A 99 28.404 27.589 9.142 1.00 82.01 C ANISOU 110 CE1 TYR A 99 9652 8951 12556 -1163 -221 -1850 C ATOM 111 CE2 TYR A 99 27.720 25.480 10.045 1.00 89.26 C ANISOU 111 CE2 TYR A 99 10532 9649 13735 -1127 -651 -1863 C ATOM 112 CZ TYR A 99 28.400 26.210 9.093 1.00 82.00 C ANISOU 112 CZ TYR A 99 9617 8852 12686 -1046 -405 -1951 C ATOM 113 OH TYR A 99 29.083 25.570 8.093 1.00 76.06 O ANISOU 113 OH TYR A 99 8824 8130 11944 -825 -343 -2124 O ATOM 114 N ARG A 100 27.351 26.485 14.541 1.00 80.15 N ANISOU 114 N ARG A 100 9210 8769 12476 -1454 -924 -1331 N ATOM 115 CA ARG A 100 28.043 25.296 15.008 1.00 79.25 C ANISOU 115 CA ARG A 100 8960 8579 12572 -1407 -1079 -1250 C ATOM 116 C ARG A 100 27.107 24.108 14.962 1.00 79.29 C ANISOU 116 C ARG A 100 8968 8446 12714 -1403 -1206 -1073 C ATOM 117 O ARG A 100 25.945 24.216 15.345 1.00 72.02 O ANISOU 117 O ARG A 100 8085 7601 11680 -1456 -1209 -893 O ATOM 118 CB ARG A 100 28.568 25.500 16.428 1.00 85.48 C ANISOU 118 CB ARG A 100 9657 9538 13283 -1395 -1196 -1144 C ATOM 119 CG ARG A 100 29.097 24.245 17.086 1.00 84.84 C ANISOU 119 CG ARG A 100 9446 9401 13390 -1329 -1381 -974 C ATOM 120 CD ARG A 100 29.571 24.538 18.492 1.00 72.82 C ANISOU 120 CD ARG A 100 7852 8111 11706 -1272 -1510 -878 C ATOM 121 NE ARG A 100 30.172 23.361 19.106 1.00 89.92 N ANISOU 121 NE ARG A 100 9890 10227 14049 -1186 -1695 -687 N ATOM 122 CZ ARG A 100 30.102 23.077 20.402 1.00 90.24 C ANISOU 122 CZ ARG A 100 9886 10478 13923 -1097 -1835 -423 C ATOM 123 NH1 ARG A 100 29.448 23.881 21.227 1.00 81.22 N ANISOU 123 NH1 ARG A 100 8816 9645 12401 -1055 -1804 -359 N ATOM 124 NH2 ARG A 100 30.675 21.980 20.873 1.00 97.85 N ANISOU 124 NH2 ARG A 100 10736 11363 15080 -1010 -2008 -217 N ATOM 125 N ILE A 101 27.604 22.985 14.460 1.00 82.95 N ANISOU 125 N ILE A 101 9370 8689 13459 -1333 -1322 -1131 N ATOM 126 CA ILE A 101 26.860 21.740 14.557 1.00 81.81 C ANISOU 126 CA ILE A 101 9187 8324 13574 -1348 -1521 -943 C ATOM 127 C ILE A 101 27.350 21.054 15.812 1.00 88.92 C ANISOU 127 C ILE A 101 9951 9236 14598 -1339 -1668 -653 C ATOM 128 O ILE A 101 28.483 20.563 15.863 1.00 94.40 O ANISOU 128 O ILE A 101 10566 9846 15456 -1239 -1753 -743 O ATOM 129 CB ILE A 101 27.060 20.835 13.328 1.00 85.70 C ANISOU 129 CB ILE A 101 9703 8519 14338 -1234 -1638 -1204 C ATOM 130 CG1 ILE A 101 26.975 21.671 12.051 1.00 89.19 C ANISOU 130 CG1 ILE A 101 10283 9057 14549 -1165 -1449 -1520 C ATOM 131 CG2 ILE A 101 26.040 19.668 13.321 1.00 70.06 C ANISOU 131 CG2 ILE A 101 7684 6230 12705 -1291 -1899 -1034 C ATOM 132 CD1 ILE A 101 27.341 20.917 10.793 1.00 84.92 C ANISOU 132 CD1 ILE A 101 9781 8333 14152 -958 -1537 -1851 C ATOM 133 N VAL A 102 26.510 21.045 16.839 1.00 77.22 N ANISOU 133 N VAL A 102 8958 9844 10538 823 -2230 -1253 N ATOM 134 CA VAL A 102 26.936 20.503 18.116 1.00 90.34 C ANISOU 134 CA VAL A 102 10558 11497 12269 821 -2587 -1048 C ATOM 135 C VAL A 102 26.603 19.030 18.250 1.00 85.46 C ANISOU 135 C VAL A 102 10257 10527 11687 1165 -2690 -1052 C ATOM 136 O VAL A 102 27.431 18.228 18.667 1.00 86.71 O ANISOU 136 O VAL A 102 10243 10688 12016 1467 -2882 -880 O ATOM 137 CB VAL A 102 26.300 21.249 19.271 1.00 84.71 C ANISOU 137 CB VAL A 102 10046 10768 11371 308 -2800 -1006 C ATOM 138 CG1 VAL A 102 26.908 20.765 20.577 1.00 99.08 C ANISOU 138 CG1 VAL A 102 11820 12615 13212 282 -3200 -763 C ATOM 139 CG2 VAL A 102 26.521 22.729 19.103 1.00 69.16 C ANISOU 139 CG2 VAL A 102 7835 9083 9359 -48 -2687 -1029 C ATOM 140 N ASN A 103 25.372 18.686 17.912 1.00 88.01 N ANISOU 140 N ASN A 103 11042 10529 11871 1108 -2585 -1241 N ATOM 141 CA ASN A 103 24.949 17.300 17.933 1.00 83.23 C ANISOU 141 CA ASN A 103 10789 9544 11290 1394 -2653 -1272 C ATOM 142 C ASN A 103 24.929 16.734 16.517 1.00 96.67 C ANISOU 142 C ASN A 103 12573 11116 13041 1779 -2365 -1470 C ATOM 143 O ASN A 103 24.831 17.485 15.546 1.00 93.63 O ANISOU 143 O ASN A 103 12112 10874 12590 1718 -2116 -1614 O ATOM 144 CB ASN A 103 23.569 17.175 18.580 1.00 62.25 C ANISOU 144 CB ASN A 103 8603 6581 8470 1045 -2741 -1350 C ATOM 145 CG ASN A 103 23.174 15.731 18.834 1.00 92.88 C ANISOU 145 CG ASN A 103 12866 10050 12373 1267 -2855 -1336 C ATOM 146 OD1 ASN A 103 23.992 14.815 18.714 1.00115.41 O ANISOU 146 OD1 ASN A 103 15647 12839 15365 1691 -2927 -1236 O ATOM 147 ND2 ASN A 103 21.918 15.520 19.191 1.00 95.39 N ANISOU 147 ND2 ASN A 103 13583 10073 12587 981 -2858 -1436 N ATOM 148 N TYR A 104 25.036 15.412 16.408 1.00 97.95 N ANISOU 148 N TYR A 104 12937 10984 13294 2167 -2405 -1474 N ATOM 149 CA TYR A 104 24.930 14.722 15.128 1.00 86.35 C ANISOU 149 CA TYR A 104 11667 9312 11830 2527 -2142 -1690 C ATOM 150 C TYR A 104 23.901 13.609 15.192 1.00 82.67 C ANISOU 150 C TYR A 104 11753 8356 11303 2562 -2244 -1803 C ATOM 151 O TYR A 104 23.730 12.970 16.224 1.00 89.55 O ANISOU 151 O TYR A 104 12787 9028 12212 2515 -2497 -1653 O ATOM 152 CB TYR A 104 26.279 14.142 14.718 1.00 93.18 C ANISOU 152 CB TYR A 104 12196 10282 12925 3056 -2008 -1620 C ATOM 153 CG TYR A 104 27.188 15.126 14.031 1.00100.89 C ANISOU 153 CG TYR A 104 12686 11687 13960 3081 -1728 -1622 C ATOM 154 CD1 TYR A 104 28.010 15.978 14.763 1.00100.42 C ANISOU 154 CD1 TYR A 104 12106 12018 14031 2898 -1863 -1401 C ATOM 155 CD2 TYR A 104 27.225 15.204 12.648 1.00 98.20 C ANISOU 155 CD2 TYR A 104 12441 11348 13524 3258 -1327 -1845 C ATOM 156 CE1 TYR A 104 28.846 16.876 14.131 1.00100.84 C ANISOU 156 CE1 TYR A 104 11704 12452 14159 2885 -1586 -1398 C ATOM 157 CE2 TYR A 104 28.050 16.095 12.013 1.00105.31 C ANISOU 157 CE2 TYR A 104 12931 12624 14459 3251 -1025 -1838 C ATOM 158 CZ TYR A 104 28.859 16.929 12.753 1.00105.26 C ANISOU 158 CZ TYR A 104 12369 13002 14624 3062 -1145 -1613 C ATOM 159 OH TYR A 104 29.680 17.814 12.101 1.00107.34 O ANISOU 159 OH TYR A 104 12218 13626 14939 3022 -822 -1604 O ATOM 160 N THR A 105 23.214 13.368 14.087 1.00 88.67 N ANISOU 160 N THR A 105 12832 8905 11953 2618 -2061 -2059 N ATOM 161 CA THR A 105 22.346 12.204 14.014 1.00 84.43 C ANISOU 161 CA THR A 105 12806 7882 11391 2684 -2149 -2183 C ATOM 162 C THR A 105 23.129 10.999 13.532 1.00 89.25 C ANISOU 162 C THR A 105 13519 8271 12120 3243 -2050 -2214 C ATOM 163 O THR A 105 24.127 11.151 12.832 1.00 94.47 O ANISOU 163 O THR A 105 13902 9147 12846 3575 -1808 -2239 O ATOM 164 CB THR A 105 21.165 12.434 13.079 1.00 78.85 C ANISOU 164 CB THR A 105 12432 7004 10523 2459 -2073 -2451 C ATOM 165 OG1 THR A 105 20.400 11.225 12.980 1.00 78.87 O ANISOU 165 OG1 THR A 105 12785 6688 10496 2415 -2092 -2454 O ATOM 166 CG2 THR A 105 21.658 12.845 11.706 1.00 78.54 C ANISOU 166 CG2 THR A 105 12334 7135 10374 2673 -1792 -2612 C ATOM 167 N PRO A 106 22.691 9.796 13.932 1.00 88.18 N ANISOU 167 N PRO A 106 13784 7689 12032 3347 -2211 -2209 N ATOM 168 CA PRO A 106 23.162 8.517 13.394 1.00 80.07 C ANISOU 168 CA PRO A 106 12951 6386 11085 3796 -2083 -2255 C ATOM 169 C PRO A 106 22.490 8.156 12.077 1.00 88.35 C ANISOU 169 C PRO A 106 14263 7383 11923 3647 -1795 -2453 C ATOM 170 O PRO A 106 22.908 7.215 11.402 1.00 91.93 O ANISOU 170 O PRO A 106 14848 7678 12403 3948 -1594 -2514 O ATOM 171 CB PRO A 106 22.766 7.507 14.476 1.00 77.77 C ANISOU 171 CB PRO A 106 12928 5773 10848 3698 -2348 -2063 C ATOM 172 CG PRO A 106 22.454 8.311 15.665 1.00 88.77 C ANISOU 172 CG PRO A 106 14236 7254 12238 3360 -2636 -1915 C ATOM 173 CD PRO A 106 21.923 9.604 15.167 1.00 84.60 C ANISOU 173 CD PRO A 106 13523 7055 11565 2984 -2495 -2059 C ATOM 174 N ASP A 107 21.444 8.887 11.723 1.00 92.53 N ANISOU 174 N ASP A 107 14854 8038 12266 3178 -1794 -2533 N ATOM 175 CA ASP A 107 20.689 8.573 10.516 1.00100.44 C ANISOU 175 CA ASP A 107 16086 8994 13083 2995 -1617 -2668 C ATOM 176 C ASP A 107 21.564 8.725 9.279 1.00101.71 C ANISOU 176 C ASP A 107 16233 9251 13160 3334 -1304 -2829 C ATOM 177 O ASP A 107 21.374 8.044 8.276 1.00 93.78 O ANISOU 177 O ASP A 107 15489 8107 12039 3372 -1134 -2950 O ATOM 178 CB ASP A 107 19.466 9.480 10.390 1.00 88.31 C ANISOU 178 CB ASP A 107 14498 7627 11427 2466 -1699 -2664 C ATOM 179 CG ASP A 107 18.609 9.479 11.627 1.00 89.49 C ANISOU 179 CG ASP A 107 14600 7731 11670 2114 -1910 -2512 C ATOM 180 OD1 ASP A 107 19.003 8.851 12.628 1.00105.85 O ANISOU 180 OD1 ASP A 107 16732 9629 13856 2255 -2039 -2408 O ATOM 181 OD2 ASP A 107 17.541 10.117 11.595 1.00 91.02 O ANISOU 181 OD2 ASP A 107 14691 8060 11831 1706 -1927 -2483 O ATOM 182 N LEU A 108 22.517 9.645 9.370 1.00 98.92 N ANISOU 182 N LEU A 108 15570 9145 12870 3569 -1215 -2839 N ATOM 183 CA LEU A 108 23.382 10.002 8.255 1.00 85.55 C ANISOU 183 CA LEU A 108 13804 7611 11091 3865 -848 -2986 C ATOM 184 C LEU A 108 24.830 9.990 8.697 1.00 87.98 C ANISOU 184 C LEU A 108 13700 8050 11679 4403 -716 -2922 C ATOM 185 O LEU A 108 25.112 10.078 9.895 1.00103.48 O ANISOU 185 O LEU A 108 15394 10046 13878 4483 -1001 -2753 O ATOM 186 CB LEU A 108 23.021 11.391 7.729 1.00 84.25 C ANISOU 186 CB LEU A 108 13579 7717 10716 3564 -812 -3061 C ATOM 187 CG LEU A 108 21.681 11.525 7.029 1.00 77.49 C ANISOU 187 CG LEU A 108 13025 6796 9621 3078 -912 -3094 C ATOM 188 CD1 LEU A 108 21.404 12.993 6.750 1.00 69.13 C ANISOU 188 CD1 LEU A 108 11843 6003 8421 2799 -935 -3107 C ATOM 189 CD2 LEU A 108 21.694 10.685 5.740 1.00 76.75 C ANISOU 189 CD2 LEU A 108 13278 6533 9350 3201 -671 -3239 C ATOM 190 N PRO A 109 25.758 9.885 7.739 1.00 85.49 N ANISOU 190 N PRO A 109 13292 7826 11364 4764 -285 -3036 N ATOM 191 CA PRO A 109 27.164 10.080 8.089 1.00 88.71 C ANISOU 191 CA PRO A 109 13126 8481 12100 5253 -115 -2947 C ATOM 192 C PRO A 109 27.425 11.500 8.592 1.00108.11 C ANISOU 192 C PRO A 109 15034 11459 14584 4867 -193 -2735 C ATOM 193 O PRO A 109 26.674 12.444 8.317 1.00109.72 O ANISOU 193 O PRO A 109 15381 11793 14516 4422 -243 -2786 O ATOM 194 CB PRO A 109 27.894 9.812 6.771 1.00 93.82 C ANISOU 194 CB PRO A 109 13814 9156 12677 5533 466 -3120 C ATOM 195 CG PRO A 109 26.981 8.908 6.028 1.00 94.59 C ANISOU 195 CG PRO A 109 14549 8876 12515 5309 479 -3262 C ATOM 196 CD PRO A 109 25.600 9.357 6.374 1.00101.40 C ANISOU 196 CD PRO A 109 15695 9690 13142 4759 58 -3230 C ATOM 197 N LYS A 110 28.500 11.638 9.351 1.00119.72 N ANISOU 197 N LYS A 110 15872 13210 16407 5035 -233 -2488 N ATOM 198 CA LYS A 110 28.899 12.925 9.877 1.00112.42 C ANISOU 198 CA LYS A 110 14400 12772 15544 4679 -313 -2279 C ATOM 199 C LYS A 110 29.242 13.887 8.739 1.00111.66 C ANISOU 199 C LYS A 110 14185 12975 15267 4577 152 -2406 C ATOM 200 O LYS A 110 29.207 15.101 8.913 1.00118.21 O ANISOU 200 O LYS A 110 14766 14136 16014 4164 108 -2302 O ATOM 201 CB LYS A 110 30.082 12.746 10.832 1.00119.47 C ANISOU 201 CB LYS A 110 14638 13877 16878 4925 -472 -1998 C ATOM 202 CG LYS A 110 31.186 11.822 10.290 1.00137.28 C ANISOU 202 CG LYS A 110 16648 16048 19465 5585 -128 -2053 C ATOM 203 CD LYS A 110 31.588 10.746 11.301 1.00130.48 C ANISOU 203 CD LYS A 110 15662 14948 18965 5948 -507 -1851 C ATOM 204 CE LYS A 110 32.891 10.082 10.900 1.00124.65 C ANISOU 204 CE LYS A 110 14453 14226 18682 6602 -180 -1850 C ATOM 205 NZ LYS A 110 33.387 9.125 11.928 1.00132.40 N ANISOU 205 NZ LYS A 110 15244 14995 20068 6974 -610 -1603 N ATOM 206 N ASP A 111 29.551 13.346 7.565 1.00102.52 N ANISOU 206 N ASP A 111 13262 11671 14019 4938 611 -2638 N ATOM 207 CA ASP A 111 29.860 14.184 6.414 1.00 93.59 C ANISOU 207 CA ASP A 111 12124 10781 12653 4838 1096 -2764 C ATOM 208 C ASP A 111 28.568 14.708 5.806 1.00 94.44 C ANISOU 208 C ASP A 111 12870 10738 12275 4420 978 -2922 C ATOM 209 O ASP A 111 28.479 15.868 5.395 1.00 92.84 O ANISOU 209 O ASP A 111 12616 10795 11865 4070 1089 -2895 O ATOM 210 CB ASP A 111 30.669 13.411 5.369 1.00112.04 C ANISOU 210 CB ASP A 111 14533 13001 15035 5370 1681 -2971 C ATOM 211 CG ASP A 111 31.379 14.331 4.389 1.00121.62 C ANISOU 211 CG ASP A 111 15535 14562 16112 5290 2258 -3024 C ATOM 212 OD1 ASP A 111 30.953 15.497 4.259 1.00130.57 O ANISOU 212 OD1 ASP A 111 16710 15917 16982 4800 2180 -2959 O ATOM 213 OD2 ASP A 111 32.366 13.902 3.755 1.00116.11 O ANISOU 213 OD2 ASP A 111 14630 13902 15582 5714 2811 -3127 O ATOM 214 N ALA A 112 27.563 13.846 5.762 1.00 86.36 N ANISOU 214 N ALA A 112 12438 9276 11098 4452 724 -3075 N ATOM 215 CA ALA A 112 26.273 14.211 5.206 1.00 81.13 C ANISOU 215 CA ALA A 112 12362 8426 10039 4082 538 -3227 C ATOM 216 C ALA A 112 25.645 15.352 5.976 1.00 96.99 C ANISOU 216 C ALA A 112 14147 10652 12054 3566 179 -3044 C ATOM 217 O ALA A 112 25.207 16.335 5.373 1.00108.93 O ANISOU 217 O ALA A 112 15805 12279 13303 3251 213 -3080 O ATOM 218 CB ALA A 112 25.346 13.021 5.203 1.00 88.16 C ANISOU 218 CB ALA A 112 13822 8811 10862 4175 281 -3391 C ATOM 219 N VAL A 113 25.585 15.218 7.301 1.00 91.48 N ANISOU 219 N VAL A 113 13141 9979 11638 3480 -164 -2851 N ATOM 220 CA VAL A 113 24.966 16.250 8.137 1.00 81.16 C ANISOU 220 CA VAL A 113 11654 8841 10342 2995 -481 -2698 C ATOM 221 C VAL A 113 25.529 17.625 7.785 1.00 76.11 C ANISOU 221 C VAL A 113 10676 8611 9631 2771 -264 -2609 C ATOM 222 O VAL A 113 24.775 18.584 7.599 1.00 83.02 O ANISOU 222 O VAL A 113 11694 9524 10327 2394 -372 -2624 O ATOM 223 CB VAL A 113 25.178 15.981 9.653 1.00 73.97 C ANISOU 223 CB VAL A 113 10408 7973 9726 2958 -797 -2472 C ATOM 224 CG1 VAL A 113 24.931 17.225 10.449 1.00 66.52 C ANISOU 224 CG1 VAL A 113 9189 7296 8790 2491 -989 -2314 C ATOM 225 CG2 VAL A 113 24.264 14.871 10.150 1.00 71.39 C ANISOU 225 CG2 VAL A 113 10495 7209 9419 2994 -1082 -2534 C ATOM 226 N ASP A 114 26.853 17.698 7.656 1.00 85.08 N ANISOU 226 N ASP A 114 11362 10030 10934 3012 53 -2518 N ATOM 227 CA ASP A 114 27.556 18.954 7.376 1.00 97.86 C ANISOU 227 CA ASP A 114 12599 12051 12534 2795 297 -2411 C ATOM 228 C ASP A 114 27.155 19.545 6.032 1.00 83.76 C ANISOU 228 C ASP A 114 11239 10227 10358 2664 572 -2572 C ATOM 229 O ASP A 114 26.799 20.721 5.945 1.00 75.18 O ANISOU 229 O ASP A 114 10159 9279 9127 2273 509 -2508 O ATOM 230 CB ASP A 114 29.081 18.752 7.415 1.00105.48 C ANISOU 230 CB ASP A 114 12966 13299 13812 3118 621 -2302 C ATOM 231 CG ASP A 114 29.582 18.213 8.754 1.00103.16 C ANISOU 231 CG ASP A 114 12228 13055 13912 3255 284 -2102 C ATOM 232 OD1 ASP A 114 28.749 17.863 9.619 1.00102.67 O ANISOU 232 OD1 ASP A 114 12400 12774 13835 3124 -148 -2064 O ATOM 233 OD2 ASP A 114 30.819 18.125 8.933 1.00100.54 O ANISOU 233 OD2 ASP A 114 11314 12975 13913 3491 453 -1976 O ATOM 234 N SER A 115 27.224 18.721 4.993 1.00 76.12 N ANISOU 234 N SER A 115 10667 9047 9209 2992 868 -2779 N ATOM 235 CA SER A 115 26.849 19.136 3.646 1.00 88.01 C ANISOU 235 CA SER A 115 12695 10470 10274 2891 1115 -2943 C ATOM 236 C SER A 115 25.441 19.747 3.615 1.00 89.52 C ANISOU 236 C SER A 115 13305 10480 10230 2487 680 -2970 C ATOM 237 O SER A 115 25.226 20.856 3.090 1.00 80.99 O ANISOU 237 O SER A 115 12336 9517 8920 2183 720 -2925 O ATOM 238 CB SER A 115 26.935 17.941 2.695 1.00 82.74 C ANISOU 238 CB SER A 115 12511 9502 9422 3303 1402 -3196 C ATOM 239 OG SER A 115 26.672 18.328 1.359 1.00101.16 O ANISOU 239 OG SER A 115 15402 11761 11273 3201 1658 -3352 O ATOM 240 N ALA A 116 24.496 19.018 4.202 1.00 85.87 N ANISOU 240 N ALA A 116 13048 9718 9859 2488 269 -3031 N ATOM 241 CA ALA A 116 23.107 19.463 4.294 1.00 82.50 C ANISOU 241 CA ALA A 116 12931 9094 9322 2137 -161 -3065 C ATOM 242 C ALA A 116 23.008 20.877 4.846 1.00 74.85 C ANISOU 242 C ALA A 116 11617 8388 8433 1746 -283 -2876 C ATOM 243 O ALA A 116 22.303 21.731 4.300 1.00 82.61 O ANISOU 243 O ALA A 116 12851 9322 9216 1481 -405 -2893 O ATOM 244 CB ALA A 116 22.301 18.494 5.164 1.00 70.74 C ANISOU 244 CB ALA A 116 11527 7308 8043 2169 -533 -3109 C ATOM 245 N VAL A 117 23.743 21.120 5.922 1.00 66.15 N ANISOU 245 N VAL A 117 9960 7547 7627 1719 -267 -2695 N ATOM 246 CA VAL A 117 23.697 22.396 6.612 1.00 67.20 C ANISOU 246 CA VAL A 117 9767 7907 7859 1342 -393 -2526 C ATOM 247 C VAL A 117 24.281 23.503 5.759 1.00 69.08 C ANISOU 247 C VAL A 117 9963 8379 7905 1199 -91 -2467 C ATOM 248 O VAL A 117 23.794 24.635 5.764 1.00 74.19 O ANISOU 248 O VAL A 117 10647 9059 8482 861 -216 -2403 O ATOM 249 CB VAL A 117 24.461 22.325 7.941 1.00 68.76 C ANISOU 249 CB VAL A 117 9420 8326 8379 1343 -463 -2348 C ATOM 250 CG1 VAL A 117 24.524 23.698 8.613 1.00 63.12 C ANISOU 250 CG1 VAL A 117 8402 7848 7733 933 -559 -2191 C ATOM 251 CG2 VAL A 117 23.824 21.294 8.856 1.00 62.29 C ANISOU 251 CG2 VAL A 117 8703 7250 7713 1431 -772 -2376 C ATOM 252 N GLU A 118 25.334 23.174 5.026 1.00 82.59 N ANISOU 252 N GLU A 118 11603 10234 9543 1458 334 -2489 N ATOM 253 CA GLU A 118 26.009 24.189 4.241 1.00 89.69 C ANISOU 253 CA GLU A 118 12443 11369 10264 1305 693 -2417 C ATOM 254 C GLU A 118 25.076 24.783 3.193 1.00 82.58 C ANISOU 254 C GLU A 118 12153 10261 8963 1108 618 -2501 C ATOM 255 O GLU A 118 24.881 25.994 3.191 1.00 86.73 O ANISOU 255 O GLU A 118 12654 10873 9426 770 545 -2382 O ATOM 256 CB GLU A 118 27.279 23.617 3.610 1.00 93.12 C ANISOU 256 CB GLU A 118 12695 11971 10714 1643 1231 -2452 C ATOM 257 CG GLU A 118 28.140 22.910 4.642 1.00 97.11 C ANISOU 257 CG GLU A 118 12596 12635 11666 1894 1219 -2363 C ATOM 258 CD GLU A 118 29.563 22.636 4.194 1.00112.67 C ANISOU 258 CD GLU A 118 14159 14855 13796 2184 1768 -2345 C ATOM 259 OE1 GLU A 118 29.805 22.497 2.973 1.00116.30 O ANISOU 259 OE1 GLU A 118 14950 15264 13974 2328 2228 -2485 O ATOM 260 OE2 GLU A 118 30.438 22.526 5.080 1.00117.26 O ANISOU 260 OE2 GLU A 118 14088 15671 14794 2272 1734 -2193 O ATOM 261 N LYS A 119 24.477 23.962 2.329 1.00 87.82 N ANISOU 261 N LYS A 119 13384 10627 9356 1304 592 -2696 N ATOM 262 CA LYS A 119 23.579 24.526 1.310 1.00 88.73 C ANISOU 262 CA LYS A 119 14105 10531 9077 1109 441 -2758 C ATOM 263 C LYS A 119 22.363 25.160 1.985 1.00 77.23 C ANISOU 263 C LYS A 119 12640 8926 7778 814 -101 -2701 C ATOM 264 O LYS A 119 21.812 26.137 1.484 1.00 73.28 O ANISOU 264 O LYS A 119 12392 8357 7094 563 -252 -2644 O ATOM 265 CB LYS A 119 23.147 23.477 0.265 1.00 92.73 C ANISOU 265 CB LYS A 119 15264 10725 9245 1353 461 -2994 C ATOM 266 CG LYS A 119 23.556 23.846 -1.196 1.00105.05 C ANISOU 266 CG LYS A 119 17343 12292 10281 1339 851 -3042 C ATOM 267 CD LYS A 119 22.536 23.400 -2.260 1.00 97.46 C ANISOU 267 CD LYS A 119 17210 10945 8876 1344 576 -3232 C ATOM 268 CE LYS A 119 22.817 23.982 -3.667 1.00101.89 C ANISOU 268 CE LYS A 119 18287 11523 8903 1218 876 -3198 C ATOM 269 NZ LYS A 119 24.150 23.651 -4.272 1.00107.63 N ANISOU 269 NZ LYS A 119 19096 12415 9385 1461 1653 -3300 N ATOM 270 N ALA A 120 21.973 24.633 3.142 1.00 76.83 N ANISOU 270 N ALA A 120 12294 8820 8081 844 -371 -2707 N ATOM 271 CA ALA A 120 20.890 25.236 3.912 1.00 66.02 C ANISOU 271 CA ALA A 120 10839 7327 6917 567 -797 -2662 C ATOM 272 C ALA A 120 21.178 26.704 4.156 1.00 68.40 C ANISOU 272 C ALA A 120 10891 7840 7256 262 -741 -2485 C ATOM 273 O ALA A 120 20.327 27.566 3.930 1.00 79.06 O ANISOU 273 O ALA A 120 12431 9045 8564 38 -983 -2462 O ATOM 274 CB ALA A 120 20.694 24.508 5.231 1.00 67.69 C ANISOU 274 CB ALA A 120 10731 7506 7481 619 -973 -2666 C ATOM 275 N LEU A 121 22.387 26.999 4.609 1.00 68.84 N ANISOU 275 N LEU A 121 10515 8222 7418 254 -437 -2356 N ATOM 276 CA LEU A 121 22.755 28.392 4.844 1.00 70.66 C ANISOU 276 CA LEU A 121 10516 8649 7684 -65 -366 -2189 C ATOM 277 C LEU A 121 23.012 29.126 3.532 1.00 75.33 C ANISOU 277 C LEU A 121 11451 9254 7917 -151 -128 -2148 C ATOM 278 O LEU A 121 22.624 30.283 3.361 1.00 63.56 O ANISOU 278 O LEU A 121 10084 7707 6358 -429 -241 -2055 O ATOM 279 CB LEU A 121 23.988 28.469 5.722 1.00 59.35 C ANISOU 279 CB LEU A 121 8501 7560 6488 -83 -154 -2060 C ATOM 280 CG LEU A 121 23.822 27.691 7.008 1.00 62.94 C ANISOU 280 CG LEU A 121 8683 7995 7238 3 -394 -2075 C ATOM 281 CD1 LEU A 121 25.094 27.716 7.826 1.00 73.66 C ANISOU 281 CD1 LEU A 121 9477 9688 8820 1 -252 -1931 C ATOM 282 CD2 LEU A 121 22.677 28.299 7.774 1.00 58.34 C ANISOU 282 CD2 LEU A 121 8175 7225 6765 -272 -748 -2086 C ATOM 283 N LYS A 122 23.675 28.446 2.604 1.00 79.34 N ANISOU 283 N LYS A 122 12148 9813 8185 91 220 -2217 N ATOM 284 CA LYS A 122 24.038 29.078 1.352 1.00 82.19 C ANISOU 284 CA LYS A 122 12877 10198 8152 0 525 -2174 C ATOM 285 C LYS A 122 22.774 29.525 0.612 1.00 83.22 C ANISOU 285 C LYS A 122 13623 9991 8005 -135 145 -2210 C ATOM 286 O LYS A 122 22.777 30.560 -0.041 1.00 93.92 O ANISOU 286 O LYS A 122 15238 11329 9117 -363 200 -2091 O ATOM 287 CB LYS A 122 24.893 28.133 0.505 1.00 69.84 C ANISOU 287 CB LYS A 122 11456 8709 6372 313 1003 -2287 C ATOM 288 CG LYS A 122 24.526 28.087 -0.971 1.00 90.19 C ANISOU 288 CG LYS A 122 14801 11066 8401 338 1111 -2384 C ATOM 289 CD LYS A 122 25.262 26.950 -1.685 1.00108.58 C ANISOU 289 CD LYS A 122 17304 13412 10540 695 1587 -2556 C ATOM 290 CE LYS A 122 24.867 26.822 -3.159 1.00112.27 C ANISOU 290 CE LYS A 122 18642 13629 10386 709 1685 -2681 C ATOM 291 NZ LYS A 122 25.013 28.098 -3.922 1.00108.91 N ANISOU 291 NZ LYS A 122 18521 13258 9600 375 1845 -2512 N ATOM 292 N VAL A 123 21.687 28.773 0.760 1.00 73.17 N ANISOU 292 N VAL A 123 12558 8440 6802 -10 -270 -2355 N ATOM 293 CA VAL A 123 20.413 29.154 0.171 1.00 68.45 C ANISOU 293 CA VAL A 123 12450 7515 6044 -130 -722 -2385 C ATOM 294 C VAL A 123 19.979 30.541 0.622 1.00 76.07 C ANISOU 294 C VAL A 123 13253 8461 7187 -439 -946 -2219 C ATOM 295 O VAL A 123 19.493 31.336 -0.187 1.00 87.56 O ANISOU 295 O VAL A 123 15123 9744 8401 -584 -1121 -2143 O ATOM 296 CB VAL A 123 19.321 28.148 0.520 1.00 72.26 C ANISOU 296 CB VAL A 123 13013 7728 6716 10 -1144 -2559 C ATOM 297 CG1 VAL A 123 17.955 28.791 0.443 1.00 68.64 C ANISOU 297 CG1 VAL A 123 12463 7106 6512 -168 -1565 -2387 C ATOM 298 CG2 VAL A 123 19.400 26.947 -0.415 1.00 74.77 C ANISOU 298 CG2 VAL A 123 13680 7954 6777 259 -1012 -2678 C ATOM 299 N TRP A 124 20.167 30.842 1.903 1.00 63.60 N ANISOU 299 N TRP A 124 11115 7037 6014 -539 -948 -2160 N ATOM 300 CA TRP A 124 19.875 32.189 2.393 1.00 68.26 C ANISOU 300 CA TRP A 124 11550 7607 6779 -833 -1091 -2020 C ATOM 301 C TRP A 124 20.996 33.151 2.047 1.00 70.96 C ANISOU 301 C TRP A 124 11835 8186 6940 -1023 -703 -1845 C ATOM 302 O TRP A 124 20.745 34.261 1.591 1.00 79.94 O ANISOU 302 O TRP A 124 13215 9203 7954 -1237 -784 -1722 O ATOM 303 CB TRP A 124 19.614 32.169 3.909 1.00 57.55 C ANISOU 303 CB TRP A 124 9693 6297 5877 -904 -1230 -2044 C ATOM 304 CG TRP A 124 18.401 31.330 4.176 1.00 58.22 C ANISOU 304 CG TRP A 124 9866 6112 6144 -770 -1594 -2205 C ATOM 305 CD1 TRP A 124 18.359 30.088 4.731 1.00 59.57 C ANISOU 305 CD1 TRP A 124 9864 6308 6462 -578 -1584 -2306 C ATOM 306 CD2 TRP A 124 17.065 31.643 3.798 1.00 54.05 C ANISOU 306 CD2 TRP A 124 9328 5411 5798 -758 -1802 -2085 C ATOM 307 NE1 TRP A 124 17.065 29.622 4.756 1.00 58.35 N ANISOU 307 NE1 TRP A 124 9579 6034 6557 -516 -1710 -2217 N ATOM 308 CE2 TRP A 124 16.256 30.563 4.183 1.00 58.48 C ANISOU 308 CE2 TRP A 124 9681 5940 6600 -609 -1850 -2096 C ATOM 309 CE3 TRP A 124 16.474 32.734 3.170 1.00 61.68 C ANISOU 309 CE3 TRP A 124 10464 6236 6735 -860 -1955 -1953 C ATOM 310 CZ2 TRP A 124 14.892 30.548 3.961 1.00 65.95 C ANISOU 310 CZ2 TRP A 124 10570 6745 7743 -576 -2029 -1996 C ATOM 311 CZ3 TRP A 124 15.131 32.719 2.960 1.00 64.73 C ANISOU 311 CZ3 TRP A 124 10780 6468 7348 -779 -2173 -1862 C ATOM 312 CH2 TRP A 124 14.346 31.640 3.358 1.00 66.56 C ANISOU 312 CH2 TRP A 124 10784 6697 7808 -646 -2201 -1891 C ATOM 313 N GLU A 125 22.231 32.707 2.247 1.00 72.72 N ANISOU 313 N GLU A 125 11729 8728 7172 -944 -285 -1826 N ATOM 314 CA GLU A 125 23.411 33.497 1.929 1.00 67.57 C ANISOU 314 CA GLU A 125 10941 8337 6396 -1132 145 -1668 C ATOM 315 C GLU A 125 23.369 34.053 0.514 1.00 74.42 C ANISOU 315 C GLU A 125 12409 9072 6794 -1220 284 -1599 C ATOM 316 O GLU A 125 23.817 35.177 0.266 1.00 79.22 O ANISOU 316 O GLU A 125 13055 9743 7302 -1505 460 -1428 O ATOM 317 CB GLU A 125 24.674 32.653 2.117 1.00 78.19 C ANISOU 317 CB GLU A 125 11870 10010 7827 -939 573 -1693 C ATOM 318 CG GLU A 125 25.940 33.319 1.599 1.00 83.01 C ANISOU 318 CG GLU A 125 12328 10898 8313 -1110 1094 -1549 C ATOM 319 CD GLU A 125 27.210 32.694 2.145 1.00 94.99 C ANISOU 319 CD GLU A 125 13208 12772 10111 -965 1444 -1541 C ATOM 320 OE1 GLU A 125 27.289 32.461 3.378 1.00 98.34 O ANISOU 320 OE1 GLU A 125 13149 13301 10914 -954 1209 -1532 O ATOM 321 OE2 GLU A 125 28.133 32.447 1.338 1.00 96.22 O ANISOU 321 OE2 GLU A 125 13353 13093 10112 -863 1957 -1539 O ATOM 322 N GLU A 126 22.809 33.275 -0.407 1.00 72.48 N ANISOU 322 N GLU A 126 12682 8619 6240 -1000 184 -1728 N ATOM 323 CA GLU A 126 22.814 33.627 -1.833 1.00 83.20 C ANISOU 323 CA GLU A 126 14715 9841 7057 -1063 325 -1675 C ATOM 324 C GLU A 126 22.083 34.912 -2.174 1.00 86.42 C ANISOU 324 C GLU A 126 15486 10004 7348 -1343 -11 -1510 C ATOM 325 O GLU A 126 22.438 35.586 -3.137 1.00 81.67 O ANISOU 325 O GLU A 126 15326 9368 6335 -1511 209 -1375 O ATOM 326 CB GLU A 126 22.169 32.521 -2.658 1.00 91.10 C ANISOU 326 CB GLU A 126 16256 10609 7751 -794 154 -1868 C ATOM 327 CG GLU A 126 23.043 31.383 -3.079 1.00 87.58 C ANISOU 327 CG GLU A 126 15827 10321 7127 -522 647 -2018 C ATOM 328 CD GLU A 126 22.193 30.296 -3.666 1.00103.65 C ANISOU 328 CD GLU A 126 18385 12064 8935 -284 347 -2233 C ATOM 329 OE1 GLU A 126 21.006 30.226 -3.261 1.00105.56 O ANISOU 329 OE1 GLU A 126 18660 12064 9386 -299 -256 -2275 O ATOM 330 OE2 GLU A 126 22.688 29.536 -4.529 1.00108.55 O ANISOU 330 OE2 GLU A 126 19384 12679 9181 -100 718 -2366 O ATOM 331 N VAL A 127 21.026 35.210 -1.422 1.00 82.35 N ANISOU 331 N VAL A 127 14818 9285 7188 -1377 -536 -1524 N ATOM 332 CA VAL A 127 20.108 36.283 -1.789 1.00 67.65 C ANISOU 332 CA VAL A 127 13330 7105 5271 -1556 -955 -1395 C ATOM 333 C VAL A 127 20.193 37.442 -0.797 1.00 74.86 C ANISOU 333 C VAL A 127 13820 8055 6568 -1809 -981 -1265 C ATOM 334 O VAL A 127 19.457 38.427 -0.903 1.00 67.67 O ANISOU 334 O VAL A 127 13127 6866 5719 -1949 -1316 -1156 O ATOM 335 CB VAL A 127 18.640 35.778 -1.875 1.00 67.91 C ANISOU 335 CB VAL A 127 13585 6791 5428 -1387 -1583 -1525 C ATOM 336 CG1 VAL A 127 18.441 34.819 -3.084 1.00 69.42 C ANISOU 336 CG1 VAL A 127 14384 6858 5136 -1202 -1646 -1638 C ATOM 337 CG2 VAL A 127 18.216 35.121 -0.588 1.00 66.02 C ANISOU 337 CG2 VAL A 127 12766 6602 5718 -1266 -1733 -1683 C ATOM 338 N THR A 128 21.110 37.321 0.153 1.00 63.81 N ANISOU 338 N THR A 128 11837 6983 5426 -1863 -643 -1278 N ATOM 339 CA THR A 128 21.275 38.316 1.198 1.00 70.38 C ANISOU 339 CA THR A 128 12265 7868 6607 -2120 -654 -1189 C ATOM 340 C THR A 128 22.715 38.803 1.251 1.00 81.07 C ANISOU 340 C THR A 128 13357 9559 7887 -2349 -140 -1053 C ATOM 341 O THR A 128 23.560 38.327 0.493 1.00 76.61 O ANISOU 341 O THR A 128 12881 9192 7036 -2281 257 -1037 O ATOM 342 CB THR A 128 20.921 37.746 2.558 1.00 60.09 C ANISOU 342 CB THR A 128 10455 6625 5753 -2022 -828 -1338 C ATOM 343 OG1 THR A 128 21.961 36.837 2.945 1.00 71.39 O ANISOU 343 OG1 THR A 128 11496 8412 7215 -1908 -493 -1391 O ATOM 344 CG2 THR A 128 19.592 37.020 2.499 1.00 65.37 C ANISOU 344 CG2 THR A 128 11307 7005 6525 -1783 -1261 -1495 C ATOM 345 N PRO A 129 23.003 39.767 2.141 1.00 81.70 N ANISOU 345 N PRO A 129 13111 9694 8238 -2638 -129 -965 N ATOM 346 CA PRO A 129 24.418 40.039 2.397 1.00 65.42 C ANISOU 346 CA PRO A 129 10650 8001 6207 -2856 323 -863 C ATOM 347 C PRO A 129 24.903 39.339 3.660 1.00 71.34 C ANISOU 347 C PRO A 129 10753 9034 7319 -2780 335 -965 C ATOM 348 O PRO A 129 25.846 39.795 4.292 1.00 87.40 O ANISOU 348 O PRO A 129 12364 11319 9526 -3028 524 -882 O ATOM 349 CB PRO A 129 24.456 41.559 2.554 1.00 76.74 C ANISOU 349 CB PRO A 129 12185 9288 7684 -3260 291 -697 C ATOM 350 CG PRO A 129 23.116 41.905 3.091 1.00 75.21 C ANISOU 350 CG PRO A 129 12146 8727 7705 -3206 -204 -777 C ATOM 351 CD PRO A 129 22.136 40.856 2.630 1.00 64.10 C ANISOU 351 CD PRO A 129 10983 7153 6218 -2822 -477 -922 C ATOM 352 N LEU A 130 24.257 38.244 4.031 1.00 79.60 N ANISOU 352 N LEU A 130 11743 10023 8477 -2461 104 -1133 N ATOM 353 CA LEU A 130 24.653 37.514 5.227 1.00 82.97 C ANISOU 353 CA LEU A 130 11633 10679 9212 -2375 73 -1212 C ATOM 354 C LEU A 130 25.932 36.757 4.921 1.00 75.24 C ANISOU 354 C LEU A 130 10337 10056 8194 -2232 474 -1185 C ATOM 355 O LEU A 130 26.312 36.629 3.768 1.00 78.32 O ANISOU 355 O LEU A 130 10979 10478 8303 -2150 782 -1156 O ATOM 356 CB LEU A 130 23.541 36.552 5.682 1.00 77.69 C ANISOU 356 CB LEU A 130 11044 9806 8667 -2092 -274 -1389 C ATOM 357 CG LEU A 130 22.196 37.164 6.086 1.00 66.49 C ANISOU 357 CG LEU A 130 9844 8031 7389 -2186 -656 -1448 C ATOM 358 CD1 LEU A 130 21.169 36.092 6.327 1.00 70.55 C ANISOU 358 CD1 LEU A 130 10429 8363 8014 -1906 -925 -1620 C ATOM 359 CD2 LEU A 130 22.345 38.018 7.330 1.00 71.14 C ANISOU 359 CD2 LEU A 130 10136 8663 8233 -2489 -712 -1415 C ATOM 360 N THR A 131 26.616 36.287 5.952 1.00 70.22 N ANISOU 360 N THR A 131 9159 9679 7844 -2209 477 -1190 N ATOM 361 CA THR A 131 27.655 35.292 5.756 1.00 72.97 C ANISOU 361 CA THR A 131 9162 10315 8246 -1951 784 -1199 C ATOM 362 C THR A 131 27.594 34.352 6.922 1.00 80.15 C ANISOU 362 C THR A 131 9728 11288 9436 -1757 519 -1272 C ATOM 363 O THR A 131 27.008 34.677 7.959 1.00 92.46 O ANISOU 363 O THR A 131 11248 12743 11139 -1924 177 -1287 O ATOM 364 CB THR A 131 29.054 35.889 5.677 1.00 88.12 C ANISOU 364 CB THR A 131 10639 12577 10265 -2191 1164 -1043 C ATOM 365 OG1 THR A 131 28.982 37.187 5.091 1.00 94.31 O ANISOU 365 OG1 THR A 131 11720 13260 10855 -2559 1279 -931 O ATOM 366 CG2 THR A 131 29.955 34.996 4.822 1.00 92.87 C ANISOU 366 CG2 THR A 131 11092 13383 10811 -1882 1631 -1069 C ATOM 367 N PHE A 132 28.198 33.185 6.765 1.00 74.31 N ANISOU 367 N PHE A 132 8773 10697 8766 -1404 692 -1319 N ATOM 368 CA PHE A 132 28.224 32.234 7.855 1.00 72.14 C ANISOU 368 CA PHE A 132 8194 10467 8747 -1205 435 -1359 C ATOM 369 C PHE A 132 29.603 31.607 7.981 1.00 71.04 C ANISOU 369 C PHE A 132 7488 10661 8843 -1013 683 -1284 C ATOM 370 O PHE A 132 30.219 31.246 6.980 1.00 84.82 O ANISOU 370 O PHE A 132 9218 12500 10511 -802 1099 -1306 O ATOM 371 CB PHE A 132 27.153 31.165 7.652 1.00 69.60 C ANISOU 371 CB PHE A 132 8284 9844 8317 -873 247 -1529 C ATOM 372 CG PHE A 132 25.749 31.713 7.510 1.00 67.69 C ANISOU 372 CG PHE A 132 8532 9266 7920 -1030 -23 -1606 C ATOM 373 CD1 PHE A 132 24.938 31.896 8.627 1.00 61.04 C ANISOU 373 CD1 PHE A 132 7678 8280 7236 -1185 -379 -1635 C ATOM 374 CD2 PHE A 132 25.228 32.013 6.262 1.00 71.85 C ANISOU 374 CD2 PHE A 132 9539 9607 8154 -1013 76 -1651 C ATOM 375 CE1 PHE A 132 23.642 32.381 8.500 1.00 59.16 C ANISOU 375 CE1 PHE A 132 7818 7726 6935 -1298 -604 -1715 C ATOM 376 CE2 PHE A 132 23.936 32.504 6.131 1.00 67.29 C ANISOU 376 CE2 PHE A 132 9357 8711 7499 -1130 -224 -1709 C ATOM 377 CZ PHE A 132 23.139 32.684 7.251 1.00 59.44 C ANISOU 377 CZ PHE A 132 8269 7582 6735 -1259 -553 -1745 C ATOM 378 N SER A 133 30.087 31.524 9.218 1.00 81.33 N ANISOU 378 N SER A 133 8332 12133 10437 -1101 428 -1195 N ATOM 379 CA SER A 133 31.365 30.879 9.545 1.00 91.08 C ANISOU 379 CA SER A 133 8947 13672 11988 -899 540 -1103 C ATOM 380 C SER A 133 31.093 29.753 10.530 1.00 86.83 C ANISOU 380 C SER A 133 8350 13037 11605 -624 164 -1130 C ATOM 381 O SER A 133 30.209 29.884 11.380 1.00 70.72 O ANISOU 381 O SER A 133 6562 10812 9495 -794 -214 -1156 O ATOM 382 CB SER A 133 32.362 31.867 10.164 1.00 88.44 C ANISOU 382 CB SER A 133 8069 13651 11884 -1304 511 -925 C ATOM 383 OG SER A 133 32.217 33.169 9.634 1.00 84.87 O ANISOU 383 OG SER A 133 7825 13180 11243 -1714 685 -891 O ATOM 384 N ARG A 134 31.846 28.660 10.444 1.00 87.23 N ANISOU 384 N ARG A 134 8080 13190 11872 -205 281 -1119 N ATOM 385 CA ARG A 134 31.555 27.521 11.304 1.00 77.08 C ANISOU 385 CA ARG A 134 6820 11760 10709 80 -75 -1132 C ATOM 386 C ARG A 134 32.405 27.516 12.569 1.00 83.21 C ANISOU 386 C ARG A 134 7040 12770 11805 -25 -421 -941 C ATOM 387 O ARG A 134 33.597 27.838 12.538 1.00 81.40 O ANISOU 387 O ARG A 134 6220 12860 11848 -70 -285 -811 O ATOM 388 CB ARG A 134 31.746 26.202 10.553 1.00 74.26 C ANISOU 388 CB ARG A 134 6530 11288 10399 643 181 -1241 C ATOM 389 CG ARG A 134 31.062 25.032 11.237 1.00 71.09 C ANISOU 389 CG ARG A 134 6395 10603 10012 912 -173 -1293 C ATOM 390 CD ARG A 134 31.269 23.745 10.480 1.00 85.35 C ANISOU 390 CD ARG A 134 8305 12257 11869 1464 86 -1414 C ATOM 391 NE ARG A 134 30.935 22.594 11.313 1.00 99.45 N ANISOU 391 NE ARG A 134 10207 13812 13768 1723 -274 -1402 N ATOM 392 CZ ARG A 134 31.093 21.323 10.950 1.00101.71 C ANISOU 392 CZ ARG A 134 10592 13905 14150 2222 -158 -1489 C ATOM 393 NH1 ARG A 134 31.582 21.014 9.749 1.00 94.23 N ANISOU 393 NH1 ARG A 134 9646 12970 13188 2534 341 -1620 N ATOM 394 NH2 ARG A 134 30.760 20.355 11.797 1.00 97.39 N ANISOU 394 NH2 ARG A 134 10183 13125 13696 2401 -522 -1448 N ATOM 395 N LEU A 135 31.772 27.153 13.681 1.00 72.47 N ANISOU 395 N LEU A 135 5885 11241 10407 -84 -877 -921 N ATOM 396 CA LEU A 135 32.483 26.900 14.925 1.00 74.67 C ANISOU 396 CA LEU A 135 5759 11679 10934 -127 -1287 -737 C ATOM 397 C LEU A 135 32.351 25.441 15.299 1.00 86.48 C ANISOU 397 C LEU A 135 7359 12976 12523 331 -1485 -733 C ATOM 398 O LEU A 135 31.330 24.813 15.021 1.00 86.11 O ANISOU 398 O LEU A 135 7838 12608 12272 502 -1447 -884 O ATOM 399 CB LEU A 135 31.942 27.776 16.051 1.00 69.95 C ANISOU 399 CB LEU A 135 5363 11044 10170 -647 -1666 -692 C ATOM 400 CG LEU A 135 32.187 29.271 15.866 1.00 74.36 C ANISOU 400 CG LEU A 135 5794 11785 10674 -1137 -1536 -670 C ATOM 401 CD1 LEU A 135 31.509 30.080 16.969 1.00 81.33 C ANISOU 401 CD1 LEU A 135 6985 12555 11361 -1621 -1875 -675 C ATOM 402 CD2 LEU A 135 33.688 29.546 15.820 1.00 75.05 C ANISOU 402 CD2 LEU A 135 5152 12261 11102 -1178 -1481 -498 C ATOM 403 N TYR A 136 33.391 24.910 15.928 1.00 98.68 N ANISOU 403 N TYR A 136 8398 14698 14400 521 -1722 -551 N ATOM 404 CA TYR A 136 33.377 23.538 16.406 1.00101.13 C ANISOU 404 CA TYR A 136 8789 14804 14831 953 -1972 -502 C ATOM 405 C TYR A 136 33.452 23.554 17.919 1.00108.49 C ANISOU 405 C TYR A 136 9703 15751 15766 700 -2576 -307 C ATOM 406 O TYR A 136 33.415 22.513 18.572 1.00117.31 O ANISOU 406 O TYR A 136 10943 16686 16945 967 -2893 -215 O ATOM 407 CB TYR A 136 34.545 22.752 15.826 1.00 99.24 C ANISOU 407 CB TYR A 136 7995 14704 15009 1481 -1752 -444 C ATOM 408 CG TYR A 136 34.560 22.713 14.321 1.00101.04 C ANISOU 408 CG TYR A 136 8278 14917 15194 1726 -1105 -645 C ATOM 409 CD1 TYR A 136 34.200 21.566 13.638 1.00107.22 C ANISOU 409 CD1 TYR A 136 9397 15404 15937 2219 -876 -803 C ATOM 410 CD2 TYR A 136 34.936 23.826 13.581 1.00 99.49 C ANISOU 410 CD2 TYR A 136 7854 14981 14967 1441 -722 -677 C ATOM 411 CE1 TYR A 136 34.216 21.525 12.264 1.00111.49 C ANISOU 411 CE1 TYR A 136 10067 15916 16379 2422 -289 -998 C ATOM 412 CE2 TYR A 136 34.950 23.795 12.211 1.00 99.22 C ANISOU 412 CE2 TYR A 136 7949 14920 14831 1638 -126 -850 C ATOM 413 CZ TYR A 136 34.590 22.643 11.555 1.00107.99 C ANISOU 413 CZ TYR A 136 9417 15741 15872 2128 88 -1017 C ATOM 414 OH TYR A 136 34.601 22.607 10.180 1.00118.31 O ANISOU 414 OH TYR A 136 10930 17004 17017 2305 682 -1203 O ATOM 415 N GLU A 137 33.558 24.762 18.460 1.00105.73 N ANISOU 415 N GLU A 137 9251 15600 15321 164 -2733 -245 N ATOM 416 CA GLU A 137 33.806 24.970 19.879 1.00100.14 C ANISOU 416 CA GLU A 137 8501 14961 14588 -154 -3305 -57 C ATOM 417 C GLU A 137 33.064 26.196 20.374 1.00 95.74 C ANISOU 417 C GLU A 137 8317 14375 13684 -768 -3363 -137 C ATOM 418 O GLU A 137 32.906 27.164 19.640 1.00 99.98 O ANISOU 418 O GLU A 137 8837 14995 14157 -992 -3016 -255 O ATOM 419 CB GLU A 137 35.300 25.141 20.133 1.00101.65 C ANISOU 419 CB GLU A 137 7903 15521 15197 -132 -3523 167 C ATOM 420 CG GLU A 137 36.031 23.857 20.469 1.00109.96 C ANISOU 420 CG GLU A 137 8636 16548 16595 388 -3816 344 C ATOM 421 CD GLU A 137 37.448 24.118 20.922 1.00116.80 C ANISOU 421 CD GLU A 137 8696 17778 17905 339 -4154 589 C ATOM 422 OE1 GLU A 137 37.928 25.255 20.720 1.00113.56 O ANISOU 422 OE1 GLU A 137 7921 17659 17567 -60 -4031 590 O ATOM 423 OE2 GLU A 137 38.078 23.197 21.489 1.00135.06 O ANISOU 423 OE2 GLU A 137 10735 20072 20510 687 -4568 789 O ATOM 424 N GLY A 138 32.606 26.154 21.618 1.00100.43 N ANISOU 424 N GLY A 138 9282 14828 14048 -1037 -3783 -75 N ATOM 425 CA GLY A 138 31.974 27.309 22.232 1.00101.83 C ANISOU 425 CA GLY A 138 9813 14963 13913 -1620 -3846 -157 C ATOM 426 C GLY A 138 30.642 27.748 21.645 1.00 97.31 C ANISOU 426 C GLY A 138 9749 14133 13093 -1728 -3451 -411 C ATOM 427 O GLY A 138 29.950 26.990 20.961 1.00 80.29 O ANISOU 427 O GLY A 138 7824 11760 10922 -1380 -3211 -531 O ATOM 428 N GLU A 139 30.282 28.998 21.914 1.00 96.82 N ANISOU 428 N GLU A 139 9857 14078 12853 -2216 -3407 -495 N ATOM 429 CA GLU A 139 28.970 29.497 21.538 1.00 91.73 C ANISOU 429 CA GLU A 139 9688 13161 12004 -2348 -3106 -721 C ATOM 430 C GLU A 139 28.945 30.144 20.162 1.00 88.89 C ANISOU 430 C GLU A 139 9181 12860 11732 -2280 -2696 -821 C ATOM 431 O GLU A 139 29.539 31.200 19.948 1.00 86.31 O ANISOU 431 O GLU A 139 8610 12728 11455 -2563 -2626 -782 O ATOM 432 CB GLU A 139 28.472 30.506 22.573 1.00 98.73 C ANISOU 432 CB GLU A 139 10994 13834 12683 -2595 -2968 -817 C ATOM 433 CG GLU A 139 28.118 29.901 23.919 1.00103.04 C ANISOU 433 CG GLU A 139 11895 14222 13032 -2612 -3155 -775 C ATOM 434 CD GLU A 139 26.910 29.015 23.848 1.00 92.28 C ANISOU 434 CD GLU A 139 10902 12587 11574 -2458 -3057 -881 C ATOM 435 OE1 GLU A 139 26.047 29.257 22.981 1.00 92.58 O ANISOU 435 OE1 GLU A 139 11044 12477 11654 -2385 -2761 -1050 O ATOM 436 OE2 GLU A 139 26.823 28.074 24.660 1.00104.46 O ANISOU 436 OE2 GLU A 139 12645 14038 13009 -2411 -3288 -785 O ATOM 437 N ALA A 140 28.233 29.511 19.239 1.00 78.73 N ANISOU 437 N ALA A 140 8091 11383 10441 -1931 -2441 -946 N ATOM 438 CA ALA A 140 27.878 30.153 17.983 1.00 74.76 C ANISOU 438 CA ALA A 140 7647 10840 9918 -1911 -2081 -1064 C ATOM 439 C ALA A 140 26.495 30.770 18.078 1.00 76.48 C ANISOU 439 C ALA A 140 8340 10750 9967 -2136 -2024 -1239 C ATOM 440 O ALA A 140 25.705 30.452 18.988 1.00 65.79 O ANISOU 440 O ALA A 140 7283 9189 8526 -2225 -2181 -1301 O ATOM 441 CB ALA A 140 27.914 29.169 16.842 1.00 70.08 C ANISOU 441 CB ALA A 140 7025 10206 9395 -1421 -1853 -1110 C ATOM 442 N ASP A 141 26.213 31.639 17.112 1.00 63.66 N ANISOU 442 N ASP A 141 6786 9088 8312 -2219 -1783 -1311 N ATOM 443 CA ASP A 141 24.965 32.369 17.042 1.00 60.18 C ANISOU 443 CA ASP A 141 6733 8343 7788 -2383 -1714 -1455 C ATOM 444 C ASP A 141 23.839 31.404 16.785 1.00 69.04 C ANISOU 444 C ASP A 141 8142 9193 8895 -2121 -1718 -1600 C ATOM 445 O ASP A 141 22.881 31.313 17.551 1.00 70.70 O ANISOU 445 O ASP A 141 8609 9095 9160 -2015 -1737 -1597 O ATOM 446 CB ASP A 141 25.031 33.429 15.942 1.00 64.67 C ANISOU 446 CB ASP A 141 7303 8941 8329 -2509 -1500 -1472 C ATOM 447 CG ASP A 141 25.882 34.623 16.334 1.00 69.80 C ANISOU 447 CG ASP A 141 7784 9720 9018 -2774 -1465 -1315 C ATOM 448 OD1 ASP A 141 25.934 34.948 17.544 1.00 77.77 O ANISOU 448 OD1 ASP A 141 8855 10625 10068 -2798 -1567 -1239 O ATOM 449 OD2 ASP A 141 26.500 35.234 15.432 1.00 80.29 O ANISOU 449 OD2 ASP A 141 8932 11253 10323 -2966 -1311 -1294 O ATOM 450 N ILE A 142 23.972 30.671 15.692 1.00 72.06 N ANISOU 450 N ILE A 142 8504 9586 9289 -1763 -1595 -1611 N ATOM 451 CA ILE A 142 23.037 29.609 15.393 1.00 60.78 C ANISOU 451 CA ILE A 142 7337 7897 7860 -1483 -1621 -1732 C ATOM 452 C ILE A 142 23.612 28.256 15.794 1.00 66.32 C ANISOU 452 C ILE A 142 7923 8664 8611 -1194 -1717 -1661 C ATOM 453 O ILE A 142 24.529 27.741 15.151 1.00 74.37 O ANISOU 453 O ILE A 142 8733 9855 9669 -917 -1612 -1594 O ATOM 454 CB ILE A 142 22.671 29.603 13.918 1.00 59.36 C ANISOU 454 CB ILE A 142 7321 7614 7618 -1279 -1458 -1816 C ATOM 455 CG1 ILE A 142 21.792 30.817 13.607 1.00 57.16 C ANISOU 455 CG1 ILE A 142 7238 7163 7316 -1534 -1445 -1889 C ATOM 456 CG2 ILE A 142 21.942 28.309 13.555 1.00 44.29 C ANISOU 456 CG2 ILE A 142 5649 5468 5712 -963 -1511 -1932 C ATOM 457 CD1 ILE A 142 21.330 30.868 12.165 1.00 70.58 C ANISOU 457 CD1 ILE A 142 9174 8725 8918 -1365 -1361 -1955 C ATOM 458 N MET A 143 23.071 27.688 16.868 1.00 56.67 N ANISOU 458 N MET A 143 6854 7284 7394 -1257 -1897 -1675 N ATOM 459 CA MET A 143 23.553 26.408 17.369 1.00 63.02 C ANISOU 459 CA MET A 143 7609 8097 8241 -1000 -2036 -1585 C ATOM 460 C MET A 143 22.660 25.285 16.873 1.00 62.60 C ANISOU 460 C MET A 143 7852 7738 8196 -722 -2009 -1714 C ATOM 461 O MET A 143 21.453 25.342 17.053 1.00 77.01 O ANISOU 461 O MET A 143 9952 9304 10005 -872 -2018 -1844 O ATOM 462 CB MET A 143 23.614 26.424 18.893 1.00 66.81 C ANISOU 462 CB MET A 143 8131 8582 8671 -1267 -2270 -1488 C ATOM 463 CG MET A 143 24.640 27.399 19.439 1.00 73.19 C ANISOU 463 CG MET A 143 8641 9696 9469 -1543 -2367 -1348 C ATOM 464 SD MET A 143 26.268 26.645 19.640 1.00 84.14 S ANISOU 464 SD MET A 143 9577 11389 11005 -1271 -2564 -1107 S ATOM 465 CE MET A 143 26.307 26.338 21.407 1.00110.26 C ANISOU 465 CE MET A 143 13069 14643 14181 -1528 -2970 -969 C ATOM 466 N ILE A 144 23.260 24.278 16.236 1.00 67.48 N ANISOU 466 N ILE A 144 8400 8375 8864 -324 -1964 -1688 N ATOM 467 CA ILE A 144 22.516 23.182 15.600 1.00 69.31 C ANISOU 467 CA ILE A 144 8937 8306 9092 -46 -1932 -1825 C ATOM 468 C ILE A 144 22.580 21.922 16.447 1.00 63.53 C ANISOU 468 C ILE A 144 8311 7416 8412 119 -2110 -1749 C ATOM 469 O ILE A 144 23.650 21.531 16.901 1.00 82.55 O ANISOU 469 O ILE A 144 10481 9992 10894 282 -2203 -1582 O ATOM 470 CB ILE A 144 23.049 22.867 14.171 1.00 60.80 C ANISOU 470 CB ILE A 144 7823 7283 7994 303 -1712 -1890 C ATOM 471 CG1 ILE A 144 22.638 23.964 13.204 1.00 67.94 C ANISOU 471 CG1 ILE A 144 8802 8224 8789 132 -1559 -1986 C ATOM 472 CG2 ILE A 144 22.436 21.611 13.621 1.00 55.06 C ANISOU 472 CG2 ILE A 144 7435 6235 7252 596 -1716 -2029 C ATOM 473 CD1 ILE A 144 21.151 24.257 13.253 1.00 64.79 C ANISOU 473 CD1 ILE A 144 8713 7537 8366 -95 -1676 -2126 C ATOM 474 N SER A 145 21.424 21.294 16.641 1.00 64.10 N ANISOU 474 N SER A 145 8734 7151 8469 70 -2169 -1863 N ATOM 475 CA SER A 145 21.264 20.213 17.604 1.00 67.51 C ANISOU 475 CA SER A 145 9357 7375 8918 119 -2340 -1783 C ATOM 476 C SER A 145 20.354 19.111 17.060 1.00 67.07 C ANISOU 476 C SER A 145 9650 6942 8891 294 -2320 -1937 C ATOM 477 O SER A 145 19.489 19.378 16.239 1.00 65.33 O ANISOU 477 O SER A 145 9559 6595 8671 231 -2230 -2119 O ATOM 478 CB SER A 145 20.672 20.767 18.898 1.00 61.71 C ANISOU 478 CB SER A 145 8728 6604 8115 -316 -2434 -1739 C ATOM 479 OG SER A 145 21.040 22.128 19.069 1.00 78.51 O ANISOU 479 OG SER A 145 10617 9011 10201 -581 -2394 -1707 O ATOM 480 N PHE A 146 20.538 17.883 17.527 1.00 70.82 N ANISOU 480 N PHE A 146 10293 7219 9396 497 -2439 -1854 N ATOM 481 CA PHE A 146 19.572 16.813 17.276 1.00 67.09 C ANISOU 481 CA PHE A 146 10202 6338 8952 568 -2453 -1987 C ATOM 482 C PHE A 146 19.057 16.304 18.611 1.00 79.74 C ANISOU 482 C PHE A 146 12038 7728 10531 327 -2588 -1880 C ATOM 483 O PHE A 146 19.848 16.111 19.534 1.00 75.14 O ANISOU 483 O PHE A 146 11399 7245 9905 356 -2733 -1663 O ATOM 484 CB PHE A 146 20.207 15.677 16.496 1.00 64.74 C ANISOU 484 CB PHE A 146 9990 5909 8701 1051 -2433 -2008 C ATOM 485 CG PHE A 146 20.437 15.991 15.054 1.00 73.18 C ANISOU 485 CG PHE A 146 10984 7081 9739 1263 -2242 -2170 C ATOM 486 CD1 PHE A 146 21.563 16.676 14.655 1.00 65.47 C ANISOU 486 CD1 PHE A 146 9642 6472 8764 1409 -2111 -2094 C ATOM 487 CD2 PHE A 146 19.522 15.592 14.094 1.00 78.57 C ANISOU 487 CD2 PHE A 146 11988 7484 10380 1289 -2199 -2397 C ATOM 488 CE1 PHE A 146 21.768 16.960 13.327 1.00 69.29 C ANISOU 488 CE1 PHE A 146 10120 7035 9172 1576 -1892 -2239 C ATOM 489 CE2 PHE A 146 19.722 15.877 12.763 1.00 82.00 C ANISOU 489 CE2 PHE A 146 12443 7995 10717 1460 -2037 -2542 C ATOM 490 CZ PHE A 146 20.845 16.560 12.378 1.00 78.54 C ANISOU 490 CZ PHE A 146 11680 7917 10246 1604 -1860 -2462 C ATOM 491 N ALA A 147 17.756 16.086 18.753 1.00 71.22 N ANISOU 491 N ALA A 147 11126 6474 9460 76 -2445 -1920 N ATOM 492 CA ALA A 147 17.300 15.606 20.051 1.00 76.12 C ANISOU 492 CA ALA A 147 11949 6949 10023 -168 -2466 -1779 C ATOM 493 C ALA A 147 16.025 14.791 20.021 1.00 76.42 C ANISOU 493 C ALA A 147 12084 6846 10108 -285 -2219 -1758 C ATOM 494 O ALA A 147 15.450 14.529 18.973 1.00 81.05 O ANISOU 494 O ALA A 147 12585 7443 10769 -193 -2069 -1838 O ATOM 495 CB ALA A 147 17.133 16.776 21.005 1.00 70.30 C ANISOU 495 CB ALA A 147 11059 6456 9196 -546 -2357 -1703 C ATOM 496 N VAL A 148 15.598 14.391 21.208 1.00 82.28 N ANISOU 496 N VAL A 148 13816 7881 9564 -1228 -2495 733 N ATOM 497 CA VAL A 148 14.428 13.566 21.360 1.00 73.40 C ANISOU 497 CA VAL A 148 12774 6432 8681 -1290 -2195 876 C ATOM 498 C VAL A 148 13.685 13.978 22.622 1.00 81.68 C ANISOU 498 C VAL A 148 14123 7620 9291 -1484 -1975 1046 C ATOM 499 O VAL A 148 14.285 14.091 23.697 1.00 70.14 O ANISOU 499 O VAL A 148 12879 6386 7384 -1488 -2120 1324 O ATOM 500 CB VAL A 148 14.824 12.073 21.408 1.00 89.38 C ANISOU 500 CB VAL A 148 14768 8135 11059 -1116 -2282 1218 C ATOM 501 CG1 VAL A 148 13.845 11.266 22.222 1.00 82.33 C ANISOU 501 CG1 VAL A 148 14102 6983 10198 -1216 -1988 1543 C ATOM 502 CG2 VAL A 148 14.946 11.516 19.998 1.00 77.40 C ANISOU 502 CG2 VAL A 148 12930 6360 10118 -991 -2312 950 C ATOM 503 N ARG A 149 12.383 14.219 22.479 1.00 79.16 N ANISOU 503 N ARG A 149 13807 7172 9098 -1649 -1632 848 N ATOM 504 CA ARG A 149 11.543 14.585 23.611 1.00 83.51 C ANISOU 504 CA ARG A 149 14614 7824 9294 -1866 -1341 943 C ATOM 505 C ARG A 149 12.102 15.796 24.326 1.00 68.78 C ANISOU 505 C ARG A 149 12887 6400 6847 -1944 -1483 877 C ATOM 506 O ARG A 149 12.348 16.813 23.695 1.00 64.88 O ANISOU 506 O ARG A 149 12238 6080 6334 -1940 -1604 530 O ATOM 507 CB ARG A 149 11.413 13.430 24.597 1.00 92.61 C ANISOU 507 CB ARG A 149 16024 8790 10375 -1887 -1208 1435 C ATOM 508 CG ARG A 149 11.032 12.116 23.977 1.00 90.21 C ANISOU 508 CG ARG A 149 15589 8022 10666 -1796 -1091 1547 C ATOM 509 CD ARG A 149 9.787 12.177 23.136 1.00 89.65 C ANISOU 509 CD ARG A 149 15291 7711 11062 -1897 -783 1155 C ATOM 510 NE ARG A 149 9.536 10.847 22.580 1.00101.28 N ANISOU 510 NE ARG A 149 16630 8742 13111 -1805 -696 1264 N ATOM 511 CZ ARG A 149 8.340 10.371 22.251 1.00 98.42 C ANISOU 511 CZ ARG A 149 16148 8056 13192 -1916 -349 1095 C ATOM 512 NH1 ARG A 149 7.251 11.120 22.414 1.00 74.71 N ANISOU 512 NH1 ARG A 149 13127 5118 10141 -2118 -58 800 N ATOM 513 NH2 ARG A 149 8.239 9.138 21.757 1.00105.77 N ANISOU 513 NH2 ARG A 149 16949 8584 14654 -1824 -295 1193 N ATOM 514 N GLU A 150 12.324 15.676 25.635 1.00 78.59 N ANISOU 514 N GLU A 150 14437 7817 7606 -2020 -1473 1212 N ATOM 515 CA GLU A 150 12.846 16.801 26.411 1.00 83.31 C ANISOU 515 CA GLU A 150 15174 8853 7627 -2109 -1606 1131 C ATOM 516 C GLU A 150 14.301 17.028 26.115 1.00 86.14 C ANISOU 516 C GLU A 150 15407 9421 7903 -1916 -2072 1131 C ATOM 517 O GLU A 150 15.111 16.104 26.186 1.00 94.56 O ANISOU 517 O GLU A 150 16481 10396 9052 -1730 -2331 1444 O ATOM 518 CB GLU A 150 12.686 16.587 27.910 1.00100.61 C ANISOU 518 CB GLU A 150 17760 11196 9271 -2253 -1477 1482 C ATOM 519 CG GLU A 150 11.273 16.713 28.403 1.00111.79 C ANISOU 519 CG GLU A 150 19316 12513 10648 -2519 -958 1389 C ATOM 520 CD GLU A 150 10.495 15.426 28.243 1.00124.77 C ANISOU 520 CD GLU A 150 20988 13709 12709 -2527 -674 1628 C ATOM 521 OE1 GLU A 150 10.893 14.571 27.422 1.00122.57 O ANISOU 521 OE1 GLU A 150 20530 13159 12884 -2317 -863 1740 O ATOM 522 OE2 GLU A 150 9.487 15.260 28.957 1.00138.84 O ANISOU 522 OE2 GLU A 150 22970 15405 14380 -2759 -237 1686 O ATOM 523 N HIS A 151 14.639 18.271 25.818 1.00 74.59 N ANISOU 523 N HIS A 151 13821 8224 6297 -1965 -2171 769 N ATOM 524 CA HIS A 151 15.984 18.572 25.410 1.00 70.28 C ANISOU 524 CA HIS A 151 13103 7858 5741 -1811 -2561 686 C ATOM 525 C HIS A 151 16.348 19.998 25.751 1.00 72.03 C ANISOU 525 C HIS A 151 13333 8457 5579 -1937 -2632 391 C ATOM 526 O HIS A 151 16.810 20.751 24.890 1.00 75.11 O ANISOU 526 O HIS A 151 13509 8904 6127 -1917 -2731 69 O ATOM 527 CB HIS A 151 16.131 18.320 23.910 1.00 70.79 C ANISOU 527 CB HIS A 151 12861 7671 6364 -1682 -2605 470 C ATOM 528 CG HIS A 151 15.198 19.130 23.060 1.00 69.75 C ANISOU 528 CG HIS A 151 12626 7448 6427 -1801 -2363 84 C ATOM 529 ND1 HIS A 151 13.923 18.714 22.749 1.00 69.97 N ANISOU 529 ND1 HIS A 151 12655 7186 6743 -1862 -2065 46 N ATOM 530 CD2 HIS A 151 15.364 20.330 22.445 1.00 78.38 C ANISOU 530 CD2 HIS A 151 13613 8682 7488 -1863 -2398 -281 C ATOM 531 CE1 HIS A 151 13.343 19.620 21.978 1.00 67.89 C ANISOU 531 CE1 HIS A 151 12284 6898 6614 -1933 -1966 -325 C ATOM 532 NE2 HIS A 151 14.194 20.612 21.781 1.00 61.63 N ANISOU 532 NE2 HIS A 151 11446 6353 5618 -1937 -2159 -509 N ATOM 533 N GLY A 152 16.125 20.371 27.008 1.00 84.40 N ANISOU 533 N GLY A 152 15162 10272 6635 -2084 -2557 492 N ATOM 534 CA GLY A 152 16.565 21.658 27.528 1.00 72.17 C ANISOU 534 CA GLY A 152 13588 9099 4735 -2184 -2617 229 C ATOM 535 C GLY A 152 15.839 22.893 27.015 1.00 77.52 C ANISOU 535 C GLY A 152 14040 9767 5647 -2288 -2299 -200 C ATOM 536 O GLY A 152 16.422 23.975 26.993 1.00 89.19 O ANISOU 536 O GLY A 152 15201 11454 7236 -2209 -2274 -435 O ATOM 537 N ASP A 153 14.586 22.746 26.594 1.00 71.67 N ANISOU 537 N ASP A 153 13447 8769 5016 -2440 -2061 -301 N ATOM 538 CA ASP A 153 13.734 23.904 26.341 1.00 62.59 C ANISOU 538 CA ASP A 153 12091 7603 4088 -2517 -1751 -659 C ATOM 539 C ASP A 153 12.258 23.623 26.597 1.00 74.93 C ANISOU 539 C ASP A 153 13879 8962 5628 -2733 -1422 -723 C ATOM 540 O ASP A 153 11.866 22.504 26.938 1.00 86.76 O ANISOU 540 O ASP A 153 15492 10300 7174 -2719 -1292 -417 O ATOM 541 CB ASP A 153 13.924 24.425 24.916 1.00 63.26 C ANISOU 541 CB ASP A 153 11777 7543 4716 -2327 -1769 -871 C ATOM 542 CG ASP A 153 13.441 23.460 23.849 1.00 80.84 C ANISOU 542 CG ASP A 153 14053 9406 7257 -2298 -1815 -851 C ATOM 543 OD1 ASP A 153 12.757 22.457 24.168 1.00 78.23 O ANISOU 543 OD1 ASP A 153 13924 8880 6919 -2373 -1718 -681 O ATOM 544 OD2 ASP A 153 13.741 23.735 22.664 1.00 84.23 O ANISOU 544 OD2 ASP A 153 14158 9759 8084 -2109 -1837 -958 O ATOM 545 N PHE A 154 11.435 24.643 26.396 1.00 72.91 N ANISOU 545 N PHE A 154 13444 8676 5584 -2797 -1183 -1057 N ATOM 546 CA PHE A 154 10.020 24.551 26.736 1.00 83.50 C ANISOU 546 CA PHE A 154 14913 9843 6972 -3008 -817 -1209 C ATOM 547 C PHE A 154 9.228 23.602 25.865 1.00 82.56 C ANISOU 547 C PHE A 154 14655 9324 7390 -2913 -702 -1157 C ATOM 548 O PHE A 154 8.070 23.303 26.167 1.00 82.80 O ANISOU 548 O PHE A 154 14689 9179 7591 -3035 -354 -1220 O ATOM 549 CB PHE A 154 9.382 25.926 26.641 1.00 87.48 C ANISOU 549 CB PHE A 154 15101 10402 7737 -2986 -626 -1549 C ATOM 550 CG PHE A 154 9.692 26.798 27.793 1.00 90.17 C ANISOU 550 CG PHE A 154 15459 11083 7717 -3070 -546 -1590 C ATOM 551 CD1 PHE A 154 9.748 28.166 27.641 1.00 83.96 C ANISOU 551 CD1 PHE A 154 14320 10405 7175 -2926 -534 -1804 C ATOM 552 CD2 PHE A 154 9.930 26.246 29.041 1.00 89.45 C ANISOU 552 CD2 PHE A 154 15743 11203 7043 -3266 -489 -1388 C ATOM 553 CE1 PHE A 154 10.047 28.974 28.718 1.00 83.99 C ANISOU 553 CE1 PHE A 154 14332 10695 6885 -3003 -470 -1876 C ATOM 554 CE2 PHE A 154 10.222 27.046 30.117 1.00 83.61 C ANISOU 554 CE2 PHE A 154 14977 10781 6010 -3317 -424 -1439 C ATOM 555 CZ PHE A 154 10.276 28.410 29.958 1.00 80.25 C ANISOU 555 CZ PHE A 154 14192 10438 5863 -3200 -414 -1714 C ATOM 556 N TYR A 155 9.848 23.140 24.782 1.00 72.64 N ANISOU 556 N TYR A 155 13262 7925 6415 -2710 -976 -1080 N ATOM 557 CA TYR A 155 9.091 22.547 23.689 1.00 77.32 C ANISOU 557 CA TYR A 155 13667 8149 7562 -2612 -915 -1171 C ATOM 558 C TYR A 155 9.547 21.155 23.308 1.00 72.19 C ANISOU 558 C TYR A 155 13000 7319 7111 -2458 -1027 -845 C ATOM 559 O TYR A 155 10.218 20.976 22.290 1.00 62.03 O ANISOU 559 O TYR A 155 11581 5963 6025 -2294 -1282 -866 O ATOM 560 CB TYR A 155 9.162 23.470 22.476 1.00 57.93 C ANISOU 560 CB TYR A 155 10872 5712 5428 -2409 -1049 -1416 C ATOM 561 CG TYR A 155 8.713 24.861 22.830 1.00 59.39 C ANISOU 561 CG TYR A 155 10852 6111 5603 -2388 -895 -1614 C ATOM 562 CD1 TYR A 155 7.388 25.106 23.170 1.00 56.37 C ANISOU 562 CD1 TYR A 155 10413 5612 5392 -2494 -624 -1820 C ATOM 563 CD2 TYR A 155 9.615 25.920 22.867 1.00 62.53 C ANISOU 563 CD2 TYR A 155 11094 6793 5873 -2267 -1006 -1613 C ATOM 564 CE1 TYR A 155 6.963 26.371 23.510 1.00 72.26 C ANISOU 564 CE1 TYR A 155 12239 7781 7436 -2465 -518 -2015 C ATOM 565 CE2 TYR A 155 9.198 27.198 23.199 1.00 62.64 C ANISOU 565 CE2 TYR A 155 10930 6941 5931 -2244 -885 -1800 C ATOM 566 CZ TYR A 155 7.867 27.416 23.521 1.00 64.94 C ANISOU 566 CZ TYR A 155 11191 7107 6376 -2339 -663 -1997 C ATOM 567 OH TYR A 155 7.429 28.669 23.865 1.00 76.26 O ANISOU 567 OH TYR A 155 12456 8639 7881 -2308 -573 -2193 O ATOM 568 N PRO A 156 9.175 20.165 24.128 1.00 71.70 N ANISOU 568 N PRO A 156 13080 7165 6999 -2523 -813 -549 N ATOM 569 CA PRO A 156 9.546 18.767 23.882 1.00 73.36 C ANISOU 569 CA PRO A 156 13287 7155 7430 -2381 -892 -212 C ATOM 570 C PRO A 156 9.195 18.309 22.487 1.00 67.82 C ANISOU 570 C PRO A 156 12321 6138 7309 -2246 -944 -401 C ATOM 571 O PRO A 156 8.108 18.629 22.015 1.00 64.45 O ANISOU 571 O PRO A 156 11759 5546 7181 -2311 -761 -708 O ATOM 572 CB PRO A 156 8.725 18.003 24.914 1.00 66.68 C ANISOU 572 CB PRO A 156 12636 6184 6516 -2539 -526 32 C ATOM 573 CG PRO A 156 8.556 18.977 26.045 1.00 78.10 C ANISOU 573 CG PRO A 156 14285 7952 7440 -2745 -372 -43 C ATOM 574 CD PRO A 156 8.477 20.343 25.417 1.00 67.02 C ANISOU 574 CD PRO A 156 12693 6683 6089 -2749 -476 -500 C ATOM 575 N PHE A 157 10.109 17.597 21.837 1.00 77.33 N ANISOU 575 N PHE A 157 13442 7266 8673 -2060 -1203 -249 N ATOM 576 CA PHE A 157 9.783 16.881 20.610 1.00 66.03 C ANISOU 576 CA PHE A 157 11789 5516 7784 -1940 -1223 -384 C ATOM 577 C PHE A 157 8.919 15.710 20.949 1.00 60.29 C ANISOU 577 C PHE A 157 11076 4472 7359 -1987 -940 -207 C ATOM 578 O PHE A 157 8.846 15.290 22.102 1.00 63.71 O ANISOU 578 O PHE A 157 11725 4927 7554 -2084 -772 110 O ATOM 579 CB PHE A 157 11.024 16.408 19.876 1.00 62.56 C ANISOU 579 CB PHE A 157 11247 5081 7441 -1746 -1537 -297 C ATOM 580 CG PHE A 157 11.706 17.490 19.130 1.00 53.37 C ANISOU 580 CG PHE A 157 10008 4132 6139 -1711 -1761 -568 C ATOM 581 CD1 PHE A 157 10.973 18.359 18.347 1.00 53.36 C ANISOU 581 CD1 PHE A 157 9931 4096 6248 -1762 -1717 -932 C ATOM 582 CD2 PHE A 157 13.071 17.670 19.229 1.00 66.07 C ANISOU 582 CD2 PHE A 157 11625 5965 7516 -1631 -2018 -466 C ATOM 583 CE1 PHE A 157 11.602 19.394 17.641 1.00 70.66 C ANISOU 583 CE1 PHE A 157 11890 6628 8329 -1624 -1779 -1065 C ATOM 584 CE2 PHE A 157 13.704 18.706 18.541 1.00 79.87 C ANISOU 584 CE2 PHE A 157 13310 7895 9142 -1632 -2176 -729 C ATOM 585 CZ PHE A 157 12.966 19.572 17.744 1.00 76.40 C ANISOU 585 CZ PHE A 157 12688 7520 8822 -1606 -2004 -985 C ATOM 586 N ASP A 158 8.278 15.179 19.922 1.00 64.53 N ANISOU 586 N ASP A 158 11394 4709 8416 -1927 -887 -419 N ATOM 587 CA ASP A 158 7.164 14.266 20.102 1.00 61.56 C ANISOU 587 CA ASP A 158 10969 3999 8424 -2013 -557 -393 C ATOM 588 C ASP A 158 7.373 12.920 19.458 1.00 73.80 C ANISOU 588 C ASP A 158 12386 5226 10430 -1876 -600 -270 C ATOM 589 O ASP A 158 6.405 12.274 19.045 1.00 76.80 O ANISOU 589 O ASP A 158 12605 5289 11288 -1913 -390 -428 O ATOM 590 CB ASP A 158 5.889 14.896 19.541 1.00 79.74 C ANISOU 590 CB ASP A 158 13083 6198 11015 -2098 -403 -851 C ATOM 591 CG ASP A 158 6.070 15.421 18.130 1.00 83.98 C ANISOU 591 CG ASP A 158 13283 6884 11740 -1872 -667 -1171 C ATOM 592 OD1 ASP A 158 6.918 14.876 17.393 1.00 75.31 O ANISOU 592 OD1 ASP A 158 12099 5785 10729 -1711 -861 -1095 O ATOM 593 OD2 ASP A 158 5.366 16.387 17.766 1.00 89.35 O ANISOU 593 OD2 ASP A 158 13696 7777 12476 -1808 -632 -1465 O ATOM 594 N GLY A 159 8.627 12.489 19.375 1.00 82.18 N ANISOU 594 N GLY A 159 13485 6354 11386 -1719 -870 -20 N ATOM 595 CA GLY A 159 8.922 11.191 18.800 1.00 75.29 C ANISOU 595 CA GLY A 159 12474 5162 10968 -1578 -919 93 C ATOM 596 C GLY A 159 8.694 11.187 17.304 1.00 74.74 C ANISOU 596 C GLY A 159 12116 4968 11312 -1487 -1025 -337 C ATOM 597 O GLY A 159 8.614 12.244 16.690 1.00 90.17 O ANISOU 597 O GLY A 159 13959 7201 13099 -1470 -1108 -652 O ATOM 598 N PRO A 160 8.566 9.995 16.714 1.00 73.53 N ANISOU 598 N PRO A 160 11750 4549 11641 -1382 -936 -346 N ATOM 599 CA PRO A 160 8.501 9.849 15.259 1.00 77.95 C ANISOU 599 CA PRO A 160 11946 5296 12373 -1225 -906 -711 C ATOM 600 C PRO A 160 7.333 10.599 14.642 1.00 78.62 C ANISOU 600 C PRO A 160 11893 5613 12366 -1275 -717 -1067 C ATOM 601 O PRO A 160 6.192 10.316 15.001 1.00 83.81 O ANISOU 601 O PRO A 160 12590 6107 13147 -1387 -485 -1102 O ATOM 602 CB PRO A 160 8.308 8.338 15.060 1.00 64.04 C ANISOU 602 CB PRO A 160 10082 3229 11022 -1161 -749 -610 C ATOM 603 CG PRO A 160 8.666 7.714 16.356 1.00 74.09 C ANISOU 603 CG PRO A 160 11610 4159 12383 -1221 -753 -133 C ATOM 604 CD PRO A 160 8.320 8.717 17.401 1.00 75.78 C ANISOU 604 CD PRO A 160 12134 4428 12232 -1422 -752 -2 C ATOM 605 N GLY A 161 7.608 11.525 13.727 1.00 71.53 N ANISOU 605 N GLY A 161 10879 5083 11217 -1197 -842 -1280 N ATOM 606 CA GLY A 161 6.546 12.174 12.982 1.00 53.68 C ANISOU 606 CA GLY A 161 8519 3041 8836 -1207 -728 -1527 C ATOM 607 C GLY A 161 6.063 13.479 13.564 1.00 66.86 C ANISOU 607 C GLY A 161 10241 4872 10291 -1304 -674 -1610 C ATOM 608 O GLY A 161 6.709 14.104 14.418 1.00 68.39 O ANISOU 608 O GLY A 161 10531 5106 10347 -1343 -796 -1507 O ATOM 609 N ASN A 162 4.912 13.898 13.061 1.00 73.45 N ANISOU 609 N ASN A 162 11043 5806 11059 -1319 -591 -1764 N ATOM 610 CA ASN A 162 4.303 15.161 13.424 1.00 66.31 C ANISOU 610 CA ASN A 162 10170 5059 9965 -1395 -532 -1868 C ATOM 611 C ASN A 162 5.277 16.342 13.394 1.00 64.16 C ANISOU 611 C ASN A 162 9804 5085 9488 -1338 -655 -1884 C ATOM 612 O ASN A 162 5.596 16.808 12.307 1.00 72.72 O ANISOU 612 O ASN A 162 10807 6396 10427 -1233 -755 -1912 O ATOM 613 CB ASN A 162 3.628 15.004 14.772 1.00 77.86 C ANISOU 613 CB ASN A 162 11798 6292 11495 -1555 -405 -1804 C ATOM 614 CG ASN A 162 2.318 14.256 14.644 1.00 76.91 C ANISOU 614 CG ASN A 162 11653 5942 11629 -1538 -465 -1842 C ATOM 615 OD1 ASN A 162 1.466 14.642 13.844 1.00 68.97 O ANISOU 615 OD1 ASN A 162 10471 5086 10649 -1437 -504 -1997 O ATOM 616 ND2 ASN A 162 2.165 13.160 15.387 1.00 71.49 N ANISOU 616 ND2 ASN A 162 10957 4945 11262 -1611 -373 -1721 N ATOM 617 N VAL A 163 5.736 16.849 14.540 1.00 74.06 N ANISOU 617 N VAL A 163 11126 6335 10679 -1390 -737 -1821 N ATOM 618 CA VAL A 163 6.761 17.921 14.528 1.00 47.46 C ANISOU 618 CA VAL A 163 7817 3251 6963 -1326 -957 -1752 C ATOM 619 C VAL A 163 8.073 17.303 14.105 1.00 65.50 C ANISOU 619 C VAL A 163 10189 5543 9156 -1252 -1147 -1593 C ATOM 620 O VAL A 163 8.470 16.279 14.641 1.00 68.76 O ANISOU 620 O VAL A 163 10756 5704 9665 -1294 -1212 -1433 O ATOM 621 CB VAL A 163 6.933 18.568 15.883 1.00 48.31 C ANISOU 621 CB VAL A 163 8170 3369 6817 -1450 -1024 -1660 C ATOM 622 CG1 VAL A 163 8.048 19.621 15.860 1.00 47.50 C ANISOU 622 CG1 VAL A 163 8159 3568 6322 -1411 -1196 -1586 C ATOM 623 CG2 VAL A 163 5.648 19.181 16.324 1.00 74.05 C ANISOU 623 CG2 VAL A 163 11299 6605 10230 -1512 -847 -1860 C ATOM 624 N LEU A 164 8.745 17.894 13.130 1.00 66.95 N ANISOU 624 N LEU A 164 10276 5977 9184 -1154 -1220 -1626 N ATOM 625 CA LEU A 164 10.018 17.339 12.680 1.00 54.22 C ANISOU 625 CA LEU A 164 8706 4371 7524 -1095 -1374 -1532 C ATOM 626 C LEU A 164 11.179 18.134 13.262 1.00 53.97 C ANISOU 626 C LEU A 164 8836 4504 7166 -1122 -1542 -1425 C ATOM 627 O LEU A 164 12.228 17.594 13.599 1.00 68.57 O ANISOU 627 O LEU A 164 10821 6272 8962 -1133 -1719 -1309 O ATOM 628 CB LEU A 164 10.084 17.330 11.158 1.00 60.04 C ANISOU 628 CB LEU A 164 9267 5244 8302 -1009 -1307 -1644 C ATOM 629 CG LEU A 164 8.982 16.507 10.515 1.00 63.39 C ANISOU 629 CG LEU A 164 9588 5527 8969 -1000 -1163 -1741 C ATOM 630 CD1 LEU A 164 9.134 16.407 9.003 1.00 65.51 C ANISOU 630 CD1 LEU A 164 9774 5914 9204 -940 -1153 -1820 C ATOM 631 CD2 LEU A 164 9.033 15.156 11.119 1.00 59.56 C ANISOU 631 CD2 LEU A 164 9149 4739 8743 -1016 -1168 -1666 C ATOM 632 N ALA A 165 10.972 19.433 13.387 1.00 54.02 N ANISOU 632 N ALA A 165 8816 4732 6978 -1136 -1486 -1472 N ATOM 633 CA ALA A 165 11.996 20.324 13.886 1.00 51.44 C ANISOU 633 CA ALA A 165 8599 4596 6350 -1169 -1584 -1399 C ATOM 634 C ALA A 165 11.340 21.617 14.305 1.00 54.81 C ANISOU 634 C ALA A 165 8988 5175 6662 -1197 -1478 -1462 C ATOM 635 O ALA A 165 10.204 21.868 13.904 1.00 49.44 O ANISOU 635 O ALA A 165 8158 4471 6157 -1166 -1349 -1580 O ATOM 636 CB ALA A 165 13.028 20.576 12.828 1.00 65.37 C ANISOU 636 CB ALA A 165 10241 6513 8082 -1096 -1593 -1429 C ATOM 637 N HIS A 166 12.053 22.428 15.095 1.00 62.22 N ANISOU 637 N HIS A 166 10039 6266 7335 -1257 -1533 -1404 N ATOM 638 CA HIS A 166 11.688 23.829 15.360 1.00 66.20 C ANISOU 638 CA HIS A 166 10459 6937 7755 -1261 -1431 -1483 C ATOM 639 C HIS A 166 12.949 24.674 15.583 1.00 63.23 C ANISOU 639 C HIS A 166 10092 6766 7167 -1272 -1474 -1443 C ATOM 640 O HIS A 166 14.048 24.130 15.699 1.00 49.05 O ANISOU 640 O HIS A 166 8378 4991 5269 -1294 -1591 -1364 O ATOM 641 CB HIS A 166 10.752 23.962 16.570 1.00 62.23 C ANISOU 641 CB HIS A 166 10087 6368 7191 -1378 -1382 -1518 C ATOM 642 CG HIS A 166 11.329 23.434 17.852 1.00 53.97 C ANISOU 642 CG HIS A 166 9369 5295 5841 -1546 -1487 -1379 C ATOM 643 ND1 HIS A 166 10.740 22.410 18.553 1.00 73.05 N ANISOU 643 ND1 HIS A 166 12036 7481 8240 -1693 -1487 -1317 N ATOM 644 CD2 HIS A 166 12.429 23.796 18.539 1.00 56.07 C ANISOU 644 CD2 HIS A 166 9762 5741 5802 -1609 -1591 -1290 C ATOM 645 CE1 HIS A 166 11.467 22.156 19.636 1.00 71.85 C ANISOU 645 CE1 HIS A 166 12217 7372 7710 -1862 -1613 -1170 C ATOM 646 NE2 HIS A 166 12.485 22.984 19.655 1.00 61.18 N ANISOU 646 NE2 HIS A 166 10762 6297 6185 -1794 -1691 -1160 N ATOM 647 N ALA A 167 12.788 25.992 15.652 1.00 54.92 N ANISOU 647 N ALA A 167 8934 5846 6086 -1257 -1386 -1522 N ATOM 648 CA ALA A 167 13.924 26.899 15.693 1.00 61.40 C ANISOU 648 CA ALA A 167 9746 6821 6762 -1270 -1407 -1513 C ATOM 649 C ALA A 167 13.518 28.225 16.319 1.00 58.55 C ANISOU 649 C ALA A 167 9401 6520 6324 -1313 -1356 -1582 C ATOM 650 O ALA A 167 12.327 28.440 16.544 1.00 64.03 O ANISOU 650 O ALA A 167 10084 7138 7107 -1316 -1301 -1653 O ATOM 651 CB ALA A 167 14.465 27.112 14.295 1.00 63.36 C ANISOU 651 CB ALA A 167 9978 7025 7072 -1219 -1418 -1498 C ATOM 652 N TYR A 168 14.492 29.113 16.578 1.00 51.19 N ANISOU 652 N TYR A 168 8472 5715 5264 -1348 -1369 -1598 N ATOM 653 CA TYR A 168 14.258 30.365 17.326 1.00 58.47 C ANISOU 653 CA TYR A 168 9400 6705 6110 -1399 -1326 -1687 C ATOM 654 C TYR A 168 14.663 31.627 16.561 1.00 65.25 C ANISOU 654 C TYR A 168 10260 7536 6995 -1402 -1306 -1721 C ATOM 655 O TYR A 168 15.665 31.623 15.853 1.00 70.05 O ANISOU 655 O TYR A 168 10867 8160 7589 -1399 -1328 -1685 O ATOM 656 CB TYR A 168 15.018 30.336 18.669 1.00 54.86 C ANISOU 656 CB TYR A 168 8954 6444 5444 -1459 -1366 -1707 C ATOM 657 CG TYR A 168 14.493 29.290 19.630 1.00 53.41 C ANISOU 657 CG TYR A 168 8873 6272 5147 -1509 -1390 -1656 C ATOM 658 CD1 TYR A 168 14.662 27.944 19.369 1.00 52.33 C ANISOU 658 CD1 TYR A 168 8857 6033 4992 -1528 -1479 -1523 C ATOM 659 CD2 TYR A 168 13.828 29.647 20.800 1.00 57.45 C ANISOU 659 CD2 TYR A 168 9497 6831 5499 -1613 -1341 -1711 C ATOM 660 CE1 TYR A 168 14.176 26.972 20.227 1.00 62.18 C ANISOU 660 CE1 TYR A 168 10362 7202 6061 -1655 -1532 -1422 C ATOM 661 CE2 TYR A 168 13.341 28.674 21.665 1.00 57.62 C ANISOU 661 CE2 TYR A 168 9776 6807 5309 -1763 -1353 -1619 C ATOM 662 CZ TYR A 168 13.521 27.337 21.369 1.00 58.38 C ANISOU 662 CZ TYR A 168 10021 6780 5381 -1788 -1456 -1463 C ATOM 663 OH TYR A 168 13.048 26.353 22.209 1.00 80.18 O ANISOU 663 OH TYR A 168 13098 9459 7907 -1963 -1476 -1353 O ATOM 664 N ALA A 169 13.899 32.707 16.731 1.00 56.97 N ANISOU 664 N ALA A 169 9214 6439 5991 -1417 -1263 -1811 N ATOM 665 CA ALA A 169 14.170 33.962 16.039 1.00 63.76 C ANISOU 665 CA ALA A 169 10106 7242 6878 -1430 -1251 -1843 C ATOM 666 C ALA A 169 15.498 34.584 16.522 1.00 66.98 C ANISOU 666 C ALA A 169 10501 7787 7162 -1499 -1252 -1886 C ATOM 667 O ALA A 169 15.988 34.233 17.592 1.00 66.78 O ANISOU 667 O ALA A 169 10434 7916 7024 -1528 -1275 -1919 O ATOM 668 CB ALA A 169 12.993 34.935 16.234 1.00 56.54 C ANISOU 668 CB ALA A 169 9177 6236 6068 -1425 -1224 -1965 C ATOM 669 N PRO A 170 16.103 35.488 15.721 1.00 66.14 N ANISOU 669 N PRO A 170 10439 7624 7068 -1530 -1235 -1895 N ATOM 670 CA PRO A 170 17.416 36.039 16.083 1.00 73.28 C ANISOU 670 CA PRO A 170 11308 8647 7890 -1600 -1233 -1968 C ATOM 671 C PRO A 170 17.455 36.665 17.470 1.00 73.88 C ANISOU 671 C PRO A 170 11331 8849 7892 -1643 -1239 -2099 C ATOM 672 O PRO A 170 16.429 37.115 17.985 1.00 85.24 O ANISOU 672 O PRO A 170 12778 10245 9364 -1639 -1217 -2158 O ATOM 673 CB PRO A 170 17.654 37.108 15.014 1.00 71.14 C ANISOU 673 CB PRO A 170 11130 8239 7659 -1645 -1190 -1970 C ATOM 674 CG PRO A 170 16.885 36.657 13.856 1.00 63.53 C ANISOU 674 CG PRO A 170 10262 7122 6754 -1582 -1202 -1848 C ATOM 675 CD PRO A 170 15.678 35.947 14.385 1.00 64.76 C ANISOU 675 CD PRO A 170 10368 7271 6969 -1506 -1231 -1835 C ATOM 676 N GLY A 171 18.647 36.711 18.052 1.00 51.35 N ANISOU 676 N GLY A 171 8417 6148 4944 -1682 -1282 -2170 N ATOM 677 CA GLY A 171 18.827 37.143 19.414 1.00 50.42 C ANISOU 677 CA GLY A 171 8264 6180 4712 -1718 -1318 -2291 C ATOM 678 C GLY A 171 19.912 36.326 20.096 1.00 62.05 C ANISOU 678 C GLY A 171 9667 7854 6055 -1699 -1432 -2311 C ATOM 679 O GLY A 171 20.493 35.435 19.496 1.00 67.56 O ANISOU 679 O GLY A 171 10324 8562 6785 -1657 -1476 -2247 O ATOM 680 N PRO A 172 20.199 36.635 21.367 1.00 60.31 N ANISOU 680 N PRO A 172 9435 7799 5683 -1725 -1499 -2417 N ATOM 681 CA PRO A 172 21.247 35.917 22.094 1.00 64.53 C ANISOU 681 CA PRO A 172 9906 8541 6070 -1685 -1659 -2454 C ATOM 682 C PRO A 172 20.781 34.586 22.643 1.00 77.42 C ANISOU 682 C PRO A 172 11573 10274 7571 -1630 -1718 -2329 C ATOM 683 O PRO A 172 19.582 34.353 22.762 1.00 76.65 O ANISOU 683 O PRO A 172 11561 10095 7469 -1646 -1624 -2244 O ATOM 684 CB PRO A 172 21.599 36.870 23.237 1.00 65.79 C ANISOU 684 CB PRO A 172 10079 8829 6090 -1741 -1713 -2613 C ATOM 685 CG PRO A 172 20.384 37.721 23.416 1.00 72.14 C ANISOU 685 CG PRO A 172 10963 9520 6928 -1808 -1563 -2631 C ATOM 686 CD PRO A 172 19.769 37.859 22.061 1.00 70.91 C ANISOU 686 CD PRO A 172 10816 9134 6994 -1795 -1445 -2541 C ATOM 687 N GLY A 173 21.738 33.722 22.970 1.00 87.27 N ANISOU 687 N GLY A 173 12751 11689 8718 -1566 -1884 -2330 N ATOM 688 CA GLY A 173 21.448 32.471 23.648 1.00 66.92 C ANISOU 688 CA GLY A 173 10225 9239 5964 -1522 -1970 -2199 C ATOM 689 C GLY A 173 20.773 31.446 22.773 1.00 71.90 C ANISOU 689 C GLY A 173 10894 9699 6726 -1510 -1898 -2029 C ATOM 690 O GLY A 173 21.277 31.102 21.702 1.00 71.92 O ANISOU 690 O GLY A 173 10806 9609 6911 -1478 -1897 -2024 O ATOM 691 N ILE A 174 19.624 30.956 23.229 1.00 70.35 N ANISOU 691 N ILE A 174 10884 9431 6415 -1582 -1841 -1893 N ATOM 692 CA ILE A 174 18.901 29.941 22.481 1.00 78.35 C ANISOU 692 CA ILE A 174 11996 10235 7539 -1598 -1802 -1732 C ATOM 693 C ILE A 174 18.216 30.572 21.273 1.00 73.82 C ANISOU 693 C ILE A 174 11301 9466 7281 -1531 -1632 -1797 C ATOM 694 O ILE A 174 17.826 29.885 20.327 1.00 65.72 O ANISOU 694 O ILE A 174 10286 8270 6413 -1501 -1602 -1713 O ATOM 695 CB ILE A 174 17.867 29.204 23.357 1.00 69.38 C ANISOU 695 CB ILE A 174 11129 9053 6178 -1715 -1799 -1584 C ATOM 696 CG1 ILE A 174 17.392 27.920 22.653 1.00 75.00 C ANISOU 696 CG1 ILE A 174 11976 9532 6989 -1727 -1837 -1415 C ATOM 697 CG2 ILE A 174 16.713 30.122 23.691 1.00 63.57 C ANISOU 697 CG2 ILE A 174 10409 8270 5477 -1764 -1612 -1697 C ATOM 698 CD1 ILE A 174 16.349 27.117 23.416 1.00 62.70 C ANISOU 698 CD1 ILE A 174 10730 7874 5220 -1870 -1824 -1274 C ATOM 699 N ASN A 175 18.083 31.886 21.280 1.00 67.49 N ANISOU 699 N ASN A 175 10476 8649 6519 -1562 -1554 -1912 N ATOM 700 CA ASN A 175 17.615 32.534 20.073 1.00 66.24 C ANISOU 700 CA ASN A 175 10307 8288 6573 -1557 -1452 -1918 C ATOM 701 C ASN A 175 18.572 32.252 18.921 1.00 65.28 C ANISOU 701 C ASN A 175 10125 8121 6557 -1525 -1480 -1891 C ATOM 702 O ASN A 175 19.789 32.186 19.100 1.00 64.16 O ANISOU 702 O ASN A 175 9905 8115 6360 -1523 -1563 -1956 O ATOM 703 CB ASN A 175 17.477 34.016 20.292 1.00 69.77 C ANISOU 703 CB ASN A 175 10753 8725 7031 -1606 -1391 -2044 C ATOM 704 CG ASN A 175 16.079 34.414 20.677 1.00 66.08 C ANISOU 704 CG ASN A 175 10336 8169 6604 -1624 -1310 -2086 C ATOM 705 OD1 ASN A 175 15.648 34.192 21.804 1.00 68.67 O ANISOU 705 OD1 ASN A 175 10706 8595 6792 -1659 -1305 -2120 O ATOM 706 ND2 ASN A 175 15.373 35.044 19.752 1.00 70.95 N ANISOU 706 ND2 ASN A 175 10952 8605 7401 -1602 -1251 -2101 N ATOM 707 N GLY A 176 18.025 32.071 17.738 1.00 65.10 N ANISOU 707 N GLY A 176 10133 7917 6682 -1495 -1420 -1820 N ATOM 708 CA GLY A 176 18.854 31.719 16.610 1.00 72.35 C ANISOU 708 CA GLY A 176 11017 8792 7682 -1474 -1430 -1803 C ATOM 709 C GLY A 176 19.076 30.225 16.434 1.00 65.23 C ANISOU 709 C GLY A 176 10079 7895 6810 -1424 -1498 -1738 C ATOM 710 O GLY A 176 19.332 29.775 15.320 1.00 68.86 O ANISOU 710 O GLY A 176 10525 8265 7372 -1398 -1481 -1721 O ATOM 711 N ASP A 177 19.004 29.451 17.515 1.00 53.59 N ANISOU 711 N ASP A 177 8602 6526 5236 -1416 -1578 -1708 N ATOM 712 CA ASP A 177 19.257 28.015 17.410 1.00 61.99 C ANISOU 712 CA ASP A 177 9659 7571 6322 -1384 -1671 -1637 C ATOM 713 C ASP A 177 18.226 27.306 16.550 1.00 56.57 C ANISOU 713 C ASP A 177 9029 6674 5792 -1345 -1613 -1556 C ATOM 714 O ASP A 177 17.124 27.803 16.351 1.00 65.78 O ANISOU 714 O ASP A 177 10237 7742 7015 -1337 -1522 -1546 O ATOM 715 CB ASP A 177 19.250 27.341 18.770 1.00 50.84 C ANISOU 715 CB ASP A 177 8423 6222 4672 -1455 -1837 -1531 C ATOM 716 CG ASP A 177 20.344 27.832 19.694 1.00 69.91 C ANISOU 716 CG ASP A 177 10774 8886 6904 -1480 -1947 -1612 C ATOM 717 OD1 ASP A 177 21.073 28.798 19.375 1.00 64.64 O ANISOU 717 OD1 ASP A 177 9921 8325 6316 -1448 -1883 -1782 O ATOM 718 OD2 ASP A 177 20.445 27.230 20.780 1.00 70.52 O ANISOU 718 OD2 ASP A 177 11006 9048 6742 -1528 -2119 -1500 O ATOM 719 N ALA A 178 18.586 26.117 16.078 1.00 63.18 N ANISOU 719 N ALA A 178 9907 7411 6688 -1336 -1709 -1502 N ATOM 720 CA ALA A 178 17.625 25.219 15.467 1.00 42.17 C ANISOU 720 CA ALA A 178 7313 4543 4167 -1298 -1695 -1434 C ATOM 721 C ALA A 178 17.764 23.782 16.001 1.00 64.43 C ANISOU 721 C ALA A 178 10314 7216 6950 -1330 -1910 -1317 C ATOM 722 O ALA A 178 18.868 23.287 16.194 1.00 72.85 O ANISOU 722 O ALA A 178 11387 8322 7972 -1340 -2083 -1307 O ATOM 723 CB ALA A 178 17.775 25.255 13.953 1.00 41.22 C ANISOU 723 CB ALA A 178 7045 4387 4230 -1232 -1582 -1514 C ATOM 724 N HIS A 179 16.627 23.127 16.239 1.00 67.94 N ANISOU 724 N HIS A 179 10904 7472 7437 -1345 -1923 -1241 N ATOM 725 CA HIS A 179 16.573 21.776 16.796 1.00 61.03 C ANISOU 725 CA HIS A 179 10259 6384 6547 -1391 -2147 -1111 C ATOM 726 C HIS A 179 15.931 20.747 15.863 1.00 65.04 C ANISOU 726 C HIS A 179 10722 6626 7363 -1322 -2120 -1131 C ATOM 727 O HIS A 179 14.917 21.022 15.221 1.00 62.44 O ANISOU 727 O HIS A 179 10267 6273 7186 -1274 -1920 -1212 O ATOM 728 CB HIS A 179 15.779 21.768 18.099 1.00 68.81 C ANISOU 728 CB HIS A 179 11515 7335 7295 -1529 -2178 -1012 C ATOM 729 CG HIS A 179 16.332 22.662 19.164 1.00 58.85 C ANISOU 729 CG HIS A 179 10296 6357 5706 -1600 -2199 -991 C ATOM 730 ND1 HIS A 179 15.767 22.747 20.417 1.00 50.47 N ANISOU 730 ND1 HIS A 179 9488 5347 4340 -1747 -2199 -910 N ATOM 731 CD2 HIS A 179 17.397 23.499 19.165 1.00 59.66 C ANISOU 731 CD2 HIS A 179 10205 6715 5747 -1551 -2195 -1067 C ATOM 732 CE1 HIS A 179 16.459 23.607 21.148 1.00 65.01 C ANISOU 732 CE1 HIS A 179 11260 7486 5956 -1758 -2201 -931 C ATOM 733 NE2 HIS A 179 17.452 24.074 20.413 1.00 54.62 N ANISOU 733 NE2 HIS A 179 9666 6281 4806 -1638 -2208 -1035 N ATOM 734 N PHE A 180 16.485 19.541 15.840 1.00 68.07 N ANISOU 734 N PHE A 180 11187 6804 7872 -1306 -2343 -1066 N ATOM 735 CA PHE A 180 15.923 18.466 15.031 1.00 57.14 C ANISOU 735 CA PHE A 180 9722 5146 6842 -1231 -2299 -1095 C ATOM 736 C PHE A 180 15.637 17.188 15.794 1.00 57.38 C ANISOU 736 C PHE A 180 9989 4787 7024 -1289 -2494 -931 C ATOM 737 O PHE A 180 16.465 16.695 16.556 1.00 76.11 O ANISOU 737 O PHE A 180 12375 7218 9327 -1229 -2636 -696 O ATOM 738 CB PHE A 180 16.851 18.156 13.868 1.00 77.04 C ANISOU 738 CB PHE A 180 12015 7706 9550 -1129 -2294 -1214 C ATOM 739 CG PHE A 180 17.099 19.332 13.000 1.00 71.09 C ANISOU 739 CG PHE A 180 11074 7251 8685 -1113 -2061 -1348 C ATOM 740 CD1 PHE A 180 18.123 20.200 13.284 1.00 60.27 C ANISOU 740 CD1 PHE A 180 9677 6105 7119 -1154 -2085 -1376 C ATOM 741 CD2 PHE A 180 16.281 19.588 11.922 1.00 71.10 C ANISOU 741 CD2 PHE A 180 10930 7294 8791 -1068 -1831 -1442 C ATOM 742 CE1 PHE A 180 18.337 21.287 12.496 1.00 64.74 C ANISOU 742 CE1 PHE A 180 10086 6881 7630 -1157 -1865 -1489 C ATOM 743 CE2 PHE A 180 16.486 20.681 11.136 1.00 58.98 C ANISOU 743 CE2 PHE A 180 9273 5975 7161 -1069 -1661 -1531 C ATOM 744 CZ PHE A 180 17.510 21.527 11.416 1.00 56.56 C ANISOU 744 CZ PHE A 180 8952 5844 6693 -1114 -1670 -1551 C ATOM 745 N ASP A 181 14.445 16.660 15.556 1.00 53.28 N ANISOU 745 N ASP A 181 9425 4062 6757 -1276 -2296 -936 N ATOM 746 CA ASP A 181 13.955 15.474 16.211 1.00 55.23 C ANISOU 746 CA ASP A 181 9743 4017 7225 -1267 -2240 -692 C ATOM 747 C ASP A 181 14.599 14.234 15.594 1.00 77.70 C ANISOU 747 C ASP A 181 12407 6648 10468 -1109 -2326 -635 C ATOM 748 O ASP A 181 14.343 13.887 14.440 1.00 82.86 O ANISOU 748 O ASP A 181 12878 7177 11429 -1053 -2265 -869 O ATOM 749 CB ASP A 181 12.434 15.436 16.095 1.00 51.16 C ANISOU 749 CB ASP A 181 9239 3303 6896 -1352 -2005 -813 C ATOM 750 CG ASP A 181 11.804 14.357 16.937 1.00 70.25 C ANISOU 750 CG ASP A 181 11709 5487 9495 -1368 -1818 -527 C ATOM 751 OD1 ASP A 181 12.507 13.749 17.773 1.00 74.76 O ANISOU 751 OD1 ASP A 181 12366 6083 9956 -1313 -1880 -176 O ATOM 752 OD2 ASP A 181 10.588 14.126 16.760 1.00 66.46 O ANISOU 752 OD2 ASP A 181 11184 4790 9277 -1436 -1607 -657 O ATOM 753 N ASP A 182 15.447 13.573 16.369 1.00 68.76 N ANISOU 753 N ASP A 182 9111 6748 10265 -580 228 -572 N ATOM 754 CA ASP A 182 16.211 12.449 15.860 1.00 72.34 C ANISOU 754 CA ASP A 182 9424 7051 11011 -621 306 -497 C ATOM 755 C ASP A 182 15.381 11.202 15.851 1.00 65.53 C ANISOU 755 C ASP A 182 8338 6055 10504 -613 416 -477 C ATOM 756 O ASP A 182 15.831 10.142 15.431 1.00 84.16 O ANISOU 756 O ASP A 182 10567 8247 13163 -636 498 -440 O ATOM 757 CB ASP A 182 17.459 12.227 16.688 1.00 73.10 C ANISOU 757 CB ASP A 182 9468 7214 11091 -671 332 -204 C ATOM 758 CG ASP A 182 18.623 11.837 15.849 1.00 78.52 C ANISOU 758 CG ASP A 182 10138 7775 11922 -696 360 -181 C ATOM 759 OD1 ASP A 182 18.593 10.724 15.286 1.00 98.27 O ANISOU 759 OD1 ASP A 182 12498 10097 14741 -682 477 -206 O ATOM 760 OD2 ASP A 182 19.563 12.650 15.747 1.00 88.48 O ANISOU 760 OD2 ASP A 182 11524 9102 12991 -724 270 -136 O ATOM 761 N ASP A 183 14.155 11.328 16.331 1.00 70.29 N ANISOU 761 N ASP A 183 8888 6721 11100 -575 425 -490 N ATOM 762 CA ASP A 183 13.208 10.242 16.199 1.00 55.23 C ANISOU 762 CA ASP A 183 6756 4667 9563 -577 499 -487 C ATOM 763 C ASP A 183 12.588 10.290 14.789 1.00 74.71 C ANISOU 763 C ASP A 183 9288 6986 12113 -583 399 -820 C ATOM 764 O ASP A 183 11.657 9.540 14.485 1.00 75.82 O ANISOU 764 O ASP A 183 9269 6988 12552 -600 401 -883 O ATOM 765 CB ASP A 183 12.146 10.305 17.302 1.00 64.10 C ANISOU 765 CB ASP A 183 7759 5922 10673 -524 566 -314 C ATOM 766 CG ASP A 183 12.573 9.552 18.561 1.00 78.16 C ANISOU 766 CG ASP A 183 9357 7780 12560 -526 701 52 C ATOM 767 OD1 ASP A 183 13.742 9.117 18.597 1.00 75.99 O ANISOU 767 OD1 ASP A 183 9065 7465 12344 -576 722 170 O ATOM 768 OD2 ASP A 183 11.756 9.387 19.502 1.00 79.76 O ANISOU 768 OD2 ASP A 183 9421 8091 12792 -469 796 248 O ATOM 769 N GLU A 184 13.112 11.167 13.928 1.00 66.42 N ANISOU 769 N GLU A 184 8464 5968 10804 -575 299 -1019 N ATOM 770 CA GLU A 184 12.850 11.046 12.501 1.00 64.85 C ANISOU 770 CA GLU A 184 8336 5635 10668 -581 213 -1313 C ATOM 771 C GLU A 184 14.019 10.317 11.842 1.00 76.99 C ANISOU 771 C GLU A 184 9892 7031 12329 -596 276 -1342 C ATOM 772 O GLU A 184 15.035 10.047 12.481 1.00 84.59 O ANISOU 772 O GLU A 184 10807 8009 13323 -605 374 -1116 O ATOM 773 CB GLU A 184 12.632 12.399 11.836 1.00 52.65 C ANISOU 773 CB GLU A 184 7008 4213 8784 -542 81 -1498 C ATOM 774 CG GLU A 184 11.884 13.421 12.668 1.00 72.20 C ANISOU 774 CG GLU A 184 9522 6856 11056 -500 53 -1425 C ATOM 775 CD GLU A 184 10.475 13.000 13.058 1.00 75.77 C ANISOU 775 CD GLU A 184 9791 7287 11713 -487 73 -1393 C ATOM 776 OE1 GLU A 184 9.944 12.002 12.515 1.00 78.31 O ANISOU 776 OE1 GLU A 184 9960 7450 12344 -531 58 -1469 O ATOM 777 OE2 GLU A 184 9.893 13.698 13.915 1.00 61.33 O ANISOU 777 OE2 GLU A 184 7970 5593 9739 -428 104 -1290 O ATOM 778 N GLN A 185 13.860 9.977 10.569 1.00 67.90 N ANISOU 778 N GLN A 185 8807 5744 11247 -590 223 -1613 N ATOM 779 CA GLN A 185 14.916 9.302 9.836 1.00 60.52 C ANISOU 779 CA GLN A 185 7916 4667 10413 -572 310 -1673 C ATOM 780 C GLN A 185 15.394 10.265 8.780 1.00 62.54 C ANISOU 780 C GLN A 185 8407 5021 10335 -516 238 -1847 C ATOM 781 O GLN A 185 14.818 10.367 7.699 1.00 77.67 O ANISOU 781 O GLN A 185 10429 6909 12175 -497 137 -2124 O ATOM 782 CB GLN A 185 14.414 7.992 9.223 1.00 78.09 C ANISOU 782 CB GLN A 185 10039 6633 13000 -596 327 -1856 C ATOM 783 CG GLN A 185 15.503 7.124 8.600 1.00 81.84 C ANISOU 783 CG GLN A 185 10543 6922 13629 -555 464 -1906 C ATOM 784 CD GLN A 185 16.478 6.606 9.622 1.00 85.72 C ANISOU 784 CD GLN A 185 10875 7387 14308 -557 641 -1552 C ATOM 785 OE1 GLN A 185 16.120 6.390 10.780 1.00101.19 O ANISOU 785 OE1 GLN A 185 12648 9388 16412 -606 666 -1302 O ATOM 786 NE2 GLN A 185 17.724 6.414 9.208 1.00 87.25 N ANISOU 786 NE2 GLN A 185 11130 7528 14493 -495 771 -1503 N ATOM 787 N TRP A 186 16.432 11.009 9.125 1.00 64.11 N ANISOU 787 N TRP A 186 8678 5348 10333 -496 275 -1662 N ATOM 788 CA TRP A 186 16.952 12.051 8.256 1.00 73.44 C ANISOU 788 CA TRP A 186 10056 6639 11209 -443 214 -1753 C ATOM 789 C TRP A 186 17.722 11.475 7.073 1.00 83.45 C ANISOU 789 C TRP A 186 11399 7796 12512 -372 310 -1881 C ATOM 790 O TRP A 186 18.555 10.591 7.232 1.00 81.08 O ANISOU 790 O TRP A 186 11011 7371 12423 -357 465 -1760 O ATOM 791 CB TRP A 186 17.832 12.997 9.060 1.00 59.55 C ANISOU 791 CB TRP A 186 8328 5024 9273 -461 206 -1493 C ATOM 792 CG TRP A 186 17.068 13.636 10.152 1.00 65.20 C ANISOU 792 CG TRP A 186 9021 5854 9897 -505 119 -1413 C ATOM 793 CD1 TRP A 186 17.135 13.351 11.487 1.00 69.14 C ANISOU 793 CD1 TRP A 186 9401 6390 10480 -551 162 -1185 C ATOM 794 CD2 TRP A 186 16.075 14.649 10.006 1.00 66.34 C ANISOU 794 CD2 TRP A 186 9266 6097 9843 -487 -9 -1556 C ATOM 795 NE1 TRP A 186 16.251 14.145 12.184 1.00 66.40 N ANISOU 795 NE1 TRP A 186 9096 6163 9972 -552 80 -1196 N ATOM 796 CE2 TRP A 186 15.588 14.949 11.292 1.00 74.34 C ANISOU 796 CE2 TRP A 186 10229 7193 10822 -512 -20 -1420 C ATOM 797 CE3 TRP A 186 15.549 15.338 8.911 1.00 71.04 C ANISOU 797 CE3 TRP A 186 9985 6726 10281 -443 -109 -1770 C ATOM 798 CZ2 TRP A 186 14.601 15.908 11.508 1.00 79.06 C ANISOU 798 CZ2 TRP A 186 10900 7884 11256 -483 -107 -1503 C ATOM 799 CZ3 TRP A 186 14.580 16.289 9.132 1.00 73.28 C ANISOU 799 CZ3 TRP A 186 10319 7102 10422 -429 -212 -1828 C ATOM 800 CH2 TRP A 186 14.112 16.564 10.416 1.00 60.68 C ANISOU 800 CH2 TRP A 186 8674 5565 8816 -444 -201 -1701 C ATOM 801 N THR A 187 17.438 11.982 5.882 1.00 80.52 N ANISOU 801 N THR A 187 11191 7478 11926 -313 229 -2118 N ATOM 802 CA THR A 187 18.034 11.431 4.680 1.00 71.20 C ANISOU 802 CA THR A 187 10113 6209 10729 -220 327 -2281 C ATOM 803 C THR A 187 18.726 12.513 3.848 1.00 66.38 C ANISOU 803 C THR A 187 9664 5763 9793 -130 321 -2257 C ATOM 804 O THR A 187 18.377 13.696 3.923 1.00 67.71 O ANISOU 804 O THR A 187 9888 6093 9746 -150 185 -2217 O ATOM 805 CB THR A 187 16.966 10.709 3.828 1.00 79.28 C ANISOU 805 CB THR A 187 11186 7118 11820 -222 236 -2636 C ATOM 806 OG1 THR A 187 15.995 11.655 3.374 1.00 86.93 O ANISOU 806 OG1 THR A 187 12243 8242 12543 -236 36 -2778 O ATOM 807 CG2 THR A 187 16.248 9.660 4.657 1.00 75.63 C ANISOU 807 CG2 THR A 187 10530 6476 11729 -318 235 -2626 C ATOM 808 N LYS A 188 19.726 12.095 3.080 1.00 79.43 N ANISOU 808 N LYS A 188 11380 7365 11434 -21 487 -2258 N ATOM 809 CA LYS A 188 20.381 12.955 2.095 1.00 76.35 C ANISOU 809 CA LYS A 188 11135 7122 10753 93 515 -2236 C ATOM 810 C LYS A 188 19.477 13.159 0.880 1.00 73.96 C ANISOU 810 C LYS A 188 11001 6895 10205 150 390 -2569 C ATOM 811 O LYS A 188 19.452 14.230 0.292 1.00 84.36 O ANISOU 811 O LYS A 188 12414 8392 11245 198 310 -2547 O ATOM 812 CB LYS A 188 21.717 12.348 1.658 1.00 93.18 C ANISOU 812 CB LYS A 188 13266 9174 12964 217 769 -2112 C ATOM 813 CG LYS A 188 22.230 12.855 0.311 1.00 99.91 C ANISOU 813 CG LYS A 188 14287 10153 13521 383 846 -2174 C ATOM 814 CD LYS A 188 23.412 12.036 -0.198 1.00 87.97 C ANISOU 814 CD LYS A 188 12780 8534 12110 540 1139 -2097 C ATOM 815 CE LYS A 188 23.710 12.337 -1.668 1.00 89.57 C ANISOU 815 CE LYS A 188 13182 8865 11986 738 1237 -2232 C ATOM 816 NZ LYS A 188 22.680 11.778 -2.604 1.00 78.11 N ANISOU 816 NZ LYS A 188 11922 7384 10371 781 1145 -2697 N ATOM 817 N ASP A 189 18.744 12.112 0.509 1.00 72.59 N ANISOU 817 N ASP A 189 10854 6578 10151 138 363 -2864 N ATOM 818 CA ASP A 189 17.768 12.172 -0.578 1.00 82.92 C ANISOU 818 CA ASP A 189 12311 7946 11248 162 197 -3201 C ATOM 819 C ASP A 189 16.345 12.351 -0.038 1.00 95.17 C ANISOU 819 C ASP A 189 13770 9502 12890 17 -41 -3286 C ATOM 820 O ASP A 189 16.154 12.580 1.157 1.00103.05 O ANISOU 820 O ASP A 189 14610 10485 14058 -77 -56 -3076 O ATOM 821 CB ASP A 189 17.846 10.899 -1.411 1.00 97.17 C ANISOU 821 CB ASP A 189 14221 9571 13126 236 286 -3505 C ATOM 822 CG ASP A 189 17.801 9.650 -0.553 1.00104.74 C ANISOU 822 CG ASP A 189 15020 10252 14524 152 370 -3500 C ATOM 823 OD1 ASP A 189 18.176 9.733 0.636 1.00111.10 O ANISOU 823 OD1 ASP A 189 15642 11033 15539 83 443 -3189 O ATOM 824 OD2 ASP A 189 17.398 8.587 -1.060 1.00114.99 O ANISOU 824 OD2 ASP A 189 16376 11354 15962 153 354 -3803 O ATOM 825 N THR A 190 15.347 12.256 -0.912 1.00 95.79 N ANISOU 825 N THR A 190 13941 9609 12847 6 -225 -3579 N ATOM 826 CA THR A 190 13.964 12.246 -0.447 1.00100.34 C ANISOU 826 CA THR A 190 14396 10157 13571 -128 -439 -3651 C ATOM 827 C THR A 190 13.498 10.817 -0.527 1.00 85.53 C ANISOU 827 C THR A 190 12472 8032 11994 -193 -464 -3880 C ATOM 828 O THR A 190 13.021 10.362 -1.561 1.00103.23 O ANISOU 828 O THR A 190 14835 10289 14097 -191 -570 -4085 O ATOM 829 CB THR A 190 13.028 13.177 -1.263 1.00125.92 C ANISOU 829 CB THR A 190 17721 13599 16524 -125 -673 -3770 C ATOM 830 OG1 THR A 190 13.280 14.547 -0.913 1.00118.73 O ANISOU 830 OG1 THR A 190 16801 12880 15431 -92 -662 -3512 O ATOM 831 CG2 THR A 190 11.569 12.877 -0.951 1.00128.22 C ANISOU 831 CG2 THR A 190 17872 13821 17025 -259 -889 -3872 C ATOM 832 N THR A 191 13.731 10.100 0.563 1.00 82.16 N ANISOU 832 N THR A 191 11869 7423 11926 -254 -336 -3723 N ATOM 833 CA THR A 191 13.271 8.729 0.757 1.00100.65 C ANISOU 833 CA THR A 191 14101 9544 14600 -331 -338 -3784 C ATOM 834 C THR A 191 13.039 8.600 2.234 1.00107.15 C ANISOU 834 C THR A 191 14667 10271 15773 -424 -285 -3544 C ATOM 835 O THR A 191 13.346 7.581 2.853 1.00116.25 O ANISOU 835 O THR A 191 15681 11222 17267 -453 -152 -3450 O ATOM 836 CB THR A 191 14.284 7.665 0.328 1.00 94.00 C ANISOU 836 CB THR A 191 13343 8518 13853 -243 -138 -3864 C ATOM 837 OG1 THR A 191 15.558 7.991 0.895 1.00 91.67 O ANISOU 837 OG1 THR A 191 13019 8205 13609 -166 102 -3677 O ATOM 838 CG2 THR A 191 14.377 7.557 -1.205 1.00 89.33 C ANISOU 838 CG2 THR A 191 13028 7993 12919 -144 -188 -4145 C ATOM 839 N GLY A 192 12.524 9.677 2.794 1.00 97.54 N ANISOU 839 N GLY A 192 13394 9237 14430 -454 -374 -3393 N ATOM 840 CA GLY A 192 12.454 9.833 4.222 1.00 86.92 C ANISOU 840 CA GLY A 192 11856 7915 13254 -502 -294 -3077 C ATOM 841 C GLY A 192 12.367 11.318 4.462 1.00 70.76 C ANISOU 841 C GLY A 192 9877 6123 10885 -469 -352 -2941 C ATOM 842 O GLY A 192 11.804 12.063 3.655 1.00 71.73 O ANISOU 842 O GLY A 192 10108 6369 10776 -449 -505 -3087 O ATOM 843 N THR A 193 12.938 11.761 5.562 1.00 69.34 N ANISOU 843 N THR A 193 9638 6019 10690 -465 -238 -2660 N ATOM 844 CA THR A 193 12.842 13.161 5.904 1.00 72.30 C ANISOU 844 CA THR A 193 10081 6597 10794 -439 -295 -2541 C ATOM 845 C THR A 193 14.163 13.847 5.570 1.00 78.68 C ANISOU 845 C THR A 193 11038 7495 11364 -375 -224 -2455 C ATOM 846 O THR A 193 15.188 13.582 6.190 1.00 75.64 O ANISOU 846 O THR A 193 10613 7076 11050 -377 -92 -2265 O ATOM 847 CB THR A 193 12.470 13.331 7.380 1.00 64.38 C ANISOU 847 CB THR A 193 8935 5632 9894 -476 -249 -2305 C ATOM 848 OG1 THR A 193 11.491 12.345 7.731 1.00 66.86 O ANISOU 848 OG1 THR A 193 9061 5821 10523 -531 -258 -2324 O ATOM 849 CG2 THR A 193 11.891 14.721 7.633 1.00 56.08 C ANISOU 849 CG2 THR A 193 7954 4750 8603 -445 -341 -2266 C ATOM 850 N ASN A 194 14.135 14.718 4.568 1.00 78.72 N ANISOU 850 N ASN A 194 11192 7616 11104 -318 -315 -2569 N ATOM 851 CA ASN A 194 15.360 15.321 4.067 1.00 66.07 C ANISOU 851 CA ASN A 194 9712 6090 9301 -248 -245 -2480 C ATOM 852 C ASN A 194 15.876 16.409 4.979 1.00 66.99 C ANISOU 852 C ASN A 194 9830 6303 9321 -265 -245 -2232 C ATOM 853 O ASN A 194 15.229 17.435 5.166 1.00 80.28 O ANISOU 853 O ASN A 194 11547 8080 10876 -269 -357 -2226 O ATOM 854 CB ASN A 194 15.148 15.892 2.665 1.00 60.10 C ANISOU 854 CB ASN A 194 9105 5442 8289 -171 -337 -2655 C ATOM 855 CG ASN A 194 16.392 16.567 2.117 1.00 68.12 C ANISOU 855 CG ASN A 194 10225 6549 9110 -84 -250 -2520 C ATOM 856 OD1 ASN A 194 16.672 17.730 2.419 1.00 81.27 O ANISOU 856 OD1 ASN A 194 11909 8315 10655 -83 -291 -2346 O ATOM 857 ND2 ASN A 194 17.153 15.834 1.313 1.00 71.47 N ANISOU 857 ND2 ASN A 194 10711 6925 9520 -4 -121 -2591 N ATOM 858 N LEU A 195 17.063 16.189 5.522 1.00 72.24 N ANISOU 858 N LEU A 195 10460 6932 10057 -275 -127 -2029 N ATOM 859 CA LEU A 195 17.677 17.154 6.412 1.00 61.23 C ANISOU 859 CA LEU A 195 9073 5611 8581 -312 -155 -1798 C ATOM 860 C LEU A 195 17.786 18.510 5.745 1.00 70.64 C ANISOU 860 C LEU A 195 10390 6912 9540 -268 -253 -1798 C ATOM 861 O LEU A 195 17.325 19.500 6.310 1.00 77.25 O ANISOU 861 O LEU A 195 11262 7803 10286 -294 -358 -1766 O ATOM 862 CB LEU A 195 19.045 16.670 6.855 1.00 57.33 C ANISOU 862 CB LEU A 195 8511 5065 8205 -331 -31 -1567 C ATOM 863 CG LEU A 195 19.575 17.323 8.128 1.00 61.23 C ANISOU 863 CG LEU A 195 8977 5610 8678 -411 -86 -1325 C ATOM 864 CD1 LEU A 195 18.450 17.641 9.107 1.00 49.30 C ANISOU 864 CD1 LEU A 195 7463 4140 7128 -455 -175 -1382 C ATOM 865 CD2 LEU A 195 20.588 16.392 8.770 1.00 60.92 C ANISOU 865 CD2 LEU A 195 8805 5504 8837 -450 34 -1100 C ATOM 866 N PHE A 196 18.346 18.560 4.535 1.00 72.64 N ANISOU 866 N PHE A 196 10711 7193 9696 -186 -208 -1834 N ATOM 867 CA PHE A 196 18.540 19.849 3.855 1.00 64.61 C ANISOU 867 CA PHE A 196 9788 6284 8477 -136 -287 -1782 C ATOM 868 C PHE A 196 17.262 20.671 3.800 1.00 56.36 C ANISOU 868 C PHE A 196 8785 5302 7326 -139 -438 -1912 C ATOM 869 O PHE A 196 17.239 21.829 4.196 1.00 68.85 O ANISOU 869 O PHE A 196 10399 6918 8842 -156 -525 -1812 O ATOM 870 CB PHE A 196 19.062 19.666 2.427 1.00 69.95 C ANISOU 870 CB PHE A 196 10532 7013 9034 -19 -203 -1830 C ATOM 871 CG PHE A 196 18.995 20.932 1.603 1.00 63.14 C ANISOU 871 CG PHE A 196 9748 6280 7962 46 -290 -1786 C ATOM 872 CD1 PHE A 196 19.795 22.026 1.920 1.00 67.48 C ANISOU 872 CD1 PHE A 196 10286 6850 8504 27 -320 -1531 C ATOM 873 CD2 PHE A 196 18.119 21.036 0.537 1.00 69.08 C ANISOU 873 CD2 PHE A 196 10575 7128 8544 117 -361 -1984 C ATOM 874 CE1 PHE A 196 19.733 23.208 1.177 1.00 54.01 C ANISOU 874 CE1 PHE A 196 8630 5245 6648 86 -395 -1460 C ATOM 875 CE2 PHE A 196 18.046 22.203 -0.214 1.00 76.29 C ANISOU 875 CE2 PHE A 196 11541 8172 9275 182 -436 -1907 C ATOM 876 CZ PHE A 196 18.855 23.294 0.109 1.00 75.44 C ANISOU 876 CZ PHE A 196 11408 8069 9186 171 -443 -1638 C ATOM 877 N LEU A 197 16.194 20.054 3.318 1.00 64.02 N ANISOU 877 N LEU A 197 9747 6273 8307 -124 -476 -2132 N ATOM 878 CA LEU A 197 14.920 20.744 3.188 1.00 65.48 C ANISOU 878 CA LEU A 197 9941 6519 8420 -120 -614 -2236 C ATOM 879 C LEU A 197 14.377 21.241 4.529 1.00 64.82 C ANISOU 879 C LEU A 197 9809 6404 8418 -176 -648 -2157 C ATOM 880 O LEU A 197 13.890 22.366 4.631 1.00 67.05 O ANISOU 880 O LEU A 197 10129 6733 8615 -154 -730 -2129 O ATOM 881 CB LEU A 197 13.901 19.820 2.535 1.00 54.74 C ANISOU 881 CB LEU A 197 8550 5144 7105 -120 -666 -2468 C ATOM 882 CG LEU A 197 14.150 19.500 1.067 1.00 61.06 C ANISOU 882 CG LEU A 197 9444 6008 7748 -46 -673 -2609 C ATOM 883 CD1 LEU A 197 13.107 18.515 0.601 1.00 62.85 C ANISOU 883 CD1 LEU A 197 9640 6186 8052 -79 -764 -2860 C ATOM 884 CD2 LEU A 197 14.103 20.797 0.259 1.00 58.95 C ANISOU 884 CD2 LEU A 197 9255 5900 7243 28 -759 -2543 C ATOM 885 N VAL A 198 14.433 20.391 5.549 1.00 64.01 N ANISOU 885 N VAL A 198 9623 6221 8476 -235 -573 -2119 N ATOM 886 CA VAL A 198 13.905 20.768 6.853 1.00 59.39 C ANISOU 886 CA VAL A 198 9005 5628 7934 -267 -581 -2047 C ATOM 887 C VAL A 198 14.798 21.848 7.434 1.00 55.90 C ANISOU 887 C VAL A 198 8655 5203 7381 -280 -605 -1894 C ATOM 888 O VAL A 198 14.329 22.877 7.919 1.00 70.31 O ANISOU 888 O VAL A 198 10540 7046 9127 -262 -667 -1886 O ATOM 889 CB VAL A 198 13.814 19.553 7.804 1.00 60.45 C ANISOU 889 CB VAL A 198 9014 5693 8260 -319 -485 -2004 C ATOM 890 CG1 VAL A 198 13.463 19.999 9.207 1.00 70.49 C ANISOU 890 CG1 VAL A 198 10276 6991 9517 -332 -471 -1899 C ATOM 891 CG2 VAL A 198 12.781 18.554 7.294 1.00 49.01 C ANISOU 891 CG2 VAL A 198 7459 4195 6969 -323 -493 -2159 C ATOM 892 N ALA A 199 16.101 21.633 7.330 1.00 62.09 N ANISOU 892 N ALA A 199 9448 5967 8175 -308 -560 -1770 N ATOM 893 CA ALA A 199 17.079 22.542 7.913 1.00 51.20 C ANISOU 893 CA ALA A 199 8134 4584 6736 -350 -609 -1600 C ATOM 894 C ALA A 199 17.021 23.966 7.344 1.00 55.31 C ANISOU 894 C ALA A 199 8754 5129 7134 -311 -716 -1599 C ATOM 895 O ALA A 199 17.098 24.949 8.091 1.00 65.09 O ANISOU 895 O ALA A 199 10066 6340 8326 -341 -800 -1549 O ATOM 896 CB ALA A 199 18.472 21.959 7.737 1.00 55.52 C ANISOU 896 CB ALA A 199 8632 5105 7359 -381 -536 -1436 C ATOM 897 N ALA A 200 16.878 24.091 6.028 1.00 57.05 N ANISOU 897 N ALA A 200 8981 5396 7299 -240 -716 -1656 N ATOM 898 CA ALA A 200 16.815 25.421 5.407 1.00 58.37 C ANISOU 898 CA ALA A 200 9215 5590 7371 -193 -808 -1617 C ATOM 899 C ALA A 200 15.552 26.194 5.812 1.00 69.69 C ANISOU 899 C ALA A 200 10684 7017 8777 -166 -883 -1724 C ATOM 900 O ALA A 200 15.597 27.418 5.964 1.00 76.05 O ANISOU 900 O ALA A 200 11555 7785 9556 -157 -961 -1665 O ATOM 901 CB ALA A 200 16.889 25.304 3.904 1.00 51.39 C ANISOU 901 CB ALA A 200 8327 4794 6405 -109 -782 -1639 C ATOM 902 N HIS A 201 14.427 25.491 5.959 1.00 49.99 N ANISOU 902 N HIS A 201 8135 4544 6316 -148 -855 -1867 N ATOM 903 CA HIS A 201 13.237 26.110 6.544 1.00 63.27 C ANISOU 903 CA HIS A 201 9826 6212 8002 -112 -888 -1935 C ATOM 904 C HIS A 201 13.528 26.652 7.950 1.00 57.62 C ANISOU 904 C HIS A 201 9188 5425 7280 -146 -885 -1881 C ATOM 905 O HIS A 201 13.178 27.783 8.260 1.00 59.38 O ANISOU 905 O HIS A 201 9492 5605 7465 -106 -934 -1889 O ATOM 906 CB HIS A 201 12.057 25.122 6.606 1.00 57.25 C ANISOU 906 CB HIS A 201 8954 5475 7322 -99 -849 -2051 C ATOM 907 CG HIS A 201 10.922 25.592 7.476 1.00 60.31 C ANISOU 907 CG HIS A 201 9326 5846 7744 -53 -835 -2075 C ATOM 908 ND1 HIS A 201 9.796 26.206 6.970 1.00 63.16 N ANISOU 908 ND1 HIS A 201 9648 6236 8114 21 -883 -2114 N ATOM 909 CD2 HIS A 201 10.744 25.537 8.819 1.00 65.15 C ANISOU 909 CD2 HIS A 201 9953 6426 8376 -54 -762 -2048 C ATOM 910 CE1 HIS A 201 8.977 26.514 7.962 1.00 62.86 C ANISOU 910 CE1 HIS A 201 9597 6168 8118 72 -822 -2109 C ATOM 911 NE2 HIS A 201 9.532 26.124 9.095 1.00 74.97 N ANISOU 911 NE2 HIS A 201 11175 7671 9639 34 -745 -2078 N ATOM 912 N GLU A 202 14.164 25.852 8.802 1.00 53.25 N ANISOU 912 N GLU A 202 8617 4858 6759 -216 -832 -1830 N ATOM 913 CA GLU A 202 14.365 26.274 10.190 1.00 51.96 C ANISOU 913 CA GLU A 202 8539 4655 6547 -248 -843 -1795 C ATOM 914 C GLU A 202 15.409 27.379 10.307 1.00 66.51 C ANISOU 914 C GLU A 202 10503 6432 8337 -299 -958 -1710 C ATOM 915 O GLU A 202 15.370 28.195 11.235 1.00 73.51 O ANISOU 915 O GLU A 202 11513 7262 9154 -305 -1015 -1737 O ATOM 916 CB GLU A 202 14.761 25.086 11.063 1.00 55.48 C ANISOU 916 CB GLU A 202 8914 5126 7039 -312 -765 -1729 C ATOM 917 CG GLU A 202 13.838 23.891 10.958 1.00 63.83 C ANISOU 917 CG GLU A 202 9826 6218 8207 -281 -658 -1785 C ATOM 918 CD GLU A 202 12.414 24.175 11.410 1.00 67.06 C ANISOU 918 CD GLU A 202 10222 6647 8609 -194 -619 -1868 C ATOM 919 OE1 GLU A 202 12.187 25.155 12.142 1.00 74.02 O ANISOU 919 OE1 GLU A 202 11225 7521 9378 -150 -636 -1883 O ATOM 920 OE2 GLU A 202 11.510 23.395 11.039 1.00 86.14 O ANISOU 920 OE2 GLU A 202 12502 9078 11150 -168 -568 -1915 O ATOM 921 N ILE A 203 16.332 27.428 9.359 1.00 64.59 N ANISOU 921 N ILE A 203 10225 6185 8133 -330 -991 -1608 N ATOM 922 CA ILE A 203 17.317 28.503 9.338 1.00 53.61 C ANISOU 922 CA ILE A 203 8909 4716 6744 -384 -1111 -1491 C ATOM 923 C ILE A 203 16.615 29.805 9.047 1.00 60.46 C ANISOU 923 C ILE A 203 9859 5523 7589 -313 -1180 -1562 C ATOM 924 O ILE A 203 16.914 30.856 9.641 1.00 55.34 O ANISOU 924 O ILE A 203 9325 4762 6940 -350 -1289 -1551 O ATOM 925 CB ILE A 203 18.405 28.241 8.290 1.00 58.94 C ANISOU 925 CB ILE A 203 9498 5415 7482 -404 -1096 -1326 C ATOM 926 CG1 ILE A 203 19.318 27.121 8.775 1.00 47.48 C ANISOU 926 CG1 ILE A 203 7969 3984 6088 -482 -1036 -1213 C ATOM 927 CG2 ILE A 203 19.244 29.456 8.084 1.00 60.61 C ANISOU 927 CG2 ILE A 203 9752 5541 7737 -445 -1221 -1179 C ATOM 928 CD1 ILE A 203 20.013 27.498 10.036 1.00 67.48 C ANISOU 928 CD1 ILE A 203 10562 6455 8624 -598 -1150 -1124 C ATOM 929 N GLY A 204 15.657 29.728 8.133 1.00 60.62 N ANISOU 929 N GLY A 204 9821 5609 7604 -215 -1125 -1635 N ATOM 930 CA GLY A 204 14.865 30.894 7.793 1.00 64.12 C ANISOU 930 CA GLY A 204 10310 6003 8050 -131 -1172 -1679 C ATOM 931 C GLY A 204 14.286 31.508 9.042 1.00 49.58 C ANISOU 931 C GLY A 204 8590 4066 6185 -112 -1182 -1786 C ATOM 932 O GLY A 204 14.280 32.728 9.192 1.00 63.29 O ANISOU 932 O GLY A 204 10424 5678 7947 -90 -1257 -1791 O ATOM 933 N HIS A 205 13.810 30.655 9.947 1.00 52.61 N ANISOU 933 N HIS A 205 8968 4499 6522 -110 -1096 -1868 N ATOM 934 CA HIS A 205 13.340 31.119 11.258 1.00 64.89 C ANISOU 934 CA HIS A 205 10658 5991 8007 -75 -1077 -1967 C ATOM 935 C HIS A 205 14.471 31.795 12.036 1.00 52.99 C ANISOU 935 C HIS A 205 9308 4374 6453 -176 -1208 -1941 C ATOM 936 O HIS A 205 14.282 32.881 12.576 1.00 68.35 O ANISOU 936 O HIS A 205 11411 6194 8367 -141 -1265 -2028 O ATOM 937 CB HIS A 205 12.768 29.964 12.086 1.00 54.01 C ANISOU 937 CB HIS A 205 9221 4714 6587 -56 -950 -2005 C ATOM 938 CG HIS A 205 11.378 29.561 11.711 1.00 55.25 C ANISOU 938 CG HIS A 205 9252 4937 6806 54 -837 -2055 C ATOM 939 ND1 HIS A 205 10.368 30.479 11.462 1.00 56.64 N ANISOU 939 ND1 HIS A 205 9446 5065 7009 176 -816 -2108 N ATOM 940 CD2 HIS A 205 10.819 28.345 11.527 1.00 49.61 C ANISOU 940 CD2 HIS A 205 8372 4315 6163 56 -750 -2042 C ATOM 941 CE1 HIS A 205 9.255 29.835 11.166 1.00 50.98 C ANISOU 941 CE1 HIS A 205 8572 4426 6371 242 -729 -2112 C ATOM 942 NE2 HIS A 205 9.497 28.534 11.203 1.00 56.30 N ANISOU 942 NE2 HIS A 205 9136 5180 7078 165 -696 -2081 N ATOM 943 N SER A 206 15.639 31.147 12.078 1.00 50.55 N ANISOU 943 N SER A 206 8949 4100 6156 -303 -1262 -1818 N ATOM 944 CA SER A 206 16.795 31.633 12.827 1.00 51.48 C ANISOU 944 CA SER A 206 9182 4129 6249 -430 -1417 -1759 C ATOM 945 C SER A 206 17.226 32.980 12.314 1.00 55.67 C ANISOU 945 C SER A 206 9782 4498 6871 -453 -1562 -1727 C ATOM 946 O SER A 206 17.860 33.753 13.020 1.00 68.51 O ANISOU 946 O SER A 206 11549 5994 8490 -541 -1722 -1740 O ATOM 947 CB SER A 206 17.951 30.667 12.713 1.00 70.28 C ANISOU 947 CB SER A 206 11440 6583 8681 -550 -1434 -1578 C ATOM 948 OG SER A 206 17.510 29.336 12.901 1.00 78.45 O ANISOU 948 OG SER A 206 12364 7751 9692 -518 -1279 -1585 O ATOM 949 N LEU A 207 16.864 33.258 11.069 1.00 60.08 N ANISOU 949 N LEU A 207 10239 5065 7525 -376 -1516 -1677 N ATOM 950 CA LEU A 207 17.202 34.517 10.456 1.00 57.16 C ANISOU 950 CA LEU A 207 9895 4548 7275 -380 -1632 -1604 C ATOM 951 C LEU A 207 16.116 35.554 10.680 1.00 61.78 C ANISOU 951 C LEU A 207 10597 5013 7862 -262 -1619 -1763 C ATOM 952 O LEU A 207 16.375 36.745 10.588 1.00 76.57 O ANISOU 952 O LEU A 207 12543 6703 9847 -275 -1735 -1742 O ATOM 953 CB LEU A 207 17.470 34.324 8.971 1.00 52.00 C ANISOU 953 CB LEU A 207 9066 3984 6705 -347 -1586 -1429 C ATOM 954 CG LEU A 207 18.763 33.526 8.746 1.00 68.16 C ANISOU 954 CG LEU A 207 11010 6101 8786 -455 -1597 -1240 C ATOM 955 CD1 LEU A 207 19.056 33.343 7.262 1.00 56.71 C ANISOU 955 CD1 LEU A 207 9411 4753 7382 -393 -1525 -1071 C ATOM 956 CD2 LEU A 207 19.939 34.214 9.441 1.00 52.70 C ANISOU 956 CD2 LEU A 207 9115 3985 6923 -604 -1783 -1125 C ATOM 957 N GLY A 208 14.906 35.114 10.995 1.00 56.02 N ANISOU 957 N GLY A 208 9873 4370 7040 -144 -1474 -1905 N ATOM 958 CA GLY A 208 13.883 36.056 11.425 1.00 63.20 C ANISOU 958 CA GLY A 208 10904 5157 7951 -16 -1434 -2054 C ATOM 959 C GLY A 208 12.576 35.977 10.664 1.00 63.02 C ANISOU 959 C GLY A 208 10752 5221 7972 138 -1296 -2060 C ATOM 960 O GLY A 208 11.694 36.815 10.832 1.00 65.94 O ANISOU 960 O GLY A 208 11183 5485 8386 264 -1244 -2139 O ATOM 961 N LEU A 209 12.438 34.954 9.838 1.00 64.10 N ANISOU 961 N LEU A 209 10709 5542 8103 129 -1240 -1977 N ATOM 962 CA LEU A 209 11.256 34.823 9.023 1.00 58.08 C ANISOU 962 CA LEU A 209 9807 4874 7386 246 -1156 -1967 C ATOM 963 C LEU A 209 10.179 34.009 9.724 1.00 55.48 C ANISOU 963 C LEU A 209 9440 4634 7007 319 -1017 -2068 C ATOM 964 O LEU A 209 10.470 33.055 10.454 1.00 54.62 O ANISOU 964 O LEU A 209 9341 4591 6820 258 -974 -2102 O ATOM 965 CB LEU A 209 11.622 34.167 7.686 1.00 64.84 C ANISOU 965 CB LEU A 209 10505 5881 8251 203 -1188 -1846 C ATOM 966 CG LEU A 209 12.216 35.118 6.659 1.00 55.62 C ANISOU 966 CG LEU A 209 9313 4665 7156 201 -1284 -1694 C ATOM 967 CD1 LEU A 209 12.775 34.316 5.507 1.00 67.17 C ANISOU 967 CD1 LEU A 209 10657 6298 8565 163 -1291 -1587 C ATOM 968 CD2 LEU A 209 11.141 36.040 6.174 1.00 63.19 C ANISOU 968 CD2 LEU A 209 10226 5587 8196 329 -1273 -1674 C ATOM 969 N PHE A 210 8.926 34.351 9.443 1.00 64.38 N ANISOU 969 N PHE A 210 10488 5768 8203 452 -944 -2077 N ATOM 970 CA PHE A 210 7.798 33.555 9.918 1.00 63.83 C ANISOU 970 CA PHE A 210 10322 5793 8137 528 -808 -2118 C ATOM 971 C PHE A 210 7.284 32.649 8.835 1.00 55.89 C ANISOU 971 C PHE A 210 9101 4942 7193 504 -831 -2056 C ATOM 972 O PHE A 210 7.684 32.770 7.676 1.00 61.11 O ANISOU 972 O PHE A 210 9708 5648 7863 459 -937 -1991 O ATOM 973 CB PHE A 210 6.666 34.453 10.379 1.00 77.77 C ANISOU 973 CB PHE A 210 12118 7467 9965 701 -699 -2150 C ATOM 974 CG PHE A 210 7.103 35.525 11.310 1.00 81.65 C ANISOU 974 CG PHE A 210 12852 7772 10398 743 -692 -2248 C ATOM 975 CD1 PHE A 210 7.069 35.322 12.671 1.00 84.26 C ANISOU 975 CD1 PHE A 210 13334 8087 10596 782 -589 -2359 C ATOM 976 CD2 PHE A 210 7.561 36.735 10.822 1.00 84.18 C ANISOU 976 CD2 PHE A 210 13256 7933 10797 741 -798 -2228 C ATOM 977 CE1 PHE A 210 7.475 36.316 13.538 1.00 96.06 C ANISOU 977 CE1 PHE A 210 15087 9404 12008 818 -607 -2487 C ATOM 978 CE2 PHE A 210 7.963 37.727 11.679 1.00 89.30 C ANISOU 978 CE2 PHE A 210 14141 8376 11416 767 -818 -2344 C ATOM 979 CZ PHE A 210 7.923 37.518 13.041 1.00 90.23 C ANISOU 979 CZ PHE A 210 14436 8475 11372 803 -731 -2493 C ATOM 980 N HIS A 211 6.383 31.747 9.212 1.00 62.32 N ANISOU 980 N HIS A 211 9794 5836 8050 537 -734 -2070 N ATOM 981 CA HIS A 211 5.732 30.871 8.256 1.00 53.07 C ANISOU 981 CA HIS A 211 8416 4786 6961 508 -779 -2034 C ATOM 982 C HIS A 211 5.017 31.642 7.165 1.00 61.31 C ANISOU 982 C HIS A 211 9366 5854 8075 577 -858 -1964 C ATOM 983 O HIS A 211 4.505 32.735 7.402 1.00 68.68 O ANISOU 983 O HIS A 211 10333 6700 9061 693 -810 -1928 O ATOM 984 CB HIS A 211 4.733 29.959 8.959 1.00 63.11 C ANISOU 984 CB HIS A 211 9551 6103 8325 543 -662 -2030 C ATOM 985 CG HIS A 211 5.373 28.887 9.780 1.00 64.27 C ANISOU 985 CG HIS A 211 9724 6269 8427 458 -602 -2060 C ATOM 986 ND1 HIS A 211 4.768 28.352 10.891 1.00 55.17 N ANISOU 986 ND1 HIS A 211 8516 5130 7316 513 -451 -2032 N ATOM 987 CD2 HIS A 211 6.565 28.246 9.644 1.00 59.56 C ANISOU 987 CD2 HIS A 211 9184 5685 7760 332 -660 -2084 C ATOM 988 CE1 HIS A 211 5.564 27.428 11.416 1.00 73.60 C ANISOU 988 CE1 HIS A 211 10871 7487 9605 416 -431 -2036 C ATOM 989 NE2 HIS A 211 6.656 27.345 10.676 1.00 51.44 N ANISOU 989 NE2 HIS A 211 8131 4674 6740 305 -556 -2070 N ATOM 990 N SER A 212 4.980 31.055 5.973 1.00 64.25 N ANISOU 990 N SER A 212 9623 6344 8445 511 -977 -1946 N ATOM 991 CA SER A 212 4.245 31.617 4.851 1.00 73.88 C ANISOU 991 CA SER A 212 10727 7634 9711 564 -1078 -1861 C ATOM 992 C SER A 212 2.986 30.800 4.652 1.00 74.18 C ANISOU 992 C SER A 212 10558 7756 9873 564 -1102 -1852 C ATOM 993 O SER A 212 2.894 29.668 5.135 1.00 63.85 O ANISOU 993 O SER A 212 9197 6457 8606 498 -1064 -1918 O ATOM 994 CB SER A 212 5.087 31.619 3.568 1.00 74.93 C ANISOU 994 CB SER A 212 10890 7864 9715 500 -1215 -1840 C ATOM 995 OG SER A 212 4.383 32.207 2.484 1.00 76.71 O ANISOU 995 OG SER A 212 11006 8185 9957 558 -1321 -1735 O ATOM 996 N ALA A 213 2.024 31.386 3.949 1.00 59.75 N ANISOU 996 N ALA A 213 8594 5979 8128 633 -1174 -1745 N ATOM 997 CA ALA A 213 0.792 30.701 3.616 1.00 58.64 C ANISOU 997 CA ALA A 213 8227 5922 8132 618 -1245 -1703 C ATOM 998 C ALA A 213 0.876 30.081 2.220 1.00 78.02 C ANISOU 998 C ALA A 213 10623 8530 10489 512 -1469 -1744 C ATOM 999 O ALA A 213 0.011 29.281 1.832 1.00 75.07 O ANISOU 999 O ALA A 213 10076 8226 10220 451 -1586 -1751 O ATOM 1000 CB ALA A 213 -0.372 31.659 3.706 1.00 60.39 C ANISOU 1000 CB ALA A 213 8311 6116 8520 758 -1197 -1540 C ATOM 1001 N ASN A 214 1.919 30.441 1.468 1.00 80.63 N ANISOU 1001 N ASN A 214 11100 8914 10621 491 -1533 -1768 N ATOM 1002 CA ASN A 214 2.162 29.833 0.153 1.00 63.01 C ANISOU 1002 CA ASN A 214 8866 6844 8232 412 -1719 -1831 C ATOM 1003 C ASN A 214 2.848 28.487 0.269 1.00 72.83 C ANISOU 1003 C ASN A 214 10184 8074 9415 301 -1711 -2016 C ATOM 1004 O ASN A 214 3.942 28.380 0.822 1.00 75.65 O ANISOU 1004 O ASN A 214 10683 8352 9708 287 -1588 -2062 O ATOM 1005 CB ASN A 214 3.002 30.755 -0.736 1.00 70.47 C ANISOU 1005 CB ASN A 214 9922 7869 8985 461 -1761 -1745 C ATOM 1006 CG ASN A 214 3.261 30.167 -2.125 1.00 80.52 C ANISOU 1006 CG ASN A 214 11216 9339 10038 410 -1932 -1809 C ATOM 1007 OD1 ASN A 214 2.802 29.067 -2.458 1.00 80.95 O ANISOU 1007 OD1 ASN A 214 11218 9454 10086 327 -2045 -1950 O ATOM 1008 ND2 ASN A 214 3.981 30.919 -2.954 1.00 78.06 N ANISOU 1008 ND2 ASN A 214 10984 9127 9547 468 -1954 -1701 N ATOM 1009 N THR A 215 2.207 27.473 -0.305 1.00 69.37 N ANISOU 1009 N THR A 215 9641 7705 9013 218 -1859 -2114 N ATOM 1010 CA THR A 215 2.620 26.085 -0.164 1.00 68.30 C ANISOU 1010 CA THR A 215 9539 7518 8893 112 -1856 -2295 C ATOM 1011 C THR A 215 3.919 25.734 -0.886 1.00 68.63 C ANISOU 1011 C THR A 215 9769 7613 8693 92 -1855 -2410 C ATOM 1012 O THR A 215 4.570 24.734 -0.554 1.00 76.15 O ANISOU 1012 O THR A 215 10782 8484 9669 30 -1781 -2535 O ATOM 1013 CB THR A 215 1.519 25.173 -0.671 1.00 79.92 C ANISOU 1013 CB THR A 215 10845 9026 10496 22 -2049 -2373 C ATOM 1014 OG1 THR A 215 1.300 25.437 -2.059 1.00 76.45 O ANISOU 1014 OG1 THR A 215 10422 8761 9865 20 -2266 -2395 O ATOM 1015 CG2 THR A 215 0.242 25.456 0.089 1.00 78.52 C ANISOU 1015 CG2 THR A 215 10446 8791 10595 51 -2022 -2218 C ATOM 1016 N GLU A 216 4.302 26.561 -1.855 1.00 59.06 N ANISOU 1016 N GLU A 216 8637 6537 7265 157 -1918 -2341 N ATOM 1017 CA GLU A 216 5.552 26.362 -2.586 1.00 67.21 C ANISOU 1017 CA GLU A 216 9840 7640 8057 172 -1886 -2402 C ATOM 1018 C GLU A 216 6.693 27.043 -1.859 1.00 62.77 C ANISOU 1018 C GLU A 216 9374 6983 7491 217 -1700 -2281 C ATOM 1019 O GLU A 216 7.867 26.778 -2.110 1.00 85.97 O ANISOU 1019 O GLU A 216 12431 9930 10305 224 -1619 -2300 O ATOM 1020 CB GLU A 216 5.446 26.899 -4.013 1.00 81.07 C ANISOU 1020 CB GLU A 216 11625 9613 9565 232 -2036 -2353 C ATOM 1021 CG GLU A 216 6.032 25.968 -5.052 1.00 97.67 C ANISOU 1021 CG GLU A 216 13859 11827 11424 219 -2093 -2538 C ATOM 1022 CD GLU A 216 5.086 24.837 -5.387 1.00115.40 C ANISOU 1022 CD GLU A 216 16047 14076 13724 119 -2280 -2760 C ATOM 1023 OE1 GLU A 216 3.857 25.070 -5.342 1.00122.32 O ANISOU 1023 OE1 GLU A 216 16761 14975 14741 80 -2435 -2704 O ATOM 1024 OE2 GLU A 216 5.565 23.717 -5.680 1.00120.56 O ANISOU 1024 OE2 GLU A 216 16808 14692 14308 78 -2272 -2980 O ATOM 1025 N ALA A 217 6.335 27.918 -0.936 1.00 63.67 N ANISOU 1025 N ALA A 217 9438 6998 7756 250 -1635 -2157 N ATOM 1026 CA ALA A 217 7.321 28.639 -0.166 1.00 67.21 C ANISOU 1026 CA ALA A 217 9981 7335 8220 275 -1499 -2056 C ATOM 1027 C ALA A 217 8.063 27.690 0.758 1.00 66.89 C ANISOU 1027 C ALA A 217 9994 7182 8239 202 -1383 -2146 C ATOM 1028 O ALA A 217 7.476 26.781 1.331 1.00 72.19 O ANISOU 1028 O ALA A 217 10593 7802 9033 150 -1365 -2245 O ATOM 1029 CB ALA A 217 6.670 29.752 0.620 1.00 67.43 C ANISOU 1029 CB ALA A 217 9965 7267 8388 334 -1463 -1944 C ATOM 1030 N LEU A 218 9.365 27.901 0.886 1.00 64.89 N ANISOU 1030 N LEU A 218 9943 7476 7236 -527 27 -1175 N ATOM 1031 CA LEU A 218 10.162 27.132 1.825 1.00 58.28 C ANISOU 1031 CA LEU A 218 9161 6600 6383 -254 -42 -1364 C ATOM 1032 C LEU A 218 9.721 27.449 3.255 1.00 65.33 C ANISOU 1032 C LEU A 218 10121 7317 7385 -218 -163 -1358 C ATOM 1033 O LEU A 218 9.916 26.641 4.164 1.00 64.19 O ANISOU 1033 O LEU A 218 10157 7062 7171 -15 -252 -1470 O ATOM 1034 CB LEU A 218 11.650 27.435 1.638 1.00 59.22 C ANISOU 1034 CB LEU A 218 8990 6913 6597 -140 5 -1488 C ATOM 1035 CG LEU A 218 12.640 26.922 2.696 1.00 68.31 C ANISOU 1035 CG LEU A 218 10117 8028 7811 143 -117 -1687 C ATOM 1036 CD1 LEU A 218 12.700 25.404 2.744 1.00 60.94 C ANISOU 1036 CD1 LEU A 218 9454 7007 6694 358 -156 -1817 C ATOM 1037 CD2 LEU A 218 14.020 27.484 2.456 1.00 67.78 C ANISOU 1037 CD2 LEU A 218 9689 8144 7921 205 -68 -1794 C ATOM 1038 N MET A 219 9.116 28.623 3.451 1.00 55.07 N ANISOU 1038 N MET A 219 8692 5983 6250 -417 -167 -1227 N ATOM 1039 CA MET A 219 8.675 29.028 4.784 1.00 57.44 C ANISOU 1039 CA MET A 219 9048 6127 6651 -400 -256 -1236 C ATOM 1040 C MET A 219 7.301 28.479 5.088 1.00 73.72 C ANISOU 1040 C MET A 219 11399 7978 8632 -474 -244 -1164 C ATOM 1041 O MET A 219 6.681 28.870 6.075 1.00 68.07 O ANISOU 1041 O MET A 219 10746 7121 7998 -512 -270 -1149 O ATOM 1042 CB MET A 219 8.673 30.544 4.916 1.00 68.19 C ANISOU 1042 CB MET A 219 10119 7528 8263 -569 -263 -1157 C ATOM 1043 CG MET A 219 10.031 31.066 5.206 1.00 54.94 C ANISOU 1043 CG MET A 219 8176 5987 6711 -452 -312 -1273 C ATOM 1044 SD MET A 219 10.710 29.972 6.445 1.00 68.76 S ANISOU 1044 SD MET A 219 10142 7663 8320 -124 -448 -1481 S ATOM 1045 CE MET A 219 12.271 29.597 5.740 1.00 57.89 C ANISOU 1045 CE MET A 219 8543 6489 6965 42 -432 -1618 C ATOM 1046 N TYR A 220 6.826 27.578 4.229 1.00 72.40 N ANISOU 1046 N TYR A 220 11402 7789 8319 -497 -195 -1131 N ATOM 1047 CA TYR A 220 5.603 26.836 4.497 1.00 60.16 C ANISOU 1047 CA TYR A 220 10132 6021 6703 -542 -183 -1088 C ATOM 1048 C TYR A 220 5.894 25.759 5.523 1.00 52.97 C ANISOU 1048 C TYR A 220 9479 4993 5653 -309 -227 -1204 C ATOM 1049 O TYR A 220 6.915 25.075 5.440 1.00 57.30 O ANISOU 1049 O TYR A 220 10050 5628 6093 -107 -270 -1320 O ATOM 1050 CB TYR A 220 5.050 26.220 3.222 1.00 56.45 C ANISOU 1050 CB TYR A 220 9755 5560 6135 -637 -144 -1033 C ATOM 1051 CG TYR A 220 3.624 25.721 3.341 1.00 63.27 C ANISOU 1051 CG TYR A 220 10833 6189 7020 -749 -134 -965 C ATOM 1052 CD1 TYR A 220 2.555 26.604 3.477 1.00 53.77 C ANISOU 1052 CD1 TYR A 220 9542 4871 6017 -963 -126 -847 C ATOM 1053 CD2 TYR A 220 3.347 24.370 3.278 1.00 55.19 C ANISOU 1053 CD2 TYR A 220 10077 5044 5851 -644 -133 -1027 C ATOM 1054 CE1 TYR A 220 1.245 26.135 3.559 1.00 62.89 C ANISOU 1054 CE1 TYR A 220 10861 5798 7237 -1070 -108 -800 C ATOM 1055 CE2 TYR A 220 2.059 23.900 3.361 1.00 70.53 C ANISOU 1055 CE2 TYR A 220 12192 6759 7848 -755 -115 -972 C ATOM 1056 CZ TYR A 220 1.011 24.772 3.501 1.00 68.84 C ANISOU 1056 CZ TYR A 220 11878 6436 7843 -968 -98 -862 C ATOM 1057 OH TYR A 220 -0.267 24.243 3.580 1.00 73.06 O ANISOU 1057 OH TYR A 220 12563 6728 8468 -1075 -72 -825 O ATOM 1058 N PRO A 221 5.009 25.611 6.517 1.00 60.46 N ANISOU 1058 N PRO A 221 10625 5734 6614 -337 -215 -1173 N ATOM 1059 CA PRO A 221 5.319 24.732 7.654 1.00 66.84 C ANISOU 1059 CA PRO A 221 11699 6420 7276 -122 -266 -1259 C ATOM 1060 C PRO A 221 5.072 23.233 7.418 1.00 71.66 C ANISOU 1060 C PRO A 221 12602 6899 7725 -16 -258 -1281 C ATOM 1061 O PRO A 221 5.498 22.416 8.245 1.00 57.47 O ANISOU 1061 O PRO A 221 11029 5007 5797 186 -323 -1346 O ATOM 1062 CB PRO A 221 4.400 25.261 8.756 1.00 61.46 C ANISOU 1062 CB PRO A 221 11116 5572 6665 -228 -214 -1207 C ATOM 1063 CG PRO A 221 3.260 25.888 8.042 1.00 54.25 C ANISOU 1063 CG PRO A 221 10070 4612 5929 -495 -121 -1092 C ATOM 1064 CD PRO A 221 3.792 26.411 6.736 1.00 51.29 C ANISOU 1064 CD PRO A 221 9421 4447 5621 -565 -153 -1065 C ATOM 1065 N LEU A 222 4.406 22.858 6.329 1.00 62.54 N ANISOU 1065 N LEU A 222 11458 5725 6582 -142 -200 -1230 N ATOM 1066 CA LEU A 222 4.163 21.431 6.107 1.00 61.12 C ANISOU 1066 CA LEU A 222 11547 5403 6274 -42 -202 -1267 C ATOM 1067 C LEU A 222 5.219 20.850 5.201 1.00 64.56 C ANISOU 1067 C LEU A 222 11912 6003 6612 113 -250 -1382 C ATOM 1068 O LEU A 222 5.473 21.398 4.121 1.00 68.06 O ANISOU 1068 O LEU A 222 12137 6638 7085 17 -221 -1378 O ATOM 1069 CB LEU A 222 2.774 21.195 5.528 1.00 53.93 C ANISOU 1069 CB LEU A 222 10719 4334 5438 -251 -128 -1175 C ATOM 1070 CG LEU A 222 1.702 21.789 6.450 1.00 74.93 C ANISOU 1070 CG LEU A 222 13419 6818 8234 -410 -49 -1080 C ATOM 1071 CD1 LEU A 222 0.298 21.388 6.026 1.00 80.44 C ANISOU 1071 CD1 LEU A 222 14210 7307 9046 -596 18 -1009 C ATOM 1072 CD2 LEU A 222 1.964 21.366 7.883 1.00 73.39 C ANISOU 1072 CD2 LEU A 222 13457 6497 7933 -251 -43 -1110 C ATOM 1073 N TYR A 223 5.830 19.747 5.647 1.00 64.77 N ANISOU 1073 N TYR A 223 12133 5949 6528 350 -319 -1482 N ATOM 1074 CA TYR A 223 6.978 19.169 4.965 1.00 58.44 C ANISOU 1074 CA TYR A 223 11249 5292 5662 539 -366 -1630 C ATOM 1075 C TYR A 223 6.642 18.898 3.522 1.00 66.12 C ANISOU 1075 C TYR A 223 12174 6346 6602 424 -292 -1645 C ATOM 1076 O TYR A 223 5.722 18.151 3.247 1.00 63.69 O ANISOU 1076 O TYR A 223 12069 5867 6264 358 -276 -1615 O ATOM 1077 CB TYR A 223 7.436 17.885 5.637 1.00 60.04 C ANISOU 1077 CB TYR A 223 11707 5327 5776 799 -466 -1723 C ATOM 1078 CG TYR A 223 8.633 17.254 4.949 1.00 62.83 C ANISOU 1078 CG TYR A 223 11955 5813 6106 1008 -514 -1904 C ATOM 1079 CD1 TYR A 223 8.561 15.974 4.430 1.00 70.69 C ANISOU 1079 CD1 TYR A 223 13130 6693 7038 1114 -525 -1993 C ATOM 1080 CD2 TYR A 223 9.826 17.954 4.791 1.00 63.29 C ANISOU 1080 CD2 TYR A 223 11711 6103 6232 1092 -535 -2001 C ATOM 1081 CE1 TYR A 223 9.646 15.388 3.797 1.00 70.19 C ANISOU 1081 CE1 TYR A 223 12957 6741 6970 1309 -552 -2184 C ATOM 1082 CE2 TYR A 223 10.914 17.375 4.145 1.00 79.63 C ANISOU 1082 CE2 TYR A 223 13658 8287 8310 1279 -549 -2186 C ATOM 1083 CZ TYR A 223 10.812 16.090 3.648 1.00 75.54 C ANISOU 1083 CZ TYR A 223 13329 7654 7719 1390 -553 -2281 C ATOM 1084 OH TYR A 223 11.875 15.487 3.012 1.00 86.37 O ANISOU 1084 OH TYR A 223 14573 9128 9115 1582 -552 -2490 O ATOM 1085 N HIS A 224 7.376 19.517 2.601 1.00 94.71 N ANISOU 1085 N HIS A 224 15535 10223 10229 392 -246 -1692 N ATOM 1086 CA HIS A 224 7.012 19.425 1.191 1.00106.50 C ANISOU 1086 CA HIS A 224 16997 11815 11651 253 -173 -1689 C ATOM 1087 C HIS A 224 7.381 18.067 0.614 1.00 87.64 C ANISOU 1087 C HIS A 224 14763 9392 9143 427 -181 -1857 C ATOM 1088 O HIS A 224 6.509 17.360 0.129 1.00 94.28 O ANISOU 1088 O HIS A 224 15795 10097 9931 359 -187 -1850 O ATOM 1089 CB HIS A 224 7.666 20.541 0.376 1.00116.05 C ANISOU 1089 CB HIS A 224 17905 13307 12881 146 -95 -1667 C ATOM 1090 CG HIS A 224 7.046 20.727 -0.972 1.00128.87 C ANISOU 1090 CG HIS A 224 19530 15020 14416 -56 -33 -1600 C ATOM 1091 ND1 HIS A 224 5.823 21.339 -1.148 1.00134.36 N ANISOU 1091 ND1 HIS A 224 20255 15624 15173 -297 -58 -1427 N ATOM 1092 CD2 HIS A 224 7.462 20.357 -2.207 1.00136.27 C ANISOU 1092 CD2 HIS A 224 20459 16119 15199 -50 41 -1692 C ATOM 1093 CE1 HIS A 224 5.519 21.349 -2.434 1.00133.32 C ANISOU 1093 CE1 HIS A 224 20142 15592 14923 -427 -32 -1402 C ATOM 1094 NE2 HIS A 224 6.497 20.760 -3.098 1.00133.57 N ANISOU 1094 NE2 HIS A 224 20165 15786 14801 -285 39 -1561 N ATOM 1095 N SER A 225 8.665 17.715 0.687 1.00 80.80 N ANISOU 1095 N SER A 225 13799 8635 8267 655 -191 -2021 N ATOM 1096 CA SER A 225 9.189 16.433 0.189 1.00 79.43 C ANISOU 1096 CA SER A 225 13735 8429 8013 854 -200 -2217 C ATOM 1097 C SER A 225 9.118 16.350 -1.317 1.00 87.96 C ANISOU 1097 C SER A 225 14773 9678 8971 746 -85 -2283 C ATOM 1098 O SER A 225 8.079 15.988 -1.862 1.00 94.22 O ANISOU 1098 O SER A 225 15742 10365 9691 610 -92 -2231 O ATOM 1099 CB SER A 225 8.429 15.249 0.778 1.00 80.89 C ANISOU 1099 CB SER A 225 14248 8302 8186 935 -295 -2213 C ATOM 1100 OG SER A 225 9.165 14.055 0.586 1.00102.74 O ANISOU 1100 OG SER A 225 17095 11015 10926 1181 -338 -2416 O ATOM 1101 N LEU A 226 10.207 16.666 -2.004 1.00 66.89 N ANISOU 1101 N LEU A 226 11877 7263 6277 802 22 -2404 N ATOM 1102 CA LEU A 226 10.104 16.801 -3.446 1.00 74.73 C ANISOU 1102 CA LEU A 226 12840 8445 7110 659 156 -2435 C ATOM 1103 C LEU A 226 10.998 15.832 -4.205 1.00 86.40 C ANISOU 1103 C LEU A 226 14314 10015 8498 850 241 -2703 C ATOM 1104 O LEU A 226 11.975 15.325 -3.660 1.00 97.28 O ANISOU 1104 O LEU A 226 15606 11368 9987 1095 215 -2868 O ATOM 1105 CB LEU A 226 10.406 18.240 -3.841 1.00 89.80 C ANISOU 1105 CB LEU A 226 14486 10597 9035 470 268 -2301 C ATOM 1106 CG LEU A 226 11.716 18.763 -3.281 1.00 83.62 C ANISOU 1106 CG LEU A 226 13415 9948 8409 609 313 -2378 C ATOM 1107 CD1 LEU A 226 12.815 18.671 -4.337 1.00 89.51 C ANISOU 1107 CD1 LEU A 226 13984 10945 9082 668 508 -2558 C ATOM 1108 CD2 LEU A 226 11.503 20.164 -2.790 1.00 68.20 C ANISOU 1108 CD2 LEU A 226 11286 8043 6585 429 298 -2167 C ATOM 1109 N THR A 227 10.649 15.594 -5.470 1.00 95.19 N ANISOU 1109 N THR A 227 15522 11230 9414 738 333 -2755 N ATOM 1110 CA THR A 227 11.198 14.484 -6.249 1.00104.44 C ANISOU 1110 CA THR A 227 16768 12439 10474 906 406 -3030 C ATOM 1111 C THR A 227 12.643 14.681 -6.709 1.00 99.73 C ANISOU 1111 C THR A 227 15902 12102 9889 1027 602 -3219 C ATOM 1112 O THR A 227 13.382 13.706 -6.898 1.00 91.01 O ANISOU 1112 O THR A 227 14792 10983 8805 1253 642 -3487 O ATOM 1113 CB THR A 227 10.332 14.203 -7.506 1.00112.81 C ANISOU 1113 CB THR A 227 18037 13536 11290 736 437 -3039 C ATOM 1114 OG1 THR A 227 10.200 15.404 -8.276 1.00129.85 O ANISOU 1114 OG1 THR A 227 20091 15932 13314 488 550 -2872 O ATOM 1115 CG2 THR A 227 8.942 13.699 -7.118 1.00 91.11 C ANISOU 1115 CG2 THR A 227 15552 10488 8576 656 239 -2924 C ATOM 1116 N ASP A 228 13.046 15.929 -6.912 1.00103.33 N ANISOU 1116 N ASP A 228 16122 12783 10356 876 732 -3089 N ATOM 1117 CA ASP A 228 14.406 16.181 -7.364 1.00111.82 C ANISOU 1117 CA ASP A 228 16914 14101 11473 966 950 -3261 C ATOM 1118 C ASP A 228 15.002 17.425 -6.724 1.00100.16 C ANISOU 1118 C ASP A 228 15127 12729 10201 905 979 -3120 C ATOM 1119 O ASP A 228 14.886 18.534 -7.258 1.00 84.35 O ANISOU 1119 O ASP A 228 13016 10902 8129 669 1105 -2941 O ATOM 1120 CB ASP A 228 14.457 16.297 -8.889 1.00114.59 C ANISOU 1120 CB ASP A 228 17305 14696 11538 815 1189 -3320 C ATOM 1121 CG ASP A 228 15.872 16.180 -9.429 1.00126.59 C ANISOU 1121 CG ASP A 228 18570 16435 13094 949 1454 -3576 C ATOM 1122 OD1 ASP A 228 16.758 15.760 -8.654 1.00126.45 O ANISOU 1122 OD1 ASP A 228 18365 16339 13339 1197 1409 -3751 O ATOM 1123 OD2 ASP A 228 16.101 16.490 -10.621 1.00136.87 O ANISOU 1123 OD2 ASP A 228 19861 17979 14166 810 1706 -3608 O ATOM 1124 N LEU A 229 15.654 17.206 -5.581 1.00 98.45 N ANISOU 1124 N LEU A 229 14779 12388 10239 1126 846 -3206 N ATOM 1125 CA LEU A 229 16.385 18.232 -4.844 1.00 89.70 C ANISOU 1125 CA LEU A 229 13358 11351 9371 1128 836 -3137 C ATOM 1126 C LEU A 229 17.291 19.087 -5.712 1.00106.22 C ANISOU 1126 C LEU A 229 15137 13736 11487 1016 1116 -3170 C ATOM 1127 O LEU A 229 17.675 20.191 -5.301 1.00 95.19 O ANISOU 1127 O LEU A 229 13484 12415 10270 927 1131 -3052 O ATOM 1128 CB LEU A 229 17.244 17.594 -3.758 1.00 86.96 C ANISOU 1128 CB LEU A 229 12912 10857 9271 1442 666 -3323 C ATOM 1129 CG LEU A 229 16.604 16.860 -2.586 1.00 94.96 C ANISOU 1129 CG LEU A 229 14198 11566 10317 1585 375 -3276 C ATOM 1130 CD1 LEU A 229 17.704 16.361 -1.668 1.00 90.98 C ANISOU 1130 CD1 LEU A 229 13550 10962 10056 1898 217 -3470 C ATOM 1131 CD2 LEU A 229 15.638 17.774 -1.835 1.00 83.39 C ANISOU 1131 CD2 LEU A 229 12822 10016 8846 1388 258 -2989 C ATOM 1132 N THR A 230 17.666 18.544 -6.876 1.00112.57 N ANISOU 1132 N THR A 230 15960 14691 12120 1029 1344 -3346 N ATOM 1133 CA THR A 230 18.464 19.256 -7.870 1.00110.20 C ANISOU 1133 CA THR A 230 15410 14677 11783 900 1670 -3379 C ATOM 1134 C THR A 230 17.921 20.653 -8.040 1.00112.43 C ANISOU 1134 C THR A 230 15644 15055 12017 590 1708 -3053 C ATOM 1135 O THR A 230 18.586 21.632 -7.698 1.00125.20 O ANISOU 1135 O THR A 230 16948 16757 13865 536 1772 -2984 O ATOM 1136 CB THR A 230 18.455 18.562 -9.251 1.00105.06 C ANISOU 1136 CB THR A 230 14928 14172 10818 869 1908 -3538 C ATOM 1137 OG1 THR A 230 18.795 17.180 -9.107 1.00109.05 O ANISOU 1137 OG1 THR A 230 15517 14550 11369 1156 1844 -3844 O ATOM 1138 CG2 THR A 230 19.431 19.239 -10.214 1.00103.20 C ANISOU 1138 CG2 THR A 230 14424 14233 10552 755 2289 -3596 C ATOM 1139 N ARG A 231 16.690 20.739 -8.533 1.00 95.73 N ANISOU 1139 N ARG A 231 13834 12903 9636 392 1642 -2855 N ATOM 1140 CA ARG A 231 16.093 22.037 -8.775 1.00105.08 C ANISOU 1140 CA ARG A 231 14992 14157 10776 95 1657 -2539 C ATOM 1141 C ARG A 231 15.002 22.416 -7.783 1.00103.83 C ANISOU 1141 C ARG A 231 14950 13773 10728 25 1363 -2320 C ATOM 1142 O ARG A 231 13.988 22.986 -8.157 1.00106.88 O ANISOU 1142 O ARG A 231 15485 14136 10987 -205 1303 -2085 O ATOM 1143 CB ARG A 231 15.586 22.115 -10.219 1.00119.37 C ANISOU 1143 CB ARG A 231 17016 16126 12211 -120 1823 -2452 C ATOM 1144 CG ARG A 231 16.774 22.123 -11.163 1.00136.65 C ANISOU 1144 CG ARG A 231 19028 18579 14315 -106 2183 -2623 C ATOM 1145 CD ARG A 231 17.561 23.357 -10.750 1.00144.85 C ANISOU 1145 CD ARG A 231 19683 19709 15644 -194 2292 -2500 C ATOM 1146 NE ARG A 231 18.936 23.462 -11.230 1.00147.79 N ANISOU 1146 NE ARG A 231 19752 20289 16111 -140 2631 -2687 N ATOM 1147 CZ ARG A 231 19.791 24.381 -10.783 1.00145.80 C ANISOU 1147 CZ ARG A 231 19116 20096 16187 -169 2725 -2646 C ATOM 1148 NH1 ARG A 231 19.395 25.285 -9.889 1.00141.82 N ANISOU 1148 NH1 ARG A 231 18507 19466 15911 -255 2503 -2425 N ATOM 1149 NH2 ARG A 231 21.036 24.400 -11.226 1.00142.39 N ANISOU 1149 NH2 ARG A 231 18392 19838 15873 -115 3047 -2839 N ATOM 1150 N PHE A 232 15.224 22.115 -6.511 1.00 88.21 N ANISOU 1150 N PHE A 232 12902 11622 8991 224 1180 -2402 N ATOM 1151 CA PHE A 232 14.575 22.876 -5.465 1.00 92.02 C ANISOU 1151 CA PHE A 232 13366 11951 9647 142 978 -2201 C ATOM 1152 C PHE A 232 14.901 24.375 -5.669 1.00 90.49 C ANISOU 1152 C PHE A 232 12890 11911 9583 -72 1091 -2017 C ATOM 1153 O PHE A 232 16.073 24.713 -5.879 1.00 95.98 O ANISOU 1153 O PHE A 232 13296 12768 10403 -26 1263 -2122 O ATOM 1154 CB PHE A 232 15.056 22.387 -4.098 1.00 94.66 C ANISOU 1154 CB PHE A 232 13644 12119 10204 406 796 -2343 C ATOM 1155 CG PHE A 232 15.043 23.448 -3.067 1.00 91.54 C ANISOU 1155 CG PHE A 232 13075 11664 10041 348 673 -2206 C ATOM 1156 CD1 PHE A 232 13.859 23.822 -2.465 1.00 80.93 C ANISOU 1156 CD1 PHE A 232 11903 10154 8694 219 519 -2010 C ATOM 1157 CD2 PHE A 232 16.205 24.131 -2.749 1.00 91.26 C ANISOU 1157 CD2 PHE A 232 12687 11741 10246 408 725 -2281 C ATOM 1158 CE1 PHE A 232 13.839 24.836 -1.546 1.00 78.01 C ANISOU 1158 CE1 PHE A 232 11373 9734 8532 160 420 -1903 C ATOM 1159 CE2 PHE A 232 16.193 25.153 -1.826 1.00 69.47 C ANISOU 1159 CE2 PHE A 232 9764 8926 7704 349 602 -2170 C ATOM 1160 CZ PHE A 232 15.011 25.506 -1.226 1.00 73.11 C ANISOU 1160 CZ PHE A 232 10416 9227 8136 227 452 -1985 C ATOM 1161 N ARG A 233 13.903 25.266 -5.650 1.00 81.96 N ANISOU 1161 N ARG A 233 11871 10771 8499 -307 1006 -1754 N ATOM 1162 CA ARG A 233 14.226 26.701 -5.648 1.00 81.01 C ANISOU 1162 CA ARG A 233 11469 10749 8564 -491 1075 -1580 C ATOM 1163 C ARG A 233 13.500 27.439 -4.546 1.00 88.28 C ANISOU 1163 C ARG A 233 12364 11485 9695 -557 861 -1428 C ATOM 1164 O ARG A 233 12.353 27.139 -4.217 1.00 87.48 O ANISOU 1164 O ARG A 233 12505 11207 9527 -593 703 -1348 O ATOM 1165 CB ARG A 233 13.913 27.413 -6.982 1.00 86.37 C ANISOU 1165 CB ARG A 233 12179 11585 9051 -769 1240 -1377 C ATOM 1166 CG ARG A 233 12.567 28.170 -7.186 1.00 91.99 C ANISOU 1166 CG ARG A 233 13042 12190 9718 -1025 1097 -1085 C ATOM 1167 CD ARG A 233 12.696 29.138 -8.403 1.00110.87 C ANISOU 1167 CD ARG A 233 15370 14766 11990 -1286 1274 -875 C ATOM 1168 NE ARG A 233 11.475 29.880 -8.800 1.00116.08 N ANISOU 1168 NE ARG A 233 16173 15334 12599 -1537 1130 -588 N ATOM 1169 CZ ARG A 233 11.383 30.710 -9.873 1.00114.99 C ANISOU 1169 CZ ARG A 233 16048 15317 12327 -1780 1229 -360 C ATOM 1170 NH1 ARG A 233 12.449 30.975 -10.648 1.00108.09 N ANISOU 1170 NH1 ARG A 233 15045 14674 11351 -1826 1513 -373 N ATOM 1171 NH2 ARG A 233 10.233 31.339 -10.172 1.00112.87 N ANISOU 1171 NH2 ARG A 233 15911 14931 12043 -1988 1048 -107 N ATOM 1172 N LEU A 234 14.210 28.411 -3.988 1.00 78.99 N ANISOU 1172 N LEU A 234 10874 10348 8790 -573 870 -1408 N ATOM 1173 CA LEU A 234 13.669 29.426 -3.106 1.00 65.42 C ANISOU 1173 CA LEU A 234 9063 8498 7296 -681 714 -1257 C ATOM 1174 C LEU A 234 12.483 30.128 -3.753 1.00 65.46 C ANISOU 1174 C LEU A 234 9187 8463 7221 -961 696 -988 C ATOM 1175 O LEU A 234 12.607 30.671 -4.849 1.00 66.38 O ANISOU 1175 O LEU A 234 9246 8725 7252 -1143 844 -854 O ATOM 1176 CB LEU A 234 14.768 30.436 -2.780 1.00 67.05 C ANISOU 1176 CB LEU A 234 8879 8800 7799 -690 775 -1281 C ATOM 1177 CG LEU A 234 14.770 30.992 -1.367 1.00 69.81 C ANISOU 1177 CG LEU A 234 9104 9000 8420 -616 571 -1312 C ATOM 1178 CD1 LEU A 234 14.641 29.823 -0.414 1.00 64.91 C ANISOU 1178 CD1 LEU A 234 8712 8238 7714 -356 406 -1492 C ATOM 1179 CD2 LEU A 234 16.067 31.710 -1.147 1.00 66.82 C ANISOU 1179 CD2 LEU A 234 8332 8726 8330 -574 631 -1407 C ATOM 1180 N SER A 235 11.335 30.087 -3.087 1.00 69.51 N ANISOU 1180 N SER A 235 9876 8771 7763 -994 516 -913 N ATOM 1181 CA SER A 235 10.168 30.868 -3.478 1.00 65.07 C ANISOU 1181 CA SER A 235 9378 8124 7222 -1247 449 -669 C ATOM 1182 C SER A 235 10.485 32.355 -3.513 1.00 70.77 C ANISOU 1182 C SER A 235 9801 8897 8190 -1426 479 -509 C ATOM 1183 O SER A 235 11.426 32.816 -2.865 1.00 69.96 O ANISOU 1183 O SER A 235 9443 8840 8298 -1341 503 -601 O ATOM 1184 CB SER A 235 9.011 30.592 -2.515 1.00 78.90 C ANISOU 1184 CB SER A 235 11306 9627 9043 -1224 271 -661 C ATOM 1185 OG SER A 235 8.342 31.783 -2.123 1.00 85.21 O ANISOU 1185 OG SER A 235 11975 10316 10084 -1403 184 -494 O ATOM 1186 N GLN A 236 9.703 33.105 -4.278 1.00 74.28 N ANISOU 1186 N GLN A 236 11607 6744 9872 422 -1353 -2945 N ATOM 1187 CA GLN A 236 9.862 34.545 -4.306 1.00 70.03 C ANISOU 1187 CA GLN A 236 11620 6030 8959 527 -1324 -2694 C ATOM 1188 C GLN A 236 9.450 35.161 -2.969 1.00 83.86 C ANISOU 1188 C GLN A 236 13343 7547 10973 688 -1107 -2525 C ATOM 1189 O GLN A 236 10.045 36.156 -2.529 1.00 90.70 O ANISOU 1189 O GLN A 236 14642 8233 11588 619 -882 -2360 O ATOM 1190 CB GLN A 236 9.048 35.148 -5.451 1.00 75.59 C ANISOU 1190 CB GLN A 236 12519 6790 9413 797 -1709 -2618 C ATOM 1191 CG GLN A 236 9.454 36.570 -5.801 1.00 81.36 C ANISOU 1191 CG GLN A 236 13920 7338 9654 852 -1668 -2363 C ATOM 1192 CD GLN A 236 10.901 36.658 -6.244 1.00 81.20 C ANISOU 1192 CD GLN A 236 14298 7358 9198 463 -1472 -2402 C ATOM 1193 OE1 GLN A 236 11.370 35.831 -7.019 1.00 85.24 O ANISOU 1193 OE1 GLN A 236 14692 8099 9594 254 -1562 -2600 O ATOM 1194 NE2 GLN A 236 11.621 37.646 -5.733 1.00 81.56 N ANISOU 1194 NE2 GLN A 236 14801 7181 9008 347 -1182 -2234 N ATOM 1195 N ASP A 237 8.436 34.575 -2.327 1.00 79.66 N ANISOU 1195 N ASP A 237 12308 7021 10939 880 -1157 -2582 N ATOM 1196 CA ASP A 237 7.978 35.029 -1.002 1.00 91.31 C ANISOU 1196 CA ASP A 237 13693 8297 12705 1028 -936 -2452 C ATOM 1197 C ASP A 237 9.121 35.020 -0.004 1.00 74.44 C ANISOU 1197 C ASP A 237 11669 6102 10514 727 -536 -2423 C ATOM 1198 O ASP A 237 9.402 36.024 0.674 1.00 78.03 O ANISOU 1198 O ASP A 237 12461 6372 10816 721 -316 -2270 O ATOM 1199 CB ASP A 237 6.845 34.142 -0.470 1.00102.43 C ANISOU 1199 CB ASP A 237 14476 9765 14678 1205 -1015 -2563 C ATOM 1200 CG ASP A 237 5.542 34.327 -1.223 1.00115.51 C ANISOU 1200 CG ASP A 237 15973 11490 16424 1550 -1398 -2570 C ATOM 1201 OD1 ASP A 237 5.559 34.908 -2.329 1.00127.79 O ANISOU 1201 OD1 ASP A 237 17858 13101 17595 1638 -1648 -2511 O ATOM 1202 OD2 ASP A 237 4.494 33.889 -0.698 1.00115.94 O ANISOU 1202 OD2 ASP A 237 15560 11563 16927 1735 -1446 -2629 O ATOM 1203 N ASP A 238 9.739 33.844 0.072 1.00 71.89 N ANISOU 1203 N ASP A 238 11039 5949 10328 485 -443 -2581 N ATOM 1204 CA ASP A 238 10.976 33.568 0.800 1.00 74.92 C ANISOU 1204 CA ASP A 238 11458 6380 10626 175 -107 -2580 C ATOM 1205 C ASP A 238 12.001 34.675 0.554 1.00 73.43 C ANISOU 1205 C ASP A 238 11860 6137 9904 -12 20 -2475 C ATOM 1206 O ASP A 238 12.469 35.327 1.487 1.00 75.08 O ANISOU 1206 O ASP A 238 12254 6256 10018 -115 291 -2371 O ATOM 1207 CB ASP A 238 11.558 32.196 0.370 1.00 60.49 C ANISOU 1207 CB ASP A 238 9313 4757 8914 -27 -106 -2770 C ATOM 1208 CG ASP A 238 10.599 31.021 0.619 1.00 73.00 C ANISOU 1208 CG ASP A 238 10319 6372 11044 110 -185 -2897 C ATOM 1209 OD1 ASP A 238 9.766 31.088 1.542 1.00 85.05 O ANISOU 1209 OD1 ASP A 238 11614 7796 12907 288 -122 -2823 O ATOM 1210 OD2 ASP A 238 10.687 30.010 -0.107 1.00 76.10 O ANISOU 1210 OD2 ASP A 238 10488 6889 11537 20 -287 -3086 O ATOM 1211 N ILE A 239 12.322 34.894 -0.718 1.00 75.21 N ANISOU 1211 N ILE A 239 12384 6423 9771 -70 -171 -2515 N ATOM 1212 CA ILE A 239 13.297 35.905 -1.117 1.00 65.79 C ANISOU 1212 CA ILE A 239 11770 5176 8052 -272 -54 -2430 C ATOM 1213 C ILE A 239 12.895 37.274 -0.630 1.00 78.38 C ANISOU 1213 C ILE A 239 13753 6497 9531 -117 37 -2236 C ATOM 1214 O ILE A 239 13.677 37.967 0.030 1.00 95.22 O ANISOU 1214 O ILE A 239 16059 8638 11481 -318 322 -2123 O ATOM 1215 CB ILE A 239 13.473 35.926 -2.637 1.00 69.56 C ANISOU 1215 CB ILE A 239 12496 5751 8180 -304 -310 -2489 C ATOM 1216 CG1 ILE A 239 14.215 34.658 -3.074 1.00 76.90 C ANISOU 1216 CG1 ILE A 239 13130 6938 9150 -548 -298 -2704 C ATOM 1217 CG2 ILE A 239 14.199 37.168 -3.069 1.00 64.56 C ANISOU 1217 CG2 ILE A 239 12514 4997 7019 -444 -205 -2359 C ATOM 1218 CD1 ILE A 239 14.358 34.480 -4.564 1.00 70.57 C ANISOU 1218 CD1 ILE A 239 12500 6276 8036 -601 -545 -2812 C ATOM 1219 N ASN A 240 11.666 37.668 -0.929 1.00 85.69 N ANISOU 1219 N ASN A 240 14671 7289 10598 253 -204 -2151 N ATOM 1220 CA ASN A 240 11.191 38.971 -0.467 1.00 85.85 C ANISOU 1220 CA ASN A 240 15055 7010 10552 453 -103 -1960 C ATOM 1221 C ASN A 240 11.275 39.109 1.047 1.00 71.58 C ANISOU 1221 C ASN A 240 13113 5103 8983 379 233 -1944 C ATOM 1222 O ASN A 240 11.710 40.135 1.562 1.00 89.26 O ANISOU 1222 O ASN A 240 15652 7242 11020 267 481 -1813 O ATOM 1223 CB ASN A 240 9.761 39.211 -0.935 1.00 91.49 C ANISOU 1223 CB ASN A 240 15661 7642 11461 913 -425 -1872 C ATOM 1224 CG ASN A 240 9.655 39.293 -2.435 1.00 84.79 C ANISOU 1224 CG ASN A 240 15024 6899 10295 1004 -761 -1852 C ATOM 1225 OD1 ASN A 240 8.948 38.509 -3.060 1.00 91.56 O ANISOU 1225 OD1 ASN A 240 15502 7962 11326 1159 -1077 -1955 O ATOM 1226 ND2 ASN A 240 10.365 40.246 -3.025 1.00 90.46 N ANISOU 1226 ND2 ASN A 240 16354 7488 10529 888 -684 -1728 N ATOM 1227 N GLY A 241 10.866 38.065 1.756 1.00 79.69 N ANISOU 1227 N GLY A 241 13568 6267 10445 419 241 -2040 N ATOM 1228 CA GLY A 241 10.920 38.069 3.203 1.00 59.95 C ANISOU 1228 CA GLY A 241 10860 3746 8173 348 542 -2013 C ATOM 1229 C GLY A 241 12.318 38.311 3.730 1.00 55.93 C ANISOU 1229 C GLY A 241 10408 3484 7358 -47 804 -1951 C ATOM 1230 O GLY A 241 12.512 39.162 4.591 1.00 67.30 O ANISOU 1230 O GLY A 241 11967 4903 8701 -117 1019 -1835 O ATOM 1231 N ILE A 242 13.299 37.572 3.221 1.00 63.50 N ANISOU 1231 N ILE A 242 11277 4692 8157 -296 786 -2031 N ATOM 1232 CA ILE A 242 14.632 37.679 3.791 1.00 67.24 C ANISOU 1232 CA ILE A 242 11738 5438 8372 -632 1027 -1963 C ATOM 1233 C ILE A 242 15.293 38.962 3.315 1.00 80.16 C ANISOU 1233 C ILE A 242 13877 7030 9549 -787 1117 -1851 C ATOM 1234 O ILE A 242 16.082 39.577 4.045 1.00 78.70 O ANISOU 1234 O ILE A 242 13783 6960 9158 -1011 1364 -1761 O ATOM 1235 CB ILE A 242 15.518 36.463 3.452 1.00 62.96 C ANISOU 1235 CB ILE A 242 10903 5190 7828 -818 1005 -2056 C ATOM 1236 CG1 ILE A 242 16.619 36.332 4.503 1.00 65.28 C ANISOU 1236 CG1 ILE A 242 11039 5753 8011 -1074 1281 -1979 C ATOM 1237 CG2 ILE A 242 16.125 36.569 2.062 1.00 67.88 C ANISOU 1237 CG2 ILE A 242 11783 5885 8125 -931 872 -2098 C ATOM 1238 CD1 ILE A 242 16.079 35.939 5.865 1.00 57.23 C ANISOU 1238 CD1 ILE A 242 9707 4718 7318 -984 1419 -1954 C ATOM 1239 N GLN A 243 14.960 39.393 2.103 1.00 67.16 N ANISOU 1239 N GLN A 243 12586 5206 7728 -674 929 -1854 N ATOM 1240 CA GLN A 243 15.507 40.649 1.633 1.00 74.88 C ANISOU 1240 CA GLN A 243 14087 6087 8279 -805 1035 -1723 C ATOM 1241 C GLN A 243 14.833 41.829 2.337 1.00 71.85 C ANISOU 1241 C GLN A 243 13958 5415 7926 -647 1174 -1600 C ATOM 1242 O GLN A 243 15.439 42.893 2.479 1.00 73.78 O ANISOU 1242 O GLN A 243 14553 5613 7866 -829 1390 -1489 O ATOM 1243 CB GLN A 243 15.388 40.766 0.106 1.00 67.87 C ANISOU 1243 CB GLN A 243 13561 5087 7139 -729 796 -1742 C ATOM 1244 CG GLN A 243 16.407 39.891 -0.608 1.00 74.68 C ANISOU 1244 CG GLN A 243 14236 6284 7855 -983 749 -1835 C ATOM 1245 CD GLN A 243 16.489 40.127 -2.118 1.00 84.81 C ANISOU 1245 CD GLN A 243 15919 7510 8795 -979 551 -1841 C ATOM 1246 OE1 GLN A 243 15.638 40.795 -2.711 1.00 86.34 O ANISOU 1246 OE1 GLN A 243 16543 7391 8870 -730 380 -1793 O ATOM 1247 NE2 GLN A 243 17.523 39.563 -2.746 1.00 74.14 N ANISOU 1247 NE2 GLN A 243 14427 6462 7281 -1229 569 -1889 N ATOM 1248 N SER A 244 13.596 41.663 2.798 1.00 65.38 N ANISOU 1248 N SER A 244 12949 4407 7486 -315 1075 -1617 N ATOM 1249 CA SER A 244 12.965 42.777 3.503 1.00 68.22 C ANISOU 1249 CA SER A 244 13502 4518 7900 -154 1227 -1497 C ATOM 1250 C SER A 244 13.660 42.974 4.842 1.00 72.87 C ANISOU 1250 C SER A 244 13917 5305 8463 -434 1539 -1487 C ATOM 1251 O SER A 244 13.742 44.089 5.326 1.00 67.77 O ANISOU 1251 O SER A 244 13551 4537 7663 -492 1755 -1399 O ATOM 1252 CB SER A 244 11.472 42.556 3.713 1.00 67.81 C ANISOU 1252 CB SER A 244 13230 4250 8284 284 1056 -1504 C ATOM 1253 OG SER A 244 11.251 41.378 4.461 1.00 93.96 O ANISOU 1253 OG SER A 244 15980 7753 11967 279 1039 -1622 O ATOM 1254 N LEU A 245 14.184 41.896 5.422 1.00 77.61 N ANISOU 1254 N LEU A 245 14086 6210 9191 -607 1571 -1576 N ATOM 1255 CA LEU A 245 14.904 41.991 6.696 1.00 74.78 C ANISOU 1255 CA LEU A 245 13578 6070 8766 -872 1855 -1561 C ATOM 1256 C LEU A 245 16.339 42.494 6.558 1.00 70.41 C ANISOU 1256 C LEU A 245 13259 5718 7774 -1266 2048 -1518 C ATOM 1257 O LEU A 245 16.833 43.182 7.439 1.00 71.16 O ANISOU 1257 O LEU A 245 13448 5878 7713 -1478 2313 -1477 O ATOM 1258 CB LEU A 245 14.940 40.630 7.401 1.00 70.44 C ANISOU 1258 CB LEU A 245 12503 5757 8504 -887 1837 -1642 C ATOM 1259 CG LEU A 245 13.614 40.062 7.867 1.00 56.08 C ANISOU 1259 CG LEU A 245 10367 3789 7153 -557 1722 -1676 C ATOM 1260 CD1 LEU A 245 13.857 38.817 8.624 1.00 50.83 C ANISOU 1260 CD1 LEU A 245 9248 3361 6703 -637 1783 -1725 C ATOM 1261 CD2 LEU A 245 12.949 41.104 8.746 1.00 61.95 C ANISOU 1261 CD2 LEU A 245 11246 4348 7944 -449 1882 -1607 C ATOM 1262 N TYR A 246 17.015 42.126 5.471 1.00 70.54 N ANISOU 1262 N TYR A 246 13347 5848 7607 -1378 1925 -1533 N ATOM 1263 CA TYR A 246 18.465 42.330 5.366 1.00 76.57 C ANISOU 1263 CA TYR A 246 14199 6866 8028 -1765 2098 -1491 C ATOM 1264 C TYR A 246 18.921 43.067 4.089 1.00 88.62 C ANISOU 1264 C TYR A 246 16174 8276 9220 -1863 2064 -1423 C ATOM 1265 O TYR A 246 20.096 43.435 3.965 1.00 85.02 O ANISOU 1265 O TYR A 246 15829 7976 8498 -2196 2231 -1364 O ATOM 1266 CB TYR A 246 19.187 40.969 5.467 1.00 80.27 C ANISOU 1266 CB TYR A 246 14214 7683 8600 -1885 2048 -1563 C ATOM 1267 CG TYR A 246 18.937 40.262 6.784 1.00 72.73 C ANISOU 1267 CG TYR A 246 12865 6855 7912 -1850 2143 -1607 C ATOM 1268 CD1 TYR A 246 19.302 40.845 7.990 1.00 68.54 C ANISOU 1268 CD1 TYR A 246 12347 6404 7290 -2046 2410 -1563 C ATOM 1269 CD2 TYR A 246 18.326 39.025 6.822 1.00 60.91 C ANISOU 1269 CD2 TYR A 246 11000 5383 6760 -1641 1984 -1694 C ATOM 1270 CE1 TYR A 246 19.058 40.203 9.209 1.00 70.95 C ANISOU 1270 CE1 TYR A 246 12319 6823 7814 -2025 2515 -1603 C ATOM 1271 CE2 TYR A 246 18.073 38.388 8.024 1.00 51.70 C ANISOU 1271 CE2 TYR A 246 9501 4303 5840 -1611 2101 -1718 C ATOM 1272 CZ TYR A 246 18.444 38.974 9.215 1.00 61.80 C ANISOU 1272 CZ TYR A 246 10812 5674 6994 -1801 2367 -1672 C ATOM 1273 OH TYR A 246 18.183 38.315 10.412 1.00 62.74 O ANISOU 1273 OH TYR A 246 10612 5883 7344 -1780 2501 -1700 O ATOM 1274 N GLY A 247 18.001 43.281 3.147 1.00 95.00 N ANISOU 1274 N GLY A 247 17243 8799 10053 -1582 1852 -1422 N ATOM 1275 CA GLY A 247 18.279 44.080 1.960 1.00 99.81 C ANISOU 1275 CA GLY A 247 18368 9237 10318 -1640 1830 -1340 C ATOM 1276 C GLY A 247 19.375 43.549 1.052 1.00 93.73 C ANISOU 1276 C GLY A 247 17546 8721 9347 -1890 1781 -1354 C ATOM 1277 O GLY A 247 19.555 42.339 0.924 1.00 97.98 O ANISOU 1277 O GLY A 247 17657 9511 10061 -1878 1638 -1460 O TER 1278 GLY A 247 ATOM 1279 N CYS B 1 9.428 25.805 12.300 1.00 59.29 N ANISOU 1279 N CYS B 1 8454 6427 7646 -1696 -794 -2436 N ATOM 1280 CA CYS B 1 8.670 24.629 12.694 1.00 58.14 C ANISOU 1280 CA CYS B 1 8404 6264 7422 -1456 -857 -2244 C ATOM 1281 C CYS B 1 8.200 23.922 11.469 1.00 63.56 C ANISOU 1281 C CYS B 1 9071 6872 8209 -1437 -694 -2123 C ATOM 1282 O CYS B 1 7.501 24.523 10.655 1.00 61.80 O ANISOU 1282 O CYS B 1 8971 6519 7992 -1551 -517 -2072 O ATOM 1283 CB CYS B 1 7.460 24.973 13.552 1.00 57.31 C ANISOU 1283 CB CYS B 1 8586 6070 7120 -1392 -839 -2123 C ATOM 1284 SG CYS B 1 6.387 23.529 13.903 1.00 60.65 S ANISOU 1284 SG CYS B 1 9159 6447 7437 -1166 -835 -1898 S ATOM 1285 N THR B 2 8.570 22.646 11.358 1.00 65.34 N ANISOU 1285 N THR B 2 9166 7159 8501 -1282 -776 -2080 N ATOM 1286 CA THR B 2 8.224 21.817 10.204 1.00 58.63 C ANISOU 1286 CA THR B 2 8288 6241 7746 -1254 -635 -1972 C ATOM 1287 C THR B 2 7.413 20.583 10.593 1.00 60.61 C ANISOU 1287 C THR B 2 8675 6451 7902 -1043 -685 -1777 C ATOM 1288 O THR B 2 7.817 19.802 11.450 1.00 63.69 O ANISOU 1288 O THR B 2 9058 6907 8234 -876 -876 -1772 O ATOM 1289 CB THR B 2 9.483 21.344 9.441 1.00 62.46 C ANISOU 1289 CB THR B 2 8478 6821 8433 -1289 -636 -2125 C ATOM 1290 OG1 THR B 2 10.126 22.463 8.820 1.00 73.17 O ANISOU 1290 OG1 THR B 2 9737 8187 9879 -1550 -506 -2307 O ATOM 1291 CG2 THR B 2 9.099 20.353 8.364 1.00 56.47 C ANISOU 1291 CG2 THR B 2 7723 5985 7747 -1235 -506 -2001 C ATOM 1292 N CYS B 3 6.275 20.412 9.930 1.00 56.77 N ANISOU 1292 N CYS B 3 8330 5843 7396 -1057 -520 -1629 N ATOM 1293 CA CYS B 3 5.318 19.378 10.279 1.00 60.89 C ANISOU 1293 CA CYS B 3 9007 6312 7815 -912 -515 -1455 C ATOM 1294 C CYS B 3 5.091 18.327 9.185 1.00 51.73 C ANISOU 1294 C CYS B 3 7811 5093 6751 -871 -421 -1354 C ATOM 1295 O CYS B 3 5.299 18.578 7.993 1.00 61.87 O ANISOU 1295 O CYS B 3 9005 6338 8163 -979 -307 -1389 O ATOM 1296 CB CYS B 3 3.978 20.032 10.618 1.00 50.13 C ANISOU 1296 CB CYS B 3 7838 4865 6345 -955 -405 -1389 C ATOM 1297 SG CYS B 3 4.015 21.079 12.044 1.00 80.59 S ANISOU 1297 SG CYS B 3 11802 8769 10049 -981 -496 -1484 S ATOM 1298 N VAL B 4 4.653 17.150 9.595 1.00 58.15 N ANISOU 1298 N VAL B 4 8732 5882 7479 -731 -461 -1228 N ATOM 1299 CA VAL B 4 3.937 16.277 8.670 1.00 67.03 C ANISOU 1299 CA VAL B 4 9902 6917 8648 -716 -334 -1101 C ATOM 1300 C VAL B 4 2.529 16.218 9.231 1.00 50.25 C ANISOU 1300 C VAL B 4 7978 4727 6389 -719 -246 -996 C ATOM 1301 O VAL B 4 2.307 15.693 10.310 1.00 54.89 O ANISOU 1301 O VAL B 4 8713 5322 6820 -644 -307 -948 O ATOM 1302 CB VAL B 4 4.573 14.887 8.536 1.00 67.80 C ANISOU 1302 CB VAL B 4 9964 7023 8773 -572 -423 -1058 C ATOM 1303 CG1 VAL B 4 4.921 14.327 9.905 1.00 82.73 C ANISOU 1303 CG1 VAL B 4 11977 8950 10508 -419 -625 -1047 C ATOM 1304 CG2 VAL B 4 3.658 13.933 7.741 1.00 53.04 C ANISOU 1304 CG2 VAL B 4 8197 5047 6910 -564 -287 -911 C ATOM 1305 N PRO B 5 1.584 16.855 8.543 1.00 68.00 N ANISOU 1305 N PRO B 5 10238 6905 8693 -814 -108 -986 N ATOM 1306 CA PRO B 5 0.225 16.909 9.080 1.00 67.78 C ANISOU 1306 CA PRO B 5 10341 6835 8579 -822 -13 -942 C ATOM 1307 C PRO B 5 -0.305 15.501 9.115 1.00 57.61 C ANISOU 1307 C PRO B 5 9145 5510 7233 -768 38 -822 C ATOM 1308 O PRO B 5 0.172 14.672 8.359 1.00 69.89 O ANISOU 1308 O PRO B 5 10655 7043 8855 -730 18 -766 O ATOM 1309 CB PRO B 5 -0.521 17.768 8.068 1.00 75.45 C ANISOU 1309 CB PRO B 5 11271 7726 9669 -900 75 -976 C ATOM 1310 CG PRO B 5 0.197 17.482 6.785 1.00 84.49 C ANISOU 1310 CG PRO B 5 12336 8834 10932 -930 69 -957 C ATOM 1311 CD PRO B 5 1.652 17.352 7.161 1.00 81.42 C ANISOU 1311 CD PRO B 5 11856 8542 10537 -908 -33 -1014 C ATOM 1312 N PRO B 6 -1.225 15.206 10.023 1.00 55.39 N ANISOU 1312 N PRO B 6 9008 5218 6820 -777 116 -796 N ATOM 1313 CA PRO B 6 -1.654 13.807 10.044 1.00 52.96 C ANISOU 1313 CA PRO B 6 8825 4859 6438 -754 176 -685 C ATOM 1314 C PRO B 6 -3.003 13.632 9.383 1.00 59.35 C ANISOU 1314 C PRO B 6 9603 5615 7331 -832 350 -673 C ATOM 1315 O PRO B 6 -3.725 14.605 9.192 1.00 63.92 O ANISOU 1315 O PRO B 6 10089 6197 7999 -881 411 -763 O ATOM 1316 CB PRO B 6 -1.743 13.498 11.533 1.00 52.16 C ANISOU 1316 CB PRO B 6 8953 4766 6101 -746 164 -675 C ATOM 1317 CG PRO B 6 -2.155 14.819 12.134 1.00 59.00 C ANISOU 1317 CG PRO B 6 9783 5678 6955 -808 211 -793 C ATOM 1318 CD PRO B 6 -1.581 15.922 11.256 1.00 47.82 C ANISOU 1318 CD PRO B 6 8148 4294 5727 -805 134 -868 C ATOM 1319 N HIS B 7 -3.343 12.397 9.048 1.00 51.69 N ANISOU 1319 N HIS B 7 8714 4589 6338 -837 412 -577 N ATOM 1320 CA HIS B 7 -4.659 12.106 8.550 1.00 45.61 C ANISOU 1320 CA HIS B 7 7912 3777 5640 -923 573 -585 C ATOM 1321 C HIS B 7 -5.643 12.416 9.646 1.00 56.88 C ANISOU 1321 C HIS B 7 9409 5235 6969 -1006 717 -671 C ATOM 1322 O HIS B 7 -5.291 12.367 10.823 1.00 57.82 O ANISOU 1322 O HIS B 7 9699 5373 6897 -1005 706 -668 O ATOM 1323 CB HIS B 7 -4.749 10.648 8.126 1.00 45.64 C ANISOU 1323 CB HIS B 7 8027 3711 5605 -930 616 -467 C ATOM 1324 CG HIS B 7 -5.925 10.340 7.259 1.00 46.66 C ANISOU 1324 CG HIS B 7 8073 3798 5859 -1016 744 -483 C ATOM 1325 ND1 HIS B 7 -7.135 9.919 7.767 1.00 56.09 N ANISOU 1325 ND1 HIS B 7 9320 4989 7004 -1135 926 -530 N ATOM 1326 CD2 HIS B 7 -6.080 10.387 5.912 1.00 44.53 C ANISOU 1326 CD2 HIS B 7 7674 3485 5761 -1012 711 -475 C ATOM 1327 CE1 HIS B 7 -7.980 9.701 6.771 1.00 57.52 C ANISOU 1327 CE1 HIS B 7 9374 5139 7342 -1187 981 -558 C ATOM 1328 NE2 HIS B 7 -7.365 9.988 5.637 1.00 51.87 N ANISOU 1328 NE2 HIS B 7 8567 4390 6751 -1106 839 -515 N ATOM 1329 N PRO B 8 -6.874 12.775 9.275 1.00 64.57 N ANISOU 1329 N PRO B 8 10250 6211 8074 -1075 844 -771 N ATOM 1330 CA PRO B 8 -7.947 12.943 10.267 1.00 58.88 C ANISOU 1330 CA PRO B 8 9562 5524 7286 -1176 1036 -893 C ATOM 1331 C PRO B 8 -8.111 11.722 11.170 1.00 71.58 C ANISOU 1331 C PRO B 8 11435 7101 8662 -1278 1179 -823 C ATOM 1332 O PRO B 8 -8.319 11.886 12.375 1.00 73.43 O ANISOU 1332 O PRO B 8 11827 7353 8721 -1350 1289 -884 O ATOM 1333 CB PRO B 8 -9.181 13.149 9.400 1.00 61.12 C ANISOU 1333 CB PRO B 8 9621 5804 7797 -1213 1119 -1009 C ATOM 1334 CG PRO B 8 -8.625 13.887 8.187 1.00 61.67 C ANISOU 1334 CG PRO B 8 9560 5838 8035 -1099 912 -982 C ATOM 1335 CD PRO B 8 -7.236 13.332 7.960 1.00 59.58 C ANISOU 1335 CD PRO B 8 9419 5549 7669 -1046 786 -814 C ATOM 1336 N GLN B 9 -8.011 10.520 10.607 1.00 55.42 N ANISOU 1336 N GLN B 9 9479 4987 6591 -1294 1182 -699 N ATOM 1337 CA GLN B 9 -8.153 9.331 11.424 1.00 59.54 C ANISOU 1337 CA GLN B 9 10317 5441 6866 -1397 1309 -625 C ATOM 1338 C GLN B 9 -7.082 9.343 12.474 1.00 52.41 C ANISOU 1338 C GLN B 9 9676 4515 5721 -1315 1166 -552 C ATOM 1339 O GLN B 9 -7.376 9.272 13.659 1.00 58.56 O ANISOU 1339 O GLN B 9 10701 5274 6276 -1416 1286 -588 O ATOM 1340 CB GLN B 9 -8.058 8.054 10.594 1.00 62.41 C ANISOU 1340 CB GLN B 9 10762 5715 7237 -1400 1295 -492 C ATOM 1341 CG GLN B 9 -8.275 6.821 11.425 1.00 78.67 C ANISOU 1341 CG GLN B 9 13204 7669 9019 -1523 1433 -418 C ATOM 1342 CD GLN B 9 -8.533 5.604 10.591 1.00 74.96 C ANISOU 1342 CD GLN B 9 12801 7105 8574 -1574 1483 -325 C ATOM 1343 OE1 GLN B 9 -9.146 5.685 9.528 1.00 73.46 O ANISOU 1343 OE1 GLN B 9 12344 6949 8618 -1608 1527 -376 O ATOM 1344 NE2 GLN B 9 -8.061 4.464 11.060 1.00 74.14 N ANISOU 1344 NE2 GLN B 9 13083 6866 8221 -1572 1455 -190 N ATOM 1345 N THR B 10 -5.836 9.462 12.021 1.00 51.29 N ANISOU 1345 N THR B 10 9479 4377 5631 -1138 909 -470 N ATOM 1346 CA THR B 10 -4.673 9.564 12.904 1.00 53.38 C ANISOU 1346 CA THR B 10 9928 4638 5718 -1021 704 -428 C ATOM 1347 C THR B 10 -4.811 10.705 13.925 1.00 54.02 C ANISOU 1347 C THR B 10 10021 4786 5717 -1064 732 -546 C ATOM 1348 O THR B 10 -4.353 10.591 15.063 1.00 56.45 O ANISOU 1348 O THR B 10 10609 5061 5777 -1048 655 -527 O ATOM 1349 CB THR B 10 -3.389 9.788 12.078 1.00 63.60 C ANISOU 1349 CB THR B 10 11024 5967 7174 -843 451 -395 C ATOM 1350 OG1 THR B 10 -3.302 8.784 11.056 1.00 65.40 O ANISOU 1350 OG1 THR B 10 11228 6130 7492 -807 447 -303 O ATOM 1351 CG2 THR B 10 -2.130 9.776 12.964 1.00 52.38 C ANISOU 1351 CG2 THR B 10 9758 4548 5596 -702 201 -379 C ATOM 1352 N ALA B 11 -5.431 11.804 13.519 1.00 52.09 N ANISOU 1352 N ALA B 11 9500 4621 5669 -1107 824 -671 N ATOM 1353 CA ALA B 11 -5.638 12.899 14.448 1.00 61.68 C ANISOU 1353 CA ALA B 11 10726 5891 6818 -1148 870 -796 C ATOM 1354 C ALA B 11 -6.522 12.375 15.571 1.00 68.33 C ANISOU 1354 C ALA B 11 11851 6688 7422 -1310 1109 -834 C ATOM 1355 O ALA B 11 -6.172 12.455 16.745 1.00 70.66 O ANISOU 1355 O ALA B 11 12423 6959 7464 -1331 1081 -835 O ATOM 1356 CB ALA B 11 -6.267 14.097 13.768 1.00 51.77 C ANISOU 1356 CB ALA B 11 9152 4698 5818 -1152 926 -934 C ATOM 1357 N PHE B 12 -7.648 11.792 15.188 1.00 55.51 N ANISOU 1357 N PHE B 12 10175 5047 5870 -1441 1347 -871 N ATOM 1358 CA PHE B 12 -8.611 11.298 16.147 1.00 57.95 C ANISOU 1358 CA PHE B 12 10724 5316 5977 -1649 1642 -944 C ATOM 1359 C PHE B 12 -7.994 10.278 17.076 1.00 71.95 C ANISOU 1359 C PHE B 12 12989 6965 7384 -1680 1591 -799 C ATOM 1360 O PHE B 12 -8.034 10.430 18.287 1.00 67.64 O ANISOU 1360 O PHE B 12 12745 6382 6573 -1771 1673 -841 O ATOM 1361 CB PHE B 12 -9.809 10.681 15.437 1.00 57.98 C ANISOU 1361 CB PHE B 12 10566 5321 6142 -1791 1883 -1010 C ATOM 1362 CG PHE B 12 -10.828 10.111 16.383 1.00 74.92 C ANISOU 1362 CG PHE B 12 12948 7430 8088 -2054 2238 -1115 C ATOM 1363 CD1 PHE B 12 -10.834 8.762 16.694 1.00 65.47 C ANISOU 1363 CD1 PHE B 12 12135 6104 6637 -2188 2338 -992 C ATOM 1364 CD2 PHE B 12 -11.770 10.929 16.975 1.00 75.89 C ANISOU 1364 CD2 PHE B 12 12932 7634 8268 -2179 2486 -1353 C ATOM 1365 CE1 PHE B 12 -11.753 8.248 17.577 1.00 75.88 C ANISOU 1365 CE1 PHE B 12 13715 7371 7744 -2474 2698 -1099 C ATOM 1366 CE2 PHE B 12 -12.699 10.411 17.857 1.00 83.00 C ANISOU 1366 CE2 PHE B 12 14049 8503 8983 -2458 2859 -1480 C ATOM 1367 CZ PHE B 12 -12.690 9.065 18.156 1.00 77.80 C ANISOU 1367 CZ PHE B 12 13796 7712 8053 -2623 2976 -1350 C ATOM 1368 N CYS B 13 -7.416 9.234 16.496 1.00 67.68 N ANISOU 1368 N CYS B 13 12556 6340 6818 -1596 1443 -633 N ATOM 1369 CA CYS B 13 -6.918 8.124 17.285 1.00 61.39 C ANISOU 1369 CA CYS B 13 12267 5386 5672 -1607 1374 -494 C ATOM 1370 C CYS B 13 -5.863 8.514 18.308 1.00 66.54 C ANISOU 1370 C CYS B 13 13178 6009 6095 -1478 1116 -460 C ATOM 1371 O CYS B 13 -5.806 7.932 19.395 1.00 73.71 O ANISOU 1371 O CYS B 13 14586 6780 6642 -1554 1133 -410 O ATOM 1372 CB CYS B 13 -6.368 7.046 16.354 1.00 60.37 C ANISOU 1372 CB CYS B 13 12155 5176 5607 -1483 1210 -337 C ATOM 1373 SG CYS B 13 -7.722 6.132 15.632 1.00 83.22 S ANISOU 1373 SG CYS B 13 15003 8028 8590 -1716 1553 -357 S ATOM 1374 N ASN B 14 -5.027 9.485 17.952 1.00 62.16 N ANISOU 1374 N ASN B 14 12310 5570 5737 -1294 872 -493 N ATOM 1375 CA ASN B 14 -3.869 9.819 18.769 1.00 63.58 C ANISOU 1375 CA ASN B 14 12675 5736 5747 -1143 566 -470 C ATOM 1376 C ASN B 14 -4.089 11.077 19.573 1.00 64.28 C ANISOU 1376 C ASN B 14 12726 5908 5790 -1217 637 -610 C ATOM 1377 O ASN B 14 -3.180 11.541 20.260 1.00 63.73 O ANISOU 1377 O ASN B 14 12771 5846 5599 -1109 387 -619 O ATOM 1378 CB ASN B 14 -2.622 9.985 17.902 1.00 68.41 C ANISOU 1378 CB ASN B 14 12984 6417 6593 -901 234 -433 C ATOM 1379 CG ASN B 14 -2.247 8.706 17.156 1.00 79.25 C ANISOU 1379 CG ASN B 14 14415 7697 7999 -794 131 -303 C ATOM 1380 OD1 ASN B 14 -2.716 7.612 17.485 1.00 91.11 O ANISOU 1380 OD1 ASN B 14 16283 9052 9284 -873 235 -214 O ATOM 1381 ND2 ASN B 14 -1.389 8.844 16.145 1.00 58.43 N ANISOU 1381 ND2 ASN B 14 11438 5136 5629 -629 -58 -304 N ATOM 1382 N SER B 15 -5.286 11.646 19.475 1.00 62.32 N ANISOU 1382 N SER B 15 12300 5723 5656 -1391 965 -738 N ATOM 1383 CA SER B 15 -5.651 12.773 20.337 1.00 67.99 C ANISOU 1383 CA SER B 15 13028 6498 6306 -1479 1083 -890 C ATOM 1384 C SER B 15 -6.335 12.271 21.615 1.00 73.41 C ANISOU 1384 C SER B 15 14198 7074 6622 -1693 1335 -920 C ATOM 1385 O SER B 15 -7.093 11.295 21.580 1.00 67.56 O ANISOU 1385 O SER B 15 13631 6252 5788 -1851 1575 -893 O ATOM 1386 CB SER B 15 -6.574 13.748 19.603 1.00 66.01 C ANISOU 1386 CB SER B 15 12328 6368 6386 -1527 1285 -1051 C ATOM 1387 OG SER B 15 -5.918 14.420 18.536 1.00 59.07 O ANISOU 1387 OG SER B 15 11076 5568 5800 -1357 1058 -1038 O ATOM 1388 N ASP B 16 -6.069 12.929 22.740 1.00 69.84 N ANISOU 1388 N ASP B 16 13987 6607 5941 -1721 1296 -985 N ATOM 1389 CA ASP B 16 -6.806 12.620 23.974 1.00 85.67 C ANISOU 1389 CA ASP B 16 16464 8504 7583 -1964 1591 -1048 C ATOM 1390 C ASP B 16 -8.193 13.279 23.950 1.00 74.18 C ANISOU 1390 C ASP B 16 14740 7145 6298 -2168 2032 -1276 C ATOM 1391 O ASP B 16 -9.187 12.718 24.414 1.00 76.89 O ANISOU 1391 O ASP B 16 15299 7427 6487 -2422 2407 -1358 O ATOM 1392 CB ASP B 16 -6.031 13.083 25.214 1.00 73.84 C ANISOU 1392 CB ASP B 16 15359 6942 5756 -1928 1385 -1045 C ATOM 1393 CG ASP B 16 -4.616 12.534 25.267 1.00 74.04 C ANISOU 1393 CG ASP B 16 15594 6885 5650 -1689 897 -866 C ATOM 1394 OD1 ASP B 16 -4.432 11.314 25.056 1.00 75.18 O ANISOU 1394 OD1 ASP B 16 15980 6904 5679 -1655 816 -720 O ATOM 1395 OD2 ASP B 16 -3.681 13.332 25.506 1.00 73.78 O ANISOU 1395 OD2 ASP B 16 15471 6916 5646 -1531 587 -891 O ATOM 1396 N LEU B 17 -8.237 14.482 23.395 1.00 77.63 N ANISOU 1396 N LEU B 17 14706 7727 7062 -2053 1977 -1397 N ATOM 1397 CA LEU B 17 -9.452 15.277 23.342 1.00 70.17 C ANISOU 1397 CA LEU B 17 13457 6878 6326 -2174 2318 -1643 C ATOM 1398 C LEU B 17 -9.822 15.590 21.903 1.00 80.37 C ANISOU 1398 C LEU B 17 14193 8275 8070 -2050 2275 -1685 C ATOM 1399 O LEU B 17 -8.968 16.027 21.136 1.00 79.71 O ANISOU 1399 O LEU B 17 13896 8227 8162 -1842 1954 -1588 O ATOM 1400 CB LEU B 17 -9.247 16.575 24.120 1.00 70.96 C ANISOU 1400 CB LEU B 17 13573 7019 6369 -2144 2285 -1779 C ATOM 1401 CG LEU B 17 -9.053 16.387 25.619 1.00 74.24 C ANISOU 1401 CG LEU B 17 14563 7324 6321 -2297 2368 -1778 C ATOM 1402 CD1 LEU B 17 -8.756 17.715 26.301 1.00 76.17 C ANISOU 1402 CD1 LEU B 17 14806 7611 6525 -2248 2296 -1906 C ATOM 1403 CD2 LEU B 17 -10.306 15.759 26.180 1.00 77.06 C ANISOU 1403 CD2 LEU B 17 15122 7632 6527 -2598 2857 -1917 C ATOM 1404 N VAL B 18 -11.076 15.345 21.525 1.00 75.52 N ANISOU 1404 N VAL B 18 13358 7701 7636 -2187 2593 -1839 N ATOM 1405 CA VAL B 18 -11.578 15.804 20.232 1.00 65.73 C ANISOU 1405 CA VAL B 18 11600 6550 6824 -2065 2545 -1924 C ATOM 1406 C VAL B 18 -12.916 16.488 20.448 1.00 67.50 C ANISOU 1406 C VAL B 18 11561 6852 7235 -2170 2869 -2241 C ATOM 1407 O VAL B 18 -13.902 15.863 20.832 1.00 77.89 O ANISOU 1407 O VAL B 18 12920 8173 8504 -2394 3224 -2382 O ATOM 1408 CB VAL B 18 -11.736 14.671 19.192 1.00 73.81 C ANISOU 1408 CB VAL B 18 12526 7550 7971 -2072 2522 -1796 C ATOM 1409 CG1 VAL B 18 -12.356 15.225 17.933 1.00 70.98 C ANISOU 1409 CG1 VAL B 18 11670 7268 8031 -1956 2472 -1912 C ATOM 1410 CG2 VAL B 18 -10.393 14.022 18.864 1.00 64.02 C ANISOU 1410 CG2 VAL B 18 11491 6236 6596 -1931 2188 -1510 C ATOM 1411 N ILE B 19 -12.922 17.791 20.210 1.00 67.51 N ANISOU 1411 N ILE B 19 11293 6907 7450 -2007 2744 -2371 N ATOM 1412 CA ILE B 19 -14.058 18.636 20.502 1.00 76.87 C ANISOU 1412 CA ILE B 19 12227 8159 8820 -2048 2996 -2697 C ATOM 1413 C ILE B 19 -14.344 19.599 19.372 1.00 78.73 C ANISOU 1413 C ILE B 19 12024 8435 9457 -1817 2791 -2805 C ATOM 1414 O ILE B 19 -13.516 19.836 18.506 1.00 68.03 O ANISOU 1414 O ILE B 19 10616 7046 8185 -1640 2455 -2621 O ATOM 1415 CB ILE B 19 -13.825 19.480 21.750 1.00 81.64 C ANISOU 1415 CB ILE B 19 13068 8751 9199 -2090 3078 -2799 C ATOM 1416 CG1 ILE B 19 -12.784 20.571 21.434 1.00 72.28 C ANISOU 1416 CG1 ILE B 19 11845 7551 8068 -1854 2695 -2696 C ATOM 1417 CG2 ILE B 19 -13.417 18.595 22.912 1.00 81.98 C ANISOU 1417 CG2 ILE B 19 13638 8719 8791 -2304 3223 -2672 C ATOM 1418 CD1 ILE B 19 -12.423 21.465 22.583 1.00 69.75 C ANISOU 1418 CD1 ILE B 19 11762 7211 7528 -1877 2717 -2778 C ATOM 1419 N ARG B 20 -15.529 20.178 19.422 1.00 84.20 N ANISOU 1419 N ARG B 20 12420 9186 10386 -1823 2999 -3126 N ATOM 1420 CA ARG B 20 -15.907 21.231 18.515 1.00 78.60 C ANISOU 1420 CA ARG B 20 11343 8485 10036 -1585 2795 -3275 C ATOM 1421 C ARG B 20 -16.166 22.478 19.364 1.00 85.73 C ANISOU 1421 C ARG B 20 12238 9395 10939 -1534 2885 -3516 C ATOM 1422 O ARG B 20 -16.901 22.417 20.351 1.00 85.41 O ANISOU 1422 O ARG B 20 12225 9405 10824 -1705 3244 -3747 O ATOM 1423 CB ARG B 20 -17.127 20.800 17.716 1.00 83.74 C ANISOU 1423 CB ARG B 20 11610 9192 11017 -1590 2906 -3476 C ATOM 1424 CG ARG B 20 -17.883 21.922 17.060 1.00103.18 C ANISOU 1424 CG ARG B 20 13689 11658 13856 -1355 2763 -3745 C ATOM 1425 CD ARG B 20 -19.101 21.409 16.285 1.00105.20 C ANISOU 1425 CD ARG B 20 13547 11977 14448 -1358 2844 -3965 C ATOM 1426 NE ARG B 20 -19.481 20.036 16.596 1.00 98.48 N ANISOU 1426 NE ARG B 20 12751 11188 13478 -1647 3163 -3944 N ATOM 1427 CZ ARG B 20 -20.491 19.414 16.002 1.00111.90 C ANISOU 1427 CZ ARG B 20 14129 12952 15436 -1710 3271 -4127 C ATOM 1428 NH1 ARG B 20 -21.215 20.069 15.106 1.00109.71 N ANISOU 1428 NH1 ARG B 20 13447 12687 15550 -1478 3060 -4352 N ATOM 1429 NH2 ARG B 20 -20.799 18.159 16.314 1.00125.58 N ANISOU 1429 NH2 ARG B 20 15957 14726 17033 -2005 3579 -4104 N ATOM 1430 N ALA B 21 -15.536 23.596 19.003 1.00 70.65 N ANISOU 1430 N ALA B 21 10324 7425 9093 -1322 2579 -3468 N ATOM 1431 CA ALA B 21 -15.515 24.778 19.863 1.00 77.77 C ANISOU 1431 CA ALA B 21 11310 8308 9930 -1275 2623 -3640 C ATOM 1432 C ALA B 21 -15.286 26.072 19.087 1.00 75.02 C ANISOU 1432 C ALA B 21 10835 7879 9792 -1010 2294 -3678 C ATOM 1433 O ALA B 21 -14.831 26.031 17.944 1.00 77.00 O ANISOU 1433 O ALA B 21 11025 8073 10157 -888 2004 -3503 O ATOM 1434 CB ALA B 21 -14.443 24.618 20.920 1.00 79.52 C ANISOU 1434 CB ALA B 21 11963 8508 9744 -1413 2635 -3444 C ATOM 1435 N LYS B 22 -15.597 27.212 19.710 1.00 75.28 N ANISOU 1435 N LYS B 22 10863 7886 9855 -935 2349 -3911 N ATOM 1436 CA LYS B 22 -15.362 28.524 19.096 1.00 73.51 C ANISOU 1436 CA LYS B 22 10597 7548 9784 -694 2043 -3956 C ATOM 1437 C LYS B 22 -14.328 29.328 19.855 1.00 72.75 C ANISOU 1437 C LYS B 22 10826 7396 9420 -723 1955 -3859 C ATOM 1438 O LYS B 22 -14.423 29.470 21.069 1.00 91.90 O ANISOU 1438 O LYS B 22 13402 9860 11656 -846 2191 -3975 O ATOM 1439 CB LYS B 22 -16.637 29.359 19.029 1.00 82.12 C ANISOU 1439 CB LYS B 22 11389 8623 11188 -520 2114 -4346 C ATOM 1440 CG LYS B 22 -17.886 28.648 18.564 1.00 89.65 C ANISOU 1440 CG LYS B 22 11964 9664 12434 -510 2267 -4558 C ATOM 1441 CD LYS B 22 -19.049 29.642 18.541 1.00 85.08 C ANISOU 1441 CD LYS B 22 11076 9062 12187 -291 2283 -4983 C ATOM 1442 CE LYS B 22 -20.373 28.973 18.831 1.00 87.28 C ANISOU 1442 CE LYS B 22 10986 9489 12687 -389 2635 -5320 C ATOM 1443 NZ LYS B 22 -21.475 29.968 18.965 1.00 88.44 N ANISOU 1443 NZ LYS B 22 10809 9628 13165 -168 2672 -5783 N ATOM 1444 N PHE B 23 -13.364 29.888 19.135 1.00 68.99 N ANISOU 1444 N PHE B 23 10465 6822 8927 -624 1626 -3670 N ATOM 1445 CA PHE B 23 -12.370 30.756 19.743 1.00 67.65 C ANISOU 1445 CA PHE B 23 10574 6594 8537 -651 1514 -3603 C ATOM 1446 C PHE B 23 -13.002 32.079 20.163 1.00 80.45 C ANISOU 1446 C PHE B 23 12178 8135 10254 -522 1549 -3894 C ATOM 1447 O PHE B 23 -13.588 32.770 19.333 1.00 72.35 O ANISOU 1447 O PHE B 23 10994 7009 9489 -318 1400 -4030 O ATOM 1448 CB PHE B 23 -11.224 30.991 18.769 1.00 65.09 C ANISOU 1448 CB PHE B 23 10347 6187 8196 -609 1185 -3360 C ATOM 1449 CG PHE B 23 -10.368 29.806 18.576 1.00 63.10 C ANISOU 1449 CG PHE B 23 10156 6014 7806 -738 1145 -3088 C ATOM 1450 CD1 PHE B 23 -9.169 29.695 19.242 1.00 67.38 C ANISOU 1450 CD1 PHE B 23 10927 6589 8083 -858 1079 -2934 C ATOM 1451 CD2 PHE B 23 -10.754 28.791 17.736 1.00 61.96 C ANISOU 1451 CD2 PHE B 23 9837 5903 7800 -727 1156 -3001 C ATOM 1452 CE1 PHE B 23 -8.372 28.597 19.073 1.00 61.13 C ANISOU 1452 CE1 PHE B 23 10182 5862 7182 -942 1016 -2707 C ATOM 1453 CE2 PHE B 23 -9.953 27.694 17.558 1.00 68.12 C ANISOU 1453 CE2 PHE B 23 10686 6742 8455 -828 1114 -2759 C ATOM 1454 CZ PHE B 23 -8.762 27.597 18.228 1.00 59.94 C ANISOU 1454 CZ PHE B 23 9871 5736 7168 -924 1040 -2617 C ATOM 1455 N VAL B 24 -12.897 32.433 21.442 1.00 83.70 N ANISOU 1455 N VAL B 24 12896 9415 9492 -1625 1676 -2348 N ATOM 1456 CA VAL B 24 -13.525 33.662 21.924 1.00 82.80 C ANISOU 1456 CA VAL B 24 12862 9244 9356 -1425 1470 -2411 C ATOM 1457 C VAL B 24 -12.543 34.604 22.589 1.00 74.43 C ANISOU 1457 C VAL B 24 12019 7963 8297 -1324 1168 -2332 C ATOM 1458 O VAL B 24 -12.566 34.807 23.791 1.00 90.60 O ANISOU 1458 O VAL B 24 14232 9929 10264 -1128 1147 -2420 O ATOM 1459 CB VAL B 24 -14.676 33.372 22.914 1.00 83.56 C ANISOU 1459 CB VAL B 24 12963 9413 9371 -1262 1701 -2583 C ATOM 1460 CG1 VAL B 24 -15.913 32.891 22.167 1.00 77.84 C ANISOU 1460 CG1 VAL B 24 11962 8915 8700 -1347 1908 -2726 C ATOM 1461 CG2 VAL B 24 -14.259 32.350 23.955 1.00 81.03 C ANISOU 1461 CG2 VAL B 24 12789 9037 8961 -1255 1962 -2536 C ATOM 1462 N GLY B 25 -11.681 35.206 21.794 1.00 80.98 N ANISOU 1462 N GLY B 25 12833 8719 9218 -1461 930 -2178 N ATOM 1463 CA GLY B 25 -10.835 36.239 22.330 1.00 79.38 C ANISOU 1463 CA GLY B 25 12796 8279 9086 -1405 613 -2132 C ATOM 1464 C GLY B 25 -9.466 36.215 21.720 1.00 75.23 C ANISOU 1464 C GLY B 25 12222 7726 8636 -1640 511 -1947 C ATOM 1465 O GLY B 25 -9.181 35.411 20.842 1.00 78.19 O ANISOU 1465 O GLY B 25 12436 8292 8980 -1817 682 -1857 O ATOM 1466 N THR B 26 -8.621 37.117 22.198 1.00 75.95 N ANISOU 1466 N THR B 26 12428 7595 8836 -1639 224 -1923 N ATOM 1467 CA THR B 26 -7.237 37.152 21.788 1.00 76.79 C ANISOU 1467 CA THR B 26 12459 7691 9029 -1870 123 -1775 C ATOM 1468 C THR B 26 -6.475 36.155 22.636 1.00 71.41 C ANISOU 1468 C THR B 26 11805 7090 8236 -1795 246 -1885 C ATOM 1469 O THR B 26 -6.873 35.877 23.757 1.00 70.65 O ANISOU 1469 O THR B 26 11859 6959 8025 -1548 300 -2048 O ATOM 1470 CB THR B 26 -6.637 38.569 21.934 1.00 74.23 C ANISOU 1470 CB THR B 26 12216 7062 8925 -1939 -248 -1720 C ATOM 1471 OG1 THR B 26 -6.578 38.933 23.317 1.00 86.83 O ANISOU 1471 OG1 THR B 26 13986 8475 10529 -1697 -417 -1967 O ATOM 1472 CG2 THR B 26 -7.487 39.578 21.197 1.00 70.36 C ANISOU 1472 CG2 THR B 26 11759 6431 8544 -1947 -389 -1594 C ATOM 1473 N PRO B 27 -5.393 35.587 22.092 1.00 86.19 N ANISOU 1473 N PRO B 27 13529 9102 10115 -1981 297 -1789 N ATOM 1474 CA PRO B 27 -4.527 34.740 22.913 1.00 79.14 C ANISOU 1474 CA PRO B 27 12674 8266 9130 -1869 347 -1893 C ATOM 1475 C PRO B 27 -3.960 35.510 24.090 1.00 80.14 C ANISOU 1475 C PRO B 27 12942 8210 9297 -1718 63 -2032 C ATOM 1476 O PRO B 27 -3.723 36.701 23.949 1.00 72.18 O ANISOU 1476 O PRO B 27 11921 7028 8476 -1833 -205 -2013 O ATOM 1477 CB PRO B 27 -3.407 34.353 21.950 1.00 79.90 C ANISOU 1477 CB PRO B 27 12535 8553 9270 -2109 370 -1782 C ATOM 1478 CG PRO B 27 -3.403 35.460 20.914 1.00 72.18 C ANISOU 1478 CG PRO B 27 11438 7548 8440 -2369 229 -1593 C ATOM 1479 CD PRO B 27 -4.867 35.736 20.723 1.00 81.39 C ANISOU 1479 CD PRO B 27 12707 8641 9577 -2271 297 -1585 C ATOM 1480 N GLU B 28 -3.765 34.845 25.225 1.00 76.27 N ANISOU 1480 N GLU B 28 12591 7753 8637 -1454 111 -2171 N ATOM 1481 CA GLU B 28 -2.966 35.392 26.325 1.00 71.23 C ANISOU 1481 CA GLU B 28 12042 7030 7994 -1284 -178 -2348 C ATOM 1482 C GLU B 28 -1.664 34.603 26.446 1.00 64.79 C ANISOU 1482 C GLU B 28 11124 6372 7120 -1276 -190 -2369 C ATOM 1483 O GLU B 28 -1.685 33.380 26.568 1.00 63.84 O ANISOU 1483 O GLU B 28 11052 6380 6825 -1145 52 -2327 O ATOM 1484 CB GLU B 28 -3.721 35.326 27.647 1.00 65.28 C ANISOU 1484 CB GLU B 28 11533 6252 7018 -909 -152 -2508 C ATOM 1485 CG GLU B 28 -4.348 36.612 28.127 1.00 74.93 C ANISOU 1485 CG GLU B 28 12853 7293 8324 -797 -399 -2669 C ATOM 1486 CD GLU B 28 -5.076 36.404 29.451 1.00 99.26 C ANISOU 1486 CD GLU B 28 16146 10458 11110 -392 -323 -2838 C ATOM 1487 OE1 GLU B 28 -5.498 35.252 29.725 1.00109.95 O ANISOU 1487 OE1 GLU B 28 17573 11979 12225 -278 18 -2733 O ATOM 1488 OE2 GLU B 28 -5.217 37.380 30.221 1.00100.03 O ANISOU 1488 OE2 GLU B 28 16334 10458 11215 -188 -600 -3077 O ATOM 1489 N VAL B 29 -0.537 35.304 26.414 1.00 66.55 N ANISOU 1489 N VAL B 29 11198 6574 7514 -1414 -478 -2445 N ATOM 1490 CA VAL B 29 0.782 34.682 26.525 1.00 69.02 C ANISOU 1490 CA VAL B 29 11358 7077 7790 -1395 -539 -2514 C ATOM 1491 C VAL B 29 1.245 34.512 27.987 1.00 82.35 C ANISOU 1491 C VAL B 29 13204 8796 9287 -1002 -723 -2755 C ATOM 1492 O VAL B 29 1.377 35.485 28.717 1.00 91.16 O ANISOU 1492 O VAL B 29 14370 9790 10475 -919 -1020 -2953 O ATOM 1493 CB VAL B 29 1.849 35.515 25.773 1.00 69.10 C ANISOU 1493 CB VAL B 29 11066 7105 8085 -1766 -751 -2494 C ATOM 1494 CG1 VAL B 29 3.253 35.009 26.095 1.00 72.04 C ANISOU 1494 CG1 VAL B 29 11245 7706 8423 -1699 -873 -2652 C ATOM 1495 CG2 VAL B 29 1.591 35.517 24.274 1.00 67.81 C ANISOU 1495 CG2 VAL B 29 10723 7014 8027 -2123 -548 -2222 C ATOM 1496 N ASN B 30 1.496 33.271 28.394 1.00 89.80 N ANISOU 1496 N ASN B 30 14232 9901 9987 -740 -560 -2744 N ATOM 1497 CA ASN B 30 2.003 32.955 29.732 1.00 79.67 C ANISOU 1497 CA ASN B 30 13108 8706 8455 -317 -720 -2929 C ATOM 1498 C ASN B 30 3.507 32.665 29.713 1.00 77.58 C ANISOU 1498 C ASN B 30 12608 8642 8226 -292 -924 -3069 C ATOM 1499 O ASN B 30 3.934 31.521 29.538 1.00 76.26 O ANISOU 1499 O ASN B 30 12425 8614 7935 -163 -772 -2996 O ATOM 1500 CB ASN B 30 1.242 31.742 30.327 1.00 84.18 C ANISOU 1500 CB ASN B 30 13979 9299 8705 10 -402 -2783 C ATOM 1501 CG ASN B 30 1.833 31.256 31.669 1.00 86.36 C ANISOU 1501 CG ASN B 30 14447 9710 8656 495 -542 -2905 C ATOM 1502 OD1 ASN B 30 2.494 32.009 32.367 1.00 75.56 O ANISOU 1502 OD1 ASN B 30 13029 8417 7264 643 -895 -3163 O ATOM 1503 ND2 ASN B 30 1.582 29.994 32.020 1.00 81.70 N ANISOU 1503 ND2 ASN B 30 14081 9140 7821 748 -272 -2719 N ATOM 1504 N GLN B 31 4.322 33.693 29.877 1.00 86.37 N ANISOU 1504 N GLN B 31 13519 9763 9535 -416 -1277 -3292 N ATOM 1505 CA GLN B 31 5.714 33.429 30.173 1.00 78.97 C ANISOU 1505 CA GLN B 31 12361 9064 8582 -297 -1508 -3503 C ATOM 1506 C GLN B 31 5.705 32.734 31.502 1.00 79.14 C ANISOU 1506 C GLN B 31 12671 9188 8209 277 -1565 -3616 C ATOM 1507 O GLN B 31 4.967 33.152 32.380 1.00108.38 O ANISOU 1507 O GLN B 31 16636 12791 11753 504 -1619 -3681 O ATOM 1508 CB GLN B 31 6.522 34.702 30.243 1.00 82.88 C ANISOU 1508 CB GLN B 31 12581 9526 9382 -541 -1889 -3760 C ATOM 1509 CG GLN B 31 6.593 35.450 28.958 1.00 96.79 C ANISOU 1509 CG GLN B 31 14072 11175 11527 -1120 -1833 -3590 C ATOM 1510 CD GLN B 31 7.289 36.762 29.148 1.00110.24 C ANISOU 1510 CD GLN B 31 15553 12755 13580 -1377 -2209 -3827 C ATOM 1511 OE1 GLN B 31 6.795 37.646 29.855 1.00112.36 O ANISOU 1511 OE1 GLN B 31 16001 12764 13925 -1286 -2429 -3993 O ATOM 1512 NE2 GLN B 31 8.466 36.890 28.555 1.00112.51 N ANISOU 1512 NE2 GLN B 31 15425 13233 14091 -1692 -2293 -3878 N ATOM 1513 N THR B 32 6.516 31.688 31.614 1.00 80.08 N ANISOU 1513 N THR B 32 12741 9524 8161 525 -1549 -3632 N ATOM 1514 CA THR B 32 6.702 30.817 32.789 1.00100.04 C ANISOU 1514 CA THR B 32 15545 12185 10280 1114 -1595 -3679 C ATOM 1515 C THR B 32 6.546 29.425 32.248 1.00104.69 C ANISOU 1515 C THR B 32 16244 12758 10776 1188 -1253 -3403 C ATOM 1516 O THR B 32 7.025 28.459 32.834 1.00124.90 O ANISOU 1516 O THR B 32 18952 15429 13077 1618 -1275 -3394 O ATOM 1517 CB THR B 32 5.708 31.015 33.990 1.00 99.19 C ANISOU 1517 CB THR B 32 15844 11993 9851 1468 -1572 -3659 C ATOM 1518 OG1 THR B 32 6.313 30.539 35.190 1.00113.51 O ANISOU 1518 OG1 THR B 32 17818 14028 11281 2035 -1774 -3801 O ATOM 1519 CG2 THR B 32 4.423 30.244 33.798 1.00105.33 C ANISOU 1519 CG2 THR B 32 16930 12591 10500 1463 -1112 -3288 C ATOM 1520 N THR B 33 5.860 29.324 31.120 1.00 77.42 N ANISOU 1520 N THR B 33 12724 9153 7539 787 -954 -3189 N ATOM 1521 CA THR B 33 5.679 28.028 30.494 1.00 76.75 C ANISOU 1521 CA THR B 33 12709 9024 7428 816 -642 -2980 C ATOM 1522 C THR B 33 6.174 28.092 29.065 1.00 84.16 C ANISOU 1522 C THR B 33 13244 10074 8661 396 -592 -3001 C ATOM 1523 O THR B 33 6.517 27.065 28.477 1.00 93.28 O ANISOU 1523 O THR B 33 14324 11295 9824 452 -452 -2964 O ATOM 1524 CB THR B 33 4.205 27.564 30.542 1.00 74.19 C ANISOU 1524 CB THR B 33 12724 8442 7023 799 -267 -2701 C ATOM 1525 OG1 THR B 33 3.348 28.586 30.021 1.00 72.33 O ANISOU 1525 OG1 THR B 33 12405 8103 6974 420 -209 -2671 O ATOM 1526 CG2 THR B 33 3.794 27.266 31.991 1.00 76.38 C ANISOU 1526 CG2 THR B 33 13408 8675 6937 1266 -258 -2631 C ATOM 1527 N GLY B 34 6.248 29.309 28.525 1.00 75.91 N ANISOU 1527 N GLY B 34 11938 9055 7850 -5 -716 -3065 N ATOM 1528 CA GLY B 34 6.606 29.502 27.132 1.00 76.05 C ANISOU 1528 CA GLY B 34 11579 9207 8110 -440 -633 -3024 C ATOM 1529 C GLY B 34 5.421 29.230 26.220 1.00 70.20 C ANISOU 1529 C GLY B 34 10934 8315 7424 -673 -292 -2784 C ATOM 1530 O GLY B 34 5.565 29.117 25.009 1.00 69.38 O ANISOU 1530 O GLY B 34 10564 8354 7443 -962 -161 -2723 O ATOM 1531 N TYR B 35 4.237 29.136 26.817 1.00 68.97 N ANISOU 1531 N TYR B 35 11136 7912 7158 -535 -149 -2667 N ATOM 1532 CA TYR B 35 3.025 28.856 26.067 1.00 73.63 C ANISOU 1532 CA TYR B 35 11809 8366 7798 -726 162 -2482 C ATOM 1533 C TYR B 35 2.034 30.003 26.150 1.00 76.34 C ANISOU 1533 C TYR B 35 12245 8546 8216 -902 138 -2418 C ATOM 1534 O TYR B 35 2.068 30.832 27.071 1.00 66.75 O ANISOU 1534 O TYR B 35 11143 7253 6967 -782 -84 -2516 O ATOM 1535 CB TYR B 35 2.363 27.563 26.558 1.00 66.34 C ANISOU 1535 CB TYR B 35 11195 7295 6715 -438 420 -2389 C ATOM 1536 CG TYR B 35 3.130 26.315 26.168 1.00 74.21 C ANISOU 1536 CG TYR B 35 12108 8386 7702 -294 487 -2434 C ATOM 1537 CD1 TYR B 35 4.256 25.925 26.874 1.00 69.67 C ANISOU 1537 CD1 TYR B 35 11546 7922 7004 40 278 -2556 C ATOM 1538 CD2 TYR B 35 2.734 25.527 25.088 1.00 75.40 C ANISOU 1538 CD2 TYR B 35 12155 8526 7967 -458 732 -2395 C ATOM 1539 CE1 TYR B 35 4.972 24.791 26.525 1.00 70.93 C ANISOU 1539 CE1 TYR B 35 11629 8159 7161 223 310 -2625 C ATOM 1540 CE2 TYR B 35 3.452 24.384 24.728 1.00 68.47 C ANISOU 1540 CE2 TYR B 35 11198 7717 7100 -290 764 -2487 C ATOM 1541 CZ TYR B 35 4.570 24.025 25.461 1.00 70.14 C ANISOU 1541 CZ TYR B 35 11439 8017 7195 59 552 -2594 C ATOM 1542 OH TYR B 35 5.303 22.904 25.141 1.00 71.51 O ANISOU 1542 OH TYR B 35 11540 8250 7380 280 553 -2709 O ATOM 1543 N GLN B 36 1.151 30.033 25.164 1.00 63.63 N ANISOU 1543 N GLN B 36 10576 6898 6704 -1158 348 -2286 N ATOM 1544 CA GLN B 36 0.051 30.963 25.141 1.00 62.76 C ANISOU 1544 CA GLN B 36 10561 6630 6653 -1281 356 -2220 C ATOM 1545 C GLN B 36 -1.247 30.169 25.109 1.00 63.77 C ANISOU 1545 C GLN B 36 10863 6669 6700 -1211 678 -2135 C ATOM 1546 O GLN B 36 -1.265 28.978 24.809 1.00 61.00 O ANISOU 1546 O GLN B 36 10512 6352 6314 -1166 895 -2108 O ATOM 1547 CB GLN B 36 0.141 31.881 23.936 1.00 69.88 C ANISOU 1547 CB GLN B 36 11208 7590 7752 -1658 283 -2132 C ATOM 1548 CG GLN B 36 -0.252 31.184 22.657 1.00 64.45 C ANISOU 1548 CG GLN B 36 10362 7052 7075 -1835 540 -2028 C ATOM 1549 CD GLN B 36 -0.162 32.096 21.462 1.00 78.79 C ANISOU 1549 CD GLN B 36 11944 8973 9020 -2176 478 -1892 C ATOM 1550 OE1 GLN B 36 0.900 32.652 21.165 1.00 81.49 O ANISOU 1550 OE1 GLN B 36 12082 9428 9454 -2353 316 -1867 O ATOM 1551 NE2 GLN B 36 -1.282 32.266 20.769 1.00 73.20 N ANISOU 1551 NE2 GLN B 36 11255 8242 8315 -2271 610 -1791 N ATOM 1552 N ARG B 37 -2.333 30.861 25.393 1.00 60.99 N ANISOU 1552 N ARG B 37 10633 6195 6345 -1211 698 -2116 N ATOM 1553 CA ARG B 37 -3.600 30.239 25.666 1.00 60.41 C ANISOU 1553 CA ARG B 37 10720 6049 6185 -1119 988 -2070 C ATOM 1554 C ARG B 37 -4.722 30.936 24.909 1.00 59.39 C ANISOU 1554 C ARG B 37 10496 5904 6164 -1312 1041 -2043 C ATOM 1555 O ARG B 37 -4.796 32.156 24.886 1.00 63.28 O ANISOU 1555 O ARG B 37 10969 6343 6731 -1361 812 -2069 O ATOM 1556 CB ARG B 37 -3.856 30.289 27.180 1.00 82.07 C ANISOU 1556 CB ARG B 37 13741 8723 8719 -789 967 -2113 C ATOM 1557 CG ARG B 37 -5.310 30.385 27.617 1.00 79.93 C ANISOU 1557 CG ARG B 37 13599 8407 8365 -721 1177 -2096 C ATOM 1558 CD ARG B 37 -5.446 30.267 29.148 1.00 64.19 C ANISOU 1558 CD ARG B 37 11876 6425 6090 -360 1198 -2117 C ATOM 1559 NE ARG B 37 -4.777 31.355 29.852 1.00 69.81 N ANISOU 1559 NE ARG B 37 12627 7157 6742 -187 817 -2288 N ATOM 1560 CZ ARG B 37 -4.898 31.572 31.154 1.00 83.53 C ANISOU 1560 CZ ARG B 37 14566 8959 8212 155 750 -2378 C ATOM 1561 NH1 ARG B 37 -5.670 30.774 31.878 1.00 78.28 N ANISOU 1561 NH1 ARG B 37 14089 8358 7296 341 1076 -2252 N ATOM 1562 NH2 ARG B 37 -4.259 32.583 31.726 1.00 96.45 N ANISOU 1562 NH2 ARG B 37 16205 10608 9833 304 365 -2597 N ATOM 1563 N TYR B 38 -5.594 30.158 24.287 1.00 64.64 N ANISOU 1563 N TYR B 38 11101 6603 6856 -1408 1324 -2010 N ATOM 1564 CA TYR B 38 -6.811 30.705 23.697 1.00 67.34 C ANISOU 1564 CA TYR B 38 11357 6964 7263 -1522 1387 -2018 C ATOM 1565 C TYR B 38 -8.039 30.265 24.491 1.00 75.89 C ANISOU 1565 C TYR B 38 12577 8000 8257 -1383 1640 -2056 C ATOM 1566 O TYR B 38 -8.234 29.068 24.772 1.00 62.70 O ANISOU 1566 O TYR B 38 10970 6299 6554 -1356 1914 -2028 O ATOM 1567 CB TYR B 38 -6.992 30.244 22.251 1.00 66.84 C ANISOU 1567 CB TYR B 38 11049 7046 7300 -1754 1505 -2003 C ATOM 1568 CG TYR B 38 -5.989 30.722 21.241 1.00 70.12 C ANISOU 1568 CG TYR B 38 11274 7595 7775 -1931 1315 -1935 C ATOM 1569 CD1 TYR B 38 -4.824 30.004 21.000 1.00 86.12 C ANISOU 1569 CD1 TYR B 38 13210 9718 9793 -1958 1319 -1942 C ATOM 1570 CD2 TYR B 38 -6.239 31.841 20.466 1.00 70.29 C ANISOU 1570 CD2 TYR B 38 11191 7666 7851 -2066 1154 -1852 C ATOM 1571 CE1 TYR B 38 -3.916 30.414 20.040 1.00 77.94 C ANISOU 1571 CE1 TYR B 38 11952 8872 8789 -2139 1187 -1877 C ATOM 1572 CE2 TYR B 38 -5.339 32.253 19.500 1.00 77.11 C ANISOU 1572 CE2 TYR B 38 11870 8678 8748 -2259 1027 -1734 C ATOM 1573 CZ TYR B 38 -4.182 31.534 19.298 1.00 69.36 C ANISOU 1573 CZ TYR B 38 10769 7839 7745 -2306 1059 -1753 C ATOM 1574 OH TYR B 38 -3.287 31.940 18.351 1.00 92.61 O ANISOU 1574 OH TYR B 38 13494 10992 10702 -2508 966 -1635 O ATOM 1575 N GLU B 39 -8.890 31.222 24.813 1.00 59.04 N ANISOU 1575 N GLU B 39 10473 5857 6101 -1305 1557 -2117 N ATOM 1576 CA GLU B 39 -10.149 30.915 25.449 1.00 66.91 C ANISOU 1576 CA GLU B 39 11528 6885 7011 -1198 1812 -2170 C ATOM 1577 C GLU B 39 -11.151 30.464 24.394 1.00 74.15 C ANISOU 1577 C GLU B 39 12218 7900 8056 -1400 2024 -2210 C ATOM 1578 O GLU B 39 -11.431 31.182 23.428 1.00 71.03 O ANISOU 1578 O GLU B 39 11659 7576 7754 -1499 1867 -2246 O ATOM 1579 CB GLU B 39 -10.681 32.127 26.211 1.00 70.57 C ANISOU 1579 CB GLU B 39 12080 7343 7390 -989 1622 -2280 C ATOM 1580 CG GLU B 39 -12.040 31.907 26.825 1.00 73.26 C ANISOU 1580 CG GLU B 39 12422 7793 7621 -875 1895 -2358 C ATOM 1581 CD GLU B 39 -12.660 33.192 27.338 1.00 87.30 C ANISOU 1581 CD GLU B 39 14229 9601 9339 -653 1674 -2527 C ATOM 1582 OE1 GLU B 39 -12.046 34.278 27.148 1.00 97.17 O ANISOU 1582 OE1 GLU B 39 15515 10722 10681 -614 1292 -2572 O ATOM 1583 OE2 GLU B 39 -13.763 33.103 27.927 1.00 75.53 O ANISOU 1583 OE2 GLU B 39 12714 8259 7727 -522 1889 -2622 O ATOM 1584 N ILE B 40 -11.686 29.267 24.593 1.00 73.61 N ANISOU 1584 N ILE B 40 12144 7829 7996 -1455 2373 -2202 N ATOM 1585 CA ILE B 40 -12.663 28.692 23.688 1.00 67.35 C ANISOU 1585 CA ILE B 40 11111 7129 7349 -1653 2589 -2298 C ATOM 1586 C ILE B 40 -13.939 28.397 24.444 1.00 79.60 C ANISOU 1586 C ILE B 40 12655 8726 8862 -1615 2889 -2354 C ATOM 1587 O ILE B 40 -13.985 28.578 25.652 1.00 70.39 O ANISOU 1587 O ILE B 40 11689 7536 7521 -1423 2942 -2289 O ATOM 1588 CB ILE B 40 -12.152 27.393 23.080 1.00 65.07 C ANISOU 1588 CB ILE B 40 10764 6769 7190 -1819 2753 -2279 C ATOM 1589 CG1 ILE B 40 -11.982 26.353 24.189 1.00 61.58 C ANISOU 1589 CG1 ILE B 40 10561 6137 6701 -1740 3011 -2154 C ATOM 1590 CG2 ILE B 40 -10.841 27.634 22.355 1.00 74.26 C ANISOU 1590 CG2 ILE B 40 11897 7957 8361 -1846 2485 -2236 C ATOM 1591 CD1 ILE B 40 -11.593 24.978 23.673 1.00 63.88 C ANISOU 1591 CD1 ILE B 40 10823 6280 7168 -1878 3184 -2155 C ATOM 1592 N LYS B 41 -14.970 27.936 23.739 1.00 93.58 N ANISOU 1592 N LYS B 41 14170 10603 10784 -1795 3088 -2491 N ATOM 1593 CA LYS B 41 -16.114 27.308 24.393 1.00 84.77 C ANISOU 1593 CA LYS B 41 12996 9525 9687 -1848 3464 -2532 C ATOM 1594 C LYS B 41 -16.500 26.041 23.646 1.00 80.43 C ANISOU 1594 C LYS B 41 12250 8915 9395 -2137 3733 -2615 C ATOM 1595 O LYS B 41 -16.776 26.087 22.448 1.00 79.87 O ANISOU 1595 O LYS B 41 11909 8971 9466 -2266 3629 -2804 O ATOM 1596 CB LYS B 41 -17.315 28.245 24.473 1.00 83.42 C ANISOU 1596 CB LYS B 41 12642 9597 9459 -1750 3431 -2711 C ATOM 1597 N MET B 42 -16.526 24.923 24.371 1.00 75.40 N ANISOU 1597 N MET B 42 11757 8078 8815 -2223 4069 -2474 N ATOM 1598 CA MET B 42 -16.721 23.599 23.794 1.00 76.98 C ANISOU 1598 CA MET B 42 11833 8103 9314 -2499 4317 -2539 C ATOM 1599 C MET B 42 -18.185 23.329 23.455 1.00 91.74 C ANISOU 1599 C MET B 42 13350 10122 11385 -2731 4575 -2769 C ATOM 1600 O MET B 42 -19.044 23.278 24.342 1.00 99.99 O ANISOU 1600 O MET B 42 14387 11224 12379 -2756 4864 -2705 O ATOM 1601 CB MET B 42 -16.199 22.524 24.754 1.00 86.68 C ANISOU 1601 CB MET B 42 13388 8997 10549 -2494 4574 -2257 C ATOM 1602 CG MET B 42 -16.345 21.091 24.250 1.00 74.85 C ANISOU 1602 CG MET B 42 11814 7209 9414 -2773 4823 -2311 C ATOM 1603 SD MET B 42 -15.991 19.870 25.533 1.00117.12 S ANISOU 1603 SD MET B 42 17594 12129 14778 -2753 5176 -1907 S ATOM 1604 CE MET B 42 -17.425 20.031 26.605 1.00100.68 C ANISOU 1604 CE MET B 42 15454 10209 12591 -2856 5605 -1774 C ATOM 1605 N THR B 43 -18.464 23.133 22.168 1.00 92.34 N ANISOU 1605 N THR B 43 10147 12043 12896 1551 5274 -1638 N ATOM 1606 CA THR B 43 -19.844 23.022 21.704 1.00 85.17 C ANISOU 1606 CA THR B 43 8516 12139 11704 1790 5244 -1676 C ATOM 1607 C THR B 43 -20.262 21.576 21.448 1.00 88.01 C ANISOU 1607 C THR B 43 8480 13001 11957 1215 5176 -1719 C ATOM 1608 O THR B 43 -21.449 21.297 21.289 1.00 99.46 O ANISOU 1608 O THR B 43 9434 15240 13116 1270 5231 -1716 O ATOM 1609 CB THR B 43 -20.064 23.834 20.423 1.00 90.73 C ANISOU 1609 CB THR B 43 8808 13208 12458 2513 4833 -1555 C ATOM 1610 OG1 THR B 43 -19.316 23.240 19.360 1.00 80.04 O ANISOU 1610 OG1 THR B 43 7350 11722 11341 2463 4398 -1367 O ATOM 1611 CG2 THR B 43 -19.620 25.288 20.613 1.00 86.28 C ANISOU 1611 CG2 THR B 43 8696 12048 12038 2942 4865 -1525 C ATOM 1612 N LYS B 44 -19.284 20.677 21.378 1.00 88.82 N ANISOU 1612 N LYS B 44 8837 12612 12298 671 5051 -1722 N ATOM 1613 CA LYS B 44 -19.532 19.242 21.442 1.00 86.24 C ANISOU 1613 CA LYS B 44 8363 12596 11808 -132 4985 -1843 C ATOM 1614 C LYS B 44 -18.214 18.526 21.661 1.00 74.64 C ANISOU 1614 C LYS B 44 7602 10311 10448 -641 4455 -1649 C ATOM 1615 O LYS B 44 -17.156 19.032 21.308 1.00 70.76 O ANISOU 1615 O LYS B 44 7404 9224 10260 -295 4153 -1448 O ATOM 1616 CB LYS B 44 -20.221 18.708 20.182 1.00 93.91 C ANISOU 1616 CB LYS B 44 8635 14293 12753 83 4643 -1683 C ATOM 1617 CG LYS B 44 -20.842 17.318 20.387 1.00104.29 C ANISOU 1617 CG LYS B 44 9832 16009 13785 -741 4624 -1841 C ATOM 1618 CD LYS B 44 -21.830 16.942 19.285 1.00114.23 C ANISOU 1618 CD LYS B 44 10495 17928 14978 -484 4399 -1682 C ATOM 1619 CE LYS B 44 -22.548 15.624 19.588 1.00105.88 C ANISOU 1619 CE LYS B 44 9406 17214 13610 -1302 4411 -1912 C ATOM 1620 NZ LYS B 44 -23.306 15.667 20.867 1.00100.48 N ANISOU 1620 NZ LYS B 44 8903 16702 12571 -1682 4791 -2182 N ATOM 1621 N MET B 45 -18.294 17.350 22.266 1.00 85.28 N ANISOU 1621 N MET B 45 9235 11647 11521 -1463 4364 -1719 N ATOM 1622 CA MET B 45 -17.124 16.542 22.567 1.00 81.63 C ANISOU 1622 CA MET B 45 9461 10461 11094 -1958 3877 -1533 C ATOM 1623 C MET B 45 -17.297 15.181 21.916 1.00 81.87 C ANISOU 1623 C MET B 45 9248 10762 11095 -2434 3663 -1511 C ATOM 1624 O MET B 45 -18.367 14.585 22.010 1.00 76.41 O ANISOU 1624 O MET B 45 8214 10696 10123 -2831 3976 -1722 O ATOM 1625 CB MET B 45 -16.948 16.390 24.073 1.00 84.60 C ANISOU 1625 CB MET B 45 10601 10429 11112 -2524 3980 -1607 C ATOM 1626 CG MET B 45 -15.541 16.084 24.491 1.00 82.22 C ANISOU 1626 CG MET B 45 11061 9305 10874 -2748 3485 -1383 C ATOM 1627 SD MET B 45 -15.473 15.178 26.038 1.00 82.05 S ANISOU 1627 SD MET B 45 11863 8977 10335 -3643 3500 -1421 S ATOM 1628 CE MET B 45 -13.799 15.566 26.494 1.00 70.06 C ANISOU 1628 CE MET B 45 11079 6602 8938 -3520 2999 -1190 C ATOM 1629 N TYR B 46 -16.251 14.696 21.254 1.00 79.78 N ANISOU 1629 N TYR B 46 9161 10043 11110 -2413 3159 -1282 N ATOM 1630 CA TYR B 46 -16.309 13.414 20.562 1.00 66.93 C ANISOU 1630 CA TYR B 46 7351 8587 9492 -2839 2954 -1255 C ATOM 1631 C TYR B 46 -15.406 12.377 21.224 1.00 66.46 C ANISOU 1631 C TYR B 46 8115 7826 9311 -3435 2605 -1105 C ATOM 1632 O TYR B 46 -15.763 11.207 21.346 1.00 75.53 O ANISOU 1632 O TYR B 46 9396 9069 10230 -4061 2651 -1163 O ATOM 1633 CB TYR B 46 -15.918 13.597 19.097 1.00 63.97 C ANISOU 1633 CB TYR B 46 6428 8338 9541 -2303 2671 -1121 C ATOM 1634 CG TYR B 46 -16.953 14.340 18.288 1.00 72.30 C ANISOU 1634 CG TYR B 46 6591 10223 10655 -1759 3008 -1253 C ATOM 1635 CD1 TYR B 46 -18.277 13.951 18.320 1.00 87.31 C ANISOU 1635 CD1 TYR B 46 7967 12959 12247 -2051 3418 -1513 C ATOM 1636 CD2 TYR B 46 -16.608 15.443 17.497 1.00 72.49 C ANISOU 1636 CD2 TYR B 46 6303 10223 11016 -942 2928 -1119 C ATOM 1637 CE1 TYR B 46 -19.238 14.614 17.588 1.00 99.00 C ANISOU 1637 CE1 TYR B 46 8862 15098 13657 -1377 3445 -1464 C ATOM 1638 CE2 TYR B 46 -17.574 16.124 16.757 1.00 66.42 C ANISOU 1638 CE2 TYR B 46 4820 10207 10209 -353 3151 -1154 C ATOM 1639 CZ TYR B 46 -18.884 15.691 16.808 1.00 89.00 C ANISOU 1639 CZ TYR B 46 7400 13760 12656 -536 3289 -1226 C ATOM 1640 OH TYR B 46 -19.865 16.325 16.092 1.00100.98 O ANISOU 1640 OH TYR B 46 8545 15754 14068 91 3301 -1005 O ATOM 1641 N LYS B 47 -14.232 12.824 21.649 1.00 61.97 N ANISOU 1641 N LYS B 47 8105 6566 8874 -3228 2274 -917 N ATOM 1642 CA LYS B 47 -13.295 11.962 22.343 1.00 80.70 C ANISOU 1642 CA LYS B 47 11270 8286 11107 -3677 1915 -746 C ATOM 1643 C LYS B 47 -12.841 12.666 23.622 1.00 96.35 C ANISOU 1643 C LYS B 47 13863 9868 12878 -3693 1948 -734 C ATOM 1644 O LYS B 47 -12.649 13.877 23.629 1.00 89.32 O ANISOU 1644 O LYS B 47 12848 8946 12144 -3208 2031 -771 O ATOM 1645 CB LYS B 47 -12.098 11.637 21.448 1.00 79.75 C ANISOU 1645 CB LYS B 47 11151 7817 11332 -3314 1313 -495 C ATOM 1646 CG LYS B 47 -11.346 10.381 21.832 1.00 78.65 C ANISOU 1646 CG LYS B 47 11399 7468 11015 -3311 814 -260 C ATOM 1647 CD LYS B 47 -10.084 10.235 21.005 1.00 64.63 C ANISOU 1647 CD LYS B 47 9438 5470 9648 -2788 283 -58 C ATOM 1648 CE LYS B 47 -9.362 8.935 21.303 1.00 60.37 C ANISOU 1648 CE LYS B 47 9113 4805 9019 -2742 70 52 C ATOM 1649 NZ LYS B 47 -7.954 9.068 20.876 1.00 47.95 N ANISOU 1649 NZ LYS B 47 7416 3120 7685 -2247 -116 93 N ATOM 1650 N GLY B 48 -12.703 11.915 24.709 1.00116.88 N ANISOU 1650 N GLY B 48 17015 12335 15058 -4018 1815 -661 N ATOM 1651 CA GLY B 48 -12.119 12.455 25.923 1.00100.17 C ANISOU 1651 CA GLY B 48 15428 9927 12703 -3979 1736 -619 C ATOM 1652 C GLY B 48 -13.030 12.508 27.133 1.00 98.70 C ANISOU 1652 C GLY B 48 15561 9886 12054 -4492 2222 -822 C ATOM 1653 O GLY B 48 -12.659 13.081 28.153 1.00 94.47 O ANISOU 1653 O GLY B 48 15440 9149 11305 -4503 2238 -834 O ATOM 1654 N PHE B 49 -14.207 11.899 27.046 1.00 91.71 N ANISOU 1654 N PHE B 49 14453 9408 10983 -4928 2617 -1000 N ATOM 1655 CA PHE B 49 -15.214 12.050 28.090 1.00 86.26 C ANISOU 1655 CA PHE B 49 13927 8975 9874 -5417 3159 -1250 C ATOM 1656 C PHE B 49 -14.742 11.668 29.494 1.00 95.43 C ANISOU 1656 C PHE B 49 15838 9850 10571 -5620 2962 -1151 C ATOM 1657 O PHE B 49 -15.494 11.795 30.464 1.00 98.07 O ANISOU 1657 O PHE B 49 16386 10354 10524 -6036 3377 -1359 O ATOM 1658 CB PHE B 49 -16.434 11.238 27.735 1.00105.69 C ANISOU 1658 CB PHE B 49 15983 12013 12160 -5804 3494 -1448 C ATOM 1659 CG PHE B 49 -17.250 11.827 26.629 1.00114.51 C ANISOU 1659 CG PHE B 49 16174 13754 13581 -5522 3838 -1633 C ATOM 1660 CD1 PHE B 49 -18.359 12.603 26.917 1.00116.46 C ANISOU 1660 CD1 PHE B 49 15957 14615 13677 -5400 4369 -1927 C ATOM 1661 CD2 PHE B 49 -16.912 11.609 25.303 1.00106.91 C ANISOU 1661 CD2 PHE B 49 14748 12856 13017 -5168 3540 -1511 C ATOM 1662 CE1 PHE B 49 -19.124 13.147 25.908 1.00107.20 C ANISOU 1662 CE1 PHE B 49 13873 14130 12729 -4895 4588 -2074 C ATOM 1663 CE2 PHE B 49 -17.680 12.140 24.290 1.00102.24 C ANISOU 1663 CE2 PHE B 49 13254 12950 12642 -4714 3759 -1662 C ATOM 1664 CZ PHE B 49 -18.789 12.915 24.593 1.00101.34 C ANISOU 1664 CZ PHE B 49 12678 13467 12358 -4553 4277 -1933 C ATOM 1665 N GLN B 50 -13.503 11.196 29.598 1.00 94.68 N ANISOU 1665 N GLN B 50 16070 9398 10506 -5318 2358 -845 N ATOM 1666 CA GLN B 50 -12.812 11.134 30.878 1.00 85.03 C ANISOU 1666 CA GLN B 50 15459 7936 8912 -5391 2156 -731 C ATOM 1667 C GLN B 50 -12.159 12.480 31.087 1.00 94.09 C ANISOU 1667 C GLN B 50 16624 8895 10231 -5082 2125 -758 C ATOM 1668 O GLN B 50 -10.933 12.565 31.074 1.00 83.61 O ANISOU 1668 O GLN B 50 15389 7354 9024 -4719 1645 -551 O ATOM 1669 CB GLN B 50 -11.750 10.027 30.910 1.00 81.93 C ANISOU 1669 CB GLN B 50 15328 7334 8467 -5204 1588 -420 C ATOM 1670 CG GLN B 50 -12.269 8.611 31.180 1.00 86.08 C ANISOU 1670 CG GLN B 50 16126 7929 8650 -5582 1646 -393 C ATOM 1671 CD GLN B 50 -13.506 8.588 32.048 1.00 99.91 C ANISOU 1671 CD GLN B 50 18106 9906 9951 -6171 2181 -661 C ATOM 1672 OE1 GLN B 50 -14.617 8.415 31.555 1.00107.10 O ANISOU 1672 OE1 GLN B 50 18682 11133 10877 -6438 2563 -886 O ATOM 1673 NE2 GLN B 50 -13.322 8.770 33.350 1.00105.78 N ANISOU 1673 NE2 GLN B 50 19388 10534 10270 -6396 2219 -667 N ATOM 1674 N ALA B 51 -12.977 13.522 31.272 1.00107.14 N ANISOU 1674 N ALA B 51 18165 10650 11894 -5234 2684 -1043 N ATOM 1675 CA ALA B 51 -12.494 14.903 31.300 1.00104.09 C ANISOU 1675 CA ALA B 51 17768 10052 11729 -4912 2775 -1127 C ATOM 1676 C ALA B 51 -11.517 15.122 32.443 1.00113.71 C ANISOU 1676 C ALA B 51 19502 11072 12632 -4908 2485 -1027 C ATOM 1677 O ALA B 51 -10.311 15.222 32.212 1.00114.27 O ANISOU 1677 O ALA B 51 19562 10988 12868 -4530 1984 -829 O ATOM 1678 CB ALA B 51 -13.663 15.888 31.398 1.00 91.49 C ANISOU 1678 CB ALA B 51 15945 8648 10169 -5042 3535 -1474 C ATOM 1679 N ASP B 57 -16.098 19.539 29.790 1.00109.80 N ANISOU 1679 N ASP B 57 16401 12094 13223 -3156 4999 -2109 N ATOM 1680 CA ASP B 57 -15.763 20.395 30.931 1.00115.90 C ANISOU 1680 CA ASP B 57 17736 12510 13790 -3258 5224 -2246 C ATOM 1681 C ASP B 57 -14.626 21.420 30.692 1.00115.58 C ANISOU 1681 C ASP B 57 17962 11913 14040 -2809 5046 -2163 C ATOM 1682 O ASP B 57 -14.133 22.001 31.660 1.00119.88 O ANISOU 1682 O ASP B 57 19055 12108 14387 -3009 5150 -2270 O ATOM 1683 CB ASP B 57 -15.383 19.508 32.129 1.00121.50 C ANISOU 1683 CB ASP B 57 19127 12989 14049 -4075 5026 -2215 C ATOM 1684 CG ASP B 57 -15.998 19.978 33.444 1.00127.28 C ANISOU 1684 CG ASP B 57 20177 13820 14364 -4420 5535 -2493 C ATOM 1685 OD1 ASP B 57 -16.762 20.964 33.429 1.00131.09 O ANISOU 1685 OD1 ASP B 57 20334 14557 14917 -4019 6062 -2726 O ATOM 1686 OD2 ASP B 57 -15.721 19.356 34.500 1.00113.80 O ANISOU 1686 OD2 ASP B 57 19058 11938 12244 -5077 5416 -2473 O ATOM 1687 N ILE B 58 -14.209 21.655 29.443 1.00106.48 N ANISOU 1687 N ILE B 58 16442 10692 13322 -2254 4804 -1997 N ATOM 1688 CA ILE B 58 -13.005 22.474 29.192 1.00 99.99 C ANISOU 1688 CA ILE B 58 15924 9318 12750 -1943 4581 -1915 C ATOM 1689 C ILE B 58 -13.239 23.727 28.324 1.00 98.39 C ANISOU 1689 C ILE B 58 15368 9111 12903 -1138 4921 -1956 C ATOM 1690 O ILE B 58 -14.019 23.708 27.363 1.00 96.59 O ANISOU 1690 O ILE B 58 14508 9311 12880 -678 5051 -1908 O ATOM 1691 CB ILE B 58 -11.855 21.630 28.526 1.00 92.03 C ANISOU 1691 CB ILE B 58 14987 8044 11935 -2056 3869 -1641 C ATOM 1692 CG1 ILE B 58 -10.521 22.398 28.530 1.00 85.97 C ANISOU 1692 CG1 ILE B 58 14619 6731 11315 -1913 3631 -1611 C ATOM 1693 CG2 ILE B 58 -12.192 21.251 27.090 1.00 78.46 C ANISOU 1693 CG2 ILE B 58 12598 6633 10578 -1636 3717 -1490 C ATOM 1694 CD1 ILE B 58 -10.115 22.905 29.913 1.00 91.09 C ANISOU 1694 CD1 ILE B 58 15878 7146 11585 -2303 3778 -1775 C ATOM 1695 N ARG B 59 -12.582 24.829 28.694 1.00 78.28 N ANISOU 1695 N ARG B 59 13256 6094 10394 -979 5094 -2054 N ATOM 1696 CA ARG B 59 -12.790 26.114 28.034 1.00 83.02 C ANISOU 1696 CA ARG B 59 13683 6582 11277 -233 5504 -2103 C ATOM 1697 C ARG B 59 -11.477 26.911 27.729 1.00 85.34 C ANISOU 1697 C ARG B 59 14228 6459 11738 -110 5143 -1919 C ATOM 1698 O ARG B 59 -11.537 28.095 27.406 1.00 78.39 O ANISOU 1698 O ARG B 59 13226 5597 10960 323 5290 -1820 O ATOM 1699 CB ARG B 59 -13.753 27.007 28.866 1.00 85.13 C ANISOU 1699 CB ARG B 59 14029 6986 11330 -103 6186 -2347 C ATOM 1700 N PHE B 60 -10.304 26.274 27.798 1.00 67.76 N ANISOU 1700 N PHE B 60 12298 6685 6762 -50 1635 -2720 N ATOM 1701 CA PHE B 60 -9.072 26.905 27.282 1.00 71.67 C ANISOU 1701 CA PHE B 60 12786 7126 7321 -175 1449 -2776 C ATOM 1702 C PHE B 60 -8.202 25.973 26.401 1.00 78.70 C ANISOU 1702 C PHE B 60 13636 8141 8125 -215 1255 -2542 C ATOM 1703 O PHE B 60 -8.163 24.762 26.598 1.00 81.70 O ANISOU 1703 O PHE B 60 14030 8719 8292 -171 1240 -2398 O ATOM 1704 CB PHE B 60 -8.216 27.433 28.422 1.00 72.57 C ANISOU 1704 CB PHE B 60 12908 7417 7248 -265 1376 -3025 C ATOM 1705 CG PHE B 60 -8.833 28.581 29.167 1.00 90.77 C ANISOU 1705 CG PHE B 60 15197 9589 9702 -251 1526 -3281 C ATOM 1706 CD1 PHE B 60 -8.646 29.881 28.739 1.00 93.60 C ANISOU 1706 CD1 PHE B 60 15523 9654 10388 -320 1544 -3417 C ATOM 1707 CD2 PHE B 60 -9.597 28.361 30.297 1.00 86.17 C ANISOU 1707 CD2 PHE B 60 14635 9162 8944 -164 1667 -3378 C ATOM 1708 CE1 PHE B 60 -9.199 30.944 29.422 1.00 92.48 C ANISOU 1708 CE1 PHE B 60 15369 9360 10408 -298 1698 -3656 C ATOM 1709 CE2 PHE B 60 -10.162 29.425 30.986 1.00 94.88 C ANISOU 1709 CE2 PHE B 60 15726 10143 10182 -143 1810 -3629 C ATOM 1710 CZ PHE B 60 -9.961 30.717 30.546 1.00 95.88 C ANISOU 1710 CZ PHE B 60 15821 9960 10648 -208 1825 -3773 C ATOM 1711 N VAL B 61 -7.489 26.556 25.442 1.00 64.71 N ANISOU 1711 N VAL B 61 11792 6251 6543 -294 1122 -2490 N ATOM 1712 CA VAL B 61 -6.575 25.802 24.591 1.00 58.35 C ANISOU 1712 CA VAL B 61 10920 5576 5675 -334 938 -2284 C ATOM 1713 C VAL B 61 -5.170 26.379 24.637 1.00 56.14 C ANISOU 1713 C VAL B 61 10643 5344 5343 -472 778 -2396 C ATOM 1714 O VAL B 61 -4.986 27.574 24.541 1.00 72.03 O ANISOU 1714 O VAL B 61 12648 7161 7559 -554 796 -2542 O ATOM 1715 CB VAL B 61 -7.053 25.788 23.127 1.00 63.16 C ANISOU 1715 CB VAL B 61 11391 6056 6550 -294 918 -2051 C ATOM 1716 CG1 VAL B 61 -5.923 25.395 22.202 1.00 59.14 C ANISOU 1716 CG1 VAL B 61 10813 5649 6010 -361 732 -1901 C ATOM 1717 CG2 VAL B 61 -8.191 24.823 22.977 1.00 69.71 C ANISOU 1717 CG2 VAL B 61 12181 6939 7366 -194 1024 -1921 C ATOM 1718 N TYR B 62 -4.176 25.522 24.772 1.00 57.90 N ANISOU 1718 N TYR B 62 10864 5821 5315 -498 638 -2320 N ATOM 1719 CA TYR B 62 -2.817 25.995 24.933 1.00 56.44 C ANISOU 1719 CA TYR B 62 10657 5744 5045 -636 481 -2436 C ATOM 1720 C TYR B 62 -1.965 25.542 23.775 1.00 62.71 C ANISOU 1720 C TYR B 62 11342 6587 5897 -657 332 -2204 C ATOM 1721 O TYR B 62 -2.097 24.417 23.292 1.00 52.58 O ANISOU 1721 O TYR B 62 10035 5396 4547 -560 324 -1986 O ATOM 1722 CB TYR B 62 -2.221 25.493 26.241 1.00 68.38 C ANISOU 1722 CB TYR B 62 12231 7585 6164 -643 432 -2563 C ATOM 1723 CG TYR B 62 -2.919 26.036 27.462 1.00 63.47 C ANISOU 1723 CG TYR B 62 11705 6971 5440 -640 573 -2834 C ATOM 1724 CD1 TYR B 62 -4.247 25.715 27.725 1.00 71.21 C ANISOU 1724 CD1 TYR B 62 12730 7862 6467 -503 759 -2777 C ATOM 1725 CD2 TYR B 62 -2.245 26.834 28.375 1.00 63.52 C ANISOU 1725 CD2 TYR B 62 11658 7131 5344 -759 507 -3114 C ATOM 1726 CE1 TYR B 62 -4.894 26.195 28.854 1.00 79.78 C ANISOU 1726 CE1 TYR B 62 13818 8999 7496 -473 883 -2980 C ATOM 1727 CE2 TYR B 62 -2.885 27.323 29.513 1.00 66.16 C ANISOU 1727 CE2 TYR B 62 11994 7524 5618 -729 624 -3341 C ATOM 1728 CZ TYR B 62 -4.209 27.001 29.740 1.00 65.68 C ANISOU 1728 CZ TYR B 62 11990 7364 5601 -581 815 -3265 C ATOM 1729 OH TYR B 62 -4.869 27.470 30.848 1.00 91.27 O ANISOU 1729 OH TYR B 62 15236 10668 8774 -541 940 -3483 O ATOM 1730 N THR B 63 -1.092 26.443 23.346 1.00 59.74 N ANISOU 1730 N THR B 63 10899 6136 5662 -795 237 -2271 N ATOM 1731 CA THR B 63 -0.157 26.206 22.267 1.00 53.92 C ANISOU 1731 CA THR B 63 10047 5455 4986 -834 101 -2076 C ATOM 1732 C THR B 63 1.063 27.073 22.530 1.00 58.46 C ANISOU 1732 C THR B 63 10570 6074 5570 -1020 -9 -2249 C ATOM 1733 O THR B 63 0.961 28.091 23.223 1.00 64.19 O ANISOU 1733 O THR B 63 11343 6673 6375 -1130 51 -2520 O ATOM 1734 CB THR B 63 -0.772 26.570 20.916 1.00 58.14 C ANISOU 1734 CB THR B 63 10507 5756 5828 -794 155 -1885 C ATOM 1735 OG1 THR B 63 -0.077 25.891 19.876 1.00 50.90 O ANISOU 1735 OG1 THR B 63 9489 4969 4882 -781 46 -1661 O ATOM 1736 CG2 THR B 63 -0.688 28.074 20.680 1.00 54.51 C ANISOU 1736 CG2 THR B 63 10018 5024 5669 -906 202 -1988 C ATOM 1737 N PRO B 64 2.225 26.682 21.993 1.00 64.88 N ANISOU 1737 N PRO B 64 11275 7065 6311 -1066 -158 -2116 N ATOM 1738 CA PRO B 64 3.440 27.503 22.124 1.00 67.27 C ANISOU 1738 CA PRO B 64 11489 7423 6649 -1267 -268 -2267 C ATOM 1739 C PRO B 64 3.283 28.972 21.698 1.00 65.46 C ANISOU 1739 C PRO B 64 11241 6832 6798 -1413 -179 -2386 C ATOM 1740 O PRO B 64 2.419 29.322 20.901 1.00 62.50 O ANISOU 1740 O PRO B 64 10879 6182 6687 -1333 -60 -2240 O ATOM 1741 CB PRO B 64 4.429 26.783 21.220 1.00 55.81 C ANISOU 1741 CB PRO B 64 9907 6155 5143 -1242 -396 -2012 C ATOM 1742 CG PRO B 64 4.038 25.352 21.388 1.00 64.54 C ANISOU 1742 CG PRO B 64 11067 7444 6010 -1039 -383 -1844 C ATOM 1743 CD PRO B 64 2.531 25.350 21.452 1.00 62.70 C ANISOU 1743 CD PRO B 64 10955 6989 5880 -936 -220 -1856 C ATOM 1744 N ALA B 65 4.141 29.827 22.240 1.00 73.19 N ANISOU 1744 N ALA B 65 12176 7825 7810 -1631 -228 -2648 N ATOM 1745 CA ALA B 65 3.945 31.257 22.111 1.00 71.82 C ANISOU 1745 CA ALA B 65 12013 7264 8014 -1783 -95 -2825 C ATOM 1746 C ALA B 65 4.361 31.823 20.760 1.00 70.17 C ANISOU 1746 C ALA B 65 11684 6830 8146 -1835 -78 -2574 C ATOM 1747 O ALA B 65 3.922 32.906 20.399 1.00 73.95 O ANISOU 1747 O ALA B 65 12178 6920 9000 -1882 83 -2592 O ATOM 1748 CB ALA B 65 4.685 31.974 23.210 1.00 72.01 C ANISOU 1748 CB ALA B 65 12026 7373 7961 -2030 -132 -3247 C ATOM 1749 N MET B 66 5.218 31.118 20.024 1.00 69.07 N ANISOU 1749 N MET B 66 11423 6934 7887 -1816 -223 -2329 N ATOM 1750 CA MET B 66 5.675 31.623 18.729 1.00 61.93 C ANISOU 1750 CA MET B 66 10394 5869 7269 -1863 -203 -2072 C ATOM 1751 C MET B 66 5.536 30.606 17.616 1.00 66.90 C ANISOU 1751 C MET B 66 10968 6662 7791 -1666 -256 -1698 C ATOM 1752 O MET B 66 5.548 29.404 17.859 1.00 72.26 O ANISOU 1752 O MET B 66 11670 7626 8159 -1543 -347 -1652 O ATOM 1753 CB MET B 66 7.119 32.065 18.807 1.00 64.06 C ANISOU 1753 CB MET B 66 10523 6254 7565 -2108 -308 -2187 C ATOM 1754 CG MET B 66 7.345 33.361 19.572 1.00 67.97 C ANISOU 1754 CG MET B 66 11034 6499 8294 -2369 -219 -2562 C ATOM 1755 SD MET B 66 8.804 33.100 20.575 1.00110.44 S ANISOU 1755 SD MET B 66 16284 12330 13348 -2605 -438 -2869 S ATOM 1756 CE MET B 66 8.337 31.627 21.515 1.00 67.82 C ANISOU 1756 CE MET B 66 10991 7369 7408 -2361 -559 -2874 C ATOM 1757 N GLU B 67 5.420 31.103 16.390 1.00 66.33 N ANISOU 1757 N GLU B 67 10813 6410 7978 -1637 -184 -1431 N ATOM 1758 CA GLU B 67 5.216 30.245 15.233 1.00 58.99 C ANISOU 1758 CA GLU B 67 9819 5645 6951 -1465 -218 -1104 C ATOM 1759 C GLU B 67 6.399 29.305 15.044 1.00 57.65 C ANISOU 1759 C GLU B 67 9553 5823 6529 -1486 -373 -1042 C ATOM 1760 O GLU B 67 6.231 28.120 14.739 1.00 57.21 O ANISOU 1760 O GLU B 67 9505 5985 6249 -1336 -420 -927 O ATOM 1761 CB GLU B 67 5.001 31.089 13.960 1.00 56.79 C ANISOU 1761 CB GLU B 67 9442 5158 6978 -1443 -114 -817 C ATOM 1762 CG GLU B 67 3.790 30.669 13.126 1.00 64.42 C ANISOU 1762 CG GLU B 67 10408 6143 7925 -1223 -55 -579 C ATOM 1763 CD GLU B 67 3.586 31.529 11.877 1.00 84.08 C ANISOU 1763 CD GLU B 67 12777 8489 10682 -1176 45 -252 C ATOM 1764 OE1 GLU B 67 4.482 32.338 11.538 1.00 64.17 O ANISOU 1764 OE1 GLU B 67 10171 5852 8360 -1311 75 -172 O ATOM 1765 OE2 GLU B 67 2.528 31.378 11.223 1.00 93.98 O ANISOU 1765 OE2 GLU B 67 14003 9769 11937 -1002 98 -59 O ATOM 1766 N SER B 68 7.598 29.829 15.243 1.00 56.90 N ANISOU 1766 N SER B 68 9358 5773 6488 -1678 -437 -1130 N ATOM 1767 CA SER B 68 8.803 29.107 14.862 1.00 67.71 C ANISOU 1767 CA SER B 68 10590 7459 7678 -1693 -565 -1018 C ATOM 1768 C SER B 68 8.934 27.835 15.672 1.00 67.60 C ANISOU 1768 C SER B 68 10629 7746 7310 -1579 -666 -1104 C ATOM 1769 O SER B 68 9.559 26.851 15.265 1.00 62.70 O ANISOU 1769 O SER B 68 9931 7382 6509 -1483 -735 -956 O ATOM 1770 CB SER B 68 10.039 29.997 15.044 1.00 59.13 C ANISOU 1770 CB SER B 68 9363 6370 6732 -1947 -610 -1127 C ATOM 1771 OG SER B 68 10.000 30.653 16.294 1.00 73.58 O ANISOU 1771 OG SER B 68 11261 8105 8591 -2109 -611 -1476 O ATOM 1772 N VAL B 69 8.322 27.843 16.832 1.00 55.54 N ANISOU 1772 N VAL B 69 9236 6181 5687 -1573 -652 -1331 N ATOM 1773 CA VAL B 69 8.577 26.758 17.724 1.00 55.09 C ANISOU 1773 CA VAL B 69 9211 6422 5297 -1476 -738 -1394 C ATOM 1774 C VAL B 69 7.287 25.957 17.845 1.00 56.66 C ANISOU 1774 C VAL B 69 9569 6551 5410 -1275 -644 -1341 C ATOM 1775 O VAL B 69 7.054 25.243 18.819 1.00 53.04 O ANISOU 1775 O VAL B 69 9195 6239 4719 -1186 -654 -1422 O ATOM 1776 CB VAL B 69 9.133 27.310 19.045 1.00 63.52 C ANISOU 1776 CB VAL B 69 10267 7614 6254 -1647 -817 -1698 C ATOM 1777 CG1 VAL B 69 8.025 27.753 19.992 1.00 82.39 C ANISOU 1777 CG1 VAL B 69 12830 9824 8649 -1650 -720 -1936 C ATOM 1778 CG2 VAL B 69 10.085 26.321 19.656 1.00 77.60 C ANISOU 1778 CG2 VAL B 69 11960 9822 7701 -1582 -958 -1667 C ATOM 1779 N CYS B 70 6.484 26.094 16.784 1.00 51.67 N ANISOU 1779 N CYS B 70 8949 5716 4965 -1207 -549 -1184 N ATOM 1780 CA CYS B 70 5.294 25.289 16.468 1.00 56.99 C ANISOU 1780 CA CYS B 70 9714 6339 5599 -1032 -459 -1088 C ATOM 1781 C CYS B 70 4.023 25.767 17.132 1.00 65.70 C ANISOU 1781 C CYS B 70 10948 7232 6784 -1009 -352 -1228 C ATOM 1782 O CYS B 70 3.123 24.963 17.387 1.00 64.14 O ANISOU 1782 O CYS B 70 10836 7049 6485 -882 -287 -1219 O ATOM 1783 CB CYS B 70 5.505 23.831 16.832 1.00 48.59 C ANISOU 1783 CB CYS B 70 8683 5505 4274 -897 -485 -1040 C ATOM 1784 SG CYS B 70 6.763 23.086 15.882 1.00 71.45 S ANISOU 1784 SG CYS B 70 11429 8622 7097 -863 -560 -848 S ATOM 1785 N GLY B 71 3.945 27.068 17.391 1.00 55.37 N ANISOU 1785 N GLY B 71 9646 5711 5682 -1133 -312 -1358 N ATOM 1786 CA GLY B 71 2.784 27.655 18.033 1.00 67.42 C ANISOU 1786 CA GLY B 71 11286 7013 7316 -1109 -186 -1508 C ATOM 1787 C GLY B 71 1.661 27.929 17.050 1.00 61.89 C ANISOU 1787 C GLY B 71 10564 6120 6832 -1000 -76 -1322 C ATOM 1788 O GLY B 71 1.890 28.448 15.969 1.00 67.86 O ANISOU 1788 O GLY B 71 11213 6802 7771 -1018 -73 -1133 O ATOM 1789 N TYR B 72 0.441 27.581 17.439 1.00 61.06 N ANISOU 1789 N TYR B 72 10542 5964 6693 -882 19 -1360 N ATOM 1790 CA TYR B 72 -0.721 27.733 16.575 1.00 63.91 C ANISOU 1790 CA TYR B 72 10853 6210 7220 -764 113 -1185 C ATOM 1791 C TYR B 72 -1.278 29.148 16.632 1.00 62.76 C ANISOU 1791 C TYR B 72 10710 5747 7389 -776 243 -1217 C ATOM 1792 O TYR B 72 -1.642 29.617 17.708 1.00 71.61 O ANISOU 1792 O TYR B 72 11939 6722 8546 -801 331 -1452 O ATOM 1793 CB TYR B 72 -1.810 26.729 16.979 1.00 53.72 C ANISOU 1793 CB TYR B 72 9625 5007 5777 -643 171 -1214 C ATOM 1794 CG TYR B 72 -3.177 27.033 16.394 1.00 58.29 C ANISOU 1794 CG TYR B 72 10143 5475 6529 -531 281 -1097 C ATOM 1795 CD1 TYR B 72 -3.530 26.579 15.129 1.00 56.76 C ANISOU 1795 CD1 TYR B 72 9813 5416 6337 -467 249 -878 C ATOM 1796 CD2 TYR B 72 -4.110 27.772 17.105 1.00 50.92 C ANISOU 1796 CD2 TYR B 72 9271 4336 5742 -485 420 -1212 C ATOM 1797 CE1 TYR B 72 -4.775 26.858 14.592 1.00 56.87 C ANISOU 1797 CE1 TYR B 72 9732 5394 6482 -361 332 -760 C ATOM 1798 CE2 TYR B 72 -5.358 28.044 16.584 1.00 51.27 C ANISOU 1798 CE2 TYR B 72 9229 4307 5945 -363 521 -1082 C ATOM 1799 CZ TYR B 72 -5.686 27.590 15.323 1.00 64.93 C ANISOU 1799 CZ TYR B 72 10803 6206 7662 -301 467 -846 C ATOM 1800 OH TYR B 72 -6.931 27.864 14.793 1.00 72.37 O ANISOU 1800 OH TYR B 72 11623 7139 8737 -176 550 -705 O ATOM 1801 N PHE B 73 -1.368 29.834 15.488 1.00 61.51 N ANISOU 1801 N PHE B 73 10431 5480 7459 -744 276 -976 N ATOM 1802 CA PHE B 73 -2.040 31.136 15.483 1.00 62.30 C ANISOU 1802 CA PHE B 73 10526 5245 7900 -707 442 -951 C ATOM 1803 C PHE B 73 -3.390 31.080 14.759 1.00 72.18 C ANISOU 1803 C PHE B 73 11687 6503 9234 -510 524 -719 C ATOM 1804 O PHE B 73 -3.489 30.675 13.601 1.00 70.07 O ANISOU 1804 O PHE B 73 11281 6435 8907 -437 458 -452 O ATOM 1805 CB PHE B 73 -1.145 32.220 14.890 1.00 60.69 C ANISOU 1805 CB PHE B 73 10248 4851 7962 -815 466 -837 C ATOM 1806 CG PHE B 73 -0.307 32.923 15.926 1.00 95.49 C ANISOU 1806 CG PHE B 73 14750 9074 12460 -1017 491 -1159 C ATOM 1807 CD1 PHE B 73 1.080 32.865 15.884 1.00101.10 C ANISOU 1807 CD1 PHE B 73 15416 9907 13092 -1199 366 -1213 C ATOM 1808 CD2 PHE B 73 -0.916 33.608 16.980 1.00105.08 C ANISOU 1808 CD2 PHE B 73 16083 10024 13817 -1034 642 -1438 C ATOM 1809 CE1 PHE B 73 1.849 33.504 16.857 1.00 95.39 C ANISOU 1809 CE1 PHE B 73 14750 9063 12431 -1413 375 -1546 C ATOM 1810 CE2 PHE B 73 -0.156 34.247 17.959 1.00 91.93 C ANISOU 1810 CE2 PHE B 73 14495 8227 12208 -1247 664 -1794 C ATOM 1811 CZ PHE B 73 1.229 34.189 17.898 1.00 81.75 C ANISOU 1811 CZ PHE B 73 13145 7083 10833 -1446 521 -1852 C ATOM 1812 N HIS B 74 -4.431 31.459 15.491 1.00 64.90 N ANISOU 1812 N HIS B 74 10832 5400 8427 -427 668 -844 N ATOM 1813 CA HIS B 74 -5.788 31.432 14.992 1.00 65.71 C ANISOU 1813 CA HIS B 74 10833 5524 8610 -237 755 -655 C ATOM 1814 C HIS B 74 -5.920 32.532 13.965 1.00 65.31 C ANISOU 1814 C HIS B 74 10639 5304 8870 -146 840 -340 C ATOM 1815 O HIS B 74 -5.812 33.694 14.312 1.00 66.44 O ANISOU 1815 O HIS B 74 10832 5091 9322 -161 990 -386 O ATOM 1816 CB HIS B 74 -6.776 31.630 16.135 1.00 79.50 C ANISOU 1816 CB HIS B 74 12686 7105 10415 -173 909 -882 C ATOM 1817 CG HIS B 74 -8.205 31.410 15.744 1.00 78.68 C ANISOU 1817 CG HIS B 74 12460 7084 10350 16 986 -714 C ATOM 1818 ND1 HIS B 74 -8.646 30.222 15.220 1.00 73.61 N ANISOU 1818 ND1 HIS B 74 11723 6779 9467 50 878 -619 N ATOM 1819 CD2 HIS B 74 -9.275 32.230 15.815 1.00 75.84 C ANISOU 1819 CD2 HIS B 74 12043 6521 10253 175 1169 -638 C ATOM 1820 CE1 HIS B 74 -9.948 30.320 14.978 1.00 80.49 C ANISOU 1820 CE1 HIS B 74 12467 7683 10435 207 974 -496 C ATOM 1821 NE2 HIS B 74 -10.353 31.519 15.325 1.00 73.87 N ANISOU 1821 NE2 HIS B 74 11643 6529 9895 301 1148 -485 N ATOM 1822 N ARG B 75 -6.118 32.147 12.703 1.00 79.10 N ANISOU 1822 N ARG B 75 12207 7316 10532 -55 755 -24 N ATOM 1823 CA ARG B 75 -6.230 33.090 11.587 1.00 77.86 C ANISOU 1823 CA ARG B 75 11881 7085 10618 62 825 357 C ATOM 1824 C ARG B 75 -7.575 33.778 11.644 1.00 84.15 C ANISOU 1824 C ARG B 75 12600 7717 11654 272 1001 491 C ATOM 1825 O ARG B 75 -7.666 35.006 11.676 1.00 86.77 O ANISOU 1825 O ARG B 75 12929 7688 12353 345 1185 612 O ATOM 1826 CB ARG B 75 -6.061 32.377 10.233 1.00 61.22 C ANISOU 1826 CB ARG B 75 9589 5402 8271 99 668 635 C ATOM 1827 N SER B 76 -8.617 32.958 11.666 1.00 94.44 N ANISOU 1827 N SER B 76 13833 9281 12767 366 961 467 N ATOM 1828 CA SER B 76 -9.984 33.430 11.788 1.00 99.53 C ANISOU 1828 CA SER B 76 14380 9841 13596 573 1116 575 C ATOM 1829 C SER B 76 -10.099 34.495 12.878 1.00101.31 C ANISOU 1829 C SER B 76 14769 9568 14158 590 1342 384 C ATOM 1830 O SER B 76 -9.305 34.547 13.825 1.00 94.55 O ANISOU 1830 O SER B 76 14123 8511 13290 409 1351 49 O ATOM 1831 CB SER B 76 -10.915 32.238 12.080 1.00 86.04 C ANISOU 1831 CB SER B 76 12633 8443 11616 587 1045 421 C ATOM 1832 OG SER B 76 -12.249 32.642 12.348 1.00 87.06 O ANISOU 1832 OG SER B 76 12665 8500 11915 776 1201 486 O ATOM 1833 N HIS B 77 -11.051 35.393 12.716 1.00117.65 N ANISOU 1833 N HIS B 77 16725 11444 16533 810 1535 598 N ATOM 1834 CA HIS B 77 -11.512 36.107 13.884 1.00134.06 C ANISOU 1834 CA HIS B 77 18952 13114 18872 848 1767 340 C ATOM 1835 C HIS B 77 -12.996 35.854 13.997 1.00146.83 C ANISOU 1835 C HIS B 77 20433 14876 20479 1060 1849 414 C ATOM 1836 O HIS B 77 -13.800 36.786 13.933 1.00148.34 O ANISOU 1836 O HIS B 77 20527 14830 21005 1283 2066 603 O ATOM 1837 CB HIS B 77 -11.195 37.605 13.842 1.00132.05 C ANISOU 1837 CB HIS B 77 18729 12347 19096 905 2004 456 C ATOM 1838 CG HIS B 77 -11.836 38.386 14.959 1.00155.41 C ANISOU 1838 CG HIS B 77 21817 14879 22354 978 2283 190 C ATOM 1839 ND1 HIS B 77 -13.199 38.427 15.147 1.00170.29 N ANISOU 1839 ND1 HIS B 77 23595 16788 24317 1218 2422 272 N ATOM 1840 CD2 HIS B 77 -11.292 39.101 15.969 1.00168.85 C ANISOU 1840 CD2 HIS B 77 23736 16152 24267 827 2447 -191 C ATOM 1841 CE1 HIS B 77 -13.475 39.171 16.213 1.00175.01 C ANISOU 1841 CE1 HIS B 77 24351 16963 25182 1233 2681 -33 C ATOM 1842 NE2 HIS B 77 -12.338 39.585 16.726 1.00175.76 N ANISOU 1842 NE2 HIS B 77 24646 16783 25354 990 2699 -333 N ATOM 1843 N ASN B 78 -13.351 34.575 14.075 1.00150.60 N ANISOU 1843 N ASN B 78 20877 15754 20589 997 1681 298 N ATOM 1844 CA ASN B 78 -14.589 34.194 14.721 1.00140.17 C ANISOU 1844 CA ASN B 78 19516 14512 19230 1103 1778 178 C ATOM 1845 C ASN B 78 -15.816 34.791 14.051 1.00129.45 C ANISOU 1845 C ASN B 78 17884 13205 18097 1391 1902 540 C ATOM 1846 O ASN B 78 -16.160 35.951 14.236 1.00121.77 O ANISOU 1846 O ASN B 78 16903 11868 17495 1565 2134 646 O ATOM 1847 CB ASN B 78 -14.502 34.608 16.199 1.00126.79 C ANISOU 1847 CB ASN B 78 18081 12448 17645 1037 1962 -224 C ATOM 1848 CG ASN B 78 -15.790 34.364 16.983 1.00122.04 C ANISOU 1848 CG ASN B 78 17450 11879 17041 1162 2114 -355 C ATOM 1849 OD1 ASN B 78 -16.820 34.025 16.433 1.00118.45 O ANISOU 1849 OD1 ASN B 78 16764 11679 16563 1311 2105 -132 O ATOM 1850 ND2 ASN B 78 -15.724 34.576 18.289 1.00124.27 N ANISOU 1850 ND2 ASN B 78 17955 11919 17341 1095 2263 -727 N ATOM 1851 N ARG B 79 -16.488 33.967 13.276 1.00123.73 N ANISOU 1851 N ARG B 79 16919 12946 17146 1441 1754 721 N ATOM 1852 CA ARG B 79 -17.795 34.312 12.793 1.00108.37 C ANISOU 1852 CA ARG B 79 14680 11156 15340 1704 1848 1018 C ATOM 1853 C ARG B 79 -18.722 33.663 13.813 1.00115.67 C ANISOU 1853 C ARG B 79 15642 12130 16178 1685 1931 723 C ATOM 1854 O ARG B 79 -19.941 33.771 13.724 1.00117.86 O ANISOU 1854 O ARG B 79 15689 12547 16546 1878 2027 870 O ATOM 1855 CB ARG B 79 -17.968 33.787 11.376 1.00 92.64 C ANISOU 1855 CB ARG B 79 12382 9696 13120 1740 1631 1348 C ATOM 1856 N SER B 80 -18.078 33.077 14.831 1.00113.03 N ANISOU 1856 N SER B 80 15600 11664 15684 1462 1912 321 N ATOM 1857 CA SER B 80 -18.574 31.993 15.687 1.00106.67 C ANISOU 1857 CA SER B 80 14865 11016 14648 1347 1909 24 C ATOM 1858 C SER B 80 -18.599 30.738 14.856 1.00 97.60 C ANISOU 1858 C SER B 80 13558 10334 13190 1217 1677 83 C ATOM 1859 O SER B 80 -19.497 29.897 14.978 1.00 83.12 O ANISOU 1859 O SER B 80 11594 8755 11232 1195 1677 17 O ATOM 1860 CB SER B 80 -19.914 32.321 16.315 1.00102.47 C ANISOU 1860 CB SER B 80 14227 10416 14291 1536 2136 8 C ATOM 1861 OG SER B 80 -19.681 33.218 17.385 1.00 99.33 O ANISOU 1861 OG SER B 80 14069 9565 14107 1576 2357 -206 O ATOM 1862 N GLU B 81 -17.576 30.660 14.001 1.00 87.94 N ANISOU 1862 N GLU B 81 12346 9204 11865 1122 1498 198 N ATOM 1863 CA GLU B 81 -17.155 29.423 13.389 1.00 80.24 C ANISOU 1863 CA GLU B 81 11329 8583 10575 937 1285 144 C ATOM 1864 C GLU B 81 -16.873 28.423 14.466 1.00 79.99 C ANISOU 1864 C GLU B 81 11535 8492 10367 756 1298 -205 C ATOM 1865 O GLU B 81 -16.219 28.719 15.466 1.00 82.02 O ANISOU 1865 O GLU B 81 12055 8450 10658 705 1374 -399 O ATOM 1866 CB GLU B 81 -15.895 29.591 12.556 1.00 74.70 C ANISOU 1866 CB GLU B 81 10670 7907 9805 859 1131 268 C ATOM 1867 CG GLU B 81 -16.045 30.394 11.315 1.00 88.69 C ANISOU 1867 CG GLU B 81 12190 9822 11685 1024 1093 663 C ATOM 1868 CD GLU B 81 -14.804 30.308 10.480 1.00 96.15 C ANISOU 1868 CD GLU B 81 13170 10863 12500 916 935 762 C ATOM 1869 OE1 GLU B 81 -13.910 31.156 10.684 1.00106.67 O ANISOU 1869 OE1 GLU B 81 14659 11861 14008 912 992 801 O ATOM 1870 OE2 GLU B 81 -14.711 29.380 9.643 1.00 93.06 O ANISOU 1870 OE2 GLU B 81 12646 10877 11836 821 766 775 O ATOM 1871 N GLU B 82 -17.363 27.222 14.249 1.00 71.30 N ANISOU 1871 N GLU B 82 10326 7692 9073 653 1231 -283 N ATOM 1872 CA GLU B 82 -16.998 26.130 15.099 1.00 70.71 C ANISOU 1872 CA GLU B 82 10460 7587 8822 483 1240 -554 C ATOM 1873 C GLU B 82 -15.783 25.507 14.463 1.00 73.27 C ANISOU 1873 C GLU B 82 10859 8018 8963 334 1060 -567 C ATOM 1874 O GLU B 82 -15.691 25.383 13.238 1.00 74.64 O ANISOU 1874 O GLU B 82 10842 8444 9074 322 926 -414 O ATOM 1875 CB GLU B 82 -18.149 25.145 15.234 1.00 82.96 C ANISOU 1875 CB GLU B 82 11861 9352 10309 437 1303 -637 C ATOM 1876 CG GLU B 82 -19.505 25.836 15.099 1.00 87.42 C ANISOU 1876 CG GLU B 82 12169 9988 11058 617 1414 -491 C ATOM 1877 CD GLU B 82 -20.566 25.189 15.940 1.00 81.62 C ANISOU 1877 CD GLU B 82 11399 9284 10328 592 1575 -640 C ATOM 1878 OE1 GLU B 82 -20.270 24.118 16.498 1.00 83.82 O ANISOU 1878 OE1 GLU B 82 11835 9551 10461 426 1592 -832 O ATOM 1879 OE2 GLU B 82 -21.682 25.745 16.049 1.00 90.76 O ANISOU 1879 OE2 GLU B 82 12365 10474 11647 749 1698 -546 O ATOM 1880 N PHE B 83 -14.836 25.149 15.309 1.00 67.12 N ANISOU 1880 N PHE B 83 11105 6865 7534 36 483 -1782 N ATOM 1881 CA PHE B 83 -13.604 24.556 14.861 1.00 60.14 C ANISOU 1881 CA PHE B 83 10361 5890 6598 -34 582 -1505 C ATOM 1882 C PHE B 83 -13.425 23.156 15.449 1.00 64.55 C ANISOU 1882 C PHE B 83 10919 6551 7056 -111 727 -1403 C ATOM 1883 O PHE B 83 -13.666 22.923 16.632 1.00 72.55 O ANISOU 1883 O PHE B 83 11883 7672 8010 -153 723 -1510 O ATOM 1884 CB PHE B 83 -12.445 25.461 15.246 1.00 52.05 C ANISOU 1884 CB PHE B 83 9392 4750 5634 -79 507 -1488 C ATOM 1885 CG PHE B 83 -12.267 26.612 14.338 1.00 39.66 C ANISOU 1885 CG PHE B 83 7909 3011 4150 -38 426 -1476 C ATOM 1886 CD1 PHE B 83 -12.879 27.821 14.599 1.00 53.71 C ANISOU 1886 CD1 PHE B 83 9645 4748 6014 21 293 -1676 C ATOM 1887 CD2 PHE B 83 -11.480 26.488 13.207 1.00 54.32 C ANISOU 1887 CD2 PHE B 83 9909 4734 5995 -71 505 -1269 C ATOM 1888 CE1 PHE B 83 -12.707 28.907 13.758 1.00 56.35 C ANISOU 1888 CE1 PHE B 83 10109 4889 6413 57 218 -1644 C ATOM 1889 CE2 PHE B 83 -11.302 27.570 12.350 1.00 60.84 C ANISOU 1889 CE2 PHE B 83 10867 5388 6863 -52 439 -1242 C ATOM 1890 CZ PHE B 83 -11.921 28.781 12.624 1.00 62.17 C ANISOU 1890 CZ PHE B 83 11026 5493 7104 19 285 -1416 C ATOM 1891 N LEU B 84 -13.017 22.211 14.620 1.00 76.82 N ANISOU 1891 N LEU B 84 12548 8057 8582 -140 868 -1196 N ATOM 1892 CA LEU B 84 -12.676 20.908 15.155 1.00 64.81 C ANISOU 1892 CA LEU B 84 11055 6579 6991 -211 1010 -1083 C ATOM 1893 C LEU B 84 -11.250 20.965 15.651 1.00 64.78 C ANISOU 1893 C LEU B 84 11245 6423 6945 -274 1041 -985 C ATOM 1894 O LEU B 84 -10.332 21.293 14.896 1.00 71.51 O ANISOU 1894 O LEU B 84 12190 7129 7853 -282 1079 -887 O ATOM 1895 CB LEU B 84 -12.841 19.807 14.117 1.00 63.44 C ANISOU 1895 CB LEU B 84 10920 6379 6806 -237 1191 -918 C ATOM 1896 CG LEU B 84 -12.459 18.518 14.829 1.00 68.85 C ANISOU 1896 CG LEU B 84 11660 7066 7434 -308 1334 -816 C ATOM 1897 CD1 LEU B 84 -13.597 17.538 14.816 1.00 58.94 C ANISOU 1897 CD1 LEU B 84 10362 5886 6147 -355 1452 -835 C ATOM 1898 CD2 LEU B 84 -11.227 17.931 14.209 1.00 80.47 C ANISOU 1898 CD2 LEU B 84 13314 8358 8904 -349 1520 -610 C ATOM 1899 N ILE B 85 -11.074 20.678 16.932 1.00 62.52 N ANISOU 1899 N ILE B 85 11040 6163 6550 -328 1021 -1038 N ATOM 1900 CA ILE B 85 -9.758 20.693 17.549 1.00 53.52 C ANISOU 1900 CA ILE B 85 10124 4862 5347 -386 1004 -992 C ATOM 1901 C ILE B 85 -9.442 19.280 18.008 1.00 55.28 C ANISOU 1901 C ILE B 85 10540 5028 5435 -424 1146 -869 C ATOM 1902 O ILE B 85 -10.239 18.635 18.696 1.00 59.43 O ANISOU 1902 O ILE B 85 11067 5672 5840 -461 1182 -893 O ATOM 1903 CB ILE B 85 -9.691 21.680 18.742 1.00 51.83 C ANISOU 1903 CB ILE B 85 9926 4695 5071 -434 806 -1173 C ATOM 1904 CG1 ILE B 85 -10.440 22.968 18.415 1.00 60.92 C ANISOU 1904 CG1 ILE B 85 10856 5932 6361 -372 690 -1331 C ATOM 1905 CG2 ILE B 85 -8.255 22.000 19.145 1.00 49.25 C ANISOU 1905 CG2 ILE B 85 9800 4175 4738 -501 707 -1165 C ATOM 1906 CD1 ILE B 85 -10.026 24.153 19.262 1.00 56.53 C ANISOU 1906 CD1 ILE B 85 10315 5354 5811 -424 523 -1493 C ATOM 1907 N ALA B 86 -8.287 18.783 17.602 1.00 59.10 N ANISOU 1907 N ALA B 86 11170 5309 5977 -410 1240 -749 N ATOM 1908 CA ALA B 86 -7.838 17.478 18.032 1.00 54.75 C ANISOU 1908 CA ALA B 86 10848 4630 5325 -404 1362 -637 C ATOM 1909 C ALA B 86 -6.441 17.657 18.596 1.00 50.08 C ANISOU 1909 C ALA B 86 10446 3760 4823 -398 1199 -639 C ATOM 1910 O ALA B 86 -5.549 18.098 17.896 1.00 67.20 O ANISOU 1910 O ALA B 86 12458 5780 7296 -383 1195 -596 O ATOM 1911 CB ALA B 86 -7.859 16.488 16.870 1.00 45.58 C ANISOU 1911 CB ALA B 86 9590 3446 4285 -361 1636 -481 C ATOM 1912 N GLY B 87 -6.263 17.331 19.868 1.00 57.75 N ANISOU 1912 N GLY B 87 11594 4766 5584 -429 999 -610 N ATOM 1913 CA GLY B 87 -5.043 17.674 20.573 1.00 54.86 C ANISOU 1913 CA GLY B 87 11067 4414 5364 -424 654 -487 C ATOM 1914 C GLY B 87 -4.780 16.823 21.804 1.00 61.00 C ANISOU 1914 C GLY B 87 11985 5272 5921 -410 428 -304 C ATOM 1915 O GLY B 87 -5.564 15.931 22.154 1.00 63.51 O ANISOU 1915 O GLY B 87 12568 5618 5945 -428 577 -265 O ATOM 1916 N LYS B 88 -3.662 17.114 22.460 1.00 59.12 N ANISOU 1916 N LYS B 88 11585 5062 5816 -391 57 -200 N ATOM 1917 CA LYS B 88 -3.185 16.321 23.575 1.00 68.88 C ANISOU 1917 CA LYS B 88 12947 6343 6883 -347 -250 23 C ATOM 1918 C LYS B 88 -3.579 16.947 24.892 1.00 76.94 C ANISOU 1918 C LYS B 88 14210 7563 7460 -523 -520 -114 C ATOM 1919 O LYS B 88 -3.685 18.174 25.012 1.00 81.94 O ANISOU 1919 O LYS B 88 14760 8293 8079 -648 -590 -363 O ATOM 1920 CB LYS B 88 -1.662 16.164 23.506 1.00 68.68 C ANISOU 1920 CB LYS B 88 12564 6229 7302 -198 -543 214 C ATOM 1921 CG LYS B 88 -1.181 15.318 22.325 1.00 64.67 C ANISOU 1921 CG LYS B 88 11829 5501 7243 -31 -263 362 C ATOM 1922 CD LYS B 88 -1.528 13.838 22.512 1.00 70.95 C ANISOU 1922 CD LYS B 88 12877 6192 7888 87 -150 605 C ATOM 1923 CE LYS B 88 -0.652 12.949 21.627 1.00 59.17 C ANISOU 1923 CE LYS B 88 11091 4467 6923 284 -7 781 C ATOM 1924 NZ LYS B 88 -0.819 13.254 20.177 1.00 66.41 N ANISOU 1924 NZ LYS B 88 11822 5287 8124 229 448 623 N ATOM 1925 N LEU B 89 -3.816 16.092 25.878 1.00 77.54 N ANISOU 1925 N LEU B 89 14623 7680 7158 -552 -646 42 N ATOM 1926 CA LEU B 89 -4.052 16.550 27.238 1.00 74.91 C ANISOU 1926 CA LEU B 89 14569 7529 6363 -749 -926 -57 C ATOM 1927 C LEU B 89 -2.742 16.408 27.962 1.00 78.74 C ANISOU 1927 C LEU B 89 14946 8031 6943 -657 -1460 183 C ATOM 1928 O LEU B 89 -2.320 15.294 28.248 1.00 78.10 O ANISOU 1928 O LEU B 89 14997 7843 6835 -513 -1618 495 O ATOM 1929 CB LEU B 89 -5.146 15.732 27.921 1.00 70.32 C ANISOU 1929 CB LEU B 89 14493 6976 5250 -891 -726 -56 C ATOM 1930 CG LEU B 89 -5.670 16.061 29.322 1.00 99.83 C ANISOU 1930 CG LEU B 89 18636 10888 8406 -1171 -881 -202 C ATOM 1931 CD1 LEU B 89 -6.999 15.334 29.534 1.00108.64 C ANISOU 1931 CD1 LEU B 89 20022 11995 9262 -1314 -443 -298 C ATOM 1932 CD2 LEU B 89 -4.691 15.692 30.461 1.00117.05 C ANISOU 1932 CD2 LEU B 89 21008 13098 10368 -1164 -1424 90 C ATOM 1933 N GLN B 90 -2.081 17.525 28.241 1.00 82.58 N ANISOU 1933 N GLN B 90 15180 8634 7562 -728 -1750 31 N ATOM 1934 CA GLN B 90 -0.894 17.473 29.064 1.00 75.81 C ANISOU 1934 CA GLN B 90 14215 7837 6752 -669 -2313 205 C ATOM 1935 C GLN B 90 -1.114 18.191 30.406 1.00 96.88 C ANISOU 1935 C GLN B 90 17171 10731 8908 -936 -2618 47 C ATOM 1936 O GLN B 90 -1.338 19.417 30.455 1.00 76.73 O ANISOU 1936 O GLN B 90 14513 8299 6344 -1122 -2557 -275 O ATOM 1937 CB GLN B 90 0.297 18.065 28.333 1.00 78.84 C ANISOU 1937 CB GLN B 90 14022 8174 7761 -542 -2445 161 C ATOM 1938 CG GLN B 90 1.594 17.744 29.043 1.00113.36 C ANISOU 1938 CG GLN B 90 18202 12581 12288 -409 -3036 359 C ATOM 1939 CD GLN B 90 2.786 18.400 28.405 1.00122.14 C ANISOU 1939 CD GLN B 90 18708 13669 14030 -334 -3152 240 C ATOM 1940 OE1 GLN B 90 3.048 19.588 28.614 1.00115.88 O ANISOU 1940 OE1 GLN B 90 17746 13014 13270 -517 -3259 -22 O ATOM 1941 NE2 GLN B 90 3.525 17.627 27.616 1.00126.83 N ANISOU 1941 NE2 GLN B 90 18969 14074 15147 -83 -3098 405 N ATOM 1942 N ASP B 91 -1.040 17.415 31.488 1.00 95.11 N ANISOU 1942 N ASP B 91 17343 10543 8252 -963 -2940 275 N ATOM 1943 CA ASP B 91 -1.262 17.951 32.828 1.00102.10 C ANISOU 1943 CA ASP B 91 18587 11635 8570 -1252 -3225 147 C ATOM 1944 C ASP B 91 -2.574 18.708 32.905 1.00 82.48 C ANISOU 1944 C ASP B 91 16323 9248 5769 -1547 -2774 -240 C ATOM 1945 O ASP B 91 -2.589 19.876 33.277 1.00102.48 O ANISOU 1945 O ASP B 91 18763 11933 8242 -1750 -2846 -542 O ATOM 1946 CB ASP B 91 -0.121 18.884 33.261 1.00112.49 C ANISOU 1946 CB ASP B 91 19553 13104 10085 -1280 -3732 57 C ATOM 1947 CG ASP B 91 1.178 18.145 33.523 1.00124.78 C ANISOU 1947 CG ASP B 91 20929 14608 11874 -1016 -4304 403 C ATOM 1948 OD1 ASP B 91 1.288 17.490 34.586 1.00127.19 O ANISOU 1948 OD1 ASP B 91 21664 14948 11716 -1044 -4707 637 O ATOM 1949 OD2 ASP B 91 2.092 18.237 32.675 1.00128.58 O ANISOU 1949 OD2 ASP B 91 20847 15003 13004 -787 -4359 425 O ATOM 1950 N GLY B 92 -3.664 18.045 32.545 1.00 77.04 N ANISOU 1950 N GLY B 92 15899 8462 4910 -1569 -2305 -258 N ATOM 1951 CA GLY B 92 -4.973 18.667 32.578 1.00 74.88 C ANISOU 1951 CA GLY B 92 15603 8269 4581 -1770 -1799 -618 C ATOM 1952 C GLY B 92 -5.295 19.600 31.415 1.00 88.51 C ANISOU 1952 C GLY B 92 16955 9960 6716 -1701 -1505 -901 C ATOM 1953 O GLY B 92 -6.457 19.945 31.207 1.00 87.97 O ANISOU 1953 O GLY B 92 16673 9936 6816 -1736 -1052 -1108 O ATOM 1954 N LEU B 93 -4.291 20.015 30.647 1.00 87.36 N ANISOU 1954 N LEU B 93 16494 9740 6961 -1538 -1714 -847 N ATOM 1955 CA LEU B 93 -4.518 21.064 29.652 1.00 79.91 C ANISOU 1955 CA LEU B 93 15220 8741 6401 -1505 -1466 -1114 C ATOM 1956 C LEU B 93 -4.564 20.527 28.234 1.00 67.57 C ANISOU 1956 C LEU B 93 13441 6987 5246 -1263 -1162 -980 C ATOM 1957 O LEU B 93 -3.713 19.751 27.823 1.00 67.45 O ANISOU 1957 O LEU B 93 13267 6868 5492 -1072 -1271 -679 O ATOM 1958 CB LEU B 93 -3.437 22.152 29.747 1.00 67.05 C ANISOU 1958 CB LEU B 93 13264 7162 5050 -1533 -1789 -1196 C ATOM 1959 CG LEU B 93 -3.220 22.674 31.166 1.00 82.67 C ANISOU 1959 CG LEU B 93 15434 9345 6632 -1785 -2143 -1317 C ATOM 1960 CD1 LEU B 93 -2.148 23.759 31.206 1.00 89.64 C ANISOU 1960 CD1 LEU B 93 15960 10279 7820 -1829 -2436 -1434 C ATOM 1961 CD2 LEU B 93 -4.527 23.175 31.751 1.00 70.53 C ANISOU 1961 CD2 LEU B 93 13956 7934 4906 -1942 -1774 -1563 C ATOM 1962 N LEU B 94 -5.568 20.971 27.494 1.00 60.04 N ANISOU 1962 N LEU B 94 12478 5983 4353 -1276 -791 -1227 N ATOM 1963 CA LEU B 94 -5.629 20.755 26.059 1.00 58.20 C ANISOU 1963 CA LEU B 94 12037 5576 4502 -1086 -511 -1162 C ATOM 1964 C LEU B 94 -4.514 21.469 25.350 1.00 59.88 C ANISOU 1964 C LEU B 94 11893 5688 5171 -1003 -641 -1115 C ATOM 1965 O LEU B 94 -4.376 22.686 25.451 1.00 71.53 O ANISOU 1965 O LEU B 94 13269 7186 6722 -1105 -732 -1334 O ATOM 1966 CB LEU B 94 -6.942 21.249 25.508 1.00 52.57 C ANISOU 1966 CB LEU B 94 11203 4907 3866 -1080 -162 -1377 C ATOM 1967 CG LEU B 94 -7.034 20.899 24.050 1.00 66.44 C ANISOU 1967 CG LEU B 94 12842 6493 5911 -912 91 -1296 C ATOM 1968 CD1 LEU B 94 -6.758 19.414 23.907 1.00 74.18 C ANISOU 1968 CD1 LEU B 94 14044 7359 6781 -840 173 -1062 C ATOM 1969 CD2 LEU B 94 -8.423 21.231 23.604 1.00 73.71 C ANISOU 1969 CD2 LEU B 94 13416 7588 7003 -849 334 -1369 C ATOM 1970 N HIS B 95 -3.724 20.710 24.615 1.00 68.74 N ANISOU 1970 N HIS B 95 12825 6681 6612 -836 -614 -852 N ATOM 1971 CA HIS B 95 -2.588 21.273 23.912 1.00 55.49 C ANISOU 1971 CA HIS B 95 10795 4894 5395 -786 -687 -824 C ATOM 1972 C HIS B 95 -2.663 21.041 22.408 1.00 52.69 C ANISOU 1972 C HIS B 95 10325 4336 5357 -679 -323 -777 C ATOM 1973 O HIS B 95 -2.987 19.948 21.954 1.00 69.12 O ANISOU 1973 O HIS B 95 12482 6350 7430 -571 -117 -618 O ATOM 1974 CB HIS B 95 -1.299 20.684 24.463 1.00 59.02 C ANISOU 1974 CB HIS B 95 11043 5370 6013 -707 -1036 -595 C ATOM 1975 CG HIS B 95 -0.641 21.558 25.479 1.00 75.79 C ANISOU 1975 CG HIS B 95 13076 7649 8071 -843 -1436 -716 C ATOM 1976 ND1 HIS B 95 -0.895 21.454 26.830 1.00 75.42 N ANISOU 1976 ND1 HIS B 95 13291 7789 7577 -948 -1731 -715 N ATOM 1977 CD2 HIS B 95 0.243 22.571 25.336 1.00 63.48 C ANISOU 1977 CD2 HIS B 95 11216 6087 6819 -923 -1568 -865 C ATOM 1978 CE1 HIS B 95 -0.182 22.357 27.477 1.00 67.37 C ANISOU 1978 CE1 HIS B 95 12118 6889 6591 -1077 -2054 -854 C ATOM 1979 NE2 HIS B 95 0.514 23.050 26.594 1.00 78.32 N ANISOU 1979 NE2 HIS B 95 13149 8164 8445 -1062 -1956 -955 N ATOM 1980 N ILE B 96 -2.347 22.066 21.632 1.00 52.16 N ANISOU 1980 N ILE B 96 10108 4157 5554 -733 -232 -919 N ATOM 1981 CA ILE B 96 -2.261 21.897 20.195 1.00 51.26 C ANISOU 1981 CA ILE B 96 9914 3836 5725 -672 94 -867 C ATOM 1982 C ILE B 96 -1.002 22.569 19.678 1.00 60.58 C ANISOU 1982 C ILE B 96 10805 4892 7321 -738 68 -894 C ATOM 1983 O ILE B 96 -0.448 23.444 20.335 1.00 71.10 O ANISOU 1983 O ILE B 96 12026 6296 8693 -846 -174 -1020 O ATOM 1984 CB ILE B 96 -3.476 22.485 19.476 1.00 57.17 C ANISOU 1984 CB ILE B 96 10889 4514 6317 -692 334 -1041 C ATOM 1985 CG1 ILE B 96 -3.664 23.942 19.863 1.00 52.27 C ANISOU 1985 CG1 ILE B 96 10318 3909 5632 -809 190 -1290 C ATOM 1986 CG2 ILE B 96 -4.735 21.703 19.781 1.00 50.77 C ANISOU 1986 CG2 ILE B 96 10312 3814 5166 -636 442 -1056 C ATOM 1987 CD1 ILE B 96 -4.650 24.666 18.984 1.00 54.93 C ANISOU 1987 CD1 ILE B 96 10565 4324 5984 -737 355 -1331 C ATOM 1988 N THR B 97 -0.549 22.151 18.503 1.00 64.15 N ANISOU 1988 N THR B 97 11137 5157 8079 -705 346 -805 N ATOM 1989 CA THR B 97 0.567 22.819 17.833 1.00 72.90 C ANISOU 1989 CA THR B 97 11998 6111 9589 -818 429 -881 C ATOM 1990 C THR B 97 0.224 23.158 16.383 1.00 62.28 C ANISOU 1990 C THR B 97 10817 4533 8315 -889 821 -924 C ATOM 1991 O THR B 97 -0.905 22.967 15.946 1.00 61.84 O ANISOU 1991 O THR B 97 11035 4464 7996 -829 967 -906 O ATOM 1992 CB THR B 97 1.825 21.951 17.823 1.00 67.54 C ANISOU 1992 CB THR B 97 10943 5404 9314 -750 384 -755 C ATOM 1993 OG1 THR B 97 1.628 20.887 16.903 1.00 68.50 O ANISOU 1993 OG1 THR B 97 11098 5393 9536 -655 709 -610 O ATOM 1994 CG2 THR B 97 2.095 21.363 19.187 1.00 57.29 C ANISOU 1994 CG2 THR B 97 9547 4313 7909 -632 -38 -646 C ATOM 1995 N THR B 98 1.211 23.648 15.642 1.00 63.52 N ANISOU 1995 N THR B 98 10803 4512 8820 -1031 986 -992 N ATOM 1996 CA THR B 98 1.092 23.852 14.201 1.00 50.89 C ANISOU 1996 CA THR B 98 9237 2838 7261 -1081 1306 -959 C ATOM 1997 C THR B 98 0.630 22.568 13.474 1.00 57.61 C ANISOU 1997 C THR B 98 10061 3786 8043 -937 1506 -773 C ATOM 1998 O THR B 98 -0.145 22.628 12.529 1.00 66.29 O ANISOU 1998 O THR B 98 11220 5060 8907 -892 1619 -707 O ATOM 1999 CB THR B 98 2.439 24.320 13.611 1.00 53.66 C ANISOU 1999 CB THR B 98 9347 3026 8017 -1275 1474 -1056 C ATOM 2000 OG1 THR B 98 2.677 25.691 13.960 1.00 74.36 O ANISOU 2000 OG1 THR B 98 12006 5621 10627 -1425 1338 -1228 O ATOM 2001 CG2 THR B 98 2.440 24.209 12.105 1.00 74.83 C ANISOU 2001 CG2 THR B 98 11989 5784 10657 -1288 1764 -956 C ATOM 2002 N CYS B 99 1.099 21.422 13.962 1.00 49.99 N ANISOU 2002 N CYS B 99 9016 2690 7287 -867 1533 -699 N ATOM 2003 CA CYS B 99 0.874 20.101 13.378 1.00 51.81 C ANISOU 2003 CA CYS B 99 9177 2984 7526 -743 1736 -537 C ATOM 2004 C CYS B 99 -0.429 19.466 13.733 1.00 52.39 C ANISOU 2004 C CYS B 99 9462 3250 7194 -601 1675 -448 C ATOM 2005 O CYS B 99 -0.825 18.469 13.141 1.00 63.75 O ANISOU 2005 O CYS B 99 10860 4798 8563 -526 1858 -346 O ATOM 2006 CB CYS B 99 1.955 19.131 13.824 1.00 55.36 C ANISOU 2006 CB CYS B 99 9375 3244 8415 -674 1744 -466 C ATOM 2007 SG CYS B 99 3.612 19.652 13.422 1.00133.68 S ANISOU 2007 SG CYS B 99 18851 13015 18927 -835 1831 -622 S ATOM 2008 N SER B 100 -1.075 19.990 14.749 1.00 54.63 N ANISOU 2008 N SER B 100 9968 3580 7211 -586 1432 -520 N ATOM 2009 CA SER B 100 -2.311 19.378 15.176 1.00 56.96 C ANISOU 2009 CA SER B 100 10451 4060 7131 -483 1405 -480 C ATOM 2010 C SER B 100 -3.378 19.564 14.109 1.00 57.67 C ANISOU 2010 C SER B 100 10506 4407 7000 -473 1550 -492 C ATOM 2011 O SER B 100 -3.324 20.496 13.310 1.00 59.38 O ANISOU 2011 O SER B 100 10657 4655 7249 -536 1566 -539 O ATOM 2012 CB SER B 100 -2.752 19.968 16.510 1.00 59.05 C ANISOU 2012 CB SER B 100 10953 4351 7135 -503 1114 -601 C ATOM 2013 OG SER B 100 -1.870 19.530 17.538 1.00 63.57 O ANISOU 2013 OG SER B 100 11328 5015 7810 -455 840 -485 O ATOM 2014 N PHE B 101 -4.343 18.662 14.096 1.00 59.23 N ANISOU 2014 N PHE B 101 10775 4761 6969 -404 1648 -441 N ATOM 2015 CA PHE B 101 -5.479 18.819 13.221 1.00 48.16 C ANISOU 2015 CA PHE B 101 9365 3577 5358 -404 1732 -450 C ATOM 2016 C PHE B 101 -6.497 19.773 13.800 1.00 54.01 C ANISOU 2016 C PHE B 101 10177 4435 5908 -396 1519 -558 C ATOM 2017 O PHE B 101 -7.224 19.434 14.736 1.00 69.04 O ANISOU 2017 O PHE B 101 12158 6425 7649 -374 1448 -598 O ATOM 2018 CB PHE B 101 -6.167 17.483 12.951 1.00 43.45 C ANISOU 2018 CB PHE B 101 8784 3098 4627 -369 1935 -365 C ATOM 2019 CG PHE B 101 -7.150 17.565 11.813 1.00 60.16 C ANISOU 2019 CG PHE B 101 10868 5377 6613 -401 2023 -337 C ATOM 2020 CD1 PHE B 101 -8.453 17.992 12.030 1.00 59.57 C ANISOU 2020 CD1 PHE B 101 10808 5419 6405 -394 1864 -372 C ATOM 2021 CD2 PHE B 101 -6.748 17.290 10.516 1.00 56.69 C ANISOU 2021 CD2 PHE B 101 10361 4943 6236 -441 2229 -292 C ATOM 2022 CE1 PHE B 101 -9.349 18.102 10.981 1.00 54.53 C ANISOU 2022 CE1 PHE B 101 10129 4860 5730 -409 1870 -341 C ATOM 2023 CE2 PHE B 101 -7.648 17.395 9.452 1.00 58.90 C ANISOU 2023 CE2 PHE B 101 10676 5328 6377 -485 2278 -251 C ATOM 2024 CZ PHE B 101 -8.951 17.799 9.690 1.00 42.45 C ANISOU 2024 CZ PHE B 101 8617 3312 4201 -464 2072 -258 C ATOM 2025 N VAL B 102 -6.562 20.955 13.216 1.00 54.73 N ANISOU 2025 N VAL B 102 9520 5040 6234 673 592 478 N ATOM 2026 CA VAL B 102 -7.517 21.972 13.598 1.00 42.21 C ANISOU 2026 CA VAL B 102 8077 3376 4584 849 701 427 C ATOM 2027 C VAL B 102 -8.084 22.580 12.335 1.00 49.28 C ANISOU 2027 C VAL B 102 8855 4330 5539 1190 581 371 C ATOM 2028 O VAL B 102 -7.335 22.930 11.439 1.00 58.66 O ANISOU 2028 O VAL B 102 9780 5731 6778 1216 347 425 O ATOM 2029 CB VAL B 102 -6.860 23.044 14.466 1.00 47.36 C ANISOU 2029 CB VAL B 102 8753 4120 5123 845 627 463 C ATOM 2030 CG1 VAL B 102 -7.770 24.262 14.626 1.00 40.61 C ANISOU 2030 CG1 VAL B 102 7996 3214 4219 1096 699 418 C ATOM 2031 CG2 VAL B 102 -6.482 22.437 15.803 1.00 50.86 C ANISOU 2031 CG2 VAL B 102 9427 4457 5441 592 752 461 C ATOM 2032 N ALA B 103 -9.405 22.712 12.265 1.00 56.01 N ANISOU 2032 N ALA B 103 9804 5021 6458 1453 760 169 N ATOM 2033 CA ALA B 103 -10.055 23.095 11.018 1.00 62.12 C ANISOU 2033 CA ALA B 103 10316 5949 7338 1849 575 -7 C ATOM 2034 C ALA B 103 -11.481 23.551 11.265 1.00 55.19 C ANISOU 2034 C ALA B 103 9246 5136 6587 2173 781 -422 C ATOM 2035 O ALA B 103 -12.127 23.096 12.201 1.00 74.02 O ANISOU 2035 O ALA B 103 11560 7546 9019 1858 1138 -630 O ATOM 2036 CB ALA B 103 -10.035 21.920 10.045 1.00 62.40 C ANISOU 2036 CB ALA B 103 10327 5950 7434 1801 530 -96 C ATOM 2037 N PRO B 104 -11.982 24.462 10.433 1.00 57.35 N ANISOU 2037 N PRO B 104 9174 5688 6928 2563 509 -517 N ATOM 2038 CA PRO B 104 -13.369 24.866 10.657 1.00 66.25 C ANISOU 2038 CA PRO B 104 9848 7089 8234 2753 661 -928 C ATOM 2039 C PRO B 104 -14.306 23.701 10.355 1.00 78.53 C ANISOU 2039 C PRO B 104 10940 8942 9958 2428 786 -1280 C ATOM 2040 O PRO B 104 -14.183 23.057 9.312 1.00 77.19 O ANISOU 2040 O PRO B 104 10667 8879 9782 2399 543 -1291 O ATOM 2041 CB PRO B 104 -13.573 26.039 9.680 1.00 46.56 C ANISOU 2041 CB PRO B 104 7110 4799 5783 3193 254 -871 C ATOM 2042 CG PRO B 104 -12.584 25.860 8.657 1.00 52.95 C ANISOU 2042 CG PRO B 104 8096 5589 6432 3078 -61 -552 C ATOM 2043 CD PRO B 104 -11.408 25.089 9.235 1.00 55.74 C ANISOU 2043 CD PRO B 104 8860 5666 6651 2666 93 -279 C ATOM 2044 N TRP B 105 -15.219 23.433 11.282 1.00 79.57 N ANISOU 2044 N TRP B 105 10818 9186 10227 2163 1185 -1570 N ATOM 2045 CA TRP B 105 -16.156 22.330 11.158 1.00 68.93 C ANISOU 2045 CA TRP B 105 9020 8101 9069 1788 1364 -1917 C ATOM 2046 C TRP B 105 -16.895 22.299 9.819 1.00 81.98 C ANISOU 2046 C TRP B 105 10115 10137 10895 2026 982 -2156 C ATOM 2047 O TRP B 105 -16.995 21.245 9.183 1.00 79.23 O ANISOU 2047 O TRP B 105 9642 9886 10575 1746 897 -2265 O ATOM 2048 CB TRP B 105 -17.159 22.400 12.289 1.00 72.35 C ANISOU 2048 CB TRP B 105 9183 8646 9659 1583 1851 -2216 C ATOM 2049 CG TRP B 105 -18.111 21.262 12.331 1.00 72.61 C ANISOU 2049 CG TRP B 105 8769 8916 9902 1126 2109 -2565 C ATOM 2050 CD1 TRP B 105 -19.451 21.310 12.088 1.00 89.73 C ANISOU 2050 CD1 TRP B 105 10201 11491 12403 1168 2175 -2986 C ATOM 2051 CD2 TRP B 105 -17.813 19.903 12.666 1.00 67.29 C ANISOU 2051 CD2 TRP B 105 8345 8071 9152 542 2343 -2525 C ATOM 2052 NE1 TRP B 105 -20.005 20.064 12.248 1.00 86.96 N ANISOU 2052 NE1 TRP B 105 9619 11239 12182 615 2446 -3217 N ATOM 2053 CE2 TRP B 105 -19.018 19.183 12.599 1.00 84.81 C ANISOU 2053 CE2 TRP B 105 9968 10604 11650 226 2556 -2938 C ATOM 2054 CE3 TRP B 105 -16.644 19.226 13.013 1.00 79.49 C ANISOU 2054 CE3 TRP B 105 10545 9213 10446 261 2378 -2175 C ATOM 2055 CZ2 TRP B 105 -19.083 17.816 12.854 1.00 86.64 C ANISOU 2055 CZ2 TRP B 105 10284 10742 11892 -374 2814 -3008 C ATOM 2056 CZ3 TRP B 105 -16.717 17.865 13.266 1.00 77.27 C ANISOU 2056 CZ3 TRP B 105 10341 8834 10184 -301 2621 -2240 C ATOM 2057 CH2 TRP B 105 -17.923 17.178 13.185 1.00 72.74 C ANISOU 2057 CH2 TRP B 105 9211 8562 9866 -619 2843 -2652 C ATOM 2058 N ASN B 106 -17.393 23.456 9.393 1.00 71.48 N ANISOU 2058 N ASN B 106 8487 9003 9671 2542 731 -2231 N ATOM 2059 CA ASN B 106 -18.207 23.546 8.192 1.00 74.96 C ANISOU 2059 CA ASN B 106 8376 9823 10281 2800 327 -2464 C ATOM 2060 C ASN B 106 -17.402 23.317 6.913 1.00 83.20 C ANISOU 2060 C ASN B 106 9699 10819 11096 2928 -135 -2237 C ATOM 2061 O ASN B 106 -17.967 23.028 5.863 1.00 94.09 O ANISOU 2061 O ASN B 106 10719 12489 12542 2995 -473 -2428 O ATOM 2062 CB ASN B 106 -18.921 24.899 8.134 1.00 70.62 C ANISOU 2062 CB ASN B 106 7466 9449 9916 3355 168 -2571 C ATOM 2063 CG ASN B 106 -20.212 24.889 8.889 1.00 87.70 C ANISOU 2063 CG ASN B 106 9021 11863 12439 3245 535 -2978 C ATOM 2064 OD1 ASN B 106 -20.697 23.824 9.268 1.00 99.14 O ANISOU 2064 OD1 ASN B 106 10238 13419 14010 2741 851 -3211 O ATOM 2065 ND2 ASN B 106 -20.803 26.068 9.098 1.00 91.79 N ANISOU 2065 ND2 ASN B 106 9258 12467 13151 3714 515 -3079 N ATOM 2066 N SER B 107 -16.086 23.426 7.002 1.00 73.70 N ANISOU 2066 N SER B 107 9132 9248 9621 2945 -142 -1839 N ATOM 2067 CA SER B 107 -15.242 23.137 5.858 1.00 67.36 C ANISOU 2067 CA SER B 107 8629 8366 8597 3024 -481 -1622 C ATOM 2068 C SER B 107 -14.929 21.651 5.707 1.00 67.67 C ANISOU 2068 C SER B 107 8793 8327 8593 2521 -335 -1678 C ATOM 2069 O SER B 107 -14.401 21.227 4.682 1.00 60.49 O ANISOU 2069 O SER B 107 8064 7394 7526 2540 -576 -1591 O ATOM 2070 CB SER B 107 -13.937 23.887 5.969 1.00 63.22 C ANISOU 2070 CB SER B 107 8691 7481 7851 3257 -541 -1172 C ATOM 2071 OG SER B 107 -13.085 23.158 6.815 1.00 67.94 O ANISOU 2071 OG SER B 107 9688 7747 8380 2865 -218 -985 O ATOM 2072 N LEU B 108 -15.208 20.861 6.736 1.00 76.22 N ANISOU 2072 N LEU B 108 9831 9332 9797 2068 82 -1811 N ATOM 2073 CA LEU B 108 -15.014 19.416 6.617 1.00 75.28 C ANISOU 2073 CA LEU B 108 9815 9118 9669 1579 227 -1888 C ATOM 2074 C LEU B 108 -16.091 18.802 5.731 1.00 63.79 C ANISOU 2074 C LEU B 108 7836 8043 8358 1458 41 -2294 C ATOM 2075 O LEU B 108 -17.209 19.325 5.660 1.00 60.86 O ANISOU 2075 O LEU B 108 6921 8019 8184 1619 -56 -2572 O ATOM 2076 CB LEU B 108 -15.027 18.746 7.990 1.00 74.71 C ANISOU 2076 CB LEU B 108 9885 8833 9668 1109 720 -1895 C ATOM 2077 CG LEU B 108 -13.969 19.285 8.950 1.00 69.11 C ANISOU 2077 CG LEU B 108 9720 7736 8803 1173 876 -1499 C ATOM 2078 CD1 LEU B 108 -14.107 18.606 10.299 1.00 61.79 C ANISOU 2078 CD1 LEU B 108 8946 6623 7907 688 1341 -1527 C ATOM 2079 CD2 LEU B 108 -12.568 19.107 8.367 1.00 48.92 C ANISOU 2079 CD2 LEU B 108 7656 4869 6064 1274 669 -1120 C ATOM 2080 N SER B 109 -15.751 17.701 5.055 1.00 56.62 N ANISOU 2080 N SER B 109 7086 7058 7368 1179 -20 -2335 N ATOM 2081 CA SER B 109 -16.731 16.957 4.259 1.00 62.91 C ANISOU 2081 CA SER B 109 7439 8178 8286 968 -193 -2737 C ATOM 2082 C SER B 109 -17.671 16.215 5.189 1.00 65.69 C ANISOU 2082 C SER B 109 7426 8620 8913 479 197 -3041 C ATOM 2083 O SER B 109 -17.377 16.093 6.372 1.00 62.84 O ANISOU 2083 O SER B 109 7291 8010 8576 264 612 -2901 O ATOM 2084 CB SER B 109 -16.034 15.966 3.334 1.00 73.70 C ANISOU 2084 CB SER B 109 9157 9380 9466 785 -319 -2702 C ATOM 2085 OG SER B 109 -15.515 14.881 4.081 1.00 75.13 O ANISOU 2085 OG SER B 109 9654 9212 9679 323 78 -2627 O ATOM 2086 N LEU B 110 -18.786 15.698 4.683 1.00 76.85 N ANISOU 2086 N LEU B 110 8298 10376 10526 271 73 -3449 N ATOM 2087 CA LEU B 110 -19.618 14.861 5.542 1.00 87.98 C ANISOU 2087 CA LEU B 110 9387 11838 12203 -271 492 -3732 C ATOM 2088 C LEU B 110 -18.795 13.659 5.978 1.00 83.93 C ANISOU 2088 C LEU B 110 9424 10898 11569 -745 814 -3578 C ATOM 2089 O LEU B 110 -18.826 13.259 7.144 1.00 84.03 O ANISOU 2089 O LEU B 110 9553 10716 11657 -1100 1280 -3539 O ATOM 2090 CB LEU B 110 -20.900 14.396 4.847 1.00104.62 C ANISOU 2090 CB LEU B 110 10811 14369 14570 -470 274 -4201 C ATOM 2091 CG LEU B 110 -21.724 13.389 5.676 1.00106.10 C ANISOU 2091 CG LEU B 110 10682 14586 15045 -1112 741 -4499 C ATOM 2092 CD1 LEU B 110 -22.643 14.091 6.671 1.00 99.91 C ANISOU 2092 CD1 LEU B 110 9383 14022 14558 -1063 1070 -4649 C ATOM 2093 CD2 LEU B 110 -22.505 12.400 4.800 1.00 95.96 C ANISOU 2093 CD2 LEU B 110 9006 13537 13918 -1490 508 -4894 C ATOM 2094 N ALA B 111 -18.029 13.115 5.038 1.00 87.32 N ANISOU 2094 N ALA B 111 10222 11160 11797 -730 567 -3477 N ATOM 2095 CA ALA B 111 -17.226 11.925 5.300 1.00102.18 C ANISOU 2095 CA ALA B 111 12614 12613 13596 -1136 826 -3341 C ATOM 2096 C ALA B 111 -16.284 12.087 6.496 1.00 89.39 C ANISOU 2096 C ALA B 111 11491 10583 11891 -1153 1170 -2939 C ATOM 2097 O ALA B 111 -15.937 11.111 7.153 1.00 97.56 O ANISOU 2097 O ALA B 111 12838 11284 12946 -1575 1486 -2859 O ATOM 2098 CB ALA B 111 -16.436 11.554 4.071 1.00 97.72 C ANISOU 2098 CB ALA B 111 12393 11922 12816 -992 513 -3264 C ATOM 2099 N GLN B 112 -15.858 13.312 6.766 1.00 68.61 N ANISOU 2099 N GLN B 112 8958 7956 9157 -700 1080 -2677 N ATOM 2100 CA GLN B 112 -15.001 13.570 7.919 1.00 66.92 C ANISOU 2100 CA GLN B 112 9204 7373 8849 -710 1351 -2304 C ATOM 2101 C GLN B 112 -15.819 13.754 9.191 1.00 67.88 C ANISOU 2101 C GLN B 112 9113 7578 9100 -952 1739 -2434 C ATOM 2102 O GLN B 112 -15.414 13.295 10.258 1.00 77.40 O ANISOU 2102 O GLN B 112 10692 8463 10255 -1270 2075 -2252 O ATOM 2103 CB GLN B 112 -14.133 14.808 7.690 1.00 56.89 C ANISOU 2103 CB GLN B 112 8175 6034 7408 -155 1096 -1964 C ATOM 2104 CG GLN B 112 -12.971 14.614 6.742 1.00 54.07 C ANISOU 2104 CG GLN B 112 8202 5455 6890 43 847 -1712 C ATOM 2105 CD GLN B 112 -12.536 15.924 6.112 1.00 67.69 C ANISOU 2105 CD GLN B 112 9962 7281 8476 613 519 -1514 C ATOM 2106 OE1 GLN B 112 -13.364 16.803 5.825 1.00 67.17 O ANISOU 2106 OE1 GLN B 112 9513 7563 8447 891 335 -1690 O ATOM 2107 NE2 GLN B 112 -11.231 16.072 5.909 1.00 58.85 N ANISOU 2107 NE2 GLN B 112 9296 5843 7220 791 448 -1138 N ATOM 2108 N ARG B 113 -16.958 14.440 9.075 1.00 64.70 N ANISOU 2108 N ARG B 113 8125 7598 8861 -791 1693 -2740 N ATOM 2109 CA ARG B 113 -17.853 14.639 10.202 1.00 75.19 C ANISOU 2109 CA ARG B 113 9176 9049 10343 -1006 2107 -2924 C ATOM 2110 C ARG B 113 -18.296 13.267 10.732 1.00 90.26 C ANISOU 2110 C ARG B 113 11077 10854 12365 -1683 2495 -3106 C ATOM 2111 O ARG B 113 -18.178 12.989 11.932 1.00 88.52 O ANISOU 2111 O ARG B 113 11156 10391 12085 -2011 2925 -2992 O ATOM 2112 CB ARG B 113 -19.064 15.490 9.799 1.00 87.03 C ANISOU 2112 CB ARG B 113 9949 11040 12080 -704 1961 -3268 C ATOM 2113 CG ARG B 113 -18.762 16.917 9.341 1.00 82.33 C ANISOU 2113 CG ARG B 113 9346 10541 11395 -30 1596 -3102 C ATOM 2114 CD ARG B 113 -19.983 17.498 8.615 1.00 96.03 C ANISOU 2114 CD ARG B 113 10319 12767 13401 259 1325 -3463 C ATOM 2115 NE ARG B 113 -19.755 18.836 8.071 1.00104.40 N ANISOU 2115 NE ARG B 113 11372 13911 14385 914 934 -3306 N ATOM 2116 CZ ARG B 113 -20.310 19.290 6.949 1.00107.99 C ANISOU 2116 CZ ARG B 113 11399 14694 14937 1272 451 -3462 C ATOM 2117 NH1 ARG B 113 -21.118 18.505 6.250 1.00114.63 N ANISOU 2117 NH1 ARG B 113 11773 15825 15956 1026 281 -3793 N ATOM 2118 NH2 ARG B 113 -20.057 20.523 6.522 1.00 96.06 N ANISOU 2118 NH2 ARG B 113 9952 13208 13340 1861 115 -3281 N ATOM 2119 N ARG B 114 -18.817 12.423 9.840 1.00 87.16 N ANISOU 2119 N ARG B 114 10368 10633 12117 -1908 2335 -3391 N ATOM 2120 CA ARG B 114 -18.928 10.999 10.131 1.00 86.61 C ANISOU 2120 CA ARG B 114 10446 10352 12111 -2541 2624 -3491 C ATOM 2121 C ARG B 114 -17.486 10.562 10.349 1.00 81.86 C ANISOU 2121 C ARG B 114 10626 9223 11255 -2554 2623 -3050 C ATOM 2122 O ARG B 114 -16.590 11.010 9.645 1.00 71.22 O ANISOU 2122 O ARG B 114 9527 7781 9751 -2134 2273 -2815 O ATOM 2123 CB ARG B 114 -19.606 10.223 8.983 1.00 76.62 C ANISOU 2123 CB ARG B 114 8766 9332 11016 -2737 2368 -3863 C ATOM 2124 N GLY B 115 -17.212 9.728 11.332 1.00 85.97 N ANISOU 2124 N GLY B 115 11545 9383 11736 -3018 3006 -2910 N ATOM 2125 CA GLY B 115 -15.815 9.397 11.531 1.00 82.33 C ANISOU 2125 CA GLY B 115 11784 8422 11074 -2967 2948 -2468 C ATOM 2126 C GLY B 115 -15.360 10.028 12.802 1.00 82.60 C ANISOU 2126 C GLY B 115 12187 8248 10947 -2922 3171 -2153 C ATOM 2127 O GLY B 115 -15.141 9.338 13.793 1.00107.31 O ANISOU 2127 O GLY B 115 15716 11046 14011 -3335 3488 -1995 O ATOM 2128 N PHE B 116 -15.244 11.349 12.779 1.00 82.31 N ANISOU 2128 N PHE B 116 12043 8399 10834 -2430 2997 -2065 N ATOM 2129 CA PHE B 116 -15.060 12.098 14.008 1.00 80.22 C ANISOU 2129 CA PHE B 116 12051 8013 10417 -2393 3226 -1859 C ATOM 2130 C PHE B 116 -16.207 11.767 14.969 1.00 79.78 C ANISOU 2130 C PHE B 116 11771 8093 10447 -2860 3734 -2144 C ATOM 2131 O PHE B 116 -15.983 11.586 16.158 1.00 81.85 O ANISOU 2131 O PHE B 116 12471 8083 10546 -3156 4061 -1961 O ATOM 2132 CB PHE B 116 -14.993 13.603 13.738 1.00 77.75 C ANISOU 2132 CB PHE B 116 11561 7926 10054 -1798 2975 -1814 C ATOM 2133 CG PHE B 116 -13.641 14.087 13.292 1.00 72.86 C ANISOU 2133 CG PHE B 116 11354 7053 9278 -1399 2598 -1408 C ATOM 2134 CD1 PHE B 116 -12.487 13.673 13.938 1.00 73.66 C ANISOU 2134 CD1 PHE B 116 12076 6685 9228 -1549 2624 -1003 C ATOM 2135 CD2 PHE B 116 -13.523 14.972 12.227 1.00 62.35 C ANISOU 2135 CD2 PHE B 116 9782 5946 7963 -877 2212 -1421 C ATOM 2136 CE1 PHE B 116 -11.228 14.141 13.523 1.00 57.94 C ANISOU 2136 CE1 PHE B 116 10404 4467 7143 -1185 2287 -631 C ATOM 2137 CE2 PHE B 116 -12.271 15.425 11.801 1.00 62.98 C ANISOU 2137 CE2 PHE B 116 10227 5790 7911 -534 1905 -1046 C ATOM 2138 CZ PHE B 116 -11.126 15.008 12.449 1.00 58.32 C ANISOU 2138 CZ PHE B 116 10199 4747 7211 -692 1954 -660 C ATOM 2139 N THR B 117 -17.427 11.662 14.444 1.00 83.86 N ANISOU 2139 N THR B 117 11614 9029 11221 -2944 3797 -2589 N ATOM 2140 CA THR B 117 -18.581 11.306 15.264 1.00 96.79 C ANISOU 2140 CA THR B 117 12948 10827 12999 -3409 4313 -2897 C ATOM 2141 C THR B 117 -18.560 9.848 15.716 1.00105.75 C ANISOU 2141 C THR B 117 14397 11655 14130 -4077 4621 -2876 C ATOM 2142 O THR B 117 -18.540 9.570 16.913 1.00119.84 O ANISOU 2142 O THR B 117 16570 13199 15766 -4450 5050 -2748 O ATOM 2143 CB THR B 117 -19.907 11.561 14.521 1.00101.36 C ANISOU 2143 CB THR B 117 12640 11950 13923 -3322 4258 -3388 C ATOM 2144 OG1 THR B 117 -19.789 11.117 13.166 1.00105.99 O ANISOU 2144 OG1 THR B 117 13024 12640 14609 -3203 3792 -3482 O ATOM 2145 CG2 THR B 117 -20.249 13.036 14.527 1.00 96.77 C ANISOU 2145 CG2 THR B 117 11718 11665 13384 -2761 4155 -3457 C ATOM 2146 N LYS B 118 -18.592 8.916 14.768 1.00 95.87 N ANISOU 2146 N LYS B 118 13007 10396 13025 -4242 4410 -3007 N ATOM 2147 CA LYS B 118 -18.722 7.507 15.128 1.00100.56 C ANISOU 2147 CA LYS B 118 13829 10785 13595 -4731 4620 -3000 C ATOM 2148 C LYS B 118 -17.847 6.548 14.312 1.00 90.93 C ANISOU 2148 C LYS B 118 12921 9349 12280 -4593 4224 -2780 C ATOM 2149 O LYS B 118 -17.623 5.418 14.737 1.00 91.42 O ANISOU 2149 O LYS B 118 13288 9253 12192 -4707 4247 -2595 O ATOM 2150 CB LYS B 118 -20.189 7.057 15.007 1.00 98.14 C ANISOU 2150 CB LYS B 118 12854 10837 13600 -5139 4892 -3501 C ATOM 2151 N THR B 119 -17.353 6.969 13.154 1.00 81.58 N ANISOU 2151 N THR B 119 11659 8151 11185 -4333 3861 -2818 N ATOM 2152 CA THR B 119 -16.699 6.002 12.268 1.00 89.69 C ANISOU 2152 CA THR B 119 12889 9028 12162 -4233 3548 -2691 C ATOM 2153 C THR B 119 -15.171 5.856 12.447 1.00 85.84 C ANISOU 2153 C THR B 119 12972 8238 11407 -3818 3294 -2119 C ATOM 2154 O THR B 119 -14.632 4.779 12.194 1.00 76.92 O ANISOU 2154 O THR B 119 12037 6963 10226 -3796 3159 -1953 O ATOM 2155 CB THR B 119 -16.988 6.332 10.783 1.00 94.77 C ANISOU 2155 CB THR B 119 13149 9852 13006 -4156 3233 -3094 C ATOM 2156 OG1 THR B 119 -18.384 6.606 10.615 1.00109.31 O ANISOU 2156 OG1 THR B 119 14273 12202 15058 -4278 3286 -3537 O ATOM 2157 CG2 THR B 119 -16.575 5.179 9.870 1.00 86.19 C ANISOU 2157 CG2 THR B 119 12227 8643 11877 -4157 3002 -3050 C ATOM 2158 N TYR B 120 -14.468 6.906 12.876 1.00 81.73 N ANISOU 2158 N TYR B 120 12659 7648 10746 -3480 3206 -1837 N ATOM 2159 CA TYR B 120 -13.007 6.820 12.995 1.00 59.89 C ANISOU 2159 CA TYR B 120 10265 4709 7782 -3059 2890 -1334 C ATOM 2160 C TYR B 120 -12.568 5.846 14.075 1.00 75.01 C ANISOU 2160 C TYR B 120 12423 6531 9548 -3120 2910 -1072 C ATOM 2161 O TYR B 120 -11.673 5.023 13.852 1.00 76.46 O ANISOU 2161 O TYR B 120 12724 6602 9725 -2958 2672 -852 O ATOM 2162 CB TYR B 120 -12.386 8.186 13.270 1.00 64.24 C ANISOU 2162 CB TYR B 120 10933 5257 8217 -2685 2753 -1102 C ATOM 2163 CG TYR B 120 -12.208 9.023 12.032 1.00 69.14 C ANISOU 2163 CG TYR B 120 11451 5876 8942 -2409 2537 -1209 C ATOM 2164 CD1 TYR B 120 -12.108 8.435 10.785 1.00 75.79 C ANISOU 2164 CD1 TYR B 120 12209 6701 9887 -2385 2362 -1366 C ATOM 2165 CD2 TYR B 120 -12.134 10.386 12.112 1.00 57.11 C ANISOU 2165 CD2 TYR B 120 9960 4354 7386 -2136 2489 -1177 C ATOM 2166 CE1 TYR B 120 -11.957 9.195 9.663 1.00 60.69 C ANISOU 2166 CE1 TYR B 120 10250 4804 8005 -2085 2134 -1513 C ATOM 2167 CE2 TYR B 120 -11.979 11.147 11.009 1.00 61.47 C ANISOU 2167 CE2 TYR B 120 10353 5048 7956 -1722 2192 -1250 C ATOM 2168 CZ TYR B 120 -11.896 10.548 9.778 1.00 62.39 C ANISOU 2168 CZ TYR B 120 10363 5212 8130 -1675 1995 -1401 C ATOM 2169 OH TYR B 120 -11.737 11.322 8.650 1.00 74.79 O ANISOU 2169 OH TYR B 120 11754 7022 9642 -1209 1651 -1430 O ATOM 2170 N THR B 121 -13.206 5.920 15.240 1.00 71.95 N ANISOU 2170 N THR B 121 12093 6182 9063 -3358 3196 -1132 N ATOM 2171 CA THR B 121 -12.830 5.070 16.362 1.00 67.17 C ANISOU 2171 CA THR B 121 11748 5469 8302 -3421 3192 -917 C ATOM 2172 C THR B 121 -12.913 3.574 15.989 1.00 75.22 C ANISOU 2172 C THR B 121 12771 6379 9429 -3626 3189 -965 C ATOM 2173 O THR B 121 -12.387 2.715 16.709 1.00 83.69 O ANISOU 2173 O THR B 121 14056 7315 10427 -3627 3103 -753 O ATOM 2174 CB THR B 121 -13.722 5.373 17.597 1.00 82.06 C ANISOU 2174 CB THR B 121 13710 7409 10060 -3713 3572 -1059 C ATOM 2175 OG1 THR B 121 -13.024 5.061 18.814 1.00 79.35 O ANISOU 2175 OG1 THR B 121 13695 6955 9502 -3630 3452 -773 O ATOM 2176 CG2 THR B 121 -15.019 4.603 17.529 1.00 85.41 C ANISOU 2176 CG2 THR B 121 13929 7899 10626 -4195 3952 -1425 C ATOM 2177 N VAL B 122 -13.556 3.268 14.861 1.00 81.03 N ANISOU 2177 N VAL B 122 13264 7168 10356 -3801 3259 -1260 N ATOM 2178 CA VAL B 122 -13.707 1.879 14.384 1.00 76.47 C ANISOU 2178 CA VAL B 122 12687 6478 9889 -4011 3261 -1349 C ATOM 2179 C VAL B 122 -12.366 1.214 14.065 1.00 70.08 C ANISOU 2179 C VAL B 122 12072 5477 9080 -3684 2920 -1025 C ATOM 2180 O VAL B 122 -12.154 0.043 14.352 1.00 84.44 O ANISOU 2180 O VAL B 122 14032 7130 10923 -3793 2912 -936 O ATOM 2181 CB VAL B 122 -14.604 1.801 13.121 1.00 74.61 C ANISOU 2181 CB VAL B 122 12108 6373 9865 -4237 3324 -1771 C ATOM 2182 CG1 VAL B 122 -14.444 0.449 12.395 1.00 77.65 C ANISOU 2182 CG1 VAL B 122 12556 6603 10346 -4344 3223 -1816 C ATOM 2183 CG2 VAL B 122 -16.059 2.028 13.477 1.00 78.97 C ANISOU 2183 CG2 VAL B 122 12334 7150 10523 -4660 3681 -2164 C ATOM 2184 N GLY B 123 -11.447 1.967 13.484 1.00 71.72 N ANISOU 2184 N GLY B 123 12258 5706 9285 -3286 2648 -856 N ATOM 2185 CA GLY B 123 -10.166 1.391 13.127 1.00 79.27 C ANISOU 2185 CA GLY B 123 13294 6523 10299 -2981 2349 -592 C ATOM 2186 C GLY B 123 -9.038 1.936 13.963 1.00 74.10 C ANISOU 2186 C GLY B 123 12726 5880 9549 -2662 2141 -254 C ATOM 2187 O GLY B 123 -7.869 1.852 13.580 1.00 63.96 O ANISOU 2187 O GLY B 123 11508 4519 8275 -2400 1967 -89 O ATOM 2188 N CYS B 124 -9.384 2.479 15.122 1.00 83.29 N ANISOU 2188 N CYS B 124 15794 4947 10906 -1217 4117 -1477 N ATOM 2189 CA CYS B 124 -8.411 3.245 15.872 1.00 88.71 C ANISOU 2189 CA CYS B 124 17070 5799 10835 -1583 4350 -1656 C ATOM 2190 C CYS B 124 -7.173 2.490 16.289 1.00 94.05 C ANISOU 2190 C CYS B 124 18497 6512 10726 -1693 3926 -1567 C ATOM 2191 O CYS B 124 -6.063 2.985 16.113 1.00108.29 O ANISOU 2191 O CYS B 124 20493 8595 12059 -1720 3614 -1676 O ATOM 2192 CB CYS B 124 -9.051 3.853 17.103 1.00 90.08 C ANISOU 2192 CB CYS B 124 17597 5844 10787 -2086 5233 -1819 C ATOM 2193 SG CYS B 124 -9.300 5.568 16.815 1.00 99.42 S ANISOU 2193 SG CYS B 124 18343 7193 12240 -2111 5591 -2050 S ATOM 2194 N GLU B 125 -7.329 1.309 16.857 1.00 93.43 N ANISOU 2194 N GLU B 125 18872 6170 10458 -1778 3858 -1350 N ATOM 2195 CA GLU B 125 -6.128 0.658 17.335 1.00111.34 C ANISOU 2195 CA GLU B 125 21508 8900 11896 -1805 3239 -1092 C ATOM 2196 C GLU B 125 -6.028 -0.817 17.012 1.00 88.30 C ANISOU 2196 C GLU B 125 18574 5906 9069 -1403 2609 -726 C ATOM 2197 O GLU B 125 -5.818 -1.617 17.895 1.00 97.45 O ANISOU 2197 O GLU B 125 20214 7103 9710 -1615 2461 -470 O ATOM 2198 CB GLU B 125 -5.971 0.878 18.845 1.00131.21 C ANISOU 2198 CB GLU B 125 24731 11527 13596 -2484 3649 -1096 C ATOM 2199 CG GLU B 125 -5.708 2.355 19.205 1.00140.92 C ANISOU 2199 CG GLU B 125 26112 12923 14508 -2894 4117 -1453 C ATOM 2200 CD GLU B 125 -4.460 2.588 20.049 1.00134.85 C ANISOU 2200 CD GLU B 125 25846 12696 12697 -3304 3757 -1354 C ATOM 2201 OE1 GLU B 125 -4.572 2.584 21.298 1.00128.36 O ANISOU 2201 OE1 GLU B 125 25716 11820 11235 -3895 4128 -1341 O ATOM 2202 OE2 GLU B 125 -3.373 2.787 19.454 1.00122.80 O ANISOU 2202 OE2 GLU B 125 24018 11651 10988 -3064 3106 -1281 O ATOM 2203 N GLU B 126 -6.214 -1.150 15.742 1.00 84.14 N ANISOU 2203 N GLU B 126 17552 5224 9193 -844 2246 -709 N ATOM 2204 CA GLU B 126 -5.338 -2.107 15.088 1.00 88.22 C ANISOU 2204 CA GLU B 126 17975 5971 9575 -304 1418 -460 C ATOM 2205 C GLU B 126 -4.865 -1.518 13.738 1.00 82.72 C ANISOU 2205 C GLU B 126 16736 5482 9213 153 1122 -636 C ATOM 2206 O GLU B 126 -3.809 -1.901 13.233 1.00 93.13 O ANISOU 2206 O GLU B 126 17929 7187 10268 560 529 -519 O ATOM 2207 CB GLU B 126 -5.995 -3.486 14.907 1.00 99.79 C ANISOU 2207 CB GLU B 126 19565 6971 11380 -62 1166 -193 C ATOM 2208 CG GLU B 126 -7.237 -3.577 14.042 1.00103.17 C ANISOU 2208 CG GLU B 126 19484 7012 12704 82 1342 -267 C ATOM 2209 CD GLU B 126 -7.760 -5.013 13.959 1.00116.80 C ANISOU 2209 CD GLU B 126 21211 8527 14641 233 984 28 C ATOM 2210 OE1 GLU B 126 -7.021 -5.899 13.476 1.00106.28 O ANISOU 2210 OE1 GLU B 126 19973 7284 13124 677 338 199 O ATOM 2211 OE2 GLU B 126 -8.905 -5.263 14.398 1.00130.53 O ANISOU 2211 OE2 GLU B 126 22847 10031 16718 -96 1359 82 O ATOM 2212 N CYS B 127 -5.611 -0.564 13.181 1.00 75.32 N ANISOU 2212 N CYS B 127 15484 4296 8837 76 1549 -908 N ATOM 2213 CA CYS B 127 -5.257 0.028 11.888 1.00 71.11 C ANISOU 2213 CA CYS B 127 14450 3953 8615 436 1276 -1053 C ATOM 2214 C CYS B 127 -4.428 1.309 11.974 1.00 77.36 C ANISOU 2214 C CYS B 127 15213 5176 9003 204 1406 -1275 C ATOM 2215 O CYS B 127 -4.668 2.165 12.838 1.00 77.80 O ANISOU 2215 O CYS B 127 15485 5214 8862 -297 1937 -1439 O ATOM 2216 CB CYS B 127 -6.517 0.340 11.089 1.00 69.20 C ANISOU 2216 CB CYS B 127 13362 3698 9233 462 1371 -1077 C ATOM 2217 SG CYS B 127 -7.603 -1.045 10.826 1.00 90.55 S ANISOU 2217 SG CYS B 127 15789 6134 12481 612 1113 -828 S ATOM 2218 N THR B 128 -3.483 1.467 11.048 1.00 67.92 N ANISOU 2218 N THR B 128 13729 4386 7691 544 945 -1283 N ATOM 2219 CA THR B 128 -2.683 2.698 11.002 1.00 74.06 C ANISOU 2219 CA THR B 128 14397 5626 8115 293 1012 -1462 C ATOM 2220 C THR B 128 -2.629 3.413 9.648 1.00 65.33 C ANISOU 2220 C THR B 128 12898 4523 7403 531 898 -1631 C ATOM 2221 O THR B 128 -2.260 2.821 8.657 1.00 76.36 O ANISOU 2221 O THR B 128 14066 6021 8926 1007 464 -1542 O ATOM 2222 CB THR B 128 -1.230 2.416 11.390 1.00 70.26 C ANISOU 2222 CB THR B 128 13947 5859 6890 317 558 -1279 C ATOM 2223 OG1 THR B 128 -1.188 1.835 12.694 1.00 73.21 O ANISOU 2223 OG1 THR B 128 14751 6254 6811 30 600 -1096 O ATOM 2224 CG2 THR B 128 -0.432 3.707 11.376 1.00 69.24 C ANISOU 2224 CG2 THR B 128 13709 6208 6392 -36 620 -1442 C ATOM 2225 N VAL B 129 -2.944 4.698 9.606 1.00 69.36 N ANISOU 2225 N VAL B 129 13364 4930 8058 192 1277 -1870 N ATOM 2226 CA VAL B 129 -2.661 5.487 8.405 1.00 64.06 C ANISOU 2226 CA VAL B 129 12260 4468 7614 320 1075 -1948 C ATOM 2227 C VAL B 129 -1.193 5.870 8.358 1.00 62.77 C ANISOU 2227 C VAL B 129 12153 4948 6748 232 812 -1974 C ATOM 2228 O VAL B 129 -0.686 6.445 9.312 1.00 63.60 O ANISOU 2228 O VAL B 129 12472 5362 6331 -227 972 -2008 O ATOM 2229 CB VAL B 129 -3.480 6.777 8.345 1.00 67.18 C ANISOU 2229 CB VAL B 129 12291 4802 8435 20 1380 -2022 C ATOM 2230 CG1 VAL B 129 -2.974 7.672 7.215 1.00 57.99 C ANISOU 2230 CG1 VAL B 129 10863 3843 7328 65 1150 -2108 C ATOM 2231 CG2 VAL B 129 -4.949 6.462 8.177 1.00 64.95 C ANISOU 2231 CG2 VAL B 129 11570 4240 8866 159 1399 -1885 C ATOM 2232 N PHE B 130 -0.536 5.577 7.239 1.00 62.28 N ANISOU 2232 N PHE B 130 11785 5183 6694 633 395 -1908 N ATOM 2233 CA PHE B 130 0.903 5.795 7.068 1.00 67.94 C ANISOU 2233 CA PHE B 130 12295 6686 6832 614 90 -1835 C ATOM 2234 C PHE B 130 1.191 6.849 6.004 1.00 67.54 C ANISOU 2234 C PHE B 130 12030 6773 6857 519 76 -1991 C ATOM 2235 O PHE B 130 0.874 6.651 4.827 1.00 57.98 O ANISOU 2235 O PHE B 130 10672 5325 6034 878 -62 -2025 O ATOM 2236 CB PHE B 130 1.589 4.481 6.680 1.00 74.01 C ANISOU 2236 CB PHE B 130 12873 7764 7482 1202 -352 -1614 C ATOM 2237 CG PHE B 130 3.089 4.570 6.613 1.00 79.56 C ANISOU 2237 CG PHE B 130 13271 9317 7640 1235 -648 -1495 C ATOM 2238 CD1 PHE B 130 3.861 4.274 7.718 1.00 92.31 C ANISOU 2238 CD1 PHE B 130 14928 11393 8751 1059 -807 -1298 C ATOM 2239 CD2 PHE B 130 3.724 4.930 5.443 1.00 89.57 C ANISOU 2239 CD2 PHE B 130 14196 10930 8906 1425 -778 -1557 C ATOM 2240 CE1 PHE B 130 5.233 4.344 7.660 1.00 92.46 C ANISOU 2240 CE1 PHE B 130 14575 12215 8339 1091 -1112 -1150 C ATOM 2241 CE2 PHE B 130 5.098 5.004 5.382 1.00 94.75 C ANISOU 2241 CE2 PHE B 130 14487 12405 9109 1449 -1009 -1432 C ATOM 2242 CZ PHE B 130 5.853 4.710 6.491 1.00 84.60 C ANISOU 2242 CZ PHE B 130 13168 11588 7389 1294 -1188 -1220 C ATOM 2243 N PRO B 131 1.799 7.974 6.402 1.00 60.35 N ANISOU 2243 N PRO B 131 11159 6230 5541 -8 193 -2076 N ATOM 2244 CA PRO B 131 2.103 9.015 5.415 1.00 58.56 C ANISOU 2244 CA PRO B 131 10776 6130 5342 -165 168 -2204 C ATOM 2245 C PRO B 131 3.224 8.609 4.451 1.00 72.29 C ANISOU 2245 C PRO B 131 12117 8511 6838 169 -203 -2077 C ATOM 2246 O PRO B 131 4.260 8.124 4.894 1.00102.64 O ANISOU 2246 O PRO B 131 15764 13001 10235 226 -413 -1904 O ATOM 2247 CB PRO B 131 2.524 10.204 6.283 1.00 61.49 C ANISOU 2247 CB PRO B 131 11365 6738 5262 -863 369 -2299 C ATOM 2248 CG PRO B 131 1.893 9.929 7.632 1.00 71.23 C ANISOU 2248 CG PRO B 131 12974 7640 6448 -1062 659 -2315 C ATOM 2249 CD PRO B 131 1.993 8.447 7.778 1.00 62.76 C ANISOU 2249 CD PRO B 131 11770 6680 5395 -562 404 -2089 C ATOM 2250 N CYS B 132 3.004 8.791 3.152 1.00 75.31 N ANISOU 2250 N CYS B 132 12501 5259 10853 512 -2433 -1487 N ATOM 2251 CA CYS B 132 4.026 8.530 2.147 1.00 67.92 C ANISOU 2251 CA CYS B 132 11387 4522 9898 338 -2459 -1179 C ATOM 2252 C CYS B 132 4.788 9.761 1.760 1.00 69.96 C ANISOU 2252 C CYS B 132 11414 4657 10512 147 -2817 -1007 C ATOM 2253 O CYS B 132 4.223 10.648 1.143 1.00 76.17 O ANISOU 2253 O CYS B 132 12069 5272 11602 10 -2954 -911 O ATOM 2254 CB CYS B 132 3.403 7.968 0.896 1.00 66.87 C ANISOU 2254 CB CYS B 132 11189 4513 9708 245 -2253 -959 C ATOM 2255 SG CYS B 132 2.975 6.270 1.058 1.00 78.48 S ANISOU 2255 SG CYS B 132 12884 6194 10741 419 -1884 -1035 S ATOM 2256 N LEU B 133 6.075 9.806 2.080 1.00 86.64 N ANISOU 2256 N LEU B 133 13460 6857 12602 126 -2977 -938 N ATOM 2257 CA LEU B 133 6.917 10.932 1.687 1.00 89.92 C ANISOU 2257 CA LEU B 133 13617 7169 13379 -79 -3347 -707 C ATOM 2258 C LEU B 133 7.488 10.745 0.282 1.00101.64 C ANISOU 2258 C LEU B 133 14830 8916 14874 -258 -3286 -264 C ATOM 2259 O LEU B 133 7.228 11.543 -0.617 1.00109.11 O ANISOU 2259 O LEU B 133 15563 9779 16117 -438 -3421 -33 O ATOM 2260 CB LEU B 133 8.053 11.122 2.687 1.00 87.27 C ANISOU 2260 CB LEU B 133 13313 6796 13048 -26 -3584 -805 C ATOM 2261 CG LEU B 133 7.631 11.555 4.089 1.00 86.75 C ANISOU 2261 CG LEU B 133 13497 6448 13017 170 -3739 -1233 C ATOM 2262 CD1 LEU B 133 8.853 11.907 4.916 1.00 92.97 C ANISOU 2262 CD1 LEU B 133 14280 7167 13879 185 -4057 -1282 C ATOM 2263 CD2 LEU B 133 6.673 12.734 4.023 1.00 79.03 C ANISOU 2263 CD2 LEU B 133 12503 5133 12393 126 -3967 -1333 C ATOM 2264 N SER B 134 8.273 9.690 0.102 1.00 97.85 N ANISOU 2264 N SER B 134 14359 8766 14055 -185 -3084 -141 N ATOM 2265 CA SER B 134 8.814 9.376 -1.206 1.00 92.30 C ANISOU 2265 CA SER B 134 13425 8369 13277 -277 -2991 269 C ATOM 2266 C SER B 134 8.005 8.259 -1.822 1.00 92.39 C ANISOU 2266 C SER B 134 13593 8550 12960 -156 -2635 231 C ATOM 2267 O SER B 134 7.217 7.607 -1.136 1.00 83.62 O ANISOU 2267 O SER B 134 12756 7353 11662 -10 -2456 -84 O ATOM 2268 CB SER B 134 10.277 8.972 -1.112 1.00102.75 C ANISOU 2268 CB SER B 134 14634 9970 14434 -254 -3026 470 C ATOM 2269 OG SER B 134 10.924 9.177 -2.355 1.00116.17 O ANISOU 2269 OG SER B 134 16014 11925 16200 -374 -3060 939 O ATOM 2270 N ILE B 135 8.212 8.028 -3.113 1.00 82.06 N ANISOU 2270 N ILE B 135 12109 7488 11582 -203 -2549 568 N ATOM 2271 CA ILE B 135 7.384 7.082 -3.837 1.00 73.55 C ANISOU 2271 CA ILE B 135 11175 6527 10243 -97 -2278 548 C ATOM 2272 C ILE B 135 8.026 5.703 -4.103 1.00 81.61 C ANISOU 2272 C ILE B 135 12311 7904 10793 96 -2059 608 C ATOM 2273 O ILE B 135 7.609 4.980 -4.997 1.00 86.55 O ANISOU 2273 O ILE B 135 13000 8676 11210 183 -1899 692 O ATOM 2274 CB ILE B 135 6.925 7.711 -5.151 1.00 78.97 C ANISOU 2274 CB ILE B 135 11643 7217 11145 -234 -2327 832 C ATOM 2275 CG1 ILE B 135 5.605 7.078 -5.611 1.00 79.84 C ANISOU 2275 CG1 ILE B 135 11949 7252 11135 -164 -2125 695 C ATOM 2276 CG2 ILE B 135 8.043 7.672 -6.187 1.00 84.50 C ANISOU 2276 CG2 ILE B 135 12072 8280 11753 -242 -2350 1264 C ATOM 2277 CD1 ILE B 135 4.549 6.983 -4.506 1.00 66.54 C ANISOU 2277 CD1 ILE B 135 10518 5270 9494 -118 -2068 305 C ATOM 2278 N PRO B 136 9.044 5.324 -3.318 1.00101.10 N ANISOU 2278 N PRO B 136 14822 10502 13089 180 -2070 554 N ATOM 2279 CA PRO B 136 9.057 3.875 -3.095 1.00101.44 C ANISOU 2279 CA PRO B 136 15132 10725 12684 398 -1830 397 C ATOM 2280 C PRO B 136 8.004 3.519 -2.029 1.00107.19 C ANISOU 2280 C PRO B 136 16148 11185 13393 461 -1736 2 C ATOM 2281 O PRO B 136 7.293 2.517 -2.118 1.00123.97 O ANISOU 2281 O PRO B 136 18489 13328 15287 578 -1551 -119 O ATOM 2282 CB PRO B 136 10.479 3.607 -2.596 1.00103.30 C ANISOU 2282 CB PRO B 136 15311 11192 12746 467 -1870 476 C ATOM 2283 CG PRO B 136 11.287 4.756 -3.113 1.00106.59 C ANISOU 2283 CG PRO B 136 15364 11666 13470 291 -2099 825 C ATOM 2284 CD PRO B 136 10.363 5.929 -3.053 1.00107.18 C ANISOU 2284 CD PRO B 136 15365 11376 13981 102 -2270 752 C ATOM 2285 N CYS B 137 7.951 4.372 -1.011 1.00 96.21 N ANISOU 2285 N CYS B 137 14751 9553 12253 393 -1888 -177 N ATOM 2286 CA CYS B 137 6.949 4.382 0.067 1.00 88.71 C ANISOU 2286 CA CYS B 137 14015 8341 11351 459 -1840 -523 C ATOM 2287 C CYS B 137 7.017 3.294 1.157 1.00 97.33 C ANISOU 2287 C CYS B 137 15370 9499 12113 657 -1668 -780 C ATOM 2288 O CYS B 137 6.981 3.639 2.348 1.00 99.03 O ANISOU 2288 O CYS B 137 15678 9564 12386 722 -1733 -1020 O ATOM 2289 CB CYS B 137 5.545 4.366 -0.503 1.00 70.26 C ANISOU 2289 CB CYS B 137 11728 5860 9109 426 -1738 -544 C ATOM 2290 SG CYS B 137 4.420 4.854 0.808 1.00 96.91 S ANISOU 2290 SG CYS B 137 15262 8916 12642 493 -1746 -893 S ATOM 2291 N LYS B 138 7.057 2.014 0.776 1.00 75.09 N ANISOU 2291 N LYS B 138 12682 6890 8958 768 -1467 -739 N ATOM 2292 CA LYS B 138 7.245 0.923 1.748 1.00 68.14 C ANISOU 2292 CA LYS B 138 12033 6097 7761 947 -1317 -944 C ATOM 2293 C LYS B 138 6.094 0.764 2.760 1.00 68.60 C ANISOU 2293 C LYS B 138 12273 5952 7842 1032 -1215 -1210 C ATOM 2294 O LYS B 138 5.925 1.552 3.688 1.00 76.26 O ANISOU 2294 O LYS B 138 13244 6752 8979 1049 -1308 -1383 O ATOM 2295 CB LYS B 138 8.569 1.112 2.506 1.00 67.77 C ANISOU 2295 CB LYS B 138 11946 6155 7648 984 -1422 -978 C ATOM 2296 N LEU B 139 5.300 -0.273 2.551 1.00 75.35 N ANISOU 2296 N LEU B 139 13276 6831 8523 1102 -1038 -1222 N ATOM 2297 CA LEU B 139 4.257 -0.678 3.480 1.00 77.39 C ANISOU 2297 CA LEU B 139 13691 6964 8750 1205 -906 -1409 C ATOM 2298 C LEU B 139 4.841 -1.540 4.609 1.00 82.62 C ANISOU 2298 C LEU B 139 14518 7750 9123 1377 -806 -1570 C ATOM 2299 O LEU B 139 5.612 -2.485 4.371 1.00 69.17 O ANISOU 2299 O LEU B 139 12889 6239 7155 1432 -756 -1512 O ATOM 2300 CB LEU B 139 3.166 -1.453 2.733 1.00 68.89 C ANISOU 2300 CB LEU B 139 12683 5849 7645 1184 -794 -1306 C ATOM 2301 CG LEU B 139 2.187 -2.220 3.613 1.00 65.18 C ANISOU 2301 CG LEU B 139 12366 5313 7088 1298 -637 -1420 C ATOM 2302 CD1 LEU B 139 1.041 -1.342 3.982 1.00 69.95 C ANISOU 2302 CD1 LEU B 139 12900 5719 7959 1273 -634 -1475 C ATOM 2303 CD2 LEU B 139 1.692 -3.490 2.946 1.00 62.58 C ANISOU 2303 CD2 LEU B 139 12154 5020 6606 1308 -561 -1300 C ATOM 2304 N GLN B 140 4.454 -1.227 5.837 1.00 79.38 N ANISOU 2304 N GLN B 140 14172 7240 8750 1486 -778 -1772 N ATOM 2305 CA GLN B 140 5.016 -1.891 7.013 1.00 87.43 C ANISOU 2305 CA GLN B 140 15336 8371 9513 1661 -694 -1937 C ATOM 2306 C GLN B 140 4.311 -3.172 7.395 1.00 76.29 C ANISOU 2306 C GLN B 140 14032 7051 7905 1756 -484 -1923 C ATOM 2307 O GLN B 140 4.921 -4.077 7.957 1.00 71.65 O ANISOU 2307 O GLN B 140 13442 6676 7106 1819 -399 -1911 O ATOM 2308 CB GLN B 140 4.974 -0.947 8.221 1.00 96.96 C ANISOU 2308 CB GLN B 140 16548 9459 10833 1771 -777 -2157 C ATOM 2309 CG GLN B 140 5.819 0.283 8.067 1.00 96.48 C ANISOU 2309 CG GLN B 140 16356 9314 10990 1672 -1039 -2164 C ATOM 2310 CD GLN B 140 7.275 -0.060 7.921 1.00 98.09 C ANISOU 2310 CD GLN B 140 16535 9694 11040 1639 -1107 -2093 C ATOM 2311 OE1 GLN B 140 7.753 -0.355 6.822 1.00 89.21 O ANISOU 2311 OE1 GLN B 140 15315 8696 9885 1516 -1111 -1871 O ATOM 2312 NE2 GLN B 140 7.997 -0.031 9.034 1.00106.27 N ANISOU 2312 NE2 GLN B 140 17657 10757 11965 1773 -1161 -2275 N ATOM 2313 N SER B 141 3.010 -3.223 7.141 1.00 75.89 N ANISOU 2313 N SER B 141 13983 6872 7979 1731 -411 -1865 N ATOM 2314 CA SER B 141 2.200 -4.344 7.600 1.00 72.02 C ANISOU 2314 CA SER B 141 13523 6466 7377 1793 -238 -1796 C ATOM 2315 C SER B 141 0.795 -4.298 7.037 1.00 65.18 C ANISOU 2315 C SER B 141 12689 5397 6680 1746 -201 -1706 C ATOM 2316 O SER B 141 0.327 -3.255 6.595 1.00 69.96 O ANISOU 2316 O SER B 141 13201 5853 7528 1664 -280 -1698 O ATOM 2317 CB SER B 141 2.098 -4.348 9.119 1.00 58.76 C ANISOU 2317 CB SER B 141 11775 4908 5643 1936 -139 -1897 C ATOM 2318 OG SER B 141 0.951 -3.607 9.512 1.00 72.79 O ANISOU 2318 OG SER B 141 13518 6547 7593 1999 -102 -1942 O ATOM 2319 N GLY B 142 0.103 -5.427 7.116 1.00 61.88 N ANISOU 2319 N GLY B 142 12350 4994 6168 1778 -92 -1603 N ATOM 2320 CA GLY B 142 -1.279 -5.511 6.689 1.00 70.73 C ANISOU 2320 CA GLY B 142 13441 5959 7475 1713 -56 -1457 C ATOM 2321 C GLY B 142 -2.229 -4.558 7.387 1.00 71.99 C ANISOU 2321 C GLY B 142 13494 6037 7822 1782 10 -1502 C ATOM 2322 O GLY B 142 -3.359 -4.373 6.935 1.00 81.86 O ANISOU 2322 O GLY B 142 14660 7168 9274 1702 24 -1362 O ATOM 2323 N THR B 143 -1.780 -3.960 8.485 1.00 61.29 N ANISOU 2323 N THR B 143 12150 4747 6392 1949 39 -1698 N ATOM 2324 CA THR B 143 -2.605 -3.040 9.253 1.00 75.92 C ANISOU 2324 CA THR B 143 13928 6544 8372 2085 89 -1775 C ATOM 2325 C THR B 143 -2.356 -1.568 8.922 1.00 83.44 C ANISOU 2325 C THR B 143 14801 7367 9538 2026 -86 -1897 C ATOM 2326 O THR B 143 -3.007 -0.677 9.477 1.00 98.84 O ANISOU 2326 O THR B 143 16695 9254 11605 2147 -88 -1982 O ATOM 2327 CB THR B 143 -2.370 -3.231 10.748 1.00 80.00 C ANISOU 2327 CB THR B 143 14443 7262 8693 2319 198 -1892 C ATOM 2328 OG1 THR B 143 -0.975 -3.064 11.023 1.00 70.07 O ANISOU 2328 OG1 THR B 143 13133 6150 7341 2277 87 -2006 O ATOM 2329 CG2 THR B 143 -2.804 -4.622 11.165 1.00 80.95 C ANISOU 2329 CG2 THR B 143 14660 7470 8628 2411 378 -1761 C ATOM 2330 N HIS B 144 -1.397 -1.314 8.041 1.00 74.18 N ANISOU 2330 N HIS B 144 13486 4839 9861 -398 -209 -1166 N ATOM 2331 CA HIS B 144 -1.122 0.036 7.589 1.00 64.72 C ANISOU 2331 CA HIS B 144 12200 4044 8348 -481 -99 -1261 C ATOM 2332 C HIS B 144 -1.878 0.334 6.311 1.00 77.33 C ANISOU 2332 C HIS B 144 13819 5764 9798 -734 -42 -1418 C ATOM 2333 O HIS B 144 -1.929 -0.505 5.422 1.00 70.94 O ANISOU 2333 O HIS B 144 13044 4815 9094 -787 -58 -1689 O ATOM 2334 CB HIS B 144 0.370 0.238 7.333 1.00 65.41 C ANISOU 2334 CB HIS B 144 12145 4269 8439 -293 -50 -1554 C ATOM 2335 CG HIS B 144 1.189 0.385 8.570 1.00 74.96 C ANISOU 2335 CG HIS B 144 13286 5494 9701 -63 -135 -1392 C ATOM 2336 ND1 HIS B 144 0.923 -0.314 9.727 1.00 71.95 N ANISOU 2336 ND1 HIS B 144 13000 4882 9455 48 -286 -1075 N ATOM 2337 CD2 HIS B 144 2.287 1.136 8.826 1.00 81.96 C ANISOU 2337 CD2 HIS B 144 14015 6611 10516 67 -105 -1504 C ATOM 2338 CE1 HIS B 144 1.816 0.007 10.646 1.00 68.28 C ANISOU 2338 CE1 HIS B 144 12454 4535 8956 238 -376 -993 C ATOM 2339 NE2 HIS B 144 2.656 0.884 10.125 1.00 65.95 N ANISOU 2339 NE2 HIS B 144 11988 4510 8559 255 -273 -1270 N ATOM 2340 N CYS B 145 -2.450 1.531 6.218 1.00 76.78 N ANISOU 2340 N CYS B 145 13722 5955 9496 -892 11 -1255 N ATOM 2341 CA CYS B 145 -2.921 2.062 4.940 1.00 67.01 C ANISOU 2341 CA CYS B 145 12484 4920 8055 -1113 40 -1378 C ATOM 2342 C CYS B 145 -1.953 3.142 4.489 1.00 69.34 C ANISOU 2342 C CYS B 145 12683 5538 8124 -1090 176 -1500 C ATOM 2343 O CYS B 145 -1.544 3.991 5.284 1.00 66.42 O ANISOU 2343 O CYS B 145 12224 5280 7734 -1001 238 -1354 O ATOM 2344 CB CYS B 145 -4.341 2.623 5.049 1.00 60.36 C ANISOU 2344 CB CYS B 145 11650 4095 7190 -1316 -17 -1076 C ATOM 2345 SG CYS B 145 -5.547 1.372 5.515 1.00 63.31 S ANISOU 2345 SG CYS B 145 12110 4077 7868 -1385 -138 -941 S ATOM 2346 N LEU B 146 -1.571 3.095 3.221 1.00 62.35 N ANISOU 2346 N LEU B 146 11815 4806 7069 -1186 239 -1788 N ATOM 2347 CA LEU B 146 -0.672 4.088 2.674 1.00 67.05 C ANISOU 2347 CA LEU B 146 12325 5701 7449 -1200 407 -1900 C ATOM 2348 C LEU B 146 -1.447 5.342 2.271 1.00 63.28 C ANISOU 2348 C LEU B 146 11840 5448 6756 -1407 409 -1621 C ATOM 2349 O LEU B 146 -2.403 5.282 1.510 1.00 68.10 O ANISOU 2349 O LEU B 146 12535 6100 7237 -1605 299 -1549 O ATOM 2350 CB LEU B 146 0.106 3.501 1.498 1.00 65.00 C ANISOU 2350 CB LEU B 146 12095 5526 7076 -1231 520 -2332 C ATOM 2351 CG LEU B 146 1.062 2.386 1.946 1.00 70.78 C ANISOU 2351 CG LEU B 146 12765 6005 8122 -985 541 -2622 C ATOM 2352 CD1 LEU B 146 1.883 1.854 0.785 1.00 76.54 C ANISOU 2352 CD1 LEU B 146 13486 6813 8784 -1019 713 -3114 C ATOM 2353 CD2 LEU B 146 1.988 2.860 3.066 1.00 65.22 C ANISOU 2353 CD2 LEU B 146 11903 5292 7586 -749 573 -2518 C ATOM 2354 N TRP B 147 -1.038 6.472 2.818 1.00 61.55 N ANISOU 2354 N TRP B 147 11496 5351 6539 -1357 515 -1463 N ATOM 2355 CA TRP B 147 -1.691 7.750 2.562 1.00 65.38 C ANISOU 2355 CA TRP B 147 11929 5992 6920 -1523 532 -1174 C ATOM 2356 C TRP B 147 -0.947 8.510 1.468 1.00 68.41 C ANISOU 2356 C TRP B 147 12291 6647 7057 -1627 697 -1271 C ATOM 2357 O TRP B 147 0.148 9.032 1.683 1.00 60.31 O ANISOU 2357 O TRP B 147 11146 5707 6061 -1530 881 -1389 O ATOM 2358 CB TRP B 147 -1.747 8.558 3.855 1.00 55.01 C ANISOU 2358 CB TRP B 147 10481 4620 5802 -1426 577 -964 C ATOM 2359 CG TRP B 147 -2.445 9.873 3.780 1.00 55.71 C ANISOU 2359 CG TRP B 147 10468 4788 5911 -1568 608 -674 C ATOM 2360 CD1 TRP B 147 -3.421 10.253 2.901 1.00 55.16 C ANISOU 2360 CD1 TRP B 147 10427 4767 5763 -1764 509 -466 C ATOM 2361 CD2 TRP B 147 -2.205 11.006 4.625 1.00 61.94 C ANISOU 2361 CD2 TRP B 147 11086 5598 6849 -1521 737 -566 C ATOM 2362 NE1 TRP B 147 -3.811 11.554 3.157 1.00 54.14 N ANISOU 2362 NE1 TRP B 147 10142 4654 5775 -1826 570 -205 N ATOM 2363 CE2 TRP B 147 -3.070 12.040 4.203 1.00 52.31 C ANISOU 2363 CE2 TRP B 147 9785 4401 5689 -1686 732 -288 C ATOM 2364 CE3 TRP B 147 -1.337 11.247 5.696 1.00 55.56 C ANISOU 2364 CE3 TRP B 147 10172 4794 6146 -1360 839 -693 C ATOM 2365 CZ2 TRP B 147 -3.104 13.294 4.825 1.00 67.43 C ANISOU 2365 CZ2 TRP B 147 11509 6302 7811 -1693 863 -157 C ATOM 2366 CZ3 TRP B 147 -1.378 12.506 6.330 1.00 52.06 C ANISOU 2366 CZ3 TRP B 147 9550 4377 5852 -1385 961 -587 C ATOM 2367 CH2 TRP B 147 -2.261 13.503 5.893 1.00 50.29 C ANISOU 2367 CH2 TRP B 147 9242 4136 5731 -1549 990 -334 C ATOM 2368 N THR B 148 -1.542 8.577 0.289 1.00 68.27 N ANISOU 2368 N THR B 148 12383 6773 6783 -1839 628 -1213 N ATOM 2369 CA THR B 148 -0.830 9.093 -0.872 1.00 64.51 C ANISOU 2369 CA THR B 148 11942 6576 5992 -1968 797 -1316 C ATOM 2370 C THR B 148 -1.287 10.463 -1.376 1.00 72.59 C ANISOU 2370 C THR B 148 12927 7766 6886 -2143 804 -930 C ATOM 2371 O THR B 148 -0.751 10.961 -2.365 1.00 77.04 O ANISOU 2371 O THR B 148 13540 8574 7157 -2279 953 -944 O ATOM 2372 CB THR B 148 -0.937 8.087 -2.011 1.00 67.50 C ANISOU 2372 CB THR B 148 12506 7059 6080 -2100 740 -1598 C ATOM 2373 OG1 THR B 148 -2.262 7.538 -2.026 1.00 83.65 O ANISOU 2373 OG1 THR B 148 14636 8981 8167 -2190 451 -1459 O ATOM 2374 CG2 THR B 148 0.042 6.954 -1.767 1.00 66.85 C ANISOU 2374 CG2 THR B 148 12412 6846 6140 -1919 861 -2056 C ATOM 2375 N ASP B 149 -2.254 11.067 -0.684 1.00 60.83 N ANISOU 2375 N ASP B 149 11341 6132 5641 -2143 663 -585 N ATOM 2376 CA ASP B 149 -2.804 12.379 -1.044 1.00 61.80 C ANISOU 2376 CA ASP B 149 11382 6329 5769 -2284 639 -178 C ATOM 2377 C ASP B 149 -1.728 13.448 -1.293 1.00 65.44 C ANISOU 2377 C ASP B 149 11746 6931 6185 -2298 921 -150 C ATOM 2378 O ASP B 149 -1.750 14.148 -2.309 1.00 69.16 O ANISOU 2378 O ASP B 149 12268 7587 6422 -2476 950 70 O ATOM 2379 CB ASP B 149 -3.750 12.889 0.057 1.00 79.11 C ANISOU 2379 CB ASP B 149 13407 8280 8371 -2222 540 88 C ATOM 2380 CG ASP B 149 -5.021 12.062 0.193 1.00 81.38 C ANISOU 2380 CG ASP B 149 13755 8421 8746 -2263 270 154 C ATOM 2381 OD1 ASP B 149 -5.365 11.285 -0.740 1.00 71.84 O ANISOU 2381 OD1 ASP B 149 12709 7313 7275 -2380 99 68 O ATOM 2382 OD2 ASP B 149 -5.685 12.220 1.250 1.00 78.23 O ANISOU 2382 OD2 ASP B 149 13227 7808 8689 -2193 247 276 O ATOM 2383 N GLN B 150 -0.803 13.583 -0.350 1.00 74.80 N ANISOU 2383 N GLN B 150 12787 8028 7605 -2121 1117 -355 N ATOM 2384 CA GLN B 150 0.296 14.544 -0.465 1.00 75.27 C ANISOU 2384 CA GLN B 150 12710 8186 7702 -2125 1404 -388 C ATOM 2385 C GLN B 150 1.117 14.369 -1.742 1.00 84.71 C ANISOU 2385 C GLN B 150 14034 9639 8513 -2254 1584 -550 C ATOM 2386 O GLN B 150 1.288 15.304 -2.518 1.00 93.90 O ANISOU 2386 O GLN B 150 15195 10945 9539 -2419 1722 -320 O ATOM 2387 CB GLN B 150 1.212 14.412 0.746 1.00 89.66 C ANISOU 2387 CB GLN B 150 14365 9895 9807 -1903 1529 -680 C ATOM 2388 CG GLN B 150 2.502 15.164 0.631 1.00 90.28 C ANISOU 2388 CG GLN B 150 14280 10070 9953 -1894 1827 -830 C ATOM 2389 CD GLN B 150 2.337 16.602 1.024 1.00 79.78 C ANISOU 2389 CD GLN B 150 12749 8661 8901 -1952 1927 -561 C ATOM 2390 OE1 GLN B 150 2.548 17.499 0.213 1.00 80.44 O ANISOU 2390 OE1 GLN B 150 12800 8830 8932 -2110 2093 -368 O ATOM 2391 NE2 GLN B 150 1.945 16.834 2.283 1.00 78.44 N ANISOU 2391 NE2 GLN B 150 12446 8319 9038 -1835 1842 -547 N ATOM 2392 N LEU B 151 1.633 13.165 -1.953 1.00 94.78 N ANISOU 2392 N LEU B 151 15418 10962 9632 -2186 1604 -947 N ATOM 2393 CA LEU B 151 2.433 12.885 -3.139 1.00 94.82 C ANISOU 2393 CA LEU B 151 15541 11218 9270 -2315 1820 -1189 C ATOM 2394 C LEU B 151 1.650 13.116 -4.427 1.00 97.19 C ANISOU 2394 C LEU B 151 16061 11750 9117 -2591 1713 -915 C ATOM 2395 O LEU B 151 2.097 13.835 -5.318 1.00109.86 O ANISOU 2395 O LEU B 151 17713 13582 10448 -2771 1921 -790 O ATOM 2396 CB LEU B 151 2.958 11.445 -3.097 1.00 94.82 C ANISOU 2396 CB LEU B 151 15600 11170 9258 -2184 1830 -1691 C ATOM 2397 CG LEU B 151 4.365 11.268 -2.511 1.00 95.39 C ANISOU 2397 CG LEU B 151 15463 11172 9608 -1980 2078 -2068 C ATOM 2398 CD1 LEU B 151 4.699 9.794 -2.305 1.00103.90 C ANISOU 2398 CD1 LEU B 151 16569 12110 10797 -1811 2014 -2499 C ATOM 2399 CD2 LEU B 151 5.416 11.940 -3.399 1.00 77.18 C ANISOU 2399 CD2 LEU B 151 13101 9104 7121 -2121 2461 -2188 C ATOM 2400 N LEU B 152 0.472 12.510 -4.513 1.00 92.87 N ANISOU 2400 N LEU B 152 15644 11149 8491 -2635 1377 -806 N ATOM 2401 CA LEU B 152 -0.283 12.458 -5.763 1.00 83.33 C ANISOU 2401 CA LEU B 152 14661 10190 6810 -2894 1199 -627 C ATOM 2402 C LEU B 152 -0.997 13.752 -6.154 1.00101.79 C ANISOU 2402 C LEU B 152 16979 12601 9095 -3053 1074 -28 C ATOM 2403 O LEU B 152 -1.099 14.067 -7.336 1.00107.66 O ANISOU 2403 O LEU B 152 17897 13639 9369 -3288 1055 158 O ATOM 2404 CB LEU B 152 -1.306 11.331 -5.688 1.00 92.83 C ANISOU 2404 CB LEU B 152 15970 11286 8015 -2887 861 -748 C ATOM 2405 CG LEU B 152 -0.746 9.920 -5.502 1.00 89.30 C ANISOU 2405 CG LEU B 152 15570 10746 7613 -2761 941 -1318 C ATOM 2406 CD1 LEU B 152 -1.871 8.898 -5.603 1.00 80.31 C ANISOU 2406 CD1 LEU B 152 14542 9503 6467 -2813 603 -1392 C ATOM 2407 CD2 LEU B 152 0.348 9.649 -6.540 1.00 92.93 C ANISOU 2407 CD2 LEU B 152 16145 11493 7670 -2876 1253 -1705 C ATOM 2408 N GLN B 153 -1.504 14.497 -5.174 1.00111.82 N ANISOU 2408 N GLN B 153 18038 13603 10847 -2932 986 276 N ATOM 2409 CA GLN B 153 -2.240 15.722 -5.477 1.00 93.52 C ANISOU 2409 CA GLN B 153 15652 11278 8605 -3057 852 851 C ATOM 2410 C GLN B 153 -1.565 16.955 -4.894 1.00 83.42 C ANISOU 2410 C GLN B 153 14139 9857 7698 -2985 1137 1018 C ATOM 2411 O GLN B 153 -1.989 18.070 -5.162 1.00 80.26 O ANISOU 2411 O GLN B 153 13655 9414 7425 -3083 1091 1491 O ATOM 2412 CB GLN B 153 -3.686 15.628 -4.977 1.00 88.09 C ANISOU 2412 CB GLN B 153 14882 10371 8216 -3023 471 1102 C ATOM 2413 N GLY B 154 -0.520 16.761 -4.098 1.00 98.38 N ANISOU 2413 N GLY B 154 15911 11662 9805 -2815 1415 631 N ATOM 2414 CA GLY B 154 0.324 17.876 -3.698 1.00102.89 C ANISOU 2414 CA GLY B 154 16265 12150 10679 -2780 1722 696 C ATOM 2415 C GLY B 154 0.001 18.521 -2.366 1.00 95.79 C ANISOU 2415 C GLY B 154 15095 10937 10365 -2621 1702 771 C ATOM 2416 O GLY B 154 0.762 19.363 -1.892 1.00 85.71 O ANISOU 2416 O GLY B 154 13610 9571 9386 -2578 1958 728 O ATOM 2417 N SER B 155 -1.121 18.136 -1.764 1.00 96.08 N ANISOU 2417 N SER B 155 15121 10811 10573 -2552 1419 855 N ATOM 2418 CA SER B 155 -1.531 18.712 -0.485 1.00100.92 C ANISOU 2418 CA SER B 155 15490 11146 11709 -2426 1421 899 C ATOM 2419 C SER B 155 -2.463 17.789 0.281 1.00101.52 C ANISOU 2419 C SER B 155 15607 11093 11873 -2326 1182 802 C ATOM 2420 O SER B 155 -3.473 17.330 -0.246 1.00101.36 O ANISOU 2420 O SER B 155 15706 11086 11721 -2411 921 984 O ATOM 2421 CB SER B 155 -2.235 20.049 -0.683 1.00107.19 C ANISOU 2421 CB SER B 155 16114 11791 12821 -2532 1394 1373 C ATOM 2422 OG SER B 155 -3.639 19.875 -0.574 1.00113.93 O ANISOU 2422 OG SER B 155 16961 12514 13816 -2550 1091 1616 O ATOM 2423 N GLU B 156 -2.145 17.575 1.549 1.00100.88 N ANISOU 2423 N GLU B 156 15416 10887 12029 -2159 1271 534 N ATOM 2424 CA GLU B 156 -2.854 16.623 2.396 1.00 99.04 C ANISOU 2424 CA GLU B 156 15238 10535 11860 -2061 1105 420 C ATOM 2425 C GLU B 156 -4.384 16.810 2.455 1.00 89.42 C ANISOU 2425 C GLU B 156 13967 9156 10853 -2143 900 736 C ATOM 2426 O GLU B 156 -5.078 15.947 3.005 1.00 88.87 O ANISOU 2426 O GLU B 156 13958 8987 10820 -2098 767 670 O ATOM 2427 CB GLU B 156 -2.263 16.681 3.815 1.00 88.79 C ANISOU 2427 CB GLU B 156 13806 9149 10783 -1895 1250 159 C ATOM 2428 CG GLU B 156 -2.704 17.893 4.660 1.00 71.48 C ANISOU 2428 CG GLU B 156 11363 6794 9004 -1907 1363 286 C ATOM 2429 CD GLU B 156 -2.200 19.240 4.135 1.00 88.98 C ANISOU 2429 CD GLU B 156 13401 9011 11395 -1995 1548 421 C ATOM 2430 OE1 GLU B 156 -1.279 19.268 3.288 1.00 85.89 O ANISOU 2430 OE1 GLU B 156 13074 8777 10783 -2032 1641 372 O ATOM 2431 OE2 GLU B 156 -2.732 20.282 4.577 1.00100.11 O ANISOU 2431 OE2 GLU B 156 14594 10246 13200 -2035 1625 571 O ATOM 2432 N LYS B 157 -4.907 17.907 1.888 1.00 64.80 N ANISOU 2432 N LYS B 157 10721 5990 7911 -2263 874 1089 N ATOM 2433 CA LYS B 157 -6.365 18.122 1.831 1.00 65.35 C ANISOU 2433 CA LYS B 157 10695 5895 8240 -2339 653 1404 C ATOM 2434 C LYS B 157 -7.040 17.407 0.645 1.00 85.12 C ANISOU 2434 C LYS B 157 13392 8534 10416 -2467 339 1567 C ATOM 2435 O LYS B 157 -7.821 18.022 -0.086 1.00 76.05 O ANISOU 2435 O LYS B 157 12172 7366 9359 -2586 146 1945 O ATOM 2436 CB LYS B 157 -6.700 19.607 1.754 1.00 61.19 C ANISOU 2436 CB LYS B 157 9909 5211 8129 -2398 722 1738 C ATOM 2437 N GLY B 158 -6.770 16.110 0.480 1.00 83.22 N ANISOU 2437 N GLY B 158 13377 8417 9825 -2443 270 1279 N ATOM 2438 CA GLY B 158 -7.227 15.373 -0.688 1.00 61.43 C ANISOU 2438 CA GLY B 158 10817 5827 6698 -2580 -1 1329 C ATOM 2439 C GLY B 158 -8.205 14.234 -0.453 1.00 61.23 C ANISOU 2439 C GLY B 158 10848 5690 6728 -2587 -233 1224 C ATOM 2440 O GLY B 158 -8.880 14.143 0.574 1.00 70.24 O ANISOU 2440 O GLY B 158 11845 6590 8251 -2515 -223 1234 O ATOM 2441 N PHE B 159 -8.268 13.329 -1.415 1.00 67.01 N ANISOU 2441 N PHE B 159 11253 5653 8554 127 -1684 -593 N ATOM 2442 CA PHE B 159 -9.356 12.377 -1.445 1.00 56.75 C ANISOU 2442 CA PHE B 159 9902 4522 7138 64 -1606 -724 C ATOM 2443 C PHE B 159 -9.343 11.346 -0.317 1.00 66.62 C ANISOU 2443 C PHE B 159 11200 5785 8326 35 -1415 -890 C ATOM 2444 O PHE B 159 -10.377 11.119 0.306 1.00 68.81 O ANISOU 2444 O PHE B 159 11387 6146 8612 42 -1383 -1039 O ATOM 2445 CB PHE B 159 -9.381 11.643 -2.765 1.00 57.60 C ANISOU 2445 CB PHE B 159 10064 4769 7051 -90 -1575 -647 C ATOM 2446 CG PHE B 159 -10.553 10.732 -2.888 1.00 71.68 C ANISOU 2446 CG PHE B 159 11788 6733 8714 -192 -1512 -788 C ATOM 2447 CD1 PHE B 159 -11.753 11.197 -3.384 1.00 78.31 C ANISOU 2447 CD1 PHE B 159 12461 7721 9571 -180 -1670 -784 C ATOM 2448 CD2 PHE B 159 -10.481 9.434 -2.451 1.00 56.95 C ANISOU 2448 CD2 PHE B 159 10021 4884 6735 -298 -1300 -921 C ATOM 2449 CE1 PHE B 159 -12.840 10.359 -3.482 1.00 68.35 C ANISOU 2449 CE1 PHE B 159 11118 6657 8195 -303 -1614 -926 C ATOM 2450 CE2 PHE B 159 -11.566 8.610 -2.538 1.00 61.97 C ANISOU 2450 CE2 PHE B 159 10606 5674 7265 -428 -1235 -1059 C ATOM 2451 CZ PHE B 159 -12.743 9.067 -3.058 1.00 59.39 C ANISOU 2451 CZ PHE B 159 10098 5528 6938 -444 -1390 -1071 C ATOM 2452 N GLN B 160 -8.204 10.691 -0.087 1.00 66.59 N ANISOU 2452 N GLN B 160 11331 5714 8255 -2 -1285 -852 N ATOM 2453 CA GLN B 160 -8.120 9.680 0.971 1.00 69.69 C ANISOU 2453 CA GLN B 160 11790 6104 8585 -23 -1115 -960 C ATOM 2454 C GLN B 160 -8.484 10.320 2.298 1.00 75.00 C ANISOU 2454 C GLN B 160 12382 6755 9359 72 -1155 -1070 C ATOM 2455 O GLN B 160 -9.163 9.731 3.134 1.00 74.60 O ANISOU 2455 O GLN B 160 12318 6773 9255 41 -1055 -1198 O ATOM 2456 CB GLN B 160 -6.718 9.054 1.037 1.00 69.30 C ANISOU 2456 CB GLN B 160 11870 5972 8488 -25 -1003 -865 C ATOM 2457 CG GLN B 160 -6.442 8.012 -0.065 1.00 55.41 C ANISOU 2457 CG GLN B 160 10215 4236 6601 -130 -875 -827 C ATOM 2458 CD GLN B 160 -4.965 7.655 -0.198 1.00 60.72 C ANISOU 2458 CD GLN B 160 10970 4830 7270 -90 -784 -719 C ATOM 2459 OE1 GLN B 160 -4.101 8.412 0.222 1.00 62.65 O ANISOU 2459 OE1 GLN B 160 11171 5030 7604 -7 -865 -636 O ATOM 2460 NE2 GLN B 160 -4.673 6.502 -0.799 1.00 63.05 N ANISOU 2460 NE2 GLN B 160 11375 5110 7469 -154 -611 -733 N ATOM 2461 N SER B 161 -8.044 11.556 2.458 1.00 63.39 N ANISOU 2461 N SER B 161 10864 5189 8030 170 -1293 -1028 N ATOM 2462 CA SER B 161 -8.282 12.290 3.665 1.00 59.08 C ANISOU 2462 CA SER B 161 10253 4608 7585 255 -1328 -1158 C ATOM 2463 C SER B 161 -9.711 12.775 3.816 1.00 63.76 C ANISOU 2463 C SER B 161 10697 5267 8263 313 -1377 -1303 C ATOM 2464 O SER B 161 -10.191 12.962 4.930 1.00 61.90 O ANISOU 2464 O SER B 161 10402 5063 8053 354 -1331 -1474 O ATOM 2465 CB SER B 161 -7.347 13.488 3.729 1.00 65.96 C ANISOU 2465 CB SER B 161 11134 5329 8598 319 -1455 -1086 C ATOM 2466 OG SER B 161 -7.769 14.327 4.770 1.00 61.22 O ANISOU 2466 OG SER B 161 10465 4684 8112 398 -1495 -1252 O ATOM 2467 N ARG B 162 -10.390 13.022 2.707 1.00 69.21 N ANISOU 2467 N ARG B 162 11310 5997 8991 321 -1474 -1237 N ATOM 2468 CA ARG B 162 -11.711 13.618 2.812 1.00 58.28 C ANISOU 2468 CA ARG B 162 9740 4679 7723 415 -1546 -1356 C ATOM 2469 C ARG B 162 -12.861 12.649 2.607 1.00 65.23 C ANISOU 2469 C ARG B 162 10526 5781 8477 316 -1462 -1448 C ATOM 2470 O ARG B 162 -14.009 13.048 2.751 1.00 68.09 O ANISOU 2470 O ARG B 162 10696 6243 8930 391 -1507 -1561 O ATOM 2471 CB ARG B 162 -11.851 14.763 1.828 1.00 65.18 C ANISOU 2471 CB ARG B 162 10547 5457 8761 524 -1752 -1212 C ATOM 2472 CG ARG B 162 -11.453 16.101 2.451 1.00 74.29 C ANISOU 2472 CG ARG B 162 11700 6385 10143 673 -1842 -1244 C ATOM 2473 CD ARG B 162 -11.444 17.214 1.437 1.00 79.57 C ANISOU 2473 CD ARG B 162 12346 6906 10981 769 -2044 -1050 C ATOM 2474 NE ARG B 162 -12.788 17.643 1.045 1.00 91.05 N ANISOU 2474 NE ARG B 162 13603 8434 12556 905 -2155 -1068 N ATOM 2475 CZ ARG B 162 -13.469 18.628 1.628 1.00 81.50 C ANISOU 2475 CZ ARG B 162 12265 7104 11595 1106 -2214 -1196 C ATOM 2476 NH1 ARG B 162 -12.950 19.298 2.651 1.00 70.45 N ANISOU 2476 NH1 ARG B 162 10934 5499 10335 1170 -2164 -1343 N ATOM 2477 NH2 ARG B 162 -14.674 18.945 1.182 1.00 90.09 N ANISOU 2477 NH2 ARG B 162 13146 8287 12795 1246 -2322 -1188 N ATOM 2478 N HIS B 163 -12.577 11.387 2.280 1.00 57.73 N ANISOU 2478 N HIS B 163 9699 4903 7332 146 -1334 -1411 N ATOM 2479 CA HIS B 163 -13.671 10.445 2.033 1.00 69.85 C ANISOU 2479 CA HIS B 163 11156 6639 8744 7 -1250 -1507 C ATOM 2480 C HIS B 163 -13.397 9.027 2.448 1.00 67.90 C ANISOU 2480 C HIS B 163 11070 6408 8321 -166 -1036 -1551 C ATOM 2481 O HIS B 163 -14.299 8.191 2.369 1.00 75.99 O ANISOU 2481 O HIS B 163 12048 7582 9243 -316 -942 -1650 O ATOM 2482 CB HIS B 163 -14.056 10.441 0.552 1.00 68.39 C ANISOU 2482 CB HIS B 163 10917 6559 8509 -58 -1372 -1398 C ATOM 2483 CG HIS B 163 -14.578 11.755 0.080 1.00 73.99 C ANISOU 2483 CG HIS B 163 11447 7275 9392 112 -1596 -1328 C ATOM 2484 ND1 HIS B 163 -13.877 12.563 -0.786 1.00 84.35 N ANISOU 2484 ND1 HIS B 163 12818 8466 10764 182 -1754 -1123 N ATOM 2485 CD2 HIS B 163 -15.710 12.426 0.395 1.00 83.14 C ANISOU 2485 CD2 HIS B 163 12367 8528 10695 241 -1684 -1426 C ATOM 2486 CE1 HIS B 163 -14.568 13.667 -1.006 1.00 99.28 C ANISOU 2486 CE1 HIS B 163 14534 10355 12834 349 -1941 -1077 C ATOM 2487 NE2 HIS B 163 -15.682 13.611 -0.298 1.00 98.01 N ANISOU 2487 NE2 HIS B 163 14181 10321 12738 405 -1903 -1266 N ATOM 2488 N LEU B 164 -12.165 8.750 2.874 1.00 67.00 N ANISOU 2488 N LEU B 164 11138 6141 8179 -148 -963 -1471 N ATOM 2489 CA LEU B 164 -11.758 7.379 3.188 1.00 61.84 C ANISOU 2489 CA LEU B 164 10661 5452 7381 -279 -768 -1466 C ATOM 2490 C LEU B 164 -11.294 7.283 4.615 1.00 64.83 C ANISOU 2490 C LEU B 164 11103 5777 7752 -228 -686 -1491 C ATOM 2491 O LEU B 164 -10.876 8.291 5.199 1.00 55.15 O ANISOU 2491 O LEU B 164 9823 4509 6623 -95 -785 -1492 O ATOM 2492 CB LEU B 164 -10.626 6.905 2.276 1.00 59.20 C ANISOU 2492 CB LEU B 164 10491 5003 7000 -303 -739 -1321 C ATOM 2493 CG LEU B 164 -10.890 6.819 0.772 1.00 71.86 C ANISOU 2493 CG LEU B 164 12081 6675 8548 -395 -794 -1286 C ATOM 2494 CD1 LEU B 164 -9.639 6.388 0.023 1.00 65.70 C ANISOU 2494 CD1 LEU B 164 11461 5783 7719 -406 -731 -1166 C ATOM 2495 CD2 LEU B 164 -12.003 5.852 0.509 1.00 56.64 C ANISOU 2495 CD2 LEU B 164 10139 4876 6503 -586 -692 -1415 C ATOM 2496 N ALA B 165 -11.335 6.064 5.157 1.00 57.44 N ANISOU 2496 N ALA B 165 10294 4836 6693 -348 -508 -1503 N ATOM 2497 CA ALA B 165 -10.772 5.784 6.475 1.00 57.47 C ANISOU 2497 CA ALA B 165 10390 4802 6645 -318 -430 -1475 C ATOM 2498 C ALA B 165 -10.056 4.451 6.429 1.00 57.73 C ANISOU 2498 C ALA B 165 10638 4708 6589 -385 -281 -1349 C ATOM 2499 O ALA B 165 -10.335 3.643 5.562 1.00 62.46 O ANISOU 2499 O ALA B 165 11310 5267 7153 -497 -195 -1354 O ATOM 2500 CB ALA B 165 -11.850 5.787 7.535 1.00 56.67 C ANISOU 2500 CB ALA B 165 10193 4852 6485 -388 -359 -1631 C ATOM 2501 N CYS B 166 -9.112 4.237 7.338 1.00 68.73 N ANISOU 2501 N CYS B 166 12129 6035 7950 -310 -257 -1238 N ATOM 2502 CA CYS B 166 -8.341 2.998 7.380 1.00 55.66 C ANISOU 2502 CA CYS B 166 10673 4232 6244 -322 -124 -1090 C ATOM 2503 C CYS B 166 -8.959 2.044 8.385 1.00 73.19 C ANISOU 2503 C CYS B 166 12997 6471 8341 -450 27 -1094 C ATOM 2504 O CYS B 166 -8.713 2.160 9.583 1.00 57.52 O ANISOU 2504 O CYS B 166 11022 4548 6283 -417 14 -1041 O ATOM 2505 CB CYS B 166 -6.883 3.286 7.740 1.00 55.17 C ANISOU 2505 CB CYS B 166 10635 4104 6222 -154 -203 -927 C ATOM 2506 SG CYS B 166 -5.729 1.915 7.504 1.00 73.33 S ANISOU 2506 SG CYS B 166 13134 6199 8528 -85 -64 -724 S ATOM 2507 N LEU B 167 -9.738 1.090 7.869 1.00 85.30 N ANISOU 2507 N LEU B 167 14617 7957 9838 -620 171 -1152 N ATOM 2508 CA LEU B 167 -10.574 0.189 8.664 1.00 76.62 C ANISOU 2508 CA LEU B 167 13608 6882 8621 -805 331 -1178 C ATOM 2509 C LEU B 167 -10.214 -1.271 8.438 1.00 71.56 C ANISOU 2509 C LEU B 167 13225 5997 7966 -882 509 -1058 C ATOM 2510 O LEU B 167 -9.699 -1.617 7.374 1.00 64.09 O ANISOU 2510 O LEU B 167 12355 4896 7101 -841 534 -1041 O ATOM 2511 CB LEU B 167 -12.048 0.405 8.313 1.00 65.02 C ANISOU 2511 CB LEU B 167 11983 5596 7128 -987 352 -1393 C ATOM 2512 CG LEU B 167 -12.483 1.853 8.476 1.00 65.67 C ANISOU 2512 CG LEU B 167 11802 5885 7263 -881 185 -1523 C ATOM 2513 CD1 LEU B 167 -13.922 2.031 8.077 1.00 76.79 C ANISOU 2513 CD1 LEU B 167 13021 7487 8668 -1029 198 -1719 C ATOM 2514 CD2 LEU B 167 -12.283 2.257 9.902 1.00 59.72 C ANISOU 2514 CD2 LEU B 167 11029 5221 6439 -821 177 -1507 C ATOM 2515 N PRO B 168 -10.500 -2.136 9.434 1.00 62.47 N ANISOU 2515 N PRO B 168 12220 4804 6713 -1000 646 -976 N ATOM 2516 CA PRO B 168 -10.242 -3.573 9.292 1.00 81.84 C ANISOU 2516 CA PRO B 168 14945 6974 9175 -1080 831 -853 C ATOM 2517 C PRO B 168 -11.172 -4.240 8.286 1.00 82.16 C ANISOU 2517 C PRO B 168 15040 6951 9227 -1323 966 -1030 C ATOM 2518 O PRO B 168 -12.304 -3.791 8.058 1.00 75.44 O ANISOU 2518 O PRO B 168 14013 6325 8326 -1492 941 -1226 O ATOM 2519 CB PRO B 168 -10.492 -4.121 10.700 1.00 72.68 C ANISOU 2519 CB PRO B 168 13900 5837 7879 -1176 918 -718 C ATOM 2520 CG PRO B 168 -11.438 -3.159 11.304 1.00 75.24 C ANISOU 2520 CG PRO B 168 13993 6495 8098 -1269 846 -886 C ATOM 2521 CD PRO B 168 -11.052 -1.812 10.760 1.00 68.52 C ANISOU 2521 CD PRO B 168 12915 5774 7346 -1069 642 -988 C ATOM 2522 N ARG B 169 -10.674 -5.308 7.684 1.00 66.22 N ANISOU 2522 N ARG B 169 13254 4630 7278 -1336 1107 -970 N ATOM 2523 CA ARG B 169 -11.436 -6.075 6.719 1.00 67.53 C ANISOU 2523 CA ARG B 169 13513 4701 7444 -1591 1253 -1147 C ATOM 2524 C ARG B 169 -11.655 -7.403 7.343 1.00 74.24 C ANISOU 2524 C ARG B 169 14640 5297 8270 -1763 1469 -1049 C ATOM 2525 O ARG B 169 -12.721 -8.010 7.244 1.00 80.89 O ANISOU 2525 O ARG B 169 15539 6149 9047 -2081 1603 -1184 O ATOM 2526 CB ARG B 169 -10.683 -6.223 5.406 1.00 75.56 C ANISOU 2526 CB ARG B 169 14591 5555 8563 -1486 1266 -1199 C ATOM 2527 CG ARG B 169 -10.574 -4.909 4.641 1.00 69.53 C ANISOU 2527 CG ARG B 169 13562 5047 7807 -1366 1056 -1291 C ATOM 2528 CD ARG B 169 -11.903 -4.624 4.003 1.00 65.73 C ANISOU 2528 CD ARG B 169 12925 4807 7242 -1624 1021 -1516 C ATOM 2529 NE ARG B 169 -11.808 -3.638 2.946 1.00 67.14 N ANISOU 2529 NE ARG B 169 12914 5165 7431 -1544 850 -1594 N ATOM 2530 CZ ARG B 169 -12.777 -3.410 2.071 1.00 68.36 C ANISOU 2530 CZ ARG B 169 12933 5524 7516 -1738 796 -1769 C ATOM 2531 NH1 ARG B 169 -13.894 -4.124 2.121 1.00 69.06 N ANISOU 2531 NH1 ARG B 169 13044 5671 7526 -2036 910 -1909 N ATOM 2532 NH2 ARG B 169 -12.620 -2.487 1.134 1.00 80.94 N ANISOU 2532 NH2 ARG B 169 14367 7274 9111 -1650 624 -1792 N ATOM 2533 N GLU B 170 -10.586 -7.828 7.995 1.00 70.88 N ANISOU 2533 N GLU B 170 14382 4645 7904 -1543 1492 -794 N ATOM 2534 CA GLU B 170 -10.537 -9.021 8.801 1.00 77.15 C ANISOU 2534 CA GLU B 170 15460 5162 8690 -1625 1665 -602 C ATOM 2535 C GLU B 170 -9.284 -8.813 9.649 1.00 85.94 C ANISOU 2535 C GLU B 170 16590 6225 9838 -1286 1553 -303 C ATOM 2536 O GLU B 170 -8.505 -7.875 9.390 1.00 77.24 O ANISOU 2536 O GLU B 170 15297 5266 8784 -1036 1377 -298 O ATOM 2537 CB GLU B 170 -10.480 -10.284 7.932 1.00 83.42 C ANISOU 2537 CB GLU B 170 16537 5556 9604 -1740 1888 -663 C ATOM 2538 CG GLU B 170 -9.275 -10.346 7.032 1.00 75.44 C ANISOU 2538 CG GLU B 170 15570 4334 8760 -1452 1882 -647 C ATOM 2539 CD GLU B 170 -9.005 -11.731 6.519 1.00 88.60 C ANISOU 2539 CD GLU B 170 17400 5712 10554 -1459 2085 -629 C ATOM 2540 OE1 GLU B 170 -9.955 -12.548 6.437 1.00 93.37 O ANISOU 2540 OE1 GLU B 170 18112 6251 11112 -1770 2238 -736 O ATOM 2541 OE2 GLU B 170 -7.827 -11.999 6.211 1.00 89.77 O ANISOU 2541 OE2 GLU B 170 17536 5721 10853 -1148 2086 -514 O ATOM 2542 N PRO B 171 -9.090 -9.650 10.675 1.00 85.79 N ANISOU 2542 N PRO B 171 16788 6025 9784 -1291 1640 -41 N ATOM 2543 CA PRO B 171 -7.945 -9.382 11.550 1.00 92.60 C ANISOU 2543 CA PRO B 171 17626 6913 10644 -981 1496 255 C ATOM 2544 C PRO B 171 -6.616 -9.552 10.826 1.00 85.16 C ANISOU 2544 C PRO B 171 16710 5737 9911 -649 1472 347 C ATOM 2545 O PRO B 171 -6.424 -10.550 10.132 1.00 77.47 O ANISOU 2545 O PRO B 171 15949 4396 9090 -642 1652 337 O ATOM 2546 CB PRO B 171 -8.103 -10.423 12.663 1.00 96.80 C ANISOU 2546 CB PRO B 171 18422 7264 11092 -1087 1616 535 C ATOM 2547 CG PRO B 171 -9.570 -10.774 12.654 1.00 82.63 C ANISOU 2547 CG PRO B 171 16688 5525 9184 -1504 1776 339 C ATOM 2548 CD PRO B 171 -9.968 -10.706 11.210 1.00 82.85 C ANISOU 2548 CD PRO B 171 16653 5493 9335 -1600 1839 12 C ATOM 2549 N GLY B 172 -5.727 -8.576 10.985 1.00 73.70 N ANISOU 2549 N GLY B 172 15036 4503 8465 -393 1264 414 N ATOM 2550 CA GLY B 172 -4.412 -8.615 10.381 1.00 73.57 C ANISOU 2550 CA GLY B 172 14984 4335 8632 -74 1228 506 C ATOM 2551 C GLY B 172 -4.386 -7.833 9.090 1.00 73.92 C ANISOU 2551 C GLY B 172 14848 4493 8745 -69 1189 229 C ATOM 2552 O GLY B 172 -3.323 -7.505 8.556 1.00 75.41 O ANISOU 2552 O GLY B 172 14926 4674 9052 173 1126 263 O ATOM 2553 N LEU B 173 -5.574 -7.530 8.586 1.00 74.65 N ANISOU 2553 N LEU B 173 14898 4712 8753 -347 1224 -35 N ATOM 2554 CA LEU B 173 -5.703 -6.760 7.356 1.00 74.26 C ANISOU 2554 CA LEU B 173 14681 4800 8734 -377 1170 -282 C ATOM 2555 C LEU B 173 -6.532 -5.486 7.520 1.00 74.70 C ANISOU 2555 C LEU B 173 14491 5225 8664 -501 995 -434 C ATOM 2556 O LEU B 173 -7.736 -5.543 7.795 1.00 70.56 O ANISOU 2556 O LEU B 173 13967 4808 8035 -747 1037 -554 O ATOM 2557 CB LEU B 173 -6.328 -7.627 6.272 1.00 75.82 C ANISOU 2557 CB LEU B 173 15047 4789 8971 -583 1376 -486 C ATOM 2558 CG LEU B 173 -6.644 -6.945 4.941 1.00 83.30 C ANISOU 2558 CG LEU B 173 15844 5903 9903 -675 1328 -742 C ATOM 2559 CD1 LEU B 173 -5.369 -6.643 4.157 1.00 80.86 C ANISOU 2559 CD1 LEU B 173 15468 5548 9707 -417 1297 -707 C ATOM 2560 CD2 LEU B 173 -7.591 -7.835 4.124 1.00 75.00 C ANISOU 2560 CD2 LEU B 173 14961 4715 8823 -978 1522 -965 C ATOM 2561 N CYS B 174 -5.886 -4.337 7.353 1.00 66.23 N ANISOU 2561 N CYS B 174 13206 4340 7619 -330 808 -430 N ATOM 2562 CA CYS B 174 -6.613 -3.089 7.222 1.00 72.96 C ANISOU 2562 CA CYS B 174 13832 5481 8406 -417 652 -597 C ATOM 2563 C CYS B 174 -6.590 -2.608 5.746 1.00 72.45 C ANISOU 2563 C CYS B 174 13676 5449 8403 -428 618 -751 C ATOM 2564 O CYS B 174 -5.649 -2.892 5.001 1.00 68.96 O ANISOU 2564 O CYS B 174 13287 4869 8048 -302 667 -703 O ATOM 2565 CB CYS B 174 -6.033 -2.033 8.176 1.00 88.80 C ANISOU 2565 CB CYS B 174 15676 7679 10385 -260 458 -495 C ATOM 2566 SG CYS B 174 -6.292 -2.364 9.966 1.00 81.47 S ANISOU 2566 SG CYS B 174 14820 6831 9306 -307 467 -349 S ATOM 2567 N THR B 175 -7.639 -1.899 5.330 1.00 60.16 N ANISOU 2567 N THR B 175 11976 4089 6793 -577 540 -929 N ATOM 2568 CA THR B 175 -7.757 -1.398 3.966 1.00 65.41 C ANISOU 2568 CA THR B 175 12550 4826 7478 -615 483 -1051 C ATOM 2569 C THR B 175 -8.456 -0.018 3.947 1.00 75.63 C ANISOU 2569 C THR B 175 13600 6378 8757 -625 279 -1138 C ATOM 2570 O THR B 175 -9.250 0.294 4.849 1.00 70.77 O ANISOU 2570 O THR B 175 12901 5889 8102 -678 242 -1186 O ATOM 2571 CB THR B 175 -8.529 -2.419 3.096 1.00 76.40 C ANISOU 2571 CB THR B 175 14077 6134 8819 -849 654 -1202 C ATOM 2572 OG1 THR B 175 -7.610 -3.325 2.467 1.00 83.55 O ANISOU 2572 OG1 THR B 175 15169 6794 9783 -786 811 -1165 O ATOM 2573 CG2 THR B 175 -9.326 -1.742 2.035 1.00 73.43 C ANISOU 2573 CG2 THR B 175 13545 5968 8389 -980 547 -1360 C ATOM 2574 N TRP B 176 -8.139 0.823 2.956 1.00 61.19 N ANISOU 2574 N TRP B 176 11661 4623 6967 -564 154 -1150 N ATOM 2575 CA TRP B 176 -8.869 2.079 2.779 1.00 64.89 C ANISOU 2575 CA TRP B 176 11916 5292 7447 -567 -35 -1221 C ATOM 2576 C TRP B 176 -10.351 1.756 2.539 1.00 71.37 C ANISOU 2576 C TRP B 176 12680 6246 8193 -777 1 -1383 C ATOM 2577 O TRP B 176 -10.683 0.881 1.744 1.00 82.05 O ANISOU 2577 O TRP B 176 14131 7567 9477 -944 116 -1457 O ATOM 2578 CB TRP B 176 -8.304 2.921 1.610 1.00 72.45 C ANISOU 2578 CB TRP B 176 12796 6286 8444 -498 -165 -1175 C ATOM 2579 CG TRP B 176 -6.977 3.624 1.886 1.00 60.90 C ANISOU 2579 CG TRP B 176 11310 4759 7070 -307 -250 -1029 C ATOM 2580 CD1 TRP B 176 -5.786 3.390 1.263 1.00 54.28 C ANISOU 2580 CD1 TRP B 176 10539 3831 6253 -237 -198 -933 C ATOM 2581 CD2 TRP B 176 -6.723 4.661 2.853 1.00 55.09 C ANISOU 2581 CD2 TRP B 176 10464 4062 6408 -184 -392 -986 C ATOM 2582 NE1 TRP B 176 -4.808 4.201 1.783 1.00 58.62 N ANISOU 2582 NE1 TRP B 176 11014 4376 6884 -89 -306 -818 N ATOM 2583 CE2 TRP B 176 -5.357 4.993 2.755 1.00 66.08 C ANISOU 2583 CE2 TRP B 176 11860 5389 7858 -63 -430 -854 C ATOM 2584 CE3 TRP B 176 -7.518 5.344 3.775 1.00 62.59 C ANISOU 2584 CE3 TRP B 176 11303 5101 7377 -173 -478 -1069 C ATOM 2585 CZ2 TRP B 176 -4.770 5.973 3.554 1.00 66.36 C ANISOU 2585 CZ2 TRP B 176 11806 5445 7964 42 -563 -801 C ATOM 2586 CZ3 TRP B 176 -6.930 6.306 4.573 1.00 63.88 C ANISOU 2586 CZ3 TRP B 176 11395 5268 7610 -55 -596 -1031 C ATOM 2587 CH2 TRP B 176 -5.570 6.615 4.454 1.00 68.50 C ANISOU 2587 CH2 TRP B 176 11997 5784 8246 39 -644 -898 C ATOM 2588 N GLN B 177 -11.242 2.469 3.216 1.00 71.24 N ANISOU 2588 N GLN B 177 12491 6389 8189 -776 -91 -1457 N ATOM 2589 CA GLN B 177 -12.668 2.155 3.147 1.00 82.72 C ANISOU 2589 CA GLN B 177 13847 8005 9577 -973 -49 -1612 C ATOM 2590 C GLN B 177 -13.517 3.423 3.239 1.00 75.36 C ANISOU 2590 C GLN B 177 12641 7282 8711 -895 -230 -1688 C ATOM 2591 O GLN B 177 -13.163 4.348 3.960 1.00 67.12 O ANISOU 2591 O GLN B 177 11521 6229 7753 -717 -324 -1655 O ATOM 2592 CB GLN B 177 -13.034 1.186 4.267 1.00 82.50 C ANISOU 2592 CB GLN B 177 13931 7935 9480 -1097 135 -1640 C ATOM 2593 CG GLN B 177 -13.678 -0.083 3.809 1.00 71.40 C ANISOU 2593 CG GLN B 177 12651 6494 7984 -1365 310 -1727 C ATOM 2594 CD GLN B 177 -13.734 -1.110 4.917 1.00 72.54 C ANISOU 2594 CD GLN B 177 12974 6517 8072 -1473 505 -1688 C ATOM 2595 OE1 GLN B 177 -12.751 -1.332 5.624 1.00 85.41 O ANISOU 2595 OE1 GLN B 177 14753 7976 9724 -1329 544 -1532 O ATOM 2596 NE2 GLN B 177 -14.887 -1.737 5.082 1.00 74.57 N ANISOU 2596 NE2 GLN B 177 13207 6878 8248 -1736 622 -1814 N ATOM 2597 N SER B 178 -14.641 3.463 2.531 1.00 73.85 N ANISOU 2597 N SER B 178 12294 7278 8488 -1026 -278 -1797 N ATOM 2598 CA SER B 178 -15.394 4.706 2.419 1.00 84.58 C ANISOU 2598 CA SER B 178 13377 8817 9942 -908 -470 -1844 C ATOM 2599 C SER B 178 -16.481 4.891 3.492 1.00102.02 C ANISOU 2599 C SER B 178 15398 11192 12172 -927 -424 -1993 C ATOM 2600 O SER B 178 -17.126 3.928 3.921 1.00103.84 O ANISOU 2600 O SER B 178 15657 11498 12299 -1136 -256 -2088 O ATOM 2601 CB SER B 178 -16.017 4.804 1.029 1.00 92.18 C ANISOU 2601 CB SER B 178 14224 9938 10862 -1005 -590 -1856 C ATOM 2602 OG SER B 178 -16.361 6.150 0.737 1.00108.08 O ANISOU 2602 OG SER B 178 16011 12049 13004 -816 -817 -1816 O ATOM 2603 N LEU B 179 -16.680 6.145 3.904 1.00 96.12 N ANISOU 2603 N LEU B 179 14461 10495 11565 -716 -561 -2020 N ATOM 2604 CA LEU B 179 -17.638 6.490 4.954 1.00 90.58 C ANISOU 2604 CA LEU B 179 13559 9956 10901 -693 -509 -2186 C ATOM 2605 C LEU B 179 -18.971 6.959 4.374 1.00 80.52 C ANISOU 2605 C LEU B 179 11966 8933 9694 -694 -616 -2293 C ATOM 2606 O LEU B 179 -19.870 6.146 4.139 1.00 87.71 O ANISOU 2606 O LEU B 179 12793 10034 10499 -918 -529 -2382 O ATOM 2607 CB LEU B 179 -17.060 7.570 5.879 1.00 82.93 C ANISOU 2607 CB LEU B 179 12574 8880 10054 -459 -568 -2194 C ATOM 2608 CG LEU B 179 -15.692 7.276 6.508 1.00 78.35 C ANISOU 2608 CG LEU B 179 12263 8093 9415 -433 -504 -2077 C ATOM 2609 CD1 LEU B 179 -14.558 7.630 5.558 1.00 75.35 C ANISOU 2609 CD1 LEU B 179 12004 7526 9099 -332 -639 -1896 C ATOM 2610 CD2 LEU B 179 -15.496 7.973 7.840 1.00 60.41 C ANISOU 2610 CD2 LEU B 179 9959 5819 7175 -317 -483 -2169 C TER 2611 LEU B 179 HETATM 2612 CA CA A 301 8.623 14.423 15.802 1.00 73.81 CA HETATM 2613 CA CA A 302 17.089 9.616 13.701 1.00 82.21 CA HETATM 2614 CA CA A 303 21.759 31.367 19.586 1.00 68.28 CA HETATM 2615 ZN ZN A 304 8.376 26.619 10.833 1.00 53.12 ZN HETATM 2616 ZN ZN A 305 13.962 22.553 21.081 1.00 71.65 ZN HETATM 2617 O HOH A 401 8.024 33.824 5.607 1.00 65.58 O HETATM 2618 O HOH A 402 22.528 33.902 19.640 1.00 67.51 O HETATM 2619 O HOH A 403 25.669 36.820 0.948 1.00109.33 O HETATM 2620 O HOH A 404 11.392 12.558 19.850 1.00 68.83 O HETATM 2621 O HOH A 405 31.020 20.929 14.377 1.00 69.20 O HETATM 2622 O HOH A 406 27.528 35.825 19.504 1.00 67.34 O HETATM 2623 O HOH A 407 10.844 8.433 21.882 1.00 81.78 O HETATM 2624 O HOH A 408 10.973 21.936 4.477 1.00 71.04 O HETATM 2625 O HOH A 409 8.438 33.629 2.783 1.00 66.04 O HETATM 2626 O HOH A 410 28.152 33.684 21.076 1.00 66.70 O HETATM 2627 O HOH A 411 26.639 26.046 27.090 1.00 83.91 O HETATM 2628 O HOH A 412 21.858 40.750 16.894 1.00 63.90 O HETATM 2629 O HOH A 413 25.633 9.512 15.382 1.00 84.25 O HETATM 2630 O HOH A 414 10.923 19.778 28.691 1.00 59.17 O HETATM 2631 O HOH A 415 36.597 31.456 22.518 1.00 83.11 O HETATM 2632 O HOH B 201 -9.415 0.562 17.534 1.00 77.00 O HETATM 2633 O HOH B 202 -6.447 5.723 19.857 1.00 89.99 O HETATM 2634 O HOH B 203 -11.191 10.987 5.995 1.00 61.95 O HETATM 2635 O HOH B 204 -3.492 14.915 19.043 1.00 60.09 O HETATM 2636 O HOH B 205 -4.229 6.518 11.894 1.00 60.51 O HETATM 2637 O HOH B 206 -5.822 4.600 12.910 1.00 59.07 O HETATM 2638 O HOH B 207 1.307 11.429 0.211 1.00 52.11 O HETATM 2639 O HOH B 208 -17.923 3.736 6.830 1.00 69.52 O HETATM 2640 O HOH B 209 2.291 33.813 9.441 1.00 65.32 O HETATM 2641 O HOH B 210 -6.800 0.000 0.000 0.50 40.75 O HETATM 2642 O HOH B 211 5.770 21.717 28.557 1.00 76.08 O HETATM 2643 O HOH B 212 3.660 20.889 22.500 1.00 69.94 O HETATM 2644 O HOH B 213 -4.787 16.737 35.887 1.00 65.52 O HETATM 2645 O HOH B 214 -5.455 35.456 33.974 1.00 83.85 O HETATM 2646 O HOH B 215 -12.664 41.692 12.635 1.00 71.61 O HETATM 2647 O HOH B 216 -7.675 33.825 34.664 1.00 67.84 O HETATM 2648 O HOH B 217 -22.079 12.871 25.417 1.00 82.65 O HETATM 2649 O HOH B 218 -20.960 0.000 0.000 0.50 91.79 O CONECT 180 2613 CONECT 181 2613 CONECT 445 2614 CONECT 532 2616 CONECT 544 2616 CONECT 592 2612 CONECT 597 2612 CONECT 608 2612 CONECT 620 2612 CONECT 646 2616 CONECT 690 2614 CONECT 702 2614 CONECT 717 2614 CONECT 730 2616 CONECT 752 2612 CONECT 756 2613 CONECT 759 2613 CONECT 772 2613 CONECT 777 2612 CONECT 911 2615 CONECT 942 2615 CONECT 989 2615 CONECT 1279 2615 CONECT 1282 2615 CONECT 1284 1784 CONECT 1297 2007 CONECT 1373 2193 CONECT 1784 1284 CONECT 2007 1297 CONECT 2193 1373 CONECT 2217 2566 CONECT 2255 2290 CONECT 2290 2255 CONECT 2345 2506 CONECT 2506 2345 CONECT 2566 2217 CONECT 2612 592 597 608 620 CONECT 2612 752 777 CONECT 2613 180 181 756 759 CONECT 2613 772 CONECT 2614 445 690 702 717 CONECT 2614 2618 CONECT 2615 911 942 989 1279 CONECT 2615 1282 CONECT 2616 532 544 646 730 CONECT 2618 2614 MASTER 684 0 5 11 23 0 7 6 2647 2 46 28 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
6mav
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
matrix metalloproteinase-3 catalytic domain (MMP-3cd)
Ligand Name
tissue inhibitor of metalloproteinase-1 (TIMP-1) mutant L34G
EC.Number
E.C.3.4.24.17
Resolution
2.37(Å)
Affinity (Kd/Ki/IC50)
Ki=33.5pM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) J.Biol.Chem. Vol. 294: pp. 9476-9488
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P01033
P08254
Entrez Gene ID
NCBI Entrez Gene ID:
7076
4314
ASD
Information of known allosteric effects of PDB entries
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