HEADER HYDROLASE/HYDROLASE INHIBITOR 18-APR-17 5Q03 TITLE HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE 1,6-BISPHOSPHATE TITLE 2 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR TITLE 3 1-(5-BROMO-1,3-THIAZOL-2-YL)-3-[5-(2-METHYLPROPYL)THIOPHEN-2- TITLE 4 YL]SULFONYLUREA COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE 1; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 SYNONYM: GROWTH-INHIBITING PROTEIN 17,CDNA FLJ75786,HIGHLY SIMILAR TO COMPND 5 HOMO SAPIENS FRUCTOSE-1,6-BISPHOSPHATASE 1 (FBP1),MRNA; COMPND 6 EC: 3.1.3.11; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FBP1, HCG_1640493; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS D3R DOCKING, HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN,M.G.RUDOLPH, AUTHOR 2 H.YANG,C.SHAO,S.K.BURLEY REVDAT 3 06-FEB-19 5Q03 1 AUTHOR JRNL REVDAT 2 16-JAN-19 5Q03 1 REMARK REVDAT 1 09-JAN-19 5Q03 0 JRNL AUTH A.RUF,C.JOSEPH,A.ALKER,D.BANNER,T.TETAZ,J.BENZ,B.KUHN, JRNL AUTH 2 M.G.RUDOLPH JRNL TITL HUMAN LIVER FRUCTOSE-1,6-BISPHOSPHATASE 1 (FRUCTOSE JRNL TITL 2 1,6-BISPHOSPHATE 1-PHOSPHATASE, E.C.3.1.3.11) COMPLEXED WITH JRNL TITL 3 THE ALLOSTERIC INHIBITOR JRNL TITL 4 1-(5-BROMO-1,3-THIAZOL-2-YL)-3-[5-(2-METHYLPROPYL) JRNL TITL 5 THIOPHEN-2-YL]SULFONYLUREA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.31 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.37 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7 REMARK 3 NUMBER OF REFLECTIONS : 133552 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6681 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 20.3694 - 7.0803 1.00 4397 238 0.1630 0.1816 REMARK 3 2 7.0803 - 5.6595 1.00 4393 241 0.1729 0.2017 REMARK 3 3 5.6595 - 4.9559 1.00 4396 214 0.1432 0.1880 REMARK 3 4 4.9559 - 4.5081 1.00 4381 233 0.1206 0.1691 REMARK 3 5 4.5081 - 4.1880 1.00 4333 232 0.1323 0.1741 REMARK 3 6 4.1880 - 3.9430 1.00 4399 240 0.1423 0.2095 REMARK 3 7 3.9430 - 3.7468 1.00 4392 246 0.1561 0.2102 REMARK 3 8 3.7468 - 3.5846 1.00 4360 242 0.1562 0.2266 REMARK 3 9 3.5846 - 3.4473 1.00 4372 225 0.1684 0.2338 REMARK 3 10 3.4473 - 3.3289 1.00 4323 222 0.1743 0.2299 REMARK 3 11 3.3289 - 3.2252 1.00 4435 208 0.1734 0.2402 REMARK 3 12 3.2252 - 3.1333 1.00 4373 219 0.1823 0.2506 REMARK 3 13 3.1333 - 3.0511 1.00 4440 213 0.1835 0.2558 REMARK 3 14 3.0511 - 2.9769 1.00 4324 241 0.1933 0.2919 REMARK 3 15 2.9769 - 2.9094 1.00 4332 231 0.1903 0.2428 REMARK 3 16 2.9094 - 2.8477 1.00 4388 260 0.1937 0.2734 REMARK 3 17 2.8477 - 2.7909 1.00 4343 210 0.2032 0.2913 REMARK 3 18 2.7909 - 2.7383 1.00 4442 234 0.2079 0.2693 REMARK 3 19 2.7383 - 2.6895 1.00 4306 216 0.2118 0.2987 REMARK 3 20 2.6895 - 2.6440 1.00 4391 232 0.2157 0.2979 REMARK 3 21 2.6440 - 2.6015 1.00 4399 222 0.2243 0.2844 REMARK 3 22 2.6015 - 2.5615 1.00 4312 238 0.2323 0.3115 REMARK 3 23 2.5615 - 2.5239 1.00 4342 254 0.2448 0.3625 REMARK 3 24 2.5239 - 2.4884 1.00 4395 232 0.2491 0.3076 REMARK 3 25 2.4884 - 2.4549 1.00 4327 211 0.2483 0.3459 REMARK 3 26 2.4549 - 2.4230 1.00 4419 247 0.2476 0.3270 REMARK 3 27 2.4230 - 2.3928 1.00 4348 224 0.2636 0.3428 REMARK 3 28 2.3928 - 2.3640 0.94 4128 206 0.2629 0.3036 REMARK 3 29 2.3640 - 2.3366 0.72 3172 166 0.2630 0.3087 REMARK 3 30 2.3366 - 2.3103 0.35 1509 84 0.2687 0.3427 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.17 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 20015 REMARK 3 ANGLE : 1.063 27047 REMARK 3 CHIRALITY : 0.063 3056 REMARK 3 PLANARITY : 0.007 3454 REMARK 3 DIHEDRAL : 10.427 12163 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 30 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 122 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.2144 16.5968 -5.5514 REMARK 3 T TENSOR REMARK 3 T11: 0.1385 T22: 0.1191 REMARK 3 T33: 0.1647 T12: -0.0266 REMARK 3 T13: 0.0107 T23: 0.0292 REMARK 3 L TENSOR REMARK 3 L11: 0.0133 L22: 0.0482 REMARK 3 L33: 0.0343 L12: 0.0002 REMARK 3 L13: 0.0064 L23: 0.0347 REMARK 3 S TENSOR REMARK 3 S11: -0.0433 S12: -0.0240 S13: 0.0148 REMARK 3 S21: -0.1211 S22: -0.0317 S23: -0.0273 REMARK 3 S31: -0.0564 S32: 0.0373 S33: -0.0105 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5790 23.5610 -7.9431 REMARK 3 T TENSOR REMARK 3 T11: 0.1922 T22: 0.0928 REMARK 3 T33: 0.2039 T12: 0.0327 REMARK 3 T13: -0.0688 T23: 0.0341 REMARK 3 L TENSOR REMARK 3 L11: 0.0097 L22: 0.0655 REMARK 3 L33: 0.0069 L12: -0.0218 REMARK 3 L13: -0.0052 L23: 0.0078 REMARK 3 S TENSOR REMARK 3 S11: -0.0645 S12: 0.0382 S13: 0.0824 REMARK 3 S21: -0.0988 S22: -0.0032 S23: 0.0710 REMARK 3 S31: -0.0700 S32: 0.0285 S33: -0.0662 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.8449 32.3410 -10.3615 REMARK 3 T TENSOR REMARK 3 T11: 0.3117 T22: 0.0280 REMARK 3 T33: 0.2381 T12: 0.0311 REMARK 3 T13: -0.1569 T23: 0.0543 REMARK 3 L TENSOR REMARK 3 L11: 0.0047 L22: 0.0186 REMARK 3 L33: 0.0146 L12: 0.0046 REMARK 3 L13: 0.0048 L23: -0.0034 REMARK 3 S TENSOR REMARK 3 S11: -0.0123 S12: -0.0015 S13: 0.0370 REMARK 3 S21: -0.0432 S22: -0.0142 S23: 0.0043 REMARK 3 S31: -0.0142 S32: -0.0055 S33: -0.0070 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 9 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.3513 -1.9773 14.6938 REMARK 3 T TENSOR REMARK 3 T11: -0.0162 T22: 0.2006 REMARK 3 T33: 0.2713 T12: 0.0228 REMARK 3 T13: 0.0218 T23: 0.0722 REMARK 3 L TENSOR REMARK 3 L11: 0.0128 L22: 0.0112 REMARK 3 L33: 0.0095 L12: -0.0025 REMARK 3 L13: 0.0024 L23: 0.0020 REMARK 3 S TENSOR REMARK 3 S11: -0.0060 S12: -0.0466 S13: -0.0824 REMARK 3 S21: -0.0216 S22: 0.0188 S23: 0.1098 REMARK 3 S31: 0.0152 S32: -0.0204 S33: -0.0027 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 132 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4723 -1.6169 23.7526 REMARK 3 T TENSOR REMARK 3 T11: 0.0827 T22: 0.2207 REMARK 3 T33: 0.2957 T12: 0.0514 REMARK 3 T13: 0.0798 T23: -0.0089 REMARK 3 L TENSOR REMARK 3 L11: 0.0057 L22: 0.0034 REMARK 3 L33: 0.0161 L12: 0.0036 REMARK 3 L13: 0.0064 L23: 0.0029 REMARK 3 S TENSOR REMARK 3 S11: 0.0152 S12: -0.0102 S13: -0.0108 REMARK 3 S21: 0.0115 S22: -0.0081 S23: 0.0073 REMARK 3 S31: 0.0265 S32: -0.0160 S33: 0.0092 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 149 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8589 19.6516 16.2938 REMARK 3 T TENSOR REMARK 3 T11: -0.0007 T22: 0.1181 REMARK 3 T33: 0.2608 T12: 0.1225 REMARK 3 T13: 0.0192 T23: -0.0557 REMARK 3 L TENSOR REMARK 3 L11: 0.0673 L22: 0.0456 REMARK 3 L33: 0.0483 L12: -0.0342 REMARK 3 L13: 0.0002 L23: 0.0353 REMARK 3 S TENSOR REMARK 3 S11: -0.0494 S12: -0.0985 S13: 0.0028 REMARK 3 S21: 0.0010 S22: -0.0556 S23: 0.0915 REMARK 3 S31: -0.1058 S32: -0.0493 S33: -0.1038 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.6631 19.6401 17.6800 REMARK 3 T TENSOR REMARK 3 T11: 0.0109 T22: 0.2022 REMARK 3 T33: 0.3955 T12: 0.0992 REMARK 3 T13: 0.0165 T23: -0.0827 REMARK 3 L TENSOR REMARK 3 L11: 0.0090 L22: 0.0037 REMARK 3 L33: 0.0199 L12: -0.0055 REMARK 3 L13: -0.0126 L23: 0.0006 REMARK 3 S TENSOR REMARK 3 S11: -0.0041 S12: -0.0274 S13: -0.0380 REMARK 3 S21: 0.0032 S22: 0.0143 S23: 0.0654 REMARK 3 S31: -0.0297 S32: -0.0291 S33: 0.0093 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.9037 -9.4277 -11.3696 REMARK 3 T TENSOR REMARK 3 T11: 0.1208 T22: 0.1350 REMARK 3 T33: 0.1147 T12: 0.0517 REMARK 3 T13: 0.0377 T23: 0.0314 REMARK 3 L TENSOR REMARK 3 L11: 0.0114 L22: 0.0289 REMARK 3 L33: 0.0185 L12: -0.0041 REMARK 3 L13: -0.0052 L23: 0.0176 REMARK 3 S TENSOR REMARK 3 S11: -0.0228 S12: 0.0260 S13: -0.0428 REMARK 3 S21: -0.1166 S22: -0.0252 S23: 0.0318 REMARK 3 S31: 0.0133 S32: -0.0078 S33: -0.0119 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 132 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 53.7014 -19.3924 -7.0035 REMARK 3 T TENSOR REMARK 3 T11: -0.0238 T22: 0.1370 REMARK 3 T33: 0.0288 T12: 0.1146 REMARK 3 T13: 0.1783 T23: -0.0187 REMARK 3 L TENSOR REMARK 3 L11: 0.0121 L22: 0.0220 REMARK 3 L33: 0.0117 L12: -0.0261 REMARK 3 L13: -0.0233 L23: 0.0194 REMARK 3 S TENSOR REMARK 3 S11: 0.0343 S12: 0.0623 S13: -0.0540 REMARK 3 S21: -0.1432 S22: -0.0022 S23: -0.0700 REMARK 3 S31: 0.0916 S32: 0.1287 S33: 0.0673 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.6862 -5.4885 24.0849 REMARK 3 T TENSOR REMARK 3 T11: 0.0050 T22: 0.1527 REMARK 3 T33: 0.0561 T12: 0.0678 REMARK 3 T13: 0.0594 T23: 0.0172 REMARK 3 L TENSOR REMARK 3 L11: 0.0158 L22: 0.0161 REMARK 3 L33: 0.0069 L12: -0.0107 REMARK 3 L13: 0.0039 L23: -0.0064 REMARK 3 S TENSOR REMARK 3 S11: -0.0297 S12: -0.0457 S13: 0.0232 REMARK 3 S21: 0.0702 S22: 0.0328 S23: -0.0305 REMARK 3 S31: -0.0004 S32: -0.0070 S33: -0.0029 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 132 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.1361 -23.5737 20.6150 REMARK 3 T TENSOR REMARK 3 T11: 0.0766 T22: 0.1257 REMARK 3 T33: 0.1006 T12: 0.0411 REMARK 3 T13: 0.0150 T23: 0.0240 REMARK 3 L TENSOR REMARK 3 L11: 0.0325 L22: 0.0222 REMARK 3 L33: 0.0323 L12: 0.0020 REMARK 3 L13: 0.0223 L23: -0.0132 REMARK 3 S TENSOR REMARK 3 S11: -0.0171 S12: -0.0575 S13: -0.0210 REMARK 3 S21: 0.0518 S22: 0.0313 S23: 0.0092 REMARK 3 S31: 0.0821 S32: 0.0178 S33: 0.0190 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.3465 -27.8794 24.8893 REMARK 3 T TENSOR REMARK 3 T11: 0.1635 T22: 0.1499 REMARK 3 T33: 0.1398 T12: 0.0870 REMARK 3 T13: 0.0026 T23: 0.0246 REMARK 3 L TENSOR REMARK 3 L11: 0.0039 L22: 0.0060 REMARK 3 L33: 0.0157 L12: -0.0051 REMARK 3 L13: -0.0039 L23: 0.0044 REMARK 3 S TENSOR REMARK 3 S11: -0.0241 S12: -0.0405 S13: 0.0034 REMARK 3 S21: 0.0491 S22: 0.0196 S23: -0.0424 REMARK 3 S31: 0.0756 S32: 0.0254 S33: -0.0021 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 9 THROUGH 179 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.3635 49.1856 44.1518 REMARK 3 T TENSOR REMARK 3 T11: 0.2798 T22: 0.0270 REMARK 3 T33: 0.1384 T12: -0.0151 REMARK 3 T13: -0.0780 T23: 0.0754 REMARK 3 L TENSOR REMARK 3 L11: 0.0646 L22: 0.0757 REMARK 3 L33: 0.0207 L12: 0.0545 REMARK 3 L13: 0.0174 L23: 0.0251 REMARK 3 S TENSOR REMARK 3 S11: 0.0558 S12: -0.0342 S13: -0.1654 REMARK 3 S21: 0.0603 S22: 0.0433 S23: -0.0502 REMARK 3 S31: 0.0262 S32: 0.0131 S33: 0.0693 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 180 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.8504 45.6875 37.5370 REMARK 3 T TENSOR REMARK 3 T11: 0.1389 T22: 0.1363 REMARK 3 T33: 0.2359 T12: -0.0871 REMARK 3 T13: -0.0015 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 0.0011 L22: 0.0300 REMARK 3 L33: 0.0234 L12: 0.0036 REMARK 3 L13: -0.0001 L23: -0.0248 REMARK 3 S TENSOR REMARK 3 S11: 0.0132 S12: 0.0011 S13: -0.0700 REMARK 3 S21: 0.0227 S22: 0.0029 S23: 0.0447 REMARK 3 S31: -0.0234 S32: -0.0311 S33: 0.0017 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.2420 36.6772 43.0122 REMARK 3 T TENSOR REMARK 3 T11: 0.3040 T22: 0.1558 REMARK 3 T33: 0.4213 T12: -0.0871 REMARK 3 T13: -0.0064 T23: 0.0347 REMARK 3 L TENSOR REMARK 3 L11: 0.0025 L22: 0.0075 REMARK 3 L33: 0.0043 L12: 0.0014 REMARK 3 L13: 0.0045 L23: -0.0035 REMARK 3 S TENSOR REMARK 3 S11: 0.0315 S12: -0.0051 S13: -0.0476 REMARK 3 S21: 0.0250 S22: -0.0273 S23: 0.0146 REMARK 3 S31: 0.0298 S32: -0.0285 S33: 0.0000 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 9 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.0983 70.8501 17.9705 REMARK 3 T TENSOR REMARK 3 T11: 0.2862 T22: 0.2032 REMARK 3 T33: 0.1716 T12: 0.0069 REMARK 3 T13: -0.0436 T23: -0.0213 REMARK 3 L TENSOR REMARK 3 L11: 0.0113 L22: 0.0098 REMARK 3 L33: 0.0042 L12: 0.0121 REMARK 3 L13: 0.0060 L23: 0.0016 REMARK 3 S TENSOR REMARK 3 S11: -0.0165 S12: 0.0789 S13: 0.0182 REMARK 3 S21: 0.0301 S22: -0.0086 S23: 0.0887 REMARK 3 S31: -0.0339 S32: 0.0215 S33: -0.0000 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 89 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.7602 71.0409 16.5301 REMARK 3 T TENSOR REMARK 3 T11: 0.4582 T22: 0.4270 REMARK 3 T33: 0.3542 T12: 0.0509 REMARK 3 T13: -0.0668 T23: 0.0731 REMARK 3 L TENSOR REMARK 3 L11: 0.0080 L22: 0.0038 REMARK 3 L33: 0.0039 L12: 0.0052 REMARK 3 L13: 0.0056 L23: 0.0040 REMARK 3 S TENSOR REMARK 3 S11: 0.0142 S12: 0.0160 S13: -0.0175 REMARK 3 S21: -0.0107 S22: -0.0130 S23: 0.0025 REMARK 3 S31: -0.0239 S32: -0.0214 S33: -0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 132 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.9236 59.9092 11.0839 REMARK 3 T TENSOR REMARK 3 T11: 0.1486 T22: 0.2208 REMARK 3 T33: 0.1292 T12: 0.0036 REMARK 3 T13: -0.0758 T23: -0.0916 REMARK 3 L TENSOR REMARK 3 L11: 0.0230 L22: 0.0068 REMARK 3 L33: 0.0167 L12: 0.0127 REMARK 3 L13: 0.0059 L23: -0.0014 REMARK 3 S TENSOR REMARK 3 S11: 0.0225 S12: 0.0830 S13: -0.0414 REMARK 3 S21: 0.0003 S22: 0.0077 S23: 0.0174 REMARK 3 S31: -0.0311 S32: 0.0022 S33: 0.0676 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 213 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.7671 36.2694 19.8899 REMARK 3 T TENSOR REMARK 3 T11: 0.2659 T22: 0.3294 REMARK 3 T33: 0.4825 T12: -0.0895 REMARK 3 T13: -0.0298 T23: -0.1694 REMARK 3 L TENSOR REMARK 3 L11: 0.0042 L22: 0.0027 REMARK 3 L33: 0.0021 L12: 0.0015 REMARK 3 L13: -0.0011 L23: 0.0025 REMARK 3 S TENSOR REMARK 3 S11: 0.0166 S12: 0.0078 S13: 0.0019 REMARK 3 S21: 0.0026 S22: 0.0234 S23: 0.0016 REMARK 3 S31: -0.0058 S32: -0.0027 S33: 0.0001 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.2853 49.7786 11.6607 REMARK 3 T TENSOR REMARK 3 T11: 0.2019 T22: 0.2952 REMARK 3 T33: 0.3386 T12: 0.0100 REMARK 3 T13: -0.0995 T23: -0.0900 REMARK 3 L TENSOR REMARK 3 L11: 0.0053 L22: 0.0032 REMARK 3 L33: 0.0038 L12: 0.0041 REMARK 3 L13: 0.0065 L23: 0.0003 REMARK 3 S TENSOR REMARK 3 S11: 0.0057 S12: 0.0768 S13: -0.0274 REMARK 3 S21: 0.0157 S22: 0.0317 S23: 0.0261 REMARK 3 S31: 0.0020 S32: -0.0506 S33: -0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 9 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.3890 75.8171 48.8846 REMARK 3 T TENSOR REMARK 3 T11: 0.2719 T22: 0.0752 REMARK 3 T33: 0.0761 T12: -0.0558 REMARK 3 T13: 0.0138 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 0.0134 L22: 0.0353 REMARK 3 L33: 0.0025 L12: 0.0117 REMARK 3 L13: -0.0003 L23: 0.0018 REMARK 3 S TENSOR REMARK 3 S11: 0.0460 S12: -0.0287 S13: 0.0224 REMARK 3 S21: 0.0036 S22: -0.0301 S23: 0.0422 REMARK 3 S31: -0.0243 S32: -0.0203 S33: -0.0099 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 107 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0532 84.1110 55.8442 REMARK 3 T TENSOR REMARK 3 T11: 0.3357 T22: 0.2125 REMARK 3 T33: 0.1372 T12: -0.1357 REMARK 3 T13: 0.0175 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 0.0089 L22: 0.0144 REMARK 3 L33: 0.0035 L12: 0.0018 REMARK 3 L13: 0.0017 L23: 0.0070 REMARK 3 S TENSOR REMARK 3 S11: 0.0290 S12: -0.0142 S13: 0.0502 REMARK 3 S21: -0.0356 S22: -0.0154 S23: 0.0101 REMARK 3 S31: -0.0010 S32: -0.0026 S33: -0.0000 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 156 THROUGH 290 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6323 85.9633 45.2613 REMARK 3 T TENSOR REMARK 3 T11: 0.2633 T22: 0.1565 REMARK 3 T33: 0.1018 T12: -0.0743 REMARK 3 T13: -0.0085 T23: 0.0018 REMARK 3 L TENSOR REMARK 3 L11: 0.0366 L22: 0.0135 REMARK 3 L33: 0.0142 L12: -0.0224 REMARK 3 L13: 0.0012 L23: -0.0008 REMARK 3 S TENSOR REMARK 3 S11: 0.0446 S12: -0.0210 S13: 0.0335 REMARK 3 S21: 0.0658 S22: -0.0233 S23: -0.0318 REMARK 3 S31: 0.0299 S32: 0.1014 S33: 0.0006 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 291 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1467 93.1434 55.1125 REMARK 3 T TENSOR REMARK 3 T11: 0.2084 T22: 0.2108 REMARK 3 T33: 0.1556 T12: -0.1164 REMARK 3 T13: -0.0195 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 0.0023 L22: 0.0023 REMARK 3 L33: 0.0027 L12: 0.0026 REMARK 3 L13: 0.0017 L23: 0.0040 REMARK 3 S TENSOR REMARK 3 S11: -0.0302 S12: -0.0174 S13: 0.0056 REMARK 3 S21: 0.0311 S22: -0.0566 S23: -0.0084 REMARK 3 S31: -0.0295 S32: 0.0148 S33: -0.0000 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 9 THROUGH 88 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3444 73.2058 16.5073 REMARK 3 T TENSOR REMARK 3 T11: 0.3249 T22: 0.1823 REMARK 3 T33: 0.1051 T12: -0.0263 REMARK 3 T13: -0.0290 T23: -0.0101 REMARK 3 L TENSOR REMARK 3 L11: 0.0068 L22: 0.0056 REMARK 3 L33: 0.0060 L12: 0.0007 REMARK 3 L13: -0.0079 L23: -0.0008 REMARK 3 S TENSOR REMARK 3 S11: -0.0207 S12: 0.0523 S13: -0.0087 REMARK 3 S21: -0.0378 S22: 0.0560 S23: -0.0230 REMARK 3 S31: 0.0220 S32: -0.0152 S33: 0.0000 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 89 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.2615 74.6490 12.3264 REMARK 3 T TENSOR REMARK 3 T11: 0.4814 T22: 0.3947 REMARK 3 T33: 0.2188 T12: -0.0433 REMARK 3 T13: 0.0435 T23: 0.0132 REMARK 3 L TENSOR REMARK 3 L11: 0.0079 L22: 0.0084 REMARK 3 L33: 0.0040 L12: 0.0009 REMARK 3 L13: -0.0021 L23: -0.0050 REMARK 3 S TENSOR REMARK 3 S11: 0.0183 S12: 0.0117 S13: -0.0357 REMARK 3 S21: -0.0337 S22: -0.0159 S23: -0.0220 REMARK 3 S31: 0.0062 S32: 0.0161 S33: -0.0000 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 132 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.3115 80.2059 3.6275 REMARK 3 T TENSOR REMARK 3 T11: 0.3250 T22: 0.2563 REMARK 3 T33: 0.1263 T12: -0.0266 REMARK 3 T13: 0.0398 T23: -0.0076 REMARK 3 L TENSOR REMARK 3 L11: 0.0051 L22: 0.0066 REMARK 3 L33: 0.0020 L12: 0.0041 REMARK 3 L13: 0.0017 L23: -0.0018 REMARK 3 S TENSOR REMARK 3 S11: 0.0037 S12: -0.0113 S13: -0.0107 REMARK 3 S21: 0.0052 S22: -0.0190 S23: -0.0230 REMARK 3 S31: 0.0025 S32: 0.0089 S33: -0.0000 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 149 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.3089 88.1862 17.8084 REMARK 3 T TENSOR REMARK 3 T11: 0.2759 T22: 0.1448 REMARK 3 T33: 0.0778 T12: -0.0697 REMARK 3 T13: 0.0144 T23: 0.0064 REMARK 3 L TENSOR REMARK 3 L11: 0.0570 L22: 0.0110 REMARK 3 L33: 0.0149 L12: 0.0208 REMARK 3 L13: 0.0303 L23: 0.0088 REMARK 3 S TENSOR REMARK 3 S11: 0.0508 S12: 0.0516 S13: 0.0110 REMARK 3 S21: -0.0702 S22: 0.0253 S23: 0.0125 REMARK 3 S31: 0.0114 S32: 0.0175 S33: 0.0156 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 213 THROUGH 247 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.8995 103.7545 30.5250 REMARK 3 T TENSOR REMARK 3 T11: 0.2943 T22: 0.2077 REMARK 3 T33: 0.2091 T12: -0.0848 REMARK 3 T13: 0.0645 T23: 0.0176 REMARK 3 L TENSOR REMARK 3 L11: 0.0053 L22: 0.0028 REMARK 3 L33: 0.0052 L12: 0.0019 REMARK 3 L13: -0.0028 L23: -0.0042 REMARK 3 S TENSOR REMARK 3 S11: -0.0130 S12: -0.0016 S13: -0.0122 REMARK 3 S21: -0.0017 S22: -0.0444 S23: 0.0189 REMARK 3 S31: -0.0282 S32: 0.0067 S33: -0.0000 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 248 THROUGH 335 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.7189 96.0203 17.1058 REMARK 3 T TENSOR REMARK 3 T11: 0.3833 T22: 0.2182 REMARK 3 T33: 0.1732 T12: -0.0779 REMARK 3 T13: 0.0333 T23: 0.0128 REMARK 3 L TENSOR REMARK 3 L11: 0.0064 L22: 0.0042 REMARK 3 L33: 0.0112 L12: 0.0002 REMARK 3 L13: 0.0078 L23: -0.0070 REMARK 3 S TENSOR REMARK 3 S11: 0.0293 S12: 0.0386 S13: -0.0039 REMARK 3 S21: -0.0306 S22: 0.0322 S23: -0.0679 REMARK 3 S31: 0.0179 S32: 0.0370 S33: 0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 1 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN B AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN C AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN D AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN E AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN F AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN G AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 7 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 61 OR RESID 72 THROUGH 139 OR REMARK 3 RESID 141 THROUGH 335)) REMARK 3 SELECTION : (CHAIN H AND (RESID 9 THROUGH 37 OR RESID REMARK 3 39 THROUGH 139 OR RESID 141 THROUGH 335)) REMARK 3 ATOM PAIRS NUMBER : 12159 REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5Q03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-17. REMARK 100 THE DEPOSITION ID IS D_1001401329. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-DEC-05 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.987 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133552 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310 REMARK 200 RESOLUTION RANGE LOW (A) : 20.369 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 0.1M AMMONIUM REMARK 280 ACETATE, 12%-25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 147.09600 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 15790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 15750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 ALA A 1 REMARK 465 ASP A 2 REMARK 465 GLN A 3 REMARK 465 ALA A 4 REMARK 465 PRO A 5 REMARK 465 PHE A 6 REMARK 465 ASP A 7 REMARK 465 THR A 8 REMARK 465 SER A 62 REMARK 465 THR A 63 REMARK 465 ASN A 64 REMARK 465 VAL A 65 REMARK 465 THR A 66 REMARK 465 GLY A 67 REMARK 465 ASP A 68 REMARK 465 GLN A 69 REMARK 465 ALA A 336 REMARK 465 GLN A 337 REMARK 465 MET B 0 REMARK 465 ALA B 1 REMARK 465 ASP B 2 REMARK 465 GLN B 3 REMARK 465 ALA B 4 REMARK 465 PRO B 5 REMARK 465 PHE B 6 REMARK 465 ASP B 7 REMARK 465 THR B 8 REMARK 465 SER B 62 REMARK 465 THR B 63 REMARK 465 ASN B 64 REMARK 465 VAL B 65 REMARK 465 THR B 66 REMARK 465 GLY B 67 REMARK 465 ASP B 68 REMARK 465 GLN B 69 REMARK 465 VAL B 70 REMARK 465 LYS B 71 REMARK 465 ALA B 336 REMARK 465 GLN B 337 REMARK 465 MET C 0 REMARK 465 ALA C 1 REMARK 465 ASP C 2 REMARK 465 GLN C 3 REMARK 465 ALA C 4 REMARK 465 PRO C 5 REMARK 465 PHE C 6 REMARK 465 ASP C 7 REMARK 465 THR C 8 REMARK 465 SER C 62 REMARK 465 THR C 63 REMARK 465 ASN C 64 REMARK 465 VAL C 65 REMARK 465 THR C 66 REMARK 465 GLY C 67 REMARK 465 ASP C 68 REMARK 465 GLN C 69 REMARK 465 VAL C 70 REMARK 465 LYS C 71 REMARK 465 ALA C 336 REMARK 465 GLN C 337 REMARK 465 MET D 0 REMARK 465 ALA D 1 REMARK 465 ASP D 2 REMARK 465 GLN D 3 REMARK 465 ALA D 4 REMARK 465 PRO D 5 REMARK 465 PHE D 6 REMARK 465 ASP D 7 REMARK 465 THR D 8 REMARK 465 SER D 62 REMARK 465 THR D 63 REMARK 465 ASN D 64 REMARK 465 VAL D 65 REMARK 465 THR D 66 REMARK 465 GLY D 67 REMARK 465 ASP D 68 REMARK 465 GLN D 69 REMARK 465 VAL D 70 REMARK 465 LYS D 71 REMARK 465 ALA D 336 REMARK 465 GLN D 337 REMARK 465 MET E 0 REMARK 465 ALA E 1 REMARK 465 ASP E 2 REMARK 465 GLN E 3 REMARK 465 ALA E 4 REMARK 465 PRO E 5 REMARK 465 PHE E 6 REMARK 465 ASP E 7 REMARK 465 THR E 8 REMARK 465 SER E 62 REMARK 465 THR E 63 REMARK 465 ASN E 64 REMARK 465 VAL E 65 REMARK 465 THR E 66 REMARK 465 GLY E 67 REMARK 465 ASP E 68 REMARK 465 GLN E 69 REMARK 465 ALA E 336 REMARK 465 GLN E 337 REMARK 465 MET F 0 REMARK 465 ALA F 1 REMARK 465 ASP F 2 REMARK 465 GLN F 3 REMARK 465 ALA F 4 REMARK 465 PRO F 5 REMARK 465 PHE F 6 REMARK 465 ASP F 7 REMARK 465 THR F 8 REMARK 465 SER F 62 REMARK 465 THR F 63 REMARK 465 ASN F 64 REMARK 465 VAL F 65 REMARK 465 THR F 66 REMARK 465 GLY F 67 REMARK 465 ASP F 68 REMARK 465 GLN F 69 REMARK 465 VAL F 70 REMARK 465 LYS F 71 REMARK 465 ALA F 336 REMARK 465 GLN F 337 REMARK 465 MET G 0 REMARK 465 ALA G 1 REMARK 465 ASP G 2 REMARK 465 GLN G 3 REMARK 465 ALA G 4 REMARK 465 PRO G 5 REMARK 465 PHE G 6 REMARK 465 ASP G 7 REMARK 465 THR G 8 REMARK 465 SER G 62 REMARK 465 THR G 63 REMARK 465 ASN G 64 REMARK 465 VAL G 65 REMARK 465 THR G 66 REMARK 465 GLY G 67 REMARK 465 ASP G 68 REMARK 465 GLN G 69 REMARK 465 VAL G 70 REMARK 465 LYS G 71 REMARK 465 ALA G 336 REMARK 465 GLN G 337 REMARK 465 MET H 0 REMARK 465 ALA H 1 REMARK 465 ASP H 2 REMARK 465 GLN H 3 REMARK 465 ALA H 4 REMARK 465 PRO H 5 REMARK 465 PHE H 6 REMARK 465 ASP H 7 REMARK 465 THR H 8 REMARK 465 SER H 62 REMARK 465 THR H 63 REMARK 465 ASN H 64 REMARK 465 VAL H 65 REMARK 465 THR H 66 REMARK 465 GLY H 67 REMARK 465 ASP H 68 REMARK 465 GLN H 69 REMARK 465 VAL H 70 REMARK 465 LYS H 71 REMARK 465 ALA H 336 REMARK 465 GLN H 337 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH D 645 O HOH D 653 2.06 REMARK 500 OG1 THR C 14 O HOH C 501 2.11 REMARK 500 OD2 ASP D 121 O HOH D 501 2.14 REMARK 500 O HOH D 644 O HOH D 671 2.14 REMARK 500 O HOH D 613 O HOH D 653 2.16 REMARK 500 O HOH C 527 O HOH C 597 2.17 REMARK 500 O HOH G 512 O HOH G 637 2.18 REMARK 500 O HOH B 507 O HOH B 575 2.18 REMARK 500 O HOH H 623 O HOH H 634 2.18 REMARK 500 O HOH B 606 O HOH C 649 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU E 211 CA - CB - CG ANGL. DEV. = 14.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 50 31.03 73.07 REMARK 500 ASP A 145 -179.66 -60.84 REMARK 500 LEU A 153 48.22 -94.08 REMARK 500 ASP A 235 32.27 -89.86 REMARK 500 ASN A 236 23.64 37.32 REMARK 500 GLU A 280 -56.96 -124.23 REMARK 500 LYS B 50 31.61 74.57 REMARK 500 ASP B 145 -111.39 -64.68 REMARK 500 LEU B 153 51.13 -97.03 REMARK 500 ASP B 235 32.01 -88.39 REMARK 500 ASN B 236 18.66 37.01 REMARK 500 GLU B 280 -57.24 -125.39 REMARK 500 LYS C 50 31.24 74.63 REMARK 500 LEU C 153 44.58 -94.46 REMARK 500 ASP C 235 32.50 -90.73 REMARK 500 ASN C 236 19.30 37.42 REMARK 500 GLU C 280 -57.45 -122.84 REMARK 500 LYS D 50 32.55 73.25 REMARK 500 CYS D 92 -30.27 -133.89 REMARK 500 ASP D 145 173.56 -58.98 REMARK 500 LEU D 153 48.48 -94.36 REMARK 500 ASP D 235 -143.70 -88.60 REMARK 500 GLU D 280 -57.98 -124.69 REMARK 500 LEU E 153 48.91 -94.08 REMARK 500 ASN E 236 20.94 48.68 REMARK 500 GLU E 280 -56.68 -125.47 REMARK 500 LYS F 50 30.36 74.25 REMARK 500 CYS F 92 -30.08 -134.37 REMARK 500 ASP F 145 -175.57 -62.24 REMARK 500 LEU F 153 46.14 -95.44 REMARK 500 ASP F 235 33.76 -93.15 REMARK 500 ASN F 236 23.09 37.77 REMARK 500 SER F 237 -175.16 -69.50 REMARK 500 GLU F 280 -56.12 -125.89 REMARK 500 LYS G 50 30.40 71.81 REMARK 500 ASP G 145 176.53 -59.73 REMARK 500 LEU G 153 44.11 -95.72 REMARK 500 ASP G 235 38.64 -91.21 REMARK 500 ASN G 236 19.34 41.45 REMARK 500 GLU G 280 -57.38 -121.91 REMARK 500 LYS H 50 30.23 71.77 REMARK 500 ASP H 145 176.39 -56.78 REMARK 500 LEU H 153 45.69 -94.99 REMARK 500 ASP H 235 -136.03 -88.30 REMARK 500 GLU H 280 -60.35 -125.27 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 E 587 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH H 644 DISTANCE = 6.09 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M B 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M C 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M D 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M E 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M F 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M G 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 95M H 401 DBREF 5Q03 A 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 B 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 C 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 D 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 E 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 F 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 G 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 DBREF 5Q03 H 0 337 UNP Q2TU34 Q2TU34_HUMAN 1 338 SEQRES 1 A 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 A 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 A 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 A 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 A 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 A 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 A 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 A 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 A 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 A 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 A 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 A 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 A 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 A 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 A 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 A 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 A 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 A 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 A 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 A 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 A 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 A 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 A 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 A 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 A 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 A 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 B 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 B 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 B 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 B 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 B 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 B 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 B 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 B 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 B 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 B 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 B 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 B 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 B 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 B 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 B 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 B 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 B 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 B 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 B 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 B 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 B 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 B 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 B 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 B 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 B 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 B 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 C 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 C 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 C 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 C 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 C 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 C 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 C 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 C 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 C 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 C 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 C 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 C 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 C 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 C 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 C 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 C 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 C 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 C 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 C 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 C 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 C 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 C 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 C 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 C 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 C 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 C 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 D 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 D 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 D 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 D 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 D 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 D 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 D 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 D 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 D 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 D 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 D 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 D 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 D 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 D 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 D 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 D 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 D 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 D 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 D 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 D 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 D 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 D 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 D 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 D 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 D 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 D 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 E 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 E 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 E 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 E 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 E 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 E 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 E 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 E 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 E 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 E 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 E 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 E 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 E 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 E 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 E 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 E 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 E 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 E 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 E 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 E 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 E 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 E 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 E 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 E 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 E 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 E 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 F 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 F 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 F 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 F 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 F 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 F 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 F 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 F 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 F 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 F 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 F 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 F 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 F 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 F 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 F 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 F 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 F 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 F 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 F 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 F 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 F 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 F 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 F 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 F 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 F 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 F 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 G 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 G 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 G 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 G 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 G 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 G 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 G 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 G 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 G 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 G 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 G 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 G 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 G 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 G 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 G 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 G 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 G 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 G 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 G 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 G 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 G 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 G 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 G 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 G 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 G 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 G 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN SEQRES 1 H 338 MET ALA ASP GLN ALA PRO PHE ASP THR ASP VAL ASN THR SEQRES 2 H 338 LEU THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG SEQRES 3 H 338 GLY THR GLY GLU LEU THR GLN LEU LEU ASN SER LEU CYS SEQRES 4 H 338 THR ALA VAL LYS ALA ILE SER SER ALA VAL ARG LYS ALA SEQRES 5 H 338 GLY ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN SEQRES 6 H 338 VAL THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER SEQRES 7 H 338 ASN ASP LEU VAL MET ASN MET LEU LYS SER SER PHE ALA SEQRES 8 H 338 THR CYS VAL LEU VAL SER GLU GLU ASP LYS HIS ALA ILE SEQRES 9 H 338 ILE VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS SEQRES 10 H 338 PHE ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU SEQRES 11 H 338 VAL SER VAL GLY THR ILE PHE GLY ILE TYR ARG LYS LYS SEQRES 12 H 338 SER THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO SEQRES 13 H 338 GLY ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SEQRES 14 H 338 SER ALA THR MET LEU VAL LEU ALA MET ASP CYS GLY VAL SEQRES 15 H 338 ASN CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE SEQRES 16 H 338 LEU VAL ASP LYS ASP VAL LYS ILE LYS LYS LYS GLY LYS SEQRES 17 H 338 ILE TYR SER LEU ASN GLU GLY TYR ALA LYS ASP PHE ASP SEQRES 18 H 338 PRO ALA VAL THR GLU TYR ILE GLN ARG LYS LYS PHE PRO SEQRES 19 H 338 PRO ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SEQRES 20 H 338 SER MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY SEQRES 21 H 338 GLY ILE PHE LEU TYR PRO ALA ASN LYS LYS SER PRO ASN SEQRES 22 H 338 GLY LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA SEQRES 23 H 338 TYR VAL MET GLU LYS ALA GLY GLY MET ALA THR THR GLY SEQRES 24 H 338 LYS GLU ALA VAL LEU ASP VAL ILE PRO THR ASP ILE HIS SEQRES 25 H 338 GLN ARG ALA PRO VAL ILE LEU GLY SER PRO ASP ASP VAL SEQRES 26 H 338 LEU GLU PHE LEU LYS VAL TYR GLU LYS HIS SER ALA GLN HET 95M A 401 22 HET 95M B 401 22 HET 95M C 401 22 HET 95M D 401 22 HET 95M E 401 22 HET 95M F 401 22 HET 95M G 401 22 HET 95M H 401 22 HETNAM 95M N-[(5-BROMO-1,3-THIAZOL-2-YL)CARBAMOYL]-5-(2- HETNAM 2 95M METHYLPROPYL)THIOPHENE-2-SULFONAMIDE FORMUL 9 95M 8(C12 H14 BR N3 O3 S3) FORMUL 17 HOH *1070(H2 O) HELIX 1 AA1 THR A 12 ARG A 25 1 14 HELIX 2 AA2 GLY A 28 ARG A 49 1 22 HELIX 3 AA3 GLY A 52 TYR A 57 1 6 HELIX 4 AA4 LYS A 72 SER A 87 1 16 HELIX 5 AA5 GLU A 106 ARG A 110 5 5 HELIX 6 AA6 GLY A 122 LEU A 129 5 8 HELIX 7 AA7 SER A 148 LEU A 153 5 6 HELIX 8 AA8 PRO A 155 LEU A 159 5 5 HELIX 9 AA9 ASN A 212 PHE A 219 5 8 HELIX 10 AB1 ASP A 220 PHE A 232 1 13 HELIX 11 AB2 SER A 247 GLY A 259 1 13 HELIX 12 AB3 GLU A 280 ALA A 291 1 12 HELIX 13 AB4 ALA A 301 VAL A 305 5 5 HELIX 14 AB5 SER A 320 HIS A 334 1 15 HELIX 15 AB6 THR B 12 ALA B 24 1 13 HELIX 16 AB7 GLY B 28 ARG B 49 1 22 HELIX 17 AB8 GLY B 52 TYR B 57 1 6 HELIX 18 AB9 LEU B 73 SER B 87 1 15 HELIX 19 AC1 GLU B 106 GLU B 108 5 3 HELIX 20 AC2 GLY B 122 LEU B 129 5 8 HELIX 21 AC3 SER B 148 LEU B 153 5 6 HELIX 22 AC4 PRO B 155 LEU B 159 5 5 HELIX 23 AC5 ASN B 212 PHE B 219 5 8 HELIX 24 AC6 ASP B 220 PHE B 232 1 13 HELIX 25 AC7 SER B 247 GLY B 259 1 13 HELIX 26 AC8 GLU B 280 ALA B 291 1 12 HELIX 27 AC9 ALA B 301 VAL B 305 5 5 HELIX 28 AD1 SER B 320 HIS B 334 1 15 HELIX 29 AD2 THR C 12 ARG C 25 1 14 HELIX 30 AD3 GLY C 28 ARG C 49 1 22 HELIX 31 AD4 GLY C 52 TYR C 57 1 6 HELIX 32 AD5 LEU C 73 SER C 87 1 15 HELIX 33 AD6 GLU C 106 GLU C 108 5 3 HELIX 34 AD7 GLY C 122 LEU C 129 5 8 HELIX 35 AD8 SER C 148 LEU C 153 5 6 HELIX 36 AD9 PRO C 155 LEU C 159 5 5 HELIX 37 AE1 ASN C 212 PHE C 219 5 8 HELIX 38 AE2 ASP C 220 PHE C 232 1 13 HELIX 39 AE3 SER C 247 GLY C 259 1 13 HELIX 40 AE4 GLU C 280 ALA C 291 1 12 HELIX 41 AE5 ALA C 301 VAL C 305 5 5 HELIX 42 AE6 SER C 320 HIS C 334 1 15 HELIX 43 AE7 THR D 12 ARG D 25 1 14 HELIX 44 AE8 GLY D 28 ARG D 49 1 22 HELIX 45 AE9 GLY D 52 TYR D 57 1 6 HELIX 46 AF1 LEU D 73 SER D 87 1 15 HELIX 47 AF2 GLU D 106 GLU D 108 5 3 HELIX 48 AF3 GLY D 122 LEU D 129 5 8 HELIX 49 AF4 SER D 148 LEU D 153 5 6 HELIX 50 AF5 PRO D 155 LEU D 159 5 5 HELIX 51 AF6 ASN D 212 PHE D 219 5 8 HELIX 52 AF7 ASP D 220 PHE D 232 1 13 HELIX 53 AF8 SER D 247 GLY D 259 1 13 HELIX 54 AF9 GLU D 280 ALA D 291 1 12 HELIX 55 AG1 ALA D 301 VAL D 305 5 5 HELIX 56 AG2 SER D 320 HIS D 334 1 15 HELIX 57 AG3 THR E 12 ALA E 24 1 13 HELIX 58 AG4 GLY E 28 ARG E 49 1 22 HELIX 59 AG5 GLY E 52 TYR E 57 1 6 HELIX 60 AG6 LYS E 72 SER E 87 1 16 HELIX 61 AG7 GLU E 106 GLU E 108 5 3 HELIX 62 AG8 GLY E 122 LEU E 129 5 8 HELIX 63 AG9 SER E 148 LEU E 153 5 6 HELIX 64 AH1 PRO E 155 LEU E 159 5 5 HELIX 65 AH2 ASN E 212 PHE E 219 5 8 HELIX 66 AH3 ASP E 220 PHE E 232 1 13 HELIX 67 AH4 SER E 247 GLY E 259 1 13 HELIX 68 AH5 GLU E 280 ALA E 291 1 12 HELIX 69 AH6 ALA E 301 VAL E 305 5 5 HELIX 70 AH7 SER E 320 HIS E 334 1 15 HELIX 71 AH8 THR F 12 ALA F 24 1 13 HELIX 72 AH9 GLY F 28 ARG F 49 1 22 HELIX 73 AI1 GLY F 52 TYR F 57 1 6 HELIX 74 AI2 LEU F 73 SER F 87 1 15 HELIX 75 AI3 GLU F 106 GLU F 108 5 3 HELIX 76 AI4 GLY F 122 LEU F 129 5 8 HELIX 77 AI5 SER F 148 LEU F 153 5 6 HELIX 78 AI6 PRO F 155 LEU F 159 5 5 HELIX 79 AI7 ASN F 212 PHE F 219 5 8 HELIX 80 AI8 ASP F 220 PHE F 232 1 13 HELIX 81 AI9 SER F 247 GLY F 259 1 13 HELIX 82 AJ1 GLU F 280 ALA F 291 1 12 HELIX 83 AJ2 ALA F 301 VAL F 305 5 5 HELIX 84 AJ3 SER F 320 HIS F 334 1 15 HELIX 85 AJ4 THR G 12 ALA G 24 1 13 HELIX 86 AJ5 GLY G 28 ARG G 49 1 22 HELIX 87 AJ6 GLY G 52 TYR G 57 1 6 HELIX 88 AJ7 LEU G 73 SER G 87 1 15 HELIX 89 AJ8 GLU G 106 GLU G 108 5 3 HELIX 90 AJ9 GLY G 122 LEU G 129 5 8 HELIX 91 AK1 SER G 148 LEU G 153 5 6 HELIX 92 AK2 PRO G 155 ARG G 157 5 3 HELIX 93 AK3 ASN G 212 PHE G 219 5 8 HELIX 94 AK4 ASP G 220 PHE G 232 1 13 HELIX 95 AK5 SER G 247 GLY G 259 1 13 HELIX 96 AK6 GLU G 280 ALA G 291 1 12 HELIX 97 AK7 ALA G 301 VAL G 305 5 5 HELIX 98 AK8 SER G 320 HIS G 334 1 15 HELIX 99 AK9 THR H 12 ARG H 25 1 14 HELIX 100 AL1 GLY H 28 ARG H 49 1 22 HELIX 101 AL2 GLY H 52 TYR H 57 1 6 HELIX 102 AL3 LEU H 73 SER H 87 1 15 HELIX 103 AL4 GLU H 106 ARG H 110 5 5 HELIX 104 AL5 GLY H 122 LEU H 129 5 8 HELIX 105 AL6 SER H 148 LEU H 153 5 6 HELIX 106 AL7 PRO H 155 LEU H 159 5 5 HELIX 107 AL8 ASN H 212 PHE H 219 5 8 HELIX 108 AL9 ASP H 220 PHE H 232 1 13 HELIX 109 AM1 SER H 247 GLY H 259 1 13 HELIX 110 AM2 GLU H 280 ALA H 291 1 12 HELIX 111 AM3 ALA H 301 VAL H 305 5 5 HELIX 112 AM4 SER H 320 HIS H 334 1 15 SHEET 1 AA1 8 ILE A 103 ILE A 104 0 SHEET 2 AA1 8 THR A 91 SER A 96 -1 N LEU A 94 O ILE A 103 SHEET 3 AA1 8 TYR A 113 ASP A 121 1 O TYR A 113 N CYS A 92 SHEET 4 AA1 8 VAL A 132 ARG A 140 -1 O TYR A 139 N VAL A 114 SHEET 5 AA1 8 ALA A 161 TYR A 167 -1 O TYR A 167 N VAL A 132 SHEET 6 AA1 8 THR A 171 MET A 177 -1 O ALA A 176 N ALA A 162 SHEET 7 AA1 8 GLY A 180 LEU A 186 -1 O ASN A 182 N LEU A 175 SHEET 8 AA1 8 PHE A 193 ASP A 197 -1 O ILE A 194 N MET A 185 SHEET 1 AA2 5 GLY A 241 ALA A 242 0 SHEET 2 AA2 5 ILE A 208 SER A 210 1 N TYR A 209 O GLY A 241 SHEET 3 AA2 5 ILE A 261 TYR A 264 1 O LEU A 263 N SER A 210 SHEET 4 AA2 5 VAL A 316 GLY A 319 -1 O VAL A 316 N TYR A 264 SHEET 5 AA2 5 MET A 294 THR A 296 -1 N MET A 294 O GLY A 319 SHEET 1 AA3 8 ILE B 103 ILE B 104 0 SHEET 2 AA3 8 THR B 91 SER B 96 -1 N LEU B 94 O ILE B 103 SHEET 3 AA3 8 ARG B 110 ASP B 121 1 O PHE B 117 N VAL B 95 SHEET 4 AA3 8 VAL B 132 ARG B 140 -1 O TYR B 139 N VAL B 114 SHEET 5 AA3 8 ALA B 161 TYR B 167 -1 O TYR B 167 N VAL B 132 SHEET 6 AA3 8 THR B 171 MET B 177 -1 O VAL B 174 N TYR B 164 SHEET 7 AA3 8 GLY B 180 LEU B 186 -1 O PHE B 184 N LEU B 173 SHEET 8 AA3 8 PHE B 193 ASP B 197 -1 O ILE B 194 N MET B 185 SHEET 1 AA4 5 GLY B 241 ALA B 242 0 SHEET 2 AA4 5 ILE B 208 SER B 210 1 N TYR B 209 O GLY B 241 SHEET 3 AA4 5 ILE B 261 TYR B 264 1 O LEU B 263 N SER B 210 SHEET 4 AA4 5 VAL B 316 GLY B 319 -1 O VAL B 316 N TYR B 264 SHEET 5 AA4 5 MET B 294 THR B 296 -1 N THR B 296 O ILE B 317 SHEET 1 AA5 8 ILE C 103 ILE C 104 0 SHEET 2 AA5 8 THR C 91 SER C 96 -1 N LEU C 94 O ILE C 103 SHEET 3 AA5 8 ARG C 110 ASP C 121 1 O PHE C 117 N VAL C 95 SHEET 4 AA5 8 VAL C 132 ARG C 140 -1 O TYR C 139 N VAL C 114 SHEET 5 AA5 8 ALA C 161 TYR C 167 -1 O ALA C 161 N ILE C 138 SHEET 6 AA5 8 THR C 171 MET C 177 -1 O VAL C 174 N TYR C 164 SHEET 7 AA5 8 GLY C 180 LEU C 186 -1 O PHE C 184 N LEU C 173 SHEET 8 AA5 8 PHE C 193 ASP C 197 -1 O ILE C 194 N MET C 185 SHEET 1 AA6 5 GLY C 241 ALA C 242 0 SHEET 2 AA6 5 ILE C 208 SER C 210 1 N TYR C 209 O GLY C 241 SHEET 3 AA6 5 ILE C 261 TYR C 264 1 O LEU C 263 N SER C 210 SHEET 4 AA6 5 VAL C 316 GLY C 319 -1 O LEU C 318 N PHE C 262 SHEET 5 AA6 5 MET C 294 THR C 296 -1 N THR C 296 O ILE C 317 SHEET 1 AA7 2 LEU C 275 ARG C 276 0 SHEET 2 AA7 2 ARG C 313 ALA C 314 -1 O ALA C 314 N LEU C 275 SHEET 1 AA8 8 ILE D 103 ILE D 104 0 SHEET 2 AA8 8 THR D 91 SER D 96 -1 N LEU D 94 O ILE D 103 SHEET 3 AA8 8 ARG D 110 ASP D 121 1 O PHE D 117 N VAL D 95 SHEET 4 AA8 8 VAL D 132 ARG D 140 -1 O GLY D 133 N ASP D 121 SHEET 5 AA8 8 ALA D 161 TYR D 167 -1 O ALA D 161 N ILE D 138 SHEET 6 AA8 8 THR D 171 MET D 177 -1 O VAL D 174 N TYR D 164 SHEET 7 AA8 8 GLY D 180 LEU D 186 -1 O PHE D 184 N LEU D 173 SHEET 8 AA8 8 PHE D 193 ASP D 197 -1 O ILE D 194 N MET D 185 SHEET 1 AA9 5 GLY D 241 ALA D 242 0 SHEET 2 AA9 5 ILE D 208 SER D 210 1 N TYR D 209 O GLY D 241 SHEET 3 AA9 5 ILE D 261 TYR D 264 1 O LEU D 263 N SER D 210 SHEET 4 AA9 5 VAL D 316 GLY D 319 -1 O LEU D 318 N PHE D 262 SHEET 5 AA9 5 MET D 294 THR D 296 -1 N THR D 296 O ILE D 317 SHEET 1 AB1 8 ILE E 103 ILE E 104 0 SHEET 2 AB1 8 THR E 91 SER E 96 -1 N LEU E 94 O ILE E 103 SHEET 3 AB1 8 ARG E 110 ASP E 121 1 O PHE E 117 N VAL E 95 SHEET 4 AB1 8 VAL E 132 ARG E 140 -1 O TYR E 139 N VAL E 114 SHEET 5 AB1 8 ALA E 161 TYR E 167 -1 O ALA E 161 N ILE E 138 SHEET 6 AB1 8 THR E 171 MET E 177 -1 O ALA E 176 N ALA E 162 SHEET 7 AB1 8 GLY E 180 LEU E 186 -1 O PHE E 184 N LEU E 173 SHEET 8 AB1 8 PHE E 193 ASP E 197 -1 O ILE E 194 N MET E 185 SHEET 1 AB2 5 GLY E 241 ALA E 242 0 SHEET 2 AB2 5 ILE E 208 SER E 210 1 N TYR E 209 O GLY E 241 SHEET 3 AB2 5 ILE E 261 TYR E 264 1 O LEU E 263 N SER E 210 SHEET 4 AB2 5 VAL E 316 GLY E 319 -1 O VAL E 316 N TYR E 264 SHEET 5 AB2 5 MET E 294 THR E 296 -1 N THR E 296 O ILE E 317 SHEET 1 AB3 8 ILE F 103 ILE F 104 0 SHEET 2 AB3 8 THR F 91 SER F 96 -1 N LEU F 94 O ILE F 103 SHEET 3 AB3 8 ARG F 110 ASP F 121 1 O GLY F 111 N THR F 91 SHEET 4 AB3 8 VAL F 132 ARG F 140 -1 O TYR F 139 N VAL F 114 SHEET 5 AB3 8 ALA F 161 TYR F 167 -1 O ALA F 161 N ILE F 138 SHEET 6 AB3 8 THR F 171 MET F 177 -1 O MET F 172 N LEU F 166 SHEET 7 AB3 8 GLY F 180 LEU F 186 -1 O PHE F 184 N LEU F 173 SHEET 8 AB3 8 PHE F 193 LYS F 198 -1 O ILE F 194 N MET F 185 SHEET 1 AB4 5 GLY F 241 ALA F 242 0 SHEET 2 AB4 5 ILE F 208 SER F 210 1 N TYR F 209 O GLY F 241 SHEET 3 AB4 5 ILE F 261 TYR F 264 1 O LEU F 263 N SER F 210 SHEET 4 AB4 5 VAL F 316 GLY F 319 -1 O VAL F 316 N TYR F 264 SHEET 5 AB4 5 MET F 294 THR F 296 -1 N THR F 296 O ILE F 317 SHEET 1 AB5 8 ILE G 103 ILE G 104 0 SHEET 2 AB5 8 THR G 91 SER G 96 -1 N LEU G 94 O ILE G 103 SHEET 3 AB5 8 ARG G 110 ASP G 121 1 O PHE G 117 N VAL G 95 SHEET 4 AB5 8 VAL G 132 ARG G 140 -1 O TYR G 139 N VAL G 114 SHEET 5 AB5 8 LEU G 159 TYR G 167 -1 O ALA G 161 N ILE G 138 SHEET 6 AB5 8 THR G 171 MET G 177 -1 O VAL G 174 N TYR G 164 SHEET 7 AB5 8 GLY G 180 LEU G 186 -1 O PHE G 184 N LEU G 173 SHEET 8 AB5 8 PHE G 193 ASP G 197 -1 O ILE G 194 N MET G 185 SHEET 1 AB6 5 GLY G 241 ALA G 242 0 SHEET 2 AB6 5 ILE G 208 SER G 210 1 N TYR G 209 O GLY G 241 SHEET 3 AB6 5 ILE G 261 TYR G 264 1 O LEU G 263 N SER G 210 SHEET 4 AB6 5 VAL G 316 GLY G 319 -1 O VAL G 316 N TYR G 264 SHEET 5 AB6 5 MET G 294 THR G 296 -1 N THR G 296 O ILE G 317 SHEET 1 AB7 8 ILE H 103 ILE H 104 0 SHEET 2 AB7 8 THR H 91 SER H 96 -1 N LEU H 94 O ILE H 103 SHEET 3 AB7 8 TYR H 113 ASP H 121 1 O PHE H 117 N VAL H 95 SHEET 4 AB7 8 VAL H 132 ARG H 140 -1 O GLY H 133 N ASP H 121 SHEET 5 AB7 8 ALA H 161 TYR H 167 -1 O TYR H 167 N VAL H 132 SHEET 6 AB7 8 THR H 171 MET H 177 -1 O ALA H 176 N ALA H 162 SHEET 7 AB7 8 GLY H 180 LEU H 186 -1 O PHE H 184 N LEU H 173 SHEET 8 AB7 8 PHE H 193 ASP H 197 -1 O ILE H 194 N MET H 185 SHEET 1 AB8 5 GLY H 241 ALA H 242 0 SHEET 2 AB8 5 ILE H 208 SER H 210 1 N TYR H 209 O GLY H 241 SHEET 3 AB8 5 ILE H 261 TYR H 264 1 O LEU H 263 N SER H 210 SHEET 4 AB8 5 VAL H 316 GLY H 319 -1 O LEU H 318 N PHE H 262 SHEET 5 AB8 5 MET H 294 THR H 296 -1 N THR H 296 O ILE H 317 SITE 1 AC1 10 GLY A 21 ARG A 22 GLY A 26 THR A 27 SITE 2 AC1 10 GLY A 28 LEU A 30 THR A 31 MET A 177 SITE 3 AC1 10 HOH A 587 95M C 401 SITE 1 AC2 10 GLY B 21 ARG B 22 ALA B 24 GLY B 26 SITE 2 AC2 10 THR B 27 GLY B 28 LEU B 30 THR B 31 SITE 3 AC2 10 MET B 177 95M D 401 SITE 1 AC3 13 95M A 401 MET C 18 GLU C 20 GLY C 21 SITE 2 AC3 13 ARG C 22 GLY C 26 THR C 27 GLY C 28 SITE 3 AC3 13 GLU C 29 LEU C 30 THR C 31 MET C 177 SITE 4 AC3 13 HOH C 567 SITE 1 AC4 12 THR B 27 95M B 401 GLU D 20 GLY D 21 SITE 2 AC4 12 ARG D 22 GLY D 26 THR D 27 GLY D 28 SITE 3 AC4 12 LEU D 30 THR D 31 MET D 177 HOH D 515 SITE 1 AC5 12 MET E 18 GLY E 21 ARG E 22 GLY E 26 SITE 2 AC5 12 THR E 27 GLY E 28 LEU E 30 THR E 31 SITE 3 AC5 12 MET E 177 HOH E 523 95M G 401 HOH G 582 SITE 1 AC6 9 MET F 18 GLY F 21 GLY F 26 THR F 27 SITE 2 AC6 9 GLY F 28 LEU F 30 THR F 31 HOH F 508 SITE 3 AC6 9 95M H 401 SITE 1 AC7 12 95M E 401 MET G 18 GLY G 21 ARG G 22 SITE 2 AC7 12 GLY G 26 THR G 27 GLY G 28 LEU G 30 SITE 3 AC7 12 THR G 31 MET G 177 HOH G 507 HOH G 582 SITE 1 AC8 12 THR F 27 95M F 401 GLU H 20 GLY H 21 SITE 2 AC8 12 ARG H 22 ALA H 24 GLY H 26 GLY H 28 SITE 3 AC8 12 LEU H 30 THR H 31 MET H 177 HOH H 511 CRYST1 66.435 294.192 83.569 90.00 97.56 90.00 P 1 21 1 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015052 0.000000 0.001999 0.00000 SCALE2 0.000000 0.003399 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012071 0.00000 ATOM 1 N ASP A 9 22.324 -3.882 -18.864 1.00 50.52 N ANISOU 1 N ASP A 9 6651 6002 6541 -19 274 106 N ATOM 2 CA ASP A 9 23.644 -3.992 -18.242 1.00 59.73 C ANISOU 2 CA ASP A 9 7790 7189 7715 -31 303 134 C ATOM 3 C ASP A 9 23.890 -2.872 -17.227 1.00 58.87 C ANISOU 3 C ASP A 9 7662 7093 7614 -39 281 133 C ATOM 4 O ASP A 9 23.490 -1.729 -17.448 1.00 64.51 O ANISOU 4 O ASP A 9 8397 7793 8322 -41 249 120 O ATOM 5 CB ASP A 9 24.738 -3.999 -19.314 1.00 71.35 C ANISOU 5 CB ASP A 9 9289 8646 9176 -41 329 159 C ATOM 6 CG ASP A 9 25.134 -5.413 -19.744 1.00 80.06 C ANISOU 6 CG ASP A 9 10387 9753 10279 -37 368 173 C ATOM 7 OD1 ASP A 9 24.561 -6.389 -19.206 1.00 83.47 O ANISOU 7 OD1 ASP A 9 10796 10199 10721 -26 375 164 O ATOM 8 OD2 ASP A 9 26.008 -5.548 -20.628 1.00 79.23 O ANISOU 8 OD2 ASP A 9 10302 9636 10164 -44 392 193 O ATOM 9 N VAL A 10 24.520 -3.212 -16.098 1.00 44.53 N ANISOU 9 N VAL A 10 5804 5304 5812 -42 298 145 N ATOM 10 CA VAL A 10 24.826 -2.212 -15.077 1.00 37.88 C ANISOU 10 CA VAL A 10 4940 4475 4977 -50 280 146 C ATOM 11 C VAL A 10 25.840 -1.191 -15.604 1.00 30.54 C ANISOU 11 C VAL A 10 4032 3534 4039 -65 281 164 C ATOM 12 O VAL A 10 26.737 -1.513 -16.393 1.00 30.73 O ANISOU 12 O VAL A 10 4071 3550 4056 -72 309 185 O ATOM 13 CB VAL A 10 25.335 -2.912 -13.798 1.00 35.65 C ANISOU 13 CB VAL A 10 4608 4224 4711 -50 301 157 C ATOM 14 CG1 VAL A 10 26.715 -3.539 -14.015 1.00 23.88 C ANISOU 14 CG1 VAL A 10 3111 2742 3222 -59 343 188 C ATOM 15 CG2 VAL A 10 25.327 -1.961 -12.610 1.00 36.45 C ANISOU 15 CG2 VAL A 10 4684 4342 4822 -55 278 150 C ATOM 16 N ASN A 11 25.714 0.054 -15.146 1.00 21.24 N ANISOU 16 N ASN A 11 2853 2354 2861 -70 250 155 N ATOM 17 CA ASN A 11 26.642 1.112 -15.515 1.00 29.83 C ANISOU 17 CA ASN A 11 3959 3433 3942 -85 249 171 C ATOM 18 C ASN A 11 27.012 1.916 -14.275 1.00 36.62 C ANISOU 18 C ASN A 11 4788 4313 4814 -92 235 173 C ATOM 19 O ASN A 11 26.186 2.120 -13.383 1.00 35.00 O ANISOU 19 O ASN A 11 4562 4118 4617 -85 211 153 O ATOM 20 CB ASN A 11 26.043 2.060 -16.567 1.00 28.71 C ANISOU 20 CB ASN A 11 3864 3260 3784 -85 219 157 C ATOM 21 CG ASN A 11 27.108 2.679 -17.462 1.00 41.61 C ANISOU 21 CG ASN A 11 5526 4878 5406 -99 232 178 C ATOM 22 OD1 ASN A 11 28.300 2.633 -17.148 1.00 52.44 O ANISOU 22 OD1 ASN A 11 6880 6262 6783 -110 257 202 O ATOM 23 ND2 ASN A 11 26.685 3.264 -18.582 1.00 42.21 N ANISOU 23 ND2 ASN A 11 5646 4924 5466 -99 214 169 N ATOM 24 N THR A 12 28.260 2.380 -14.236 1.00 37.17 N ANISOU 24 N THR A 12 4854 4386 4883 -106 251 196 N ATOM 25 CA THR A 12 28.776 3.211 -13.157 1.00 34.53 C ANISOU 25 CA THR A 12 4493 4069 4558 -115 241 201 C ATOM 26 C THR A 12 29.263 4.554 -13.690 1.00 37.56 C ANISOU 26 C THR A 12 4904 4434 4931 -128 225 207 C ATOM 27 O THR A 12 29.447 4.748 -14.896 1.00 39.12 O ANISOU 27 O THR A 12 5141 4609 5115 -132 229 212 O ATOM 28 CB THR A 12 29.916 2.506 -12.415 1.00 35.40 C ANISOU 28 CB THR A 12 4565 4204 4680 -120 277 225 C ATOM 29 OG1 THR A 12 31.051 2.394 -13.279 1.00 32.96 O ANISOU 29 OG1 THR A 12 4274 3887 4363 -131 306 250 O ATOM 30 CG2 THR A 12 29.476 1.103 -11.932 1.00 25.56 C ANISOU 30 CG2 THR A 12 3293 2976 3444 -108 295 221 C ATOM 31 N LEU A 13 29.524 5.470 -12.751 1.00 40.34 N ANISOU 31 N LEU A 13 5236 4799 5291 -134 208 206 N ATOM 32 CA LEU A 13 29.999 6.815 -13.090 1.00 31.43 C ANISOU 32 CA LEU A 13 4130 3656 4155 -147 191 211 C ATOM 33 C LEU A 13 31.307 6.758 -13.864 1.00 30.52 C ANISOU 33 C LEU A 13 4030 3534 4033 -160 222 239 C ATOM 34 O LEU A 13 31.449 7.398 -14.912 1.00 35.18 O ANISOU 34 O LEU A 13 4659 4099 4608 -167 216 241 O ATOM 35 CB LEU A 13 30.198 7.627 -11.810 1.00 24.32 C ANISOU 35 CB LEU A 13 3199 2776 3267 -153 173 209 C ATOM 36 CG LEU A 13 30.734 9.063 -11.777 1.00 25.10 C ANISOU 36 CG LEU A 13 3309 2867 3362 -166 154 213 C ATOM 37 CD1 LEU A 13 30.113 9.978 -12.807 1.00 16.75 C ANISOU 37 CD1 LEU A 13 2298 1778 2288 -167 125 200 C ATOM 38 CD2 LEU A 13 30.515 9.600 -10.363 1.00 41.61 C ANISOU 38 CD2 LEU A 13 5364 4980 5466 -166 132 204 C ATOM 39 N THR A 14 32.271 5.988 -13.356 1.00 29.43 N ANISOU 39 N THR A 14 3861 3417 3904 -164 257 260 N ATOM 40 CA THR A 14 33.566 5.879 -14.012 1.00 37.02 C ANISOU 40 CA THR A 14 4832 4373 4860 -177 289 286 C ATOM 41 C THR A 14 33.405 5.258 -15.394 1.00 37.96 C ANISOU 41 C THR A 14 4988 4470 4965 -174 305 289 C ATOM 42 O THR A 14 33.946 5.770 -16.381 1.00 37.74 O ANISOU 42 O THR A 14 4993 4421 4924 -183 310 299 O ATOM 43 CB THR A 14 34.519 5.033 -13.153 1.00 41.66 C ANISOU 43 CB THR A 14 5377 4990 5462 -179 323 306 C ATOM 44 OG1 THR A 14 34.631 5.592 -11.839 1.00 38.34 O ANISOU 44 OG1 THR A 14 4923 4591 5055 -182 308 303 O ATOM 45 CG2 THR A 14 35.906 5.002 -13.766 1.00 41.85 C ANISOU 45 CG2 THR A 14 5410 5010 5481 -193 356 334 C ATOM 46 N ARG A 15 32.600 4.192 -15.496 1.00 38.96 N ANISOU 46 N ARG A 15 5111 4598 5093 -159 310 278 N ATOM 47 CA ARG A 15 32.392 3.546 -16.793 1.00 42.66 C ANISOU 47 CA ARG A 15 5614 5045 5548 -155 324 279 C ATOM 48 C ARG A 15 31.673 4.480 -17.773 1.00 33.18 C ANISOU 48 C ARG A 15 4460 3815 4332 -155 293 263 C ATOM 49 O ARG A 15 32.051 4.569 -18.945 1.00 39.09 O ANISOU 49 O ARG A 15 5244 4541 5067 -161 304 273 O ATOM 50 CB ARG A 15 31.630 2.227 -16.584 1.00 37.59 C ANISOU 50 CB ARG A 15 4956 4414 4913 -139 334 269 C ATOM 51 CG ARG A 15 31.228 1.451 -17.834 1.00 39.58 C ANISOU 51 CG ARG A 15 5240 4645 5153 -132 347 266 C ATOM 52 CD ARG A 15 30.398 0.189 -17.500 1.00 43.79 C ANISOU 52 CD ARG A 15 5755 5190 5694 -116 354 254 C ATOM 53 NE ARG A 15 31.274 -0.958 -17.204 1.00 42.24 N ANISOU 53 NE ARG A 15 5530 5012 5506 -117 395 275 N ATOM 54 CZ ARG A 15 30.866 -2.204 -16.961 1.00 34.24 C ANISOU 54 CZ ARG A 15 4499 4010 4499 -105 411 271 C ATOM 55 NH1 ARG A 15 29.572 -2.505 -16.979 1.00 31.42 N ANISOU 55 NH1 ARG A 15 4147 3648 4142 -92 391 247 N ATOM 56 NH2 ARG A 15 31.760 -3.159 -16.704 1.00 27.02 N ANISOU 56 NH2 ARG A 15 3560 3113 3592 -107 448 292 N ATOM 57 N PHE A 16 30.655 5.201 -17.301 1.00 32.04 N ANISOU 57 N PHE A 16 4317 3668 4190 -149 254 239 N ATOM 58 CA PHE A 16 29.925 6.146 -18.142 1.00 26.11 C ANISOU 58 CA PHE A 16 3608 2889 3425 -148 222 223 C ATOM 59 C PHE A 16 30.830 7.278 -18.616 1.00 30.69 C ANISOU 59 C PHE A 16 4211 3456 3996 -165 220 238 C ATOM 60 O PHE A 16 30.835 7.629 -19.802 1.00 37.44 O ANISOU 60 O PHE A 16 5108 4284 4835 -168 217 239 O ATOM 61 CB PHE A 16 28.728 6.691 -17.358 1.00 24.31 C ANISOU 61 CB PHE A 16 3369 2666 3203 -138 181 195 C ATOM 62 CG PHE A 16 28.007 7.840 -18.015 1.00 29.83 C ANISOU 62 CG PHE A 16 4108 3338 3889 -138 143 178 C ATOM 63 CD1 PHE A 16 28.489 9.134 -17.915 1.00 28.13 C ANISOU 63 CD1 PHE A 16 3901 3116 3670 -151 126 182 C ATOM 64 CD2 PHE A 16 26.809 7.637 -18.674 1.00 37.03 C ANISOU 64 CD2 PHE A 16 5044 4231 4792 -125 123 155 C ATOM 65 CE1 PHE A 16 27.810 10.197 -18.501 1.00 32.19 C ANISOU 65 CE1 PHE A 16 4452 3606 4173 -150 90 166 C ATOM 66 CE2 PHE A 16 26.131 8.696 -19.261 1.00 33.60 C ANISOU 66 CE2 PHE A 16 4647 3773 4347 -125 87 138 C ATOM 67 CZ PHE A 16 26.631 9.981 -19.165 1.00 32.67 C ANISOU 67 CZ PHE A 16 4539 3649 4225 -137 71 144 C ATOM 68 N VAL A 17 31.628 7.846 -17.713 1.00 29.90 N ANISOU 68 N VAL A 17 4084 3373 3905 -175 222 249 N ATOM 69 CA VAL A 17 32.454 8.972 -18.131 1.00 30.78 C ANISOU 69 CA VAL A 17 4217 3472 4008 -191 218 262 C ATOM 70 C VAL A 17 33.576 8.503 -19.059 1.00 32.74 C ANISOU 70 C VAL A 17 4480 3711 4247 -201 257 288 C ATOM 71 O VAL A 17 33.991 9.239 -19.963 1.00 23.77 O ANISOU 71 O VAL A 17 3380 2553 3098 -212 255 295 O ATOM 72 CB VAL A 17 32.950 9.771 -16.913 1.00 26.70 C ANISOU 72 CB VAL A 17 3667 2975 3504 -200 207 266 C ATOM 73 CG1 VAL A 17 33.916 10.837 -17.340 1.00 28.98 C ANISOU 73 CG1 VAL A 17 3975 3251 3784 -217 208 282 C ATOM 74 CG2 VAL A 17 31.745 10.448 -16.223 1.00 27.12 C ANISOU 74 CG2 VAL A 17 3715 3029 3561 -190 164 238 C ATOM 75 N MET A 18 34.101 7.295 -18.855 1.00 35.98 N ANISOU 75 N MET A 18 4866 4139 4667 -199 292 302 N ATOM 76 CA MET A 18 35.123 6.797 -19.773 1.00 38.22 C ANISOU 76 CA MET A 18 5165 4414 4942 -207 329 325 C ATOM 77 C MET A 18 34.562 6.603 -21.186 1.00 34.33 C ANISOU 77 C MET A 18 4720 3892 4432 -202 327 318 C ATOM 78 O MET A 18 35.244 6.890 -22.176 1.00 30.13 O ANISOU 78 O MET A 18 4218 3342 3887 -213 341 332 O ATOM 79 CB MET A 18 35.730 5.503 -19.235 1.00 34.30 C ANISOU 79 CB MET A 18 4631 3942 4458 -204 367 340 C ATOM 80 CG MET A 18 36.679 5.718 -18.069 1.00 42.34 C ANISOU 80 CG MET A 18 5608 4987 5491 -213 378 355 C ATOM 81 SD MET A 18 37.494 4.200 -17.479 1.00 45.24 S ANISOU 81 SD MET A 18 5933 5383 5873 -210 423 374 S ATOM 82 CE MET A 18 36.085 3.184 -16.997 1.00 41.30 C ANISOU 82 CE MET A 18 5418 4893 5381 -189 411 351 C ATOM 83 N GLU A 19 33.316 6.137 -21.301 1.00 33.13 N ANISOU 83 N GLU A 19 4574 3734 4278 -187 309 296 N ATOM 84 CA GLU A 19 32.728 5.939 -22.623 1.00 34.45 C ANISOU 84 CA GLU A 19 4786 3874 4429 -181 306 289 C ATOM 85 C GLU A 19 32.462 7.267 -23.337 1.00 36.46 C ANISOU 85 C GLU A 19 5083 4101 4669 -188 275 280 C ATOM 86 O GLU A 19 32.705 7.383 -24.543 1.00 31.39 O ANISOU 86 O GLU A 19 4480 3436 4011 -193 283 287 O ATOM 87 CB GLU A 19 31.430 5.135 -22.529 1.00 35.29 C ANISOU 87 CB GLU A 19 4889 3982 4539 -162 293 266 C ATOM 88 CG GLU A 19 31.628 3.690 -22.168 1.00 57.55 C ANISOU 88 CG GLU A 19 7677 6821 7369 -155 326 274 C ATOM 89 CD GLU A 19 30.327 3.006 -21.827 1.00 75.74 C ANISOU 89 CD GLU A 19 9970 9129 9677 -137 310 251 C ATOM 90 OE1 GLU A 19 29.293 3.709 -21.785 1.00 83.12 O ANISOU 90 OE1 GLU A 19 10919 10054 10609 -131 272 227 O ATOM 91 OE2 GLU A 19 30.344 1.781 -21.563 1.00 78.27 O ANISOU 91 OE2 GLU A 19 10268 9466 10007 -129 335 255 O ATOM 92 N GLU A 20 31.932 8.269 -22.633 1.00 31.18 N ANISOU 92 N GLU A 20 4408 3436 4005 -187 239 265 N ATOM 93 CA GLU A 20 31.714 9.546 -23.300 1.00 36.96 C ANISOU 93 CA GLU A 20 5179 4141 4722 -194 210 257 C ATOM 94 C GLU A 20 33.042 10.150 -23.734 1.00 36.52 C ANISOU 94 C GLU A 20 5137 4079 4659 -213 230 282 C ATOM 95 O GLU A 20 33.143 10.747 -24.812 1.00 31.30 O ANISOU 95 O GLU A 20 4519 3391 3981 -219 224 285 O ATOM 96 CB GLU A 20 30.944 10.493 -22.387 1.00 31.55 C ANISOU 96 CB GLU A 20 4482 3462 4044 -190 169 237 C ATOM 97 CG GLU A 20 29.535 10.004 -22.068 1.00 42.36 C ANISOU 97 CG GLU A 20 5844 4834 5418 -171 146 210 C ATOM 98 CD GLU A 20 28.567 10.022 -23.239 1.00 47.05 C ANISOU 98 CD GLU A 20 6482 5398 5996 -162 127 193 C ATOM 99 OE1 GLU A 20 28.728 10.861 -24.141 1.00 54.14 O ANISOU 99 OE1 GLU A 20 7421 6272 6879 -170 116 195 O ATOM 100 OE2 GLU A 20 27.628 9.190 -23.247 1.00 48.37 O ANISOU 100 OE2 GLU A 20 6645 5568 6166 -147 124 177 O ATOM 101 N GLY A 21 34.087 9.945 -22.935 1.00 36.64 N ANISOU 101 N GLY A 21 5116 4118 4688 -222 255 301 N ATOM 102 CA GLY A 21 35.388 10.480 -23.281 1.00 29.16 C ANISOU 102 CA GLY A 21 4177 3166 3735 -240 275 325 C ATOM 103 C GLY A 21 36.013 9.766 -24.458 1.00 39.07 C ANISOU 103 C GLY A 21 5458 4409 4980 -245 310 342 C ATOM 104 O GLY A 21 36.561 10.408 -25.356 1.00 43.00 O ANISOU 104 O GLY A 21 5989 4886 5463 -257 314 352 O ATOM 105 N ARG A 22 35.926 8.431 -24.486 1.00 40.97 N ANISOU 105 N ARG A 22 5681 4659 5225 -235 335 345 N ATOM 106 CA ARG A 22 36.439 7.706 -25.646 1.00 43.06 C ANISOU 106 CA ARG A 22 5971 4910 5478 -237 367 360 C ATOM 107 C ARG A 22 35.635 8.039 -26.903 1.00 41.42 C ANISOU 107 C ARG A 22 5817 4671 5252 -233 348 346 C ATOM 108 O ARG A 22 36.190 8.119 -27.999 1.00 40.84 O ANISOU 108 O ARG A 22 5776 4578 5164 -242 364 359 O ATOM 109 CB ARG A 22 36.429 6.189 -25.392 1.00 31.58 C ANISOU 109 CB ARG A 22 4490 3476 4035 -227 397 364 C ATOM 110 CG ARG A 22 37.428 5.660 -24.346 1.00 32.42 C ANISOU 110 CG ARG A 22 4547 3613 4158 -232 426 382 C ATOM 111 CD ARG A 22 37.445 4.111 -24.327 1.00 34.86 C ANISOU 111 CD ARG A 22 4835 3935 4474 -221 457 388 C ATOM 112 NE ARG A 22 37.966 3.592 -25.603 1.00 35.67 N ANISOU 112 NE ARG A 22 4969 4021 4564 -226 486 402 N ATOM 113 CZ ARG A 22 37.911 2.320 -26.016 1.00 40.93 C ANISOU 113 CZ ARG A 22 5632 4689 5230 -217 512 406 C ATOM 114 NH1 ARG A 22 37.354 1.379 -25.262 1.00 34.71 N ANISOU 114 NH1 ARG A 22 4813 3920 4454 -203 515 397 N ATOM 115 NH2 ARG A 22 38.422 1.983 -27.203 1.00 41.38 N ANISOU 115 NH2 ARG A 22 5719 4728 5273 -222 536 418 N ATOM 116 N LYS A 23 34.330 8.243 -26.753 1.00 43.59 N ANISOU 116 N LYS A 23 6098 4938 5525 -219 312 321 N ATOM 117 CA LYS A 23 33.470 8.589 -27.876 1.00 37.47 C ANISOU 117 CA LYS A 23 5371 4132 4732 -214 290 305 C ATOM 118 C LYS A 23 33.828 9.952 -28.470 1.00 43.36 C ANISOU 118 C LYS A 23 6154 4856 5465 -228 273 309 C ATOM 119 O LYS A 23 33.819 10.128 -29.696 1.00 47.51 O ANISOU 119 O LYS A 23 6724 5355 5973 -231 274 311 O ATOM 120 CB LYS A 23 32.021 8.522 -27.398 1.00 36.05 C ANISOU 120 CB LYS A 23 5186 3955 4558 -196 255 276 C ATOM 121 CG LYS A 23 30.977 8.299 -28.443 1.00 49.67 C ANISOU 121 CG LYS A 23 6950 5654 6269 -184 239 259 C ATOM 122 CD LYS A 23 29.592 8.141 -27.809 1.00 58.49 C ANISOU 122 CD LYS A 23 8053 6778 7394 -167 208 231 C ATOM 123 CE LYS A 23 28.972 9.456 -27.383 1.00 69.74 C ANISOU 123 CE LYS A 23 9485 8196 8818 -167 164 213 C ATOM 124 NZ LYS A 23 27.523 9.255 -27.055 1.00 75.24 N ANISOU 124 NZ LYS A 23 10177 8893 9519 -149 133 183 N ATOM 125 N ALA A 24 34.155 10.921 -27.627 1.00 34.45 N ANISOU 125 N ALA A 24 5008 3738 4344 -237 257 310 N ATOM 126 CA ALA A 24 34.460 12.283 -28.055 1.00 34.49 C ANISOU 126 CA ALA A 24 5045 3723 4337 -250 237 312 C ATOM 127 C ALA A 24 35.935 12.507 -28.365 1.00 32.31 C ANISOU 127 C ALA A 24 4771 3447 4058 -269 270 341 C ATOM 128 O ALA A 24 36.306 13.628 -28.725 1.00 35.27 O ANISOU 128 O ALA A 24 5172 3807 4423 -282 257 345 O ATOM 129 CB ALA A 24 34.001 13.290 -26.990 1.00 40.49 C ANISOU 129 CB ALA A 24 5786 4493 5106 -249 201 298 C ATOM 130 N ARG A 25 36.780 11.484 -28.191 1.00 24.37 N ANISOU 130 N ARG A 25 3739 2460 3061 -272 310 359 N ATOM 131 CA ARG A 25 38.193 11.524 -28.559 1.00 23.63 C ANISOU 131 CA ARG A 25 3647 2367 2964 -289 345 386 C ATOM 132 C ARG A 25 38.999 12.539 -27.730 1.00 28.85 C ANISOU 132 C ARG A 25 4287 3040 3633 -304 339 396 C ATOM 133 O ARG A 25 39.931 13.165 -28.234 1.00 29.94 O ANISOU 133 O ARG A 25 4445 3169 3764 -321 352 412 O ATOM 134 CB ARG A 25 38.337 11.812 -30.059 1.00 43.48 C ANISOU 134 CB ARG A 25 6216 4849 5456 -296 350 391 C ATOM 135 CG ARG A 25 37.546 10.856 -30.971 1.00 64.42 C ANISOU 135 CG ARG A 25 8891 7486 8099 -282 355 382 C ATOM 136 CD ARG A 25 37.682 11.259 -32.461 1.00 82.17 C ANISOU 136 CD ARG A 25 11196 9701 10324 -289 357 387 C ATOM 137 NE ARG A 25 36.889 10.421 -33.368 1.00 92.71 N ANISOU 137 NE ARG A 25 12556 11021 11649 -276 359 377 N ATOM 138 CZ ARG A 25 35.637 10.684 -33.745 1.00 96.61 C ANISOU 138 CZ ARG A 25 13077 11496 12134 -263 324 354 C ATOM 139 NH1 ARG A 25 35.022 11.774 -33.307 1.00 96.87 N ANISOU 139 NH1 ARG A 25 13116 11525 12167 -262 285 337 N ATOM 140 NH2 ARG A 25 34.993 9.858 -34.563 1.00 96.64 N ANISOU 140 NH2 ARG A 25 13102 11487 12129 -251 329 346 N ATOM 141 N GLY A 26 38.671 12.692 -26.424 1.00 34.83 N ANISOU 141 N GLY A 26 5005 3821 4408 -299 322 386 N ATOM 142 CA GLY A 26 39.442 13.585 -25.573 1.00 19.38 C ANISOU 142 CA GLY A 26 3026 1878 2460 -312 318 395 C ATOM 143 C GLY A 26 40.738 12.951 -25.057 1.00 23.66 C ANISOU 143 C GLY A 26 3531 2444 3015 -322 359 419 C ATOM 144 O GLY A 26 40.964 11.746 -25.153 1.00 29.21 O ANISOU 144 O GLY A 26 4219 3158 3722 -316 389 427 O ATOM 145 N THR A 27 41.574 13.785 -24.437 1.00 20.43 N ANISOU 145 N THR A 27 3106 2045 2612 -336 358 429 N ATOM 146 CA THR A 27 42.866 13.339 -23.923 1.00 26.24 C ANISOU 146 CA THR A 27 3807 2803 3360 -346 395 452 C ATOM 147 C THR A 27 42.747 12.536 -22.635 1.00 38.18 C ANISOU 147 C THR A 27 5266 4348 4892 -335 401 450 C ATOM 148 O THR A 27 43.681 11.796 -22.288 1.00 31.37 O ANISOU 148 O THR A 27 4374 3504 4040 -339 435 468 O ATOM 149 CB THR A 27 43.774 14.535 -23.603 1.00 30.36 C ANISOU 149 CB THR A 27 4326 3325 3883 -365 390 463 C ATOM 150 OG1 THR A 27 43.270 15.239 -22.449 1.00 29.51 O ANISOU 150 OG1 THR A 27 4194 3232 3787 -361 358 449 O ATOM 151 CG2 THR A 27 43.842 15.505 -24.790 1.00 24.30 C ANISOU 151 CG2 THR A 27 3612 2526 3095 -376 380 464 C ATOM 152 N GLY A 28 41.625 12.671 -21.930 1.00 35.36 N ANISOU 152 N GLY A 28 4897 3996 4541 -322 368 428 N ATOM 153 CA GLY A 28 41.423 12.069 -20.635 1.00 33.46 C ANISOU 153 CA GLY A 28 4607 3786 4319 -312 369 423 C ATOM 154 C GLY A 28 41.522 13.014 -19.451 1.00 34.94 C ANISOU 154 C GLY A 28 4768 3989 4519 -317 346 419 C ATOM 155 O GLY A 28 41.215 12.582 -18.330 1.00 27.55 O ANISOU 155 O GLY A 28 3792 3078 3598 -308 341 412 O ATOM 156 N GLU A 29 41.903 14.290 -19.660 1.00 31.42 N ANISOU 156 N GLU A 29 4342 3530 4065 -331 330 422 N ATOM 157 CA GLU A 29 42.102 15.192 -18.526 1.00 31.00 C ANISOU 157 CA GLU A 29 4261 3492 4024 -337 310 419 C ATOM 158 C GLU A 29 40.811 15.414 -17.768 1.00 36.19 C ANISOU 158 C GLU A 29 4907 4155 4687 -323 272 394 C ATOM 159 O GLU A 29 40.807 15.398 -16.530 1.00 35.42 O ANISOU 159 O GLU A 29 4769 4083 4605 -320 266 390 O ATOM 160 CB GLU A 29 42.671 16.547 -18.947 1.00 32.26 C ANISOU 160 CB GLU A 29 4448 3635 4174 -355 298 425 C ATOM 161 CG GLU A 29 44.123 16.752 -18.538 1.00 44.74 C ANISOU 161 CG GLU A 29 6005 5231 5763 -371 325 449 C ATOM 162 CD GLU A 29 44.625 18.177 -18.777 1.00 51.19 C ANISOU 162 CD GLU A 29 6845 6033 6573 -388 310 453 C ATOM 163 OE1 GLU A 29 44.318 19.051 -17.944 1.00 49.46 O ANISOU 163 OE1 GLU A 29 6612 5820 6360 -389 280 442 O ATOM 164 OE2 GLU A 29 45.327 18.428 -19.778 1.00 55.48 O ANISOU 164 OE2 GLU A 29 7418 6558 7103 -401 327 467 O ATOM 165 N LEU A 30 39.697 15.586 -18.483 1.00 29.69 N ANISOU 165 N LEU A 30 4119 3309 3851 -313 247 375 N ATOM 166 CA LEU A 30 38.434 15.785 -17.783 1.00 31.57 C ANISOU 166 CA LEU A 30 4348 3553 4096 -299 210 349 C ATOM 167 C LEU A 30 38.027 14.535 -16.989 1.00 39.37 C ANISOU 167 C LEU A 30 5296 4565 5097 -285 223 344 C ATOM 168 O LEU A 30 37.535 14.639 -15.859 1.00 37.12 O ANISOU 168 O LEU A 30 4980 4300 4826 -278 204 332 O ATOM 169 CB LEU A 30 37.351 16.177 -18.787 1.00 17.04 C ANISOU 169 CB LEU A 30 2554 1682 2239 -292 182 330 C ATOM 170 CG LEU A 30 35.961 16.400 -18.186 1.00 24.47 C ANISOU 170 CG LEU A 30 3488 2625 3183 -277 143 302 C ATOM 171 CD1 LEU A 30 35.985 17.521 -17.133 1.00 26.52 C ANISOU 171 CD1 LEU A 30 3727 2896 3452 -282 115 295 C ATOM 172 CD2 LEU A 30 34.952 16.706 -19.268 1.00 21.82 C ANISOU 172 CD2 LEU A 30 3200 2259 2832 -269 118 284 C ATOM 173 N THR A 31 38.266 13.344 -17.542 1.00 34.87 N ANISOU 173 N THR A 31 4727 3996 4526 -280 255 354 N ATOM 174 CA THR A 31 37.913 12.113 -16.840 1.00 35.82 C ANISOU 174 CA THR A 31 4812 4140 4659 -267 269 351 C ATOM 175 C THR A 31 38.719 11.944 -15.549 1.00 25.84 C ANISOU 175 C THR A 31 3498 2907 3413 -271 284 363 C ATOM 176 O THR A 31 38.179 11.522 -14.522 1.00 23.75 O ANISOU 176 O THR A 31 3200 2663 3162 -261 276 352 O ATOM 177 CB THR A 31 38.072 10.928 -17.803 1.00 32.89 C ANISOU 177 CB THR A 31 4456 3761 4281 -262 301 360 C ATOM 178 OG1 THR A 31 36.942 10.902 -18.674 1.00 45.03 O ANISOU 178 OG1 THR A 31 6030 5274 5805 -252 281 342 O ATOM 179 CG2 THR A 31 38.119 9.601 -17.096 1.00 20.47 C ANISOU 179 CG2 THR A 31 2843 2213 2721 -252 326 365 C ATOM 180 N GLN A 32 40.007 12.270 -15.580 1.00 18.70 N ANISOU 180 N GLN A 32 2588 2007 2510 -287 306 385 N ATOM 181 CA GLN A 32 40.801 12.258 -14.359 1.00 27.93 C ANISOU 181 CA GLN A 32 3712 3205 3696 -292 317 397 C ATOM 182 C GLN A 32 40.283 13.276 -13.340 1.00 32.03 C ANISOU 182 C GLN A 32 4215 3732 4222 -292 280 381 C ATOM 183 O GLN A 32 40.285 13.004 -12.129 1.00 27.28 O ANISOU 183 O GLN A 32 3573 3157 3637 -287 279 379 O ATOM 184 CB GLN A 32 42.265 12.523 -14.693 1.00 29.70 C ANISOU 184 CB GLN A 32 3938 3429 3919 -310 346 422 C ATOM 185 CG GLN A 32 42.951 11.332 -15.307 1.00 35.54 C ANISOU 185 CG GLN A 32 4676 4170 4656 -310 388 440 C ATOM 186 CD GLN A 32 44.293 11.682 -15.898 1.00 41.95 C ANISOU 186 CD GLN A 32 5500 4976 5464 -328 414 463 C ATOM 187 OE1 GLN A 32 44.438 12.703 -16.571 1.00 46.16 O ANISOU 187 OE1 GLN A 32 6066 5488 5985 -339 401 464 O ATOM 188 NE2 GLN A 32 45.285 10.833 -15.662 1.00 41.45 N ANISOU 188 NE2 GLN A 32 5410 4930 5409 -331 452 483 N ATOM 189 N LEU A 33 39.868 14.463 -13.811 1.00 27.25 N ANISOU 189 N LEU A 33 3643 3105 3606 -297 249 370 N ATOM 190 CA LEU A 33 39.282 15.477 -12.934 1.00 24.97 C ANISOU 190 CA LEU A 33 3343 2821 3322 -296 211 353 C ATOM 191 C LEU A 33 38.037 14.939 -12.245 1.00 28.77 C ANISOU 191 C LEU A 33 3806 3314 3812 -277 191 331 C ATOM 192 O LEU A 33 37.896 15.029 -11.021 1.00 30.35 O ANISOU 192 O LEU A 33 3968 3536 4025 -274 181 325 O ATOM 193 CB LEU A 33 38.927 16.744 -13.735 1.00 19.89 C ANISOU 193 CB LEU A 33 2744 2149 2664 -302 182 344 C ATOM 194 CG LEU A 33 38.512 18.064 -13.039 1.00 24.74 C ANISOU 194 CG LEU A 33 3355 2762 3281 -305 142 330 C ATOM 195 CD1 LEU A 33 38.614 19.284 -13.998 1.00 20.81 C ANISOU 195 CD1 LEU A 33 2904 2236 2768 -317 124 329 C ATOM 196 CD2 LEU A 33 37.095 18.001 -12.439 1.00 19.78 C ANISOU 196 CD2 LEU A 33 2719 2140 2658 -288 108 302 C ATOM 197 N LEU A 34 37.103 14.405 -13.028 1.00 29.21 N ANISOU 197 N LEU A 34 3887 3354 3858 -266 186 318 N ATOM 198 CA LEU A 34 35.830 13.984 -12.466 1.00 27.74 C ANISOU 198 CA LEU A 34 3688 3175 3678 -249 164 294 C ATOM 199 C LEU A 34 36.009 12.772 -11.558 1.00 28.48 C ANISOU 199 C LEU A 34 3736 3298 3787 -241 189 300 C ATOM 200 O LEU A 34 35.332 12.657 -10.533 1.00 24.60 O ANISOU 200 O LEU A 34 3216 2823 3307 -232 172 285 O ATOM 201 CB LEU A 34 34.843 13.711 -13.606 1.00 24.15 C ANISOU 201 CB LEU A 34 3273 2695 3209 -239 153 279 C ATOM 202 CG LEU A 34 34.317 14.946 -14.367 1.00 26.83 C ANISOU 202 CG LEU A 34 3656 3005 3534 -243 119 266 C ATOM 203 CD1 LEU A 34 33.566 14.527 -15.638 1.00 19.71 C ANISOU 203 CD1 LEU A 34 2795 2077 2617 -234 116 257 C ATOM 204 CD2 LEU A 34 33.395 15.801 -13.512 1.00 20.33 C ANISOU 204 CD2 LEU A 34 2822 2186 2716 -237 77 243 C ATOM 205 N ASN A 35 36.931 11.867 -11.906 1.00 24.97 N ANISOU 205 N ASN A 35 3285 2858 3343 -245 229 322 N ATOM 206 CA ASN A 35 37.186 10.716 -11.047 1.00 27.90 C ANISOU 206 CA ASN A 35 3614 3258 3729 -238 254 329 C ATOM 207 C ASN A 35 37.802 11.155 -9.728 1.00 28.11 C ANISOU 207 C ASN A 35 3600 3310 3770 -245 252 335 C ATOM 208 O ASN A 35 37.476 10.602 -8.671 1.00 29.42 O ANISOU 208 O ASN A 35 3730 3499 3949 -236 251 329 O ATOM 209 CB ASN A 35 38.063 9.684 -11.764 1.00 39.45 C ANISOU 209 CB ASN A 35 5081 4720 5188 -241 297 351 C ATOM 210 CG ASN A 35 38.401 8.476 -10.881 1.00 40.12 C ANISOU 210 CG ASN A 35 5122 4833 5288 -235 324 360 C ATOM 211 OD1 ASN A 35 39.513 8.354 -10.390 1.00 39.14 O ANISOU 211 OD1 ASN A 35 4973 4726 5173 -244 348 379 O ATOM 212 ND2 ASN A 35 37.413 7.614 -10.639 1.00 30.97 N ANISOU 212 ND2 ASN A 35 3954 3681 4134 -219 320 345 N ATOM 213 N SER A 36 38.681 12.162 -9.766 1.00 26.77 N ANISOU 213 N SER A 36 3436 3136 3598 -260 250 348 N ATOM 214 CA SER A 36 39.228 12.707 -8.531 1.00 24.55 C ANISOU 214 CA SER A 36 3119 2878 3331 -267 244 352 C ATOM 215 C SER A 36 38.135 13.382 -7.699 1.00 30.05 C ANISOU 215 C SER A 36 3806 3579 4032 -259 203 328 C ATOM 216 O SER A 36 38.112 13.259 -6.467 1.00 30.25 O ANISOU 216 O SER A 36 3792 3629 4072 -255 199 325 O ATOM 217 CB SER A 36 40.347 13.699 -8.851 1.00 27.28 C ANISOU 217 CB SER A 36 3477 3215 3672 -285 250 369 C ATOM 218 OG SER A 36 41.387 13.064 -9.571 1.00 32.30 O ANISOU 218 OG SER A 36 4120 3849 4305 -293 288 392 O ATOM 219 N LEU A 37 37.229 14.114 -8.353 1.00 16.20 N ANISOU 219 N LEU A 37 2088 1801 2267 -256 172 310 N ATOM 220 CA LEU A 37 36.154 14.776 -7.624 1.00 24.96 C ANISOU 220 CA LEU A 37 3190 2913 3380 -248 132 285 C ATOM 221 C LEU A 37 35.202 13.766 -7.009 1.00 30.44 C ANISOU 221 C LEU A 37 3860 3623 4083 -231 130 270 C ATOM 222 O LEU A 37 34.674 13.980 -5.911 1.00 36.05 O ANISOU 222 O LEU A 37 4543 4350 4804 -226 110 256 O ATOM 223 CB LEU A 37 35.414 15.737 -8.555 1.00 23.45 C ANISOU 223 CB LEU A 37 3045 2692 3174 -249 101 269 C ATOM 224 CG LEU A 37 34.205 16.505 -8.043 1.00 24.78 C ANISOU 224 CG LEU A 37 3214 2857 3343 -240 56 242 C ATOM 225 CD1 LEU A 37 34.614 17.379 -6.833 1.00 16.20 C ANISOU 225 CD1 LEU A 37 2097 1789 2269 -248 42 243 C ATOM 226 CD2 LEU A 37 33.629 17.352 -9.185 1.00 17.94 C ANISOU 226 CD2 LEU A 37 2398 1958 2461 -242 31 230 C ATOM 227 N CYS A 38 34.951 12.674 -7.725 1.00 24.09 N ANISOU 227 N CYS A 38 3068 2812 3274 -223 151 271 N ATOM 228 CA CYS A 38 34.070 11.634 -7.223 1.00 24.71 C ANISOU 228 CA CYS A 38 3125 2904 3359 -207 152 257 C ATOM 229 C CYS A 38 34.667 10.940 -5.992 1.00 20.93 C ANISOU 229 C CYS A 38 2597 2458 2898 -207 173 269 C ATOM 230 O CYS A 38 33.935 10.547 -5.085 1.00 20.85 O ANISOU 230 O CYS A 38 2560 2464 2897 -196 162 254 O ATOM 231 CB CYS A 38 33.783 10.653 -8.372 1.00 36.09 C ANISOU 231 CB CYS A 38 4593 4329 4791 -200 171 259 C ATOM 232 SG CYS A 38 33.351 8.971 -7.891 1.00 68.32 S ANISOU 232 SG CYS A 38 8645 8431 8883 -185 195 256 S ATOM 233 N THR A 39 35.990 10.754 -5.950 1.00 21.31 N ANISOU 233 N THR A 39 2633 2515 2949 -218 204 295 N ATOM 234 CA THR A 39 36.606 10.203 -4.754 1.00 16.11 C ANISOU 234 CA THR A 39 1927 1887 2306 -218 222 306 C ATOM 235 C THR A 39 36.422 11.154 -3.580 1.00 30.98 C ANISOU 235 C THR A 39 3787 3785 4199 -220 194 295 C ATOM 236 O THR A 39 36.047 10.733 -2.473 1.00 34.10 O ANISOU 236 O THR A 39 4148 4203 4607 -212 190 287 O ATOM 237 CB THR A 39 38.101 9.940 -5.004 1.00 26.15 C ANISOU 237 CB THR A 39 3193 3165 3579 -230 259 335 C ATOM 238 OG1 THR A 39 38.270 8.810 -5.864 1.00 29.15 O ANISOU 238 OG1 THR A 39 3586 3537 3954 -226 290 345 O ATOM 239 CG2 THR A 39 38.835 9.679 -3.714 1.00 21.05 C ANISOU 239 CG2 THR A 39 2500 2549 2949 -232 273 346 C ATOM 240 N ALA A 40 36.621 12.455 -3.824 1.00 25.33 N ANISOU 240 N ALA A 40 3091 3055 3477 -231 172 294 N ATOM 241 CA ALA A 40 36.398 13.458 -2.788 1.00 29.13 C ANISOU 241 CA ALA A 40 3553 3547 3966 -233 142 283 C ATOM 242 C ALA A 40 34.956 13.433 -2.290 1.00 29.05 C ANISOU 242 C ALA A 40 3539 3540 3960 -219 111 255 C ATOM 243 O ALA A 40 34.702 13.619 -1.092 1.00 23.18 O ANISOU 243 O ALA A 40 2763 2817 3227 -215 97 246 O ATOM 244 CB ALA A 40 36.768 14.840 -3.318 1.00 27.45 C ANISOU 244 CB ALA A 40 3370 3317 3745 -246 124 285 C ATOM 245 N VAL A 41 33.998 13.238 -3.198 1.00 19.08 N ANISOU 245 N VAL A 41 2308 2256 2686 -210 100 239 N ATOM 246 CA VAL A 41 32.588 13.184 -2.810 1.00 22.83 C ANISOU 246 CA VAL A 41 2780 2731 3162 -196 70 211 C ATOM 247 C VAL A 41 32.303 11.965 -1.923 1.00 30.63 C ANISOU 247 C VAL A 41 3731 3744 4162 -185 86 209 C ATOM 248 O VAL A 41 31.486 12.035 -1.000 1.00 28.82 O ANISOU 248 O VAL A 41 3480 3528 3941 -177 65 190 O ATOM 249 CB VAL A 41 31.698 13.235 -4.065 1.00 17.50 C ANISOU 249 CB VAL A 41 2150 2027 2473 -190 56 197 C ATOM 250 CG1 VAL A 41 30.276 12.850 -3.759 1.00 10.34 C ANISOU 250 CG1 VAL A 41 1239 1122 1569 -174 34 169 C ATOM 251 CG2 VAL A 41 31.714 14.683 -4.651 1.00 19.49 C ANISOU 251 CG2 VAL A 41 2436 2256 2714 -200 28 192 C ATOM 252 N LYS A 42 32.928 10.822 -2.203 1.00 23.61 N ANISOU 252 N LYS A 42 2834 2862 3275 -184 124 227 N ATOM 253 CA LYS A 42 32.708 9.668 -1.334 1.00 19.16 C ANISOU 253 CA LYS A 42 2235 2323 2724 -174 140 226 C ATOM 254 C LYS A 42 33.293 9.885 0.069 1.00 21.06 C ANISOU 254 C LYS A 42 2432 2591 2978 -179 141 233 C ATOM 255 O LYS A 42 32.713 9.427 1.051 1.00 25.79 O ANISOU 255 O LYS A 42 3002 3209 3587 -170 136 221 O ATOM 256 CB LYS A 42 33.292 8.413 -1.982 1.00 19.10 C ANISOU 256 CB LYS A 42 2229 2314 2713 -173 181 244 C ATOM 257 CG LYS A 42 32.523 7.983 -3.206 1.00 29.02 C ANISOU 257 CG LYS A 42 3522 3546 3957 -165 179 234 C ATOM 258 CD LYS A 42 32.954 6.608 -3.756 1.00 29.73 C ANISOU 258 CD LYS A 42 3612 3638 4046 -161 219 249 C ATOM 259 CE LYS A 42 34.330 6.607 -4.435 1.00 20.09 C ANISOU 259 CE LYS A 42 2401 2411 2820 -174 249 277 C ATOM 260 NZ LYS A 42 34.672 5.188 -4.823 1.00 20.34 N ANISOU 260 NZ LYS A 42 2428 2448 2852 -169 287 291 N ATOM 261 N ALA A 43 34.439 10.575 0.189 1.00 26.50 N ANISOU 261 N ALA A 43 3117 3284 3669 -192 149 251 N ATOM 262 CA ALA A 43 35.008 10.855 1.509 1.00 20.43 C ANISOU 262 CA ALA A 43 2308 2541 2913 -197 149 258 C ATOM 263 C ALA A 43 34.189 11.905 2.263 1.00 27.85 C ANISOU 263 C ALA A 43 3243 3483 3857 -195 108 236 C ATOM 264 O ALA A 43 33.987 11.791 3.481 1.00 23.08 O ANISOU 264 O ALA A 43 2603 2901 3264 -191 101 229 O ATOM 265 CB ALA A 43 36.458 11.301 1.387 1.00 14.31 C ANISOU 265 CB ALA A 43 1531 1768 2139 -212 168 284 C ATOM 266 N ILE A 44 33.684 12.917 1.560 1.00 14.49 N ANISOU 266 N ILE A 44 1584 1767 2154 -198 80 223 N ATOM 267 CA ILE A 44 32.769 13.849 2.208 1.00 22.39 C ANISOU 267 CA ILE A 44 2582 2769 3158 -194 39 199 C ATOM 268 C ILE A 44 31.519 13.106 2.696 1.00 21.94 C ANISOU 268 C ILE A 44 2511 2721 3105 -179 28 177 C ATOM 269 O ILE A 44 31.111 13.248 3.855 1.00 16.45 O ANISOU 269 O ILE A 44 1786 2045 2421 -174 13 166 O ATOM 270 CB ILE A 44 32.437 15.019 1.253 1.00 10.17 C ANISOU 270 CB ILE A 44 1076 1192 1596 -200 12 190 C ATOM 271 CG1 ILE A 44 33.674 15.917 1.064 1.00 24.38 C ANISOU 271 CG1 ILE A 44 2883 2988 3394 -217 19 211 C ATOM 272 CG2 ILE A 44 31.327 15.902 1.792 1.00 10.95 C ANISOU 272 CG2 ILE A 44 1175 1289 1697 -194 -31 163 C ATOM 273 CD1 ILE A 44 33.524 16.999 -0.055 1.00 20.10 C ANISOU 273 CD1 ILE A 44 2386 2414 2837 -223 -2 206 C ATOM 274 N SER A 45 30.921 12.265 1.837 1.00 19.59 N ANISOU 274 N SER A 45 2234 2409 2800 -170 38 171 N ATOM 275 CA SER A 45 29.745 11.498 2.245 1.00 9.75 C ANISOU 275 CA SER A 45 975 1170 1558 -155 30 150 C ATOM 276 C SER A 45 30.023 10.678 3.499 1.00 23.55 C ANISOU 276 C SER A 45 2678 2950 3321 -151 48 157 C ATOM 277 O SER A 45 29.179 10.588 4.394 1.00 19.40 O ANISOU 277 O SER A 45 2131 2438 2803 -143 30 138 O ATOM 278 CB SER A 45 29.300 10.547 1.126 1.00 12.79 C ANISOU 278 CB SER A 45 1386 1539 1934 -147 45 148 C ATOM 279 OG SER A 45 28.077 9.858 1.482 1.00 11.89 O ANISOU 279 OG SER A 45 1262 1430 1824 -133 35 126 O ATOM 280 N SER A 46 31.190 10.037 3.556 1.00 29.65 N ANISOU 280 N SER A 46 3436 3734 4098 -157 83 183 N ATOM 281 CA SER A 46 31.508 9.179 4.687 1.00 19.66 C ANISOU 281 CA SER A 46 2128 2498 2845 -153 103 191 C ATOM 282 C SER A 46 31.573 9.991 5.972 1.00 22.40 C ANISOU 282 C SER A 46 2445 2863 3202 -157 82 185 C ATOM 283 O SER A 46 31.070 9.553 7.013 1.00 19.74 O ANISOU 283 O SER A 46 2078 2546 2875 -149 78 175 O ATOM 284 CB SER A 46 32.830 8.458 4.427 1.00 21.24 C ANISOU 284 CB SER A 46 2320 2704 3047 -160 144 220 C ATOM 285 OG SER A 46 33.196 7.611 5.504 1.00 33.21 O ANISOU 285 OG SER A 46 3795 4247 4574 -156 164 229 O ATOM 286 N ALA A 47 32.150 11.203 5.892 1.00 21.89 N ANISOU 286 N ALA A 47 2390 2791 3135 -169 68 191 N ATOM 287 CA ALA A 47 32.279 12.082 7.048 1.00 20.20 C ANISOU 287 CA ALA A 47 2151 2594 2931 -173 47 186 C ATOM 288 C ALA A 47 30.943 12.691 7.449 1.00 34.35 C ANISOU 288 C ALA A 47 3945 4382 4722 -165 8 156 C ATOM 289 O ALA A 47 30.631 12.776 8.646 1.00 29.59 O ANISOU 289 O ALA A 47 3312 3801 4131 -162 -5 146 O ATOM 290 CB ALA A 47 33.279 13.196 6.746 1.00 20.71 C ANISOU 290 CB ALA A 47 2227 2650 2991 -188 44 201 C ATOM 291 N VAL A 48 30.134 13.101 6.464 1.00 17.41 N ANISOU 291 N VAL A 48 1837 2212 2566 -162 -13 140 N ATOM 292 CA VAL A 48 28.832 13.684 6.763 1.00 18.61 C ANISOU 292 CA VAL A 48 1994 2360 2719 -154 -51 110 C ATOM 293 C VAL A 48 27.935 12.672 7.496 1.00 28.40 C ANISOU 293 C VAL A 48 3208 3616 3966 -141 -49 95 C ATOM 294 O VAL A 48 27.176 13.047 8.398 1.00 30.20 O ANISOU 294 O VAL A 48 3419 3855 4201 -136 -74 76 O ATOM 295 CB VAL A 48 28.181 14.190 5.455 1.00 22.89 C ANISOU 295 CB VAL A 48 2582 2869 3245 -153 -70 98 C ATOM 296 CG1 VAL A 48 26.732 14.462 5.651 1.00 13.85 C ANISOU 296 CG1 VAL A 48 1442 1719 2101 -142 -104 66 C ATOM 297 CG2 VAL A 48 28.885 15.452 4.939 1.00 20.28 C ANISOU 297 CG2 VAL A 48 2274 2522 2908 -166 -81 108 C ATOM 298 N ARG A 49 27.999 11.371 7.118 1.00 26.34 N ANISOU 298 N ARG A 49 2946 3357 3705 -135 -18 104 N ATOM 299 CA ARG A 49 27.256 10.301 7.813 1.00 22.84 C ANISOU 299 CA ARG A 49 2478 2931 3269 -123 -12 92 C ATOM 300 C ARG A 49 27.875 9.901 9.161 1.00 27.27 C ANISOU 300 C ARG A 49 2995 3523 3843 -124 4 104 C ATOM 301 O ARG A 49 27.372 8.965 9.804 1.00 23.59 O ANISOU 301 O ARG A 49 2506 3073 3385 -115 13 97 O ATOM 302 CB ARG A 49 27.141 9.033 6.939 1.00 15.97 C ANISOU 302 CB ARG A 49 1623 2053 2394 -116 16 98 C ATOM 303 CG ARG A 49 25.968 8.981 5.944 1.00 25.17 C ANISOU 303 CG ARG A 49 2821 3193 3549 -107 -1 76 C ATOM 304 CD ARG A 49 26.112 10.033 4.825 1.00 28.54 C ANISOU 304 CD ARG A 49 3289 3593 3963 -115 -18 77 C ATOM 305 NE ARG A 49 25.263 9.776 3.673 1.00 29.76 N ANISOU 305 NE ARG A 49 3478 3723 4107 -107 -25 63 N ATOM 306 CZ ARG A 49 24.053 10.298 3.486 1.00 29.10 C ANISOU 306 CZ ARG A 49 3412 3627 4020 -100 -58 35 C ATOM 307 NH1 ARG A 49 23.532 11.115 4.385 1.00 22.82 N ANISOU 307 NH1 ARG A 49 2601 2840 3231 -99 -89 18 N ATOM 308 NH2 ARG A 49 23.359 10.001 2.388 1.00 29.73 N ANISOU 308 NH2 ARG A 49 3524 3684 4090 -93 -62 24 N ATOM 309 N LYS A 50 28.954 10.566 9.581 1.00 21.81 N ANISOU 309 N LYS A 50 2291 2840 3156 -136 8 121 N ATOM 310 CA LYS A 50 29.507 10.472 10.931 1.00 23.86 C ANISOU 310 CA LYS A 50 2509 3128 3428 -138 15 130 C ATOM 311 C LYS A 50 30.217 9.144 11.181 1.00 35.96 C ANISOU 311 C LYS A 50 4020 4677 4966 -136 55 150 C ATOM 312 O LYS A 50 30.260 8.669 12.322 1.00 36.41 O ANISOU 312 O LYS A 50 4042 4759 5034 -132 62 151 O ATOM 313 CB LYS A 50 28.425 10.712 11.993 1.00 20.19 C ANISOU 313 CB LYS A 50 2024 2677 2971 -130 -13 104 C ATOM 314 CG LYS A 50 27.829 12.123 11.959 1.00 24.63 C ANISOU 314 CG LYS A 50 2602 3226 3529 -133 -54 85 C ATOM 315 CD LYS A 50 28.892 13.179 12.186 1.00 24.66 C ANISOU 315 CD LYS A 50 2603 3232 3535 -146 -58 101 C ATOM 316 CE LYS A 50 28.286 14.587 12.170 1.00 28.62 C ANISOU 316 CE LYS A 50 3120 3721 4033 -149 -99 81 C ATOM 317 NZ LYS A 50 29.320 15.633 12.426 1.00 34.93 N ANISOU 317 NZ LYS A 50 3915 4523 4834 -162 -104 96 N ATOM 318 N ALA A 51 30.809 8.553 10.139 1.00 28.20 N ANISOU 318 N ALA A 51 3057 3682 3977 -138 82 167 N ATOM 319 CA ALA A 51 31.619 7.352 10.332 1.00 30.46 C ANISOU 319 CA ALA A 51 3323 3983 4268 -137 121 189 C ATOM 320 C ALA A 51 32.787 7.651 11.256 1.00 29.43 C ANISOU 320 C ALA A 51 3163 3874 4147 -146 132 208 C ATOM 321 O ALA A 51 33.515 8.627 11.058 1.00 31.75 O ANISOU 321 O ALA A 51 3465 4162 4439 -157 125 218 O ATOM 322 CB ALA A 51 32.156 6.834 8.987 1.00 19.91 C ANISOU 322 CB ALA A 51 2015 2628 2921 -139 147 205 C ATOM 323 N GLY A 52 32.986 6.796 12.253 1.00 33.31 N ANISOU 323 N GLY A 52 3619 4390 4648 -141 149 214 N ATOM 324 CA GLY A 52 34.049 7.046 13.211 1.00 24.74 C ANISOU 324 CA GLY A 52 2503 3326 3573 -148 158 231 C ATOM 325 C GLY A 52 33.744 8.086 14.277 1.00 23.04 C ANISOU 325 C GLY A 52 2269 3122 3363 -151 127 218 C ATOM 326 O GLY A 52 34.647 8.450 15.040 1.00 26.35 O ANISOU 326 O GLY A 52 2684 3552 3775 -154 128 222 O ATOM 327 N ILE A 53 32.513 8.599 14.357 1.00 23.33 N ANISOU 327 N ILE A 53 2316 3151 3398 -145 95 191 N ATOM 328 CA ILE A 53 32.216 9.591 15.391 1.00 14.74 C ANISOU 328 CA ILE A 53 1210 2075 2316 -147 65 178 C ATOM 329 C ILE A 53 32.430 9.019 16.795 1.00 28.11 C ANISOU 329 C ILE A 53 2892 3791 3997 -138 72 167 C ATOM 330 O ILE A 53 32.763 9.769 17.723 1.00 26.90 O ANISOU 330 O ILE A 53 2735 3647 3838 -140 58 160 O ATOM 331 CB ILE A 53 30.801 10.168 15.212 1.00 23.71 C ANISOU 331 CB ILE A 53 2364 3197 3448 -141 29 147 C ATOM 332 CG1 ILE A 53 30.663 11.413 16.085 1.00 25.87 C ANISOU 332 CG1 ILE A 53 2625 3478 3726 -145 -3 136 C ATOM 333 CG2 ILE A 53 29.707 9.097 15.490 1.00 11.56 C ANISOU 333 CG2 ILE A 53 816 1664 1911 -127 31 130 C ATOM 334 CD1 ILE A 53 29.324 12.058 16.014 1.00 33.29 C ANISOU 334 CD1 ILE A 53 3579 4406 4662 -139 -40 106 C ATOM 335 N ALA A 54 32.313 7.685 16.967 1.00 28.36 N ANISOU 335 N ALA A 54 2930 3829 4018 -127 94 162 N ATOM 336 CA ALA A 54 32.577 7.073 18.275 1.00 25.79 C ANISOU 336 CA ALA A 54 2606 3520 3673 -119 100 148 C ATOM 337 C ALA A 54 33.949 7.452 18.782 1.00 29.26 C ANISOU 337 C ALA A 54 3046 3965 4107 -126 109 160 C ATOM 338 O ALA A 54 34.166 7.547 19.996 1.00 25.10 O ANISOU 338 O ALA A 54 2518 3450 3570 -122 102 146 O ATOM 339 CB ALA A 54 32.511 5.538 18.226 1.00 11.63 C ANISOU 339 CB ALA A 54 821 1729 1869 -110 124 146 C ATOM 340 N HIS A 55 34.899 7.646 17.872 1.00 22.25 N ANISOU 340 N HIS A 55 2162 3068 3224 -135 124 185 N ATOM 341 CA HIS A 55 36.231 8.005 18.315 1.00 19.68 C ANISOU 341 CA HIS A 55 1837 2747 2893 -141 133 196 C ATOM 342 C HIS A 55 36.294 9.432 18.852 1.00 25.80 C ANISOU 342 C HIS A 55 2603 3525 3674 -148 108 191 C ATOM 343 O HIS A 55 37.110 9.716 19.737 1.00 38.37 O ANISOU 343 O HIS A 55 4194 5125 5259 -149 108 189 O ATOM 344 CB HIS A 55 37.211 7.740 17.188 1.00 17.46 C ANISOU 344 CB HIS A 55 1564 2455 2614 -148 158 222 C ATOM 345 CG HIS A 55 37.504 6.283 17.004 1.00 26.85 C ANISOU 345 CG HIS A 55 2764 3645 3793 -140 183 224 C ATOM 346 ND1 HIS A 55 38.523 5.641 17.674 1.00 31.27 N ANISOU 346 ND1 HIS A 55 3329 4213 4340 -137 197 225 N ATOM 347 CD2 HIS A 55 36.877 5.329 16.272 1.00 27.68 C ANISOU 347 CD2 HIS A 55 2876 3743 3897 -135 195 225 C ATOM 348 CE1 HIS A 55 38.531 4.361 17.340 1.00 28.37 C ANISOU 348 CE1 HIS A 55 2971 3843 3965 -131 216 225 C ATOM 349 NE2 HIS A 55 37.541 4.146 16.493 1.00 26.72 N ANISOU 349 NE2 HIS A 55 2763 3626 3762 -129 216 226 N ATOM 350 N LEU A 56 35.444 10.332 18.361 1.00 21.60 N ANISOU 350 N LEU A 56 2066 2985 3154 -153 84 188 N ATOM 351 CA LEU A 56 35.408 11.684 18.908 1.00 22.61 C ANISOU 351 CA LEU A 56 2189 3116 3287 -159 57 181 C ATOM 352 C LEU A 56 34.847 11.715 20.309 1.00 22.78 C ANISOU 352 C LEU A 56 2207 3151 3297 -149 42 153 C ATOM 353 O LEU A 56 35.075 12.683 21.027 1.00 27.96 O ANISOU 353 O LEU A 56 2860 3813 3952 -152 25 146 O ATOM 354 CB LEU A 56 34.575 12.637 18.050 1.00 28.69 C ANISOU 354 CB LEU A 56 2955 3872 4073 -168 30 182 C ATOM 355 CG LEU A 56 35.190 13.232 16.783 1.00 40.47 C ANISOU 355 CG LEU A 56 4450 5348 5580 -184 34 209 C ATOM 356 CD1 LEU A 56 34.147 14.035 16.020 1.00 45.60 C ANISOU 356 CD1 LEU A 56 5124 5975 6226 -185 3 191 C ATOM 357 CD2 LEU A 56 36.384 14.106 17.131 1.00 35.84 C ANISOU 357 CD2 LEU A 56 3862 4766 4991 -195 36 221 C ATOM 358 N TYR A 57 34.069 10.715 20.692 1.00 21.26 N ANISOU 358 N TYR A 57 2016 2964 3097 -137 46 137 N ATOM 359 CA TYR A 57 33.471 10.688 22.011 1.00 22.39 C ANISOU 359 CA TYR A 57 2159 3121 3228 -128 34 109 C ATOM 360 C TYR A 57 34.167 9.698 22.964 1.00 15.74 C ANISOU 360 C TYR A 57 1319 2287 2373 -122 55 105 C ATOM 361 O TYR A 57 33.605 9.346 23.999 1.00 23.97 O ANISOU 361 O TYR A 57 2363 3340 3406 -114 49 82 O ATOM 362 CB TYR A 57 31.983 10.398 21.853 1.00 27.49 C ANISOU 362 CB TYR A 57 2804 3766 3874 -121 19 90 C ATOM 363 CG TYR A 57 31.265 11.614 21.332 1.00 31.23 C ANISOU 363 CG TYR A 57 3275 4231 4359 -126 -11 87 C ATOM 364 CD1 TYR A 57 31.339 11.966 19.988 1.00 29.60 C ANISOU 364 CD1 TYR A 57 3068 4007 4170 -135 -14 106 C ATOM 365 CD2 TYR A 57 30.535 12.428 22.178 1.00 25.07 C ANISOU 365 CD2 TYR A 57 2495 3460 3572 -123 -38 64 C ATOM 366 CE1 TYR A 57 30.688 13.089 19.503 1.00 24.53 C ANISOU 366 CE1 TYR A 57 2426 3353 3540 -141 -46 100 C ATOM 367 CE2 TYR A 57 29.888 13.558 21.708 1.00 20.86 C ANISOU 367 CE2 TYR A 57 1963 2916 3048 -128 -68 59 C ATOM 368 CZ TYR A 57 29.957 13.889 20.367 1.00 27.43 C ANISOU 368 CZ TYR A 57 2795 3727 3899 -137 -74 76 C ATOM 369 OH TYR A 57 29.297 15.031 19.904 1.00 26.75 O ANISOU 369 OH TYR A 57 2713 3627 3824 -142 -109 67 O ATOM 370 N GLY A 58 35.397 9.291 22.662 1.00 22.15 N ANISOU 370 N GLY A 58 2135 3097 3184 -126 77 125 N ATOM 371 CA GLY A 58 36.222 8.586 23.625 1.00 30.58 C ANISOU 371 CA GLY A 58 3206 4171 4241 -122 92 121 C ATOM 372 C GLY A 58 36.110 7.077 23.689 1.00 34.23 C ANISOU 372 C GLY A 58 3676 4635 4696 -115 111 117 C ATOM 373 O GLY A 58 36.349 6.510 24.758 1.00 36.95 O ANISOU 373 O GLY A 58 4021 4985 5031 -109 115 104 O ATOM 374 N ILE A 59 35.781 6.397 22.580 1.00 36.28 N ANISOU 374 N ILE A 59 3939 4887 4957 -114 123 128 N ATOM 375 CA ILE A 59 35.631 4.937 22.625 1.00 29.31 C ANISOU 375 CA ILE A 59 3064 4006 4066 -106 140 124 C ATOM 376 C ILE A 59 36.964 4.255 22.914 1.00 27.29 C ANISOU 376 C ILE A 59 2814 3750 3803 -107 159 134 C ATOM 377 O ILE A 59 36.999 3.151 23.474 1.00 22.51 O ANISOU 377 O ILE A 59 2215 3149 3189 -101 168 125 O ATOM 378 CB ILE A 59 35.024 4.389 21.322 1.00 31.29 C ANISOU 378 CB ILE A 59 3318 4247 4322 -105 148 133 C ATOM 379 CG1 ILE A 59 34.585 2.944 21.530 1.00 29.16 C ANISOU 379 CG1 ILE A 59 3056 3980 4042 -96 160 123 C ATOM 380 CG2 ILE A 59 36.047 4.441 20.165 1.00 21.26 C ANISOU 380 CG2 ILE A 59 2054 2968 3058 -113 166 161 C ATOM 381 CD1 ILE A 59 34.086 2.289 20.273 1.00 34.06 C ANISOU 381 CD1 ILE A 59 3682 4592 4667 -94 172 133 C ATOM 382 N ALA A 60 38.078 4.880 22.543 1.00 22.03 N ANISOU 382 N ALA A 60 2148 3081 3141 -115 165 153 N ATOM 383 CA ALA A 60 39.389 4.357 22.885 1.00 23.83 C ANISOU 383 CA ALA A 60 2380 3310 3362 -116 181 162 C ATOM 384 C ALA A 60 40.025 5.152 24.016 1.00 33.65 C ANISOU 384 C ALA A 60 3619 4561 4607 -118 171 155 C ATOM 385 O ALA A 60 41.249 5.110 24.189 1.00 40.33 O ANISOU 385 O ALA A 60 4467 5408 5450 -121 181 165 O ATOM 386 CB ALA A 60 40.294 4.342 21.653 1.00 15.46 C ANISOU 386 CB ALA A 60 1326 2242 2306 -122 198 187 C ATOM 387 N GLY A 61 39.207 5.869 24.788 1.00 39.42 N ANISOU 387 N GLY A 61 4342 5296 5339 -116 151 137 N ATOM 388 CA GLY A 61 39.672 6.726 25.864 1.00 48.27 C ANISOU 388 CA GLY A 61 5458 6423 6460 -118 139 129 C ATOM 389 C GLY A 61 40.056 8.122 25.395 1.00 53.46 C ANISOU 389 C GLY A 61 6109 7078 7126 -127 129 142 C ATOM 390 O GLY A 61 40.123 9.059 26.194 1.00 56.15 O ANISOU 390 O GLY A 61 6444 7423 7469 -129 114 133 O ATOM 391 N VAL A 70 37.793 16.627 15.157 1.00 93.67 N ANISOU 391 N VAL A 70 11231 12048 12311 -229 18 249 N ATOM 392 CA VAL A 70 39.079 17.168 14.738 1.00 91.70 C ANISOU 392 CA VAL A 70 10989 11794 12060 -243 33 271 C ATOM 393 C VAL A 70 38.859 18.504 14.030 1.00 91.72 C ANISOU 393 C VAL A 70 11024 11772 12054 -252 5 262 C ATOM 394 O VAL A 70 39.008 19.571 14.632 1.00 96.43 O ANISOU 394 O VAL A 70 11613 12374 12654 -258 -17 258 O ATOM 395 CB VAL A 70 39.842 16.177 13.827 1.00 87.87 C ANISOU 395 CB VAL A 70 10514 11302 11570 -245 71 292 C ATOM 396 CG1 VAL A 70 41.352 16.333 14.002 1.00 86.54 C ANISOU 396 CG1 VAL A 70 10330 11143 11407 -257 95 318 C ATOM 397 CG2 VAL A 70 39.403 14.745 14.095 1.00 83.36 C ANISOU 397 CG2 VAL A 70 9927 10744 11003 -232 91 290 C ATOM 398 N LYS A 71 38.498 18.432 12.749 1.00 81.75 N ANISOU 398 N LYS A 71 9799 10484 10778 -251 6 259 N ATOM 399 CA LYS A 71 38.211 19.597 11.923 1.00 67.30 C ANISOU 399 CA LYS A 71 8005 8628 8937 -258 -19 250 C ATOM 400 C LYS A 71 36.710 19.767 11.712 1.00 52.58 C ANISOU 400 C LYS A 71 6159 6750 7067 -247 -50 222 C ATOM 401 O LYS A 71 35.940 18.802 11.724 1.00 49.85 O ANISOU 401 O LYS A 71 5810 6408 6722 -235 -45 212 O ATOM 402 CB LYS A 71 38.890 19.490 10.556 1.00 63.48 C ANISOU 402 CB LYS A 71 7554 8122 8442 -266 2 267 C ATOM 403 CG LYS A 71 40.251 20.140 10.472 1.00 64.05 C ANISOU 403 CG LYS A 71 7625 8195 8516 -282 16 289 C ATOM 404 CD LYS A 71 40.636 20.328 9.013 1.00 68.39 C ANISOU 404 CD LYS A 71 8216 8718 9053 -290 27 299 C ATOM 405 CE LYS A 71 42.060 19.895 8.738 1.00 69.16 C ANISOU 405 CE LYS A 71 8305 8820 9152 -300 65 327 C ATOM 406 NZ LYS A 71 42.156 19.254 7.396 1.00 69.98 N ANISOU 406 NZ LYS A 71 8440 8904 9244 -300 87 336 N ATOM 407 N LYS A 72 36.302 21.016 11.525 1.00 34.91 N ANISOU 407 N LYS A 72 3942 4498 4825 -251 -83 209 N ATOM 408 CA LYS A 72 34.953 21.286 11.062 1.00 38.95 C ANISOU 408 CA LYS A 72 4479 4992 5329 -242 -113 183 C ATOM 409 C LYS A 72 34.742 20.684 9.677 1.00 41.46 C ANISOU 409 C LYS A 72 4832 5287 5634 -240 -98 186 C ATOM 410 O LYS A 72 35.680 20.503 8.892 1.00 30.95 O ANISOU 410 O LYS A 72 3515 3946 4297 -248 -72 207 O ATOM 411 CB LYS A 72 34.674 22.787 11.026 1.00 44.04 C ANISOU 411 CB LYS A 72 5141 5624 5970 -249 -150 170 C ATOM 412 CG LYS A 72 34.247 23.344 12.357 1.00 57.85 C ANISOU 412 CG LYS A 72 6860 7392 7729 -246 -175 156 C ATOM 413 CD LYS A 72 33.419 22.326 13.138 1.00 59.01 C ANISOU 413 CD LYS A 72 6979 7557 7883 -232 -173 142 C ATOM 414 CE LYS A 72 33.151 22.792 14.554 1.00 54.50 C ANISOU 414 CE LYS A 72 6375 7009 7325 -230 -194 131 C ATOM 415 NZ LYS A 72 32.509 21.714 15.341 1.00 63.90 N ANISOU 415 NZ LYS A 72 7537 8220 8523 -217 -186 121 N ATOM 416 N LEU A 73 33.482 20.351 9.411 1.00 41.16 N ANISOU 416 N LEU A 73 4807 5239 5591 -227 -114 164 N ATOM 417 CA LEU A 73 33.109 19.585 8.233 1.00 32.84 C ANISOU 417 CA LEU A 73 3783 4167 4528 -221 -100 163 C ATOM 418 C LEU A 73 33.286 20.406 6.963 1.00 36.46 C ANISOU 418 C LEU A 73 4286 4596 4972 -230 -109 166 C ATOM 419 O LEU A 73 33.691 19.874 5.931 1.00 32.04 O ANISOU 419 O LEU A 73 3748 4022 4404 -232 -85 180 O ATOM 420 CB LEU A 73 31.671 19.117 8.388 1.00 22.58 C ANISOU 420 CB LEU A 73 2484 2867 3228 -206 -119 137 C ATOM 421 CG LEU A 73 31.379 17.664 8.069 1.00 35.25 C ANISOU 421 CG LEU A 73 4086 4475 4833 -196 -92 139 C ATOM 422 CD1 LEU A 73 32.515 16.794 8.588 1.00 38.98 C ANISOU 422 CD1 LEU A 73 4527 4969 5314 -200 -54 164 C ATOM 423 CD2 LEU A 73 30.105 17.279 8.770 1.00 26.45 C ANISOU 423 CD2 LEU A 73 2955 3370 3723 -182 -111 114 C ATOM 424 N ASP A 74 32.995 21.708 7.016 1.00 39.11 N ANISOU 424 N ASP A 74 4635 4921 5305 -235 -142 154 N ATOM 425 CA ASP A 74 33.186 22.532 5.826 1.00 34.66 C ANISOU 425 CA ASP A 74 4114 4328 4727 -243 -151 158 C ATOM 426 C ASP A 74 34.658 22.805 5.546 1.00 34.57 C ANISOU 426 C ASP A 74 4104 4317 4716 -259 -126 186 C ATOM 427 O ASP A 74 35.045 22.916 4.376 1.00 38.15 O ANISOU 427 O ASP A 74 4591 4748 5157 -266 -116 196 O ATOM 428 CB ASP A 74 32.409 23.839 5.963 1.00 48.48 C ANISOU 428 CB ASP A 74 5879 6067 6475 -244 -195 136 C ATOM 429 CG ASP A 74 32.776 24.616 7.212 1.00 62.47 C ANISOU 429 CG ASP A 74 7618 7858 8258 -249 -210 136 C ATOM 430 OD1 ASP A 74 33.589 24.132 8.035 1.00 65.69 O ANISOU 430 OD1 ASP A 74 7992 8291 8677 -253 -187 151 O ATOM 431 OD2 ASP A 74 32.214 25.715 7.380 1.00 66.12 O ANISOU 431 OD2 ASP A 74 8091 8312 8718 -250 -245 119 O ATOM 432 N VAL A 75 35.493 22.896 6.585 1.00 25.83 N ANISOU 432 N VAL A 75 2961 3234 3621 -265 -116 198 N ATOM 433 CA VAL A 75 36.939 23.003 6.372 1.00 28.97 C ANISOU 433 CA VAL A 75 3355 3633 4018 -280 -88 226 C ATOM 434 C VAL A 75 37.473 21.702 5.763 1.00 26.81 C ANISOU 434 C VAL A 75 3083 3361 3743 -278 -47 244 C ATOM 435 O VAL A 75 38.257 21.727 4.808 1.00 20.18 O ANISOU 435 O VAL A 75 2266 2506 2895 -287 -28 261 O ATOM 436 CB VAL A 75 37.679 23.324 7.698 1.00 33.39 C ANISOU 436 CB VAL A 75 3874 4220 4593 -286 -87 234 C ATOM 437 CG1 VAL A 75 39.207 23.294 7.508 1.00 26.86 C ANISOU 437 CG1 VAL A 75 3040 3397 3767 -300 -55 263 C ATOM 438 CG2 VAL A 75 37.233 24.638 8.333 1.00 30.39 C ANISOU 438 CG2 VAL A 75 3492 3840 4216 -289 -126 218 C ATOM 439 N LEU A 76 37.057 20.545 6.313 1.00 19.21 N ANISOU 439 N LEU A 76 2095 2416 2788 -266 -34 240 N ATOM 440 CA LEU A 76 37.544 19.253 5.815 1.00 26.32 C ANISOU 440 CA LEU A 76 2993 3319 3687 -263 5 256 C ATOM 441 C LEU A 76 37.092 19.012 4.381 1.00 27.35 C ANISOU 441 C LEU A 76 3167 3422 3803 -260 7 253 C ATOM 442 O LEU A 76 37.867 18.517 3.555 1.00 29.15 O ANISOU 442 O LEU A 76 3409 3642 4025 -266 37 272 O ATOM 443 CB LEU A 76 37.074 18.097 6.717 1.00 31.56 C ANISOU 443 CB LEU A 76 3622 4007 4361 -250 15 250 C ATOM 444 CG LEU A 76 37.458 16.664 6.273 1.00 28.12 C ANISOU 444 CG LEU A 76 3183 3575 3925 -245 54 266 C ATOM 445 CD1 LEU A 76 38.952 16.419 6.469 1.00 18.13 C ANISOU 445 CD1 LEU A 76 1899 2324 2667 -256 87 294 C ATOM 446 CD2 LEU A 76 36.655 15.566 6.959 1.00 20.86 C ANISOU 446 CD2 LEU A 76 2239 2673 3014 -230 58 254 C ATOM 447 N SER A 77 35.834 19.340 4.075 1.00 29.12 N ANISOU 447 N SER A 77 3412 3630 4020 -252 -23 228 N ATOM 448 CA SER A 77 35.342 19.207 2.709 1.00 34.03 C ANISOU 448 CA SER A 77 4078 4224 4627 -249 -24 223 C ATOM 449 C SER A 77 36.153 20.073 1.753 1.00 34.84 C ANISOU 449 C SER A 77 4212 4305 4719 -264 -21 237 C ATOM 450 O SER A 77 36.569 19.600 0.685 1.00 37.28 O ANISOU 450 O SER A 77 4546 4600 5019 -267 2 250 O ATOM 451 CB SER A 77 33.869 19.589 2.643 1.00 24.68 C ANISOU 451 CB SER A 77 2910 3028 3439 -238 -62 193 C ATOM 452 OG SER A 77 33.096 18.743 3.478 1.00 24.34 O ANISOU 452 OG SER A 77 2838 3004 3405 -224 -63 180 O ATOM 453 N ASN A 78 36.432 21.328 2.146 1.00 13.74 N ANISOU 453 N ASN A 78 1540 1633 2049 -273 -44 236 N ATOM 454 CA ASN A 78 37.244 22.197 1.302 1.00 19.98 C ANISOU 454 CA ASN A 78 2359 2403 2829 -288 -41 250 C ATOM 455 C ASN A 78 38.627 21.608 1.093 1.00 31.26 C ANISOU 455 C ASN A 78 3777 3839 4260 -298 1 279 C ATOM 456 O ASN A 78 39.150 21.618 -0.029 1.00 39.20 O ANISOU 456 O ASN A 78 4813 4826 5254 -306 17 291 O ATOM 457 CB ASN A 78 37.349 23.612 1.887 1.00 13.83 C ANISOU 457 CB ASN A 78 1577 1624 2052 -297 -71 244 C ATOM 458 CG ASN A 78 37.884 24.612 0.860 1.00 23.20 C ANISOU 458 CG ASN A 78 2803 2785 3227 -311 -76 252 C ATOM 459 OD1 ASN A 78 37.393 24.660 -0.263 1.00 23.98 O ANISOU 459 OD1 ASN A 78 2941 2859 3312 -309 -82 246 O ATOM 460 ND2 ASN A 78 38.869 25.407 1.239 1.00 20.27 N ANISOU 460 ND2 ASN A 78 2422 2420 2860 -325 -74 266 N ATOM 461 N ASP A 79 39.218 21.054 2.157 1.00 26.91 N ANISOU 461 N ASP A 79 3184 3318 3724 -298 19 289 N ATOM 462 CA ASP A 79 40.530 20.421 2.053 1.00 18.49 C ANISOU 462 CA ASP A 79 2103 2261 2660 -307 59 316 C ATOM 463 C ASP A 79 40.491 19.184 1.134 1.00 27.84 C ANISOU 463 C ASP A 79 3303 3438 3839 -300 89 323 C ATOM 464 O ASP A 79 41.441 18.931 0.375 1.00 27.35 O ANISOU 464 O ASP A 79 3252 3367 3771 -309 117 343 O ATOM 465 CB ASP A 79 41.007 20.008 3.451 1.00 32.06 C ANISOU 465 CB ASP A 79 3772 4014 4397 -305 70 322 C ATOM 466 CG ASP A 79 41.342 21.206 4.370 1.00 42.89 C ANISOU 466 CG ASP A 79 5125 5395 5775 -314 48 321 C ATOM 467 OD1 ASP A 79 41.341 22.389 3.932 1.00 40.59 O ANISOU 467 OD1 ASP A 79 4860 5085 5477 -323 26 316 O ATOM 468 OD2 ASP A 79 41.626 20.939 5.554 1.00 38.92 O ANISOU 468 OD2 ASP A 79 4582 4918 5286 -311 52 324 O ATOM 469 N LEU A 80 39.408 18.395 1.201 1.00 19.08 N ANISOU 469 N LEU A 80 2190 2329 2729 -285 82 307 N ATOM 470 CA LEU A 80 39.286 17.195 0.376 1.00 21.07 C ANISOU 470 CA LEU A 80 2456 2574 2975 -277 109 312 C ATOM 471 C LEU A 80 39.158 17.550 -1.104 1.00 32.98 C ANISOU 471 C LEU A 80 4013 4050 4466 -282 106 312 C ATOM 472 O LEU A 80 39.839 16.963 -1.954 1.00 28.99 O ANISOU 472 O LEU A 80 3522 3537 3955 -286 137 329 O ATOM 473 CB LEU A 80 38.081 16.353 0.821 1.00 13.05 C ANISOU 473 CB LEU A 80 1427 1568 1964 -260 99 293 C ATOM 474 CG LEU A 80 38.153 15.480 2.075 1.00 20.17 C ANISOU 474 CG LEU A 80 2282 2500 2881 -252 113 295 C ATOM 475 CD1 LEU A 80 36.778 15.095 2.531 1.00 20.17 C ANISOU 475 CD1 LEU A 80 2274 2505 2883 -237 91 270 C ATOM 476 CD2 LEU A 80 38.969 14.222 1.816 1.00 22.26 C ANISOU 476 CD2 LEU A 80 2536 2775 3148 -252 156 316 C ATOM 477 N VAL A 81 38.265 18.490 -1.426 1.00 32.94 N ANISOU 477 N VAL A 81 4035 4027 4453 -280 70 292 N ATOM 478 CA VAL A 81 38.049 18.896 -2.814 1.00 23.21 C ANISOU 478 CA VAL A 81 2853 2763 3205 -284 64 290 C ATOM 479 C VAL A 81 39.292 19.565 -3.384 1.00 26.26 C ANISOU 479 C VAL A 81 3254 3139 3585 -302 79 312 C ATOM 480 O VAL A 81 39.716 19.261 -4.508 1.00 27.82 O ANISOU 480 O VAL A 81 3480 3320 3772 -307 100 324 O ATOM 481 CB VAL A 81 36.827 19.823 -2.914 1.00 20.73 C ANISOU 481 CB VAL A 81 2560 2432 2883 -278 20 264 C ATOM 482 CG1 VAL A 81 36.626 20.272 -4.364 1.00 17.71 C ANISOU 482 CG1 VAL A 81 2230 2017 2483 -282 13 262 C ATOM 483 CG2 VAL A 81 35.591 19.123 -2.370 1.00 17.64 C ANISOU 483 CG2 VAL A 81 2154 2051 2498 -260 6 242 C ATOM 484 N MET A 82 39.876 20.508 -2.625 1.00 23.33 N ANISOU 484 N MET A 82 2865 2778 3220 -312 68 317 N ATOM 485 CA MET A 82 41.072 21.202 -3.085 1.00 22.73 C ANISOU 485 CA MET A 82 2802 2694 3140 -330 82 336 C ATOM 486 C MET A 82 42.184 20.213 -3.370 1.00 30.23 C ANISOU 486 C MET A 82 3740 3653 4093 -335 127 361 C ATOM 487 O MET A 82 42.875 20.323 -4.391 1.00 35.76 O ANISOU 487 O MET A 82 4467 4335 4783 -345 145 376 O ATOM 488 CB MET A 82 41.547 22.245 -2.052 1.00 13.85 C ANISOU 488 CB MET A 82 1653 1583 2025 -339 65 338 C ATOM 489 CG MET A 82 40.797 23.532 -2.080 1.00 21.35 C ANISOU 489 CG MET A 82 2626 2518 2970 -340 23 319 C ATOM 490 SD MET A 82 41.192 24.587 -3.510 1.00 33.29 S ANISOU 490 SD MET A 82 4192 3995 4464 -355 17 326 S ATOM 491 CE MET A 82 40.775 26.176 -2.799 1.00 37.95 C ANISOU 491 CE MET A 82 4782 4582 5056 -360 -28 309 C ATOM 492 N ASN A 83 42.382 19.253 -2.463 1.00 26.46 N ANISOU 492 N ASN A 83 3222 3202 3629 -328 146 366 N ATOM 493 CA ASN A 83 43.540 18.374 -2.571 1.00 29.32 C ANISOU 493 CA ASN A 83 3568 3576 3996 -333 188 390 C ATOM 494 C ASN A 83 43.392 17.367 -3.711 1.00 30.16 C ANISOU 494 C ASN A 83 3700 3668 4092 -328 212 395 C ATOM 495 O ASN A 83 44.391 17.030 -4.369 1.00 26.05 O ANISOU 495 O ASN A 83 3186 3143 3568 -337 243 415 O ATOM 496 CB ASN A 83 43.795 17.649 -1.248 1.00 24.90 C ANISOU 496 CB ASN A 83 2958 3050 3454 -327 201 394 C ATOM 497 CG ASN A 83 45.058 16.836 -1.294 1.00 36.62 C ANISOU 497 CG ASN A 83 4424 4547 4943 -333 243 420 C ATOM 498 OD1 ASN A 83 45.019 15.612 -1.308 1.00 46.44 O ANISOU 498 OD1 ASN A 83 5655 5799 6190 -324 267 424 O ATOM 499 ND2 ASN A 83 46.199 17.519 -1.377 1.00 43.74 N ANISOU 499 ND2 ASN A 83 5326 5448 5846 -349 254 436 N ATOM 500 N MET A 84 42.174 16.822 -3.918 1.00 17.71 N ANISOU 500 N MET A 84 2133 2084 2511 -313 199 377 N ATOM 501 CA MET A 84 41.991 15.853 -4.994 1.00 19.83 C ANISOU 501 CA MET A 84 2426 2339 2770 -307 220 380 C ATOM 502 C MET A 84 42.081 16.521 -6.366 1.00 23.38 C ANISOU 502 C MET A 84 2925 2757 3203 -316 216 383 C ATOM 503 O MET A 84 42.660 15.943 -7.290 1.00 26.31 O ANISOU 503 O MET A 84 3312 3117 3566 -320 245 397 O ATOM 504 CB MET A 84 40.662 15.097 -4.850 1.00 17.89 C ANISOU 504 CB MET A 84 2177 2094 2525 -288 207 359 C ATOM 505 CG MET A 84 40.597 14.095 -3.676 1.00 27.83 C ANISOU 505 CG MET A 84 3390 3384 3799 -278 220 359 C ATOM 506 SD MET A 84 41.941 12.871 -3.619 1.00 30.27 S ANISOU 506 SD MET A 84 3674 3712 4117 -282 271 388 S ATOM 507 CE MET A 84 41.754 11.926 -5.154 1.00 19.79 C ANISOU 507 CE MET A 84 2384 2361 2775 -277 295 393 C ATOM 508 N LEU A 85 41.609 17.771 -6.486 1.00 26.09 N ANISOU 508 N LEU A 85 3289 3084 3539 -320 181 369 N ATOM 509 CA LEU A 85 41.677 18.483 -7.760 1.00 22.78 C ANISOU 509 CA LEU A 85 2918 2635 3103 -329 175 371 C ATOM 510 C LEU A 85 43.117 18.860 -8.093 1.00 26.91 C ANISOU 510 C LEU A 85 3445 3156 3625 -347 201 396 C ATOM 511 O LEU A 85 43.586 18.649 -9.218 1.00 31.74 O ANISOU 511 O LEU A 85 4085 3749 4224 -354 222 408 O ATOM 512 CB LEU A 85 40.786 19.728 -7.712 1.00 23.38 C ANISOU 512 CB LEU A 85 3015 2695 3173 -328 130 350 C ATOM 513 CG LEU A 85 39.271 19.501 -7.770 1.00 26.95 C ANISOU 513 CG LEU A 85 3478 3139 3621 -311 102 324 C ATOM 514 CD1 LEU A 85 38.555 20.814 -7.724 1.00 27.20 C ANISOU 514 CD1 LEU A 85 3531 3157 3648 -312 59 305 C ATOM 515 CD2 LEU A 85 38.807 18.669 -9.005 1.00 24.90 C ANISOU 515 CD2 LEU A 85 3251 2860 3349 -304 116 322 C ATOM 516 N LYS A 86 43.841 19.418 -7.129 1.00 31.84 N ANISOU 516 N LYS A 86 4039 3799 4261 -356 200 404 N ATOM 517 CA LYS A 86 45.253 19.695 -7.361 1.00 32.07 C ANISOU 517 CA LYS A 86 4066 3829 4290 -373 226 427 C ATOM 518 C LYS A 86 45.989 18.446 -7.845 1.00 30.49 C ANISOU 518 C LYS A 86 3859 3634 4090 -373 270 446 C ATOM 519 O LYS A 86 46.714 18.492 -8.846 1.00 28.61 O ANISOU 519 O LYS A 86 3647 3381 3843 -384 291 461 O ATOM 520 CB LYS A 86 45.891 20.244 -6.087 1.00 23.21 C ANISOU 520 CB LYS A 86 2905 2731 3183 -380 222 433 C ATOM 521 CG LYS A 86 45.466 21.662 -5.769 1.00 31.67 C ANISOU 521 CG LYS A 86 3987 3795 4253 -385 182 419 C ATOM 522 CD LYS A 86 46.029 22.101 -4.424 1.00 37.14 C ANISOU 522 CD LYS A 86 4637 4513 4962 -390 178 423 C ATOM 523 CE LYS A 86 45.657 23.525 -4.100 1.00 44.61 C ANISOU 523 CE LYS A 86 5593 5450 5905 -396 139 410 C ATOM 524 NZ LYS A 86 46.171 23.949 -2.759 1.00 47.57 N ANISOU 524 NZ LYS A 86 5926 5851 6296 -400 134 413 N ATOM 525 N SER A 87 45.783 17.308 -7.165 1.00 21.70 N ANISOU 525 N SER A 87 2713 2543 2988 -361 284 445 N ATOM 526 CA SER A 87 46.478 16.064 -7.483 1.00 30.03 C ANISOU 526 CA SER A 87 3758 3607 4046 -359 325 463 C ATOM 527 C SER A 87 45.931 15.363 -8.739 1.00 26.83 C ANISOU 527 C SER A 87 3388 3179 3626 -352 335 459 C ATOM 528 O SER A 87 46.492 14.349 -9.157 1.00 28.87 O ANISOU 528 O SER A 87 3642 3441 3884 -352 370 474 O ATOM 529 CB SER A 87 46.430 15.114 -6.263 1.00 25.94 C ANISOU 529 CB SER A 87 3192 3120 3545 -348 336 462 C ATOM 530 OG SER A 87 45.109 14.655 -6.019 1.00 24.33 O ANISOU 530 OG SER A 87 2987 2917 3341 -331 315 442 O ATOM 531 N SER A 88 44.887 15.888 -9.374 1.00 28.03 N ANISOU 531 N SER A 88 3576 3308 3766 -347 306 441 N ATOM 532 CA SER A 88 44.425 15.342 -10.648 1.00 23.78 C ANISOU 532 CA SER A 88 3074 2747 3213 -342 314 439 C ATOM 533 C SER A 88 45.303 15.747 -11.820 1.00 25.48 C ANISOU 533 C SER A 88 3324 2941 3415 -358 332 455 C ATOM 534 O SER A 88 45.274 15.076 -12.849 1.00 29.21 O ANISOU 534 O SER A 88 3822 3399 3878 -355 351 460 O ATOM 535 CB SER A 88 43.003 15.811 -10.931 1.00 23.56 C ANISOU 535 CB SER A 88 3074 2701 3176 -332 276 413 C ATOM 536 OG SER A 88 43.016 17.204 -11.235 1.00 23.42 O ANISOU 536 OG SER A 88 3083 2665 3150 -343 250 409 O ATOM 537 N PHE A 89 46.105 16.805 -11.679 1.00 33.60 N ANISOU 537 N PHE A 89 4354 3968 4444 -374 328 464 N ATOM 538 CA PHE A 89 46.891 17.352 -12.787 1.00 41.94 C ANISOU 538 CA PHE A 89 5445 5002 5487 -389 342 478 C ATOM 539 C PHE A 89 46.004 17.855 -13.928 1.00 42.52 C ANISOU 539 C PHE A 89 5570 5043 5542 -387 319 465 C ATOM 540 O PHE A 89 46.430 17.904 -15.082 1.00 51.40 O ANISOU 540 O PHE A 89 6729 6147 6653 -396 335 475 O ATOM 541 CB PHE A 89 47.934 16.345 -13.296 1.00 44.48 C ANISOU 541 CB PHE A 89 5761 5329 5810 -394 388 501 C ATOM 542 CG PHE A 89 49.120 16.184 -12.381 1.00 58.22 C ANISOU 542 CG PHE A 89 7459 7096 7566 -403 411 518 C ATOM 543 CD1 PHE A 89 48.957 16.048 -11.008 1.00 72.39 C ANISOU 543 CD1 PHE A 89 9210 8918 9377 -395 402 512 C ATOM 544 CD2 PHE A 89 50.404 16.192 -12.891 1.00 57.14 C ANISOU 544 CD2 PHE A 89 7327 6958 7428 -418 443 540 C ATOM 545 CE1 PHE A 89 50.054 15.919 -10.160 1.00 73.66 C ANISOU 545 CE1 PHE A 89 9332 9103 9553 -403 422 528 C ATOM 546 CE2 PHE A 89 51.505 16.059 -12.053 1.00 64.83 C ANISOU 546 CE2 PHE A 89 8260 7955 8416 -426 464 556 C ATOM 547 CZ PHE A 89 51.328 15.922 -10.684 1.00 70.78 C ANISOU 547 CZ PHE A 89 8972 8737 9187 -418 454 550 C ATOM 548 N ALA A 90 44.770 18.251 -13.616 1.00 27.65 N ANISOU 548 N ALA A 90 3693 3155 3657 -376 281 441 N ATOM 549 CA ALA A 90 43.817 18.662 -14.633 1.00 21.37 C ANISOU 549 CA ALA A 90 2944 2329 2845 -371 258 426 C ATOM 550 C ALA A 90 43.307 20.093 -14.480 1.00 25.85 C ANISOU 550 C ALA A 90 3530 2884 3408 -376 216 412 C ATOM 551 O ALA A 90 42.440 20.511 -15.256 1.00 27.16 O ANISOU 551 O ALA A 90 3734 3025 3560 -371 192 397 O ATOM 552 CB ALA A 90 42.624 17.697 -14.638 1.00 13.59 C ANISOU 552 CB ALA A 90 1958 1346 1861 -351 250 409 C ATOM 553 N THR A 91 43.784 20.851 -13.496 1.00 29.00 N ANISOU 553 N THR A 91 3902 3299 3818 -384 206 414 N ATOM 554 CA THR A 91 43.216 22.165 -13.206 1.00 31.02 C ANISOU 554 CA THR A 91 4171 3545 4071 -386 165 399 C ATOM 555 C THR A 91 44.329 23.206 -13.111 1.00 31.11 C ANISOU 555 C THR A 91 4183 3555 4083 -406 169 414 C ATOM 556 O THR A 91 45.512 22.866 -12.947 1.00 26.54 O ANISOU 556 O THR A 91 3584 2990 3510 -417 202 435 O ATOM 557 CB THR A 91 42.368 22.131 -11.894 1.00 37.13 C ANISOU 557 CB THR A 91 4907 4340 4858 -373 139 380 C ATOM 558 OG1 THR A 91 43.212 21.960 -10.742 1.00 32.62 O ANISOU 558 OG1 THR A 91 4290 3800 4305 -378 155 393 O ATOM 559 CG2 THR A 91 41.341 20.966 -11.929 1.00 22.20 C ANISOU 559 CG2 THR A 91 3011 2453 2969 -353 140 367 C ATOM 560 N CYS A 92 43.950 24.490 -13.217 1.00 21.12 N ANISOU 560 N CYS A 92 2941 2273 2810 -412 135 403 N ATOM 561 CA CYS A 92 44.947 25.546 -13.062 1.00 25.31 C ANISOU 561 CA CYS A 92 3472 2803 3342 -431 136 416 C ATOM 562 C CYS A 92 44.484 26.664 -12.142 1.00 26.30 C ANISOU 562 C CYS A 92 3586 2934 3474 -431 97 401 C ATOM 563 O CYS A 92 45.319 27.375 -11.571 1.00 36.92 O ANISOU 563 O CYS A 92 4914 4288 4825 -444 99 411 O ATOM 564 CB CYS A 92 45.352 26.160 -14.414 1.00 32.11 C ANISOU 564 CB CYS A 92 4383 3632 4184 -444 141 424 C ATOM 565 SG CYS A 92 44.001 26.836 -15.373 1.00 32.78 S ANISOU 565 SG CYS A 92 4522 3683 4250 -436 101 401 S ATOM 566 N VAL A 93 43.173 26.883 -12.050 1.00 26.99 N ANISOU 566 N VAL A 93 3685 3013 3558 -417 62 377 N ATOM 567 CA VAL A 93 42.602 27.921 -11.187 1.00 22.70 C ANISOU 567 CA VAL A 93 3131 2473 3019 -415 22 360 C ATOM 568 C VAL A 93 41.407 27.321 -10.463 1.00 25.17 C ANISOU 568 C VAL A 93 3422 2800 3341 -395 3 339 C ATOM 569 O VAL A 93 40.567 26.666 -11.088 1.00 36.47 O ANISOU 569 O VAL A 93 4873 4221 4765 -383 1 328 O ATOM 570 CB VAL A 93 42.166 29.184 -11.969 1.00 26.02 C ANISOU 570 CB VAL A 93 3599 2863 3424 -421 -9 350 C ATOM 571 CG1 VAL A 93 41.506 30.209 -11.033 1.00 24.84 C ANISOU 571 CG1 VAL A 93 3437 2718 3281 -418 -51 331 C ATOM 572 CG2 VAL A 93 43.336 29.805 -12.721 1.00 20.29 C ANISOU 572 CG2 VAL A 93 2898 2123 2690 -442 9 371 C ATOM 573 N LEU A 94 41.329 27.538 -9.152 1.00 28.05 N ANISOU 573 N LEU A 94 3746 3189 3721 -392 -10 333 N ATOM 574 CA LEU A 94 40.262 26.996 -8.312 1.00 30.28 C ANISOU 574 CA LEU A 94 4003 3488 4014 -374 -28 313 C ATOM 575 C LEU A 94 39.655 28.129 -7.489 1.00 29.88 C ANISOU 575 C LEU A 94 3946 3441 3968 -373 -69 295 C ATOM 576 O LEU A 94 40.383 28.898 -6.854 1.00 23.11 O ANISOU 576 O LEU A 94 3070 2592 3117 -385 -72 303 O ATOM 577 CB LEU A 94 40.788 25.875 -7.401 1.00 33.55 C ANISOU 577 CB LEU A 94 4369 3935 4445 -370 3 324 C ATOM 578 CG LEU A 94 41.518 24.674 -8.032 1.00 33.01 C ANISOU 578 CG LEU A 94 4299 3868 4373 -371 47 344 C ATOM 579 CD1 LEU A 94 42.218 23.848 -6.936 1.00 25.73 C ANISOU 579 CD1 LEU A 94 3327 2980 3470 -370 74 357 C ATOM 580 CD2 LEU A 94 40.592 23.771 -8.909 1.00 15.24 C ANISOU 580 CD2 LEU A 94 2074 1603 2113 -357 50 334 C ATOM 581 N VAL A 95 38.343 28.305 -7.587 1.00 31.47 N ANISOU 581 N VAL A 95 4163 3631 4165 -360 -102 270 N ATOM 582 CA VAL A 95 37.618 29.284 -6.788 1.00 25.56 C ANISOU 582 CA VAL A 95 3406 2885 3422 -356 -143 250 C ATOM 583 C VAL A 95 36.657 28.533 -5.876 1.00 33.08 C ANISOU 583 C VAL A 95 4326 3858 4386 -338 -153 232 C ATOM 584 O VAL A 95 35.895 27.669 -6.341 1.00 29.61 O ANISOU 584 O VAL A 95 3896 3413 3941 -325 -150 223 O ATOM 585 CB VAL A 95 36.878 30.308 -7.668 1.00 22.95 C ANISOU 585 CB VAL A 95 3124 2523 3075 -356 -177 235 C ATOM 586 CG1 VAL A 95 35.865 31.102 -6.858 1.00 23.88 C ANISOU 586 CG1 VAL A 95 3231 2643 3197 -348 -221 210 C ATOM 587 CG2 VAL A 95 37.881 31.237 -8.337 1.00 19.05 C ANISOU 587 CG2 VAL A 95 2657 2011 2571 -376 -171 252 C ATOM 588 N SER A 96 36.703 28.856 -4.578 1.00 31.52 N ANISOU 588 N SER A 96 4089 3684 4202 -338 -165 228 N ATOM 589 CA SER A 96 35.891 28.201 -3.559 1.00 27.58 C ANISOU 589 CA SER A 96 3555 3208 3716 -323 -174 212 C ATOM 590 C SER A 96 35.188 29.242 -2.697 1.00 27.84 C ANISOU 590 C SER A 96 3578 3245 3755 -320 -215 191 C ATOM 591 O SER A 96 35.732 30.305 -2.390 1.00 34.33 O ANISOU 591 O SER A 96 4399 4066 4578 -332 -228 196 O ATOM 592 CB SER A 96 36.736 27.256 -2.658 1.00 26.63 C ANISOU 592 CB SER A 96 3388 3119 3611 -324 -139 229 C ATOM 593 OG SER A 96 35.978 26.769 -1.551 1.00 32.50 O ANISOU 593 OG SER A 96 4096 3885 4367 -311 -151 214 O ATOM 594 N GLU A 97 33.975 28.901 -2.281 1.00 28.17 N ANISOU 594 N GLU A 97 3610 3291 3800 -304 -237 168 N ATOM 595 CA GLU A 97 33.222 29.738 -1.356 1.00 28.22 C ANISOU 595 CA GLU A 97 3602 3305 3813 -299 -275 147 C ATOM 596 C GLU A 97 34.056 30.092 -0.130 1.00 33.74 C ANISOU 596 C GLU A 97 4261 4031 4527 -308 -270 158 C ATOM 597 O GLU A 97 33.879 31.170 0.452 1.00 32.48 O ANISOU 597 O GLU A 97 4098 3873 4372 -311 -299 147 O ATOM 598 CB GLU A 97 31.934 28.979 -0.980 1.00 37.58 C ANISOU 598 CB GLU A 97 4776 4499 5004 -280 -288 123 C ATOM 599 CG GLU A 97 30.662 29.790 -0.647 1.00 50.17 C ANISOU 599 CG GLU A 97 6378 6087 6598 -271 -335 93 C ATOM 600 CD GLU A 97 30.176 29.662 0.782 1.00 62.36 C ANISOU 600 CD GLU A 97 7877 7658 8158 -263 -348 79 C ATOM 601 OE1 GLU A 97 30.823 28.967 1.596 1.00 59.58 O ANISOU 601 OE1 GLU A 97 7487 7333 7818 -264 -322 93 O ATOM 602 OE2 GLU A 97 29.107 30.242 1.073 1.00 67.57 O ANISOU 602 OE2 GLU A 97 8541 8313 8818 -254 -385 54 O ATOM 603 N GLU A 98 35.011 29.227 0.233 1.00 28.25 N ANISOU 603 N GLU A 98 3538 3357 3841 -312 -232 179 N ATOM 604 CA GLU A 98 35.773 29.334 1.471 1.00 32.08 C ANISOU 604 CA GLU A 98 3980 3870 4341 -318 -223 189 C ATOM 605 C GLU A 98 37.007 30.217 1.385 1.00 28.25 C ANISOU 605 C GLU A 98 3498 3381 3854 -337 -215 209 C ATOM 606 O GLU A 98 37.560 30.558 2.432 1.00 26.49 O ANISOU 606 O GLU A 98 3243 3180 3644 -342 -216 215 O ATOM 607 CB GLU A 98 36.215 27.939 1.933 1.00 28.64 C ANISOU 607 CB GLU A 98 3509 3458 3915 -313 -187 203 C ATOM 608 CG GLU A 98 35.039 27.043 2.117 1.00 49.92 C ANISOU 608 CG GLU A 98 6197 6159 6613 -295 -193 184 C ATOM 609 CD GLU A 98 34.071 27.627 3.111 1.00 62.70 C ANISOU 609 CD GLU A 98 7798 7787 8239 -287 -230 159 C ATOM 610 OE1 GLU A 98 34.529 28.041 4.203 1.00 62.77 O ANISOU 610 OE1 GLU A 98 7774 7816 8259 -292 -234 163 O ATOM 611 OE2 GLU A 98 32.870 27.724 2.770 1.00 59.64 O ANISOU 611 OE2 GLU A 98 7430 7386 7846 -276 -256 136 O ATOM 612 N ASP A 99 37.436 30.617 0.193 1.00 22.74 N ANISOU 612 N ASP A 99 2839 2657 3142 -347 -209 219 N ATOM 613 CA ASP A 99 38.695 31.332 0.023 1.00 34.29 C ANISOU 613 CA ASP A 99 4308 4117 4605 -365 -196 240 C ATOM 614 C ASP A 99 38.445 32.692 -0.618 1.00 35.60 C ANISOU 614 C ASP A 99 4513 4256 4759 -373 -227 232 C ATOM 615 O ASP A 99 37.697 32.791 -1.597 1.00 46.37 O ANISOU 615 O ASP A 99 5915 5594 6108 -368 -241 220 O ATOM 616 CB ASP A 99 39.670 30.504 -0.816 1.00 48.20 C ANISOU 616 CB ASP A 99 6078 5874 6360 -372 -153 264 C ATOM 617 CG ASP A 99 40.232 29.312 -0.056 1.00 57.55 C ANISOU 617 CG ASP A 99 7220 7089 7559 -368 -119 278 C ATOM 618 OD1 ASP A 99 41.062 29.540 0.851 1.00 61.87 O ANISOU 618 OD1 ASP A 99 7734 7656 8118 -376 -111 289 O ATOM 619 OD2 ASP A 99 39.854 28.156 -0.364 1.00 50.19 O ANISOU 619 OD2 ASP A 99 6286 6158 6625 -358 -102 277 O ATOM 620 N LYS A 100 39.060 33.740 -0.054 1.00 34.43 N ANISOU 620 N LYS A 100 4355 4112 4615 -385 -238 237 N ATOM 621 CA LYS A 100 38.852 35.104 -0.552 1.00 29.72 C ANISOU 621 CA LYS A 100 3793 3491 4008 -393 -269 228 C ATOM 622 C LYS A 100 39.370 35.277 -1.976 1.00 35.71 C ANISOU 622 C LYS A 100 4597 4222 4750 -404 -254 242 C ATOM 623 O LYS A 100 38.766 35.989 -2.778 1.00 22.96 O ANISOU 623 O LYS A 100 3023 2580 3122 -404 -279 231 O ATOM 624 CB LYS A 100 39.534 36.116 0.369 1.00 40.22 C ANISOU 624 CB LYS A 100 5101 4835 5348 -405 -280 234 C ATOM 625 CG LYS A 100 39.520 37.568 -0.144 1.00 39.44 C ANISOU 625 CG LYS A 100 5038 4711 5238 -416 -308 229 C ATOM 626 CD LYS A 100 38.123 38.125 -0.312 1.00 43.41 C ANISOU 626 CD LYS A 100 5564 5197 5734 -404 -351 201 C ATOM 627 CE LYS A 100 38.185 39.491 -0.977 1.00 46.99 C ANISOU 627 CE LYS A 100 6057 5622 6175 -415 -376 198 C ATOM 628 NZ LYS A 100 36.843 40.088 -1.247 1.00 47.49 N ANISOU 628 NZ LYS A 100 6148 5667 6231 -404 -418 171 N ATOM 629 N HIS A 101 40.518 34.689 -2.288 1.00 44.78 N ANISOU 629 N HIS A 101 5739 5376 5899 -414 -214 267 N ATOM 630 CA HIS A 101 41.115 34.806 -3.604 1.00 41.41 C ANISOU 630 CA HIS A 101 5353 4924 5458 -425 -196 282 C ATOM 631 C HIS A 101 41.152 33.451 -4.293 1.00 41.90 C ANISOU 631 C HIS A 101 5419 4985 5515 -418 -163 290 C ATOM 632 O HIS A 101 41.113 32.398 -3.643 1.00 33.15 O ANISOU 632 O HIS A 101 4277 3901 4419 -409 -145 292 O ATOM 633 CB HIS A 101 42.532 35.369 -3.508 1.00 41.81 C ANISOU 633 CB HIS A 101 5396 4979 5512 -445 -176 304 C ATOM 634 CG HIS A 101 42.593 36.701 -2.844 1.00 50.43 C ANISOU 634 CG HIS A 101 6482 6071 6607 -453 -206 298 C ATOM 635 ND1 HIS A 101 42.234 37.867 -3.486 1.00 50.18 N ANISOU 635 ND1 HIS A 101 6490 6012 6562 -459 -235 289 N ATOM 636 CD2 HIS A 101 42.969 37.055 -1.592 1.00 52.24 C ANISOU 636 CD2 HIS A 101 6671 6325 6852 -456 -212 299 C ATOM 637 CE1 HIS A 101 42.386 38.883 -2.656 1.00 50.45 C ANISOU 637 CE1 HIS A 101 6510 6055 6604 -465 -257 284 C ATOM 638 NE2 HIS A 101 42.832 38.418 -1.501 1.00 48.88 N ANISOU 638 NE2 HIS A 101 6263 5888 6423 -464 -244 290 N ATOM 639 N ALA A 102 41.218 33.506 -5.629 1.00 37.92 N ANISOU 639 N ALA A 102 4960 4454 4995 -423 -156 296 N ATOM 640 CA ALA A 102 41.370 32.303 -6.437 1.00 34.58 C ANISOU 640 CA ALA A 102 4547 4026 4566 -419 -123 306 C ATOM 641 C ALA A 102 42.689 31.628 -6.105 1.00 38.34 C ANISOU 641 C ALA A 102 4992 4524 5053 -428 -80 331 C ATOM 642 O ALA A 102 43.696 32.298 -5.856 1.00 30.75 O ANISOU 642 O ALA A 102 4022 3566 4095 -444 -73 345 O ATOM 643 CB ALA A 102 41.321 32.647 -7.931 1.00 22.21 C ANISOU 643 CB ALA A 102 3035 2425 2980 -425 -123 308 C ATOM 644 N ILE A 103 42.688 30.292 -6.138 1.00 39.56 N ANISOU 644 N ILE A 103 5130 4690 5211 -419 -53 337 N ATOM 645 CA ILE A 103 43.888 29.497 -5.895 1.00 30.18 C ANISOU 645 CA ILE A 103 3914 3522 4032 -426 -10 360 C ATOM 646 C ILE A 103 44.516 29.187 -7.244 1.00 32.99 C ANISOU 646 C ILE A 103 4305 3857 4374 -435 18 377 C ATOM 647 O ILE A 103 43.854 28.649 -8.139 1.00 38.72 O ANISOU 647 O ILE A 103 5058 4566 5088 -426 19 370 O ATOM 648 CB ILE A 103 43.546 28.196 -5.141 1.00 29.87 C ANISOU 648 CB ILE A 103 3836 3509 4006 -411 4 357 C ATOM 649 CG1 ILE A 103 43.032 28.505 -3.739 1.00 34.68 C ANISOU 649 CG1 ILE A 103 4408 4140 4629 -403 -21 343 C ATOM 650 CG2 ILE A 103 44.736 27.247 -5.117 1.00 29.53 C ANISOU 650 CG2 ILE A 103 3770 3481 3969 -417 50 382 C ATOM 651 CD1 ILE A 103 43.998 29.231 -2.864 1.00 39.38 C ANISOU 651 CD1 ILE A 103 4976 4752 5235 -416 -20 354 C ATOM 652 N ILE A 104 45.795 29.502 -7.390 1.00 29.50 N ANISOU 652 N ILE A 104 3860 3416 3933 -452 41 398 N ATOM 653 CA ILE A 104 46.510 29.263 -8.634 1.00 30.77 C ANISOU 653 CA ILE A 104 4052 3558 4081 -462 70 415 C ATOM 654 C ILE A 104 47.390 28.039 -8.425 1.00 34.41 C ANISOU 654 C ILE A 104 4482 4041 4552 -463 114 434 C ATOM 655 O ILE A 104 48.307 28.066 -7.593 1.00 31.05 O ANISOU 655 O ILE A 104 4021 3637 4140 -470 129 446 O ATOM 656 CB ILE A 104 47.329 30.498 -9.054 1.00 31.59 C ANISOU 656 CB ILE A 104 4179 3647 4178 -483 67 425 C ATOM 657 CG1 ILE A 104 46.452 31.751 -8.993 1.00 30.96 C ANISOU 657 CG1 ILE A 104 4121 3549 4091 -482 21 405 C ATOM 658 CG2 ILE A 104 47.850 30.353 -10.481 1.00 30.34 C ANISOU 658 CG2 ILE A 104 4062 3464 4004 -493 91 439 C ATOM 659 CD1 ILE A 104 45.235 31.678 -9.887 1.00 26.32 C ANISOU 659 CD1 ILE A 104 3575 2938 3489 -470 -1 388 C ATOM 660 N VAL A 105 47.117 26.975 -9.199 1.00 32.36 N ANISOU 660 N VAL A 105 4236 3773 4285 -454 134 436 N ATOM 661 CA VAL A 105 47.824 25.700 -9.060 1.00 23.97 C ANISOU 661 CA VAL A 105 3146 2730 3231 -452 174 452 C ATOM 662 C VAL A 105 49.283 25.858 -9.476 1.00 33.31 C ANISOU 662 C VAL A 105 4331 3913 4414 -471 207 476 C ATOM 663 O VAL A 105 49.599 26.487 -10.497 1.00 42.58 O ANISOU 663 O VAL A 105 5543 5061 5573 -483 208 482 O ATOM 664 CB VAL A 105 47.098 24.614 -9.884 1.00 26.50 C ANISOU 664 CB VAL A 105 3487 3040 3543 -438 185 446 C ATOM 665 CG1 VAL A 105 47.830 23.240 -9.896 1.00 19.95 C ANISOU 665 CG1 VAL A 105 2633 2227 2720 -436 228 464 C ATOM 666 CG2 VAL A 105 45.671 24.408 -9.378 1.00 21.49 C ANISOU 666 CG2 VAL A 105 2845 2408 2910 -419 153 422 C ATOM 667 N GLU A 106 50.183 25.262 -8.697 1.00 35.51 N ANISOU 667 N GLU A 106 4567 4217 4707 -473 234 491 N ATOM 668 CA GLU A 106 51.607 25.365 -8.972 1.00 37.79 C ANISOU 668 CA GLU A 106 4853 4508 4997 -491 266 514 C ATOM 669 C GLU A 106 51.957 24.682 -10.296 1.00 43.50 C ANISOU 669 C GLU A 106 5607 5214 5708 -494 296 526 C ATOM 670 O GLU A 106 51.271 23.751 -10.726 1.00 50.92 O ANISOU 670 O GLU A 106 6556 6150 6643 -481 302 520 O ATOM 671 CB GLU A 106 52.424 24.729 -7.857 1.00 45.51 C ANISOU 671 CB GLU A 106 5778 5520 5995 -491 289 526 C ATOM 672 CG GLU A 106 52.156 23.268 -7.649 1.00 53.85 C ANISOU 672 CG GLU A 106 6812 6592 7057 -475 309 527 C ATOM 673 CD GLU A 106 52.968 22.722 -6.496 1.00 66.70 C ANISOU 673 CD GLU A 106 8388 8252 8704 -475 330 538 C ATOM 674 OE1 GLU A 106 53.689 23.521 -5.862 1.00 72.91 O ANISOU 674 OE1 GLU A 106 9156 9048 9498 -487 326 544 O ATOM 675 OE2 GLU A 106 52.904 21.505 -6.230 1.00 68.44 O ANISOU 675 OE2 GLU A 106 8586 8488 8931 -463 350 541 O ATOM 676 N PRO A 107 53.028 25.129 -10.958 1.00 40.13 N ANISOU 676 N PRO A 107 5196 4776 5274 -512 316 543 N ATOM 677 CA PRO A 107 53.269 24.697 -12.347 1.00 41.52 C ANISOU 677 CA PRO A 107 5411 4930 5436 -517 340 552 C ATOM 678 C PRO A 107 53.394 23.192 -12.523 1.00 47.48 C ANISOU 678 C PRO A 107 6150 5696 6194 -506 373 560 C ATOM 679 O PRO A 107 52.841 22.642 -13.483 1.00 43.26 O ANISOU 679 O PRO A 107 5646 5144 5647 -499 378 556 O ATOM 680 CB PRO A 107 54.584 25.404 -12.700 1.00 40.40 C ANISOU 680 CB PRO A 107 5276 4782 5291 -539 359 571 C ATOM 681 CG PRO A 107 54.666 26.561 -11.772 1.00 41.71 C ANISOU 681 CG PRO A 107 5426 4957 5466 -546 332 565 C ATOM 682 CD PRO A 107 54.032 26.105 -10.500 1.00 36.01 C ANISOU 682 CD PRO A 107 4662 4261 4759 -530 317 554 C ATOM 683 N GLU A 108 54.072 22.499 -11.604 1.00 55.21 N ANISOU 683 N GLU A 108 7083 6705 7191 -505 395 570 N ATOM 684 CA GLU A 108 54.321 21.070 -11.775 1.00 55.05 C ANISOU 684 CA GLU A 108 7047 6695 7174 -496 429 580 C ATOM 685 C GLU A 108 53.039 20.246 -11.745 1.00 47.47 C ANISOU 685 C GLU A 108 6089 5735 6212 -475 416 563 C ATOM 686 O GLU A 108 53.083 19.050 -12.040 1.00 36.20 O ANISOU 686 O GLU A 108 4655 4313 4785 -467 442 569 O ATOM 687 CB GLU A 108 55.265 20.558 -10.671 1.00 60.77 C ANISOU 687 CB GLU A 108 7719 7452 7918 -498 452 593 C ATOM 688 CG GLU A 108 56.678 21.177 -10.645 1.00 70.38 C ANISOU 688 CG GLU A 108 8928 8673 9138 -518 471 611 C ATOM 689 CD GLU A 108 56.754 22.511 -9.859 1.00 77.18 C ANISOU 689 CD GLU A 108 9780 9538 10006 -527 442 605 C ATOM 690 OE1 GLU A 108 55.716 22.971 -9.325 1.00 75.57 O ANISOU 690 OE1 GLU A 108 9576 9335 9803 -518 407 587 O ATOM 691 OE2 GLU A 108 57.858 23.104 -9.781 1.00 77.36 O ANISOU 691 OE2 GLU A 108 9797 9565 10033 -544 455 618 O ATOM 692 N LYS A 109 51.904 20.839 -11.382 1.00 47.42 N ANISOU 692 N LYS A 109 6090 5724 6204 -466 377 542 N ATOM 693 CA LYS A 109 50.654 20.099 -11.322 1.00 45.81 C ANISOU 693 CA LYS A 109 5886 5519 5998 -447 363 525 C ATOM 694 C LYS A 109 49.540 20.713 -12.160 1.00 41.36 C ANISOU 694 C LYS A 109 5370 4927 5419 -442 331 508 C ATOM 695 O LYS A 109 48.402 20.237 -12.072 1.00 43.02 O ANISOU 695 O LYS A 109 5581 5136 5627 -426 314 491 O ATOM 696 CB LYS A 109 50.210 19.968 -9.861 1.00 58.92 C ANISOU 696 CB LYS A 109 7503 7208 7676 -436 345 515 C ATOM 697 CG LYS A 109 51.196 19.209 -8.994 1.00 58.56 C ANISOU 697 CG LYS A 109 7410 7191 7647 -437 376 531 C ATOM 698 CD LYS A 109 50.686 19.061 -7.582 1.00 57.46 C ANISOU 698 CD LYS A 109 7230 7079 7524 -425 358 520 C ATOM 699 CE LYS A 109 51.680 18.290 -6.720 1.00 56.51 C ANISOU 699 CE LYS A 109 7064 6988 7420 -426 389 536 C ATOM 700 NZ LYS A 109 51.326 18.368 -5.269 1.00 61.45 N ANISOU 700 NZ LYS A 109 7649 7639 8060 -418 370 526 N ATOM 701 N ARG A 110 49.830 21.727 -12.989 1.00 39.68 N ANISOU 701 N ARG A 110 5193 4690 5192 -456 323 511 N ATOM 702 CA ARG A 110 48.791 22.463 -13.711 1.00 31.43 C ANISOU 702 CA ARG A 110 4193 3618 4132 -453 290 493 C ATOM 703 C ARG A 110 48.201 21.694 -14.886 1.00 33.66 C ANISOU 703 C ARG A 110 4509 3880 4400 -444 299 490 C ATOM 704 O ARG A 110 48.907 21.038 -15.650 1.00 36.09 O ANISOU 704 O ARG A 110 4827 4183 4703 -450 333 506 O ATOM 705 CB ARG A 110 49.320 23.784 -14.265 1.00 37.49 C ANISOU 705 CB ARG A 110 4991 4365 4889 -471 280 499 C ATOM 706 CG ARG A 110 49.292 24.914 -13.319 1.00 46.63 C ANISOU 706 CG ARG A 110 6132 5530 6055 -477 251 491 C ATOM 707 CD ARG A 110 49.850 26.153 -13.954 1.00 41.72 C ANISOU 707 CD ARG A 110 5544 4887 5422 -495 243 498 C ATOM 708 NE ARG A 110 50.264 27.059 -12.904 1.00 39.66 N ANISOU 708 NE ARG A 110 5256 4642 5173 -504 228 498 N ATOM 709 CZ ARG A 110 50.910 28.191 -13.108 1.00 43.38 C ANISOU 709 CZ ARG A 110 5742 5101 5638 -521 222 505 C ATOM 710 NH1 ARG A 110 51.216 28.556 -14.344 1.00 46.81 N ANISOU 710 NH1 ARG A 110 6221 5509 6057 -532 231 512 N ATOM 711 NH2 ARG A 110 51.253 28.948 -12.071 1.00 39.26 N ANISOU 711 NH2 ARG A 110 5193 4596 5130 -527 209 505 N ATOM 712 N GLY A 111 46.894 21.831 -15.048 1.00 39.93 N ANISOU 712 N GLY A 111 5323 4662 5188 -431 267 468 N ATOM 713 CA GLY A 111 46.169 21.342 -16.203 1.00 29.39 C ANISOU 713 CA GLY A 111 4026 3303 3837 -422 267 461 C ATOM 714 C GLY A 111 45.350 22.498 -16.735 1.00 32.89 C ANISOU 714 C GLY A 111 4510 3720 4266 -423 228 444 C ATOM 715 O GLY A 111 45.579 23.644 -16.323 1.00 35.07 O ANISOU 715 O GLY A 111 4787 3995 4545 -433 208 443 O ATOM 716 N LYS A 112 44.388 22.232 -17.617 1.00 29.81 N ANISOU 716 N LYS A 112 4155 3309 3863 -413 216 431 N ATOM 717 CA LYS A 112 43.772 23.281 -18.418 1.00 39.06 C ANISOU 717 CA LYS A 112 5374 4449 5018 -416 185 419 C ATOM 718 C LYS A 112 42.398 23.733 -17.929 1.00 43.27 C ANISOU 718 C LYS A 112 5909 4980 5553 -401 141 392 C ATOM 719 O LYS A 112 41.780 24.584 -18.583 1.00 38.04 O ANISOU 719 O LYS A 112 5285 4292 4876 -402 112 380 O ATOM 720 CB LYS A 112 43.682 22.817 -19.867 1.00 46.15 C ANISOU 720 CB LYS A 112 6315 5321 5898 -415 201 423 C ATOM 721 CG LYS A 112 42.780 21.628 -20.062 1.00 52.40 C ANISOU 721 CG LYS A 112 7105 6115 6690 -396 204 412 C ATOM 722 CD LYS A 112 42.998 20.977 -21.419 1.00 54.71 C ANISOU 722 CD LYS A 112 7432 6388 6967 -398 230 422 C ATOM 723 CE LYS A 112 42.063 19.793 -21.594 1.00 61.93 C ANISOU 723 CE LYS A 112 8344 7304 7882 -378 233 410 C ATOM 724 NZ LYS A 112 42.449 18.909 -22.725 1.00 66.80 N ANISOU 724 NZ LYS A 112 8984 7909 8488 -379 266 423 N ATOM 725 N TYR A 113 41.919 23.235 -16.787 1.00 36.37 N ANISOU 725 N TYR A 113 4994 4132 4695 -389 133 382 N ATOM 726 CA TYR A 113 40.552 23.521 -16.368 1.00 35.37 C ANISOU 726 CA TYR A 113 4868 4003 4569 -374 93 355 C ATOM 727 C TYR A 113 40.487 24.443 -15.153 1.00 35.35 C ANISOU 727 C TYR A 113 4837 4016 4578 -377 66 347 C ATOM 728 O TYR A 113 41.353 24.426 -14.270 1.00 22.98 O ANISOU 728 O TYR A 113 3234 2473 3026 -384 82 360 O ATOM 729 CB TYR A 113 39.782 22.228 -16.061 1.00 29.79 C ANISOU 729 CB TYR A 113 4139 3310 3869 -355 100 345 C ATOM 730 CG TYR A 113 39.429 21.411 -17.289 1.00 33.01 C ANISOU 730 CG TYR A 113 4580 3699 4264 -348 115 345 C ATOM 731 CD1 TYR A 113 38.361 21.769 -18.107 1.00 30.84 C ANISOU 731 CD1 TYR A 113 4347 3398 3975 -340 87 327 C ATOM 732 CD2 TYR A 113 40.182 20.295 -17.640 1.00 36.63 C ANISOU 732 CD2 TYR A 113 5029 4165 4724 -350 157 364 C ATOM 733 CE1 TYR A 113 38.045 21.016 -19.240 1.00 33.04 C ANISOU 733 CE1 TYR A 113 4656 3658 4241 -334 100 327 C ATOM 734 CE2 TYR A 113 39.885 19.550 -18.754 1.00 41.26 C ANISOU 734 CE2 TYR A 113 5646 4734 5298 -344 171 364 C ATOM 735 CZ TYR A 113 38.825 19.910 -19.559 1.00 37.87 C ANISOU 735 CZ TYR A 113 5257 4279 4855 -336 143 346 C ATOM 736 OH TYR A 113 38.553 19.145 -20.672 1.00 36.08 O ANISOU 736 OH TYR A 113 5059 4035 4615 -330 158 347 O ATOM 737 N VAL A 114 39.406 25.221 -15.116 1.00 31.25 N ANISOU 737 N VAL A 114 4336 3483 4054 -369 25 325 N ATOM 738 CA VAL A 114 39.071 26.109 -14.014 1.00 25.31 C ANISOU 738 CA VAL A 114 3561 2743 3312 -369 -7 312 C ATOM 739 C VAL A 114 37.825 25.532 -13.356 1.00 30.77 C ANISOU 739 C VAL A 114 4232 3446 4011 -349 -28 289 C ATOM 740 O VAL A 114 36.859 25.189 -14.045 1.00 41.04 O ANISOU 740 O VAL A 114 5560 4731 5303 -337 -40 274 O ATOM 741 CB VAL A 114 38.824 27.552 -14.505 1.00 28.72 C ANISOU 741 CB VAL A 114 4032 3149 3731 -377 -41 303 C ATOM 742 CG1 VAL A 114 38.602 28.507 -13.334 1.00 23.73 C ANISOU 742 CG1 VAL A 114 3375 2531 3111 -378 -72 292 C ATOM 743 CG2 VAL A 114 39.963 28.052 -15.430 1.00 26.42 C ANISOU 743 CG2 VAL A 114 3770 2840 3428 -396 -20 325 C ATOM 744 N VAL A 115 37.845 25.415 -12.030 1.00 28.35 N ANISOU 744 N VAL A 115 3880 3168 3722 -345 -31 286 N ATOM 745 CA VAL A 115 36.738 24.824 -11.283 1.00 30.80 C ANISOU 745 CA VAL A 115 4166 3493 4042 -327 -48 265 C ATOM 746 C VAL A 115 36.297 25.827 -10.227 1.00 29.63 C ANISOU 746 C VAL A 115 3999 3355 3903 -326 -84 250 C ATOM 747 O VAL A 115 37.130 26.360 -9.486 1.00 28.25 O ANISOU 747 O VAL A 115 3801 3196 3738 -338 -80 261 O ATOM 748 CB VAL A 115 37.124 23.467 -10.644 1.00 30.46 C ANISOU 748 CB VAL A 115 4081 3478 4013 -321 -13 276 C ATOM 749 CG1 VAL A 115 35.906 22.756 -10.112 1.00 21.49 C ANISOU 749 CG1 VAL A 115 2928 2353 2883 -302 -28 254 C ATOM 750 CG2 VAL A 115 37.841 22.564 -11.657 1.00 29.24 C ANISOU 750 CG2 VAL A 115 3944 3316 3851 -325 27 296 C ATOM 751 N CYS A 116 35.002 26.133 -10.208 1.00 32.49 N ANISOU 751 N CYS A 116 4374 3708 4262 -314 -120 224 N ATOM 752 CA CYS A 116 34.368 26.927 -9.164 1.00 21.23 C ANISOU 752 CA CYS A 116 2929 2292 2845 -309 -156 205 C ATOM 753 C CYS A 116 33.478 26.016 -8.347 1.00 22.36 C ANISOU 753 C CYS A 116 3039 2455 3000 -292 -160 189 C ATOM 754 O CYS A 116 32.658 25.286 -8.920 1.00 20.01 O ANISOU 754 O CYS A 116 2757 2149 2697 -280 -160 178 O ATOM 755 CB CYS A 116 33.532 28.074 -9.754 1.00 33.70 C ANISOU 755 CB CYS A 116 4549 3844 4412 -308 -197 186 C ATOM 756 SG CYS A 116 34.418 29.199 -10.882 1.00 33.78 S ANISOU 756 SG CYS A 116 4606 3824 4405 -328 -196 202 S ATOM 757 N PHE A 117 33.637 26.035 -7.020 1.00 21.96 N ANISOU 757 N PHE A 117 2945 2434 2967 -292 -162 188 N ATOM 758 CA PHE A 117 32.829 25.104 -6.243 1.00 22.25 C ANISOU 758 CA PHE A 117 2950 2490 3014 -276 -164 174 C ATOM 759 C PHE A 117 32.480 25.670 -4.872 1.00 30.06 C ANISOU 759 C PHE A 117 3904 3500 4017 -273 -189 160 C ATOM 760 O PHE A 117 33.158 26.556 -4.339 1.00 30.67 O ANISOU 760 O PHE A 117 3970 3583 4098 -285 -196 168 O ATOM 761 CB PHE A 117 33.499 23.720 -6.067 1.00 17.13 C ANISOU 761 CB PHE A 117 2275 1862 2374 -274 -120 192 C ATOM 762 CG PHE A 117 34.813 23.753 -5.349 1.00 18.83 C ANISOU 762 CG PHE A 117 2457 2097 2598 -287 -95 216 C ATOM 763 CD1 PHE A 117 35.974 24.110 -6.008 1.00 25.50 C ANISOU 763 CD1 PHE A 117 3319 2932 3437 -303 -74 238 C ATOM 764 CD2 PHE A 117 34.873 23.469 -3.989 1.00 23.73 C ANISOU 764 CD2 PHE A 117 3031 2749 3236 -283 -94 214 C ATOM 765 CE1 PHE A 117 37.196 24.152 -5.338 1.00 28.30 C ANISOU 765 CE1 PHE A 117 3644 3307 3801 -315 -51 259 C ATOM 766 CE2 PHE A 117 36.074 23.519 -3.307 1.00 25.04 C ANISOU 766 CE2 PHE A 117 3168 2935 3413 -295 -72 235 C ATOM 767 CZ PHE A 117 37.248 23.861 -3.985 1.00 30.45 C ANISOU 767 CZ PHE A 117 3870 3610 4091 -311 -51 258 C ATOM 768 N ASP A 118 31.387 25.131 -4.325 1.00 22.82 N ANISOU 768 N ASP A 118 2970 2593 3107 -257 -204 139 N ATOM 769 CA ASP A 118 30.987 25.274 -2.935 1.00 30.21 C ANISOU 769 CA ASP A 118 3866 3554 4058 -252 -221 127 C ATOM 770 C ASP A 118 31.118 23.897 -2.281 1.00 27.43 C ANISOU 770 C ASP A 118 3476 3229 3718 -244 -191 133 C ATOM 771 O ASP A 118 30.305 23.002 -2.566 1.00 20.36 O ANISOU 771 O ASP A 118 2584 2330 2820 -231 -188 122 O ATOM 772 CB ASP A 118 29.554 25.811 -2.826 1.00 30.43 C ANISOU 772 CB ASP A 118 3906 3572 4083 -240 -264 95 C ATOM 773 CG ASP A 118 29.189 26.214 -1.397 1.00 41.16 C ANISOU 773 CG ASP A 118 5227 4955 5457 -236 -286 81 C ATOM 774 OD1 ASP A 118 29.871 25.735 -0.468 1.00 39.06 O ANISOU 774 OD1 ASP A 118 4921 4715 5204 -239 -264 95 O ATOM 775 OD2 ASP A 118 28.249 27.021 -1.195 1.00 40.77 O ANISOU 775 OD2 ASP A 118 5187 4898 5408 -231 -325 58 O ATOM 776 N PRO A 119 32.138 23.671 -1.440 1.00 29.37 N ANISOU 776 N PRO A 119 3685 3498 3974 -252 -168 152 N ATOM 777 CA PRO A 119 32.425 22.292 -0.976 1.00 33.24 C ANISOU 777 CA PRO A 119 4144 4012 4475 -246 -134 163 C ATOM 778 C PRO A 119 31.379 21.710 -0.023 1.00 26.54 C ANISOU 778 C PRO A 119 3266 3181 3636 -231 -147 142 C ATOM 779 O PRO A 119 31.150 20.494 -0.049 1.00 16.94 O ANISOU 779 O PRO A 119 2039 1974 2424 -222 -126 143 O ATOM 780 CB PRO A 119 33.802 22.424 -0.294 1.00 26.37 C ANISOU 780 CB PRO A 119 3245 3160 3613 -259 -110 187 C ATOM 781 CG PRO A 119 33.888 23.844 0.105 1.00 27.51 C ANISOU 781 CG PRO A 119 3393 3302 3759 -268 -141 182 C ATOM 782 CD PRO A 119 33.111 24.652 -0.928 1.00 16.29 C ANISOU 782 CD PRO A 119 2018 1848 2322 -267 -170 166 C ATOM 783 N LEU A 120 30.729 22.528 0.807 1.00 23.94 N ANISOU 783 N LEU A 120 2924 2858 3313 -228 -181 123 N ATOM 784 CA LEU A 120 29.682 22.010 1.688 1.00 27.46 C ANISOU 784 CA LEU A 120 3344 3321 3769 -214 -195 102 C ATOM 785 C LEU A 120 28.614 23.102 1.877 1.00 31.80 C ANISOU 785 C LEU A 120 3906 3859 4316 -209 -242 74 C ATOM 786 O LEU A 120 28.566 23.813 2.881 1.00 33.03 O ANISOU 786 O LEU A 120 4040 4030 4481 -211 -262 67 O ATOM 787 CB LEU A 120 30.236 21.529 3.029 1.00 24.79 C ANISOU 787 CB LEU A 120 2957 3016 3447 -214 -178 111 C ATOM 788 CG LEU A 120 29.264 20.609 3.780 1.00 30.13 C ANISOU 788 CG LEU A 120 3607 3710 4132 -199 -181 94 C ATOM 789 CD1 LEU A 120 28.939 19.321 2.994 1.00 28.18 C ANISOU 789 CD1 LEU A 120 3372 3456 3880 -190 -157 95 C ATOM 790 CD2 LEU A 120 29.740 20.305 5.181 1.00 25.82 C ANISOU 790 CD2 LEU A 120 3013 3197 3602 -200 -170 101 C ATOM 791 N ASP A 121 27.739 23.225 0.883 1.00 34.27 N ANISOU 791 N ASP A 121 4256 4147 4617 -202 -259 58 N ATOM 792 CA ASP A 121 26.658 24.196 0.935 1.00 34.23 C ANISOU 792 CA ASP A 121 4267 4130 4609 -197 -303 31 C ATOM 793 C ASP A 121 25.595 23.781 1.939 1.00 28.88 C ANISOU 793 C ASP A 121 3560 3471 3943 -183 -320 8 C ATOM 794 O ASP A 121 25.266 22.598 2.071 1.00 32.22 O ANISOU 794 O ASP A 121 3967 3904 4370 -174 -301 6 O ATOM 795 CB ASP A 121 26.009 24.362 -0.437 1.00 43.12 C ANISOU 795 CB ASP A 121 5442 5223 5719 -192 -316 21 C ATOM 796 CG ASP A 121 24.910 25.426 -0.434 1.00 47.54 C ANISOU 796 CG ASP A 121 6020 5769 6276 -187 -363 -8 C ATOM 797 OD1 ASP A 121 25.234 26.635 -0.400 1.00 48.08 O ANISOU 797 OD1 ASP A 121 6100 5829 6341 -196 -384 -6 O ATOM 798 OD2 ASP A 121 23.720 25.049 -0.445 1.00 47.36 O ANISOU 798 OD2 ASP A 121 5999 5743 6253 -173 -380 -32 O ATOM 799 N GLY A 122 25.069 24.764 2.662 1.00 29.66 N ANISOU 799 N GLY A 122 3650 3573 4046 -182 -355 -10 N ATOM 800 CA GLY A 122 24.028 24.520 3.646 1.00 38.94 C ANISOU 800 CA GLY A 122 4798 4766 5232 -170 -373 -34 C ATOM 801 C GLY A 122 24.513 24.054 4.997 1.00 40.38 C ANISOU 801 C GLY A 122 4931 4981 5430 -171 -357 -26 C ATOM 802 O GLY A 122 23.685 23.751 5.863 1.00 43.68 O ANISOU 802 O GLY A 122 5324 5416 5858 -161 -370 -44 O ATOM 803 N SER A 123 25.829 24.028 5.213 1.00 43.35 N ANISOU 803 N SER A 123 5588 4915 5968 393 -431 221 N ATOM 804 CA SER A 123 26.446 23.421 6.387 1.00 52.31 C ANISOU 804 CA SER A 123 6704 6067 7103 406 -398 208 C ATOM 805 C SER A 123 26.239 24.210 7.671 1.00 52.27 C ANISOU 805 C SER A 123 6683 6062 7114 411 -394 188 C ATOM 806 O SER A 123 26.494 23.665 8.749 1.00 46.98 O ANISOU 806 O SER A 123 5996 5409 6445 423 -364 172 O ATOM 807 CB SER A 123 27.947 23.231 6.136 1.00 55.79 C ANISOU 807 CB SER A 123 7155 6522 7522 393 -385 231 C ATOM 808 OG SER A 123 28.606 24.466 5.886 1.00 53.86 O ANISOU 808 OG SER A 123 6924 6264 7277 375 -407 249 O ATOM 809 N SER A 124 25.760 25.453 7.599 1.00 58.46 N ANISOU 809 N SER A 124 7472 6828 7910 402 -421 188 N ATOM 810 CA SER A 124 25.564 26.214 8.829 1.00 67.01 C ANISOU 810 CA SER A 124 8542 7912 9008 407 -417 170 C ATOM 811 C SER A 124 24.493 25.587 9.709 1.00 76.87 C ANISOU 811 C SER A 124 9771 9174 10263 421 -395 141 C ATOM 812 O SER A 124 24.611 25.605 10.941 1.00 82.24 O ANISOU 812 O SER A 124 10437 9865 10946 429 -374 125 O ATOM 813 CB SER A 124 25.186 27.654 8.501 1.00 60.96 C ANISOU 813 CB SER A 124 7785 7124 8254 394 -452 176 C ATOM 814 OG SER A 124 23.943 27.670 7.836 1.00 63.03 O ANISOU 814 OG SER A 124 8050 7377 8520 394 -468 170 O ATOM 815 N ASN A 125 23.483 24.972 9.100 1.00 85.60 N ANISOU 815 N ASN A 125 10878 10280 11367 425 -396 135 N ATOM 816 CA ASN A 125 22.423 24.292 9.829 1.00 92.59 C ANISOU 816 CA ASN A 125 11747 11179 12256 437 -374 110 C ATOM 817 C ASN A 125 22.625 22.778 9.880 1.00 85.57 C ANISOU 817 C ASN A 125 10851 10311 11352 447 -341 105 C ATOM 818 O ASN A 125 21.656 22.038 10.078 1.00 88.46 O ANISOU 818 O ASN A 125 11207 10686 11718 455 -326 89 O ATOM 819 CB ASN A 125 21.056 24.630 9.222 1.00101.96 C ANISOU 819 CB ASN A 125 12936 12352 13452 434 -397 104 C ATOM 820 CG ASN A 125 20.726 26.114 9.299 1.00108.14 C ANISOU 820 CG ASN A 125 13724 13116 14250 424 -427 105 C ATOM 821 OD1 ASN A 125 20.519 26.773 8.281 1.00110.57 O ANISOU 821 OD1 ASN A 125 14045 13405 14561 414 -458 119 O ATOM 822 ND2 ASN A 125 20.652 26.640 10.516 1.00110.09 N ANISOU 822 ND2 ASN A 125 13958 13366 14504 428 -417 91 N ATOM 823 N ILE A 126 23.863 22.299 9.722 1.00 66.55 N ANISOU 823 N ILE A 126 8446 7909 8932 447 -330 119 N ATOM 824 CA ILE A 126 24.099 20.858 9.739 1.00 63.50 C ANISOU 824 CA ILE A 126 8052 7543 8531 458 -298 115 C ATOM 825 C ILE A 126 23.912 20.267 11.129 1.00 57.81 C ANISOU 825 C ILE A 126 7313 6845 7808 469 -262 92 C ATOM 826 O ILE A 126 23.845 19.035 11.260 1.00 52.33 O ANISOU 826 O ILE A 126 6611 6169 7101 478 -233 84 O ATOM 827 CB ILE A 126 25.498 20.527 9.159 1.00 60.95 C ANISOU 827 CB ILE A 126 7740 7222 8197 454 -296 138 C ATOM 828 CG1 ILE A 126 25.538 19.084 8.626 1.00 57.32 C ANISOU 828 CG1 ILE A 126 7279 6777 7723 461 -275 139 C ATOM 829 CG2 ILE A 126 26.607 20.767 10.178 1.00 59.74 C ANISOU 829 CG2 ILE A 126 7579 7078 8042 456 -279 137 C ATOM 830 CD1 ILE A 126 26.883 18.646 8.083 1.00 46.40 C ANISOU 830 CD1 ILE A 126 5906 5401 6324 455 -269 162 C ATOM 831 N ASP A 127 23.811 21.126 12.160 1.00 52.08 N ANISOU 831 N ASP A 127 6580 6117 7090 469 -262 81 N ATOM 832 CA ASP A 127 23.485 20.724 13.527 1.00 49.03 C ANISOU 832 CA ASP A 127 6178 5750 6699 477 -231 61 C ATOM 833 C ASP A 127 22.109 20.083 13.633 1.00 47.14 C ANISOU 833 C ASP A 127 5933 5519 6460 482 -220 45 C ATOM 834 O ASP A 127 21.862 19.330 14.584 1.00 48.06 O ANISOU 834 O ASP A 127 6039 5655 6565 489 -188 31 O ATOM 835 CB ASP A 127 23.534 21.935 14.459 1.00 65.69 C ANISOU 835 CB ASP A 127 8286 7853 8821 474 -241 55 C ATOM 836 CG ASP A 127 24.874 22.630 14.440 1.00 82.98 C ANISOU 836 CG ASP A 127 10481 10035 11012 468 -251 70 C ATOM 837 OD1 ASP A 127 25.873 21.984 14.829 1.00 91.96 O ANISOU 837 OD1 ASP A 127 11615 11189 12139 473 -227 72 O ATOM 838 OD2 ASP A 127 24.930 23.811 14.021 1.00 84.22 O ANISOU 838 OD2 ASP A 127 10647 10170 11181 459 -283 80 O ATOM 839 N CYS A 128 21.194 20.391 12.709 1.00 31.62 N ANISOU 839 N CYS A 128 3974 3536 4504 477 -247 48 N ATOM 840 CA CYS A 128 19.870 19.785 12.725 1.00 28.90 C ANISOU 840 CA CYS A 128 3624 3197 4160 481 -239 35 C ATOM 841 C CYS A 128 19.747 18.627 11.741 1.00 26.81 C ANISOU 841 C CYS A 128 3362 2938 3885 484 -232 39 C ATOM 842 O CYS A 128 18.641 18.108 11.554 1.00 28.49 O ANISOU 842 O CYS A 128 3572 3154 4100 486 -228 30 O ATOM 843 CB CYS A 128 18.790 20.849 12.449 1.00 37.50 C ANISOU 843 CB CYS A 128 4716 4265 5266 474 -271 31 C ATOM 844 SG CYS A 128 18.666 21.592 10.757 1.00 46.15 S ANISOU 844 SG CYS A 128 5829 5333 6373 464 -317 50 S ATOM 845 N LEU A 129 20.869 18.194 11.145 1.00 19.72 N ANISOU 845 N LEU A 129 2471 2043 2978 484 -228 54 N ATOM 846 CA LEU A 129 20.973 17.067 10.208 1.00 22.01 C ANISOU 846 CA LEU A 129 2766 2340 3258 488 -221 61 C ATOM 847 C LEU A 129 20.196 17.311 8.923 1.00 18.68 C ANISOU 847 C LEU A 129 2355 1899 2844 482 -253 69 C ATOM 848 O LEU A 129 19.818 16.352 8.239 1.00 23.65 O ANISOU 848 O LEU A 129 2985 2534 3466 485 -247 69 O ATOM 849 CB LEU A 129 20.505 15.742 10.830 1.00 22.38 C ANISOU 849 CB LEU A 129 2800 2412 3292 497 -182 45 C ATOM 850 CG LEU A 129 21.115 15.302 12.171 1.00 28.04 C ANISOU 850 CG LEU A 129 3507 3153 3996 503 -146 35 C ATOM 851 CD1 LEU A 129 20.508 13.968 12.563 1.00 31.41 C ANISOU 851 CD1 LEU A 129 3925 3601 4407 510 -112 23 C ATOM 852 CD2 LEU A 129 22.636 15.247 12.162 1.00 21.13 C ANISOU 852 CD2 LEU A 129 2634 2283 3113 504 -138 47 C ATOM 853 N VAL A 130 19.936 18.582 8.606 1.00 20.65 N ANISOU 853 N VAL A 130 2613 2127 3107 473 -287 75 N ATOM 854 CA VAL A 130 19.403 18.953 7.301 1.00 30.39 C ANISOU 854 CA VAL A 130 3861 3341 4346 465 -321 87 C ATOM 855 C VAL A 130 20.340 18.443 6.205 1.00 23.80 C ANISOU 855 C VAL A 130 3041 2505 3497 462 -327 109 C ATOM 856 O VAL A 130 21.552 18.260 6.420 1.00 27.44 O ANISOU 856 O VAL A 130 3503 2973 3949 462 -314 119 O ATOM 857 CB VAL A 130 19.231 20.483 7.219 1.00 40.20 C ANISOU 857 CB VAL A 130 5110 4561 5601 454 -355 92 C ATOM 858 CG1 VAL A 130 20.592 21.181 7.233 1.00 38.18 C ANISOU 858 CG1 VAL A 130 4865 4300 5343 447 -364 111 C ATOM 859 CG2 VAL A 130 18.451 20.896 5.971 1.00 41.07 C ANISOU 859 CG2 VAL A 130 5235 4653 5717 446 -390 101 C ATOM 860 N SER A 131 19.770 18.200 5.029 1.00 25.37 N ANISOU 860 N SER A 131 3251 2693 3693 458 -346 117 N ATOM 861 CA SER A 131 20.559 17.860 3.847 1.00 31.43 C ANISOU 861 CA SER A 131 4038 3458 4447 452 -358 141 C ATOM 862 C SER A 131 21.584 18.946 3.546 1.00 31.28 C ANISOU 862 C SER A 131 4035 3425 4426 438 -380 164 C ATOM 863 O SER A 131 21.334 20.133 3.751 1.00 31.05 O ANISOU 863 O SER A 131 4008 3382 4409 431 -401 164 O ATOM 864 CB SER A 131 19.653 17.662 2.639 1.00 29.41 C ANISOU 864 CB SER A 131 3794 3191 4190 448 -380 146 C ATOM 865 OG SER A 131 18.703 16.637 2.860 1.00 38.98 O ANISOU 865 OG SER A 131 4992 4416 5404 459 -359 126 O ATOM 866 N VAL A 132 22.757 18.519 3.083 1.00 31.16 N ANISOU 866 N VAL A 132 4032 3414 4394 434 -375 186 N ATOM 867 CA VAL A 132 23.834 19.394 2.653 1.00 22.96 C ANISOU 867 CA VAL A 132 3012 2366 3347 418 -393 212 C ATOM 868 C VAL A 132 24.357 18.865 1.320 1.00 25.92 C ANISOU 868 C VAL A 132 3406 2755 3686 399 -389 234 C ATOM 869 O VAL A 132 24.005 17.769 0.887 1.00 26.95 O ANISOU 869 O VAL A 132 3535 2899 3805 403 -373 229 O ATOM 870 CB VAL A 132 24.958 19.489 3.704 1.00 20.95 C ANISOU 870 CB VAL A 132 2746 2129 3087 418 -367 210 C ATOM 871 CG1 VAL A 132 24.486 20.319 4.902 1.00 17.43 C ANISOU 871 CG1 VAL A 132 2284 1673 2668 427 -371 190 C ATOM 872 CG2 VAL A 132 25.403 18.084 4.169 1.00 11.04 C ANISOU 872 CG2 VAL A 132 1476 905 1813 425 -321 200 C ATOM 873 N GLY A 133 25.221 19.648 0.673 1.00 27.57 N ANISOU 873 N GLY A 133 3634 2962 3878 376 -401 258 N ATOM 874 CA GLY A 133 25.662 19.249 -0.653 1.00 26.83 C ANISOU 874 CA GLY A 133 3562 2879 3752 357 -400 280 C ATOM 875 C GLY A 133 26.956 19.901 -1.089 1.00 26.85 C ANISOU 875 C GLY A 133 3581 2889 3733 333 -400 306 C ATOM 876 O GLY A 133 27.482 20.802 -0.435 1.00 24.11 O ANISOU 876 O GLY A 133 3231 2534 3396 330 -406 308 O ATOM 877 N THR A 134 27.480 19.398 -2.209 1.00 24.05 N ANISOU 877 N THR A 134 3244 2548 3345 316 -393 325 N ATOM 878 CA THR A 134 28.652 19.949 -2.877 1.00 27.25 C ANISOU 878 CA THR A 134 3669 2959 3727 292 -394 353 C ATOM 879 C THR A 134 28.241 20.441 -4.261 1.00 27.91 C ANISOU 879 C THR A 134 3778 3024 3802 278 -427 372 C ATOM 880 O THR A 134 27.649 19.683 -5.033 1.00 27.18 O ANISOU 880 O THR A 134 3692 2935 3699 280 -428 371 O ATOM 881 CB THR A 134 29.749 18.878 -2.979 1.00 25.48 C ANISOU 881 CB THR A 134 3444 2769 3468 283 -352 360 C ATOM 882 OG1 THR A 134 30.059 18.401 -1.670 1.00 20.10 O ANISOU 882 OG1 THR A 134 2739 2104 2796 297 -322 341 O ATOM 883 CG2 THR A 134 30.999 19.430 -3.602 1.00 30.45 C ANISOU 883 CG2 THR A 134 4093 3405 4073 258 -351 387 C ATOM 884 N ILE A 135 28.578 21.687 -4.601 1.00 26.41 N ANISOU 884 N ILE A 135 3603 2816 3615 264 -454 389 N ATOM 885 CA ILE A 135 28.209 22.266 -5.899 1.00 28.41 C ANISOU 885 CA ILE A 135 3882 3050 3862 250 -487 407 C ATOM 886 C ILE A 135 29.478 22.515 -6.702 1.00 25.68 C ANISOU 886 C ILE A 135 3557 2716 3485 225 -480 436 C ATOM 887 O ILE A 135 30.490 22.960 -6.146 1.00 23.55 O ANISOU 887 O ILE A 135 3284 2454 3212 216 -468 442 O ATOM 888 CB ILE A 135 27.391 23.570 -5.756 1.00 25.33 C ANISOU 888 CB ILE A 135 3494 2625 3504 255 -530 404 C ATOM 889 CG1 ILE A 135 26.210 23.364 -4.811 1.00 20.38 C ANISOU 889 CG1 ILE A 135 2845 1988 2911 281 -534 375 C ATOM 890 CG2 ILE A 135 26.902 24.064 -7.127 1.00 27.69 C ANISOU 890 CG2 ILE A 135 3820 2905 3797 244 -564 422 C ATOM 891 CD1 ILE A 135 25.417 24.648 -4.505 1.00 21.43 C ANISOU 891 CD1 ILE A 135 2978 2088 3078 288 -574 369 C ATOM 892 N PHE A 136 29.445 22.197 -7.999 1.00 17.95 N ANISOU 892 N PHE A 136 2600 1738 2482 213 -487 453 N ATOM 893 CA PHE A 136 30.649 22.410 -8.794 1.00 27.29 C ANISOU 893 CA PHE A 136 3803 2932 3633 188 -479 481 C ATOM 894 C PHE A 136 30.328 22.862 -10.215 1.00 29.59 C ANISOU 894 C PHE A 136 4123 3206 3913 174 -510 501 C ATOM 895 O PHE A 136 29.308 22.493 -10.795 1.00 27.40 O ANISOU 895 O PHE A 136 3852 2920 3640 183 -526 495 O ATOM 896 CB PHE A 136 31.540 21.171 -8.851 1.00 25.52 C ANISOU 896 CB PHE A 136 3575 2742 3378 183 -436 484 C ATOM 897 CG PHE A 136 30.896 19.966 -9.474 1.00 32.73 C ANISOU 897 CG PHE A 136 4491 3667 4279 190 -427 478 C ATOM 898 CD1 PHE A 136 30.123 19.106 -8.712 1.00 30.05 C ANISOU 898 CD1 PHE A 136 4129 3334 3954 213 -412 452 C ATOM 899 CD2 PHE A 136 31.092 19.678 -10.830 1.00 30.51 C ANISOU 899 CD2 PHE A 136 4235 3390 3969 175 -431 499 C ATOM 900 CE1 PHE A 136 29.535 17.994 -9.280 1.00 25.50 C ANISOU 900 CE1 PHE A 136 3554 2768 3366 219 -403 446 C ATOM 901 CE2 PHE A 136 30.509 18.572 -11.401 1.00 24.16 C ANISOU 901 CE2 PHE A 136 3433 2596 3153 182 -422 493 C ATOM 902 CZ PHE A 136 29.726 17.726 -10.622 1.00 30.79 C ANISOU 902 CZ PHE A 136 4249 3442 4009 204 -408 466 C ATOM 903 N GLY A 137 31.220 23.691 -10.759 1.00 23.22 N ANISOU 903 N GLY A 137 3335 2394 3092 153 -518 526 N ATOM 904 CA GLY A 137 31.172 24.096 -12.152 1.00 21.72 C ANISOU 904 CA GLY A 137 3175 2193 2886 137 -542 549 C ATOM 905 C GLY A 137 32.570 24.166 -12.721 1.00 22.27 C ANISOU 905 C GLY A 137 3260 2277 2923 114 -524 575 C ATOM 906 O GLY A 137 33.481 24.653 -12.054 1.00 24.04 O ANISOU 906 O GLY A 137 3478 2508 3150 107 -512 579 O ATOM 907 N ILE A 138 32.755 23.670 -13.940 1.00 25.42 N ANISOU 907 N ILE A 138 3682 2685 3293 101 -522 592 N ATOM 908 CA ILE A 138 34.068 23.463 -14.539 1.00 24.95 C ANISOU 908 CA ILE A 138 3637 2644 3200 80 -499 616 C ATOM 909 C ILE A 138 34.154 24.238 -15.854 1.00 25.22 C ANISOU 909 C ILE A 138 3704 2661 3220 62 -527 642 C ATOM 910 O ILE A 138 33.339 24.018 -16.761 1.00 24.79 O ANISOU 910 O ILE A 138 3663 2596 3160 64 -546 645 O ATOM 911 CB ILE A 138 34.323 21.964 -14.802 1.00 26.32 C ANISOU 911 CB ILE A 138 3806 2847 3345 82 -463 613 C ATOM 912 CG1 ILE A 138 34.289 21.135 -13.512 1.00 22.31 C ANISOU 912 CG1 ILE A 138 3268 2359 2850 100 -433 588 C ATOM 913 CG2 ILE A 138 35.614 21.774 -15.602 1.00 28.09 C ANISOU 913 CG2 ILE A 138 4050 3090 3534 59 -442 640 C ATOM 914 CD1 ILE A 138 34.152 19.622 -13.781 1.00 22.55 C ANISOU 914 CD1 ILE A 138 3294 2414 2860 107 -404 580 C ATOM 915 N TYR A 139 35.170 25.083 -15.988 1.00 25.46 N ANISOU 915 N TYR A 139 3745 2688 3242 43 -527 663 N ATOM 916 CA TYR A 139 35.404 25.815 -17.235 1.00 36.38 C ANISOU 916 CA TYR A 139 5154 4061 4609 25 -545 684 C ATOM 917 C TYR A 139 36.739 25.412 -17.838 1.00 41.63 C ANISOU 917 C TYR A 139 5830 4749 5237 5 -514 705 C ATOM 918 O TYR A 139 37.625 24.900 -17.148 1.00 50.03 O ANISOU 918 O TYR A 139 6884 5830 6293 2 -487 708 O ATOM 919 CB TYR A 139 35.422 27.345 -17.045 1.00 25.34 C ANISOU 919 CB TYR A 139 3755 2640 3231 19 -570 685 C ATOM 920 CG TYR A 139 34.139 27.969 -16.537 1.00 27.97 C ANISOU 920 CG TYR A 139 4078 2950 3601 36 -602 664 C ATOM 921 CD1 TYR A 139 33.244 28.545 -17.428 1.00 22.44 C ANISOU 921 CD1 TYR A 139 3390 2232 2905 35 -630 662 C ATOM 922 CD2 TYR A 139 33.835 28.014 -15.169 1.00 19.97 C ANISOU 922 CD2 TYR A 139 3041 1929 2616 53 -603 647 C ATOM 923 CE1 TYR A 139 32.067 29.127 -16.997 1.00 24.59 C ANISOU 923 CE1 TYR A 139 3651 2483 3209 50 -659 642 C ATOM 924 CE2 TYR A 139 32.647 28.619 -14.723 1.00 23.97 C ANISOU 924 CE2 TYR A 139 3537 2415 3156 69 -631 626 C ATOM 925 CZ TYR A 139 31.770 29.177 -15.657 1.00 27.60 C ANISOU 925 CZ TYR A 139 4009 2859 3619 66 -658 624 C ATOM 926 OH TYR A 139 30.580 29.783 -15.289 1.00 35.26 O ANISOU 926 OH TYR A 139 4969 3809 4620 80 -685 604 O ATOM 927 N ARG A 140 36.884 25.663 -19.139 1.00 40.90 N ANISOU 927 N ARG A 140 5758 4657 5125 -10 -519 717 N ATOM 928 CA ARG A 140 38.190 25.606 -19.776 1.00 34.93 C ANISOU 928 CA ARG A 140 5013 3920 4339 -30 -493 737 C ATOM 929 C ARG A 140 38.805 27.003 -19.763 1.00 42.66 C ANISOU 929 C ARG A 140 5997 4886 5327 -43 -506 746 C ATOM 930 O ARG A 140 38.133 27.987 -20.101 1.00 44.03 O ANISOU 930 O ARG A 140 6176 5036 5516 -43 -537 744 O ATOM 931 CB ARG A 140 38.090 25.067 -21.201 1.00 39.49 C ANISOU 931 CB ARG A 140 5609 4507 4888 -37 -488 745 C ATOM 932 CG ARG A 140 39.269 24.176 -21.612 1.00 54.07 C ANISOU 932 CG ARG A 140 7459 6383 6700 -50 -448 757 C ATOM 933 CD AARG A 140 39.042 23.568 -23.004 0.50 56.51 C ANISOU 933 CD AARG A 140 7785 6701 6984 -54 -444 762 C ATOM 934 CD BARG A 140 39.628 24.359 -23.082 0.50 57.74 C ANISOU 934 CD BARG A 140 7945 6853 7142 -65 -446 771 C ATOM 935 NE AARG A 140 39.943 22.452 -23.292 0.50 55.20 N ANISOU 935 NE AARG A 140 7619 6566 6789 -60 -404 769 N ATOM 936 NE BARG A 140 41.018 24.005 -23.368 0.50 56.16 N ANISOU 936 NE BARG A 140 7746 6676 6914 -79 -410 784 N ATOM 937 CZ AARG A 140 39.953 21.768 -24.434 0.50 47.97 C ANISOU 937 CZ AARG A 140 6716 5663 5848 -64 -393 774 C ATOM 938 CZ BARG A 140 42.052 24.811 -23.144 0.50 51.32 C ANISOU 938 CZ BARG A 140 7133 6065 6303 -92 -403 794 C ATOM 939 NH1AARG A 140 39.112 22.085 -25.409 0.50 47.92 N ANISOU 939 NH1AARG A 140 6724 5641 5843 -63 -419 774 N ATOM 940 NH1BARG A 140 41.858 26.014 -22.618 0.50 46.96 N ANISOU 940 NH1BARG A 140 6578 5489 5775 -93 -428 793 N ATOM 941 NH2AARG A 140 40.804 20.762 -24.603 0.50 39.51 N ANISOU 941 NH2AARG A 140 5641 4620 4751 -69 -356 778 N ATOM 942 NH2BARG A 140 43.282 24.412 -23.438 0.50 50.81 N ANISOU 942 NH2BARG A 140 7068 6022 6214 -104 -369 804 N ATOM 943 N LYS A 141 40.068 27.090 -19.332 1.00 41.38 N ANISOU 943 N LYS A 141 5830 4738 5156 -55 -481 756 N ATOM 944 CA LYS A 141 40.796 28.349 -19.399 1.00 36.94 C ANISOU 944 CA LYS A 141 5272 4165 4598 -70 -489 767 C ATOM 945 C LYS A 141 40.802 28.873 -20.831 1.00 46.36 C ANISOU 945 C LYS A 141 6487 5352 5775 -83 -500 779 C ATOM 946 O LYS A 141 41.127 28.145 -21.778 1.00 39.45 O ANISOU 946 O LYS A 141 5623 4495 4873 -90 -482 787 O ATOM 947 CB LYS A 141 42.227 28.143 -18.905 1.00 33.46 C ANISOU 947 CB LYS A 141 4825 3745 4145 -81 -456 778 C ATOM 948 CG LYS A 141 43.108 29.395 -18.863 1.00 35.94 C ANISOU 948 CG LYS A 141 5142 4050 4464 -97 -461 789 C ATOM 949 CD LYS A 141 44.530 28.989 -18.511 1.00 40.88 C ANISOU 949 CD LYS A 141 5761 4700 5072 -108 -424 799 C ATOM 950 CE LYS A 141 45.422 30.161 -18.111 1.00 41.65 C ANISOU 950 CE LYS A 141 5855 4788 5180 -120 -428 807 C ATOM 951 NZ LYS A 141 45.310 31.334 -19.016 1.00 43.86 N ANISOU 951 NZ LYS A 141 6152 5050 5463 -131 -452 816 N ATOM 952 N LYS A 142 40.475 30.153 -20.981 1.00 59.66 N ANISOU 952 N LYS A 142 8177 7013 7477 -86 -530 780 N ATOM 953 CA LYS A 142 40.213 30.729 -22.293 1.00 71.29 C ANISOU 953 CA LYS A 142 9671 8476 8940 -96 -547 789 C ATOM 954 C LYS A 142 41.359 31.579 -22.820 1.00 72.82 C ANISOU 954 C LYS A 142 9875 8672 9122 -115 -540 806 C ATOM 955 O LYS A 142 41.572 31.621 -24.035 1.00 79.98 O ANISOU 955 O LYS A 142 10799 9581 10008 -126 -538 817 O ATOM 956 CB LYS A 142 38.920 31.553 -22.269 1.00 75.95 C ANISOU 956 CB LYS A 142 10262 9039 9557 -85 -588 777 C ATOM 957 CG LYS A 142 37.642 30.710 -22.284 1.00 79.37 C ANISOU 957 CG LYS A 142 10691 9469 9996 -67 -598 761 C ATOM 958 CD LYS A 142 37.490 29.911 -23.572 1.00 83.79 C ANISOU 958 CD LYS A 142 11267 10040 10528 -71 -590 768 C ATOM 959 CE LYS A 142 36.148 29.189 -23.620 1.00 84.35 C ANISOU 959 CE LYS A 142 11335 10106 10608 -54 -605 752 C ATOM 960 NZ LYS A 142 35.943 28.461 -24.909 1.00 88.68 N ANISOU 960 NZ LYS A 142 11900 10664 11130 -57 -599 757 N ATOM 961 N SER A 143 42.116 32.233 -21.947 1.00 64.84 N ANISOU 961 N SER A 143 8854 7659 8124 -121 -535 809 N ATOM 962 CA SER A 143 43.202 33.083 -22.396 1.00 60.22 C ANISOU 962 CA SER A 143 8279 7074 7530 -139 -529 825 C ATOM 963 C SER A 143 44.525 32.316 -22.390 1.00 61.38 C ANISOU 963 C SER A 143 8422 7248 7652 -149 -488 835 C ATOM 964 O SER A 143 44.634 31.200 -21.881 1.00 57.38 O ANISOU 964 O SER A 143 7904 6759 7137 -141 -465 829 O ATOM 965 CB SER A 143 43.278 34.339 -21.525 1.00 61.81 C ANISOU 965 CB SER A 143 8471 7255 7758 -140 -549 823 C ATOM 966 OG SER A 143 44.041 34.122 -20.353 1.00 65.52 O ANISOU 966 OG SER A 143 8923 7736 8235 -139 -529 821 O ATOM 967 N THR A 144 45.518 32.891 -23.052 1.00 70.75 N ANISOU 967 N THR A 144 9619 8438 8825 -165 -478 850 N ATOM 968 CA THR A 144 46.857 32.323 -23.073 1.00 77.23 C ANISOU 968 CA THR A 144 10436 9283 9625 -176 -440 859 C ATOM 969 C THR A 144 47.803 33.009 -22.085 1.00 73.19 C ANISOU 969 C THR A 144 9912 8770 9126 -183 -432 863 C ATOM 970 O THR A 144 48.980 32.635 -22.002 1.00 71.12 O ANISOU 970 O THR A 144 9645 8528 8849 -192 -401 870 O ATOM 971 CB THR A 144 47.406 32.369 -24.506 1.00 86.07 C ANISOU 971 CB THR A 144 11574 10410 10719 -188 -429 873 C ATOM 972 OG1 THR A 144 48.663 31.683 -24.569 1.00 91.57 O ANISOU 972 OG1 THR A 144 12266 11132 11394 -196 -390 880 O ATOM 973 CG2 THR A 144 47.543 33.814 -25.000 1.00 88.06 C ANISOU 973 CG2 THR A 144 11838 10640 10980 -200 -453 883 C ATOM 974 N ASP A 145 47.307 33.991 -21.327 1.00 64.52 N ANISOU 974 N ASP A 145 8808 7650 8057 -179 -461 857 N ATOM 975 CA ASP A 145 48.054 34.665 -20.271 1.00 62.47 C ANISOU 975 CA ASP A 145 8536 7387 7814 -183 -458 858 C ATOM 976 C ASP A 145 48.486 33.692 -19.182 1.00 61.71 C ANISOU 976 C ASP A 145 8420 7310 7716 -176 -431 851 C ATOM 977 O ASP A 145 48.195 32.493 -19.241 1.00 57.42 O ANISOU 977 O ASP A 145 7874 6783 7160 -168 -415 845 O ATOM 978 CB ASP A 145 47.211 35.762 -19.617 1.00 65.03 C ANISOU 978 CB ASP A 145 8855 7683 8170 -176 -495 850 C ATOM 979 CG ASP A 145 46.762 36.825 -20.591 1.00 81.10 C ANISOU 979 CG ASP A 145 10908 9698 10209 -183 -523 856 C ATOM 980 OD1 ASP A 145 47.377 36.956 -21.672 1.00 90.29 O ANISOU 980 OD1 ASP A 145 12087 10868 11352 -196 -513 869 O ATOM 981 OD2 ASP A 145 45.783 37.533 -20.269 1.00 84.37 O ANISOU 981 OD2 ASP A 145 11320 10090 10647 -174 -555 846 O ATOM 982 N GLU A 146 49.156 34.197 -18.186 1.00 62.35 N ANISOU 982 N GLU A 146 8488 7389 7812 -180 -428 852 N ATOM 983 CA GLU A 146 49.439 33.301 -17.082 1.00 50.89 C ANISOU 983 CA GLU A 146 7019 5955 6363 -171 -405 844 C ATOM 984 C GLU A 146 48.171 33.159 -16.249 1.00 44.13 C ANISOU 984 C GLU A 146 6151 5084 5531 -152 -428 827 C ATOM 985 O GLU A 146 47.381 34.104 -16.162 1.00 46.59 O ANISOU 985 O GLU A 146 6466 5371 5866 -147 -462 822 O ATOM 986 CB GLU A 146 50.575 33.843 -16.226 1.00 51.68 C ANISOU 986 CB GLU A 146 7107 6057 6471 -181 -393 849 C ATOM 987 CG GLU A 146 51.937 33.560 -16.820 1.00 66.99 C ANISOU 987 CG GLU A 146 9051 8018 8385 -197 -360 862 C ATOM 988 CD GLU A 146 52.399 32.136 -16.585 1.00 74.77 C ANISOU 988 CD GLU A 146 10027 9033 9350 -193 -323 858 C ATOM 989 OE1 GLU A 146 52.337 31.667 -15.426 1.00 76.88 O ANISOU 989 OE1 GLU A 146 10277 9306 9629 -183 -316 849 O ATOM 990 OE2 GLU A 146 52.791 31.477 -17.571 1.00 75.45 O ANISOU 990 OE2 GLU A 146 10122 9136 9409 -199 -302 864 O ATOM 991 N PRO A 147 47.913 31.976 -15.701 1.00 32.10 N ANISOU 991 N PRO A 147 4617 3576 4004 -139 -411 818 N ATOM 992 CA PRO A 147 46.650 31.763 -14.990 1.00 28.91 C ANISOU 992 CA PRO A 147 4204 3159 3623 -119 -432 801 C ATOM 993 C PRO A 147 46.525 32.736 -13.830 1.00 31.19 C ANISOU 993 C PRO A 147 4479 3428 3945 -113 -453 793 C ATOM 994 O PRO A 147 47.480 32.981 -13.084 1.00 36.74 O ANISOU 994 O PRO A 147 5171 4136 4651 -119 -439 798 O ATOM 995 CB PRO A 147 46.743 30.305 -14.515 1.00 29.06 C ANISOU 995 CB PRO A 147 4211 3201 3628 -110 -403 795 C ATOM 996 CG PRO A 147 48.230 29.984 -14.521 1.00 25.19 C ANISOU 996 CG PRO A 147 3718 2735 3116 -125 -367 807 C ATOM 997 CD PRO A 147 48.796 30.793 -15.651 1.00 35.77 C ANISOU 997 CD PRO A 147 5077 4072 4444 -143 -371 821 C ATOM 998 N SER A 148 45.347 33.326 -13.714 1.00 31.39 N ANISOU 998 N SER A 148 4504 3430 3994 -100 -486 782 N ATOM 999 CA SER A 148 45.069 34.270 -12.648 1.00 37.53 C ANISOU 999 CA SER A 148 5268 4187 4805 -92 -507 771 C ATOM 1000 C SER A 148 43.579 34.227 -12.348 1.00 41.65 C ANISOU 1000 C SER A 148 5783 4692 5349 -71 -533 752 C ATOM 1001 O SER A 148 42.814 33.496 -12.985 1.00 38.71 O ANISOU 1001 O SER A 148 5418 4323 4967 -64 -535 748 O ATOM 1002 CB SER A 148 45.489 35.689 -13.026 1.00 33.89 C ANISOU 1002 CB SER A 148 4817 3710 4351 -107 -526 781 C ATOM 1003 OG SER A 148 44.463 36.300 -13.789 1.00 42.23 O ANISOU 1003 OG SER A 148 5885 4747 5414 -104 -556 778 O ATOM 1004 N GLU A 149 43.177 35.039 -11.372 1.00 43.95 N ANISOU 1004 N GLU A 149 6061 4964 5673 -61 -554 739 N ATOM 1005 CA GLU A 149 41.780 35.114 -10.961 1.00 39.02 C ANISOU 1005 CA GLU A 149 5428 4324 5075 -40 -578 718 C ATOM 1006 C GLU A 149 40.876 35.503 -12.128 1.00 35.18 C ANISOU 1006 C GLU A 149 4958 3824 4584 -42 -602 719 C ATOM 1007 O GLU A 149 39.718 35.070 -12.187 1.00 32.68 O ANISOU 1007 O GLU A 149 4639 3502 4277 -26 -614 704 O ATOM 1008 CB GLU A 149 41.670 36.112 -9.806 1.00 38.59 C ANISOU 1008 CB GLU A 149 5358 4252 5054 -31 -595 706 C ATOM 1009 CG GLU A 149 40.350 36.192 -9.109 1.00 39.78 C ANISOU 1009 CG GLU A 149 5494 4386 5233 -8 -616 681 C ATOM 1010 CD GLU A 149 40.494 36.858 -7.744 1.00 39.59 C ANISOU 1010 CD GLU A 149 5451 4353 5240 1 -621 668 C ATOM 1011 OE1 GLU A 149 41.221 36.298 -6.887 1.00 40.63 O ANISOU 1011 OE1 GLU A 149 5564 4504 5368 5 -591 661 O ATOM 1012 OE2 GLU A 149 39.850 37.899 -7.507 1.00 37.78 O ANISOU 1012 OE2 GLU A 149 5217 4103 5033 6 -647 658 O ATOM 1013 N LYS A 150 41.402 36.289 -13.085 1.00 36.59 N ANISOU 1013 N LYS A 150 5155 3999 4749 -61 -609 735 N ATOM 1014 CA LYS A 150 40.608 36.717 -14.235 1.00 37.72 C ANISOU 1014 CA LYS A 150 5315 4129 4888 -64 -632 737 C ATOM 1015 C LYS A 150 40.031 35.527 -14.997 1.00 41.06 C ANISOU 1015 C LYS A 150 5745 4564 5291 -59 -623 736 C ATOM 1016 O LYS A 150 38.917 35.612 -15.534 1.00 35.27 O ANISOU 1016 O LYS A 150 5019 3819 4564 -51 -645 727 O ATOM 1017 CB LYS A 150 41.485 37.531 -15.191 1.00 49.40 C ANISOU 1017 CB LYS A 150 6813 5607 6349 -87 -632 758 C ATOM 1018 CG LYS A 150 42.086 38.802 -14.613 1.00 65.26 C ANISOU 1018 CG LYS A 150 8817 7604 8377 -96 -642 761 C ATOM 1019 CD LYS A 150 43.051 39.463 -15.598 1.00 69.07 C ANISOU 1019 CD LYS A 150 9318 8088 8839 -118 -638 783 C ATOM 1020 CE LYS A 150 43.664 40.731 -15.009 1.00 74.83 C ANISOU 1020 CE LYS A 150 10042 8804 9586 -127 -648 787 C ATOM 1021 NZ LYS A 150 44.613 41.425 -15.930 1.00 77.20 N ANISOU 1021 NZ LYS A 150 10359 9105 9870 -148 -644 807 N ATOM 1022 N ASP A 151 40.752 34.397 -15.018 1.00 34.68 N ANISOU 1022 N ASP A 151 4937 3780 4459 -62 -590 743 N ATOM 1023 CA ASP A 151 40.299 33.239 -15.781 1.00 39.44 C ANISOU 1023 CA ASP A 151 5547 4396 5041 -57 -580 742 C ATOM 1024 C ASP A 151 39.011 32.655 -15.233 1.00 39.71 C ANISOU 1024 C ASP A 151 5570 4424 5095 -34 -592 721 C ATOM 1025 O ASP A 151 38.343 31.899 -15.950 1.00 37.24 O ANISOU 1025 O ASP A 151 5265 4115 4770 -29 -592 718 O ATOM 1026 CB ASP A 151 41.368 32.149 -15.828 1.00 37.09 C ANISOU 1026 CB ASP A 151 5250 4127 4716 -65 -541 753 C ATOM 1027 CG ASP A 151 42.534 32.519 -16.723 1.00 44.93 C ANISOU 1027 CG ASP A 151 6258 5130 5683 -88 -527 774 C ATOM 1028 OD1 ASP A 151 42.293 32.924 -17.876 1.00 52.12 O ANISOU 1028 OD1 ASP A 151 7187 6034 6584 -96 -540 782 O ATOM 1029 OD2 ASP A 151 43.694 32.397 -16.284 1.00 46.64 O ANISOU 1029 OD2 ASP A 151 6469 5361 5891 -98 -502 783 O ATOM 1030 N ALA A 152 38.637 33.001 -13.997 1.00 28.51 N ANISOU 1030 N ALA A 152 4131 2993 3706 -20 -602 705 N ATOM 1031 CA ALA A 152 37.403 32.506 -13.406 1.00 26.83 C ANISOU 1031 CA ALA A 152 3905 2774 3515 3 -613 683 C ATOM 1032 C ALA A 152 36.207 33.418 -13.670 1.00 34.02 C ANISOU 1032 C ALA A 152 4817 3659 4448 10 -648 671 C ATOM 1033 O ALA A 152 35.076 33.062 -13.310 1.00 37.07 O ANISOU 1033 O ALA A 152 5193 4039 4853 29 -659 651 O ATOM 1034 CB ALA A 152 37.590 32.317 -11.891 1.00 27.50 C ANISOU 1034 CB ALA A 152 3966 2861 3622 17 -602 670 C ATOM 1035 N LEU A 153 36.415 34.547 -14.339 1.00 38.79 N ANISOU 1035 N LEU A 153 5435 4252 5051 -5 -666 682 N ATOM 1036 CA LEU A 153 35.354 35.525 -14.583 1.00 34.96 C ANISOU 1036 CA LEU A 153 4952 3743 4586 0 -700 671 C ATOM 1037 C LEU A 153 34.685 35.299 -15.941 1.00 33.53 C ANISOU 1037 C LEU A 153 4791 3560 4389 -4 -712 676 C ATOM 1038 O LEU A 153 34.530 36.222 -16.727 1.00 33.00 O ANISOU 1038 O LEU A 153 4738 3480 4321 -14 -733 683 O ATOM 1039 CB LEU A 153 35.923 36.938 -14.488 1.00 37.09 C ANISOU 1039 CB LEU A 153 5226 4000 4866 -13 -714 680 C ATOM 1040 CG LEU A 153 36.506 37.393 -13.140 1.00 33.58 C ANISOU 1040 CG LEU A 153 4763 3554 4442 -10 -708 674 C ATOM 1041 CD1 LEU A 153 37.136 38.783 -13.251 1.00 24.29 C ANISOU 1041 CD1 LEU A 153 3594 2365 3271 -25 -721 685 C ATOM 1042 CD2 LEU A 153 35.440 37.334 -12.019 1.00 21.05 C ANISOU 1042 CD2 LEU A 153 3154 1957 2887 14 -719 647 C ATOM 1043 N GLN A 154 34.301 34.021 -16.246 1.00 29.02 N ANISOU 1043 N GLN A 154 4220 3002 3805 5 -699 672 N ATOM 1044 CA GLN A 154 33.586 33.750 -17.467 1.00 26.91 C ANISOU 1044 CA GLN A 154 3969 2732 3523 3 -711 674 C ATOM 1045 C GLN A 154 32.092 33.643 -17.184 1.00 34.01 C ANISOU 1045 C GLN A 154 4858 3618 4448 23 -732 651 C ATOM 1046 O GLN A 154 31.693 33.258 -16.082 1.00 40.51 O ANISOU 1046 O GLN A 154 5660 4441 5291 40 -728 634 O ATOM 1047 CB GLN A 154 34.077 32.452 -18.122 1.00 33.89 C ANISOU 1047 CB GLN A 154 4863 3639 4375 -2 -683 685 C ATOM 1048 CG GLN A 154 35.596 32.332 -18.250 1.00 41.23 C ANISOU 1048 CG GLN A 154 5798 4587 5279 -20 -655 706 C ATOM 1049 CD GLN A 154 36.022 31.067 -18.988 1.00 45.17 C ANISOU 1049 CD GLN A 154 6307 5110 5746 -25 -628 716 C ATOM 1050 OE1 GLN A 154 35.304 30.582 -19.857 1.00 48.16 O ANISOU 1050 OE1 GLN A 154 6696 5488 6114 -21 -635 714 O ATOM 1051 NE2 GLN A 154 37.200 30.537 -18.651 1.00 44.69 N ANISOU 1051 NE2 GLN A 154 6243 5070 5668 -33 -596 726 N ATOM 1052 N PRO A 155 31.234 33.976 -18.146 1.00 27.86 N ANISOU 1052 N PRO A 155 4091 2826 3668 22 -756 650 N ATOM 1053 CA PRO A 155 29.794 33.772 -17.951 1.00 34.72 C ANISOU 1053 CA PRO A 155 4950 3683 4559 40 -775 627 C ATOM 1054 C PRO A 155 29.445 32.290 -17.972 1.00 35.43 C ANISOU 1054 C PRO A 155 5035 3788 4638 53 -757 620 C ATOM 1055 O PRO A 155 30.136 31.460 -18.578 1.00 34.57 O ANISOU 1055 O PRO A 155 4937 3697 4500 44 -736 635 O ATOM 1056 CB PRO A 155 29.160 34.494 -19.149 1.00 30.38 C ANISOU 1056 CB PRO A 155 4420 3119 4006 32 -803 632 C ATOM 1057 CG PRO A 155 30.173 34.343 -20.217 1.00 29.58 C ANISOU 1057 CG PRO A 155 4341 3030 3870 13 -789 657 C ATOM 1058 CD PRO A 155 31.530 34.463 -19.504 1.00 31.43 C ANISOU 1058 CD PRO A 155 4569 3276 4098 4 -765 668 C ATOM 1059 N GLY A 156 28.314 31.977 -17.335 1.00 29.76 N ANISOU 1059 N GLY A 156 4300 3063 3945 73 -767 597 N ATOM 1060 CA GLY A 156 27.882 30.592 -17.238 1.00 30.33 C ANISOU 1060 CA GLY A 156 4364 3148 4011 87 -751 587 C ATOM 1061 C GLY A 156 27.760 29.878 -18.574 1.00 28.43 C ANISOU 1061 C GLY A 156 4145 2916 3743 79 -749 599 C ATOM 1062 O GLY A 156 27.902 28.654 -18.628 1.00 34.45 O ANISOU 1062 O GLY A 156 4906 3695 4490 85 -727 599 O ATOM 1063 N ARG A 157 27.536 30.629 -19.669 1.00 23.51 N ANISOU 1063 N ARG A 157 3540 2281 3112 67 -771 608 N ATOM 1064 CA ARG A 157 27.437 30.042 -21.007 1.00 27.55 C ANISOU 1064 CA ARG A 157 4072 2799 3595 60 -770 619 C ATOM 1065 C ARG A 157 28.614 29.153 -21.348 1.00 18.35 C ANISOU 1065 C ARG A 157 2916 1658 2397 49 -738 637 C ATOM 1066 O ARG A 157 28.462 28.202 -22.116 1.00 33.45 O ANISOU 1066 O ARG A 157 4838 3581 4289 49 -729 641 O ATOM 1067 CB ARG A 157 27.370 31.139 -22.092 1.00 27.22 C ANISOU 1067 CB ARG A 157 4051 2743 3547 45 -794 631 C ATOM 1068 CG ARG A 157 26.109 31.966 -22.092 1.00 28.48 C ANISOU 1068 CG ARG A 157 4206 2879 3734 53 -829 615 C ATOM 1069 CD ARG A 157 24.928 31.095 -22.470 1.00 39.13 C ANISOU 1069 CD ARG A 157 5554 4227 5087 67 -837 600 C ATOM 1070 NE ARG A 157 23.669 31.805 -22.289 1.00 40.52 N ANISOU 1070 NE ARG A 157 5722 4382 5292 78 -867 581 N ATOM 1071 CZ ARG A 157 22.507 31.192 -22.117 1.00 43.40 C ANISOU 1071 CZ ARG A 157 6075 4743 5673 94 -875 562 C ATOM 1072 NH1 ARG A 157 22.466 29.861 -22.094 1.00 41.88 N ANISOU 1072 NH1 ARG A 157 5878 4566 5469 103 -855 558 N ATOM 1073 NH2 ARG A 157 21.399 31.909 -21.954 1.00 40.60 N ANISOU 1073 NH2 ARG A 157 5712 4369 5344 102 -902 545 N ATOM 1074 N ASN A 158 29.783 29.433 -20.783 1.00 17.27 N ANISOU 1074 N ASN A 158 2777 1530 2256 39 -719 649 N ATOM 1075 CA ASN A 158 31.027 28.770 -21.161 1.00 27.41 C ANISOU 1075 CA ASN A 158 4071 2838 3507 26 -688 668 C ATOM 1076 C ASN A 158 31.304 27.448 -20.414 1.00 28.96 C ANISOU 1076 C ASN A 158 4253 3054 3697 36 -658 662 C ATOM 1077 O ASN A 158 32.352 26.833 -20.660 1.00 29.21 O ANISOU 1077 O ASN A 158 4291 3107 3702 25 -630 677 O ATOM 1078 CB ASN A 158 32.184 29.754 -20.939 1.00 23.24 C ANISOU 1078 CB ASN A 158 3545 2309 2976 9 -682 682 C ATOM 1079 CG ASN A 158 32.069 30.994 -21.833 1.00 36.53 C ANISOU 1079 CG ASN A 158 5246 3975 4660 -4 -708 691 C ATOM 1080 OD1 ASN A 158 31.069 31.174 -22.535 1.00 48.07 O ANISOU 1080 OD1 ASN A 158 6715 5423 6126 1 -732 685 O ATOM 1081 ND2 ASN A 158 33.066 31.870 -21.775 1.00 23.89 N ANISOU 1081 ND2 ASN A 158 3649 2372 3054 -19 -704 705 N ATOM 1082 N LEU A 159 30.413 26.996 -19.520 1.00 25.84 N ANISOU 1082 N LEU A 159 3838 2653 3326 57 -663 641 N ATOM 1083 CA LEU A 159 30.675 25.810 -18.689 1.00 27.70 C ANISOU 1083 CA LEU A 159 4059 2906 3558 68 -635 635 C ATOM 1084 C LEU A 159 30.811 24.535 -19.525 1.00 32.10 C ANISOU 1084 C LEU A 159 4628 3484 4085 66 -615 642 C ATOM 1085 O LEU A 159 30.087 24.337 -20.501 1.00 24.30 O ANISOU 1085 O LEU A 159 3652 2491 3090 66 -629 641 O ATOM 1086 CB LEU A 159 29.546 25.619 -17.680 1.00 29.98 C ANISOU 1086 CB LEU A 159 4326 3184 3882 93 -647 608 C ATOM 1087 CG LEU A 159 29.526 26.432 -16.384 1.00 29.62 C ANISOU 1087 CG LEU A 159 4260 3127 3868 101 -654 596 C ATOM 1088 CD1 LEU A 159 28.116 26.470 -15.822 1.00 26.76 C ANISOU 1088 CD1 LEU A 159 3880 2749 3539 123 -673 569 C ATOM 1089 CD2 LEU A 159 30.480 25.788 -15.398 1.00 24.24 C ANISOU 1089 CD2 LEU A 159 3566 2463 3182 104 -623 598 C ATOM 1090 N VAL A 160 31.748 23.668 -19.133 1.00 39.18 N ANISOU 1090 N VAL A 160 5520 4403 4963 63 -582 650 N ATOM 1091 CA VAL A 160 31.942 22.361 -19.776 1.00 36.86 C ANISOU 1091 CA VAL A 160 5234 4130 4639 61 -559 656 C ATOM 1092 C VAL A 160 31.153 21.253 -19.085 1.00 32.62 C ANISOU 1092 C VAL A 160 4680 3601 4115 83 -550 634 C ATOM 1093 O VAL A 160 30.648 20.340 -19.739 1.00 27.97 O ANISOU 1093 O VAL A 160 4097 3019 3512 87 -546 632 O ATOM 1094 CB VAL A 160 33.443 22.024 -19.832 1.00 35.87 C ANISOU 1094 CB VAL A 160 5114 4029 4484 44 -525 675 C ATOM 1095 CG1 VAL A 160 33.648 20.596 -20.240 1.00 38.15 C ANISOU 1095 CG1 VAL A 160 5407 4342 4745 44 -497 678 C ATOM 1096 CG2 VAL A 160 34.128 22.908 -20.854 1.00 32.99 C ANISOU 1096 CG2 VAL A 160 4769 3663 4102 22 -529 693 C ATOM 1097 N ALA A 161 31.071 21.284 -17.760 1.00 37.48 N ANISOU 1097 N ALA A 161 5267 4219 4755 96 -538 614 N ATOM 1098 CA ALA A 161 30.246 20.358 -16.997 1.00 28.99 C ANISOU 1098 CA ALA A 161 4166 3152 3696 119 -526 586 C ATOM 1099 C ALA A 161 29.976 21.025 -15.661 1.00 33.70 C ANISOU 1099 C ALA A 161 4739 3738 4328 132 -532 567 C ATOM 1100 O ALA A 161 30.718 21.914 -15.241 1.00 35.85 O ANISOU 1100 O ALA A 161 5011 4005 4605 122 -533 575 O ATOM 1101 CB ALA A 161 30.890 18.972 -16.811 1.00 16.79 C ANISOU 1101 CB ALA A 161 2611 1642 2127 120 -481 581 C ATOM 1102 N ALA A 162 28.866 20.648 -15.043 1.00 32.52 N ANISOU 1102 N ALA A 162 4571 3582 4204 154 -537 541 N ATOM 1103 CA ALA A 162 28.493 21.190 -13.748 1.00 35.92 C ANISOU 1103 CA ALA A 162 4976 4001 4669 169 -542 521 C ATOM 1104 C ALA A 162 27.598 20.168 -13.071 1.00 38.86 C ANISOU 1104 C ALA A 162 5325 4382 5056 192 -528 493 C ATOM 1105 O ALA A 162 27.069 19.253 -13.726 1.00 29.04 O ANISOU 1105 O ALA A 162 4087 3146 3802 196 -525 490 O ATOM 1106 CB ALA A 162 27.777 22.550 -13.866 1.00 13.21 C ANISOU 1106 CB ALA A 162 2109 1090 1819 169 -588 523 C ATOM 1107 N GLY A 163 27.456 20.314 -11.752 1.00 27.60 N ANISOU 1107 N GLY A 163 3874 2956 3657 206 -520 472 N ATOM 1108 CA GLY A 163 26.506 19.496 -11.015 1.00 32.87 C ANISOU 1108 CA GLY A 163 4519 3627 4345 230 -510 444 C ATOM 1109 C GLY A 163 26.636 19.643 -9.501 1.00 34.91 C ANISOU 1109 C GLY A 163 4749 3888 4626 244 -494 425 C ATOM 1110 O GLY A 163 27.165 20.637 -8.985 1.00 32.52 O ANISOU 1110 O GLY A 163 4446 3578 4334 238 -502 430 O ATOM 1111 N TYR A 164 26.111 18.642 -8.804 1.00 25.89 N ANISOU 1111 N TYR A 164 3585 2759 3493 263 -472 401 N ATOM 1112 CA TYR A 164 26.105 18.665 -7.353 1.00 28.41 C ANISOU 1112 CA TYR A 164 3878 3081 3836 278 -456 380 C ATOM 1113 C TYR A 164 26.000 17.246 -6.822 1.00 25.71 C ANISOU 1113 C TYR A 164 3517 2765 3488 293 -419 362 C ATOM 1114 O TYR A 164 25.494 16.344 -7.494 1.00 27.17 O ANISOU 1114 O TYR A 164 3705 2956 3661 296 -414 360 O ATOM 1115 CB TYR A 164 24.956 19.519 -6.811 1.00 29.27 C ANISOU 1115 CB TYR A 164 3977 3159 3984 294 -489 364 C ATOM 1116 CG TYR A 164 23.586 19.117 -7.321 1.00 26.46 C ANISOU 1116 CG TYR A 164 3622 2790 3642 307 -509 352 C ATOM 1117 CD1 TYR A 164 22.842 18.122 -6.681 1.00 19.42 C ANISOU 1117 CD1 TYR A 164 2709 1906 2764 328 -491 327 C ATOM 1118 CD2 TYR A 164 23.034 19.734 -8.447 1.00 21.09 C ANISOU 1118 CD2 TYR A 164 2964 2088 2962 298 -546 366 C ATOM 1119 CE1 TYR A 164 21.575 17.756 -7.142 1.00 22.18 C ANISOU 1119 CE1 TYR A 164 3058 2242 3127 340 -510 316 C ATOM 1120 CE2 TYR A 164 21.765 19.367 -8.928 1.00 29.98 C ANISOU 1120 CE2 TYR A 164 4091 3200 4101 310 -566 355 C ATOM 1121 CZ TYR A 164 21.043 18.379 -8.271 1.00 29.63 C ANISOU 1121 CZ TYR A 164 4024 3165 4071 331 -547 330 C ATOM 1122 OH TYR A 164 19.794 18.024 -8.741 1.00 20.65 O ANISOU 1122 OH TYR A 164 2886 2013 2946 343 -566 319 O ATOM 1123 N ALA A 165 26.476 17.067 -5.595 1.00 27.60 N ANISOU 1123 N ALA A 165 3734 3017 3735 302 -393 348 N ATOM 1124 CA ALA A 165 26.207 15.871 -4.812 1.00 21.34 C ANISOU 1124 CA ALA A 165 2919 2243 2945 320 -360 326 C ATOM 1125 C ALA A 165 25.280 16.282 -3.693 1.00 24.24 C ANISOU 1125 C ALA A 165 3266 2592 3352 342 -372 301 C ATOM 1126 O ALA A 165 25.535 17.276 -3.006 1.00 22.91 O ANISOU 1126 O ALA A 165 3092 2411 3201 342 -383 301 O ATOM 1127 CB ALA A 165 27.483 15.232 -4.244 1.00 14.73 C ANISOU 1127 CB ALA A 165 2073 1437 2086 315 -318 329 C ATOM 1128 N LEU A 166 24.199 15.543 -3.538 1.00 22.24 N ANISOU 1128 N LEU A 166 3000 2336 3114 360 -370 281 N ATOM 1129 CA LEU A 166 23.262 15.753 -2.452 1.00 24.81 C ANISOU 1129 CA LEU A 166 3305 2647 3477 383 -377 256 C ATOM 1130 C LEU A 166 23.480 14.660 -1.407 1.00 29.30 C ANISOU 1130 C LEU A 166 3849 3239 4044 398 -335 236 C ATOM 1131 O LEU A 166 23.434 13.469 -1.735 1.00 19.70 O ANISOU 1131 O LEU A 166 2632 2044 2811 401 -312 233 O ATOM 1132 CB LEU A 166 21.830 15.755 -2.985 1.00 16.92 C ANISOU 1132 CB LEU A 166 2306 1624 2497 394 -407 246 C ATOM 1133 CG LEU A 166 20.740 15.748 -1.940 1.00 23.27 C ANISOU 1133 CG LEU A 166 3087 2414 3339 419 -411 218 C ATOM 1134 CD1 LEU A 166 20.913 16.941 -0.981 1.00 13.48 C ANISOU 1134 CD1 LEU A 166 1840 1158 2123 422 -424 214 C ATOM 1135 CD2 LEU A 166 19.429 15.834 -2.692 1.00 16.07 C ANISOU 1135 CD2 LEU A 166 2182 1481 2442 424 -441 213 C ATOM 1136 N TYR A 167 23.787 15.068 -0.170 1.00 30.65 N ANISOU 1136 N TYR A 167 4004 3410 4232 407 -325 225 N ATOM 1137 CA TYR A 167 23.932 14.140 0.963 1.00 29.92 C ANISOU 1137 CA TYR A 167 3888 3338 4142 424 -287 204 C ATOM 1138 C TYR A 167 22.615 14.151 1.741 1.00 22.89 C ANISOU 1138 C TYR A 167 2979 2429 3289 449 -298 178 C ATOM 1139 O TYR A 167 22.456 14.847 2.741 1.00 24.94 O ANISOU 1139 O TYR A 167 3226 2676 3574 459 -304 166 O ATOM 1140 CB TYR A 167 25.147 14.514 1.836 1.00 22.20 C ANISOU 1140 CB TYR A 167 2903 2373 3157 418 -267 208 C ATOM 1141 CG TYR A 167 26.399 14.809 1.033 1.00 19.35 C ANISOU 1141 CG TYR A 167 2562 2024 2764 392 -264 236 C ATOM 1142 CD1 TYR A 167 27.123 13.789 0.425 1.00 29.36 C ANISOU 1142 CD1 TYR A 167 3837 3320 3998 382 -236 247 C ATOM 1143 CD2 TYR A 167 26.819 16.122 0.817 1.00 21.81 C ANISOU 1143 CD2 TYR A 167 2888 2319 3080 378 -292 253 C ATOM 1144 CE1 TYR A 167 28.264 14.073 -0.350 1.00 23.60 C ANISOU 1144 CE1 TYR A 167 3128 2601 3240 357 -234 273 C ATOM 1145 CE2 TYR A 167 27.951 16.419 0.039 1.00 19.68 C ANISOU 1145 CE2 TYR A 167 2636 2058 2781 353 -290 279 C ATOM 1146 CZ TYR A 167 28.674 15.400 -0.538 1.00 24.25 C ANISOU 1146 CZ TYR A 167 3222 2665 3327 343 -261 289 C ATOM 1147 OH TYR A 167 29.794 15.707 -1.315 1.00 19.47 O ANISOU 1147 OH TYR A 167 2635 2068 2693 319 -260 316 O ATOM 1148 N GLY A 168 21.636 13.397 1.221 1.00 15.01 N ANISOU 1148 N GLY A 168 1980 1429 2296 458 -301 169 N ATOM 1149 CA GLY A 168 20.311 13.299 1.806 1.00 12.04 C ANISOU 1149 CA GLY A 168 1586 1042 1946 475 -304 143 C ATOM 1150 C GLY A 168 20.037 11.969 2.481 1.00 21.14 C ANISOU 1150 C GLY A 168 2718 2218 3095 490 -264 123 C ATOM 1151 O GLY A 168 20.910 11.428 3.168 1.00 18.48 O ANISOU 1151 O GLY A 168 2373 1899 2751 496 -235 120 O ATOM 1152 N SER A 169 18.830 11.421 2.283 1.00 23.77 N ANISOU 1152 N SER A 169 3045 2554 3434 494 -261 108 N ATOM 1153 CA SER A 169 18.555 10.072 2.777 1.00 24.62 C ANISOU 1153 CA SER A 169 3135 2684 3534 505 -223 91 C ATOM 1154 C SER A 169 19.462 9.046 2.103 1.00 24.70 C ANISOU 1154 C SER A 169 3154 2705 3525 510 -211 103 C ATOM 1155 O SER A 169 19.834 8.038 2.720 1.00 26.76 O ANISOU 1155 O SER A 169 3401 2989 3777 519 -174 93 O ATOM 1156 CB SER A 169 17.080 9.722 2.581 1.00 16.64 C ANISOU 1156 CB SER A 169 2118 1672 2532 507 -226 76 C ATOM 1157 OG SER A 169 16.720 9.722 1.213 1.00 27.81 O ANISOU 1157 OG SER A 169 3550 3072 3945 502 -256 88 O ATOM 1158 N ALA A 170 19.850 9.298 0.854 1.00 16.95 N ANISOU 1158 N ALA A 170 2196 1717 2528 496 -234 127 N ATOM 1159 CA ALA A 170 20.969 8.616 0.229 1.00 21.43 C ANISOU 1159 CA ALA A 170 2775 2312 3055 479 -209 144 C ATOM 1160 C ALA A 170 21.856 9.686 -0.385 1.00 23.88 C ANISOU 1160 C ALA A 170 3107 2617 3350 455 -229 171 C ATOM 1161 O ALA A 170 21.491 10.863 -0.429 1.00 19.33 O ANISOU 1161 O ALA A 170 2537 2014 2793 453 -264 174 O ATOM 1162 CB ALA A 170 20.519 7.593 -0.833 1.00 17.57 C ANISOU 1162 CB ALA A 170 2295 1832 2549 476 -206 147 C ATOM 1163 N THR A 171 23.039 9.275 -0.833 1.00 22.00 N ANISOU 1163 N THR A 171 2879 2403 3076 438 -207 188 N ATOM 1164 CA THR A 171 23.985 10.165 -1.497 1.00 24.95 C ANISOU 1164 CA THR A 171 3274 2774 3431 414 -222 215 C ATOM 1165 C THR A 171 23.847 9.958 -3.006 1.00 23.32 C ANISOU 1165 C THR A 171 3091 2566 3202 399 -238 233 C ATOM 1166 O THR A 171 23.877 8.817 -3.482 1.00 22.12 O ANISOU 1166 O THR A 171 2941 2434 3031 399 -216 233 O ATOM 1167 CB THR A 171 25.424 9.903 -1.045 1.00 30.08 C ANISOU 1167 CB THR A 171 3922 3452 4056 404 -187 224 C ATOM 1168 OG1 THR A 171 25.566 10.230 0.344 1.00 29.62 O ANISOU 1168 OG1 THR A 171 3844 3392 4019 418 -176 208 O ATOM 1169 CG2 THR A 171 26.399 10.768 -1.851 1.00 30.29 C ANISOU 1169 CG2 THR A 171 3972 3476 4062 379 -202 252 C ATOM 1170 N MET A 172 23.582 11.038 -3.739 1.00 23.17 N ANISOU 1170 N MET A 172 3090 2524 3190 388 -277 248 N ATOM 1171 CA MET A 172 23.445 10.990 -5.192 1.00 22.95 C ANISOU 1171 CA MET A 172 3087 2492 3143 374 -296 266 C ATOM 1172 C MET A 172 24.317 12.053 -5.859 1.00 23.77 C ANISOU 1172 C MET A 172 3213 2588 3230 350 -315 294 C ATOM 1173 O MET A 172 24.425 13.179 -5.365 1.00 25.52 O ANISOU 1173 O MET A 172 3434 2793 3471 349 -333 295 O ATOM 1174 CB MET A 172 21.987 11.187 -5.622 1.00 21.19 C ANISOU 1174 CB MET A 172 2866 2242 2945 385 -330 256 C ATOM 1175 CG MET A 172 21.839 11.318 -7.127 1.00 29.53 C ANISOU 1175 CG MET A 172 3948 3289 3982 370 -355 276 C ATOM 1176 SD MET A 172 20.138 11.308 -7.680 1.00 34.11 S ANISOU 1176 SD MET A 172 4529 3842 4588 384 -390 263 S ATOM 1177 CE MET A 172 19.789 9.549 -7.605 1.00 31.60 C ANISOU 1177 CE MET A 172 4196 3550 4260 398 -354 246 C ATOM 1178 N LEU A 173 24.918 11.694 -6.996 1.00 24.38 N ANISOU 1178 N LEU A 173 3311 2677 3274 332 -310 315 N ATOM 1179 CA LEU A 173 25.677 12.620 -7.828 1.00 31.12 C ANISOU 1179 CA LEU A 173 4190 3525 4111 309 -329 342 C ATOM 1180 C LEU A 173 24.899 12.897 -9.107 1.00 32.65 C ANISOU 1180 C LEU A 173 4405 3698 4303 303 -364 353 C ATOM 1181 O LEU A 173 24.623 11.974 -9.886 1.00 26.12 O ANISOU 1181 O LEU A 173 3585 2881 3458 303 -357 355 O ATOM 1182 CB LEU A 173 27.055 12.075 -8.187 1.00 34.71 C ANISOU 1182 CB LEU A 173 4654 4008 4528 292 -297 361 C ATOM 1183 CG LEU A 173 27.934 13.193 -8.748 1.00 34.82 C ANISOU 1183 CG LEU A 173 4689 4014 4529 269 -314 387 C ATOM 1184 CD1 LEU A 173 28.387 14.073 -7.617 1.00 27.86 C ANISOU 1184 CD1 LEU A 173 3793 3125 3666 272 -314 382 C ATOM 1185 CD2 LEU A 173 29.108 12.608 -9.446 1.00 40.92 C ANISOU 1185 CD2 LEU A 173 5475 4811 5262 250 -289 408 C ATOM 1186 N VAL A 174 24.592 14.173 -9.323 1.00 25.66 N ANISOU 1186 N VAL A 174 3530 2785 3434 298 -401 361 N ATOM 1187 CA VAL A 174 23.894 14.676 -10.497 1.00 26.02 C ANISOU 1187 CA VAL A 174 3597 2808 3480 291 -439 372 C ATOM 1188 C VAL A 174 24.920 15.381 -11.371 1.00 28.99 C ANISOU 1188 C VAL A 174 4000 3185 3830 266 -448 403 C ATOM 1189 O VAL A 174 25.497 16.399 -10.967 1.00 30.08 O ANISOU 1189 O VAL A 174 4139 3314 3975 258 -456 411 O ATOM 1190 CB VAL A 174 22.767 15.631 -10.083 1.00 26.19 C ANISOU 1190 CB VAL A 174 3612 2798 3541 305 -476 359 C ATOM 1191 CG1 VAL A 174 22.141 16.278 -11.291 1.00 22.35 C ANISOU 1191 CG1 VAL A 174 3150 2287 3054 296 -517 373 C ATOM 1192 CG2 VAL A 174 21.725 14.880 -9.214 1.00 15.49 C ANISOU 1192 CG2 VAL A 174 2231 1443 2212 330 -466 328 C ATOM 1193 N LEU A 175 25.127 14.865 -12.576 1.00 28.43 N ANISOU 1193 N LEU A 175 3950 3123 3730 254 -447 419 N ATOM 1194 CA LEU A 175 26.151 15.377 -13.481 1.00 23.97 C ANISOU 1194 CA LEU A 175 3411 2561 3137 229 -451 449 C ATOM 1195 C LEU A 175 25.489 15.906 -14.739 1.00 22.49 C ANISOU 1195 C LEU A 175 3249 2351 2947 222 -489 462 C ATOM 1196 O LEU A 175 24.736 15.179 -15.391 1.00 29.00 O ANISOU 1196 O LEU A 175 4079 3175 3766 228 -494 457 O ATOM 1197 CB LEU A 175 27.172 14.302 -13.839 1.00 19.88 C ANISOU 1197 CB LEU A 175 2897 2075 2581 219 -412 459 C ATOM 1198 CG LEU A 175 28.229 14.846 -14.798 1.00 27.09 C ANISOU 1198 CG LEU A 175 3837 2990 3464 193 -416 490 C ATOM 1199 CD1 LEU A 175 28.943 16.056 -14.169 1.00 17.74 C ANISOU 1199 CD1 LEU A 175 2651 1797 2292 185 -423 498 C ATOM 1200 CD2 LEU A 175 29.247 13.756 -15.217 1.00 28.62 C ANISOU 1200 CD2 LEU A 175 4037 3217 3620 182 -377 502 C ATOM 1201 N ALA A 176 25.729 17.174 -15.056 1.00 22.86 N ANISOU 1201 N ALA A 176 3311 2376 2997 210 -517 478 N ATOM 1202 CA ALA A 176 25.209 17.769 -16.284 1.00 28.91 C ANISOU 1202 CA ALA A 176 4104 3120 3759 201 -555 494 C ATOM 1203 C ALA A 176 26.350 18.118 -17.234 1.00 31.22 C ANISOU 1203 C ALA A 176 4424 3420 4018 176 -552 525 C ATOM 1204 O ALA A 176 27.319 18.791 -16.840 1.00 25.71 O ANISOU 1204 O ALA A 176 3727 2726 3317 164 -544 536 O ATOM 1205 CB ALA A 176 24.360 19.006 -15.982 1.00 35.21 C ANISOU 1205 CB ALA A 176 4901 3886 4593 208 -595 487 C ATOM 1206 N MET A 177 26.233 17.650 -18.480 1.00 30.95 N ANISOU 1206 N MET A 177 4412 3388 3959 168 -558 538 N ATOM 1207 CA MET A 177 27.158 18.011 -19.552 1.00 29.56 C ANISOU 1207 CA MET A 177 4265 3214 3751 144 -560 568 C ATOM 1208 C MET A 177 26.337 18.261 -20.811 1.00 37.06 C ANISOU 1208 C MET A 177 5241 4144 4698 141 -596 578 C ATOM 1209 O MET A 177 25.104 18.218 -20.782 1.00 41.14 O ANISOU 1209 O MET A 177 5751 4644 5237 157 -619 561 O ATOM 1210 CB MET A 177 28.197 16.904 -19.787 1.00 24.21 C ANISOU 1210 CB MET A 177 3590 2571 3039 135 -518 578 C ATOM 1211 CG MET A 177 28.715 16.262 -18.529 1.00 32.65 C ANISOU 1211 CG MET A 177 4629 3663 4112 143 -480 561 C ATOM 1212 SD MET A 177 30.079 15.157 -18.842 1.00 43.66 S ANISOU 1212 SD MET A 177 6028 5095 5464 129 -432 576 S ATOM 1213 CE MET A 177 29.203 13.613 -19.014 1.00 43.57 C ANISOU 1213 CE MET A 177 6008 5100 5448 146 -417 556 C ATOM 1214 N ASP A 178 27.019 18.452 -21.947 1.00 45.88 N ANISOU 1214 N ASP A 178 6382 5266 5784 121 -596 601 N ATOM 1215 CA ASP A 178 26.295 18.672 -23.199 1.00 48.75 C ANISOU 1215 CA ASP A 178 6763 5620 6142 116 -619 603 C ATOM 1216 C ASP A 178 25.369 17.504 -23.525 1.00 39.10 C ANISOU 1216 C ASP A 178 5538 4401 4917 131 -619 590 C ATOM 1217 O ASP A 178 24.256 17.711 -24.010 1.00 21.82 O ANISOU 1217 O ASP A 178 3352 2196 2743 138 -646 579 O ATOM 1218 CB ASP A 178 27.269 18.908 -24.353 1.00 64.05 C ANISOU 1218 CB ASP A 178 8724 7568 8044 93 -610 627 C ATOM 1219 CG ASP A 178 26.556 19.202 -25.676 1.00 77.52 C ANISOU 1219 CG ASP A 178 10449 9262 9744 88 -635 629 C ATOM 1220 OD1 ASP A 178 25.993 20.309 -25.814 1.00 80.92 O ANISOU 1220 OD1 ASP A 178 10881 9670 10193 87 -665 625 O ATOM 1221 OD2 ASP A 178 26.572 18.335 -26.581 1.00 80.86 O ANISOU 1221 OD2 ASP A 178 10884 9699 10142 84 -624 635 O ATOM 1222 N CYS A 179 25.768 16.273 -23.198 1.00 42.93 N ANISOU 1222 N CYS A 179 6018 4906 5386 136 -590 590 N ATOM 1223 CA CYS A 179 24.883 15.170 -23.545 1.00 41.69 C ANISOU 1223 CA CYS A 179 5859 4755 5228 150 -589 577 C ATOM 1224 C CYS A 179 23.641 15.107 -22.670 1.00 49.31 C ANISOU 1224 C CYS A 179 6798 5706 6231 173 -602 548 C ATOM 1225 O CYS A 179 22.782 14.258 -22.929 1.00 57.91 O ANISOU 1225 O CYS A 179 7883 6797 7323 186 -603 534 O ATOM 1226 CB CYS A 179 25.607 13.831 -23.476 1.00 42.14 C ANISOU 1226 CB CYS A 179 5908 4846 5257 148 -543 576 C ATOM 1227 SG CYS A 179 26.183 13.348 -21.868 1.00 51.62 S ANISOU 1227 SG CYS A 179 7073 6069 6470 158 -502 557 S ATOM 1228 N GLY A 180 23.534 15.944 -21.634 1.00 43.17 N ANISOU 1228 N GLY A 180 6003 4915 5483 180 -610 537 N ATOM 1229 CA GLY A 180 22.360 15.931 -20.776 1.00 36.02 C ANISOU 1229 CA GLY A 180 5074 3997 4617 202 -622 509 C ATOM 1230 C GLY A 180 22.688 15.714 -19.306 1.00 30.11 C ANISOU 1230 C GLY A 180 4294 3262 3885 213 -593 491 C ATOM 1231 O GLY A 180 23.848 15.861 -18.916 1.00 23.05 O ANISOU 1231 O GLY A 180 3398 2384 2976 202 -569 501 O ATOM 1232 N VAL A 181 21.680 15.374 -18.493 1.00 26.89 N ANISOU 1232 N VAL A 181 3861 2849 3508 235 -594 464 N ATOM 1233 CA VAL A 181 21.808 15.219 -17.043 1.00 30.58 C ANISOU 1233 CA VAL A 181 4298 3326 3996 248 -570 444 C ATOM 1234 C VAL A 181 21.610 13.754 -16.659 1.00 29.95 C ANISOU 1234 C VAL A 181 4200 3270 3911 261 -536 425 C ATOM 1235 O VAL A 181 20.657 13.104 -17.106 1.00 26.26 O ANISOU 1235 O VAL A 181 3732 2798 3448 272 -545 415 O ATOM 1236 CB VAL A 181 20.811 16.106 -16.277 1.00 34.00 C ANISOU 1236 CB VAL A 181 4717 3731 4472 263 -600 426 C ATOM 1237 CG1 VAL A 181 21.005 15.940 -14.739 1.00 22.58 C ANISOU 1237 CG1 VAL A 181 3239 2295 3045 277 -573 405 C ATOM 1238 CG2 VAL A 181 20.945 17.555 -16.697 1.00 17.22 C ANISOU 1238 CG2 VAL A 181 2610 1580 2352 250 -635 444 C ATOM 1239 N ASN A 182 22.499 13.249 -15.814 1.00 28.42 N ANISOU 1239 N ASN A 182 3990 3102 3708 261 -497 421 N ATOM 1240 CA ASN A 182 22.441 11.883 -15.327 1.00 25.11 C ANISOU 1240 CA ASN A 182 3550 2706 3282 273 -461 404 C ATOM 1241 C ASN A 182 22.631 11.812 -13.813 1.00 31.12 C ANISOU 1241 C ASN A 182 4282 3476 4065 287 -437 385 C ATOM 1242 O ASN A 182 23.439 12.548 -13.229 1.00 29.86 O ANISOU 1242 O ASN A 182 4121 3318 3907 279 -432 392 O ATOM 1243 CB ASN A 182 23.467 11.040 -16.053 1.00 20.43 C ANISOU 1243 CB ASN A 182 2973 2142 2649 258 -432 422 C ATOM 1244 CG ASN A 182 23.085 10.832 -17.495 1.00 30.55 C ANISOU 1244 CG ASN A 182 4281 3417 3911 249 -452 436 C ATOM 1245 OD1 ASN A 182 22.257 9.981 -17.780 1.00 30.22 O ANISOU 1245 OD1 ASN A 182 4234 3377 3872 261 -452 424 O ATOM 1246 ND2 ASN A 182 23.665 11.613 -18.414 1.00 27.05 N ANISOU 1246 ND2 ASN A 182 3864 2965 3448 229 -470 462 N ATOM 1247 N CYS A 183 21.883 10.900 -13.192 1.00 31.76 N ANISOU 1247 N CYS A 183 4342 3564 4162 306 -422 360 N ATOM 1248 CA CYS A 183 21.798 10.757 -11.744 1.00 24.29 C ANISOU 1248 CA CYS A 183 3367 2624 3240 323 -401 338 C ATOM 1249 C CYS A 183 22.391 9.412 -11.345 1.00 26.08 C ANISOU 1249 C CYS A 183 3579 2884 3446 327 -354 330 C ATOM 1250 O CYS A 183 22.035 8.376 -11.922 1.00 24.31 O ANISOU 1250 O CYS A 183 3358 2671 3208 330 -344 327 O ATOM 1251 CB CYS A 183 20.348 10.852 -11.282 1.00 26.22 C ANISOU 1251 CB CYS A 183 3594 2845 3522 345 -423 313 C ATOM 1252 SG CYS A 183 19.478 12.335 -11.909 1.00 29.06 S ANISOU 1252 SG CYS A 183 3971 3164 3905 342 -481 321 S ATOM 1253 N PHE A 184 23.324 9.438 -10.395 1.00 24.55 N ANISOU 1253 N PHE A 184 3373 2706 3249 326 -327 329 N ATOM 1254 CA PHE A 184 24.034 8.254 -9.923 1.00 21.44 C ANISOU 1254 CA PHE A 184 2966 2345 2835 328 -281 323 C ATOM 1255 C PHE A 184 23.839 8.081 -8.411 1.00 25.75 C ANISOU 1255 C PHE A 184 3481 2894 3406 348 -261 298 C ATOM 1256 O PHE A 184 23.961 9.043 -7.646 1.00 22.63 O ANISOU 1256 O PHE A 184 3079 2486 3032 350 -272 295 O ATOM 1257 CB PHE A 184 25.516 8.354 -10.263 1.00 21.76 C ANISOU 1257 CB PHE A 184 3021 2406 2843 306 -262 347 C ATOM 1258 CG PHE A 184 25.807 8.528 -11.741 1.00 23.61 C ANISOU 1258 CG PHE A 184 3285 2636 3048 286 -279 373 C ATOM 1259 CD1 PHE A 184 26.189 7.441 -12.521 1.00 29.86 C ANISOU 1259 CD1 PHE A 184 4087 3450 3808 279 -256 382 C ATOM 1260 CD2 PHE A 184 25.716 9.785 -12.343 1.00 23.25 C ANISOU 1260 CD2 PHE A 184 3259 2566 3009 275 -317 389 C ATOM 1261 CE1 PHE A 184 26.475 7.603 -13.891 1.00 34.84 C ANISOU 1261 CE1 PHE A 184 4747 4079 4413 260 -272 406 C ATOM 1262 CE2 PHE A 184 25.990 9.960 -13.706 1.00 25.44 C ANISOU 1262 CE2 PHE A 184 3565 2839 3260 256 -332 413 C ATOM 1263 CZ PHE A 184 26.381 8.872 -14.490 1.00 22.80 C ANISOU 1263 CZ PHE A 184 3241 2528 2894 249 -310 422 C ATOM 1264 N MET A 185 23.498 6.865 -7.988 1.00 22.47 N ANISOU 1264 N MET A 185 3049 2496 2992 363 -233 280 N ATOM 1265 CA MET A 185 23.278 6.536 -6.584 1.00 19.22 C ANISOU 1265 CA MET A 185 2610 2091 2603 383 -211 255 C ATOM 1266 C MET A 185 24.533 5.878 -5.993 1.00 27.17 C ANISOU 1266 C MET A 185 3608 3129 3586 378 -167 258 C ATOM 1267 O MET A 185 25.048 4.904 -6.546 1.00 29.19 O ANISOU 1267 O MET A 185 3871 3409 3813 370 -143 266 O ATOM 1268 CB MET A 185 22.047 5.629 -6.454 1.00 20.47 C ANISOU 1268 CB MET A 185 2753 2246 2779 403 -208 232 C ATOM 1269 CG MET A 185 21.565 5.498 -5.021 1.00 27.01 C ANISOU 1269 CG MET A 185 3553 3072 3638 426 -194 205 C ATOM 1270 SD MET A 185 20.711 6.980 -4.419 1.00 30.33 S ANISOU 1270 SD MET A 185 3968 3454 4101 435 -235 196 S ATOM 1271 CE MET A 185 19.023 6.773 -4.950 1.00 15.66 C ANISOU 1271 CE MET A 185 2109 1573 2269 450 -265 181 C ATOM 1272 N LEU A 186 25.050 6.420 -4.893 1.00 27.89 N ANISOU 1272 N LEU A 186 3686 3221 3690 382 -158 252 N ATOM 1273 CA LEU A 186 26.225 5.815 -4.255 1.00 31.11 C ANISOU 1273 CA LEU A 186 4085 3659 4078 378 -117 253 C ATOM 1274 C LEU A 186 25.815 4.532 -3.535 1.00 22.01 C ANISOU 1274 C LEU A 186 2911 2524 2930 398 -84 230 C ATOM 1275 O LEU A 186 24.904 4.563 -2.710 1.00 23.36 O ANISOU 1275 O LEU A 186 3062 2681 3130 418 -89 207 O ATOM 1276 CB LEU A 186 26.879 6.792 -3.273 1.00 16.86 C ANISOU 1276 CB LEU A 186 2272 1848 2284 377 -118 253 C ATOM 1277 CG LEU A 186 28.088 6.264 -2.469 1.00 16.80 C ANISOU 1277 CG LEU A 186 2253 1870 2260 375 -76 253 C ATOM 1278 CD1 LEU A 186 29.253 5.814 -3.373 1.00 11.87 C ANISOU 1278 CD1 LEU A 186 1646 1269 1595 353 -58 277 C ATOM 1279 CD2 LEU A 186 28.584 7.290 -1.467 1.00 16.07 C ANISOU 1279 CD2 LEU A 186 2152 1769 2184 376 -81 251 C ATOM 1280 N ASP A 187 26.439 3.384 -3.894 1.00 24.56 N ANISOU 1280 N ASP A 187 3236 2876 3222 392 -51 235 N ATOM 1281 CA ASP A 187 26.259 2.113 -3.178 1.00 25.05 C ANISOU 1281 CA ASP A 187 3276 2957 3283 410 -15 214 C ATOM 1282 C ASP A 187 27.370 1.996 -2.150 1.00 25.87 C ANISOU 1282 C ASP A 187 3368 3083 3379 410 18 212 C ATOM 1283 O ASP A 187 28.521 1.714 -2.514 1.00 28.01 O ANISOU 1283 O ASP A 187 3648 3375 3619 393 38 229 O ATOM 1284 CB ASP A 187 26.285 0.886 -4.103 1.00 27.38 C ANISOU 1284 CB ASP A 187 3580 3273 3551 405 3 220 C ATOM 1285 CG ASP A 187 25.906 -0.435 -3.371 1.00 38.13 C ANISOU 1285 CG ASP A 187 4919 4653 4916 425 38 196 C ATOM 1286 OD1 ASP A 187 26.043 -0.537 -2.125 1.00 30.76 O ANISOU 1286 OD1 ASP A 187 3965 3725 3997 438 59 180 O ATOM 1287 OD2 ASP A 187 25.451 -1.386 -4.052 1.00 37.69 O ANISOU 1287 OD2 ASP A 187 4867 4605 4849 427 45 194 O ATOM 1288 N PRO A 188 27.082 2.240 -0.869 1.00 24.55 N ANISOU 1288 N PRO A 188 3180 2910 3239 427 24 192 N ATOM 1289 CA PRO A 188 28.159 2.255 0.129 1.00 23.16 C ANISOU 1289 CA PRO A 188 2992 2751 3056 427 52 191 C ATOM 1290 C PRO A 188 28.745 0.877 0.432 1.00 27.01 C ANISOU 1290 C PRO A 188 3470 3272 3521 431 97 185 C ATOM 1291 O PRO A 188 29.828 0.814 1.030 1.00 22.44 O ANISOU 1291 O PRO A 188 2887 2712 2929 426 122 188 O ATOM 1292 CB PRO A 188 27.493 2.873 1.372 1.00 22.84 C ANISOU 1292 CB PRO A 188 2933 2692 3053 447 42 169 C ATOM 1293 CG PRO A 188 26.047 2.678 1.183 1.00 25.03 C ANISOU 1293 CG PRO A 188 3205 2949 3354 462 23 154 C ATOM 1294 CD PRO A 188 25.769 2.575 -0.297 1.00 22.91 C ANISOU 1294 CD PRO A 188 2958 2676 3069 448 3 171 C ATOM 1295 N ALA A 189 28.100 -0.221 0.027 1.00 24.62 N ANISOU 1295 N ALA A 189 3164 2977 3212 439 109 176 N ATOM 1296 CA ALA A 189 28.694 -1.532 0.284 1.00 20.65 C ANISOU 1296 CA ALA A 189 2653 2507 2687 442 153 171 C ATOM 1297 C ALA A 189 29.925 -1.770 -0.582 1.00 27.89 C ANISOU 1297 C ALA A 189 3588 3445 3565 419 167 196 C ATOM 1298 O ALA A 189 30.811 -2.551 -0.211 1.00 38.70 O ANISOU 1298 O ALA A 189 4950 4842 4913 417 204 197 O ATOM 1299 CB ALA A 189 27.664 -2.632 0.045 1.00 12.71 C ANISOU 1299 CB ALA A 189 1640 1504 1686 457 161 155 C ATOM 1300 N ILE A 190 30.009 -1.106 -1.735 1.00 28.69 N ANISOU 1300 N ILE A 190 3712 3535 3656 400 138 218 N ATOM 1301 CA ILE A 190 31.133 -1.283 -2.645 1.00 27.23 C ANISOU 1301 CA ILE A 190 3546 3368 3434 377 149 243 C ATOM 1302 C ILE A 190 31.749 0.036 -3.076 1.00 30.67 C ANISOU 1302 C ILE A 190 3999 3788 3866 358 122 265 C ATOM 1303 O ILE A 190 32.735 0.030 -3.816 1.00 30.50 O ANISOU 1303 O ILE A 190 3994 3780 3816 338 130 288 O ATOM 1304 CB ILE A 190 30.741 -2.119 -3.883 1.00 26.58 C ANISOU 1304 CB ILE A 190 3478 3292 3331 371 148 251 C ATOM 1305 CG1 ILE A 190 29.582 -1.473 -4.634 1.00 19.73 C ANISOU 1305 CG1 ILE A 190 2622 2394 2482 372 106 252 C ATOM 1306 CG2 ILE A 190 30.394 -3.548 -3.478 1.00 30.33 C ANISOU 1306 CG2 ILE A 190 3936 3786 3802 388 182 232 C ATOM 1307 CD1 ILE A 190 29.262 -2.154 -5.982 1.00 25.20 C ANISOU 1307 CD1 ILE A 190 3331 3090 3152 364 100 263 C ATOM 1308 N GLY A 191 31.199 1.170 -2.638 1.00 26.77 N ANISOU 1308 N GLY A 191 3502 3268 3402 363 92 260 N ATOM 1309 CA GLY A 191 31.744 2.466 -2.991 1.00 25.22 C ANISOU 1309 CA GLY A 191 3322 3056 3206 346 65 279 C ATOM 1310 C GLY A 191 31.720 2.785 -4.472 1.00 28.42 C ANISOU 1310 C GLY A 191 3753 3452 3592 327 41 303 C ATOM 1311 O GLY A 191 32.711 3.286 -5.009 1.00 34.38 O ANISOU 1311 O GLY A 191 4525 4212 4328 306 39 325 O ATOM 1312 N GLU A 192 30.580 2.553 -5.133 1.00 31.47 N ANISOU 1312 N GLU A 192 4146 3825 3989 334 20 297 N ATOM 1313 CA GLU A 192 30.400 2.859 -6.547 1.00 31.22 C ANISOU 1313 CA GLU A 192 4140 3781 3942 318 -6 318 C ATOM 1314 C GLU A 192 29.137 3.679 -6.752 1.00 25.54 C ANISOU 1314 C GLU A 192 3423 3028 3253 326 -49 310 C ATOM 1315 O GLU A 192 28.107 3.407 -6.131 1.00 25.46 O ANISOU 1315 O GLU A 192 3395 3009 3269 347 -52 287 O ATOM 1316 CB GLU A 192 30.270 1.587 -7.409 1.00 26.44 C ANISOU 1316 CB GLU A 192 3541 3194 3311 316 11 320 C ATOM 1317 CG GLU A 192 31.502 0.816 -7.646 1.00 20.26 C ANISOU 1317 CG GLU A 192 2763 2442 2492 303 47 334 C ATOM 1318 CD GLU A 192 32.455 1.541 -8.536 1.00 33.13 C ANISOU 1318 CD GLU A 192 4417 4071 4099 278 36 363 C ATOM 1319 OE1 GLU A 192 32.005 2.369 -9.333 1.00 42.30 O ANISOU 1319 OE1 GLU A 192 5597 5210 5266 270 0 374 O ATOM 1320 OE2 GLU A 192 33.666 1.286 -8.442 1.00 43.35 O ANISOU 1320 OE2 GLU A 192 5713 5387 5369 266 63 374 O ATOM 1321 N PHE A 193 29.211 4.638 -7.676 1.00 26.23 N ANISOU 1321 N PHE A 193 3533 3097 3335 310 -81 331 N ATOM 1322 CA PHE A 193 28.051 5.421 -8.102 1.00 25.41 C ANISOU 1322 CA PHE A 193 3436 2962 3256 315 -124 328 C ATOM 1323 C PHE A 193 27.388 4.669 -9.248 1.00 26.07 C ANISOU 1323 C PHE A 193 3534 3046 3326 314 -131 331 C ATOM 1324 O PHE A 193 27.944 4.593 -10.342 1.00 30.86 O ANISOU 1324 O PHE A 193 4162 3659 3904 296 -133 354 O ATOM 1325 CB PHE A 193 28.473 6.823 -8.552 1.00 22.04 C ANISOU 1325 CB PHE A 193 3028 2515 2830 298 -155 349 C ATOM 1326 CG PHE A 193 28.835 7.767 -7.419 1.00 26.32 C ANISOU 1326 CG PHE A 193 3557 3049 3394 301 -158 343 C ATOM 1327 CD1 PHE A 193 27.849 8.498 -6.752 1.00 31.12 C ANISOU 1327 CD1 PHE A 193 4153 3631 4039 316 -183 326 C ATOM 1328 CD2 PHE A 193 30.156 7.935 -7.034 1.00 21.46 C ANISOU 1328 CD2 PHE A 193 2942 2451 2762 289 -135 354 C ATOM 1329 CE1 PHE A 193 28.176 9.383 -5.722 1.00 17.75 C ANISOU 1329 CE1 PHE A 193 2450 1930 2366 320 -187 321 C ATOM 1330 CE2 PHE A 193 30.489 8.807 -6.012 1.00 21.48 C ANISOU 1330 CE2 PHE A 193 2932 2445 2783 292 -138 349 C ATOM 1331 CZ PHE A 193 29.489 9.539 -5.353 1.00 19.47 C ANISOU 1331 CZ PHE A 193 2667 2166 2567 308 -165 332 C ATOM 1332 N ILE A 194 26.177 4.168 -9.015 1.00 23.44 N ANISOU 1332 N ILE A 194 3187 2704 3015 333 -137 310 N ATOM 1333 CA ILE A 194 25.453 3.310 -9.951 1.00 24.98 C ANISOU 1333 CA ILE A 194 3390 2900 3200 336 -141 308 C ATOM 1334 C ILE A 194 24.478 4.175 -10.743 1.00 32.23 C ANISOU 1334 C ILE A 194 4324 3788 4136 335 -188 313 C ATOM 1335 O ILE A 194 23.710 4.949 -10.153 1.00 24.12 O ANISOU 1335 O ILE A 194 3287 2736 3141 346 -212 300 O ATOM 1336 CB ILE A 194 24.707 2.193 -9.190 1.00 30.38 C ANISOU 1336 CB ILE A 194 4049 3594 3899 359 -118 281 C ATOM 1337 CG1 ILE A 194 25.660 1.383 -8.320 1.00 23.30 C ANISOU 1337 CG1 ILE A 194 3137 2729 2988 361 -72 275 C ATOM 1338 CG2 ILE A 194 23.896 1.293 -10.124 1.00 30.23 C ANISOU 1338 CG2 ILE A 194 4037 3576 3872 363 -123 278 C ATOM 1339 CD1 ILE A 194 26.681 0.580 -9.114 1.00 24.05 C ANISOU 1339 CD1 ILE A 194 3247 2851 3041 345 -46 294 C ATOM 1340 N LEU A 195 24.482 4.036 -12.077 1.00 30.08 N ANISOU 1340 N LEU A 195 4076 3514 3840 321 -202 331 N ATOM 1341 CA LEU A 195 23.583 4.839 -12.905 1.00 23.93 C ANISOU 1341 CA LEU A 195 3313 2704 3074 319 -247 337 C ATOM 1342 C LEU A 195 22.146 4.365 -12.703 1.00 29.96 C ANISOU 1342 C LEU A 195 4062 3455 3865 341 -259 312 C ATOM 1343 O LEU A 195 21.844 3.188 -12.919 1.00 32.59 O ANISOU 1343 O LEU A 195 4390 3803 4189 348 -240 303 O ATOM 1344 CB LEU A 195 23.969 4.740 -14.379 1.00 24.42 C ANISOU 1344 CB LEU A 195 3405 2770 3103 300 -257 362 C ATOM 1345 CG LEU A 195 23.095 5.481 -15.410 1.00 23.85 C ANISOU 1345 CG LEU A 195 3353 2668 3039 296 -303 370 C ATOM 1346 CD1 LEU A 195 23.122 6.977 -15.159 1.00 21.56 C ANISOU 1346 CD1 LEU A 195 3069 2354 2769 291 -334 377 C ATOM 1347 CD2 LEU A 195 23.542 5.201 -16.836 1.00 29.59 C ANISOU 1347 CD2 LEU A 195 4110 3403 3730 278 -307 394 C ATOM 1348 N VAL A 196 21.268 5.261 -12.258 1.00 18.91 N ANISOU 1348 N VAL A 196 2656 2028 2502 351 -290 301 N ATOM 1349 CA VAL A 196 19.890 4.888 -11.958 1.00 22.97 C ANISOU 1349 CA VAL A 196 3154 2528 3046 373 -301 276 C ATOM 1350 C VAL A 196 18.858 5.731 -12.702 1.00 26.00 C ANISOU 1350 C VAL A 196 3551 2879 3448 373 -349 279 C ATOM 1351 O VAL A 196 17.718 5.263 -12.866 1.00 26.26 O ANISOU 1351 O VAL A 196 3578 2902 3499 387 -361 263 O ATOM 1352 CB VAL A 196 19.605 4.960 -10.436 1.00 24.26 C ANISOU 1352 CB VAL A 196 3287 2689 3240 392 -287 252 C ATOM 1353 CG1 VAL A 196 20.478 4.016 -9.660 1.00 10.35 C ANISOU 1353 CG1 VAL A 196 1511 960 1463 395 -239 246 C ATOM 1354 CG2 VAL A 196 19.732 6.409 -9.942 1.00 24.16 C ANISOU 1354 CG2 VAL A 196 3275 2655 3248 389 -312 257 C ATOM 1355 N ASP A 197 19.211 6.932 -13.184 1.00 25.97 N ANISOU 1355 N ASP A 197 3566 2858 3441 358 -378 299 N ATOM 1356 CA ASP A 197 18.304 7.801 -13.943 1.00 33.36 C ANISOU 1356 CA ASP A 197 4518 3763 4393 357 -424 303 C ATOM 1357 C ASP A 197 19.056 8.409 -15.120 1.00 36.32 C ANISOU 1357 C ASP A 197 4924 4136 4739 333 -441 334 C ATOM 1358 O ASP A 197 20.008 9.173 -14.933 1.00 35.54 O ANISOU 1358 O ASP A 197 4832 4039 4631 320 -438 349 O ATOM 1359 CB ASP A 197 17.711 8.892 -13.060 1.00 39.26 C ANISOU 1359 CB ASP A 197 5252 4485 5179 368 -448 291 C ATOM 1360 CG ASP A 197 16.605 8.375 -12.171 1.00 62.89 C ANISOU 1360 CG ASP A 197 8218 7472 8206 393 -444 261 C ATOM 1361 OD1 ASP A 197 16.125 7.250 -12.417 1.00 72.20 O ANISOU 1361 OD1 ASP A 197 9390 8661 9379 402 -429 250 O ATOM 1362 OD2 ASP A 197 16.232 9.068 -11.203 1.00 75.18 O ANISOU 1362 OD2 ASP A 197 9759 9014 9794 404 -453 247 O ATOM 1363 N LYS A 198 18.650 8.031 -16.327 1.00 34.14 N ANISOU 1363 N LYS A 198 4668 3857 4448 328 -456 342 N ATOM 1364 CA LYS A 198 19.306 8.433 -17.560 1.00 31.63 C ANISOU 1364 CA LYS A 198 4381 3538 4099 306 -470 371 C ATOM 1365 C LYS A 198 18.546 9.574 -18.207 1.00 30.59 C ANISOU 1365 C LYS A 198 4267 3373 3984 304 -519 378 C ATOM 1366 O LYS A 198 17.310 9.566 -18.235 1.00 22.88 O ANISOU 1366 O LYS A 198 3284 2377 3034 319 -542 362 O ATOM 1367 CB LYS A 198 19.409 7.255 -18.529 1.00 42.37 C ANISOU 1367 CB LYS A 198 5755 4918 5428 301 -454 378 C ATOM 1368 CG LYS A 198 20.208 6.085 -17.986 1.00 54.10 C ANISOU 1368 CG LYS A 198 7225 6437 6893 302 -405 373 C ATOM 1369 CD LYS A 198 20.282 4.912 -18.966 1.00 63.41 C ANISOU 1369 CD LYS A 198 8416 7634 8042 298 -389 379 C ATOM 1370 CE LYS A 198 18.949 4.177 -19.097 1.00 73.02 C ANISOU 1370 CE LYS A 198 9623 8843 9277 316 -400 358 C ATOM 1371 NZ LYS A 198 18.498 3.583 -17.803 1.00 80.91 N ANISOU 1371 NZ LYS A 198 10590 9850 10303 337 -377 330 N ATOM 1372 N ASP A 199 19.294 10.585 -18.655 1.00 34.70 N ANISOU 1372 N ASP A 199 4807 3885 4491 286 -534 401 N ATOM 1373 CA ASP A 199 18.797 11.641 -19.541 1.00 29.32 C ANISOU 1373 CA ASP A 199 4149 3175 3816 278 -579 414 C ATOM 1374 C ASP A 199 17.499 12.258 -19.007 1.00 33.21 C ANISOU 1374 C ASP A 199 4628 3639 4352 296 -611 394 C ATOM 1375 O ASP A 199 16.432 12.169 -19.619 1.00 39.34 O ANISOU 1375 O ASP A 199 5410 4398 5139 304 -638 387 O ATOM 1376 CB ASP A 199 18.619 11.100 -20.954 1.00 39.06 C ANISOU 1376 CB ASP A 199 5408 4410 5022 270 -589 428 C ATOM 1377 CG ASP A 199 18.667 12.188 -22.005 1.00 52.06 C ANISOU 1377 CG ASP A 199 7085 6035 6661 255 -627 451 C ATOM 1378 OD1 ASP A 199 19.010 13.344 -21.673 1.00 51.18 O ANISOU 1378 OD1 ASP A 199 6977 5910 6561 248 -641 459 O ATOM 1379 OD2 ASP A 199 18.354 11.879 -23.172 1.00 61.18 O ANISOU 1379 OD2 ASP A 199 8262 7186 7799 250 -642 461 O ATOM 1380 N VAL A 200 17.612 12.863 -17.823 1.00 29.26 N ANISOU 1380 N VAL A 200 4107 3133 3876 303 -606 383 N ATOM 1381 CA VAL A 200 16.477 13.347 -17.045 1.00 27.23 C ANISOU 1381 CA VAL A 200 3832 2854 3662 322 -628 361 C ATOM 1382 C VAL A 200 15.987 14.687 -17.594 1.00 29.89 C ANISOU 1382 C VAL A 200 4182 3163 4011 314 -670 368 C ATOM 1383 O VAL A 200 16.765 15.518 -18.089 1.00 34.52 O ANISOU 1383 O VAL A 200 4789 3747 4582 295 -679 390 O ATOM 1384 CB VAL A 200 16.910 13.445 -15.565 1.00 36.97 C ANISOU 1384 CB VAL A 200 5038 4096 4912 331 -602 346 C ATOM 1385 CG1 VAL A 200 15.777 13.895 -14.661 1.00 37.67 C ANISOU 1385 CG1 VAL A 200 5105 4162 5045 351 -621 322 C ATOM 1386 CG2 VAL A 200 17.456 12.097 -15.100 1.00 41.24 C ANISOU 1386 CG2 VAL A 200 5564 4671 5436 335 -555 338 C ATOM 1387 N LYS A 201 14.673 14.898 -17.525 1.00 20.64 N ANISOU 1387 N LYS A 201 2998 1978 2868 324 -687 345 N ATOM 1388 CA LYS A 201 14.049 16.145 -17.948 1.00 32.86 C ANISOU 1388 CA LYS A 201 4551 3506 4429 315 -720 344 C ATOM 1389 C LYS A 201 13.036 16.617 -16.908 1.00 36.42 C ANISOU 1389 C LYS A 201 4974 3946 4918 329 -725 316 C ATOM 1390 O LYS A 201 12.282 15.809 -16.357 1.00 32.23 O ANISOU 1390 O LYS A 201 4422 3421 4405 346 -712 293 O ATOM 1391 CB LYS A 201 13.348 15.980 -19.311 1.00 24.93 C ANISOU 1391 CB LYS A 201 3567 2494 3413 310 -743 349 C ATOM 1392 CG LYS A 201 14.252 15.493 -20.457 1.00 27.63 C ANISOU 1392 CG LYS A 201 3938 2847 3714 295 -738 377 C ATOM 1393 CD LYS A 201 15.301 16.541 -20.815 1.00 30.08 C ANISOU 1393 CD LYS A 201 4268 3155 4006 274 -744 402 C ATOM 1394 CE LYS A 201 16.268 16.051 -21.889 1.00 24.69 C ANISOU 1394 CE LYS A 201 3613 2486 3282 258 -735 429 C ATOM 1395 NZ LYS A 201 17.330 17.056 -22.165 1.00 25.17 N ANISOU 1395 NZ LYS A 201 3692 2547 3326 237 -737 452 N ATOM 1396 N ILE A 202 12.977 17.938 -16.689 1.00 30.61 N ANISOU 1396 N ILE A 202 4238 3196 4196 321 -744 316 N ATOM 1397 CA ILE A 202 12.068 18.523 -15.709 1.00 26.32 C ANISOU 1397 CA ILE A 202 3670 2643 3687 332 -749 291 C ATOM 1398 C ILE A 202 10.673 18.636 -16.321 1.00 30.69 C ANISOU 1398 C ILE A 202 4222 3183 4255 335 -774 276 C ATOM 1399 O ILE A 202 10.519 18.792 -17.534 1.00 30.44 O ANISOU 1399 O ILE A 202 4213 3144 4209 325 -796 289 O ATOM 1400 CB ILE A 202 12.609 19.903 -15.252 1.00 33.07 C ANISOU 1400 CB ILE A 202 4527 3489 4550 322 -759 298 C ATOM 1401 CG1 ILE A 202 11.897 20.415 -13.991 1.00 29.37 C ANISOU 1401 CG1 ILE A 202 4029 3014 4114 333 -757 273 C ATOM 1402 CG2 ILE A 202 12.481 20.954 -16.391 1.00 25.43 C ANISOU 1402 CG2 ILE A 202 3583 2504 3573 305 -793 314 C ATOM 1403 CD1 ILE A 202 12.592 21.615 -13.330 1.00 24.49 C ANISOU 1403 CD1 ILE A 202 3410 2391 3503 325 -760 279 C ATOM 1404 N LYS A 203 9.646 18.533 -15.479 1.00 31.43 N ANISOU 1404 N LYS A 203 4290 3274 4378 349 -770 249 N ATOM 1405 CA LYS A 203 8.266 18.761 -15.909 1.00 33.51 C ANISOU 1405 CA LYS A 203 4550 3525 4659 352 -794 233 C ATOM 1406 C LYS A 203 8.101 20.168 -16.479 1.00 36.97 C ANISOU 1406 C LYS A 203 5003 3943 5100 338 -827 242 C ATOM 1407 O LYS A 203 8.724 21.125 -16.011 1.00 40.68 O ANISOU 1407 O LYS A 203 5474 4409 5572 331 -830 250 O ATOM 1408 CB LYS A 203 7.321 18.601 -14.725 1.00 41.34 C ANISOU 1408 CB LYS A 203 5509 4518 5680 367 -781 203 C ATOM 1409 CG LYS A 203 6.951 17.196 -14.370 1.00 45.95 C ANISOU 1409 CG LYS A 203 6077 5117 6266 382 -754 188 C ATOM 1410 CD LYS A 203 6.162 17.219 -13.061 1.00 56.23 C ANISOU 1410 CD LYS A 203 7347 6421 7596 394 -739 160 C ATOM 1411 CE LYS A 203 5.963 15.825 -12.473 1.00 60.98 C ANISOU 1411 CE LYS A 203 7929 7041 8199 409 -706 144 C ATOM 1412 NZ LYS A 203 5.455 14.822 -13.456 1.00 67.55 N ANISOU 1412 NZ LYS A 203 8770 7875 9022 412 -710 144 N ATOM 1413 N LYS A 204 7.244 20.298 -17.489 1.00 42.28 N ANISOU 1413 N LYS A 204 5688 4605 5773 335 -854 241 N ATOM 1414 CA LYS A 204 6.973 21.611 -18.075 1.00 38.54 C ANISOU 1414 CA LYS A 204 5229 4112 5303 322 -886 248 C ATOM 1415 C LYS A 204 6.342 22.570 -17.059 1.00 45.96 C ANISOU 1415 C LYS A 204 6148 5043 6274 326 -893 230 C ATOM 1416 O LYS A 204 6.594 23.784 -17.111 1.00 43.06 O ANISOU 1416 O LYS A 204 5789 4663 5908 316 -911 238 O ATOM 1417 CB LYS A 204 6.095 21.442 -19.327 1.00 36.35 C ANISOU 1417 CB LYS A 204 4965 3824 5020 320 -912 248 C ATOM 1418 CG LYS A 204 5.865 22.704 -20.135 1.00 42.48 C ANISOU 1418 CG LYS A 204 5762 4583 5798 306 -947 258 C ATOM 1419 CD LYS A 204 5.104 22.426 -21.426 1.00 52.96 C ANISOU 1419 CD LYS A 204 7105 5901 7116 303 -970 260 C ATOM 1420 CE LYS A 204 4.832 23.704 -22.240 1.00 51.32 C ANISOU 1420 CE LYS A 204 6917 5674 6909 290 -1005 269 C ATOM 1421 NZ LYS A 204 3.750 24.561 -21.669 1.00 47.56 N ANISOU 1421 NZ LYS A 204 6424 5184 6465 295 -1023 248 N ATOM 1422 N LYS A 205 5.535 22.056 -16.125 1.00 41.32 N ANISOU 1422 N LYS A 205 5532 4459 5707 341 -878 205 N ATOM 1423 CA LYS A 205 4.934 22.898 -15.096 1.00 31.92 C ANISOU 1423 CA LYS A 205 4322 3262 4544 345 -881 186 C ATOM 1424 C LYS A 205 4.669 22.065 -13.844 1.00 34.07 C ANISOU 1424 C LYS A 205 4565 3549 4830 360 -849 165 C ATOM 1425 O LYS A 205 4.276 20.896 -13.930 1.00 35.68 O ANISOU 1425 O LYS A 205 4762 3763 5032 370 -834 156 O ATOM 1426 CB LYS A 205 3.655 23.559 -15.613 1.00 37.21 C ANISOU 1426 CB LYS A 205 4994 3915 5231 343 -913 175 C ATOM 1427 CG LYS A 205 3.092 24.671 -14.743 1.00 36.56 C ANISOU 1427 CG LYS A 205 4895 3822 5173 343 -923 161 C ATOM 1428 CD LYS A 205 1.831 25.278 -15.385 1.00 37.12 C ANISOU 1428 CD LYS A 205 4970 3876 5259 340 -956 151 C ATOM 1429 CE LYS A 205 1.055 26.223 -14.459 1.00 37.74 C ANISOU 1429 CE LYS A 205 5030 3946 5364 343 -963 133 C ATOM 1430 NZ LYS A 205 0.337 25.496 -13.361 1.00 47.84 N ANISOU 1430 NZ LYS A 205 6280 5236 6660 356 -938 109 N ATOM 1431 N GLY A 206 4.919 22.667 -12.683 1.00 28.97 N ANISOU 1431 N GLY A 206 3904 2906 4198 362 -837 157 N ATOM 1432 CA GLY A 206 4.831 21.964 -11.414 1.00 25.07 C ANISOU 1432 CA GLY A 206 3384 2428 3715 375 -804 139 C ATOM 1433 C GLY A 206 3.784 22.477 -10.447 1.00 37.82 C ANISOU 1433 C GLY A 206 4976 4038 5357 381 -805 115 C ATOM 1434 O GLY A 206 2.900 23.246 -10.837 1.00 40.32 O ANISOU 1434 O GLY A 206 5295 4339 5685 377 -832 110 O ATOM 1435 N LYS A 207 3.866 22.058 -9.171 1.00 34.73 N ANISOU 1435 N LYS A 207 4561 3660 4973 391 -774 100 N ATOM 1436 CA LYS A 207 2.873 22.455 -8.179 1.00 39.08 C ANISOU 1436 CA LYS A 207 5090 4210 5548 396 -770 78 C ATOM 1437 C LYS A 207 3.508 22.919 -6.871 1.00 39.96 C ANISOU 1437 C LYS A 207 5189 4329 5664 398 -750 74 C ATOM 1438 O LYS A 207 2.834 22.919 -5.830 1.00 28.49 O ANISOU 1438 O LYS A 207 3715 2882 4228 405 -735 54 O ATOM 1439 CB LYS A 207 1.887 21.317 -7.900 1.00 43.15 C ANISOU 1439 CB LYS A 207 5588 4736 6070 407 -751 58 C ATOM 1440 CG LYS A 207 1.004 20.961 -9.063 1.00 56.68 C ANISOU 1440 CG LYS A 207 7311 6440 7784 406 -774 57 C ATOM 1441 CD LYS A 207 0.247 19.669 -8.821 1.00 67.23 C ANISOU 1441 CD LYS A 207 8631 7790 9124 417 -751 40 C ATOM 1442 CE LYS A 207 -0.628 19.321 -10.022 1.00 72.52 C ANISOU 1442 CE LYS A 207 9310 8450 9794 416 -774 39 C ATOM 1443 NZ LYS A 207 -1.182 17.940 -9.919 1.00 77.30 N ANISOU 1443 NZ LYS A 207 9903 9069 10400 426 -751 26 N ATOM 1444 N ILE A 208 4.781 23.320 -6.894 1.00 36.50 N ANISOU 1444 N ILE A 208 4763 3892 5213 392 -748 92 N ATOM 1445 CA ILE A 208 5.480 23.716 -5.680 1.00 24.13 C ANISOU 1445 CA ILE A 208 3185 2333 3651 394 -728 90 C ATOM 1446 C ILE A 208 6.337 24.942 -5.970 1.00 28.32 C ANISOU 1446 C ILE A 208 3732 2851 4176 381 -750 108 C ATOM 1447 O ILE A 208 7.116 24.953 -6.928 1.00 27.55 O ANISOU 1447 O ILE A 208 3657 2751 4062 373 -761 130 O ATOM 1448 CB ILE A 208 6.358 22.578 -5.109 1.00 34.35 C ANISOU 1448 CB ILE A 208 4472 3648 4932 402 -691 91 C ATOM 1449 CG1 ILE A 208 5.535 21.352 -4.745 1.00 38.18 C ANISOU 1449 CG1 ILE A 208 4939 4148 5421 414 -667 71 C ATOM 1450 CG2 ILE A 208 7.016 23.003 -3.806 1.00 31.43 C ANISOU 1450 CG2 ILE A 208 4089 3287 4567 404 -671 86 C ATOM 1451 CD1 ILE A 208 6.408 20.174 -4.345 1.00 40.73 C ANISOU 1451 CD1 ILE A 208 5257 4491 5730 422 -631 74 C ATOM 1452 N TYR A 209 6.258 25.935 -5.089 1.00 28.92 N ANISOU 1452 N TYR A 209 3799 2922 4266 380 -753 101 N ATOM 1453 CA TYR A 209 7.141 27.085 -5.097 1.00 29.92 C ANISOU 1453 CA TYR A 209 3938 3040 4391 369 -768 117 C ATOM 1454 C TYR A 209 7.953 27.059 -3.812 1.00 31.33 C ANISOU 1454 C TYR A 209 4103 3232 4570 374 -739 113 C ATOM 1455 O TYR A 209 7.497 26.533 -2.793 1.00 28.19 O ANISOU 1455 O TYR A 209 3685 2846 4182 385 -715 93 O ATOM 1456 CB TYR A 209 6.373 28.420 -5.187 1.00 33.56 C ANISOU 1456 CB TYR A 209 4400 3482 4868 362 -799 112 C ATOM 1457 CG TYR A 209 5.631 28.789 -3.922 1.00 32.39 C ANISOU 1457 CG TYR A 209 4230 3337 4741 369 -789 90 C ATOM 1458 CD1 TYR A 209 4.352 28.321 -3.678 1.00 26.70 C ANISOU 1458 CD1 TYR A 209 3494 2618 4033 377 -785 69 C ATOM 1459 CD2 TYR A 209 6.243 29.566 -2.941 1.00 41.68 C ANISOU 1459 CD2 TYR A 209 5400 4515 5923 368 -782 89 C ATOM 1460 CE1 TYR A 209 3.679 28.662 -2.504 1.00 23.34 C ANISOU 1460 CE1 TYR A 209 3049 2196 3625 382 -775 50 C ATOM 1461 CE2 TYR A 209 5.590 29.892 -1.763 1.00 41.96 C ANISOU 1461 CE2 TYR A 209 5415 4553 5975 374 -772 70 C ATOM 1462 CZ TYR A 209 4.311 29.436 -1.553 1.00 32.33 C ANISOU 1462 CZ TYR A 209 4181 3335 4766 381 -768 50 C ATOM 1463 OH TYR A 209 3.664 29.767 -0.389 1.00 36.37 O ANISOU 1463 OH TYR A 209 4674 3850 5293 386 -758 32 O ATOM 1464 N SER A 210 9.151 27.648 -3.862 1.00 26.13 N ANISOU 1464 N SER A 210 3456 2570 3901 366 -743 131 N ATOM 1465 CA SER A 210 10.155 27.493 -2.812 1.00 16.38 C ANISOU 1465 CA SER A 210 2212 1349 2663 370 -715 131 C ATOM 1466 C SER A 210 10.890 28.807 -2.570 1.00 22.00 C ANISOU 1466 C SER A 210 2931 2051 3377 360 -730 143 C ATOM 1467 O SER A 210 11.702 29.232 -3.400 1.00 30.21 O ANISOU 1467 O SER A 210 3991 3083 4404 348 -746 165 O ATOM 1468 CB SER A 210 11.139 26.393 -3.206 1.00 19.40 C ANISOU 1468 CB SER A 210 2603 1745 3024 372 -695 145 C ATOM 1469 OG SER A 210 12.070 26.125 -2.194 1.00 25.89 O ANISOU 1469 OG SER A 210 3414 2581 3842 377 -667 144 O ATOM 1470 N LEU A 211 10.645 29.428 -1.417 1.00 31.81 N ANISOU 1470 N LEU A 211 4158 3294 4636 364 -724 128 N ATOM 1471 CA LEU A 211 11.377 30.622 -1.009 1.00 29.89 C ANISOU 1471 CA LEU A 211 3918 3042 4396 355 -734 136 C ATOM 1472 C LEU A 211 11.055 30.917 0.450 1.00 29.90 C ANISOU 1472 C LEU A 211 3898 3050 4413 363 -718 116 C ATOM 1473 O LEU A 211 10.067 30.422 0.992 1.00 32.90 O ANISOU 1473 O LEU A 211 4262 3436 4802 373 -706 96 O ATOM 1474 CB LEU A 211 11.024 31.816 -1.900 1.00 34.30 C ANISOU 1474 CB LEU A 211 4494 3580 4960 342 -773 146 C ATOM 1475 CG LEU A 211 9.763 32.613 -1.563 1.00 34.49 C ANISOU 1475 CG LEU A 211 4507 3593 5004 344 -790 129 C ATOM 1476 CD1 LEU A 211 9.636 33.794 -2.529 1.00 35.79 C ANISOU 1476 CD1 LEU A 211 4690 3737 5171 330 -828 142 C ATOM 1477 CD2 LEU A 211 8.489 31.754 -1.549 1.00 29.22 C ANISOU 1477 CD2 LEU A 211 3827 2931 4345 354 -783 109 C ATOM 1478 N ASN A 212 11.884 31.755 1.068 1.00 30.24 N ANISOU 1478 N ASN A 212 3942 3091 4458 359 -718 122 N ATOM 1479 CA ASN A 212 11.706 32.153 2.470 1.00 33.78 C ANISOU 1479 CA ASN A 212 4371 3545 4919 365 -703 104 C ATOM 1480 C ASN A 212 10.668 33.267 2.581 1.00 33.84 C ANISOU 1480 C ASN A 212 4375 3537 4945 361 -729 94 C ATOM 1481 O ASN A 212 10.990 34.445 2.431 1.00 38.97 O ANISOU 1481 O ASN A 212 5034 4173 5600 352 -751 103 O ATOM 1482 CB ASN A 212 13.031 32.622 3.067 1.00 21.35 C ANISOU 1482 CB ASN A 212 2799 1974 3340 362 -695 115 C ATOM 1483 CG ASN A 212 12.931 32.898 4.567 1.00 28.57 C ANISOU 1483 CG ASN A 212 3694 2896 4266 369 -676 97 C ATOM 1484 OD1 ASN A 212 11.838 32.916 5.152 1.00 27.63 O ANISOU 1484 OD1 ASN A 212 3561 2778 4159 375 -672 77 O ATOM 1485 ND2 ASN A 212 14.075 33.142 5.188 1.00 29.16 N ANISOU 1485 ND2 ASN A 212 3769 2977 4336 368 -664 104 N ATOM 1486 N GLU A 213 9.421 32.908 2.879 1.00 38.84 N ANISOU 1486 N GLU A 213 4996 4174 5590 369 -724 75 N ATOM 1487 CA GLU A 213 8.368 33.913 3.004 1.00 29.93 C ANISOU 1487 CA GLU A 213 3863 3031 4478 366 -747 64 C ATOM 1488 C GLU A 213 8.462 34.713 4.295 1.00 34.56 C ANISOU 1488 C GLU A 213 4436 3618 5075 368 -740 54 C ATOM 1489 O GLU A 213 7.680 35.657 4.482 1.00 34.39 O ANISOU 1489 O GLU A 213 4412 3585 5069 364 -759 46 O ATOM 1490 CB GLU A 213 7.005 33.244 2.957 1.00 31.83 C ANISOU 1490 CB GLU A 213 4094 3275 4727 373 -744 47 C ATOM 1491 CG GLU A 213 6.635 32.630 1.646 1.00 41.34 C ANISOU 1491 CG GLU A 213 5310 4474 5924 371 -757 55 C ATOM 1492 CD GLU A 213 5.144 32.325 1.569 1.00 48.70 C ANISOU 1492 CD GLU A 213 6231 5404 6867 376 -762 37 C ATOM 1493 OE1 GLU A 213 4.334 33.267 1.693 1.00 48.45 O ANISOU 1493 OE1 GLU A 213 6198 5361 6852 373 -783 30 O ATOM 1494 OE2 GLU A 213 4.788 31.134 1.435 1.00 52.12 O ANISOU 1494 OE2 GLU A 213 6659 5849 7296 384 -744 31 O ATOM 1495 N GLY A 214 9.377 34.351 5.198 1.00 39.21 N ANISOU 1495 N GLY A 214 5018 4221 5657 372 -713 54 N ATOM 1496 CA GLY A 214 9.525 35.100 6.429 1.00 34.35 C ANISOU 1496 CA GLY A 214 4392 3608 5051 374 -705 45 C ATOM 1497 C GLY A 214 10.019 36.522 6.252 1.00 46.29 C ANISOU 1497 C GLY A 214 5915 5104 6570 363 -733 56 C ATOM 1498 O GLY A 214 9.839 37.340 7.161 1.00 51.10 O ANISOU 1498 O GLY A 214 6515 5710 7189 363 -734 47 O ATOM 1499 N TYR A 215 10.631 36.843 5.108 1.00 43.53 N ANISOU 1499 N TYR A 215 5584 4743 6212 353 -754 76 N ATOM 1500 CA TYR A 215 11.123 38.192 4.831 1.00 43.42 C ANISOU 1500 CA TYR A 215 5583 4713 6203 341 -781 89 C ATOM 1501 C TYR A 215 10.183 38.974 3.923 1.00 35.92 C ANISOU 1501 C TYR A 215 4641 3744 5261 333 -816 91 C ATOM 1502 O TYR A 215 10.621 39.856 3.170 1.00 35.88 O ANISOU 1502 O TYR A 215 4653 3725 5255 322 -841 107 O ATOM 1503 CB TYR A 215 12.524 38.127 4.226 1.00 50.75 C ANISOU 1503 CB TYR A 215 6526 5641 7115 333 -781 112 C ATOM 1504 CG TYR A 215 13.566 37.567 5.178 1.00 59.97 C ANISOU 1504 CG TYR A 215 7685 6825 8275 340 -750 112 C ATOM 1505 CD1 TYR A 215 13.318 37.471 6.554 1.00 63.95 C ANISOU 1505 CD1 TYR A 215 8171 7341 8788 349 -728 92 C ATOM 1506 CD2 TYR A 215 14.789 37.116 4.702 1.00 63.83 C ANISOU 1506 CD2 TYR A 215 8186 7319 8747 335 -742 131 C ATOM 1507 CE1 TYR A 215 14.268 36.947 7.418 1.00 64.00 C ANISOU 1507 CE1 TYR A 215 8168 7362 8786 355 -699 92 C ATOM 1508 CE2 TYR A 215 15.746 36.596 5.556 1.00 67.37 C ANISOU 1508 CE2 TYR A 215 8626 7782 9189 341 -714 130 C ATOM 1509 CZ TYR A 215 15.484 36.511 6.908 1.00 71.96 C ANISOU 1509 CZ TYR A 215 9188 8374 9779 351 -693 110 C ATOM 1510 OH TYR A 215 16.457 35.990 7.737 1.00 79.07 O ANISOU 1510 OH TYR A 215 10081 9289 10671 357 -665 110 O ATOM 1511 N ALA A 216 8.891 38.656 3.978 1.00 30.27 N ANISOU 1511 N ALA A 216 3916 3029 4556 340 -817 74 N ATOM 1512 CA ALA A 216 7.937 39.246 3.048 1.00 36.91 C ANISOU 1512 CA ALA A 216 4766 3854 5406 333 -849 75 C ATOM 1513 C ALA A 216 7.855 40.765 3.191 1.00 41.76 C ANISOU 1513 C ALA A 216 5383 4452 6032 325 -875 77 C ATOM 1514 O ALA A 216 7.557 41.458 2.213 1.00 42.40 O ANISOU 1514 O ALA A 216 5478 4517 6115 316 -905 86 O ATOM 1515 CB ALA A 216 6.565 38.600 3.254 1.00 32.74 C ANISOU 1515 CB ALA A 216 4224 3330 4886 343 -842 55 C ATOM 1516 N LYS A 217 8.135 41.294 4.388 1.00 43.40 N ANISOU 1516 N LYS A 217 5579 4663 6247 327 -864 69 N ATOM 1517 CA LYS A 217 8.083 42.737 4.617 1.00 47.50 C ANISOU 1517 CA LYS A 217 6101 5168 6778 320 -887 70 C ATOM 1518 C LYS A 217 8.998 43.488 3.659 1.00 46.55 C ANISOU 1518 C LYS A 217 6001 5035 6649 306 -911 93 C ATOM 1519 O LYS A 217 8.736 44.651 3.335 1.00 32.85 O ANISOU 1519 O LYS A 217 4273 3284 4923 298 -938 97 O ATOM 1520 CB LYS A 217 8.467 43.049 6.072 1.00 42.05 C ANISOU 1520 CB LYS A 217 5397 4487 6094 325 -868 59 C ATOM 1521 CG LYS A 217 8.298 44.502 6.490 1.00 50.73 C ANISOU 1521 CG LYS A 217 6495 5573 7208 319 -889 57 C ATOM 1522 CD LYS A 217 8.613 44.774 7.977 1.00 50.54 C ANISOU 1522 CD LYS A 217 6456 5558 7189 325 -869 45 C ATOM 1523 CE LYS A 217 10.103 44.609 8.320 1.00 50.65 C ANISOU 1523 CE LYS A 217 6474 5580 7192 323 -852 57 C ATOM 1524 NZ LYS A 217 10.373 44.848 9.799 1.00 49.45 N ANISOU 1524 NZ LYS A 217 6307 5438 7045 330 -832 45 N ATOM 1525 N ASP A 218 10.062 42.835 3.192 1.00 50.42 N ANISOU 1525 N ASP A 218 6502 5532 7123 304 -899 109 N ATOM 1526 CA ASP A 218 11.054 43.431 2.310 1.00 45.93 C ANISOU 1526 CA ASP A 218 5953 4953 6543 291 -917 132 C ATOM 1527 C ASP A 218 10.899 42.992 0.862 1.00 41.89 C ANISOU 1527 C ASP A 218 5459 4436 6019 285 -932 146 C ATOM 1528 O ASP A 218 11.746 43.338 0.037 1.00 47.94 O ANISOU 1528 O ASP A 218 6245 5197 6774 273 -944 168 O ATOM 1529 CB ASP A 218 12.460 43.138 2.833 1.00 48.92 C ANISOU 1529 CB ASP A 218 6333 5344 6911 291 -895 143 C ATOM 1530 CG ASP A 218 12.717 43.814 4.165 1.00 63.20 C ANISOU 1530 CG ASP A 218 8127 7154 8731 294 -885 132 C ATOM 1531 OD1 ASP A 218 11.934 44.725 4.507 1.00 68.35 O ANISOU 1531 OD1 ASP A 218 8774 7797 9399 293 -902 121 O ATOM 1532 OD2 ASP A 218 13.662 43.427 4.887 1.00 67.90 O ANISOU 1532 OD2 ASP A 218 8717 7762 9320 298 -862 134 O ATOM 1533 N PHE A 219 9.852 42.232 0.540 1.00 41.26 N ANISOU 1533 N PHE A 219 5375 4359 5942 292 -930 135 N ATOM 1534 CA PHE A 219 9.675 41.732 -0.818 1.00 40.07 C ANISOU 1534 CA PHE A 219 5241 4205 5780 287 -943 147 C ATOM 1535 C PHE A 219 9.627 42.880 -1.814 1.00 46.20 C ANISOU 1535 C PHE A 219 6036 4962 6557 273 -978 161 C ATOM 1536 O PHE A 219 9.090 43.957 -1.532 1.00 46.41 O ANISOU 1536 O PHE A 219 6060 4977 6599 270 -997 154 O ATOM 1537 CB PHE A 219 8.365 40.957 -0.976 1.00 35.83 C ANISOU 1537 CB PHE A 219 4694 3670 5250 297 -941 130 C ATOM 1538 CG PHE A 219 8.414 39.524 -0.545 1.00 35.09 C ANISOU 1538 CG PHE A 219 4589 3595 5149 309 -908 121 C ATOM 1539 CD1 PHE A 219 9.601 38.923 -0.141 1.00 32.36 C ANISOU 1539 CD1 PHE A 219 4242 3262 4789 311 -883 130 C ATOM 1540 CD2 PHE A 219 7.256 38.749 -0.613 1.00 30.39 C ANISOU 1540 CD2 PHE A 219 3983 3003 4559 317 -903 105 C ATOM 1541 CE1 PHE A 219 9.621 37.572 0.243 1.00 26.39 C ANISOU 1541 CE1 PHE A 219 3476 2525 4028 322 -852 121 C ATOM 1542 CE2 PHE A 219 7.264 37.415 -0.241 1.00 35.82 C ANISOU 1542 CE2 PHE A 219 4661 3710 5241 328 -873 97 C ATOM 1543 CZ PHE A 219 8.453 36.818 0.182 1.00 31.71 C ANISOU 1543 CZ PHE A 219 4139 3202 4707 331 -847 105 C ATOM 1544 N ASP A 220 10.182 42.635 -2.991 1.00 40.78 N ANISOU 1544 N ASP A 220 5370 4272 5852 264 -987 181 N ATOM 1545 CA ASP A 220 9.906 43.486 -4.129 1.00 38.41 C ANISOU 1545 CA ASP A 220 5089 3955 5550 252 -1020 194 C ATOM 1546 C ASP A 220 8.401 43.426 -4.411 1.00 35.91 C ANISOU 1546 C ASP A 220 4766 3631 5246 258 -1035 177 C ATOM 1547 O ASP A 220 7.748 42.425 -4.102 1.00 39.07 O ANISOU 1547 O ASP A 220 5153 4041 5650 269 -1019 162 O ATOM 1548 CB ASP A 220 10.726 42.984 -5.323 1.00 50.52 C ANISOU 1548 CB ASP A 220 6645 5490 7060 243 -1021 217 C ATOM 1549 CG ASP A 220 10.648 43.886 -6.534 1.00 64.14 C ANISOU 1549 CG ASP A 220 8392 7198 8779 229 -1054 233 C ATOM 1550 OD1 ASP A 220 9.671 43.784 -7.320 1.00 65.80 O ANISOU 1550 OD1 ASP A 220 8609 7401 8992 229 -1071 229 O ATOM 1551 OD2 ASP A 220 11.591 44.685 -6.707 1.00 71.21 O ANISOU 1551 OD2 ASP A 220 9300 8089 9668 217 -1061 250 O ATOM 1552 N PRO A 221 7.805 44.507 -4.919 1.00 42.19 N ANISOU 1552 N PRO A 221 5570 4410 6052 250 -1066 178 N ATOM 1553 CA PRO A 221 6.360 44.467 -5.223 1.00 34.87 C ANISOU 1553 CA PRO A 221 4637 3475 5137 255 -1082 162 C ATOM 1554 C PRO A 221 5.966 43.343 -6.163 1.00 34.86 C ANISOU 1554 C PRO A 221 4643 3478 5124 258 -1080 164 C ATOM 1555 O PRO A 221 4.844 42.831 -6.073 1.00 41.19 O ANISOU 1555 O PRO A 221 5433 4281 5936 267 -1079 147 O ATOM 1556 CB PRO A 221 6.100 45.841 -5.866 1.00 33.99 C ANISOU 1556 CB PRO A 221 4540 3344 5032 243 -1117 170 C ATOM 1557 CG PRO A 221 7.103 46.702 -5.296 1.00 39.42 C ANISOU 1557 CG PRO A 221 5229 4031 5720 236 -1115 179 C ATOM 1558 CD PRO A 221 8.353 45.864 -5.055 1.00 46.04 C ANISOU 1558 CD PRO A 221 6069 4884 6541 238 -1087 191 C ATOM 1559 N ALA A 222 6.853 42.959 -7.079 1.00 34.39 N ANISOU 1559 N ALA A 222 4604 3421 5044 251 -1079 185 N ATOM 1560 CA ALA A 222 6.550 41.875 -8.005 1.00 36.65 C ANISOU 1560 CA ALA A 222 4897 3711 5317 253 -1077 189 C ATOM 1561 C ALA A 222 6.578 40.505 -7.322 1.00 40.78 C ANISOU 1561 C ALA A 222 5404 4253 5838 267 -1043 177 C ATOM 1562 O ALA A 222 5.749 39.640 -7.629 1.00 42.21 O ANISOU 1562 O ALA A 222 5580 4438 6020 274 -1040 167 O ATOM 1563 CB ALA A 222 7.524 41.928 -9.174 1.00 38.50 C ANISOU 1563 CB ALA A 222 5159 3943 5528 240 -1086 215 C ATOM 1564 N VAL A 223 7.527 40.283 -6.405 1.00 43.30 N ANISOU 1564 N VAL A 223 5714 4584 6153 270 -1018 179 N ATOM 1565 CA VAL A 223 7.571 39.028 -5.646 1.00 36.74 C ANISOU 1565 CA VAL A 223 4867 3772 5322 283 -984 167 C ATOM 1566 C VAL A 223 6.323 38.881 -4.785 1.00 43.63 C ANISOU 1566 C VAL A 223 5717 4647 6215 295 -979 140 C ATOM 1567 O VAL A 223 5.755 37.784 -4.664 1.00 44.65 O ANISOU 1567 O VAL A 223 5835 4786 6344 305 -962 128 O ATOM 1568 CB VAL A 223 8.846 38.957 -4.786 1.00 28.89 C ANISOU 1568 CB VAL A 223 3868 2789 4320 283 -960 174 C ATOM 1569 CG1 VAL A 223 8.794 37.732 -3.849 1.00 25.32 C ANISOU 1569 CG1 VAL A 223 3396 2357 3869 298 -925 159 C ATOM 1570 CG2 VAL A 223 10.082 38.946 -5.658 1.00 18.28 C ANISOU 1570 CG2 VAL A 223 2546 1445 2953 272 -963 201 C ATOM 1571 N THR A 224 5.880 39.980 -4.165 1.00 39.90 N ANISOU 1571 N THR A 224 5236 4165 5760 293 -992 131 N ATOM 1572 CA THR A 224 4.638 39.942 -3.404 1.00 38.76 C ANISOU 1572 CA THR A 224 5072 4022 5635 303 -989 107 C ATOM 1573 C THR A 224 3.468 39.477 -4.259 1.00 48.17 C ANISOU 1573 C THR A 224 6266 5208 6830 305 -1003 100 C ATOM 1574 O THR A 224 2.649 38.670 -3.804 1.00 51.05 O ANISOU 1574 O THR A 224 6614 5581 7202 315 -988 82 O ATOM 1575 CB THR A 224 4.338 41.312 -2.807 1.00 41.49 C ANISOU 1575 CB THR A 224 5411 4355 5997 298 -1006 100 C ATOM 1576 OG1 THR A 224 5.411 41.694 -1.941 1.00 40.80 O ANISOU 1576 OG1 THR A 224 5320 4274 5907 297 -991 106 O ATOM 1577 CG2 THR A 224 3.029 41.274 -2.022 1.00 37.96 C ANISOU 1577 CG2 THR A 224 4944 3910 5570 308 -1002 76 C ATOM 1578 N GLU A 225 3.350 39.987 -5.492 1.00 46.45 N ANISOU 1578 N GLU A 225 6067 4975 6607 295 -1033 113 N ATOM 1579 CA GLU A 225 2.195 39.609 -6.303 1.00 46.78 C ANISOU 1579 CA GLU A 225 6111 5010 6652 297 -1049 105 C ATOM 1580 C GLU A 225 2.266 38.156 -6.761 1.00 41.56 C ANISOU 1580 C GLU A 225 5452 4362 5978 303 -1030 107 C ATOM 1581 O GLU A 225 1.277 37.428 -6.655 1.00 46.33 O ANISOU 1581 O GLU A 225 6044 4971 6590 312 -1024 90 O ATOM 1582 CB GLU A 225 2.034 40.539 -7.509 1.00 46.73 C ANISOU 1582 CB GLU A 225 6127 4985 6643 285 -1086 119 C ATOM 1583 CG GLU A 225 0.766 40.212 -8.314 1.00 49.14 C ANISOU 1583 CG GLU A 225 6434 5283 6955 287 -1104 109 C ATOM 1584 CD GLU A 225 0.441 41.232 -9.383 1.00 53.90 C ANISOU 1584 CD GLU A 225 7056 5865 7558 276 -1141 119 C ATOM 1585 OE1 GLU A 225 1.072 42.306 -9.397 1.00 61.78 O ANISOU 1585 OE1 GLU A 225 8063 6855 8554 266 -1154 131 O ATOM 1586 OE2 GLU A 225 -0.489 40.988 -10.177 1.00 57.97 O ANISOU 1586 OE2 GLU A 225 7576 6374 8076 277 -1158 114 O ATOM 1587 N TYR A 226 3.431 37.697 -7.222 1.00 39.54 N ANISOU 1587 N TYR A 226 5210 4113 5702 299 -1020 125 N ATOM 1588 CA TYR A 226 3.521 36.329 -7.725 1.00 37.05 C ANISOU 1588 CA TYR A 226 4897 3809 5372 305 -1004 128 C ATOM 1589 C TYR A 226 3.185 35.320 -6.637 1.00 36.49 C ANISOU 1589 C TYR A 226 4802 3755 5309 319 -971 108 C ATOM 1590 O TYR A 226 2.453 34.352 -6.885 1.00 37.98 O ANISOU 1590 O TYR A 226 4985 3949 5498 326 -964 98 O ATOM 1591 CB TYR A 226 4.914 36.045 -8.267 1.00 39.52 C ANISOU 1591 CB TYR A 226 5228 4127 5660 298 -995 152 C ATOM 1592 CG TYR A 226 5.113 34.619 -8.740 1.00 42.21 C ANISOU 1592 CG TYR A 226 5571 4480 5985 303 -977 155 C ATOM 1593 CD1 TYR A 226 4.642 34.208 -9.979 1.00 37.65 C ANISOU 1593 CD1 TYR A 226 5009 3897 5399 301 -993 161 C ATOM 1594 CD2 TYR A 226 5.783 33.686 -7.952 1.00 37.85 C ANISOU 1594 CD2 TYR A 226 5008 3947 5427 312 -942 153 C ATOM 1595 CE1 TYR A 226 4.831 32.906 -10.428 1.00 36.39 C ANISOU 1595 CE1 TYR A 226 4853 3750 5225 306 -976 165 C ATOM 1596 CE2 TYR A 226 5.975 32.376 -8.388 1.00 28.16 C ANISOU 1596 CE2 TYR A 226 3783 2732 4185 317 -925 156 C ATOM 1597 CZ TYR A 226 5.495 31.993 -9.631 1.00 37.29 C ANISOU 1597 CZ TYR A 226 4954 3881 5332 314 -942 162 C ATOM 1598 OH TYR A 226 5.687 30.698 -10.089 1.00 35.28 O ANISOU 1598 OH TYR A 226 4703 3639 5063 319 -926 166 O ATOM 1599 N ILE A 227 3.715 35.527 -5.427 1.00 28.69 N ANISOU 1599 N ILE A 227 3800 2775 4325 323 -950 103 N ATOM 1600 CA ILE A 227 3.397 34.622 -4.328 1.00 39.05 C ANISOU 1600 CA ILE A 227 5089 4104 5644 336 -918 84 C ATOM 1601 C ILE A 227 1.916 34.714 -4.005 1.00 46.06 C ANISOU 1601 C ILE A 227 5962 4987 6551 341 -925 63 C ATOM 1602 O ILE A 227 1.271 33.712 -3.664 1.00 42.40 O ANISOU 1602 O ILE A 227 5484 4535 6091 351 -906 48 O ATOM 1603 CB ILE A 227 4.290 34.904 -3.106 1.00 35.76 C ANISOU 1603 CB ILE A 227 4663 3697 5228 338 -896 84 C ATOM 1604 CG1 ILE A 227 5.755 34.638 -3.475 1.00 39.66 C ANISOU 1604 CG1 ILE A 227 5171 4196 5701 333 -887 105 C ATOM 1605 CG2 ILE A 227 3.871 34.055 -1.919 1.00 34.56 C ANISOU 1605 CG2 ILE A 227 4486 3561 5082 351 -863 63 C ATOM 1606 CD1 ILE A 227 6.003 33.244 -4.086 1.00 37.33 C ANISOU 1606 CD1 ILE A 227 4881 3913 5390 337 -870 111 C ATOM 1607 N GLN A 228 1.348 35.916 -4.128 1.00 46.96 N ANISOU 1607 N GLN A 228 6078 5085 6678 335 -954 61 N ATOM 1608 CA GLN A 228 -0.079 36.078 -3.898 1.00 49.24 C ANISOU 1608 CA GLN A 228 6354 5369 6986 339 -963 41 C ATOM 1609 C GLN A 228 -0.885 35.263 -4.911 1.00 50.34 C ANISOU 1609 C GLN A 228 6499 5506 7122 341 -972 39 C ATOM 1610 O GLN A 228 -1.900 34.647 -4.560 1.00 53.97 O ANISOU 1610 O GLN A 228 6943 5971 7592 350 -963 21 O ATOM 1611 CB GLN A 228 -0.431 37.563 -3.953 1.00 61.39 C ANISOU 1611 CB GLN A 228 7898 6890 8538 331 -994 42 C ATOM 1612 CG GLN A 228 -1.836 37.925 -3.531 1.00 71.17 C ANISOU 1612 CG GLN A 228 9122 8122 9797 335 -1004 22 C ATOM 1613 CD GLN A 228 -2.013 37.828 -2.027 1.00 78.96 C ANISOU 1613 CD GLN A 228 10086 9121 10794 343 -977 6 C ATOM 1614 OE1 GLN A 228 -1.037 37.707 -1.282 1.00 76.49 O ANISOU 1614 OE1 GLN A 228 9770 8820 10474 345 -954 10 O ATOM 1615 NE2 GLN A 228 -3.259 37.905 -1.570 1.00 85.54 N ANISOU 1615 NE2 GLN A 228 10904 9953 11644 347 -979 -13 N ATOM 1616 N ARG A 229 -0.417 35.201 -6.167 1.00 44.06 N ANISOU 1616 N ARG A 229 5726 4703 6313 334 -990 57 N ATOM 1617 CA ARG A 229 -1.111 34.400 -7.174 1.00 48.85 C ANISOU 1617 CA ARG A 229 6338 5308 6915 336 -999 55 C ATOM 1618 C ARG A 229 -0.988 32.900 -6.926 1.00 49.61 C ANISOU 1618 C ARG A 229 6425 5423 7002 346 -966 50 C ATOM 1619 O ARG A 229 -1.860 32.136 -7.347 1.00 51.13 O ANISOU 1619 O ARG A 229 6613 5616 7197 351 -967 40 O ATOM 1620 CB ARG A 229 -0.579 34.713 -8.573 1.00 55.14 C ANISOU 1620 CB ARG A 229 7162 6092 7695 325 -1024 77 C ATOM 1621 CG ARG A 229 -0.909 36.078 -9.140 1.00 52.80 C ANISOU 1621 CG ARG A 229 6879 5777 7407 315 -1060 83 C ATOM 1622 CD ARG A 229 -0.213 36.234 -10.489 1.00 64.90 C ANISOU 1622 CD ARG A 229 8439 7300 8919 304 -1079 107 C ATOM 1623 NE ARG A 229 -0.500 35.096 -11.366 1.00 75.35 N ANISOU 1623 NE ARG A 229 9769 8628 10231 308 -1077 108 N ATOM 1624 CZ ARG A 229 -1.460 35.059 -12.286 1.00 82.05 C ANISOU 1624 CZ ARG A 229 10626 9466 11083 306 -1101 104 C ATOM 1625 NH1 ARG A 229 -2.250 36.110 -12.477 1.00 82.94 N ANISOU 1625 NH1 ARG A 229 10739 9562 11210 302 -1129 99 N ATOM 1626 NH2 ARG A 229 -1.627 33.961 -13.015 1.00 81.67 N ANISOU 1626 NH2 ARG A 229 10583 9423 11023 310 -1096 106 N ATOM 1627 N LYS A 230 0.078 32.453 -6.260 1.00 50.66 N ANISOU 1627 N LYS A 230 6554 5570 7124 349 -938 55 N ATOM 1628 CA LYS A 230 0.221 31.026 -5.988 1.00 44.76 C ANISOU 1628 CA LYS A 230 5797 4841 6369 359 -906 50 C ATOM 1629 C LYS A 230 -0.685 30.560 -4.850 1.00 39.18 C ANISOU 1629 C LYS A 230 5064 4145 5677 370 -884 26 C ATOM 1630 O LYS A 230 -1.257 29.468 -4.925 1.00 38.66 O ANISOU 1630 O LYS A 230 4990 4088 5610 377 -870 16 O ATOM 1631 CB LYS A 230 1.692 30.706 -5.695 1.00 37.66 C ANISOU 1631 CB LYS A 230 4903 3954 5452 359 -884 65 C ATOM 1632 CG LYS A 230 2.634 30.993 -6.861 1.00 38.77 C ANISOU 1632 CG LYS A 230 5069 4086 5574 348 -902 90 C ATOM 1633 CD LYS A 230 2.300 30.104 -8.061 1.00 45.98 C ANISOU 1633 CD LYS A 230 5995 4999 6476 348 -910 95 C ATOM 1634 CE LYS A 230 1.544 30.808 -9.181 1.00 38.90 C ANISOU 1634 CE LYS A 230 5113 4082 5583 340 -948 99 C ATOM 1635 NZ LYS A 230 1.161 29.825 -10.253 1.00 40.96 N ANISOU 1635 NZ LYS A 230 5385 4345 5834 342 -952 102 N ATOM 1636 N LYS A 231 -0.875 31.386 -3.818 1.00 35.31 N ANISOU 1636 N LYS A 231 4562 3653 5201 370 -882 17 N ATOM 1637 CA LYS A 231 -1.735 30.979 -2.709 1.00 39.19 C ANISOU 1637 CA LYS A 231 5030 4155 5705 379 -860 -5 C ATOM 1638 C LYS A 231 -3.202 31.243 -3.012 1.00 40.45 C ANISOU 1638 C LYS A 231 5184 4304 5881 379 -881 -19 C ATOM 1639 O LYS A 231 -4.061 30.413 -2.701 1.00 39.35 O ANISOU 1639 O LYS A 231 5031 4173 5748 386 -866 -34 O ATOM 1640 CB LYS A 231 -1.368 31.733 -1.434 1.00 35.68 C ANISOU 1640 CB LYS A 231 4574 3714 5267 379 -848 -10 C ATOM 1641 CG LYS A 231 0.050 31.618 -0.956 1.00 42.54 C ANISOU 1641 CG LYS A 231 5447 4594 6123 379 -827 1 C ATOM 1642 CD LYS A 231 0.216 32.555 0.233 1.00 46.46 C ANISOU 1642 CD LYS A 231 5933 5090 6629 379 -822 -5 C ATOM 1643 CE LYS A 231 1.602 32.489 0.786 1.00 45.66 C ANISOU 1643 CE LYS A 231 5833 4999 6515 379 -802 5 C ATOM 1644 NZ LYS A 231 1.828 33.510 1.845 1.00 46.55 N ANISOU 1644 NZ LYS A 231 5939 5110 6637 377 -800 1 N ATOM 1645 N PHE A 232 -3.498 32.362 -3.670 1.00 37.30 N ANISOU 1645 N PHE A 232 4796 3885 5489 370 -917 -13 N ATOM 1646 CA PHE A 232 -4.865 32.786 -3.947 1.00 39.24 C ANISOU 1646 CA PHE A 232 5038 4119 5752 370 -940 -25 C ATOM 1647 C PHE A 232 -5.006 32.959 -5.455 1.00 41.23 C ANISOU 1647 C PHE A 232 5311 4356 5999 363 -972 -13 C ATOM 1648 O PHE A 232 -5.076 34.086 -5.964 1.00 39.10 O ANISOU 1648 O PHE A 232 5053 4069 5734 354 -1003 -6 O ATOM 1649 CB PHE A 232 -5.200 34.087 -3.220 1.00 38.24 C ANISOU 1649 CB PHE A 232 4905 3983 5642 366 -953 -31 C ATOM 1650 CG PHE A 232 -4.991 34.032 -1.719 1.00 42.29 C ANISOU 1650 CG PHE A 232 5400 4511 6159 372 -922 -42 C ATOM 1651 CD1 PHE A 232 -5.983 33.531 -0.880 1.00 40.98 C ANISOU 1651 CD1 PHE A 232 5213 4353 6003 379 -904 -61 C ATOM 1652 CD2 PHE A 232 -3.815 34.514 -1.146 1.00 43.12 C ANISOU 1652 CD2 PHE A 232 5507 4619 6256 369 -912 -32 C ATOM 1653 CE1 PHE A 232 -5.793 33.489 0.506 1.00 44.60 C ANISOU 1653 CE1 PHE A 232 5656 4825 6464 384 -875 -70 C ATOM 1654 CE2 PHE A 232 -3.614 34.480 0.237 1.00 36.36 C ANISOU 1654 CE2 PHE A 232 4635 3776 5403 375 -884 -42 C ATOM 1655 CZ PHE A 232 -4.603 33.966 1.066 1.00 38.35 C ANISOU 1655 CZ PHE A 232 4869 4038 5666 382 -866 -60 C ATOM 1656 N PRO A 233 -5.073 31.858 -6.195 1.00 48.89 N ANISOU 1656 N PRO A 233 6286 5331 6958 366 -967 -11 N ATOM 1657 CA PRO A 233 -5.094 31.948 -7.659 1.00 54.39 C ANISOU 1657 CA PRO A 233 7004 6015 7647 359 -996 2 C ATOM 1658 C PRO A 233 -6.323 32.707 -8.123 1.00 61.99 C ANISOU 1658 C PRO A 233 7967 6960 8626 356 -1028 -7 C ATOM 1659 O PRO A 233 -7.435 32.483 -7.617 1.00 57.91 O ANISOU 1659 O PRO A 233 7433 6446 8125 362 -1024 -25 O ATOM 1660 CB PRO A 233 -5.128 30.478 -8.112 1.00 50.08 C ANISOU 1660 CB PRO A 233 6458 5481 7089 366 -978 1 C ATOM 1661 CG PRO A 233 -4.661 29.692 -6.925 1.00 53.98 C ANISOU 1661 CG PRO A 233 6934 5995 7580 375 -937 -6 C ATOM 1662 CD PRO A 233 -5.130 30.464 -5.727 1.00 50.17 C ANISOU 1662 CD PRO A 233 6434 5512 7115 376 -932 -20 C ATOM 1663 N PRO A 234 -6.165 33.624 -9.078 1.00 70.42 N ANISOU 1663 N PRO A 234 9056 8011 9691 346 -1061 7 N ATOM 1664 CA PRO A 234 -7.325 34.424 -9.497 1.00 75.79 C ANISOU 1664 CA PRO A 234 9736 8674 10387 342 -1093 -2 C ATOM 1665 C PRO A 234 -8.455 33.584 -10.052 1.00 74.04 C ANISOU 1665 C PRO A 234 9510 8451 10171 348 -1098 -14 C ATOM 1666 O PRO A 234 -9.623 33.908 -9.811 1.00 74.07 O ANISOU 1666 O PRO A 234 9502 8449 10193 350 -1110 -29 O ATOM 1667 CB PRO A 234 -6.738 35.355 -10.566 1.00 80.34 C ANISOU 1667 CB PRO A 234 10338 9234 10952 331 -1124 18 C ATOM 1668 CG PRO A 234 -5.526 34.619 -11.081 1.00 82.53 C ANISOU 1668 CG PRO A 234 10631 9521 11206 329 -1109 37 C ATOM 1669 CD PRO A 234 -4.969 33.893 -9.896 1.00 74.49 C ANISOU 1669 CD PRO A 234 9595 8522 10186 337 -1070 30 C ATOM 1670 N ASP A 235 -8.154 32.476 -10.729 1.00 76.72 N ANISOU 1670 N ASP A 235 9857 8798 10495 351 -1088 -7 N ATOM 1671 CA ASP A 235 -9.193 31.598 -11.254 1.00 79.12 C ANISOU 1671 CA ASP A 235 10156 9102 10804 356 -1092 -19 C ATOM 1672 C ASP A 235 -9.600 30.521 -10.266 1.00 79.21 C ANISOU 1672 C ASP A 235 10142 9131 10821 367 -1057 -36 C ATOM 1673 O ASP A 235 -9.911 29.405 -10.691 1.00 75.34 O ANISOU 1673 O ASP A 235 9651 8649 10326 372 -1048 -40 O ATOM 1674 CB ASP A 235 -8.751 30.960 -12.571 1.00 75.17 C ANISOU 1674 CB ASP A 235 9677 8600 10284 353 -1101 -4 C ATOM 1675 CG ASP A 235 -7.478 30.171 -12.440 1.00 75.67 C ANISOU 1675 CG ASP A 235 9745 8679 10327 355 -1074 9 C ATOM 1676 OD1 ASP A 235 -6.982 30.012 -11.304 1.00 77.71 O ANISOU 1676 OD1 ASP A 235 9989 8951 10587 360 -1045 5 O ATOM 1677 OD2 ASP A 235 -6.972 29.708 -13.482 1.00 73.39 O ANISOU 1677 OD2 ASP A 235 9476 8390 10020 352 -1080 24 O ATOM 1678 N ASN A 236 -9.550 30.819 -8.963 1.00 87.41 N ANISOU 1678 N ASN A 236 11164 10179 11870 370 -1037 -45 N ATOM 1679 CA ASN A 236 -9.949 29.937 -7.864 1.00 94.01 C ANISOU 1679 CA ASN A 236 11976 11032 12712 380 -1003 -61 C ATOM 1680 C ASN A 236 -9.620 28.451 -8.046 1.00 90.11 C ANISOU 1680 C ASN A 236 11481 10554 12204 387 -976 -60 C ATOM 1681 O ASN A 236 -10.272 27.590 -7.446 1.00 93.28 O ANISOU 1681 O ASN A 236 11863 10967 12610 394 -953 -75 O ATOM 1682 CB ASN A 236 -11.436 30.162 -7.555 1.00106.71 C ANISOU 1682 CB ASN A 236 13569 12635 14342 382 -1013 -81 C ATOM 1683 CG ASN A 236 -12.348 29.859 -8.727 1.00121.76 C ANISOU 1683 CG ASN A 236 15483 14530 16252 381 -1038 -83 C ATOM 1684 OD1 ASN A 236 -12.092 28.964 -9.522 1.00125.37 O ANISOU 1684 OD1 ASN A 236 15949 14989 16695 383 -1036 -77 O ATOM 1685 ND2 ASN A 236 -13.411 30.644 -8.856 1.00130.13 N ANISOU 1685 ND2 ASN A 236 16540 15575 17330 378 -1064 -93 N ATOM 1686 N SER A 237 -8.626 28.143 -8.878 1.00 77.66 N ANISOU 1686 N SER A 237 9923 8978 10608 384 -979 -43 N ATOM 1687 CA SER A 237 -8.105 26.788 -9.031 1.00 68.06 C ANISOU 1687 CA SER A 237 8706 7777 9376 390 -952 -39 C ATOM 1688 C SER A 237 -7.344 26.385 -7.760 1.00 67.58 C ANISOU 1688 C SER A 237 8631 7735 9310 395 -914 -42 C ATOM 1689 O SER A 237 -7.345 27.088 -6.744 1.00 66.98 O ANISOU 1689 O SER A 237 8544 7661 9244 395 -907 -48 O ATOM 1690 CB SER A 237 -7.212 26.685 -10.261 1.00 59.34 C ANISOU 1690 CB SER A 237 7628 6668 8252 384 -967 -18 C ATOM 1691 OG SER A 237 -6.065 27.496 -10.113 1.00 56.28 O ANISOU 1691 OG SER A 237 7251 6277 7854 378 -969 -2 O ATOM 1692 N ALA A 238 -6.693 25.215 -7.803 1.00 63.66 N ANISOU 1692 N ALA A 238 8135 7254 8798 401 -888 -37 N ATOM 1693 CA ALA A 238 -6.013 24.676 -6.632 1.00 55.95 C ANISOU 1693 CA ALA A 238 7145 6297 7817 407 -849 -41 C ATOM 1694 C ALA A 238 -4.705 25.425 -6.344 1.00 52.54 C ANISOU 1694 C ALA A 238 6723 5865 7376 402 -847 -25 C ATOM 1695 O ALA A 238 -3.917 25.682 -7.263 1.00 46.19 O ANISOU 1695 O ALA A 238 5940 5054 6558 395 -864 -7 O ATOM 1696 CB ALA A 238 -5.717 23.194 -6.835 1.00 53.02 C ANISOU 1696 CB ALA A 238 6772 5942 7432 414 -823 -40 C ATOM 1697 N PRO A 239 -4.456 25.770 -5.072 1.00 42.03 N ANISOU 1697 N PRO A 239 5377 4541 6049 404 -827 -32 N ATOM 1698 CA PRO A 239 -3.196 26.423 -4.702 1.00 38.56 C ANISOU 1698 CA PRO A 239 4946 4104 5602 400 -823 -18 C ATOM 1699 C PRO A 239 -2.008 25.489 -4.859 1.00 40.65 C ANISOU 1699 C PRO A 239 5217 4382 5846 403 -800 -6 C ATOM 1700 O PRO A 239 -2.137 24.262 -4.789 1.00 41.42 O ANISOU 1700 O PRO A 239 5307 4493 5937 410 -776 -12 O ATOM 1701 CB PRO A 239 -3.397 26.775 -3.221 1.00 42.69 C ANISOU 1701 CB PRO A 239 5449 4634 6136 403 -802 -32 C ATOM 1702 CG PRO A 239 -4.851 26.603 -2.947 1.00 44.35 C ANISOU 1702 CG PRO A 239 5644 4844 6363 407 -804 -51 C ATOM 1703 CD PRO A 239 -5.318 25.556 -3.900 1.00 38.73 C ANISOU 1703 CD PRO A 239 4937 4134 5646 410 -806 -52 C ATOM 1704 N TYR A 240 -0.840 26.091 -5.063 1.00 31.78 N ANISOU 1704 N TYR A 240 4109 3255 4712 396 -806 12 N ATOM 1705 CA TYR A 240 0.411 25.350 -5.036 1.00 33.49 C ANISOU 1705 CA TYR A 240 4330 3484 4909 398 -783 24 C ATOM 1706 C TYR A 240 0.754 24.921 -3.606 1.00 40.08 C ANISOU 1706 C TYR A 240 5145 4337 5745 406 -745 13 C ATOM 1707 O TYR A 240 0.251 25.476 -2.622 1.00 42.67 O ANISOU 1707 O TYR A 240 5459 4666 6087 408 -741 0 O ATOM 1708 CB TYR A 240 1.548 26.198 -5.589 1.00 27.89 C ANISOU 1708 CB TYR A 240 3642 2766 4189 388 -801 47 C ATOM 1709 CG TYR A 240 1.659 26.221 -7.096 1.00 39.27 C ANISOU 1709 CG TYR A 240 5107 4195 5618 380 -828 64 C ATOM 1710 CD1 TYR A 240 0.539 26.145 -7.908 1.00 44.00 C ANISOU 1710 CD1 TYR A 240 5710 4785 6225 380 -850 57 C ATOM 1711 CD2 TYR A 240 2.901 26.355 -7.705 1.00 39.01 C ANISOU 1711 CD2 TYR A 240 5093 4162 5566 373 -832 87 C ATOM 1712 CE1 TYR A 240 0.663 26.183 -9.308 1.00 48.21 C ANISOU 1712 CE1 TYR A 240 6266 5307 6746 372 -875 73 C ATOM 1713 CE2 TYR A 240 3.033 26.396 -9.079 1.00 34.29 C ANISOU 1713 CE2 TYR A 240 4519 3554 4955 365 -856 103 C ATOM 1714 CZ TYR A 240 1.920 26.309 -9.878 1.00 41.73 C ANISOU 1714 CZ TYR A 240 5465 4486 5904 365 -878 97 C ATOM 1715 OH TYR A 240 2.084 26.346 -11.247 1.00 40.96 O ANISOU 1715 OH TYR A 240 5392 4380 5792 356 -901 114 O ATOM 1716 N GLY A 241 1.586 23.888 -3.490 1.00 33.40 N ANISOU 1716 N GLY A 241 4299 3507 4884 411 -718 19 N ATOM 1717 CA GLY A 241 2.218 23.592 -2.225 1.00 35.61 C ANISOU 1717 CA GLY A 241 4565 3804 5161 417 -684 13 C ATOM 1718 C GLY A 241 3.498 24.392 -2.037 1.00 38.58 C ANISOU 1718 C GLY A 241 4951 4177 5530 411 -687 29 C ATOM 1719 O GLY A 241 4.161 24.762 -3.009 1.00 34.23 O ANISOU 1719 O GLY A 241 4420 3617 4969 403 -708 48 O ATOM 1720 N ALA A 242 3.866 24.615 -0.767 1.00 31.78 N ANISOU 1720 N ALA A 242 4076 3325 4672 415 -665 22 N ATOM 1721 CA ALA A 242 5.090 25.327 -0.409 1.00 33.96 C ANISOU 1721 CA ALA A 242 4360 3602 4943 410 -665 35 C ATOM 1722 C ALA A 242 6.072 24.372 0.270 1.00 36.95 C ANISOU 1722 C ALA A 242 4731 4000 5308 417 -628 36 C ATOM 1723 O ALA A 242 5.674 23.542 1.094 1.00 34.27 O ANISOU 1723 O ALA A 242 4375 3676 4969 426 -598 21 O ATOM 1724 CB ALA A 242 4.791 26.517 0.506 1.00 24.11 C ANISOU 1724 CB ALA A 242 3103 2346 3710 407 -672 26 C ATOM 1725 N ARG A 243 7.351 24.465 -0.117 1.00 33.92 N ANISOU 1725 N ARG A 243 4361 3616 4910 412 -629 55 N ATOM 1726 CA ARG A 243 8.449 23.716 0.496 1.00 33.12 C ANISOU 1726 CA ARG A 243 4256 3533 4796 418 -596 59 C ATOM 1727 C ARG A 243 9.694 24.589 0.487 1.00 37.59 C ANISOU 1727 C ARG A 243 4834 4093 5356 410 -606 77 C ATOM 1728 O ARG A 243 10.031 25.171 -0.551 1.00 44.18 O ANISOU 1728 O ARG A 243 5687 4913 6185 400 -634 95 O ATOM 1729 CB ARG A 243 8.768 22.413 -0.262 1.00 32.33 C ANISOU 1729 CB ARG A 243 4162 3443 4680 422 -583 66 C ATOM 1730 CG ARG A 243 7.643 21.383 -0.382 1.00 33.95 C ANISOU 1730 CG ARG A 243 4356 3655 4888 430 -572 51 C ATOM 1731 CD ARG A 243 7.284 20.706 0.933 1.00 38.81 C ANISOU 1731 CD ARG A 243 4949 4289 5507 440 -536 31 C ATOM 1732 NE ARG A 243 6.394 19.567 0.689 1.00 40.69 N ANISOU 1732 NE ARG A 243 5180 4536 5745 447 -523 19 N ATOM 1733 CZ ARG A 243 5.081 19.677 0.472 1.00 42.01 C ANISOU 1733 CZ ARG A 243 5342 4696 5925 447 -537 8 C ATOM 1734 NH1 ARG A 243 4.496 20.867 0.470 1.00 37.41 N ANISOU 1734 NH1 ARG A 243 4760 4096 5356 441 -565 5 N ATOM 1735 NH2 ARG A 243 4.340 18.602 0.262 1.00 40.70 N ANISOU 1735 NH2 ARG A 243 5169 4539 5758 453 -524 -2 N ATOM 1736 N TYR A 244 10.403 24.645 1.612 1.00 23.72 N ANISOU 1736 N TYR A 244 3066 2347 3598 414 -583 73 N ATOM 1737 CA TYR A 244 11.667 25.381 1.652 1.00 23.17 C ANISOU 1737 CA TYR A 244 3007 2273 3522 406 -589 90 C ATOM 1738 C TYR A 244 12.557 24.720 2.705 1.00 28.34 C ANISOU 1738 C TYR A 244 3651 2948 4170 414 -553 86 C ATOM 1739 O TYR A 244 12.395 24.970 3.901 1.00 29.58 O ANISOU 1739 O TYR A 244 3792 3111 4335 419 -537 72 O ATOM 1740 CB TYR A 244 11.436 26.864 1.941 1.00 22.74 C ANISOU 1740 CB TYR A 244 2955 2203 3483 399 -614 89 C ATOM 1741 CG TYR A 244 12.677 27.728 1.823 1.00 21.11 C ANISOU 1741 CG TYR A 244 2762 1990 3271 389 -625 109 C ATOM 1742 CD1 TYR A 244 13.290 27.936 0.598 1.00 29.86 C ANISOU 1742 CD1 TYR A 244 3892 3087 4366 378 -646 132 C ATOM 1743 CD2 TYR A 244 13.212 28.367 2.937 1.00 31.38 C ANISOU 1743 CD2 TYR A 244 4053 3293 4577 389 -615 104 C ATOM 1744 CE1 TYR A 244 14.414 28.726 0.490 1.00 29.32 C ANISOU 1744 CE1 TYR A 244 3837 3014 4292 368 -656 151 C ATOM 1745 CE2 TYR A 244 14.336 29.165 2.834 1.00 31.42 C ANISOU 1745 CE2 TYR A 244 4070 3291 4577 380 -626 122 C ATOM 1746 CZ TYR A 244 14.929 29.338 1.604 1.00 30.51 C ANISOU 1746 CZ TYR A 244 3976 3166 4449 369 -646 146 C ATOM 1747 OH TYR A 244 16.049 30.131 1.495 1.00 41.71 O ANISOU 1747 OH TYR A 244 5407 4579 5862 358 -656 164 O ATOM 1748 N VAL A 245 13.490 23.879 2.244 1.00 30.22 N ANISOU 1748 N VAL A 245 3896 3194 4390 416 -540 100 N ATOM 1749 CA VAL A 245 14.440 23.231 3.140 1.00 28.63 C ANISOU 1749 CA VAL A 245 3686 3012 4181 423 -506 98 C ATOM 1750 C VAL A 245 15.387 24.269 3.729 1.00 32.26 C ANISOU 1750 C VAL A 245 4148 3466 4643 417 -511 106 C ATOM 1751 O VAL A 245 15.801 24.166 4.898 1.00 31.90 O ANISOU 1751 O VAL A 245 4089 3433 4599 423 -487 96 O ATOM 1752 CB VAL A 245 15.229 22.126 2.395 1.00 28.19 C ANISOU 1752 CB VAL A 245 3640 2966 4106 424 -494 113 C ATOM 1753 CG1 VAL A 245 16.279 21.505 3.297 1.00 23.11 C ANISOU 1753 CG1 VAL A 245 2987 2340 3454 432 -460 112 C ATOM 1754 CG2 VAL A 245 14.310 21.036 1.859 1.00 27.43 C ANISOU 1754 CG2 VAL A 245 3540 2875 4007 431 -487 104 C ATOM 1755 N GLY A 246 15.725 25.296 2.954 1.00 22.17 N ANISOU 1755 N GLY A 246 2888 2171 3366 404 -543 124 N ATOM 1756 CA GLY A 246 16.729 26.241 3.379 1.00 26.88 C ANISOU 1756 CA GLY A 246 3488 2762 3962 397 -548 135 C ATOM 1757 C GLY A 246 18.129 25.825 3.029 1.00 31.90 C ANISOU 1757 C GLY A 246 4136 3405 4581 393 -539 156 C ATOM 1758 O GLY A 246 19.076 26.541 3.365 1.00 35.12 O ANISOU 1758 O GLY A 246 4547 3809 4987 387 -542 166 O ATOM 1759 N SER A 247 18.278 24.701 2.343 1.00 30.49 N ANISOU 1759 N SER A 247 3963 3234 4388 396 -528 162 N ATOM 1760 CA SER A 247 19.547 24.212 1.836 1.00 29.81 C ANISOU 1760 CA SER A 247 3890 3155 4283 391 -521 185 C ATOM 1761 C SER A 247 19.390 24.121 0.326 1.00 28.16 C ANISOU 1761 C SER A 247 3703 2936 4062 381 -544 204 C ATOM 1762 O SER A 247 18.562 23.347 -0.163 1.00 27.01 O ANISOU 1762 O SER A 247 3555 2792 3914 387 -543 196 O ATOM 1763 CB SER A 247 19.890 22.853 2.470 1.00 29.11 C ANISOU 1763 CB SER A 247 3787 3088 4186 406 -483 175 C ATOM 1764 OG SER A 247 21.193 22.415 2.154 1.00 28.48 O ANISOU 1764 OG SER A 247 3717 3015 4088 401 -473 196 O ATOM 1765 N MET A 248 20.172 24.930 -0.403 1.00 35.61 N ANISOU 1765 N MET A 248 5171 3617 4741 100 -1004 208 N ATOM 1766 CA MET A 248 19.917 25.168 -1.828 1.00 22.78 C ANISOU 1766 CA MET A 248 3555 1988 3113 101 -1006 211 C ATOM 1767 C MET A 248 19.921 23.874 -2.645 1.00 19.73 C ANISOU 1767 C MET A 248 3174 1603 2718 101 -999 215 C ATOM 1768 O MET A 248 19.075 23.687 -3.528 1.00 23.33 O ANISOU 1768 O MET A 248 3636 2058 3170 102 -1003 213 O ATOM 1769 CB MET A 248 20.973 26.123 -2.373 1.00 27.68 C ANISOU 1769 CB MET A 248 4176 2604 3735 101 -1004 218 C ATOM 1770 CG MET A 248 20.689 26.592 -3.799 1.00 39.68 C ANISOU 1770 CG MET A 248 5704 4119 5252 101 -1007 221 C ATOM 1771 SD MET A 248 22.161 27.123 -4.702 1.00 45.49 S ANISOU 1771 SD MET A 248 6445 4852 5989 101 -999 231 S ATOM 1772 CE MET A 248 21.382 27.897 -6.121 1.00 42.29 C ANISOU 1772 CE MET A 248 6046 4440 5581 102 -1007 232 C ATOM 1773 N VAL A 249 20.882 22.978 -2.383 1.00 22.45 N ANISOU 1773 N VAL A 249 3517 1951 3059 100 -989 219 N ATOM 1774 CA VAL A 249 20.991 21.748 -3.164 1.00 21.53 C ANISOU 1774 CA VAL A 249 3408 1838 2936 100 -982 223 C ATOM 1775 C VAL A 249 19.774 20.850 -2.964 1.00 27.98 C ANISOU 1775 C VAL A 249 4224 2657 3749 101 -986 216 C ATOM 1776 O VAL A 249 19.348 20.159 -3.892 1.00 27.54 O ANISOU 1776 O VAL A 249 4175 2601 3687 101 -985 217 O ATOM 1777 CB VAL A 249 22.290 21.000 -2.841 1.00 23.66 C ANISOU 1777 CB VAL A 249 3675 2110 3203 100 -971 228 C ATOM 1778 CG1 VAL A 249 22.419 19.769 -3.784 1.00 14.47 C ANISOU 1778 CG1 VAL A 249 2519 949 2032 100 -964 233 C ATOM 1779 CG2 VAL A 249 23.474 21.916 -2.959 1.00 15.84 C ANISOU 1779 CG2 VAL A 249 2684 1117 2217 99 -968 235 C ATOM 1780 N ALA A 250 19.240 20.776 -1.739 1.00 27.38 N ANISOU 1780 N ALA A 250 4142 2585 3677 101 -990 209 N ATOM 1781 CA ALA A 250 18.037 19.967 -1.531 1.00 22.30 C ANISOU 1781 CA ALA A 250 3498 1944 3031 101 -994 203 C ATOM 1782 C ALA A 250 16.817 20.586 -2.212 1.00 22.29 C ANISOU 1782 C ALA A 250 3500 1939 3030 102 -1004 199 C ATOM 1783 O ALA A 250 15.991 19.866 -2.782 1.00 20.18 O ANISOU 1783 O ALA A 250 3237 1672 2757 103 -1005 197 O ATOM 1784 CB ALA A 250 17.771 19.780 -0.040 1.00 24.44 C ANISOU 1784 CB ALA A 250 3762 2219 3306 101 -995 197 C ATOM 1785 N ASP A 251 16.648 21.914 -2.105 1.00 16.90 N ANISOU 1785 N ASP A 251 2816 1253 2353 103 -1011 197 N ATOM 1786 CA ASP A 251 15.493 22.555 -2.730 1.00 28.14 C ANISOU 1786 CA ASP A 251 4243 2673 3778 104 -1021 193 C ATOM 1787 C ASP A 251 15.595 22.483 -4.251 1.00 26.93 C ANISOU 1787 C ASP A 251 4097 2515 3618 104 -1019 198 C ATOM 1788 O ASP A 251 14.603 22.207 -4.935 1.00 33.52 O ANISOU 1788 O ASP A 251 4937 3349 4450 105 -1024 196 O ATOM 1789 CB ASP A 251 15.363 24.022 -2.278 1.00 30.81 C ANISOU 1789 CB ASP A 251 4576 3006 4123 104 -1028 190 C ATOM 1790 CG ASP A 251 14.858 24.171 -0.819 1.00 28.01 C ANISOU 1790 CG ASP A 251 4213 2655 3774 104 -1033 183 C ATOM 1791 OD1 ASP A 251 13.923 23.454 -0.420 1.00 25.42 O ANISOU 1791 OD1 ASP A 251 3885 2329 3445 104 -1038 177 O ATOM 1792 OD2 ASP A 251 15.373 25.037 -0.084 1.00 25.19 O ANISOU 1792 OD2 ASP A 251 3851 2296 3423 104 -1035 183 O ATOM 1793 N VAL A 252 16.794 22.673 -4.798 1.00 22.44 N ANISOU 1793 N VAL A 252 3532 1945 3049 103 -1012 206 N ATOM 1794 CA VAL A 252 16.941 22.607 -6.252 1.00 32.02 C ANISOU 1794 CA VAL A 252 4753 3155 4257 104 -1010 211 C ATOM 1795 C VAL A 252 16.777 21.165 -6.752 1.00 30.33 C ANISOU 1795 C VAL A 252 4544 2945 4035 104 -1004 213 C ATOM 1796 O VAL A 252 16.216 20.938 -7.828 1.00 26.31 O ANISOU 1796 O VAL A 252 4042 2434 3522 104 -1006 213 O ATOM 1797 CB VAL A 252 18.275 23.234 -6.708 1.00 26.36 C ANISOU 1797 CB VAL A 252 4039 2436 3542 103 -1004 219 C ATOM 1798 CG1 VAL A 252 18.517 22.923 -8.181 1.00 21.94 C ANISOU 1798 CG1 VAL A 252 3488 1874 2976 103 -1000 226 C ATOM 1799 CG2 VAL A 252 18.276 24.758 -6.490 1.00 18.17 C ANISOU 1799 CG2 VAL A 252 2999 1395 2512 103 -1012 218 C ATOM 1800 N HIS A 253 17.281 20.167 -6.006 1.00 30.39 N ANISOU 1800 N HIS A 253 4549 2958 4042 103 -997 213 N ATOM 1801 CA HIS A 253 17.099 18.784 -6.464 1.00 32.82 C ANISOU 1801 CA HIS A 253 4861 3268 4341 103 -991 214 C ATOM 1802 C HIS A 253 15.631 18.377 -6.460 1.00 27.92 C ANISOU 1802 C HIS A 253 4241 2649 3719 103 -999 207 C ATOM 1803 O HIS A 253 15.162 17.748 -7.413 1.00 32.57 O ANISOU 1803 O HIS A 253 4837 3237 4302 104 -998 208 O ATOM 1804 CB HIS A 253 17.894 17.792 -5.621 1.00 25.78 C ANISOU 1804 CB HIS A 253 3965 2381 3448 102 -982 216 C ATOM 1805 CG HIS A 253 17.779 16.377 -6.108 1.00 28.97 C ANISOU 1805 CG HIS A 253 4374 2789 3844 102 -976 217 C ATOM 1806 ND1 HIS A 253 18.331 15.956 -7.296 1.00 28.83 N ANISOU 1806 ND1 HIS A 253 4363 2769 3821 102 -970 224 N ATOM 1807 CD2 HIS A 253 17.162 15.292 -5.576 1.00 27.88 C ANISOU 1807 CD2 HIS A 253 4234 2655 3703 102 -975 213 C ATOM 1808 CE1 HIS A 253 18.060 14.673 -7.479 1.00 26.79 C ANISOU 1808 CE1 HIS A 253 4108 2514 3556 102 -966 224 C ATOM 1809 NE2 HIS A 253 17.360 14.245 -6.447 1.00 25.34 N ANISOU 1809 NE2 HIS A 253 3919 2334 3374 102 -969 217 N ATOM 1810 N ARG A 254 14.880 18.758 -5.422 1.00 23.81 N ANISOU 1810 N ARG A 254 3714 2129 3203 104 -1006 200 N ATOM 1811 CA ARG A 254 13.440 18.515 -5.433 1.00 30.65 C ANISOU 1811 CA ARG A 254 4581 2996 4069 104 -1014 193 C ATOM 1812 C ARG A 254 12.775 19.232 -6.612 1.00 31.02 C ANISOU 1812 C ARG A 254 4634 3037 4115 105 -1021 193 C ATOM 1813 O ARG A 254 11.848 18.691 -7.223 1.00 32.11 O ANISOU 1813 O ARG A 254 4777 3176 4249 105 -1024 191 O ATOM 1814 CB ARG A 254 12.811 18.957 -4.108 1.00 31.38 C ANISOU 1814 CB ARG A 254 4666 3090 4168 104 -1020 186 C ATOM 1815 CG ARG A 254 11.332 18.569 -3.933 1.00 27.42 C ANISOU 1815 CG ARG A 254 4163 2590 3665 105 -1028 178 C ATOM 1816 CD ARG A 254 10.626 19.472 -2.890 1.00 34.09 C ANISOU 1816 CD ARG A 254 5003 3433 4518 105 -1040 170 C ATOM 1817 NE ARG A 254 10.750 20.880 -3.269 1.00 34.66 N ANISOU 1817 NE ARG A 254 5075 3500 4595 106 -1045 172 N ATOM 1818 CZ ARG A 254 11.485 21.785 -2.630 1.00 34.84 C ANISOU 1818 CZ ARG A 254 5093 3522 4624 105 -1044 173 C ATOM 1819 NH1 ARG A 254 12.154 21.463 -1.526 1.00 27.77 N ANISOU 1819 NH1 ARG A 254 4192 2630 3731 105 -1040 173 N ATOM 1820 NH2 ARG A 254 11.541 23.024 -3.098 1.00 31.32 N ANISOU 1820 NH2 ARG A 254 4647 3071 4181 106 -1049 174 N ATOM 1821 N THR A 255 13.232 20.452 -6.948 1.00 24.60 N ANISOU 1821 N THR A 255 3821 2220 3306 105 -1023 196 N ATOM 1822 CA THR A 255 12.681 21.148 -8.115 1.00 26.33 C ANISOU 1822 CA THR A 255 4046 2434 3524 106 -1030 197 C ATOM 1823 C THR A 255 12.908 20.330 -9.385 1.00 29.30 C ANISOU 1823 C THR A 255 4431 2810 3892 106 -1024 202 C ATOM 1824 O THR A 255 12.007 20.201 -10.217 1.00 35.13 O ANISOU 1824 O THR A 255 5174 3545 4626 106 -1029 200 O ATOM 1825 CB THR A 255 13.277 22.561 -8.275 1.00 32.12 C ANISOU 1825 CB THR A 255 4778 3162 4262 106 -1032 200 C ATOM 1826 OG1 THR A 255 13.136 23.311 -7.064 1.00 37.34 O ANISOU 1826 OG1 THR A 255 5432 3824 4931 106 -1037 195 O ATOM 1827 CG2 THR A 255 12.527 23.339 -9.367 1.00 33.94 C ANISOU 1827 CG2 THR A 255 5015 3387 4492 107 -1040 199 C ATOM 1828 N LEU A 256 14.085 19.722 -9.523 1.00 29.36 N ANISOU 1828 N LEU A 256 4441 2819 3897 105 -1014 209 N ATOM 1829 CA LEU A 256 14.338 18.849 -10.666 1.00 31.91 C ANISOU 1829 CA LEU A 256 4771 3142 4211 105 -1007 214 C ATOM 1830 C LEU A 256 13.431 17.609 -10.661 1.00 39.26 C ANISOU 1830 C LEU A 256 5704 4076 5137 105 -1008 210 C ATOM 1831 O LEU A 256 12.806 17.291 -11.688 1.00 34.22 O ANISOU 1831 O LEU A 256 5073 3437 4494 105 -1010 210 O ATOM 1832 CB LEU A 256 15.814 18.440 -10.681 1.00 26.12 C ANISOU 1832 CB LEU A 256 4038 2410 3476 104 -996 221 C ATOM 1833 CG LEU A 256 16.323 17.493 -11.772 1.00 21.00 C ANISOU 1833 CG LEU A 256 3397 1762 2820 104 -988 228 C ATOM 1834 CD1 LEU A 256 16.191 18.154 -13.152 1.00 14.85 C ANISOU 1834 CD1 LEU A 256 2626 977 2039 104 -991 231 C ATOM 1835 CD2 LEU A 256 17.764 17.121 -11.518 1.00 22.55 C ANISOU 1835 CD2 LEU A 256 3592 1960 3015 104 -976 234 C ATOM 1836 N VAL A 257 13.321 16.910 -9.509 1.00 32.70 N ANISOU 1836 N VAL A 257 4867 3250 4307 104 -1006 206 N ATOM 1837 CA VAL A 257 12.649 15.604 -9.484 1.00 31.40 C ANISOU 1837 CA VAL A 257 4704 3089 4137 104 -1004 203 C ATOM 1838 C VAL A 257 11.139 15.781 -9.600 1.00 34.04 C ANISOU 1838 C VAL A 257 5040 3423 4472 105 -1015 196 C ATOM 1839 O VAL A 257 10.454 14.981 -10.252 1.00 28.64 O ANISOU 1839 O VAL A 257 4361 2739 3782 105 -1015 195 O ATOM 1840 CB VAL A 257 13.012 14.786 -8.212 1.00 29.96 C ANISOU 1840 CB VAL A 257 4515 2912 3955 104 -999 201 C ATOM 1841 CG1 VAL A 257 12.125 13.506 -8.079 1.00 16.27 C ANISOU 1841 CG1 VAL A 257 2783 1183 2216 103 -999 197 C ATOM 1842 CG2 VAL A 257 14.493 14.388 -8.159 1.00 22.04 C ANISOU 1842 CG2 VAL A 257 3512 1911 2950 103 -987 208 C ATOM 1843 N TYR A 258 10.594 16.836 -8.989 1.00 27.10 N ANISOU 1843 N TYR A 258 4155 2542 3599 105 -1023 191 N ATOM 1844 CA TYR A 258 9.151 17.025 -8.970 1.00 28.43 C ANISOU 1844 CA TYR A 258 4323 2709 3769 106 -1033 184 C ATOM 1845 C TYR A 258 8.658 18.196 -9.818 1.00 29.06 C ANISOU 1845 C TYR A 258 4407 2784 3852 107 -1042 184 C ATOM 1846 O TYR A 258 7.450 18.294 -10.051 1.00 38.86 O ANISOU 1846 O TYR A 258 5649 4024 5093 107 -1050 178 O ATOM 1847 CB TYR A 258 8.668 17.215 -7.521 1.00 31.80 C ANISOU 1847 CB TYR A 258 4741 3139 4202 106 -1038 177 C ATOM 1848 CG TYR A 258 8.786 15.964 -6.685 1.00 52.28 C ANISOU 1848 CG TYR A 258 7331 5738 6793 106 -1031 175 C ATOM 1849 CD1 TYR A 258 8.771 14.711 -7.274 1.00 64.32 C ANISOU 1849 CD1 TYR A 258 8862 7266 8310 105 -1026 178 C ATOM 1850 CD2 TYR A 258 8.933 16.036 -5.303 1.00 62.99 C ANISOU 1850 CD2 TYR A 258 8681 7098 8155 105 -1033 171 C ATOM 1851 CE1 TYR A 258 8.888 13.563 -6.515 1.00 71.35 C ANISOU 1851 CE1 TYR A 258 9750 8162 9198 104 -1020 176 C ATOM 1852 CE2 TYR A 258 9.051 14.892 -4.535 1.00 67.69 C ANISOU 1852 CE2 TYR A 258 9273 7697 8747 104 -1028 170 C ATOM 1853 CZ TYR A 258 9.028 13.658 -5.148 1.00 71.55 C ANISOU 1853 CZ TYR A 258 9768 8190 9229 104 -1021 172 C ATOM 1854 OH TYR A 258 9.143 12.504 -4.407 1.00 73.63 O ANISOU 1854 OH TYR A 258 10029 8458 9490 103 -1016 171 O ATOM 1855 N GLY A 259 9.536 19.105 -10.250 1.00 28.70 N ANISOU 1855 N GLY A 259 4362 2734 3808 107 -1040 189 N ATOM 1856 CA GLY A 259 9.114 20.296 -10.960 1.00 32.88 C ANISOU 1856 CA GLY A 259 4894 3258 4340 108 -1048 189 C ATOM 1857 C GLY A 259 8.638 21.390 -10.024 1.00 29.60 C ANISOU 1857 C GLY A 259 4472 2842 3934 108 -1056 183 C ATOM 1858 O GLY A 259 8.410 21.172 -8.832 1.00 29.44 O ANISOU 1858 O GLY A 259 4445 2825 3917 108 -1057 178 O ATOM 1859 N GLY A 260 8.425 22.587 -10.596 1.00 23.79 N ANISOU 1859 N GLY A 260 3738 2100 3201 109 -1063 183 N ATOM 1860 CA GLY A 260 8.033 23.760 -9.832 1.00 25.88 C ANISOU 1860 CA GLY A 260 3996 2363 3473 109 -1071 178 C ATOM 1861 C GLY A 260 9.073 24.875 -9.930 1.00 32.34 C ANISOU 1861 C GLY A 260 4814 3178 4296 109 -1070 183 C ATOM 1862 O GLY A 260 9.806 24.973 -10.920 1.00 32.70 O ANISOU 1862 O GLY A 260 4866 3221 4338 109 -1065 190 O ATOM 1863 N ILE A 261 9.144 25.703 -8.871 1.00 32.17 N ANISOU 1863 N ILE A 261 4785 3156 4281 110 -1073 180 N ATOM 1864 CA ILE A 261 9.942 26.932 -8.912 1.00 32.34 C ANISOU 1864 CA ILE A 261 4805 3174 4308 109 -1074 183 C ATOM 1865 C ILE A 261 10.660 27.192 -7.587 1.00 28.93 C ANISOU 1865 C ILE A 261 4365 2745 3882 109 -1071 183 C ATOM 1866 O ILE A 261 10.139 26.912 -6.502 1.00 33.59 O ANISOU 1866 O ILE A 261 4949 3338 4474 109 -1073 177 O ATOM 1867 CB ILE A 261 9.075 28.151 -9.321 1.00 33.52 C ANISOU 1867 CB ILE A 261 4956 3319 4462 111 -1085 180 C ATOM 1868 CG1 ILE A 261 9.922 29.401 -9.583 1.00 29.10 C ANISOU 1868 CG1 ILE A 261 4396 2754 3906 110 -1086 184 C ATOM 1869 CG2 ILE A 261 8.040 28.478 -8.291 1.00 27.36 C ANISOU 1869 CG2 ILE A 261 4169 2539 3687 111 -1093 171 C ATOM 1870 CD1 ILE A 261 9.146 30.493 -10.344 1.00 25.57 C ANISOU 1870 CD1 ILE A 261 3952 2301 3461 111 -1096 183 C ATOM 1871 N PHE A 262 11.870 27.745 -7.705 1.00 21.13 N ANISOU 1871 N PHE A 262 3378 1755 2896 108 -1066 189 N ATOM 1872 CA PHE A 262 12.735 28.136 -6.607 1.00 27.18 C ANISOU 1872 CA PHE A 262 4138 2524 3668 108 -1063 189 C ATOM 1873 C PHE A 262 13.133 29.602 -6.801 1.00 31.01 C ANISOU 1873 C PHE A 262 4621 3003 4157 108 -1067 191 C ATOM 1874 O PHE A 262 13.562 29.984 -7.899 1.00 32.11 O ANISOU 1874 O PHE A 262 4767 3139 4295 108 -1066 197 O ATOM 1875 CB PHE A 262 13.980 27.223 -6.563 1.00 35.16 C ANISOU 1875 CB PHE A 262 5148 3537 4673 107 -1050 196 C ATOM 1876 CG PHE A 262 15.015 27.651 -5.552 1.00 37.25 C ANISOU 1876 CG PHE A 262 5407 3804 4944 106 -1046 197 C ATOM 1877 CD1 PHE A 262 14.867 27.325 -4.210 1.00 34.80 C ANISOU 1877 CD1 PHE A 262 5089 3497 4637 106 -1046 193 C ATOM 1878 CD2 PHE A 262 16.131 28.381 -5.941 1.00 37.98 C ANISOU 1878 CD2 PHE A 262 5500 3893 5038 105 -1043 204 C ATOM 1879 CE1 PHE A 262 15.812 27.729 -3.269 1.00 36.53 C ANISOU 1879 CE1 PHE A 262 5302 3717 4860 105 -1043 194 C ATOM 1880 CE2 PHE A 262 17.090 28.783 -5.006 1.00 34.66 C ANISOU 1880 CE2 PHE A 262 5074 3473 4622 104 -1039 206 C ATOM 1881 CZ PHE A 262 16.928 28.462 -3.674 1.00 32.75 C ANISOU 1881 CZ PHE A 262 4825 3236 4383 104 -1039 201 C ATOM 1882 N LEU A 263 13.002 30.419 -5.738 1.00 28.86 N ANISOU 1882 N LEU A 263 4342 2731 3892 108 -1072 187 N ATOM 1883 CA LEU A 263 13.277 31.865 -5.800 1.00 28.56 C ANISOU 1883 CA LEU A 263 4303 2688 3860 108 -1077 188 C ATOM 1884 C LEU A 263 14.209 32.320 -4.682 1.00 33.64 C ANISOU 1884 C LEU A 263 4940 3333 4510 107 -1074 188 C ATOM 1885 O LEU A 263 13.981 32.007 -3.509 1.00 33.39 O ANISOU 1885 O LEU A 263 4902 3305 4480 107 -1075 184 O ATOM 1886 CB LEU A 263 12.006 32.714 -5.685 1.00 22.22 C ANISOU 1886 CB LEU A 263 3498 1882 3061 110 -1090 180 C ATOM 1887 CG LEU A 263 10.822 32.504 -6.611 1.00 27.58 C ANISOU 1887 CG LEU A 263 4184 2560 3738 111 -1096 178 C ATOM 1888 CD1 LEU A 263 9.910 31.468 -5.996 1.00 19.74 C ANISOU 1888 CD1 LEU A 263 3188 1570 2742 111 -1097 171 C ATOM 1889 CD2 LEU A 263 10.106 33.833 -6.862 1.00 20.71 C ANISOU 1889 CD2 LEU A 263 3313 1683 2872 112 -1107 174 C ATOM 1890 N TYR A 264 15.245 33.075 -5.053 1.00 43.00 N ANISOU 1890 N TYR A 264 6127 4516 5697 107 -1071 195 N ATOM 1891 CA TYR A 264 16.019 33.901 -4.121 1.00 41.90 C ANISOU 1891 CA TYR A 264 5982 4376 5564 106 -1071 195 C ATOM 1892 C TYR A 264 16.233 35.258 -4.786 1.00 38.16 C ANISOU 1892 C TYR A 264 5510 3895 5093 106 -1076 198 C ATOM 1893 O TYR A 264 17.327 35.571 -5.277 1.00 34.56 O ANISOU 1893 O TYR A 264 5057 3438 4637 105 -1071 205 O ATOM 1894 CB TYR A 264 17.345 33.231 -3.737 1.00 44.59 C ANISOU 1894 CB TYR A 264 6320 4719 5903 105 -1060 201 C ATOM 1895 CG TYR A 264 17.862 33.677 -2.378 1.00 52.98 C ANISOU 1895 CG TYR A 264 7375 5784 6972 104 -1059 199 C ATOM 1896 CD1 TYR A 264 17.940 35.030 -2.067 1.00 60.85 C ANISOU 1896 CD1 TYR A 264 8369 6777 7975 104 -1066 197 C ATOM 1897 CD2 TYR A 264 18.263 32.765 -1.416 1.00 53.35 C ANISOU 1897 CD2 TYR A 264 7417 5836 7017 103 -1053 198 C ATOM 1898 CE1 TYR A 264 18.392 35.471 -0.844 1.00 60.10 C ANISOU 1898 CE1 TYR A 264 8267 6684 7886 104 -1066 195 C ATOM 1899 CE2 TYR A 264 18.732 33.200 -0.174 1.00 64.39 C ANISOU 1899 CE2 TYR A 264 8808 7235 8421 103 -1053 196 C ATOM 1900 CZ TYR A 264 18.793 34.564 0.099 1.00 62.45 C ANISOU 1900 CZ TYR A 264 8559 6986 8182 103 -1060 195 C ATOM 1901 OH TYR A 264 19.248 35.040 1.308 1.00 53.04 O ANISOU 1901 OH TYR A 264 7361 5796 6997 102 -1060 193 O ATOM 1902 N PRO A 265 15.212 36.109 -4.780 1.00 35.18 N ANISOU 1902 N PRO A 265 5132 3515 4720 107 -1087 192 N ATOM 1903 CA PRO A 265 15.211 37.294 -5.640 1.00 40.90 C ANISOU 1903 CA PRO A 265 5861 4234 5447 108 -1092 194 C ATOM 1904 C PRO A 265 15.819 38.534 -4.984 1.00 47.30 C ANISOU 1904 C PRO A 265 6667 5042 6264 107 -1095 195 C ATOM 1905 O PRO A 265 16.143 38.551 -3.794 1.00 47.93 O ANISOU 1905 O PRO A 265 6739 5124 6347 107 -1094 192 O ATOM 1906 CB PRO A 265 13.711 37.490 -5.915 1.00 41.36 C ANISOU 1906 CB PRO A 265 5920 4290 5504 109 -1103 187 C ATOM 1907 CG PRO A 265 13.001 36.870 -4.709 1.00 36.79 C ANISOU 1907 CG PRO A 265 5335 3717 4928 110 -1104 180 C ATOM 1908 CD PRO A 265 14.006 36.043 -3.940 1.00 34.99 C ANISOU 1908 CD PRO A 265 5103 3493 4698 109 -1094 183 C ATOM 1909 N ALA A 266 15.972 39.581 -5.805 1.00 44.86 N ANISOU 1909 N ALA A 266 6361 4727 5956 107 -1099 198 N ATOM 1910 CA ALA A 266 16.479 40.878 -5.366 1.00 45.73 C ANISOU 1910 CA ALA A 266 6469 4834 6074 107 -1103 198 C ATOM 1911 C ALA A 266 15.379 41.720 -4.717 1.00 45.07 C ANISOU 1911 C ALA A 266 6380 4749 5996 108 -1114 190 C ATOM 1912 O ALA A 266 14.193 41.571 -5.024 1.00 45.94 O ANISOU 1912 O ALA A 266 6492 4858 6104 110 -1120 185 O ATOM 1913 CB ALA A 266 17.091 41.632 -6.547 1.00 43.28 C ANISOU 1913 CB ALA A 266 6165 4519 5763 107 -1103 205 C ATOM 1914 N ASN A 267 15.782 42.588 -3.786 1.00 49.03 N ANISOU 1914 N ASN A 267 6876 5250 6504 108 -1116 188 N ATOM 1915 CA ASN A 267 14.879 43.572 -3.175 1.00 51.38 C ANISOU 1915 CA ASN A 267 7170 5545 6808 109 -1127 181 C ATOM 1916 C ASN A 267 15.621 44.899 -2.999 1.00 63.09 C ANISOU 1916 C ASN A 267 8651 7024 8297 109 -1129 183 C ATOM 1917 O ASN A 267 16.721 45.105 -3.525 1.00 54.71 O ANISOU 1917 O ASN A 267 7593 5961 7235 107 -1124 191 O ATOM 1918 CB ASN A 267 14.295 43.111 -1.831 1.00 37.56 C ANISOU 1918 CB ASN A 267 5413 3798 5061 110 -1131 173 C ATOM 1919 CG ASN A 267 15.354 42.674 -0.848 1.00 47.24 C ANISOU 1919 CG ASN A 267 6633 5028 6287 108 -1123 176 C ATOM 1920 OD1 ASN A 267 16.156 43.473 -0.396 1.00 53.18 O ANISOU 1920 OD1 ASN A 267 7383 5779 7045 107 -1122 178 O ATOM 1921 ND2 ASN A 267 15.326 41.403 -0.471 1.00 57.84 N ANISOU 1921 ND2 ASN A 267 7975 6376 7626 108 -1117 175 N ATOM 1922 N LYS A 268 14.974 45.810 -2.258 1.00 78.59 N ANISOU 1922 N LYS A 268 10610 8985 10266 110 -1140 177 N ATOM 1923 CA LYS A 268 15.505 47.152 -2.016 1.00 77.36 C ANISOU 1923 CA LYS A 268 10452 8824 10116 109 -1143 178 C ATOM 1924 C LYS A 268 16.746 47.125 -1.127 1.00 62.55 C ANISOU 1924 C LYS A 268 8571 6951 8243 108 -1136 182 C ATOM 1925 O LYS A 268 17.719 47.840 -1.394 1.00 58.42 O ANISOU 1925 O LYS A 268 8049 6425 7721 107 -1133 187 O ATOM 1926 CB LYS A 268 14.403 48.012 -1.386 1.00 92.90 C ANISOU 1926 CB LYS A 268 12417 10790 12091 111 -1157 169 C ATOM 1927 CG LYS A 268 13.970 47.510 0.009 1.00101.66 C ANISOU 1927 CG LYS A 268 13520 11903 13203 111 -1160 162 C ATOM 1928 CD LYS A 268 12.904 48.355 0.689 1.00105.11 C ANISOU 1928 CD LYS A 268 13953 12337 13647 112 -1173 153 C ATOM 1929 CE LYS A 268 12.596 47.787 2.075 1.00105.42 C ANISOU 1929 CE LYS A 268 13986 12380 13688 112 -1175 147 C ATOM 1930 NZ LYS A 268 11.528 48.536 2.786 1.00105.68 N ANISOU 1930 NZ LYS A 268 14016 12411 13728 113 -1188 138 N ATOM 1931 N LYS A 269 16.746 46.287 -0.086 1.00 46.44 N ANISOU 1931 N LYS A 269 6526 4916 6203 107 -1133 178 N ATOM 1932 CA LYS A 269 17.900 46.188 0.790 1.00 48.27 C ANISOU 1932 CA LYS A 269 6753 5150 6437 106 -1126 181 C ATOM 1933 C LYS A 269 19.043 45.424 0.140 1.00 53.19 C ANISOU 1933 C LYS A 269 7379 5776 7054 104 -1113 190 C ATOM 1934 O LYS A 269 20.202 45.625 0.515 1.00 57.43 O ANISOU 1934 O LYS A 269 7915 6314 7593 103 -1108 195 O ATOM 1935 CB LYS A 269 17.507 45.516 2.112 1.00 60.95 C ANISOU 1935 CB LYS A 269 8353 6761 8044 105 -1128 175 C ATOM 1936 CG LYS A 269 16.519 46.321 2.979 1.00 71.69 C ANISOU 1936 CG LYS A 269 9709 8118 9411 106 -1141 166 C ATOM 1937 CD LYS A 269 16.173 45.583 4.280 1.00 76.73 C ANISOU 1937 CD LYS A 269 10342 8761 10051 106 -1142 159 C ATOM 1938 CE LYS A 269 15.179 46.354 5.152 1.00 79.25 C ANISOU 1938 CE LYS A 269 10657 9078 10377 107 -1155 150 C ATOM 1939 NZ LYS A 269 15.709 47.628 5.698 1.00 79.18 N ANISOU 1939 NZ LYS A 269 10644 9065 10374 107 -1159 150 N ATOM 1940 N SER A 270 18.746 44.568 -0.834 1.00 51.70 N ANISOU 1940 N SER A 270 7197 5588 6859 105 -1110 193 N ATOM 1941 CA SER A 270 19.748 43.723 -1.483 1.00 40.78 C ANISOU 1941 CA SER A 270 5818 4207 5471 103 -1099 200 C ATOM 1942 C SER A 270 19.472 43.744 -2.981 1.00 38.38 C ANISOU 1942 C SER A 270 5522 3899 5162 104 -1100 204 C ATOM 1943 O SER A 270 18.903 42.800 -3.541 1.00 39.65 O ANISOU 1943 O SER A 270 5686 4062 5317 105 -1099 204 O ATOM 1944 CB SER A 270 19.697 42.302 -0.923 1.00 39.82 C ANISOU 1944 CB SER A 270 5694 4091 5344 103 -1093 199 C ATOM 1945 OG SER A 270 19.928 42.304 0.477 1.00 40.81 O ANISOU 1945 OG SER A 270 5811 4220 5475 103 -1092 195 O ATOM 1946 N PRO A 271 19.861 44.820 -3.670 1.00 29.54 N ANISOU 1946 N PRO A 271 4406 2774 4044 104 -1103 208 N ATOM 1947 CA PRO A 271 19.505 44.947 -5.091 1.00 42.05 C ANISOU 1947 CA PRO A 271 5999 4355 5625 104 -1106 211 C ATOM 1948 C PRO A 271 20.183 43.927 -5.980 1.00 42.76 C ANISOU 1948 C PRO A 271 6094 4447 5707 103 -1096 218 C ATOM 1949 O PRO A 271 19.840 43.854 -7.164 1.00 49.86 O ANISOU 1949 O PRO A 271 7000 5343 6602 104 -1097 220 O ATOM 1950 CB PRO A 271 19.937 46.381 -5.451 1.00 38.45 C ANISOU 1950 CB PRO A 271 5544 3893 5173 104 -1110 214 C ATOM 1951 CG PRO A 271 20.590 46.953 -4.227 1.00 36.87 C ANISOU 1951 CG PRO A 271 5336 3693 4979 103 -1110 213 C ATOM 1952 CD PRO A 271 20.832 45.840 -3.256 1.00 32.86 C ANISOU 1952 CD PRO A 271 4824 3193 4470 103 -1103 211 C ATOM 1953 N ASN A 272 21.155 43.174 -5.470 1.00 41.29 N ANISOU 1953 N ASN A 272 5904 4264 5519 102 -1086 222 N ATOM 1954 CA ASN A 272 21.839 42.146 -6.239 1.00 35.08 C ANISOU 1954 CA ASN A 272 5124 3480 4726 102 -1076 228 C ATOM 1955 C ASN A 272 21.575 40.723 -5.754 1.00 37.80 C ANISOU 1955 C ASN A 272 5466 3830 5067 102 -1071 226 C ATOM 1956 O ASN A 272 22.271 39.802 -6.186 1.00 44.95 O ANISOU 1956 O ASN A 272 6375 4738 5967 101 -1061 232 O ATOM 1957 CB ASN A 272 23.334 42.426 -6.203 1.00 37.38 C ANISOU 1957 CB ASN A 272 5414 3771 5019 100 -1068 236 C ATOM 1958 CG ASN A 272 23.727 43.496 -7.178 1.00 48.96 C ANISOU 1958 CG ASN A 272 6885 5230 6486 100 -1071 241 C ATOM 1959 OD1 ASN A 272 23.102 43.646 -8.225 1.00 53.12 O ANISOU 1959 OD1 ASN A 272 7419 5755 7011 101 -1075 241 O ATOM 1960 ND2 ASN A 272 24.729 44.291 -6.818 1.00 51.86 N ANISOU 1960 ND2 ASN A 272 7250 5596 6858 99 -1069 245 N ATOM 1961 N GLY A 273 20.611 40.510 -4.873 1.00 39.02 N ANISOU 1961 N GLY A 273 5616 3988 5224 103 -1076 218 N ATOM 1962 CA GLY A 273 20.386 39.175 -4.357 1.00 45.89 C ANISOU 1962 CA GLY A 273 6484 4863 6090 103 -1071 216 C ATOM 1963 C GLY A 273 21.378 38.812 -3.260 1.00 48.86 C ANISOU 1963 C GLY A 273 6854 5243 6468 102 -1063 217 C ATOM 1964 O GLY A 273 22.107 39.668 -2.736 1.00 48.13 O ANISOU 1964 O GLY A 273 6758 5150 6381 101 -1064 219 O ATOM 1965 N LYS A 274 21.394 37.509 -2.898 1.00 46.46 N ANISOU 1965 N LYS A 274 6549 4945 6160 101 -1057 217 N ATOM 1966 CA LYS A 274 22.295 36.981 -1.868 1.00 48.04 C ANISOU 1966 CA LYS A 274 6744 5149 6361 100 -1049 218 C ATOM 1967 C LYS A 274 23.168 35.822 -2.323 1.00 42.51 C ANISOU 1967 C LYS A 274 6046 4451 5654 100 -1038 225 C ATOM 1968 O LYS A 274 24.338 35.774 -1.943 1.00 35.43 O ANISOU 1968 O LYS A 274 5148 3556 4760 98 -1031 230 O ATOM 1969 CB LYS A 274 21.517 36.545 -0.629 1.00 58.27 C ANISOU 1969 CB LYS A 274 8032 6448 7658 101 -1053 210 C ATOM 1970 CG LYS A 274 21.027 37.713 0.182 1.00 69.29 C ANISOU 1970 CG LYS A 274 9423 7842 9062 101 -1062 205 C ATOM 1971 CD LYS A 274 22.163 38.677 0.449 1.00 69.56 C ANISOU 1971 CD LYS A 274 9455 7873 9101 100 -1060 209 C ATOM 1972 CE LYS A 274 21.712 39.766 1.381 1.00 75.68 C ANISOU 1972 CE LYS A 274 10225 8648 9884 100 -1069 203 C ATOM 1973 NZ LYS A 274 21.430 39.196 2.711 1.00 83.95 N ANISOU 1973 NZ LYS A 274 11265 9699 10933 100 -1069 197 N ATOM 1974 N LEU A 275 22.644 34.900 -3.138 1.00 40.63 N ANISOU 1974 N LEU A 275 5813 4214 5409 100 -1036 225 N ATOM 1975 CA LEU A 275 23.412 33.734 -3.574 1.00 33.59 C ANISOU 1975 CA LEU A 275 4925 3326 4512 100 -1025 231 C ATOM 1976 C LEU A 275 24.569 34.157 -4.482 1.00 30.09 C ANISOU 1976 C LEU A 275 4486 2879 4068 99 -1019 240 C ATOM 1977 O LEU A 275 24.550 35.232 -5.089 1.00 26.61 O ANISOU 1977 O LEU A 275 4047 2433 3629 99 -1024 242 O ATOM 1978 CB LEU A 275 22.504 32.719 -4.294 1.00 29.15 C ANISOU 1978 CB LEU A 275 4367 2765 3943 101 -1025 230 C ATOM 1979 CG LEU A 275 21.302 32.154 -3.506 1.00 30.49 C ANISOU 1979 CG LEU A 275 4534 2938 4113 101 -1030 221 C ATOM 1980 CD1 LEU A 275 20.472 31.123 -4.270 1.00 24.73 C ANISOU 1980 CD1 LEU A 275 3809 2210 3377 102 -1030 220 C ATOM 1981 CD2 LEU A 275 21.759 31.554 -2.175 1.00 29.13 C ANISOU 1981 CD2 LEU A 275 4354 2771 3943 101 -1025 219 C ATOM 1982 N ARG A 276 25.621 33.332 -4.502 1.00 28.74 N ANISOU 1982 N ARG A 276 4315 2710 3893 98 -1009 246 N ATOM 1983 CA ARG A 276 26.857 33.628 -5.223 1.00 26.62 C ANISOU 1983 CA ARG A 276 4050 2440 3625 98 -1002 255 C ATOM 1984 C ARG A 276 26.814 33.122 -6.671 1.00 30.39 C ANISOU 1984 C ARG A 276 4536 2915 4095 98 -998 260 C ATOM 1985 O ARG A 276 26.522 31.946 -6.924 1.00 37.29 O ANISOU 1985 O ARG A 276 5413 3793 4964 99 -994 260 O ATOM 1986 CB ARG A 276 28.029 33.018 -4.454 1.00 31.33 C ANISOU 1986 CB ARG A 276 4642 3040 4222 96 -992 259 C ATOM 1987 CG ARG A 276 28.100 33.461 -2.994 1.00 35.22 C ANISOU 1987 CG ARG A 276 5127 3535 4721 96 -995 255 C ATOM 1988 CD ARG A 276 28.742 34.835 -2.822 1.00 37.53 C ANISOU 1988 CD ARG A 276 5417 3823 5020 95 -998 257 C ATOM 1989 NE ARG A 276 28.733 35.238 -1.412 1.00 38.11 N ANISOU 1989 NE ARG A 276 5482 3898 5099 94 -1002 252 N ATOM 1990 CZ ARG A 276 29.229 36.379 -0.928 1.00 39.31 C ANISOU 1990 CZ ARG A 276 5630 4048 5257 94 -1005 252 C ATOM 1991 NH1 ARG A 276 29.826 37.282 -1.718 1.00 29.47 N ANISOU 1991 NH1 ARG A 276 4388 2797 4012 93 -1005 258 N ATOM 1992 NH2 ARG A 276 29.136 36.617 0.371 1.00 47.75 N ANISOU 1992 NH2 ARG A 276 6692 5118 6331 93 -1008 247 N ATOM 1993 N LEU A 277 27.180 33.992 -7.616 1.00 28.87 N ANISOU 1993 N LEU A 277 4348 2717 3902 98 -1000 265 N ATOM 1994 CA LEU A 277 26.987 33.673 -9.035 1.00 31.45 C ANISOU 1994 CA LEU A 277 4684 3042 4223 99 -998 269 C ATOM 1995 C LEU A 277 27.900 32.539 -9.498 1.00 29.40 C ANISOU 1995 C LEU A 277 4428 2786 3958 98 -986 275 C ATOM 1996 O LEU A 277 27.464 31.652 -10.242 1.00 30.80 O ANISOU 1996 O LEU A 277 4609 2963 4128 99 -984 276 O ATOM 1997 CB LEU A 277 27.201 34.923 -9.896 1.00 35.42 C ANISOU 1997 CB LEU A 277 5191 3539 4729 99 -1002 272 C ATOM 1998 CG LEU A 277 27.202 34.820 -11.431 1.00 29.03 C ANISOU 1998 CG LEU A 277 4391 2727 3914 99 -1001 277 C ATOM 1999 CD1 LEU A 277 25.827 34.473 -11.991 1.00 21.67 C ANISOU 1999 CD1 LEU A 277 3463 1794 2978 100 -1007 272 C ATOM 2000 CD2 LEU A 277 27.742 36.099 -12.084 1.00 15.61 C ANISOU 2000 CD2 LEU A 277 2693 1021 2217 99 -1003 282 C ATOM 2001 N LEU A 278 29.161 32.533 -9.063 1.00 24.63 N ANISOU 2001 N LEU A 278 3819 2182 3355 98 -978 281 N ATOM 2002 CA LEU A 278 30.127 31.641 -9.690 1.00 25.86 C ANISOU 2002 CA LEU A 278 3980 2340 3507 97 -967 288 C ATOM 2003 C LEU A 278 29.886 30.178 -9.314 1.00 26.29 C ANISOU 2003 C LEU A 278 4033 2400 3556 98 -961 286 C ATOM 2004 O LEU A 278 29.831 29.309 -10.197 1.00 24.06 O ANISOU 2004 O LEU A 278 3757 2118 3268 98 -956 289 O ATOM 2005 CB LEU A 278 31.546 32.068 -9.321 1.00 22.29 C ANISOU 2005 CB LEU A 278 3524 1887 3058 96 -960 295 C ATOM 2006 CG LEU A 278 32.187 32.856 -10.467 1.00 31.09 C ANISOU 2006 CG LEU A 278 4644 2996 4172 96 -959 302 C ATOM 2007 CD1 LEU A 278 31.518 34.203 -10.616 1.00 20.94 C ANISOU 2007 CD1 LEU A 278 3359 1706 2892 96 -970 298 C ATOM 2008 CD2 LEU A 278 33.708 33.001 -10.326 1.00 30.97 C ANISOU 2008 CD2 LEU A 278 4627 2981 4159 95 -950 310 C ATOM 2009 N TYR A 279 29.657 29.890 -8.024 1.00 21.63 N ANISOU 2009 N TYR A 279 3436 1813 2969 97 -963 281 N ATOM 2010 CA TYR A 279 29.649 28.508 -7.547 1.00 25.32 C ANISOU 2010 CA TYR A 279 3902 2287 3433 97 -956 280 C ATOM 2011 C TYR A 279 28.323 28.095 -6.923 1.00 27.35 C ANISOU 2011 C TYR A 279 4156 2546 3689 98 -963 271 C ATOM 2012 O TYR A 279 28.210 26.967 -6.439 1.00 30.56 O ANISOU 2012 O TYR A 279 4561 2958 4093 98 -959 269 O ATOM 2013 CB TYR A 279 30.802 28.290 -6.555 1.00 26.72 C ANISOU 2013 CB TYR A 279 4073 2467 3613 97 -949 283 C ATOM 2014 CG TYR A 279 31.012 29.483 -5.619 1.00 31.17 C ANISOU 2014 CG TYR A 279 4630 3029 4184 96 -954 280 C ATOM 2015 CD1 TYR A 279 30.235 29.651 -4.493 1.00 24.94 C ANISOU 2015 CD1 TYR A 279 3835 2242 3399 96 -961 272 C ATOM 2016 CD2 TYR A 279 31.954 30.456 -5.903 1.00 30.01 C ANISOU 2016 CD2 TYR A 279 4483 2878 4041 95 -953 286 C ATOM 2017 CE1 TYR A 279 30.398 30.727 -3.673 1.00 23.95 C ANISOU 2017 CE1 TYR A 279 3704 2115 3281 95 -966 270 C ATOM 2018 CE2 TYR A 279 32.123 31.541 -5.092 1.00 35.15 C ANISOU 2018 CE2 TYR A 279 5128 3527 4699 94 -958 284 C ATOM 2019 CZ TYR A 279 31.350 31.673 -3.958 1.00 36.99 C ANISOU 2019 CZ TYR A 279 5355 3762 4936 94 -965 276 C ATOM 2020 OH TYR A 279 31.517 32.769 -3.127 1.00 23.72 O ANISOU 2020 OH TYR A 279 3669 2080 3262 94 -970 274 O ATOM 2021 N GLU A 280 27.291 28.930 -7.005 1.00 27.11 N ANISOU 2021 N GLU A 280 4126 2513 3662 98 -974 265 N ATOM 2022 CA GLU A 280 25.952 28.505 -6.623 1.00 30.82 C ANISOU 2022 CA GLU A 280 4594 2984 4130 99 -981 257 C ATOM 2023 C GLU A 280 24.954 28.707 -7.752 1.00 40.85 C ANISOU 2023 C GLU A 280 5872 4252 5398 100 -987 255 C ATOM 2024 O GLU A 280 24.325 27.734 -8.194 1.00 43.28 O ANISOU 2024 O GLU A 280 6184 4562 5700 101 -986 254 O ATOM 2025 CB GLU A 280 25.513 29.250 -5.362 1.00 26.08 C ANISOU 2025 CB GLU A 280 3986 2385 3537 99 -988 250 C ATOM 2026 CG GLU A 280 26.337 28.898 -4.152 1.00 19.23 C ANISOU 2026 CG GLU A 280 3113 1522 2673 98 -982 251 C ATOM 2027 CD GLU A 280 25.972 29.753 -2.922 1.00 33.42 C ANISOU 2027 CD GLU A 280 4902 3319 4478 98 -990 244 C ATOM 2028 OE1 GLU A 280 25.364 30.844 -3.078 1.00 40.18 O ANISOU 2028 OE1 GLU A 280 5758 4171 5337 98 -999 241 O ATOM 2029 OE2 GLU A 280 26.301 29.335 -1.792 1.00 43.86 O ANISOU 2029 OE2 GLU A 280 6218 4645 5801 97 -987 243 O ATOM 2030 N CYS A 281 24.816 29.941 -8.258 1.00 36.20 N ANISOU 2030 N CYS A 281 5285 3658 4812 100 -994 256 N ATOM 2031 CA CYS A 281 23.789 30.238 -9.253 1.00 28.75 C ANISOU 2031 CA CYS A 281 4348 2711 3866 101 -1001 254 C ATOM 2032 C CYS A 281 24.120 29.626 -10.617 1.00 27.85 C ANISOU 2032 C CYS A 281 4242 2596 3745 101 -995 260 C ATOM 2033 O CYS A 281 23.254 29.021 -11.265 1.00 19.24 O ANISOU 2033 O CYS A 281 3156 1506 2650 102 -997 258 O ATOM 2034 CB CYS A 281 23.626 31.755 -9.402 1.00 33.77 C ANISOU 2034 CB CYS A 281 4983 3342 4508 101 -1010 253 C ATOM 2035 SG CYS A 281 23.068 32.637 -7.955 1.00 40.35 S ANISOU 2035 SG CYS A 281 5806 4175 5349 101 -1019 245 S ATOM 2036 N ASN A 282 25.346 29.832 -11.103 1.00 23.93 N ANISOU 2036 N ASN A 282 3748 2098 3248 101 -988 268 N ATOM 2037 CA ASN A 282 25.664 29.373 -12.453 1.00 23.21 C ANISOU 2037 CA ASN A 282 3665 2004 3150 101 -982 274 C ATOM 2038 C ASN A 282 25.551 27.856 -12.573 1.00 32.74 C ANISOU 2038 C ASN A 282 4873 3215 4350 101 -975 275 C ATOM 2039 O ASN A 282 24.837 27.389 -13.475 1.00 25.43 O ANISOU 2039 O ASN A 282 3953 2289 3419 102 -977 274 O ATOM 2040 CB ASN A 282 27.051 29.882 -12.870 1.00 17.75 C ANISOU 2040 CB ASN A 282 2974 1310 2460 100 -975 283 C ATOM 2041 CG ASN A 282 27.007 31.229 -13.631 1.00 25.85 C ANISOU 2041 CG ASN A 282 4003 2330 3488 100 -982 285 C ATOM 2042 OD1 ASN A 282 25.999 31.600 -14.215 1.00 20.52 O ANISOU 2042 OD1 ASN A 282 3332 1652 2813 101 -990 281 O ATOM 2043 ND2 ASN A 282 28.130 31.923 -13.659 1.00 26.46 N ANISOU 2043 ND2 ASN A 282 4080 2405 3569 100 -978 291 N ATOM 2044 N PRO A 283 26.153 27.038 -11.683 1.00 28.27 N ANISOU 2044 N PRO A 283 4303 2655 3785 101 -968 275 N ATOM 2045 CA PRO A 283 26.018 25.578 -11.837 1.00 23.76 C ANISOU 2045 CA PRO A 283 3734 2088 3207 101 -962 275 C ATOM 2046 C PRO A 283 24.579 25.085 -11.765 1.00 35.69 C ANISOU 2046 C PRO A 283 5245 3600 4715 102 -969 268 C ATOM 2047 O PRO A 283 24.187 24.201 -12.549 1.00 38.32 O ANISOU 2047 O PRO A 283 5584 3933 5041 102 -967 268 O ATOM 2048 CB PRO A 283 26.868 25.033 -10.685 1.00 18.79 C ANISOU 2048 CB PRO A 283 3097 1463 2579 100 -954 276 C ATOM 2049 CG PRO A 283 27.852 26.127 -10.402 1.00 25.71 C ANISOU 2049 CG PRO A 283 3971 2337 3462 100 -954 280 C ATOM 2050 CD PRO A 283 27.058 27.382 -10.569 1.00 19.94 C ANISOU 2050 CD PRO A 283 3240 1601 2735 100 -965 276 C ATOM 2051 N MET A 284 23.768 25.643 -10.860 1.00 26.28 N ANISOU 2051 N MET A 284 4048 2409 3528 102 -978 260 N ATOM 2052 CA MET A 284 22.369 25.249 -10.838 1.00 20.09 C ANISOU 2052 CA MET A 284 3266 1626 2743 102 -985 253 C ATOM 2053 C MET A 284 21.644 25.732 -12.096 1.00 26.30 C ANISOU 2053 C MET A 284 4059 2407 3526 103 -991 253 C ATOM 2054 O MET A 284 20.712 25.067 -12.568 1.00 29.76 O ANISOU 2054 O MET A 284 4501 2847 3960 103 -994 250 O ATOM 2055 CB MET A 284 21.675 25.775 -9.576 1.00 18.47 C ANISOU 2055 CB MET A 284 3052 1422 2543 102 -993 245 C ATOM 2056 CG MET A 284 22.229 25.221 -8.262 1.00 24.10 C ANISOU 2056 CG MET A 284 3758 2140 3259 102 -987 244 C ATOM 2057 SD MET A 284 22.276 23.396 -8.226 1.00 39.80 S ANISOU 2057 SD MET A 284 5748 4134 5240 102 -978 245 S ATOM 2058 CE MET A 284 22.439 23.080 -6.453 1.00 25.47 C ANISOU 2058 CE MET A 284 3923 2324 3429 101 -977 240 C ATOM 2059 N ALA A 285 22.028 26.891 -12.640 1.00 24.52 N ANISOU 2059 N ALA A 285 3835 2177 3304 103 -994 257 N ATOM 2060 CA ALA A 285 21.417 27.331 -13.897 1.00 20.47 C ANISOU 2060 CA ALA A 285 3330 1660 2789 103 -999 257 C ATOM 2061 C ALA A 285 21.746 26.375 -15.033 1.00 21.98 C ANISOU 2061 C ALA A 285 3529 1852 2972 104 -992 263 C ATOM 2062 O ALA A 285 20.861 25.986 -15.797 1.00 21.53 O ANISOU 2062 O ALA A 285 3477 1793 2910 104 -995 261 O ATOM 2063 CB ALA A 285 21.864 28.747 -14.244 1.00 20.49 C ANISOU 2063 CB ALA A 285 3333 1657 2796 103 -1003 260 C ATOM 2064 N TYR A 286 23.003 25.928 -15.109 1.00 17.17 N ANISOU 2064 N TYR A 286 2920 1243 2361 103 -981 270 N ATOM 2065 CA TYR A 286 23.411 24.995 -16.153 1.00 20.18 C ANISOU 2065 CA TYR A 286 3308 1625 2734 103 -973 276 C ATOM 2066 C TYR A 286 22.657 23.663 -16.053 1.00 32.10 C ANISOU 2066 C TYR A 286 4819 3139 4239 104 -972 272 C ATOM 2067 O TYR A 286 22.153 23.160 -17.063 1.00 31.03 O ANISOU 2067 O TYR A 286 4690 3002 4096 104 -972 272 O ATOM 2068 CB TYR A 286 24.921 24.782 -16.085 1.00 27.32 C ANISOU 2068 CB TYR A 286 4212 2530 3639 103 -962 283 C ATOM 2069 CG TYR A 286 25.487 23.929 -17.191 1.00 28.37 C ANISOU 2069 CG TYR A 286 4353 2664 3765 103 -953 290 C ATOM 2070 CD1 TYR A 286 25.695 22.568 -16.990 1.00 21.17 C ANISOU 2070 CD1 TYR A 286 3440 1755 2847 103 -945 291 C ATOM 2071 CD2 TYR A 286 25.795 24.467 -18.443 1.00 31.96 C ANISOU 2071 CD2 TYR A 286 4814 3113 4217 103 -953 296 C ATOM 2072 CE1 TYR A 286 26.206 21.755 -17.996 1.00 27.50 C ANISOU 2072 CE1 TYR A 286 4248 2557 3642 103 -937 297 C ATOM 2073 CE2 TYR A 286 26.318 23.658 -19.475 1.00 27.19 C ANISOU 2073 CE2 TYR A 286 4216 2508 3605 103 -944 302 C ATOM 2074 CZ TYR A 286 26.520 22.298 -19.233 1.00 36.88 C ANISOU 2074 CZ TYR A 286 5443 3740 4828 104 -936 302 C ATOM 2075 OH TYR A 286 27.032 21.466 -20.206 1.00 35.04 O ANISOU 2075 OH TYR A 286 5217 3507 4588 104 -928 308 O ATOM 2076 N VAL A 287 22.562 23.075 -14.848 1.00 33.93 N ANISOU 2076 N VAL A 287 5044 3376 4472 103 -970 268 N ATOM 2077 CA VAL A 287 21.805 21.826 -14.696 1.00 34.05 C ANISOU 2077 CA VAL A 287 5060 3395 4482 104 -970 263 C ATOM 2078 C VAL A 287 20.366 22.006 -15.170 1.00 30.23 C ANISOU 2078 C VAL A 287 4580 2909 3997 104 -980 257 C ATOM 2079 O VAL A 287 19.819 21.161 -15.890 1.00 30.76 O ANISOU 2079 O VAL A 287 4652 2976 4057 104 -979 257 O ATOM 2080 CB VAL A 287 21.824 21.316 -13.238 1.00 37.37 C ANISOU 2080 CB VAL A 287 5472 3820 4905 103 -968 259 C ATOM 2081 CG1 VAL A 287 20.844 20.139 -13.096 1.00 14.94 C ANISOU 2081 CG1 VAL A 287 2633 983 2060 103 -969 254 C ATOM 2082 CG2 VAL A 287 23.210 20.894 -12.774 1.00 24.06 C ANISOU 2082 CG2 VAL A 287 3784 2138 3220 103 -957 265 C ATOM 2083 N MET A 288 19.713 23.084 -14.732 1.00 31.34 N ANISOU 2083 N MET A 288 4717 3047 4143 104 -990 252 N ATOM 2084 CA MET A 288 18.318 23.313 -15.113 1.00 33.93 C ANISOU 2084 CA MET A 288 5047 3373 4471 105 -1000 246 C ATOM 2085 C MET A 288 18.156 23.406 -16.629 1.00 33.79 C ANISOU 2085 C MET A 288 5038 3351 4448 105 -1001 250 C ATOM 2086 O MET A 288 17.244 22.802 -17.210 1.00 33.26 O ANISOU 2086 O MET A 288 4977 3285 4377 105 -1004 248 O ATOM 2087 CB MET A 288 17.785 24.579 -14.434 1.00 32.75 C ANISOU 2087 CB MET A 288 4893 3222 4330 105 -1010 241 C ATOM 2088 CG MET A 288 17.378 24.323 -12.994 1.00 35.73 C ANISOU 2088 CG MET A 288 5261 3603 4711 105 -1012 235 C ATOM 2089 SD MET A 288 15.938 23.235 -12.970 1.00 38.53 S ANISOU 2089 SD MET A 288 5618 3961 5061 105 -1016 228 S ATOM 2090 CE MET A 288 15.452 23.249 -11.264 1.00 46.89 C ANISOU 2090 CE MET A 288 6667 5025 6126 105 -1020 220 C ATOM 2091 N GLU A 289 19.023 24.166 -17.291 1.00 28.63 N ANISOU 2091 N GLU A 289 4389 2694 3796 105 -998 257 N ATOM 2092 CA GLU A 289 18.836 24.348 -18.725 1.00 33.19 C ANISOU 2092 CA GLU A 289 4975 3267 4369 105 -1000 260 C ATOM 2093 C GLU A 289 19.039 23.028 -19.467 1.00 40.76 C ANISOU 2093 C GLU A 289 5940 4228 5319 105 -992 264 C ATOM 2094 O GLU A 289 18.241 22.683 -20.340 1.00 29.04 O ANISOU 2094 O GLU A 289 4461 2742 3829 105 -995 263 O ATOM 2095 CB GLU A 289 19.759 25.465 -19.241 1.00 28.01 C ANISOU 2095 CB GLU A 289 4321 2607 3716 105 -999 266 C ATOM 2096 CG GLU A 289 19.253 26.882 -18.870 1.00 29.64 C ANISOU 2096 CG GLU A 289 4523 2809 3929 105 -1009 262 C ATOM 2097 CD GLU A 289 19.812 28.029 -19.740 1.00 36.78 C ANISOU 2097 CD GLU A 289 5432 3708 4836 105 -1011 268 C ATOM 2098 OE1 GLU A 289 20.428 27.775 -20.799 1.00 33.39 O ANISOU 2098 OE1 GLU A 289 5009 3276 4401 105 -1005 274 O ATOM 2099 OE2 GLU A 289 19.608 29.207 -19.363 1.00 33.60 O ANISOU 2099 OE2 GLU A 289 5026 3303 4439 105 -1018 265 O ATOM 2100 N LYS A 290 20.032 22.227 -19.057 1.00 39.42 N ANISOU 2100 N LYS A 290 5768 4062 5148 105 -981 268 N ATOM 2101 CA LYS A 290 20.276 20.932 -19.682 1.00 30.21 C ANISOU 2101 CA LYS A 290 4608 2899 3974 105 -973 271 C ATOM 2102 C LYS A 290 19.150 19.931 -19.454 1.00 36.65 C ANISOU 2102 C LYS A 290 5423 3717 4785 105 -976 265 C ATOM 2103 O LYS A 290 19.031 18.961 -20.219 1.00 35.02 O ANISOU 2103 O LYS A 290 5223 3512 4572 105 -972 267 O ATOM 2104 CB LYS A 290 21.589 20.347 -19.170 1.00 23.46 C ANISOU 2104 CB LYS A 290 3749 2047 3118 105 -961 277 C ATOM 2105 CG LYS A 290 22.787 21.097 -19.717 1.00 33.40 C ANISOU 2105 CG LYS A 290 5010 3302 4379 104 -956 285 C ATOM 2106 CD LYS A 290 22.772 21.136 -21.252 1.00 32.93 C ANISOU 2106 CD LYS A 290 4960 3238 4314 105 -956 289 C ATOM 2107 CE LYS A 290 24.017 21.844 -21.755 1.00 44.63 C ANISOU 2107 CE LYS A 290 6443 4717 5797 105 -950 297 C ATOM 2108 NZ LYS A 290 23.971 22.172 -23.199 1.00 48.57 N ANISOU 2108 NZ LYS A 290 6951 5211 6292 105 -951 302 N ATOM 2109 N ALA A 291 18.323 20.142 -18.434 1.00 30.21 N ANISOU 2109 N ALA A 291 4601 2904 3974 105 -983 258 N ATOM 2110 CA ALA A 291 17.162 19.307 -18.179 1.00 30.62 C ANISOU 2110 CA ALA A 291 4653 2959 4024 105 -987 251 C ATOM 2111 C ALA A 291 15.875 19.934 -18.702 1.00 30.86 C ANISOU 2111 C ALA A 291 4687 2986 4055 106 -999 246 C ATOM 2112 O ALA A 291 14.785 19.431 -18.402 1.00 30.28 O ANISOU 2112 O ALA A 291 4612 2914 3979 106 -1004 240 O ATOM 2113 CB ALA A 291 17.051 19.014 -16.673 1.00 33.15 C ANISOU 2113 CB ALA A 291 4964 3283 4347 105 -987 246 C ATOM 2114 N GLY A 292 15.986 21.010 -19.490 1.00 35.69 N ANISOU 2114 N GLY A 292 5302 3592 4668 106 -1003 249 N ATOM 2115 CA GLY A 292 14.839 21.674 -20.085 1.00 26.02 C ANISOU 2115 CA GLY A 292 4081 2364 3444 106 -1014 245 C ATOM 2116 C GLY A 292 14.120 22.722 -19.256 1.00 33.78 C ANISOU 2116 C GLY A 292 5057 3345 4434 106 -1024 239 C ATOM 2117 O GLY A 292 12.949 22.990 -19.537 1.00 40.18 O ANISOU 2117 O GLY A 292 5869 4154 5245 107 -1033 233 O ATOM 2118 N GLY A 293 14.753 23.300 -18.228 1.00 36.10 N ANISOU 2118 N GLY A 293 5343 3640 4735 106 -1023 238 N ATOM 2119 CA GLY A 293 14.148 24.336 -17.419 1.00 29.10 C ANISOU 2119 CA GLY A 293 4450 2752 3855 107 -1032 232 C ATOM 2120 C GLY A 293 14.740 25.716 -17.667 1.00 33.67 C ANISOU 2120 C GLY A 293 5028 3325 4438 107 -1035 236 C ATOM 2121 O GLY A 293 15.495 25.939 -18.618 1.00 26.30 O ANISOU 2121 O GLY A 293 4100 2389 3503 106 -1030 243 O ATOM 2122 N MET A 294 14.404 26.654 -16.767 1.00 33.27 N ANISOU 2122 N MET A 294 4971 3274 4395 107 -1042 231 N ATOM 2123 CA MET A 294 14.825 28.051 -16.909 1.00 42.95 C ANISOU 2123 CA MET A 294 6196 4495 5627 107 -1046 233 C ATOM 2124 C MET A 294 15.435 28.589 -15.617 1.00 40.52 C ANISOU 2124 C MET A 294 5880 4189 5326 107 -1045 232 C ATOM 2125 O MET A 294 15.149 28.100 -14.524 1.00 50.09 O ANISOU 2125 O MET A 294 7086 5406 6541 107 -1044 227 O ATOM 2126 CB MET A 294 13.675 29.013 -17.291 1.00 49.98 C ANISOU 2126 CB MET A 294 7088 5381 6520 108 -1058 228 C ATOM 2127 CG MET A 294 13.086 28.916 -18.677 1.00 57.97 C ANISOU 2127 CG MET A 294 8109 6390 7527 108 -1061 230 C ATOM 2128 SD MET A 294 11.844 30.234 -18.935 1.00 49.97 S ANISOU 2128 SD MET A 294 7096 5371 6518 109 -1076 224 S ATOM 2129 CE MET A 294 12.835 31.684 -18.625 1.00 53.81 C ANISOU 2129 CE MET A 294 7579 5855 7012 109 -1076 227 C ATOM 2130 N ALA A 295 16.257 29.637 -15.759 1.00 35.42 N ANISOU 2130 N ALA A 295 5234 3540 4685 106 -1044 236 N ATOM 2131 CA ALA A 295 16.884 30.303 -14.612 1.00 34.81 C ANISOU 2131 CA ALA A 295 5149 3464 4614 106 -1044 235 C ATOM 2132 C ALA A 295 17.230 31.738 -15.002 1.00 37.86 C ANISOU 2132 C ALA A 295 5536 3844 5005 106 -1048 238 C ATOM 2133 O ALA A 295 18.094 31.945 -15.863 1.00 32.88 O ANISOU 2133 O ALA A 295 4910 3211 4371 106 -1043 245 O ATOM 2134 CB ALA A 295 18.129 29.539 -14.146 1.00 29.31 C ANISOU 2134 CB ALA A 295 4450 2771 3916 105 -1032 240 C ATOM 2135 N THR A 296 16.564 32.718 -14.364 1.00 33.28 N ANISOU 2135 N THR A 296 4951 3262 4431 106 -1058 232 N ATOM 2136 CA THR A 296 16.720 34.143 -14.652 1.00 28.68 C ANISOU 2136 CA THR A 296 4369 2675 3854 106 -1064 233 C ATOM 2137 C THR A 296 17.014 34.934 -13.375 1.00 41.56 C ANISOU 2137 C THR A 296 5992 4307 5493 106 -1066 230 C ATOM 2138 O THR A 296 16.755 34.470 -12.259 1.00 44.01 O ANISOU 2138 O THR A 296 6295 4620 5805 106 -1066 225 O ATOM 2139 CB THR A 296 15.466 34.743 -15.312 1.00 37.42 C ANISOU 2139 CB THR A 296 5479 3777 4960 107 -1075 229 C ATOM 2140 OG1 THR A 296 15.652 36.155 -15.521 1.00 39.94 O ANISOU 2140 OG1 THR A 296 5799 4092 5286 107 -1081 230 O ATOM 2141 CG2 THR A 296 14.239 34.522 -14.429 1.00 32.52 C ANISOU 2141 CG2 THR A 296 4854 3160 4343 108 -1082 220 C ATOM 2142 N THR A 297 17.576 36.146 -13.553 1.00 37.18 N ANISOU 2142 N THR A 297 5436 3747 4942 106 -1069 233 N ATOM 2143 CA THR A 297 17.662 37.130 -12.476 1.00 34.54 C ANISOU 2143 CA THR A 297 5095 3412 4615 106 -1074 230 C ATOM 2144 C THR A 297 16.459 38.055 -12.417 1.00 34.65 C ANISOU 2144 C THR A 297 5108 3423 4634 107 -1086 223 C ATOM 2145 O THR A 297 16.332 38.818 -11.454 1.00 35.13 O ANISOU 2145 O THR A 297 5162 3483 4701 107 -1091 219 O ATOM 2146 CB THR A 297 18.887 38.040 -12.631 1.00 26.62 C ANISOU 2146 CB THR A 297 4092 2406 3616 105 -1070 236 C ATOM 2147 OG1 THR A 297 18.654 38.959 -13.716 1.00 31.61 O ANISOU 2147 OG1 THR A 297 4730 3032 4248 105 -1076 238 O ATOM 2148 CG2 THR A 297 20.140 37.231 -12.900 1.00 23.66 C ANISOU 2148 CG2 THR A 297 3720 2034 3237 104 -1058 244 C ATOM 2149 N GLY A 298 15.566 38.000 -13.395 1.00 37.51 N ANISOU 2149 N GLY A 298 5477 3783 4993 108 -1091 222 N ATOM 2150 CA GLY A 298 14.560 39.035 -13.498 1.00 37.98 C ANISOU 2150 CA GLY A 298 5536 3839 5057 109 -1103 216 C ATOM 2151 C GLY A 298 14.858 40.025 -14.610 1.00 42.27 C ANISOU 2151 C GLY A 298 6085 4376 5600 109 -1106 221 C ATOM 2152 O GLY A 298 13.941 40.452 -15.317 1.00 43.01 O ANISOU 2152 O GLY A 298 6183 4466 5693 109 -1114 219 O ATOM 2153 N LYS A 299 16.120 40.429 -14.761 1.00 48.95 N ANISOU 2153 N LYS A 299 6932 5220 6447 107 -1100 228 N ATOM 2154 CA LYS A 299 16.509 41.295 -15.874 1.00 46.08 C ANISOU 2154 CA LYS A 299 6575 4851 6083 107 -1102 234 C ATOM 2155 C LYS A 299 17.191 40.552 -17.012 1.00 44.62 C ANISOU 2155 C LYS A 299 6397 4666 5891 106 -1093 241 C ATOM 2156 O LYS A 299 17.137 41.023 -18.150 1.00 43.81 O ANISOU 2156 O LYS A 299 6301 4559 5786 106 -1095 245 O ATOM 2157 CB LYS A 299 17.429 42.432 -15.401 1.00 39.87 C ANISOU 2157 CB LYS A 299 5785 4062 5303 106 -1102 236 C ATOM 2158 CG LYS A 299 16.720 43.483 -14.548 1.00 50.22 C ANISOU 2158 CG LYS A 299 7089 5371 6621 107 -1112 229 C ATOM 2159 CD LYS A 299 17.689 44.483 -13.909 1.00 59.94 C ANISOU 2159 CD LYS A 299 8316 6600 7858 106 -1111 232 C ATOM 2160 CE LYS A 299 16.951 45.422 -12.963 1.00 67.21 C ANISOU 2160 CE LYS A 299 9230 7519 8786 107 -1121 224 C ATOM 2161 NZ LYS A 299 17.869 46.256 -12.138 1.00 72.28 N ANISOU 2161 NZ LYS A 299 9867 8161 9434 106 -1120 226 N ATOM 2162 N GLU A 300 17.821 39.406 -16.735 1.00 44.49 N ANISOU 2162 N GLU A 300 6380 4655 5871 106 -1083 244 N ATOM 2163 CA GLU A 300 18.613 38.685 -17.726 1.00 42.21 C ANISOU 2163 CA GLU A 300 6097 4366 5575 105 -1074 252 C ATOM 2164 C GLU A 300 18.801 37.240 -17.282 1.00 40.20 C ANISOU 2164 C GLU A 300 5841 4117 5316 105 -1065 252 C ATOM 2165 O GLU A 300 18.475 36.867 -16.153 1.00 41.93 O ANISOU 2165 O GLU A 300 6054 4340 5538 105 -1066 246 O ATOM 2166 CB GLU A 300 19.961 39.377 -17.935 1.00 38.91 C ANISOU 2166 CB GLU A 300 5680 3945 5160 104 -1068 259 C ATOM 2167 CG GLU A 300 20.705 39.570 -16.655 1.00 47.99 C ANISOU 2167 CG GLU A 300 6822 5098 6315 104 -1065 259 C ATOM 2168 CD GLU A 300 21.824 40.572 -16.782 1.00 56.00 C ANISOU 2168 CD GLU A 300 7836 6108 7332 103 -1062 265 C ATOM 2169 OE1 GLU A 300 22.419 40.676 -17.873 1.00 56.10 O ANISOU 2169 OE1 GLU A 300 7855 6118 7342 102 -1058 272 O ATOM 2170 OE2 GLU A 300 22.099 41.267 -15.782 1.00 62.22 O ANISOU 2170 OE2 GLU A 300 8617 6896 8127 102 -1065 263 O ATOM 2171 N ALA A 301 19.313 36.425 -18.202 1.00 37.58 N ANISOU 2171 N ALA A 301 5516 3786 4978 105 -1057 258 N ATOM 2172 CA ALA A 301 19.669 35.041 -17.888 1.00 36.98 C ANISOU 2172 CA ALA A 301 5439 3716 4897 105 -1048 259 C ATOM 2173 C ALA A 301 20.857 34.968 -16.934 1.00 31.41 C ANISOU 2173 C ALA A 301 4727 3012 4194 104 -1040 262 C ATOM 2174 O ALA A 301 21.830 35.714 -17.078 1.00 38.89 O ANISOU 2174 O ALA A 301 5674 3957 5144 103 -1037 267 O ATOM 2175 CB ALA A 301 19.996 34.267 -19.173 1.00 22.01 C ANISOU 2175 CB ALA A 301 3551 1818 2993 105 -1041 265 C ATOM 2176 N VAL A 302 20.776 34.054 -15.953 1.00 24.74 N ANISOU 2176 N VAL A 302 3876 2173 3349 104 -1036 259 N ATOM 2177 CA VAL A 302 21.894 33.844 -15.026 1.00 19.53 C ANISOU 2177 CA VAL A 302 3211 1516 2692 103 -1028 261 C ATOM 2178 C VAL A 302 23.183 33.539 -15.785 1.00 22.82 C ANISOU 2178 C VAL A 302 3633 1933 3105 103 -1018 271 C ATOM 2179 O VAL A 302 24.243 34.129 -15.530 1.00 22.72 O ANISOU 2179 O VAL A 302 3617 1919 3096 102 -1014 275 O ATOM 2180 CB VAL A 302 21.568 32.704 -14.039 1.00 23.85 C ANISOU 2180 CB VAL A 302 3754 2070 3239 103 -1025 257 C ATOM 2181 CG1 VAL A 302 22.806 32.287 -13.301 1.00 23.63 C ANISOU 2181 CG1 VAL A 302 3721 2046 3211 102 -1015 261 C ATOM 2182 CG2 VAL A 302 20.504 33.137 -13.039 1.00 21.80 C ANISOU 2182 CG2 VAL A 302 3488 1811 2984 104 -1035 248 C ATOM 2183 N LEU A 303 23.100 32.626 -16.751 1.00 30.78 N ANISOU 2183 N LEU A 303 4648 2942 4107 103 -1013 274 N ATOM 2184 CA LEU A 303 24.262 32.176 -17.500 1.00 30.90 C ANISOU 2184 CA LEU A 303 4667 2956 4117 102 -1002 283 C ATOM 2185 C LEU A 303 24.842 33.258 -18.417 1.00 30.81 C ANISOU 2185 C LEU A 303 4660 2939 4107 102 -1003 288 C ATOM 2186 O LEU A 303 25.960 33.077 -18.915 1.00 38.24 O ANISOU 2186 O LEU A 303 5603 3879 5045 102 -994 296 O ATOM 2187 CB LEU A 303 23.875 30.931 -18.312 1.00 30.44 C ANISOU 2187 CB LEU A 303 4615 2900 4050 103 -998 284 C ATOM 2188 CG LEU A 303 23.454 29.643 -17.580 1.00 31.53 C ANISOU 2188 CG LEU A 303 4750 3044 4186 103 -995 279 C ATOM 2189 CD1 LEU A 303 23.044 28.564 -18.595 1.00 23.69 C ANISOU 2189 CD1 LEU A 303 3765 2052 3185 104 -992 281 C ATOM 2190 CD2 LEU A 303 24.545 29.096 -16.656 1.00 29.12 C ANISOU 2190 CD2 LEU A 303 4440 2743 3883 103 -985 282 C ATOM 2191 N ASP A 304 24.127 34.368 -18.655 1.00 19.79 N ANISOU 2191 N ASP A 304 3265 1539 2715 102 -1014 285 N ATOM 2192 CA ASP A 304 24.638 35.469 -19.473 1.00 27.00 C ANISOU 2192 CA ASP A 304 4183 2447 3630 102 -1015 290 C ATOM 2193 C ASP A 304 25.275 36.617 -18.679 1.00 43.44 C ANISOU 2193 C ASP A 304 6259 4527 5719 101 -1017 291 C ATOM 2194 O ASP A 304 25.856 37.519 -19.295 1.00 48.06 O ANISOU 2194 O ASP A 304 6847 5108 6306 101 -1018 296 O ATOM 2195 CB ASP A 304 23.514 36.063 -20.330 1.00 33.15 C ANISOU 2195 CB ASP A 304 4966 3221 4407 102 -1026 287 C ATOM 2196 CG ASP A 304 23.082 35.151 -21.425 1.00 38.86 C ANISOU 2196 CG ASP A 304 5698 3945 5123 103 -1023 289 C ATOM 2197 OD1 ASP A 304 23.948 34.398 -21.935 1.00 42.82 O ANISOU 2197 OD1 ASP A 304 6202 4447 5619 103 -1013 295 O ATOM 2198 OD2 ASP A 304 21.874 35.178 -21.757 1.00 41.91 O ANISOU 2198 OD2 ASP A 304 6086 4329 5508 104 -1032 283 O ATOM 2199 N VAL A 305 25.187 36.629 -17.347 1.00 38.55 N ANISOU 2199 N VAL A 305 5632 3912 5106 101 -1019 286 N ATOM 2200 CA VAL A 305 25.813 37.709 -16.595 1.00 30.32 C ANISOU 2200 CA VAL A 305 4583 2867 4070 100 -1021 286 C ATOM 2201 C VAL A 305 27.322 37.581 -16.699 1.00 35.76 C ANISOU 2201 C VAL A 305 5272 3557 4759 100 -1010 295 C ATOM 2202 O VAL A 305 27.883 36.483 -16.579 1.00 38.87 O ANISOU 2202 O VAL A 305 5666 3954 5148 99 -1001 298 O ATOM 2203 CB VAL A 305 25.347 37.726 -15.134 1.00 30.47 C ANISOU 2203 CB VAL A 305 4594 2890 4094 101 -1025 279 C ATOM 2204 CG1 VAL A 305 26.119 38.810 -14.359 1.00 25.72 C ANISOU 2204 CG1 VAL A 305 3986 2286 3500 100 -1026 280 C ATOM 2205 CG2 VAL A 305 23.834 38.016 -15.050 1.00 15.83 C ANISOU 2205 CG2 VAL A 305 2739 1035 2241 101 -1037 270 C ATOM 2206 N ILE A 306 27.982 38.699 -16.971 1.00 42.28 N ANISOU 2206 N ILE A 306 6098 4377 5588 99 -1011 299 N ATOM 2207 CA ILE A 306 29.436 38.761 -17.054 1.00 39.83 C ANISOU 2207 CA ILE A 306 5788 4067 5278 98 -1002 307 C ATOM 2208 C ILE A 306 29.956 39.217 -15.690 1.00 42.73 C ANISOU 2208 C ILE A 306 6147 4436 5652 97 -1002 305 C ATOM 2209 O ILE A 306 29.641 40.335 -15.265 1.00 38.34 O ANISOU 2209 O ILE A 306 5587 3878 5102 97 -1010 302 O ATOM 2210 CB ILE A 306 29.894 39.712 -18.162 1.00 39.69 C ANISOU 2210 CB ILE A 306 5776 4043 5260 98 -1003 313 C ATOM 2211 CG1 ILE A 306 29.408 39.201 -19.515 1.00 39.33 C ANISOU 2211 CG1 ILE A 306 5739 3996 5208 98 -1002 315 C ATOM 2212 CG2 ILE A 306 31.416 39.766 -18.197 1.00 39.07 C ANISOU 2212 CG2 ILE A 306 5697 3964 5182 97 -993 322 C ATOM 2213 CD1 ILE A 306 30.030 39.925 -20.669 1.00 32.38 C ANISOU 2213 CD1 ILE A 306 4866 3111 4327 98 -1001 322 C ATOM 2214 N PRO A 307 30.691 38.387 -14.966 1.00 35.80 N ANISOU 2214 N PRO A 307 5264 3563 4774 97 -993 307 N ATOM 2215 CA PRO A 307 31.086 38.786 -13.620 1.00 34.59 C ANISOU 2215 CA PRO A 307 5103 3413 4628 96 -994 305 C ATOM 2216 C PRO A 307 32.295 39.710 -13.641 1.00 44.10 C ANISOU 2216 C PRO A 307 6306 4614 5836 95 -991 311 C ATOM 2217 O PRO A 307 33.151 39.635 -14.526 1.00 43.00 O ANISOU 2217 O PRO A 307 6172 4472 5694 95 -984 319 O ATOM 2218 CB PRO A 307 31.400 37.447 -12.939 1.00 29.09 C ANISOU 2218 CB PRO A 307 4403 2722 3928 96 -985 304 C ATOM 2219 CG PRO A 307 31.794 36.558 -14.045 1.00 39.50 C ANISOU 2219 CG PRO A 307 5728 4040 5239 97 -977 311 C ATOM 2220 CD PRO A 307 31.002 36.975 -15.249 1.00 34.36 C ANISOU 2220 CD PRO A 307 5084 3385 4585 97 -983 310 C ATOM 2221 N THR A 308 32.345 40.588 -12.626 1.00 38.32 N ANISOU 2221 N THR A 308 5568 3881 5111 94 -996 307 N ATOM 2222 CA THR A 308 33.478 41.464 -12.349 1.00 34.09 C ANISOU 2222 CA THR A 308 5030 3343 4581 93 -994 313 C ATOM 2223 C THR A 308 34.164 41.141 -11.027 1.00 36.13 C ANISOU 2223 C THR A 308 5280 3606 4842 92 -989 312 C ATOM 2224 O THR A 308 35.275 41.621 -10.797 1.00 40.43 O ANISOU 2224 O THR A 308 5822 4149 5390 91 -984 317 O ATOM 2225 CB THR A 308 33.055 42.949 -12.322 1.00 29.28 C ANISOU 2225 CB THR A 308 4419 2729 3977 93 -1004 310 C ATOM 2226 OG1 THR A 308 32.125 43.156 -11.258 1.00 37.31 O ANISOU 2226 OG1 THR A 308 5430 3747 4997 93 -1013 301 O ATOM 2227 CG2 THR A 308 32.431 43.421 -13.655 1.00 23.43 C ANISOU 2227 CG2 THR A 308 3686 1983 3233 94 -1010 311 C ATOM 2228 N ASP A 309 33.558 40.317 -10.175 1.00 27.29 N ANISOU 2228 N ASP A 309 4156 2490 3722 93 -989 306 N ATOM 2229 CA ASP A 309 34.148 39.926 -8.900 1.00 30.87 C ANISOU 2229 CA ASP A 309 4602 2948 4178 92 -985 305 C ATOM 2230 C ASP A 309 33.835 38.453 -8.653 1.00 31.54 C ANISOU 2230 C ASP A 309 4687 3039 4259 93 -979 303 C ATOM 2231 O ASP A 309 32.671 38.059 -8.771 1.00 34.72 O ANISOU 2231 O ASP A 309 5090 3442 4658 94 -984 297 O ATOM 2232 CB ASP A 309 33.580 40.807 -7.773 1.00 31.74 C ANISOU 2232 CB ASP A 309 4705 3058 4295 92 -994 298 C ATOM 2233 CG ASP A 309 34.215 40.521 -6.420 1.00 43.12 C ANISOU 2233 CG ASP A 309 6139 4504 5741 91 -990 297 C ATOM 2234 OD1 ASP A 309 35.031 41.336 -5.938 1.00 49.33 O ANISOU 2234 OD1 ASP A 309 6922 5289 6533 90 -990 299 O ATOM 2235 OD2 ASP A 309 33.886 39.475 -5.835 1.00 43.89 O ANISOU 2235 OD2 ASP A 309 6233 4606 5836 91 -987 293 O ATOM 2236 N ILE A 310 34.845 37.644 -8.280 1.00 34.86 N ANISOU 2236 N ILE A 310 5104 3463 4677 92 -969 307 N ATOM 2237 CA ILE A 310 34.614 36.188 -8.180 1.00 39.03 C ANISOU 2237 CA ILE A 310 5633 3997 5201 93 -963 306 C ATOM 2238 C ILE A 310 33.616 35.846 -7.075 1.00 39.57 C ANISOU 2238 C ILE A 310 5696 4069 5271 93 -969 297 C ATOM 2239 O ILE A 310 33.048 34.749 -7.079 1.00 31.94 O ANISOU 2239 O ILE A 310 4731 3106 4300 94 -967 294 O ATOM 2240 CB ILE A 310 35.887 35.335 -7.955 1.00 29.78 C ANISOU 2240 CB ILE A 310 4460 2829 4028 92 -950 313 C ATOM 2241 CG1 ILE A 310 36.606 35.701 -6.668 1.00 28.52 C ANISOU 2241 CG1 ILE A 310 4293 2671 3874 91 -949 312 C ATOM 2242 CG2 ILE A 310 36.835 35.427 -9.129 1.00 31.27 C ANISOU 2242 CG2 ILE A 310 4655 3014 4213 92 -943 322 C ATOM 2243 CD1 ILE A 310 37.750 34.767 -6.339 1.00 26.14 C ANISOU 2243 CD1 ILE A 310 3988 2372 3570 90 -938 318 C ATOM 2244 N HIS A 311 33.399 36.748 -6.116 1.00 33.64 N ANISOU 2244 N HIS A 311 4939 3317 4526 92 -976 292 N ATOM 2245 CA HIS A 311 32.433 36.545 -5.043 1.00 24.75 C ANISOU 2245 CA HIS A 311 3808 2194 3402 93 -982 284 C ATOM 2246 C HIS A 311 31.220 37.460 -5.165 1.00 23.69 C ANISOU 2246 C HIS A 311 3674 2056 3270 94 -994 277 C ATOM 2247 O HIS A 311 30.541 37.718 -4.167 1.00 30.81 O ANISOU 2247 O HIS A 311 4571 2959 4176 94 -1001 270 O ATOM 2248 CB HIS A 311 33.117 36.707 -3.687 1.00 21.33 C ANISOU 2248 CB HIS A 311 3367 1764 2975 92 -980 283 C ATOM 2249 CG HIS A 311 34.109 35.626 -3.402 1.00 24.55 C ANISOU 2249 CG HIS A 311 3772 2175 3379 91 -968 288 C ATOM 2250 ND1 HIS A 311 33.743 34.299 -3.289 1.00 24.39 N ANISOU 2250 ND1 HIS A 311 3753 2160 3355 92 -964 286 N ATOM 2251 CD2 HIS A 311 35.451 35.661 -3.250 1.00 22.50 C ANISOU 2251 CD2 HIS A 311 3511 1916 3121 90 -960 294 C ATOM 2252 CE1 HIS A 311 34.818 33.565 -3.070 1.00 22.40 C ANISOU 2252 CE1 HIS A 311 3499 1910 3100 91 -954 291 C ATOM 2253 NE2 HIS A 311 35.868 34.369 -3.042 1.00 24.42 N ANISOU 2253 NE2 HIS A 311 3754 2163 3360 90 -951 296 N ATOM 2254 N GLN A 312 30.917 37.929 -6.372 1.00 18.50 N ANISOU 2254 N GLN A 312 3023 1394 2610 94 -997 279 N ATOM 2255 CA GLN A 312 29.753 38.781 -6.572 1.00 31.91 C ANISOU 2255 CA GLN A 312 4723 3089 4311 95 -1009 273 C ATOM 2256 C GLN A 312 28.465 37.962 -6.496 1.00 32.46 C ANISOU 2256 C GLN A 312 4793 3162 4378 96 -1013 266 C ATOM 2257 O GLN A 312 28.430 36.771 -6.825 1.00 33.72 O ANISOU 2257 O GLN A 312 4955 3325 4531 96 -1007 268 O ATOM 2258 CB GLN A 312 29.828 39.523 -7.926 1.00 33.61 C ANISOU 2258 CB GLN A 312 4945 3299 4525 95 -1011 278 C ATOM 2259 CG GLN A 312 29.123 38.859 -9.110 1.00 27.89 C ANISOU 2259 CG GLN A 312 4228 2574 3793 96 -1011 279 C ATOM 2260 CD GLN A 312 29.204 39.708 -10.398 1.00 39.07 C ANISOU 2260 CD GLN A 312 5652 3984 5209 96 -1014 283 C ATOM 2261 OE1 GLN A 312 30.275 40.209 -10.778 1.00 34.20 O ANISOU 2261 OE1 GLN A 312 5037 3365 4593 95 -1009 290 O ATOM 2262 NE2 GLN A 312 28.051 39.909 -11.042 1.00 35.12 N ANISOU 2262 NE2 GLN A 312 5156 3481 4707 97 -1022 279 N ATOM 2263 N ARG A 313 27.394 38.624 -6.077 1.00 28.59 N ANISOU 2263 N ARG A 313 4301 2671 3891 97 -1023 259 N ATOM 2264 CA ARG A 313 26.105 37.986 -5.881 1.00 30.02 C ANISOU 2264 CA ARG A 313 4482 2854 4070 98 -1028 252 C ATOM 2265 C ARG A 313 25.187 38.228 -7.076 1.00 31.18 C ANISOU 2265 C ARG A 313 4635 2997 4213 99 -1034 251 C ATOM 2266 O ARG A 313 25.403 39.127 -7.892 1.00 31.91 O ANISOU 2266 O ARG A 313 4732 3084 4307 99 -1037 254 O ATOM 2267 CB ARG A 313 25.452 38.503 -4.593 1.00 42.09 C ANISOU 2267 CB ARG A 313 6003 4384 5605 98 -1036 244 C ATOM 2268 CG ARG A 313 26.379 38.455 -3.382 1.00 55.17 C ANISOU 2268 CG ARG A 313 7652 6043 7265 97 -1031 245 C ATOM 2269 CD ARG A 313 25.710 38.973 -2.125 1.00 67.91 C ANISOU 2269 CD ARG A 313 9259 7658 8885 97 -1039 236 C ATOM 2270 NE ARG A 313 25.608 37.931 -1.101 1.00 81.02 N ANISOU 2270 NE ARG A 313 10914 9324 10544 97 -1035 233 N ATOM 2271 CZ ARG A 313 26.242 37.954 0.069 1.00 85.65 C ANISOU 2271 CZ ARG A 313 11495 9914 11136 96 -1032 232 C ATOM 2272 NH1 ARG A 313 27.031 38.975 0.385 1.00 87.18 N ANISOU 2272 NH1 ARG A 313 11685 10104 11334 95 -1033 235 N ATOM 2273 NH2 ARG A 313 26.084 36.953 0.927 1.00 86.68 N ANISOU 2273 NH2 ARG A 313 11621 10049 11264 96 -1028 229 N ATOM 2274 N ALA A 314 24.129 37.421 -7.150 1.00 31.27 N ANISOU 2274 N ALA A 314 4648 3011 4221 100 -1037 246 N ATOM 2275 CA ALA A 314 23.152 37.557 -8.209 1.00 33.33 C ANISOU 2275 CA ALA A 314 4916 3269 4480 101 -1043 244 C ATOM 2276 C ALA A 314 21.836 36.989 -7.713 1.00 37.08 C ANISOU 2276 C ALA A 314 5388 3747 4953 102 -1049 236 C ATOM 2277 O ALA A 314 21.835 35.945 -7.039 1.00 28.83 O ANISOU 2277 O ALA A 314 4341 2707 3907 102 -1044 234 O ATOM 2278 CB ALA A 314 23.603 36.832 -9.480 1.00 38.01 C ANISOU 2278 CB ALA A 314 5516 3861 5064 101 -1036 251 C ATOM 2279 N PRO A 315 20.713 37.611 -8.039 1.00 36.72 N ANISOU 2279 N PRO A 315 5345 3699 4910 103 -1059 231 N ATOM 2280 CA PRO A 315 19.424 36.994 -7.727 1.00 41.84 C ANISOU 2280 CA PRO A 315 5991 4349 5556 104 -1064 223 C ATOM 2281 C PRO A 315 19.135 35.859 -8.699 1.00 38.20 C ANISOU 2281 C PRO A 315 5538 3890 5088 104 -1059 225 C ATOM 2282 O PRO A 315 19.658 35.824 -9.813 1.00 31.64 O ANISOU 2282 O PRO A 315 4713 3057 4253 104 -1055 232 O ATOM 2283 CB PRO A 315 18.433 38.157 -7.884 1.00 44.95 C ANISOU 2283 CB PRO A 315 6386 4739 5954 105 -1076 218 C ATOM 2284 CG PRO A 315 19.092 39.106 -8.822 1.00 36.27 C ANISOU 2284 CG PRO A 315 5291 3634 4855 105 -1076 224 C ATOM 2285 CD PRO A 315 20.575 38.933 -8.682 1.00 31.64 C ANISOU 2285 CD PRO A 315 4703 3048 4269 103 -1066 231 C ATOM 2286 N VAL A 316 18.324 34.895 -8.255 1.00 43.21 N ANISOU 2286 N VAL A 316 6170 4529 5720 105 -1060 220 N ATOM 2287 CA VAL A 316 18.054 33.710 -9.069 1.00 40.42 C ANISOU 2287 CA VAL A 316 5822 4177 5358 105 -1055 222 C ATOM 2288 C VAL A 316 16.599 33.288 -8.893 1.00 34.72 C ANISOU 2288 C VAL A 316 5100 3457 4635 106 -1063 214 C ATOM 2289 O VAL A 316 16.051 33.335 -7.784 1.00 37.40 O ANISOU 2289 O VAL A 316 5433 3799 4979 106 -1067 208 O ATOM 2290 CB VAL A 316 19.023 32.554 -8.727 1.00 48.56 C ANISOU 2290 CB VAL A 316 6852 5213 6386 104 -1044 226 C ATOM 2291 CG1 VAL A 316 18.882 32.144 -7.264 1.00 50.94 C ANISOU 2291 CG1 VAL A 316 7146 5519 6691 104 -1043 221 C ATOM 2292 CG2 VAL A 316 18.838 31.371 -9.676 1.00 45.74 C ANISOU 2292 CG2 VAL A 316 6502 4857 6020 104 -1038 229 C ATOM 2293 N ILE A 317 15.961 32.936 -10.015 1.00 29.47 N ANISOU 2293 N ILE A 317 4442 2789 3965 107 -1064 215 N ATOM 2294 CA ILE A 317 14.631 32.326 -10.077 1.00 27.21 C ANISOU 2294 CA ILE A 317 4157 2505 3676 108 -1070 208 C ATOM 2295 C ILE A 317 14.699 31.179 -11.089 1.00 34.50 C ANISOU 2295 C ILE A 317 5087 3430 4591 107 -1064 212 C ATOM 2296 O ILE A 317 14.908 31.428 -12.284 1.00 35.73 O ANISOU 2296 O ILE A 317 5251 3582 4744 107 -1063 217 O ATOM 2297 CB ILE A 317 13.559 33.349 -10.518 1.00 18.24 C ANISOU 2297 CB ILE A 317 3023 1365 2543 109 -1082 204 C ATOM 2298 CG1 ILE A 317 13.442 34.521 -9.534 1.00 24.77 C ANISOU 2298 CG1 ILE A 317 3842 2190 3378 109 -1089 200 C ATOM 2299 CG2 ILE A 317 12.200 32.675 -10.767 1.00 19.78 C ANISOU 2299 CG2 ILE A 317 3219 1560 2734 110 -1087 198 C ATOM 2300 CD1 ILE A 317 14.278 35.762 -9.923 1.00 31.00 C ANISOU 2300 CD1 ILE A 317 4633 2974 4171 109 -1089 205 C ATOM 2301 N LEU A 318 14.475 29.935 -10.643 1.00 32.12 N ANISOU 2301 N LEU A 318 4784 3133 4285 107 -1059 210 N ATOM 2302 CA LEU A 318 14.687 28.801 -11.543 1.00 27.51 C ANISOU 2302 CA LEU A 318 4207 2551 3694 107 -1052 215 C ATOM 2303 C LEU A 318 13.639 27.705 -11.351 1.00 27.83 C ANISOU 2303 C LEU A 318 4248 2596 3731 107 -1053 209 C ATOM 2304 O LEU A 318 12.888 27.680 -10.375 1.00 27.70 O ANISOU 2304 O LEU A 318 4226 2582 3718 108 -1058 202 O ATOM 2305 CB LEU A 318 16.089 28.209 -11.388 1.00 29.63 C ANISOU 2305 CB LEU A 318 4475 2822 3960 106 -1040 222 C ATOM 2306 CG LEU A 318 16.579 27.679 -10.049 1.00 29.34 C ANISOU 2306 CG LEU A 318 4431 2791 3926 105 -1035 220 C ATOM 2307 CD1 LEU A 318 15.999 26.303 -9.765 1.00 27.41 C ANISOU 2307 CD1 LEU A 318 4186 2551 3677 105 -1032 217 C ATOM 2308 CD2 LEU A 318 18.082 27.631 -10.057 1.00 20.95 C ANISOU 2308 CD2 LEU A 318 3368 1728 2863 105 -1025 228 C ATOM 2309 N GLY A 319 13.595 26.787 -12.322 1.00 24.18 N ANISOU 2309 N GLY A 319 3793 2134 3262 107 -1049 213 N ATOM 2310 CA GLY A 319 12.670 25.665 -12.289 1.00 23.60 C ANISOU 2310 CA GLY A 319 3720 2064 3183 107 -1050 208 C ATOM 2311 C GLY A 319 11.960 25.364 -13.598 1.00 27.65 C ANISOU 2311 C GLY A 319 4242 2574 3690 108 -1053 209 C ATOM 2312 O GLY A 319 12.490 25.609 -14.693 1.00 30.70 O ANISOU 2312 O GLY A 319 4634 2957 4073 108 -1050 215 O ATOM 2313 N SER A 320 10.754 24.815 -13.475 1.00 23.78 N ANISOU 2313 N SER A 320 3751 2085 3198 108 -1058 203 N ATOM 2314 CA SER A 320 9.927 24.486 -14.626 1.00 29.13 C ANISOU 2314 CA SER A 320 4437 2761 3871 109 -1062 203 C ATOM 2315 C SER A 320 9.657 25.734 -15.470 1.00 39.59 C ANISOU 2315 C SER A 320 5765 4079 5198 109 -1069 203 C ATOM 2316 O SER A 320 9.326 26.793 -14.921 1.00 33.61 O ANISOU 2316 O SER A 320 5003 3320 4447 110 -1077 200 O ATOM 2317 CB SER A 320 8.599 23.907 -14.150 1.00 34.73 C ANISOU 2317 CB SER A 320 5144 3473 4580 109 -1068 195 C ATOM 2318 OG SER A 320 8.813 22.738 -13.397 1.00 36.06 O ANISOU 2318 OG SER A 320 5310 3648 4746 109 -1061 194 O ATOM 2319 N PRO A 321 9.679 25.615 -16.806 1.00 34.77 N ANISOU 2319 N PRO A 321 5163 3466 4582 109 -1068 208 N ATOM 2320 CA PRO A 321 9.629 26.820 -17.656 1.00 33.00 C ANISOU 2320 CA PRO A 321 4943 3236 4360 109 -1074 210 C ATOM 2321 C PRO A 321 8.324 27.610 -17.570 1.00 32.93 C ANISOU 2321 C PRO A 321 4933 3225 4356 110 -1087 203 C ATOM 2322 O PRO A 321 8.361 28.845 -17.610 1.00 37.44 O ANISOU 2322 O PRO A 321 5503 3792 4932 111 -1093 203 O ATOM 2323 CB PRO A 321 9.878 26.258 -19.066 1.00 33.82 C ANISOU 2323 CB PRO A 321 5057 3338 4456 109 -1070 216 C ATOM 2324 CG PRO A 321 9.461 24.821 -18.989 1.00 21.86 C ANISOU 2324 CG PRO A 321 3543 1827 2935 109 -1066 214 C ATOM 2325 CD PRO A 321 9.778 24.373 -17.592 1.00 30.52 C ANISOU 2325 CD PRO A 321 4632 2930 4036 109 -1062 211 C ATOM 2326 N ASP A 322 7.167 26.947 -17.542 1.00 36.70 N ANISOU 2326 N ASP A 322 5411 3704 4830 111 -1091 197 N ATOM 2327 CA ASP A 322 5.906 27.679 -17.408 1.00 37.08 C ANISOU 2327 CA ASP A 322 5456 3749 4883 112 -1103 191 C ATOM 2328 C ASP A 322 5.872 28.477 -16.111 1.00 40.23 C ANISOU 2328 C ASP A 322 5846 4149 5290 112 -1107 186 C ATOM 2329 O ASP A 322 5.331 29.590 -16.070 1.00 36.40 O ANISOU 2329 O ASP A 322 5359 3660 4810 113 -1116 183 O ATOM 2330 CB ASP A 322 4.709 26.722 -17.472 1.00 43.13 C ANISOU 2330 CB ASP A 322 6225 4518 5646 112 -1107 185 C ATOM 2331 CG ASP A 322 4.409 26.243 -18.886 1.00 46.20 C ANISOU 2331 CG ASP A 322 6622 4904 6027 112 -1107 189 C ATOM 2332 OD1 ASP A 322 5.124 26.678 -19.813 1.00 48.22 O ANISOU 2332 OD1 ASP A 322 6884 5157 6281 111 -1104 195 O ATOM 2333 OD2 ASP A 322 3.487 25.404 -19.068 1.00 39.62 O ANISOU 2333 OD2 ASP A 322 5791 4072 5189 112 -1109 185 O ATOM 2334 N ASP A 323 6.463 27.935 -15.041 1.00 38.37 N ANISOU 2334 N ASP A 323 5605 3918 5055 112 -1101 186 N ATOM 2335 CA ASP A 323 6.417 28.638 -13.765 1.00 31.35 C ANISOU 2335 CA ASP A 323 4707 3030 4174 112 -1104 181 C ATOM 2336 C ASP A 323 7.317 29.867 -13.774 1.00 29.46 C ANISOU 2336 C ASP A 323 4467 2787 3940 112 -1105 185 C ATOM 2337 O ASP A 323 6.898 30.943 -13.332 1.00 33.78 O ANISOU 2337 O ASP A 323 5009 3331 4493 113 -1112 181 O ATOM 2338 CB ASP A 323 6.794 27.689 -12.632 1.00 30.85 C ANISOU 2338 CB ASP A 323 4638 2973 4111 112 -1097 180 C ATOM 2339 CG ASP A 323 5.736 26.619 -12.386 1.00 33.81 C ANISOU 2339 CG ASP A 323 5012 3351 4482 112 -1099 174 C ATOM 2340 OD1 ASP A 323 4.544 26.963 -12.237 1.00 29.21 O ANISOU 2340 OD1 ASP A 323 4429 2768 3903 113 -1109 168 O ATOM 2341 OD2 ASP A 323 6.095 25.424 -12.342 1.00 38.69 O ANISOU 2341 OD2 ASP A 323 5632 3974 5096 111 -1091 176 O ATOM 2342 N VAL A 324 8.539 29.745 -14.295 1.00 30.42 N ANISOU 2342 N VAL A 324 4591 2908 4058 111 -1096 193 N ATOM 2343 CA VAL A 324 9.441 30.899 -14.348 1.00 34.16 C ANISOU 2343 CA VAL A 324 5064 3378 4536 111 -1096 197 C ATOM 2344 C VAL A 324 8.874 31.999 -15.253 1.00 38.97 C ANISOU 2344 C VAL A 324 5678 3981 5148 112 -1105 197 C ATOM 2345 O VAL A 324 8.981 33.195 -14.943 1.00 40.49 O ANISOU 2345 O VAL A 324 5867 4171 5346 112 -1110 196 O ATOM 2346 CB VAL A 324 10.841 30.461 -14.814 1.00 31.19 C ANISOU 2346 CB VAL A 324 4692 3003 4157 110 -1084 205 C ATOM 2347 CG1 VAL A 324 11.786 31.663 -14.861 1.00 21.81 C ANISOU 2347 CG1 VAL A 324 3503 1811 2973 109 -1084 210 C ATOM 2348 CG2 VAL A 324 11.381 29.327 -13.938 1.00 32.71 C ANISOU 2348 CG2 VAL A 324 4880 3201 4347 109 -1075 206 C ATOM 2349 N LEU A 325 8.251 31.615 -16.374 1.00 31.64 N ANISOU 2349 N LEU A 325 4757 3051 4214 112 -1107 197 N ATOM 2350 CA LEU A 325 7.654 32.606 -17.272 1.00 38.65 C ANISOU 2350 CA LEU A 325 5649 3933 5103 112 -1116 197 C ATOM 2351 C LEU A 325 6.553 33.390 -16.578 1.00 42.66 C ANISOU 2351 C LEU A 325 6151 4439 5617 114 -1127 189 C ATOM 2352 O LEU A 325 6.449 34.608 -16.755 1.00 42.06 O ANISOU 2352 O LEU A 325 6075 4359 5546 114 -1134 188 O ATOM 2353 CB LEU A 325 7.093 31.927 -18.519 1.00 32.16 C ANISOU 2353 CB LEU A 325 4836 3110 4274 112 -1116 198 C ATOM 2354 CG LEU A 325 8.129 31.429 -19.513 1.00 30.04 C ANISOU 2354 CG LEU A 325 4574 2841 3999 111 -1107 207 C ATOM 2355 CD1 LEU A 325 7.447 30.592 -20.546 1.00 26.92 C ANISOU 2355 CD1 LEU A 325 4187 2446 3597 111 -1107 207 C ATOM 2356 CD2 LEU A 325 8.779 32.633 -20.165 1.00 26.62 C ANISOU 2356 CD2 LEU A 325 4145 2403 3569 111 -1108 212 C ATOM 2357 N GLU A 326 5.714 32.707 -15.795 1.00 38.20 N ANISOU 2357 N GLU A 326 5582 3878 5052 114 -1129 182 N ATOM 2358 CA GLU A 326 4.639 33.405 -15.111 1.00 30.21 C ANISOU 2358 CA GLU A 326 4565 2866 4047 115 -1139 175 C ATOM 2359 C GLU A 326 5.203 34.408 -14.124 1.00 38.37 C ANISOU 2359 C GLU A 326 5592 3899 5088 116 -1140 174 C ATOM 2360 O GLU A 326 4.598 35.463 -13.886 1.00 42.58 O ANISOU 2360 O GLU A 326 6123 4429 5628 117 -1149 169 O ATOM 2361 CB GLU A 326 3.691 32.421 -14.427 1.00 35.73 C ANISOU 2361 CB GLU A 326 5261 3570 4745 116 -1140 168 C ATOM 2362 CG GLU A 326 2.457 33.112 -13.839 1.00 49.40 C ANISOU 2362 CG GLU A 326 6987 5299 6482 117 -1153 160 C ATOM 2363 CD GLU A 326 1.490 32.181 -13.131 1.00 57.99 C ANISOU 2363 CD GLU A 326 8073 6390 7569 117 -1157 153 C ATOM 2364 OE1 GLU A 326 1.572 30.950 -13.353 1.00 62.76 O ANISOU 2364 OE1 GLU A 326 8680 6998 8167 117 -1150 155 O ATOM 2365 OE2 GLU A 326 0.619 32.696 -12.384 1.00 55.26 O ANISOU 2365 OE2 GLU A 326 7723 6043 7230 118 -1167 146 O ATOM 2366 N PHE A 327 6.347 34.102 -13.525 1.00 38.87 N ANISOU 2366 N PHE A 327 5651 3965 5151 115 -1131 177 N ATOM 2367 CA PHE A 327 6.957 35.093 -12.650 1.00 41.24 C ANISOU 2367 CA PHE A 327 5946 4264 5458 115 -1132 177 C ATOM 2368 C PHE A 327 7.430 36.314 -13.434 1.00 39.54 C ANISOU 2368 C PHE A 327 5734 4043 5246 114 -1135 182 C ATOM 2369 O PHE A 327 7.221 37.456 -13.005 1.00 48.12 O ANISOU 2369 O PHE A 327 6818 5127 6339 115 -1142 179 O ATOM 2370 CB PHE A 327 8.120 34.487 -11.859 1.00 34.20 C ANISOU 2370 CB PHE A 327 5051 3378 4567 113 -1122 181 C ATOM 2371 CG PHE A 327 8.948 35.520 -11.182 1.00 24.01 C ANISOU 2371 CG PHE A 327 3755 2085 3283 113 -1122 182 C ATOM 2372 CD1 PHE A 327 10.087 36.017 -11.781 1.00 28.70 C ANISOU 2372 CD1 PHE A 327 4353 2677 3877 112 -1117 189 C ATOM 2373 CD2 PHE A 327 8.554 36.036 -9.966 1.00 29.92 C ANISOU 2373 CD2 PHE A 327 4495 2835 4038 114 -1127 176 C ATOM 2374 CE1 PHE A 327 10.815 37.020 -11.177 1.00 29.95 C ANISOU 2374 CE1 PHE A 327 4506 2832 4040 112 -1117 191 C ATOM 2375 CE2 PHE A 327 9.276 37.008 -9.362 1.00 31.36 C ANISOU 2375 CE2 PHE A 327 4674 3016 4226 113 -1127 177 C ATOM 2376 CZ PHE A 327 10.417 37.502 -9.967 1.00 33.16 C ANISOU 2376 CZ PHE A 327 4905 3241 4454 112 -1122 184 C ATOM 2377 N LEU A 328 8.061 36.096 -14.586 1.00 41.48 N ANISOU 2377 N LEU A 328 5988 4287 5486 114 -1130 189 N ATOM 2378 CA LEU A 328 8.588 37.213 -15.367 1.00 37.31 C ANISOU 2378 CA LEU A 328 5463 3753 4959 113 -1132 193 C ATOM 2379 C LEU A 328 7.478 38.142 -15.847 1.00 30.63 C ANISOU 2379 C LEU A 328 4620 2903 4117 115 -1144 189 C ATOM 2380 O LEU A 328 7.714 39.338 -16.034 1.00 38.45 O ANISOU 2380 O LEU A 328 5609 3888 5111 115 -1149 190 O ATOM 2381 CB LEU A 328 9.420 36.698 -16.546 1.00 35.72 C ANISOU 2381 CB LEU A 328 5270 3551 4751 112 -1124 202 C ATOM 2382 CG LEU A 328 10.804 36.169 -16.120 1.00 35.35 C ANISOU 2382 CG LEU A 328 5221 3507 4703 111 -1113 207 C ATOM 2383 CD1 LEU A 328 11.561 35.437 -17.245 1.00 21.04 C ANISOU 2383 CD1 LEU A 328 3417 1695 2884 110 -1104 215 C ATOM 2384 CD2 LEU A 328 11.657 37.285 -15.485 1.00 30.59 C ANISOU 2384 CD2 LEU A 328 4613 2902 4107 111 -1113 209 C ATOM 2385 N LYS A 329 6.283 37.612 -16.097 1.00 31.61 N ANISOU 2385 N LYS A 329 4744 3027 4238 115 -1150 184 N ATOM 2386 CA LYS A 329 5.172 38.469 -16.488 1.00 42.37 C ANISOU 2386 CA LYS A 329 6109 4386 5604 117 -1161 179 C ATOM 2387 C LYS A 329 4.810 39.462 -15.385 1.00 49.95 C ANISOU 2387 C LYS A 329 7061 5345 6572 118 -1168 174 C ATOM 2388 O LYS A 329 4.601 40.651 -15.661 1.00 47.22 O ANISOU 2388 O LYS A 329 6717 4995 6232 118 -1176 173 O ATOM 2389 CB LYS A 329 3.965 37.623 -16.880 1.00 44.42 C ANISOU 2389 CB LYS A 329 6372 4647 5860 117 -1165 175 C ATOM 2390 CG LYS A 329 2.801 38.465 -17.344 1.00 55.67 C ANISOU 2390 CG LYS A 329 7798 6067 7287 118 -1177 171 C ATOM 2391 CD LYS A 329 1.716 37.636 -18.004 1.00 60.79 C ANISOU 2391 CD LYS A 329 8451 6715 7930 119 -1180 168 C ATOM 2392 CE LYS A 329 0.618 38.531 -18.559 1.00 63.49 C ANISOU 2392 CE LYS A 329 8795 7053 8275 120 -1192 164 C ATOM 2393 NZ LYS A 329 -0.486 37.771 -19.207 1.00 66.50 N ANISOU 2393 NZ LYS A 329 9181 7434 8652 121 -1195 161 N ATOM 2394 N VAL A 330 4.719 38.989 -14.128 1.00 47.65 N ANISOU 2394 N VAL A 330 6763 5059 6284 118 -1166 169 N ATOM 2395 CA VAL A 330 4.423 39.878 -13.000 1.00 34.99 C ANISOU 2395 CA VAL A 330 5151 3455 4689 119 -1172 163 C ATOM 2396 C VAL A 330 5.548 40.886 -12.788 1.00 38.88 C ANISOU 2396 C VAL A 330 5642 3945 5185 118 -1170 168 C ATOM 2397 O VAL A 330 5.296 42.066 -12.505 1.00 40.10 O ANISOU 2397 O VAL A 330 5794 4096 5346 119 -1178 165 O ATOM 2398 CB VAL A 330 4.161 39.062 -11.715 1.00 35.23 C ANISOU 2398 CB VAL A 330 5175 3490 4720 119 -1172 158 C ATOM 2399 CG1 VAL A 330 3.928 39.990 -10.502 1.00 20.04 C ANISOU 2399 CG1 VAL A 330 3245 1566 2806 119 -1180 152 C ATOM 2400 CG2 VAL A 330 2.969 38.114 -11.891 1.00 25.09 C ANISOU 2400 CG2 VAL A 330 3893 2207 3432 119 -1176 153 C ATOM 2401 N TYR A 331 6.805 40.440 -12.913 1.00 32.61 N ANISOU 2401 N TYR A 331 4850 3153 4389 117 -1160 175 N ATOM 2402 CA TYR A 331 7.940 41.333 -12.699 1.00 26.38 C ANISOU 2402 CA TYR A 331 4059 2361 3602 116 -1157 179 C ATOM 2403 C TYR A 331 7.920 42.475 -13.704 1.00 42.94 C ANISOU 2403 C TYR A 331 6162 4452 5702 116 -1163 182 C ATOM 2404 O TYR A 331 8.209 43.631 -13.370 1.00 40.79 O ANISOU 2404 O TYR A 331 5886 4177 5435 116 -1168 182 O ATOM 2405 CB TYR A 331 9.252 40.543 -12.799 1.00 25.09 C ANISOU 2405 CB TYR A 331 3897 2201 3435 114 -1145 186 C ATOM 2406 CG TYR A 331 10.522 41.326 -12.497 1.00 31.59 C ANISOU 2406 CG TYR A 331 4718 3023 4262 113 -1141 191 C ATOM 2407 CD1 TYR A 331 11.190 42.027 -13.499 1.00 39.71 C ANISOU 2407 CD1 TYR A 331 5752 4046 5289 112 -1140 198 C ATOM 2408 CD2 TYR A 331 11.069 41.339 -11.219 1.00 46.56 C ANISOU 2408 CD2 TYR A 331 6607 4922 6163 113 -1138 190 C ATOM 2409 CE1 TYR A 331 12.341 42.736 -13.233 1.00 42.61 C ANISOU 2409 CE1 TYR A 331 6118 4412 5660 112 -1137 203 C ATOM 2410 CE2 TYR A 331 12.226 42.049 -10.944 1.00 52.21 C ANISOU 2410 CE2 TYR A 331 7321 5636 6882 112 -1134 195 C ATOM 2411 CZ TYR A 331 12.854 42.749 -11.958 1.00 55.89 C ANISOU 2411 CZ TYR A 331 7792 6097 7346 111 -1134 201 C ATOM 2412 OH TYR A 331 14.006 43.459 -11.698 1.00 66.71 O ANISOU 2412 OH TYR A 331 9161 7466 8721 110 -1130 206 O ATOM 2413 N GLU A 332 7.611 42.161 -14.952 1.00 51.89 N ANISOU 2413 N GLU A 332 7303 5583 6829 116 -1164 185 N ATOM 2414 CA GLU A 332 7.588 43.204 -15.957 1.00 69.54 C ANISOU 2414 CA GLU A 332 9544 7813 9066 116 -1170 187 C ATOM 2415 C GLU A 332 6.411 44.152 -15.762 1.00 70.58 C ANISOU 2415 C GLU A 332 9673 7941 9203 118 -1182 180 C ATOM 2416 O GLU A 332 6.543 45.358 -16.003 1.00 72.56 O ANISOU 2416 O GLU A 332 9924 8187 9458 118 -1187 181 O ATOM 2417 CB GLU A 332 7.554 42.563 -17.335 1.00 81.28 C ANISOU 2417 CB GLU A 332 11040 9298 10545 115 -1167 192 C ATOM 2418 CG GLU A 332 7.279 43.545 -18.406 1.00100.72 C ANISOU 2418 CG GLU A 332 13508 11754 13008 116 -1174 194 C ATOM 2419 CD GLU A 332 7.106 42.884 -19.723 1.00118.93 C ANISOU 2419 CD GLU A 332 15823 14059 15306 115 -1172 198 C ATOM 2420 OE1 GLU A 332 7.263 41.646 -19.800 1.00125.63 O ANISOU 2420 OE1 GLU A 332 16673 14912 16149 115 -1164 199 O ATOM 2421 OE2 GLU A 332 6.679 43.588 -20.648 1.00125.62 O ANISOU 2421 OE2 GLU A 332 16676 14901 16153 116 -1178 199 O ATOM 2422 N LYS A 333 5.271 43.643 -15.299 1.00 61.52 N ANISOU 2422 N LYS A 333 8522 6796 8055 119 -1187 173 N ATOM 2423 CA LYS A 333 4.134 44.522 -15.057 1.00 60.32 C ANISOU 2423 CA LYS A 333 8368 6641 7909 120 -1198 167 C ATOM 2424 C LYS A 333 4.489 45.602 -14.048 1.00 67.98 C ANISOU 2424 C LYS A 333 9331 7610 8887 121 -1201 164 C ATOM 2425 O LYS A 333 3.968 46.719 -14.124 1.00 76.87 O ANISOU 2425 O LYS A 333 10457 8732 10018 122 -1210 161 O ATOM 2426 CB LYS A 333 2.917 43.703 -14.616 1.00 55.39 C ANISOU 2426 CB LYS A 333 7741 6020 7284 122 -1202 159 C ATOM 2427 CG LYS A 333 1.703 44.513 -14.185 1.00 56.83 C ANISOU 2427 CG LYS A 333 7921 6199 7473 123 -1216 151 C ATOM 2428 CD LYS A 333 0.484 43.616 -13.948 1.00 66.25 C ANISOU 2428 CD LYS A 333 9113 7394 8664 124 -1221 144 C ATOM 2429 CE LYS A 333 0.502 42.918 -12.602 1.00 72.94 C ANISOU 2429 CE LYS A 333 9954 8247 9514 124 -1219 140 C ATOM 2430 NZ LYS A 333 -0.792 42.215 -12.359 1.00 76.03 N ANISOU 2430 NZ LYS A 333 10345 8639 9904 125 -1226 133 N ATOM 2431 N HIS A 334 5.378 45.293 -13.106 1.00 62.86 N ANISOU 2431 N HIS A 334 8678 6966 8240 120 -1194 166 N ATOM 2432 CA HIS A 334 5.840 46.256 -12.120 1.00 48.63 C ANISOU 2432 CA HIS A 334 6870 5163 6446 120 -1196 164 C ATOM 2433 C HIS A 334 7.093 46.998 -12.581 1.00 58.39 C ANISOU 2433 C HIS A 334 8108 6395 7682 119 -1192 172 C ATOM 2434 O HIS A 334 7.828 47.532 -11.741 1.00 57.59 O ANISOU 2434 O HIS A 334 8001 6294 7585 118 -1190 172 O ATOM 2435 CB HIS A 334 6.081 45.544 -10.787 1.00 44.76 C ANISOU 2435 CB HIS A 334 6372 4678 5957 120 -1192 161 C ATOM 2436 CG HIS A 334 4.835 44.981 -10.180 1.00 45.52 C ANISOU 2436 CG HIS A 334 6466 4777 6055 121 -1199 153 C ATOM 2437 ND1 HIS A 334 4.286 45.465 -9.012 1.00 51.38 N ANISOU 2437 ND1 HIS A 334 7202 5518 6803 122 -1207 145 N ATOM 2438 CD2 HIS A 334 4.013 43.987 -10.599 1.00 48.81 C ANISOU 2438 CD2 HIS A 334 6886 5195 6466 121 -1200 150 C ATOM 2439 CE1 HIS A 334 3.189 44.782 -8.728 1.00 53.62 C ANISOU 2439 CE1 HIS A 334 7484 5803 7086 122 -1213 139 C ATOM 2440 NE2 HIS A 334 2.999 43.882 -9.677 1.00 45.98 N ANISOU 2440 NE2 HIS A 334 6522 4837 6111 122 -1208 142 N ATOM 2441 N SER A 335 7.332 47.061 -13.893 1.00 79.16 N ANISOU 2441 N SER A 335 10747 9022 10308 118 -1191 177 N ATOM 2442 CA SER A 335 8.465 47.779 -14.497 1.00 91.23 C ANISOU 2442 CA SER A 335 12279 10548 11837 117 -1188 185 C ATOM 2443 C SER A 335 9.818 47.422 -13.882 1.00 98.56 C ANISOU 2443 C SER A 335 13204 11479 12764 115 -1177 190 C ATOM 2444 O SER A 335 9.960 46.433 -13.164 1.00100.62 O ANISOU 2444 O SER A 335 13461 11745 13024 115 -1171 188 O ATOM 2445 CB SER A 335 8.249 49.297 -14.421 1.00 95.65 C ANISOU 2445 CB SER A 335 12837 11102 12403 117 -1197 183 C ATOM 2446 OG SER A 335 7.321 49.744 -15.397 1.00 95.80 O ANISOU 2446 OG SER A 335 12862 11117 12422 118 -1205 181 O TER 2447 SER A 335 ATOM 2448 N ASP B 9 32.925 9.829 29.930 1.00 49.65 N ANISOU 2448 N ASP B 9 5625 6777 6464 220 271 486 N ATOM 2449 CA ASP B 9 32.923 8.461 29.400 1.00 53.66 C ANISOU 2449 CA ASP B 9 6124 7274 6990 216 270 487 C ATOM 2450 C ASP B 9 31.953 8.210 28.229 1.00 47.12 C ANISOU 2450 C ASP B 9 5284 6434 6185 209 263 477 C ATOM 2451 O ASP B 9 30.794 8.636 28.269 1.00 48.84 O ANISOU 2451 O ASP B 9 5492 6649 6414 208 264 477 O ATOM 2452 CB ASP B 9 32.610 7.485 30.529 1.00 60.08 C ANISOU 2452 CB ASP B 9 6929 8086 7813 218 278 506 C ATOM 2453 CG ASP B 9 33.856 6.926 31.167 1.00 68.60 C ANISOU 2453 CG ASP B 9 8019 9170 8877 223 281 514 C ATOM 2454 OD1 ASP B 9 34.969 7.284 30.721 1.00 72.85 O ANISOU 2454 OD1 ASP B 9 8569 9713 9397 223 277 505 O ATOM 2455 OD2 ASP B 9 33.722 6.140 32.125 1.00 69.03 O ANISOU 2455 OD2 ASP B 9 8067 9223 8938 225 288 530 O ATOM 2456 N VAL B 10 32.427 7.472 27.217 1.00 30.74 N ANISOU 2456 N VAL B 10 3210 4353 4118 205 258 467 N ATOM 2457 CA VAL B 10 31.588 7.133 26.073 1.00 26.69 C ANISOU 2457 CA VAL B 10 2684 3828 3627 199 251 457 C ATOM 2458 C VAL B 10 30.423 6.263 26.542 1.00 29.94 C ANISOU 2458 C VAL B 10 3080 4232 4063 198 254 470 C ATOM 2459 O VAL B 10 30.536 5.501 27.517 1.00 27.69 O ANISOU 2459 O VAL B 10 2792 3947 3780 200 262 486 O ATOM 2460 CB VAL B 10 32.408 6.398 24.999 1.00 26.59 C ANISOU 2460 CB VAL B 10 2676 3811 3617 196 244 446 C ATOM 2461 CG1 VAL B 10 32.774 4.986 25.483 1.00 18.90 C ANISOU 2461 CG1 VAL B 10 1698 2832 2651 196 248 459 C ATOM 2462 CG2 VAL B 10 31.670 6.363 23.653 1.00 18.34 C ANISOU 2462 CG2 VAL B 10 1622 2756 2591 190 234 432 C ATOM 2463 N ASN B 11 29.274 6.415 25.876 1.00 27.78 N ANISOU 2463 N ASN B 11 2796 3952 3809 194 249 464 N ATOM 2464 CA ASN B 11 28.096 5.603 26.165 1.00 20.83 C ANISOU 2464 CA ASN B 11 1899 3062 2954 192 252 474 C ATOM 2465 C ASN B 11 27.400 5.238 24.860 1.00 20.65 C ANISOU 2465 C ASN B 11 1866 3028 2952 186 242 462 C ATOM 2466 O ASN B 11 27.507 5.960 23.862 1.00 18.80 O ANISOU 2466 O ASN B 11 1636 2794 2713 184 234 446 O ATOM 2467 CB ASN B 11 27.111 6.307 27.093 1.00 25.94 C ANISOU 2467 CB ASN B 11 2541 3713 3603 194 258 484 C ATOM 2468 CG ASN B 11 26.410 5.334 28.033 1.00 40.48 C ANISOU 2468 CG ASN B 11 4370 5550 5460 195 265 503 C ATOM 2469 OD1 ASN B 11 26.456 4.111 27.846 1.00 36.96 O ANISOU 2469 OD1 ASN B 11 3919 5097 5029 193 264 507 O ATOM 2470 ND2 ASN B 11 25.761 5.874 29.054 1.00 48.68 N ANISOU 2470 ND2 ASN B 11 5407 6594 6497 198 272 513 N ATOM 2471 N THR B 12 26.720 4.090 24.859 1.00 23.47 N ANISOU 2471 N THR B 12 2210 3375 3332 183 242 471 N ATOM 2472 CA THR B 12 25.957 3.616 23.708 1.00 29.29 C ANISOU 2472 CA THR B 12 2936 4101 4092 178 232 461 C ATOM 2473 C THR B 12 24.485 3.467 24.077 1.00 31.87 C ANISOU 2473 C THR B 12 3248 4421 4439 176 234 471 C ATOM 2474 O THR B 12 24.109 3.506 25.253 1.00 38.22 O ANISOU 2474 O THR B 12 4049 5229 5242 180 243 486 O ATOM 2475 CB THR B 12 26.500 2.271 23.194 1.00 28.60 C ANISOU 2475 CB THR B 12 2847 4006 4015 175 229 462 C ATOM 2476 OG1 THR B 12 26.206 1.241 24.137 1.00 27.32 O ANISOU 2476 OG1 THR B 12 2676 3839 3863 176 236 480 O ATOM 2477 CG2 THR B 12 27.998 2.330 23.020 1.00 28.13 C ANISOU 2477 CG2 THR B 12 2802 3952 3933 177 229 455 C ATOM 2478 N LEU B 13 23.639 3.260 23.065 1.00 21.16 N ANISOU 2478 N LEU B 13 1881 3055 3103 172 224 462 N ATOM 2479 CA LEU B 13 22.210 3.102 23.346 1.00 31.03 C ANISOU 2479 CA LEU B 13 3118 4300 4374 170 225 471 C ATOM 2480 C LEU B 13 21.920 1.869 24.213 1.00 25.13 C ANISOU 2480 C LEU B 13 2361 3547 3641 171 233 490 C ATOM 2481 O LEU B 13 21.236 1.976 25.239 1.00 22.68 O ANISOU 2481 O LEU B 13 2046 3239 3335 173 240 504 O ATOM 2482 CB LEU B 13 21.425 3.056 22.039 1.00 34.30 C ANISOU 2482 CB LEU B 13 3522 4703 4805 165 213 458 C ATOM 2483 CG LEU B 13 19.908 2.924 22.084 1.00 33.64 C ANISOU 2483 CG LEU B 13 3424 4612 4745 163 211 464 C ATOM 2484 CD1 LEU B 13 19.301 3.749 23.191 1.00 39.13 C ANISOU 2484 CD1 LEU B 13 4118 5316 5435 167 220 474 C ATOM 2485 CD2 LEU B 13 19.485 3.549 20.796 1.00 34.54 C ANISOU 2485 CD2 LEU B 13 3537 4724 4864 160 199 446 C ATOM 2486 N THR B 14 22.450 0.697 23.834 1.00 22.51 N ANISOU 2486 N THR B 14 2028 3208 3316 169 230 491 N ATOM 2487 CA THR B 14 22.188 -0.525 24.607 1.00 28.61 C ANISOU 2487 CA THR B 14 2792 3974 4103 169 237 509 C ATOM 2488 C THR B 14 22.781 -0.462 26.015 1.00 29.25 C ANISOU 2488 C THR B 14 2880 4065 4168 174 249 524 C ATOM 2489 O THR B 14 22.146 -0.905 26.978 1.00 30.90 O ANISOU 2489 O THR B 14 3082 4273 4388 176 257 540 O ATOM 2490 CB THR B 14 22.648 -1.766 23.831 1.00 27.40 C ANISOU 2490 CB THR B 14 2637 3812 3962 165 231 506 C ATOM 2491 OG1 THR B 14 21.747 -1.968 22.732 1.00 29.73 O ANISOU 2491 OG1 THR B 14 2922 4097 4277 160 220 497 O ATOM 2492 CG2 THR B 14 22.686 -3.046 24.721 1.00 27.29 C ANISOU 2492 CG2 THR B 14 2617 3793 3958 166 238 525 C ATOM 2493 N ARG B 15 23.994 0.070 26.159 1.00 28.77 N ANISOU 2493 N ARG B 15 2834 4014 4083 177 251 518 N ATOM 2494 CA ARG B 15 24.563 0.236 27.492 1.00 39.52 C ANISOU 2494 CA ARG B 15 4203 5385 5427 183 262 532 C ATOM 2495 C ARG B 15 23.754 1.228 28.336 1.00 38.85 C ANISOU 2495 C ARG B 15 4116 5307 5339 186 268 538 C ATOM 2496 O ARG B 15 23.538 0.992 29.527 1.00 43.88 O ANISOU 2496 O ARG B 15 4751 5947 5976 190 277 554 O ATOM 2497 CB ARG B 15 26.018 0.682 27.367 1.00 41.62 C ANISOU 2497 CB ARG B 15 4486 5661 5668 186 262 523 C ATOM 2498 CG ARG B 15 26.666 1.077 28.656 1.00 40.85 C ANISOU 2498 CG ARG B 15 4397 5574 5549 192 272 535 C ATOM 2499 CD ARG B 15 28.052 1.650 28.394 1.00 40.70 C ANISOU 2499 CD ARG B 15 4395 5565 5505 194 270 524 C ATOM 2500 NE ARG B 15 29.118 0.658 28.455 1.00 32.48 N ANISOU 2500 NE ARG B 15 3359 4523 4460 195 272 528 N ATOM 2501 CZ ARG B 15 30.399 0.975 28.345 1.00 27.71 C ANISOU 2501 CZ ARG B 15 2769 3925 3833 197 271 521 C ATOM 2502 NH1 ARG B 15 30.744 2.247 28.162 1.00 21.19 N ANISOU 2502 NH1 ARG B 15 1954 3109 2989 199 269 511 N ATOM 2503 NH2 ARG B 15 31.336 0.034 28.448 1.00 24.90 N ANISOU 2503 NH2 ARG B 15 2418 3569 3475 198 273 525 N ATOM 2504 N PHE B 16 23.302 2.338 27.741 1.00 32.59 N ANISOU 2504 N PHE B 16 3324 4516 4542 185 263 525 N ATOM 2505 CA PHE B 16 22.513 3.342 28.469 1.00 28.42 C ANISOU 2505 CA PHE B 16 2793 3994 4010 187 267 530 C ATOM 2506 C PHE B 16 21.172 2.779 28.940 1.00 29.80 C ANISOU 2506 C PHE B 16 2952 4161 4209 186 270 543 C ATOM 2507 O PHE B 16 20.741 3.058 30.067 1.00 29.90 O ANISOU 2507 O PHE B 16 2962 4178 4219 190 279 556 O ATOM 2508 CB PHE B 16 22.321 4.585 27.586 1.00 24.42 C ANISOU 2508 CB PHE B 16 2292 3491 3497 186 260 512 C ATOM 2509 CG PHE B 16 21.375 5.628 28.143 1.00 24.22 C ANISOU 2509 CG PHE B 16 2263 3470 3471 188 263 515 C ATOM 2510 CD1 PHE B 16 21.841 6.660 28.928 1.00 27.31 C ANISOU 2510 CD1 PHE B 16 2664 3874 3840 193 269 517 C ATOM 2511 CD2 PHE B 16 20.025 5.611 27.822 1.00 26.17 C ANISOU 2511 CD2 PHE B 16 2496 3709 3739 185 260 515 C ATOM 2512 CE1 PHE B 16 20.966 7.643 29.431 1.00 30.58 C ANISOU 2512 CE1 PHE B 16 3075 4292 4253 195 272 520 C ATOM 2513 CE2 PHE B 16 19.147 6.586 28.325 1.00 33.85 C ANISOU 2513 CE2 PHE B 16 3465 4686 4711 186 263 518 C ATOM 2514 CZ PHE B 16 19.626 7.601 29.134 1.00 33.04 C ANISOU 2514 CZ PHE B 16 3373 4596 4586 191 269 520 C ATOM 2515 N VAL B 17 20.482 1.998 28.095 1.00 28.52 N ANISOU 2515 N VAL B 17 2779 3987 4071 181 263 540 N ATOM 2516 CA VAL B 17 19.177 1.472 28.499 1.00 26.00 C ANISOU 2516 CA VAL B 17 2445 3660 3774 180 266 552 C ATOM 2517 C VAL B 17 19.331 0.416 29.595 1.00 30.30 C ANISOU 2517 C VAL B 17 2986 4203 4324 182 275 572 C ATOM 2518 O VAL B 17 18.507 0.339 30.515 1.00 29.12 O ANISOU 2518 O VAL B 17 2829 4053 4183 184 282 586 O ATOM 2519 CB VAL B 17 18.392 0.911 27.291 1.00 22.74 C ANISOU 2519 CB VAL B 17 2021 3234 3385 174 255 544 C ATOM 2520 CG1 VAL B 17 17.066 0.213 27.755 1.00 14.41 C ANISOU 2520 CG1 VAL B 17 949 2170 2355 172 258 558 C ATOM 2521 CG2 VAL B 17 18.070 2.001 26.251 1.00 18.21 C ANISOU 2521 CG2 VAL B 17 1449 2662 2809 171 246 526 C ATOM 2522 N MET B 18 20.376 -0.417 29.516 1.00 27.33 N ANISOU 2522 N MET B 18 2616 3826 3943 182 276 573 N ATOM 2523 CA MET B 18 20.584 -1.447 30.532 1.00 25.01 C ANISOU 2523 CA MET B 18 2319 3531 3653 185 284 591 C ATOM 2524 C MET B 18 20.851 -0.838 31.893 1.00 33.56 C ANISOU 2524 C MET B 18 3409 4625 4718 191 295 602 C ATOM 2525 O MET B 18 20.416 -1.375 32.917 1.00 33.49 O ANISOU 2525 O MET B 18 3394 4615 4717 193 303 619 O ATOM 2526 CB MET B 18 21.759 -2.342 30.154 1.00 21.69 C ANISOU 2526 CB MET B 18 1905 3108 3228 184 282 589 C ATOM 2527 CG MET B 18 21.511 -3.330 29.077 1.00 28.15 C ANISOU 2527 CG MET B 18 2716 3913 4066 178 274 583 C ATOM 2528 SD MET B 18 23.037 -4.241 28.826 1.00 34.62 S ANISOU 2528 SD MET B 18 3546 4734 4876 179 273 581 S ATOM 2529 CE MET B 18 22.511 -5.395 27.558 1.00 35.53 C ANISOU 2529 CE MET B 18 3649 4832 5019 172 263 575 C ATOM 2530 N GLU B 19 21.600 0.267 31.919 1.00 39.13 N ANISOU 2530 N GLU B 19 4127 5341 5399 194 295 593 N ATOM 2531 CA GLU B 19 21.952 0.933 33.166 1.00 28.08 C ANISOU 2531 CA GLU B 19 2735 3954 3981 200 304 603 C ATOM 2532 C GLU B 19 20.731 1.583 33.809 1.00 35.93 C ANISOU 2532 C GLU B 19 3721 4950 4982 202 308 610 C ATOM 2533 O GLU B 19 20.496 1.419 35.014 1.00 36.30 O ANISOU 2533 O GLU B 19 3765 4999 5027 206 317 626 O ATOM 2534 CB GLU B 19 23.049 1.960 32.886 1.00 26.62 C ANISOU 2534 CB GLU B 19 2566 3779 3768 203 301 590 C ATOM 2535 CG GLU B 19 24.395 1.308 32.557 1.00 40.42 C ANISOU 2535 CG GLU B 19 4324 5528 5506 203 300 586 C ATOM 2536 CD GLU B 19 25.402 2.261 31.912 1.00 53.33 C ANISOU 2536 CD GLU B 19 5973 7170 7118 203 294 570 C ATOM 2537 OE1 GLU B 19 25.016 3.391 31.534 1.00 48.84 O ANISOU 2537 OE1 GLU B 19 5407 6606 6544 203 291 560 O ATOM 2538 OE2 GLU B 19 26.592 1.882 31.813 1.00 57.75 O ANISOU 2538 OE2 GLU B 19 6543 7734 7666 205 294 568 O ATOM 2539 N GLU B 20 19.926 2.302 33.015 1.00 39.12 N ANISOU 2539 N GLU B 20 4121 5351 5393 198 301 598 N ATOM 2540 CA GLU B 20 18.675 2.856 33.536 1.00 35.39 C ANISOU 2540 CA GLU B 20 3639 4879 4930 199 304 605 C ATOM 2541 C GLU B 20 17.724 1.739 33.979 1.00 40.28 C ANISOU 2541 C GLU B 20 4243 5488 5574 197 308 620 C ATOM 2542 O GLU B 20 17.013 1.879 34.983 1.00 45.56 O ANISOU 2542 O GLU B 20 4905 6158 6246 200 315 633 O ATOM 2543 CB GLU B 20 17.994 3.725 32.469 1.00 24.78 C ANISOU 2543 CB GLU B 20 2292 3532 3591 195 296 588 C ATOM 2544 CG GLU B 20 18.685 5.037 32.069 1.00 32.44 C ANISOU 2544 CG GLU B 20 3276 4513 4538 197 292 573 C ATOM 2545 CD GLU B 20 18.641 6.128 33.156 1.00 43.42 C ANISOU 2545 CD GLU B 20 4672 5915 5911 202 300 579 C ATOM 2546 OE1 GLU B 20 17.701 6.144 33.979 1.00 42.53 O ANISOU 2546 OE1 GLU B 20 4551 5802 5808 204 305 592 O ATOM 2547 OE2 GLU B 20 19.551 6.987 33.170 1.00 43.10 O ANISOU 2547 OE2 GLU B 20 4645 5884 5847 205 299 572 O ATOM 2548 N GLY B 21 17.726 0.611 33.260 1.00 30.75 N ANISOU 2548 N GLY B 21 3031 4271 4384 193 303 619 N ATOM 2549 CA GLY B 21 16.817 -0.477 33.589 1.00 30.86 C ANISOU 2549 CA GLY B 21 3029 4273 4422 191 306 633 C ATOM 2550 C GLY B 21 17.195 -1.211 34.860 1.00 38.21 C ANISOU 2550 C GLY B 21 3962 5207 5351 195 316 651 C ATOM 2551 O GLY B 21 16.329 -1.530 35.679 1.00 43.86 O ANISOU 2551 O GLY B 21 4667 5920 6078 197 322 666 O ATOM 2552 N ARG B 22 18.491 -1.507 35.035 1.00 30.60 N ANISOU 2552 N ARG B 22 3009 4249 4370 198 318 651 N ATOM 2553 CA ARG B 22 18.962 -2.077 36.287 1.00 25.84 C ANISOU 2553 CA ARG B 22 2408 3650 3761 203 328 668 C ATOM 2554 C ARG B 22 18.764 -1.093 37.430 1.00 43.70 C ANISOU 2554 C ARG B 22 4673 5922 6008 209 335 676 C ATOM 2555 O ARG B 22 18.488 -1.500 38.566 1.00 43.52 O ANISOU 2555 O ARG B 22 4646 5901 5989 212 344 693 O ATOM 2556 CB ARG B 22 20.440 -2.450 36.183 1.00 27.47 C ANISOU 2556 CB ARG B 22 2626 3860 3950 205 327 665 C ATOM 2557 CG ARG B 22 20.778 -3.640 35.300 1.00 35.16 C ANISOU 2557 CG ARG B 22 3598 4823 4938 200 322 661 C ATOM 2558 CD ARG B 22 22.266 -3.939 35.419 1.00 41.47 C ANISOU 2558 CD ARG B 22 4410 5628 5718 203 323 660 C ATOM 2559 NE ARG B 22 22.620 -4.372 36.769 1.00 48.39 N ANISOU 2559 NE ARG B 22 5288 6510 6589 209 333 678 N ATOM 2560 CZ ARG B 22 23.862 -4.443 37.241 1.00 47.30 C ANISOU 2560 CZ ARG B 22 5161 6379 6430 213 337 680 C ATOM 2561 NH1 ARG B 22 24.893 -4.095 36.479 1.00 42.14 N ANISOU 2561 NH1 ARG B 22 4520 5730 5762 212 331 665 N ATOM 2562 NH2 ARG B 22 24.074 -4.842 38.490 1.00 49.52 N ANISOU 2562 NH2 ARG B 22 5443 6665 6707 218 345 696 N ATOM 2563 N LYS B 23 18.896 0.203 37.138 1.00 44.69 N ANISOU 2563 N LYS B 23 4806 6056 6117 210 332 664 N ATOM 2564 CA LYS B 23 18.665 1.229 38.146 1.00 46.50 C ANISOU 2564 CA LYS B 23 5039 6296 6333 215 339 669 C ATOM 2565 C LYS B 23 17.232 1.164 38.656 1.00 46.56 C ANISOU 2565 C LYS B 23 5033 6299 6361 214 342 680 C ATOM 2566 O LYS B 23 16.983 1.335 39.852 1.00 42.49 O ANISOU 2566 O LYS B 23 4515 5788 5840 219 351 694 O ATOM 2567 CB LYS B 23 18.991 2.604 37.558 1.00 43.56 C ANISOU 2567 CB LYS B 23 4677 5932 5943 215 334 653 C ATOM 2568 CG LYS B 23 19.340 3.666 38.561 1.00 50.19 C ANISOU 2568 CG LYS B 23 5526 6785 6760 221 339 657 C ATOM 2569 CD LYS B 23 19.699 4.981 37.872 1.00 61.23 C ANISOU 2569 CD LYS B 23 6934 8190 8141 221 334 639 C ATOM 2570 CE LYS B 23 20.911 4.809 36.956 1.00 69.53 C ANISOU 2570 CE LYS B 23 7997 9241 9181 219 327 626 C ATOM 2571 NZ LYS B 23 21.182 6.019 36.125 1.00 74.30 N ANISOU 2571 NZ LYS B 23 8609 9850 9771 218 320 608 N ATOM 2572 N ALA B 24 16.285 0.885 37.765 1.00 50.20 N ANISOU 2572 N ALA B 24 5482 6749 6843 208 336 674 N ATOM 2573 CA ALA B 24 14.872 0.797 38.097 1.00 44.22 C ANISOU 2573 CA ALA B 24 4710 5985 6105 207 338 683 C ATOM 2574 C ALA B 24 14.454 -0.600 38.544 1.00 43.77 C ANISOU 2574 C ALA B 24 4643 5919 6069 206 343 699 C ATOM 2575 O ALA B 24 13.284 -0.799 38.875 1.00 38.27 O ANISOU 2575 O ALA B 24 3934 5217 5391 205 345 708 O ATOM 2576 CB ALA B 24 14.031 1.213 36.892 1.00 34.41 C ANISOU 2576 CB ALA B 24 3462 4737 4877 201 329 669 C ATOM 2577 N ARG B 25 15.374 -1.568 38.532 1.00 44.70 N ANISOU 2577 N ARG B 25 4765 6035 6186 206 343 703 N ATOM 2578 CA ARG B 25 15.117 -2.918 39.029 1.00 40.04 C ANISOU 2578 CA ARG B 25 4165 5436 5613 206 348 718 C ATOM 2579 C ARG B 25 14.036 -3.619 38.200 1.00 38.15 C ANISOU 2579 C ARG B 25 3911 5182 5402 199 341 717 C ATOM 2580 O ARG B 25 13.239 -4.398 38.720 1.00 38.65 O ANISOU 2580 O ARG B 25 3964 5238 5484 199 345 731 O ATOM 2581 CB ARG B 25 14.723 -2.862 40.506 1.00 44.18 C ANISOU 2581 CB ARG B 25 4686 5965 6134 212 358 737 C ATOM 2582 CG ARG B 25 15.719 -2.111 41.402 1.00 55.14 C ANISOU 2582 CG ARG B 25 6088 7368 7495 218 364 739 C ATOM 2583 CD ARG B 25 16.985 -2.886 41.715 1.00 68.63 C ANISOU 2583 CD ARG B 25 7805 9078 9192 221 367 743 C ATOM 2584 NE ARG B 25 16.765 -4.022 42.613 1.00 77.42 N ANISOU 2584 NE ARG B 25 8911 10187 10318 223 374 762 N ATOM 2585 CZ ARG B 25 16.787 -3.933 43.943 1.00 81.18 C ANISOU 2585 CZ ARG B 25 9388 10671 10787 229 383 777 C ATOM 2586 NH1 ARG B 25 17.020 -2.764 44.527 1.00 85.09 N ANISOU 2586 NH1 ARG B 25 9891 11178 11261 234 386 775 N ATOM 2587 NH2 ARG B 25 16.587 -5.012 44.691 1.00 75.98 N ANISOU 2587 NH2 ARG B 25 8722 10006 10140 231 389 794 N ATOM 2588 N GLY B 26 14.009 -3.354 36.879 1.00 34.02 N ANISOU 2588 N GLY B 26 3389 4655 4882 194 331 700 N ATOM 2589 CA GLY B 26 13.031 -3.991 36.013 1.00 26.98 C ANISOU 2589 CA GLY B 26 2484 3749 4017 188 324 698 C ATOM 2590 C GLY B 26 13.434 -5.394 35.611 1.00 30.48 C ANISOU 2590 C GLY B 26 2925 4182 4473 185 321 701 C ATOM 2591 O GLY B 26 14.558 -5.834 35.831 1.00 33.18 O ANISOU 2591 O GLY B 26 3276 4528 4804 188 324 703 O ATOM 2592 N THR B 27 12.502 -6.106 34.974 1.00 36.15 N ANISOU 2592 N THR B 27 3631 4888 5218 180 316 702 N ATOM 2593 CA THR B 27 12.773 -7.493 34.596 1.00 32.67 C ANISOU 2593 CA THR B 27 3185 4435 4791 177 313 706 C ATOM 2594 C THR B 27 13.641 -7.632 33.346 1.00 40.64 C ANISOU 2594 C THR B 27 4203 5444 5796 174 303 690 C ATOM 2595 O THR B 27 14.169 -8.727 33.104 1.00 33.26 O ANISOU 2595 O THR B 27 3267 4501 4868 172 302 693 O ATOM 2596 CB THR B 27 11.472 -8.270 34.368 1.00 36.30 C ANISOU 2596 CB THR B 27 3629 4881 5281 173 310 714 C ATOM 2597 OG1 THR B 27 10.779 -7.741 33.229 1.00 40.34 O ANISOU 2597 OG1 THR B 27 4136 5388 5802 168 300 699 O ATOM 2598 CG2 THR B 27 10.583 -8.217 35.611 1.00 33.46 C ANISOU 2598 CG2 THR B 27 3262 4524 4929 176 320 731 C ATOM 2599 N GLY B 28 13.769 -6.579 32.527 1.00 35.25 N ANISOU 2599 N GLY B 28 3526 4765 5102 173 296 672 N ATOM 2600 CA GLY B 28 14.517 -6.676 31.287 1.00 35.78 C ANISOU 2600 CA GLY B 28 3599 4829 5165 169 287 656 C ATOM 2601 C GLY B 28 13.683 -6.787 30.030 1.00 40.97 C ANISOU 2601 C GLY B 28 4248 5476 5842 163 275 645 C ATOM 2602 O GLY B 28 14.253 -6.849 28.931 1.00 44.54 O ANISOU 2602 O GLY B 28 4705 5926 6292 160 266 630 O ATOM 2603 N GLU B 29 12.358 -6.864 30.151 1.00 32.88 N ANISOU 2603 N GLU B 29 3211 4445 4838 161 274 652 N ATOM 2604 CA GLU B 29 11.530 -6.998 28.961 1.00 34.29 C ANISOU 2604 CA GLU B 29 3381 4612 5036 156 263 642 C ATOM 2605 C GLU B 29 11.619 -5.748 28.080 1.00 33.44 C ANISOU 2605 C GLU B 29 3280 4510 4915 155 255 622 C ATOM 2606 O GLU B 29 11.832 -5.852 26.865 1.00 24.16 O ANISOU 2606 O GLU B 29 2107 3330 3744 151 244 608 O ATOM 2607 CB GLU B 29 10.094 -7.315 29.390 1.00 27.43 C ANISOU 2607 CB GLU B 29 2497 3734 4189 154 265 654 C ATOM 2608 CG GLU B 29 9.339 -8.187 28.413 1.00 37.42 C ANISOU 2608 CG GLU B 29 3751 4984 5481 148 255 652 C ATOM 2609 CD GLU B 29 8.019 -8.705 28.958 1.00 41.42 C ANISOU 2609 CD GLU B 29 4244 5482 6012 147 258 667 C ATOM 2610 OE1 GLU B 29 8.005 -9.260 30.074 1.00 45.10 O ANISOU 2610 OE1 GLU B 29 4706 5949 6480 150 268 684 O ATOM 2611 OE2 GLU B 29 6.988 -8.548 28.279 1.00 44.42 O ANISOU 2611 OE2 GLU B 29 4615 5855 6409 143 250 662 O ATOM 2612 N LEU B 30 11.560 -4.559 28.683 1.00 26.02 N ANISOU 2612 N LEU B 30 2346 3583 3960 159 260 621 N ATOM 2613 CA LEU B 30 11.654 -3.332 27.897 1.00 30.21 C ANISOU 2613 CA LEU B 30 2883 4119 4478 158 253 603 C ATOM 2614 C LEU B 30 13.026 -3.196 27.242 1.00 32.90 C ANISOU 2614 C LEU B 30 3237 4465 4800 159 249 590 C ATOM 2615 O LEU B 30 13.133 -2.685 26.120 1.00 29.28 O ANISOU 2615 O LEU B 30 2781 4005 4338 156 239 573 O ATOM 2616 CB LEU B 30 11.361 -2.109 28.768 1.00 18.88 C ANISOU 2616 CB LEU B 30 1451 2696 3028 163 261 606 C ATOM 2617 CG LEU B 30 11.488 -0.744 28.073 1.00 20.86 C ANISOU 2617 CG LEU B 30 1709 2953 3263 163 255 588 C ATOM 2618 CD1 LEU B 30 10.531 -0.606 26.919 1.00 18.08 C ANISOU 2618 CD1 LEU B 30 1348 2592 2929 158 243 577 C ATOM 2619 CD2 LEU B 30 11.304 0.409 29.041 1.00 20.80 C ANISOU 2619 CD2 LEU B 30 1705 2958 3241 167 263 592 C ATOM 2620 N THR B 31 14.086 -3.631 27.935 1.00 26.70 N ANISOU 2620 N THR B 31 2460 3685 4001 162 257 597 N ATOM 2621 CA THR B 31 15.417 -3.594 27.344 1.00 30.96 C ANISOU 2621 CA THR B 31 3012 4229 4523 162 253 585 C ATOM 2622 C THR B 31 15.524 -4.541 26.152 1.00 38.37 C ANISOU 2622 C THR B 31 3947 5156 5477 157 242 577 C ATOM 2623 O THR B 31 16.064 -4.165 25.106 1.00 30.56 O ANISOU 2623 O THR B 31 2964 4167 4479 155 234 560 O ATOM 2624 CB THR B 31 16.469 -3.928 28.391 1.00 27.02 C ANISOU 2624 CB THR B 31 2522 3738 4008 167 263 596 C ATOM 2625 OG1 THR B 31 16.656 -2.790 29.220 1.00 29.14 O ANISOU 2625 OG1 THR B 31 2797 4019 4255 172 270 597 O ATOM 2626 CG2 THR B 31 17.814 -4.239 27.729 1.00 30.46 C ANISOU 2626 CG2 THR B 31 2968 4175 4431 166 259 586 C ATOM 2627 N GLN B 32 14.974 -5.753 26.272 1.00 39.22 N ANISOU 2627 N GLN B 32 4044 5253 5607 155 243 589 N ATOM 2628 CA GLN B 32 14.955 -6.664 25.132 1.00 28.71 C ANISOU 2628 CA GLN B 32 2707 3908 4291 150 232 582 C ATOM 2629 C GLN B 32 14.175 -6.053 23.978 1.00 27.60 C ANISOU 2629 C GLN B 32 2563 3764 4160 146 220 567 C ATOM 2630 O GLN B 32 14.531 -6.244 22.805 1.00 25.93 O ANISOU 2630 O GLN B 32 2353 3547 3951 143 209 554 O ATOM 2631 CB GLN B 32 14.350 -8.020 25.529 1.00 30.95 C ANISOU 2631 CB GLN B 32 2979 4181 4599 148 235 599 C ATOM 2632 CG GLN B 32 15.247 -8.965 26.346 1.00 34.72 C ANISOU 2632 CG GLN B 32 3461 4660 5072 150 244 611 C ATOM 2633 CD GLN B 32 14.450 -10.125 26.975 1.00 35.79 C ANISOU 2633 CD GLN B 32 3583 4784 5230 149 248 630 C ATOM 2634 OE1 GLN B 32 13.367 -9.918 27.505 1.00 39.52 O ANISOU 2634 OE1 GLN B 32 4046 5255 5713 149 252 639 O ATOM 2635 NE2 GLN B 32 14.992 -11.334 26.920 1.00 30.75 N ANISOU 2635 NE2 GLN B 32 2945 4140 4600 148 248 636 N ATOM 2636 N LEU B 33 13.085 -5.346 24.293 1.00 26.90 N ANISOU 2636 N LEU B 33 2467 3676 4078 146 222 570 N ATOM 2637 CA LEU B 33 12.298 -4.663 23.266 1.00 30.38 C ANISOU 2637 CA LEU B 33 2904 4113 4526 143 211 557 C ATOM 2638 C LEU B 33 13.131 -3.615 22.535 1.00 27.58 C ANISOU 2638 C LEU B 33 2562 3767 4149 144 205 538 C ATOM 2639 O LEU B 33 13.274 -3.662 21.311 1.00 22.76 O ANISOU 2639 O LEU B 33 1953 3152 3543 141 193 523 O ATOM 2640 CB LEU B 33 11.062 -4.008 23.900 1.00 23.22 C ANISOU 2640 CB LEU B 33 1989 3207 3626 144 215 564 C ATOM 2641 CG LEU B 33 9.975 -3.414 22.987 1.00 23.74 C ANISOU 2641 CG LEU B 33 2047 3268 3705 141 204 554 C ATOM 2642 CD1 LEU B 33 8.714 -3.222 23.750 1.00 21.38 C ANISOU 2642 CD1 LEU B 33 1738 2967 3419 141 210 566 C ATOM 2643 CD2 LEU B 33 10.377 -2.070 22.349 1.00 34.95 C ANISOU 2643 CD2 LEU B 33 3478 4698 5106 142 199 535 C ATOM 2644 N LEU B 34 13.712 -2.673 23.287 1.00 37.17 N ANISOU 2644 N LEU B 34 3786 4995 5341 149 213 538 N ATOM 2645 CA LEU B 34 14.425 -1.547 22.687 1.00 29.90 C ANISOU 2645 CA LEU B 34 2877 4084 4399 150 209 520 C ATOM 2646 C LEU B 34 15.680 -2.010 21.952 1.00 31.45 C ANISOU 2646 C LEU B 34 3083 4280 4586 149 204 510 C ATOM 2647 O LEU B 34 16.074 -1.389 20.953 1.00 23.70 O ANISOU 2647 O LEU B 34 2108 3301 3596 148 195 493 O ATOM 2648 CB LEU B 34 14.756 -0.498 23.763 1.00 26.68 C ANISOU 2648 CB LEU B 34 2477 3690 3969 155 219 524 C ATOM 2649 CG LEU B 34 13.643 0.385 24.399 1.00 27.40 C ANISOU 2649 CG LEU B 34 2563 3785 4064 157 224 530 C ATOM 2650 CD1 LEU B 34 14.149 1.222 25.581 1.00 19.03 C ANISOU 2650 CD1 LEU B 34 1511 2738 2981 162 235 536 C ATOM 2651 CD2 LEU B 34 12.939 1.325 23.399 1.00 23.10 C ANISOU 2651 CD2 LEU B 34 2015 3238 3522 154 213 514 C ATOM 2652 N ASN B 35 16.329 -3.084 22.430 1.00 25.34 N ANISOU 2652 N ASN B 35 2310 3504 3813 150 209 521 N ATOM 2653 CA ASN B 35 17.479 -3.634 21.709 1.00 33.51 C ANISOU 2653 CA ASN B 35 3352 4537 4841 148 204 512 C ATOM 2654 C ASN B 35 17.061 -4.220 20.366 1.00 34.15 C ANISOU 2654 C ASN B 35 3428 4607 4942 143 190 502 C ATOM 2655 O ASN B 35 17.771 -4.072 19.365 1.00 25.89 O ANISOU 2655 O ASN B 35 2389 3562 3888 142 182 486 O ATOM 2656 CB ASN B 35 18.180 -4.702 22.545 1.00 27.44 C ANISOU 2656 CB ASN B 35 2586 3769 4072 150 213 526 C ATOM 2657 CG ASN B 35 19.323 -5.392 21.788 1.00 26.85 C ANISOU 2657 CG ASN B 35 2518 3691 3992 149 207 518 C ATOM 2658 OD1 ASN B 35 19.168 -6.514 21.287 1.00 25.19 O ANISOU 2658 OD1 ASN B 35 2302 3471 3800 145 202 520 O ATOM 2659 ND2 ASN B 35 20.468 -4.725 21.709 1.00 16.71 N ANISOU 2659 ND2 ASN B 35 1247 2418 2684 151 208 508 N ATOM 2660 N SER B 36 15.917 -4.897 20.336 1.00 30.57 N ANISOU 2660 N SER B 36 2960 4142 4512 140 188 510 N ATOM 2661 CA SER B 36 15.401 -5.442 19.092 1.00 23.28 C ANISOU 2661 CA SER B 36 2030 3206 3608 135 175 502 C ATOM 2662 C SER B 36 14.998 -4.349 18.117 1.00 26.96 C ANISOU 2662 C SER B 36 2498 3675 4071 134 164 485 C ATOM 2663 O SER B 36 15.201 -4.488 16.906 1.00 25.90 O ANISOU 2663 O SER B 36 2366 3535 3940 131 152 471 O ATOM 2664 CB SER B 36 14.225 -6.354 19.396 1.00 13.42 C ANISOU 2664 CB SER B 36 767 1946 2387 133 175 517 C ATOM 2665 OG SER B 36 14.691 -7.415 20.192 1.00 30.74 O ANISOU 2665 OG SER B 36 2960 4137 4583 134 184 531 O ATOM 2666 N LEU B 37 14.377 -3.284 18.621 1.00 33.56 N ANISOU 2666 N LEU B 37 3332 4517 4901 136 169 486 N ATOM 2667 CA LEU B 37 13.985 -2.166 17.766 1.00 33.47 C ANISOU 2667 CA LEU B 37 3323 4508 4885 136 160 470 C ATOM 2668 C LEU B 37 15.206 -1.492 17.156 1.00 32.10 C ANISOU 2668 C LEU B 37 3164 4343 4688 137 156 453 C ATOM 2669 O LEU B 37 15.205 -1.132 15.973 1.00 30.11 O ANISOU 2669 O LEU B 37 2914 4089 4437 135 144 437 O ATOM 2670 CB LEU B 37 13.157 -1.173 18.582 1.00 22.36 C ANISOU 2670 CB LEU B 37 1913 3108 3475 138 167 475 C ATOM 2671 CG LEU B 37 12.764 0.126 17.905 1.00 29.65 C ANISOU 2671 CG LEU B 37 2839 4036 4391 138 159 460 C ATOM 2672 CD1 LEU B 37 11.927 -0.128 16.649 1.00 28.82 C ANISOU 2672 CD1 LEU B 37 2725 3918 4306 134 145 451 C ATOM 2673 CD2 LEU B 37 12.013 0.987 18.914 1.00 22.54 C ANISOU 2673 CD2 LEU B 37 1934 3141 3487 141 168 468 C ATOM 2674 N ACYS B 38 16.272 -1.356 17.948 0.54 30.42 N ANISOU 2674 N ACYS B 38 2961 4141 4456 141 166 457 N ATOM 2675 N BCYS B 38 16.266 -1.320 17.946 0.46 30.33 N ANISOU 2675 N BCYS B 38 2950 4130 4445 141 166 457 N ATOM 2676 CA ACYS B 38 17.507 -0.727 17.501 0.54 28.34 C ANISOU 2676 CA ACYS B 38 2712 3886 4170 143 164 443 C ATOM 2677 CA BCYS B 38 17.479 -0.711 17.417 0.46 28.47 C ANISOU 2677 CA BCYS B 38 2728 3902 4187 142 163 442 C ATOM 2678 C ACYS B 38 18.231 -1.570 16.449 0.54 29.63 C ANISOU 2678 C ACYS B 38 2878 4043 4337 140 154 434 C ATOM 2679 C BCYS B 38 18.112 -1.562 16.331 0.46 29.27 C ANISOU 2679 C BCYS B 38 2831 3996 4293 139 153 433 C ATOM 2680 O ACYS B 38 18.997 -1.029 15.644 0.54 31.10 O ANISOU 2680 O ACYS B 38 3074 4234 4509 140 148 418 O ATOM 2681 O BCYS B 38 18.724 -1.023 15.402 0.46 31.02 O ANISOU 2681 O BCYS B 38 3061 4221 4504 139 145 416 O ATOM 2682 CB ACYS B 38 18.378 -0.451 18.734 0.54 27.85 C ANISOU 2682 CB ACYS B 38 2659 3835 4087 147 177 452 C ATOM 2683 CB BCYS B 38 18.478 -0.469 18.541 0.46 28.05 C ANISOU 2683 CB BCYS B 38 2685 3860 4112 147 176 449 C ATOM 2684 SG ACYS B 38 20.166 -0.604 18.596 0.54 32.20 S ANISOU 2684 SG ACYS B 38 3225 4393 4615 149 179 445 S ATOM 2685 SG BCYS B 38 18.034 0.940 19.516 0.46 30.90 S ANISOU 2685 SG BCYS B 38 3049 4233 4459 151 184 453 S ATOM 2686 N THR B 39 17.997 -2.885 16.430 1.00 24.31 N ANISOU 2686 N THR B 39 2197 3359 3682 137 153 443 N ATOM 2687 CA THR B 39 18.525 -3.718 15.360 1.00 24.66 C ANISOU 2687 CA THR B 39 2242 3396 3733 134 143 435 C ATOM 2688 C THR B 39 17.743 -3.472 14.067 1.00 30.96 C ANISOU 2688 C THR B 39 3034 4185 4543 131 128 422 C ATOM 2689 O THR B 39 18.338 -3.345 12.987 1.00 29.03 O ANISOU 2689 O THR B 39 2797 3941 4293 130 118 406 O ATOM 2690 CB THR B 39 18.524 -5.193 15.792 1.00 26.84 C ANISOU 2690 CB THR B 39 2510 3662 4024 133 147 450 C ATOM 2691 OG1 THR B 39 19.539 -5.372 16.795 1.00 22.50 O ANISOU 2691 OG1 THR B 39 1969 3121 3459 136 159 459 O ATOM 2692 CG2 THR B 39 18.840 -6.151 14.601 1.00 13.78 C ANISOU 2692 CG2 THR B 39 856 1998 2382 129 135 442 C ATOM 2693 N ALA B 40 16.411 -3.344 14.165 1.00 19.30 N ANISOU 2693 N ALA B 40 1547 2703 3084 129 127 427 N ATOM 2694 CA ALA B 40 15.617 -3.007 12.988 1.00 24.03 C ANISOU 2694 CA ALA B 40 2140 3295 3693 126 113 415 C ATOM 2695 C ALA B 40 15.995 -1.632 12.423 1.00 27.81 C ANISOU 2695 C ALA B 40 2629 3784 4152 128 108 398 C ATOM 2696 O ALA B 40 16.195 -1.496 11.210 1.00 35.05 O ANISOU 2696 O ALA B 40 3549 4698 5069 126 96 382 O ATOM 2697 CB ALA B 40 14.123 -3.073 13.318 1.00 18.47 C ANISOU 2697 CB ALA B 40 1423 2584 3011 124 113 426 C ATOM 2698 N VAL B 41 16.164 -0.617 13.287 1.00 28.17 N ANISOU 2698 N VAL B 41 2680 3841 4181 132 118 399 N ATOM 2699 CA VAL B 41 16.508 0.730 12.810 1.00 24.33 C ANISOU 2699 CA VAL B 41 2203 3365 3676 134 114 383 C ATOM 2700 C VAL B 41 17.840 0.721 12.064 1.00 19.83 C ANISOU 2700 C VAL B 41 1645 2799 3091 134 109 369 C ATOM 2701 O VAL B 41 17.999 1.394 11.042 1.00 21.97 O ANISOU 2701 O VAL B 41 1921 3071 3355 134 99 353 O ATOM 2702 CB VAL B 41 16.524 1.743 13.973 1.00 21.55 C ANISOU 2702 CB VAL B 41 1855 3024 3308 138 127 389 C ATOM 2703 CG1 VAL B 41 17.226 3.027 13.545 1.00 15.96 C ANISOU 2703 CG1 VAL B 41 1159 2327 2577 140 124 373 C ATOM 2704 CG2 VAL B 41 15.103 2.093 14.404 1.00 15.34 C ANISOU 2704 CG2 VAL B 41 1057 2234 2536 137 128 397 C ATOM 2705 N LYS B 42 18.813 -0.045 12.549 1.00 18.48 N ANISOU 2705 N LYS B 42 1480 2630 2914 135 116 376 N ATOM 2706 CA LYS B 42 20.079 -0.136 11.830 1.00 18.23 C ANISOU 2706 CA LYS B 42 1459 2601 2868 136 111 363 C ATOM 2707 C LYS B 42 19.910 -0.823 10.476 1.00 24.52 C ANISOU 2707 C LYS B 42 2252 3387 3679 132 96 354 C ATOM 2708 O LYS B 42 20.618 -0.493 9.509 1.00 22.65 O ANISOU 2708 O LYS B 42 2023 3152 3432 132 87 337 O ATOM 2709 CB LYS B 42 21.128 -0.867 12.684 1.00 18.96 C ANISOU 2709 CB LYS B 42 1557 2697 2951 137 121 374 C ATOM 2710 CG LYS B 42 21.665 -0.055 13.852 1.00 22.15 C ANISOU 2710 CG LYS B 42 1969 3113 3334 142 135 380 C ATOM 2711 CD LYS B 42 22.852 -0.745 14.502 1.00 19.70 C ANISOU 2711 CD LYS B 42 1666 2806 3013 144 143 387 C ATOM 2712 CE LYS B 42 22.378 -2.020 15.201 1.00 18.16 C ANISOU 2712 CE LYS B 42 1461 2603 2836 142 149 406 C ATOM 2713 NZ LYS B 42 23.492 -2.836 15.745 1.00 12.78 N ANISOU 2713 NZ LYS B 42 786 1925 2147 144 156 414 N ATOM 2714 N ALA B 43 18.996 -1.788 10.395 1.00 17.40 N ANISOU 2714 N ALA B 43 1337 2472 2801 129 93 363 N ATOM 2715 CA ALA B 43 18.733 -2.444 9.123 1.00 17.48 C ANISOU 2715 CA ALA B 43 1343 2471 2826 125 78 355 C ATOM 2716 C ALA B 43 17.990 -1.518 8.155 1.00 19.36 C ANISOU 2716 C ALA B 43 1581 2709 3067 124 66 342 C ATOM 2717 O ALA B 43 18.223 -1.555 6.938 1.00 19.08 O ANISOU 2717 O ALA B 43 1548 2669 3031 122 53 328 O ATOM 2718 CB ALA B 43 17.946 -3.726 9.380 1.00 24.60 C ANISOU 2718 CB ALA B 43 2233 3360 3753 122 79 371 C ATOM 2719 N ILE B 44 17.070 -0.707 8.677 1.00 17.26 N ANISOU 2719 N ILE B 44 1309 2445 2802 125 70 346 N ATOM 2720 CA ILE B 44 16.379 0.281 7.860 1.00 20.61 C ANISOU 2720 CA ILE B 44 1733 2870 3227 124 60 333 C ATOM 2721 C ILE B 44 17.356 1.332 7.344 1.00 21.59 C ANISOU 2721 C ILE B 44 1870 3005 3327 127 57 316 C ATOM 2722 O ILE B 44 17.315 1.716 6.171 1.00 25.74 O ANISOU 2722 O ILE B 44 2399 3530 3852 126 44 301 O ATOM 2723 CB ILE B 44 15.240 0.925 8.666 1.00 25.72 C ANISOU 2723 CB ILE B 44 2373 3520 3881 125 67 342 C ATOM 2724 CG1 ILE B 44 14.151 -0.110 8.947 1.00 21.07 C ANISOU 2724 CG1 ILE B 44 1770 2918 3318 122 67 357 C ATOM 2725 CG2 ILE B 44 14.709 2.174 7.940 1.00 17.61 C ANISOU 2725 CG2 ILE B 44 1347 2496 2848 126 58 328 C ATOM 2726 CD1 ILE B 44 13.078 0.403 9.868 1.00 24.29 C ANISOU 2726 CD1 ILE B 44 2169 3327 3732 123 75 368 C ATOM 2727 N SER B 45 18.221 1.852 8.219 1.00 24.35 N ANISOU 2727 N SER B 45 2229 3367 3657 130 69 317 N ATOM 2728 CA SER B 45 19.198 2.836 7.755 1.00 28.53 C ANISOU 2728 CA SER B 45 2771 3906 4163 133 66 301 C ATOM 2729 C SER B 45 20.051 2.277 6.618 1.00 25.77 C ANISOU 2729 C SER B 45 2428 3553 3811 132 55 289 C ATOM 2730 O SER B 45 20.335 2.975 5.642 1.00 18.60 O ANISOU 2730 O SER B 45 1525 2647 2894 132 45 272 O ATOM 2731 CB SER B 45 20.088 3.286 8.910 1.00 23.42 C ANISOU 2731 CB SER B 45 2133 3270 3496 137 81 307 C ATOM 2732 OG SER B 45 20.953 4.338 8.500 1.00 23.97 O ANISOU 2732 OG SER B 45 2215 3348 3544 139 78 291 O ATOM 2733 N SER B 46 20.477 1.020 6.737 1.00 28.80 N ANISOU 2733 N SER B 46 2809 3930 4203 130 57 297 N ATOM 2734 CA SER B 46 21.365 0.438 5.736 1.00 25.24 C ANISOU 2734 CA SER B 46 2365 3477 3750 129 48 286 C ATOM 2735 C SER B 46 20.697 0.384 4.375 1.00 13.58 C ANISOU 2735 C SER B 46 884 1992 2286 126 31 275 C ATOM 2736 O SER B 46 21.322 0.681 3.358 1.00 21.98 O ANISOU 2736 O SER B 46 1955 3057 3339 126 21 260 O ATOM 2737 CB SER B 46 21.789 -0.964 6.175 1.00 26.74 C ANISOU 2737 CB SER B 46 2551 3660 3948 128 53 299 C ATOM 2738 OG SER B 46 22.606 -1.587 5.209 1.00 25.78 O ANISOU 2738 OG SER B 46 2435 3535 3825 126 44 289 O ATOM 2739 N ALA B 47 19.421 0.020 4.346 1.00 23.85 N ANISOU 2739 N ALA B 47 2173 3283 3608 123 28 284 N ATOM 2740 CA ALA B 47 18.677 -0.036 3.100 1.00 20.78 C ANISOU 2740 CA ALA B 47 1780 2885 3232 120 12 275 C ATOM 2741 C ALA B 47 18.337 1.365 2.575 1.00 27.50 C ANISOU 2741 C ALA B 47 2634 3742 4072 122 6 262 C ATOM 2742 O ALA B 47 18.340 1.582 1.356 1.00 33.52 O ANISOU 2742 O ALA B 47 3400 4502 4835 121 -8 248 O ATOM 2743 CB ALA B 47 17.426 -0.882 3.298 1.00 19.56 C ANISOU 2743 CB ALA B 47 1611 2717 3104 117 11 290 C ATOM 2744 N VAL B 48 18.027 2.322 3.466 1.00 19.40 N ANISOU 2744 N VAL B 48 1608 2725 3038 125 16 265 N ATOM 2745 CA VAL B 48 17.693 3.688 3.029 1.00 22.80 C ANISOU 2745 CA VAL B 48 2043 3162 3459 126 11 253 C ATOM 2746 C VAL B 48 18.892 4.384 2.378 1.00 22.15 C ANISOU 2746 C VAL B 48 1973 3088 3353 129 6 235 C ATOM 2747 O VAL B 48 18.732 5.140 1.406 1.00 23.92 O ANISOU 2747 O VAL B 48 2202 3315 3573 129 -5 221 O ATOM 2748 CB VAL B 48 17.126 4.522 4.193 1.00 27.76 C ANISOU 2748 CB VAL B 48 2667 3797 4082 129 23 261 C ATOM 2749 CG1 VAL B 48 17.101 6.042 3.833 1.00 21.70 C ANISOU 2749 CG1 VAL B 48 1906 3038 3299 131 19 247 C ATOM 2750 CG2 VAL B 48 15.737 4.025 4.576 1.00 11.89 C ANISOU 2750 CG2 VAL B 48 644 1778 2097 126 24 275 C ATOM 2751 N ARG B 49 20.100 4.178 2.903 1.00 19.99 N ANISOU 2751 N ARG B 49 1708 2821 3065 131 15 236 N ATOM 2752 CA ARG B 49 21.296 4.708 2.247 1.00 16.99 C ANISOU 2752 CA ARG B 49 1341 2448 2665 133 10 220 C ATOM 2753 C ARG B 49 21.722 3.881 1.013 1.00 27.67 C ANISOU 2753 C ARG B 49 2696 3794 4024 131 -3 211 C ATOM 2754 O ARG B 49 22.809 4.124 0.468 1.00 27.70 O ANISOU 2754 O ARG B 49 2711 3803 4012 132 -7 198 O ATOM 2755 CB ARG B 49 22.468 4.805 3.223 1.00 16.31 C ANISOU 2755 CB ARG B 49 1264 2371 2562 135 24 224 C ATOM 2756 CG ARG B 49 22.543 6.069 4.107 1.00 13.10 C ANISOU 2756 CG ARG B 49 863 1975 2140 138 34 224 C ATOM 2757 CD ARG B 49 21.419 6.106 5.150 1.00 23.83 C ANISOU 2757 CD ARG B 49 2212 3333 3511 138 43 240 C ATOM 2758 NE ARG B 49 21.744 6.985 6.269 1.00 23.15 N ANISOU 2758 NE ARG B 49 2131 3256 3408 141 57 245 N ATOM 2759 CZ ARG B 49 21.417 8.275 6.334 1.00 22.24 C ANISOU 2759 CZ ARG B 49 2020 3147 3285 143 57 238 C ATOM 2760 NH1 ARG B 49 20.756 8.863 5.336 1.00 19.96 N ANISOU 2760 NH1 ARG B 49 1728 2856 3000 142 45 226 N ATOM 2761 NH2 ARG B 49 21.769 8.987 7.393 1.00 17.39 N ANISOU 2761 NH2 ARG B 49 1411 2541 2655 146 70 245 N ATOM 2762 N LYS B 50 20.919 2.883 0.622 1.00 21.69 N ANISOU 2762 N LYS B 50 1929 3025 3288 127 -10 219 N ATOM 2763 CA LYS B 50 21.045 2.151 -0.641 1.00 26.36 C ANISOU 2763 CA LYS B 50 2520 3607 3887 124 -24 211 C ATOM 2764 C LYS B 50 22.214 1.161 -0.656 1.00 27.53 C ANISOU 2764 C LYS B 50 2674 3755 4031 124 -22 212 C ATOM 2765 O LYS B 50 22.809 0.900 -1.700 1.00 22.06 O ANISOU 2765 O LYS B 50 1987 3061 3335 124 -33 201 O ATOM 2766 CB LYS B 50 21.116 3.107 -1.845 1.00 28.60 C ANISOU 2766 CB LYS B 50 2812 3896 4161 125 -37 193 C ATOM 2767 CG LYS B 50 19.818 3.954 -1.996 1.00 26.12 C ANISOU 2767 CG LYS B 50 2491 3580 3854 125 -41 193 C ATOM 2768 CD LYS B 50 18.604 3.031 -2.152 1.00 21.15 C ANISOU 2768 CD LYS B 50 1849 2936 3252 120 -46 205 C ATOM 2769 CE LYS B 50 17.326 3.800 -2.271 1.00 26.99 C ANISOU 2769 CE LYS B 50 2582 3673 4000 120 -50 205 C ATOM 2770 NZ LYS B 50 16.182 2.862 -2.443 1.00 40.70 N ANISOU 2770 NZ LYS B 50 4306 5394 5764 115 -55 216 N ATOM 2771 N ALA B 51 22.561 0.580 0.483 1.00 23.41 N ANISOU 2771 N ALA B 51 2151 3235 3510 125 -9 226 N ATOM 2772 CA ALA B 51 23.516 -0.522 0.449 1.00 27.44 C ANISOU 2772 CA ALA B 51 2664 3742 4020 124 -7 228 C ATOM 2773 C ALA B 51 22.930 -1.700 -0.339 1.00 29.98 C ANISOU 2773 C ALA B 51 2978 4049 4365 120 -18 232 C ATOM 2774 O ALA B 51 21.735 -2.007 -0.230 1.00 20.64 O ANISOU 2774 O ALA B 51 1783 2857 3201 117 -20 242 O ATOM 2775 CB ALA B 51 23.907 -0.955 1.866 1.00 24.21 C ANISOU 2775 CB ALA B 51 2254 3336 3609 126 9 244 C ATOM 2776 N GLY B 52 23.763 -2.286 -1.214 1.00 28.23 N ANISOU 2776 N GLY B 52 2762 3825 4140 119 -27 224 N ATOM 2777 CA GLY B 52 23.396 -3.410 -2.056 1.00 28.71 C ANISOU 2777 CA GLY B 52 2817 3872 4220 115 -38 226 C ATOM 2778 C GLY B 52 22.553 -3.084 -3.269 1.00 39.58 C ANISOU 2778 C GLY B 52 4192 5241 5605 113 -53 218 C ATOM 2779 O GLY B 52 22.091 -4.008 -3.952 1.00 34.37 O ANISOU 2779 O GLY B 52 3527 4568 4964 109 -63 221 O ATOM 2780 N ILE B 53 22.305 -1.803 -3.544 1.00 37.70 N ANISOU 2780 N ILE B 53 3958 5011 5356 115 -56 207 N ATOM 2781 CA ILE B 53 21.492 -1.441 -4.701 1.00 30.07 C ANISOU 2781 CA ILE B 53 2991 4038 4398 113 -71 199 C ATOM 2782 C ILE B 53 22.146 -1.909 -6.009 1.00 26.56 C ANISOU 2782 C ILE B 53 2553 3588 3951 111 -85 189 C ATOM 2783 O ILE B 53 21.448 -2.188 -6.990 1.00 23.21 O ANISOU 2783 O ILE B 53 2126 3153 3541 107 -98 187 O ATOM 2784 CB ILE B 53 21.202 0.077 -4.673 1.00 25.95 C ANISOU 2784 CB ILE B 53 2472 3527 3861 116 -71 190 C ATOM 2785 CG1 ILE B 53 20.078 0.418 -5.631 1.00 30.54 C ANISOU 2785 CG1 ILE B 53 3048 4099 4454 113 -84 187 C ATOM 2786 CG2 ILE B 53 22.450 0.898 -5.004 1.00 20.57 C ANISOU 2786 CG2 ILE B 53 1805 2859 3154 120 -71 175 C ATOM 2787 CD1 ILE B 53 19.782 1.877 -5.690 1.00 31.53 C ANISOU 2787 CD1 ILE B 53 3178 4235 4566 116 -85 177 C ATOM 2788 N ALA B 54 23.480 -2.058 -6.033 1.00 21.36 N ANISOU 2788 N ALA B 54 1903 2937 3275 114 -83 182 N ATOM 2789 CA ALA B 54 24.148 -2.549 -7.238 1.00 25.59 C ANISOU 2789 CA ALA B 54 2446 3469 3808 112 -95 172 C ATOM 2790 C ALA B 54 23.622 -3.915 -7.673 1.00 37.12 C ANISOU 2790 C ALA B 54 3899 4911 5294 107 -102 181 C ATOM 2791 O ALA B 54 23.543 -4.183 -8.880 1.00 35.19 O ANISOU 2791 O ALA B 54 3656 4656 5059 104 -117 177 O ATOM 2792 CB ALA B 54 25.669 -2.612 -7.029 1.00 20.91 C ANISOU 2792 CB ALA B 54 1863 2886 3195 116 -89 166 C ATOM 2793 N HIS B 55 23.255 -4.786 -6.716 1.00 41.81 N ANISOU 2793 N HIS B 55 4483 5499 5903 106 -93 197 N ATOM 2794 CA HIS B 55 22.686 -6.095 -7.058 1.00 37.66 C ANISOU 2794 CA HIS B 55 3949 4954 5406 100 -99 208 C ATOM 2795 C HIS B 55 21.292 -5.956 -7.651 1.00 38.59 C ANISOU 2795 C HIS B 55 4059 5059 5545 96 -109 211 C ATOM 2796 O HIS B 55 20.872 -6.800 -8.448 1.00 44.78 O ANISOU 2796 O HIS B 55 4839 5825 6351 92 -121 214 O ATOM 2797 CB HIS B 55 22.634 -7.017 -5.828 1.00 29.21 C ANISOU 2797 CB HIS B 55 2871 3882 4346 100 -86 224 C ATOM 2798 CG HIS B 55 23.959 -7.593 -5.445 1.00 33.14 C ANISOU 2798 CG HIS B 55 3375 4386 4831 102 -78 224 C ATOM 2799 ND1 HIS B 55 24.426 -8.789 -5.951 1.00 39.90 N ANISOU 2799 ND1 HIS B 55 4230 5230 5700 100 -84 229 N ATOM 2800 CD2 HIS B 55 24.931 -7.130 -4.622 1.00 37.16 C ANISOU 2800 CD2 HIS B 55 3892 4911 5317 107 -66 221 C ATOM 2801 CE1 HIS B 55 25.626 -9.039 -5.454 1.00 40.38 C ANISOU 2801 CE1 HIS B 55 4298 5301 5745 103 -76 228 C ATOM 2802 NE2 HIS B 55 25.956 -8.048 -4.645 1.00 39.67 N ANISOU 2802 NE2 HIS B 55 4213 5227 5632 107 -65 223 N ATOM 2803 N LEU B 56 20.558 -4.911 -7.262 1.00 38.65 N ANISOU 2803 N LEU B 56 4065 5075 5546 98 -106 208 N ATOM 2804 CA LEU B 56 19.252 -4.654 -7.863 1.00 36.00 C ANISOU 2804 CA LEU B 56 3723 4728 5228 95 -116 209 C ATOM 2805 C LEU B 56 19.376 -4.206 -9.318 1.00 31.37 C ANISOU 2805 C LEU B 56 3144 4137 4639 93 -132 196 C ATOM 2806 O LEU B 56 18.477 -4.464 -10.119 1.00 37.10 O ANISOU 2806 O LEU B 56 3864 4846 5385 89 -144 197 O ATOM 2807 CB LEU B 56 18.500 -3.596 -7.050 1.00 29.89 C ANISOU 2807 CB LEU B 56 2944 3963 4448 97 -107 211 C ATOM 2808 CG LEU B 56 17.803 -3.959 -5.727 1.00 43.01 C ANISOU 2808 CG LEU B 56 4595 5623 6122 97 -93 228 C ATOM 2809 CD1 LEU B 56 18.691 -4.800 -4.759 1.00 35.16 C ANISOU 2809 CD1 LEU B 56 3602 4634 5125 99 -81 237 C ATOM 2810 CD2 LEU B 56 17.306 -2.682 -5.018 1.00 47.44 C ANISOU 2810 CD2 LEU B 56 5155 6196 6673 100 -85 228 C ATOM 2811 N TYR B 57 20.499 -3.596 -9.699 1.00 22.08 N ANISOU 2811 N TYR B 57 1980 2973 3438 97 -133 183 N ATOM 2812 CA TYR B 57 20.695 -3.117 -11.061 1.00 27.45 C ANISOU 2812 CA TYR B 57 2667 3649 4112 95 -148 170 C ATOM 2813 C TYR B 57 21.596 -4.053 -11.878 1.00 33.43 C ANISOU 2813 C TYR B 57 3430 4398 4874 93 -157 168 C ATOM 2814 O TYR B 57 22.213 -3.615 -12.856 1.00 33.00 O ANISOU 2814 O TYR B 57 3386 4345 4807 94 -167 155 O ATOM 2815 CB TYR B 57 21.232 -1.671 -11.029 1.00 29.68 C ANISOU 2815 CB TYR B 57 2960 3952 4365 101 -145 157 C ATOM 2816 CG TYR B 57 20.139 -0.643 -10.728 1.00 31.72 C ANISOU 2816 CG TYR B 57 3214 4215 4623 102 -143 156 C ATOM 2817 CD1 TYR B 57 19.664 -0.444 -9.429 1.00 31.22 C ANISOU 2817 CD1 TYR B 57 3143 4158 4562 104 -129 166 C ATOM 2818 CD2 TYR B 57 19.559 0.103 -11.751 1.00 24.23 C ANISOU 2818 CD2 TYR B 57 2269 3263 3676 100 -156 148 C ATOM 2819 CE1 TYR B 57 18.649 0.470 -9.175 1.00 32.22 C ANISOU 2819 CE1 TYR B 57 3265 4287 4692 104 -128 167 C ATOM 2820 CE2 TYR B 57 18.551 1.026 -11.497 1.00 23.58 C ANISOU 2820 CE2 TYR B 57 2182 3184 3594 101 -154 148 C ATOM 2821 CZ TYR B 57 18.094 1.196 -10.219 1.00 28.78 C ANISOU 2821 CZ TYR B 57 2832 3848 4256 103 -141 158 C ATOM 2822 OH TYR B 57 17.087 2.107 -9.994 1.00 28.74 O ANISOU 2822 OH TYR B 57 2822 3845 4254 103 -140 159 O ATOM 2823 N GLY B 58 21.722 -5.319 -11.457 1.00 31.94 N ANISOU 2823 N GLY B 58 3235 4199 4701 91 -153 179 N ATOM 2824 CA GLY B 58 22.291 -6.363 -12.292 1.00 35.75 C ANISOU 2824 CA GLY B 58 3721 4668 5195 88 -163 178 C ATOM 2825 C GLY B 58 23.791 -6.577 -12.263 1.00 34.64 C ANISOU 2825 C GLY B 58 3589 4538 5035 91 -159 173 C ATOM 2826 O GLY B 58 24.358 -7.004 -13.279 1.00 39.54 O ANISOU 2826 O GLY B 58 4216 5150 5658 89 -171 166 O ATOM 2827 N ILE B 59 24.461 -6.311 -11.138 1.00 28.06 N ANISOU 2827 N ILE B 59 2757 3721 4182 96 -144 175 N ATOM 2828 CA ILE B 59 25.920 -6.414 -11.120 1.00 20.87 C ANISOU 2828 CA ILE B 59 1856 2821 3252 99 -140 168 C ATOM 2829 C ILE B 59 26.389 -7.864 -11.264 1.00 28.01 C ANISOU 2829 C ILE B 59 2758 3713 4172 96 -142 176 C ATOM 2830 O ILE B 59 27.464 -8.120 -11.815 1.00 30.97 O ANISOU 2830 O ILE B 59 3141 4089 4536 97 -146 169 O ATOM 2831 CB ILE B 59 26.469 -5.755 -9.838 1.00 29.70 C ANISOU 2831 CB ILE B 59 2977 3959 4347 105 -123 168 C ATOM 2832 CG1 ILE B 59 27.968 -5.485 -9.960 1.00 23.61 C ANISOU 2832 CG1 ILE B 59 2218 3202 3550 109 -120 157 C ATOM 2833 CG2 ILE B 59 26.218 -6.644 -8.609 1.00 25.94 C ANISOU 2833 CG2 ILE B 59 2492 3481 3884 104 -109 184 C ATOM 2834 CD1 ILE B 59 28.578 -4.954 -8.689 1.00 32.31 C ANISOU 2834 CD1 ILE B 59 3324 4322 4632 114 -103 157 C ATOM 2835 N ALA B 60 25.598 -8.839 -10.813 1.00 32.78 N ANISOU 2835 N ALA B 60 3351 4303 4802 93 -140 190 N ATOM 2836 CA ALA B 60 25.954 -10.245 -10.980 1.00 30.22 C ANISOU 2836 CA ALA B 60 3023 3965 4495 89 -142 198 C ATOM 2837 C ALA B 60 25.120 -10.928 -12.052 1.00 39.10 C ANISOU 2837 C ALA B 60 4143 5066 5647 83 -159 199 C ATOM 2838 O ALA B 60 25.094 -12.162 -12.109 1.00 42.88 O ANISOU 2838 O ALA B 60 4616 5530 6146 79 -161 208 O ATOM 2839 CB ALA B 60 25.803 -11.007 -9.656 1.00 27.02 C ANISOU 2839 CB ALA B 60 2609 3560 4098 90 -128 214 C ATOM 2840 N GLY B 61 24.461 -10.151 -12.915 1.00 40.36 N ANISOU 2840 N GLY B 61 4305 5222 5809 81 -170 191 N ATOM 2841 CA GLY B 61 23.602 -10.676 -13.966 1.00 35.46 C ANISOU 2841 CA GLY B 61 3680 4578 5214 75 -186 191 C ATOM 2842 C GLY B 61 22.173 -10.979 -13.552 1.00 39.58 C ANISOU 2842 C GLY B 61 4189 5088 5761 72 -185 202 C ATOM 2843 O GLY B 61 21.637 -10.349 -12.648 1.00 48.37 O ANISOU 2843 O GLY B 61 5298 6213 6869 74 -174 207 O ATOM 2844 N LYS B 72 8.753 -0.629 -1.948 1.00 55.40 N ANISOU 2844 N LYS B 72 6097 7178 7776 93 -69 283 N ATOM 2845 CA LYS B 72 9.348 -1.784 -1.292 1.00 46.94 C ANISOU 2845 CA LYS B 72 5023 6103 6709 93 -60 294 C ATOM 2846 C LYS B 72 10.002 -1.378 0.024 1.00 44.65 C ANISOU 2846 C LYS B 72 4735 5828 6401 97 -43 299 C ATOM 2847 O LYS B 72 9.969 -2.149 0.994 1.00 42.63 O ANISOU 2847 O LYS B 72 4473 5570 6153 97 -33 314 O ATOM 2848 CB LYS B 72 10.371 -2.461 -2.199 1.00 37.17 C ANISOU 2848 CB LYS B 72 3793 4862 5467 91 -69 285 C ATOM 2849 CG LYS B 72 10.986 -3.745 -1.634 1.00 43.83 C ANISOU 2849 CG LYS B 72 4636 5702 6317 90 -62 296 C ATOM 2850 CD LYS B 72 9.999 -4.911 -1.638 1.00 45.16 C ANISOU 2850 CD LYS B 72 4792 5852 6515 86 -65 309 C ATOM 2851 CE LYS B 72 10.506 -6.130 -0.828 1.00 47.68 C ANISOU 2851 CE LYS B 72 5107 6168 6840 85 -55 322 C ATOM 2852 NZ LYS B 72 10.314 -6.092 0.675 1.00 41.10 N ANISOU 2852 NZ LYS B 72 4268 5341 6005 88 -38 337 N ATOM 2853 N LEU B 73 10.565 -0.160 0.063 1.00 35.99 N ANISOU 2853 N LEU B 73 3648 4747 5281 101 -41 288 N ATOM 2854 CA LEU B 73 11.374 0.254 1.212 1.00 32.80 C ANISOU 2854 CA LEU B 73 3249 4357 4857 106 -26 292 C ATOM 2855 C LEU B 73 10.518 0.436 2.455 1.00 33.89 C ANISOU 2855 C LEU B 73 3377 4496 5002 106 -13 306 C ATOM 2856 O LEU B 73 10.908 0.015 3.550 1.00 37.86 O ANISOU 2856 O LEU B 73 3879 5003 5503 108 0 318 O ATOM 2857 CB LEU B 73 12.126 1.541 0.902 1.00 32.68 C ANISOU 2857 CB LEU B 73 3245 4356 4816 109 -27 276 C ATOM 2858 CG LEU B 73 13.570 1.588 1.381 1.00 29.36 C ANISOU 2858 CG LEU B 73 2834 3946 4373 113 -18 273 C ATOM 2859 CD1 LEU B 73 14.264 0.249 1.133 1.00 28.72 C ANISOU 2859 CD1 LEU B 73 2755 3858 4300 111 -20 277 C ATOM 2860 CD2 LEU B 73 14.299 2.726 0.686 1.00 20.80 C ANISOU 2860 CD2 LEU B 73 1763 2874 3267 116 -24 255 C ATOM 2861 N ASP B 74 9.323 1.009 2.305 1.00 23.31 N ANISOU 2861 N ASP B 74 2030 3153 3673 105 -17 307 N ATOM 2862 CA ASP B 74 8.440 1.074 3.455 1.00 40.31 C ANISOU 2862 CA ASP B 74 4174 5307 5836 106 -6 321 C ATOM 2863 C ASP B 74 7.888 -0.312 3.819 1.00 42.67 C ANISOU 2863 C ASP B 74 4463 5592 6159 102 -4 337 C ATOM 2864 O ASP B 74 7.621 -0.576 4.995 1.00 53.36 O ANISOU 2864 O ASP B 74 5810 6946 7517 103 9 352 O ATOM 2865 CB ASP B 74 7.325 2.081 3.185 1.00 51.55 C ANISOU 2865 CB ASP B 74 5593 6730 7263 106 -11 317 C ATOM 2866 CG ASP B 74 6.556 1.772 1.924 1.00 64.46 C ANISOU 2866 CG ASP B 74 7224 8351 8917 102 -28 311 C ATOM 2867 OD1 ASP B 74 6.929 0.820 1.206 1.00 71.23 O ANISOU 2867 OD1 ASP B 74 8082 9199 9782 99 -35 310 O ATOM 2868 OD2 ASP B 74 5.580 2.491 1.642 1.00 72.81 O ANISOU 2868 OD2 ASP B 74 8278 9407 9980 101 -33 308 O ATOM 2869 N VAL B 75 7.723 -1.207 2.836 1.00 34.28 N ANISOU 2869 N VAL B 75 3398 4515 5113 98 -16 335 N ATOM 2870 CA VAL B 75 7.321 -2.589 3.113 1.00 36.82 C ANISOU 2870 CA VAL B 75 3709 4823 5456 95 -15 349 C ATOM 2871 C VAL B 75 8.442 -3.367 3.809 1.00 33.22 C ANISOU 2871 C VAL B 75 3259 4372 4993 96 -4 356 C ATOM 2872 O VAL B 75 8.197 -4.133 4.743 1.00 23.53 O ANISOU 2872 O VAL B 75 2024 3141 3776 96 5 372 O ATOM 2873 CB VAL B 75 6.870 -3.278 1.814 1.00 38.96 C ANISOU 2873 CB VAL B 75 3978 5078 5746 90 -31 344 C ATOM 2874 CG1 VAL B 75 6.673 -4.763 2.052 1.00 43.36 C ANISOU 2874 CG1 VAL B 75 4528 5622 6326 86 -30 358 C ATOM 2875 CG2 VAL B 75 5.586 -2.654 1.315 1.00 30.75 C ANISOU 2875 CG2 VAL B 75 2932 4033 4720 88 -39 341 C ATOM 2876 N LEU B 76 9.681 -3.230 3.341 1.00 31.67 N ANISOU 2876 N LEU B 76 3073 4182 4777 98 -7 345 N ATOM 2877 CA LEU B 76 10.777 -3.895 4.035 1.00 32.29 C ANISOU 2877 CA LEU B 76 3156 4266 4847 100 3 351 C ATOM 2878 C LEU B 76 10.931 -3.347 5.459 1.00 36.95 C ANISOU 2878 C LEU B 76 3746 4868 5423 104 20 360 C ATOM 2879 O LEU B 76 11.213 -4.099 6.397 1.00 39.59 O ANISOU 2879 O LEU B 76 4078 5202 5761 104 31 374 O ATOM 2880 CB LEU B 76 12.072 -3.729 3.249 1.00 29.73 C ANISOU 2880 CB LEU B 76 2845 3948 4504 101 -3 336 C ATOM 2881 CG LEU B 76 13.304 -4.323 3.925 1.00 29.11 C ANISOU 2881 CG LEU B 76 2772 3875 4412 103 7 341 C ATOM 2882 CD1 LEU B 76 13.254 -5.863 3.876 1.00 21.26 C ANISOU 2882 CD1 LEU B 76 1772 2867 3439 100 6 351 C ATOM 2883 CD2 LEU B 76 14.592 -3.762 3.311 1.00 31.83 C ANISOU 2883 CD2 LEU B 76 3131 4231 4734 106 4 324 C ATOM 2884 N SER B 77 10.775 -2.029 5.633 1.00 27.89 N ANISOU 2884 N SER B 77 2603 3732 4262 107 22 353 N ATOM 2885 CA SER B 77 10.872 -1.439 6.965 1.00 26.37 C ANISOU 2885 CA SER B 77 2412 3551 4058 110 38 362 C ATOM 2886 C SER B 77 9.822 -2.024 7.913 1.00 28.27 C ANISOU 2886 C SER B 77 2640 3785 4318 109 46 381 C ATOM 2887 O SER B 77 10.125 -2.340 9.074 1.00 28.53 O ANISOU 2887 O SER B 77 2672 3822 4347 111 59 393 O ATOM 2888 CB SER B 77 10.726 0.084 6.866 1.00 26.54 C ANISOU 2888 CB SER B 77 2438 3584 4063 113 37 351 C ATOM 2889 OG SER B 77 11.759 0.664 6.072 1.00 20.52 O ANISOU 2889 OG SER B 77 1688 2829 3281 115 31 334 O ATOM 2890 N ASN B 78 8.574 -2.158 7.442 1.00 26.34 N ANISOU 2890 N ASN B 78 2385 3529 4094 106 38 383 N ATOM 2891 CA ASN B 78 7.533 -2.742 8.284 1.00 28.11 C ANISOU 2891 CA ASN B 78 2596 3745 4338 104 45 400 C ATOM 2892 C ASN B 78 7.861 -4.194 8.632 1.00 34.98 C ANISOU 2892 C ASN B 78 3462 4606 5220 102 49 413 C ATOM 2893 O ASN B 78 7.647 -4.627 9.770 1.00 34.32 O ANISOU 2893 O ASN B 78 3374 4523 5142 103 61 428 O ATOM 2894 CB ASN B 78 6.168 -2.632 7.611 1.00 25.58 C ANISOU 2894 CB ASN B 78 2266 3414 4038 101 34 399 C ATOM 2895 CG ASN B 78 5.011 -2.883 8.585 1.00 29.97 C ANISOU 2895 CG ASN B 78 2810 3965 4612 100 43 416 C ATOM 2896 OD1 ASN B 78 4.936 -2.270 9.643 1.00 39.44 O ANISOU 2896 OD1 ASN B 78 4009 5175 5801 104 55 422 O ATOM 2897 ND2 ASN B 78 4.122 -3.805 8.235 1.00 29.88 N ANISOU 2897 ND2 ASN B 78 2789 3939 4627 96 36 423 N ATOM 2898 N ASP B 79 8.383 -4.959 7.663 1.00 31.06 N ANISOU 2898 N ASP B 79 2969 4103 4729 100 38 406 N ATOM 2899 CA ASP B 79 8.753 -6.348 7.925 1.00 34.31 C ANISOU 2899 CA ASP B 79 3379 4506 5153 98 41 417 C ATOM 2900 C ASP B 79 9.888 -6.448 8.935 1.00 32.90 C ANISOU 2900 C ASP B 79 3206 4338 4955 102 55 422 C ATOM 2901 O ASP B 79 9.891 -7.344 9.789 1.00 34.97 O ANISOU 2901 O ASP B 79 3463 4597 5225 102 64 438 O ATOM 2902 CB ASP B 79 9.155 -7.051 6.623 1.00 36.54 C ANISOU 2902 CB ASP B 79 3664 4779 5442 95 27 407 C ATOM 2903 CG ASP B 79 7.976 -7.383 5.744 1.00 36.48 C ANISOU 2903 CG ASP B 79 3647 4755 5458 90 14 406 C ATOM 2904 OD1 ASP B 79 6.826 -7.242 6.204 1.00 34.78 O ANISOU 2904 OD1 ASP B 79 3422 4536 5257 89 17 415 O ATOM 2905 OD2 ASP B 79 8.209 -7.768 4.580 1.00 37.93 O ANISOU 2905 OD2 ASP B 79 3834 4931 5647 87 1 396 O ATOM 2906 N LEU B 80 10.857 -5.539 8.862 1.00 32.73 N ANISOU 2906 N LEU B 80 3197 4331 4908 105 57 411 N ATOM 2907 CA LEU B 80 11.976 -5.584 9.796 1.00 36.46 C ANISOU 2907 CA LEU B 80 3677 4814 5362 109 70 416 C ATOM 2908 C LEU B 80 11.514 -5.307 11.225 1.00 34.69 C ANISOU 2908 C LEU B 80 3448 4596 5137 112 85 431 C ATOM 2909 O LEU B 80 11.835 -6.064 12.151 1.00 34.54 O ANISOU 2909 O LEU B 80 3428 4577 5120 112 95 445 O ATOM 2910 CB LEU B 80 13.036 -4.570 9.376 1.00 38.14 C ANISOU 2910 CB LEU B 80 3903 5039 5548 112 68 399 C ATOM 2911 CG LEU B 80 13.883 -4.935 8.173 1.00 38.03 C ANISOU 2911 CG LEU B 80 3896 5022 5530 110 56 385 C ATOM 2912 CD1 LEU B 80 14.523 -3.676 7.675 1.00 38.82 C ANISOU 2912 CD1 LEU B 80 4008 5135 5607 113 53 368 C ATOM 2913 CD2 LEU B 80 14.931 -5.974 8.537 1.00 38.76 C ANISOU 2913 CD2 LEU B 80 3993 5115 5620 111 62 392 C ATOM 2914 N VAL B 81 10.742 -4.232 11.417 1.00 22.01 N ANISOU 2914 N VAL B 81 1840 2995 3528 113 86 429 N ATOM 2915 CA VAL B 81 10.277 -3.864 12.757 1.00 26.08 C ANISOU 2915 CA VAL B 81 2351 3516 4041 116 99 442 C ATOM 2916 C VAL B 81 9.352 -4.938 13.326 1.00 25.67 C ANISOU 2916 C VAL B 81 2286 3452 4014 113 103 460 C ATOM 2917 O VAL B 81 9.470 -5.320 14.494 1.00 32.58 O ANISOU 2917 O VAL B 81 3159 4331 4888 115 116 475 O ATOM 2918 CB VAL B 81 9.614 -2.472 12.732 1.00 23.47 C ANISOU 2918 CB VAL B 81 2021 3194 3704 117 98 435 C ATOM 2919 CG1 VAL B 81 9.027 -2.143 14.072 1.00 12.88 C ANISOU 2919 CG1 VAL B 81 674 1857 2362 120 112 449 C ATOM 2920 CG2 VAL B 81 10.666 -1.390 12.358 1.00 18.66 C ANISOU 2920 CG2 VAL B 81 1426 2598 3068 120 97 418 C ATOM 2921 N MET B 82 8.412 -5.430 12.515 1.00 27.81 N ANISOU 2921 N MET B 82 2549 3711 4308 109 92 459 N ATOM 2922 CA MET B 82 7.469 -6.458 12.972 1.00 32.76 C ANISOU 2922 CA MET B 82 3163 4325 4960 106 95 476 C ATOM 2923 C MET B 82 8.192 -7.724 13.448 1.00 36.30 C ANISOU 2923 C MET B 82 3611 4769 5412 106 101 487 C ATOM 2924 O MET B 82 7.886 -8.267 14.517 1.00 38.94 O ANISOU 2924 O MET B 82 3940 5103 5754 107 112 503 O ATOM 2925 CB MET B 82 6.488 -6.799 11.842 1.00 31.82 C ANISOU 2925 CB MET B 82 3035 4191 4863 101 80 471 C ATOM 2926 CG MET B 82 5.363 -5.792 11.603 1.00 31.86 C ANISOU 2926 CG MET B 82 3036 4197 4873 101 76 466 C ATOM 2927 SD MET B 82 4.112 -5.866 12.898 1.00 36.15 S ANISOU 2927 SD MET B 82 3566 4738 5431 102 87 486 S ATOM 2928 CE MET B 82 2.986 -4.540 12.416 1.00 17.52 C ANISOU 2928 CE MET B 82 1203 2380 3073 101 80 476 C ATOM 2929 N ASN B 83 9.159 -8.206 12.665 1.00 32.18 N ANISOU 2929 N ASN B 83 3097 4246 4885 105 94 478 N ATOM 2930 CA ASN B 83 9.802 -9.477 12.986 1.00 34.85 C ANISOU 2930 CA ASN B 83 3435 4578 5228 104 98 487 C ATOM 2931 C ASN B 83 10.742 -9.362 14.186 1.00 34.94 C ANISOU 2931 C ASN B 83 3452 4602 5220 109 113 495 C ATOM 2932 O ASN B 83 10.818 -10.286 15.001 1.00 39.17 O ANISOU 2932 O ASN B 83 3985 5135 5764 109 122 510 O ATOM 2933 CB ASN B 83 10.573 -10.009 11.779 1.00 33.93 C ANISOU 2933 CB ASN B 83 3324 4457 5112 102 86 475 C ATOM 2934 CG ASN B 83 11.113 -11.404 12.022 1.00 43.61 C ANISOU 2934 CG ASN B 83 4548 5675 6347 100 89 485 C ATOM 2935 OD1 ASN B 83 10.378 -12.375 11.842 1.00 56.85 O ANISOU 2935 OD1 ASN B 83 6215 7337 8047 97 85 493 O ATOM 2936 ND2 ASN B 83 12.369 -11.517 12.466 1.00 27.47 N ANISOU 2936 ND2 ASN B 83 2514 3641 4284 103 97 485 N ATOM 2937 N MET B 84 11.512 -8.272 14.288 1.00 31.45 N ANISOU 2937 N MET B 84 3021 4174 4752 112 116 485 N ATOM 2938 CA MET B 84 12.397 -8.128 15.443 1.00 34.55 C ANISOU 2938 CA MET B 84 3421 4579 5126 117 131 493 C ATOM 2939 C MET B 84 11.605 -7.914 16.726 1.00 36.36 C ANISOU 2939 C MET B 84 3644 4812 5360 119 143 509 C ATOM 2940 O MET B 84 12.065 -8.302 17.803 1.00 37.50 O ANISOU 2940 O MET B 84 3790 4961 5498 122 155 522 O ATOM 2941 CB MET B 84 13.391 -6.978 15.251 1.00 28.20 C ANISOU 2941 CB MET B 84 2632 3790 4295 120 131 478 C ATOM 2942 CG MET B 84 14.465 -7.224 14.202 1.00 28.63 C ANISOU 2942 CG MET B 84 2695 3844 4340 119 122 464 C ATOM 2943 SD MET B 84 15.400 -8.753 14.501 1.00 35.42 S ANISOU 2943 SD MET B 84 3555 4698 5204 118 126 474 S ATOM 2944 CE MET B 84 16.097 -8.465 16.135 1.00 34.50 C ANISOU 2944 CE MET B 84 3446 4596 5068 124 145 487 C ATOM 2945 N LEU B 85 10.438 -7.270 16.637 1.00 36.10 N ANISOU 2945 N LEU B 85 3604 4777 5336 118 140 508 N ATOM 2946 CA LEU B 85 9.609 -7.079 17.822 1.00 37.42 C ANISOU 2946 CA LEU B 85 3763 4945 5508 120 151 523 C ATOM 2947 C LEU B 85 8.924 -8.388 18.241 1.00 42.33 C ANISOU 2947 C LEU B 85 4373 5554 6155 117 153 540 C ATOM 2948 O LEU B 85 8.919 -8.746 19.428 1.00 41.72 O ANISOU 2948 O LEU B 85 4294 5480 6078 120 165 556 O ATOM 2949 CB LEU B 85 8.593 -5.958 17.569 1.00 36.04 C ANISOU 2949 CB LEU B 85 3585 4774 5336 120 146 517 C ATOM 2950 CG LEU B 85 9.119 -4.509 17.567 1.00 28.02 C ANISOU 2950 CG LEU B 85 2580 3772 4295 123 148 504 C ATOM 2951 CD1 LEU B 85 8.011 -3.522 17.331 1.00 28.81 C ANISOU 2951 CD1 LEU B 85 2674 3872 4399 123 144 499 C ATOM 2952 CD2 LEU B 85 9.816 -4.172 18.883 1.00 25.84 C ANISOU 2952 CD2 LEU B 85 2310 3508 3999 128 163 513 C ATOM 2953 N LYS B 86 8.328 -9.112 17.283 1.00 32.42 N ANISOU 2953 N LYS B 86 3111 4285 4922 113 142 538 N ATOM 2954 CA LYS B 86 7.711 -10.402 17.590 1.00 32.27 C ANISOU 2954 CA LYS B 86 3081 4254 4928 110 143 553 C ATOM 2955 C LYS B 86 8.679 -11.349 18.286 1.00 32.16 C ANISOU 2955 C LYS B 86 3070 4240 4908 111 152 563 C ATOM 2956 O LYS B 86 8.341 -11.971 19.298 1.00 36.09 O ANISOU 2956 O LYS B 86 3562 4735 5415 112 162 581 O ATOM 2957 CB LYS B 86 7.181 -11.063 16.318 1.00 37.48 C ANISOU 2957 CB LYS B 86 3735 4898 5609 104 128 546 C ATOM 2958 CG LYS B 86 5.908 -10.466 15.741 1.00 34.40 C ANISOU 2958 CG LYS B 86 3337 4502 5232 102 120 541 C ATOM 2959 CD LYS B 86 5.603 -11.095 14.385 1.00 29.47 C ANISOU 2959 CD LYS B 86 2709 3863 4625 97 104 533 C ATOM 2960 CE LYS B 86 4.310 -10.549 13.803 1.00 33.98 C ANISOU 2960 CE LYS B 86 3273 4428 5211 94 95 528 C ATOM 2961 NZ LYS B 86 4.013 -11.053 12.428 1.00 36.71 N ANISOU 2961 NZ LYS B 86 3615 4759 5572 89 79 519 N ATOM 2962 N SER B 87 9.882 -11.485 17.743 1.00 27.77 N ANISOU 2962 N SER B 87 2524 3688 4338 112 149 553 N ATOM 2963 CA SER B 87 10.885 -12.407 18.256 1.00 30.86 C ANISOU 2963 CA SER B 87 2920 4080 4725 113 155 561 C ATOM 2964 C SER B 87 11.599 -11.901 19.507 1.00 34.34 C ANISOU 2964 C SER B 87 3369 4535 5143 119 170 568 C ATOM 2965 O SER B 87 12.477 -12.601 20.029 1.00 31.27 O ANISOU 2965 O SER B 87 2984 4148 4748 120 177 576 O ATOM 2966 CB SER B 87 11.901 -12.708 17.153 1.00 38.10 C ANISOU 2966 CB SER B 87 3846 4996 5635 112 146 547 C ATOM 2967 OG SER B 87 12.654 -11.550 16.846 1.00 45.08 O ANISOU 2967 OG SER B 87 4742 5893 6494 114 144 532 O ATOM 2968 N SER B 88 11.269 -10.703 19.991 1.00 32.71 N ANISOU 2968 N SER B 88 3164 4339 4924 122 175 567 N ATOM 2969 CA SER B 88 11.855 -10.215 21.232 1.00 35.03 C ANISOU 2969 CA SER B 88 3465 4646 5198 127 189 575 C ATOM 2970 C SER B 88 11.224 -10.847 22.469 1.00 34.06 C ANISOU 2970 C SER B 88 3333 4521 5088 128 200 596 C ATOM 2971 O SER B 88 11.828 -10.802 23.550 1.00 21.14 O ANISOU 2971 O SER B 88 1701 2893 3437 133 211 606 O ATOM 2972 CB SER B 88 11.719 -8.688 21.304 1.00 33.07 C ANISOU 2972 CB SER B 88 3223 4411 4934 130 190 565 C ATOM 2973 OG SER B 88 10.368 -8.307 21.520 1.00 30.25 O ANISOU 2973 OG SER B 88 2854 4049 4590 129 189 570 O ATOM 2974 N PHE B 89 10.039 -11.441 22.322 1.00 35.04 N ANISOU 2974 N PHE B 89 3444 4632 5237 125 196 603 N ATOM 2975 CA PHE B 89 9.270 -11.970 23.445 1.00 46.72 C ANISOU 2975 CA PHE B 89 4914 6108 6730 126 206 623 C ATOM 2976 C PHE B 89 8.883 -10.873 24.430 1.00 43.04 C ANISOU 2976 C PHE B 89 4448 5653 6252 130 215 628 C ATOM 2977 O PHE B 89 8.645 -11.139 25.606 1.00 48.20 O ANISOU 2977 O PHE B 89 5097 6308 6907 133 226 644 O ATOM 2978 CB PHE B 89 10.020 -13.109 24.154 1.00 49.12 C ANISOU 2978 CB PHE B 89 5219 6410 7035 127 214 636 C ATOM 2979 CG PHE B 89 10.081 -14.386 23.353 1.00 59.57 C ANISOU 2979 CG PHE B 89 6538 7720 8377 123 205 636 C ATOM 2980 CD1 PHE B 89 10.786 -14.446 22.160 1.00 68.71 C ANISOU 2980 CD1 PHE B 89 7702 8876 9531 120 195 620 C ATOM 2981 CD2 PHE B 89 9.432 -15.526 23.794 1.00 64.62 C ANISOU 2981 CD2 PHE B 89 7166 8347 9039 121 208 652 C ATOM 2982 CE1 PHE B 89 10.835 -15.618 21.419 1.00 69.71 C ANISOU 2982 CE1 PHE B 89 7824 8988 9674 116 187 620 C ATOM 2983 CE2 PHE B 89 9.482 -16.697 23.063 1.00 65.98 C ANISOU 2983 CE2 PHE B 89 7334 8506 9229 117 201 652 C ATOM 2984 CZ PHE B 89 10.179 -16.742 21.874 1.00 69.70 C ANISOU 2984 CZ PHE B 89 7812 8975 9695 114 190 636 C ATOM 2985 N ALA B 90 8.798 -9.627 23.964 1.00 38.90 N ANISOU 2985 N ALA B 90 3929 5137 5715 131 211 614 N ATOM 2986 CA ALA B 90 8.487 -8.507 24.845 1.00 33.98 C ANISOU 2986 CA ALA B 90 3307 4524 5078 135 219 617 C ATOM 2987 C ALA B 90 7.209 -7.772 24.470 1.00 33.78 C ANISOU 2987 C ALA B 90 3274 4497 5065 133 214 613 C ATOM 2988 O ALA B 90 6.831 -6.826 25.173 1.00 36.11 O ANISOU 2988 O ALA B 90 3569 4800 5350 136 220 615 O ATOM 2989 CB ALA B 90 9.649 -7.502 24.867 1.00 31.43 C ANISOU 2989 CB ALA B 90 2999 4216 4726 139 222 606 C ATOM 2990 N THR B 91 6.509 -8.191 23.414 1.00 31.31 N ANISOU 2990 N THR B 91 2953 4170 4772 128 202 607 N ATOM 2991 CA THR B 91 5.341 -7.469 22.931 1.00 28.58 C ANISOU 2991 CA THR B 91 2600 3822 4436 126 195 601 C ATOM 2992 C THR B 91 4.164 -8.424 22.776 1.00 30.19 C ANISOU 2992 C THR B 91 2791 4011 4671 122 191 611 C ATOM 2993 O THR B 91 4.328 -9.647 22.731 1.00 34.58 O ANISOU 2993 O THR B 91 3342 4557 5240 120 191 619 O ATOM 2994 CB THR B 91 5.626 -6.746 21.591 1.00 36.89 C ANISOU 2994 CB THR B 91 3659 4875 5481 124 182 579 C ATOM 2995 OG1 THR B 91 5.807 -7.696 20.539 1.00 37.80 O ANISOU 2995 OG1 THR B 91 3773 4979 5610 120 172 574 O ATOM 2996 CG2 THR B 91 6.878 -5.894 21.697 1.00 38.55 C ANISOU 2996 CG2 THR B 91 3884 5100 5661 128 186 569 C ATOM 2997 N CYS B 92 2.963 -7.845 22.699 1.00 36.90 N ANISOU 2997 N CYS B 92 3632 4858 5532 121 189 611 N ATOM 2998 CA CYS B 92 1.752 -8.624 22.447 1.00 37.75 C ANISOU 2998 CA CYS B 92 3725 4950 5668 116 184 619 C ATOM 2999 C CYS B 92 0.877 -7.998 21.362 1.00 42.88 C ANISOU 2999 C CYS B 92 4371 5594 6327 113 171 606 C ATOM 3000 O CYS B 92 0.165 -8.730 20.668 1.00 52.47 O ANISOU 3000 O CYS B 92 5577 6795 7565 109 162 607 O ATOM 3001 CB CYS B 92 0.940 -8.813 23.735 1.00 34.17 C ANISOU 3001 CB CYS B 92 3263 4496 5224 118 196 638 C ATOM 3002 SG CYS B 92 0.495 -7.298 24.621 1.00 43.51 S ANISOU 3002 SG CYS B 92 4447 5694 6390 123 204 638 S ATOM 3003 N VAL B 93 0.912 -6.665 21.203 1.00 34.80 N ANISOU 3003 N VAL B 93 3353 4581 5287 115 170 594 N ATOM 3004 CA VAL B 93 0.119 -5.954 20.197 1.00 26.96 C ANISOU 3004 CA VAL B 93 2357 3585 4301 113 158 581 C ATOM 3005 C VAL B 93 0.991 -4.923 19.482 1.00 35.34 C ANISOU 3005 C VAL B 93 3431 4656 5339 114 153 562 C ATOM 3006 O VAL B 93 1.688 -4.129 20.126 1.00 27.92 O ANISOU 3006 O VAL B 93 2501 3731 4376 119 161 561 O ATOM 3007 CB VAL B 93 -1.113 -5.259 20.808 1.00 35.75 C ANISOU 3007 CB VAL B 93 3462 4699 5421 114 163 588 C ATOM 3008 CG1 VAL B 93 -1.860 -4.466 19.738 1.00 33.27 C ANISOU 3008 CG1 VAL B 93 3145 4382 5112 111 150 574 C ATOM 3009 CG2 VAL B 93 -2.049 -6.275 21.442 1.00 37.35 C ANISOU 3009 CG2 VAL B 93 3651 4891 5648 112 167 606 C ATOM 3010 N LEU B 94 0.907 -4.898 18.150 1.00 36.59 N ANISOU 3010 N LEU B 94 3591 4808 5504 111 138 548 N ATOM 3011 CA LEU B 94 1.722 -4.021 17.321 1.00 39.97 C ANISOU 3011 CA LEU B 94 4031 5245 5912 112 131 529 C ATOM 3012 C LEU B 94 0.822 -3.241 16.366 1.00 41.31 C ANISOU 3012 C LEU B 94 4198 5411 6089 110 120 517 C ATOM 3013 O LEU B 94 0.061 -3.845 15.602 1.00 39.41 O ANISOU 3013 O LEU B 94 3948 5156 5869 105 110 517 O ATOM 3014 CB LEU B 94 2.774 -4.842 16.557 1.00 47.86 C ANISOU 3014 CB LEU B 94 5036 6239 6908 110 125 523 C ATOM 3015 CG LEU B 94 3.691 -5.763 17.398 1.00 39.18 C ANISOU 3015 CG LEU B 94 3941 5143 5805 112 135 535 C ATOM 3016 CD1 LEU B 94 4.457 -6.758 16.530 1.00 20.44 C ANISOU 3016 CD1 LEU B 94 1571 2761 3435 109 127 529 C ATOM 3017 CD2 LEU B 94 4.660 -4.944 18.250 1.00 43.87 C ANISOU 3017 CD2 LEU B 94 4545 5752 6370 117 147 534 C ATOM 3018 N VAL B 95 0.899 -1.903 16.416 1.00 37.71 N ANISOU 3018 N VAL B 95 3747 4966 5614 113 121 508 N ATOM 3019 CA VAL B 95 0.160 -1.010 15.518 1.00 33.26 C ANISOU 3019 CA VAL B 95 3181 4402 5053 111 110 495 C ATOM 3020 C VAL B 95 1.139 -0.293 14.592 1.00 32.53 C ANISOU 3020 C VAL B 95 3102 4317 4941 112 102 476 C ATOM 3021 O VAL B 95 2.081 0.369 15.050 1.00 37.12 O ANISOU 3021 O VAL B 95 3694 4912 5499 116 109 472 O ATOM 3022 CB VAL B 95 -0.700 0.010 16.291 1.00 34.20 C ANISOU 3022 CB VAL B 95 3296 4528 5170 114 117 499 C ATOM 3023 CG1 VAL B 95 -1.167 1.152 15.358 1.00 29.95 C ANISOU 3023 CG1 VAL B 95 2760 3992 4628 114 106 483 C ATOM 3024 CG2 VAL B 95 -1.891 -0.683 16.915 1.00 27.49 C ANISOU 3024 CG2 VAL B 95 2432 3668 4344 112 121 516 C ATOM 3025 N SER B 96 0.878 -0.375 13.293 1.00 29.03 N ANISOU 3025 N SER B 96 2658 3865 4507 109 87 464 N ATOM 3026 CA SER B 96 1.766 0.174 12.283 1.00 35.80 C ANISOU 3026 CA SER B 96 3526 4727 5348 109 78 446 C ATOM 3027 C SER B 96 0.998 1.018 11.279 1.00 31.43 C ANISOU 3027 C SER B 96 2971 4171 4798 108 66 433 C ATOM 3028 O SER B 96 -0.124 0.682 10.887 1.00 32.99 O ANISOU 3028 O SER B 96 3159 4357 5018 105 59 436 O ATOM 3029 CB SER B 96 2.499 -0.954 11.543 1.00 38.56 C ANISOU 3029 CB SER B 96 3880 5069 5704 107 71 443 C ATOM 3030 OG SER B 96 3.177 -0.450 10.419 1.00 39.17 O ANISOU 3030 OG SER B 96 3967 5149 5768 106 60 425 O ATOM 3031 N GLU B 97 1.625 2.103 10.839 1.00 32.95 N ANISOU 3031 N GLU B 97 3174 4374 4969 110 63 418 N ATOM 3032 CA GLU B 97 1.032 2.890 9.771 1.00 42.81 C ANISOU 3032 CA GLU B 97 4424 5622 6221 109 50 404 C ATOM 3033 C GLU B 97 0.724 2.023 8.547 1.00 42.03 C ANISOU 3033 C GLU B 97 4321 5507 6141 104 35 400 C ATOM 3034 O GLU B 97 -0.232 2.298 7.814 1.00 40.08 O ANISOU 3034 O GLU B 97 4068 5253 5906 102 25 395 O ATOM 3035 CB GLU B 97 1.965 4.045 9.411 1.00 42.44 C ANISOU 3035 CB GLU B 97 4390 5588 6147 113 48 388 C ATOM 3036 CG GLU B 97 1.253 5.279 8.881 1.00 55.06 C ANISOU 3036 CG GLU B 97 5988 7190 7742 113 41 377 C ATOM 3037 CD GLU B 97 1.360 5.434 7.383 1.00 59.78 C ANISOU 3037 CD GLU B 97 6590 7783 8341 111 25 361 C ATOM 3038 OE1 GLU B 97 1.947 4.546 6.728 1.00 61.29 O ANISOU 3038 OE1 GLU B 97 6784 7967 8535 109 18 358 O ATOM 3039 OE2 GLU B 97 0.853 6.450 6.864 1.00 59.96 O ANISOU 3039 OE2 GLU B 97 6614 7809 8360 112 18 351 O ATOM 3040 N GLU B 98 1.484 0.941 8.351 1.00 41.02 N ANISOU 3040 N GLU B 98 4196 5374 6016 103 34 402 N ATOM 3041 CA GLU B 98 1.384 0.087 7.173 1.00 46.76 C ANISOU 3041 CA GLU B 98 4921 6087 6758 98 20 397 C ATOM 3042 C GLU B 98 0.299 -0.974 7.265 1.00 47.03 C ANISOU 3042 C GLU B 98 4942 6105 6822 94 18 411 C ATOM 3043 O GLU B 98 0.145 -1.728 6.303 1.00 44.98 O ANISOU 3043 O GLU B 98 4681 5833 6578 90 6 407 O ATOM 3044 CB GLU B 98 2.717 -0.617 6.899 1.00 49.74 C ANISOU 3044 CB GLU B 98 5308 6466 7126 98 20 393 C ATOM 3045 CG GLU B 98 3.859 0.340 6.696 1.00 54.02 C ANISOU 3045 CG GLU B 98 5863 7023 7640 102 20 379 C ATOM 3046 CD GLU B 98 3.579 1.299 5.565 1.00 65.89 C ANISOU 3046 CD GLU B 98 7371 8527 9138 102 7 363 C ATOM 3047 OE1 GLU B 98 3.144 0.836 4.487 1.00 69.77 O ANISOU 3047 OE1 GLU B 98 7859 9005 9644 98 -6 358 O ATOM 3048 OE2 GLU B 98 3.765 2.518 5.766 1.00 68.14 O ANISOU 3048 OE2 GLU B 98 7662 8825 9405 105 10 355 O ATOM 3049 N ASP B 99 -0.377 -1.122 8.408 1.00 52.26 N ANISOU 3049 N ASP B 99 5596 6768 7493 95 30 426 N ATOM 3050 CA ASP B 99 -1.300 -2.229 8.661 1.00 48.00 C ANISOU 3050 CA ASP B 99 5044 6214 6981 91 30 441 C ATOM 3051 C ASP B 99 -2.693 -1.728 9.037 1.00 51.30 C ANISOU 3051 C ASP B 99 5451 6629 7412 91 31 447 C ATOM 3052 O ASP B 99 -2.837 -0.838 9.887 1.00 46.35 O ANISOU 3052 O ASP B 99 4824 6013 6772 95 41 450 O ATOM 3053 CB ASP B 99 -0.745 -3.126 9.763 1.00 42.25 C ANISOU 3053 CB ASP B 99 4314 5487 6252 92 43 456 C ATOM 3054 CG ASP B 99 0.455 -3.925 9.306 1.00 50.65 C ANISOU 3054 CG ASP B 99 5386 6549 7309 92 40 451 C ATOM 3055 OD1 ASP B 99 0.290 -4.892 8.529 1.00 53.37 O ANISOU 3055 OD1 ASP B 99 5728 6880 7672 87 30 451 O ATOM 3056 OD2 ASP B 99 1.581 -3.546 9.688 1.00 54.09 O ANISOU 3056 OD2 ASP B 99 5832 6998 7722 95 47 447 O ATOM 3057 N LYS B 100 -3.716 -2.306 8.400 1.00 57.86 N ANISOU 3057 N LYS B 100 6272 7443 8267 86 21 450 N ATOM 3058 CA LYS B 100 -5.093 -1.863 8.617 1.00 55.21 C ANISOU 3058 CA LYS B 100 5927 7105 7947 86 21 455 C ATOM 3059 C LYS B 100 -5.568 -2.160 10.034 1.00 49.24 C ANISOU 3059 C LYS B 100 5162 6350 7196 87 36 473 C ATOM 3060 O LYS B 100 -6.213 -1.314 10.661 1.00 54.61 O ANISOU 3060 O LYS B 100 5839 7038 7874 89 42 476 O ATOM 3061 CB LYS B 100 -6.013 -2.527 7.593 1.00 62.35 C ANISOU 3061 CB LYS B 100 6823 7990 8876 80 7 454 C ATOM 3062 CG LYS B 100 -7.481 -2.172 7.718 1.00 74.73 C ANISOU 3062 CG LYS B 100 8380 9552 10461 79 5 459 C ATOM 3063 CD LYS B 100 -8.316 -2.970 6.716 1.00 81.51 C ANISOU 3063 CD LYS B 100 9232 10392 11347 73 -9 458 C ATOM 3064 CE LYS B 100 -9.804 -2.678 6.852 1.00 84.19 C ANISOU 3064 CE LYS B 100 9560 10724 11705 72 -10 464 C ATOM 3065 NZ LYS B 100 -10.618 -3.606 6.018 1.00 85.94 N ANISOU 3065 NZ LYS B 100 9773 10925 11953 66 -23 466 N ATOM 3066 N HIS B 101 -5.275 -3.360 10.546 1.00 42.92 N ANISOU 3066 N HIS B 101 4358 5544 6405 86 42 485 N ATOM 3067 CA HIS B 101 -5.629 -3.804 11.891 1.00 46.26 C ANISOU 3067 CA HIS B 101 4774 5968 6835 87 56 503 C ATOM 3068 C HIS B 101 -4.380 -4.071 12.726 1.00 49.95 C ANISOU 3068 C HIS B 101 5249 6445 7284 91 68 508 C ATOM 3069 O HIS B 101 -3.295 -4.335 12.199 1.00 47.91 O ANISOU 3069 O HIS B 101 5001 6190 7015 91 65 500 O ATOM 3070 CB HIS B 101 -6.467 -5.094 11.876 1.00 54.52 C ANISOU 3070 CB HIS B 101 5808 6997 7911 83 54 516 C ATOM 3071 CG HIS B 101 -7.772 -4.976 11.157 1.00 69.74 C ANISOU 3071 CG HIS B 101 7727 8913 9860 79 43 514 C ATOM 3072 ND1 HIS B 101 -8.886 -4.400 11.730 1.00 72.68 N ANISOU 3072 ND1 HIS B 101 8090 9286 10239 80 47 520 N ATOM 3073 CD2 HIS B 101 -8.141 -5.356 9.911 1.00 71.76 C ANISOU 3073 CD2 HIS B 101 7981 9154 10130 75 27 506 C ATOM 3074 CE1 HIS B 101 -9.887 -4.437 10.870 1.00 73.07 C ANISOU 3074 CE1 HIS B 101 8133 9323 10307 76 35 516 C ATOM 3075 NE2 HIS B 101 -9.461 -5.011 9.758 1.00 73.89 N ANISOU 3075 NE2 HIS B 101 8241 9417 10415 73 23 508 N ATOM 3076 N ALA B 102 -4.554 -4.033 14.044 1.00 45.43 N ANISOU 3076 N ALA B 102 4673 5880 6709 94 83 522 N ATOM 3077 CA ALA B 102 -3.464 -4.389 14.937 1.00 43.61 C ANISOU 3077 CA ALA B 102 4449 5658 6464 97 95 529 C ATOM 3078 C ALA B 102 -3.037 -5.842 14.722 1.00 54.06 C ANISOU 3078 C ALA B 102 5771 6970 7800 94 93 536 C ATOM 3079 O ALA B 102 -3.852 -6.718 14.426 1.00 61.07 O ANISOU 3079 O ALA B 102 6649 7843 8713 90 87 543 O ATOM 3080 CB ALA B 102 -3.876 -4.170 16.392 1.00 31.21 C ANISOU 3080 CB ALA B 102 2874 4095 4891 100 110 545 C ATOM 3081 N ILE B 103 -1.737 -6.089 14.874 1.00 49.17 N ANISOU 3081 N ILE B 103 5162 6358 7164 96 97 534 N ATOM 3082 CA ILE B 103 -1.148 -7.420 14.770 1.00 41.57 C ANISOU 3082 CA ILE B 103 4198 5386 6209 94 96 540 C ATOM 3083 C ILE B 103 -1.028 -7.996 16.176 1.00 40.53 C ANISOU 3083 C ILE B 103 4063 5257 6078 96 112 558 C ATOM 3084 O ILE B 103 -0.502 -7.332 17.080 1.00 37.37 O ANISOU 3084 O ILE B 103 3668 4871 5658 101 123 561 O ATOM 3085 CB ILE B 103 0.226 -7.357 14.079 1.00 44.29 C ANISOU 3085 CB ILE B 103 4556 5736 6535 94 91 526 C ATOM 3086 CG1 ILE B 103 0.073 -6.935 12.613 1.00 40.79 C ANISOU 3086 CG1 ILE B 103 4116 5288 6094 92 75 508 C ATOM 3087 CG2 ILE B 103 0.966 -8.697 14.189 1.00 38.68 C ANISOU 3087 CG2 ILE B 103 3846 5019 5830 93 94 534 C ATOM 3088 CD1 ILE B 103 -0.706 -7.905 11.824 1.00 37.17 C ANISOU 3088 CD1 ILE B 103 3648 4812 5663 86 64 511 C ATOM 3089 N ILE B 104 -1.520 -9.217 16.372 1.00 39.76 N ANISOU 3089 N ILE B 104 3956 5147 6004 93 112 571 N ATOM 3090 CA ILE B 104 -1.469 -9.881 17.673 1.00 46.08 C ANISOU 3090 CA ILE B 104 4752 5948 6806 95 126 590 C ATOM 3091 C ILE B 104 -0.359 -10.926 17.645 1.00 52.65 C ANISOU 3091 C ILE B 104 5590 6779 7636 95 128 592 C ATOM 3092 O ILE B 104 -0.389 -11.856 16.826 1.00 48.88 O ANISOU 3092 O ILE B 104 5109 6288 7174 91 118 590 O ATOM 3093 CB ILE B 104 -2.817 -10.525 18.033 1.00 47.56 C ANISOU 3093 CB ILE B 104 4925 6123 7021 93 127 604 C ATOM 3094 CG1 ILE B 104 -3.950 -9.524 17.830 1.00 51.83 C ANISOU 3094 CG1 ILE B 104 5461 6666 7568 92 123 599 C ATOM 3095 CG2 ILE B 104 -2.798 -11.022 19.482 1.00 36.04 C ANISOU 3095 CG2 ILE B 104 3462 4669 5563 96 143 623 C ATOM 3096 CD1 ILE B 104 -3.812 -8.280 18.673 1.00 58.05 C ANISOU 3096 CD1 ILE B 104 6253 7469 8333 97 133 599 C ATOM 3097 N VAL B 105 0.624 -10.777 18.538 1.00 49.44 N ANISOU 3097 N VAL B 105 5191 6385 7209 99 139 597 N ATOM 3098 CA VAL B 105 1.761 -11.692 18.569 1.00 48.18 C ANISOU 3098 CA VAL B 105 5038 6224 7044 100 142 599 C ATOM 3099 C VAL B 105 1.284 -13.086 18.980 1.00 57.54 C ANISOU 3099 C VAL B 105 6213 7397 8254 97 144 615 C ATOM 3100 O VAL B 105 0.420 -13.235 19.860 1.00 59.67 O ANISOU 3100 O VAL B 105 6474 7664 8535 98 152 630 O ATOM 3101 CB VAL B 105 2.838 -11.135 19.519 1.00 37.55 C ANISOU 3101 CB VAL B 105 3702 4895 5671 105 154 600 C ATOM 3102 CG1 VAL B 105 4.006 -12.068 19.630 1.00 32.01 C ANISOU 3102 CG1 VAL B 105 3007 4193 4963 106 157 603 C ATOM 3103 CG2 VAL B 105 3.296 -9.777 19.038 1.00 33.72 C ANISOU 3103 CG2 VAL B 105 3227 4421 5163 107 150 583 C ATOM 3104 N GLU B 106 1.822 -14.119 18.328 1.00 54.32 N ANISOU 3104 N GLU B 106 5807 6979 7854 94 138 614 N ATOM 3105 CA GLU B 106 1.377 -15.483 18.603 1.00 56.46 C ANISOU 3105 CA GLU B 106 6068 7237 8149 91 139 628 C ATOM 3106 C GLU B 106 1.763 -15.932 20.019 1.00 58.81 C ANISOU 3106 C GLU B 106 6365 7540 8440 95 155 646 C ATOM 3107 O GLU B 106 2.770 -15.484 20.567 1.00 58.06 O ANISOU 3107 O GLU B 106 6280 7458 8322 99 163 644 O ATOM 3108 CB GLU B 106 1.902 -16.432 17.528 1.00 61.81 C ANISOU 3108 CB GLU B 106 6747 7903 8835 87 128 621 C ATOM 3109 CG GLU B 106 3.394 -16.474 17.337 1.00 78.19 C ANISOU 3109 CG GLU B 106 8834 9985 10888 89 129 613 C ATOM 3110 CD GLU B 106 3.761 -17.297 16.115 1.00 89.51 C ANISOU 3110 CD GLU B 106 10270 11408 12333 85 116 604 C ATOM 3111 OE1 GLU B 106 2.823 -17.755 15.429 1.00 94.26 O ANISOU 3111 OE1 GLU B 106 10862 11995 12956 81 106 604 O ATOM 3112 OE2 GLU B 106 4.967 -17.480 15.833 1.00 91.25 O ANISOU 3112 OE2 GLU B 106 10500 11633 12538 86 115 597 O ATOM 3113 N PRO B 107 0.981 -16.846 20.618 1.00 64.90 N ANISOU 3113 N PRO B 107 7125 8301 9233 94 159 662 N ATOM 3114 CA PRO B 107 1.043 -17.046 22.085 1.00 60.83 C ANISOU 3114 CA PRO B 107 6608 7793 8714 98 175 679 C ATOM 3115 C PRO B 107 2.411 -17.367 22.657 1.00 56.77 C ANISOU 3115 C PRO B 107 6103 7287 8180 101 183 682 C ATOM 3116 O PRO B 107 2.723 -16.903 23.761 1.00 52.68 O ANISOU 3116 O PRO B 107 5588 6781 7646 106 196 690 O ATOM 3117 CB PRO B 107 0.070 -18.211 22.316 1.00 58.29 C ANISOU 3117 CB PRO B 107 6272 7455 8421 94 175 695 C ATOM 3118 CG PRO B 107 -0.867 -18.156 21.169 1.00 60.34 C ANISOU 3118 CG PRO B 107 6525 7703 8699 89 161 686 C ATOM 3119 CD PRO B 107 -0.059 -17.683 19.995 1.00 65.41 C ANISOU 3119 CD PRO B 107 7178 8348 9328 88 150 666 C ATOM 3120 N GLU B 108 3.210 -18.197 21.990 1.00 54.97 N ANISOU 3120 N GLU B 108 5879 7053 7954 99 177 678 N ATOM 3121 CA GLU B 108 4.523 -18.540 22.534 1.00 57.06 C ANISOU 3121 CA GLU B 108 6154 7327 8201 103 185 681 C ATOM 3122 C GLU B 108 5.516 -17.376 22.521 1.00 53.27 C ANISOU 3122 C GLU B 108 5687 6863 7690 107 188 668 C ATOM 3123 O GLU B 108 6.593 -17.497 23.113 1.00 50.57 O ANISOU 3123 O GLU B 108 5353 6529 7331 110 196 671 O ATOM 3124 CB GLU B 108 5.101 -19.744 21.784 1.00 64.06 C ANISOU 3124 CB GLU B 108 7041 8202 9098 99 178 679 C ATOM 3125 CG GLU B 108 4.359 -21.044 22.058 1.00 77.09 C ANISOU 3125 CG GLU B 108 8679 9837 10776 96 179 694 C ATOM 3126 CD GLU B 108 3.123 -21.226 21.207 1.00 88.09 C ANISOU 3126 CD GLU B 108 10061 11215 12194 91 167 691 C ATOM 3127 OE1 GLU B 108 2.812 -20.334 20.387 1.00 91.26 O ANISOU 3127 OE1 GLU B 108 10465 11619 12592 90 158 677 O ATOM 3128 OE2 GLU B 108 2.460 -22.270 21.367 1.00 92.97 O ANISOU 3128 OE2 GLU B 108 10669 11820 12835 88 167 704 O ATOM 3129 N LYS B 109 5.181 -16.244 21.907 1.00 43.16 N ANISOU 3129 N LYS B 109 4409 5587 6402 106 181 654 N ATOM 3130 CA LYS B 109 6.118 -15.136 21.813 1.00 47.72 C ANISOU 3130 CA LYS B 109 4999 6180 6952 110 182 641 C ATOM 3131 C LYS B 109 5.620 -13.893 22.538 1.00 49.90 C ANISOU 3131 C LYS B 109 5275 6467 7216 113 190 642 C ATOM 3132 O LYS B 109 6.240 -12.831 22.421 1.00 56.03 O ANISOU 3132 O LYS B 109 6062 7256 7970 116 190 630 O ATOM 3133 CB LYS B 109 6.374 -14.820 20.336 1.00 53.59 C ANISOU 3133 CB LYS B 109 5748 6920 7693 106 168 621 C ATOM 3134 CG LYS B 109 6.983 -15.978 19.543 1.00 51.91 C ANISOU 3134 CG LYS B 109 5536 6697 7490 103 160 618 C ATOM 3135 CD LYS B 109 7.251 -15.564 18.108 1.00 48.10 C ANISOU 3135 CD LYS B 109 5060 6213 7004 100 145 598 C ATOM 3136 CE LYS B 109 7.870 -16.684 17.280 1.00 58.24 C ANISOU 3136 CE LYS B 109 6346 7487 8297 97 137 594 C ATOM 3137 NZ LYS B 109 9.188 -17.145 17.802 1.00 62.77 N ANISOU 3137 NZ LYS B 109 6928 8068 8855 100 145 598 N ATOM 3138 N ARG B 110 4.545 -14.003 23.317 1.00 46.37 N ANISOU 3138 N ARG B 110 4818 6017 6783 113 196 656 N ATOM 3139 CA ARG B 110 3.899 -12.832 23.892 1.00 46.29 C ANISOU 3139 CA ARG B 110 4807 6016 6766 116 201 657 C ATOM 3140 C ARG B 110 4.674 -12.262 25.066 1.00 41.66 C ANISOU 3140 C ARG B 110 4229 5445 6155 122 214 662 C ATOM 3141 O ARG B 110 5.273 -12.995 25.854 1.00 39.64 O ANISOU 3141 O ARG B 110 3976 5191 5897 124 223 674 O ATOM 3142 CB ARG B 110 2.484 -13.163 24.348 1.00 50.29 C ANISOU 3142 CB ARG B 110 5299 6512 7295 115 203 670 C ATOM 3143 CG ARG B 110 1.503 -13.140 23.230 1.00 55.48 C ANISOU 3143 CG ARG B 110 5949 7159 7972 110 190 662 C ATOM 3144 CD ARG B 110 0.125 -13.501 23.690 1.00 52.26 C ANISOU 3144 CD ARG B 110 5527 6741 7588 108 192 675 C ATOM 3145 NE ARG B 110 -0.650 -13.939 22.542 1.00 51.03 N ANISOU 3145 NE ARG B 110 5364 6571 7455 102 178 669 N ATOM 3146 CZ ARG B 110 -1.884 -14.415 22.624 1.00 58.78 C ANISOU 3146 CZ ARG B 110 6332 7540 8460 99 177 678 C ATOM 3147 NH1 ARG B 110 -2.473 -14.505 23.816 1.00 60.81 N ANISOU 3147 NH1 ARG B 110 6583 7800 8723 102 188 695 N ATOM 3148 NH2 ARG B 110 -2.525 -14.792 21.518 1.00 50.29 N ANISOU 3148 NH2 ARG B 110 5251 6452 7405 94 163 672 N ATOM 3149 N GLY B 111 4.693 -10.933 25.135 1.00 43.57 N ANISOU 3149 N GLY B 111 4476 5698 6379 125 215 653 N ATOM 3150 CA GLY B 111 5.198 -10.172 26.255 1.00 31.33 C ANISOU 3150 CA GLY B 111 2934 4163 4806 131 228 658 C ATOM 3151 C GLY B 111 4.183 -9.119 26.635 1.00 34.20 C ANISOU 3151 C GLY B 111 3293 4532 5171 132 230 659 C ATOM 3152 O GLY B 111 3.043 -9.169 26.162 1.00 39.02 O ANISOU 3152 O GLY B 111 3893 5133 5801 129 224 659 O ATOM 3153 N LYS B 112 4.578 -8.150 27.463 1.00 40.04 N ANISOU 3153 N LYS B 112 4039 5285 5888 137 239 660 N ATOM 3154 CA LYS B 112 3.619 -7.257 28.096 1.00 44.03 C ANISOU 3154 CA LYS B 112 4540 5795 6394 139 244 664 C ATOM 3155 C LYS B 112 3.540 -5.869 27.469 1.00 47.27 C ANISOU 3155 C LYS B 112 4956 6214 6791 139 238 647 C ATOM 3156 O LYS B 112 2.812 -5.028 28.004 1.00 55.23 O ANISOU 3156 O LYS B 112 5961 7227 7797 141 242 650 O ATOM 3157 CB LYS B 112 3.929 -7.103 29.595 1.00 44.03 C ANISOU 3157 CB LYS B 112 4543 5806 6381 145 259 679 C ATOM 3158 CG LYS B 112 5.217 -6.371 29.928 1.00 48.49 C ANISOU 3158 CG LYS B 112 5123 6385 6915 149 264 672 C ATOM 3159 CD LYS B 112 5.606 -6.543 31.397 1.00 55.10 C ANISOU 3159 CD LYS B 112 5963 7231 7743 155 278 689 C ATOM 3160 CE LYS B 112 6.878 -5.765 31.724 1.00 59.86 C ANISOU 3160 CE LYS B 112 6581 7848 8315 159 282 682 C ATOM 3161 NZ LYS B 112 7.519 -6.119 33.025 1.00 52.39 N ANISOU 3161 NZ LYS B 112 5640 6909 7358 164 294 697 N ATOM 3162 N TYR B 113 4.243 -5.592 26.366 1.00 37.74 N ANISOU 3162 N TYR B 113 3757 5007 5574 138 228 630 N ATOM 3163 CA TYR B 113 4.290 -4.230 25.835 1.00 34.91 C ANISOU 3163 CA TYR B 113 3406 4658 5201 139 223 614 C ATOM 3164 C TYR B 113 3.556 -4.070 24.508 1.00 27.31 C ANISOU 3164 C TYR B 113 2437 3686 4252 134 209 601 C ATOM 3165 O TYR B 113 3.450 -5.002 23.708 1.00 31.07 O ANISOU 3165 O TYR B 113 2909 4151 4746 130 201 599 O ATOM 3166 CB TYR B 113 5.725 -3.718 25.670 1.00 37.07 C ANISOU 3166 CB TYR B 113 3694 4942 5447 141 224 603 C ATOM 3167 CG TYR B 113 6.403 -3.383 26.976 1.00 39.99 C ANISOU 3167 CG TYR B 113 4072 5325 5798 147 238 613 C ATOM 3168 CD1 TYR B 113 6.060 -2.221 27.675 1.00 36.30 C ANISOU 3168 CD1 TYR B 113 3607 4868 5319 151 244 613 C ATOM 3169 CD2 TYR B 113 7.408 -4.195 27.498 1.00 37.76 C ANISOU 3169 CD2 TYR B 113 3795 5044 5509 149 244 621 C ATOM 3170 CE1 TYR B 113 6.675 -1.891 28.875 1.00 37.58 C ANISOU 3170 CE1 TYR B 113 3775 5041 5461 156 256 622 C ATOM 3171 CE2 TYR B 113 8.039 -3.866 28.696 1.00 42.65 C ANISOU 3171 CE2 TYR B 113 4421 5674 6108 154 256 630 C ATOM 3172 CZ TYR B 113 7.663 -2.719 29.379 1.00 41.79 C ANISOU 3172 CZ TYR B 113 4315 5576 5989 158 262 631 C ATOM 3173 OH TYR B 113 8.281 -2.394 30.557 1.00 40.35 O ANISOU 3173 OH TYR B 113 4139 5405 5787 163 273 640 O ATOM 3174 N VAL B 114 3.062 -2.849 24.295 1.00 24.53 N ANISOU 3174 N VAL B 114 2087 3341 3894 135 206 591 N ATOM 3175 CA VAL B 114 2.368 -2.423 23.080 1.00 28.61 C ANISOU 3175 CA VAL B 114 2600 3851 4421 131 193 578 C ATOM 3176 C VAL B 114 3.217 -1.369 22.389 1.00 35.65 C ANISOU 3176 C VAL B 114 3503 4752 5290 132 188 559 C ATOM 3177 O VAL B 114 3.719 -0.448 23.047 1.00 43.55 O ANISOU 3177 O VAL B 114 4512 5766 6269 137 195 557 O ATOM 3178 CB VAL B 114 0.981 -1.847 23.422 1.00 35.02 C ANISOU 3178 CB VAL B 114 3401 4661 5245 131 194 583 C ATOM 3179 CG1 VAL B 114 0.175 -1.486 22.160 1.00 31.47 C ANISOU 3179 CG1 VAL B 114 2946 4204 4808 127 180 569 C ATOM 3180 CG2 VAL B 114 0.233 -2.806 24.328 1.00 38.78 C ANISOU 3180 CG2 VAL B 114 3865 5130 5740 131 202 603 C ATOM 3181 N VAL B 115 3.381 -1.496 21.070 1.00 29.30 N ANISOU 3181 N VAL B 115 2701 3941 4490 129 175 545 N ATOM 3182 CA VAL B 115 4.193 -0.559 20.303 1.00 23.88 C ANISOU 3182 CA VAL B 115 2026 3263 3783 130 168 526 C ATOM 3183 C VAL B 115 3.372 -0.031 19.134 1.00 31.01 C ANISOU 3183 C VAL B 115 2926 4161 4697 127 155 513 C ATOM 3184 O VAL B 115 2.817 -0.811 18.353 1.00 35.18 O ANISOU 3184 O VAL B 115 3446 4676 5245 123 145 512 O ATOM 3185 CB VAL B 115 5.513 -1.177 19.784 1.00 23.34 C ANISOU 3185 CB VAL B 115 1968 3195 3705 130 165 519 C ATOM 3186 CG1 VAL B 115 6.424 -0.055 19.283 1.00 21.20 C ANISOU 3186 CG1 VAL B 115 1710 2936 3409 132 162 502 C ATOM 3187 CG2 VAL B 115 6.239 -1.986 20.850 1.00 14.04 C ANISOU 3187 CG2 VAL B 115 793 2021 2523 132 177 534 C ATOM 3188 N CYS B 116 3.311 1.291 19.006 1.00 33.60 N ANISOU 3188 N CYS B 116 3258 4498 5009 129 154 502 N ATOM 3189 CA CYS B 116 2.744 1.957 17.843 1.00 28.03 C ANISOU 3189 CA CYS B 116 2552 3790 4309 127 141 487 C ATOM 3190 C CYS B 116 3.890 2.543 17.029 1.00 22.77 C ANISOU 3190 C CYS B 116 1898 3130 3621 128 134 469 C ATOM 3191 O CYS B 116 4.762 3.211 17.587 1.00 23.29 O ANISOU 3191 O CYS B 116 1975 3209 3665 132 142 467 O ATOM 3192 CB CYS B 116 1.767 3.057 18.267 1.00 34.90 C ANISOU 3192 CB CYS B 116 3417 4665 5178 129 144 487 C ATOM 3193 SG CYS B 116 0.461 2.501 19.403 1.00 33.93 S ANISOU 3193 SG CYS B 116 3280 4536 5077 128 153 509 S ATOM 3194 N PHE B 117 3.931 2.269 15.724 1.00 28.53 N ANISOU 3194 N PHE B 117 2629 3852 4358 124 121 457 N ATOM 3195 CA PHE B 117 5.077 2.793 14.988 1.00 23.19 C ANISOU 3195 CA PHE B 117 1965 3183 3662 126 115 440 C ATOM 3196 C PHE B 117 4.700 3.171 13.565 1.00 26.15 C ANISOU 3196 C PHE B 117 2341 3553 4043 123 99 424 C ATOM 3197 O PHE B 117 3.743 2.646 12.992 1.00 37.05 O ANISOU 3197 O PHE B 117 3711 4921 5445 119 91 426 O ATOM 3198 CB PHE B 117 6.281 1.812 14.977 1.00 16.27 C ANISOU 3198 CB PHE B 117 1095 2306 2780 125 117 442 C ATOM 3199 CG PHE B 117 6.017 0.468 14.314 1.00 26.38 C ANISOU 3199 CG PHE B 117 2369 3572 4083 121 109 446 C ATOM 3200 CD1 PHE B 117 6.258 0.286 12.960 1.00 29.68 C ANISOU 3200 CD1 PHE B 117 2790 3984 4504 118 95 432 C ATOM 3201 CD2 PHE B 117 5.587 -0.624 15.052 1.00 35.00 C ANISOU 3201 CD2 PHE B 117 3452 4656 5192 120 116 464 C ATOM 3202 CE1 PHE B 117 6.053 -0.952 12.351 1.00 29.59 C ANISOU 3202 CE1 PHE B 117 2772 3958 4512 114 87 436 C ATOM 3203 CE2 PHE B 117 5.375 -1.866 14.443 1.00 37.81 C ANISOU 3203 CE2 PHE B 117 3801 4997 5567 115 108 467 C ATOM 3204 CZ PHE B 117 5.608 -2.026 13.090 1.00 34.00 C ANISOU 3204 CZ PHE B 117 3322 4508 5089 112 94 453 C ATOM 3205 N ASP B 118 5.475 4.112 13.017 1.00 27.62 N ANISOU 3205 N ASP B 118 2538 3749 4208 125 95 408 N ATOM 3206 CA ASP B 118 5.523 4.469 11.601 1.00 31.15 C ANISOU 3206 CA ASP B 118 2989 4193 4655 123 80 391 C ATOM 3207 C ASP B 118 6.907 4.070 11.089 1.00 36.27 C ANISOU 3207 C ASP B 118 3647 4843 5289 123 77 382 C ATOM 3208 O ASP B 118 7.903 4.751 11.393 1.00 32.46 O ANISOU 3208 O ASP B 118 3177 4373 4785 127 83 376 O ATOM 3209 CB ASP B 118 5.276 5.977 11.420 1.00 32.62 C ANISOU 3209 CB ASP B 118 3179 4388 4827 125 78 379 C ATOM 3210 CG ASP B 118 5.110 6.404 9.947 1.00 43.47 C ANISOU 3210 CG ASP B 118 4555 5758 6203 124 62 361 C ATOM 3211 OD1 ASP B 118 5.497 5.648 9.038 1.00 49.46 O ANISOU 3211 OD1 ASP B 118 5316 6510 6968 121 52 356 O ATOM 3212 OD2 ASP B 118 4.639 7.537 9.697 1.00 47.92 O ANISOU 3212 OD2 ASP B 118 5120 6328 6761 125 58 353 O ATOM 3213 N PRO B 119 7.036 2.965 10.346 1.00 34.78 N ANISOU 3213 N PRO B 119 3456 4643 5114 120 69 382 N ATOM 3214 CA PRO B 119 8.385 2.457 10.031 1.00 32.57 C ANISOU 3214 CA PRO B 119 3187 4366 4823 120 68 376 C ATOM 3215 C PRO B 119 9.171 3.317 9.052 1.00 22.74 C ANISOU 3215 C PRO B 119 1953 3127 3558 121 59 356 C ATOM 3216 O PRO B 119 10.406 3.285 9.084 1.00 28.75 O ANISOU 3216 O PRO B 119 2725 3896 4303 123 62 351 O ATOM 3217 CB PRO B 119 8.123 1.040 9.489 1.00 29.08 C ANISOU 3217 CB PRO B 119 2737 3909 4403 116 61 382 C ATOM 3218 CG PRO B 119 6.705 1.066 9.027 1.00 33.16 C ANISOU 3218 CG PRO B 119 3243 4415 4941 113 53 384 C ATOM 3219 CD PRO B 119 5.974 2.038 9.918 1.00 33.75 C ANISOU 3219 CD PRO B 119 3315 4498 5012 115 62 389 C ATOM 3220 N LEU B 120 8.526 4.033 8.143 1.00 31.56 N ANISOU 3220 N LEU B 120 3069 4243 4679 120 48 345 N ATOM 3221 CA LEU B 120 9.332 4.888 7.262 1.00 32.98 C ANISOU 3221 CA LEU B 120 3260 4430 4839 122 40 326 C ATOM 3222 C LEU B 120 8.485 6.120 6.912 1.00 39.94 C ANISOU 3222 C LEU B 120 4141 5316 5720 123 35 318 C ATOM 3223 O LEU B 120 7.919 6.231 5.828 1.00 44.00 O ANISOU 3223 O LEU B 120 4652 5823 6242 121 22 309 O ATOM 3224 CB LEU B 120 9.818 4.150 6.013 1.00 17.00 C ANISOU 3224 CB LEU B 120 1240 2398 2820 119 27 317 C ATOM 3225 CG LEU B 120 11.025 4.844 5.378 1.00 26.41 C ANISOU 3225 CG LEU B 120 2445 3600 3989 122 23 300 C ATOM 3226 CD1 LEU B 120 12.186 4.928 6.392 1.00 21.99 C ANISOU 3226 CD1 LEU B 120 1894 3051 3410 125 37 304 C ATOM 3227 CD2 LEU B 120 11.476 4.171 4.087 1.00 29.99 C ANISOU 3227 CD2 LEU B 120 2903 4046 4447 119 9 290 C ATOM 3228 N ASP B 121 8.433 7.068 7.851 1.00 47.55 N ANISOU 3228 N ASP B 121 5106 6290 6671 126 46 320 N ATOM 3229 CA ASP B 121 7.652 8.286 7.668 1.00 51.51 C ANISOU 3229 CA ASP B 121 5606 6796 7170 127 42 313 C ATOM 3230 C ASP B 121 8.255 9.197 6.613 1.00 44.30 C ANISOU 3230 C ASP B 121 4704 5888 6240 129 32 293 C ATOM 3231 O ASP B 121 9.473 9.363 6.522 1.00 39.15 O ANISOU 3231 O ASP B 121 4062 5243 5569 131 34 285 O ATOM 3232 CB ASP B 121 7.533 9.069 8.974 1.00 64.24 C ANISOU 3232 CB ASP B 121 7219 8418 8771 131 57 321 C ATOM 3233 CG ASP B 121 6.709 10.352 8.809 1.00 69.12 C ANISOU 3233 CG ASP B 121 7835 9040 9386 132 53 314 C ATOM 3234 OD1 ASP B 121 5.469 10.254 8.692 1.00 70.54 O ANISOU 3234 OD1 ASP B 121 8005 9213 9585 130 50 319 O ATOM 3235 OD2 ASP B 121 7.311 11.454 8.778 1.00 68.49 O ANISOU 3235 OD2 ASP B 121 7765 8971 9286 135 55 303 O ATOM 3236 N GLY B 122 7.386 9.779 5.802 1.00 50.58 N ANISOU 3236 N GLY B 122 5496 6681 7043 128 21 285 N ATOM 3237 CA GLY B 122 7.837 10.670 4.762 1.00 45.50 C ANISOU 3237 CA GLY B 122 4862 6043 6385 129 11 267 C ATOM 3238 C GLY B 122 8.285 9.991 3.499 1.00 39.37 C ANISOU 3238 C GLY B 122 4088 5258 5612 126 -2 258 C ATOM 3239 O GLY B 122 8.761 10.684 2.593 1.00 40.97 O ANISOU 3239 O GLY B 122 4299 5465 5801 127 -11 242 O ATOM 3240 N SER B 123 8.105 8.665 3.395 1.00 43.02 N ANISOU 3240 N SER B 123 4545 5710 6093 123 -4 267 N ATOM 3241 CA SER B 123 8.654 7.857 2.305 1.00 40.82 C ANISOU 3241 CA SER B 123 4269 5423 5818 120 -16 260 C ATOM 3242 C SER B 123 7.966 8.100 0.966 1.00 41.97 C ANISOU 3242 C SER B 123 4414 5561 5972 118 -32 250 C ATOM 3243 O SER B 123 8.493 7.669 -0.064 1.00 43.42 O ANISOU 3243 O SER B 123 4602 5740 6155 116 -43 242 O ATOM 3244 CB SER B 123 8.576 6.364 2.663 1.00 49.65 C ANISOU 3244 CB SER B 123 5381 6531 6955 117 -12 275 C ATOM 3245 OG SER B 123 7.237 5.916 2.875 1.00 54.28 O ANISOU 3245 OG SER B 123 5953 7105 7564 114 -13 287 O ATOM 3246 N SER B 124 6.825 8.792 0.949 1.00 41.69 N ANISOU 3246 N SER B 124 4371 5524 5944 118 -35 251 N ATOM 3247 CA SER B 124 6.148 9.077 -0.314 1.00 53.27 C ANISOU 3247 CA SER B 124 5837 6983 7419 115 -51 241 C ATOM 3248 C SER B 124 6.970 10.011 -1.199 1.00 54.67 C ANISOU 3248 C SER B 124 6027 7170 7575 118 -58 223 C ATOM 3249 O SER B 124 6.860 9.948 -2.430 1.00 46.13 O ANISOU 3249 O SER B 124 4948 6081 6497 116 -73 214 O ATOM 3250 CB SER B 124 4.757 9.666 -0.050 1.00 56.54 C ANISOU 3250 CB SER B 124 6242 7395 7846 115 -51 246 C ATOM 3251 OG SER B 124 4.819 10.918 0.620 1.00 60.88 O ANISOU 3251 OG SER B 124 6795 7958 8378 119 -42 243 O ATOM 3252 N ASN B 125 7.778 10.887 -0.592 1.00 58.82 N ANISOU 3252 N ASN B 125 6561 7710 8078 122 -49 218 N ATOM 3253 CA ASN B 125 8.668 11.796 -1.305 1.00 67.11 C ANISOU 3253 CA ASN B 125 7624 8770 9106 125 -55 201 C ATOM 3254 C ASN B 125 10.119 11.316 -1.312 1.00 65.76 C ANISOU 3254 C ASN B 125 7462 8603 8920 126 -52 196 C ATOM 3255 O ASN B 125 11.032 12.135 -1.467 1.00 63.78 O ANISOU 3255 O ASN B 125 7222 8364 8649 130 -52 184 O ATOM 3256 CB ASN B 125 8.616 13.204 -0.701 1.00 77.25 C ANISOU 3256 CB ASN B 125 8911 10067 10374 129 -48 195 C ATOM 3257 CG ASN B 125 7.240 13.825 -0.757 1.00 78.81 C ANISOU 3257 CG ASN B 125 9100 10261 10583 128 -52 198 C ATOM 3258 OD1 ASN B 125 6.673 14.184 0.276 1.00 83.60 O ANISOU 3258 OD1 ASN B 125 9701 10872 11193 130 -41 206 O ATOM 3259 ND2 ASN B 125 6.695 13.963 -1.962 1.00 72.61 N ANISOU 3259 ND2 ASN B 125 8314 9469 9804 126 -66 190 N ATOM 3260 N ILE B 126 10.359 10.015 -1.129 1.00 60.45 N ANISOU 3260 N ILE B 126 6786 7923 8259 124 -50 206 N ATOM 3261 CA ILE B 126 11.736 9.532 -1.100 1.00 53.20 C ANISOU 3261 CA ILE B 126 5877 7009 7328 125 -47 203 C ATOM 3262 C ILE B 126 12.401 9.574 -2.474 1.00 47.90 C ANISOU 3262 C ILE B 126 5214 6337 6648 124 -61 188 C ATOM 3263 O ILE B 126 13.625 9.428 -2.561 1.00 39.93 O ANISOU 3263 O ILE B 126 4214 5333 5624 126 -59 181 O ATOM 3264 CB ILE B 126 11.770 8.122 -0.471 1.00 49.48 C ANISOU 3264 CB ILE B 126 5399 6529 6872 122 -40 218 C ATOM 3265 CG1 ILE B 126 13.153 7.827 0.118 1.00 49.82 C ANISOU 3265 CG1 ILE B 126 5450 6580 6899 125 -31 218 C ATOM 3266 CG2 ILE B 126 11.382 7.071 -1.486 1.00 56.04 C ANISOU 3266 CG2 ILE B 126 6226 7346 7722 118 -53 219 C ATOM 3267 CD1 ILE B 126 13.282 6.439 0.710 1.00 47.15 C ANISOU 3267 CD1 ILE B 126 5107 6235 6575 122 -24 233 C ATOM 3268 N ASP B 127 11.631 9.807 -3.548 1.00 48.47 N ANISOU 3268 N ASP B 127 5285 6403 6730 122 -75 182 N ATOM 3269 CA ASP B 127 12.215 9.964 -4.878 1.00 42.53 C ANISOU 3269 CA ASP B 127 4542 5650 5968 122 -88 167 C ATOM 3270 C ASP B 127 13.157 11.164 -4.964 1.00 40.13 C ANISOU 3270 C ASP B 127 4249 5361 5636 127 -87 153 C ATOM 3271 O ASP B 127 14.087 11.159 -5.785 1.00 41.74 O ANISOU 3271 O ASP B 127 4464 5568 5828 127 -94 142 O ATOM 3272 CB ASP B 127 11.115 10.103 -5.927 1.00 53.04 C ANISOU 3272 CB ASP B 127 5868 6970 7313 119 -103 165 C ATOM 3273 CG ASP B 127 10.158 8.949 -5.912 1.00 65.80 C ANISOU 3273 CG ASP B 127 7473 8570 8957 114 -105 178 C ATOM 3274 OD1 ASP B 127 10.609 7.798 -6.120 1.00 65.68 O ANISOU 3274 OD1 ASP B 127 7458 8547 8951 111 -107 182 O ATOM 3275 OD2 ASP B 127 8.948 9.200 -5.725 1.00 72.36 O ANISOU 3275 OD2 ASP B 127 8295 9396 9802 112 -106 184 O ATOM 3276 N CYS B 128 12.946 12.202 -4.146 1.00 27.73 N ANISOU 3276 N CYS B 128 2680 3801 4057 130 -78 152 N ATOM 3277 CA CYS B 128 13.857 13.341 -4.147 1.00 33.45 C ANISOU 3277 CA CYS B 128 3415 4539 4756 134 -75 139 C ATOM 3278 C CYS B 128 14.878 13.286 -3.011 1.00 43.23 C ANISOU 3278 C CYS B 128 4658 5784 5982 137 -61 142 C ATOM 3279 O CYS B 128 15.562 14.287 -2.766 1.00 44.27 O ANISOU 3279 O CYS B 128 4798 5926 6095 140 -56 132 O ATOM 3280 CB CYS B 128 13.093 14.674 -4.108 1.00 36.78 C ANISOU 3280 CB CYS B 128 3836 4966 5174 136 -76 133 C ATOM 3281 SG CYS B 128 12.263 15.124 -2.588 1.00 41.93 S ANISOU 3281 SG CYS B 128 4479 5621 5831 137 -61 146 S ATOM 3282 N LEU B 129 14.994 12.145 -2.312 1.00 37.67 N ANISOU 3282 N LEU B 129 3949 5075 5290 135 -53 155 N ATOM 3283 CA LEU B 129 16.006 11.932 -1.277 1.00 24.03 C ANISOU 3283 CA LEU B 129 2226 3353 3551 137 -39 160 C ATOM 3284 C LEU B 129 15.839 12.885 -0.101 1.00 21.56 C ANISOU 3284 C LEU B 129 1914 3049 3231 139 -26 164 C ATOM 3285 O LEU B 129 16.811 13.201 0.577 1.00 24.79 O ANISOU 3285 O LEU B 129 2330 3464 3624 142 -16 163 O ATOM 3286 CB LEU B 129 17.434 12.034 -1.854 1.00 25.30 C ANISOU 3286 CB LEU B 129 2401 3520 3694 139 -42 147 C ATOM 3287 CG LEU B 129 17.745 11.093 -3.033 1.00 24.48 C ANISOU 3287 CG LEU B 129 2297 3408 3595 136 -55 142 C ATOM 3288 CD1 LEU B 129 19.158 11.216 -3.587 1.00 16.87 C ANISOU 3288 CD1 LEU B 129 1346 2450 2612 138 -59 128 C ATOM 3289 CD2 LEU B 129 17.525 9.650 -2.574 1.00 35.26 C ANISOU 3289 CD2 LEU B 129 3654 4764 4978 133 -51 158 C ATOM 3290 N VAL B 130 14.625 13.397 0.116 1.00 30.54 N ANISOU 3290 N VAL B 130 3042 4184 4377 139 -26 169 N ATOM 3291 CA VAL B 130 14.311 14.094 1.362 1.00 38.40 C ANISOU 3291 CA VAL B 130 4035 5185 5369 141 -12 177 C ATOM 3292 C VAL B 130 14.576 13.168 2.558 1.00 45.47 C ANISOU 3292 C VAL B 130 4928 6080 6270 140 1 194 C ATOM 3293 O VAL B 130 14.598 11.933 2.438 1.00 42.09 O ANISOU 3293 O VAL B 130 4495 5644 5854 138 0 202 O ATOM 3294 CB VAL B 130 12.853 14.584 1.349 1.00 34.25 C ANISOU 3294 CB VAL B 130 3500 4657 4856 140 -16 181 C ATOM 3295 CG1 VAL B 130 11.910 13.407 1.370 1.00 35.40 C ANISOU 3295 CG1 VAL B 130 3634 4792 5027 137 -18 194 C ATOM 3296 CG2 VAL B 130 12.575 15.502 2.535 1.00 32.42 C ANISOU 3296 CG2 VAL B 130 3267 4432 4617 143 -3 186 C ATOM 3297 N SER B 131 14.813 13.783 3.718 1.00 43.19 N ANISOU 3297 N SER B 131 4642 5799 5970 143 15 200 N ATOM 3298 CA SER B 131 14.932 13.045 4.975 1.00 31.73 C ANISOU 3298 CA SER B 131 3187 4347 4522 143 29 218 C ATOM 3299 C SER B 131 13.698 12.192 5.257 1.00 30.93 C ANISOU 3299 C SER B 131 3071 4237 4445 140 30 232 C ATOM 3300 O SER B 131 12.568 12.601 4.980 1.00 42.24 O ANISOU 3300 O SER B 131 4495 5665 5887 139 24 232 O ATOM 3301 CB SER B 131 15.142 14.027 6.118 1.00 36.51 C ANISOU 3301 CB SER B 131 3798 4962 5114 146 43 222 C ATOM 3302 OG SER B 131 16.309 14.800 5.893 1.00 46.71 O ANISOU 3302 OG SER B 131 5102 6260 6383 148 43 210 O ATOM 3303 N VAL B 132 13.923 11.007 5.841 1.00 25.48 N ANISOU 3303 N VAL B 132 2357 3497 3826 502 519 -131 N ATOM 3304 CA VAL B 132 12.856 10.111 6.289 1.00 25.14 C ANISOU 3304 CA VAL B 132 2311 3451 3790 499 523 -129 C ATOM 3305 C VAL B 132 13.162 9.645 7.717 1.00 17.13 C ANISOU 3305 C VAL B 132 1295 2434 2779 497 527 -127 C ATOM 3306 O VAL B 132 14.242 9.883 8.250 1.00 25.74 O ANISOU 3306 O VAL B 132 2387 3524 3868 499 526 -127 O ATOM 3307 CB VAL B 132 12.675 8.900 5.340 1.00 24.25 C ANISOU 3307 CB VAL B 132 2197 3333 3682 501 522 -129 C ATOM 3308 CG1 VAL B 132 12.033 9.334 4.025 1.00 29.03 C ANISOU 3308 CG1 VAL B 132 2803 3943 4285 501 520 -130 C ATOM 3309 CG2 VAL B 132 14.012 8.242 5.070 1.00 14.88 C ANISOU 3309 CG2 VAL B 132 1013 2143 2497 505 520 -129 C ATOM 3310 N GLY B 133 12.196 8.975 8.342 1.00 20.02 N ANISOU 3310 N GLY B 133 1658 2798 3152 493 531 -125 N ATOM 3311 CA GLY B 133 12.398 8.568 9.722 1.00 27.13 C ANISOU 3311 CA GLY B 133 2556 3696 4055 491 535 -123 C ATOM 3312 C GLY B 133 11.454 7.476 10.176 1.00 28.71 C ANISOU 3312 C GLY B 133 2752 3892 4264 488 540 -121 C ATOM 3313 O GLY B 133 10.493 7.123 9.492 1.00 29.00 O ANISOU 3313 O GLY B 133 2787 3928 4302 487 540 -121 O ATOM 3314 N THR B 134 11.750 6.949 11.363 1.00 23.23 N ANISOU 3314 N THR B 134 2057 3195 3574 487 543 -119 N ATOM 3315 CA THR B 134 10.931 5.957 12.055 1.00 26.76 C ANISOU 3315 CA THR B 134 2500 3639 4029 483 548 -117 C ATOM 3316 C THR B 134 10.449 6.566 13.369 1.00 24.29 C ANISOU 3316 C THR B 134 2185 3329 3715 479 552 -116 C ATOM 3317 O THR B 134 11.231 7.184 14.091 1.00 28.75 O ANISOU 3317 O THR B 134 2751 3895 4276 479 551 -116 O ATOM 3318 CB THR B 134 11.720 4.638 12.308 1.00 30.16 C ANISOU 3318 CB THR B 134 2931 4063 4467 485 548 -115 C ATOM 3319 OG1 THR B 134 12.170 4.079 11.068 1.00 27.10 O ANISOU 3319 OG1 THR B 134 2545 3671 4079 489 545 -116 O ATOM 3320 CG2 THR B 134 10.887 3.587 13.049 1.00 26.04 C ANISOU 3320 CG2 THR B 134 2404 3536 3953 481 554 -113 C ATOM 3321 N ILE B 135 9.157 6.447 13.646 1.00 27.28 N ANISOU 3321 N ILE B 135 2560 3710 4096 474 555 -115 N ATOM 3322 CA ILE B 135 8.539 7.016 14.838 1.00 29.87 C ANISOU 3322 CA ILE B 135 2885 4040 4422 470 559 -114 C ATOM 3323 C ILE B 135 7.944 5.879 15.663 1.00 31.47 C ANISOU 3323 C ILE B 135 3084 4239 4634 467 564 -112 C ATOM 3324 O ILE B 135 7.381 4.932 15.103 1.00 32.18 O ANISOU 3324 O ILE B 135 3173 4326 4729 466 565 -111 O ATOM 3325 CB ILE B 135 7.470 8.057 14.449 1.00 24.98 C ANISOU 3325 CB ILE B 135 2265 3427 3798 468 559 -116 C ATOM 3326 CG1 ILE B 135 8.036 8.985 13.370 1.00 23.85 C ANISOU 3326 CG1 ILE B 135 2126 3288 3648 472 553 -118 C ATOM 3327 CG2 ILE B 135 7.032 8.862 15.694 1.00 26.06 C ANISOU 3327 CG2 ILE B 135 2400 3569 3932 464 562 -115 C ATOM 3328 CD1 ILE B 135 7.038 10.032 12.821 1.00 25.46 C ANISOU 3328 CD1 ILE B 135 2330 3498 3846 470 552 -120 C ATOM 3329 N PHE B 136 8.104 5.936 16.984 1.00 27.65 N ANISOU 3329 N PHE B 136 2600 3755 4151 464 568 -110 N ATOM 3330 CA PHE B 136 7.588 4.841 17.801 1.00 29.72 C ANISOU 3330 CA PHE B 136 2857 4012 4421 461 573 -107 C ATOM 3331 C PHE B 136 7.125 5.364 19.154 1.00 33.00 C ANISOU 3331 C PHE B 136 3271 4432 4836 457 577 -106 C ATOM 3332 O PHE B 136 7.683 6.327 19.691 1.00 34.55 O ANISOU 3332 O PHE B 136 3469 4631 5026 457 576 -107 O ATOM 3333 CB PHE B 136 8.629 3.722 18.011 1.00 20.35 C ANISOU 3333 CB PHE B 136 1672 2819 3241 464 573 -106 C ATOM 3334 CG PHE B 136 9.861 4.177 18.728 1.00 22.32 C ANISOU 3334 CG PHE B 136 1925 3069 3488 466 571 -106 C ATOM 3335 CD1 PHE B 136 9.938 4.110 20.118 1.00 32.07 C ANISOU 3335 CD1 PHE B 136 3158 4304 4725 463 575 -104 C ATOM 3336 CD2 PHE B 136 10.903 4.749 18.040 1.00 18.76 C ANISOU 3336 CD2 PHE B 136 1478 2619 3031 470 566 -108 C ATOM 3337 CE1 PHE B 136 11.051 4.577 20.798 1.00 24.37 C ANISOU 3337 CE1 PHE B 136 2185 3328 3746 465 574 -104 C ATOM 3338 CE2 PHE B 136 12.027 5.206 18.714 1.00 19.44 C ANISOU 3338 CE2 PHE B 136 1566 2705 3114 472 565 -108 C ATOM 3339 CZ PHE B 136 12.099 5.122 20.091 1.00 20.12 C ANISOU 3339 CZ PHE B 136 1652 2791 3203 469 569 -106 C ATOM 3340 N GLY B 137 6.101 4.701 19.700 1.00 29.11 N ANISOU 3340 N GLY B 137 2774 3938 4348 452 582 -104 N ATOM 3341 CA GLY B 137 5.633 4.899 21.059 1.00 25.43 C ANISOU 3341 CA GLY B 137 2305 3474 3883 448 586 -103 C ATOM 3342 C GLY B 137 5.302 3.571 21.720 1.00 27.78 C ANISOU 3342 C GLY B 137 2599 3766 4190 445 591 -100 C ATOM 3343 O GLY B 137 4.747 2.668 21.082 1.00 28.51 O ANISOU 3343 O GLY B 137 2690 3856 4288 444 592 -99 O ATOM 3344 N ILE B 138 5.664 3.422 22.985 1.00 26.41 N ANISOU 3344 N ILE B 138 2424 3591 4018 443 594 -98 N ATOM 3345 CA ILE B 138 5.594 2.145 23.691 1.00 31.14 C ANISOU 3345 CA ILE B 138 3021 4184 4626 441 599 -95 C ATOM 3346 C ILE B 138 4.719 2.293 24.940 1.00 38.99 C ANISOU 3346 C ILE B 138 4011 5182 5621 435 604 -93 C ATOM 3347 O ILE B 138 4.969 3.171 25.779 1.00 31.12 O ANISOU 3347 O ILE B 138 3016 4189 4620 434 605 -94 O ATOM 3348 CB ILE B 138 7.010 1.666 24.050 1.00 29.68 C ANISOU 3348 CB ILE B 138 2839 3995 4444 445 597 -94 C ATOM 3349 CG1 ILE B 138 7.833 1.483 22.772 1.00 23.00 C ANISOU 3349 CG1 ILE B 138 1996 3145 3596 450 592 -96 C ATOM 3350 CG2 ILE B 138 6.972 0.400 24.890 1.00 31.26 C ANISOU 3350 CG2 ILE B 138 3036 4189 4653 442 602 -91 C ATOM 3351 CD1 ILE B 138 9.328 1.411 22.980 1.00 15.79 C ANISOU 3351 CD1 ILE B 138 1088 2230 2683 455 589 -95 C ATOM 3352 N TYR B 139 3.687 1.442 25.056 1.00 42.09 N ANISOU 3352 N TYR B 139 4400 5573 6020 431 608 -92 N ATOM 3353 CA TYR B 139 2.791 1.392 26.216 1.00 25.11 C ANISOU 3353 CA TYR B 139 2244 3424 3871 425 614 -90 C ATOM 3354 C TYR B 139 2.828 0.020 26.892 1.00 25.23 C ANISOU 3354 C TYR B 139 2257 3433 3896 423 618 -87 C ATOM 3355 O TYR B 139 2.962 -1.011 26.236 1.00 33.67 O ANISOU 3355 O TYR B 139 3326 4496 4971 425 617 -86 O ATOM 3356 CB TYR B 139 1.331 1.663 25.839 1.00 19.29 C ANISOU 3356 CB TYR B 139 1504 2692 3133 421 615 -91 C ATOM 3357 CG TYR B 139 1.074 2.997 25.196 1.00 31.98 C ANISOU 3357 CG TYR B 139 3114 4306 4732 423 612 -94 C ATOM 3358 CD1 TYR B 139 0.794 4.133 25.964 1.00 31.61 C ANISOU 3358 CD1 TYR B 139 3067 4266 4679 420 613 -95 C ATOM 3359 CD2 TYR B 139 1.080 3.116 23.811 1.00 32.16 C ANISOU 3359 CD2 TYR B 139 3139 4329 4752 426 607 -96 C ATOM 3360 CE1 TYR B 139 0.555 5.363 25.356 1.00 44.19 C ANISOU 3360 CE1 TYR B 139 4662 5865 6264 422 609 -97 C ATOM 3361 CE2 TYR B 139 0.845 4.331 23.195 1.00 48.45 C ANISOU 3361 CE2 TYR B 139 5203 6398 6807 427 604 -99 C ATOM 3362 CZ TYR B 139 0.584 5.454 23.961 1.00 54.53 C ANISOU 3362 CZ TYR B 139 5973 7174 7571 425 605 -99 C ATOM 3363 OH TYR B 139 0.354 6.651 23.308 1.00 55.18 O ANISOU 3363 OH TYR B 139 6058 7263 7646 427 601 -102 O ATOM 3364 N ARG B 140 2.653 0.004 28.209 1.00 35.23 N ANISOU 3364 N ARG B 140 3521 4700 5164 419 623 -85 N ATOM 3365 CA ARG B 140 2.325 -1.250 28.870 1.00 44.75 C ANISOU 3365 CA ARG B 140 4724 5902 6379 416 628 -81 C ATOM 3366 C ARG B 140 0.885 -1.630 28.540 1.00 39.66 C ANISOU 3366 C ARG B 140 4074 5259 5737 411 630 -81 C ATOM 3367 O ARG B 140 0.011 -0.763 28.443 1.00 34.41 O ANISOU 3367 O ARG B 140 3408 4600 5066 409 631 -83 O ATOM 3368 CB ARG B 140 2.517 -1.131 30.382 1.00 49.44 C ANISOU 3368 CB ARG B 140 5315 6496 6973 412 632 -79 C ATOM 3369 CG AARG B 140 2.876 -2.443 31.043 0.48 50.27 C ANISOU 3369 CG AARG B 140 5419 6594 7087 412 635 -76 C ATOM 3370 CG BARG B 140 2.759 -2.470 31.032 0.52 50.26 C ANISOU 3370 CG BARG B 140 5418 6593 7087 411 636 -76 C ATOM 3371 CD AARG B 140 3.746 -2.229 32.271 0.48 52.53 C ANISOU 3371 CD AARG B 140 5706 6879 7373 411 637 -74 C ATOM 3372 CD BARG B 140 2.152 -2.591 32.421 0.52 51.36 C ANISOU 3372 CD BARG B 140 5552 6734 7228 405 642 -73 C ATOM 3373 NE AARG B 140 4.986 -1.525 31.955 0.48 52.45 N ANISOU 3373 NE AARG B 140 5702 6870 7358 417 632 -76 N ATOM 3374 NE BARG B 140 2.266 -3.976 32.864 0.52 49.20 N ANISOU 3374 NE BARG B 140 5277 6454 6965 404 646 -70 N ATOM 3375 CZ AARG B 140 6.048 -1.496 32.754 0.48 46.51 C ANISOU 3375 CZ AARG B 140 4951 6115 6605 419 632 -75 C ATOM 3376 CZ BARG B 140 1.319 -4.892 32.698 0.52 43.95 C ANISOU 3376 CZ BARG B 140 4607 5786 6305 400 649 -69 C ATOM 3377 NH1AARG B 140 6.014 -2.142 33.915 0.48 46.83 N ANISOU 3377 NH1AARG B 140 4988 6152 6651 415 637 -72 N ATOM 3378 NH1BARG B 140 0.163 -4.566 32.129 0.52 32.80 N ANISOU 3378 NH1BARG B 140 3193 4379 4891 397 649 -70 N ATOM 3379 NH2AARG B 140 7.143 -0.830 32.394 0.48 36.42 N ANISOU 3379 NH2AARG B 140 3679 4838 5323 424 627 -77 N ATOM 3380 NH2BARG B 140 1.527 -6.134 33.112 0.52 46.20 N ANISOU 3380 NH2BARG B 140 4891 6065 6599 399 652 -66 N ATOM 3381 N LYS B 141 0.643 -2.927 28.336 1.00 38.96 N ANISOU 3381 N LYS B 141 3983 5164 5657 410 633 -79 N ATOM 3382 CA LYS B 141 -0.689 -3.391 27.953 1.00 44.78 C ANISOU 3382 CA LYS B 141 4716 5902 6397 406 635 -79 C ATOM 3383 C LYS B 141 -1.673 -3.262 29.121 1.00 49.73 C ANISOU 3383 C LYS B 141 5339 6533 7025 400 641 -77 C ATOM 3384 O LYS B 141 -1.287 -3.057 30.275 1.00 49.98 O ANISOU 3384 O LYS B 141 5370 6566 7056 398 644 -76 O ATOM 3385 CB LYS B 141 -0.647 -4.843 27.490 1.00 45.57 C ANISOU 3385 CB LYS B 141 4814 5994 6506 407 636 -77 C ATOM 3386 CG LYS B 141 -0.692 -5.806 28.646 1.00 45.79 C ANISOU 3386 CG LYS B 141 4839 6018 6541 403 642 -74 C ATOM 3387 CD LYS B 141 -0.732 -7.232 28.199 1.00 38.75 C ANISOU 3387 CD LYS B 141 3946 5119 5659 404 643 -72 C ATOM 3388 CE LYS B 141 -0.523 -8.145 29.397 1.00 41.44 C ANISOU 3388 CE LYS B 141 4283 5455 6007 401 648 -68 C ATOM 3389 NZ LYS B 141 -0.090 -9.498 28.938 1.00 52.46 N ANISOU 3389 NZ LYS B 141 5679 6842 7412 403 648 -66 N ATOM 3390 N LYS B 142 -2.968 -3.361 28.807 1.00 59.48 N ANISOU 3390 N LYS B 142 6570 7771 8260 395 643 -78 N ATOM 3391 CA LYS B 142 -4.000 -3.038 29.791 1.00 65.29 C ANISOU 3391 CA LYS B 142 7301 8512 8995 389 648 -77 C ATOM 3392 C LYS B 142 -4.684 -4.237 30.437 1.00 82.90 C ANISOU 3392 C LYS B 142 9526 10739 11233 384 654 -74 C ATOM 3393 O LYS B 142 -4.897 -4.229 31.653 1.00 84.55 O ANISOU 3393 O LYS B 142 9732 10949 11443 379 658 -72 O ATOM 3394 CB LYS B 142 -5.084 -2.164 29.155 1.00 52.75 C ANISOU 3394 CB LYS B 142 5711 6930 7400 388 647 -80 C ATOM 3395 CG LYS B 142 -4.762 -0.701 29.069 1.00 51.35 C ANISOU 3395 CG LYS B 142 5538 6760 7214 390 643 -82 C ATOM 3396 CD LYS B 142 -4.667 -0.144 30.486 1.00 61.27 C ANISOU 3396 CD LYS B 142 6793 8019 8467 387 646 -81 C ATOM 3397 CE LYS B 142 -4.503 1.376 30.504 1.00 54.60 C ANISOU 3397 CE LYS B 142 5951 7181 7612 389 643 -84 C ATOM 3398 NZ LYS B 142 -4.486 1.890 31.892 1.00 47.45 N ANISOU 3398 NZ LYS B 142 5045 6279 6705 385 646 -83 N ATOM 3399 N SER B 143 -5.013 -5.286 29.701 1.00 93.48 N ANISOU 3399 N SER B 143 10865 12074 12580 384 654 -73 N ATOM 3400 CA SER B 143 -5.734 -6.371 30.346 1.00104.19 C ANISOU 3400 CA SER B 143 12215 13427 13944 378 660 -70 C ATOM 3401 C SER B 143 -4.815 -7.532 30.670 1.00106.47 C ANISOU 3401 C SER B 143 12505 13708 14241 380 661 -67 C ATOM 3402 O SER B 143 -3.685 -7.626 30.185 1.00104.95 O ANISOU 3402 O SER B 143 12317 13511 14049 386 657 -68 O ATOM 3403 CB SER B 143 -6.895 -6.862 29.474 1.00112.78 C ANISOU 3403 CB SER B 143 13301 14517 15035 376 661 -71 C ATOM 3404 OG SER B 143 -6.458 -7.850 28.556 1.00119.12 O ANISOU 3404 OG SER B 143 14104 15312 15844 379 659 -70 O ATOM 3405 N THR B 144 -5.314 -8.404 31.539 1.00110.09 N ANISOU 3405 N THR B 144 12959 14164 14706 375 667 -64 N ATOM 3406 CA THR B 144 -4.655 -9.663 31.827 1.00108.20 C ANISOU 3406 CA THR B 144 12719 13917 14476 376 669 -61 C ATOM 3407 C THR B 144 -5.290 -10.820 31.074 1.00110.94 C ANISOU 3407 C THR B 144 13063 14259 14831 374 670 -60 C ATOM 3408 O THR B 144 -4.758 -11.935 31.108 1.00111.85 O ANISOU 3408 O THR B 144 13177 14366 14953 376 671 -58 O ATOM 3409 CB THR B 144 -4.715 -9.946 33.328 1.00 99.90 C ANISOU 3409 CB THR B 144 11665 12865 13428 370 675 -58 C ATOM 3410 OG1 THR B 144 -4.274 -11.285 33.577 1.00102.22 O ANISOU 3410 OG1 THR B 144 11958 13151 13732 371 677 -55 O ATOM 3411 CG2 THR B 144 -6.147 -9.773 33.835 1.00 92.27 C ANISOU 3411 CG2 THR B 144 10694 11905 12461 363 679 -58 C ATOM 3412 N ASP B 145 -6.400 -10.565 30.383 1.00111.44 N ANISOU 3412 N ASP B 145 13124 14326 14891 372 670 -62 N ATOM 3413 CA ASP B 145 -7.081 -11.548 29.554 1.00111.30 C ANISOU 3413 CA ASP B 145 13103 14304 14880 371 670 -61 C ATOM 3414 C ASP B 145 -6.213 -11.979 28.378 1.00103.27 C ANISOU 3414 C ASP B 145 12091 13282 13866 378 665 -63 C ATOM 3415 O ASP B 145 -5.185 -12.646 28.543 1.00 96.61 O ANISOU 3415 O ASP B 145 11249 12432 13027 381 665 -61 O ATOM 3416 CB ASP B 145 -8.413 -10.978 29.044 1.00117.09 C ANISOU 3416 CB ASP B 145 13835 15046 15610 367 671 -63 C ATOM 3417 CG ASP B 145 -9.367 -10.595 30.169 1.00118.86 C ANISOU 3417 CG ASP B 145 14054 15276 15831 360 676 -62 C ATOM 3418 OD1 ASP B 145 -9.197 -11.094 31.299 1.00120.46 O ANISOU 3418 OD1 ASP B 145 14255 15476 16038 356 680 -60 O ATOM 3419 OD2 ASP B 145 -10.291 -9.789 29.920 1.00117.97 O ANISOU 3419 OD2 ASP B 145 13940 15170 15712 357 676 -65 O ATOM 3420 N GLU B 146 -6.645 -11.582 27.181 1.00 95.82 N ANISOU 3420 N GLU B 146 11148 12341 12918 380 662 -65 N ATOM 3421 CA GLU B 146 -6.021 -11.792 25.895 1.00 81.84 C ANISOU 3421 CA GLU B 146 9381 10566 11148 386 656 -67 C ATOM 3422 C GLU B 146 -5.750 -10.473 25.196 1.00 69.14 C ANISOU 3422 C GLU B 146 7777 8964 9530 390 651 -71 C ATOM 3423 O GLU B 146 -6.527 -9.522 25.327 1.00 69.26 O ANISOU 3423 O GLU B 146 7791 8986 9538 387 651 -72 O ATOM 3424 CB GLU B 146 -6.906 -12.633 24.979 1.00 81.87 C ANISOU 3424 CB GLU B 146 9382 10568 11157 385 657 -67 C ATOM 3425 CG GLU B 146 -6.791 -14.096 25.187 1.00 90.29 C ANISOU 3425 CG GLU B 146 10445 11626 12235 384 660 -64 C ATOM 3426 CD GLU B 146 -7.841 -14.839 24.413 1.00 97.43 C ANISOU 3426 CD GLU B 146 11346 12529 13144 381 661 -64 C ATOM 3427 OE1 GLU B 146 -8.768 -14.173 23.902 1.00 98.05 O ANISOU 3427 OE1 GLU B 146 11424 12614 13217 379 661 -66 O ATOM 3428 OE2 GLU B 146 -7.741 -16.080 24.320 1.00100.94 O ANISOU 3428 OE2 GLU B 146 11789 12967 13598 381 663 -62 O ATOM 3429 N PRO B 147 -4.637 -10.384 24.484 1.00 56.70 N ANISOU 3429 N PRO B 147 6206 7385 7953 397 646 -72 N ATOM 3430 CA PRO B 147 -4.305 -9.157 23.756 1.00 51.74 C ANISOU 3430 CA PRO B 147 5582 6761 7315 401 640 -75 C ATOM 3431 C PRO B 147 -5.335 -8.840 22.680 1.00 54.00 C ANISOU 3431 C PRO B 147 5867 7051 7598 400 639 -78 C ATOM 3432 O PRO B 147 -5.814 -9.731 21.973 1.00 58.07 O ANISOU 3432 O PRO B 147 6381 7564 8120 400 639 -77 O ATOM 3433 CB PRO B 147 -2.938 -9.471 23.145 1.00 51.99 C ANISOU 3433 CB PRO B 147 5619 6787 7347 408 636 -76 C ATOM 3434 CG PRO B 147 -2.851 -10.970 23.146 1.00 54.36 C ANISOU 3434 CG PRO B 147 5917 7079 7658 408 638 -73 C ATOM 3435 CD PRO B 147 -3.603 -11.419 24.352 1.00 56.23 C ANISOU 3435 CD PRO B 147 6149 7317 7900 401 645 -71 C ATOM 3436 N SER B 148 -5.690 -7.561 22.569 1.00 52.39 N ANISOU 3436 N SER B 148 5664 6855 7385 400 637 -80 N ATOM 3437 CA SER B 148 -6.604 -7.119 21.523 1.00 51.47 C ANISOU 3437 CA SER B 148 5548 6744 7266 400 635 -82 C ATOM 3438 C SER B 148 -6.254 -5.692 21.124 1.00 52.02 C ANISOU 3438 C SER B 148 5621 6818 7324 403 630 -85 C ATOM 3439 O SER B 148 -5.369 -5.056 21.704 1.00 51.73 O ANISOU 3439 O SER B 148 5588 6783 7284 405 629 -85 O ATOM 3440 CB SER B 148 -8.068 -7.194 21.962 1.00 49.09 C ANISOU 3440 CB SER B 148 5240 6446 6965 393 640 -82 C ATOM 3441 OG SER B 148 -8.415 -6.052 22.724 1.00 53.64 O ANISOU 3441 OG SER B 148 5817 7030 7535 390 641 -82 O ATOM 3442 N GLU B 149 -6.984 -5.192 20.123 1.00 52.08 N ANISOU 3442 N GLU B 149 5695 6628 7465 467 406 -268 N ATOM 3443 CA GLU B 149 -6.741 -3.855 19.599 1.00 41.24 C ANISOU 3443 CA GLU B 149 4333 5252 6083 476 385 -279 C ATOM 3444 C GLU B 149 -6.883 -2.791 20.674 1.00 36.76 C ANISOU 3444 C GLU B 149 3762 4707 5497 494 385 -286 C ATOM 3445 O GLU B 149 -6.167 -1.783 20.644 1.00 38.59 O ANISOU 3445 O GLU B 149 4006 4943 5713 501 373 -283 O ATOM 3446 CB GLU B 149 -7.719 -3.558 18.464 1.00 38.20 C ANISOU 3446 CB GLU B 149 3946 4849 5718 476 371 -303 C ATOM 3447 CG GLU B 149 -7.105 -3.447 17.097 1.00 46.12 C ANISOU 3447 CG GLU B 149 4965 5831 6726 465 354 -300 C ATOM 3448 CD GLU B 149 -7.926 -2.581 16.148 1.00 55.78 C ANISOU 3448 CD GLU B 149 6191 7043 7962 471 334 -327 C ATOM 3449 OE1 GLU B 149 -8.492 -1.553 16.603 1.00 58.04 O ANISOU 3449 OE1 GLU B 149 6472 7338 8241 486 327 -344 O ATOM 3450 OE2 GLU B 149 -7.994 -2.931 14.948 1.00 51.87 O ANISOU 3450 OE2 GLU B 149 5700 6527 7480 460 325 -331 O ATOM 3451 N LYS B 150 -7.774 -3.011 21.646 1.00 35.56 N ANISOU 3451 N LYS B 150 3594 4571 5348 503 399 -293 N ATOM 3452 CA LYS B 150 -8.016 -2.003 22.673 1.00 45.25 C ANISOU 3452 CA LYS B 150 4815 5817 6559 522 399 -301 C ATOM 3453 C LYS B 150 -6.747 -1.634 23.424 1.00 40.13 C ANISOU 3453 C LYS B 150 4177 5186 5885 525 401 -281 C ATOM 3454 O LYS B 150 -6.622 -0.500 23.900 1.00 43.24 O ANISOU 3454 O LYS B 150 4574 5591 6264 539 394 -286 O ATOM 3455 CB LYS B 150 -9.099 -2.474 23.651 1.00 45.45 C ANISOU 3455 CB LYS B 150 4820 5857 6591 529 416 -309 C ATOM 3456 CG LYS B 150 -10.474 -2.649 23.016 1.00 56.03 C ANISOU 3456 CG LYS B 150 6150 7184 7956 529 413 -333 C ATOM 3457 CD LYS B 150 -11.514 -3.160 24.009 1.00 68.87 C ANISOU 3457 CD LYS B 150 7755 8823 9588 535 431 -340 C ATOM 3458 CE LYS B 150 -12.888 -3.281 23.353 1.00 73.75 C ANISOU 3458 CE LYS B 150 8363 9427 10231 535 426 -366 C ATOM 3459 NZ LYS B 150 -13.941 -3.727 24.305 1.00 72.25 N ANISOU 3459 NZ LYS B 150 8152 9250 10048 542 444 -374 N ATOM 3460 N ASP B 151 -5.792 -2.560 23.518 1.00 38.67 N ANISOU 3460 N ASP B 151 3996 5001 5695 511 410 -258 N ATOM 3461 CA ASP B 151 -4.574 -2.292 24.263 1.00 40.43 C ANISOU 3461 CA ASP B 151 4226 5240 5894 513 413 -240 C ATOM 3462 C ASP B 151 -3.770 -1.140 23.663 1.00 40.11 C ANISOU 3462 C ASP B 151 4203 5193 5842 516 393 -240 C ATOM 3463 O ASP B 151 -2.939 -0.550 24.357 1.00 43.33 O ANISOU 3463 O ASP B 151 4618 5618 6229 523 392 -231 O ATOM 3464 CB ASP B 151 -3.736 -3.572 24.316 1.00 44.39 C ANISOU 3464 CB ASP B 151 4731 5738 6397 495 425 -217 C ATOM 3465 CG ASP B 151 -4.272 -4.603 25.319 1.00 47.34 C ANISOU 3465 CG ASP B 151 5088 6125 6774 495 447 -213 C ATOM 3466 OD1 ASP B 151 -4.454 -4.260 26.509 1.00 47.82 O ANISOU 3466 OD1 ASP B 151 5139 6210 6821 508 456 -214 O ATOM 3467 OD2 ASP B 151 -4.519 -5.757 24.917 1.00 48.79 O ANISOU 3467 OD2 ASP B 151 5269 6295 6976 481 457 -207 O ATOM 3468 N ALA B 152 -4.015 -0.789 22.406 1.00 36.63 N ANISOU 3468 N ALA B 152 3771 4731 5415 512 377 -252 N ATOM 3469 CA ALA B 152 -3.327 0.311 21.746 1.00 40.73 C ANISOU 3469 CA ALA B 152 4308 5243 5926 515 358 -254 C ATOM 3470 C ALA B 152 -4.079 1.634 21.804 1.00 42.81 C ANISOU 3470 C ALA B 152 4570 5508 6189 532 345 -276 C ATOM 3471 O ALA B 152 -3.603 2.623 21.241 1.00 46.28 O ANISOU 3471 O ALA B 152 5022 5938 6622 535 328 -279 O ATOM 3472 CB ALA B 152 -3.070 -0.040 20.283 1.00 47.69 C ANISOU 3472 CB ALA B 152 5199 6098 6822 500 347 -253 C ATOM 3473 N LEU B 153 -5.256 1.674 22.410 1.00 40.16 N ANISOU 3473 N LEU B 153 4219 5180 5861 542 353 -291 N ATOM 3474 CA LEU B 153 -6.066 2.890 22.451 1.00 33.63 C ANISOU 3474 CA LEU B 153 3391 4352 5036 557 340 -314 C ATOM 3475 C LEU B 153 -5.878 3.666 23.756 1.00 39.52 C ANISOU 3475 C LEU B 153 4134 5120 5763 573 346 -311 C ATOM 3476 O LEU B 153 -6.841 3.954 24.450 1.00 45.61 O ANISOU 3476 O LEU B 153 4892 5899 6537 584 352 -326 O ATOM 3477 CB LEU B 153 -7.531 2.550 22.205 1.00 24.85 C ANISOU 3477 CB LEU B 153 2264 3232 3946 558 342 -336 C ATOM 3478 CG LEU B 153 -7.794 1.962 20.814 1.00 36.89 C ANISOU 3478 CG LEU B 153 3792 4733 5491 544 333 -343 C ATOM 3479 CD1 LEU B 153 -9.248 1.556 20.636 1.00 40.02 C ANISOU 3479 CD1 LEU B 153 4173 5124 5909 545 336 -364 C ATOM 3480 CD2 LEU B 153 -7.373 2.907 19.686 1.00 37.29 C ANISOU 3480 CD2 LEU B 153 3860 4767 5542 542 309 -351 C ATOM 3481 N GLN B 154 -4.616 3.955 24.163 1.00 34.89 N ANISOU 3481 N GLN B 154 3558 4543 5156 573 347 -292 N ATOM 3482 CA GLN B 154 -4.360 4.763 25.351 1.00 27.20 C ANISOU 3482 CA GLN B 154 2582 3589 4163 588 351 -289 C ATOM 3483 C GLN B 154 -3.942 6.194 24.989 1.00 36.63 C ANISOU 3483 C GLN B 154 3791 4774 5351 596 332 -297 C ATOM 3484 O GLN B 154 -3.371 6.431 23.922 1.00 44.18 O ANISOU 3484 O GLN B 154 4762 5714 6311 587 317 -296 O ATOM 3485 CB GLN B 154 -3.276 4.105 26.199 1.00 32.63 C ANISOU 3485 CB GLN B 154 3269 4297 4831 584 365 -264 C ATOM 3486 CG GLN B 154 -3.509 2.619 26.415 1.00 43.27 C ANISOU 3486 CG GLN B 154 4606 5650 6186 573 382 -255 C ATOM 3487 CD GLN B 154 -2.460 1.986 27.289 1.00 46.86 C ANISOU 3487 CD GLN B 154 5059 6124 6621 569 395 -233 C ATOM 3488 OE1 GLN B 154 -1.896 2.638 28.164 1.00 52.95 O ANISOU 3488 OE1 GLN B 154 5832 6914 7372 579 396 -227 O ATOM 3489 NE2 GLN B 154 -2.192 0.704 27.060 1.00 50.20 N ANISOU 3489 NE2 GLN B 154 5480 6543 7052 552 404 -222 N ATOM 3490 N PRO B 155 -4.208 7.178 25.849 1.00 37.60 N ANISOU 3490 N PRO B 155 3911 4907 5466 611 331 -306 N ATOM 3491 CA PRO B 155 -3.729 8.546 25.597 1.00 41.80 C ANISOU 3491 CA PRO B 155 4459 5432 5993 617 313 -313 C ATOM 3492 C PRO B 155 -2.226 8.690 25.802 1.00 40.03 C ANISOU 3492 C PRO B 155 4247 5215 5749 615 313 -289 C ATOM 3493 O PRO B 155 -1.586 7.930 26.532 1.00 38.44 O ANISOU 3493 O PRO B 155 4040 5031 5532 612 329 -269 O ATOM 3494 CB PRO B 155 -4.505 9.388 26.616 1.00 37.92 C ANISOU 3494 CB PRO B 155 3959 4950 5500 634 316 -328 C ATOM 3495 CG PRO B 155 -4.732 8.452 27.751 1.00 38.56 C ANISOU 3495 CG PRO B 155 4023 5053 5573 637 340 -315 C ATOM 3496 CD PRO B 155 -4.973 7.095 27.106 1.00 41.68 C ANISOU 3496 CD PRO B 155 4412 5444 5980 623 347 -310 C ATOM 3497 N GLY B 156 -1.674 9.720 25.160 1.00 41.71 N ANISOU 3497 N GLY B 156 4476 5413 5959 615 295 -294 N ATOM 3498 CA GLY B 156 -0.236 9.929 25.182 1.00 36.53 C ANISOU 3498 CA GLY B 156 3833 4761 5285 611 292 -273 C ATOM 3499 C GLY B 156 0.368 10.053 26.565 1.00 39.98 C ANISOU 3499 C GLY B 156 4266 5223 5702 621 306 -258 C ATOM 3500 O GLY B 156 1.534 9.702 26.757 1.00 43.99 O ANISOU 3500 O GLY B 156 4779 5741 6194 615 310 -238 O ATOM 3501 N ARG B 157 -0.412 10.525 27.550 1.00 42.35 N ANISOU 3501 N ARG B 157 4555 5533 6002 634 313 -269 N ATOM 3502 CA ARG B 157 0.064 10.582 28.940 1.00 42.71 C ANISOU 3502 CA ARG B 157 4595 5605 6030 644 328 -254 C ATOM 3503 C ARG B 157 0.596 9.228 29.424 1.00 41.47 C ANISOU 3503 C ARG B 157 4430 5469 5860 637 345 -233 C ATOM 3504 O ARG B 157 1.416 9.175 30.343 1.00 39.36 O ANISOU 3504 O ARG B 157 4162 5223 5572 641 354 -217 O ATOM 3505 CB ARG B 157 -1.065 11.056 29.879 1.00 42.25 C ANISOU 3505 CB ARG B 157 4523 5553 5976 658 336 -270 C ATOM 3506 CG ARG B 157 -1.499 12.514 29.722 1.00 46.71 C ANISOU 3506 CG ARG B 157 5095 6102 6550 667 319 -294 C ATOM 3507 CD ARG B 157 -0.474 13.561 30.219 1.00 53.31 C ANISOU 3507 CD ARG B 157 5942 6940 7372 672 313 -286 C ATOM 3508 NE ARG B 157 -0.838 14.935 29.828 1.00 51.76 N ANISOU 3508 NE ARG B 157 5755 6725 7186 677 292 -312 N ATOM 3509 CZ ARG B 157 0.010 15.964 29.804 1.00 49.15 C ANISOU 3509 CZ ARG B 157 5438 6388 6848 679 279 -312 C ATOM 3510 NH1 ARG B 157 1.276 15.790 30.166 1.00 45.13 N ANISOU 3510 NH1 ARG B 157 4936 5889 6323 677 287 -286 N ATOM 3511 NH2 ARG B 157 -0.401 17.166 29.405 1.00 45.08 N ANISOU 3511 NH2 ARG B 157 4931 5856 6341 683 258 -339 N ATOM 3512 N ASN B 158 0.131 8.124 28.831 1.00 47.06 N ANISOU 3512 N ASN B 158 5131 6170 6579 625 349 -235 N ATOM 3513 CA ASN B 158 0.474 6.778 29.282 1.00 47.31 C ANISOU 3513 CA ASN B 158 5153 6219 6603 616 365 -220 C ATOM 3514 C ASN B 158 1.777 6.243 28.701 1.00 44.60 C ANISOU 3514 C ASN B 158 4821 5872 6252 600 359 -204 C ATOM 3515 O ASN B 158 2.136 5.101 28.992 1.00 41.93 O ANISOU 3515 O ASN B 158 4477 5544 5910 589 370 -194 O ATOM 3516 CB ASN B 158 -0.657 5.794 28.951 1.00 45.50 C ANISOU 3516 CB ASN B 158 4911 5983 6393 610 373 -229 C ATOM 3517 CG ASN B 158 -1.888 5.989 29.826 1.00 45.32 C ANISOU 3517 CG ASN B 158 4872 5971 6375 624 383 -241 C ATOM 3518 OD1 ASN B 158 -1.958 6.920 30.639 1.00 43.04 O ANISOU 3518 OD1 ASN B 158 4583 5692 6077 639 385 -244 O ATOM 3519 ND2 ASN B 158 -2.878 5.113 29.646 1.00 41.04 N ANISOU 3519 ND2 ASN B 158 4319 5426 5850 620 392 -249 N ATOM 3520 N LEU B 159 2.483 7.013 27.882 1.00 35.30 N ANISOU 3520 N LEU B 159 3661 4679 5073 597 343 -204 N ATOM 3521 CA LEU B 159 3.655 6.474 27.215 1.00 21.75 C ANISOU 3521 CA LEU B 159 1955 2955 3352 580 337 -190 C ATOM 3522 C LEU B 159 4.743 6.111 28.219 1.00 26.41 C ANISOU 3522 C LEU B 159 2544 3570 3922 577 346 -176 C ATOM 3523 O LEU B 159 5.015 6.856 29.166 1.00 28.79 O ANISOU 3523 O LEU B 159 2844 3890 4206 591 347 -174 O ATOM 3524 CB LEU B 159 4.182 7.485 26.195 1.00 28.44 C ANISOU 3524 CB LEU B 159 2821 3783 4203 579 318 -193 C ATOM 3525 CG LEU B 159 3.461 7.542 24.838 1.00 28.87 C ANISOU 3525 CG LEU B 159 2881 3809 4280 573 306 -206 C ATOM 3526 CD1 LEU B 159 3.748 8.857 24.130 1.00 23.42 C ANISOU 3526 CD1 LEU B 159 2206 3102 3590 577 287 -214 C ATOM 3527 CD2 LEU B 159 3.845 6.367 23.963 1.00 24.03 C ANISOU 3527 CD2 LEU B 159 2271 3184 3676 552 308 -197 C ATOM 3528 N VAL B 160 5.387 4.965 27.986 1.00 28.33 N ANISOU 3528 N VAL B 160 2788 3810 4167 558 351 -165 N ATOM 3529 CA VAL B 160 6.550 4.539 28.771 1.00 31.95 C ANISOU 3529 CA VAL B 160 3246 4285 4610 550 357 -153 C ATOM 3530 C VAL B 160 7.853 5.041 28.142 1.00 29.08 C ANISOU 3530 C VAL B 160 2899 3910 4239 541 343 -145 C ATOM 3531 O VAL B 160 8.775 5.469 28.841 1.00 30.13 O ANISOU 3531 O VAL B 160 3035 4058 4354 543 342 -141 O ATOM 3532 CB VAL B 160 6.551 2.994 28.901 1.00 37.10 C ANISOU 3532 CB VAL B 160 3889 4934 5272 531 372 -144 C ATOM 3533 CG1 VAL B 160 7.838 2.506 29.522 1.00 34.88 C ANISOU 3533 CG1 VAL B 160 3611 4660 4980 517 378 -131 C ATOM 3534 CG2 VAL B 160 5.364 2.493 29.722 1.00 28.46 C ANISOU 3534 CG2 VAL B 160 2777 3856 4182 540 387 -152 C ATOM 3535 N ALA B 161 7.938 5.020 26.816 1.00 32.36 N ANISOU 3535 N ALA B 161 3327 4299 4669 531 333 -144 N ATOM 3536 CA ALA B 161 9.078 5.548 26.079 1.00 28.76 C ANISOU 3536 CA ALA B 161 2889 3830 4209 523 319 -136 C ATOM 3537 C ALA B 161 8.604 5.870 24.673 1.00 26.85 C ANISOU 3537 C ALA B 161 2656 3561 3983 520 307 -143 C ATOM 3538 O ALA B 161 7.649 5.267 24.183 1.00 25.51 O ANISOU 3538 O ALA B 161 2481 3381 3831 517 311 -149 O ATOM 3539 CB ALA B 161 10.244 4.550 26.044 1.00 14.35 C ANISOU 3539 CB ALA B 161 1069 1999 2384 500 326 -119 C ATOM 3540 N ALA B 162 9.238 6.862 24.054 1.00 29.41 N ANISOU 3540 N ALA B 162 2996 3876 4303 523 291 -143 N ATOM 3541 CA ALA B 162 8.888 7.243 22.691 1.00 21.21 C ANISOU 3541 CA ALA B 162 1967 2812 3280 520 278 -150 C ATOM 3542 C ALA B 162 10.067 7.978 22.080 1.00 18.34 C ANISOU 3542 C ALA B 162 1621 2438 2908 515 264 -143 C ATOM 3543 O ALA B 162 10.935 8.484 22.791 1.00 20.23 O ANISOU 3543 O ALA B 162 1864 2692 3131 519 263 -137 O ATOM 3544 CB ALA B 162 7.631 8.115 22.646 1.00 27.03 C ANISOU 3544 CB ALA B 162 2700 3546 4025 537 272 -169 C ATOM 3545 N GLY B 163 10.079 8.049 20.754 1.00 25.88 N ANISOU 3545 N GLY B 163 2586 3370 3877 506 252 -145 N ATOM 3546 CA GLY B 163 11.112 8.812 20.074 1.00 26.67 C ANISOU 3546 CA GLY B 163 2703 3458 3971 502 238 -140 C ATOM 3547 C GLY B 163 11.109 8.529 18.585 1.00 26.45 C ANISOU 3547 C GLY B 163 2686 3406 3960 488 229 -139 C ATOM 3548 O GLY B 163 10.107 8.080 18.030 1.00 27.39 O ANISOU 3548 O GLY B 163 2799 3514 4094 487 230 -148 O ATOM 3549 N TYR B 164 12.253 8.780 17.953 1.00 26.96 N ANISOU 3549 N TYR B 164 2764 3459 4019 478 220 -129 N ATOM 3550 CA TYR B 164 12.328 8.663 16.504 1.00 20.97 C ANISOU 3550 CA TYR B 164 2017 2678 3275 467 210 -128 C ATOM 3551 C TYR B 164 13.761 8.418 16.066 1.00 24.52 C ANISOU 3551 C TYR B 164 2478 3119 3719 450 208 -110 C ATOM 3552 O TYR B 164 14.716 8.675 16.804 1.00 26.64 O ANISOU 3552 O TYR B 164 2750 3399 3973 450 210 -100 O ATOM 3553 CB TYR B 164 11.763 9.906 15.787 1.00 14.32 C ANISOU 3553 CB TYR B 164 1181 1823 2437 479 192 -145 C ATOM 3554 CG TYR B 164 12.371 11.228 16.181 1.00 17.23 C ANISOU 3554 CG TYR B 164 1558 2196 2791 491 182 -147 C ATOM 3555 CD1 TYR B 164 13.518 11.698 15.564 1.00 16.99 C ANISOU 3555 CD1 TYR B 164 1544 2157 2756 484 171 -138 C ATOM 3556 CD2 TYR B 164 11.775 12.033 17.158 1.00 25.84 C ANISOU 3556 CD2 TYR B 164 2643 3301 3876 510 183 -158 C ATOM 3557 CE1 TYR B 164 14.068 12.920 15.916 1.00 16.17 C ANISOU 3557 CE1 TYR B 164 1448 2057 2639 495 162 -140 C ATOM 3558 CE2 TYR B 164 12.325 13.275 17.521 1.00 16.86 C ANISOU 3558 CE2 TYR B 164 1514 2166 2727 521 174 -160 C ATOM 3559 CZ TYR B 164 13.475 13.698 16.900 1.00 15.26 C ANISOU 3559 CZ TYR B 164 1327 1953 2518 513 163 -151 C ATOM 3560 OH TYR B 164 14.039 14.905 17.241 1.00 20.84 O ANISOU 3560 OH TYR B 164 2042 2661 3214 523 154 -152 O ATOM 3561 N ALA B 165 13.884 7.858 14.865 1.00 20.00 N ANISOU 3561 N ALA B 165 1912 2526 3160 435 204 -104 N ATOM 3562 CA ALA B 165 15.136 7.791 14.130 1.00 23.31 C ANISOU 3562 CA ALA B 165 2347 2933 3578 419 199 -88 C ATOM 3563 C ALA B 165 15.010 8.745 12.952 1.00 28.49 C ANISOU 3563 C ALA B 165 3014 3574 4239 423 181 -99 C ATOM 3564 O ALA B 165 14.005 8.712 12.243 1.00 30.25 O ANISOU 3564 O ALA B 165 3233 3786 4474 427 175 -112 O ATOM 3565 CB ALA B 165 15.428 6.363 13.641 1.00 20.50 C ANISOU 3565 CB ALA B 165 1990 2565 3234 398 211 -71 C ATOM 3566 N LEU B 166 15.985 9.630 12.781 1.00 33.10 N ANISOU 3566 N LEU B 166 3610 4155 4812 424 170 -94 N ATOM 3567 CA LEU B 166 16.013 10.533 11.638 1.00 28.96 C ANISOU 3567 CA LEU B 166 3097 3614 4291 427 152 -102 C ATOM 3568 C LEU B 166 17.084 10.043 10.668 1.00 28.60 C ANISOU 3568 C LEU B 166 3063 3553 4249 406 151 -85 C ATOM 3569 O LEU B 166 18.252 9.902 11.043 1.00 24.65 O ANISOU 3569 O LEU B 166 2569 3058 3740 397 156 -68 O ATOM 3570 CB LEU B 166 16.265 11.983 12.077 1.00 24.66 C ANISOU 3570 CB LEU B 166 2560 3076 3734 443 140 -110 C ATOM 3571 CG LEU B 166 16.518 12.971 10.918 1.00 29.19 C ANISOU 3571 CG LEU B 166 3148 3632 4311 444 121 -116 C ATOM 3572 CD1 LEU B 166 15.349 12.974 9.938 1.00 30.22 C ANISOU 3572 CD1 LEU B 166 3277 3748 4457 446 113 -132 C ATOM 3573 CD2 LEU B 166 16.790 14.383 11.425 1.00 23.46 C ANISOU 3573 CD2 LEU B 166 2430 2911 3574 460 111 -123 C ATOM 3574 N TYR B 167 16.685 9.739 9.436 1.00 31.01 N ANISOU 3574 N TYR B 167 3371 3842 4568 399 144 -88 N ATOM 3575 CA TYR B 167 17.651 9.384 8.395 1.00 33.73 C ANISOU 3575 CA TYR B 167 3728 4171 4916 381 142 -72 C ATOM 3576 C TYR B 167 17.898 10.639 7.543 1.00 34.06 C ANISOU 3576 C TYR B 167 3782 4203 4955 387 122 -81 C ATOM 3577 O TYR B 167 17.345 10.830 6.458 1.00 29.97 O ANISOU 3577 O TYR B 167 3268 3672 4447 388 111 -91 O ATOM 3578 CB TYR B 167 17.170 8.168 7.577 1.00 30.28 C ANISOU 3578 CB TYR B 167 3287 3721 4496 367 149 -68 C ATOM 3579 CG TYR B 167 16.611 7.014 8.406 1.00 37.06 C ANISOU 3579 CG TYR B 167 4132 4589 5360 364 167 -64 C ATOM 3580 CD1 TYR B 167 17.448 6.216 9.193 1.00 34.56 C ANISOU 3580 CD1 TYR B 167 3815 4278 5038 352 183 -44 C ATOM 3581 CD2 TYR B 167 15.248 6.708 8.385 1.00 30.59 C ANISOU 3581 CD2 TYR B 167 3301 3771 4552 371 168 -81 C ATOM 3582 CE1 TYR B 167 16.935 5.171 9.951 1.00 27.60 C ANISOU 3582 CE1 TYR B 167 2922 3404 4162 350 199 -40 C ATOM 3583 CE2 TYR B 167 14.731 5.663 9.128 1.00 24.78 C ANISOU 3583 CE2 TYR B 167 2553 3042 3821 369 185 -77 C ATOM 3584 CZ TYR B 167 15.568 4.889 9.914 1.00 31.71 C ANISOU 3584 CZ TYR B 167 3430 3925 4693 358 200 -56 C ATOM 3585 OH TYR B 167 15.044 3.836 10.670 1.00 23.05 O ANISOU 3585 OH TYR B 167 2321 2835 3602 356 217 -52 O ATOM 3586 N GLY B 168 18.738 11.522 8.071 1.00 27.78 N ANISOU 3586 N GLY B 168 2995 3415 4147 393 117 -77 N ATOM 3587 CA GLY B 168 19.054 12.760 7.390 1.00 17.58 C ANISOU 3587 CA GLY B 168 1716 2113 2850 400 99 -84 C ATOM 3588 C GLY B 168 20.453 12.713 6.814 1.00 26.61 C ANISOU 3588 C GLY B 168 2872 3248 3990 384 97 -66 C ATOM 3589 O GLY B 168 20.851 11.696 6.233 1.00 18.95 O ANISOU 3589 O GLY B 168 1902 2270 3027 366 105 -51 O ATOM 3590 N SER B 169 21.208 13.808 6.951 1.00 21.62 N ANISOU 3590 N SER B 169 2251 2618 3348 390 86 -65 N ATOM 3591 CA SER B 169 22.602 13.776 6.523 1.00 30.19 C ANISOU 3591 CA SER B 169 3346 3695 4429 375 86 -47 C ATOM 3592 C SER B 169 23.412 12.759 7.337 1.00 24.56 C ANISOU 3592 C SER B 169 2629 2992 3713 361 104 -27 C ATOM 3593 O SER B 169 24.400 12.209 6.840 1.00 17.58 O ANISOU 3593 O SER B 169 1751 2098 2830 342 109 -7 O ATOM 3594 CB SER B 169 23.192 15.194 6.587 1.00 26.26 C ANISOU 3594 CB SER B 169 2860 3196 3920 386 71 -51 C ATOM 3595 OG SER B 169 23.148 15.710 7.909 1.00 39.63 O ANISOU 3595 OG SER B 169 4549 4907 5603 400 74 -57 O ATOM 3596 N ALA B 170 23.030 12.516 8.592 1.00 27.34 N ANISOU 3596 N ALA B 170 2969 3359 4058 369 115 -30 N ATOM 3597 CA ALA B 170 23.453 11.332 9.337 1.00 18.71 C ANISOU 3597 CA ALA B 170 1869 2274 2966 355 134 -13 C ATOM 3598 C ALA B 170 22.203 10.741 9.958 1.00 22.36 C ANISOU 3598 C ALA B 170 2316 2746 3433 364 143 -24 C ATOM 3599 O ALA B 170 21.124 11.322 9.836 1.00 26.17 O ANISOU 3599 O ALA B 170 2795 3231 3918 380 134 -44 O ATOM 3600 CB ALA B 170 24.512 11.641 10.402 1.00 27.21 C ANISOU 3600 CB ALA B 170 2947 3363 4028 355 138 -2 C ATOM 3601 N THR B 171 22.345 9.556 10.579 1.00 18.81 N ANISOU 3601 N THR B 171 1859 2301 2985 353 160 -10 N ATOM 3602 CA THR B 171 21.249 8.850 11.250 1.00 20.65 C ANISOU 3602 CA THR B 171 2078 2544 3223 359 171 -18 C ATOM 3603 C THR B 171 21.301 9.065 12.768 1.00 18.64 C ANISOU 3603 C THR B 171 1815 2312 2956 370 179 -20 C ATOM 3604 O THR B 171 22.326 8.811 13.413 1.00 18.77 O ANISOU 3604 O THR B 171 1834 2334 2964 362 187 -4 O ATOM 3605 CB THR B 171 21.293 7.358 10.930 1.00 18.94 C ANISOU 3605 CB THR B 171 1860 2318 3019 340 187 0 C ATOM 3606 OG1 THR B 171 21.011 7.171 9.540 1.00 24.23 O ANISOU 3606 OG1 THR B 171 2535 2969 3701 333 179 -2 O ATOM 3607 CG2 THR B 171 20.249 6.629 11.720 1.00 13.39 C ANISOU 3607 CG2 THR B 171 1142 1626 2321 346 199 -7 C ATOM 3608 N MET B 172 20.228 9.571 13.333 1.00 16.01 N ANISOU 3608 N MET B 172 1472 1991 2620 390 176 -40 N ATOM 3609 CA MET B 172 20.196 9.831 14.766 1.00 17.49 C ANISOU 3609 CA MET B 172 1650 2201 2794 402 183 -44 C ATOM 3610 C MET B 172 18.930 9.232 15.354 1.00 29.67 C ANISOU 3610 C MET B 172 3178 3755 4342 410 193 -55 C ATOM 3611 O MET B 172 17.848 9.333 14.765 1.00 29.54 O ANISOU 3611 O MET B 172 3157 3731 4335 418 188 -68 O ATOM 3612 CB MET B 172 20.274 11.343 15.058 1.00 15.93 C ANISOU 3612 CB MET B 172 1458 2012 2585 421 168 -58 C ATOM 3613 CG MET B 172 20.080 11.732 16.542 1.00 29.63 C ANISOU 3613 CG MET B 172 3182 3771 4305 437 174 -65 C ATOM 3614 SD MET B 172 20.378 13.483 17.000 1.00 27.39 S ANISOU 3614 SD MET B 172 2905 3496 4006 459 159 -76 S ATOM 3615 CE MET B 172 22.148 13.549 17.155 1.00 12.16 C ANISOU 3615 CE MET B 172 986 1567 2067 444 158 -58 C ATOM 3616 N LEU B 173 19.069 8.623 16.525 1.00 27.74 N ANISOU 3616 N LEU B 173 2924 3526 4092 409 207 -48 N ATOM 3617 CA LEU B 173 17.936 8.110 17.273 1.00 18.01 C ANISOU 3617 CA LEU B 173 1675 2307 2862 418 218 -58 C ATOM 3618 C LEU B 173 17.742 9.013 18.483 1.00 22.99 C ANISOU 3618 C LEU B 173 2298 2961 3476 439 216 -70 C ATOM 3619 O LEU B 173 18.688 9.255 19.243 1.00 20.29 O ANISOU 3619 O LEU B 173 1959 2631 3122 438 218 -62 O ATOM 3620 CB LEU B 173 18.154 6.657 17.689 1.00 22.24 C ANISOU 3620 CB LEU B 173 2205 2842 3403 402 237 -40 C ATOM 3621 CG LEU B 173 16.888 5.968 18.185 1.00 29.66 C ANISOU 3621 CG LEU B 173 3128 3790 4350 408 248 -50 C ATOM 3622 CD1 LEU B 173 16.736 4.599 17.558 1.00 33.73 C ANISOU 3622 CD1 LEU B 173 3645 4289 4883 390 258 -36 C ATOM 3623 CD2 LEU B 173 16.926 5.849 19.682 1.00 33.45 C ANISOU 3623 CD2 LEU B 173 3598 4295 4818 416 259 -50 C ATOM 3624 N VAL B 174 16.541 9.574 18.604 1.00 18.91 N ANISOU 3624 N VAL B 174 1774 2449 2961 457 212 -88 N ATOM 3625 CA VAL B 174 16.152 10.393 19.739 1.00 11.11 C ANISOU 3625 CA VAL B 174 778 1483 1959 478 213 -99 C ATOM 3626 C VAL B 174 15.224 9.553 20.612 1.00 19.45 C ANISOU 3626 C VAL B 174 1818 2555 3018 482 228 -103 C ATOM 3627 O VAL B 174 14.181 9.086 20.140 1.00 28.23 O ANISOU 3627 O VAL B 174 2924 3658 4144 482 231 -109 O ATOM 3628 CB VAL B 174 15.468 11.699 19.287 1.00 21.91 C ANISOU 3628 CB VAL B 174 2152 2843 3329 496 198 -114 C ATOM 3629 CG1 VAL B 174 14.944 12.449 20.471 1.00 15.96 C ANISOU 3629 CG1 VAL B 174 1391 2109 2565 516 202 -123 C ATOM 3630 CG2 VAL B 174 16.438 12.621 18.523 1.00 23.04 C ANISOU 3630 CG2 VAL B 174 2313 2972 3469 493 183 -110 C ATOM 3631 N LEU B 175 15.610 9.328 21.874 1.00 19.94 N ANISOU 3631 N LEU B 175 1871 2638 3067 484 239 -98 N ATOM 3632 CA LEU B 175 14.847 8.506 22.816 1.00 25.84 C ANISOU 3632 CA LEU B 175 2602 3402 3815 487 254 -101 C ATOM 3633 C LEU B 175 14.436 9.332 24.029 1.00 31.55 C ANISOU 3633 C LEU B 175 3315 4150 4522 510 256 -112 C ATOM 3634 O LEU B 175 15.291 9.844 24.768 1.00 26.52 O ANISOU 3634 O LEU B 175 2680 3527 3869 513 254 -109 O ATOM 3635 CB LEU B 175 15.646 7.280 23.279 1.00 25.85 C ANISOU 3635 CB LEU B 175 2600 3405 3817 467 269 -84 C ATOM 3636 CG LEU B 175 14.978 6.335 24.306 1.00 23.72 C ANISOU 3636 CG LEU B 175 2313 3151 3548 468 286 -85 C ATOM 3637 CD1 LEU B 175 13.690 5.685 23.812 1.00 25.77 C ANISOU 3637 CD1 LEU B 175 2565 3402 3824 469 292 -91 C ATOM 3638 CD2 LEU B 175 15.951 5.260 24.767 1.00 27.81 C ANISOU 3638 CD2 LEU B 175 2832 3667 4067 447 300 -65 C ATOM 3639 N ALA B 176 13.133 9.416 24.260 1.00 25.23 N ANISOU 3639 N ALA B 176 2505 3354 3727 524 260 -123 N ATOM 3640 CA ALA B 176 12.584 10.078 25.431 1.00 24.57 C ANISOU 3640 CA ALA B 176 2412 3293 3632 545 265 -131 C ATOM 3641 C ALA B 176 11.987 9.032 26.358 1.00 37.25 C ANISOU 3641 C ALA B 176 4000 4917 5237 544 282 -131 C ATOM 3642 O ALA B 176 11.248 8.147 25.913 1.00 33.66 O ANISOU 3642 O ALA B 176 3539 4453 4798 536 289 -133 O ATOM 3643 CB ALA B 176 11.507 11.098 25.059 1.00 20.30 C ANISOU 3643 CB ALA B 176 1874 2741 3100 561 258 -143 C ATOM 3644 N MET B 177 12.349 9.110 27.635 1.00 43.16 N ANISOU 3644 N MET B 177 4739 5691 5968 551 290 -131 N ATOM 3645 CA MET B 177 11.708 8.318 28.665 1.00 28.50 C ANISOU 3645 CA MET B 177 2865 3855 4110 554 305 -133 C ATOM 3646 C MET B 177 11.454 9.253 29.834 1.00 40.80 C ANISOU 3646 C MET B 177 4416 5437 5649 577 308 -139 C ATOM 3647 O MET B 177 11.633 10.472 29.733 1.00 43.20 O ANISOU 3647 O MET B 177 4730 5738 5947 590 299 -138 O ATOM 3648 CB MET B 177 12.543 7.096 29.077 1.00 34.94 C ANISOU 3648 CB MET B 177 3676 4673 4925 531 316 -124 C ATOM 3649 CG MET B 177 13.192 6.318 27.923 1.00 43.27 C ANISOU 3649 CG MET B 177 4743 5700 5997 507 314 -111 C ATOM 3650 SD MET B 177 13.910 4.737 28.466 1.00 42.67 S ANISOU 3650 SD MET B 177 4664 5621 5928 481 333 -92 S ATOM 3651 CE MET B 177 15.622 5.190 28.751 1.00 36.81 C ANISOU 3651 CE MET B 177 3934 4879 5174 471 327 -81 C ATOM 3652 N ASP B 178 11.043 8.669 30.958 1.00 49.53 N ANISOU 3652 N ASP B 178 5505 6566 6748 581 322 -142 N ATOM 3653 CA ASP B 178 10.756 9.468 32.138 1.00 50.42 C ANISOU 3653 CA ASP B 178 5617 6698 6844 597 325 -144 C ATOM 3654 C ASP B 178 11.974 10.266 32.589 1.00 40.47 C ANISOU 3654 C ASP B 178 4368 5444 5565 595 315 -140 C ATOM 3655 O ASP B 178 11.825 11.395 33.063 1.00 40.70 O ANISOU 3655 O ASP B 178 4404 5474 5585 611 314 -136 O ATOM 3656 CB ASP B 178 10.259 8.557 33.256 1.00 60.32 C ANISOU 3656 CB ASP B 178 6852 7973 8094 595 340 -148 C ATOM 3657 CG ASP B 178 9.845 9.326 34.478 1.00 68.14 C ANISOU 3657 CG ASP B 178 7841 8982 9068 612 345 -148 C ATOM 3658 OD1 ASP B 178 8.781 9.975 34.416 1.00 77.36 O ANISOU 3658 OD1 ASP B 178 9008 10141 10245 629 350 -145 O ATOM 3659 OD2 ASP B 178 10.579 9.291 35.486 1.00 68.54 O ANISOU 3659 OD2 ASP B 178 7889 9052 9100 607 345 -151 O ATOM 3660 N CYS B 179 13.183 9.712 32.415 1.00 36.30 N ANISOU 3660 N CYS B 179 3843 4914 5036 576 311 -140 N ATOM 3661 CA CYS B 179 14.444 10.353 32.799 1.00 35.65 C ANISOU 3661 CA CYS B 179 3770 4836 4939 570 301 -140 C ATOM 3662 C CYS B 179 14.861 11.533 31.909 1.00 48.45 C ANISOU 3662 C CYS B 179 5410 6440 6559 578 286 -133 C ATOM 3663 O CYS B 179 15.861 12.188 32.227 1.00 51.24 O ANISOU 3663 O CYS B 179 5772 6798 6899 576 278 -132 O ATOM 3664 CB CYS B 179 15.561 9.310 32.803 1.00 37.86 C ANISOU 3664 CB CYS B 179 4045 5112 5229 545 306 -138 C ATOM 3665 SG CYS B 179 15.831 8.485 31.185 1.00 46.29 S ANISOU 3665 SG CYS B 179 5121 6148 6320 527 305 -123 S ATOM 3666 N GLY B 180 14.154 11.818 30.802 1.00 41.63 N ANISOU 3666 N GLY B 180 4551 5555 5710 585 283 -130 N ATOM 3667 CA GLY B 180 14.493 12.930 29.931 1.00 37.66 C ANISOU 3667 CA GLY B 180 4065 5032 5211 591 270 -125 C ATOM 3668 C GLY B 180 14.651 12.497 28.476 1.00 32.46 C ANISOU 3668 C GLY B 180 3412 4352 4570 581 263 -125 C ATOM 3669 O GLY B 180 14.186 11.426 28.063 1.00 24.78 O ANISOU 3669 O GLY B 180 2432 3372 3609 568 268 -127 O ATOM 3670 N VAL B 181 15.254 13.382 27.674 1.00 30.53 N ANISOU 3670 N VAL B 181 3183 4089 4327 580 249 -122 N ATOM 3671 CA VAL B 181 15.455 13.175 26.238 1.00 34.19 C ANISOU 3671 CA VAL B 181 3659 4525 4806 565 239 -121 C ATOM 3672 C VAL B 181 16.950 13.059 25.979 1.00 35.35 C ANISOU 3672 C VAL B 181 3816 4669 4946 549 231 -113 C ATOM 3673 O VAL B 181 17.715 13.945 26.381 1.00 26.55 O ANISOU 3673 O VAL B 181 2708 3562 3818 556 225 -111 O ATOM 3674 CB VAL B 181 14.860 14.325 25.406 1.00 35.70 C ANISOU 3674 CB VAL B 181 3862 4693 5010 575 227 -127 C ATOM 3675 CG1 VAL B 181 15.020 14.044 23.922 1.00 27.80 C ANISOU 3675 CG1 VAL B 181 2873 3666 4024 559 216 -127 C ATOM 3676 CG2 VAL B 181 13.403 14.546 25.758 1.00 39.43 C ANISOU 3676 CG2 VAL B 181 4324 5163 5493 589 234 -137 C ATOM 3677 N ASN B 182 17.361 12.005 25.261 1.00 33.88 N ANISOU 3677 N ASN B 182 3632 4469 4771 526 233 -106 N ATOM 3678 CA ASN B 182 18.763 11.791 24.928 1.00 30.83 C ANISOU 3678 CA ASN B 182 3255 4074 4383 507 229 -95 C ATOM 3679 C ASN B 182 18.906 11.444 23.452 1.00 32.03 C ANISOU 3679 C ASN B 182 3420 4197 4552 491 223 -87 C ATOM 3680 O ASN B 182 18.053 10.741 22.894 1.00 28.52 O ANISOU 3680 O ASN B 182 2972 3743 4122 486 227 -88 O ATOM 3681 CB ASN B 182 19.356 10.684 25.776 1.00 33.00 C ANISOU 3681 CB ASN B 182 3521 4359 4657 490 243 -87 C ATOM 3682 CG ASN B 182 19.395 11.050 27.234 1.00 34.23 C ANISOU 3682 CG ASN B 182 3665 4544 4797 503 248 -96 C ATOM 3683 OD1 ASN B 182 20.290 11.764 27.686 1.00 34.53 O ANISOU 3683 OD1 ASN B 182 3708 4590 4823 506 241 -97 O ATOM 3684 ND2 ASN B 182 18.423 10.562 27.984 1.00 29.02 N ANISOU 3684 ND2 ASN B 182 2990 3900 4137 511 259 -103 N ATOM 3685 N CYS B 183 19.990 11.935 22.830 1.00 15.24 N ANISOU 3685 N CYS B 183 1309 2058 2425 482 212 -80 N ATOM 3686 CA CYS B 183 20.208 11.845 21.388 1.00 19.49 C ANISOU 3686 CA CYS B 183 1860 2570 2976 469 204 -73 C ATOM 3687 C CYS B 183 21.442 11.001 21.084 1.00 24.93 C ANISOU 3687 C CYS B 183 2557 3247 3670 444 210 -53 C ATOM 3688 O CYS B 183 22.542 11.299 21.570 1.00 23.18 O ANISOU 3688 O CYS B 183 2339 3031 3438 439 209 -46 O ATOM 3689 CB CYS B 183 20.361 13.234 20.762 1.00 17.13 C ANISOU 3689 CB CYS B 183 1575 2262 2674 482 186 -80 C ATOM 3690 SG CYS B 183 18.988 14.360 21.139 1.00 32.11 S ANISOU 3690 SG CYS B 183 3466 4165 4568 511 182 -98 S ATOM 3691 N PHE B 184 21.257 9.985 20.238 1.00 17.30 N ANISOU 3691 N PHE B 184 1592 2262 2718 428 216 -42 N ATOM 3692 CA PHE B 184 22.280 9.000 19.904 1.00 20.18 C ANISOU 3692 CA PHE B 184 1965 2614 3090 403 225 -18 C ATOM 3693 C PHE B 184 22.568 9.011 18.399 1.00 20.77 C ANISOU 3693 C PHE B 184 2054 2663 3176 391 216 -11 C ATOM 3694 O PHE B 184 21.658 8.855 17.573 1.00 27.72 O ANISOU 3694 O PHE B 184 2933 3533 4067 394 212 -19 O ATOM 3695 CB PHE B 184 21.817 7.592 20.319 1.00 25.26 C ANISOU 3695 CB PHE B 184 2598 3258 3741 393 243 -8 C ATOM 3696 CG PHE B 184 21.430 7.471 21.769 1.00 24.87 C ANISOU 3696 CG PHE B 184 2534 3233 3682 404 254 -16 C ATOM 3697 CD1 PHE B 184 22.319 6.943 22.703 1.00 25.26 C ANISOU 3697 CD1 PHE B 184 2583 3291 3725 394 266 1 C ATOM 3698 CD2 PHE B 184 20.169 7.872 22.197 1.00 20.04 C ANISOU 3698 CD2 PHE B 184 1909 2637 3068 424 252 -38 C ATOM 3699 CE1 PHE B 184 21.954 6.810 24.052 1.00 23.15 C ANISOU 3699 CE1 PHE B 184 2301 3046 3449 403 276 -7 C ATOM 3700 CE2 PHE B 184 19.800 7.762 23.530 1.00 23.34 C ANISOU 3700 CE2 PHE B 184 2313 3079 3477 433 261 -45 C ATOM 3701 CZ PHE B 184 20.697 7.228 24.467 1.00 21.19 C ANISOU 3701 CZ PHE B 184 2039 2815 3199 423 273 -30 C ATOM 3702 N MET B 185 23.835 9.130 18.044 1.00 24.98 N ANISOU 3702 N MET B 185 2599 3186 3706 378 213 5 N ATOM 3703 CA MET B 185 24.264 9.167 16.652 1.00 18.70 C ANISOU 3703 CA MET B 185 1817 2367 2919 366 205 14 C ATOM 3704 C MET B 185 24.761 7.782 16.218 1.00 18.80 C ANISOU 3704 C MET B 185 1835 2365 2943 343 219 40 C ATOM 3705 O MET B 185 25.709 7.242 16.802 1.00 23.06 O ANISOU 3705 O MET B 185 2378 2907 3478 331 230 61 O ATOM 3706 CB MET B 185 25.366 10.221 16.495 1.00 15.48 C ANISOU 3706 CB MET B 185 1422 1958 2503 366 193 16 C ATOM 3707 CG MET B 185 25.736 10.593 15.050 1.00 18.87 C ANISOU 3707 CG MET B 185 1865 2366 2939 358 180 20 C ATOM 3708 SD MET B 185 24.574 11.752 14.286 1.00 30.69 S ANISOU 3708 SD MET B 185 3363 3859 4440 380 161 -8 S ATOM 3709 CE MET B 185 25.185 13.307 14.917 1.00 30.08 C ANISOU 3709 CE MET B 185 3290 3793 4345 396 147 -17 C ATOM 3710 N LEU B 186 24.173 7.232 15.155 1.00 31.67 N ANISOU 3710 N LEU B 186 3468 3979 4588 336 218 40 N ATOM 3711 CA LEU B 186 24.655 5.958 14.618 1.00 21.91 C ANISOU 3711 CA LEU B 186 2238 2726 3362 315 231 65 C ATOM 3712 C LEU B 186 25.997 6.170 13.913 1.00 23.68 C ANISOU 3712 C LEU B 186 2478 2936 3583 301 226 85 C ATOM 3713 O LEU B 186 26.116 7.033 13.033 1.00 19.73 O ANISOU 3713 O LEU B 186 1984 2427 3083 303 211 76 O ATOM 3714 CB LEU B 186 23.644 5.346 13.652 1.00 14.70 C ANISOU 3714 CB LEU B 186 1321 1799 2464 313 230 59 C ATOM 3715 CG LEU B 186 24.112 4.051 12.958 1.00 19.03 C ANISOU 3715 CG LEU B 186 1878 2329 3024 292 242 85 C ATOM 3716 CD1 LEU B 186 24.423 2.887 13.954 1.00 21.20 C ANISOU 3716 CD1 LEU B 186 2150 2608 3297 284 261 106 C ATOM 3717 CD2 LEU B 186 23.132 3.600 11.892 1.00 18.31 C ANISOU 3717 CD2 LEU B 186 1784 2224 2949 290 239 75 C ATOM 3718 N ASP B 187 27.026 5.432 14.365 1.00 15.82 N ANISOU 3718 N ASP B 187 1489 1938 2583 287 239 112 N ATOM 3719 CA ASP B 187 28.348 5.338 13.759 1.00 18.28 C ANISOU 3719 CA ASP B 187 1816 2236 2894 271 239 136 C ATOM 3720 C ASP B 187 28.339 4.135 12.822 1.00 26.68 C ANISOU 3720 C ASP B 187 2887 3279 3971 255 247 155 C ATOM 3721 O ASP B 187 28.520 2.998 13.273 1.00 22.26 O ANISOU 3721 O ASP B 187 2327 2717 3412 247 263 175 O ATOM 3722 CB ASP B 187 29.415 5.185 14.845 1.00 26.66 C ANISOU 3722 CB ASP B 187 2881 3307 3943 267 249 155 C ATOM 3723 CG ASP B 187 30.837 5.195 14.305 1.00 27.36 C ANISOU 3723 CG ASP B 187 2986 3382 4027 251 248 181 C ATOM 3724 OD1 ASP B 187 31.041 4.919 13.102 1.00 23.25 O ANISOU 3724 OD1 ASP B 187 2475 2843 3516 240 245 190 O ATOM 3725 OD2 ASP B 187 31.767 5.426 15.121 1.00 24.56 O ANISOU 3725 OD2 ASP B 187 2634 3037 3660 251 251 192 O ATOM 3726 N PRO B 188 28.184 4.335 11.510 1.00 18.83 N ANISOU 3726 N PRO B 188 1899 2270 2987 250 238 150 N ATOM 3727 CA PRO B 188 28.009 3.179 10.618 1.00 18.88 C ANISOU 3727 CA PRO B 188 1910 2258 3007 236 245 164 C ATOM 3728 C PRO B 188 29.242 2.306 10.489 1.00 22.97 C ANISOU 3728 C PRO B 188 2441 2763 3523 219 256 200 C ATOM 3729 O PRO B 188 29.126 1.180 9.984 1.00 24.74 O ANISOU 3729 O PRO B 188 2670 2974 3757 208 265 215 O ATOM 3730 CB PRO B 188 27.638 3.819 9.271 1.00 21.54 C ANISOU 3730 CB PRO B 188 2249 2583 3350 236 230 149 C ATOM 3731 CG PRO B 188 28.098 5.215 9.342 1.00 22.05 C ANISOU 3731 CG PRO B 188 2317 2656 3404 245 216 137 C ATOM 3732 CD PRO B 188 28.126 5.619 10.805 1.00 17.41 C ANISOU 3732 CD PRO B 188 1721 2089 2804 257 219 131 C ATOM 3733 N ALA B 189 30.412 2.766 10.932 1.00 23.03 N ANISOU 3733 N ALA B 189 2457 2775 3518 215 256 214 N ATOM 3734 CA ALA B 189 31.599 1.918 10.870 1.00 24.09 C ANISOU 3734 CA ALA B 189 2605 2898 3649 200 266 248 C ATOM 3735 C ALA B 189 31.538 0.763 11.876 1.00 28.85 C ANISOU 3735 C ALA B 189 3205 3505 4250 201 282 265 C ATOM 3736 O ALA B 189 32.221 -0.254 11.694 1.00 34.18 O ANISOU 3736 O ALA B 189 3892 4167 4927 190 292 294 O ATOM 3737 CB ALA B 189 32.858 2.764 11.097 1.00 7.78 C ANISOU 3737 CB ALA B 189 549 837 1570 198 261 258 C ATOM 3738 N ILE B 190 30.760 0.885 12.948 1.00 17.39 N ANISOU 3738 N ILE B 190 1740 2071 2795 214 286 249 N ATOM 3739 CA ILE B 190 30.669 -0.195 13.923 1.00 26.50 C ANISOU 3739 CA ILE B 190 2891 3231 3948 214 301 264 C ATOM 3740 C ILE B 190 29.243 -0.606 14.224 1.00 27.42 C ANISOU 3740 C ILE B 190 2991 3353 4073 223 305 244 C ATOM 3741 O ILE B 190 29.039 -1.596 14.929 1.00 28.24 O ANISOU 3741 O ILE B 190 3092 3460 4180 224 318 256 O ATOM 3742 CB ILE B 190 31.420 0.148 15.224 1.00 14.42 C ANISOU 3742 CB ILE B 190 1359 1717 2400 220 305 272 C ATOM 3743 CG1 ILE B 190 30.916 1.463 15.831 1.00 14.93 C ANISOU 3743 CG1 ILE B 190 1412 1803 2459 234 295 241 C ATOM 3744 CG2 ILE B 190 32.930 0.214 14.941 1.00 17.79 C ANISOU 3744 CG2 ILE B 190 1804 2136 2819 209 303 298 C ATOM 3745 CD1 ILE B 190 31.561 1.798 17.223 1.00 18.61 C ANISOU 3745 CD1 ILE B 190 1874 2289 2907 240 299 245 C ATOM 3746 N GLY B 191 28.244 0.080 13.660 1.00 24.88 N ANISOU 3746 N GLY B 191 2661 3033 3760 231 295 215 N ATOM 3747 CA GLY B 191 26.860 -0.290 13.911 1.00 15.77 C ANISOU 3747 CA GLY B 191 1491 1885 2614 240 298 196 C ATOM 3748 C GLY B 191 26.529 -0.158 15.375 1.00 23.24 C ANISOU 3748 C GLY B 191 2425 2854 3551 252 305 188 C ATOM 3749 O GLY B 191 26.043 -1.106 16.001 1.00 31.06 O ANISOU 3749 O GLY B 191 3409 3847 4545 253 318 194 O ATOM 3750 N GLU B 192 26.874 0.999 15.944 1.00 24.30 N ANISOU 3750 N GLU B 192 2557 3003 3671 261 297 176 N ATOM 3751 CA GLU B 192 26.595 1.336 17.329 1.00 23.29 C ANISOU 3751 CA GLU B 192 2417 2899 3533 274 301 164 C ATOM 3752 C GLU B 192 26.014 2.748 17.399 1.00 18.73 C ANISOU 3752 C GLU B 192 1830 2335 2949 290 285 132 C ATOM 3753 O GLU B 192 26.445 3.633 16.660 1.00 24.66 O ANISOU 3753 O GLU B 192 2590 3081 3699 289 272 127 O ATOM 3754 CB GLU B 192 27.895 1.212 18.145 1.00 30.17 C ANISOU 3754 CB GLU B 192 3297 3777 4391 268 308 188 C ATOM 3755 CG GLU B 192 27.704 0.960 19.600 1.00 28.22 C ANISOU 3755 CG GLU B 192 3038 3549 4134 276 318 188 C ATOM 3756 CD GLU B 192 27.029 -0.376 19.920 1.00 30.41 C ANISOU 3756 CD GLU B 192 3310 3824 4421 274 334 197 C ATOM 3757 OE1 GLU B 192 27.427 -1.453 19.405 1.00 25.53 O ANISOU 3757 OE1 GLU B 192 2702 3187 3810 262 341 223 O ATOM 3758 OE2 GLU B 192 26.067 -0.338 20.701 1.00 34.79 O ANISOU 3758 OE2 GLU B 192 3848 4394 4975 285 338 179 O ATOM 3759 N PHE B 193 25.030 2.959 18.276 1.00 19.87 N ANISOU 3759 N PHE B 193 1959 2499 3092 305 287 111 N ATOM 3760 CA PHE B 193 24.449 4.280 18.529 1.00 22.52 C ANISOU 3760 CA PHE B 193 2287 2851 3420 323 273 81 C ATOM 3761 C PHE B 193 25.186 4.970 19.682 1.00 26.57 C ANISOU 3761 C PHE B 193 2797 3382 3916 330 273 80 C ATOM 3762 O PHE B 193 25.192 4.456 20.802 1.00 41.71 O ANISOU 3762 O PHE B 193 4706 5313 5827 331 286 86 O ATOM 3763 CB PHE B 193 22.962 4.151 18.854 1.00 24.86 C ANISOU 3763 CB PHE B 193 2567 3158 3722 337 275 59 C ATOM 3764 CG PHE B 193 22.077 3.861 17.658 1.00 32.29 C ANISOU 3764 CG PHE B 193 3508 4083 4679 335 270 51 C ATOM 3765 CD1 PHE B 193 21.620 4.887 16.841 1.00 33.99 C ANISOU 3765 CD1 PHE B 193 3725 4294 4895 345 253 31 C ATOM 3766 CD2 PHE B 193 21.682 2.563 17.370 1.00 28.64 C ANISOU 3766 CD2 PHE B 193 3044 3608 4230 324 283 63 C ATOM 3767 CE1 PHE B 193 20.790 4.618 15.769 1.00 27.20 C ANISOU 3767 CE1 PHE B 193 2866 3420 4050 343 249 23 C ATOM 3768 CE2 PHE B 193 20.869 2.297 16.311 1.00 27.92 C ANISOU 3768 CE2 PHE B 193 2952 3503 4153 322 279 55 C ATOM 3769 CZ PHE B 193 20.418 3.331 15.507 1.00 29.04 C ANISOU 3769 CZ PHE B 193 3096 3642 4296 332 261 34 C ATOM 3770 N ILE B 194 25.827 6.111 19.405 1.00 26.17 N ANISOU 3770 N ILE B 194 2754 3332 3857 333 259 74 N ATOM 3771 CA ILE B 194 26.682 6.835 20.367 1.00 20.11 C ANISOU 3771 CA ILE B 194 1987 2580 3075 338 257 74 C ATOM 3772 C ILE B 194 25.918 8.017 20.977 1.00 26.09 C ANISOU 3772 C ILE B 194 2732 3357 3823 361 245 43 C ATOM 3773 O ILE B 194 25.293 8.808 20.257 1.00 26.89 O ANISOU 3773 O ILE B 194 2835 3455 3928 372 231 24 O ATOM 3774 CB ILE B 194 27.968 7.326 19.677 1.00 18.15 C ANISOU 3774 CB ILE B 194 1755 2318 2824 327 249 89 C ATOM 3775 CG1 ILE B 194 28.689 6.166 18.962 1.00 17.12 C ANISOU 3775 CG1 ILE B 194 1637 2167 2702 306 259 121 C ATOM 3776 CG2 ILE B 194 28.897 8.040 20.656 1.00 13.96 C ANISOU 3776 CG2 ILE B 194 1224 1803 2278 331 247 90 C ATOM 3777 CD1 ILE B 194 29.200 5.085 19.858 1.00 16.80 C ANISOU 3777 CD1 ILE B 194 1596 2130 2656 297 277 145 C ATOM 3778 N LEU B 195 25.977 8.155 22.302 1.00 27.75 N ANISOU 3778 N LEU B 195 2932 3588 4022 369 251 37 N ATOM 3779 CA LEU B 195 25.298 9.256 22.995 1.00 24.62 C ANISOU 3779 CA LEU B 195 2525 3214 3616 392 242 9 C ATOM 3780 C LEU B 195 26.010 10.596 22.744 1.00 21.03 C ANISOU 3780 C LEU B 195 2080 2759 3153 400 224 1 C ATOM 3781 O LEU B 195 27.204 10.722 23.014 1.00 24.02 O ANISOU 3781 O LEU B 195 2465 3136 3525 390 225 14 O ATOM 3782 CB LEU B 195 25.244 8.931 24.488 1.00 29.01 C ANISOU 3782 CB LEU B 195 3068 3792 4163 397 254 7 C ATOM 3783 CG LEU B 195 24.691 9.987 25.447 1.00 29.42 C ANISOU 3783 CG LEU B 195 3107 3869 4202 420 246 -20 C ATOM 3784 CD1 LEU B 195 23.282 10.301 25.071 1.00 10.52 C ANISOU 3784 CD1 LEU B 195 707 1479 1812 438 240 -40 C ATOM 3785 CD2 LEU B 195 24.731 9.441 26.866 1.00 21.01 C ANISOU 3785 CD2 LEU B 195 2029 2823 3130 420 261 -19 C ATOM 3786 N VAL B 196 25.322 11.593 22.188 1.00 23.70 N ANISOU 3786 N VAL B 196 2419 3096 3490 417 209 -19 N ATOM 3787 CA VAL B 196 26.005 12.839 21.846 1.00 23.65 C ANISOU 3787 CA VAL B 196 2424 3087 3477 424 192 -24 C ATOM 3788 C VAL B 196 25.370 14.088 22.453 1.00 29.08 C ANISOU 3788 C VAL B 196 3106 3792 4151 452 181 -47 C ATOM 3789 O VAL B 196 26.081 15.098 22.621 1.00 22.98 O ANISOU 3789 O VAL B 196 2340 3022 3368 459 171 -50 O ATOM 3790 CB VAL B 196 26.136 13.009 20.313 1.00 28.96 C ANISOU 3790 CB VAL B 196 3111 3734 4160 416 182 -18 C ATOM 3791 CG1 VAL B 196 26.941 11.869 19.733 1.00 20.63 C ANISOU 3791 CG1 VAL B 196 2063 2661 3114 389 193 8 C ATOM 3792 CG2 VAL B 196 24.767 13.159 19.634 1.00 18.30 C ANISOU 3792 CG2 VAL B 196 1759 2378 2818 429 176 -33 C ATOM 3793 N ASP B 197 24.097 14.055 22.854 1.00 24.07 N ANISOU 3793 N ASP B 197 2461 3170 3516 468 185 -60 N ATOM 3794 CA ASP B 197 23.439 15.198 23.487 1.00 21.38 C ANISOU 3794 CA ASP B 197 2115 2845 3162 495 178 -76 C ATOM 3795 C ASP B 197 22.621 14.651 24.657 1.00 29.84 C ANISOU 3795 C ASP B 197 3169 3940 4228 504 192 -83 C ATOM 3796 O ASP B 197 21.671 13.888 24.445 1.00 30.80 O ANISOU 3796 O ASP B 197 3284 4059 4360 502 200 -85 O ATOM 3797 CB ASP B 197 22.556 15.917 22.479 1.00 32.02 C ANISOU 3797 CB ASP B 197 3473 4176 4519 508 169 -81 C ATOM 3798 CG ASP B 197 23.364 16.612 21.417 1.00 47.08 C ANISOU 3798 CG ASP B 197 5397 6061 6428 501 154 -76 C ATOM 3799 OD1 ASP B 197 24.275 17.384 21.767 1.00 55.00 O ANISOU 3799 OD1 ASP B 197 6407 7069 7421 505 148 -74 O ATOM 3800 OD2 ASP B 197 23.128 16.339 20.219 1.00 54.30 O ANISOU 3800 OD2 ASP B 197 6320 6955 7358 491 150 -74 O ATOM 3801 N LYS B 198 23.003 15.001 25.890 1.00 21.55 N ANISOU 3801 N LYS B 198 2111 2913 3163 513 194 -89 N ATOM 3802 CA LYS B 198 22.384 14.433 27.090 1.00 27.80 C ANISOU 3802 CA LYS B 198 2885 3728 3949 519 207 -96 C ATOM 3803 C LYS B 198 21.329 15.370 27.669 1.00 30.58 C ANISOU 3803 C LYS B 198 3237 4092 4290 544 207 -103 C ATOM 3804 O LYS B 198 21.555 16.579 27.771 1.00 30.88 O ANISOU 3804 O LYS B 198 3286 4128 4319 556 199 -101 O ATOM 3805 CB LYS B 198 23.432 14.124 28.163 1.00 26.63 C ANISOU 3805 CB LYS B 198 2730 3594 3795 507 213 -96 C ATOM 3806 CG LYS B 198 24.515 13.133 27.745 1.00 33.48 C ANISOU 3806 CG LYS B 198 3605 4442 4676 476 221 -76 C ATOM 3807 CD LYS B 198 25.530 12.890 28.867 1.00 46.33 C ANISOU 3807 CD LYS B 198 5226 6078 6298 465 230 -70 C ATOM 3808 CE LYS B 198 26.709 12.039 28.395 1.00 59.31 C ANISOU 3808 CE LYS B 198 6882 7702 7951 437 238 -40 C ATOM 3809 NZ LYS B 198 27.654 12.753 27.471 1.00 66.02 N ANISOU 3809 NZ LYS B 198 7748 8535 8800 432 225 -32 N ATOM 3810 N ASP B 199 20.175 14.813 28.023 1.00 29.59 N ANISOU 3810 N ASP B 199 3100 3976 4169 551 217 -107 N ATOM 3811 CA ASP B 199 19.159 15.526 28.790 1.00 34.62 C ANISOU 3811 CA ASP B 199 3734 4622 4798 571 223 -109 C ATOM 3812 C ASP B 199 18.874 16.896 28.170 1.00 39.94 C ANISOU 3812 C ASP B 199 4422 5274 5480 586 216 -103 C ATOM 3813 O ASP B 199 19.070 17.950 28.784 1.00 41.00 O ANISOU 3813 O ASP B 199 4561 5407 5609 596 216 -98 O ATOM 3814 CB ASP B 199 19.563 15.646 30.255 1.00 38.26 C ANISOU 3814 CB ASP B 199 4189 5108 5239 573 228 -111 C ATOM 3815 CG ASP B 199 18.377 15.917 31.157 1.00 45.21 C ANISOU 3815 CG ASP B 199 5061 5999 6116 592 241 -108 C ATOM 3816 OD1 ASP B 199 17.224 15.861 30.672 1.00 45.32 O ANISOU 3816 OD1 ASP B 199 5072 6000 6147 600 247 -108 O ATOM 3817 OD2 ASP B 199 18.600 16.200 32.345 1.00 46.20 O ANISOU 3817 OD2 ASP B 199 5184 6144 6225 597 246 -106 O ATOM 3818 N VAL B 200 18.399 16.848 26.923 1.00 36.10 N ANISOU 3818 N VAL B 200 3939 4766 5012 585 210 -106 N ATOM 3819 CA VAL B 200 18.279 18.013 26.057 1.00 26.92 C ANISOU 3819 CA VAL B 200 2790 3577 3864 593 199 -108 C ATOM 3820 C VAL B 200 17.061 18.816 26.468 1.00 26.03 C ANISOU 3820 C VAL B 200 2672 3454 3765 608 203 -117 C ATOM 3821 O VAL B 200 16.052 18.254 26.900 1.00 25.89 O ANISOU 3821 O VAL B 200 2641 3444 3752 612 214 -123 O ATOM 3822 CB VAL B 200 18.169 17.534 24.590 1.00 28.85 C ANISOU 3822 CB VAL B 200 3042 3798 4123 577 189 -112 C ATOM 3823 CG1 VAL B 200 17.830 18.676 23.681 1.00 23.23 C ANISOU 3823 CG1 VAL B 200 2343 3056 3426 581 175 -120 C ATOM 3824 CG2 VAL B 200 19.462 16.865 24.160 1.00 26.53 C ANISOU 3824 CG2 VAL B 200 2753 3506 3820 559 184 -103 C ATOM 3825 N LYS B 201 17.158 20.143 26.348 1.00 35.04 N ANISOU 3825 N LYS B 201 3824 4575 4916 613 193 -124 N ATOM 3826 CA LYS B 201 16.065 21.073 26.628 1.00 32.25 C ANISOU 3826 CA LYS B 201 3467 4206 4579 623 190 -143 C ATOM 3827 C LYS B 201 15.962 22.100 25.503 1.00 34.21 C ANISOU 3827 C LYS B 201 3731 4424 4842 620 167 -159 C ATOM 3828 O LYS B 201 16.981 22.541 24.969 1.00 36.82 O ANISOU 3828 O LYS B 201 4076 4746 5169 614 156 -152 O ATOM 3829 CB LYS B 201 16.263 21.786 27.964 1.00 27.05 C ANISOU 3829 CB LYS B 201 2803 3557 3916 633 198 -141 C ATOM 3830 CG LYS B 201 16.421 20.847 29.146 1.00 29.47 C ANISOU 3830 CG LYS B 201 3094 3895 4207 638 221 -123 C ATOM 3831 CD LYS B 201 15.144 20.042 29.411 1.00 35.38 C ANISOU 3831 CD LYS B 201 3829 4653 4962 641 232 -130 C ATOM 3832 CE LYS B 201 15.368 18.990 30.509 1.00 30.31 C ANISOU 3832 CE LYS B 201 3177 4041 4299 637 249 -115 C ATOM 3833 NZ LYS B 201 14.195 18.083 30.713 1.00 32.42 N ANISOU 3833 NZ LYS B 201 3429 4318 4570 640 261 -121 N ATOM 3834 N ILE B 202 14.727 22.485 25.144 1.00 29.50 N ANISOU 3834 N ILE B 202 3133 3813 4262 624 158 -183 N ATOM 3835 CA ILE B 202 14.490 23.403 24.030 1.00 22.32 C ANISOU 3835 CA ILE B 202 2237 2876 3366 622 134 -202 C ATOM 3836 C ILE B 202 14.623 24.871 24.457 1.00 29.21 C ANISOU 3836 C ILE B 202 3118 3739 4241 630 119 -219 C ATOM 3837 O ILE B 202 14.411 25.229 25.626 1.00 28.89 O ANISOU 3837 O ILE B 202 3069 3710 4198 639 127 -224 O ATOM 3838 CB ILE B 202 13.103 23.121 23.421 1.00 30.62 C ANISOU 3838 CB ILE B 202 3284 3919 4432 622 129 -222 C ATOM 3839 CG1 ILE B 202 12.951 23.792 22.047 1.00 33.98 C ANISOU 3839 CG1 ILE B 202 3724 4318 4869 617 105 -238 C ATOM 3840 CG2 ILE B 202 12.007 23.594 24.358 1.00 28.88 C ANISOU 3840 CG2 ILE B 202 3052 3703 4218 634 131 -243 C ATOM 3841 CD1 ILE B 202 11.723 23.318 21.281 1.00 36.72 C ANISOU 3841 CD1 ILE B 202 4065 4657 5229 616 100 -253 C ATOM 3842 N LYS B 203 14.991 25.734 23.496 1.00 32.00 N ANISOU 3842 N LYS B 203 3488 4071 4599 626 97 -228 N ATOM 3843 CA LYS B 203 14.952 27.181 23.707 1.00 35.03 C ANISOU 3843 CA LYS B 203 3880 4442 4985 634 78 -250 C ATOM 3844 C LYS B 203 13.555 27.634 24.103 1.00 39.68 C ANISOU 3844 C LYS B 203 4462 5031 5584 644 71 -279 C ATOM 3845 O LYS B 203 12.557 27.186 23.535 1.00 48.26 O ANISOU 3845 O LYS B 203 5544 6114 6680 643 69 -290 O ATOM 3846 CB LYS B 203 15.307 27.955 22.437 1.00 38.28 C ANISOU 3846 CB LYS B 203 4311 4830 5402 629 53 -258 C ATOM 3847 CG LYS B 203 16.747 28.236 22.113 1.00 37.50 C ANISOU 3847 CG LYS B 203 4227 4727 5296 622 49 -240 C ATOM 3848 CD LYS B 203 16.763 28.928 20.739 1.00 34.97 C ANISOU 3848 CD LYS B 203 3923 4380 4983 617 24 -252 C ATOM 3849 CE LYS B 203 18.158 29.118 20.174 1.00 39.71 C ANISOU 3849 CE LYS B 203 4538 4973 5577 608 20 -233 C ATOM 3850 NZ LYS B 203 18.139 29.049 18.673 1.00 46.08 N ANISOU 3850 NZ LYS B 203 5356 5761 6390 600 5 -234 N ATOM 3851 N LYS B 204 13.500 28.586 25.039 1.00 37.53 N ANISOU 3851 N LYS B 204 4189 4762 5309 654 66 -293 N ATOM 3852 CA LYS B 204 12.233 29.170 25.460 1.00 34.51 C ANISOU 3852 CA LYS B 204 3800 4378 4933 664 56 -324 C ATOM 3853 C LYS B 204 11.540 29.904 24.314 1.00 36.48 C ANISOU 3853 C LYS B 204 4061 4606 5192 665 29 -349 C ATOM 3854 O LYS B 204 10.304 29.928 24.253 1.00 43.20 O ANISOU 3854 O LYS B 204 4906 5457 6052 671 24 -371 O ATOM 3855 CB LYS B 204 12.482 30.099 26.660 1.00 45.69 C ANISOU 3855 CB LYS B 204 5215 5802 6343 674 54 -334 C ATOM 3856 CG LYS B 204 11.240 30.670 27.345 1.00 45.21 C ANISOU 3856 CG LYS B 204 5146 5746 6286 686 47 -364 C ATOM 3857 CD LYS B 204 11.639 31.437 28.595 1.00 48.36 C ANISOU 3857 CD LYS B 204 5544 6155 6677 694 47 -370 C ATOM 3858 CE LYS B 204 10.450 32.097 29.292 1.00 48.69 C ANISOU 3858 CE LYS B 204 5578 6202 6721 707 39 -402 C ATOM 3859 NZ LYS B 204 9.965 33.309 28.568 1.00 50.32 N ANISOU 3859 NZ LYS B 204 5799 6390 6932 713 6 -432 N ATOM 3860 N LYS B 205 12.304 30.508 23.399 1.00 36.10 N ANISOU 3860 N LYS B 205 4031 4542 5144 660 11 -347 N ATOM 3861 CA LYS B 205 11.702 31.197 22.263 1.00 37.33 C ANISOU 3861 CA LYS B 205 4198 4676 5308 660 -15 -370 C ATOM 3862 C LYS B 205 12.653 31.200 21.062 1.00 32.17 C ANISOU 3862 C LYS B 205 3561 4008 4655 650 -24 -355 C ATOM 3863 O LYS B 205 13.854 31.451 21.195 1.00 24.24 O ANISOU 3863 O LYS B 205 2565 3002 3643 646 -23 -338 O ATOM 3864 CB LYS B 205 11.300 32.627 22.650 1.00 44.62 C ANISOU 3864 CB LYS B 205 5130 5594 6232 672 -38 -400 C ATOM 3865 CG LYS B 205 10.403 33.316 21.637 1.00 58.83 C ANISOU 3865 CG LYS B 205 6938 7376 8039 675 -65 -427 C ATOM 3866 CD LYS B 205 10.040 34.738 22.061 1.00 59.15 C ANISOU 3866 CD LYS B 205 6986 7411 8078 687 -89 -456 C ATOM 3867 CE LYS B 205 9.372 35.503 20.924 1.00 53.93 C ANISOU 3867 CE LYS B 205 6337 6730 7423 690 -119 -480 C ATOM 3868 NZ LYS B 205 8.959 36.867 21.327 1.00 55.22 N ANISOU 3868 NZ LYS B 205 6508 6889 7583 702 -143 -509 N ATOM 3869 N GLY B 206 12.094 30.965 19.878 1.00 28.36 N ANISOU 3869 N GLY B 206 3082 3512 4180 645 -34 -362 N ATOM 3870 CA GLY B 206 12.870 30.849 18.669 1.00 34.70 C ANISOU 3870 CA GLY B 206 3900 4301 4985 634 -42 -348 C ATOM 3871 C GLY B 206 12.611 31.980 17.691 1.00 36.49 C ANISOU 3871 C GLY B 206 4142 4506 5216 636 -73 -370 C ATOM 3872 O GLY B 206 11.999 33.000 18.016 1.00 38.86 O ANISOU 3872 O GLY B 206 4446 4802 5518 647 -90 -395 O ATOM 3873 N LYS B 207 13.118 31.784 16.466 1.00 41.16 N ANISOU 3873 N LYS B 207 4746 5084 5810 627 -80 -359 N ATOM 3874 CA LYS B 207 13.074 32.791 15.408 1.00 42.30 C ANISOU 3874 CA LYS B 207 4907 5207 5958 627 -108 -374 C ATOM 3875 C LYS B 207 12.665 32.180 14.069 1.00 40.56 C ANISOU 3875 C LYS B 207 4689 4977 5746 619 -113 -373 C ATOM 3876 O LYS B 207 12.918 32.783 13.015 1.00 39.83 O ANISOU 3876 O LYS B 207 4611 4867 5654 616 -133 -377 O ATOM 3877 CB LYS B 207 14.444 33.463 15.254 1.00 38.68 C ANISOU 3877 CB LYS B 207 4466 4740 5492 623 -115 -360 C ATOM 3878 CG LYS B 207 14.899 34.259 16.463 1.00 60.36 C ANISOU 3878 CG LYS B 207 7212 7492 8230 631 -116 -364 C ATOM 3879 CD LYS B 207 16.381 34.621 16.363 1.00 66.73 C ANISOU 3879 CD LYS B 207 8032 8292 9029 624 -117 -344 C ATOM 3880 CE LYS B 207 16.835 35.374 17.607 1.00 69.84 C ANISOU 3880 CE LYS B 207 8426 8694 9415 632 -116 -348 C ATOM 3881 NZ LYS B 207 18.319 35.524 17.683 1.00 68.68 N ANISOU 3881 NZ LYS B 207 8289 8545 9261 626 -112 -326 N ATOM 3882 N ILE B 208 12.029 31.011 14.097 1.00 34.88 N ANISOU 3882 N ILE B 208 3954 4268 5031 616 -95 -368 N ATOM 3883 CA ILE B 208 11.668 30.246 12.914 1.00 30.21 C ANISOU 3883 CA ILE B 208 3361 3669 4447 607 -96 -364 C ATOM 3884 C ILE B 208 10.255 29.712 13.113 1.00 34.95 C ANISOU 3884 C ILE B 208 3946 4278 5057 612 -91 -382 C ATOM 3885 O ILE B 208 9.915 29.249 14.208 1.00 31.30 O ANISOU 3885 O ILE B 208 3468 3831 4592 617 -73 -380 O ATOM 3886 CB ILE B 208 12.671 29.099 12.685 1.00 34.65 C ANISOU 3886 CB ILE B 208 3922 4238 5006 594 -75 -332 C ATOM 3887 CG1 ILE B 208 14.075 29.668 12.437 1.00 41.16 C ANISOU 3887 CG1 ILE B 208 4763 5054 5822 589 -80 -316 C ATOM 3888 CG2 ILE B 208 12.246 28.205 11.530 1.00 33.58 C ANISOU 3888 CG2 ILE B 208 3785 4097 4879 585 -74 -329 C ATOM 3889 CD1 ILE B 208 15.169 28.629 12.448 1.00 44.22 C ANISOU 3889 CD1 ILE B 208 5149 5451 6203 578 -59 -284 C ATOM 3890 N TYR B 209 9.411 29.838 12.082 1.00 28.14 N ANISOU 3890 N TYR B 209 3085 3402 4202 613 -108 -399 N ATOM 3891 CA TYR B 209 8.113 29.181 12.053 1.00 26.03 C ANISOU 3891 CA TYR B 209 2803 3141 3945 615 -103 -414 C ATOM 3892 C TYR B 209 8.071 28.238 10.859 1.00 27.62 C ANISOU 3892 C TYR B 209 3004 3337 4154 604 -100 -403 C ATOM 3893 O TYR B 209 8.744 28.466 9.851 1.00 36.95 O ANISOU 3893 O TYR B 209 4200 4505 5334 597 -111 -395 O ATOM 3894 CB TYR B 209 6.943 30.184 12.005 1.00 26.65 C ANISOU 3894 CB TYR B 209 2882 3214 4028 627 -127 -448 C ATOM 3895 CG TYR B 209 6.805 30.917 10.698 1.00 33.68 C ANISOU 3895 CG TYR B 209 3788 4086 4923 627 -154 -462 C ATOM 3896 CD1 TYR B 209 7.531 32.080 10.448 1.00 34.53 C ANISOU 3896 CD1 TYR B 209 3914 4182 5024 630 -174 -464 C ATOM 3897 CD2 TYR B 209 5.989 30.415 9.674 1.00 29.57 C ANISOU 3897 CD2 TYR B 209 3264 3559 4412 624 -161 -471 C ATOM 3898 CE1 TYR B 209 7.422 32.755 9.218 1.00 25.88 C ANISOU 3898 CE1 TYR B 209 2833 3069 3930 629 -200 -475 C ATOM 3899 CE2 TYR B 209 5.881 31.080 8.456 1.00 31.23 C ANISOU 3899 CE2 TYR B 209 3489 3754 4626 624 -186 -482 C ATOM 3900 CZ TYR B 209 6.599 32.244 8.238 1.00 28.44 C ANISOU 3900 CZ TYR B 209 3153 3389 4264 627 -205 -484 C ATOM 3901 OH TYR B 209 6.490 32.889 7.032 1.00 28.33 O ANISOU 3901 OH TYR B 209 3153 3359 4252 627 -231 -495 O ATOM 3902 N SER B 210 7.275 27.172 10.974 1.00 28.36 N ANISOU 3902 N SER B 210 3081 3439 4254 602 -85 -403 N ATOM 3903 CA SER B 210 7.342 26.041 10.051 1.00 28.64 C ANISOU 3903 CA SER B 210 3114 3472 4295 590 -76 -389 C ATOM 3904 C SER B 210 5.947 25.510 9.757 1.00 30.87 C ANISOU 3904 C SER B 210 3383 3755 4590 592 -77 -408 C ATOM 3905 O SER B 210 5.332 24.866 10.616 1.00 25.96 O ANISOU 3905 O SER B 210 2745 3147 3971 595 -60 -410 O ATOM 3906 CB SER B 210 8.224 24.931 10.637 1.00 29.89 C ANISOU 3906 CB SER B 210 3266 3644 4447 581 -48 -359 C ATOM 3907 OG SER B 210 8.380 23.828 9.756 1.00 32.69 O ANISOU 3907 OG SER B 210 3618 3996 4806 569 -40 -344 O ATOM 3908 N LEU B 211 5.472 25.723 8.532 1.00 32.96 N ANISOU 3908 N LEU B 211 3655 4007 4863 590 -96 -422 N ATOM 3909 CA LEU B 211 4.201 25.146 8.104 1.00 31.44 C ANISOU 3909 CA LEU B 211 3450 3814 4683 591 -98 -439 C ATOM 3910 C LEU B 211 4.095 25.316 6.600 1.00 30.37 C ANISOU 3910 C LEU B 211 3325 3663 4554 586 -117 -446 C ATOM 3911 O LEU B 211 4.867 26.057 5.996 1.00 30.62 O ANISOU 3911 O LEU B 211 3373 3683 4579 584 -132 -441 O ATOM 3912 CB LEU B 211 2.996 25.794 8.794 1.00 38.32 C ANISOU 3912 CB LEU B 211 4312 4689 5557 604 -107 -468 C ATOM 3913 CG LEU B 211 2.434 27.083 8.193 1.00 37.40 C ANISOU 3913 CG LEU B 211 4207 4561 5443 613 -139 -496 C ATOM 3914 CD1 LEU B 211 1.175 27.449 8.935 1.00 34.64 C ANISOU 3914 CD1 LEU B 211 3844 4218 5098 626 -144 -524 C ATOM 3915 CD2 LEU B 211 3.442 28.206 8.295 1.00 38.76 C ANISOU 3915 CD2 LEU B 211 4396 4726 5604 616 -151 -491 C ATOM 3916 N ASN B 212 3.133 24.602 6.004 1.00 33.10 N ANISOU 3916 N ASN B 212 3660 4007 4911 583 -117 -456 N ATOM 3917 CA ASN B 212 2.836 24.658 4.569 1.00 41.85 C ANISOU 3917 CA ASN B 212 4774 5101 6025 579 -136 -465 C ATOM 3918 C ASN B 212 1.960 25.881 4.269 1.00 46.90 C ANISOU 3918 C ASN B 212 5419 5733 6667 592 -165 -497 C ATOM 3919 O ASN B 212 0.728 25.817 4.305 1.00 47.76 O ANISOU 3919 O ASN B 212 5517 5845 6785 598 -170 -520 O ATOM 3920 CB ASN B 212 2.152 23.361 4.136 1.00 41.15 C ANISOU 3920 CB ASN B 212 4671 5015 5948 572 -123 -464 C ATOM 3921 CG ASN B 212 1.898 23.280 2.624 1.00 42.66 C ANISOU 3921 CG ASN B 212 4869 5193 6147 567 -140 -471 C ATOM 3922 OD1 ASN B 212 2.021 24.267 1.888 1.00 37.20 O ANISOU 3922 OD1 ASN B 212 4192 4491 5453 571 -164 -482 O ATOM 3923 ND2 ASN B 212 1.560 22.079 2.158 1.00 38.29 N ANISOU 3923 ND2 ASN B 212 4305 4641 5603 558 -128 -465 N ATOM 3924 N GLU B 213 2.595 27.002 3.903 1.00 48.26 N ANISOU 3924 N GLU B 213 5610 5896 6832 596 -184 -499 N ATOM 3925 CA GLU B 213 1.824 28.217 3.632 1.00 55.87 C ANISOU 3925 CA GLU B 213 6581 6853 7796 608 -213 -528 C ATOM 3926 C GLU B 213 1.088 28.192 2.302 1.00 55.28 C ANISOU 3926 C GLU B 213 6508 6768 7730 608 -232 -544 C ATOM 3927 O GLU B 213 0.289 29.096 2.048 1.00 59.13 O ANISOU 3927 O GLU B 213 6998 7250 8217 618 -256 -570 O ATOM 3928 CB GLU B 213 2.707 29.476 3.654 1.00 55.73 C ANISOU 3928 CB GLU B 213 6582 6826 7767 612 -229 -526 C ATOM 3929 CG GLU B 213 3.226 29.874 5.030 1.00 59.33 C ANISOU 3929 CG GLU B 213 7037 7292 8214 617 -218 -520 C ATOM 3930 CD GLU B 213 3.691 31.320 5.095 1.00 59.34 C ANISOU 3930 CD GLU B 213 7056 7284 8207 625 -240 -528 C ATOM 3931 OE1 GLU B 213 2.867 32.228 4.836 1.00 60.44 O ANISOU 3931 OE1 GLU B 213 7200 7418 8348 636 -265 -555 O ATOM 3932 OE2 GLU B 213 4.889 31.543 5.375 1.00 53.24 O ANISOU 3932 OE2 GLU B 213 6294 6511 7426 621 -234 -508 O ATOM 3933 N GLY B 214 1.311 27.188 1.456 1.00 50.73 N ANISOU 3933 N GLY B 214 5929 6189 7159 596 -222 -529 N ATOM 3934 CA GLY B 214 0.581 27.153 0.207 1.00 46.39 C ANISOU 3934 CA GLY B 214 5380 5629 6616 596 -241 -545 C ATOM 3935 C GLY B 214 -0.904 26.948 0.379 1.00 47.08 C ANISOU 3935 C GLY B 214 5452 5722 6714 603 -245 -571 C ATOM 3936 O GLY B 214 -1.674 27.283 -0.527 1.00 56.95 O ANISOU 3936 O GLY B 214 6704 6966 7970 608 -267 -592 O ATOM 3937 N TYR B 215 -1.326 26.439 1.533 1.00 41.72 N ANISOU 3937 N TYR B 215 4758 5057 6039 605 -226 -572 N ATOM 3938 CA TYR B 215 -2.736 26.246 1.848 1.00 47.60 C ANISOU 3938 CA TYR B 215 5486 5807 6793 612 -228 -598 C ATOM 3939 C TYR B 215 -3.291 27.373 2.729 1.00 49.71 C ANISOU 3939 C TYR B 215 5753 6079 7056 627 -241 -620 C ATOM 3940 O TYR B 215 -4.221 27.151 3.514 1.00 53.55 O ANISOU 3940 O TYR B 215 6224 6575 7548 633 -234 -635 O ATOM 3941 CB TYR B 215 -2.919 24.864 2.480 1.00 57.02 C ANISOU 3941 CB TYR B 215 6660 7011 7993 604 -198 -584 C ATOM 3942 CG TYR B 215 -2.567 23.778 1.472 1.00 68.81 C ANISOU 3942 CG TYR B 215 8153 8499 9492 590 -189 -567 C ATOM 3943 CD1 TYR B 215 -2.509 24.089 0.110 1.00 77.76 C ANISOU 3943 CD1 TYR B 215 9297 9620 10627 588 -209 -572 C ATOM 3944 CD2 TYR B 215 -2.234 22.477 1.861 1.00 67.17 C ANISOU 3944 CD2 TYR B 215 7935 8299 9289 580 -160 -545 C ATOM 3945 CE1 TYR B 215 -2.168 23.152 -0.845 1.00 75.18 C ANISOU 3945 CE1 TYR B 215 8971 9288 10305 576 -203 -557 C ATOM 3946 CE2 TYR B 215 -1.882 21.515 0.897 1.00 69.57 C ANISOU 3946 CE2 TYR B 215 8239 8597 9598 567 -153 -529 C ATOM 3947 CZ TYR B 215 -1.852 21.875 -0.464 1.00 71.85 C ANISOU 3947 CZ TYR B 215 8538 8873 9888 565 -175 -536 C ATOM 3948 OH TYR B 215 -1.519 20.991 -1.475 1.00 65.81 O ANISOU 3948 OH TYR B 215 7774 8102 9127 553 -170 -523 O ATOM 3949 N ALA B 216 -2.723 28.585 2.607 1.00 39.38 N ANISOU 3949 N ALA B 216 4463 4764 5738 633 -261 -623 N ATOM 3950 CA ALA B 216 -3.129 29.722 3.437 1.00 36.07 C ANISOU 3950 CA ALA B 216 4045 4348 5313 647 -275 -644 C ATOM 3951 C ALA B 216 -4.575 30.126 3.192 1.00 39.84 C ANISOU 3951 C ALA B 216 4514 4825 5797 658 -295 -678 C ATOM 3952 O ALA B 216 -5.218 30.683 4.089 1.00 42.61 O ANISOU 3952 O ALA B 216 4859 5183 6147 668 -299 -696 O ATOM 3953 CB ALA B 216 -2.217 30.925 3.191 1.00 25.68 C ANISOU 3953 CB ALA B 216 2751 3021 3985 651 -293 -640 C ATOM 3954 N LYS B 217 -5.090 29.888 1.980 1.00 35.53 N ANISOU 3954 N LYS B 217 3970 4271 5259 656 -309 -687 N ATOM 3955 CA LYS B 217 -6.491 30.165 1.679 1.00 37.81 C ANISOU 3955 CA LYS B 217 4249 4561 5555 665 -328 -719 C ATOM 3956 C LYS B 217 -7.427 29.410 2.614 1.00 37.50 C ANISOU 3956 C LYS B 217 4188 4535 5525 667 -309 -728 C ATOM 3957 O LYS B 217 -8.565 29.841 2.812 1.00 42.62 O ANISOU 3957 O LYS B 217 4828 5187 6178 677 -323 -757 O ATOM 3958 CB LYS B 217 -6.797 29.783 0.229 1.00 48.11 C ANISOU 3958 CB LYS B 217 5556 5856 6866 660 -340 -723 C ATOM 3959 CG LYS B 217 -8.172 30.164 -0.291 1.00 47.51 C ANISOU 3959 CG LYS B 217 5475 5780 6798 671 -364 -756 C ATOM 3960 CD LYS B 217 -8.310 29.789 -1.774 1.00 45.84 C ANISOU 3960 CD LYS B 217 5267 5559 6593 665 -376 -757 C ATOM 3961 CE LYS B 217 -8.312 28.271 -1.963 1.00 43.83 C ANISOU 3961 CE LYS B 217 4998 5308 6349 652 -350 -741 C ATOM 3962 NZ LYS B 217 -8.415 27.886 -3.386 1.00 41.25 N ANISOU 3962 NZ LYS B 217 4675 4972 6027 646 -362 -742 N ATOM 3963 N ASP B 218 -6.978 28.294 3.187 1.00 33.56 N ANISOU 3963 N ASP B 218 3678 4043 5028 656 -278 -705 N ATOM 3964 CA ASP B 218 -7.785 27.476 4.082 1.00 36.68 C ANISOU 3964 CA ASP B 218 4053 4451 5432 656 -258 -711 C ATOM 3965 C ASP B 218 -7.492 27.759 5.545 1.00 45.14 C ANISOU 3965 C ASP B 218 5121 5534 6497 662 -243 -705 C ATOM 3966 O ASP B 218 -8.075 27.105 6.409 1.00 52.04 O ANISOU 3966 O ASP B 218 5978 6419 7376 662 -224 -708 O ATOM 3967 CB ASP B 218 -7.548 25.982 3.816 1.00 46.49 C ANISOU 3967 CB ASP B 218 5286 5696 6683 642 -232 -689 C ATOM 3968 CG ASP B 218 -8.024 25.526 2.431 1.00 59.08 C ANISOU 3968 CG ASP B 218 6879 7280 8287 637 -244 -696 C ATOM 3969 OD1 ASP B 218 -8.794 26.259 1.774 1.00 61.82 O ANISOU 3969 OD1 ASP B 218 7229 7622 8636 645 -271 -722 O ATOM 3970 OD2 ASP B 218 -7.602 24.431 1.989 1.00 61.21 O ANISOU 3970 OD2 ASP B 218 7146 7549 8562 624 -227 -676 O ATOM 3971 N PHE B 219 -6.612 28.718 5.843 1.00 45.24 N ANISOU 3971 N PHE B 219 5149 5543 6497 666 -251 -698 N ATOM 3972 CA PHE B 219 -6.174 28.942 7.217 1.00 43.48 C ANISOU 3972 CA PHE B 219 4923 5331 6265 669 -236 -690 C ATOM 3973 C PHE B 219 -7.316 29.330 8.145 1.00 46.97 C ANISOU 3973 C PHE B 219 5352 5783 6710 682 -239 -717 C ATOM 3974 O PHE B 219 -8.210 30.095 7.782 1.00 50.36 O ANISOU 3974 O PHE B 219 5783 6209 7142 692 -264 -745 O ATOM 3975 CB PHE B 219 -5.105 30.036 7.272 1.00 38.64 C ANISOU 3975 CB PHE B 219 4331 4711 5639 672 -249 -682 C ATOM 3976 CG PHE B 219 -3.725 29.553 6.959 1.00 34.84 C ANISOU 3976 CG PHE B 219 3860 4225 5153 660 -234 -649 C ATOM 3977 CD1 PHE B 219 -3.480 28.195 6.748 1.00 32.28 C ANISOU 3977 CD1 PHE B 219 3526 3904 4834 647 -210 -627 C ATOM 3978 CD2 PHE B 219 -2.656 30.438 6.959 1.00 36.06 C ANISOU 3978 CD2 PHE B 219 4033 4374 5296 661 -244 -639 C ATOM 3979 CE1 PHE B 219 -2.198 27.738 6.473 1.00 31.53 C ANISOU 3979 CE1 PHE B 219 3440 3806 4734 636 -197 -597 C ATOM 3980 CE2 PHE B 219 -1.358 29.992 6.702 1.00 46.11 C ANISOU 3980 CE2 PHE B 219 5315 5643 6564 649 -230 -608 C ATOM 3981 CZ PHE B 219 -1.128 28.638 6.455 1.00 37.55 C ANISOU 3981 CZ PHE B 219 4221 4562 5485 637 -207 -587 C ATOM 3982 N ASP B 220 -7.249 28.827 9.372 1.00 51.74 N ANISOU 3982 N ASP B 220 5944 6400 7312 682 -214 -707 N ATOM 3983 CA ASP B 220 -8.068 29.358 10.445 1.00 55.68 C ANISOU 3983 CA ASP B 220 6434 6911 7811 694 -216 -729 C ATOM 3984 C ASP B 220 -7.674 30.819 10.676 1.00 55.54 C ANISOU 3984 C ASP B 220 6432 6889 7782 704 -239 -740 C ATOM 3985 O ASP B 220 -6.506 31.183 10.503 1.00 56.23 O ANISOU 3985 O ASP B 220 6535 6969 7860 700 -241 -721 O ATOM 3986 CB ASP B 220 -7.853 28.517 11.705 1.00 62.44 C ANISOU 3986 CB ASP B 220 7276 7782 8665 691 -183 -711 C ATOM 3987 CG ASP B 220 -8.791 28.879 12.832 1.00 72.42 C ANISOU 3987 CG ASP B 220 8527 9059 9930 703 -182 -733 C ATOM 3988 OD1 ASP B 220 -9.832 28.203 12.978 1.00 76.14 O ANISOU 3988 OD1 ASP B 220 8982 9537 10412 704 -173 -744 O ATOM 3989 OD2 ASP B 220 -8.486 29.831 13.578 1.00 76.38 O ANISOU 3989 OD2 ASP B 220 9035 9564 10421 712 -189 -738 O ATOM 3990 N PRO B 221 -8.622 31.683 11.054 1.00 47.38 N ANISOU 3990 N PRO B 221 5395 5858 6748 718 -257 -770 N ATOM 3991 CA PRO B 221 -8.281 33.108 11.209 1.00 43.60 C ANISOU 3991 CA PRO B 221 4933 5375 6259 728 -281 -782 C ATOM 3992 C PRO B 221 -7.159 33.359 12.188 1.00 40.76 C ANISOU 3992 C PRO B 221 4579 5020 5887 727 -267 -762 C ATOM 3993 O PRO B 221 -6.383 34.304 11.991 1.00 32.72 O ANISOU 3993 O PRO B 221 3579 3993 4860 729 -283 -759 O ATOM 3994 CB PRO B 221 -9.592 33.731 11.702 1.00 45.28 C ANISOU 3994 CB PRO B 221 5136 5595 6475 742 -297 -816 C ATOM 3995 CG PRO B 221 -10.634 32.844 11.198 1.00 50.13 C ANISOU 3995 CG PRO B 221 5734 6211 7102 738 -292 -826 C ATOM 3996 CD PRO B 221 -10.066 31.448 11.198 1.00 47.99 C ANISOU 3996 CD PRO B 221 5455 5942 6835 724 -260 -796 C ATOM 3997 N ALA B 222 -7.053 32.534 13.241 1.00 41.20 N ANISOU 3997 N ALA B 222 4621 5090 5944 724 -237 -747 N ATOM 3998 CA ALA B 222 -5.985 32.703 14.222 1.00 42.71 C ANISOU 3998 CA ALA B 222 4817 5287 6124 723 -222 -727 C ATOM 3999 C ALA B 222 -4.636 32.304 13.635 1.00 42.52 C ANISOU 3999 C ALA B 222 4805 5255 6095 710 -213 -696 C ATOM 4000 O ALA B 222 -3.623 32.976 13.881 1.00 36.54 O ANISOU 4000 O ALA B 222 4062 4494 5328 711 -217 -685 O ATOM 4001 CB ALA B 222 -6.293 31.896 15.483 1.00 42.46 C ANISOU 4001 CB ALA B 222 4766 5274 6093 724 -193 -721 C ATOM 4002 N VAL B 223 -4.611 31.232 12.834 1.00 35.01 N ANISOU 4002 N VAL B 223 3850 4300 5152 699 -202 -681 N ATOM 4003 CA VAL B 223 -3.390 30.855 12.128 1.00 37.09 C ANISOU 4003 CA VAL B 223 4125 4554 5412 687 -196 -653 C ATOM 4004 C VAL B 223 -2.978 31.976 11.183 1.00 46.27 C ANISOU 4004 C VAL B 223 5309 5701 6570 690 -225 -661 C ATOM 4005 O VAL B 223 -1.795 32.331 11.096 1.00 50.89 O ANISOU 4005 O VAL B 223 5908 6280 7147 685 -226 -643 O ATOM 4006 CB VAL B 223 -3.591 29.513 11.388 1.00 37.32 C ANISOU 4006 CB VAL B 223 4145 4583 5451 675 -180 -639 C ATOM 4007 CG1 VAL B 223 -2.408 29.175 10.443 1.00 29.39 C ANISOU 4007 CG1 VAL B 223 3154 3567 4444 663 -178 -613 C ATOM 4008 CG2 VAL B 223 -3.811 28.378 12.393 1.00 36.33 C ANISOU 4008 CG2 VAL B 223 4001 4474 5330 672 -148 -627 C ATOM 4009 N THR B 224 -3.949 32.571 10.480 1.00 46.96 N ANISOU 4009 N THR B 224 5398 5781 6663 697 -251 -688 N ATOM 4010 CA THR B 224 -3.639 33.720 9.632 1.00 43.19 C ANISOU 4010 CA THR B 224 4941 5289 6181 701 -282 -698 C ATOM 4011 C THR B 224 -3.049 34.863 10.450 1.00 42.79 C ANISOU 4011 C THR B 224 4901 5239 6118 709 -291 -701 C ATOM 4012 O THR B 224 -2.001 35.423 10.102 1.00 37.03 O ANISOU 4012 O THR B 224 4189 4500 5381 706 -299 -688 O ATOM 4013 CB THR B 224 -4.887 34.209 8.893 1.00 45.02 C ANISOU 4013 CB THR B 224 5171 5516 6419 709 -308 -729 C ATOM 4014 OG1 THR B 224 -5.459 33.151 8.106 1.00 48.13 O ANISOU 4014 OG1 THR B 224 5554 5909 6824 702 -301 -728 O ATOM 4015 CG2 THR B 224 -4.507 35.362 7.977 1.00 42.26 C ANISOU 4015 CG2 THR B 224 4843 5151 6063 713 -339 -737 C ATOM 4016 N GLU B 225 -3.688 35.203 11.571 1.00 42.24 N ANISOU 4016 N GLU B 225 4821 5180 6046 719 -288 -718 N ATOM 4017 CA GLU B 225 -3.195 36.346 12.326 1.00 40.80 C ANISOU 4017 CA GLU B 225 4649 4998 5853 728 -299 -723 C ATOM 4018 C GLU B 225 -1.826 36.062 12.938 1.00 45.28 C ANISOU 4018 C GLU B 225 5222 5569 6413 720 -278 -693 C ATOM 4019 O GLU B 225 -0.944 36.932 12.927 1.00 45.87 O ANISOU 4019 O GLU B 225 5313 5636 6479 721 -290 -688 O ATOM 4020 CB GLU B 225 -4.193 36.751 13.399 1.00 47.26 C ANISOU 4020 CB GLU B 225 5455 5829 6672 741 -302 -748 C ATOM 4021 CG GLU B 225 -3.724 37.995 14.125 1.00 54.66 C ANISOU 4021 CG GLU B 225 6404 6766 7598 750 -316 -757 C ATOM 4022 CD GLU B 225 -4.735 38.555 15.079 1.00 56.55 C ANISOU 4022 CD GLU B 225 6633 7016 7837 764 -323 -784 C ATOM 4023 OE1 GLU B 225 -5.905 38.131 15.032 1.00 59.66 O ANISOU 4023 OE1 GLU B 225 7012 7416 8239 767 -322 -801 O ATOM 4024 OE2 GLU B 225 -4.347 39.424 15.882 1.00 59.73 O ANISOU 4024 OE2 GLU B 225 7043 7422 8231 771 -329 -789 O ATOM 4025 N TYR B 226 -1.618 34.855 13.468 1.00 42.18 N ANISOU 4025 N TYR B 226 4815 5188 6024 712 -247 -672 N ATOM 4026 CA TYR B 226 -0.328 34.553 14.078 1.00 39.05 C ANISOU 4026 CA TYR B 226 4422 4796 5619 705 -226 -643 C ATOM 4027 C TYR B 226 0.798 34.643 13.046 1.00 40.49 C ANISOU 4027 C TYR B 226 4623 4964 5799 695 -233 -623 C ATOM 4028 O TYR B 226 1.825 35.291 13.290 1.00 36.80 O ANISOU 4028 O TYR B 226 4168 4492 5322 695 -236 -613 O ATOM 4029 CB TYR B 226 -0.371 33.176 14.762 1.00 35.35 C ANISOU 4029 CB TYR B 226 3935 4343 5154 698 -192 -624 C ATOM 4030 CG TYR B 226 0.961 32.755 15.318 1.00 30.67 C ANISOU 4030 CG TYR B 226 3345 3755 4553 691 -170 -593 C ATOM 4031 CD1 TYR B 226 1.446 33.295 16.507 1.00 33.87 C ANISOU 4031 CD1 TYR B 226 3751 4170 4949 697 -164 -591 C ATOM 4032 CD2 TYR B 226 1.737 31.822 14.659 1.00 20.87 C ANISOU 4032 CD2 TYR B 226 2106 2510 3313 677 -155 -565 C ATOM 4033 CE1 TYR B 226 2.674 32.934 17.000 1.00 28.44 C ANISOU 4033 CE1 TYR B 226 3066 3487 4254 690 -145 -562 C ATOM 4034 CE2 TYR B 226 2.975 31.455 15.136 1.00 23.01 C ANISOU 4034 CE2 TYR B 226 2380 2786 3576 671 -136 -536 C ATOM 4035 CZ TYR B 226 3.436 32.009 16.311 1.00 30.02 C ANISOU 4035 CZ TYR B 226 3268 3682 4454 677 -131 -535 C ATOM 4036 OH TYR B 226 4.664 31.637 16.789 1.00 30.15 O ANISOU 4036 OH TYR B 226 3287 3705 4463 671 -113 -506 O ATOM 4037 N ILE B 227 0.594 34.081 11.854 1.00 35.79 N ANISOU 4037 N ILE B 227 4029 4360 5211 688 -236 -620 N ATOM 4038 CA ILE B 227 1.638 34.166 10.836 1.00 36.52 C ANISOU 4038 CA ILE B 227 4138 4438 5300 678 -243 -601 C ATOM 4039 C ILE B 227 1.882 35.620 10.416 1.00 37.35 C ANISOU 4039 C ILE B 227 4263 4530 5399 686 -274 -616 C ATOM 4040 O ILE B 227 3.025 36.025 10.168 1.00 39.60 O ANISOU 4040 O ILE B 227 4563 4806 5677 681 -277 -600 O ATOM 4041 CB ILE B 227 1.299 33.245 9.654 1.00 33.16 C ANISOU 4041 CB ILE B 227 3708 4007 4884 669 -241 -596 C ATOM 4042 CG1 ILE B 227 1.292 31.802 10.154 1.00 40.98 C ANISOU 4042 CG1 ILE B 227 4681 5010 5878 661 -208 -577 C ATOM 4043 CG2 ILE B 227 2.272 33.417 8.533 1.00 31.56 C ANISOU 4043 CG2 ILE B 227 3524 3790 4678 661 -250 -580 C ATOM 4044 CD1 ILE B 227 2.588 31.403 10.907 1.00 35.21 C ANISOU 4044 CD1 ILE B 227 3952 4287 5139 654 -184 -546 C ATOM 4045 N GLN B 228 0.826 36.433 10.364 1.00 35.58 N ANISOU 4045 N GLN B 228 4038 4303 5176 698 -297 -647 N ATOM 4046 CA GLN B 228 0.996 37.848 10.029 1.00 48.80 C ANISOU 4046 CA GLN B 228 5731 5965 6844 706 -328 -662 C ATOM 4047 C GLN B 228 1.917 38.557 11.026 1.00 46.94 C ANISOU 4047 C GLN B 228 5504 5732 6599 709 -325 -655 C ATOM 4048 O GLN B 228 2.748 39.384 10.636 1.00 35.68 O ANISOU 4048 O GLN B 228 4096 4293 5166 709 -340 -649 O ATOM 4049 CB GLN B 228 -0.380 38.517 9.980 1.00 64.93 C ANISOU 4049 CB GLN B 228 7770 8009 8891 720 -351 -697 C ATOM 4050 CG GLN B 228 -0.400 39.992 9.583 1.00 78.59 C ANISOU 4050 CG GLN B 228 9518 9726 10615 730 -385 -716 C ATOM 4051 CD GLN B 228 -0.098 40.222 8.118 1.00 88.27 C ANISOU 4051 CD GLN B 228 10760 10936 11842 725 -404 -711 C ATOM 4052 OE1 GLN B 228 -0.084 39.282 7.319 1.00 92.94 O ANISOU 4052 OE1 GLN B 228 11347 11525 12439 715 -393 -699 O ATOM 4053 NE2 GLN B 228 0.134 41.480 7.752 1.00 89.69 N ANISOU 4053 NE2 GLN B 228 10959 11103 12015 732 -431 -722 N ATOM 4054 N ARG B 229 1.819 38.202 12.312 1.00 48.54 N ANISOU 4054 N ARG B 229 5692 5950 6800 712 -304 -653 N ATOM 4055 CA ARG B 229 2.666 38.761 13.361 1.00 50.55 C ANISOU 4055 CA ARG B 229 5952 6210 7046 715 -299 -645 C ATOM 4056 C ARG B 229 4.126 38.322 13.241 1.00 56.96 C ANISOU 4056 C ARG B 229 6772 7019 7853 703 -282 -612 C ATOM 4057 O ARG B 229 5.002 38.990 13.803 1.00 59.14 O ANISOU 4057 O ARG B 229 7058 7293 8120 704 -284 -606 O ATOM 4058 CB ARG B 229 2.118 38.333 14.723 1.00 62.20 C ANISOU 4058 CB ARG B 229 7408 7704 8520 721 -279 -651 C ATOM 4059 CG ARG B 229 0.736 38.889 15.038 1.00 71.89 C ANISOU 4059 CG ARG B 229 8628 8937 9752 734 -295 -684 C ATOM 4060 CD ARG B 229 0.147 38.288 16.320 1.00 74.54 C ANISOU 4060 CD ARG B 229 8942 9292 10088 738 -272 -688 C ATOM 4061 NE ARG B 229 1.017 38.457 17.476 1.00 71.49 N ANISOU 4061 NE ARG B 229 8556 8915 9693 739 -258 -675 N ATOM 4062 CZ ARG B 229 0.888 39.449 18.346 1.00 63.45 C ANISOU 4062 CZ ARG B 229 7541 7901 8668 751 -269 -692 C ATOM 4063 NH1 ARG B 229 -0.080 40.341 18.181 1.00 57.06 N ANISOU 4063 NH1 ARG B 229 6733 7088 7859 762 -295 -723 N ATOM 4064 NH2 ARG B 229 1.719 39.545 19.375 1.00 62.24 N ANISOU 4064 NH2 ARG B 229 7387 7756 8506 751 -255 -679 N ATOM 4065 N LYS B 230 4.405 37.183 12.588 1.00 48.08 N ANISOU 4065 N LYS B 230 5643 5894 6733 691 -265 -591 N ATOM 4066 CA LYS B 230 5.789 36.759 12.383 1.00 39.62 C ANISOU 4066 CA LYS B 230 4579 4818 5656 679 -251 -559 C ATOM 4067 C LYS B 230 6.480 37.557 11.281 1.00 39.49 C ANISOU 4067 C LYS B 230 4585 4783 5638 676 -274 -557 C ATOM 4068 O LYS B 230 7.700 37.761 11.336 1.00 38.24 O ANISOU 4068 O LYS B 230 4438 4621 5473 670 -270 -537 O ATOM 4069 CB LYS B 230 5.862 35.258 12.055 1.00 33.51 C ANISOU 4069 CB LYS B 230 3793 4052 4889 667 -225 -537 C ATOM 4070 CG LYS B 230 5.315 34.310 13.139 1.00 34.65 C ANISOU 4070 CG LYS B 230 3914 4214 5035 668 -199 -534 C ATOM 4071 CD LYS B 230 6.068 34.462 14.461 1.00 35.35 C ANISOU 4071 CD LYS B 230 4001 4315 5115 671 -183 -523 C ATOM 4072 CE LYS B 230 5.246 35.260 15.453 1.00 36.21 C ANISOU 4072 CE LYS B 230 4104 4432 5222 685 -193 -549 C ATOM 4073 NZ LYS B 230 5.978 35.539 16.699 1.00 39.39 N ANISOU 4073 NZ LYS B 230 4506 4846 5616 688 -181 -540 N ATOM 4074 N LYS B 231 5.737 37.966 10.254 1.00 43.23 N ANISOU 4074 N LYS B 231 5065 5246 6116 679 -297 -575 N ATOM 4075 CA LYS B 231 6.305 38.739 9.154 1.00 45.30 C ANISOU 4075 CA LYS B 231 5348 5489 6375 677 -320 -573 C ATOM 4076 C LYS B 231 6.326 40.242 9.423 1.00 43.29 C ANISOU 4076 C LYS B 231 5108 5226 6114 688 -346 -593 C ATOM 4077 O LYS B 231 7.306 40.916 9.088 1.00 39.68 O ANISOU 4077 O LYS B 231 4669 4758 5651 685 -357 -583 O ATOM 4078 CB LYS B 231 5.514 38.458 7.874 1.00 41.14 C ANISOU 4078 CB LYS B 231 4821 4955 5856 675 -333 -583 C ATOM 4079 CG LYS B 231 5.460 36.989 7.483 1.00 40.76 C ANISOU 4079 CG LYS B 231 4759 4912 5814 664 -309 -565 C ATOM 4080 CD LYS B 231 4.565 36.788 6.284 1.00 41.44 C ANISOU 4080 CD LYS B 231 4844 4992 5908 664 -324 -579 C ATOM 4081 CE LYS B 231 4.504 35.341 5.886 1.00 41.17 C ANISOU 4081 CE LYS B 231 4797 4963 5881 652 -301 -562 C ATOM 4082 NZ LYS B 231 3.511 35.137 4.801 1.00 37.54 N ANISOU 4082 NZ LYS B 231 4335 4499 5431 653 -315 -578 N ATOM 4083 N PHE B 232 5.285 40.770 10.068 1.00 36.21 N ANISOU 4083 N PHE B 232 4204 4336 5218 701 -357 -620 N ATOM 4084 CA PHE B 232 5.126 42.206 10.302 1.00 42.04 C ANISOU 4084 CA PHE B 232 4955 5067 5950 713 -385 -641 C ATOM 4085 C PHE B 232 4.914 42.431 11.793 1.00 47.60 C ANISOU 4085 C PHE B 232 5648 5786 6650 721 -375 -651 C ATOM 4086 O PHE B 232 3.781 42.622 12.261 1.00 45.68 O ANISOU 4086 O PHE B 232 5394 5551 6410 732 -382 -675 O ATOM 4087 CB PHE B 232 3.974 42.769 9.478 1.00 32.19 C ANISOU 4087 CB PHE B 232 3711 3812 4706 722 -412 -668 C ATOM 4088 CG PHE B 232 4.096 42.478 8.023 1.00 40.24 C ANISOU 4088 CG PHE B 232 4740 4820 5730 714 -420 -660 C ATOM 4089 CD1 PHE B 232 4.847 43.300 7.200 1.00 47.54 C ANISOU 4089 CD1 PHE B 232 5686 5727 6649 713 -440 -654 C ATOM 4090 CD2 PHE B 232 3.477 41.367 7.475 1.00 39.36 C ANISOU 4090 CD2 PHE B 232 4615 4714 5628 708 -408 -657 C ATOM 4091 CE1 PHE B 232 4.961 43.028 5.840 1.00 42.63 C ANISOU 4091 CE1 PHE B 232 5072 5094 6030 706 -448 -646 C ATOM 4092 CE2 PHE B 232 3.594 41.082 6.122 1.00 41.46 C ANISOU 4092 CE2 PHE B 232 4888 4969 5897 701 -416 -649 C ATOM 4093 CZ PHE B 232 4.341 41.920 5.306 1.00 40.58 C ANISOU 4093 CZ PHE B 232 4798 4840 5778 700 -436 -644 C ATOM 4094 N PRO B 233 5.982 42.374 12.574 1.00 47.16 N ANISOU 4094 N PRO B 233 5595 5735 6589 717 -359 -632 N ATOM 4095 CA PRO B 233 5.842 42.447 14.033 1.00 63.77 C ANISOU 4095 CA PRO B 233 7687 7854 8689 724 -347 -638 C ATOM 4096 C PRO B 233 5.313 43.801 14.468 1.00 70.11 C ANISOU 4096 C PRO B 233 8498 8654 9488 739 -373 -667 C ATOM 4097 O PRO B 233 5.799 44.844 14.006 1.00 69.49 O ANISOU 4097 O PRO B 233 8438 8561 9405 741 -396 -671 O ATOM 4098 CB PRO B 233 7.277 42.214 14.543 1.00 61.38 C ANISOU 4098 CB PRO B 233 7388 7553 8380 716 -328 -610 C ATOM 4099 CG PRO B 233 8.014 41.573 13.377 1.00 57.99 C ANISOU 4099 CG PRO B 233 6967 7114 7954 702 -322 -586 C ATOM 4100 CD PRO B 233 7.376 42.170 12.146 1.00 48.83 C ANISOU 4100 CD PRO B 233 5818 5938 6797 705 -351 -603 C ATOM 4101 N PRO B 234 4.301 43.828 15.337 1.00 81.74 N ANISOU 4101 N PRO B 234 9955 10140 10961 749 -371 -688 N ATOM 4102 CA PRO B 234 3.810 45.124 15.830 1.00 89.30 C ANISOU 4102 CA PRO B 234 10920 11096 11915 763 -396 -715 C ATOM 4103 C PRO B 234 4.845 45.880 16.649 1.00 89.42 C ANISOU 4103 C PRO B 234 10945 11110 11920 765 -397 -709 C ATOM 4104 O PRO B 234 4.852 47.117 16.619 1.00 90.65 O ANISOU 4104 O PRO B 234 11116 11256 12072 774 -424 -726 O ATOM 4105 CB PRO B 234 2.577 44.740 16.661 1.00 90.01 C ANISOU 4105 CB PRO B 234 10988 11203 12008 772 -388 -734 C ATOM 4106 CG PRO B 234 2.796 43.320 17.036 1.00 89.97 C ANISOU 4106 CG PRO B 234 10967 11212 12007 762 -352 -711 C ATOM 4107 CD PRO B 234 3.519 42.702 15.871 1.00 86.63 C ANISOU 4107 CD PRO B 234 10551 10777 11587 748 -347 -687 C ATOM 4108 N ASP B 235 5.741 45.183 17.357 1.00 77.13 N ANISOU 4108 N ASP B 235 9382 9563 10361 758 -370 -685 N ATOM 4109 CA ASP B 235 6.788 45.841 18.129 1.00 73.06 C ANISOU 4109 CA ASP B 235 8876 9047 9837 759 -370 -678 C ATOM 4110 C ASP B 235 8.050 46.100 17.309 1.00 76.52 C ANISOU 4110 C ASP B 235 9333 9467 10272 749 -376 -657 C ATOM 4111 O ASP B 235 9.159 46.057 17.860 1.00 80.13 O ANISOU 4111 O ASP B 235 9794 9927 10724 744 -363 -639 O ATOM 4112 CB ASP B 235 7.135 45.024 19.376 1.00 74.93 C ANISOU 4112 CB ASP B 235 9095 9303 10071 757 -338 -663 C ATOM 4113 CG ASP B 235 7.607 43.615 19.053 1.00 78.93 C ANISOU 4113 CG ASP B 235 9593 9816 10582 743 -309 -633 C ATOM 4114 OD1 ASP B 235 7.760 43.280 17.861 1.00 80.66 O ANISOU 4114 OD1 ASP B 235 9819 10023 10806 734 -313 -623 O ATOM 4115 OD2 ASP B 235 7.871 42.848 20.005 1.00 78.86 O ANISOU 4115 OD2 ASP B 235 9570 9824 10571 740 -282 -619 O ATOM 4116 N ASN B 236 7.898 46.345 16.003 1.00 74.95 N ANISOU 4116 N ASN B 236 9147 9252 10077 746 -395 -659 N ATOM 4117 CA ASN B 236 8.949 46.624 15.019 1.00 82.46 C ANISOU 4117 CA ASN B 236 10118 10186 11026 737 -403 -642 C ATOM 4118 C ASN B 236 10.258 45.845 15.199 1.00 84.11 C ANISOU 4118 C ASN B 236 10326 10398 11234 723 -378 -609 C ATOM 4119 O ASN B 236 11.288 46.230 14.633 1.00 87.46 O ANISOU 4119 O ASN B 236 10767 10808 11655 717 -385 -594 O ATOM 4120 CB ASN B 236 9.221 48.145 14.950 1.00 85.26 C ANISOU 4120 CB ASN B 236 10494 10526 11376 745 -434 -657 C ATOM 4121 CG ASN B 236 9.768 48.740 16.253 1.00 89.19 C ANISOU 4121 CG ASN B 236 10992 11031 11866 751 -431 -660 C ATOM 4122 OD1 ASN B 236 10.512 48.102 16.995 1.00 93.48 O ANISOU 4122 OD1 ASN B 236 11526 11584 12407 745 -406 -641 O ATOM 4123 ND2 ASN B 236 9.386 49.984 16.530 1.00 89.06 N ANISOU 4123 ND2 ASN B 236 10985 11009 11846 763 -457 -684 N ATOM 4124 N SER B 237 10.230 44.740 15.949 1.00 76.57 N ANISOU 4124 N SER B 237 9352 9461 10280 720 -348 -596 N ATOM 4125 CA SER B 237 11.377 43.840 16.053 1.00 69.62 C ANISOU 4125 CA SER B 237 8468 8585 9399 707 -322 -564 C ATOM 4126 C SER B 237 11.571 43.065 14.737 1.00 65.91 C ANISOU 4126 C SER B 237 8002 8106 8934 695 -318 -546 C ATOM 4127 O SER B 237 10.823 43.226 13.767 1.00 65.82 O ANISOU 4127 O SER B 237 7995 8085 8928 696 -335 -559 O ATOM 4128 CB SER B 237 11.207 42.902 17.249 1.00 65.86 C ANISOU 4128 CB SER B 237 7971 8132 8922 707 -292 -556 C ATOM 4129 OG SER B 237 10.051 42.090 17.126 1.00 64.49 O ANISOU 4129 OG SER B 237 7781 7968 8756 709 -284 -564 O ATOM 4130 N ALA B 238 12.591 42.209 14.703 1.00 56.76 N ANISOU 4130 N ALA B 238 6841 6951 7774 683 -295 -517 N ATOM 4131 CA ALA B 238 12.930 41.500 13.474 1.00 46.71 C ANISOU 4131 CA ALA B 238 5572 5669 6506 671 -291 -498 C ATOM 4132 C ALA B 238 11.937 40.374 13.181 1.00 48.80 C ANISOU 4132 C ALA B 238 5820 5944 6779 669 -278 -500 C ATOM 4133 O ALA B 238 11.529 39.651 14.094 1.00 55.97 O ANISOU 4133 O ALA B 238 6709 6869 7687 671 -257 -498 O ATOM 4134 CB ALA B 238 14.336 40.921 13.566 1.00 39.30 C ANISOU 4134 CB ALA B 238 4636 4732 5563 659 -271 -466 C ATOM 4135 N PRO B 239 11.521 40.220 11.922 1.00 45.67 N ANISOU 4135 N PRO B 239 5429 5536 6387 665 -289 -503 N ATOM 4136 CA PRO B 239 10.652 39.093 11.535 1.00 46.35 C ANISOU 4136 CA PRO B 239 5499 5630 6482 661 -276 -502 C ATOM 4137 C PRO B 239 11.341 37.737 11.669 1.00 44.38 C ANISOU 4137 C PRO B 239 5238 5391 6232 649 -245 -472 C ATOM 4138 O PRO B 239 12.569 37.627 11.666 1.00 42.20 O ANISOU 4138 O PRO B 239 4970 5113 5952 641 -236 -449 O ATOM 4139 CB PRO B 239 10.325 39.386 10.066 1.00 41.65 C ANISOU 4139 CB PRO B 239 4916 5019 5891 659 -298 -510 C ATOM 4140 CG PRO B 239 10.664 40.816 9.859 1.00 40.96 C ANISOU 4140 CG PRO B 239 4849 4916 5798 666 -326 -522 C ATOM 4141 CD PRO B 239 11.770 41.138 10.800 1.00 37.44 C ANISOU 4141 CD PRO B 239 4408 4474 5345 664 -317 -509 C ATOM 4142 N TYR B 240 10.518 36.700 11.847 1.00 42.53 N ANISOU 4142 N TYR B 240 4985 5168 6004 648 -228 -473 N ATOM 4143 CA TYR B 240 11.005 35.319 11.865 1.00 37.01 C ANISOU 4143 CA TYR B 240 4275 4479 5306 637 -200 -445 C ATOM 4144 C TYR B 240 11.345 34.823 10.452 1.00 40.05 C ANISOU 4144 C TYR B 240 4669 4853 5695 626 -203 -432 C ATOM 4145 O TYR B 240 10.761 35.259 9.457 1.00 42.39 O ANISOU 4145 O TYR B 240 4972 5136 5996 627 -224 -448 O ATOM 4146 CB TYR B 240 9.954 34.383 12.458 1.00 36.12 C ANISOU 4146 CB TYR B 240 4141 4383 5199 640 -182 -451 C ATOM 4147 CG TYR B 240 9.805 34.366 13.970 1.00 40.89 C ANISOU 4147 CG TYR B 240 4733 5004 5799 647 -167 -454 C ATOM 4148 CD1 TYR B 240 9.903 35.533 14.739 1.00 38.58 C ANISOU 4148 CD1 TYR B 240 4447 4711 5501 657 -180 -469 C ATOM 4149 CD2 TYR B 240 9.535 33.169 14.632 1.00 43.57 C ANISOU 4149 CD2 TYR B 240 5053 5361 6140 644 -140 -442 C ATOM 4150 CE1 TYR B 240 9.732 35.492 16.139 1.00 38.86 C ANISOU 4150 CE1 TYR B 240 4470 4764 5533 665 -166 -472 C ATOM 4151 CE2 TYR B 240 9.371 33.121 16.023 1.00 35.25 C ANISOU 4151 CE2 TYR B 240 3988 4324 5082 652 -125 -444 C ATOM 4152 CZ TYR B 240 9.475 34.273 16.759 1.00 33.74 C ANISOU 4152 CZ TYR B 240 3803 4132 4885 662 -138 -459 C ATOM 4153 OH TYR B 240 9.309 34.179 18.108 1.00 40.15 O ANISOU 4153 OH TYR B 240 4601 4961 5692 668 -123 -460 O ATOM 4154 N GLY B 241 12.266 33.852 10.373 1.00 32.64 N ANISOU 4154 N GLY B 241 3727 3919 4754 614 -181 -403 N ATOM 4155 CA GLY B 241 12.464 33.102 9.146 1.00 24.67 C ANISOU 4155 CA GLY B 241 2721 2903 3749 603 -179 -390 C ATOM 4156 C GLY B 241 11.492 31.927 9.024 1.00 30.71 C ANISOU 4156 C GLY B 241 3468 3678 4523 600 -165 -392 C ATOM 4157 O GLY B 241 10.893 31.496 10.012 1.00 31.79 O ANISOU 4157 O GLY B 241 3589 3829 4660 605 -150 -396 O ATOM 4158 N ALA B 242 11.335 31.425 7.796 1.00 28.75 N ANISOU 4158 N ALA B 242 3223 3421 4280 593 -169 -388 N ATOM 4159 CA ALA B 242 10.473 30.283 7.502 1.00 34.02 C ANISOU 4159 CA ALA B 242 3874 4094 4956 589 -157 -389 C ATOM 4160 C ALA B 242 11.300 29.076 7.061 1.00 38.22 C ANISOU 4160 C ALA B 242 4404 4630 5487 575 -137 -360 C ATOM 4161 O ALA B 242 12.286 29.230 6.335 1.00 35.55 O ANISOU 4161 O ALA B 242 4079 4282 5144 567 -142 -345 O ATOM 4162 CB ALA B 242 9.456 30.629 6.409 1.00 33.93 C ANISOU 4162 CB ALA B 242 3867 4072 4953 592 -180 -413 C ATOM 4163 N ARG B 243 10.923 27.876 7.539 1.00 31.13 N ANISOU 4163 N ARG B 243 3489 3746 4592 571 -115 -352 N ATOM 4164 CA ARG B 243 11.502 26.613 7.075 1.00 27.86 C ANISOU 4164 CA ARG B 243 3071 3336 4178 558 -97 -327 C ATOM 4165 C ARG B 243 10.409 25.555 7.047 1.00 31.01 C ANISOU 4165 C ARG B 243 3453 3742 4587 556 -85 -334 C ATOM 4166 O ARG B 243 9.593 25.492 7.968 1.00 26.92 O ANISOU 4166 O ARG B 243 2923 3235 4071 565 -79 -346 O ATOM 4167 CB ARG B 243 12.672 26.114 7.957 1.00 26.11 C ANISOU 4167 CB ARG B 243 2848 3127 3946 553 -75 -300 C ATOM 4168 CG ARG B 243 13.847 27.066 8.015 1.00 21.83 C ANISOU 4168 CG ARG B 243 2322 2578 3394 553 -84 -292 C ATOM 4169 CD ARG B 243 14.536 27.179 6.668 1.00 26.09 C ANISOU 4169 CD ARG B 243 2876 3102 3934 543 -96 -283 C ATOM 4170 NE ARG B 243 15.769 27.951 6.744 1.00 30.02 N ANISOU 4170 NE ARG B 243 3388 3594 4422 541 -102 -271 N ATOM 4171 CZ ARG B 243 15.813 29.286 6.761 1.00 37.16 C ANISOU 4171 CZ ARG B 243 4305 4488 5325 550 -122 -286 C ATOM 4172 NH1 ARG B 243 14.697 30.009 6.703 1.00 30.28 N ANISOU 4172 NH1 ARG B 243 3434 3611 4460 560 -140 -313 N ATOM 4173 NH2 ARG B 243 16.980 29.906 6.832 1.00 41.70 N ANISOU 4173 NH2 ARG B 243 4894 5058 5892 547 -126 -273 N ATOM 4174 N TYR B 244 10.351 24.759 5.971 1.00 34.24 N ANISOU 4174 N TYR B 244 3863 4146 5003 546 -84 -328 N ATOM 4175 CA TYR B 244 9.396 23.645 5.921 1.00 38.60 C ANISOU 4175 CA TYR B 244 4397 4704 5564 544 -72 -332 C ATOM 4176 C TYR B 244 9.918 22.558 4.977 1.00 40.99 C ANISOU 4176 C TYR B 244 4702 5005 5870 529 -64 -312 C ATOM 4177 O TYR B 244 9.744 22.671 3.761 1.00 39.47 O ANISOU 4177 O TYR B 244 4516 4799 5682 525 -78 -319 O ATOM 4178 CB TYR B 244 8.017 24.133 5.494 1.00 34.73 C ANISOU 4178 CB TYR B 244 3904 4208 5085 552 -91 -362 C ATOM 4179 CG TYR B 244 6.925 23.077 5.614 1.00 36.18 C ANISOU 4179 CG TYR B 244 4070 4399 5279 551 -78 -370 C ATOM 4180 CD1 TYR B 244 6.497 22.632 6.860 1.00 30.73 C ANISOU 4180 CD1 TYR B 244 3364 3723 4588 556 -60 -370 C ATOM 4181 CD2 TYR B 244 6.310 22.545 4.485 1.00 30.25 C ANISOU 4181 CD2 TYR B 244 3316 3640 4539 546 -85 -377 C ATOM 4182 CE1 TYR B 244 5.502 21.686 6.971 1.00 27.88 C ANISOU 4182 CE1 TYR B 244 2987 3369 4237 555 -49 -376 C ATOM 4183 CE2 TYR B 244 5.317 21.598 4.595 1.00 28.62 C ANISOU 4183 CE2 TYR B 244 3093 3439 4342 544 -74 -384 C ATOM 4184 CZ TYR B 244 4.921 21.169 5.842 1.00 29.52 C ANISOU 4184 CZ TYR B 244 3192 3567 4455 549 -56 -384 C ATOM 4185 OH TYR B 244 3.928 20.220 5.973 1.00 36.27 O ANISOU 4185 OH TYR B 244 4031 4429 5321 547 -45 -391 O ATOM 4186 N VAL B 245 10.532 21.505 5.545 1.00 35.33 N ANISOU 4186 N VAL B 245 3977 4299 5147 521 -40 -290 N ATOM 4187 CA VAL B 245 11.031 20.360 4.766 1.00 28.70 C ANISOU 4187 CA VAL B 245 3136 3458 4310 506 -31 -271 C ATOM 4188 C VAL B 245 9.885 19.513 4.211 1.00 26.21 C ANISOU 4188 C VAL B 245 2810 3141 4009 503 -29 -283 C ATOM 4189 O VAL B 245 9.990 18.955 3.109 1.00 36.77 O ANISOU 4189 O VAL B 245 4149 4469 5351 493 -32 -278 O ATOM 4190 CB VAL B 245 11.988 19.486 5.617 1.00 22.29 C ANISOU 4190 CB VAL B 245 2319 2661 3488 498 -7 -245 C ATOM 4191 CG1 VAL B 245 12.399 18.226 4.867 1.00 11.82 C ANISOU 4191 CG1 VAL B 245 992 1334 2166 482 3 -228 C ATOM 4192 CG2 VAL B 245 13.241 20.247 5.977 1.00 24.45 C ANISOU 4192 CG2 VAL B 245 2607 2936 3749 499 -10 -232 C ATOM 4193 N GLY B 246 8.782 19.402 4.939 1.00 24.16 N ANISOU 4193 N GLY B 246 2536 2889 3754 512 -24 -299 N ATOM 4194 CA GLY B 246 7.712 18.513 4.538 1.00 28.84 C ANISOU 4194 CA GLY B 246 3116 3481 4360 509 -20 -309 C ATOM 4195 C GLY B 246 7.845 17.086 5.029 1.00 35.72 C ANISOU 4195 C GLY B 246 3975 4365 5233 499 5 -291 C ATOM 4196 O GLY B 246 6.978 16.261 4.733 1.00 30.22 O ANISOU 4196 O GLY B 246 3267 3667 4548 496 9 -299 O ATOM 4197 N SER B 247 8.874 16.781 5.808 1.00 38.17 N ANISOU 4197 N SER B 247 4287 4685 5532 495 20 -269 N ATOM 4198 CA SER B 247 9.029 15.482 6.444 1.00 33.76 C ANISOU 4198 CA SER B 247 3716 4139 4972 487 43 -253 C ATOM 4199 C SER B 247 9.005 15.738 7.940 1.00 34.02 C ANISOU 4199 C SER B 247 3742 4189 4996 498 54 -251 C ATOM 4200 O SER B 247 9.894 16.418 8.467 1.00 35.99 O ANISOU 4200 O SER B 247 3999 4442 5232 502 53 -242 O ATOM 4201 CB SER B 247 10.335 14.812 6.014 1.00 32.95 C ANISOU 4201 CB SER B 247 3622 4036 4863 472 50 -227 C ATOM 4202 OG SER B 247 10.405 13.486 6.476 1.00 37.37 O ANISOU 4202 OG SER B 247 4170 4604 5424 463 70 -213 O ATOM 4203 N MET B 248 7.978 15.213 8.614 1.00 31.76 N ANISOU 4203 N MET B 248 3021 3924 5123 436 1 -553 N ATOM 4204 CA MET B 248 7.693 15.646 9.979 1.00 32.16 C ANISOU 4204 CA MET B 248 3069 3984 5168 445 12 -544 C ATOM 4205 C MET B 248 8.889 15.428 10.901 1.00 36.70 C ANISOU 4205 C MET B 248 3647 4563 5733 443 17 -541 C ATOM 4206 O MET B 248 9.216 16.290 11.725 1.00 30.83 O ANISOU 4206 O MET B 248 2909 3828 4979 449 24 -539 O ATOM 4207 CB MET B 248 6.480 14.903 10.514 1.00 38.47 C ANISOU 4207 CB MET B 248 3855 4784 5977 448 16 -535 C ATOM 4208 CG MET B 248 6.011 15.422 11.863 1.00 45.31 C ANISOU 4208 CG MET B 248 4718 5660 6839 458 27 -526 C ATOM 4209 SD MET B 248 5.027 14.190 12.739 1.00 55.83 S ANISOU 4209 SD MET B 248 6036 6995 8183 460 34 -514 S ATOM 4210 CE MET B 248 4.382 15.163 14.113 1.00 51.32 C ANISOU 4210 CE MET B 248 5463 6435 7604 472 46 -505 C ATOM 4211 N VAL B 249 9.557 14.281 10.773 1.00 32.96 N ANISOU 4211 N VAL B 249 3174 4087 5264 436 15 -542 N ATOM 4212 CA VAL B 249 10.701 13.999 11.626 1.00 25.82 C ANISOU 4212 CA VAL B 249 2273 3187 4350 434 21 -539 C ATOM 4213 C VAL B 249 11.793 15.054 11.427 1.00 31.01 C ANISOU 4213 C VAL B 249 2942 3845 4994 434 19 -546 C ATOM 4214 O VAL B 249 12.399 15.524 12.398 1.00 29.36 O ANISOU 4214 O VAL B 249 2737 3645 4775 437 26 -543 O ATOM 4215 CB VAL B 249 11.210 12.572 11.352 1.00 24.57 C ANISOU 4215 CB VAL B 249 2112 3023 4200 426 17 -539 C ATOM 4216 CG1 VAL B 249 12.386 12.221 12.259 1.00 23.94 C ANISOU 4216 CG1 VAL B 249 2036 2949 4111 425 23 -536 C ATOM 4217 CG2 VAL B 249 10.086 11.593 11.561 1.00 24.74 C ANISOU 4217 CG2 VAL B 249 2122 3043 4234 427 20 -531 C ATOM 4218 N ALA B 250 12.035 15.476 10.172 1.00 25.90 N ANISOU 4218 N ALA B 250 2302 3192 4348 429 9 -557 N ATOM 4219 CA ALA B 250 13.041 16.511 9.927 1.00 18.98 C ANISOU 4219 CA ALA B 250 1437 2317 3458 428 7 -564 C ATOM 4220 C ALA B 250 12.610 17.879 10.472 1.00 17.39 C ANISOU 4220 C ALA B 250 1238 2122 3249 437 12 -563 C ATOM 4221 O ALA B 250 13.435 18.615 11.027 1.00 24.66 O ANISOU 4221 O ALA B 250 2165 3048 4157 439 16 -564 O ATOM 4222 CB ALA B 250 13.376 16.601 8.439 1.00 18.69 C ANISOU 4222 CB ALA B 250 1406 2271 3424 421 -5 -575 C ATOM 4223 N ASP B 251 11.346 18.265 10.272 1.00 15.81 N ANISOU 4223 N ASP B 251 1031 1921 3054 442 12 -561 N ATOM 4224 CA ASP B 251 10.866 19.558 10.762 1.00 23.88 C ANISOU 4224 CA ASP B 251 2055 2949 4069 451 17 -559 C ATOM 4225 C ASP B 251 10.773 19.586 12.287 1.00 30.62 C ANISOU 4225 C ASP B 251 2904 3812 4917 458 29 -549 C ATOM 4226 O ASP B 251 11.135 20.581 12.920 1.00 30.00 O ANISOU 4226 O ASP B 251 2832 3739 4827 463 34 -548 O ATOM 4227 CB ASP B 251 9.520 19.872 10.113 1.00 29.79 C ANISOU 4227 CB ASP B 251 2799 3695 4827 455 14 -559 C ATOM 4228 CG ASP B 251 9.670 20.344 8.676 1.00 33.71 C ANISOU 4228 CG ASP B 251 3301 4183 5323 450 3 -570 C ATOM 4229 OD1 ASP B 251 10.532 21.230 8.451 1.00 29.93 O ANISOU 4229 OD1 ASP B 251 2833 3706 4835 449 1 -577 O ATOM 4230 OD2 ASP B 251 8.965 19.800 7.782 1.00 31.65 O ANISOU 4230 OD2 ASP B 251 3035 3916 5074 447 -4 -572 O ATOM 4231 N VAL B 252 10.335 18.484 12.897 1.00 29.34 N ANISOU 4231 N VAL B 252 2733 3651 4763 458 33 -540 N ATOM 4232 CA VAL B 252 10.252 18.432 14.346 1.00 22.07 C ANISOU 4232 CA VAL B 252 1809 2740 3838 464 44 -531 C ATOM 4233 C VAL B 252 11.656 18.462 14.941 1.00 31.86 C ANISOU 4233 C VAL B 252 3056 3983 5066 462 48 -532 C ATOM 4234 O VAL B 252 11.912 19.144 15.944 1.00 33.46 O ANISOU 4234 O VAL B 252 3262 4194 5259 468 56 -528 O ATOM 4235 CB VAL B 252 9.479 17.169 14.796 1.00 23.87 C ANISOU 4235 CB VAL B 252 2025 2967 4077 464 48 -522 C ATOM 4236 CG1 VAL B 252 9.567 16.998 16.291 1.00 24.53 C ANISOU 4236 CG1 VAL B 252 2105 3060 4156 470 59 -512 C ATOM 4237 CG2 VAL B 252 8.029 17.220 14.389 1.00 22.09 C ANISOU 4237 CG2 VAL B 252 1792 2739 3862 468 46 -520 C ATOM 4238 N HIS B 253 12.598 17.752 14.323 1.00 15.84 N ANISOU 4238 N HIS B 253 1032 1949 3039 453 42 -537 N ATOM 4239 CA HIS B 253 13.941 17.707 14.889 1.00 17.07 C ANISOU 4239 CA HIS B 253 1194 2109 3184 450 45 -538 C ATOM 4240 C HIS B 253 14.621 19.068 14.816 1.00 31.10 C ANISOU 4240 C HIS B 253 2980 3888 4947 452 44 -544 C ATOM 4241 O HIS B 253 15.330 19.460 15.748 1.00 35.81 O ANISOU 4241 O HIS B 253 3581 4491 5532 455 51 -542 O ATOM 4242 CB HIS B 253 14.777 16.629 14.192 1.00 18.08 C ANISOU 4242 CB HIS B 253 1324 2231 3316 441 38 -542 C ATOM 4243 CG HIS B 253 16.117 16.412 14.826 1.00 27.69 C ANISOU 4243 CG HIS B 253 2545 3451 4523 438 41 -542 C ATOM 4244 ND1 HIS B 253 16.262 15.868 16.089 1.00 20.80 N ANISOU 4244 ND1 HIS B 253 1668 2586 3648 441 51 -533 N ATOM 4245 CD2 HIS B 253 17.370 16.663 14.378 1.00 26.62 C ANISOU 4245 CD2 HIS B 253 2420 3315 4380 432 37 -550 C ATOM 4246 CE1 HIS B 253 17.546 15.802 16.389 1.00 24.36 C ANISOU 4246 CE1 HIS B 253 2126 3039 4090 438 52 -535 C ATOM 4247 NE2 HIS B 253 18.240 16.270 15.369 1.00 20.42 N ANISOU 4247 NE2 HIS B 253 1636 2536 3588 432 43 -545 N ATOM 4248 N ARG B 254 14.420 19.807 13.719 1.00 40.09 N ANISOU 4248 N ARG B 254 4125 5022 6087 451 37 -553 N ATOM 4249 CA ARG B 254 14.958 21.165 13.645 1.00 37.22 C ANISOU 4249 CA ARG B 254 3771 4661 5711 454 37 -559 C ATOM 4250 C ARG B 254 14.362 22.069 14.721 1.00 32.92 C ANISOU 4250 C ARG B 254 3224 4124 5160 464 46 -552 C ATOM 4251 O ARG B 254 15.064 22.924 15.273 1.00 37.09 O ANISOU 4251 O ARG B 254 3760 4658 5676 466 51 -553 O ATOM 4252 CB ARG B 254 14.736 21.780 12.260 1.00 31.02 C ANISOU 4252 CB ARG B 254 2990 3868 4928 451 27 -568 C ATOM 4253 CG ARG B 254 15.405 23.151 12.104 1.00 29.00 C ANISOU 4253 CG ARG B 254 2746 3615 4660 452 26 -575 C ATOM 4254 CD ARG B 254 14.795 24.003 10.976 1.00 29.97 C ANISOU 4254 CD ARG B 254 2870 3732 4784 453 19 -583 C ATOM 4255 NE ARG B 254 13.355 24.149 11.154 1.00 33.45 N ANISOU 4255 NE ARG B 254 3303 4173 5232 460 22 -577 N ATOM 4256 CZ ARG B 254 12.456 23.589 10.353 1.00 31.51 C ANISOU 4256 CZ ARG B 254 3051 3922 4999 458 16 -577 C ATOM 4257 NH1 ARG B 254 12.867 22.889 9.302 1.00 21.69 N ANISOU 4257 NH1 ARG B 254 1810 2671 3762 450 7 -584 N ATOM 4258 NH2 ARG B 254 11.156 23.751 10.580 1.00 25.78 N ANISOU 4258 NH2 ARG B 254 2317 3197 4279 465 19 -571 N ATOM 4259 N THR B 255 13.065 21.923 15.012 1.00 32.27 N ANISOU 4259 N THR B 255 3132 4042 5085 470 50 -545 N ATOM 4260 CA THR B 255 12.447 22.730 16.069 1.00 30.13 C ANISOU 4260 CA THR B 255 2859 3779 4809 480 59 -538 C ATOM 4261 C THR B 255 13.087 22.446 17.434 1.00 32.16 C ANISOU 4261 C THR B 255 3116 4045 5059 482 69 -531 C ATOM 4262 O THR B 255 13.377 23.375 18.198 1.00 25.31 O ANISOU 4262 O THR B 255 2253 3184 4181 488 75 -529 O ATOM 4263 CB THR B 255 10.934 22.462 16.107 1.00 29.35 C ANISOU 4263 CB THR B 255 2750 3680 4721 485 61 -532 C ATOM 4264 OG1 THR B 255 10.388 22.646 14.802 1.00 28.05 O ANISOU 4264 OG1 THR B 255 2586 3508 4564 482 51 -539 O ATOM 4265 CG2 THR B 255 10.215 23.425 17.030 1.00 25.59 C ANISOU 4265 CG2 THR B 255 2272 3211 4240 495 69 -526 C ATOM 4266 N LEU B 256 13.357 21.172 17.735 1.00 30.01 N ANISOU 4266 N LEU B 256 2838 3772 4792 478 70 -526 N ATOM 4267 CA LEU B 256 14.035 20.812 18.983 1.00 31.75 C ANISOU 4267 CA LEU B 256 3058 3999 5005 479 78 -520 C ATOM 4268 C LEU B 256 15.436 21.412 19.050 1.00 31.59 C ANISOU 4268 C LEU B 256 3049 3982 4972 476 78 -526 C ATOM 4269 O LEU B 256 15.843 21.966 20.081 1.00 27.76 O ANISOU 4269 O LEU B 256 2566 3504 4476 481 86 -522 O ATOM 4270 CB LEU B 256 14.110 19.290 19.106 1.00 33.57 C ANISOU 4270 CB LEU B 256 3282 4229 5246 474 78 -515 C ATOM 4271 CG LEU B 256 14.819 18.661 20.307 1.00 34.74 C ANISOU 4271 CG LEU B 256 3429 4384 5388 475 86 -508 C ATOM 4272 CD1 LEU B 256 14.078 18.988 21.558 1.00 23.41 C ANISOU 4272 CD1 LEU B 256 1988 2956 3950 484 96 -498 C ATOM 4273 CD2 LEU B 256 14.969 17.143 20.153 1.00 31.87 C ANISOU 4273 CD2 LEU B 256 3060 4016 5034 468 83 -505 C ATOM 4274 N VAL B 257 16.200 21.296 17.961 1.00 25.42 N ANISOU 4274 N VAL B 257 2274 3194 4191 468 69 -535 N ATOM 4275 CA VAL B 257 17.610 21.691 17.993 1.00 30.69 C ANISOU 4275 CA VAL B 257 2952 3863 4846 464 68 -541 C ATOM 4276 C VAL B 257 17.764 23.217 17.949 1.00 33.00 C ANISOU 4276 C VAL B 257 3252 4158 5128 469 69 -546 C ATOM 4277 O VAL B 257 18.674 23.777 18.564 1.00 31.32 O ANISOU 4277 O VAL B 257 3046 3950 4903 470 73 -547 O ATOM 4278 CB VAL B 257 18.386 20.997 16.850 1.00 29.53 C ANISOU 4278 CB VAL B 257 2808 3708 4703 454 58 -549 C ATOM 4279 CG1 VAL B 257 19.764 21.585 16.708 1.00 27.83 C ANISOU 4279 CG1 VAL B 257 2605 3494 4476 450 56 -557 C ATOM 4280 CG2 VAL B 257 18.502 19.473 17.091 1.00 23.80 C ANISOU 4280 CG2 VAL B 257 2076 2981 3986 449 58 -544 C ATOM 4281 N TYR B 258 16.901 23.921 17.219 1.00 34.95 N ANISOU 4281 N TYR B 258 3500 4401 5379 471 65 -550 N ATOM 4282 CA TYR B 258 17.055 25.358 17.028 1.00 30.70 C ANISOU 4282 CA TYR B 258 2969 3864 4831 475 65 -556 C ATOM 4283 C TYR B 258 16.004 26.208 17.725 1.00 35.03 C ANISOU 4283 C TYR B 258 3514 4417 5377 485 72 -550 C ATOM 4284 O TYR B 258 16.193 27.426 17.827 1.00 35.99 O ANISOU 4284 O TYR B 258 3643 4542 5490 489 74 -553 O ATOM 4285 CB TYR B 258 17.042 25.704 15.528 1.00 35.84 C ANISOU 4285 CB TYR B 258 3626 4507 5486 470 53 -566 C ATOM 4286 CG TYR B 258 18.311 25.317 14.817 1.00 47.89 C ANISOU 4286 CG TYR B 258 5159 6029 7009 460 46 -574 C ATOM 4287 CD1 TYR B 258 19.505 25.246 15.503 1.00 61.84 C ANISOU 4287 CD1 TYR B 258 6930 7800 8765 458 50 -574 C ATOM 4288 CD2 TYR B 258 18.319 25.021 13.467 1.00 54.27 C ANISOU 4288 CD2 TYR B 258 5969 6828 7824 453 35 -582 C ATOM 4289 CE1 TYR B 258 20.675 24.897 14.868 1.00 69.46 C ANISOU 4289 CE1 TYR B 258 7902 8761 9727 449 44 -582 C ATOM 4290 CE2 TYR B 258 19.489 24.668 12.823 1.00 57.38 C ANISOU 4290 CE2 TYR B 258 6368 7218 8214 444 29 -590 C ATOM 4291 CZ TYR B 258 20.662 24.606 13.531 1.00 64.13 C ANISOU 4291 CZ TYR B 258 7229 8079 9060 442 33 -590 C ATOM 4292 OH TYR B 258 21.844 24.258 12.918 1.00 69.63 O ANISOU 4292 OH TYR B 258 7932 8772 9753 434 26 -597 O ATOM 4293 N GLY B 259 14.907 25.619 18.190 1.00 34.26 N ANISOU 4293 N GLY B 259 3407 4322 5290 490 76 -541 N ATOM 4294 CA GLY B 259 13.807 26.389 18.725 1.00 28.85 C ANISOU 4294 CA GLY B 259 2717 3640 4604 499 82 -535 C ATOM 4295 C GLY B 259 12.920 26.914 17.612 1.00 32.72 C ANISOU 4295 C GLY B 259 3208 4124 5101 500 75 -541 C ATOM 4296 O GLY B 259 13.258 26.878 16.424 1.00 36.47 O ANISOU 4296 O GLY B 259 3687 4593 5579 493 66 -549 O ATOM 4297 N GLY B 260 11.768 27.453 18.017 1.00 28.22 N ANISOU 4297 N GLY B 260 2633 3557 4533 509 80 -535 N ATOM 4298 CA GLY B 260 10.765 27.925 17.090 1.00 29.42 C ANISOU 4298 CA GLY B 260 2782 3704 4691 511 75 -538 C ATOM 4299 C GLY B 260 9.453 27.176 17.263 1.00 32.77 C ANISOU 4299 C GLY B 260 3196 4129 5128 514 76 -530 C ATOM 4300 O GLY B 260 9.146 26.671 18.351 1.00 28.87 O ANISOU 4300 O GLY B 260 2695 3640 4635 518 84 -521 O ATOM 4301 N ILE B 261 8.683 27.117 16.177 1.00 25.66 N ANISOU 4301 N ILE B 261 2292 3221 4236 512 69 -534 N ATOM 4302 CA ILE B 261 7.332 26.564 16.212 1.00 33.37 C ANISOU 4302 CA ILE B 261 3258 4197 5225 516 70 -528 C ATOM 4303 C ILE B 261 7.060 25.794 14.918 1.00 38.84 C ANISOU 4303 C ILE B 261 3947 4881 5929 508 59 -533 C ATOM 4304 O ILE B 261 7.490 26.200 13.828 1.00 33.03 O ANISOU 4304 O ILE B 261 3218 4139 5192 504 51 -543 O ATOM 4305 CB ILE B 261 6.280 27.674 16.455 1.00 25.96 C ANISOU 4305 CB ILE B 261 2317 3262 4284 526 74 -525 C ATOM 4306 CG1 ILE B 261 4.898 27.072 16.694 1.00 36.72 C ANISOU 4306 CG1 ILE B 261 3668 4625 5659 530 76 -517 C ATOM 4307 CG2 ILE B 261 6.223 28.659 15.313 1.00 27.43 C ANISOU 4307 CG2 ILE B 261 2511 3443 4468 525 67 -534 C ATOM 4308 CD1 ILE B 261 3.887 28.080 17.243 1.00 44.26 C ANISOU 4308 CD1 ILE B 261 4621 5586 6611 541 83 -512 C ATOM 4309 N PHE B 262 6.332 24.681 15.047 1.00 36.98 N ANISOU 4309 N PHE B 262 3701 4644 5705 507 59 -527 N ATOM 4310 CA PHE B 262 5.941 23.822 13.933 1.00 31.97 C ANISOU 4310 CA PHE B 262 3062 4001 5083 501 50 -531 C ATOM 4311 C PHE B 262 4.434 23.657 13.978 1.00 31.83 C ANISOU 4311 C PHE B 262 3034 3984 5075 506 52 -525 C ATOM 4312 O PHE B 262 3.881 23.337 15.030 1.00 35.79 O ANISOU 4312 O PHE B 262 3528 4491 5578 512 60 -516 O ATOM 4313 CB PHE B 262 6.654 22.461 14.011 1.00 27.70 C ANISOU 4313 CB PHE B 262 2519 3458 4547 493 49 -530 C ATOM 4314 CG PHE B 262 6.144 21.420 13.025 1.00 25.91 C ANISOU 4314 CG PHE B 262 2286 3224 4334 486 41 -532 C ATOM 4315 CD1 PHE B 262 6.548 21.429 11.708 1.00 22.26 C ANISOU 4315 CD1 PHE B 262 1830 2753 3874 479 30 -542 C ATOM 4316 CD2 PHE B 262 5.303 20.394 13.448 1.00 28.50 C ANISOU 4316 CD2 PHE B 262 2603 3552 4673 487 44 -524 C ATOM 4317 CE1 PHE B 262 6.095 20.466 10.818 1.00 28.43 C ANISOU 4317 CE1 PHE B 262 2605 3527 4668 473 23 -544 C ATOM 4318 CE2 PHE B 262 4.860 19.421 12.562 1.00 25.08 C ANISOU 4318 CE2 PHE B 262 2165 3112 4253 481 36 -526 C ATOM 4319 CZ PHE B 262 5.260 19.459 11.247 1.00 24.20 C ANISOU 4319 CZ PHE B 262 2059 2992 4143 474 26 -536 C ATOM 4320 N LEU B 263 3.771 23.849 12.834 1.00 43.71 N ANISOU 4320 N LEU B 263 4538 5482 6587 505 44 -530 N ATOM 4321 CA LEU B 263 2.312 23.863 12.773 1.00 39.24 C ANISOU 4321 CA LEU B 263 3963 4916 6030 511 45 -525 C ATOM 4322 C LEU B 263 1.808 22.903 11.699 1.00 36.01 C ANISOU 4322 C LEU B 263 3548 4499 5635 504 36 -529 C ATOM 4323 O LEU B 263 2.301 22.916 10.566 1.00 29.90 O ANISOU 4323 O LEU B 263 2779 3718 4861 498 27 -538 O ATOM 4324 CB LEU B 263 1.791 25.298 12.498 1.00 29.38 C ANISOU 4324 CB LEU B 263 2719 3670 4776 518 45 -528 C ATOM 4325 CG LEU B 263 2.209 26.444 13.450 1.00 35.79 C ANISOU 4325 CG LEU B 263 3536 4488 5573 525 53 -526 C ATOM 4326 CD1 LEU B 263 3.541 27.094 13.028 1.00 31.31 C ANISOU 4326 CD1 LEU B 263 2982 3919 4995 521 50 -535 C ATOM 4327 CD2 LEU B 263 1.097 27.523 13.632 1.00 30.46 C ANISOU 4327 CD2 LEU B 263 2860 3817 4897 536 57 -523 C ATOM 4328 N TYR B 264 0.852 22.052 12.072 1.00 40.75 N ANISOU 4328 N TYR B 264 4137 5100 6245 506 39 -521 N ATOM 4329 CA TYR B 264 0.005 21.332 11.116 1.00 42.17 C ANISOU 4329 CA TYR B 264 4311 5274 6440 502 32 -523 C ATOM 4330 C TYR B 264 -1.413 21.379 11.666 1.00 42.65 C ANISOU 4330 C TYR B 264 4360 5338 6506 510 37 -515 C ATOM 4331 O TYR B 264 -1.945 20.375 12.156 1.00 45.55 O ANISOU 4331 O TYR B 264 4719 5707 6882 510 40 -508 O ATOM 4332 CB TYR B 264 0.500 19.899 10.912 1.00 51.66 C ANISOU 4332 CB TYR B 264 5509 6471 7649 493 28 -523 C ATOM 4333 CG TYR B 264 0.193 19.344 9.542 1.00 55.24 C ANISOU 4333 CG TYR B 264 5961 6916 8114 486 18 -530 C ATOM 4334 CD1 TYR B 264 1.202 18.857 8.730 1.00 57.96 C ANISOU 4334 CD1 TYR B 264 6311 7253 8457 477 10 -537 C ATOM 4335 CD2 TYR B 264 -1.095 19.374 9.036 1.00 54.51 C ANISOU 4335 CD2 TYR B 264 5861 6821 8030 489 15 -529 C ATOM 4336 CE1 TYR B 264 0.928 18.368 7.470 1.00 64.10 C ANISOU 4336 CE1 TYR B 264 7088 8023 9246 471 0 -544 C ATOM 4337 CE2 TYR B 264 -1.380 18.886 7.785 1.00 56.58 C ANISOU 4337 CE2 TYR B 264 6121 7074 8302 483 5 -535 C ATOM 4338 CZ TYR B 264 -0.369 18.386 7.002 1.00 66.78 C ANISOU 4338 CZ TYR B 264 7419 8359 9594 474 -2 -542 C ATOM 4339 OH TYR B 264 -0.664 17.904 5.744 1.00 76.80 O ANISOU 4339 OH TYR B 264 8687 9620 10872 468 -12 -548 O ATOM 4340 N PRO B 265 -2.079 22.525 11.547 1.00 44.33 N ANISOU 4340 N PRO B 265 4575 5554 6715 518 38 -515 N ATOM 4341 CA PRO B 265 -3.276 22.794 12.346 1.00 44.11 C ANISOU 4341 CA PRO B 265 4539 5532 6690 527 45 -506 C ATOM 4342 C PRO B 265 -4.566 22.382 11.654 1.00 41.92 C ANISOU 4342 C PRO B 265 4253 5251 6426 528 41 -506 C ATOM 4343 O PRO B 265 -4.583 22.006 10.482 1.00 38.29 O ANISOU 4343 O PRO B 265 3793 4783 5973 521 32 -512 O ATOM 4344 CB PRO B 265 -3.224 24.320 12.520 1.00 39.93 C ANISOU 4344 CB PRO B 265 4017 5006 6148 535 48 -508 C ATOM 4345 CG PRO B 265 -2.468 24.819 11.288 1.00 44.59 C ANISOU 4345 CG PRO B 265 4617 5590 6735 529 39 -520 C ATOM 4346 CD PRO B 265 -1.797 23.632 10.618 1.00 46.68 C ANISOU 4346 CD PRO B 265 4882 5849 7007 518 32 -524 C ATOM 4347 N ALA B 266 -5.658 22.498 12.406 1.00 44.57 N ANISOU 4347 N ALA B 266 4580 5592 6764 536 48 -497 N ATOM 4348 CA ALA B 266 -6.982 22.218 11.875 1.00 54.11 C ANISOU 4348 CA ALA B 266 5779 6797 7984 538 44 -496 C ATOM 4349 C ALA B 266 -7.499 23.402 11.058 1.00 71.24 C ANISOU 4349 C ALA B 266 7952 8965 10151 542 40 -501 C ATOM 4350 O ALA B 266 -7.177 24.568 11.330 1.00 70.43 O ANISOU 4350 O ALA B 266 7857 8866 10036 547 43 -502 O ATOM 4351 CB ALA B 266 -7.958 21.898 13.015 1.00 38.43 C ANISOU 4351 CB ALA B 266 3782 4818 6001 545 53 -485 C ATOM 4352 N ASN B 267 -8.303 23.085 10.040 1.00 82.43 N ANISOU 4352 N ASN B 267 9365 10377 11579 540 33 -504 N ATOM 4353 CA ASN B 267 -9.021 24.075 9.232 1.00 89.17 C ANISOU 4353 CA ASN B 267 10220 11230 12432 544 28 -508 C ATOM 4354 C ASN B 267 -10.416 23.515 8.959 1.00 87.05 C ANISOU 4354 C ASN B 267 9940 10960 12177 546 27 -504 C ATOM 4355 O ASN B 267 -10.812 22.493 9.527 1.00 84.35 O ANISOU 4355 O ASN B 267 9588 10619 11842 545 30 -498 O ATOM 4356 CB ASN B 267 -8.240 24.438 7.955 1.00 92.44 C ANISOU 4356 CB ASN B 267 10643 11636 12843 538 18 -520 C ATOM 4357 CG ASN B 267 -7.822 23.222 7.125 1.00 90.02 C ANISOU 4357 CG ASN B 267 10335 11322 12546 527 10 -524 C ATOM 4358 OD1 ASN B 267 -8.654 22.542 6.526 1.00 93.33 O ANISOU 4358 OD1 ASN B 267 10747 11737 12977 525 6 -524 O ATOM 4359 ND2 ASN B 267 -6.520 22.969 7.066 1.00 83.00 N ANISOU 4359 ND2 ASN B 267 9454 10430 11651 520 8 -529 N ATOM 4360 N LYS B 268 -11.202 24.186 8.115 1.00 87.65 N ANISOU 4360 N LYS B 268 10015 11034 12255 550 22 -508 N ATOM 4361 CA LYS B 268 -12.549 23.673 7.891 1.00 90.58 C ANISOU 4361 CA LYS B 268 10374 11404 12638 552 21 -504 C ATOM 4362 C LYS B 268 -12.514 22.368 7.099 1.00 94.60 C ANISOU 4362 C LYS B 268 10878 11905 13159 542 13 -507 C ATOM 4363 O LYS B 268 -13.303 21.455 7.366 1.00 95.87 O ANISOU 4363 O LYS B 268 11029 12067 13331 542 15 -501 O ATOM 4364 CB LYS B 268 -13.436 24.698 7.178 1.00 93.77 C ANISOU 4364 CB LYS B 268 10779 11808 13042 558 17 -507 C ATOM 4365 CG LYS B 268 -13.103 24.963 5.717 1.00 96.11 C ANISOU 4365 CG LYS B 268 11082 12097 13340 553 6 -517 C ATOM 4366 CD LYS B 268 -14.130 25.895 5.096 1.00 93.16 C ANISOU 4366 CD LYS B 268 10707 11724 12966 560 4 -519 C ATOM 4367 CE LYS B 268 -13.873 26.107 3.615 1.00 87.03 C ANISOU 4367 CE LYS B 268 9936 10939 12192 554 -7 -529 C ATOM 4368 NZ LYS B 268 -14.874 27.049 3.052 1.00 85.35 N ANISOU 4368 NZ LYS B 268 9721 10727 11979 562 -9 -530 N ATOM 4369 N LYS B 269 -11.587 22.254 6.139 1.00 97.17 N ANISOU 4369 N LYS B 269 11213 12225 13484 534 5 -516 N ATOM 4370 CA LYS B 269 -11.498 21.072 5.284 1.00 95.58 C ANISOU 4370 CA LYS B 269 11008 12016 13294 524 -3 -520 C ATOM 4371 C LYS B 269 -10.933 19.856 6.015 1.00 92.71 C ANISOU 4371 C LYS B 269 10641 11652 12934 519 1 -515 C ATOM 4372 O LYS B 269 -11.212 18.721 5.614 1.00 93.89 O ANISOU 4372 O LYS B 269 10783 11796 13095 513 -3 -515 O ATOM 4373 CB LYS B 269 -10.637 21.398 4.061 1.00 94.53 C ANISOU 4373 CB LYS B 269 10885 11876 13158 518 -13 -531 C ATOM 4374 CG LYS B 269 -11.248 22.463 3.161 1.00 93.62 C ANISOU 4374 CG LYS B 269 10772 11759 13040 522 -18 -536 C ATOM 4375 CD LYS B 269 -10.348 22.788 1.984 1.00 95.47 C ANISOU 4375 CD LYS B 269 11017 11987 13271 516 -27 -548 C ATOM 4376 CE LYS B 269 -10.968 23.852 1.090 1.00 95.27 C ANISOU 4376 CE LYS B 269 10994 11960 13244 521 -32 -553 C ATOM 4377 NZ LYS B 269 -12.208 23.388 0.410 1.00 93.60 N ANISOU 4377 NZ LYS B 269 10773 11746 13045 521 -37 -552 N ATOM 4378 N SER B 270 -10.148 20.063 7.069 1.00 85.32 N ANISOU 4378 N SER B 270 9709 10721 11988 521 8 -512 N ATOM 4379 CA SER B 270 -9.535 18.975 7.830 1.00 74.28 C ANISOU 4379 CA SER B 270 8308 9323 10591 516 13 -507 C ATOM 4380 C SER B 270 -9.635 19.368 9.289 1.00 78.46 C ANISOU 4380 C SER B 270 8835 9862 11113 524 24 -498 C ATOM 4381 O SER B 270 -8.645 19.770 9.910 1.00 83.30 O ANISOU 4381 O SER B 270 9456 10479 11715 525 28 -498 O ATOM 4382 CB SER B 270 -8.079 18.760 7.421 1.00 59.95 C ANISOU 4382 CB SER B 270 6504 7505 8772 508 8 -514 C ATOM 4383 OG SER B 270 -7.980 18.456 6.047 1.00 54.90 O ANISOU 4383 OG SER B 270 5866 6856 8138 500 -3 -523 O ATOM 4384 N PRO B 271 -10.824 19.246 9.885 1.00 78.27 N ANISOU 4384 N PRO B 271 8802 9843 11095 531 29 -490 N ATOM 4385 CA PRO B 271 -11.015 19.766 11.249 1.00 79.39 C ANISOU 4385 CA PRO B 271 8942 9994 11230 539 40 -482 C ATOM 4386 C PRO B 271 -10.235 19.004 12.301 1.00 79.73 C ANISOU 4386 C PRO B 271 8985 10040 11269 537 47 -477 C ATOM 4387 O PRO B 271 -10.081 19.504 13.426 1.00 77.25 O ANISOU 4387 O PRO B 271 8672 9734 10947 543 56 -471 O ATOM 4388 CB PRO B 271 -12.530 19.633 11.473 1.00 78.20 C ANISOU 4388 CB PRO B 271 8779 9845 11087 546 43 -475 C ATOM 4389 CG PRO B 271 -13.090 18.955 10.230 1.00 76.22 C ANISOU 4389 CG PRO B 271 8523 9586 10849 540 34 -480 C ATOM 4390 CD PRO B 271 -11.954 18.421 9.434 1.00 76.09 C ANISOU 4390 CD PRO B 271 8514 9563 10833 529 26 -488 C ATOM 4391 N ASN B 272 -9.728 17.822 11.960 1.00 75.54 N ANISOU 4391 N ASN B 272 8452 9503 10745 528 43 -479 N ATOM 4392 CA ASN B 272 -8.922 17.008 12.853 1.00 66.82 C ANISOU 4392 CA ASN B 272 7348 8402 9640 524 48 -474 C ATOM 4393 C ASN B 272 -7.476 16.888 12.389 1.00 57.24 C ANISOU 4393 C ASN B 272 6144 7183 8419 516 43 -482 C ATOM 4394 O ASN B 272 -6.773 15.966 12.806 1.00 55.09 O ANISOU 4394 O ASN B 272 5873 6911 8149 511 45 -480 O ATOM 4395 CB ASN B 272 -9.573 15.636 13.020 1.00 70.34 C ANISOU 4395 CB ASN B 272 7782 8845 10098 521 49 -469 C ATOM 4396 CG ASN B 272 -10.678 15.649 14.062 1.00 70.23 C ANISOU 4396 CG ASN B 272 7759 8838 10087 529 57 -459 C ATOM 4397 OD1 ASN B 272 -10.623 16.415 15.027 1.00 72.42 O ANISOU 4397 OD1 ASN B 272 8038 9123 10355 537 65 -454 O ATOM 4398 ND2 ASN B 272 -11.704 14.833 13.853 1.00 64.39 N ANISOU 4398 ND2 ASN B 272 7008 8096 9360 528 56 -456 N ATOM 4399 N GLY B 273 -7.039 17.741 11.473 1.00 52.59 N ANISOU 4399 N GLY B 273 5565 6592 7826 515 37 -490 N ATOM 4400 CA GLY B 273 -5.669 17.657 11.022 1.00 39.69 C ANISOU 4400 CA GLY B 273 3941 4954 6186 507 32 -497 C ATOM 4401 C GLY B 273 -5.473 16.541 10.024 1.00 40.90 C ANISOU 4401 C GLY B 273 4093 5098 6350 497 24 -502 C ATOM 4402 O GLY B 273 -6.422 15.979 9.480 1.00 41.20 O ANISOU 4402 O GLY B 273 4123 5133 6400 496 20 -502 O ATOM 4403 N LYS B 274 -4.196 16.235 9.771 1.00 43.45 N ANISOU 4403 N LYS B 274 4423 5418 6668 490 21 -508 N ATOM 4404 CA LYS B 274 -3.806 15.177 8.845 1.00 48.39 C ANISOU 4404 CA LYS B 274 5049 6035 7302 480 13 -513 C ATOM 4405 C LYS B 274 -2.881 14.158 9.501 1.00 45.84 C ANISOU 4405 C LYS B 274 4726 5712 6979 475 16 -510 C ATOM 4406 O LYS B 274 -2.931 12.964 9.195 1.00 43.55 O ANISOU 4406 O LYS B 274 4431 5417 6699 469 13 -509 O ATOM 4407 CB LYS B 274 -3.158 15.766 7.594 1.00 56.35 C ANISOU 4407 CB LYS B 274 6067 7037 8307 475 3 -524 C ATOM 4408 CG LYS B 274 -4.161 16.405 6.650 1.00 69.70 C ANISOU 4408 CG LYS B 274 7756 8725 10003 478 -3 -528 C ATOM 4409 CD LYS B 274 -5.326 15.455 6.386 1.00 76.55 C ANISOU 4409 CD LYS B 274 8612 9590 10886 477 -5 -524 C ATOM 4410 CE LYS B 274 -6.232 15.980 5.293 1.00 79.43 C ANISOU 4410 CE LYS B 274 8975 9950 11255 479 -12 -529 C ATOM 4411 NZ LYS B 274 -5.515 15.955 3.989 1.00 82.65 N ANISOU 4411 NZ LYS B 274 9391 10350 11664 471 -22 -540 N ATOM 4412 N LEU B 275 -2.016 14.612 10.388 1.00 44.06 N ANISOU 4412 N LEU B 275 4506 5492 6741 477 22 -508 N ATOM 4413 CA LEU B 275 -1.065 13.698 10.999 1.00 43.79 C ANISOU 4413 CA LEU B 275 4473 5459 6705 473 26 -505 C ATOM 4414 C LEU B 275 -1.792 12.691 11.892 1.00 41.18 C ANISOU 4414 C LEU B 275 4132 5132 6384 475 32 -495 C ATOM 4415 O LEU B 275 -2.917 12.923 12.348 1.00 35.23 O ANISOU 4415 O LEU B 275 3370 4382 5634 481 37 -489 O ATOM 4416 CB LEU B 275 -0.022 14.498 11.786 1.00 39.72 C ANISOU 4416 CB LEU B 275 3967 4951 6175 475 31 -505 C ATOM 4417 CG LEU B 275 0.693 15.524 10.900 1.00 35.55 C ANISOU 4417 CG LEU B 275 3450 4420 5639 474 25 -515 C ATOM 4418 CD1 LEU B 275 1.719 16.313 11.685 1.00 35.19 C ANISOU 4418 CD1 LEU B 275 3413 4380 5578 476 30 -515 C ATOM 4419 CD2 LEU B 275 1.347 14.845 9.695 1.00 32.66 C ANISOU 4419 CD2 LEU B 275 3088 4044 5278 463 14 -523 C ATOM 4420 N ARG B 276 -1.179 11.525 12.069 1.00 39.39 N ANISOU 4420 N ARG B 276 3903 4902 6161 468 33 -493 N ATOM 4421 CA ARG B 276 -1.807 10.444 12.822 1.00 36.53 C ANISOU 4421 CA ARG B 276 3529 4542 5807 469 38 -484 C ATOM 4422 C ARG B 276 -1.473 10.573 14.298 1.00 35.85 C ANISOU 4422 C ARG B 276 3444 4466 5713 474 49 -476 C ATOM 4423 O ARG B 276 -0.317 10.808 14.663 1.00 33.71 O ANISOU 4423 O ARG B 276 3181 4197 5431 473 51 -478 O ATOM 4424 CB ARG B 276 -1.356 9.076 12.310 1.00 41.38 C ANISOU 4424 CB ARG B 276 4143 5149 6431 459 34 -486 C ATOM 4425 CG ARG B 276 -1.526 8.842 10.822 1.00 44.37 C ANISOU 4425 CG ARG B 276 4522 5518 6818 453 23 -495 C ATOM 4426 CD ARG B 276 -2.951 8.531 10.499 1.00 48.69 C ANISOU 4426 CD ARG B 276 5060 6063 7378 455 21 -492 C ATOM 4427 NE ARG B 276 -3.123 8.250 9.083 1.00 56.83 N ANISOU 4427 NE ARG B 276 6091 7084 8417 448 11 -500 N ATOM 4428 CZ ARG B 276 -4.295 7.974 8.520 1.00 64.61 C ANISOU 4428 CZ ARG B 276 7068 8066 9414 449 7 -500 C ATOM 4429 NH1 ARG B 276 -5.398 7.942 9.261 1.00 68.45 N ANISOU 4429 NH1 ARG B 276 7546 8558 9905 455 14 -492 N ATOM 4430 NH2 ARG B 276 -4.363 7.720 7.223 1.00 64.83 N ANISOU 4430 NH2 ARG B 276 7098 8086 9450 443 -3 -508 N ATOM 4431 N LEU B 277 -2.496 10.399 15.145 1.00 32.34 N ANISOU 4431 N LEU B 277 2989 4026 5272 481 56 -467 N ATOM 4432 CA LEU B 277 -2.340 10.646 16.576 1.00 27.18 C ANISOU 4432 CA LEU B 277 2335 3382 4611 487 67 -459 C ATOM 4433 C LEU B 277 -1.444 9.613 17.254 1.00 32.72 C ANISOU 4433 C LEU B 277 3036 4084 5311 483 71 -455 C ATOM 4434 O LEU B 277 -0.597 9.972 18.078 1.00 42.49 O ANISOU 4434 O LEU B 277 4280 5328 6538 485 76 -453 O ATOM 4435 CB LEU B 277 -3.713 10.660 17.245 1.00 32.12 C ANISOU 4435 CB LEU B 277 2951 4013 5243 495 73 -451 C ATOM 4436 CG LEU B 277 -3.703 10.815 18.767 1.00 29.95 C ANISOU 4436 CG LEU B 277 2673 3747 4960 502 84 -442 C ATOM 4437 CD1 LEU B 277 -3.196 12.193 19.117 1.00 17.53 C ANISOU 4437 CD1 LEU B 277 1108 2180 3372 508 87 -444 C ATOM 4438 CD2 LEU B 277 -5.093 10.631 19.330 1.00 34.17 C ANISOU 4438 CD2 LEU B 277 3196 4285 5502 509 89 -434 C ATOM 4439 N LEU B 278 -1.622 8.329 16.934 1.00 33.27 N ANISOU 4439 N LEU B 278 3099 4148 5392 477 68 -454 N ATOM 4440 CA LEU B 278 -1.029 7.254 17.735 1.00 37.55 C ANISOU 4440 CA LEU B 278 3640 4693 5935 474 73 -448 C ATOM 4441 C LEU B 278 0.472 7.114 17.513 1.00 32.42 C ANISOU 4441 C LEU B 278 3000 4041 5278 468 70 -454 C ATOM 4442 O LEU B 278 1.210 6.807 18.456 1.00 29.48 O ANISOU 4442 O LEU B 278 2629 3674 4899 468 77 -449 O ATOM 4443 CB LEU B 278 -1.702 5.917 17.426 1.00 45.36 C ANISOU 4443 CB LEU B 278 4620 5676 6940 469 71 -446 C ATOM 4444 CG LEU B 278 -2.740 5.457 18.440 1.00 42.34 C ANISOU 4444 CG LEU B 278 4225 5299 6563 475 79 -436 C ATOM 4445 CD1 LEU B 278 -3.942 6.361 18.330 1.00 33.71 C ANISOU 4445 CD1 LEU B 278 3128 4208 5471 482 79 -435 C ATOM 4446 CD2 LEU B 278 -3.131 4.021 18.171 1.00 38.67 C ANISOU 4446 CD2 LEU B 278 3753 4828 6113 469 77 -433 C ATOM 4447 N TYR B 279 0.926 7.207 16.259 1.00 30.23 N ANISOU 4447 N TYR B 279 2729 3756 5002 461 61 -463 N ATOM 4448 CA TYR B 279 2.319 6.936 15.917 1.00 33.88 C ANISOU 4448 CA TYR B 279 3200 4215 5459 454 57 -469 C ATOM 4449 C TYR B 279 3.014 8.089 15.189 1.00 35.83 C ANISOU 4449 C TYR B 279 3457 4460 5695 453 52 -478 C ATOM 4450 O TYR B 279 4.112 7.881 14.658 1.00 38.02 O ANISOU 4450 O TYR B 279 3743 4734 5970 447 47 -484 O ATOM 4451 CB TYR B 279 2.416 5.655 15.084 1.00 41.11 C ANISOU 4451 CB TYR B 279 4112 5121 6386 445 51 -472 C ATOM 4452 CG TYR B 279 1.319 5.530 14.065 1.00 46.57 C ANISOU 4452 CG TYR B 279 4799 5806 7090 444 44 -475 C ATOM 4453 CD1 TYR B 279 1.396 6.196 12.846 1.00 43.59 C ANISOU 4453 CD1 TYR B 279 4428 5423 6712 441 35 -484 C ATOM 4454 CD2 TYR B 279 0.196 4.753 14.322 1.00 45.48 C ANISOU 4454 CD2 TYR B 279 4649 5668 6964 445 47 -468 C ATOM 4455 CE1 TYR B 279 0.385 6.085 11.917 1.00 45.96 C ANISOU 4455 CE1 TYR B 279 4722 5717 7023 440 29 -487 C ATOM 4456 CE2 TYR B 279 -0.811 4.635 13.395 1.00 43.69 C ANISOU 4456 CE2 TYR B 279 4417 5434 6748 444 40 -471 C ATOM 4457 CZ TYR B 279 -0.714 5.300 12.194 1.00 45.88 C ANISOU 4457 CZ TYR B 279 4701 5706 7025 441 31 -481 C ATOM 4458 OH TYR B 279 -1.727 5.177 11.279 1.00 49.31 O ANISOU 4458 OH TYR B 279 5130 6135 7470 440 25 -484 O ATOM 4459 N GLU B 280 2.394 9.280 15.118 1.00 30.35 N ANISOU 4459 N GLU B 280 2765 3769 4997 460 52 -479 N ATOM 4460 CA GLU B 280 3.052 10.517 14.689 1.00 28.40 C ANISOU 4460 CA GLU B 280 2529 3524 4740 461 49 -487 C ATOM 4461 C GLU B 280 2.911 11.637 15.717 1.00 23.09 C ANISOU 4461 C GLU B 280 1858 2860 4056 470 57 -482 C ATOM 4462 O GLU B 280 3.924 12.185 16.164 1.00 33.35 O ANISOU 4462 O GLU B 280 3165 4164 5343 471 60 -484 O ATOM 4463 CB GLU B 280 2.532 10.997 13.318 1.00 30.03 C ANISOU 4463 CB GLU B 280 2737 3723 4951 458 39 -495 C ATOM 4464 CG GLU B 280 2.911 10.109 12.128 1.00 31.57 C ANISOU 4464 CG GLU B 280 2933 3907 5154 448 29 -502 C ATOM 4465 CD GLU B 280 2.318 10.564 10.777 1.00 36.85 C ANISOU 4465 CD GLU B 280 3603 4569 5829 447 20 -510 C ATOM 4466 OE1 GLU B 280 1.312 11.320 10.741 1.00 38.73 O ANISOU 4466 OE1 GLU B 280 3838 4809 6068 453 21 -509 O ATOM 4467 OE2 GLU B 280 2.883 10.164 9.732 1.00 45.85 O ANISOU 4467 OE2 GLU B 280 4748 5702 6973 439 11 -518 O ATOM 4468 N CYS B 281 1.694 12.021 16.098 1.00 21.39 N ANISOU 4468 N CYS B 281 1636 2649 3844 477 61 -477 N ATOM 4469 CA CYS B 281 1.540 13.187 16.968 1.00 34.52 C ANISOU 4469 CA CYS B 281 3300 4320 5496 486 68 -474 C ATOM 4470 C CYS B 281 1.991 12.886 18.397 1.00 30.43 C ANISOU 4470 C CYS B 281 2780 3809 4971 490 78 -465 C ATOM 4471 O CYS B 281 2.794 13.633 18.963 1.00 36.02 O ANISOU 4471 O CYS B 281 3497 4524 5667 493 82 -466 O ATOM 4472 CB CYS B 281 0.090 13.692 16.950 1.00 37.97 C ANISOU 4472 CB CYS B 281 3731 4758 5939 494 69 -470 C ATOM 4473 SG CYS B 281 -0.518 14.317 15.353 1.00 36.93 S ANISOU 4473 SG CYS B 281 3602 4619 5813 492 58 -480 S ATOM 4474 N ASN B 282 1.524 11.773 18.982 1.00 25.76 N ANISOU 4474 N ASN B 282 2181 3220 4389 490 82 -458 N ATOM 4475 CA ASN B 282 1.821 11.483 20.391 1.00 26.31 C ANISOU 4475 CA ASN B 282 2247 3297 4452 494 92 -449 C ATOM 4476 C ASN B 282 3.310 11.302 20.670 1.00 35.95 C ANISOU 4476 C ASN B 282 3476 4520 5664 489 93 -451 C ATOM 4477 O ASN B 282 3.817 11.911 21.636 1.00 30.44 O ANISOU 4477 O ASN B 282 2782 3829 4954 494 100 -448 O ATOM 4478 CB ASN B 282 1.060 10.231 20.855 1.00 31.97 C ANISOU 4478 CB ASN B 282 2952 4013 5180 493 96 -441 C ATOM 4479 CG ASN B 282 -0.327 10.543 21.406 1.00 39.87 C ANISOU 4479 CG ASN B 282 3944 5019 6186 501 101 -434 C ATOM 4480 OD1 ASN B 282 -0.628 11.668 21.820 1.00 36.29 O ANISOU 4480 OD1 ASN B 282 3493 4571 5724 509 105 -433 O ATOM 4481 ND2 ASN B 282 -1.167 9.521 21.447 1.00 35.65 N ANISOU 4481 ND2 ASN B 282 3400 4482 5664 500 101 -430 N ATOM 4482 N PRO B 283 4.061 10.481 19.919 1.00 28.30 N ANISOU 4482 N PRO B 283 2510 3543 4698 480 87 -456 N ATOM 4483 CA PRO B 283 5.487 10.385 20.229 1.00 22.80 C ANISOU 4483 CA PRO B 283 1821 2849 3992 476 88 -458 C ATOM 4484 C PRO B 283 6.210 11.725 20.135 1.00 30.98 C ANISOU 4484 C PRO B 283 2869 3889 5015 479 87 -464 C ATOM 4485 O PRO B 283 7.006 12.035 21.032 1.00 35.52 O ANISOU 4485 O PRO B 283 3448 4470 5579 481 94 -462 O ATOM 4486 CB PRO B 283 5.989 9.342 19.215 1.00 27.20 C ANISOU 4486 CB PRO B 283 2379 3397 4557 466 80 -464 C ATOM 4487 CG PRO B 283 4.802 8.505 18.951 1.00 23.78 C ANISOU 4487 CG PRO B 283 1937 2961 4140 466 78 -460 C ATOM 4488 CD PRO B 283 3.660 9.469 18.916 1.00 16.95 C ANISOU 4488 CD PRO B 283 1068 2098 3276 473 79 -459 C ATOM 4489 N MET B 284 5.897 12.574 19.141 1.00 29.57 N ANISOU 4489 N MET B 284 2694 3706 4837 479 81 -472 N ATOM 4490 CA MET B 284 6.565 13.880 19.056 1.00 24.36 C ANISOU 4490 CA MET B 284 2044 3048 4163 481 80 -477 C ATOM 4491 C MET B 284 6.119 14.813 20.183 1.00 25.57 C ANISOU 4491 C MET B 284 2197 3211 4309 491 89 -471 C ATOM 4492 O MET B 284 6.939 15.542 20.757 1.00 27.12 O ANISOU 4492 O MET B 284 2399 3412 4492 494 94 -472 O ATOM 4493 CB MET B 284 6.290 14.534 17.694 1.00 24.94 C ANISOU 4493 CB MET B 284 2122 3114 4240 478 71 -487 C ATOM 4494 CG MET B 284 6.769 13.718 16.483 1.00 16.96 C ANISOU 4494 CG MET B 284 1113 2094 3236 468 61 -494 C ATOM 4495 SD MET B 284 8.520 13.315 16.586 1.00 36.51 S ANISOU 4495 SD MET B 284 3598 4569 5703 461 60 -498 S ATOM 4496 CE MET B 284 8.852 12.761 14.909 1.00 39.72 C ANISOU 4496 CE MET B 284 4009 4964 6119 451 47 -508 C ATOM 4497 N ALA B 285 4.834 14.785 20.537 1.00 27.30 N ANISOU 4497 N ALA B 285 2406 3431 4534 497 93 -465 N ATOM 4498 CA ALA B 285 4.365 15.594 21.660 1.00 36.15 C ANISOU 4498 CA ALA B 285 3526 4561 5648 507 102 -458 C ATOM 4499 C ALA B 285 5.056 15.187 22.955 1.00 34.00 C ANISOU 4499 C ALA B 285 3253 4296 5369 509 111 -451 C ATOM 4500 O ALA B 285 5.454 16.044 23.754 1.00 27.46 O ANISOU 4500 O ALA B 285 2430 3476 4529 514 117 -449 O ATOM 4501 CB ALA B 285 2.847 15.477 21.797 1.00 36.36 C ANISOU 4501 CB ALA B 285 3542 4588 5685 513 104 -452 C ATOM 4502 N TYR B 286 5.230 13.881 23.160 1.00 40.43 N ANISOU 4502 N TYR B 286 4062 5109 6190 504 112 -447 N ATOM 4503 CA TYR B 286 5.940 13.398 24.337 1.00 30.14 C ANISOU 4503 CA TYR B 286 2759 3813 4881 505 120 -441 C ATOM 4504 C TYR B 286 7.378 13.896 24.345 1.00 31.24 C ANISOU 4504 C TYR B 286 2909 3954 5007 502 119 -446 C ATOM 4505 O TYR B 286 7.857 14.412 25.360 1.00 38.00 O ANISOU 4505 O TYR B 286 3768 4818 5852 507 126 -443 O ATOM 4506 CB TYR B 286 5.897 11.873 24.364 1.00 23.32 C ANISOU 4506 CB TYR B 286 1887 2946 4027 500 119 -437 C ATOM 4507 CG TYR B 286 6.485 11.179 25.583 1.00 23.22 C ANISOU 4507 CG TYR B 286 1873 2941 4011 501 127 -429 C ATOM 4508 CD1 TYR B 286 5.773 11.062 26.759 1.00 26.70 C ANISOU 4508 CD1 TYR B 286 2305 3388 4451 508 136 -420 C ATOM 4509 CD2 TYR B 286 7.732 10.588 25.522 1.00 27.49 C ANISOU 4509 CD2 TYR B 286 2418 3480 4547 494 125 -432 C ATOM 4510 CE1 TYR B 286 6.300 10.392 27.851 1.00 34.87 C ANISOU 4510 CE1 TYR B 286 3338 4429 5482 509 143 -413 C ATOM 4511 CE2 TYR B 286 8.265 9.920 26.596 1.00 36.90 C ANISOU 4511 CE2 TYR B 286 3608 4677 5735 495 133 -425 C ATOM 4512 CZ TYR B 286 7.551 9.823 27.759 1.00 36.01 C ANISOU 4512 CZ TYR B 286 3487 4572 5622 502 142 -416 C ATOM 4513 OH TYR B 286 8.091 9.149 28.824 1.00 38.77 O ANISOU 4513 OH TYR B 286 3835 4928 5968 503 149 -409 O ATOM 4514 N VAL B 287 8.083 13.760 23.217 1.00 32.87 N ANISOU 4514 N VAL B 287 3122 4153 5216 494 110 -455 N ATOM 4515 CA VAL B 287 9.466 14.234 23.158 1.00 31.14 C ANISOU 4515 CA VAL B 287 2914 3935 4984 491 109 -461 C ATOM 4516 C VAL B 287 9.536 15.725 23.502 1.00 33.02 C ANISOU 4516 C VAL B 287 3158 4179 5211 498 112 -463 C ATOM 4517 O VAL B 287 10.362 16.146 24.321 1.00 25.35 O ANISOU 4517 O VAL B 287 2191 3213 4227 500 118 -461 O ATOM 4518 CB VAL B 287 10.089 13.935 21.781 1.00 25.32 C ANISOU 4518 CB VAL B 287 2181 3188 4250 481 98 -471 C ATOM 4519 CG1 VAL B 287 11.484 14.569 21.694 1.00 22.51 C ANISOU 4519 CG1 VAL B 287 1837 2833 3881 478 96 -477 C ATOM 4520 CG2 VAL B 287 10.177 12.433 21.542 1.00 22.62 C ANISOU 4520 CG2 VAL B 287 1834 2841 3919 475 95 -469 C ATOM 4521 N MET B 288 8.659 16.542 22.895 1.00 36.56 N ANISOU 4521 N MET B 288 3606 4624 5662 501 109 -466 N ATOM 4522 CA MET B 288 8.679 17.984 23.152 1.00 32.82 C ANISOU 4522 CA MET B 288 3138 4154 5176 508 112 -468 C ATOM 4523 C MET B 288 8.465 18.281 24.629 1.00 31.56 C ANISOU 4523 C MET B 288 2976 4006 5011 516 124 -459 C ATOM 4524 O MET B 288 9.223 19.048 25.233 1.00 37.33 O ANISOU 4524 O MET B 288 3713 4741 5728 519 128 -459 O ATOM 4525 CB MET B 288 7.632 18.726 22.293 1.00 31.21 C ANISOU 4525 CB MET B 288 2934 3946 4978 510 107 -472 C ATOM 4526 CG MET B 288 8.083 18.993 20.845 1.00 22.60 C ANISOU 4526 CG MET B 288 1850 2847 3889 503 96 -483 C ATOM 4527 SD MET B 288 9.473 20.173 20.749 1.00 26.17 S ANISOU 4527 SD MET B 288 2317 3301 4325 502 95 -491 S ATOM 4528 CE MET B 288 9.690 20.382 18.995 1.00 35.88 C ANISOU 4528 CE MET B 288 3552 4520 5558 494 82 -504 C ATOM 4529 N GLU B 289 7.465 17.658 25.249 1.00 37.39 N ANISOU 4529 N GLU B 289 3703 4746 5756 520 128 -450 N ATOM 4530 CA GLU B 289 7.209 17.989 26.652 1.00 36.18 C ANISOU 4530 CA GLU B 289 3548 4603 5597 529 139 -441 C ATOM 4531 C GLU B 289 8.370 17.553 27.532 1.00 36.00 C ANISOU 4531 C GLU B 289 3528 4585 5565 527 145 -438 C ATOM 4532 O GLU B 289 8.776 18.291 28.439 1.00 36.17 O ANISOU 4532 O GLU B 289 3553 4614 5576 533 152 -436 O ATOM 4533 CB GLU B 289 5.892 17.370 27.140 1.00 30.83 C ANISOU 4533 CB GLU B 289 2858 3927 4930 534 143 -433 C ATOM 4534 CG GLU B 289 4.629 18.110 26.665 1.00 33.88 C ANISOU 4534 CG GLU B 289 3241 4312 5321 539 141 -433 C ATOM 4535 CD GLU B 289 3.372 17.848 27.521 1.00 42.74 C ANISOU 4535 CD GLU B 289 4352 5438 6449 546 148 -424 C ATOM 4536 OE1 GLU B 289 3.473 17.308 28.647 1.00 45.04 O ANISOU 4536 OE1 GLU B 289 4640 5737 6738 549 156 -416 O ATOM 4537 OE2 GLU B 289 2.264 18.179 27.048 1.00 45.97 O ANISOU 4537 OE2 GLU B 289 4757 5846 6865 550 146 -424 O ATOM 4538 N LYS B 290 8.961 16.389 27.246 1.00 36.12 N ANISOU 4538 N LYS B 290 3542 4597 5586 520 141 -439 N ATOM 4539 CA LYS B 290 10.108 15.952 28.032 1.00 20.52 C ANISOU 4539 CA LYS B 290 1569 2626 3602 518 146 -437 C ATOM 4540 C LYS B 290 11.305 16.883 27.878 1.00 30.84 C ANISOU 4540 C LYS B 290 2887 3934 4895 516 144 -444 C ATOM 4541 O LYS B 290 12.113 16.978 28.808 1.00 34.14 O ANISOU 4541 O LYS B 290 3309 4359 5304 518 151 -441 O ATOM 4542 CB LYS B 290 10.495 14.520 27.631 1.00 17.64 C ANISOU 4542 CB LYS B 290 1200 2256 3246 509 141 -437 C ATOM 4543 CG LYS B 290 9.548 13.417 28.119 1.00 29.70 C ANISOU 4543 CG LYS B 290 2716 3784 4785 511 145 -428 C ATOM 4544 CD LYS B 290 9.430 13.442 29.647 1.00 34.07 C ANISOU 4544 CD LYS B 290 3266 4348 5332 519 156 -418 C ATOM 4545 CE LYS B 290 8.576 12.300 30.160 1.00 40.86 C ANISOU 4545 CE LYS B 290 4114 5209 6203 520 160 -410 C ATOM 4546 NZ LYS B 290 8.240 12.445 31.618 1.00 42.10 N ANISOU 4546 NZ LYS B 290 4266 5376 6354 528 171 -400 N ATOM 4547 N ALA B 291 11.387 17.649 26.782 1.00 36.77 N ANISOU 4547 N ALA B 291 3645 4679 5646 513 137 -453 N ATOM 4548 CA ALA B 291 12.472 18.600 26.556 1.00 34.61 C ANISOU 4548 CA ALA B 291 3383 4406 5360 512 135 -460 C ATOM 4549 C ALA B 291 12.106 20.034 26.971 1.00 40.70 C ANISOU 4549 C ALA B 291 4159 5183 6124 520 140 -460 C ATOM 4550 O ALA B 291 12.846 20.980 26.654 1.00 32.84 O ANISOU 4550 O ALA B 291 3173 4187 5119 519 138 -467 O ATOM 4551 CB ALA B 291 12.891 18.564 25.080 1.00 29.02 C ANISOU 4551 CB ALA B 291 2681 3689 4657 503 124 -471 C ATOM 4552 N GLY B 292 10.990 20.211 27.677 1.00 44.51 N ANISOU 4552 N GLY B 292 4634 5669 6608 528 146 -453 N ATOM 4553 CA GLY B 292 10.570 21.518 28.148 1.00 42.82 C ANISOU 4553 CA GLY B 292 4423 5461 6387 537 151 -452 C ATOM 4554 C GLY B 292 9.798 22.353 27.154 1.00 44.64 C ANISOU 4554 C GLY B 292 4654 5685 6620 538 145 -457 C ATOM 4555 O GLY B 292 9.697 23.571 27.337 1.00 46.10 O ANISOU 4555 O GLY B 292 4845 5873 6798 544 148 -459 O ATOM 4556 N GLY B 293 9.242 21.735 26.108 1.00 41.36 N ANISOU 4556 N GLY B 293 4236 5262 6218 533 137 -461 N ATOM 4557 CA GLY B 293 8.426 22.420 25.136 1.00 28.00 C ANISOU 4557 CA GLY B 293 2544 3565 4530 534 132 -466 C ATOM 4558 C GLY B 293 6.962 22.083 25.325 1.00 35.17 C ANISOU 4558 C GLY B 293 3442 4474 5449 540 134 -459 C ATOM 4559 O GLY B 293 6.562 21.481 26.322 1.00 43.94 O ANISOU 4559 O GLY B 293 4544 5589 6561 543 141 -450 O ATOM 4560 N MET B 294 6.163 22.457 24.328 1.00 31.16 N ANISOU 4560 N MET B 294 2932 3959 4947 540 127 -463 N ATOM 4561 CA MET B 294 4.716 22.319 24.395 1.00 24.78 C ANISOU 4561 CA MET B 294 2114 3151 4149 545 129 -457 C ATOM 4562 C MET B 294 4.187 21.697 23.109 1.00 30.97 C ANISOU 4562 C MET B 294 2895 3927 4946 539 119 -462 C ATOM 4563 O MET B 294 4.813 21.789 22.056 1.00 29.21 O ANISOU 4563 O MET B 294 2678 3697 4722 532 111 -471 O ATOM 4564 CB MET B 294 4.055 23.681 24.611 1.00 20.70 C ANISOU 4564 CB MET B 294 1600 2639 3626 554 133 -457 C ATOM 4565 CG MET B 294 4.338 24.301 25.973 1.00 29.83 C ANISOU 4565 CG MET B 294 2759 3804 4771 562 143 -451 C ATOM 4566 SD MET B 294 3.492 25.870 26.124 1.00 39.95 S ANISOU 4566 SD MET B 294 4043 5090 6047 572 147 -451 S ATOM 4567 CE MET B 294 2.162 25.374 27.206 1.00 40.23 C ANISOU 4567 CE MET B 294 4065 5131 6089 581 156 -438 C ATOM 4568 N ALA B 295 3.005 21.086 23.192 1.00 21.98 N ANISOU 4568 N ALA B 295 1746 2788 3819 541 120 -456 N ATOM 4569 CA ALA B 295 2.386 20.504 22.007 1.00 30.73 C ANISOU 4569 CA ALA B 295 2849 3887 4939 536 111 -460 C ATOM 4570 C ALA B 295 0.880 20.463 22.225 1.00 34.52 C ANISOU 4570 C ALA B 295 3319 4369 5427 543 114 -454 C ATOM 4571 O ALA B 295 0.394 19.697 23.063 1.00 41.40 O ANISOU 4571 O ALA B 295 4182 5245 6304 545 119 -446 O ATOM 4572 CB ALA B 295 2.956 19.116 21.708 1.00 23.01 C ANISOU 4572 CB ALA B 295 1869 2905 3969 527 107 -461 C ATOM 4573 N THR B 296 0.154 21.262 21.438 1.00 30.30 N ANISOU 4573 N THR B 296 2786 3832 4896 545 109 -458 N ATOM 4574 CA THR B 296 -1.282 21.463 21.531 1.00 27.96 C ANISOU 4574 CA THR B 296 2481 3537 4606 552 111 -453 C ATOM 4575 C THR B 296 -1.948 21.153 20.199 1.00 31.35 C ANISOU 4575 C THR B 296 2907 3957 5046 548 102 -459 C ATOM 4576 O THR B 296 -1.303 21.108 19.143 1.00 42.20 O ANISOU 4576 O THR B 296 4288 5325 6422 540 93 -467 O ATOM 4577 CB THR B 296 -1.641 22.916 21.920 1.00 38.38 C ANISOU 4577 CB THR B 296 3805 4861 5916 562 116 -453 C ATOM 4578 OG1 THR B 296 -3.063 23.074 21.904 1.00 39.14 O ANISOU 4578 OG1 THR B 296 3893 4959 6020 568 117 -448 O ATOM 4579 CG2 THR B 296 -1.034 23.939 20.939 1.00 27.15 C ANISOU 4579 CG2 THR B 296 2393 3434 4487 559 110 -463 C ATOM 4580 N THR B 297 -3.243 20.880 20.277 1.00 28.53 N ANISOU 4580 N THR B 297 2540 3601 4699 552 103 -454 N ATOM 4581 CA THR B 297 -4.126 20.873 19.115 1.00 36.51 C ANISOU 4581 CA THR B 297 3548 4606 5720 550 95 -458 C ATOM 4582 C THR B 297 -4.734 22.251 18.878 1.00 38.60 C ANISOU 4582 C THR B 297 3816 4872 5980 558 95 -460 C ATOM 4583 O THR B 297 -5.449 22.446 17.888 1.00 35.83 O ANISOU 4583 O THR B 297 3462 4515 5635 557 89 -464 O ATOM 4584 CB THR B 297 -5.249 19.833 19.284 1.00 33.76 C ANISOU 4584 CB THR B 297 3186 4256 5385 550 96 -451 C ATOM 4585 OG1 THR B 297 -6.209 20.287 20.249 1.00 38.39 O ANISOU 4585 OG1 THR B 297 3767 4851 5970 560 104 -443 O ATOM 4586 CG2 THR B 297 -4.672 18.508 19.774 1.00 30.74 C ANISOU 4586 CG2 THR B 297 2800 3873 5006 544 98 -447 C ATOM 4587 N GLY B 298 -4.452 23.208 19.765 1.00 41.43 N ANISOU 4587 N GLY B 298 4179 5237 6326 565 103 -457 N ATOM 4588 CA GLY B 298 -5.147 24.478 19.792 1.00 43.06 C ANISOU 4588 CA GLY B 298 4387 5447 6528 574 105 -457 C ATOM 4589 C GLY B 298 -6.156 24.499 20.920 1.00 44.28 C ANISOU 4589 C GLY B 298 4533 5608 6683 583 114 -447 C ATOM 4590 O GLY B 298 -6.271 25.490 21.639 1.00 49.22 O ANISOU 4590 O GLY B 298 5162 6240 7299 591 121 -444 O ATOM 4591 N LYS B 299 -6.869 23.389 21.111 1.00 51.81 N ANISOU 4591 N LYS B 299 5476 6562 7648 581 115 -441 N ATOM 4592 CA LYS B 299 -7.840 23.271 22.188 1.00 47.16 C ANISOU 4592 CA LYS B 299 4878 5980 7061 589 123 -431 C ATOM 4593 C LYS B 299 -7.310 22.540 23.413 1.00 47.27 C ANISOU 4593 C LYS B 299 4889 6000 7072 589 131 -424 C ATOM 4594 O LYS B 299 -7.784 22.802 24.522 1.00 48.21 O ANISOU 4594 O LYS B 299 5004 6125 7187 597 140 -417 O ATOM 4595 CB LYS B 299 -9.097 22.565 21.684 1.00 49.74 C ANISOU 4595 CB LYS B 299 5193 6303 7402 589 120 -429 C ATOM 4596 CG LYS B 299 -9.874 23.400 20.682 1.00 60.67 C ANISOU 4596 CG LYS B 299 6579 7685 8790 592 114 -434 C ATOM 4597 CD LYS B 299 -11.004 22.617 20.045 1.00 68.00 C ANISOU 4597 CD LYS B 299 7496 8608 9732 590 109 -433 C ATOM 4598 CE LYS B 299 -11.704 23.455 18.972 1.00 78.17 C ANISOU 4598 CE LYS B 299 8786 9892 11022 592 103 -438 C ATOM 4599 NZ LYS B 299 -12.680 22.653 18.177 1.00 79.65 N ANISOU 4599 NZ LYS B 299 8964 10074 11224 589 97 -439 N ATOM 4600 N GLU B 300 -6.334 21.648 23.262 1.00 47.92 N ANISOU 4600 N GLU B 300 4973 6078 7155 580 128 -427 N ATOM 4601 CA GLU B 300 -5.845 20.892 24.408 1.00 51.62 C ANISOU 4601 CA GLU B 300 5440 6552 7622 580 135 -420 C ATOM 4602 C GLU B 300 -4.477 20.317 24.076 1.00 50.93 C ANISOU 4602 C GLU B 300 5359 6461 7532 571 131 -425 C ATOM 4603 O GLU B 300 -4.047 20.306 22.920 1.00 47.99 O ANISOU 4603 O GLU B 300 4991 6081 7162 564 122 -434 O ATOM 4604 CB GLU B 300 -6.801 19.761 24.790 1.00 56.47 C ANISOU 4604 CB GLU B 300 6041 7167 8249 580 137 -413 C ATOM 4605 CG GLU B 300 -7.057 18.798 23.651 1.00 62.40 C ANISOU 4605 CG GLU B 300 6787 7909 9012 571 128 -417 C ATOM 4606 CD GLU B 300 -8.215 17.874 23.928 1.00 66.62 C ANISOU 4606 CD GLU B 300 7310 8444 9560 573 130 -410 C ATOM 4607 OE1 GLU B 300 -8.457 17.547 25.112 1.00 64.51 O ANISOU 4607 OE1 GLU B 300 7037 8184 9291 577 139 -402 O ATOM 4608 OE2 GLU B 300 -8.871 17.455 22.955 1.00 73.11 O ANISOU 4608 OE2 GLU B 300 8126 9259 10392 569 123 -413 O ATOM 4609 N ALA B 301 -3.815 19.805 25.111 1.00 46.54 N ANISOU 4609 N ALA B 301 4802 5909 6971 570 138 -420 N ATOM 4610 CA ALA B 301 -2.554 19.098 24.929 1.00 39.90 C ANISOU 4610 CA ALA B 301 3967 5066 6129 562 135 -424 C ATOM 4611 C ALA B 301 -2.763 17.812 24.143 1.00 44.53 C ANISOU 4611 C ALA B 301 4546 5644 6728 553 128 -425 C ATOM 4612 O ALA B 301 -3.699 17.047 24.403 1.00 51.04 O ANISOU 4612 O ALA B 301 5361 6470 7563 554 130 -420 O ATOM 4613 CB ALA B 301 -1.937 18.770 26.285 1.00 25.21 C ANISOU 4613 CB ALA B 301 2106 3213 4261 564 144 -417 C ATOM 4614 N VAL B 302 -1.858 17.563 23.192 1.00 44.22 N ANISOU 4614 N VAL B 302 4514 5598 6689 545 120 -433 N ATOM 4615 CA VAL B 302 -1.936 16.359 22.364 1.00 39.40 C ANISOU 4615 CA VAL B 302 3899 4980 6091 536 113 -436 C ATOM 4616 C VAL B 302 -1.996 15.107 23.236 1.00 37.83 C ANISOU 4616 C VAL B 302 3693 4784 5898 535 118 -428 C ATOM 4617 O VAL B 302 -2.853 14.238 23.041 1.00 40.04 O ANISOU 4617 O VAL B 302 3963 5060 6190 533 117 -425 O ATOM 4618 CB VAL B 302 -0.753 16.329 21.372 1.00 29.75 C ANISOU 4618 CB VAL B 302 2687 3752 4866 527 105 -446 C ATOM 4619 CG1 VAL B 302 -0.656 14.989 20.683 1.00 31.63 C ANISOU 4619 CG1 VAL B 302 2921 3982 5116 518 99 -447 C ATOM 4620 CG2 VAL B 302 -0.927 17.433 20.330 1.00 27.68 C ANISOU 4620 CG2 VAL B 302 2430 3485 4601 528 98 -454 C ATOM 4621 N LEU B 303 -1.162 15.047 24.273 1.00 31.03 N ANISOU 4621 N LEU B 303 2834 3930 5028 536 125 -424 N ATOM 4622 CA LEU B 303 -1.066 13.864 25.118 1.00 35.82 C ANISOU 4622 CA LEU B 303 3433 4538 5637 535 131 -417 C ATOM 4623 C LEU B 303 -2.339 13.576 25.915 1.00 40.29 C ANISOU 4623 C LEU B 303 3989 5109 6211 541 137 -407 C ATOM 4624 O LEU B 303 -2.450 12.481 26.486 1.00 39.84 O ANISOU 4624 O LEU B 303 3925 5054 6160 540 140 -401 O ATOM 4625 CB LEU B 303 0.111 14.027 26.076 1.00 18.07 C ANISOU 4625 CB LEU B 303 1192 2296 3377 536 137 -414 C ATOM 4626 CG LEU B 303 1.504 14.140 25.428 1.00 30.21 C ANISOU 4626 CG LEU B 303 2741 3830 4908 528 131 -423 C ATOM 4627 CD1 LEU B 303 2.574 14.375 26.504 1.00 21.94 C ANISOU 4627 CD1 LEU B 303 1698 2790 3847 530 139 -420 C ATOM 4628 CD2 LEU B 303 1.859 12.928 24.559 1.00 26.09 C ANISOU 4628 CD2 LEU B 303 2217 3300 4396 518 124 -426 C ATOM 4629 N ASP B 304 -3.295 14.512 25.965 1.00 37.78 N ANISOU 4629 N ASP B 304 3669 4794 5892 549 139 -406 N ATOM 4630 CA ASP B 304 -4.546 14.312 26.691 1.00 39.27 C ANISOU 4630 CA ASP B 304 3847 4987 6086 556 145 -398 C ATOM 4631 C ASP B 304 -5.692 13.820 25.822 1.00 41.85 C ANISOU 4631 C ASP B 304 4165 5307 6427 553 139 -399 C ATOM 4632 O ASP B 304 -6.769 13.548 26.355 1.00 49.56 O ANISOU 4632 O ASP B 304 5132 6287 7410 558 143 -392 O ATOM 4633 CB ASP B 304 -4.986 15.600 27.390 1.00 36.92 C ANISOU 4633 CB ASP B 304 3551 4697 5780 566 151 -395 C ATOM 4634 CG ASP B 304 -4.119 15.939 28.582 1.00 42.63 C ANISOU 4634 CG ASP B 304 4280 5429 6490 570 159 -391 C ATOM 4635 OD1 ASP B 304 -3.610 14.987 29.229 1.00 44.28 O ANISOU 4635 OD1 ASP B 304 4485 5639 6699 567 163 -387 O ATOM 4636 OD2 ASP B 304 -3.968 17.151 28.879 1.00 35.78 O ANISOU 4636 OD2 ASP B 304 3418 4566 5612 576 163 -392 O ATOM 4637 N VAL B 305 -5.513 13.741 24.507 1.00 44.75 N ANISOU 4637 N VAL B 305 4536 5666 6800 547 129 -407 N ATOM 4638 CA VAL B 305 -6.554 13.197 23.647 1.00 37.74 C ANISOU 4638 CA VAL B 305 3641 4772 5926 544 123 -408 C ATOM 4639 C VAL B 305 -6.667 11.694 23.898 1.00 38.49 C ANISOU 4639 C VAL B 305 3728 4865 6032 539 124 -404 C ATOM 4640 O VAL B 305 -5.660 10.976 23.910 1.00 36.76 O ANISOU 4640 O VAL B 305 3511 4643 5811 532 123 -405 O ATOM 4641 CB VAL B 305 -6.232 13.495 22.173 1.00 31.86 C ANISOU 4641 CB VAL B 305 2903 4019 5184 538 112 -419 C ATOM 4642 CG1 VAL B 305 -7.286 12.892 21.255 1.00 35.34 C ANISOU 4642 CG1 VAL B 305 3335 4453 5639 535 106 -420 C ATOM 4643 CG2 VAL B 305 -6.056 14.988 21.935 1.00 30.66 C ANISOU 4643 CG2 VAL B 305 2760 3869 5021 543 112 -423 C ATOM 4644 N ILE B 306 -7.884 11.206 24.107 1.00 33.11 N ANISOU 4644 N ILE B 306 3035 4183 5360 541 126 -398 N ATOM 4645 CA ILE B 306 -8.134 9.774 24.264 1.00 39.78 C ANISOU 4645 CA ILE B 306 3871 5025 6217 536 127 -394 C ATOM 4646 C ILE B 306 -8.598 9.211 22.923 1.00 43.44 C ANISOU 4646 C ILE B 306 4332 5479 6693 530 117 -400 C ATOM 4647 O ILE B 306 -9.652 9.630 22.419 1.00 49.36 O ANISOU 4647 O ILE B 306 5078 6228 7449 533 114 -400 O ATOM 4648 CB ILE B 306 -9.147 9.488 25.379 1.00 40.12 C ANISOU 4648 CB ILE B 306 3905 5076 6264 543 135 -384 C ATOM 4649 CG1 ILE B 306 -8.530 9.852 26.737 1.00 35.37 C ANISOU 4649 CG1 ILE B 306 3306 4483 5649 549 145 -378 C ATOM 4650 CG2 ILE B 306 -9.565 8.031 25.337 1.00 41.21 C ANISOU 4650 CG2 ILE B 306 4034 5210 6416 538 134 -380 C ATOM 4651 CD1 ILE B 306 -9.319 9.343 27.919 1.00 32.05 C ANISOU 4651 CD1 ILE B 306 2876 4069 5233 555 153 -368 C ATOM 4652 N PRO B 307 -7.848 8.303 22.304 1.00 36.81 N ANISOU 4652 N PRO B 307 3495 4633 5858 520 112 -404 N ATOM 4653 CA PRO B 307 -8.200 7.845 20.955 1.00 44.66 C ANISOU 4653 CA PRO B 307 4488 5618 6864 513 102 -410 C ATOM 4654 C PRO B 307 -9.301 6.792 20.958 1.00 56.92 C ANISOU 4654 C PRO B 307 6028 7167 8431 512 102 -405 C ATOM 4655 O PRO B 307 -9.504 6.061 21.932 1.00 64.21 O ANISOU 4655 O PRO B 307 6945 8095 9357 514 109 -397 O ATOM 4656 CB PRO B 307 -6.886 7.250 20.434 1.00 34.51 C ANISOU 4656 CB PRO B 307 3209 4326 5576 504 97 -416 C ATOM 4657 CG PRO B 307 -6.195 6.782 21.665 1.00 35.58 C ANISOU 4657 CG PRO B 307 3345 4468 5706 505 105 -409 C ATOM 4658 CD PRO B 307 -6.560 7.757 22.759 1.00 28.93 C ANISOU 4658 CD PRO B 307 2502 3635 4854 516 114 -403 C ATOM 4659 N THR B 308 -10.039 6.746 19.844 1.00 50.31 N ANISOU 4659 N THR B 308 5188 6324 7604 510 95 -410 N ATOM 4660 CA THR B 308 -11.040 5.713 19.616 1.00 43.21 C ANISOU 4660 CA THR B 308 4278 5421 6720 507 93 -407 C ATOM 4661 C THR B 308 -10.738 4.838 18.411 1.00 48.37 C ANISOU 4661 C THR B 308 4932 6064 7383 497 84 -413 C ATOM 4662 O THR B 308 -11.406 3.816 18.229 1.00 54.49 O ANISOU 4662 O THR B 308 5698 6834 8170 494 83 -411 O ATOM 4663 CB THR B 308 -12.437 6.331 19.433 1.00 46.50 C ANISOU 4663 CB THR B 308 4688 5839 7141 514 93 -405 C ATOM 4664 OG1 THR B 308 -12.466 7.132 18.242 1.00 46.32 O ANISOU 4664 OG1 THR B 308 4671 5811 7117 512 85 -414 O ATOM 4665 CG2 THR B 308 -12.797 7.194 20.634 1.00 49.63 C ANISOU 4665 CG2 THR B 308 5083 6245 7528 524 102 -398 C ATOM 4666 N ASP B 309 -9.770 5.209 17.582 1.00 46.26 N ANISOU 4666 N ASP B 309 4675 5791 7110 492 77 -422 N ATOM 4667 CA ASP B 309 -9.418 4.451 16.392 1.00 47.02 C ANISOU 4667 CA ASP B 309 4773 5878 7215 483 68 -429 C ATOM 4668 C ASP B 309 -7.908 4.493 16.230 1.00 44.85 C ANISOU 4668 C ASP B 309 4509 5601 6930 477 66 -434 C ATOM 4669 O ASP B 309 -7.293 5.552 16.387 1.00 46.79 O ANISOU 4669 O ASP B 309 4763 5851 7164 481 67 -436 O ATOM 4670 CB ASP B 309 -10.123 5.016 15.144 1.00 48.61 C ANISOU 4670 CB ASP B 309 4975 6074 7421 482 60 -436 C ATOM 4671 CG ASP B 309 -9.861 4.190 13.881 1.00 57.66 C ANISOU 4671 CG ASP B 309 6122 7210 8577 472 50 -443 C ATOM 4672 OD1 ASP B 309 -8.750 4.276 13.315 1.00 58.45 O ANISOU 4672 OD1 ASP B 309 6231 7305 8671 467 45 -449 O ATOM 4673 OD2 ASP B 309 -10.768 3.448 13.452 1.00 64.05 O ANISOU 4673 OD2 ASP B 309 6923 8015 9400 470 48 -442 O ATOM 4674 N ILE B 310 -7.310 3.338 15.921 1.00 40.52 N ANISOU 4674 N ILE B 310 3960 5047 6388 469 63 -435 N ATOM 4675 CA ILE B 310 -5.853 3.272 15.896 1.00 41.94 C ANISOU 4675 CA ILE B 310 4151 5226 6560 464 62 -439 C ATOM 4676 C ILE B 310 -5.260 4.166 14.811 1.00 46.45 C ANISOU 4676 C ILE B 310 4731 5793 7124 462 54 -449 C ATOM 4677 O ILE B 310 -4.078 4.516 14.883 1.00 56.46 O ANISOU 4677 O ILE B 310 6009 7062 8382 460 54 -453 O ATOM 4678 CB ILE B 310 -5.353 1.819 15.733 1.00 37.56 C ANISOU 4678 CB ILE B 310 3594 4666 6013 456 61 -438 C ATOM 4679 CG1 ILE B 310 -5.867 1.190 14.447 1.00 38.44 C ANISOU 4679 CG1 ILE B 310 3702 4767 6138 449 52 -444 C ATOM 4680 CG2 ILE B 310 -5.760 0.969 16.925 1.00 36.19 C ANISOU 4680 CG2 ILE B 310 3411 4497 5844 458 70 -428 C ATOM 4681 CD1 ILE B 310 -5.204 -0.151 14.145 1.00 39.67 C ANISOU 4681 CD1 ILE B 310 3857 4916 6300 440 49 -445 C ATOM 4682 N HIS B 311 -6.046 4.540 13.797 1.00 39.11 N ANISOU 4682 N HIS B 311 3800 4859 6201 461 47 -454 N ATOM 4683 CA HIS B 311 -5.574 5.394 12.715 1.00 34.09 C ANISOU 4683 CA HIS B 311 3173 4218 5560 459 39 -464 C ATOM 4684 C HIS B 311 -6.217 6.785 12.718 1.00 33.34 C ANISOU 4684 C HIS B 311 3080 4128 5458 467 40 -465 C ATOM 4685 O HIS B 311 -6.208 7.464 11.685 1.00 35.07 O ANISOU 4685 O HIS B 311 3305 4344 5677 466 32 -473 O ATOM 4686 CB HIS B 311 -5.813 4.698 11.375 1.00 25.53 C ANISOU 4686 CB HIS B 311 2089 3125 4488 451 29 -471 C ATOM 4687 CG HIS B 311 -5.069 3.405 11.215 1.00 34.76 C ANISOU 4687 CG HIS B 311 3258 4288 5663 443 27 -471 C ATOM 4688 ND1 HIS B 311 -3.691 3.326 11.225 1.00 34.79 N ANISOU 4688 ND1 HIS B 311 3270 4290 5658 438 26 -475 N ATOM 4689 CD2 HIS B 311 -5.517 2.138 11.037 1.00 31.98 C ANISOU 4689 CD2 HIS B 311 2898 3931 5324 438 26 -469 C ATOM 4690 CE1 HIS B 311 -3.326 2.067 11.056 1.00 37.57 C ANISOU 4690 CE1 HIS B 311 3621 4638 6018 431 25 -474 C ATOM 4691 NE2 HIS B 311 -4.415 1.326 10.938 1.00 33.38 N ANISOU 4691 NE2 HIS B 311 3080 4104 5501 431 25 -471 N ATOM 4692 N GLN B 312 -6.725 7.250 13.856 1.00 31.19 N ANISOU 4692 N GLN B 312 2804 3865 5182 476 48 -457 N ATOM 4693 CA GLN B 312 -7.374 8.557 13.883 1.00 43.90 C ANISOU 4693 CA GLN B 312 4415 5480 6786 484 50 -458 C ATOM 4694 C GLN B 312 -6.347 9.686 13.797 1.00 45.85 C ANISOU 4694 C GLN B 312 4674 5728 7018 485 49 -463 C ATOM 4695 O GLN B 312 -5.184 9.531 14.170 1.00 43.06 O ANISOU 4695 O GLN B 312 4327 5376 6657 482 50 -464 O ATOM 4696 CB GLN B 312 -8.241 8.717 15.143 1.00 46.40 C ANISOU 4696 CB GLN B 312 4724 5805 7102 493 60 -447 C ATOM 4697 CG GLN B 312 -7.604 9.400 16.352 1.00 34.54 C ANISOU 4697 CG GLN B 312 3227 4312 5586 499 68 -443 C ATOM 4698 CD GLN B 312 -8.576 9.489 17.540 1.00 41.02 C ANISOU 4698 CD GLN B 312 4039 5141 6407 508 78 -433 C ATOM 4699 OE1 GLN B 312 -9.240 8.514 17.890 1.00 53.48 O ANISOU 4699 OE1 GLN B 312 5607 6718 7995 507 80 -427 O ATOM 4700 NE2 GLN B 312 -8.669 10.663 18.150 1.00 31.55 N ANISOU 4700 NE2 GLN B 312 2842 3948 5197 516 83 -431 N ATOM 4701 N ARG B 313 -6.790 10.827 13.271 1.00 48.90 N ANISOU 4701 N ARG B 313 5064 6116 7401 490 46 -467 N ATOM 4702 CA ARG B 313 -5.951 12.001 13.074 1.00 43.66 C ANISOU 4702 CA ARG B 313 4411 5453 6724 491 44 -473 C ATOM 4703 C ARG B 313 -6.137 13.034 14.188 1.00 47.01 C ANISOU 4703 C ARG B 313 4837 5888 7138 501 53 -467 C ATOM 4704 O ARG B 313 -7.090 12.983 14.968 1.00 53.78 O ANISOU 4704 O ARG B 313 5686 6750 7999 507 60 -460 O ATOM 4705 CB ARG B 313 -6.247 12.633 11.713 1.00 40.65 C ANISOU 4705 CB ARG B 313 4035 5067 6346 489 34 -482 C ATOM 4706 CG ARG B 313 -6.174 11.644 10.573 1.00 45.31 C ANISOU 4706 CG ARG B 313 4623 5647 6947 480 25 -488 C ATOM 4707 CD ARG B 313 -6.508 12.317 9.238 1.00 53.80 C ANISOU 4707 CD ARG B 313 5701 6716 8023 479 16 -497 C ATOM 4708 NE ARG B 313 -6.596 11.356 8.135 1.00 54.93 N ANISOU 4708 NE ARG B 313 5843 6850 8179 470 7 -502 N ATOM 4709 CZ ARG B 313 -5.599 11.068 7.301 1.00 57.37 C ANISOU 4709 CZ ARG B 313 6159 7152 8487 462 0 -510 C ATOM 4710 NH1 ARG B 313 -4.427 11.679 7.428 1.00 56.19 N ANISOU 4710 NH1 ARG B 313 6020 7005 8325 461 0 -514 N ATOM 4711 NH2 ARG B 313 -5.775 10.173 6.332 1.00 49.75 N ANISOU 4711 NH2 ARG B 313 5190 6179 7533 455 -7 -514 N ATOM 4712 N ALA B 314 -5.180 13.969 14.269 1.00 43.74 N ANISOU 4712 N ALA B 314 4433 5475 6710 502 54 -472 N ATOM 4713 CA ALA B 314 -5.219 15.054 15.243 1.00 42.91 C ANISOU 4713 CA ALA B 314 4330 5379 6594 511 62 -467 C ATOM 4714 C ALA B 314 -4.359 16.205 14.745 1.00 37.78 C ANISOU 4714 C ALA B 314 3694 4729 5933 511 58 -475 C ATOM 4715 O ALA B 314 -3.285 15.953 14.183 1.00 43.17 O ANISOU 4715 O ALA B 314 4384 5407 6613 504 53 -482 O ATOM 4716 CB ALA B 314 -4.743 14.584 16.622 1.00 41.72 C ANISOU 4716 CB ALA B 314 4178 5236 6439 513 71 -459 C ATOM 4717 N PRO B 315 -4.775 17.454 14.930 1.00 40.77 N ANISOU 4717 N PRO B 315 4075 5112 6304 519 61 -475 N ATOM 4718 CA PRO B 315 -3.896 18.593 14.619 1.00 47.61 C ANISOU 4718 CA PRO B 315 4953 5979 7158 520 59 -482 C ATOM 4719 C PRO B 315 -2.851 18.833 15.704 1.00 47.24 C ANISOU 4719 C PRO B 315 4911 5938 7098 521 66 -479 C ATOM 4720 O PRO B 315 -3.046 18.501 16.873 1.00 47.88 O ANISOU 4720 O PRO B 315 4988 6026 7179 526 75 -471 O ATOM 4721 CB PRO B 315 -4.873 19.769 14.516 1.00 50.76 C ANISOU 4721 CB PRO B 315 5351 6381 7555 528 60 -482 C ATOM 4722 CG PRO B 315 -6.027 19.382 15.377 1.00 49.85 C ANISOU 4722 CG PRO B 315 5225 6271 7446 535 67 -472 C ATOM 4723 CD PRO B 315 -6.110 17.872 15.388 1.00 41.58 C ANISOU 4723 CD PRO B 315 4169 5220 6410 528 66 -469 C ATOM 4724 N VAL B 316 -1.724 19.433 15.312 1.00 44.76 N ANISOU 4724 N VAL B 316 4609 5623 6775 518 63 -487 N ATOM 4725 CA VAL B 316 -0.595 19.593 16.228 1.00 39.13 C ANISOU 4725 CA VAL B 316 3902 4915 6051 518 69 -485 C ATOM 4726 C VAL B 316 0.085 20.944 15.992 1.00 37.08 C ANISOU 4726 C VAL B 316 3654 4657 5779 521 68 -491 C ATOM 4727 O VAL B 316 0.261 21.375 14.845 1.00 36.41 O ANISOU 4727 O VAL B 316 3574 4565 5693 517 60 -500 O ATOM 4728 CB VAL B 316 0.395 18.396 16.108 1.00 36.91 C ANISOU 4728 CB VAL B 316 3622 4630 5772 509 66 -486 C ATOM 4729 CG1 VAL B 316 0.929 18.217 14.695 1.00 36.64 C ANISOU 4729 CG1 VAL B 316 3594 4587 5742 500 55 -497 C ATOM 4730 CG2 VAL B 316 1.543 18.504 17.098 1.00 29.70 C ANISOU 4730 CG2 VAL B 316 2714 3722 4847 509 73 -484 C ATOM 4731 N ILE B 317 0.410 21.632 17.100 1.00 33.28 N ANISOU 4731 N ILE B 317 3175 4183 5285 527 77 -487 N ATOM 4732 CA ILE B 317 1.223 22.853 17.135 1.00 30.12 C ANISOU 4732 CA ILE B 317 2786 3785 4872 529 78 -492 C ATOM 4733 C ILE B 317 2.207 22.690 18.287 1.00 33.77 C ANISOU 4733 C ILE B 317 3252 4254 5326 530 85 -488 C ATOM 4734 O ILE B 317 1.790 22.652 19.450 1.00 38.46 O ANISOU 4734 O ILE B 317 3841 4855 5917 536 95 -479 O ATOM 4735 CB ILE B 317 0.364 24.124 17.350 1.00 34.94 C ANISOU 4735 CB ILE B 317 3398 4400 5478 539 82 -490 C ATOM 4736 CG1 ILE B 317 -0.639 24.313 16.207 1.00 37.95 C ANISOU 4736 CG1 ILE B 317 3776 4775 5869 539 74 -494 C ATOM 4737 CG2 ILE B 317 1.233 25.397 17.493 1.00 23.00 C ANISOU 4737 CG2 ILE B 317 1897 2890 3951 542 84 -495 C ATOM 4738 CD1 ILE B 317 -1.987 23.700 16.489 1.00 33.25 C ANISOU 4738 CD1 ILE B 317 3168 4181 5285 543 77 -487 C ATOM 4739 N LEU B 318 3.509 22.649 17.988 1.00 30.39 N ANISOU 4739 N LEU B 318 2833 3824 4891 523 82 -494 N ATOM 4740 CA LEU B 318 4.493 22.278 19.001 1.00 25.70 C ANISOU 4740 CA LEU B 318 2241 3235 4290 522 88 -490 C ATOM 4741 C LEU B 318 5.756 23.105 18.842 1.00 25.02 C ANISOU 4741 C LEU B 318 2167 3149 4190 520 87 -498 C ATOM 4742 O LEU B 318 5.987 23.737 17.815 1.00 33.48 O ANISOU 4742 O LEU B 318 3245 4215 5260 517 80 -506 O ATOM 4743 CB LEU B 318 4.823 20.768 18.946 1.00 23.08 C ANISOU 4743 CB LEU B 318 1904 2900 3966 514 86 -488 C ATOM 4744 CG LEU B 318 5.273 20.158 17.612 1.00 25.53 C ANISOU 4744 CG LEU B 318 2217 3201 4283 504 75 -497 C ATOM 4745 CD1 LEU B 318 6.686 20.501 17.304 1.00 27.30 C ANISOU 4745 CD1 LEU B 318 2452 3424 4497 499 72 -504 C ATOM 4746 CD2 LEU B 318 5.127 18.629 17.621 1.00 34.68 C ANISOU 4746 CD2 LEU B 318 3368 4357 5454 499 74 -493 C ATOM 4747 N GLY B 319 6.591 23.074 19.870 1.00 23.30 N ANISOU 4747 N GLY B 319 1952 2938 3964 521 94 -494 N ATOM 4748 CA GLY B 319 7.835 23.816 19.836 1.00 33.76 C ANISOU 4748 CA GLY B 319 3288 4263 5276 519 94 -500 C ATOM 4749 C GLY B 319 8.161 24.582 21.109 1.00 37.39 C ANISOU 4749 C GLY B 319 3751 4732 5723 526 104 -495 C ATOM 4750 O GLY B 319 7.753 24.189 22.214 1.00 31.01 O ANISOU 4750 O GLY B 319 2937 3931 4916 531 112 -486 O ATOM 4751 N SER B 320 8.894 25.686 20.942 1.00 25.09 N ANISOU 4751 N SER B 320 2203 3175 4154 526 103 -502 N ATOM 4752 CA SER B 320 9.290 26.523 22.067 1.00 24.25 C ANISOU 4752 CA SER B 320 2102 3077 4036 533 113 -498 C ATOM 4753 C SER B 320 8.074 27.027 22.845 1.00 36.69 C ANISOU 4753 C SER B 320 3670 4657 5612 544 120 -490 C ATOM 4754 O SER B 320 7.022 27.304 22.252 1.00 40.51 O ANISOU 4754 O SER B 320 4150 5138 6102 546 117 -490 O ATOM 4755 CB SER B 320 10.113 27.706 21.570 1.00 25.31 C ANISOU 4755 CB SER B 320 2248 3210 4159 532 110 -507 C ATOM 4756 OG SER B 320 11.330 27.260 20.998 1.00 33.33 O ANISOU 4756 OG SER B 320 3270 4222 5173 523 103 -514 O ATOM 4757 N PRO B 321 8.165 27.119 24.186 1.00 31.79 N ANISOU 4757 N PRO B 321 3049 4046 4985 549 131 -482 N ATOM 4758 CA PRO B 321 6.986 27.508 24.979 1.00 29.38 C ANISOU 4758 CA PRO B 321 2737 3746 4682 559 138 -474 C ATOM 4759 C PRO B 321 6.522 28.940 24.747 1.00 21.76 C ANISOU 4759 C PRO B 321 1777 2781 3710 566 139 -477 C ATOM 4760 O PRO B 321 5.318 29.153 24.570 1.00 20.56 O ANISOU 4760 O PRO B 321 1618 2628 3564 571 139 -474 O ATOM 4761 CB PRO B 321 7.442 27.283 26.432 1.00 32.15 C ANISOU 4761 CB PRO B 321 3086 4105 5025 563 148 -466 C ATOM 4762 CG PRO B 321 8.919 27.312 26.385 1.00 32.73 C ANISOU 4762 CG PRO B 321 3168 4178 5089 557 147 -472 C ATOM 4763 CD PRO B 321 9.306 26.741 25.034 1.00 33.82 C ANISOU 4763 CD PRO B 321 3308 4307 5234 547 135 -480 C ATOM 4764 N ASP B 322 7.428 29.931 24.721 1.00 29.68 N ANISOU 4764 N ASP B 322 2790 3785 4701 566 139 -483 N ATOM 4765 CA ASP B 322 6.974 31.305 24.459 1.00 34.23 C ANISOU 4765 CA ASP B 322 3372 4361 5273 572 140 -486 C ATOM 4766 C ASP B 322 6.229 31.409 23.128 1.00 40.65 C ANISOU 4766 C ASP B 322 4184 5167 6095 570 131 -492 C ATOM 4767 O ASP B 322 5.266 32.179 23.004 1.00 35.23 O ANISOU 4767 O ASP B 322 3496 4481 5410 577 132 -491 O ATOM 4768 CB ASP B 322 8.138 32.303 24.452 1.00 36.38 C ANISOU 4768 CB ASP B 322 3656 4634 5531 571 141 -493 C ATOM 4769 CG ASP B 322 8.637 32.661 25.854 1.00 52.06 C ANISOU 4769 CG ASP B 322 5645 6628 7506 577 152 -487 C ATOM 4770 OD1 ASP B 322 8.133 32.101 26.856 1.00 55.16 O ANISOU 4770 OD1 ASP B 322 6030 7028 7902 581 159 -478 O ATOM 4771 OD2 ASP B 322 9.514 33.552 25.950 1.00 54.78 O ANISOU 4771 OD2 ASP B 322 6000 6975 7840 577 153 -492 O ATOM 4772 N ASP B 323 6.654 30.634 22.124 1.00 39.60 N ANISOU 4772 N ASP B 323 4051 5027 5968 561 122 -498 N ATOM 4773 CA ASP B 323 6.005 30.713 20.824 1.00 31.57 C ANISOU 4773 CA ASP B 323 3033 4002 4959 558 112 -503 C ATOM 4774 C ASP B 323 4.628 30.058 20.847 1.00 32.69 C ANISOU 4774 C ASP B 323 3163 4143 5113 562 113 -497 C ATOM 4775 O ASP B 323 3.667 30.621 20.309 1.00 35.34 O ANISOU 4775 O ASP B 323 3496 4477 5453 566 110 -498 O ATOM 4776 CB ASP B 323 6.898 30.079 19.765 1.00 26.16 C ANISOU 4776 CB ASP B 323 2352 3310 4277 547 102 -512 C ATOM 4777 CG ASP B 323 8.193 30.841 19.577 1.00 30.97 C ANISOU 4777 CG ASP B 323 2974 3919 4874 544 101 -520 C ATOM 4778 OD1 ASP B 323 8.137 32.092 19.461 1.00 24.91 O ANISOU 4778 OD1 ASP B 323 2213 3152 4099 549 102 -523 O ATOM 4779 OD2 ASP B 323 9.261 30.183 19.532 1.00 38.80 O ANISOU 4779 OD2 ASP B 323 3969 4910 5865 536 98 -523 O ATOM 4780 N VAL B 324 4.507 28.877 21.467 1.00 30.75 N ANISOU 4780 N VAL B 324 2909 3900 4874 560 116 -490 N ATOM 4781 CA VAL B 324 3.202 28.218 21.546 1.00 39.46 C ANISOU 4781 CA VAL B 324 4001 5003 5990 563 117 -483 C ATOM 4782 C VAL B 324 2.230 29.040 22.386 1.00 41.66 C ANISOU 4782 C VAL B 324 4275 5288 6264 575 125 -476 C ATOM 4783 O VAL B 324 1.040 29.128 22.067 1.00 39.90 O ANISOU 4783 O VAL B 324 4047 5064 6050 579 124 -474 O ATOM 4784 CB VAL B 324 3.347 26.782 22.085 1.00 37.90 C ANISOU 4784 CB VAL B 324 3795 4807 5799 559 118 -477 C ATOM 4785 CG1 VAL B 324 1.973 26.108 22.185 1.00 19.60 C ANISOU 4785 CG1 VAL B 324 1465 2489 3493 562 119 -470 C ATOM 4786 CG2 VAL B 324 4.285 25.968 21.188 1.00 41.27 C ANISOU 4786 CG2 VAL B 324 4226 5227 6229 548 110 -484 C ATOM 4787 N LEU B 325 2.715 29.647 23.475 1.00 44.28 N ANISOU 4787 N LEU B 325 4611 5626 6585 580 134 -472 N ATOM 4788 CA LEU B 325 1.856 30.510 24.288 1.00 40.14 C ANISOU 4788 CA LEU B 325 4085 5109 6057 591 142 -466 C ATOM 4789 C LEU B 325 1.376 31.718 23.491 1.00 46.44 C ANISOU 4789 C LEU B 325 4889 5904 6853 595 139 -472 C ATOM 4790 O LEU B 325 0.203 32.101 23.577 1.00 46.81 O ANISOU 4790 O LEU B 325 4930 5952 6903 602 141 -468 O ATOM 4791 CB LEU B 325 2.612 30.968 25.532 1.00 39.01 C ANISOU 4791 CB LEU B 325 3947 4974 5902 595 152 -462 C ATOM 4792 CG LEU B 325 2.908 29.947 26.628 1.00 37.76 C ANISOU 4792 CG LEU B 325 3783 4821 5744 594 158 -455 C ATOM 4793 CD1 LEU B 325 3.818 30.569 27.681 1.00 38.60 C ANISOU 4793 CD1 LEU B 325 3896 4934 5836 598 166 -453 C ATOM 4794 CD2 LEU B 325 1.632 29.408 27.242 1.00 37.36 C ANISOU 4794 CD2 LEU B 325 3720 4774 5702 600 163 -445 C ATOM 4795 N GLU B 326 2.277 32.340 22.716 1.00 51.04 N ANISOU 4795 N GLU B 326 5481 6482 7429 590 133 -481 N ATOM 4796 CA GLU B 326 1.879 33.462 21.871 1.00 49.31 C ANISOU 4796 CA GLU B 326 5268 6260 7208 593 129 -487 C ATOM 4797 C GLU B 326 0.847 33.026 20.838 1.00 46.64 C ANISOU 4797 C GLU B 326 4923 5916 6883 591 121 -489 C ATOM 4798 O GLU B 326 -0.101 33.764 20.548 1.00 43.10 O ANISOU 4798 O GLU B 326 4473 5466 6436 598 121 -488 O ATOM 4799 CB GLU B 326 3.103 34.073 21.181 1.00 45.39 C ANISOU 4799 CB GLU B 326 4783 5759 6703 587 124 -498 C ATOM 4800 CG GLU B 326 2.781 35.301 20.302 1.00 47.82 C ANISOU 4800 CG GLU B 326 5099 6064 7008 590 120 -504 C ATOM 4801 CD GLU B 326 4.003 35.898 19.576 1.00 56.24 C ANISOU 4801 CD GLU B 326 6176 7125 8065 584 114 -515 C ATOM 4802 OE1 GLU B 326 5.159 35.656 20.007 1.00 58.47 O ANISOU 4802 OE1 GLU B 326 6465 7411 8342 580 116 -516 O ATOM 4803 OE2 GLU B 326 3.805 36.592 18.548 1.00 55.07 O ANISOU 4803 OE2 GLU B 326 6033 6973 7918 584 108 -522 O ATOM 4804 N PHE B 327 0.992 31.813 20.297 1.00 44.16 N ANISOU 4804 N PHE B 327 4604 5597 6578 583 115 -490 N ATOM 4805 CA PHE B 327 -0.018 31.324 19.370 1.00 39.10 C ANISOU 4805 CA PHE B 327 3956 4951 5950 581 108 -491 C ATOM 4806 C PHE B 327 -1.357 31.129 20.065 1.00 41.05 C ANISOU 4806 C PHE B 327 4192 5202 6204 589 114 -481 C ATOM 4807 O PHE B 327 -2.396 31.549 19.542 1.00 46.21 O ANISOU 4807 O PHE B 327 4842 5854 6862 594 112 -481 O ATOM 4808 CB PHE B 327 0.425 30.007 18.727 1.00 38.50 C ANISOU 4808 CB PHE B 327 3876 4868 5882 571 100 -494 C ATOM 4809 CG PHE B 327 -0.685 29.311 17.993 1.00 39.19 C ANISOU 4809 CG PHE B 327 3955 4951 5984 569 95 -493 C ATOM 4810 CD1 PHE B 327 -1.000 29.667 16.698 1.00 43.21 C ANISOU 4810 CD1 PHE B 327 4466 5453 6497 567 86 -500 C ATOM 4811 CD2 PHE B 327 -1.432 28.321 18.606 1.00 36.88 C ANISOU 4811 CD2 PHE B 327 3651 4661 5701 571 99 -485 C ATOM 4812 CE1 PHE B 327 -2.038 29.052 16.027 1.00 39.59 C ANISOU 4812 CE1 PHE B 327 4000 4992 6052 566 81 -500 C ATOM 4813 CE2 PHE B 327 -2.475 27.711 17.936 1.00 39.85 C ANISOU 4813 CE2 PHE B 327 4019 5033 6090 570 93 -484 C ATOM 4814 CZ PHE B 327 -2.770 28.076 16.644 1.00 36.26 C ANISOU 4814 CZ PHE B 327 3566 4572 5639 567 85 -491 C ATOM 4815 N LEU B 328 -1.350 30.520 21.255 1.00 43.98 N ANISOU 4815 N LEU B 328 4557 5579 6574 592 122 -473 N ATOM 4816 CA LEU B 328 -2.607 30.246 21.952 1.00 52.75 C ANISOU 4816 CA LEU B 328 5658 6694 7691 599 128 -464 C ATOM 4817 C LEU B 328 -3.318 31.539 22.333 1.00 49.81 C ANISOU 4817 C LEU B 328 5287 6327 7313 610 134 -461 C ATOM 4818 O LEU B 328 -4.551 31.612 22.287 1.00 48.84 O ANISOU 4818 O LEU B 328 5156 6204 7196 615 134 -457 O ATOM 4819 CB LEU B 328 -2.358 29.358 23.176 1.00 49.76 C ANISOU 4819 CB LEU B 328 5273 6322 7313 599 135 -455 C ATOM 4820 CG LEU B 328 -2.126 27.870 22.870 1.00 48.20 C ANISOU 4820 CG LEU B 328 5069 6119 7125 590 131 -455 C ATOM 4821 CD1 LEU B 328 -1.563 27.144 24.082 1.00 46.02 C ANISOU 4821 CD1 LEU B 328 4791 5849 6845 590 138 -448 C ATOM 4822 CD2 LEU B 328 -3.434 27.195 22.408 1.00 42.23 C ANISOU 4822 CD2 LEU B 328 4302 5361 6383 590 127 -452 C ATOM 4823 N LYS B 329 -2.555 32.581 22.672 1.00 52.03 N ANISOU 4823 N LYS B 329 5577 6610 7580 613 137 -464 N ATOM 4824 CA LYS B 329 -3.161 33.879 22.955 1.00 55.82 C ANISOU 4824 CA LYS B 329 6061 7094 8054 623 143 -462 C ATOM 4825 C LYS B 329 -3.944 34.393 21.750 1.00 47.81 C ANISOU 4825 C LYS B 329 5046 6073 7045 624 135 -468 C ATOM 4826 O LYS B 329 -5.089 34.840 21.887 1.00 50.51 O ANISOU 4826 O LYS B 329 5384 6418 7391 632 138 -463 O ATOM 4827 CB LYS B 329 -2.082 34.875 23.389 1.00 65.78 C ANISOU 4827 CB LYS B 329 7334 8358 9301 624 147 -466 C ATOM 4828 CG LYS B 329 -2.615 36.272 23.700 1.00 78.55 C ANISOU 4828 CG LYS B 329 8955 9978 10911 635 153 -465 C ATOM 4829 CD LYS B 329 -1.566 37.173 24.373 1.00 86.11 C ANISOU 4829 CD LYS B 329 9924 10940 11854 637 159 -466 C ATOM 4830 CE LYS B 329 -2.162 38.537 24.763 1.00 88.47 C ANISOU 4830 CE LYS B 329 10226 11242 12145 647 165 -464 C ATOM 4831 NZ LYS B 329 -1.183 39.437 25.440 1.00 87.52 N ANISOU 4831 NZ LYS B 329 10117 11126 12011 650 171 -466 N ATOM 4832 N VAL B 330 -3.358 34.315 20.555 1.00 42.80 N ANISOU 4832 N VAL B 330 4418 5432 6413 615 125 -477 N ATOM 4833 CA VAL B 330 -4.115 34.689 19.368 1.00 38.48 C ANISOU 4833 CA VAL B 330 3870 4879 5871 616 118 -482 C ATOM 4834 C VAL B 330 -5.277 33.725 19.167 1.00 43.32 C ANISOU 4834 C VAL B 330 4470 5490 6498 616 116 -477 C ATOM 4835 O VAL B 330 -6.374 34.121 18.745 1.00 39.61 O ANISOU 4835 O VAL B 330 3997 5021 6034 621 114 -476 O ATOM 4836 CB VAL B 330 -3.207 34.748 18.131 1.00 43.06 C ANISOU 4836 CB VAL B 330 4459 5452 6451 607 108 -493 C ATOM 4837 CG1 VAL B 330 -4.027 35.104 16.910 1.00 43.34 C ANISOU 4837 CG1 VAL B 330 4492 5481 6492 607 100 -498 C ATOM 4838 CG2 VAL B 330 -2.094 35.760 18.332 1.00 46.08 C ANISOU 4838 CG2 VAL B 330 4853 5835 6819 607 110 -498 C ATOM 4839 N TYR B 331 -5.053 32.443 19.453 1.00 37.42 N ANISOU 4839 N TYR B 331 3717 4744 5758 610 115 -474 N ATOM 4840 CA TYR B 331 -6.119 31.460 19.278 1.00 45.53 C ANISOU 4840 CA TYR B 331 4732 5769 6799 609 113 -469 C ATOM 4841 C TYR B 331 -7.281 31.760 20.204 1.00 53.48 C ANISOU 4841 C TYR B 331 5731 6782 7806 620 121 -460 C ATOM 4842 O TYR B 331 -8.445 31.656 19.804 1.00 58.36 O ANISOU 4842 O TYR B 331 6341 7399 8433 623 119 -458 O ATOM 4843 CB TYR B 331 -5.596 30.042 19.523 1.00 39.07 C ANISOU 4843 CB TYR B 331 3909 4949 5986 601 112 -467 C ATOM 4844 CG TYR B 331 -6.600 28.955 19.226 1.00 39.42 C ANISOU 4844 CG TYR B 331 3941 4991 6045 599 109 -463 C ATOM 4845 CD1 TYR B 331 -6.788 28.495 17.930 1.00 42.58 C ANISOU 4845 CD1 TYR B 331 4340 5384 6455 592 98 -470 C ATOM 4846 CD2 TYR B 331 -7.349 28.377 20.236 1.00 54.18 C ANISOU 4846 CD2 TYR B 331 5801 6866 7919 603 116 -454 C ATOM 4847 CE1 TYR B 331 -7.701 27.494 17.650 1.00 50.51 C ANISOU 4847 CE1 TYR B 331 5334 6386 7473 590 96 -466 C ATOM 4848 CE2 TYR B 331 -8.273 27.368 19.963 1.00 53.68 C ANISOU 4848 CE2 TYR B 331 5727 6801 7869 601 113 -450 C ATOM 4849 CZ TYR B 331 -8.442 26.933 18.672 1.00 52.50 C ANISOU 4849 CZ TYR B 331 5575 6642 7728 595 103 -457 C ATOM 4850 OH TYR B 331 -9.354 25.932 18.403 1.00 56.04 O ANISOU 4850 OH TYR B 331 6013 7089 8190 592 100 -454 O ATOM 4851 N GLU B 332 -6.977 32.124 21.453 1.00 52.54 N ANISOU 4851 N GLU B 332 5613 6671 7678 625 131 -454 N ATOM 4852 CA GLU B 332 -8.018 32.424 22.426 1.00 54.85 C ANISOU 4852 CA GLU B 332 5900 6971 7971 636 140 -445 C ATOM 4853 C GLU B 332 -8.739 33.728 22.093 1.00 55.39 C ANISOU 4853 C GLU B 332 5971 7040 8035 644 141 -446 C ATOM 4854 O GLU B 332 -9.943 33.850 22.343 1.00 54.19 O ANISOU 4854 O GLU B 332 5811 6890 7887 651 144 -441 O ATOM 4855 CB GLU B 332 -7.392 32.472 23.820 1.00 64.47 C ANISOU 4855 CB GLU B 332 7120 8197 9180 639 150 -439 C ATOM 4856 CG GLU B 332 -6.838 31.114 24.276 1.00 77.99 C ANISOU 4856 CG GLU B 332 8827 9909 10896 632 150 -436 C ATOM 4857 CD GLU B 332 -5.798 31.219 25.395 1.00 89.74 C ANISOU 4857 CD GLU B 332 10321 11404 12374 633 158 -433 C ATOM 4858 OE1 GLU B 332 -5.533 32.346 25.874 1.00 93.26 O ANISOU 4858 OE1 GLU B 332 10774 11853 12808 639 163 -434 O ATOM 4859 OE2 GLU B 332 -5.234 30.168 25.786 1.00 90.84 O ANISOU 4859 OE2 GLU B 332 10456 11542 12515 627 158 -431 O ATOM 4860 N LYS B 333 -8.035 34.704 21.512 1.00 59.56 N ANISOU 4860 N LYS B 333 6510 7564 8554 643 138 -454 N ATOM 4861 CA LYS B 333 -8.698 35.946 21.126 1.00 56.30 C ANISOU 4861 CA LYS B 333 6101 7152 8139 651 138 -456 C ATOM 4862 C LYS B 333 -9.820 35.692 20.130 1.00 58.53 C ANISOU 4862 C LYS B 333 6376 7429 8432 651 131 -457 C ATOM 4863 O LYS B 333 -10.862 36.357 20.187 1.00 66.22 O ANISOU 4863 O LYS B 333 7348 8406 9408 659 134 -454 O ATOM 4864 CB LYS B 333 -7.703 36.936 20.525 1.00 54.76 C ANISOU 4864 CB LYS B 333 5919 6953 7933 649 135 -465 C ATOM 4865 CG LYS B 333 -8.401 38.178 20.013 1.00 63.40 C ANISOU 4865 CG LYS B 333 7017 8046 9024 656 134 -467 C ATOM 4866 CD LYS B 333 -7.475 39.224 19.452 1.00 66.57 C ANISOU 4866 CD LYS B 333 7432 8445 9416 655 131 -476 C ATOM 4867 CE LYS B 333 -7.096 38.902 18.024 1.00 65.55 C ANISOU 4867 CE LYS B 333 7306 8308 9292 645 119 -485 C ATOM 4868 NZ LYS B 333 -6.381 40.052 17.422 1.00 64.17 N ANISOU 4868 NZ LYS B 333 7144 8130 9108 645 117 -494 N ATOM 4869 N HIS B 334 -9.651 34.713 19.238 1.00 52.11 N ANISOU 4869 N HIS B 334 5560 6610 7628 641 122 -462 N ATOM 4870 CA HIS B 334 -10.683 34.376 18.269 1.00 54.79 C ANISOU 4870 CA HIS B 334 5893 6946 7980 640 115 -463 C ATOM 4871 C HIS B 334 -11.671 33.361 18.831 1.00 64.47 C ANISOU 4871 C HIS B 334 7105 8174 9216 642 118 -454 C ATOM 4872 O HIS B 334 -12.385 32.709 18.060 1.00 67.00 O ANISOU 4872 O HIS B 334 7418 8490 9548 639 111 -455 O ATOM 4873 CB HIS B 334 -10.047 33.844 16.980 1.00 46.82 C ANISOU 4873 CB HIS B 334 4887 5928 6976 629 104 -472 C ATOM 4874 CG HIS B 334 -9.217 34.859 16.261 1.00 48.83 C ANISOU 4874 CG HIS B 334 5154 6178 7221 628 99 -481 C ATOM 4875 ND1 HIS B 334 -9.573 35.385 15.036 1.00 49.66 N ANISOU 4875 ND1 HIS B 334 5262 6278 7328 627 91 -488 N ATOM 4876 CD2 HIS B 334 -8.056 35.465 16.607 1.00 47.34 C ANISOU 4876 CD2 HIS B 334 4976 5991 7020 627 102 -485 C ATOM 4877 CE1 HIS B 334 -8.664 36.266 14.657 1.00 45.45 C ANISOU 4877 CE1 HIS B 334 4741 5743 6786 626 90 -495 C ATOM 4878 NE2 HIS B 334 -7.732 36.332 15.592 1.00 47.42 N ANISOU 4878 NE2 HIS B 334 4995 5996 7026 626 96 -493 N ATOM 4879 N SER B 335 -11.752 33.263 20.160 1.00 72.11 N ANISOU 4879 N SER B 335 8069 9149 10179 647 128 -446 N ATOM 4880 CA SER B 335 -12.683 32.401 20.882 1.00 80.24 C ANISOU 4880 CA SER B 335 9087 10183 11219 650 132 -437 C ATOM 4881 C SER B 335 -12.644 30.953 20.402 1.00 88.73 C ANISOU 4881 C SER B 335 10155 11253 12305 640 126 -438 C ATOM 4882 O SER B 335 -11.739 30.522 19.684 1.00 90.74 O ANISOU 4882 O SER B 335 10415 11502 12561 631 119 -445 O ATOM 4883 CB SER B 335 -14.109 32.963 20.786 1.00 78.15 C ANISOU 4883 CB SER B 335 8815 9920 10957 659 134 -433 C ATOM 4884 OG SER B 335 -14.277 34.084 21.652 1.00 75.02 O ANISOU 4884 OG SER B 335 8424 9531 10551 670 142 -429 O TER 4885 SER B 335 ATOM 4886 N ASP C 9 51.770 12.680 -2.660 1.00 34.26 N ANISOU 4886 N ASP C 9 4210 4575 4234 470 325 479 N ATOM 4887 CA ASP C 9 50.360 12.829 -3.048 1.00 37.75 C ANISOU 4887 CA ASP C 9 4649 5029 4664 479 324 481 C ATOM 4888 C ASP C 9 49.623 11.482 -3.061 1.00 49.52 C ANISOU 4888 C ASP C 9 6142 6518 6157 484 330 487 C ATOM 4889 O ASP C 9 50.152 10.469 -3.520 1.00 52.62 O ANISOU 4889 O ASP C 9 6544 6901 6550 493 343 492 O ATOM 4890 CB ASP C 9 50.247 13.492 -4.415 1.00 46.89 C ANISOU 4890 CB ASP C 9 5818 6194 5803 499 335 484 C ATOM 4891 CG ASP C 9 50.106 15.011 -4.333 1.00 53.74 C ANISOU 4891 CG ASP C 9 6681 7072 6665 495 325 478 C ATOM 4892 OD1 ASP C 9 50.073 15.577 -3.215 1.00 51.72 O ANISOU 4892 OD1 ASP C 9 6412 6818 6422 475 311 471 O ATOM 4893 OD2 ASP C 9 50.067 15.641 -5.412 1.00 46.05 O ANISOU 4893 OD2 ASP C 9 5722 6102 5672 505 330 478 O ATOM 4894 N VAL C 10 48.382 11.486 -2.572 1.00 44.74 N ANISOU 4894 N VAL C 10 5527 5921 5552 478 322 486 N ATOM 4895 CA VAL C 10 47.590 10.268 -2.534 1.00 35.58 C ANISOU 4895 CA VAL C 10 4368 4759 4392 482 326 492 C ATOM 4896 C VAL C 10 47.289 9.738 -3.939 1.00 37.82 C ANISOU 4896 C VAL C 10 4664 5045 4659 508 344 498 C ATOM 4897 O VAL C 10 47.151 10.496 -4.905 1.00 42.65 O ANISOU 4897 O VAL C 10 5285 5666 5254 522 349 498 O ATOM 4898 CB VAL C 10 46.299 10.562 -1.758 1.00 33.07 C ANISOU 4898 CB VAL C 10 4040 4451 4075 471 312 491 C ATOM 4899 CG1 VAL C 10 45.424 11.531 -2.539 1.00 29.68 C ANISOU 4899 CG1 VAL C 10 3607 4042 3630 482 317 485 C ATOM 4900 CG2 VAL C 10 45.569 9.278 -1.411 1.00 32.15 C ANISOU 4900 CG2 VAL C 10 3924 4332 3959 468 317 499 C ATOM 4901 N ASN C 11 47.209 8.415 -4.059 1.00 36.24 N ANISOU 4901 N ASN C 11 4470 4838 4462 513 354 505 N ATOM 4902 CA ASN C 11 46.874 7.780 -5.325 1.00 24.90 C ANISOU 4902 CA ASN C 11 3051 3401 3008 532 369 507 C ATOM 4903 C ASN C 11 45.949 6.591 -5.090 1.00 32.73 C ANISOU 4903 C ASN C 11 4040 4393 4004 533 373 512 C ATOM 4904 O ASN C 11 46.024 5.912 -4.057 1.00 32.77 O ANISOU 4904 O ASN C 11 4034 4391 4027 522 369 517 O ATOM 4905 CB ASN C 11 48.106 7.307 -6.079 1.00 17.15 C ANISOU 4905 CB ASN C 11 2089 2405 2023 528 382 502 C ATOM 4906 CG ASN C 11 47.916 7.381 -7.602 1.00 36.34 C ANISOU 4906 CG ASN C 11 4550 4835 4423 531 389 496 C ATOM 4907 OD1 ASN C 11 46.797 7.560 -8.074 1.00 37.36 O ANISOU 4907 OD1 ASN C 11 4689 4971 4535 536 383 496 O ATOM 4908 ND2 ASN C 11 49.000 7.202 -8.363 1.00 26.87 N ANISOU 4908 ND2 ASN C 11 3370 3624 3217 527 398 492 N ATOM 4909 N THR C 12 45.095 6.331 -6.078 1.00 29.40 N ANISOU 4909 N THR C 12 3634 3976 3561 541 380 508 N ATOM 4910 CA THR C 12 44.146 5.230 -6.077 1.00 34.30 C ANISOU 4910 CA THR C 12 4252 4599 4182 544 387 508 C ATOM 4911 C THR C 12 44.416 4.288 -7.239 1.00 40.91 C ANISOU 4911 C THR C 12 5116 5425 5003 546 403 503 C ATOM 4912 O THR C 12 45.226 4.572 -8.125 1.00 44.56 O ANISOU 4912 O THR C 12 5602 5879 5450 545 406 500 O ATOM 4913 CB THR C 12 42.713 5.739 -6.180 1.00 34.97 C ANISOU 4913 CB THR C 12 4335 4691 4262 547 363 501 C ATOM 4914 OG1 THR C 12 42.502 6.274 -7.491 1.00 25.78 O ANISOU 4914 OG1 THR C 12 3205 3519 3073 547 346 492 O ATOM 4915 CG2 THR C 12 42.477 6.836 -5.153 1.00 37.87 C ANISOU 4915 CG2 THR C 12 4679 5072 4638 547 350 510 C ATOM 4916 N LEU C 13 43.713 3.149 -7.222 1.00 35.88 N ANISOU 4916 N LEU C 13 4474 4784 4374 546 408 494 N ATOM 4917 CA LEU C 13 43.879 2.156 -8.284 1.00 31.53 C ANISOU 4917 CA LEU C 13 3948 4220 3813 546 418 485 C ATOM 4918 C LEU C 13 43.468 2.715 -9.643 1.00 30.13 C ANISOU 4918 C LEU C 13 3804 4034 3611 546 397 473 C ATOM 4919 O LEU C 13 44.174 2.531 -10.632 1.00 26.45 O ANISOU 4919 O LEU C 13 3365 3560 3125 547 409 473 O ATOM 4920 CB LEU C 13 43.086 0.883 -7.950 1.00 27.90 C ANISOU 4920 CB LEU C 13 3474 3753 3373 543 418 472 C ATOM 4921 CG LEU C 13 43.071 -0.387 -8.826 1.00 34.86 C ANISOU 4921 CG LEU C 13 4374 4620 4251 542 429 460 C ATOM 4922 CD1 LEU C 13 44.405 -0.830 -9.427 1.00 17.75 C ANISOU 4922 CD1 LEU C 13 2226 2449 2070 544 458 470 C ATOM 4923 CD2 LEU C 13 42.663 -1.474 -7.870 1.00 46.47 C ANISOU 4923 CD2 LEU C 13 5818 6091 5749 540 438 458 C ATOM 4924 N THR C 14 42.312 3.378 -9.715 1.00 28.32 N ANISOU 4924 N THR C 14 3574 3806 3382 544 365 462 N ATOM 4925 CA THR C 14 41.824 3.886 -10.990 1.00 28.88 C ANISOU 4925 CA THR C 14 3676 3869 3430 544 342 449 C ATOM 4926 C THR C 14 42.751 4.959 -11.537 1.00 31.62 C ANISOU 4926 C THR C 14 4043 4218 3753 547 347 461 C ATOM 4927 O THR C 14 43.127 4.945 -12.714 1.00 34.43 O ANISOU 4927 O THR C 14 4429 4565 4086 548 350 457 O ATOM 4928 CB THR C 14 40.428 4.476 -10.811 1.00 34.54 C ANISOU 4928 CB THR C 14 4384 4587 4153 543 307 436 C ATOM 4929 OG1 THR C 14 39.556 3.508 -10.229 1.00 40.55 O ANISOU 4929 OG1 THR C 14 5124 5345 4936 540 303 425 O ATOM 4930 CG2 THR C 14 39.863 4.860 -12.152 1.00 23.01 C ANISOU 4930 CG2 THR C 14 2956 3117 2670 543 284 422 C ATOM 4931 N ARG C 15 43.146 5.890 -10.675 1.00 34.99 N ANISOU 4931 N ARG C 15 4452 4658 4185 548 349 476 N ATOM 4932 CA ARG C 15 44.025 6.977 -11.079 1.00 32.56 C ANISOU 4932 CA ARG C 15 4161 4355 3857 551 353 488 C ATOM 4933 C ARG C 15 45.402 6.459 -11.499 1.00 24.48 C ANISOU 4933 C ARG C 15 3147 3324 2830 548 381 490 C ATOM 4934 O ARG C 15 46.005 6.989 -12.435 1.00 35.19 O ANISOU 4934 O ARG C 15 4527 4674 4170 546 379 485 O ATOM 4935 CB ARG C 15 44.121 7.993 -9.943 1.00 42.58 C ANISOU 4935 CB ARG C 15 5402 5638 5140 549 347 496 C ATOM 4936 CG ARG C 15 45.117 9.103 -10.182 1.00 58.08 C ANISOU 4936 CG ARG C 15 7369 7599 7101 541 346 490 C ATOM 4937 CD ARG C 15 45.280 9.953 -8.948 1.00 58.74 C ANISOU 4937 CD ARG C 15 7419 7693 7205 536 341 491 C ATOM 4938 NE ARG C 15 44.389 11.091 -8.895 1.00 52.02 N ANISOU 4938 NE ARG C 15 6568 6850 6347 534 315 488 N ATOM 4939 CZ ARG C 15 44.435 11.983 -7.917 1.00 40.11 C ANISOU 4939 CZ ARG C 15 5035 5352 4854 528 309 487 C ATOM 4940 NH1 ARG C 15 45.320 11.842 -6.929 1.00 30.03 N ANISOU 4940 NH1 ARG C 15 3731 4079 3600 525 327 490 N ATOM 4941 NH2 ARG C 15 43.617 13.017 -7.939 1.00 26.10 N ANISOU 4941 NH2 ARG C 15 3262 3581 3072 525 285 482 N ATOM 4942 N PHE C 16 45.928 5.442 -10.808 1.00 19.30 N ANISOU 4942 N PHE C 16 2472 2666 2196 546 402 491 N ATOM 4943 CA PHE C 16 47.221 4.880 -11.189 1.00 28.67 C ANISOU 4943 CA PHE C 16 3666 3840 3388 541 419 487 C ATOM 4944 C PHE C 16 47.141 4.234 -12.569 1.00 38.65 C ANISOU 4944 C PHE C 16 4966 5095 4627 544 427 482 C ATOM 4945 O PHE C 16 48.075 4.347 -13.375 1.00 43.58 O ANISOU 4945 O PHE C 16 5608 5709 5241 540 432 478 O ATOM 4946 CB PHE C 16 47.697 3.873 -10.135 1.00 33.36 C ANISOU 4946 CB PHE C 16 4233 4431 4013 537 431 488 C ATOM 4947 CG PHE C 16 49.024 3.186 -10.457 1.00 28.80 C ANISOU 4947 CG PHE C 16 3664 3839 3442 531 445 484 C ATOM 4948 CD1 PHE C 16 49.069 1.945 -11.086 1.00 23.88 C ANISOU 4948 CD1 PHE C 16 3055 3206 2814 532 461 481 C ATOM 4949 CD2 PHE C 16 50.221 3.762 -10.058 1.00 26.43 C ANISOU 4949 CD2 PHE C 16 3355 3534 3153 524 442 484 C ATOM 4950 CE1 PHE C 16 50.280 1.322 -11.352 1.00 25.56 C ANISOU 4950 CE1 PHE C 16 3274 3405 3032 526 472 478 C ATOM 4951 CE2 PHE C 16 51.438 3.140 -10.326 1.00 31.26 C ANISOU 4951 CE2 PHE C 16 3974 4134 3771 519 453 481 C ATOM 4952 CZ PHE C 16 51.465 1.923 -10.975 1.00 27.19 C ANISOU 4952 CZ PHE C 16 3472 3608 3249 519 468 478 C ATOM 4953 N VAL C 17 46.043 3.528 -12.846 1.00 27.28 N ANISOU 4953 N VAL C 17 3535 3656 3175 551 427 484 N ATOM 4954 CA VAL C 17 45.914 2.847 -14.125 1.00 30.08 C ANISOU 4954 CA VAL C 17 3919 3996 3513 550 426 471 C ATOM 4955 C VAL C 17 45.718 3.863 -15.254 1.00 35.04 C ANISOU 4955 C VAL C 17 4578 4620 4115 551 405 465 C ATOM 4956 O VAL C 17 46.301 3.722 -16.335 1.00 35.89 O ANISOU 4956 O VAL C 17 4716 4720 4202 552 415 464 O ATOM 4957 CB VAL C 17 44.767 1.809 -14.071 1.00 23.96 C ANISOU 4957 CB VAL C 17 3136 3214 2754 548 414 453 C ATOM 4958 CG1 VAL C 17 44.557 1.163 -15.458 1.00 23.38 C ANISOU 4958 CG1 VAL C 17 3095 3125 2664 547 410 438 C ATOM 4959 CG2 VAL C 17 45.038 0.702 -13.037 1.00 9.18 C ANISOU 4959 CG2 VAL C 17 1237 1345 908 547 437 459 C ATOM 4960 N MET C 18 44.937 4.926 -15.011 1.00 30.32 N ANISOU 4960 N MET C 18 3974 4029 3516 551 378 463 N ATOM 4961 CA MET C 18 44.710 5.927 -16.055 1.00 25.15 C ANISOU 4961 CA MET C 18 3348 3370 2837 552 357 457 C ATOM 4962 C MET C 18 45.995 6.657 -16.419 1.00 33.29 C ANISOU 4962 C MET C 18 4394 4404 3852 552 373 470 C ATOM 4963 O MET C 18 46.256 6.916 -17.601 1.00 41.62 O ANISOU 4963 O MET C 18 5480 5449 4884 552 369 464 O ATOM 4964 CB MET C 18 43.653 6.938 -15.621 1.00 20.55 C ANISOU 4964 CB MET C 18 2754 2795 2259 552 324 453 C ATOM 4965 CG MET C 18 42.242 6.420 -15.600 1.00 22.26 C ANISOU 4965 CG MET C 18 2964 3007 2489 549 300 434 C ATOM 4966 SD MET C 18 41.089 7.769 -15.246 1.00 33.20 S ANISOU 4966 SD MET C 18 4339 4400 3875 549 261 429 S ATOM 4967 CE MET C 18 41.724 8.360 -13.676 1.00 46.02 C ANISOU 4967 CE MET C 18 5927 6041 5518 550 276 450 C ATOM 4968 N GLU C 19 46.824 6.982 -15.427 1.00 35.10 N ANISOU 4968 N GLU C 19 4593 4637 4105 545 382 472 N ATOM 4969 CA GLU C 19 48.083 7.663 -15.727 1.00 35.64 C ANISOU 4969 CA GLU C 19 4666 4702 4176 537 388 469 C ATOM 4970 C GLU C 19 49.049 6.736 -16.460 1.00 41.64 C ANISOU 4970 C GLU C 19 5440 5448 4931 535 409 465 C ATOM 4971 O GLU C 19 49.677 7.147 -17.438 1.00 49.38 O ANISOU 4971 O GLU C 19 6445 6422 5897 532 409 461 O ATOM 4972 CB GLU C 19 48.705 8.204 -14.442 1.00 32.28 C ANISOU 4972 CB GLU C 19 4204 4284 3778 532 390 472 C ATOM 4973 CG GLU C 19 47.909 9.379 -13.869 1.00 50.58 C ANISOU 4973 CG GLU C 19 6508 6612 6096 532 368 474 C ATOM 4974 CD GLU C 19 48.256 9.711 -12.417 1.00 61.29 C ANISOU 4974 CD GLU C 19 7827 7979 7482 528 370 477 C ATOM 4975 OE1 GLU C 19 49.016 8.942 -11.778 1.00 57.85 O ANISOU 4975 OE1 GLU C 19 7373 7539 7067 527 387 479 O ATOM 4976 OE2 GLU C 19 47.743 10.741 -11.913 1.00 68.27 O ANISOU 4976 OE2 GLU C 19 8699 8872 8368 527 354 478 O ATOM 4977 N GLU C 20 49.171 5.478 -16.013 1.00 43.99 N ANISOU 4977 N GLU C 20 5726 5744 5244 536 426 467 N ATOM 4978 CA GLU C 20 49.980 4.520 -16.754 1.00 36.47 C ANISOU 4978 CA GLU C 20 4789 4779 4288 534 445 463 C ATOM 4979 C GLU C 20 49.426 4.314 -18.154 1.00 37.42 C ANISOU 4979 C GLU C 20 4949 4893 4377 539 441 459 C ATOM 4980 O GLU C 20 50.192 4.075 -19.092 1.00 32.60 O ANISOU 4980 O GLU C 20 4359 4271 3755 536 450 454 O ATOM 4981 CB GLU C 20 50.078 3.181 -16.014 1.00 30.90 C ANISOU 4981 CB GLU C 20 4064 4072 3604 534 462 465 C ATOM 4982 CG GLU C 20 50.907 3.238 -14.737 1.00 36.17 C ANISOU 4982 CG GLU C 20 4697 4741 4303 528 465 468 C ATOM 4983 CD GLU C 20 52.397 3.466 -14.992 1.00 46.54 C ANISOU 4983 CD GLU C 20 6014 6047 5622 521 471 465 C ATOM 4984 OE1 GLU C 20 52.911 3.051 -16.048 1.00 53.71 O ANISOU 4984 OE1 GLU C 20 6946 6945 6515 520 481 461 O ATOM 4985 OE2 GLU C 20 53.055 4.100 -14.143 1.00 53.81 O ANISOU 4985 OE2 GLU C 20 6914 6970 6560 516 466 467 O ATOM 4986 N GLY C 21 48.106 4.415 -18.313 1.00 33.56 N ANISOU 4986 N GLY C 21 4471 4409 3873 547 426 460 N ATOM 4987 CA GLY C 21 47.515 4.270 -19.629 1.00 36.32 C ANISOU 4987 CA GLY C 21 4858 4750 4191 553 418 454 C ATOM 4988 C GLY C 21 47.805 5.449 -20.541 1.00 44.40 C ANISOU 4988 C GLY C 21 5905 5770 5195 550 402 450 C ATOM 4989 O GLY C 21 48.097 5.271 -21.728 1.00 40.77 O ANISOU 4989 O GLY C 21 5476 5299 4715 550 405 444 O ATOM 4990 N ARG C 22 47.699 6.670 -20.013 1.00 45.87 N ANISOU 4990 N ARG C 22 6077 5964 5387 547 386 452 N ATOM 4991 CA ARG C 22 48.053 7.843 -20.807 1.00 43.57 C ANISOU 4991 CA ARG C 22 5805 5669 5080 543 372 447 C ATOM 4992 C ARG C 22 49.554 7.888 -21.085 1.00 42.70 C ANISOU 4992 C ARG C 22 5695 5553 4977 534 391 446 C ATOM 4993 O ARG C 22 49.964 8.307 -22.172 1.00 46.11 O ANISOU 4993 O ARG C 22 6153 5976 5390 531 388 441 O ATOM 4994 CB ARG C 22 47.546 9.118 -20.116 1.00 39.13 C ANISOU 4994 CB ARG C 22 5226 5118 4524 541 350 449 C ATOM 4995 CG ARG C 22 46.008 9.238 -20.083 1.00 40.93 C ANISOU 4995 CG ARG C 22 5459 5350 4741 550 325 449 C ATOM 4996 CD ARG C 22 45.515 10.569 -19.495 1.00 45.68 C ANISOU 4996 CD ARG C 22 6046 5962 5350 548 301 449 C ATOM 4997 NE ARG C 22 45.844 11.715 -20.335 1.00 54.69 N ANISOU 4997 NE ARG C 22 7207 7099 6475 543 288 443 N ATOM 4998 CZ ARG C 22 45.771 12.989 -19.951 1.00 59.13 C ANISOU 4998 CZ ARG C 22 7758 7667 7042 538 272 443 C ATOM 4999 NH1 ARG C 22 45.384 13.307 -18.721 1.00 64.41 N ANISOU 4999 NH1 ARG C 22 8395 8347 7732 537 266 447 N ATOM 5000 NH2 ARG C 22 46.100 13.950 -20.803 1.00 56.25 N ANISOU 5000 NH2 ARG C 22 7413 7296 6662 533 263 437 N ATOM 5001 N LYS C 23 50.381 7.423 -20.141 1.00 44.48 N ANISOU 5001 N LYS C 23 5892 5781 5229 530 409 450 N ATOM 5002 CA LYS C 23 51.818 7.340 -20.390 1.00 45.70 C ANISOU 5002 CA LYS C 23 6045 5927 5390 522 425 448 C ATOM 5003 C LYS C 23 52.114 6.427 -21.575 1.00 56.92 C ANISOU 5003 C LYS C 23 7496 7337 6795 523 437 443 C ATOM 5004 O LYS C 23 52.993 6.722 -22.395 1.00 64.85 O ANISOU 5004 O LYS C 23 8517 8334 7790 518 441 440 O ATOM 5005 CB LYS C 23 52.543 6.824 -19.152 1.00 44.72 C ANISOU 5005 CB LYS C 23 5886 5807 5298 519 439 452 C ATOM 5006 CG LYS C 23 54.026 7.155 -19.089 1.00 53.58 C ANISOU 5006 CG LYS C 23 7002 6925 6432 510 447 451 C ATOM 5007 CD LYS C 23 54.709 6.550 -17.840 1.00 55.20 C ANISOU 5007 CD LYS C 23 7173 7131 6668 508 458 454 C ATOM 5008 CE LYS C 23 54.105 7.045 -16.535 1.00 70.44 C ANISOU 5008 CE LYS C 23 9074 9073 8616 509 447 458 C ATOM 5009 NZ LYS C 23 54.641 6.309 -15.335 1.00 76.18 N ANISOU 5009 NZ LYS C 23 9772 9801 9373 507 455 461 N ATOM 5010 N ALA C 24 51.386 5.321 -21.694 1.00 47.77 N ANISOU 5010 N ALA C 24 6343 6175 5631 530 443 443 N ATOM 5011 CA ALA C 24 51.623 4.386 -22.782 1.00 40.89 C ANISOU 5011 CA ALA C 24 5500 5293 4745 531 456 438 C ATOM 5012 C ALA C 24 50.811 4.713 -24.024 1.00 39.60 C ANISOU 5012 C ALA C 24 5374 5124 4549 537 440 432 C ATOM 5013 O ALA C 24 50.946 4.010 -25.024 1.00 51.55 O ANISOU 5013 O ALA C 24 6914 6627 6047 538 449 427 O ATOM 5014 CB ALA C 24 51.316 2.949 -22.341 1.00 32.32 C ANISOU 5014 CB ALA C 24 4404 4205 3671 535 471 439 C ATOM 5015 N ARG C 25 49.953 5.735 -23.976 1.00 41.25 N ANISOU 5015 N ARG C 25 5587 5339 4748 540 417 433 N ATOM 5016 CA ARG C 25 49.178 6.182 -25.144 1.00 45.15 C ANISOU 5016 CA ARG C 25 6117 5828 5212 544 397 426 C ATOM 5017 C ARG C 25 48.295 5.074 -25.703 1.00 42.93 C ANISOU 5017 C ARG C 25 5857 5541 4914 553 398 423 C ATOM 5018 O ARG C 25 48.088 4.976 -26.911 1.00 47.36 O ANISOU 5018 O ARG C 25 6453 6092 5450 556 392 415 O ATOM 5019 CB ARG C 25 50.059 6.762 -26.258 1.00 50.42 C ANISOU 5019 CB ARG C 25 6808 6486 5864 538 398 421 C ATOM 5020 CG ARG C 25 50.862 7.998 -25.904 1.00 64.96 C ANISOU 5020 CG ARG C 25 8633 8332 7715 530 394 424 C ATOM 5021 CD ARG C 25 51.720 8.423 -27.091 1.00 88.93 C ANISOU 5021 CD ARG C 25 11695 11359 10736 524 397 419 C ATOM 5022 NE ARG C 25 52.449 9.672 -26.866 1.00103.79 N ANISOU 5022 NE ARG C 25 13565 13244 12625 516 391 420 N ATOM 5023 CZ ARG C 25 53.635 9.789 -26.269 1.00112.64 C ANISOU 5023 CZ ARG C 25 14664 14368 13767 509 406 424 C ATOM 5024 NH1 ARG C 25 54.275 8.724 -25.809 1.00112.98 N ANISOU 5024 NH1 ARG C 25 14692 14409 13826 508 426 426 N ATOM 5025 NH2 ARG C 25 54.188 10.990 -26.147 1.00117.57 N ANISOU 5025 NH2 ARG C 25 15281 14995 14394 502 399 424 N ATOM 5026 N GLY C 26 47.768 4.237 -24.826 1.00 33.51 N ANISOU 5026 N GLY C 26 4642 4353 3738 556 404 425 N ATOM 5027 CA GLY C 26 46.845 3.206 -25.230 1.00 25.17 C ANISOU 5027 CA GLY C 26 3590 3286 2689 555 393 406 C ATOM 5028 C GLY C 26 45.448 3.769 -25.424 1.00 26.73 C ANISOU 5028 C GLY C 26 3789 3482 2885 554 354 392 C ATOM 5029 O GLY C 26 45.183 4.941 -25.167 1.00 27.16 O ANISOU 5029 O GLY C 26 3840 3544 2935 555 337 396 O ATOM 5030 N THR C 27 44.551 2.906 -25.914 1.00 20.47 N ANISOU 5030 N THR C 27 3002 2679 2095 553 342 373 N ATOM 5031 CA THR C 27 43.171 3.272 -26.216 1.00 28.31 C ANISOU 5031 CA THR C 27 4000 3670 3088 552 306 357 C ATOM 5032 C THR C 27 42.246 3.373 -25.012 1.00 32.77 C ANISOU 5032 C THR C 27 4529 4243 3678 551 290 355 C ATOM 5033 O THR C 27 41.181 3.985 -25.137 1.00 36.73 O ANISOU 5033 O THR C 27 5032 4745 4178 551 258 344 O ATOM 5034 CB THR C 27 42.558 2.233 -27.133 1.00 34.84 C ANISOU 5034 CB THR C 27 4845 4483 3910 551 299 338 C ATOM 5035 OG1 THR C 27 42.484 1.001 -26.411 1.00 34.54 O ANISOU 5035 OG1 THR C 27 4783 4444 3896 549 315 336 O ATOM 5036 CG2 THR C 27 43.391 2.057 -28.424 1.00 34.33 C ANISOU 5036 CG2 THR C 27 4817 4408 3819 552 314 338 C ATOM 5037 N GLY C 28 42.583 2.753 -23.877 1.00 25.73 N ANISOU 5037 N GLY C 28 3607 3358 2810 550 310 363 N ATOM 5038 CA GLY C 28 41.704 2.707 -22.729 1.00 23.44 C ANISOU 5038 CA GLY C 28 3283 3076 2546 548 296 361 C ATOM 5039 C GLY C 28 40.966 1.397 -22.505 1.00 34.98 C ANISOU 5039 C GLY C 28 4732 4532 4028 546 296 347 C ATOM 5040 O GLY C 28 40.315 1.256 -21.464 1.00 32.53 O ANISOU 5040 O GLY C 28 4391 4227 3740 544 289 346 O ATOM 5041 N GLU C 29 41.059 0.434 -23.433 1.00 37.54 N ANISOU 5041 N GLU C 29 5078 4844 4344 545 305 337 N ATOM 5042 CA GLU C 29 40.317 -0.817 -23.288 1.00 30.00 C ANISOU 5042 CA GLU C 29 4111 3881 3406 543 304 323 C ATOM 5043 C GLU C 29 40.767 -1.611 -22.060 1.00 30.13 C ANISOU 5043 C GLU C 29 4096 3904 3449 541 329 333 C ATOM 5044 O GLU C 29 39.947 -2.246 -21.388 1.00 21.70 O ANISOU 5044 O GLU C 29 3005 2836 2403 539 322 325 O ATOM 5045 CB GLU C 29 40.481 -1.667 -24.543 1.00 28.40 C ANISOU 5045 CB GLU C 29 3939 3664 3187 543 311 312 C ATOM 5046 CG GLU C 29 39.265 -2.523 -24.822 1.00 35.21 C ANISOU 5046 CG GLU C 29 4801 4517 4059 540 293 290 C ATOM 5047 CD GLU C 29 39.348 -3.281 -26.133 1.00 39.46 C ANISOU 5047 CD GLU C 29 5371 5041 4580 540 297 278 C ATOM 5048 OE1 GLU C 29 39.723 -2.663 -27.164 1.00 45.25 O ANISOU 5048 OE1 GLU C 29 6135 5770 5287 542 293 278 O ATOM 5049 OE2 GLU C 29 38.984 -4.483 -26.139 1.00 24.57 O ANISOU 5049 OE2 GLU C 29 3480 3148 2707 538 303 268 O ATOM 5050 N LEU C 30 42.078 -1.641 -21.797 1.00 26.48 N ANISOU 5050 N LEU C 30 3632 3446 2983 543 359 351 N ATOM 5051 CA LEU C 30 42.605 -2.348 -20.641 1.00 26.84 C ANISOU 5051 CA LEU C 30 3648 3498 3052 542 385 362 C ATOM 5052 C LEU C 30 42.198 -1.659 -19.332 1.00 32.65 C ANISOU 5052 C LEU C 30 4351 4248 3808 542 374 370 C ATOM 5053 O LEU C 30 41.946 -2.324 -18.320 1.00 28.14 O ANISOU 5053 O LEU C 30 3751 3680 3261 541 382 371 O ATOM 5054 CB LEU C 30 44.126 -2.449 -20.761 1.00 18.89 C ANISOU 5054 CB LEU C 30 2650 2492 2035 545 418 379 C ATOM 5055 CG LEU C 30 44.830 -3.161 -19.608 1.00 25.36 C ANISOU 5055 CG LEU C 30 3440 3317 2877 544 447 392 C ATOM 5056 CD1 LEU C 30 44.383 -4.634 -19.477 1.00 19.76 C ANISOU 5056 CD1 LEU C 30 2722 2600 2185 542 455 381 C ATOM 5057 CD2 LEU C 30 46.338 -3.049 -19.755 1.00 30.93 C ANISOU 5057 CD2 LEU C 30 4155 4025 3570 547 477 409 C ATOM 5058 N THR C 31 42.165 -0.325 -19.332 1.00 29.12 N ANISOU 5058 N THR C 31 3908 3808 3350 544 358 376 N ATOM 5059 CA THR C 31 41.704 0.425 -18.174 1.00 26.64 C ANISOU 5059 CA THR C 31 3564 3506 3051 543 345 382 C ATOM 5060 C THR C 31 40.246 0.126 -17.882 1.00 26.95 C ANISOU 5060 C THR C 31 3589 3543 3107 541 319 365 C ATOM 5061 O THR C 31 39.849 -0.049 -16.718 1.00 23.29 O ANISOU 5061 O THR C 31 3094 3088 2668 539 318 367 O ATOM 5062 CB THR C 31 41.910 1.925 -18.420 1.00 26.97 C ANISOU 5062 CB THR C 31 3617 3554 3075 545 331 389 C ATOM 5063 OG1 THR C 31 43.278 2.275 -18.144 1.00 25.47 O ANISOU 5063 OG1 THR C 31 3426 3371 2879 547 358 409 O ATOM 5064 CG2 THR C 31 40.932 2.797 -17.605 1.00 14.56 C ANISOU 5064 CG2 THR C 31 2023 1993 1516 545 304 387 C ATOM 5065 N GLN C 32 39.433 0.050 -18.927 1.00 27.49 N ANISOU 5065 N GLN C 32 3681 3602 3163 540 297 347 N ATOM 5066 CA GLN C 32 38.041 -0.324 -18.740 1.00 22.80 C ANISOU 5066 CA GLN C 32 3075 3005 2584 537 272 329 C ATOM 5067 C GLN C 32 37.929 -1.739 -18.165 1.00 24.80 C ANISOU 5067 C GLN C 32 3309 3255 2860 535 290 325 C ATOM 5068 O GLN C 32 37.117 -1.981 -17.257 1.00 26.55 O ANISOU 5068 O GLN C 32 3503 3480 3104 533 280 320 O ATOM 5069 CB GLN C 32 37.294 -0.167 -20.068 1.00 19.32 C ANISOU 5069 CB GLN C 32 2665 2553 2123 538 247 311 C ATOM 5070 CG GLN C 32 36.929 1.282 -20.442 1.00 22.31 C ANISOU 5070 CG GLN C 32 3056 2937 2485 539 220 311 C ATOM 5071 CD GLN C 32 36.474 1.462 -21.920 1.00 30.08 C ANISOU 5071 CD GLN C 32 4077 3909 3444 540 200 296 C ATOM 5072 OE1 GLN C 32 37.086 0.942 -22.844 1.00 29.11 O ANISOU 5072 OE1 GLN C 32 3978 3776 3305 541 215 294 O ATOM 5073 NE2 GLN C 32 35.400 2.204 -22.122 1.00 34.86 N ANISOU 5073 NE2 GLN C 32 4685 4515 4046 540 167 284 N ATOM 5074 N LEU C 33 38.779 -2.672 -18.633 1.00 21.13 N ANISOU 5074 N LEU C 33 2858 2782 2390 535 316 328 N ATOM 5075 CA LEU C 33 38.762 -4.041 -18.097 1.00 26.54 C ANISOU 5075 CA LEU C 33 3525 3463 3096 533 335 325 C ATOM 5076 C LEU C 33 39.090 -4.055 -16.603 1.00 22.11 C ANISOU 5076 C LEU C 33 2928 2915 2559 533 350 340 C ATOM 5077 O LEU C 33 38.327 -4.591 -15.794 1.00 17.89 O ANISOU 5077 O LEU C 33 2369 2382 2048 531 345 334 O ATOM 5078 CB LEU C 33 39.726 -4.949 -18.875 1.00 19.43 C ANISOU 5078 CB LEU C 33 2645 2552 2183 534 362 327 C ATOM 5079 CG LEU C 33 39.620 -6.477 -18.648 1.00 15.46 C ANISOU 5079 CG LEU C 33 2132 2042 1698 532 380 320 C ATOM 5080 CD1 LEU C 33 40.246 -7.224 -19.812 1.00 12.74 C ANISOU 5080 CD1 LEU C 33 1819 1686 1337 533 396 316 C ATOM 5081 CD2 LEU C 33 40.258 -6.974 -17.345 1.00 21.15 C ANISOU 5081 CD2 LEU C 33 2822 2771 2442 532 406 335 C ATOM 5082 N LEU C 34 40.213 -3.439 -16.229 1.00 28.46 N ANISOU 5082 N LEU C 34 3729 3728 3358 536 368 359 N ATOM 5083 CA LEU C 34 40.684 -3.463 -14.852 1.00 28.13 C ANISOU 5083 CA LEU C 34 3655 3698 3337 536 386 375 C ATOM 5084 C LEU C 34 39.742 -2.723 -13.924 1.00 23.81 C ANISOU 5084 C LEU C 34 3082 3160 2805 535 362 374 C ATOM 5085 O LEU C 34 39.528 -3.160 -12.785 1.00 20.85 O ANISOU 5085 O LEU C 34 2677 2790 2453 533 368 377 O ATOM 5086 CB LEU C 34 42.080 -2.864 -14.777 1.00 21.71 C ANISOU 5086 CB LEU C 34 2847 2891 2512 539 408 395 C ATOM 5087 CG LEU C 34 43.120 -3.806 -15.347 1.00 18.65 C ANISOU 5087 CG LEU C 34 2475 2495 2116 540 438 399 C ATOM 5088 CD1 LEU C 34 44.398 -3.068 -15.400 1.00 21.21 C ANISOU 5088 CD1 LEU C 34 2808 2826 2426 543 456 417 C ATOM 5089 CD2 LEU C 34 43.227 -5.055 -14.460 1.00 18.20 C ANISOU 5089 CD2 LEU C 34 2394 2438 2084 539 459 401 C ATOM 5090 N ASN C 35 39.133 -1.633 -14.404 1.00 23.15 N ANISOU 5090 N ASN C 35 3011 3078 2708 535 334 368 N ATOM 5091 CA ASN C 35 38.133 -0.939 -13.593 1.00 23.71 C ANISOU 5091 CA ASN C 35 3059 3158 2793 534 309 364 C ATOM 5092 C ASN C 35 36.927 -1.832 -13.331 1.00 20.29 C ANISOU 5092 C ASN C 35 2611 2719 2378 531 295 347 C ATOM 5093 O ASN C 35 36.390 -1.847 -12.215 1.00 27.53 O ANISOU 5093 O ASN C 35 3498 3644 3318 529 290 348 O ATOM 5094 CB ASN C 35 37.695 0.368 -14.271 1.00 23.96 C ANISOU 5094 CB ASN C 35 3109 3191 2805 535 280 360 C ATOM 5095 CG ASN C 35 36.531 1.046 -13.551 1.00 29.46 C ANISOU 5095 CG ASN C 35 3784 3895 3515 534 251 354 C ATOM 5096 OD1 ASN C 35 35.388 0.945 -13.983 1.00 29.69 O ANISOU 5096 OD1 ASN C 35 3818 3918 3544 532 226 336 O ATOM 5097 ND2 ASN C 35 36.809 1.695 -12.434 1.00 31.39 N ANISOU 5097 ND2 ASN C 35 4003 4152 3771 534 255 368 N ATOM 5098 N SER C 36 36.496 -2.594 -14.340 1.00 30.70 N ANISOU 5098 N SER C 36 3951 4024 3689 529 290 331 N ATOM 5099 CA SER C 36 35.395 -3.538 -14.134 1.00 33.42 C ANISOU 5099 CA SER C 36 4284 4363 4052 526 280 314 C ATOM 5100 C SER C 36 35.780 -4.663 -13.172 1.00 21.55 C ANISOU 5100 C SER C 36 2755 2860 2571 524 306 321 C ATOM 5101 O SER C 36 35.000 -5.014 -12.292 1.00 20.83 O ANISOU 5101 O SER C 36 2638 2772 2504 522 299 315 O ATOM 5102 CB SER C 36 34.935 -4.126 -15.473 1.00 31.09 C ANISOU 5102 CB SER C 36 4017 4052 3741 525 270 295 C ATOM 5103 OG SER C 36 34.427 -3.114 -16.323 1.00 38.13 O ANISOU 5103 OG SER C 36 4931 4943 4614 526 242 288 O ATOM 5104 N LEU C 37 36.983 -5.217 -13.299 1.00 18.88 N ANISOU 5104 N LEU C 37 2424 2520 2228 526 338 332 N ATOM 5105 CA LEU C 37 37.369 -6.292 -12.398 1.00 31.81 C ANISOU 5105 CA LEU C 37 4040 4159 3888 525 363 339 C ATOM 5106 C LEU C 37 37.387 -5.791 -10.948 1.00 30.14 C ANISOU 5106 C LEU C 37 3793 3961 3696 525 365 352 C ATOM 5107 O LEU C 37 36.882 -6.464 -10.046 1.00 31.07 O ANISOU 5107 O LEU C 37 3886 4081 3838 523 368 349 O ATOM 5108 CB LEU C 37 38.733 -6.851 -12.833 1.00 32.81 C ANISOU 5108 CB LEU C 37 4182 4282 4004 527 396 350 C ATOM 5109 CG LEU C 37 39.419 -7.996 -12.078 1.00 29.67 C ANISOU 5109 CG LEU C 37 3766 3883 3624 527 428 359 C ATOM 5110 CD1 LEU C 37 38.580 -9.263 -12.108 1.00 17.03 C ANISOU 5110 CD1 LEU C 37 2160 2272 2038 524 426 343 C ATOM 5111 CD2 LEU C 37 40.777 -8.262 -12.667 1.00 32.06 C ANISOU 5111 CD2 LEU C 37 4088 4182 3911 530 456 370 C ATOM 5112 N ACYS C 38 37.922 -4.584 -10.727 0.49 27.51 N ANISOU 5112 N ACYS C 38 3461 3639 3354 528 363 366 N ATOM 5113 N BCYS C 38 37.913 -4.587 -10.717 0.51 27.47 N ANISOU 5113 N BCYS C 38 3455 3634 3349 528 363 366 N ATOM 5114 CA ACYS C 38 38.037 -4.025 -9.383 0.49 25.95 C ANISOU 5114 CA ACYS C 38 3232 3455 3173 528 366 379 C ATOM 5115 CA BCYS C 38 38.007 -4.076 -9.353 0.51 25.96 C ANISOU 5115 CA BCYS C 38 3232 3456 3176 528 366 379 C ATOM 5116 C ACYS C 38 36.670 -3.772 -8.756 0.49 25.98 C ANISOU 5116 C ACYS C 38 3214 3463 3194 525 338 368 C ATOM 5117 C BCYS C 38 36.635 -3.839 -8.751 0.51 26.17 C ANISOU 5117 C BCYS C 38 3238 3486 3219 525 338 367 C ATOM 5118 O ACYS C 38 36.506 -3.934 -7.538 0.49 26.52 O ANISOU 5118 O ACYS C 38 3253 3540 3285 524 343 374 O ATOM 5119 O BCYS C 38 36.431 -4.051 -7.546 0.51 26.30 O ANISOU 5119 O BCYS C 38 3224 3510 3258 524 343 373 O ATOM 5120 CB ACYS C 38 38.888 -2.750 -9.442 0.49 28.26 C ANISOU 5120 CB ACYS C 38 3531 3757 3449 531 368 395 C ATOM 5121 CB BCYS C 38 38.834 -2.802 -9.332 0.51 27.97 C ANISOU 5121 CB BCYS C 38 3492 3721 3415 531 368 395 C ATOM 5122 SG ACYS C 38 38.255 -1.265 -8.643 0.49 38.03 S ANISOU 5122 SG ACYS C 38 4750 5009 4692 532 341 400 S ATOM 5123 SG BCYS C 38 40.523 -3.186 -9.696 0.51 29.50 S ANISOU 5123 SG BCYS C 38 3701 3913 3596 534 405 411 S ATOM 5124 N THR C 39 35.678 -3.403 -9.569 1.00 22.08 N ANISOU 5124 N THR C 39 2737 2963 2690 524 309 351 N ATOM 5125 CA THR C 39 34.301 -3.333 -9.091 1.00 20.15 C ANISOU 5125 CA THR C 39 2474 2720 2461 521 282 337 C ATOM 5126 C THR C 39 33.814 -4.716 -8.664 1.00 29.87 C ANISOU 5126 C THR C 39 3690 3945 3715 518 292 328 C ATOM 5127 O THR C 39 33.159 -4.855 -7.619 1.00 25.92 O ANISOU 5127 O THR C 39 3161 3451 3237 516 286 327 O ATOM 5128 CB THR C 39 33.397 -2.727 -10.178 1.00 25.13 C ANISOU 5128 CB THR C 39 3129 3345 3075 521 250 321 C ATOM 5129 OG1 THR C 39 33.707 -1.336 -10.324 1.00 19.78 O ANISOU 5129 OG1 THR C 39 2459 2675 2382 524 239 330 O ATOM 5130 CG2 THR C 39 31.926 -2.841 -9.804 1.00 22.48 C ANISOU 5130 CG2 THR C 39 2776 3008 2756 517 224 304 C ATOM 5131 N ALA C 40 34.150 -5.759 -9.449 1.00 24.91 N ANISOU 5131 N ALA C 40 3081 3305 3080 518 307 322 N ATOM 5132 CA ALA C 40 33.784 -7.122 -9.070 1.00 15.81 C ANISOU 5132 CA ALA C 40 1914 2145 1947 515 319 314 C ATOM 5133 C ALA C 40 34.428 -7.536 -7.753 1.00 15.64 C ANISOU 5133 C ALA C 40 1863 2132 1946 515 344 330 C ATOM 5134 O ALA C 40 33.811 -8.239 -6.944 1.00 17.94 O ANISOU 5134 O ALA C 40 2131 2424 2261 512 345 325 O ATOM 5135 CB ALA C 40 34.196 -8.102 -10.155 1.00 16.24 C ANISOU 5135 CB ALA C 40 1995 2187 1990 515 333 307 C ATOM 5136 N VAL C 41 35.697 -7.180 -7.562 1.00 17.57 N ANISOU 5136 N VAL C 41 2110 2384 2183 518 367 349 N ATOM 5137 CA VAL C 41 36.404 -7.561 -6.352 1.00 16.87 C ANISOU 5137 CA VAL C 41 1995 2302 2112 519 392 366 C ATOM 5138 C VAL C 41 35.761 -6.911 -5.137 1.00 21.18 C ANISOU 5138 C VAL C 41 2510 2860 2676 518 378 369 C ATOM 5139 O VAL C 41 35.619 -7.544 -4.089 1.00 25.92 O ANISOU 5139 O VAL C 41 3083 3464 3300 516 389 373 O ATOM 5140 CB VAL C 41 37.889 -7.200 -6.483 1.00 20.69 C ANISOU 5140 CB VAL C 41 2489 2791 2582 523 417 385 C ATOM 5141 CG1 VAL C 41 38.614 -7.299 -5.112 1.00 15.85 C ANISOU 5141 CG1 VAL C 41 1846 2188 1987 525 440 404 C ATOM 5142 CG2 VAL C 41 38.529 -8.119 -7.510 1.00 20.58 C ANISOU 5142 CG2 VAL C 41 2500 2764 2554 524 435 381 C ATOM 5143 N LYS C 42 35.329 -5.650 -5.264 1.00 25.46 N ANISOU 5143 N LYS C 42 3055 3408 3209 519 353 368 N ATOM 5144 CA LYS C 42 34.705 -4.989 -4.123 1.00 20.97 C ANISOU 5144 CA LYS C 42 2457 2852 2657 517 339 372 C ATOM 5145 C LYS C 42 33.406 -5.677 -3.752 1.00 24.99 C ANISOU 5145 C LYS C 42 2951 3357 3187 513 324 355 C ATOM 5146 O LYS C 42 33.112 -5.838 -2.564 1.00 26.95 O ANISOU 5146 O LYS C 42 3170 3613 3458 512 327 359 O ATOM 5147 CB LYS C 42 34.479 -3.490 -4.391 1.00 15.25 C ANISOU 5147 CB LYS C 42 1741 2135 1919 519 314 373 C ATOM 5148 CG LYS C 42 35.788 -2.699 -4.425 1.00 22.52 C ANISOU 5148 CG LYS C 42 2670 3063 2824 523 331 393 C ATOM 5149 CD LYS C 42 35.614 -1.162 -4.480 1.00 25.09 C ANISOU 5149 CD LYS C 42 2999 3397 3137 525 308 397 C ATOM 5150 CE LYS C 42 35.074 -0.672 -5.805 1.00 26.60 C ANISOU 5150 CE LYS C 42 3220 3580 3306 525 284 383 C ATOM 5151 NZ LYS C 42 34.788 0.811 -5.802 1.00 26.80 N ANISOU 5151 NZ LYS C 42 3247 3614 3320 526 260 386 N ATOM 5152 N ALA C 43 32.654 -6.169 -4.739 1.00 17.09 N ANISOU 5152 N ALA C 43 1969 2344 2180 511 309 336 N ATOM 5153 CA ALA C 43 31.437 -6.901 -4.392 1.00 19.50 C ANISOU 5153 CA ALA C 43 2259 2645 2505 507 296 319 C ATOM 5154 C ALA C 43 31.770 -8.263 -3.782 1.00 24.42 C ANISOU 5154 C ALA C 43 2867 3264 3147 505 323 322 C ATOM 5155 O ALA C 43 31.081 -8.731 -2.874 1.00 25.07 O ANISOU 5155 O ALA C 43 2925 3349 3253 502 321 318 O ATOM 5156 CB ALA C 43 30.533 -7.055 -5.614 1.00 11.63 C ANISOU 5156 CB ALA C 43 1287 1636 1496 505 273 297 C ATOM 5157 N ILE C 44 32.818 -8.916 -4.273 1.00 21.09 N ANISOU 5157 N ILE C 44 2462 2837 2716 507 349 329 N ATOM 5158 CA ILE C 44 33.223 -10.184 -3.687 1.00 17.81 C ANISOU 5158 CA ILE C 44 2033 2418 2317 506 377 333 C ATOM 5159 C ILE C 44 33.680 -9.981 -2.245 1.00 18.55 C ANISOU 5159 C ILE C 44 2101 2521 2427 499 386 348 C ATOM 5160 O ILE C 44 33.285 -10.728 -1.346 1.00 20.64 O ANISOU 5160 O ILE C 44 2351 2781 2708 484 383 342 O ATOM 5161 CB ILE C 44 34.292 -10.860 -4.568 1.00 12.30 C ANISOU 5161 CB ILE C 44 1360 1711 1604 509 401 338 C ATOM 5162 CG1 ILE C 44 33.626 -11.368 -5.863 1.00 25.63 C ANISOU 5162 CG1 ILE C 44 3075 3385 3280 507 387 317 C ATOM 5163 CG2 ILE C 44 35.021 -11.987 -3.835 1.00 13.50 C ANISOU 5163 CG2 ILE C 44 1496 1861 1771 509 434 348 C ATOM 5164 CD1 ILE C 44 34.584 -11.949 -6.906 1.00 19.32 C ANISOU 5164 CD1 ILE C 44 2303 2576 2462 509 407 319 C ATOM 5165 N SER C 45 34.512 -8.965 -2.005 1.00 14.12 N ANISOU 5165 N SER C 45 1546 1967 1852 494 384 362 N ATOM 5166 CA SER C 45 34.960 -8.692 -0.647 1.00 10.43 C ANISOU 5166 CA SER C 45 1070 1502 1392 471 378 368 C ATOM 5167 C SER C 45 33.776 -8.492 0.283 1.00 17.95 C ANISOU 5167 C SER C 45 2002 2457 2362 460 355 357 C ATOM 5168 O SER C 45 33.747 -9.047 1.380 1.00 23.58 O ANISOU 5168 O SER C 45 2706 3165 3087 442 353 354 O ATOM 5169 CB SER C 45 35.868 -7.458 -0.621 1.00 18.54 C ANISOU 5169 CB SER C 45 2107 2536 2403 469 376 383 C ATOM 5170 OG SER C 45 36.436 -7.235 0.673 1.00 20.34 O ANISOU 5170 OG SER C 45 2330 2763 2635 448 371 390 O ATOM 5171 N SER C 46 32.771 -7.724 -0.155 1.00 26.84 N ANISOU 5171 N SER C 46 3123 3590 3487 473 336 350 N ATOM 5172 CA SER C 46 31.614 -7.463 0.692 1.00 21.20 C ANISOU 5172 CA SER C 46 2390 2878 2789 462 312 339 C ATOM 5173 C SER C 46 30.844 -8.745 0.992 1.00 19.59 C ANISOU 5173 C SER C 46 2174 2665 2603 458 314 325 C ATOM 5174 O SER C 46 30.318 -8.909 2.093 1.00 20.80 O ANISOU 5174 O SER C 46 2314 2818 2772 441 303 318 O ATOM 5175 CB SER C 46 30.704 -6.424 0.046 1.00 18.88 C ANISOU 5175 CB SER C 46 2094 2591 2489 478 289 333 C ATOM 5176 OG SER C 46 29.565 -6.155 0.854 1.00 21.25 O ANISOU 5176 OG SER C 46 2376 2894 2804 467 265 321 O ATOM 5177 N ALA C 47 30.737 -9.650 0.021 1.00 25.13 N ANISOU 5177 N ALA C 47 2882 3361 3306 473 328 320 N ATOM 5178 CA ALA C 47 30.030 -10.905 0.277 1.00 28.52 C ANISOU 5178 CA ALA C 47 3301 3781 3753 469 331 308 C ATOM 5179 C ALA C 47 30.847 -11.834 1.161 1.00 26.05 C ANISOU 5179 C ALA C 47 2990 3463 3447 450 348 312 C ATOM 5180 O ALA C 47 30.285 -12.539 2.004 1.00 18.95 O ANISOU 5180 O ALA C 47 2078 2559 2564 437 343 303 O ATOM 5181 CB ALA C 47 29.680 -11.614 -1.032 1.00 20.87 C ANISOU 5181 CB ALA C 47 2341 2807 2782 492 341 300 C ATOM 5182 N VAL C 48 32.169 -11.862 0.973 1.00 19.69 N ANISOU 5182 N VAL C 48 2199 2656 2628 448 366 326 N ATOM 5183 CA VAL C 48 33.014 -12.748 1.769 1.00 20.45 C ANISOU 5183 CA VAL C 48 2298 2744 2728 432 379 331 C ATOM 5184 C VAL C 48 32.985 -12.353 3.249 1.00 22.28 C ANISOU 5184 C VAL C 48 2520 2978 2967 411 364 331 C ATOM 5185 O VAL C 48 32.940 -13.217 4.136 1.00 24.37 O ANISOU 5185 O VAL C 48 2779 3236 3243 398 366 327 O ATOM 5186 CB VAL C 48 34.447 -12.745 1.204 1.00 20.75 C ANISOU 5186 CB VAL C 48 2356 2780 2749 435 398 345 C ATOM 5187 CG1 VAL C 48 35.433 -13.349 2.192 1.00 11.44 C ANISOU 5187 CG1 VAL C 48 1180 1594 1574 418 405 352 C ATOM 5188 CG2 VAL C 48 34.486 -13.478 -0.114 1.00 22.03 C ANISOU 5188 CG2 VAL C 48 2528 2936 2905 453 417 342 C ATOM 5189 N ARG C 49 33.000 -11.050 3.542 1.00 20.14 N ANISOU 5189 N ARG C 49 2248 2715 2689 409 350 337 N ATOM 5190 CA ARG C 49 32.893 -10.546 4.912 1.00 21.45 C ANISOU 5190 CA ARG C 49 2407 2884 2860 391 335 336 C ATOM 5191 C ARG C 49 31.480 -10.642 5.458 1.00 22.53 C ANISOU 5191 C ARG C 49 2526 3021 3013 386 317 319 C ATOM 5192 O ARG C 49 31.261 -10.241 6.606 1.00 25.69 O ANISOU 5192 O ARG C 49 2921 3423 3418 371 304 316 O ATOM 5193 CB ARG C 49 33.355 -9.079 4.986 1.00 16.15 C ANISOU 5193 CB ARG C 49 1741 2221 2176 390 325 346 C ATOM 5194 CG ARG C 49 34.854 -8.854 5.165 1.00 17.99 C ANISOU 5194 CG ARG C 49 1989 2452 2395 385 337 362 C ATOM 5195 CD ARG C 49 35.644 -9.341 3.958 1.00 23.24 C ANISOU 5195 CD ARG C 49 2667 3114 3050 400 357 370 C ATOM 5196 NE ARG C 49 36.962 -8.711 3.859 1.00 18.57 N ANISOU 5196 NE ARG C 49 2090 2522 2443 399 364 386 N ATOM 5197 CZ ARG C 49 38.095 -9.196 4.348 1.00 14.40 C ANISOU 5197 CZ ARG C 49 1571 1986 1913 391 373 393 C ATOM 5198 NH1 ARG C 49 38.131 -10.354 5.008 1.00 16.24 N ANISOU 5198 NH1 ARG C 49 1801 2211 2159 381 377 388 N ATOM 5199 NH2 ARG C 49 39.206 -8.508 4.174 1.00 21.18 N ANISOU 5199 NH2 ARG C 49 2442 2846 2759 392 376 407 N ATOM 5200 N LYS C 50 30.535 -11.178 4.673 1.00 17.83 N ANISOU 5200 N LYS C 50 1924 2425 2426 398 316 308 N ATOM 5201 CA LYS C 50 29.190 -11.541 5.124 1.00 12.22 C ANISOU 5201 CA LYS C 50 1196 1713 1733 394 302 292 C ATOM 5202 C LYS C 50 28.264 -10.342 5.342 1.00 21.09 C ANISOU 5202 C LYS C 50 2311 2845 2858 394 277 285 C ATOM 5203 O LYS C 50 27.372 -10.392 6.199 1.00 21.39 O ANISOU 5203 O LYS C 50 2336 2882 2909 383 262 273 O ATOM 5204 CB LYS C 50 29.247 -12.374 6.407 1.00 21.09 C ANISOU 5204 CB LYS C 50 2316 2830 2868 375 304 287 C ATOM 5205 CG LYS C 50 29.957 -13.701 6.250 1.00 24.56 C ANISOU 5205 CG LYS C 50 2762 3261 3309 375 326 291 C ATOM 5206 CD LYS C 50 29.302 -14.604 5.208 1.00 23.49 C ANISOU 5206 CD LYS C 50 2623 3121 3181 389 334 282 C ATOM 5207 CE LYS C 50 30.053 -15.925 5.140 1.00 22.05 C ANISOU 5207 CE LYS C 50 2449 2929 3000 387 356 285 C ATOM 5208 NZ LYS C 50 29.491 -16.886 4.201 1.00 23.69 N ANISOU 5208 NZ LYS C 50 2654 3130 3215 399 366 276 N ATOM 5209 N ALA C 51 28.428 -9.257 4.583 1.00 30.53 N ANISOU 5209 N ALA C 51 3512 4047 4039 406 271 292 N ATOM 5210 CA ALA C 51 27.445 -8.172 4.634 1.00 26.65 C ANISOU 5210 CA ALA C 51 3013 3563 3551 407 245 285 C ATOM 5211 C ALA C 51 26.076 -8.696 4.197 1.00 25.96 C ANISOU 5211 C ALA C 51 2913 3473 3478 417 233 268 C ATOM 5212 O ALA C 51 25.945 -9.363 3.168 1.00 28.86 O ANISOU 5212 O ALA C 51 3284 3837 3846 433 242 266 O ATOM 5213 CB ALA C 51 27.887 -7.013 3.739 1.00 26.45 C ANISOU 5213 CB ALA C 51 2998 3545 3506 421 241 295 C ATOM 5214 N GLY C 52 25.055 -8.402 4.985 1.00 23.16 N ANISOU 5214 N GLY C 52 2545 3120 3135 406 212 255 N ATOM 5215 CA GLY C 52 23.734 -8.934 4.729 1.00 19.84 C ANISOU 5215 CA GLY C 52 2111 2697 2731 412 199 239 C ATOM 5216 C GLY C 52 23.437 -10.367 5.178 1.00 28.64 C ANISOU 5216 C GLY C 52 3218 3802 3861 405 211 230 C ATOM 5217 O GLY C 52 22.311 -10.827 4.948 1.00 33.21 O ANISOU 5217 O GLY C 52 3786 4379 4455 411 200 216 O ATOM 5218 N ILE C 53 24.356 -11.073 5.863 1.00 28.60 N ANISOU 5218 N ILE C 53 3219 3793 3855 393 231 237 N ATOM 5219 CA ILE C 53 24.063 -12.452 6.302 1.00 27.68 C ANISOU 5219 CA ILE C 53 3096 3668 3753 386 241 228 C ATOM 5220 C ILE C 53 22.811 -12.514 7.188 1.00 39.43 C ANISOU 5220 C ILE C 53 4568 5156 5257 375 222 211 C ATOM 5221 O ILE C 53 22.062 -13.503 7.150 1.00 41.05 O ANISOU 5221 O ILE C 53 4763 5356 5477 377 223 199 O ATOM 5222 CB ILE C 53 25.285 -13.082 7.025 1.00 23.48 C ANISOU 5222 CB ILE C 53 2573 3131 3215 373 261 239 C ATOM 5223 CG1 ILE C 53 25.095 -14.595 7.253 1.00 35.85 C ANISOU 5223 CG1 ILE C 53 4136 4690 4795 369 274 231 C ATOM 5224 CG2 ILE C 53 25.538 -12.437 8.387 1.00 14.82 C ANISOU 5224 CG2 ILE C 53 1478 2038 2116 355 252 241 C ATOM 5225 CD1 ILE C 53 25.147 -15.459 6.004 1.00 44.11 C ANISOU 5225 CD1 ILE C 53 5186 5731 5844 386 290 231 C ATOM 5226 N ALA C 54 22.521 -11.441 7.934 1.00 31.38 N ANISOU 5226 N ALA C 54 3546 4142 4235 366 204 209 N ATOM 5227 CA ALA C 54 21.320 -11.401 8.762 1.00 24.55 C ANISOU 5227 CA ALA C 54 2668 3278 3384 356 185 192 C ATOM 5228 C ALA C 54 20.040 -11.614 7.950 1.00 31.29 C ANISOU 5228 C ALA C 54 3509 4131 4250 369 171 178 C ATOM 5229 O ALA C 54 19.085 -12.217 8.455 1.00 24.28 O ANISOU 5229 O ALA C 54 2609 3241 3376 363 164 163 O ATOM 5230 CB ALA C 54 21.258 -10.065 9.511 1.00 20.56 C ANISOU 5230 CB ALA C 54 2163 2778 2870 346 168 192 C ATOM 5231 N HIS C 55 19.986 -11.139 6.698 1.00 28.66 N ANISOU 5231 N HIS C 55 3179 3801 3911 387 166 182 N ATOM 5232 CA HIS C 55 18.774 -11.379 5.917 1.00 34.53 C ANISOU 5232 CA HIS C 55 3911 4543 4666 401 152 169 C ATOM 5233 C HIS C 55 18.630 -12.848 5.550 1.00 38.33 C ANISOU 5233 C HIS C 55 4389 5015 5159 406 169 164 C ATOM 5234 O HIS C 55 17.510 -13.359 5.512 1.00 45.07 O ANISOU 5234 O HIS C 55 5229 5866 6028 408 158 149 O ATOM 5235 CB HIS C 55 18.733 -10.496 4.662 1.00 35.84 C ANISOU 5235 CB HIS C 55 4084 4714 4821 421 140 175 C ATOM 5236 CG HIS C 55 18.361 -9.070 4.947 1.00 41.72 C ANISOU 5236 CG HIS C 55 4828 5466 5559 416 115 173 C ATOM 5237 ND1 HIS C 55 19.288 -8.051 5.017 1.00 45.13 N ANISOU 5237 ND1 HIS C 55 5271 5903 5972 414 117 187 N ATOM 5238 CD2 HIS C 55 17.165 -8.503 5.236 1.00 44.14 C ANISOU 5238 CD2 HIS C 55 5123 5775 5874 413 88 159 C ATOM 5239 CE1 HIS C 55 18.678 -6.915 5.314 1.00 42.96 C ANISOU 5239 CE1 HIS C 55 4994 5633 5697 409 93 181 C ATOM 5240 NE2 HIS C 55 17.389 -7.163 5.454 1.00 43.95 N ANISOU 5240 NE2 HIS C 55 5106 5757 5838 408 75 164 N ATOM 5241 N LEU C 56 19.741 -13.565 5.371 1.00 39.21 N ANISOU 5241 N LEU C 56 4512 5123 5264 407 195 176 N ATOM 5242 CA LEU C 56 19.667 -14.994 5.078 1.00 37.92 C ANISOU 5242 CA LEU C 56 4346 4950 5112 410 213 171 C ATOM 5243 C LEU C 56 19.163 -15.802 6.260 1.00 43.22 C ANISOU 5243 C LEU C 56 5007 5618 5797 393 213 160 C ATOM 5244 O LEU C 56 18.628 -16.892 6.056 1.00 55.12 O ANISOU 5244 O LEU C 56 6507 7118 7318 395 220 150 O ATOM 5245 CB LEU C 56 21.028 -15.533 4.627 1.00 32.86 C ANISOU 5245 CB LEU C 56 3722 4306 4459 414 241 186 C ATOM 5246 CG LEU C 56 21.422 -15.302 3.159 1.00 36.75 C ANISOU 5246 CG LEU C 56 4226 4797 4939 438 248 193 C ATOM 5247 CD1 LEU C 56 21.204 -13.867 2.674 1.00 36.79 C ANISOU 5247 CD1 LEU C 56 4234 4812 4932 448 227 197 C ATOM 5248 CD2 LEU C 56 22.866 -15.719 2.937 1.00 43.72 C ANISOU 5248 CD2 LEU C 56 5126 5677 5808 437 276 208 C ATOM 5249 N TYR C 57 19.306 -15.291 7.481 1.00 31.17 N ANISOU 5249 N TYR C 57 3479 4096 4267 375 205 160 N ATOM 5250 CA TYR C 57 18.861 -15.975 8.682 1.00 32.28 C ANISOU 5250 CA TYR C 57 3613 4235 4418 359 204 151 C ATOM 5251 C TYR C 57 17.570 -15.391 9.259 1.00 42.15 C ANISOU 5251 C TYR C 57 4850 5490 5676 353 179 135 C ATOM 5252 O TYR C 57 17.278 -15.606 10.438 1.00 51.96 O ANISOU 5252 O TYR C 57 6089 6734 6921 339 175 128 O ATOM 5253 CB TYR C 57 19.974 -15.960 9.732 1.00 29.89 C ANISOU 5253 CB TYR C 57 3322 3933 4104 344 216 162 C ATOM 5254 CG TYR C 57 21.053 -17.007 9.493 1.00 30.92 C ANISOU 5254 CG TYR C 57 3462 4057 4231 344 241 173 C ATOM 5255 CD1 TYR C 57 22.047 -16.811 8.547 1.00 34.79 C ANISOU 5255 CD1 TYR C 57 3964 4546 4709 355 255 187 C ATOM 5256 CD2 TYR C 57 21.060 -18.208 10.216 1.00 26.41 C ANISOU 5256 CD2 TYR C 57 2889 3480 3667 335 252 169 C ATOM 5257 CE1 TYR C 57 23.038 -17.780 8.320 1.00 33.88 C ANISOU 5257 CE1 TYR C 57 3859 4424 4589 356 279 196 C ATOM 5258 CE2 TYR C 57 22.038 -19.180 10.000 1.00 27.58 C ANISOU 5258 CE2 TYR C 57 3048 3621 3812 335 274 178 C ATOM 5259 CZ TYR C 57 23.025 -18.961 9.048 1.00 36.38 C ANISOU 5259 CZ TYR C 57 4173 4734 4914 346 288 191 C ATOM 5260 OH TYR C 57 24.005 -19.913 8.825 1.00 36.26 O ANISOU 5260 OH TYR C 57 4170 4713 4896 346 310 200 O ATOM 5261 N GLY C 58 16.791 -14.662 8.463 1.00 31.41 N ANISOU 5261 N GLY C 58 3483 4133 4318 365 160 129 N ATOM 5262 CA GLY C 58 15.443 -14.310 8.862 1.00 32.98 C ANISOU 5262 CA GLY C 58 3669 4336 4528 362 136 112 C ATOM 5263 C GLY C 58 15.241 -13.033 9.657 1.00 40.45 C ANISOU 5263 C GLY C 58 4615 5288 5465 352 117 109 C ATOM 5264 O GLY C 58 14.264 -12.941 10.412 1.00 41.76 O ANISOU 5264 O GLY C 58 4772 5457 5637 344 102 95 O ATOM 5265 N ILE C 59 16.102 -12.021 9.485 1.00 38.74 N ANISOU 5265 N ILE C 59 4410 5075 5234 353 117 123 N ATOM 5266 CA ILE C 59 15.925 -10.791 10.254 1.00 27.69 C ANISOU 5266 CA ILE C 59 3013 3681 3828 343 100 120 C ATOM 5267 C ILE C 59 14.650 -10.077 9.828 1.00 40.11 C ANISOU 5267 C ILE C 59 4576 5258 5408 350 73 106 C ATOM 5268 O ILE C 59 14.025 -9.381 10.636 1.00 36.59 O ANISOU 5268 O ILE C 59 4126 4814 4961 340 56 95 O ATOM 5269 CB ILE C 59 17.153 -9.872 10.150 1.00 23.61 C ANISOU 5269 CB ILE C 59 2510 3166 3294 342 108 137 C ATOM 5270 CG1 ILE C 59 17.084 -8.798 11.227 1.00 24.97 C ANISOU 5270 CG1 ILE C 59 2685 3341 3460 329 95 134 C ATOM 5271 CG2 ILE C 59 17.287 -9.200 8.738 1.00 16.11 C ANISOU 5271 CG2 ILE C 59 1564 2219 2338 361 102 146 C ATOM 5272 CD1 ILE C 59 18.221 -7.811 11.135 1.00 33.61 C ANISOU 5272 CD1 ILE C 59 3794 4439 4539 328 100 151 C ATOM 5273 N ALA C 60 14.212 -10.264 8.581 1.00 40.47 N ANISOU 5273 N ALA C 60 4616 5302 5459 367 67 104 N ATOM 5274 CA ALA C 60 12.930 -9.729 8.138 1.00 37.03 C ANISOU 5274 CA ALA C 60 4170 4868 5031 374 39 90 C ATOM 5275 C ALA C 60 11.856 -10.814 8.054 1.00 47.37 C ANISOU 5275 C ALA C 60 5466 6176 6358 376 36 75 C ATOM 5276 O ALA C 60 10.818 -10.601 7.420 1.00 50.15 O ANISOU 5276 O ALA C 60 5809 6528 6717 386 14 64 O ATOM 5277 CB ALA C 60 13.081 -9.031 6.787 1.00 33.53 C ANISOU 5277 CB ALA C 60 3733 4427 4581 392 29 99 C ATOM 5278 N GLY C 61 12.067 -11.950 8.722 1.00 52.05 N ANISOU 5278 N GLY C 61 6056 6765 6955 368 55 74 N ATOM 5279 CA GLY C 61 11.132 -13.066 8.682 1.00 55.07 C ANISOU 5279 CA GLY C 61 6427 7145 7353 369 56 61 C ATOM 5280 C GLY C 61 11.291 -14.045 7.524 1.00 58.19 C ANISOU 5280 C GLY C 61 6821 7531 7759 384 69 64 C ATOM 5281 O GLY C 61 11.786 -13.706 6.444 1.00 58.70 O ANISOU 5281 O GLY C 61 6893 7593 7819 399 71 74 O ATOM 5282 N LYS C 72 25.452 -19.814 -3.278 1.00 41.27 N ANISOU 5282 N LYS C 72 4943 5306 5430 467 354 190 N ATOM 5283 CA LYS C 72 26.737 -20.279 -2.777 1.00 42.44 C ANISOU 5283 CA LYS C 72 5087 5457 5580 470 388 210 C ATOM 5284 C LYS C 72 27.828 -19.297 -3.201 1.00 36.03 C ANISOU 5284 C LYS C 72 4291 4652 4745 476 393 226 C ATOM 5285 O LYS C 72 27.779 -18.735 -4.295 1.00 26.58 O ANISOU 5285 O LYS C 72 3120 3452 3527 477 377 219 O ATOM 5286 CB LYS C 72 27.013 -21.688 -3.296 1.00 48.27 C ANISOU 5286 CB LYS C 72 5838 6182 6321 469 408 203 C ATOM 5287 CG LYS C 72 28.276 -22.333 -2.775 1.00 60.11 C ANISOU 5287 CG LYS C 72 7332 7683 7824 472 444 222 C ATOM 5288 CD LYS C 72 28.640 -23.561 -3.619 1.00 71.98 C ANISOU 5288 CD LYS C 72 8855 9171 9322 472 462 215 C ATOM 5289 CE LYS C 72 27.950 -24.836 -3.157 1.00 77.08 C ANISOU 5289 CE LYS C 72 9486 9809 9991 467 469 204 C ATOM 5290 NZ LYS C 72 28.643 -25.477 -2.003 1.00 78.46 N ANISOU 5290 NZ LYS C 72 9640 9989 10184 468 498 220 N ATOM 5291 N LEU C 73 28.842 -19.140 -2.352 1.00 35.30 N ANISOU 5291 N LEU C 73 4185 4568 4658 479 415 247 N ATOM 5292 CA LEU C 73 29.781 -18.029 -2.513 1.00 31.33 C ANISOU 5292 CA LEU C 73 3692 4075 4136 484 418 263 C ATOM 5293 C LEU C 73 30.681 -18.185 -3.737 1.00 33.33 C ANISOU 5293 C LEU C 73 3978 4321 4366 487 430 265 C ATOM 5294 O LEU C 73 30.948 -17.206 -4.445 1.00 35.02 O ANISOU 5294 O LEU C 73 4211 4538 4559 490 418 267 O ATOM 5295 CB LEU C 73 30.626 -17.879 -1.252 1.00 29.84 C ANISOU 5295 CB LEU C 73 3488 3894 3954 474 429 280 C ATOM 5296 CG LEU C 73 30.867 -16.465 -0.720 1.00 34.66 C ANISOU 5296 CG LEU C 73 4096 4517 4557 469 412 290 C ATOM 5297 CD1 LEU C 73 29.593 -15.605 -0.819 1.00 27.68 C ANISOU 5297 CD1 LEU C 73 3199 3639 3678 478 387 281 C ATOM 5298 CD2 LEU C 73 31.379 -16.518 0.729 1.00 31.26 C ANISOU 5298 CD2 LEU C 73 3657 4087 4132 444 408 297 C ATOM 5299 N ASP C 74 31.152 -19.392 -4.024 1.00 30.08 N ANISOU 5299 N ASP C 74 3574 3899 3957 487 453 264 N ATOM 5300 CA ASP C 74 31.984 -19.513 -5.213 1.00 40.06 C ANISOU 5300 CA ASP C 74 4869 5156 5197 490 463 265 C ATOM 5301 C ASP C 74 31.151 -19.339 -6.480 1.00 34.01 C ANISOU 5301 C ASP C 74 4128 4380 4415 488 437 245 C ATOM 5302 O ASP C 74 31.649 -18.797 -7.469 1.00 34.13 O ANISOU 5302 O ASP C 74 4169 4394 4406 491 434 246 O ATOM 5303 CB ASP C 74 32.736 -20.849 -5.207 1.00 40.58 C ANISOU 5303 CB ASP C 74 4937 5213 5268 490 495 269 C ATOM 5304 CG ASP C 74 31.817 -22.022 -5.076 1.00 49.58 C ANISOU 5304 CG ASP C 74 6069 6343 6427 486 493 253 C ATOM 5305 OD1 ASP C 74 30.599 -21.794 -4.896 1.00 45.33 O ANISOU 5305 OD1 ASP C 74 5521 5806 5898 482 468 239 O ATOM 5306 OD2 ASP C 74 32.311 -23.169 -5.152 1.00 62.11 O ANISOU 5306 OD2 ASP C 74 7659 7922 8018 486 517 254 O ATOM 5307 N VAL C 75 29.872 -19.723 -6.439 1.00 31.41 N ANISOU 5307 N VAL C 75 3791 4046 4098 483 417 226 N ATOM 5308 CA VAL C 75 28.966 -19.457 -7.552 1.00 34.16 C ANISOU 5308 CA VAL C 75 4159 4386 4433 482 389 206 C ATOM 5309 C VAL C 75 28.706 -17.954 -7.692 1.00 35.54 C ANISOU 5309 C VAL C 75 4338 4570 4595 483 364 208 C ATOM 5310 O VAL C 75 28.770 -17.403 -8.799 1.00 34.64 O ANISOU 5310 O VAL C 75 4251 4453 4458 485 351 203 O ATOM 5311 CB VAL C 75 27.655 -20.253 -7.376 1.00 28.29 C ANISOU 5311 CB VAL C 75 3405 3636 3709 476 375 186 C ATOM 5312 CG1 VAL C 75 26.621 -19.794 -8.371 1.00 32.06 C ANISOU 5312 CG1 VAL C 75 3899 4107 4174 474 343 166 C ATOM 5313 CG2 VAL C 75 27.900 -21.745 -7.588 1.00 14.47 C ANISOU 5313 CG2 VAL C 75 1658 1873 1966 474 398 181 C ATOM 5314 N LEU C 76 28.427 -17.261 -6.579 1.00 27.75 N ANISOU 5314 N LEU C 76 3325 3596 3622 483 356 216 N ATOM 5315 CA LEU C 76 28.185 -15.817 -6.668 1.00 21.93 C ANISOU 5315 CA LEU C 76 2591 2868 2874 485 332 219 C ATOM 5316 C LEU C 76 29.421 -15.090 -7.169 1.00 18.89 C ANISOU 5316 C LEU C 76 2225 2488 2466 490 344 235 C ATOM 5317 O LEU C 76 29.323 -14.205 -8.028 1.00 16.10 O ANISOU 5317 O LEU C 76 1892 2133 2091 492 325 231 O ATOM 5318 CB LEU C 76 27.761 -15.240 -5.310 1.00 26.49 C ANISOU 5318 CB LEU C 76 3135 3458 3471 484 325 226 C ATOM 5319 CG LEU C 76 27.543 -13.716 -5.135 1.00 32.66 C ANISOU 5319 CG LEU C 76 3913 4252 4244 486 302 231 C ATOM 5320 CD1 LEU C 76 26.298 -13.229 -5.827 1.00 31.91 C ANISOU 5320 CD1 LEU C 76 3829 4153 4143 483 267 211 C ATOM 5321 CD2 LEU C 76 27.491 -13.278 -3.681 1.00 30.98 C ANISOU 5321 CD2 LEU C 76 3667 4052 4051 485 304 244 C ATOM 5322 N SER C 77 30.600 -15.471 -6.662 1.00 11.24 N ANISOU 5322 N SER C 77 1250 1522 1500 492 375 253 N ATOM 5323 CA SER C 77 31.824 -14.816 -7.097 1.00 16.09 C ANISOU 5323 CA SER C 77 1881 2140 2093 497 388 269 C ATOM 5324 C SER C 77 32.053 -15.006 -8.596 1.00 19.85 C ANISOU 5324 C SER C 77 2394 2605 2545 498 386 260 C ATOM 5325 O SER C 77 32.446 -14.070 -9.291 1.00 20.61 O ANISOU 5325 O SER C 77 2509 2703 2619 501 378 264 O ATOM 5326 CB SER C 77 33.010 -15.327 -6.288 1.00 9.52 C ANISOU 5326 CB SER C 77 1036 1313 1270 500 423 289 C ATOM 5327 OG SER C 77 32.865 -15.003 -4.920 1.00 22.21 O ANISOU 5327 OG SER C 77 2611 2931 2897 499 424 299 O ATOM 5328 N ASN C 78 31.823 -16.218 -9.099 1.00 25.04 N ANISOU 5328 N ASN C 78 3059 3249 3205 496 394 247 N ATOM 5329 CA ASN C 78 31.997 -16.487 -10.518 1.00 22.16 C ANISOU 5329 CA ASN C 78 2728 2872 2818 497 392 237 C ATOM 5330 C ASN C 78 31.070 -15.606 -11.347 1.00 22.34 C ANISOU 5330 C ASN C 78 2767 2894 2827 496 358 222 C ATOM 5331 O ASN C 78 31.493 -15.028 -12.354 1.00 21.79 O ANISOU 5331 O ASN C 78 2725 2822 2733 499 353 223 O ATOM 5332 CB ASN C 78 31.732 -17.975 -10.785 1.00 24.02 C ANISOU 5332 CB ASN C 78 2966 3095 3064 494 405 225 C ATOM 5333 CG ASN C 78 32.213 -18.439 -12.172 1.00 33.10 C ANISOU 5333 CG ASN C 78 4151 4233 4193 495 412 218 C ATOM 5334 OD1 ASN C 78 33.367 -18.220 -12.560 1.00 33.14 O ANISOU 5334 OD1 ASN C 78 4172 4240 4182 499 430 232 O ATOM 5335 ND2 ASN C 78 31.325 -19.097 -12.909 1.00 21.44 N ANISOU 5335 ND2 ASN C 78 2686 2745 2716 492 398 198 N ATOM 5336 N ASP C 79 29.816 -15.450 -10.903 1.00 22.29 N ANISOU 5336 N ASP C 79 2744 2889 2835 493 333 210 N ATOM 5337 CA ASP C 79 28.834 -14.643 -11.630 1.00 24.17 C ANISOU 5337 CA ASP C 79 2995 3126 3061 492 299 195 C ATOM 5338 C ASP C 79 29.214 -13.169 -11.641 1.00 28.58 C ANISOU 5338 C ASP C 79 3560 3696 3605 496 287 207 C ATOM 5339 O ASP C 79 28.983 -12.466 -12.638 1.00 30.62 O ANISOU 5339 O ASP C 79 3842 3951 3842 497 267 199 O ATOM 5340 CB ASP C 79 27.445 -14.827 -11.016 1.00 19.92 C ANISOU 5340 CB ASP C 79 2436 2589 2545 488 277 179 C ATOM 5341 CG ASP C 79 26.881 -16.217 -11.280 1.00 32.52 C ANISOU 5341 CG ASP C 79 4032 4172 4153 484 282 163 C ATOM 5342 OD1 ASP C 79 27.509 -16.947 -12.062 1.00 31.22 O ANISOU 5342 OD1 ASP C 79 3888 3998 3977 485 299 162 O ATOM 5343 OD2 ASP C 79 25.836 -16.594 -10.700 1.00 37.63 O ANISOU 5343 OD2 ASP C 79 4659 4818 4820 480 270 151 O ATOM 5344 N LEU C 80 29.781 -12.680 -10.538 1.00 20.52 N ANISOU 5344 N LEU C 80 2516 2687 2594 497 299 225 N ATOM 5345 CA LEU C 80 30.182 -11.278 -10.469 1.00 25.10 C ANISOU 5345 CA LEU C 80 3099 3277 3160 500 290 237 C ATOM 5346 C LEU C 80 31.311 -10.973 -11.451 1.00 28.24 C ANISOU 5346 C LEU C 80 3526 3672 3531 504 303 246 C ATOM 5347 O LEU C 80 31.249 -9.978 -12.186 1.00 19.99 O ANISOU 5347 O LEU C 80 2501 2628 2466 506 285 244 O ATOM 5348 CB LEU C 80 30.594 -10.935 -9.034 1.00 20.83 C ANISOU 5348 CB LEU C 80 2526 2750 2637 501 303 255 C ATOM 5349 CG LEU C 80 29.424 -10.765 -8.047 1.00 23.04 C ANISOU 5349 CG LEU C 80 2777 3036 2940 498 283 248 C ATOM 5350 CD1 LEU C 80 29.876 -10.873 -6.585 1.00 20.33 C ANISOU 5350 CD1 LEU C 80 2401 2704 2618 498 302 264 C ATOM 5351 CD2 LEU C 80 28.787 -9.415 -8.295 1.00 25.97 C ANISOU 5351 CD2 LEU C 80 3153 3414 3300 499 251 243 C ATOM 5352 N VAL C 81 32.363 -11.812 -11.452 1.00 20.97 N ANISOU 5352 N VAL C 81 2609 2748 2610 505 335 256 N ATOM 5353 CA VAL C 81 33.506 -11.621 -12.338 1.00 18.94 C ANISOU 5353 CA VAL C 81 2380 2488 2329 509 350 265 C ATOM 5354 C VAL C 81 33.098 -11.791 -13.804 1.00 24.49 C ANISOU 5354 C VAL C 81 3116 3178 3012 509 336 248 C ATOM 5355 O VAL C 81 33.502 -11.008 -14.666 1.00 25.52 O ANISOU 5355 O VAL C 81 3270 3307 3118 511 329 251 O ATOM 5356 CB VAL C 81 34.646 -12.582 -11.958 1.00 21.35 C ANISOU 5356 CB VAL C 81 2679 2791 2642 510 388 279 C ATOM 5357 CG1 VAL C 81 35.814 -12.429 -12.957 1.00 18.92 C ANISOU 5357 CG1 VAL C 81 2401 2479 2308 514 404 287 C ATOM 5358 CG2 VAL C 81 35.113 -12.310 -10.531 1.00 13.89 C ANISOU 5358 CG2 VAL C 81 1703 1860 1715 511 402 297 C ATOM 5359 N MET C 82 32.321 -12.839 -14.105 1.00 33.52 N ANISOU 5359 N MET C 82 4260 4311 4165 505 331 231 N ATOM 5360 CA MET C 82 31.867 -13.089 -15.470 1.00 36.38 C ANISOU 5360 CA MET C 82 4653 4661 4510 505 317 213 C ATOM 5361 C MET C 82 31.087 -11.901 -16.016 1.00 34.77 C ANISOU 5361 C MET C 82 4460 4459 4291 505 283 204 C ATOM 5362 O MET C 82 31.275 -11.497 -17.171 1.00 29.87 O ANISOU 5362 O MET C 82 3870 3833 3646 507 275 200 O ATOM 5363 CB MET C 82 31.004 -14.362 -15.520 1.00 26.24 C ANISOU 5363 CB MET C 82 3362 3365 3241 501 315 195 C ATOM 5364 CG MET C 82 31.792 -15.676 -15.471 1.00 25.22 C ANISOU 5364 CG MET C 82 3234 3229 3119 500 348 200 C ATOM 5365 SD MET C 82 32.664 -16.121 -17.001 1.00 34.29 S ANISOU 5365 SD MET C 82 4423 4366 4240 503 363 198 S ATOM 5366 CE MET C 82 31.209 -16.399 -17.980 1.00 46.85 C ANISOU 5366 CE MET C 82 6030 5946 5827 499 330 169 C ATOM 5367 N ASN C 83 30.184 -11.344 -15.209 1.00 27.17 N ANISOU 5367 N ASN C 83 3475 3504 3344 504 262 201 N ATOM 5368 CA ASN C 83 29.299 -10.297 -15.721 1.00 25.76 C ANISOU 5368 CA ASN C 83 3306 3327 3153 504 227 190 C ATOM 5369 C ASN C 83 30.034 -8.973 -15.918 1.00 31.01 C ANISOU 5369 C ASN C 83 3983 4001 3799 508 225 205 C ATOM 5370 O ASN C 83 29.846 -8.305 -16.941 1.00 41.83 O ANISOU 5370 O ASN C 83 5379 5367 5147 510 206 198 O ATOM 5371 CB ASN C 83 28.101 -10.133 -14.792 1.00 30.25 C ANISOU 5371 CB ASN C 83 3847 3902 3746 501 206 182 C ATOM 5372 CG ASN C 83 27.093 -9.118 -15.302 1.00 47.01 C ANISOU 5372 CG ASN C 83 5979 6026 5858 501 169 169 C ATOM 5373 OD1 ASN C 83 26.296 -9.416 -16.197 1.00 58.29 O ANISOU 5373 OD1 ASN C 83 7424 7445 7280 500 151 150 O ATOM 5374 ND2 ASN C 83 27.111 -7.914 -14.722 1.00 47.02 N ANISOU 5374 ND2 ASN C 83 5968 6039 5858 503 158 179 N ATOM 5375 N MET C 84 30.905 -8.593 -14.974 1.00 33.58 N ANISOU 5375 N MET C 84 4291 4337 4131 510 244 225 N ATOM 5376 CA MET C 84 31.615 -7.322 -15.105 1.00 25.75 C ANISOU 5376 CA MET C 84 3308 3353 3121 513 242 240 C ATOM 5377 C MET C 84 32.628 -7.353 -16.242 1.00 27.03 C ANISOU 5377 C MET C 84 3504 3509 3258 516 257 245 C ATOM 5378 O MET C 84 32.888 -6.318 -16.867 1.00 23.77 O ANISOU 5378 O MET C 84 3111 3099 2824 519 246 248 O ATOM 5379 CB MET C 84 32.302 -6.967 -13.793 1.00 23.09 C ANISOU 5379 CB MET C 84 2944 3030 2799 514 259 260 C ATOM 5380 CG MET C 84 31.323 -6.631 -12.657 1.00 31.57 C ANISOU 5380 CG MET C 84 3986 4113 3895 512 242 257 C ATOM 5381 SD MET C 84 30.148 -5.296 -12.997 1.00 30.73 S ANISOU 5381 SD MET C 84 3884 4010 3780 512 199 246 S ATOM 5382 CE MET C 84 31.284 -3.922 -13.272 1.00 24.08 C ANISOU 5382 CE MET C 84 3059 3177 2915 517 203 265 C ATOM 5383 N LEU C 85 33.224 -8.518 -16.513 1.00 25.98 N ANISOU 5383 N LEU C 85 3378 3368 3127 516 282 245 N ATOM 5384 CA LEU C 85 34.173 -8.612 -17.620 1.00 22.05 C ANISOU 5384 CA LEU C 85 2912 2863 2604 518 296 249 C ATOM 5385 C LEU C 85 33.445 -8.583 -18.973 1.00 29.31 C ANISOU 5385 C LEU C 85 3861 3770 3504 518 273 229 C ATOM 5386 O LEU C 85 33.834 -7.830 -19.879 1.00 33.71 O ANISOU 5386 O LEU C 85 4445 4326 4037 521 267 231 O ATOM 5387 CB LEU C 85 35.020 -9.874 -17.466 1.00 17.09 C ANISOU 5387 CB LEU C 85 2281 2229 1984 518 331 255 C ATOM 5388 CG LEU C 85 36.046 -9.811 -16.336 1.00 15.70 C ANISOU 5388 CG LEU C 85 2082 2063 1819 519 357 277 C ATOM 5389 CD1 LEU C 85 36.786 -11.113 -16.266 1.00 27.13 C ANISOU 5389 CD1 LEU C 85 3529 3505 3275 519 389 281 C ATOM 5390 CD2 LEU C 85 37.038 -8.703 -16.493 1.00 12.41 C ANISOU 5390 CD2 LEU C 85 1676 1655 1384 523 364 293 C ATOM 5391 N LYS C 86 32.380 -9.387 -19.124 1.00 18.41 N ANISOU 5391 N LYS C 86 2478 2383 2136 515 260 210 N ATOM 5392 CA LYS C 86 31.566 -9.353 -20.343 1.00 27.28 C ANISOU 5392 CA LYS C 86 3627 3495 3243 514 235 190 C ATOM 5393 C LYS C 86 31.083 -7.944 -20.669 1.00 27.42 C ANISOU 5393 C LYS C 86 3654 3519 3246 516 205 188 C ATOM 5394 O LYS C 86 31.136 -7.509 -21.831 1.00 24.20 O ANISOU 5394 O LYS C 86 3277 3105 2814 518 194 182 O ATOM 5395 CB LYS C 86 30.346 -10.279 -20.231 1.00 22.01 C ANISOU 5395 CB LYS C 86 2948 2821 2594 510 221 170 C ATOM 5396 CG LYS C 86 30.645 -11.765 -20.319 1.00 22.73 C ANISOU 5396 CG LYS C 86 3039 2902 2695 508 246 166 C ATOM 5397 CD LYS C 86 29.402 -12.601 -20.062 1.00 19.87 C ANISOU 5397 CD LYS C 86 2662 2535 2353 504 232 147 C ATOM 5398 CE LYS C 86 29.716 -14.089 -20.178 1.00 31.08 C ANISOU 5398 CE LYS C 86 4083 3945 3782 502 257 143 C ATOM 5399 NZ LYS C 86 28.572 -14.945 -19.779 1.00 35.54 N ANISOU 5399 NZ LYS C 86 4630 4505 4369 498 246 126 N ATOM 5400 N SER C 87 30.554 -7.242 -19.660 1.00 23.32 N ANISOU 5400 N SER C 87 3109 3011 2742 516 191 192 N ATOM 5401 CA SER C 87 29.955 -5.919 -19.848 1.00 25.25 C ANISOU 5401 CA SER C 87 3359 3261 2976 517 161 189 C ATOM 5402 C SER C 87 30.985 -4.807 -19.958 1.00 25.88 C ANISOU 5402 C SER C 87 3450 3348 3037 521 169 208 C ATOM 5403 O SER C 87 30.606 -3.659 -20.194 1.00 32.94 O ANISOU 5403 O SER C 87 4350 4246 3918 523 145 207 O ATOM 5404 CB SER C 87 28.974 -5.607 -18.705 1.00 32.33 C ANISOU 5404 CB SER C 87 4222 4166 3896 515 143 186 C ATOM 5405 OG SER C 87 29.647 -5.429 -17.457 1.00 39.33 O ANISOU 5405 OG SER C 87 5082 5065 4798 515 163 205 O ATOM 5406 N SER C 88 32.268 -5.110 -19.809 1.00 23.82 N ANISOU 5406 N SER C 88 3190 3088 2772 522 201 224 N ATOM 5407 CA SER C 88 33.277 -4.088 -20.028 1.00 26.36 C ANISOU 5407 CA SER C 88 3525 3416 3074 526 208 241 C ATOM 5408 C SER C 88 33.524 -3.807 -21.510 1.00 28.17 C ANISOU 5408 C SER C 88 3794 3636 3274 528 202 235 C ATOM 5409 O SER C 88 34.193 -2.821 -21.819 1.00 30.05 O ANISOU 5409 O SER C 88 4047 3878 3494 531 202 246 O ATOM 5410 CB SER C 88 34.594 -4.495 -19.365 1.00 25.59 C ANISOU 5410 CB SER C 88 3416 3323 2983 527 245 261 C ATOM 5411 OG SER C 88 35.196 -5.581 -20.066 1.00 25.67 O ANISOU 5411 OG SER C 88 3444 3322 2987 527 267 258 O ATOM 5412 N PHE C 89 33.048 -4.667 -22.418 1.00 31.31 N ANISOU 5412 N PHE C 89 4210 4020 3666 527 197 218 N ATOM 5413 CA PHE C 89 33.362 -4.602 -23.853 1.00 33.68 C ANISOU 5413 CA PHE C 89 4548 4310 3938 529 195 211 C ATOM 5414 C PHE C 89 34.844 -4.767 -24.120 1.00 37.72 C ANISOU 5414 C PHE C 89 5073 4821 4436 531 227 228 C ATOM 5415 O PHE C 89 35.345 -4.307 -25.146 1.00 40.28 O ANISOU 5415 O PHE C 89 5429 5141 4736 533 227 229 O ATOM 5416 CB PHE C 89 32.870 -3.307 -24.513 1.00 30.77 C ANISOU 5416 CB PHE C 89 4199 3944 3550 531 164 207 C ATOM 5417 CG PHE C 89 31.398 -3.253 -24.669 1.00 40.72 C ANISOU 5417 CG PHE C 89 5456 5201 4816 529 131 186 C ATOM 5418 CD1 PHE C 89 30.580 -3.083 -23.566 1.00 34.77 C ANISOU 5418 CD1 PHE C 89 4669 4454 4085 527 117 184 C ATOM 5419 CD2 PHE C 89 30.819 -3.413 -25.923 1.00 46.47 C ANISOU 5419 CD2 PHE C 89 6213 5917 5527 530 112 169 C ATOM 5420 CE1 PHE C 89 29.219 -3.051 -23.709 1.00 45.56 C ANISOU 5420 CE1 PHE C 89 6033 5819 5459 526 86 165 C ATOM 5421 CE2 PHE C 89 29.452 -3.386 -26.076 1.00 43.40 C ANISOU 5421 CE2 PHE C 89 5820 5525 5144 528 81 149 C ATOM 5422 CZ PHE C 89 28.647 -3.208 -24.968 1.00 50.09 C ANISOU 5422 CZ PHE C 89 6636 6381 6015 526 68 147 C ATOM 5423 N ALA C 90 35.576 -5.421 -23.225 1.00 29.55 N ANISOU 5423 N ALA C 90 4018 3791 3419 530 256 241 N ATOM 5424 CA ALA C 90 37.010 -5.505 -23.405 1.00 22.11 C ANISOU 5424 CA ALA C 90 3086 2849 2465 532 287 257 C ATOM 5425 C ALA C 90 37.533 -6.929 -23.500 1.00 19.94 C ANISOU 5425 C ALA C 90 2813 2566 2199 531 315 256 C ATOM 5426 O ALA C 90 38.751 -7.106 -23.682 1.00 17.08 O ANISOU 5426 O ALA C 90 2460 2203 1827 532 342 270 O ATOM 5427 CB ALA C 90 37.718 -4.725 -22.282 1.00 21.14 C ANISOU 5427 CB ALA C 90 2941 2741 2351 533 299 278 C ATOM 5428 N THR C 91 36.663 -7.949 -23.458 1.00 11.28 N ANISOU 5428 N THR C 91 1708 1462 1117 528 309 241 N ATOM 5429 CA THR C 91 37.129 -9.340 -23.400 1.00 33.17 C ANISOU 5429 CA THR C 91 4477 4227 3899 526 336 240 C ATOM 5430 C THR C 91 36.464 -10.182 -24.483 1.00 27.68 C ANISOU 5430 C THR C 91 3803 3517 3197 525 326 219 C ATOM 5431 O THR C 91 35.401 -9.816 -24.999 1.00 20.52 O ANISOU 5431 O THR C 91 2905 2606 2284 524 296 204 O ATOM 5432 CB THR C 91 36.850 -9.991 -22.004 1.00 28.05 C ANISOU 5432 CB THR C 91 3790 3585 3283 524 345 244 C ATOM 5433 OG1 THR C 91 35.442 -10.187 -21.825 1.00 23.78 O ANISOU 5433 OG1 THR C 91 3237 3042 2755 521 319 226 O ATOM 5434 CG2 THR C 91 37.347 -9.092 -20.874 1.00 26.17 C ANISOU 5434 CG2 THR C 91 3529 3362 3054 526 351 263 C ATOM 5435 N CYS C 92 37.071 -11.354 -24.788 1.00 21.23 N ANISOU 5435 N CYS C 92 2994 2692 2381 524 351 219 N ATOM 5436 CA CYS C 92 36.457 -12.272 -25.759 1.00 21.45 C ANISOU 5436 CA CYS C 92 3041 2706 2404 522 344 199 C ATOM 5437 C CYS C 92 36.402 -13.750 -25.342 1.00 30.69 C ANISOU 5437 C CYS C 92 4196 3869 3594 520 363 194 C ATOM 5438 O CYS C 92 35.508 -14.482 -25.784 1.00 30.54 O ANISOU 5438 O CYS C 92 4182 3842 3581 517 351 176 O ATOM 5439 CB CYS C 92 37.164 -12.166 -27.127 1.00 19.56 C ANISOU 5439 CB CYS C 92 2839 2458 2135 525 351 198 C ATOM 5440 SG CYS C 92 38.925 -12.468 -27.106 1.00 29.51 S ANISOU 5440 SG CYS C 92 4107 3719 3387 527 392 220 S ATOM 5441 N VAL C 93 37.344 -14.221 -24.525 1.00 34.52 N ANISOU 5441 N VAL C 93 4663 4359 4092 520 394 210 N ATOM 5442 CA VAL C 93 37.375 -15.611 -24.062 1.00 27.72 C ANISOU 5442 CA VAL C 93 3788 3493 3251 518 414 207 C ATOM 5443 C VAL C 93 37.638 -15.599 -22.557 1.00 21.69 C ANISOU 5443 C VAL C 93 2989 2742 2513 518 428 222 C ATOM 5444 O VAL C 93 38.536 -14.891 -22.099 1.00 22.31 O ANISOU 5444 O VAL C 93 3060 2829 2586 520 440 241 O ATOM 5445 CB VAL C 93 38.454 -16.442 -24.790 1.00 23.83 C ANISOU 5445 CB VAL C 93 3316 2991 2747 519 443 211 C ATOM 5446 CG1 VAL C 93 38.505 -17.858 -24.247 1.00 19.19 C ANISOU 5446 CG1 VAL C 93 2712 2399 2181 517 464 209 C ATOM 5447 CG2 VAL C 93 38.206 -16.474 -26.279 1.00 23.50 C ANISOU 5447 CG2 VAL C 93 3311 2938 2681 520 430 197 C ATOM 5448 N LEU C 94 36.864 -16.377 -21.794 1.00 13.79 N ANISOU 5448 N LEU C 94 1963 1740 1537 515 425 214 N ATOM 5449 CA LEU C 94 36.957 -16.393 -20.322 1.00 23.53 C ANISOU 5449 CA LEU C 94 3161 2985 2795 514 436 227 C ATOM 5450 C LEU C 94 37.082 -17.828 -19.799 1.00 27.22 C ANISOU 5450 C LEU C 94 3613 3446 3283 512 459 226 C ATOM 5451 O LEU C 94 36.198 -18.655 -20.049 1.00 25.23 O ANISOU 5451 O LEU C 94 3362 3185 3040 509 449 208 O ATOM 5452 CB LEU C 94 35.719 -15.715 -19.708 1.00 17.01 C ANISOU 5452 CB LEU C 94 2316 2165 1981 512 405 219 C ATOM 5453 CG LEU C 94 35.334 -14.288 -20.194 1.00 24.07 C ANISOU 5453 CG LEU C 94 3223 3065 2857 514 376 217 C ATOM 5454 CD1 LEU C 94 33.931 -13.885 -19.787 1.00 18.19 C ANISOU 5454 CD1 LEU C 94 2463 2323 2125 511 344 204 C ATOM 5455 CD2 LEU C 94 36.301 -13.204 -19.772 1.00 15.52 C ANISOU 5455 CD2 LEU C 94 2138 1994 1766 517 385 238 C ATOM 5456 N VAL C 95 38.162 -18.131 -19.069 1.00 20.75 N ANISOU 5456 N VAL C 95 2781 2632 2472 514 489 244 N ATOM 5457 CA VAL C 95 38.348 -19.438 -18.433 1.00 11.12 C ANISOU 5457 CA VAL C 95 1544 1409 1273 512 512 245 C ATOM 5458 C VAL C 95 38.284 -19.284 -16.905 1.00 29.90 C ANISOU 5458 C VAL C 95 3886 3800 3676 512 517 256 C ATOM 5459 O VAL C 95 38.961 -18.427 -16.318 1.00 26.94 O ANISOU 5459 O VAL C 95 3502 3436 3299 515 524 274 O ATOM 5460 CB VAL C 95 39.662 -20.119 -18.856 1.00 22.50 C ANISOU 5460 CB VAL C 95 3000 2845 2705 515 545 255 C ATOM 5461 CG1 VAL C 95 39.982 -21.313 -17.900 1.00 12.59 C ANISOU 5461 CG1 VAL C 95 1721 1589 1474 514 572 261 C ATOM 5462 CG2 VAL C 95 39.560 -20.646 -20.298 1.00 31.65 C ANISOU 5462 CG2 VAL C 95 4192 3989 3844 514 542 240 C ATOM 5463 N SER C 96 37.473 -20.126 -16.265 1.00 25.62 N ANISOU 5463 N SER C 96 3323 3255 3157 509 515 247 N ATOM 5464 CA SER C 96 37.227 -20.083 -14.834 1.00 23.76 C ANISOU 5464 CA SER C 96 3053 3029 2947 508 518 255 C ATOM 5465 C SER C 96 37.359 -21.461 -14.220 1.00 25.97 C ANISOU 5465 C SER C 96 3317 3304 3248 506 541 256 C ATOM 5466 O SER C 96 36.958 -22.473 -14.808 1.00 29.21 O ANISOU 5466 O SER C 96 3737 3702 3659 504 542 241 O ATOM 5467 CB SER C 96 35.822 -19.534 -14.513 1.00 19.05 C ANISOU 5467 CB SER C 96 2443 2436 2359 504 484 242 C ATOM 5468 OG SER C 96 35.530 -19.697 -13.141 1.00 27.73 O ANISOU 5468 OG SER C 96 3507 3543 3484 503 488 248 O ATOM 5469 N GLU C 97 37.866 -21.481 -12.991 1.00 37.59 N ANISOU 5469 N GLU C 97 4761 4785 4735 507 558 272 N ATOM 5470 CA GLU C 97 37.937 -22.730 -12.246 1.00 35.17 C ANISOU 5470 CA GLU C 97 4436 4475 4451 506 579 273 C ATOM 5471 C GLU C 97 36.586 -23.421 -12.169 1.00 30.13 C ANISOU 5471 C GLU C 97 3790 3830 3830 501 562 253 C ATOM 5472 O GLU C 97 36.522 -24.657 -12.119 1.00 25.46 O ANISOU 5472 O GLU C 97 3195 3230 3250 499 577 247 O ATOM 5473 CB GLU C 97 38.457 -22.476 -10.837 1.00 35.76 C ANISOU 5473 CB GLU C 97 4481 4563 4544 507 594 292 C ATOM 5474 CG GLU C 97 39.213 -23.676 -10.277 1.00 51.13 C ANISOU 5474 CG GLU C 97 6417 6506 6504 508 627 300 C ATOM 5475 CD GLU C 97 38.409 -24.499 -9.294 1.00 57.85 C ANISOU 5475 CD GLU C 97 7241 7356 7383 505 627 294 C ATOM 5476 OE1 GLU C 97 37.222 -24.185 -9.042 1.00 58.90 O ANISOU 5476 OE1 GLU C 97 7364 7491 7526 501 602 282 O ATOM 5477 OE2 GLU C 97 38.973 -25.492 -8.798 1.00 63.70 O ANISOU 5477 OE2 GLU C 97 7974 8094 8136 502 648 300 O ATOM 5478 N GLU C 98 35.503 -22.644 -12.212 1.00 27.07 N ANISOU 5478 N GLU C 98 3398 3445 3442 498 531 242 N ATOM 5479 CA GLU C 98 34.147 -23.128 -11.994 1.00 23.26 C ANISOU 5479 CA GLU C 98 2904 2958 2976 494 511 224 C ATOM 5480 C GLU C 98 33.468 -23.704 -13.222 1.00 30.64 C ANISOU 5480 C GLU C 98 3863 3879 3901 491 498 202 C ATOM 5481 O GLU C 98 32.404 -24.304 -13.064 1.00 37.88 O ANISOU 5481 O GLU C 98 4770 4790 4832 487 486 187 O ATOM 5482 CB GLU C 98 33.258 -21.992 -11.482 1.00 22.58 C ANISOU 5482 CB GLU C 98 2803 2882 2895 492 482 221 C ATOM 5483 CG GLU C 98 33.755 -21.330 -10.185 1.00 40.00 C ANISOU 5483 CG GLU C 98 4983 5104 5113 494 491 241 C ATOM 5484 CD GLU C 98 33.880 -22.298 -9.025 1.00 48.30 C ANISOU 5484 CD GLU C 98 6006 6156 6190 493 513 248 C ATOM 5485 OE1 GLU C 98 32.924 -23.072 -8.819 1.00 54.19 O ANISOU 5485 OE1 GLU C 98 6742 6895 6952 489 506 233 O ATOM 5486 OE2 GLU C 98 34.927 -22.284 -8.331 1.00 44.19 O ANISOU 5486 OE2 GLU C 98 5474 5642 5673 496 537 267 O ATOM 5487 N ASP C 99 34.027 -23.538 -14.429 1.00 25.22 N ANISOU 5487 N ASP C 99 3207 3186 3189 493 500 201 N ATOM 5488 CA ASP C 99 33.327 -23.889 -15.662 1.00 23.82 C ANISOU 5488 CA ASP C 99 3055 2996 2999 491 483 180 C ATOM 5489 C ASP C 99 34.104 -24.915 -16.471 1.00 29.58 C ANISOU 5489 C ASP C 99 3806 3714 3719 492 507 179 C ATOM 5490 O ASP C 99 35.298 -24.734 -16.745 1.00 27.00 O ANISOU 5490 O ASP C 99 3491 3388 3378 496 527 193 O ATOM 5491 CB ASP C 99 33.058 -22.655 -16.512 1.00 25.23 C ANISOU 5491 CB ASP C 99 3255 3178 3156 493 457 175 C ATOM 5492 CG ASP C 99 31.987 -21.789 -15.921 1.00 34.86 C ANISOU 5492 CG ASP C 99 4455 4405 4384 491 428 170 C ATOM 5493 OD1 ASP C 99 30.839 -22.245 -15.923 1.00 41.09 O ANISOU 5493 OD1 ASP C 99 5238 5189 5185 487 411 152 O ATOM 5494 OD2 ASP C 99 32.273 -20.655 -15.483 1.00 36.02 O ANISOU 5494 OD2 ASP C 99 4596 4564 4527 493 422 183 O ATOM 5495 N LYS C 100 33.395 -25.967 -16.891 1.00 34.83 N ANISOU 5495 N LYS C 100 4475 4367 4391 489 504 161 N ATOM 5496 CA LYS C 100 34.049 -27.101 -17.533 1.00 33.47 C ANISOU 5496 CA LYS C 100 4320 4183 4214 489 528 159 C ATOM 5497 C LYS C 100 34.681 -26.696 -18.864 1.00 29.48 C ANISOU 5497 C LYS C 100 3850 3673 3679 492 527 159 C ATOM 5498 O LYS C 100 35.776 -27.158 -19.201 1.00 39.65 O ANISOU 5498 O LYS C 100 5150 4957 4958 495 553 168 O ATOM 5499 CB LYS C 100 33.056 -28.255 -17.694 1.00 35.56 C ANISOU 5499 CB LYS C 100 4581 4436 4493 484 522 139 C ATOM 5500 CG LYS C 100 33.673 -29.511 -18.311 1.00 45.34 C ANISOU 5500 CG LYS C 100 5836 5662 5728 485 547 136 C ATOM 5501 CD LYS C 100 32.664 -30.634 -18.497 1.00 55.42 C ANISOU 5501 CD LYS C 100 7110 6927 7019 480 541 116 C ATOM 5502 CE LYS C 100 33.325 -31.867 -19.118 1.00 64.37 C ANISOU 5502 CE LYS C 100 8261 8049 8149 480 566 114 C ATOM 5503 NZ LYS C 100 32.326 -32.920 -19.485 1.00 69.40 N ANISOU 5503 NZ LYS C 100 8899 8673 8796 475 558 92 N ATOM 5504 N HIS C 101 34.012 -25.859 -19.643 1.00 27.51 N ANISOU 5504 N HIS C 101 3616 3422 3413 492 499 148 N ATOM 5505 CA HIS C 101 34.598 -25.370 -20.884 1.00 30.84 C ANISOU 5505 CA HIS C 101 4071 3840 3806 495 497 148 C ATOM 5506 C HIS C 101 34.766 -23.854 -20.838 1.00 28.73 C ANISOU 5506 C HIS C 101 3807 3585 3525 498 481 158 C ATOM 5507 O HIS C 101 34.061 -23.165 -20.103 1.00 25.70 O ANISOU 5507 O HIS C 101 3403 3209 3152 497 462 158 O ATOM 5508 CB HIS C 101 33.746 -25.765 -22.081 1.00 39.51 C ANISOU 5508 CB HIS C 101 5194 4926 4893 493 478 125 C ATOM 5509 CG HIS C 101 33.534 -27.239 -22.189 1.00 44.37 C ANISOU 5509 CG HIS C 101 5808 5529 5522 490 492 114 C ATOM 5510 ND1 HIS C 101 34.505 -28.098 -22.666 1.00 46.54 N ANISOU 5510 ND1 HIS C 101 6097 5796 5789 491 520 119 N ATOM 5511 CD2 HIS C 101 32.467 -28.008 -21.875 1.00 40.16 C ANISOU 5511 CD2 HIS C 101 5260 4990 5008 485 482 98 C ATOM 5512 CE1 HIS C 101 34.044 -29.336 -22.637 1.00 43.89 C ANISOU 5512 CE1 HIS C 101 5757 5451 5469 488 526 107 C ATOM 5513 NE2 HIS C 101 32.810 -29.309 -22.164 1.00 46.92 N ANISOU 5513 NE2 HIS C 101 6122 5835 5868 484 504 94 N ATOM 5514 N ALA C 102 35.674 -23.344 -21.680 1.00 32.80 N ANISOU 5514 N ALA C 102 4348 4099 4016 501 488 166 N ATOM 5515 CA ALA C 102 35.878 -21.907 -21.831 1.00 22.81 C ANISOU 5515 CA ALA C 102 3090 2843 2734 504 474 174 C ATOM 5516 C ALA C 102 34.584 -21.223 -22.222 1.00 20.97 C ANISOU 5516 C ALA C 102 2862 2610 2497 502 436 157 C ATOM 5517 O ALA C 102 33.731 -21.810 -22.884 1.00 31.23 O ANISOU 5517 O ALA C 102 4172 3899 3795 500 422 138 O ATOM 5518 CB ALA C 102 36.909 -21.609 -22.919 1.00 12.98 C ANISOU 5518 CB ALA C 102 1876 1593 1460 508 485 181 C ATOM 5519 N ILE C 103 34.411 -19.991 -21.749 1.00 26.15 N ANISOU 5519 N ILE C 103 3507 3277 3150 503 420 165 N ATOM 5520 CA ILE C 103 33.239 -19.173 -22.077 1.00 34.06 C ANISOU 5520 CA ILE C 103 4513 4280 4147 502 383 151 C ATOM 5521 C ILE C 103 33.598 -18.179 -23.188 1.00 33.10 C ANISOU 5521 C ILE C 103 4424 4158 3996 506 371 152 C ATOM 5522 O ILE C 103 34.524 -17.365 -23.026 1.00 21.51 O ANISOU 5522 O ILE C 103 2958 2698 2517 509 382 169 O ATOM 5523 CB ILE C 103 32.737 -18.414 -20.842 1.00 36.84 C ANISOU 5523 CB ILE C 103 4834 4645 4517 502 370 158 C ATOM 5524 CG1 ILE C 103 32.326 -19.393 -19.726 1.00 40.92 C ANISOU 5524 CG1 ILE C 103 5320 5163 5065 498 381 156 C ATOM 5525 CG2 ILE C 103 31.597 -17.512 -21.272 1.00 24.51 C ANISOU 5525 CG2 ILE C 103 3280 3085 2949 501 333 143 C ATOM 5526 CD1 ILE C 103 31.212 -20.315 -20.077 1.00 48.03 C ANISOU 5526 CD1 ILE C 103 6222 6053 5975 494 368 134 C ATOM 5527 N ILE C 104 32.807 -18.170 -24.266 1.00 31.40 N ANISOU 5527 N ILE C 104 4231 3934 3767 505 348 133 N ATOM 5528 CA ILE C 104 33.039 -17.304 -25.422 1.00 27.97 C ANISOU 5528 CA ILE C 104 3827 3496 3302 508 336 131 C ATOM 5529 C ILE C 104 32.052 -16.143 -25.343 1.00 36.78 C ANISOU 5529 C ILE C 104 4939 4618 4416 508 301 125 C ATOM 5530 O ILE C 104 30.834 -16.360 -25.391 1.00 38.13 O ANISOU 5530 O ILE C 104 5106 4787 4597 505 277 107 O ATOM 5531 CB ILE C 104 32.856 -18.071 -26.747 1.00 29.54 C ANISOU 5531 CB ILE C 104 4057 3681 3487 507 334 115 C ATOM 5532 CG1 ILE C 104 33.606 -19.404 -26.736 1.00 22.27 C ANISOU 5532 CG1 ILE C 104 3136 2752 2573 506 366 118 C ATOM 5533 CG2 ILE C 104 33.275 -17.214 -27.949 1.00 26.72 C ANISOU 5533 CG2 ILE C 104 3734 3321 3098 510 325 115 C ATOM 5534 CD1 ILE C 104 35.056 -19.257 -26.513 1.00 33.74 C ANISOU 5534 CD1 ILE C 104 4591 4209 4018 509 396 140 C ATOM 5535 N VAL C 105 32.573 -14.913 -25.239 1.00 25.99 N ANISOU 5535 N VAL C 105 3577 3262 3037 511 297 139 N ATOM 5536 CA VAL C 105 31.732 -13.721 -25.124 1.00 29.81 C ANISOU 5536 CA VAL C 105 4056 3752 3517 511 265 134 C ATOM 5537 C VAL C 105 30.940 -13.482 -26.417 1.00 33.36 C ANISOU 5537 C VAL C 105 4534 4192 3947 511 237 115 C ATOM 5538 O VAL C 105 31.427 -13.728 -27.528 1.00 28.82 O ANISOU 5538 O VAL C 105 3990 3609 3352 513 244 112 O ATOM 5539 CB VAL C 105 32.602 -12.500 -24.761 1.00 34.49 C ANISOU 5539 CB VAL C 105 4648 4357 4100 515 270 155 C ATOM 5540 CG1 VAL C 105 31.771 -11.212 -24.725 1.00 28.18 C ANISOU 5540 CG1 VAL C 105 3846 3564 3295 515 237 151 C ATOM 5541 CG2 VAL C 105 33.320 -12.716 -23.422 1.00 21.85 C ANISOU 5541 CG2 VAL C 105 3016 2766 2520 514 296 174 C ATOM 5542 N GLU C 106 29.697 -13.018 -26.278 1.00 38.31 N ANISOU 5542 N GLU C 106 5153 4822 4581 510 205 102 N ATOM 5543 CA GLU C 106 28.844 -12.777 -27.435 1.00 40.90 C ANISOU 5543 CA GLU C 106 5506 5142 4893 510 177 82 C ATOM 5544 C GLU C 106 29.379 -11.643 -28.316 1.00 43.19 C ANISOU 5544 C GLU C 106 5825 5433 5153 515 169 89 C ATOM 5545 O GLU C 106 30.030 -10.717 -27.829 1.00 38.53 O ANISOU 5545 O GLU C 106 5228 4853 4558 517 174 106 O ATOM 5546 CB GLU C 106 27.415 -12.464 -26.991 1.00 34.44 C ANISOU 5546 CB GLU C 106 4670 4327 4090 508 145 67 C ATOM 5547 CG GLU C 106 27.260 -11.274 -26.085 1.00 57.19 C ANISOU 5547 CG GLU C 106 7530 7221 6977 509 132 78 C ATOM 5548 CD GLU C 106 25.833 -11.143 -25.560 1.00 76.53 C ANISOU 5548 CD GLU C 106 9959 9673 9444 507 103 63 C ATOM 5549 OE1 GLU C 106 24.992 -11.996 -25.917 1.00 83.16 O ANISOU 5549 OE1 GLU C 106 10801 10504 10292 504 94 44 O ATOM 5550 OE2 GLU C 106 25.566 -10.235 -24.740 1.00 82.14 O ANISOU 5550 OE2 GLU C 106 10651 10396 10164 507 91 70 O ATOM 5551 N PRO C 107 29.104 -11.699 -29.628 1.00 41.70 N ANISOU 5551 N PRO C 107 5668 5233 4942 516 155 75 N ATOM 5552 CA PRO C 107 29.785 -10.788 -30.572 1.00 36.07 C ANISOU 5552 CA PRO C 107 4986 4520 4200 519 153 82 C ATOM 5553 C PRO C 107 29.592 -9.316 -30.268 1.00 34.65 C ANISOU 5553 C PRO C 107 4801 4350 4012 522 132 89 C ATOM 5554 O PRO C 107 30.535 -8.537 -30.444 1.00 30.59 O ANISOU 5554 O PRO C 107 4300 3841 3482 525 142 105 O ATOM 5555 CB PRO C 107 29.171 -11.164 -31.930 1.00 31.51 C ANISOU 5555 CB PRO C 107 4439 3929 3605 520 136 61 C ATOM 5556 CG PRO C 107 28.707 -12.571 -31.761 1.00 34.60 C ANISOU 5556 CG PRO C 107 4818 4312 4015 516 144 48 C ATOM 5557 CD PRO C 107 28.263 -12.690 -30.320 1.00 34.29 C ANISOU 5557 CD PRO C 107 4740 4283 4007 513 145 52 C ATOM 5558 N GLU C 108 28.395 -8.894 -29.850 1.00 39.28 N ANISOU 5558 N GLU C 108 5372 4941 4611 521 103 78 N ATOM 5559 CA GLU C 108 28.181 -7.462 -29.623 1.00 50.44 C ANISOU 5559 CA GLU C 108 6784 6365 6018 523 82 84 C ATOM 5560 C GLU C 108 28.956 -6.904 -28.425 1.00 46.84 C ANISOU 5560 C GLU C 108 6302 5921 5572 524 100 107 C ATOM 5561 O GLU C 108 28.988 -5.680 -28.256 1.00 45.21 O ANISOU 5561 O GLU C 108 6097 5724 5358 526 86 115 O ATOM 5562 CB GLU C 108 26.688 -7.143 -29.465 1.00 63.29 C ANISOU 5562 CB GLU C 108 8399 7992 7655 522 46 66 C ATOM 5563 CG GLU C 108 25.980 -7.825 -28.300 1.00 84.24 C ANISOU 5563 CG GLU C 108 11016 10650 10341 518 47 62 C ATOM 5564 CD GLU C 108 25.480 -9.223 -28.634 1.00100.09 C ANISOU 5564 CD GLU C 108 13026 12646 12359 514 51 45 C ATOM 5565 OE1 GLU C 108 26.020 -9.845 -29.575 1.00104.88 O ANISOU 5565 OE1 GLU C 108 13657 13242 12950 515 65 42 O ATOM 5566 OE2 GLU C 108 24.541 -9.699 -27.957 1.00106.27 O ANISOU 5566 OE2 GLU C 108 13784 13430 13165 511 41 34 O ATOM 5567 N LYS C 109 29.596 -7.746 -27.608 1.00 45.65 N ANISOU 5567 N LYS C 109 6131 5773 5439 522 129 117 N ATOM 5568 CA LYS C 109 30.331 -7.280 -26.432 1.00 42.12 C ANISOU 5568 CA LYS C 109 5660 5339 5005 522 146 138 C ATOM 5569 C LYS C 109 31.822 -7.607 -26.488 1.00 40.09 C ANISOU 5569 C LYS C 109 5411 5082 4739 524 183 156 C ATOM 5570 O LYS C 109 32.542 -7.360 -25.506 1.00 27.52 O ANISOU 5570 O LYS C 109 3799 3500 3159 524 201 175 O ATOM 5571 CB LYS C 109 29.725 -7.879 -25.157 1.00 35.01 C ANISOU 5571 CB LYS C 109 4721 4443 4136 519 148 137 C ATOM 5572 CG LYS C 109 28.291 -7.448 -24.871 1.00 43.70 C ANISOU 5572 CG LYS C 109 5808 5547 5248 517 114 122 C ATOM 5573 CD LYS C 109 27.817 -8.027 -23.548 1.00 53.73 C ANISOU 5573 CD LYS C 109 7041 6823 6551 514 119 122 C ATOM 5574 CE LYS C 109 26.401 -7.583 -23.185 1.00 55.03 C ANISOU 5574 CE LYS C 109 7190 6991 6728 512 85 107 C ATOM 5575 NZ LYS C 109 26.333 -6.116 -23.035 1.00 56.71 N ANISOU 5575 NZ LYS C 109 7403 7214 6930 515 66 115 N ATOM 5576 N ARG C 110 32.319 -8.094 -27.626 1.00 31.16 N ANISOU 5576 N ARG C 110 4310 3939 3589 525 193 152 N ATOM 5577 CA ARG C 110 33.676 -8.615 -27.682 1.00 28.88 C ANISOU 5577 CA ARG C 110 4028 3649 3295 526 228 167 C ATOM 5578 C ARG C 110 34.725 -7.513 -27.690 1.00 35.74 C ANISOU 5578 C ARG C 110 4906 4526 4147 529 238 186 C ATOM 5579 O ARG C 110 34.575 -6.479 -28.349 1.00 42.04 O ANISOU 5579 O ARG C 110 5723 5325 4925 531 218 185 O ATOM 5580 CB ARG C 110 33.859 -9.505 -28.899 1.00 28.24 C ANISOU 5580 CB ARG C 110 3977 3555 3200 526 236 156 C ATOM 5581 CG ARG C 110 33.391 -10.896 -28.675 1.00 32.89 C ANISOU 5581 CG ARG C 110 4553 4137 3809 522 244 144 C ATOM 5582 CD ARG C 110 33.529 -11.745 -29.927 1.00 25.69 C ANISOU 5582 CD ARG C 110 3671 3210 2881 522 251 132 C ATOM 5583 NE ARG C 110 32.674 -12.929 -29.806 1.00 36.50 N ANISOU 5583 NE ARG C 110 5028 4571 4268 519 247 115 N ATOM 5584 CZ ARG C 110 32.480 -13.830 -30.765 1.00 45.22 C ANISOU 5584 CZ ARG C 110 6154 5662 5364 518 249 101 C ATOM 5585 NH1 ARG C 110 33.077 -13.702 -31.948 1.00 41.21 N ANISOU 5585 NH1 ARG C 110 5680 5147 4830 520 253 100 N ATOM 5586 NH2 ARG C 110 31.680 -14.865 -30.539 1.00 46.59 N ANISOU 5586 NH2 ARG C 110 6315 5830 5557 514 245 86 N ATOM 5587 N GLY C 111 35.809 -7.767 -26.966 1.00 34.57 N ANISOU 5587 N GLY C 111 4743 4384 4008 529 269 204 N ATOM 5588 CA GLY C 111 36.981 -6.920 -26.945 1.00 36.08 C ANISOU 5588 CA GLY C 111 4942 4582 4184 532 284 224 C ATOM 5589 C GLY C 111 38.214 -7.752 -27.203 1.00 33.92 C ANISOU 5589 C GLY C 111 4678 4304 3906 533 320 234 C ATOM 5590 O GLY C 111 38.091 -8.898 -27.655 1.00 39.33 O ANISOU 5590 O GLY C 111 5371 4979 4595 531 328 223 O ATOM 5591 N LYS C 112 39.403 -7.224 -26.918 1.00 21.60 N ANISOU 5591 N LYS C 112 3118 2751 2339 535 341 253 N ATOM 5592 CA LYS C 112 40.602 -7.866 -27.430 1.00 25.82 C ANISOU 5592 CA LYS C 112 3668 3279 2862 536 372 261 C ATOM 5593 C LYS C 112 41.342 -8.747 -26.421 1.00 23.99 C ANISOU 5593 C LYS C 112 3411 3051 2652 536 404 274 C ATOM 5594 O LYS C 112 42.375 -9.322 -26.784 1.00 30.01 O ANISOU 5594 O LYS C 112 4185 3809 3407 537 431 281 O ATOM 5595 CB LYS C 112 41.545 -6.801 -28.006 1.00 34.05 C ANISOU 5595 CB LYS C 112 4732 4324 3879 539 377 274 C ATOM 5596 CG LYS C 112 42.133 -5.792 -27.046 1.00 41.74 C ANISOU 5596 CG LYS C 112 5688 5313 4859 541 383 293 C ATOM 5597 CD LYS C 112 42.782 -4.630 -27.841 1.00 44.36 C ANISOU 5597 CD LYS C 112 6047 5646 5162 543 380 301 C ATOM 5598 CE LYS C 112 43.440 -3.595 -26.923 1.00 45.38 C ANISOU 5598 CE LYS C 112 6158 5789 5295 545 387 321 C ATOM 5599 NZ LYS C 112 43.783 -2.297 -27.591 1.00 46.94 N ANISOU 5599 NZ LYS C 112 6379 5989 5467 547 376 327 N ATOM 5600 N TYR C 113 40.811 -8.943 -25.208 1.00 20.57 N ANISOU 5600 N TYR C 113 2945 2626 2246 534 401 275 N ATOM 5601 CA TYR C 113 41.555 -9.620 -24.147 1.00 25.97 C ANISOU 5601 CA TYR C 113 3603 3315 2950 534 430 289 C ATOM 5602 C TYR C 113 40.961 -10.983 -23.780 1.00 20.56 C ANISOU 5602 C TYR C 113 2902 2624 2287 531 436 277 C ATOM 5603 O TYR C 113 39.753 -11.231 -23.917 1.00 20.07 O ANISOU 5603 O TYR C 113 2837 2557 2231 528 412 260 O ATOM 5604 CB TYR C 113 41.638 -8.719 -22.901 1.00 27.00 C ANISOU 5604 CB TYR C 113 3705 3462 3094 534 427 303 C ATOM 5605 CG TYR C 113 42.501 -7.476 -23.110 1.00 30.20 C ANISOU 5605 CG TYR C 113 4121 3873 3479 537 430 318 C ATOM 5606 CD1 TYR C 113 43.888 -7.561 -23.104 1.00 26.56 C ANISOU 5606 CD1 TYR C 113 3666 3414 3011 539 461 335 C ATOM 5607 CD2 TYR C 113 41.925 -6.217 -23.353 1.00 30.38 C ANISOU 5607 CD2 TYR C 113 4152 3901 3491 538 402 316 C ATOM 5608 CE1 TYR C 113 44.697 -6.421 -23.283 1.00 20.89 C ANISOU 5608 CE1 TYR C 113 2959 2703 2275 542 464 349 C ATOM 5609 CE2 TYR C 113 42.729 -5.068 -23.557 1.00 25.50 C ANISOU 5609 CE2 TYR C 113 3546 3290 2855 541 405 329 C ATOM 5610 CZ TYR C 113 44.117 -5.189 -23.525 1.00 30.41 C ANISOU 5610 CZ TYR C 113 4172 3913 3470 543 436 346 C ATOM 5611 OH TYR C 113 44.946 -4.097 -23.737 1.00 30.98 O ANISOU 5611 OH TYR C 113 4255 3991 3523 545 441 359 O ATOM 5612 N VAL C 114 41.851 -11.864 -23.327 1.00 17.36 N ANISOU 5612 N VAL C 114 2486 2217 1891 531 467 288 N ATOM 5613 CA VAL C 114 41.530 -13.182 -22.765 1.00 28.36 C ANISOU 5613 CA VAL C 114 3860 3606 3308 529 479 281 C ATOM 5614 C VAL C 114 41.843 -13.149 -21.267 1.00 20.41 C ANISOU 5614 C VAL C 114 2818 2612 2325 529 493 297 C ATOM 5615 O VAL C 114 42.905 -12.650 -20.876 1.00 33.23 O ANISOU 5615 O VAL C 114 4437 4243 3944 532 511 315 O ATOM 5616 CB VAL C 114 42.337 -14.309 -23.447 1.00 24.25 C ANISOU 5616 CB VAL C 114 3358 3075 2781 529 506 281 C ATOM 5617 CG1 VAL C 114 41.975 -15.676 -22.868 1.00 24.09 C ANISOU 5617 CG1 VAL C 114 3319 3050 2785 527 518 274 C ATOM 5618 CG2 VAL C 114 42.086 -14.336 -24.941 1.00 20.34 C ANISOU 5618 CG2 VAL C 114 2899 2568 2261 529 494 266 C ATOM 5619 N VAL C 115 40.933 -13.672 -20.433 1.00 18.95 N ANISOU 5619 N VAL C 115 2608 2428 2164 526 484 289 N ATOM 5620 CA VAL C 115 41.090 -13.673 -18.963 1.00 26.84 C ANISOU 5620 CA VAL C 115 3571 3439 3188 526 495 302 C ATOM 5621 C VAL C 115 40.928 -15.092 -18.395 1.00 24.09 C ANISOU 5621 C VAL C 115 3205 3085 2862 524 512 298 C ATOM 5622 O VAL C 115 39.867 -15.715 -18.543 1.00 17.64 O ANISOU 5622 O VAL C 115 2386 2261 2054 521 497 281 O ATOM 5623 CB VAL C 115 40.097 -12.718 -18.266 1.00 27.44 C ANISOU 5623 CB VAL C 115 3628 3525 3273 525 467 300 C ATOM 5624 CG1 VAL C 115 40.425 -12.614 -16.791 1.00 20.45 C ANISOU 5624 CG1 VAL C 115 2708 2651 2410 525 480 315 C ATOM 5625 CG2 VAL C 115 40.091 -11.294 -18.897 1.00 13.58 C ANISOU 5625 CG2 VAL C 115 1892 1774 1496 527 446 302 C ATOM 5626 N CYS C 116 41.939 -15.567 -17.670 1.00 16.79 N ANISOU 5626 N CYS C 116 2267 2166 1948 526 542 314 N ATOM 5627 CA CYS C 116 41.836 -16.815 -16.916 1.00 24.90 C ANISOU 5627 CA CYS C 116 3272 3189 2998 524 559 312 C ATOM 5628 C CYS C 116 41.740 -16.492 -15.425 1.00 26.12 C ANISOU 5628 C CYS C 116 3392 3358 3177 524 561 324 C ATOM 5629 O CYS C 116 42.569 -15.749 -14.894 1.00 24.49 O ANISOU 5629 O CYS C 116 3176 3161 2967 527 572 342 O ATOM 5630 CB CYS C 116 43.038 -17.730 -17.189 1.00 27.62 C ANISOU 5630 CB CYS C 116 3627 3528 3339 526 594 321 C ATOM 5631 SG CYS C 116 43.370 -18.092 -18.984 1.00 33.71 S ANISOU 5631 SG CYS C 116 4443 4285 4082 526 596 309 S ATOM 5632 N PHE C 117 40.734 -17.031 -14.740 1.00 24.80 N ANISOU 5632 N PHE C 117 3202 3189 3031 521 551 314 N ATOM 5633 CA PHE C 117 40.617 -16.636 -13.344 1.00 30.34 C ANISOU 5633 CA PHE C 117 3871 3904 3753 521 551 325 C ATOM 5634 C PHE C 117 40.046 -17.756 -12.478 1.00 28.66 C ANISOU 5634 C PHE C 117 3633 3688 3567 518 558 320 C ATOM 5635 O PHE C 117 39.326 -18.642 -12.948 1.00 28.26 O ANISOU 5635 O PHE C 117 3589 3626 3521 515 552 303 O ATOM 5636 CB PHE C 117 39.789 -15.340 -13.195 1.00 30.37 C ANISOU 5636 CB PHE C 117 3869 3915 3753 520 519 322 C ATOM 5637 CG PHE C 117 38.378 -15.435 -13.720 1.00 30.26 C ANISOU 5637 CG PHE C 117 3862 3894 3740 516 489 300 C ATOM 5638 CD1 PHE C 117 38.102 -15.231 -15.073 1.00 29.64 C ANISOU 5638 CD1 PHE C 117 3816 3807 3640 516 473 287 C ATOM 5639 CD2 PHE C 117 37.326 -15.729 -12.862 1.00 28.89 C ANISOU 5639 CD2 PHE C 117 3663 3724 3591 513 476 292 C ATOM 5640 CE1 PHE C 117 36.800 -15.308 -15.549 1.00 25.98 C ANISOU 5640 CE1 PHE C 117 3357 3337 3177 513 445 267 C ATOM 5641 CE2 PHE C 117 36.011 -15.821 -13.339 1.00 25.54 C ANISOU 5641 CE2 PHE C 117 3244 3293 3168 510 448 271 C ATOM 5642 CZ PHE C 117 35.750 -15.606 -14.676 1.00 22.18 C ANISOU 5642 CZ PHE C 117 2850 2859 2720 510 432 258 C ATOM 5643 N ASP C 118 40.396 -17.681 -11.186 1.00 18.31 N ANISOU 5643 N ASP C 118 2294 2388 2275 519 571 335 N ATOM 5644 CA ASP C 118 39.813 -18.449 -10.080 1.00 16.58 C ANISOU 5644 CA ASP C 118 2045 2170 2083 516 575 332 C ATOM 5645 C ASP C 118 39.060 -17.449 -9.221 1.00 16.67 C ANISOU 5645 C ASP C 118 2035 2194 2106 515 552 334 C ATOM 5646 O ASP C 118 39.685 -16.681 -8.471 1.00 18.32 O ANISOU 5646 O ASP C 118 2230 2415 2316 518 559 351 O ATOM 5647 CB ASP C 118 40.906 -19.151 -9.253 1.00 16.63 C ANISOU 5647 CB ASP C 118 2036 2180 2102 519 609 349 C ATOM 5648 CG ASP C 118 40.348 -20.174 -8.210 1.00 29.48 C ANISOU 5648 CG ASP C 118 3640 3803 3757 507 604 343 C ATOM 5649 OD1 ASP C 118 39.161 -20.141 -7.828 1.00 29.94 O ANISOU 5649 OD1 ASP C 118 3681 3865 3830 510 593 334 O ATOM 5650 OD2 ASP C 118 41.134 -21.043 -7.766 1.00 41.11 O ANISOU 5650 OD2 ASP C 118 5113 5268 5238 494 611 348 O ATOM 5651 N PRO C 119 37.733 -17.409 -9.295 1.00 12.26 N ANISOU 5651 N PRO C 119 1472 1633 1554 511 525 317 N ATOM 5652 CA PRO C 119 37.005 -16.324 -8.638 1.00 19.25 C ANISOU 5652 CA PRO C 119 2340 2528 2445 510 500 318 C ATOM 5653 C PRO C 119 37.065 -16.397 -7.112 1.00 22.67 C ANISOU 5653 C PRO C 119 2737 2972 2903 510 511 330 C ATOM 5654 O PRO C 119 37.014 -15.349 -6.457 1.00 23.44 O ANISOU 5654 O PRO C 119 2821 3082 3003 511 500 339 O ATOM 5655 CB PRO C 119 35.565 -16.507 -9.159 1.00 23.15 C ANISOU 5655 CB PRO C 119 2840 3015 2943 506 471 294 C ATOM 5656 CG PRO C 119 35.475 -17.985 -9.515 1.00 13.46 C ANISOU 5656 CG PRO C 119 1618 1774 1722 504 486 284 C ATOM 5657 CD PRO C 119 36.846 -18.378 -9.970 1.00 16.02 C ANISOU 5657 CD PRO C 119 1959 2096 2034 508 516 296 C ATOM 5658 N LEU C 120 37.163 -17.604 -6.519 1.00 26.76 N ANISOU 5658 N LEU C 120 3241 3486 3440 509 531 330 N ATOM 5659 CA LEU C 120 37.229 -17.748 -5.049 1.00 28.62 C ANISOU 5659 CA LEU C 120 3451 3727 3697 496 529 338 C ATOM 5660 C LEU C 120 38.076 -18.978 -4.711 1.00 28.47 C ANISOU 5660 C LEU C 120 3437 3698 3684 483 543 341 C ATOM 5661 O LEU C 120 37.570 -20.073 -4.420 1.00 24.43 O ANISOU 5661 O LEU C 120 2916 3178 3188 478 546 331 O ATOM 5662 CB LEU C 120 35.846 -17.842 -4.408 1.00 29.16 C ANISOU 5662 CB LEU C 120 3496 3798 3786 495 511 326 C ATOM 5663 CG LEU C 120 35.799 -17.545 -2.901 1.00 27.41 C ANISOU 5663 CG LEU C 120 3255 3582 3579 475 494 331 C ATOM 5664 CD1 LEU C 120 36.290 -16.143 -2.613 1.00 18.04 C ANISOU 5664 CD1 LEU C 120 2069 2405 2380 473 482 343 C ATOM 5665 CD2 LEU C 120 34.406 -17.724 -2.392 1.00 30.99 C ANISOU 5665 CD2 LEU C 120 3688 4037 4051 474 478 318 C ATOM 5666 N ASP C 121 39.393 -18.789 -4.770 1.00 33.35 N ANISOU 5666 N ASP C 121 4068 4314 4290 477 551 354 N ATOM 5667 CA ASP C 121 40.321 -19.867 -4.470 1.00 20.98 C ANISOU 5667 CA ASP C 121 2507 2737 2728 466 562 357 C ATOM 5668 C ASP C 121 40.358 -20.158 -2.965 1.00 31.91 C ANISOU 5668 C ASP C 121 3874 4121 4131 448 549 360 C ATOM 5669 O ASP C 121 40.486 -19.248 -2.135 1.00 24.35 O ANISOU 5669 O ASP C 121 2906 3170 3174 441 533 366 O ATOM 5670 CB ASP C 121 41.712 -19.504 -4.980 1.00 38.88 C ANISOU 5670 CB ASP C 121 4793 5001 4977 466 571 369 C ATOM 5671 CG ASP C 121 42.697 -20.644 -4.825 1.00 56.41 C ANISOU 5671 CG ASP C 121 7021 7211 7203 457 583 372 C ATOM 5672 OD1 ASP C 121 42.601 -21.613 -5.612 1.00 59.04 O ANISOU 5672 OD1 ASP C 121 7364 7535 7533 463 599 364 O ATOM 5673 OD2 ASP C 121 43.559 -20.575 -3.925 1.00 66.53 O ANISOU 5673 OD2 ASP C 121 8298 8491 8489 446 575 380 O ATOM 5674 N GLY C 122 40.336 -21.443 -2.622 1.00 37.93 N ANISOU 5674 N GLY C 122 4632 4874 4905 441 556 354 N ATOM 5675 CA GLY C 122 40.313 -21.872 -1.241 1.00 31.79 C ANISOU 5675 CA GLY C 122 3839 4095 4144 425 545 354 C ATOM 5676 C GLY C 122 38.940 -21.948 -0.611 1.00 28.13 C ANISOU 5676 C GLY C 122 3356 3636 3697 422 532 343 C ATOM 5677 O GLY C 122 38.849 -22.183 0.598 1.00 38.25 O ANISOU 5677 O GLY C 122 4626 4917 4990 409 521 342 O ATOM 5678 N SER C 123 37.866 -21.776 -1.389 1.00 35.90 N ANISOU 5678 N SER C 123 4337 4622 4680 435 533 333 N ATOM 5679 CA SER C 123 36.521 -21.690 -0.817 1.00 45.18 C ANISOU 5679 CA SER C 123 5493 5802 5871 433 518 322 C ATOM 5680 C SER C 123 36.000 -23.017 -0.281 1.00 54.61 C ANISOU 5680 C SER C 123 6677 6988 7083 425 521 312 C ATOM 5681 O SER C 123 34.932 -23.024 0.340 1.00 63.16 O ANISOU 5681 O SER C 123 7743 8073 8180 421 507 302 O ATOM 5682 CB SER C 123 35.521 -21.149 -1.842 1.00 41.63 C ANISOU 5682 CB SER C 123 5043 5357 5418 451 516 313 C ATOM 5683 OG SER C 123 35.428 -22.002 -2.968 1.00 46.51 O ANISOU 5683 OG SER C 123 5673 5965 6032 463 534 305 O ATOM 5684 N SER C 124 36.667 -24.141 -0.560 1.00 57.06 N ANISOU 5684 N SER C 124 6998 7289 7394 423 538 312 N ATOM 5685 CA SER C 124 36.206 -25.410 -0.006 1.00 64.15 C ANISOU 5685 CA SER C 124 7886 8178 8308 415 541 303 C ATOM 5686 C SER C 124 36.394 -25.459 1.509 1.00 71.46 C ANISOU 5686 C SER C 124 8802 9106 9243 398 527 307 C ATOM 5687 O SER C 124 35.595 -26.094 2.208 1.00 71.66 O ANISOU 5687 O SER C 124 8814 9130 9284 390 521 298 O ATOM 5688 CB SER C 124 36.916 -26.589 -0.678 1.00 61.67 C ANISOU 5688 CB SER C 124 7588 7853 7991 417 562 303 C ATOM 5689 OG SER C 124 38.307 -26.582 -0.417 1.00 65.63 O ANISOU 5689 OG SER C 124 8100 8352 8483 410 566 317 O ATOM 5690 N ASN C 125 37.424 -24.790 2.038 1.00 72.23 N ANISOU 5690 N ASN C 125 8906 9208 9332 391 521 320 N ATOM 5691 CA ASN C 125 37.640 -24.717 3.478 1.00 74.91 C ANISOU 5691 CA ASN C 125 9237 9548 9678 376 507 323 C ATOM 5692 C ASN C 125