HEADER MEMBRANE PROTEIN 09-NOV-20 7DFP TITLE HUMAN DOPAMINE D2 RECEPTOR IN COMPLEX WITH SPIPERONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: D(2) DOPAMINE RECEPTOR,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: DOPAMINE D2 RECEPTOR,CYTOCHROME B-562,CYTOCHROME B-562, COMPND 5 DOPAMINE D2 RECEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: CHIMERA PROTEIN OF RESIDUES 35-220 FROM D(2) DOPAMINE COMPND 9 RECEPTOR, RESIDUES 23-62 AND 88-128 FROM SOLUBLE CYTOCHROME B562, COMPND 10 RESIDUES 364-443 FROM D(2) DOPAMINE RECEPTOR.; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: FABL; COMPND 13 CHAIN: B; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: FABH; COMPND 16 CHAIN: C SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: DRD2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090 KEYWDS G-PROTEIN COUPLED RECEPTOR, DOPAMINE RECEPTOR, SPIPERONE, MEMBRANE KEYWDS 2 PROTEIN, ANTIPSYCHOTIC, SCHIZOPHRENIA EXPDTA X-RAY DIFFRACTION AUTHOR D.IM,T.SHIMAMURA,S.IWATA REVDAT 2 13-JAN-21 7DFP 1 JRNL REVDAT 1 30-DEC-20 7DFP 0 JRNL AUTH D.IM,A.INOUE,T.FUJIWARA,T.NAKANE,Y.YAMANAKA,T.UEMURA,C.MORI, JRNL AUTH 2 Y.SHIIMURA,K.T.KIMURA,H.ASADA,N.NOMURA,T.TANAKA,A.YAMASHITA, JRNL AUTH 3 E.NANGO,K.TONO,F.M.N.KADJI,J.AOKI,S.IWATA,T.SHIMAMURA JRNL TITL STRUCTURE OF THE DOPAMINE D 2 RECEPTOR IN COMPLEX WITH THE JRNL TITL 2 ANTIPSYCHOTIC DRUG SPIPERONE. JRNL REF NAT COMMUN V. 11 6442 2020 JRNL REFN ESSN 2041-1723 JRNL PMID 33353947 JRNL DOI 10.1038/S41467-020-20221-0 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.16_3549 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.12 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 18048 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.020 REMARK 3 FREE R VALUE TEST SET COUNT : 1087 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 43.1200 - 6.1900 0.99 2222 144 0.1811 0.2258 REMARK 3 2 6.1900 - 4.9200 1.00 2142 136 0.1837 0.2203 REMARK 3 3 4.9200 - 4.3000 1.00 2139 134 0.1493 0.1782 REMARK 3 4 4.3000 - 3.9100 1.00 2100 143 0.1662 0.1967 REMARK 3 5 3.9100 - 3.6300 1.00 2088 128 0.1943 0.2021 REMARK 3 6 3.6300 - 3.4100 1.00 2087 136 0.2052 0.2328 REMARK 3 7 3.4100 - 3.2400 1.00 2119 137 0.2184 0.2353 REMARK 3 8 3.2400 - 3.1000 1.00 2064 129 0.2655 0.3190 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) : 0.317 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.648 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 73.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.39 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 : 0.002 6054 REMARK 3 ANGLE : 0.567 8265 REMARK 3 CHIRALITY : 0.041 979 REMARK 3 PLANARITY : 0.005 1029 REMARK 3 DIHEDRAL : 13.232 3600 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 35 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -95.1003 -19.7508 223.0478 REMARK 3 T TENSOR REMARK 3 T11: 1.3470 T22: 1.4418 REMARK 3 T33: 0.5033 T12: -0.0224 REMARK 3 T13: 0.0054 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 2.4069 L22: 1.5016 REMARK 3 L33: 6.4700 L12: -0.3243 REMARK 3 L13: 1.6094 L23: 0.2257 REMARK 3 S TENSOR REMARK 3 S11: 0.1058 S12: -0.6415 S13: 0.1974 REMARK 3 S21: 0.2535 S22: -0.2969 S23: 0.1503 REMARK 3 S31: 0.0386 S32: -0.9388 S33: 0.1397 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'A' AND (RESID 215 THROUGH 216 )) OR (CHAIN REMARK 3 'A' AND (RESID 1003 THROUGH 1083)) REMARK 3 ORIGIN FOR THE GROUP (A): -71.5140 0.8357 264.5368 REMARK 3 T TENSOR REMARK 3 T11: 0.8743 T22: 1.2316 REMARK 3 T33: 0.7317 T12: 0.1153 REMARK 3 T13: -0.0797 T23: -0.0898 REMARK 3 L TENSOR REMARK 3 L11: 8.9139 L22: 7.8762 REMARK 3 L33: 5.5337 L12: 1.9050 REMARK 3 L13: 5.0326 L23: 1.5154 REMARK 3 S TENSOR REMARK 3 S11: -0.2329 S12: -0.6387 S13: 0.9192 REMARK 3 S21: 0.3778 S22: 0.0526 S23: 0.7448 REMARK 3 S31: -0.1146 S32: -1.1465 S33: 0.2334 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND (RESID 1084 THROUGH 1106 )) OR (CHAIN REMARK 3 'A' AND (RESID 364 THROUGH 442 )) REMARK 3 ORIGIN FOR THE GROUP (A): -83.9017 -19.2150 233.7401 REMARK 3 T TENSOR REMARK 3 T11: 1.3891 T22: 1.6222 REMARK 3 T33: 0.7176 T12: 0.0271 REMARK 3 T13: -0.1603 T23: -0.0359 REMARK 3 L TENSOR REMARK 3 L11: 1.4614 L22: 2.4834 REMARK 3 L33: 4.6051 L12: 0.4991 REMARK 3 L13: 2.7963 L23: 3.0313 REMARK 3 S TENSOR REMARK 3 S11: 0.1307 S12: -0.3511 S13: 0.1584 REMARK 3 S21: 0.3791 S22: 0.2092 S23: -0.0590 REMARK 3 S31: 0.1668 S32: 0.9264 S33: -0.3325 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A):-112.4895 -20.8513 171.9207 REMARK 3 T TENSOR REMARK 3 T11: 0.6517 T22: 0.9251 REMARK 3 T33: 0.6829 T12: 0.0410 REMARK 3 T13: 0.0561 T23: -0.0842 REMARK 3 L TENSOR REMARK 3 L11: 6.1004 L22: 3.8834 REMARK 3 L33: 5.1021 L12: -1.7774 REMARK 3 L13: 2.1850 L23: -4.5605 REMARK 3 S TENSOR REMARK 3 S11: -0.3097 S12: -0.5014 S13: -0.4695 REMARK 3 S21: 0.0138 S22: 0.9292 S23: 1.1651 REMARK 3 S31: -0.2285 S32: -2.3768 S33: -0.6661 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A):-106.5582 -18.5224 172.9086 REMARK 3 T TENSOR REMARK 3 T11: 0.5163 T22: 0.5884 REMARK 3 T33: 0.6259 T12: 0.1664 REMARK 3 T13: 0.0400 T23: 0.0393 REMARK 3 L TENSOR REMARK 3 L11: 2.5082 L22: 1.5492 REMARK 3 L33: 4.3436 L12: -0.0007 REMARK 3 L13: -0.1782 L23: 0.4816 REMARK 3 S TENSOR REMARK 3 S11: -0.1395 S12: -0.8453 S13: 0.0653 REMARK 3 S21: 0.5419 S22: 0.0826 S23: 0.2905 REMARK 3 S31: -0.3008 S32: -0.8400 S33: 0.0049 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): -99.8032 -31.3434 145.5676 REMARK 3 T TENSOR REMARK 3 T11: 0.2951 T22: 0.2464 REMARK 3 T33: 0.5438 T12: -0.0330 REMARK 3 T13: -0.0603 T23: 0.0933 REMARK 3 L TENSOR REMARK 3 L11: 5.9681 L22: 8.5144 REMARK 3 L33: 3.9353 L12: -5.2736 REMARK 3 L13: -3.4716 L23: 4.9531 REMARK 3 S TENSOR REMARK 3 S11: -0.2320 S12: -0.2057 S13: -0.1875 REMARK 3 S21: 0.0911 S22: 0.1600 S23: 0.4196 REMARK 3 S31: 0.0910 S32: 0.1128 S33: 0.0047 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -83.1780 -21.1960 178.2062 REMARK 3 T TENSOR REMARK 3 T11: 0.8509 T22: 0.6417 REMARK 3 T33: 0.5152 T12: 0.0051 REMARK 3 T13: -0.1687 T23: 0.0539 REMARK 3 L TENSOR REMARK 3 L11: 9.4628 L22: 6.1782 REMARK 3 L33: 4.4919 L12: -5.1338 REMARK 3 L13: -4.9720 L23: 5.2739 REMARK 3 S TENSOR REMARK 3 S11: -0.1264 S12: -0.9791 S13: 0.9206 REMARK 3 S21: -0.4774 S22: 0.3837 S23: -1.3641 REMARK 3 S31: -0.9130 S32: 0.7240 S33: -0.1699 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 18 THROUGH 40 ) REMARK 3 ORIGIN FOR THE GROUP (A): -88.9716 -17.7077 186.9957 REMARK 3 T TENSOR REMARK 3 T11: 0.8019 T22: 0.6946 REMARK 3 T33: 0.4413 T12: 0.0994 REMARK 3 T13: -0.1128 T23: -0.1562 REMARK 3 L TENSOR REMARK 3 L11: 6.9414 L22: 5.8051 REMARK 3 L33: 4.6399 L12: 2.1909 REMARK 3 L13: -2.0486 L23: -1.8823 REMARK 3 S TENSOR REMARK 3 S11: 0.0675 S12: -1.5171 S13: 0.9849 REMARK 3 S21: 1.0120 S22: -0.1193 S23: -0.1680 REMARK 3 S31: -1.5109 S32: 0.3630 S33: 0.0699 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -92.0257 -26.7865 188.9424 REMARK 3 T TENSOR REMARK 3 T11: 0.8574 T22: 0.9089 REMARK 3 T33: 0.3383 T12: 0.2329 REMARK 3 T13: -0.0315 T23: 0.0888 REMARK 3 L TENSOR REMARK 3 L11: 5.7695 L22: 6.7049 REMARK 3 L33: 6.4545 L12: 2.3582 REMARK 3 L13: 1.5501 L23: 2.8864 REMARK 3 S TENSOR REMARK 3 S11: 0.0525 S12: -1.0149 S13: -0.1565 REMARK 3 S21: 0.4383 S22: -0.2828 S23: 0.3704 REMARK 3 S31: -0.1963 S32: -1.0530 S33: 0.2347 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 74 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): -84.1542 -26.8733 183.8684 REMARK 3 T TENSOR REMARK 3 T11: 0.7965 T22: 0.8115 REMARK 3 T33: 0.3953 T12: -0.0076 REMARK 3 T13: -0.1983 T23: 0.0828 REMARK 3 L TENSOR REMARK 3 L11: 2.6792 L22: 8.9135 REMARK 3 L33: 6.7127 L12: 0.0888 REMARK 3 L13: 0.5281 L23: 5.9961 REMARK 3 S TENSOR REMARK 3 S11: -0.4166 S12: -1.0132 S13: -0.0753 REMARK 3 S21: 0.1212 S22: 0.4297 S23: -0.0186 REMARK 3 S31: 0.2135 S32: 0.5609 S33: 0.0669 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 92 THROUGH 131 ) REMARK 3 ORIGIN FOR THE GROUP (A): -89.8695 -21.7694 174.5619 REMARK 3 T TENSOR REMARK 3 T11: 0.4701 T22: 0.3936 REMARK 3 T33: 0.5475 T12: 0.0845 REMARK 3 T13: -0.1181 T23: 0.0726 REMARK 3 L TENSOR REMARK 3 L11: 1.8888 L22: 2.2700 REMARK 3 L33: 3.8259 L12: -0.2829 REMARK 3 L13: -2.0284 L23: 1.2950 REMARK 3 S TENSOR REMARK 3 S11: -0.3701 S12: -0.5289 S13: -0.0639 REMARK 3 S21: 0.6448 S22: 0.1805 S23: -0.0651 REMARK 3 S31: 0.3787 S32: 0.2396 S33: 0.1934 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 132 THROUGH 152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -91.2682 -23.8537 140.9602 REMARK 3 T TENSOR REMARK 3 T11: 0.3469 T22: 0.3099 REMARK 3 T33: 0.5962 T12: -0.0432 REMARK 3 T13: -0.1174 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 3.4884 L22: 8.8605 REMARK 3 L33: 6.0166 L12: -1.8905 REMARK 3 L13: -3.0238 L23: -1.1011 REMARK 3 S TENSOR REMARK 3 S11: 0.5477 S12: 0.5876 S13: -0.2917 REMARK 3 S21: -1.4283 S22: -0.2239 S23: 0.8198 REMARK 3 S31: 1.4901 S32: -0.9992 S33: -0.4467 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): -83.2738 -19.1516 154.5300 REMARK 3 T TENSOR REMARK 3 T11: 0.2268 T22: 0.2875 REMARK 3 T33: 0.4473 T12: -0.0205 REMARK 3 T13: 0.0100 T23: -0.1348 REMARK 3 L TENSOR REMARK 3 L11: 3.5138 L22: 9.2706 REMARK 3 L33: 9.5330 L12: -5.4011 REMARK 3 L13: 5.7532 L23: -8.8494 REMARK 3 S TENSOR REMARK 3 S11: 0.3430 S12: 0.0205 S13: 0.3222 REMARK 3 S21: 0.1721 S22: -0.0631 S23: 0.9578 REMARK 3 S31: -0.0320 S32: -0.2061 S33: -0.3630 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 165 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -85.9469 -20.1629 147.3745 REMARK 3 T TENSOR REMARK 3 T11: 0.2464 T22: 0.1450 REMARK 3 T33: 0.5492 T12: 0.0481 REMARK 3 T13: -0.0312 T23: -0.0676 REMARK 3 L TENSOR REMARK 3 L11: 2.9980 L22: 2.0936 REMARK 3 L33: 7.4294 L12: -0.5932 REMARK 3 L13: 1.7422 L23: -2.9345 REMARK 3 S TENSOR REMARK 3 S11: 0.0868 S12: -0.0683 S13: 0.0284 REMARK 3 S21: -0.1959 S22: 0.0386 S23: 0.1501 REMARK 3 S31: -0.0340 S32: 0.1235 S33: -0.1503 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7DFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-20. REMARK 100 THE DEPOSITION ID IS D_1300019286. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-FEB-17 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : BL3 REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.77 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MPCCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL 0.6.2 REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL 0.6.2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18069 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 43.120 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 99.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: D3R (PDB ID: 3PBL) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.0, 0.1M LITHIUM REMARK 280 ACETATE DIHYDRATE, 30% (V/V) POLYETHYLENE GLYCOL 400, 5% (V/V) REMARK 280 DIMETHYL SULFOXIDE, 0.01M ADENOSINE TRIPHOSPHATE, 1MM SPIPERONE, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.95000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.25000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.95000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.25000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 34 REMARK 465 LEU A 141 REMARK 465 TYR A 142 REMARK 465 ASN A 143 REMARK 465 THR A 144 REMARK 465 ARG A 145 REMARK 465 TYR A 146 REMARK 465 SER A 147 REMARK 465 ARG A 217 REMARK 465 ARG A 218 REMARK 465 ARG A 219 REMARK 465 ARG A 220 REMARK 465 ALA A 1001 REMARK 465 ASP A 1002 REMARK 465 GLY A 1063 REMARK 465 SER A 1064 REMARK 465 GLY A 1065 REMARK 465 CYS A 443 REMARK 465 GLY A 444 REMARK 465 GLU A 445 REMARK 465 ASN A 446 REMARK 465 LEU A 447 REMARK 465 TYR A 448 REMARK 465 PHE A 449 REMARK 465 GLN A 450 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 63 CG CD CE NZ REMARK 470 LYS A 121 CG CD CE NZ REMARK 470 LEU A 125 CG CD1 CD2 REMARK 470 LYS A 149 CD CE NZ REMARK 470 ARG A 150 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1027 CD CE NZ REMARK 470 GLU A1081 CG CD OE1 OE2 REMARK 470 LYS A1104 CG CD CE NZ REMARK 470 TYR A1105 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 367 CG CD CE NZ REMARK 470 LYS A 370 CG CD CE NZ REMARK 470 PHE A 433 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 435 CG CD CE NZ REMARK 470 LYS A 439 CG CD CE NZ REMARK 470 ARG B 24 CZ NH1 NH2 REMARK 470 LYS B 45 CD CE NZ REMARK 470 LYS B 169 CD CE NZ 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 101 32.12 -97.32 REMARK 500 THR B 51 -10.78 72.66 REMARK 500 SER C 120 32.01 -97.49 REMARK 500 SER C 156 72.85 64.07 REMARK 500 SER C 163 19.22 57.60 REMARK 500 SER C 169 34.00 -97.43 REMARK 500 GLN C 178 118.49 -160.05 REMARK 500 REMARK 500 REMARK: NULL DBREF 7DFP A 35 220 UNP P14416 DRD2_HUMAN 35 220 DBREF 7DFP A 1001 1040 UNP P0ABE7 C562_ECOLX 23 62 DBREF 7DFP A 1066 1106 UNP P0ABE7 C562_ECOLX 88 128 DBREF 7DFP A 364 443 UNP P14416 DRD2_HUMAN 364 443 DBREF 7DFP B 1 215 PDB 7DFP 7DFP 1 215 DBREF 7DFP C 1 220 PDB 7DFP 7DFP 1 220 SEQADV 7DFP MET A 34 UNP P14416 INITIATING METHIONINE SEQADV 7DFP LYS A 121 UNP P14416 SER 121 ENGINEERED MUTATION SEQADV 7DFP TRP A 123 UNP P14416 LEU 123 ENGINEERED MUTATION SEQADV 7DFP TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 7DFP GLY A 1041 UNP P0ABE7 LINKER SEQADV 7DFP SER A 1042 UNP P0ABE7 LINKER SEQADV 7DFP GLY A 1063 UNP P0ABE7 LINKER SEQADV 7DFP SER A 1064 UNP P0ABE7 LINKER SEQADV 7DFP GLY A 1065 UNP P0ABE7 LINKER SEQADV 7DFP ILE A 1098 UNP P0ABE7 ARG 120 ENGINEERED MUTATION SEQADV 7DFP ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 7DFP GLY A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 7DFP GLY A 444 UNP P14416 EXPRESSION TAG SEQADV 7DFP GLU A 445 UNP P14416 EXPRESSION TAG SEQADV 7DFP ASN A 446 UNP P14416 EXPRESSION TAG SEQADV 7DFP LEU A 447 UNP P14416 EXPRESSION TAG SEQADV 7DFP TYR A 448 UNP P14416 EXPRESSION TAG SEQADV 7DFP PHE A 449 UNP P14416 EXPRESSION TAG SEQADV 7DFP GLN A 450 UNP P14416 EXPRESSION TAG SEQRES 1 A 360 MET ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA SEQRES 2 A 360 VAL ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SEQRES 3 A 360 SER ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU SEQRES 4 A 360 ILE VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR SEQRES 5 A 360 LEU VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY SEQRES 6 A 360 GLU TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL SEQRES 7 A 360 THR LEU ASP VAL MET MET CYS THR ALA LYS ILE TRP ASN SEQRES 8 A 360 LEU CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA SEQRES 9 A 360 MET PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG SEQRES 10 A 360 ARG VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER SEQRES 11 A 360 PHE THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN SEQRES 12 A 360 ALA ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE SEQRES 13 A 360 VAL VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE SEQRES 14 A 360 ILE VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL SEQRES 15 A 360 LEU ARG ARG ARG ARG ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 16 A 360 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 17 A 360 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 18 A 360 ALA ALA ALA LEU ASP ALA GLY SER GLY SER GLY ASP ILE SEQRES 19 A 360 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 20 A 360 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 21 A 360 LEU LYS THR THR ILE ASN ALA TYR ILE GLN LYS TYR GLY SEQRES 22 A 360 SER GLN GLN LYS GLU LYS LYS ALA THR GLN MET LEU ALA SEQRES 23 A 360 ILE VAL LEU GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE SEQRES 24 A 360 PHE ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN SEQRES 25 A 360 ILE PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY SEQRES 26 A 360 TYR VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR SEQRES 27 A 360 PHE ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU SEQRES 28 A 360 HIS CYS GLY GLU ASN LEU TYR PHE GLN SEQRES 1 B 215 ASP ILE VAL MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 B 215 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 B 215 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 215 PRO ASP GLY THR VAL LYS LEU LEU LEU TYR TYR THR SER SEQRES 5 B 215 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 B 215 GLU PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 B 215 SER LYS LEU PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 215 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 215 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 215 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 215 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 215 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 215 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 215 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 215 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 215 PHE ASN ARG ASN GLU CYS ASN SEQRES 1 C 220 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 C 220 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 C 220 TYR SER PHE THR GLY TYR ASN MET ASN TRP VAL LYS GLN SEQRES 4 C 220 SER ARG GLY LYS SER LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 C 220 PRO PHE TYR GLY THR THR ASN TYR ASN GLN ARG PHE LYS SEQRES 6 C 220 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 C 220 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 C 220 ALA VAL TYR TYR CYS ALA ARG ARG TYR LEU THR GLY THR SEQRES 9 C 220 GLY ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 C 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 C 220 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL SEQRES 12 C 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER SEQRES 13 C 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER SEQRES 14 C 220 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR SEQRES 15 C 220 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 C 220 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA SEQRES 17 C 220 SER SER THR THR VAL ASP LYS LYS LEU GLU PRO SER HET SIP A1201 29 HETNAM SIP 8-[4-(4-FLUOROPHENYL)-4-OXIDANYLIDENE-BUTYL]-1-PHENYL- HETNAM 2 SIP 1,3,8-TRIAZASPIRO[4.5]DECAN-4-ONE HETSYN SIP SPIPERONE FORMUL 4 SIP C23 H26 F N3 O2 HELIX 1 AA1 ASN A 35 GLU A 62 1 28 HELIX 2 AA2 LYS A 63 GLN A 66 5 4 HELIX 3 AA3 THR A 67 VAL A 87 1 21 HELIX 4 AA4 VAL A 87 GLY A 98 1 12 HELIX 5 AA5 SER A 103 MET A 138 1 36 HELIX 6 AA6 LYS A 149 PHE A 172 1 24 HELIX 7 AA7 ASN A 186 PHE A 198 1 13 HELIX 8 AA8 PHE A 198 VAL A 215 1 18 HELIX 9 AA9 GLU A 1004 ALA A 1020 1 17 HELIX 10 AB1 ALA A 1023 LEU A 1038 1 16 HELIX 11 AB2 ILE A 1067 GLU A 1081 1 15 HELIX 12 AB3 LYS A 1083 ASP A 400 1 61 HELIX 13 AB4 PRO A 404 ASN A 430 1 27 HELIX 14 AB5 ASN A 430 LEU A 441 1 12 HELIX 15 AB6 GLU B 79 ILE B 83 5 5 HELIX 16 AB7 SER B 121 THR B 126 1 6 HELIX 17 AB8 LYS B 183 GLU B 187 1 5 HELIX 18 AB9 ASN B 212 CYS B 214 5 3 HELIX 19 AC1 THR C 87 SER C 91 5 5 HELIX 20 AC2 SER C 163 SER C 165 5 3 HELIX 21 AC3 SER C 193 TRP C 195 5 3 SHEET 1 AA1 4 MET B 4 THR B 5 0 SHEET 2 AA1 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA1 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA1 4 PHE B 62 SER B 67 -1 N SER B 65 O SER B 72 SHEET 1 AA2 6 SER B 10 ALA B 13 0 SHEET 2 AA2 6 THR B 102 ILE B 106 1 O GLU B 105 N ALA B 13 SHEET 3 AA2 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA2 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AA2 6 VAL B 44 TYR B 49 -1 O LYS B 45 N GLN B 37 SHEET 6 AA2 6 ARG B 53 LEU B 54 -1 O ARG B 53 N TYR B 49 SHEET 1 AA3 4 SER B 10 ALA B 13 0 SHEET 2 AA3 4 THR B 102 ILE B 106 1 O GLU B 105 N ALA B 13 SHEET 3 AA3 4 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA3 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AA4 4 THR B 114 PHE B 118 0 SHEET 2 AA4 4 GLY B 129 PHE B 139 -1 O ASN B 137 N THR B 114 SHEET 3 AA4 4 TYR B 173 THR B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 AA4 4 VAL B 159 TRP B 163 -1 N LEU B 160 O THR B 178 SHEET 1 AA5 4 SER B 153 ARG B 155 0 SHEET 2 AA5 4 ILE B 144 ILE B 150 -1 N ILE B 150 O SER B 153 SHEET 3 AA5 4 SER B 191 HIS B 198 -1 O GLU B 195 N LYS B 147 SHEET 4 AA5 4 ILE B 205 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 AA6 4 GLN C 3 GLN C 6 0 SHEET 2 AA6 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AA6 4 THR C 78 LEU C 83 -1 O ALA C 79 N CYS C 22 SHEET 4 AA6 4 ALA C 68 ASP C 73 -1 N THR C 71 O TYR C 80 SHEET 1 AA7 6 GLU C 10 VAL C 12 0 SHEET 2 AA7 6 THR C 114 VAL C 118 1 O SER C 115 N GLU C 10 SHEET 3 AA7 6 ALA C 92 ARG C 99 -1 N ALA C 92 O VAL C 116 SHEET 4 AA7 6 MET C 34 GLN C 39 -1 N GLN C 39 O VAL C 93 SHEET 5 AA7 6 LEU C 45 ILE C 51 -1 O GLU C 46 N LYS C 38 SHEET 6 AA7 6 THR C 58 TYR C 60 -1 O ASN C 59 N TYR C 50 SHEET 1 AA8 4 GLU C 10 VAL C 12 0 SHEET 2 AA8 4 THR C 114 VAL C 118 1 O SER C 115 N GLU C 10 SHEET 3 AA8 4 ALA C 92 ARG C 99 -1 N ALA C 92 O VAL C 116 SHEET 4 AA8 4 MET C 107 TRP C 110 -1 O TYR C 109 N ARG C 98 SHEET 1 AA9 4 SER C 127 LEU C 131 0 SHEET 2 AA9 4 SER C 142 TYR C 152 -1 O LEU C 148 N TYR C 129 SHEET 3 AA9 4 LEU C 181 PRO C 191 -1 O TYR C 182 N TYR C 152 SHEET 4 AA9 4 HIS C 171 GLN C 178 -1 N PHE C 173 O SER C 185 SHEET 1 AB1 3 THR C 158 TRP C 161 0 SHEET 2 AB1 3 THR C 201 HIS C 206 -1 O SER C 203 N THR C 160 SHEET 3 AB1 3 THR C 211 LYS C 216 -1 O THR C 211 N HIS C 206 SSBOND 1 CYS A 107 CYS A 182 1555 1555 2.03 SSBOND 2 CYS A 399 CYS A 401 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 5 CYS B 214 CYS C 135 1555 1555 2.03 SSBOND 6 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 7 CYS C 147 CYS C 202 1555 1555 2.03 CISPEP 1 LEU B 94 PRO B 95 0 0.55 CISPEP 2 TYR B 140 PRO B 141 0 0.08 CISPEP 3 PHE C 153 PRO C 154 0 -0.75 CISPEP 4 TRP C 195 PRO C 196 0 7.92 CRYST1 161.900 40.500 165.900 90.00 116.50 90.00 C 1 2 1 4 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 0.006177 0.000000 0.003080 0.00000 SCALE2 0.000000 0.024691 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006735 0.00000 ATOM 1 N ASN A 35 -92.907 -39.908 207.170 1.00128.34 N ANISOU 1 N ASN A 35 24003 15373 9387 270 -2339 248 N ATOM 2 CA ASN A 35 -92.942 -41.359 207.308 1.00135.39 C ANISOU 2 CA ASN A 35 25568 15759 10115 165 -2634 244 C ATOM 3 C ASN A 35 -91.860 -41.859 208.260 1.00145.91 C ANISOU 3 C ASN A 35 27191 16872 11377 413 -2697 343 C ATOM 4 O ASN A 35 -92.111 -42.704 209.116 1.00144.24 O ANISOU 4 O ASN A 35 27391 16339 11075 98 -2858 449 O ATOM 5 CB ASN A 35 -92.779 -42.028 205.940 1.00135.58 C ANISOU 5 CB ASN A 35 25938 15553 10022 494 -2829 59 C ATOM 6 CG ASN A 35 -94.025 -41.916 205.082 1.00138.49 C ANISOU 6 CG ASN A 35 26191 16021 10409 142 -2865 -36 C ATOM 7 OD1 ASN A 35 -94.297 -40.869 204.495 1.00139.66 O ANISOU 7 OD1 ASN A 35 25828 16572 10664 210 -2671 -79 O ATOM 8 ND2 ASN A 35 -94.787 -43.001 205.002 1.00140.27 N ANISOU 8 ND2 ASN A 35 26906 15872 10517 -244 -3131 -65 N ATOM 9 N TYR A 36 -90.647 -41.332 208.090 1.00158.42 N ANISOU 9 N TYR A 36 28555 18651 12986 973 -2578 315 N ATOM 10 CA TYR A 36 -89.549 -41.625 209.012 1.00171.66 C ANISOU 10 CA TYR A 36 30391 20230 14603 1255 -2610 405 C ATOM 11 C TYR A 36 -89.679 -40.846 210.322 1.00184.90 C ANISOU 11 C TYR A 36 31698 22162 16394 934 -2416 571 C ATOM 12 O TYR A 36 -89.948 -41.421 211.380 1.00188.85 O ANISOU 12 O TYR A 36 32478 22445 16831 614 -2511 697 O ATOM 13 CB TYR A 36 -88.214 -41.317 208.324 1.00169.57 C ANISOU 13 CB TYR A 36 29962 20165 14302 1952 -2548 310 C ATOM 14 CG TYR A 36 -87.009 -41.997 208.935 1.00171.16 C ANISOU 14 CG TYR A 36 30473 20195 14367 2383 -2681 340 C ATOM 15 CD1 TYR A 36 -86.620 -43.265 208.521 1.00174.55 C ANISOU 15 CD1 TYR A 36 31532 20196 14594 2730 -2974 236 C ATOM 16 CD2 TYR A 36 -86.250 -41.365 209.912 1.00170.54 C ANISOU 16 CD2 TYR A 36 30066 20386 14346 2470 -2531 458 C ATOM 17 CE1 TYR A 36 -85.515 -43.887 209.070 1.00177.77 C ANISOU 17 CE1 TYR A 36 32227 20460 14858 3183 -3113 252 C ATOM 18 CE2 TYR A 36 -85.143 -41.980 210.466 1.00172.89 C ANISOU 18 CE2 TYR A 36 30621 20566 14504 2889 -2664 480 C ATOM 19 CZ TYR A 36 -84.781 -43.241 210.042 1.00175.90 C ANISOU 19 CZ TYR A 36 31614 20533 14687 3260 -2952 378 C ATOM 20 OH TYR A 36 -83.681 -43.861 210.589 1.00176.52 O ANISOU 20 OH TYR A 36 31875 20500 14694 3704 -3070 378 O ATOM 21 N TYR A 37 -89.486 -39.527 210.259 1.00195.40 N ANISOU 21 N TYR A 37 32421 23946 17875 1013 -2151 574 N ATOM 22 CA TYR A 37 -89.655 -38.646 211.413 1.00195.35 C ANISOU 22 CA TYR A 37 32033 24210 17980 731 -1959 696 C ATOM 23 C TYR A 37 -91.096 -38.551 211.913 1.00188.13 C ANISOU 23 C TYR A 37 31043 23334 17103 107 -1923 749 C ATOM 24 O TYR A 37 -91.316 -38.045 213.018 1.00188.63 O ANISOU 24 O TYR A 37 30886 23577 17209 -154 -1800 849 O ATOM 25 CB TYR A 37 -89.139 -37.248 211.063 1.00196.93 C ANISOU 25 CB TYR A 37 31657 24844 18324 969 -1717 667 C ATOM 26 CG TYR A 37 -87.885 -37.240 210.213 1.00201.89 C ANISOU 26 CG TYR A 37 32264 25542 18902 1548 -1726 596 C ATOM 27 CD1 TYR A 37 -86.627 -37.312 210.795 1.00204.40 C ANISOU 27 CD1 TYR A 37 32581 25920 19163 1882 -1733 646 C ATOM 28 CD2 TYR A 37 -87.963 -37.162 208.827 1.00203.56 C ANISOU 28 CD2 TYR A 37 32437 25808 19100 1764 -1728 478 C ATOM 29 CE1 TYR A 37 -85.478 -37.305 210.021 1.00206.72 C ANISOU 29 CE1 TYR A 37 32803 26359 19381 2412 -1732 579 C ATOM 30 CE2 TYR A 37 -86.821 -37.157 208.045 1.00205.84 C ANISOU 30 CE2 TYR A 37 32678 26224 19309 2292 -1721 415 C ATOM 31 CZ TYR A 37 -85.582 -37.228 208.648 1.00207.02 C ANISOU 31 CZ TYR A 37 32795 26465 19396 2612 -1718 466 C ATOM 32 OH TYR A 37 -84.442 -37.224 207.878 1.00206.92 O ANISOU 32 OH TYR A 37 32686 26657 19277 3137 -1702 402 O ATOM 33 N ALA A 38 -92.073 -38.991 211.121 1.00176.15 N ANISOU 33 N ALA A 38 29672 21700 15557 -129 -2023 674 N ATOM 34 CA ALA A 38 -93.474 -39.032 211.544 1.00170.14 C ANISOU 34 CA ALA A 38 28838 21014 14794 -740 -2010 720 C ATOM 35 C ALA A 38 -93.694 -39.592 212.953 1.00174.56 C ANISOU 35 C ALA A 38 29620 21447 15258 -1133 -2060 886 C ATOM 36 O ALA A 38 -94.082 -38.859 213.876 1.00168.85 O ANISOU 36 O ALA A 38 28535 21037 14585 -1384 -1881 960 O ATOM 37 CB ALA A 38 -94.283 -39.843 210.531 1.00166.60 C ANISOU 37 CB ALA A 38 28692 20341 14267 -926 -2204 626 C ATOM 38 N THR A 39 -93.360 -40.870 213.166 1.00176.61 N ANISOU 38 N THR A 39 30496 21245 15363 -1146 -2307 948 N ATOM 39 CA THR A 39 -93.513 -41.430 214.507 1.00187.42 C ANISOU 39 CA THR A 39 32120 22474 16617 -1516 -2366 1132 C ATOM 40 C THR A 39 -92.551 -40.820 215.516 1.00192.18 C ANISOU 40 C THR A 39 32507 23258 17255 -1250 -2225 1213 C ATOM 41 O THR A 39 -92.904 -40.689 216.696 1.00196.04 O ANISOU 41 O THR A 39 32909 23880 17697 -1604 -2146 1350 O ATOM 42 CB THR A 39 -93.324 -42.947 214.452 1.00196.17 C ANISOU 42 CB THR A 39 34011 22985 17540 -1556 -2698 1184 C ATOM 43 OG1 THR A 39 -94.247 -43.509 213.510 1.00199.09 O ANISOU 43 OG1 THR A 39 34594 23181 17871 -1846 -2848 1098 O ATOM 44 CG2 THR A 39 -93.572 -43.568 215.814 1.00202.16 C ANISOU 44 CG2 THR A 39 35078 23580 18154 -2001 -2774 1404 C ATOM 45 N LEU A 40 -91.366 -40.393 215.088 1.00190.04 N ANISOU 45 N LEU A 40 32108 23045 17053 -654 -2181 1131 N ATOM 46 CA LEU A 40 -90.387 -39.955 216.074 1.00186.19 C ANISOU 46 CA LEU A 40 31471 22700 16572 -419 -2092 1211 C ATOM 47 C LEU A 40 -90.850 -38.652 216.714 1.00181.11 C ANISOU 47 C LEU A 40 30231 22527 16057 -655 -1821 1229 C ATOM 48 O LEU A 40 -90.892 -38.516 217.948 1.00186.79 O ANISOU 48 O LEU A 40 30899 23347 16726 -875 -1764 1345 O ATOM 49 CB LEU A 40 -89.008 -39.795 215.431 1.00183.23 C ANISOU 49 CB LEU A 40 31056 22343 16222 249 -2109 1118 C ATOM 50 CG LEU A 40 -88.599 -40.839 214.389 1.00182.23 C ANISOU 50 CG LEU A 40 31408 21846 15985 606 -2344 1019 C ATOM 51 CD1 LEU A 40 -87.397 -40.363 213.587 1.00178.40 C ANISOU 51 CD1 LEU A 40 30679 21569 15535 1240 -2279 903 C ATOM 52 CD2 LEU A 40 -88.309 -42.178 215.050 1.00186.42 C ANISOU 52 CD2 LEU A 40 32613 21901 16318 616 -2622 1115 C ATOM 53 N LEU A 41 -91.199 -37.672 215.884 1.00168.96 N ANISOU 53 N LEU A 41 28254 21274 14668 -591 -1661 1109 N ATOM 54 CA LEU A 41 -91.787 -36.476 216.452 1.00155.26 C ANISOU 54 CA LEU A 41 26012 19944 13037 -817 -1435 1106 C ATOM 55 C LEU A 41 -93.159 -36.719 217.074 1.00150.53 C ANISOU 55 C LEU A 41 25404 19429 12360 -1398 -1417 1165 C ATOM 56 O LEU A 41 -93.556 -35.932 217.938 1.00149.02 O ANISOU 56 O LEU A 41 24875 19556 12191 -1587 -1254 1187 O ATOM 57 CB LEU A 41 -91.888 -35.412 215.359 1.00148.39 C ANISOU 57 CB LEU A 41 24736 19319 12328 -605 -1300 970 C ATOM 58 CG LEU A 41 -90.653 -35.324 214.456 1.00143.18 C ANISOU 58 CG LEU A 41 24103 18592 11708 -74 -1330 912 C ATOM 59 CD1 LEU A 41 -90.771 -34.172 213.499 1.00137.24 C ANISOU 59 CD1 LEU A 41 22944 18102 11098 81 -1183 815 C ATOM 60 CD2 LEU A 41 -89.382 -35.170 215.285 1.00143.86 C ANISOU 60 CD2 LEU A 41 24173 18712 11774 188 -1314 982 C ATOM 61 N THR A 42 -93.909 -37.766 216.683 1.00148.15 N ANISOU 61 N THR A 42 25455 18883 11954 -1700 -1582 1188 N ATOM 62 CA THR A 42 -95.105 -38.070 217.470 1.00139.00 C ANISOU 62 CA THR A 42 24288 17847 10680 -2303 -1566 1284 C ATOM 63 C THR A 42 -94.736 -38.399 218.914 1.00137.31 C ANISOU 63 C THR A 42 24252 17585 10336 -2458 -1572 1454 C ATOM 64 O THR A 42 -95.412 -37.977 219.866 1.00138.62 O ANISOU 64 O THR A 42 24150 18076 10442 -2806 -1431 1516 O ATOM 65 CB THR A 42 -95.877 -39.228 216.836 1.00137.13 C ANISOU 65 CB THR A 42 24457 17316 10332 -2647 -1776 1300 C ATOM 66 OG1 THR A 42 -96.147 -38.931 215.460 1.00137.40 O ANISOU 66 OG1 THR A 42 24337 17393 10474 -2460 -1783 1133 O ATOM 67 CG2 THR A 42 -97.192 -39.459 217.567 1.00134.70 C ANISOU 67 CG2 THR A 42 24056 17231 9895 -3327 -1739 1403 C ATOM 68 N LEU A 43 -93.616 -39.111 219.083 1.00135.05 N ANISOU 68 N LEU A 43 24400 16926 9988 -2153 -1734 1521 N ATOM 69 CA LEU A 43 -93.113 -39.443 220.413 1.00134.70 C ANISOU 69 CA LEU A 43 24559 16810 9809 -2223 -1765 1685 C ATOM 70 C LEU A 43 -92.680 -38.197 221.166 1.00128.04 C ANISOU 70 C LEU A 43 23215 16377 9056 -2047 -1540 1654 C ATOM 71 O LEU A 43 -92.930 -38.068 222.371 1.00124.47 O ANISOU 71 O LEU A 43 22692 16103 8497 -2319 -1465 1762 O ATOM 72 CB LEU A 43 -91.963 -40.448 220.327 1.00136.81 C ANISOU 72 CB LEU A 43 25395 16600 9987 -1845 -2009 1739 C ATOM 73 CG LEU A 43 -92.173 -41.701 219.476 1.00138.94 C ANISOU 73 CG LEU A 43 26249 16377 10164 -1893 -2278 1735 C ATOM 74 CD1 LEU A 43 -90.872 -42.471 219.311 1.00141.72 C ANISOU 74 CD1 LEU A 43 27084 16323 10440 -1343 -2501 1733 C ATOM 75 CD2 LEU A 43 -93.253 -42.587 220.081 1.00141.11 C ANISOU 75 CD2 LEU A 43 26882 16475 10259 -2576 -2393 1906 C ATOM 76 N LEU A 44 -92.028 -37.270 220.463 1.00125.90 N ANISOU 76 N LEU A 44 22609 16260 8966 -1608 -1439 1508 N ATOM 77 CA LEU A 44 -91.676 -35.997 221.088 1.00124.08 C ANISOU 77 CA LEU A 44 21912 16402 8833 -1473 -1240 1461 C ATOM 78 C LEU A 44 -92.911 -35.217 221.533 1.00125.46 C ANISOU 78 C LEU A 44 21692 16960 9016 -1854 -1056 1423 C ATOM 79 O LEU A 44 -92.923 -34.639 222.627 1.00129.88 O ANISOU 79 O LEU A 44 22049 17769 9530 -1950 -943 1450 O ATOM 80 CB LEU A 44 -90.835 -35.157 220.126 1.00117.97 C ANISOU 80 CB LEU A 44 20874 15709 8241 -998 -1178 1327 C ATOM 81 CG LEU A 44 -90.600 -33.702 220.538 1.00115.06 C ANISOU 81 CG LEU A 44 20019 15703 7997 -895 -984 1255 C ATOM 82 CD1 LEU A 44 -89.686 -33.627 221.753 1.00115.88 C ANISOU 82 CD1 LEU A 44 20156 15848 8026 -804 -994 1336 C ATOM 83 CD2 LEU A 44 -90.031 -32.895 219.382 1.00113.09 C ANISOU 83 CD2 LEU A 44 19526 15526 7917 -535 -926 1140 C ATOM 84 N ILE A 45 -93.948 -35.169 220.693 1.00119.60 N ANISOU 84 N ILE A 45 20824 16300 8318 -2045 -1030 1344 N ATOM 85 CA ILE A 45 -95.192 -34.502 221.078 1.00113.73 C ANISOU 85 CA ILE A 45 19694 15966 7552 -2383 -869 1295 C ATOM 86 C ILE A 45 -95.751 -35.106 222.361 1.00115.20 C ANISOU 86 C ILE A 45 20009 16243 7517 -2840 -868 1448 C ATOM 87 O ILE A 45 -96.137 -34.389 223.296 1.00116.42 O ANISOU 87 O ILE A 45 19850 16770 7617 -2964 -711 1433 O ATOM 88 CB ILE A 45 -96.219 -34.572 219.933 1.00114.43 C ANISOU 88 CB ILE A 45 19673 16117 7688 -2529 -885 1200 C ATOM 89 CG1 ILE A 45 -95.729 -33.780 218.720 1.00113.32 C ANISOU 89 CG1 ILE A 45 19345 15961 7749 -2078 -854 1051 C ATOM 90 CG2 ILE A 45 -97.574 -34.054 220.397 1.00114.15 C ANISOU 90 CG2 ILE A 45 19246 16548 7580 -2898 -739 1157 C ATOM 91 CD1 ILE A 45 -96.709 -33.765 217.565 1.00114.16 C ANISOU 91 CD1 ILE A 45 19326 16151 7897 -2177 -874 948 C ATOM 92 N ALA A 46 -95.806 -36.441 222.420 1.00120.65 N ANISOU 92 N ALA A 46 21191 16590 8061 -3099 -1053 1600 N ATOM 93 CA ALA A 46 -96.342 -37.098 223.610 1.00124.41 C ANISOU 93 CA ALA A 46 21840 17130 8299 -3586 -1066 1784 C ATOM 94 C ALA A 46 -95.494 -36.813 224.846 1.00127.37 C ANISOU 94 C ALA A 46 22231 17560 8603 -3428 -1016 1863 C ATOM 95 O ALA A 46 -96.032 -36.584 225.938 1.00124.68 O ANISOU 95 O ALA A 46 21716 17548 8107 -3733 -896 1931 O ATOM 96 CB ALA A 46 -96.451 -38.604 223.371 1.00125.05 C ANISOU 96 CB ALA A 46 22535 16742 8237 -3876 -1314 1944 C ATOM 97 N VAL A 47 -94.167 -36.817 224.692 1.00132.34 N ANISOU 97 N VAL A 47 23046 17911 9325 -2949 -1108 1849 N ATOM 98 CA VAL A 47 -93.278 -36.511 225.812 1.00136.70 C ANISOU 98 CA VAL A 47 23595 18531 9816 -2766 -1080 1909 C ATOM 99 C VAL A 47 -93.529 -35.101 226.333 1.00138.67 C ANISOU 99 C VAL A 47 23283 19269 10137 -2717 -846 1774 C ATOM 100 O VAL A 47 -93.621 -34.874 227.548 1.00139.13 O ANISOU 100 O VAL A 47 23257 19559 10047 -2876 -768 1835 O ATOM 101 CB VAL A 47 -91.808 -36.705 225.395 1.00135.57 C ANISOU 101 CB VAL A 47 23677 18068 9764 -2229 -1221 1891 C ATOM 102 CG1 VAL A 47 -90.875 -36.028 226.388 1.00133.70 C ANISOU 102 CG1 VAL A 47 23271 18015 9516 -1987 -1160 1892 C ATOM 103 CG2 VAL A 47 -91.481 -38.186 225.280 1.00138.83 C ANISOU 103 CG2 VAL A 47 24732 17986 10031 -2253 -1481 2043 C ATOM 104 N ILE A 48 -93.627 -34.130 225.421 1.00137.53 N ANISOU 104 N ILE A 48 22778 19272 10205 -2478 -745 1585 N ATOM 105 CA ILE A 48 -93.894 -32.748 225.817 1.00135.88 C ANISOU 105 CA ILE A 48 22085 19475 10069 -2397 -552 1435 C ATOM 106 C ILE A 48 -95.201 -32.656 226.595 1.00136.13 C ANISOU 106 C ILE A 48 21910 19890 9922 -2826 -425 1446 C ATOM 107 O ILE A 48 -95.267 -32.044 227.673 1.00136.98 O ANISOU 107 O ILE A 48 21822 20296 9929 -2863 -314 1421 O ATOM 108 CB ILE A 48 -93.911 -31.828 224.583 1.00135.32 C ANISOU 108 CB ILE A 48 21730 19450 10236 -2107 -494 1253 C ATOM 109 CG1 ILE A 48 -92.547 -31.818 223.896 1.00136.49 C ANISOU 109 CG1 ILE A 48 22022 19310 10530 -1684 -592 1247 C ATOM 110 CG2 ILE A 48 -94.288 -30.416 224.982 1.00134.96 C ANISOU 110 CG2 ILE A 48 21246 19783 10248 -2027 -323 1093 C ATOM 111 CD1 ILE A 48 -92.525 -31.047 222.594 1.00136.48 C ANISOU 111 CD1 ILE A 48 21799 19324 10735 -1427 -549 1106 C ATOM 112 N VAL A 49 -96.268 -33.243 226.041 1.00135.84 N ANISOU 112 N VAL A 49 21893 19890 9828 -3155 -441 1474 N ATOM 113 CA VAL A 49 -97.575 -33.182 226.692 1.00130.79 C ANISOU 113 CA VAL A 49 21001 19695 8997 -3585 -313 1484 C ATOM 114 C VAL A 49 -97.503 -33.766 228.098 1.00135.85 C ANISOU 114 C VAL A 49 21839 20403 9374 -3885 -313 1673 C ATOM 115 O VAL A 49 -97.969 -33.155 229.070 1.00134.30 O ANISOU 115 O VAL A 49 21345 20647 9034 -3992 -157 1631 O ATOM 116 CB VAL A 49 -98.635 -33.899 225.837 1.00121.18 C ANISOU 116 CB VAL A 49 19820 18478 7744 -3940 -369 1513 C ATOM 117 CG1 VAL A 49 -99.917 -34.098 226.632 1.00121.38 C ANISOU 117 CG1 VAL A 49 19628 18980 7509 -4472 -257 1580 C ATOM 118 CG2 VAL A 49 -98.910 -33.112 224.565 1.00117.11 C ANISOU 118 CG2 VAL A 49 19008 18033 7455 -3650 -332 1303 C ATOM 119 N PHE A 50 -96.908 -34.957 228.227 1.00139.91 N ANISOU 119 N PHE A 50 22879 20480 9802 -3999 -498 1879 N ATOM 120 CA PHE A 50 -96.828 -35.607 229.532 1.00148.42 C ANISOU 120 CA PHE A 50 24124 21531 10736 -4233 -516 2058 C ATOM 121 C PHE A 50 -96.058 -34.749 230.527 1.00147.33 C ANISOU 121 C PHE A 50 23792 21568 10620 -3911 -424 1988 C ATOM 122 O PHE A 50 -96.518 -34.520 231.652 1.00152.52 O ANISOU 122 O PHE A 50 24240 22562 11150 -4096 -301 2008 O ATOM 123 CB PHE A 50 -96.192 -36.992 229.403 1.00153.10 C ANISOU 123 CB PHE A 50 25327 21535 11310 -4285 -763 2258 C ATOM 124 CG PHE A 50 -95.992 -37.692 230.723 1.00158.51 C ANISOU 124 CG PHE A 50 26233 22136 11856 -4481 -809 2451 C ATOM 125 CD1 PHE A 50 -94.801 -37.568 231.422 1.00157.56 C ANISOU 125 CD1 PHE A 50 26227 21873 11766 -4104 -861 2472 C ATOM 126 CD2 PHE A 50 -97.006 -38.460 231.271 1.00165.31 C ANISOU 126 CD2 PHE A 50 27174 23093 12543 -5061 -804 2615 C ATOM 127 CE1 PHE A 50 -94.623 -38.206 232.636 1.00161.72 C ANISOU 127 CE1 PHE A 50 26961 22333 12151 -4268 -910 2649 C ATOM 128 CE2 PHE A 50 -96.834 -39.100 232.486 1.00169.31 C ANISOU 128 CE2 PHE A 50 27896 23523 12912 -5250 -848 2801 C ATOM 129 CZ PHE A 50 -95.641 -38.972 233.168 1.00167.10 C ANISOU 129 CZ PHE A 50 27745 23083 12664 -4837 -902 2816 C ATOM 130 N GLY A 51 -94.867 -34.286 230.136 1.00146.48 N ANISOU 130 N GLY A 51 23755 21244 10656 -3440 -491 1906 N ATOM 131 CA GLY A 51 -94.052 -33.499 231.048 1.00138.33 C ANISOU 131 CA GLY A 51 22571 20354 9634 -3158 -436 1842 C ATOM 132 C GLY A 51 -94.746 -32.238 231.526 1.00135.78 C ANISOU 132 C GLY A 51 21763 20547 9280 -3170 -225 1657 C ATOM 133 O GLY A 51 -94.709 -31.908 232.718 1.00129.41 O ANISOU 133 O GLY A 51 20831 19969 8371 -3188 -151 1650 O ATOM 134 N ASN A 52 -95.407 -31.521 230.613 1.00135.30 N ANISOU 134 N ASN A 52 21436 20681 9292 -3136 -137 1493 N ATOM 135 CA ASN A 52 -96.030 -30.266 231.022 1.00141.81 C ANISOU 135 CA ASN A 52 21810 21972 10098 -3059 42 1283 C ATOM 136 C ASN A 52 -97.274 -30.505 231.872 1.00147.44 C ANISOU 136 C ASN A 52 22312 23098 10609 -3434 171 1316 C ATOM 137 O ASN A 52 -97.523 -29.761 232.831 1.00143.20 O ANISOU 137 O ASN A 52 21513 22915 9983 -3372 294 1202 O ATOM 138 CB ASN A 52 -96.353 -29.412 229.798 1.00139.71 C ANISOU 138 CB ASN A 52 21272 21725 10085 -2808 84 1077 C ATOM 139 CG ASN A 52 -95.109 -28.827 229.160 1.00134.96 C ANISOU 139 CG ASN A 52 20737 20797 9745 -2377 1 1002 C ATOM 140 OD1 ASN A 52 -94.407 -28.019 229.770 1.00126.69 O ANISOU 140 OD1 ASN A 52 19613 19797 8725 -2158 17 918 O ATOM 141 ND2 ASN A 52 -94.824 -29.236 227.933 1.00137.85 N ANISOU 141 ND2 ASN A 52 21242 20850 10285 -2270 -92 1033 N ATOM 142 N VAL A 53 -98.077 -31.522 231.539 1.00154.97 N ANISOU 142 N VAL A 53 23369 24025 11487 -3828 141 1462 N ATOM 143 CA VAL A 53 -99.201 -31.870 232.406 1.00153.68 C ANISOU 143 CA VAL A 53 23006 24262 11122 -4239 256 1530 C ATOM 144 C VAL A 53 -98.701 -32.246 233.797 1.00152.34 C ANISOU 144 C VAL A 53 22995 24052 10834 -4304 246 1669 C ATOM 145 O VAL A 53 -99.315 -31.894 234.815 1.00157.09 O ANISOU 145 O VAL A 53 23317 25089 11282 -4420 388 1626 O ATOM 146 CB VAL A 53 -100.038 -32.999 231.775 1.00157.51 C ANISOU 146 CB VAL A 53 23637 24671 11538 -4713 187 1693 C ATOM 147 CG1 VAL A 53 -101.079 -33.510 232.759 1.00160.84 C ANISOU 147 CG1 VAL A 53 23894 25484 11734 -5207 284 1814 C ATOM 148 CG2 VAL A 53 -100.714 -32.507 230.505 1.00157.85 C ANISOU 148 CG2 VAL A 53 23434 24885 11657 -4658 220 1527 C ATOM 149 N LEU A 54 -97.566 -32.949 233.862 1.00148.28 N ANISOU 149 N LEU A 54 22925 23036 10379 -4196 73 1826 N ATOM 150 CA LEU A 54 -96.971 -33.304 235.146 1.00142.38 C ANISOU 150 CA LEU A 54 22353 22226 9519 -4205 39 1958 C ATOM 151 C LEU A 54 -96.598 -32.061 235.944 1.00140.56 C ANISOU 151 C LEU A 54 21829 22300 9277 -3875 153 1761 C ATOM 152 O LEU A 54 -96.895 -31.965 237.141 1.00142.78 O ANISOU 152 O LEU A 54 21988 22873 9390 -3989 242 1781 O ATOM 153 CB LEU A 54 -95.745 -34.187 234.914 1.00134.94 C ANISOU 153 CB LEU A 54 21918 20698 8655 -4046 -187 2122 C ATOM 154 CG LEU A 54 -95.038 -34.774 236.135 1.00134.73 C ANISOU 154 CG LEU A 54 22155 20530 8505 -4044 -272 2292 C ATOM 155 CD1 LEU A 54 -95.920 -35.800 236.826 1.00139.23 C ANISOU 155 CD1 LEU A 54 22867 21158 8877 -4568 -267 2510 C ATOM 156 CD2 LEU A 54 -93.704 -35.387 235.734 1.00133.35 C ANISOU 156 CD2 LEU A 54 22406 19828 8435 -3731 -497 2382 C ATOM 157 N VAL A 55 -95.923 -31.106 235.297 1.00137.82 N ANISOU 157 N VAL A 55 21390 21876 9097 -3474 138 1572 N ATOM 158 CA VAL A 55 -95.555 -29.859 235.970 1.00138.73 C ANISOU 158 CA VAL A 55 21263 22242 9205 -3173 218 1364 C ATOM 159 C VAL A 55 -96.799 -29.157 236.506 1.00139.55 C ANISOU 159 C VAL A 55 20956 22892 9173 -3282 414 1202 C ATOM 160 O VAL A 55 -96.842 -28.713 237.666 1.00141.69 O ANISOU 160 O VAL A 55 21099 23430 9305 -3237 488 1135 O ATOM 161 CB VAL A 55 -94.761 -28.946 235.018 1.00135.91 C ANISOU 161 CB VAL A 55 20876 21716 9047 -2796 163 1193 C ATOM 162 CG1 VAL A 55 -94.448 -27.620 235.695 1.00133.70 C ANISOU 162 CG1 VAL A 55 20374 21678 8747 -2530 226 966 C ATOM 163 CG2 VAL A 55 -93.478 -29.627 234.576 1.00134.64 C ANISOU 163 CG2 VAL A 55 21081 21080 8996 -2650 -26 1344 C ATOM 164 N CYS A 56 -97.822 -29.030 235.656 1.00137.48 N ANISOU 164 N CYS A 56 20472 22827 8939 -3400 493 1123 N ATOM 165 CA CYS A 56 -99.037 -28.324 236.048 1.00138.06 C ANISOU 165 CA CYS A 56 20109 23466 8883 -3446 673 942 C ATOM 166 C CYS A 56 -99.686 -28.978 237.261 1.00147.22 C ANISOU 166 C CYS A 56 21205 24923 9808 -3796 756 1086 C ATOM 167 O CYS A 56 -100.046 -28.294 238.224 1.00147.88 O ANISOU 167 O CYS A 56 21033 25402 9752 -3698 875 944 O ATOM 168 CB CYS A 56 -100.017 -28.270 234.875 1.00136.69 C ANISOU 168 CB CYS A 56 19718 23454 8762 -3541 719 867 C ATOM 169 SG CYS A 56 -99.465 -27.259 233.482 1.00134.30 S ANISOU 169 SG CYS A 56 19406 22921 8700 -3101 653 654 S ATOM 170 N MET A 57 -99.838 -30.305 237.237 1.00154.62 N ANISOU 170 N MET A 57 22394 25667 10688 -4211 685 1367 N ATOM 171 CA MET A 57 -100.456 -30.991 238.371 1.00166.98 C ANISOU 171 CA MET A 57 23924 27504 12018 -4600 753 1534 C ATOM 172 C MET A 57 -99.613 -30.850 239.635 1.00170.52 C ANISOU 172 C MET A 57 24522 27893 12375 -4429 733 1567 C ATOM 173 O MET A 57 -100.148 -30.606 240.728 1.00177.90 O ANISOU 173 O MET A 57 25230 29254 13109 -4514 859 1531 O ATOM 174 CB MET A 57 -100.676 -32.466 238.034 1.00175.41 C ANISOU 174 CB MET A 57 25318 28280 13049 -5088 638 1839 C ATOM 175 CG MET A 57 -101.685 -32.714 236.921 1.00181.22 C ANISOU 175 CG MET A 57 25886 29153 13816 -5362 658 1824 C ATOM 176 SD MET A 57 -103.312 -32.008 237.254 1.00189.81 S ANISOU 176 SD MET A 57 26289 31112 14718 -5536 899 1639 S ATOM 177 CE MET A 57 -103.302 -30.578 236.174 1.00185.36 C ANISOU 177 CE MET A 57 25417 30662 14351 -4971 952 1279 C ATOM 178 N ALA A 58 -98.291 -31.014 239.503 1.00168.82 N ANISOU 178 N ALA A 58 24674 27179 12290 -4182 570 1632 N ATOM 179 CA ALA A 58 -97.397 -30.917 240.653 1.00165.21 C ANISOU 179 CA ALA A 58 24373 26654 11744 -4009 524 1667 C ATOM 180 C ALA A 58 -97.523 -29.567 241.342 1.00164.21 C ANISOU 180 C ALA A 58 23907 26935 11551 -3714 653 1382 C ATOM 181 O ALA A 58 -97.530 -29.491 242.576 1.00161.30 O ANISOU 181 O ALA A 58 23502 26794 10991 -3737 704 1393 O ATOM 182 CB ALA A 58 -95.954 -31.162 240.218 1.00156.63 C ANISOU 182 CB ALA A 58 23661 25028 10825 -3734 322 1737 C ATOM 183 N VAL A 59 -97.622 -28.488 240.565 1.00161.20 N ANISOU 183 N VAL A 59 23299 26636 11313 -3426 694 1118 N ATOM 184 CA VAL A 59 -97.800 -27.191 241.211 1.00160.97 C ANISOU 184 CA VAL A 59 22986 26967 11210 -3135 796 826 C ATOM 185 C VAL A 59 -99.238 -27.022 241.696 1.00161.93 C ANISOU 185 C VAL A 59 22721 27668 11137 -3313 987 740 C ATOM 186 O VAL A 59 -99.482 -26.356 242.709 1.00161.86 O ANISOU 186 O VAL A 59 22530 28007 10964 -3178 1076 582 O ATOM 187 CB VAL A 59 -97.381 -26.053 240.266 1.00158.65 C ANISOU 187 CB VAL A 59 22619 26540 11119 -2754 754 570 C ATOM 188 CG1 VAL A 59 -97.614 -24.696 240.923 1.00158.42 C ANISOU 188 CG1 VAL A 59 22344 26846 11003 -2447 834 248 C ATOM 189 CG2 VAL A 59 -95.923 -26.211 239.865 1.00157.17 C ANISOU 189 CG2 VAL A 59 22770 25848 11098 -2596 569 660 C ATOM 190 N SER A 60 -100.203 -27.635 241.005 1.00162.25 N ANISOU 190 N SER A 60 22626 27845 11178 -3622 1044 840 N ATOM 191 CA SER A 60 -101.609 -27.443 241.341 1.00159.26 C ANISOU 191 CA SER A 60 21813 28082 10616 -3788 1221 745 C ATOM 192 C SER A 60 -101.936 -28.008 242.716 1.00159.35 C ANISOU 192 C SER A 60 21797 28387 10361 -4074 1296 899 C ATOM 193 O SER A 60 -102.630 -27.359 243.507 1.00157.99 O ANISOU 193 O SER A 60 21285 28738 10007 -3979 1436 723 O ATOM 194 CB SER A 60 -102.497 -28.082 240.274 1.00158.61 C ANISOU 194 CB SER A 60 21607 28074 10584 -4112 1238 844 C ATOM 195 OG SER A 60 -102.507 -29.492 240.397 1.00162.78 O ANISOU 195 OG SER A 60 22407 28395 11045 -4611 1169 1186 O ATOM 196 N ARG A 61 -101.450 -29.212 243.025 1.00164.14 N ANISOU 196 N ARG A 61 22771 28666 10928 -4406 1196 1223 N ATOM 197 CA ARG A 61 -101.885 -29.855 244.261 1.00170.39 C ANISOU 197 CA ARG A 61 23541 29752 11449 -4746 1266 1403 C ATOM 198 C ARG A 61 -100.948 -29.613 245.440 1.00167.70 C ANISOU 198 C ARG A 61 23405 29306 11006 -4515 1224 1400 C ATOM 199 O ARG A 61 -101.417 -29.552 246.582 1.00170.15 O ANISOU 199 O ARG A 61 23548 30034 11066 -4615 1334 1401 O ATOM 200 CB ARG A 61 -102.064 -31.364 244.048 1.00174.43 C ANISOU 200 CB ARG A 61 24340 30013 11922 -5298 1177 1769 C ATOM 201 CG ARG A 61 -100.793 -32.191 244.150 1.00176.66 C ANISOU 201 CG ARG A 61 25195 29642 12284 -5285 973 2006 C ATOM 202 CD ARG A 61 -101.115 -33.675 244.204 1.00184.89 C ANISOU 202 CD ARG A 61 26537 30490 13224 -5853 886 2361 C ATOM 203 NE ARG A 61 -100.008 -34.453 244.751 1.00188.25 N ANISOU 203 NE ARG A 61 27479 30416 13631 -5823 709 2588 N ATOM 204 CZ ARG A 61 -100.071 -35.752 245.024 1.00193.21 C ANISOU 204 CZ ARG A 61 28473 30792 14147 -6258 595 2907 C ATOM 205 NH1 ARG A 61 -99.015 -36.378 245.522 1.00194.55 N ANISOU 205 NH1 ARG A 61 29108 30514 14298 -6145 424 3086 N ATOM 206 NH2 ARG A 61 -101.195 -36.423 244.813 1.00196.68 N ANISOU 206 NH2 ARG A 61 28815 31435 14480 -6809 639 3044 N ATOM 207 N GLU A 62 -99.645 -29.473 245.209 1.00163.10 N ANISOU 207 N GLU A 62 23161 28214 10594 -4214 1065 1395 N ATOM 208 CA GLU A 62 -98.685 -29.326 246.296 1.00161.77 C ANISOU 208 CA GLU A 62 23205 27936 10324 -4016 996 1409 C ATOM 209 C GLU A 62 -98.530 -27.855 246.663 1.00164.16 C ANISOU 209 C GLU A 62 23274 28481 10620 -3570 1056 1046 C ATOM 210 O GLU A 62 -98.224 -27.022 245.804 1.00158.47 O ANISOU 210 O GLU A 62 22496 27612 10104 -3266 1015 830 O ATOM 211 CB GLU A 62 -97.334 -29.930 245.915 1.00155.59 C ANISOU 211 CB GLU A 62 22881 26530 9704 -3912 777 1582 C ATOM 212 CG GLU A 62 -97.360 -31.444 245.774 1.00155.57 C ANISOU 212 CG GLU A 62 23209 26231 9671 -4318 680 1946 C ATOM 213 CD GLU A 62 -97.703 -32.151 247.074 1.00158.20 C ANISOU 213 CD GLU A 62 23618 26779 9713 -4628 723 2155 C ATOM 214 OE1 GLU A 62 -97.402 -31.599 248.154 1.00157.94 O ANISOU 214 OE1 GLU A 62 23520 26968 9523 -4435 764 2058 O ATOM 215 OE2 GLU A 62 -98.274 -33.260 247.015 1.00160.61 O ANISOU 215 OE2 GLU A 62 24064 27026 9936 -5080 707 2418 O ATOM 216 N LYS A 63 -98.739 -27.543 247.945 1.00172.30 N ANISOU 216 N LYS A 63 24191 29871 11402 -3537 1140 979 N ATOM 217 CA LYS A 63 -98.713 -26.159 248.404 1.00168.50 C ANISOU 217 CA LYS A 63 23504 29644 10875 -3132 1191 618 C ATOM 218 C LYS A 63 -97.302 -25.632 248.631 1.00164.86 C ANISOU 218 C LYS A 63 23328 28808 10505 -2803 1018 525 C ATOM 219 O LYS A 63 -97.120 -24.413 248.713 1.00164.38 O ANISOU 219 O LYS A 63 23161 28825 10471 -2454 1010 206 O ATOM 220 CB LYS A 63 -99.522 -26.019 249.695 1.00172.11 C ANISOU 220 CB LYS A 63 23722 30663 11010 -3215 1347 565 C ATOM 221 N ALA A 64 -96.306 -26.515 248.746 1.00160.39 N ANISOU 221 N ALA A 64 23120 27847 9974 -2905 866 788 N ATOM 222 CA ALA A 64 -94.927 -26.054 248.875 1.00151.15 C ANISOU 222 CA ALA A 64 22184 26351 8894 -2608 685 708 C ATOM 223 C ALA A 64 -94.471 -25.299 247.633 1.00142.54 C ANISOU 223 C ALA A 64 21072 24998 8090 -2368 605 524 C ATOM 224 O ALA A 64 -93.607 -24.419 247.722 1.00142.42 O ANISOU 224 O ALA A 64 21114 24863 8136 -2089 493 328 O ATOM 225 CB ALA A 64 -93.999 -27.238 249.149 1.00148.78 C ANISOU 225 CB ALA A 64 22249 25705 8573 -2742 530 1037 C ATOM 226 N LEU A 65 -95.037 -25.628 246.473 1.00137.66 N ANISOU 226 N LEU A 65 20375 24294 7635 -2494 650 587 N ATOM 227 CA LEU A 65 -94.670 -25.010 245.206 1.00131.48 C ANISOU 227 CA LEU A 65 19578 23264 7115 -2296 582 444 C ATOM 228 C LEU A 65 -95.540 -23.814 244.840 1.00134.40 C ANISOU 228 C LEU A 65 19634 23925 7508 -2107 699 118 C ATOM 229 O LEU A 65 -95.247 -23.140 243.849 1.00130.40 O ANISOU 229 O LEU A 65 19115 23231 7198 -1914 639 -30 O ATOM 230 CB LEU A 65 -94.739 -26.041 244.074 1.00125.37 C ANISOU 230 CB LEU A 65 18928 22202 6505 -2508 543 688 C ATOM 231 CG LEU A 65 -93.846 -27.275 244.201 1.00127.41 C ANISOU 231 CG LEU A 65 19544 22097 6771 -2642 393 1005 C ATOM 232 CD1 LEU A 65 -94.281 -28.352 243.223 1.00119.39 C ANISOU 232 CD1 LEU A 65 18638 20868 5856 -2905 382 1228 C ATOM 233 CD2 LEU A 65 -92.397 -26.891 243.962 1.00116.88 C ANISOU 233 CD2 LEU A 65 18389 20444 5575 -2354 210 955 C ATOM 234 N GLN A 66 -96.594 -23.532 245.606 1.00138.47 N ANISOU 234 N GLN A 66 19895 24900 7817 -2139 857 1 N ATOM 235 CA GLN A 66 -97.574 -22.515 245.225 1.00133.95 C ANISOU 235 CA GLN A 66 19004 24642 7249 -1939 971 -302 C ATOM 236 C GLN A 66 -97.015 -21.134 245.559 1.00136.40 C ANISOU 236 C GLN A 66 19346 24915 7565 -1542 890 -639 C ATOM 237 O GLN A 66 -97.283 -20.545 246.609 1.00146.72 O ANISOU 237 O GLN A 66 20562 26511 8673 -1402 939 -823 O ATOM 238 CB GLN A 66 -98.908 -22.775 245.913 1.00140.76 C ANISOU 238 CB GLN A 66 19556 26052 7876 -2114 1163 -298 C ATOM 239 CG GLN A 66 -99.563 -24.076 245.476 1.00130.32 C ANISOU 239 CG GLN A 66 18190 24779 6548 -2554 1229 17 C ATOM 240 CD GLN A 66 -100.932 -24.285 246.090 1.00137.58 C ANISOU 240 CD GLN A 66 18744 26304 7225 -2764 1418 15 C ATOM 241 OE1 GLN A 66 -101.319 -23.589 247.029 1.00146.14 O ANISOU 241 OE1 GLN A 66 19633 27778 8116 -2581 1505 -188 O ATOM 242 NE2 GLN A 66 -101.675 -25.250 245.560 1.00136.72 N ANISOU 242 NE2 GLN A 66 18537 26294 7115 -3161 1474 238 N ATOM 243 N THR A 67 -96.215 -20.616 244.629 1.00144.39 N ANISOU 243 N THR A 67 20504 25557 8800 -1371 752 -719 N ATOM 244 CA THR A 67 -95.646 -19.278 244.700 1.00146.53 C ANISOU 244 CA THR A 67 20842 25724 9110 -1031 640 -1037 C ATOM 245 C THR A 67 -95.857 -18.574 243.365 1.00140.82 C ANISOU 245 C THR A 67 20054 24860 8590 -848 612 -1198 C ATOM 246 O THR A 67 -96.287 -19.178 242.377 1.00139.20 O ANISOU 246 O THR A 67 19772 24609 8507 -988 666 -1045 O ATOM 247 CB THR A 67 -94.151 -19.309 245.055 1.00151.16 C ANISOU 247 CB THR A 67 21721 25976 9738 -1031 449 -958 C ATOM 248 OG1 THR A 67 -93.431 -20.040 244.055 1.00151.27 O ANISOU 248 OG1 THR A 67 21878 25641 9958 -1172 362 -711 O ATOM 249 CG2 THR A 67 -93.930 -19.955 246.418 1.00153.82 C ANISOU 249 CG2 THR A 67 22135 26455 9854 -1171 462 -812 C ATOM 250 N THR A 68 -95.550 -17.276 243.347 1.00135.81 N ANISOU 250 N THR A 68 19477 24144 7981 -533 510 -1515 N ATOM 251 CA THR A 68 -95.829 -16.451 242.174 1.00127.78 C ANISOU 251 CA THR A 68 18414 23012 7124 -306 473 -1707 C ATOM 252 C THR A 68 -94.944 -16.842 240.995 1.00127.98 C ANISOU 252 C THR A 68 18596 22652 7376 -432 366 -1508 C ATOM 253 O THR A 68 -95.424 -16.999 239.864 1.00126.49 O ANISOU 253 O THR A 68 18316 22425 7318 -436 410 -1462 O ATOM 254 CB THR A 68 -95.632 -14.977 242.523 1.00129.45 C ANISOU 254 CB THR A 68 18720 23171 7293 58 353 -2091 C ATOM 255 OG1 THR A 68 -94.235 -14.710 242.701 1.00126.24 O ANISOU 255 OG1 THR A 68 18588 22439 6939 20 158 -2076 O ATOM 256 CG2 THR A 68 -96.367 -14.636 243.812 1.00130.63 C ANISOU 256 CG2 THR A 68 18741 23692 7199 190 446 -2281 C ATOM 257 N THR A 69 -93.640 -16.988 241.240 1.00128.59 N ANISOU 257 N THR A 69 18897 22466 7494 -526 219 -1395 N ATOM 258 CA THR A 69 -92.731 -17.398 240.175 1.00133.37 C ANISOU 258 CA THR A 69 19629 22620 8427 -620 115 -1174 C ATOM 259 C THR A 69 -93.098 -18.777 239.640 1.00139.48 C ANISOU 259 C THR A 69 20362 23430 9205 -881 215 -865 C ATOM 260 O THR A 69 -93.034 -19.021 238.429 1.00148.74 O ANISOU 260 O THR A 69 21539 24333 10642 -890 197 -755 O ATOM 261 CB THR A 69 -91.289 -17.383 240.685 1.00133.46 C ANISOU 261 CB THR A 69 19837 22388 8483 -669 -57 -1096 C ATOM 262 OG1 THR A 69 -91.014 -16.122 241.309 1.00132.48 O ANISOU 262 OG1 THR A 69 19773 22252 8313 -471 -163 -1396 O ATOM 263 CG2 THR A 69 -90.315 -17.592 239.536 1.00133.20 C ANISOU 263 CG2 THR A 69 19894 21920 8797 -703 -169 -916 C ATOM 264 N ASN A 70 -93.514 -19.687 240.522 1.00141.76 N ANISOU 264 N ASN A 70 20622 23957 9284 -1080 310 -712 N ATOM 265 CA ASN A 70 -93.980 -20.982 240.043 1.00140.16 C ANISOU 265 CA ASN A 70 20409 23726 9120 -1339 387 -426 C ATOM 266 C ASN A 70 -95.310 -20.869 239.306 1.00148.10 C ANISOU 266 C ASN A 70 21171 24955 10144 -1338 525 -513 C ATOM 267 O ASN A 70 -95.585 -21.672 238.410 1.00151.80 O ANISOU 267 O ASN A 70 21648 25316 10712 -1511 545 -331 O ATOM 268 CB ASN A 70 -94.103 -21.958 241.211 1.00132.95 C ANISOU 268 CB ASN A 70 19544 22946 8023 -1555 435 -228 C ATOM 269 CG ASN A 70 -92.756 -22.397 241.750 1.00127.05 C ANISOU 269 CG ASN A 70 19056 21942 7274 -1576 280 -69 C ATOM 270 OD1 ASN A 70 -92.108 -23.282 241.192 1.00122.97 O ANISOU 270 OD1 ASN A 70 18719 21135 6869 -1677 192 168 O ATOM 271 ND2 ASN A 70 -92.328 -21.781 242.846 1.00127.88 N ANISOU 271 ND2 ASN A 70 19183 22162 7241 -1457 236 -210 N ATOM 272 N TYR A 71 -96.136 -19.876 239.646 1.00150.67 N ANISOU 272 N TYR A 71 21285 25593 10369 -1125 605 -803 N ATOM 273 CA TYR A 71 -97.325 -19.597 238.844 1.00151.38 C ANISOU 273 CA TYR A 71 21122 25908 10487 -1046 709 -927 C ATOM 274 C TYR A 71 -96.942 -19.216 237.417 1.00148.04 C ANISOU 274 C TYR A 71 20778 25183 10286 -915 616 -959 C ATOM 275 O TYR A 71 -97.544 -19.692 236.444 1.00146.55 O ANISOU 275 O TYR A 71 20488 24987 10206 -1010 662 -865 O ATOM 276 CB TYR A 71 -98.154 -18.496 239.506 1.00154.08 C ANISOU 276 CB TYR A 71 21247 26616 10681 -750 781 -1264 C ATOM 277 CG TYR A 71 -99.067 -19.006 240.599 1.00157.06 C ANISOU 277 CG TYR A 71 21406 27440 10829 -913 935 -1219 C ATOM 278 CD1 TYR A 71 -99.623 -20.277 240.528 1.00157.33 C ANISOU 278 CD1 TYR A 71 21344 27615 10818 -1303 1033 -932 C ATOM 279 CD2 TYR A 71 -99.362 -18.222 241.707 1.00159.40 C ANISOU 279 CD2 TYR A 71 21606 28016 10941 -691 973 -1461 C ATOM 280 CE1 TYR A 71 -100.454 -20.750 241.527 1.00161.84 C ANISOU 280 CE1 TYR A 71 21708 28622 11162 -1494 1171 -874 C ATOM 281 CE2 TYR A 71 -100.192 -18.687 242.711 1.00162.70 C ANISOU 281 CE2 TYR A 71 21804 28884 11131 -847 1121 -1412 C ATOM 282 CZ TYR A 71 -100.735 -19.951 242.615 1.00164.23 C ANISOU 282 CZ TYR A 71 21883 29237 11279 -1261 1223 -1110 C ATOM 283 OH TYR A 71 -101.561 -20.419 243.611 1.00168.36 O ANISOU 283 OH TYR A 71 22179 30233 11559 -1456 1366 -1046 O ATOM 284 N LEU A 72 -95.940 -18.344 237.276 1.00145.30 N ANISOU 284 N LEU A 72 20606 24452 10147 -686 468 -1070 N ATOM 285 CA LEU A 72 -95.441 -18.002 235.946 1.00139.27 C ANISOU 285 CA LEU A 72 19932 23237 9747 -562 364 -1043 C ATOM 286 C LEU A 72 -94.881 -19.233 235.239 1.00137.89 C ANISOU 286 C LEU A 72 19876 22798 9717 -817 337 -718 C ATOM 287 O LEU A 72 -95.041 -19.392 234.020 1.00139.74 O ANISOU 287 O LEU A 72 20092 22840 10164 -797 326 -653 O ATOM 288 CB LEU A 72 -94.380 -16.907 236.049 1.00136.24 C ANISOU 288 CB LEU A 72 19728 22515 9520 -352 203 -1186 C ATOM 289 CG LEU A 72 -94.866 -15.496 236.387 1.00137.51 C ANISOU 289 CG LEU A 72 19856 22774 9619 -26 172 -1540 C ATOM 290 CD1 LEU A 72 -93.688 -14.546 236.539 1.00136.67 C ANISOU 290 CD1 LEU A 72 19985 22284 9661 83 -16 -1636 C ATOM 291 CD2 LEU A 72 -95.832 -14.991 235.326 1.00136.66 C ANISOU 291 CD2 LEU A 72 19617 22680 9629 186 208 -1665 C ATOM 292 N ILE A 73 -94.220 -20.114 235.992 1.00135.70 N ANISOU 292 N ILE A 73 19742 22506 9312 -1030 312 -519 N ATOM 293 CA ILE A 73 -93.689 -21.347 235.412 1.00133.38 C ANISOU 293 CA ILE A 73 19606 21957 9116 -1234 265 -222 C ATOM 294 C ILE A 73 -94.825 -22.217 234.883 1.00131.97 C ANISOU 294 C ILE A 73 19327 21950 8867 -1447 373 -111 C ATOM 295 O ILE A 73 -94.711 -22.839 233.819 1.00132.46 O ANISOU 295 O ILE A 73 19468 21754 9107 -1506 331 32 O ATOM 296 CB ILE A 73 -92.835 -22.097 236.451 1.00131.19 C ANISOU 296 CB ILE A 73 19521 21658 8666 -1386 202 -45 C ATOM 297 CG1 ILE A 73 -91.506 -21.376 236.674 1.00126.00 C ANISOU 297 CG1 ILE A 73 18969 20767 8138 -1200 58 -115 C ATOM 298 CG2 ILE A 73 -92.591 -23.535 236.017 1.00131.28 C ANISOU 298 CG2 ILE A 73 19721 21472 8689 -1603 162 258 C ATOM 299 CD1 ILE A 73 -90.634 -22.035 237.719 1.00127.17 C ANISOU 299 CD1 ILE A 73 19288 20924 8106 -1304 -24 38 C ATOM 300 N VAL A 74 -95.942 -22.266 235.610 1.00125.13 N ANISOU 300 N VAL A 74 18272 21548 7724 -1572 508 -181 N ATOM 301 CA VAL A 74 -97.082 -23.061 235.162 1.00126.12 C ANISOU 301 CA VAL A 74 18263 21902 7754 -1828 609 -78 C ATOM 302 C VAL A 74 -97.718 -22.436 233.928 1.00130.81 C ANISOU 302 C VAL A 74 18670 22472 8561 -1630 624 -235 C ATOM 303 O VAL A 74 -98.198 -23.144 233.036 1.00129.02 O ANISOU 303 O VAL A 74 18426 22190 8407 -1798 629 -114 O ATOM 304 CB VAL A 74 -98.104 -23.230 236.299 1.00126.48 C ANISOU 304 CB VAL A 74 18085 22392 7579 -1974 748 -107 C ATOM 305 CG1 VAL A 74 -99.315 -24.016 235.819 1.00126.09 C ANISOU 305 CG1 VAL A 74 17850 22582 7477 -2267 842 -2 C ATOM 306 CG2 VAL A 74 -97.464 -23.943 237.454 1.00130.22 C ANISOU 306 CG2 VAL A 74 18760 22772 7944 -2146 714 82 C ATOM 307 N SER A 75 -97.742 -21.104 233.856 1.00133.14 N ANISOU 307 N SER A 75 18850 22793 8945 -1269 613 -508 N ATOM 308 CA SER A 75 -98.205 -20.457 232.630 1.00132.43 C ANISOU 308 CA SER A 75 18639 22608 9071 -1040 595 -642 C ATOM 309 C SER A 75 -97.321 -20.834 231.444 1.00131.64 C ANISOU 309 C SER A 75 18752 21989 9277 -1041 479 -474 C ATOM 310 O SER A 75 -97.819 -21.115 230.345 1.00132.34 O ANISOU 310 O SER A 75 18776 22022 9484 -1061 480 -434 O ATOM 311 CB SER A 75 -98.242 -18.941 232.814 1.00135.49 C ANISOU 311 CB SER A 75 18959 23026 9495 -636 565 -952 C ATOM 312 OG SER A 75 -98.560 -18.287 231.597 1.00134.46 O ANISOU 312 OG SER A 75 18773 22735 9582 -395 518 -1059 O ATOM 313 N LEU A 76 -96.002 -20.847 231.653 1.00137.76 N ANISOU 313 N LEU A 76 19763 22417 10161 -1012 376 -379 N ATOM 314 CA LEU A 76 -95.083 -21.290 230.606 1.00136.46 C ANISOU 314 CA LEU A 76 19783 21822 10243 -1007 274 -212 C ATOM 315 C LEU A 76 -95.352 -22.739 230.204 1.00137.46 C ANISOU 315 C LEU A 76 19996 21910 10320 -1288 283 19 C ATOM 316 O LEU A 76 -95.297 -23.089 229.016 1.00134.50 O ANISOU 316 O LEU A 76 19674 21313 10117 -1268 240 92 O ATOM 317 CB LEU A 76 -93.640 -21.122 231.082 1.00128.96 C ANISOU 317 CB LEU A 76 19024 20616 9358 -946 167 -151 C ATOM 318 CG LEU A 76 -92.517 -21.620 230.171 1.00125.03 C ANISOU 318 CG LEU A 76 18697 19742 9067 -920 63 25 C ATOM 319 CD1 LEU A 76 -92.592 -20.949 228.810 1.00121.62 C ANISOU 319 CD1 LEU A 76 18206 19132 8873 -740 44 -44 C ATOM 320 CD2 LEU A 76 -91.161 -21.381 230.820 1.00124.50 C ANISOU 320 CD2 LEU A 76 18749 19539 9015 -865 -37 61 C ATOM 321 N ALA A 77 -95.638 -23.596 231.187 1.00138.35 N ANISOU 321 N ALA A 77 20155 22226 10185 -1561 328 138 N ATOM 322 CA ALA A 77 -95.944 -24.993 230.892 1.00135.80 C ANISOU 322 CA ALA A 77 19972 21839 9787 -1872 314 364 C ATOM 323 C ALA A 77 -97.232 -25.122 230.089 1.00132.82 C ANISOU 323 C ALA A 77 19390 21670 9406 -1985 385 312 C ATOM 324 O ALA A 77 -97.324 -25.961 229.187 1.00132.30 O ANISOU 324 O ALA A 77 19450 21397 9422 -2119 326 442 O ATOM 325 CB ALA A 77 -96.035 -25.796 232.189 1.00141.31 C ANISOU 325 CB ALA A 77 20778 22724 10188 -2168 344 513 C ATOM 326 N VAL A 78 -98.237 -24.303 230.405 1.00132.54 N ANISOU 326 N VAL A 78 19036 22062 9260 -1916 500 111 N ATOM 327 CA VAL A 78 -99.474 -24.300 229.627 1.00126.35 C ANISOU 327 CA VAL A 78 18000 21540 8466 -1977 561 32 C ATOM 328 C VAL A 78 -99.194 -23.865 228.195 1.00120.55 C ANISOU 328 C VAL A 78 17297 20475 8030 -1711 477 -28 C ATOM 329 O VAL A 78 -99.753 -24.418 227.238 1.00119.21 O ANISOU 329 O VAL A 78 17097 20284 7913 -1834 456 26 O ATOM 330 CB VAL A 78 -100.532 -23.404 230.299 1.00124.11 C ANISOU 330 CB VAL A 78 17349 21823 7986 -1864 694 -203 C ATOM 331 CG1 VAL A 78 -101.750 -23.249 229.401 1.00119.71 C ANISOU 331 CG1 VAL A 78 16492 21558 7435 -1845 738 -315 C ATOM 332 CG2 VAL A 78 -100.941 -23.985 231.642 1.00128.12 C ANISOU 332 CG2 VAL A 78 17797 22730 8152 -2188 796 -115 C ATOM 333 N ALA A 79 -98.328 -22.864 228.028 1.00119.14 N ANISOU 333 N ALA A 79 17188 20045 8036 -1366 422 -136 N ATOM 334 CA ALA A 79 -97.942 -22.434 226.687 1.00119.51 C ANISOU 334 CA ALA A 79 17291 19768 8348 -1130 342 -163 C ATOM 335 C ALA A 79 -97.305 -23.579 225.905 1.00126.68 C ANISOU 335 C ALA A 79 18445 20327 9360 -1283 257 57 C ATOM 336 O ALA A 79 -97.665 -23.835 224.748 1.00129.62 O ANISOU 336 O ALA A 79 18804 20609 9835 -1270 225 72 O ATOM 337 CB ALA A 79 -96.989 -21.241 226.772 1.00117.62 C ANISOU 337 CB ALA A 79 17127 19304 8260 -816 286 -273 C ATOM 338 N ASP A 80 -96.346 -24.275 226.522 1.00132.62 N ANISOU 338 N ASP A 80 19435 20882 10071 -1397 207 217 N ATOM 339 CA ASP A 80 -95.687 -25.387 225.838 1.00131.14 C ANISOU 339 CA ASP A 80 19517 20355 9957 -1483 107 408 C ATOM 340 C ASP A 80 -96.668 -26.516 225.531 1.00129.42 C ANISOU 340 C ASP A 80 19335 20220 9617 -1805 107 506 C ATOM 341 O ASP A 80 -96.581 -27.159 224.475 1.00130.53 O ANISOU 341 O ASP A 80 19621 20121 9853 -1815 26 576 O ATOM 342 CB ASP A 80 -94.522 -25.905 226.683 1.00130.40 C ANISOU 342 CB ASP A 80 19665 20078 9803 -1509 40 547 C ATOM 343 CG ASP A 80 -93.241 -25.129 226.448 1.00128.99 C ANISOU 343 CG ASP A 80 19520 19689 9801 -1208 -18 510 C ATOM 344 OD1 ASP A 80 -93.280 -24.120 225.713 1.00127.74 O ANISOU 344 OD1 ASP A 80 19217 19516 9803 -1004 -1 382 O ATOM 345 OD2 ASP A 80 -92.194 -25.528 227.001 1.00127.70 O ANISOU 345 OD2 ASP A 80 19528 19389 9602 -1186 -90 616 O ATOM 346 N LEU A 81 -97.610 -26.769 226.444 1.00127.90 N ANISOU 346 N LEU A 81 19013 20384 9197 -2088 192 510 N ATOM 347 CA LEU A 81 -98.637 -27.778 226.204 1.00122.14 C ANISOU 347 CA LEU A 81 18286 19791 8330 -2466 192 606 C ATOM 348 C LEU A 81 -99.496 -27.409 225.002 1.00113.02 C ANISOU 348 C LEU A 81 16904 18753 7285 -2384 204 476 C ATOM 349 O LEU A 81 -99.821 -28.266 224.172 1.00105.77 O ANISOU 349 O LEU A 81 16109 17694 6383 -2571 125 560 O ATOM 350 CB LEU A 81 -99.500 -27.948 227.454 1.00124.72 C ANISOU 350 CB LEU A 81 18448 20575 8366 -2788 306 629 C ATOM 351 CG LEU A 81 -100.599 -29.012 227.417 1.00129.75 C ANISOU 351 CG LEU A 81 19070 21424 8806 -3285 314 757 C ATOM 352 CD1 LEU A 81 -99.999 -30.396 227.233 1.00132.25 C ANISOU 352 CD1 LEU A 81 19868 21272 9109 -3538 157 1006 C ATOM 353 CD2 LEU A 81 -101.440 -28.954 228.684 1.00131.52 C ANISOU 353 CD2 LEU A 81 19048 22202 8720 -3568 459 760 C ATOM 354 N LEU A 82 -99.872 -26.132 224.895 1.00110.07 N ANISOU 354 N LEU A 82 16223 18624 6975 -2092 282 263 N ATOM 355 CA LEU A 82 -100.654 -25.681 223.749 1.00104.64 C ANISOU 355 CA LEU A 82 15320 18051 6386 -1954 279 131 C ATOM 356 C LEU A 82 -99.860 -25.819 222.457 1.00101.44 C ANISOU 356 C LEU A 82 15141 17186 6214 -1758 162 181 C ATOM 357 O LEU A 82 -100.415 -26.197 221.419 1.00101.16 O ANISOU 357 O LEU A 82 15079 17136 6219 -1816 112 178 O ATOM 358 CB LEU A 82 -101.112 -24.238 223.960 1.00103.05 C ANISOU 358 CB LEU A 82 14807 18154 6195 -1618 360 -108 C ATOM 359 CG LEU A 82 -102.257 -24.079 224.962 1.00107.33 C ANISOU 359 CG LEU A 82 15022 19289 6470 -1772 486 -210 C ATOM 360 CD1 LEU A 82 -102.545 -22.613 225.241 1.00109.17 C ANISOU 360 CD1 LEU A 82 15017 19759 6704 -1354 539 -471 C ATOM 361 CD2 LEU A 82 -103.506 -24.784 224.453 1.00107.91 C ANISOU 361 CD2 LEU A 82 14877 19706 6416 -2078 504 -188 C ATOM 362 N VAL A 83 -98.562 -25.507 222.500 1.00102.88 N ANISOU 362 N VAL A 83 15528 17028 6534 -1527 118 223 N ATOM 363 CA VAL A 83 -97.713 -25.724 221.328 1.00103.04 C ANISOU 363 CA VAL A 83 15756 16656 6737 -1350 18 288 C ATOM 364 C VAL A 83 -97.770 -27.186 220.903 1.00102.40 C ANISOU 364 C VAL A 83 15926 16388 6595 -1614 -73 439 C ATOM 365 O VAL A 83 -98.035 -27.505 219.738 1.00 97.88 O ANISOU 365 O VAL A 83 15394 15706 6090 -1586 -136 430 O ATOM 366 CB VAL A 83 -96.261 -25.297 221.615 1.00102.62 C ANISOU 366 CB VAL A 83 15860 16340 6793 -1124 -12 332 C ATOM 367 CG1 VAL A 83 -95.388 -25.553 220.394 1.00 96.88 C ANISOU 367 CG1 VAL A 83 15308 15284 6219 -940 -99 401 C ATOM 368 CG2 VAL A 83 -96.190 -23.845 222.011 1.00102.45 C ANISOU 368 CG2 VAL A 83 15648 16448 6830 -894 48 180 C ATOM 369 N ALA A 84 -97.513 -28.094 221.847 1.00105.28 N ANISOU 369 N ALA A 84 16495 16691 6815 -1867 -97 578 N ATOM 370 CA ALA A 84 -97.456 -29.516 221.518 1.00106.88 C ANISOU 370 CA ALA A 84 17030 16633 6948 -2107 -219 731 C ATOM 371 C ALA A 84 -98.795 -30.044 221.016 1.00105.94 C ANISOU 371 C ALA A 84 16812 16704 6737 -2430 -231 714 C ATOM 372 O ALA A 84 -98.836 -30.909 220.132 1.00103.46 O ANISOU 372 O ALA A 84 16730 16140 6439 -2518 -355 767 O ATOM 373 CB ALA A 84 -96.996 -30.316 222.734 1.00111.48 C ANISOU 373 CB ALA A 84 17869 17123 7367 -2324 -253 893 C ATOM 374 N THR A 85 -99.902 -29.538 221.561 1.00107.15 N ANISOU 374 N THR A 85 16612 17323 6775 -2603 -111 629 N ATOM 375 CA THR A 85 -101.208 -30.103 221.235 1.00106.90 C ANISOU 375 CA THR A 85 16444 17558 6615 -2977 -120 627 C ATOM 376 C THR A 85 -101.784 -29.520 219.949 1.00106.87 C ANISOU 376 C THR A 85 16208 17659 6740 -2766 -134 468 C ATOM 377 O THR A 85 -102.219 -30.264 219.064 1.00107.66 O ANISOU 377 O THR A 85 16414 17657 6833 -2949 -240 495 O ATOM 378 CB THR A 85 -102.177 -29.882 222.398 1.00110.85 C ANISOU 378 CB THR A 85 16628 18599 6892 -3263 19 608 C ATOM 379 OG1 THR A 85 -102.112 -28.515 222.823 1.00111.59 O ANISOU 379 OG1 THR A 85 16412 18951 7038 -2891 145 433 O ATOM 380 CG2 THR A 85 -101.824 -30.792 223.566 1.00113.81 C ANISOU 380 CG2 THR A 85 17287 18875 7082 -3608 4 814 C ATOM 381 N LEU A 86 -101.797 -28.194 219.829 1.00107.19 N ANISOU 381 N LEU A 86 15958 17884 6886 -2382 -44 302 N ATOM 382 CA LEU A 86 -102.525 -27.536 218.751 1.00108.19 C ANISOU 382 CA LEU A 86 15823 18193 7092 -2182 -51 146 C ATOM 383 C LEU A 86 -101.704 -27.392 217.475 1.00109.70 C ANISOU 383 C LEU A 86 16222 17969 7488 -1858 -148 144 C ATOM 384 O LEU A 86 -102.232 -27.600 216.378 1.00115.85 O ANISOU 384 O LEU A 86 16965 18757 8294 -1859 -221 100 O ATOM 385 CB LEU A 86 -103.004 -26.156 219.210 1.00104.55 C ANISOU 385 CB LEU A 86 14986 18117 6620 -1898 69 -39 C ATOM 386 CG LEU A 86 -103.830 -26.111 220.497 1.00102.44 C ANISOU 386 CG LEU A 86 14448 18352 6121 -2138 190 -75 C ATOM 387 CD1 LEU A 86 -104.349 -24.703 220.747 1.00100.31 C ANISOU 387 CD1 LEU A 86 13825 18450 5839 -1763 279 -303 C ATOM 388 CD2 LEU A 86 -104.976 -27.109 220.440 1.00103.25 C ANISOU 388 CD2 LEU A 86 14410 18790 6031 -2626 180 -14 C ATOM 389 N VAL A 87 -100.428 -27.045 217.590 1.00106.26 N ANISOU 389 N VAL A 87 15988 17207 7179 -1592 -151 191 N ATOM 390 CA VAL A 87 -99.624 -26.629 216.445 1.00102.56 C ANISOU 390 CA VAL A 87 15638 16442 6888 -1244 -209 178 C ATOM 391 C VAL A 87 -98.769 -27.768 215.903 1.00109.84 C ANISOU 391 C VAL A 87 16934 16969 7830 -1290 -323 310 C ATOM 392 O VAL A 87 -98.761 -28.024 214.699 1.00113.53 O ANISOU 392 O VAL A 87 17488 17296 8350 -1185 -403 295 O ATOM 393 CB VAL A 87 -98.756 -25.409 216.826 1.00 97.13 C ANISOU 393 CB VAL A 87 14900 15691 6316 -919 -145 138 C ATOM 394 CG1 VAL A 87 -97.753 -25.111 215.727 1.00 94.03 C ANISOU 394 CG1 VAL A 87 14657 14994 6078 -627 -200 174 C ATOM 395 CG2 VAL A 87 -99.637 -24.200 217.101 1.00 88.79 C ANISOU 395 CG2 VAL A 87 13520 14973 5244 -780 -68 -29 C ATOM 396 N MET A 88 -98.041 -28.460 216.779 1.00114.14 N ANISOU 396 N MET A 88 17715 17338 8316 -1415 -343 432 N ATOM 397 CA MET A 88 -97.087 -29.465 216.319 1.00116.46 C ANISOU 397 CA MET A 88 18386 17245 8620 -1362 -465 540 C ATOM 398 C MET A 88 -97.674 -30.570 215.437 1.00117.83 C ANISOU 398 C MET A 88 18762 17281 8727 -1553 -596 553 C ATOM 399 O MET A 88 -96.948 -31.030 214.539 1.00123.38 O ANISOU 399 O MET A 88 19709 17695 9475 -1344 -696 569 O ATOM 400 CB MET A 88 -96.368 -30.080 217.530 1.00123.02 C ANISOU 400 CB MET A 88 19441 17940 9359 -1481 -483 667 C ATOM 401 CG MET A 88 -95.504 -29.093 218.302 1.00125.98 C ANISOU 401 CG MET A 88 19682 18381 9802 -1257 -391 656 C ATOM 402 SD MET A 88 -94.546 -29.861 219.624 1.00129.93 S ANISOU 402 SD MET A 88 20463 18719 10186 -1345 -440 808 S ATOM 403 CE MET A 88 -93.431 -30.900 218.688 1.00130.15 C ANISOU 403 CE MET A 88 20879 18335 10239 -1114 -605 888 C ATOM 404 N PRO A 89 -98.913 -31.051 215.628 1.00115.88 N ANISOU 404 N PRO A 89 18436 17235 8358 -1944 -612 545 N ATOM 405 CA PRO A 89 -99.426 -32.077 214.698 1.00113.87 C ANISOU 405 CA PRO A 89 18399 16821 8045 -2138 -765 548 C ATOM 406 C PRO A 89 -99.414 -31.642 213.242 1.00115.29 C ANISOU 406 C PRO A 89 18502 16966 8336 -1827 -802 434 C ATOM 407 O PRO A 89 -99.037 -32.430 212.366 1.00121.10 O ANISOU 407 O PRO A 89 19550 17396 9064 -1755 -943 442 O ATOM 408 CB PRO A 89 -100.852 -32.324 215.209 1.00115.39 C ANISOU 408 CB PRO A 89 18377 17377 8091 -2622 -739 543 C ATOM 409 CG PRO A 89 -100.777 -32.023 216.653 1.00117.96 C ANISOU 409 CG PRO A 89 18584 17893 8342 -2746 -614 609 C ATOM 410 CD PRO A 89 -99.813 -30.879 216.786 1.00116.44 C ANISOU 410 CD PRO A 89 18267 17673 8303 -2272 -511 552 C ATOM 411 N TRP A 90 -99.819 -30.404 212.953 1.00110.91 N ANISOU 411 N TRP A 90 17562 16710 7867 -1622 -689 324 N ATOM 412 CA TRP A 90 -99.820 -29.937 211.571 1.00108.17 C ANISOU 412 CA TRP A 90 17150 16340 7608 -1325 -726 234 C ATOM 413 C TRP A 90 -98.404 -29.759 211.037 1.00103.75 C ANISOU 413 C TRP A 90 16794 15478 7149 -934 -734 277 C ATOM 414 O TRP A 90 -98.162 -29.968 209.842 1.00102.52 O ANISOU 414 O TRP A 90 16760 15182 7011 -745 -813 246 O ATOM 415 CB TRP A 90 -100.616 -28.639 211.462 1.00110.71 C ANISOU 415 CB TRP A 90 17046 17041 7977 -1188 -621 116 C ATOM 416 CG TRP A 90 -101.917 -28.719 212.193 1.00117.75 C ANISOU 416 CG TRP A 90 17670 18325 8745 -1536 -582 68 C ATOM 417 CD1 TRP A 90 -102.170 -28.284 213.458 1.00118.17 C ANISOU 417 CD1 TRP A 90 17527 18629 8745 -1646 -464 68 C ATOM 418 CD2 TRP A 90 -103.138 -29.297 211.714 1.00120.98 C ANISOU 418 CD2 TRP A 90 17961 18966 9042 -1838 -663 13 C ATOM 419 NE1 TRP A 90 -103.475 -28.545 213.796 1.00119.34 N ANISOU 419 NE1 TRP A 90 17418 19184 8743 -1986 -450 20 N ATOM 420 CE2 TRP A 90 -104.092 -29.164 212.741 1.00121.84 C ANISOU 420 CE2 TRP A 90 17766 19503 9025 -2126 -574 -10 C ATOM 421 CE3 TRP A 90 -103.518 -29.907 210.515 1.00123.92 C ANISOU 421 CE3 TRP A 90 18441 19251 9391 -1897 -806 -25 C ATOM 422 CZ2 TRP A 90 -105.402 -29.618 212.607 1.00125.57 C ANISOU 422 CZ2 TRP A 90 18012 20349 9350 -2493 -618 -59 C ATOM 423 CZ3 TRP A 90 -104.820 -30.357 210.384 1.00127.13 C ANISOU 423 CZ3 TRP A 90 18650 19989 9664 -2267 -867 -80 C ATOM 424 CH2 TRP A 90 -105.745 -30.211 211.424 1.00126.84 C ANISOU 424 CH2 TRP A 90 18283 20407 9504 -2572 -770 -91 C ATOM 425 N VAL A 91 -97.458 -29.382 211.899 1.00100.91 N ANISOU 425 N VAL A 91 16455 15050 6836 -814 -656 346 N ATOM 426 CA VAL A 91 -96.070 -29.289 211.462 1.00101.30 C ANISOU 426 CA VAL A 91 16665 14870 6952 -479 -665 398 C ATOM 427 C VAL A 91 -95.528 -30.674 211.125 1.00104.83 C ANISOU 427 C VAL A 91 17509 15008 7312 -488 -811 450 C ATOM 428 O VAL A 91 -94.763 -30.841 210.168 1.00107.67 O ANISOU 428 O VAL A 91 18004 15222 7683 -198 -860 443 O ATOM 429 CB VAL A 91 -95.218 -28.585 212.534 1.00101.64 C ANISOU 429 CB VAL A 91 16622 14947 7051 -388 -564 454 C ATOM 430 CG1 VAL A 91 -93.796 -28.383 212.035 1.00101.87 C ANISOU 430 CG1 VAL A 91 16742 14825 7139 -57 -565 508 C ATOM 431 CG2 VAL A 91 -95.848 -27.257 212.926 1.00101.13 C ANISOU 431 CG2 VAL A 91 16220 15154 7052 -379 -449 378 C ATOM 432 N VAL A 92 -95.938 -31.693 211.886 1.00106.56 N ANISOU 432 N VAL A 92 17939 15127 7421 -816 -891 502 N ATOM 433 CA VAL A 92 -95.566 -33.065 211.547 1.00109.39 C ANISOU 433 CA VAL A 92 18744 15141 7677 -837 -1069 540 C ATOM 434 C VAL A 92 -96.208 -33.476 210.228 1.00114.01 C ANISOU 434 C VAL A 92 19414 15671 8233 -844 -1181 444 C ATOM 435 O VAL A 92 -95.587 -34.154 209.400 1.00118.13 O ANISOU 435 O VAL A 92 20237 15936 8712 -614 -1305 418 O ATOM 436 CB VAL A 92 -95.947 -34.024 212.689 1.00110.95 C ANISOU 436 CB VAL A 92 19182 15224 7748 -1241 -1144 639 C ATOM 437 CG1 VAL A 92 -95.603 -35.459 212.318 1.00113.52 C ANISOU 437 CG1 VAL A 92 20045 15131 7958 -1259 -1367 673 C ATOM 438 CG2 VAL A 92 -95.235 -33.629 213.972 1.00109.53 C ANISOU 438 CG2 VAL A 92 18934 15103 7580 -1198 -1044 730 C ATOM 439 N TYR A 93 -97.463 -33.074 210.014 1.00115.92 N ANISOU 439 N TYR A 93 19385 16179 8480 -1086 -1146 376 N ATOM 440 CA TYR A 93 -98.139 -33.360 208.752 1.00120.05 C ANISOU 440 CA TYR A 93 19941 16702 8971 -1099 -1254 274 C ATOM 441 C TYR A 93 -97.382 -32.760 207.572 1.00117.34 C ANISOU 441 C TYR A 93 19550 16333 8700 -620 -1227 216 C ATOM 442 O TYR A 93 -97.211 -33.411 206.533 1.00117.19 O ANISOU 442 O TYR A 93 19779 16129 8619 -484 -1360 158 O ATOM 443 CB TYR A 93 -99.572 -32.828 208.803 1.00124.30 C ANISOU 443 CB TYR A 93 20103 17625 9502 -1390 -1201 208 C ATOM 444 CG TYR A 93 -100.311 -32.876 207.485 1.00128.37 C ANISOU 444 CG TYR A 93 20560 18224 9992 -1367 -1299 91 C ATOM 445 CD1 TYR A 93 -100.583 -34.086 206.860 1.00132.31 C ANISOU 445 CD1 TYR A 93 21409 18481 10380 -1563 -1503 61 C ATOM 446 CD2 TYR A 93 -100.745 -31.709 206.869 1.00127.17 C ANISOU 446 CD2 TYR A 93 20030 18377 9913 -1144 -1206 6 C ATOM 447 CE1 TYR A 93 -101.262 -34.132 205.656 1.00132.53 C ANISOU 447 CE1 TYR A 93 21383 18600 10372 -1547 -1606 -57 C ATOM 448 CE2 TYR A 93 -101.424 -31.744 205.666 1.00128.75 C ANISOU 448 CE2 TYR A 93 20172 18672 10074 -1108 -1305 -100 C ATOM 449 CZ TYR A 93 -101.680 -32.959 205.064 1.00130.06 C ANISOU 449 CZ TYR A 93 20661 18625 10130 -1316 -1501 -134 C ATOM 450 OH TYR A 93 -102.355 -33.000 203.867 1.00128.37 O ANISOU 450 OH TYR A 93 20391 18517 9865 -1285 -1613 -249 O ATOM 451 N LEU A 94 -96.915 -31.517 207.720 1.00113.05 N ANISOU 451 N LEU A 94 18708 15975 8270 -372 -1062 234 N ATOM 452 CA LEU A 94 -96.144 -30.881 206.656 1.00109.97 C ANISOU 452 CA LEU A 94 18264 15587 7931 40 -1022 214 C ATOM 453 C LEU A 94 -94.775 -31.526 206.482 1.00113.99 C ANISOU 453 C LEU A 94 19064 15850 8395 313 -1070 263 C ATOM 454 O LEU A 94 -94.272 -31.612 205.356 1.00117.27 O ANISOU 454 O LEU A 94 19565 16221 8772 604 -1107 225 O ATOM 455 CB LEU A 94 -95.988 -29.388 206.940 1.00104.79 C ANISOU 455 CB LEU A 94 17258 15160 7397 182 -854 238 C ATOM 456 CG LEU A 94 -97.064 -28.469 206.362 1.00104.24 C ANISOU 456 CG LEU A 94 16902 15340 7363 181 -821 156 C ATOM 457 CD1 LEU A 94 -96.809 -27.027 206.767 1.00 98.56 C ANISOU 457 CD1 LEU A 94 15928 14767 6754 334 -684 183 C ATOM 458 CD2 LEU A 94 -97.106 -28.601 204.850 1.00105.48 C ANISOU 458 CD2 LEU A 94 17134 15468 7474 384 -901 104 C ATOM 459 N GLU A 95 -94.155 -31.978 207.575 1.00112.40 N ANISOU 459 N GLU A 95 19007 15520 8178 249 -1072 343 N ATOM 460 CA GLU A 95 -92.882 -32.682 207.462 1.00114.92 C ANISOU 460 CA GLU A 95 19606 15629 8428 538 -1141 376 C ATOM 461 C GLU A 95 -93.052 -34.038 206.788 1.00116.30 C ANISOU 461 C GLU A 95 20204 15520 8466 546 -1348 308 C ATOM 462 O GLU A 95 -92.104 -34.556 206.187 1.00117.65 O ANISOU 462 O GLU A 95 20593 15554 8554 900 -1421 280 O ATOM 463 CB GLU A 95 -92.248 -32.847 208.845 1.00119.39 C ANISOU 463 CB GLU A 95 20232 16134 8997 468 -1115 476 C ATOM 464 CG GLU A 95 -90.824 -33.385 208.824 1.00125.25 C ANISOU 464 CG GLU A 95 21184 16738 9667 829 -1170 511 C ATOM 465 CD GLU A 95 -89.822 -32.377 208.294 1.00126.30 C ANISOU 465 CD GLU A 95 21025 17102 9860 1168 -1034 527 C ATOM 466 OE1 GLU A 95 -90.098 -31.162 208.371 1.00125.26 O ANISOU 466 OE1 GLU A 95 20554 17192 9848 1080 -890 547 O ATOM 467 OE2 GLU A 95 -88.757 -32.802 207.798 1.00127.58 O ANISOU 467 OE2 GLU A 95 21307 17234 9933 1523 -1079 520 O ATOM 468 N VAL A 96 -94.247 -34.618 206.871 1.00118.22 N ANISOU 468 N VAL A 96 20564 15687 8666 161 -1454 272 N ATOM 469 CA VAL A 96 -94.495 -35.919 206.256 1.00126.20 C ANISOU 469 CA VAL A 96 22025 16387 9540 107 -1682 202 C ATOM 470 C VAL A 96 -94.830 -35.768 204.777 1.00132.17 C ANISOU 470 C VAL A 96 22732 17217 10270 284 -1726 74 C ATOM 471 O VAL A 96 -94.135 -36.310 203.909 1.00134.74 O ANISOU 471 O VAL A 96 23320 17377 10500 633 -1828 1 O ATOM 472 CB VAL A 96 -95.610 -36.668 207.008 1.00129.53 C ANISOU 472 CB VAL A 96 22615 16696 9902 -451 -1795 238 C ATOM 473 CG1 VAL A 96 -96.077 -37.871 206.201 1.00134.49 C ANISOU 473 CG1 VAL A 96 23687 17018 10396 -576 -2049 148 C ATOM 474 CG2 VAL A 96 -95.120 -37.106 208.374 1.00129.80 C ANISOU 474 CG2 VAL A 96 22836 16574 9907 -581 -1801 371 C ATOM 475 N VAL A 97 -95.897 -35.031 204.463 1.00133.73 N ANISOU 475 N VAL A 97 22593 17687 10531 77 -1655 36 N ATOM 476 CA VAL A 97 -96.387 -35.006 203.087 1.00134.85 C ANISOU 476 CA VAL A 97 22721 17893 10623 188 -1731 -87 C ATOM 477 C VAL A 97 -95.743 -33.921 202.228 1.00135.00 C ANISOU 477 C VAL A 97 22466 18134 10695 618 -1584 -93 C ATOM 478 O VAL A 97 -95.728 -34.052 200.996 1.00133.85 O ANISOU 478 O VAL A 97 22401 17990 10467 838 -1655 -185 O ATOM 479 CB VAL A 97 -97.919 -34.854 203.055 1.00133.57 C ANISOU 479 CB VAL A 97 22349 17935 10468 -237 -1766 -136 C ATOM 480 CG1 VAL A 97 -98.574 -35.913 203.929 1.00135.47 C ANISOU 480 CG1 VAL A 97 22844 17994 10635 -736 -1904 -102 C ATOM 481 CG2 VAL A 97 -98.330 -33.463 203.505 1.00131.68 C ANISOU 481 CG2 VAL A 97 21598 18075 10359 -257 -1556 -94 C ATOM 482 N GLY A 98 -95.212 -32.861 202.832 1.00137.30 N ANISOU 482 N GLY A 98 22456 18608 11104 724 -1390 7 N ATOM 483 CA GLY A 98 -94.528 -31.826 202.085 1.00136.90 C ANISOU 483 CA GLY A 98 22177 18746 11091 1078 -1256 35 C ATOM 484 C GLY A 98 -95.420 -30.828 201.381 1.00132.98 C ANISOU 484 C GLY A 98 21388 18497 10643 1057 -1203 0 C ATOM 485 O GLY A 98 -94.900 -29.895 200.755 1.00133.39 O ANISOU 485 O GLY A 98 21270 18694 10719 1319 -1098 47 O ATOM 486 N GLU A 99 -96.740 -30.989 201.454 1.00129.66 N ANISOU 486 N GLU A 99 20900 18145 10220 753 -1281 -73 N ATOM 487 CA GLU A 99 -97.681 -30.079 200.807 1.00127.07 C ANISOU 487 CA GLU A 99 20287 18075 9919 759 -1256 -122 C ATOM 488 C GLU A 99 -98.853 -29.860 201.748 1.00122.84 C ANISOU 488 C GLU A 99 19527 17711 9434 403 -1241 -145 C ATOM 489 O GLU A 99 -99.515 -30.822 202.148 1.00124.89 O ANISOU 489 O GLU A 99 19910 17912 9631 68 -1352 -188 O ATOM 490 CB GLU A 99 -98.172 -30.633 199.463 1.00130.18 C ANISOU 490 CB GLU A 99 20819 18460 10185 829 -1409 -237 C ATOM 491 CG GLU A 99 -97.075 -30.923 198.450 1.00130.38 C ANISOU 491 CG GLU A 99 21063 18363 10113 1205 -1428 -237 C ATOM 492 CD GLU A 99 -97.616 -31.492 197.152 1.00133.12 C ANISOU 492 CD GLU A 99 21562 18705 10313 1271 -1593 -371 C ATOM 493 OE1 GLU A 99 -98.855 -31.573 197.007 1.00134.79 O ANISOU 493 OE1 GLU A 99 21676 19026 10510 1016 -1693 -455 O ATOM 494 OE2 GLU A 99 -96.804 -31.858 196.277 1.00133.81 O ANISOU 494 OE2 GLU A 99 21850 18710 10281 1584 -1626 -400 O ATOM 495 N TRP A 100 -99.113 -28.603 202.097 1.00119.14 N ANISOU 495 N TRP A 100 18742 17462 9062 472 -1114 -118 N ATOM 496 CA TRP A 100 -100.244 -28.269 202.960 1.00119.44 C ANISOU 496 CA TRP A 100 18516 17741 9124 203 -1086 -162 C ATOM 497 C TRP A 100 -101.530 -28.410 202.157 1.00115.56 C ANISOU 497 C TRP A 100 17890 17471 8549 96 -1203 -283 C ATOM 498 O TRP A 100 -101.870 -27.548 201.345 1.00122.45 O ANISOU 498 O TRP A 100 18590 18508 9426 334 -1201 -324 O ATOM 499 CB TRP A 100 -100.092 -26.858 203.516 1.00122.09 C ANISOU 499 CB TRP A 100 18597 18222 9570 376 -938 -124 C ATOM 500 CG TRP A 100 -101.289 -26.388 204.277 1.00122.14 C ANISOU 500 CG TRP A 100 18300 18535 9572 196 -908 -200 C ATOM 501 CD1 TRP A 100 -102.325 -25.639 203.801 1.00120.97 C ANISOU 501 CD1 TRP A 100 17887 18676 9402 294 -932 -299 C ATOM 502 CD2 TRP A 100 -101.580 -26.645 205.655 1.00123.20 C ANISOU 502 CD2 TRP A 100 18352 18759 9699 -91 -849 -191 C ATOM 503 NE1 TRP A 100 -103.241 -25.409 204.799 1.00123.05 N ANISOU 503 NE1 TRP A 100 17884 19231 9639 106 -887 -365 N ATOM 504 CE2 TRP A 100 -102.807 -26.017 205.947 1.00125.35 C ANISOU 504 CE2 TRP A 100 18281 19412 9936 -147 -828 -296 C ATOM 505 CE3 TRP A 100 -100.921 -27.343 206.671 1.00121.10 C ANISOU 505 CE3 TRP A 100 18268 18311 9433 -287 -816 -104 C ATOM 506 CZ2 TRP A 100 -103.388 -26.067 207.213 1.00125.93 C ANISOU 506 CZ2 TRP A 100 18171 19714 9964 -405 -759 -317 C ATOM 507 CZ3 TRP A 100 -101.499 -27.391 207.927 1.00122.36 C ANISOU 507 CZ3 TRP A 100 18273 18664 9554 -561 -755 -110 C ATOM 508 CH2 TRP A 100 -102.720 -26.757 208.186 1.00123.42 C ANISOU 508 CH2 TRP A 100 18047 19204 9644 -624 -719 -216 C ATOM 509 N LYS A 101 -102.269 -29.492 202.398 1.00111.23 N ANISOU 509 N LYS A 101 17421 16933 7909 -284 -1318 -332 N ATOM 510 CA LYS A 101 -103.439 -29.835 201.600 1.00112.12 C ANISOU 510 CA LYS A 101 17432 17250 7918 -444 -1462 -450 C ATOM 511 C LYS A 101 -104.742 -29.374 202.244 1.00118.64 C ANISOU 511 C LYS A 101 17845 18514 8720 -685 -1427 -512 C ATOM 512 O LYS A 101 -105.778 -30.027 202.081 1.00117.75 O ANISOU 512 O LYS A 101 17648 18596 8496 -1024 -1550 -588 O ATOM 513 CB LYS A 101 -103.472 -31.341 201.342 1.00110.50 C ANISOU 513 CB LYS A 101 17594 16787 7603 -742 -1644 -474 C ATOM 514 CG LYS A 101 -102.218 -31.874 200.665 1.00105.61 C ANISOU 514 CG LYS A 101 17388 15768 6971 -451 -1696 -446 C ATOM 515 CD LYS A 101 -102.464 -33.220 200.002 1.00106.82 C ANISOU 515 CD LYS A 101 17910 15689 6985 -652 -1928 -530 C ATOM 516 CE LYS A 101 -101.292 -33.619 199.119 1.00100.64 C ANISOU 516 CE LYS A 101 17493 14590 6157 -254 -1983 -545 C ATOM 517 NZ LYS A 101 -101.590 -34.835 198.312 1.00104.88 N ANISOU 517 NZ LYS A 101 18408 14901 6541 -386 -2234 -665 N ATOM 518 N PHE A 102 -104.715 -28.260 202.973 1.00123.22 N ANISOU 518 N PHE A 102 18161 19274 9383 -516 -1271 -490 N ATOM 519 CA PHE A 102 -105.905 -27.718 203.612 1.00131.70 C ANISOU 519 CA PHE A 102 18817 20811 10414 -656 -1225 -570 C ATOM 520 C PHE A 102 -106.070 -26.250 203.231 1.00134.00 C ANISOU 520 C PHE A 102 18857 21296 10762 -206 -1163 -626 C ATOM 521 O PHE A 102 -105.251 -25.674 202.508 1.00133.86 O ANISOU 521 O PHE A 102 19001 21039 10819 153 -1152 -578 O ATOM 522 CB PHE A 102 -105.834 -27.876 205.137 1.00137.72 C ANISOU 522 CB PHE A 102 19524 21623 11180 -925 -1107 -506 C ATOM 523 CG PHE A 102 -105.979 -29.295 205.606 1.00143.96 C ANISOU 523 CG PHE A 102 20528 22295 11875 -1434 -1188 -447 C ATOM 524 CD1 PHE A 102 -107.229 -29.884 205.698 1.00149.14 C ANISOU 524 CD1 PHE A 102 20980 23300 12389 -1864 -1269 -506 C ATOM 525 CD2 PHE A 102 -104.865 -30.040 205.955 1.00145.02 C ANISOU 525 CD2 PHE A 102 21077 21975 12047 -1488 -1196 -328 C ATOM 526 CE1 PHE A 102 -107.365 -31.190 206.130 1.00153.45 C ANISOU 526 CE1 PHE A 102 21771 23700 12835 -2382 -1362 -430 C ATOM 527 CE2 PHE A 102 -104.994 -31.346 206.387 1.00148.63 C ANISOU 527 CE2 PHE A 102 21798 22269 12405 -1946 -1298 -264 C ATOM 528 CZ PHE A 102 -106.246 -31.921 206.475 1.00152.97 C ANISOU 528 CZ PHE A 102 22181 23125 12816 -2414 -1384 -307 C ATOM 529 N SER A 103 -107.151 -25.651 203.725 1.00135.37 N ANISOU 529 N SER A 103 18638 21917 10879 -227 -1131 -727 N ATOM 530 CA SER A 103 -107.548 -24.309 203.326 1.00133.95 C ANISOU 530 CA SER A 103 18224 21952 10718 207 -1119 -810 C ATOM 531 C SER A 103 -106.518 -23.277 203.779 1.00127.36 C ANISOU 531 C SER A 103 17527 20844 10021 534 -1000 -732 C ATOM 532 O SER A 103 -105.712 -23.513 204.685 1.00123.50 O ANISOU 532 O SER A 103 17192 20135 9598 398 -904 -641 O ATOM 533 CB SER A 103 -108.925 -23.965 203.895 1.00136.24 C ANISOU 533 CB SER A 103 18052 22822 10890 131 -1112 -955 C ATOM 534 OG SER A 103 -108.959 -24.143 205.300 1.00133.12 O ANISOU 534 OG SER A 103 17553 22549 10478 -126 -988 -935 O ATOM 535 N ARG A 104 -106.551 -22.113 203.125 1.00125.39 N ANISOU 535 N ARG A 104 17237 20604 9802 959 -1026 -762 N ATOM 536 CA ARG A 104 -105.657 -21.025 203.510 1.00126.04 C ANISOU 536 CA ARG A 104 17457 20431 10002 1246 -939 -690 C ATOM 537 C ARG A 104 -105.983 -20.504 204.905 1.00130.57 C ANISOU 537 C ARG A 104 17836 21197 10577 1221 -843 -764 C ATOM 538 O ARG A 104 -105.077 -20.149 205.665 1.00130.50 O ANISOU 538 O ARG A 104 17982 20941 10662 1239 -753 -687 O ATOM 539 CB ARG A 104 -105.731 -19.891 202.486 1.00126.78 C ANISOU 539 CB ARG A 104 17585 20484 10104 1680 -1015 -699 C ATOM 540 CG ARG A 104 -104.837 -18.703 202.818 1.00127.54 C ANISOU 540 CG ARG A 104 17861 20289 10310 1941 -954 -614 C ATOM 541 CD ARG A 104 -104.682 -17.743 201.645 1.00131.42 C ANISOU 541 CD ARG A 104 18498 20637 10800 2307 -1042 -558 C ATOM 542 NE ARG A 104 -103.984 -18.347 200.513 1.00135.27 N ANISOU 542 NE ARG A 104 19192 20928 11276 2260 -1068 -429 N ATOM 543 CZ ARG A 104 -104.587 -18.845 199.439 1.00137.68 C ANISOU 543 CZ ARG A 104 19447 21388 11477 2289 -1172 -474 C ATOM 544 NH1 ARG A 104 -103.869 -19.377 198.460 1.00134.13 N ANISOU 544 NH1 ARG A 104 19206 20755 11001 2272 -1189 -366 N ATOM 545 NH2 ARG A 104 -105.909 -18.808 199.340 1.00141.75 N ANISOU 545 NH2 ARG A 104 19689 22273 11896 2347 -1265 -639 N ATOM 546 N ILE A 105 -107.270 -20.450 205.260 1.00133.25 N ANISOU 546 N ILE A 105 17819 22013 10795 1185 -863 -921 N ATOM 547 CA ILE A 105 -107.648 -20.001 206.597 1.00132.42 C ANISOU 547 CA ILE A 105 17502 22160 10651 1174 -765 -1011 C ATOM 548 C ILE A 105 -107.164 -20.988 207.655 1.00128.52 C ANISOU 548 C ILE A 105 17087 21584 10162 735 -663 -919 C ATOM 549 O ILE A 105 -106.776 -20.590 208.758 1.00129.65 O ANISOU 549 O ILE A 105 17243 21687 10330 747 -564 -916 O ATOM 550 CB ILE A 105 -109.170 -19.771 206.675 1.00136.39 C ANISOU 550 CB ILE A 105 17556 23279 10985 1248 -806 -1207 C ATOM 551 CG1 ILE A 105 -109.941 -20.997 206.176 1.00139.00 C ANISOU 551 CG1 ILE A 105 17718 23896 11201 850 -874 -1215 C ATOM 552 CG2 ILE A 105 -109.562 -18.530 205.886 1.00137.41 C ANISOU 552 CG2 ILE A 105 17640 23462 11108 1792 -908 -1309 C ATOM 553 CD1 ILE A 105 -110.448 -21.904 207.280 1.00141.17 C ANISOU 553 CD1 ILE A 105 17779 24502 11359 356 -789 -1221 C ATOM 554 N HIS A 106 -107.176 -22.284 207.335 1.00124.56 N ANISOU 554 N HIS A 106 16670 21036 9622 351 -704 -843 N ATOM 555 CA HIS A 106 -106.636 -23.296 208.240 1.00119.66 C ANISOU 555 CA HIS A 106 16209 20260 8998 -56 -638 -730 C ATOM 556 C HIS A 106 -105.177 -23.003 208.576 1.00116.48 C ANISOU 556 C HIS A 106 16132 19383 8741 85 -574 -604 C ATOM 557 O HIS A 106 -104.791 -22.911 209.755 1.00117.38 O ANISOU 557 O HIS A 106 16260 19476 8863 -7 -478 -573 O ATOM 558 CB HIS A 106 -106.785 -24.671 207.581 1.00118.54 C ANISOU 558 CB HIS A 106 16210 20032 8798 -421 -742 -670 C ATOM 559 CG HIS A 106 -106.622 -25.828 208.516 1.00123.34 C ANISOU 559 CG HIS A 106 16948 20572 9344 -899 -713 -571 C ATOM 560 ND1 HIS A 106 -107.278 -27.026 208.329 1.00126.96 N ANISOU 560 ND1 HIS A 106 17422 21136 9682 -1347 -809 -555 N ATOM 561 CD2 HIS A 106 -105.866 -25.982 209.627 1.00124.43 C ANISOU 561 CD2 HIS A 106 17238 20526 9513 -1009 -617 -474 C ATOM 562 CE1 HIS A 106 -106.943 -27.863 209.294 1.00128.06 C ANISOU 562 CE1 HIS A 106 17740 21142 9778 -1714 -774 -441 C ATOM 563 NE2 HIS A 106 -106.088 -27.255 210.095 1.00126.11 N ANISOU 563 NE2 HIS A 106 17566 20730 9618 -1502 -654 -391 N ATOM 564 N CYS A 107 -104.352 -22.848 207.536 1.00111.87 N ANISOU 564 N CYS A 107 15796 18454 8256 304 -629 -529 N ATOM 565 CA CYS A 107 -102.942 -22.538 207.726 1.00109.61 C ANISOU 565 CA CYS A 107 15780 17772 8094 437 -574 -405 C ATOM 566 C CYS A 107 -102.760 -21.224 208.472 1.00106.23 C ANISOU 566 C CYS A 107 15270 17369 7725 677 -502 -448 C ATOM 567 O CYS A 107 -101.920 -21.130 209.370 1.00 99.80 O ANISOU 567 O CYS A 107 14569 16387 6964 622 -431 -381 O ATOM 568 CB CYS A 107 -102.230 -22.492 206.375 1.00112.61 C ANISOU 568 CB CYS A 107 16374 17881 8530 646 -639 -328 C ATOM 569 SG CYS A 107 -100.537 -21.873 206.460 1.00112.53 S ANISOU 569 SG CYS A 107 16617 17488 8650 837 -570 -175 S ATOM 570 N ASP A 108 -103.515 -20.190 208.093 1.00108.02 N ANISOU 570 N ASP A 108 15326 17784 7932 966 -540 -565 N ATOM 571 CA ASP A 108 -103.394 -18.897 208.762 1.00109.76 C ANISOU 571 CA ASP A 108 15520 17988 8194 1227 -505 -629 C ATOM 572 C ASP A 108 -103.676 -19.022 210.254 1.00107.90 C ANISOU 572 C ASP A 108 15134 17971 7894 1052 -413 -703 C ATOM 573 O ASP A 108 -102.927 -18.497 211.085 1.00105.64 O ANISOU 573 O ASP A 108 14965 17507 7666 1096 -360 -678 O ATOM 574 CB ASP A 108 -104.340 -17.881 208.120 1.00115.54 C ANISOU 574 CB ASP A 108 16102 18919 8880 1588 -589 -767 C ATOM 575 CG ASP A 108 -103.916 -17.492 206.720 1.00117.91 C ANISOU 575 CG ASP A 108 16600 18960 9239 1809 -678 -674 C ATOM 576 OD1 ASP A 108 -102.851 -17.963 206.267 1.00117.99 O ANISOU 576 OD1 ASP A 108 16843 18663 9323 1690 -660 -510 O ATOM 577 OD2 ASP A 108 -104.648 -16.716 206.072 1.00121.13 O ANISOU 577 OD2 ASP A 108 16928 19496 9600 2117 -770 -765 O ATOM 578 N ILE A 109 -104.749 -19.733 210.610 1.00111.08 N ANISOU 578 N ILE A 109 15270 18779 8158 826 -394 -787 N ATOM 579 CA ILE A 109 -105.133 -19.865 212.013 1.00109.23 C ANISOU 579 CA ILE A 109 14855 18830 7818 646 -297 -854 C ATOM 580 C ILE A 109 -104.048 -20.593 212.793 1.00108.11 C ANISOU 580 C ILE A 109 14953 18399 7726 360 -233 -697 C ATOM 581 O ILE A 109 -103.651 -20.170 213.888 1.00103.68 O ANISOU 581 O ILE A 109 14411 17822 7160 379 -162 -714 O ATOM 582 CB ILE A 109 -106.491 -20.581 212.131 1.00105.31 C ANISOU 582 CB ILE A 109 14009 18866 7138 392 -291 -943 C ATOM 583 CG1 ILE A 109 -107.629 -19.649 211.707 1.00100.26 C ANISOU 583 CG1 ILE A 109 13055 18628 6413 750 -340 -1144 C ATOM 584 CG2 ILE A 109 -106.712 -21.089 213.549 1.00104.13 C ANISOU 584 CG2 ILE A 109 13726 18981 6858 68 -177 -941 C ATOM 585 CD1 ILE A 109 -107.612 -18.308 212.407 1.00103.31 C ANISOU 585 CD1 ILE A 109 13401 19057 6796 1160 -310 -1286 C ATOM 586 N PHE A 110 -103.542 -21.698 212.243 1.00108.89 N ANISOU 586 N PHE A 110 15251 18262 7859 117 -272 -552 N ATOM 587 CA PHE A 110 -102.581 -22.458 213.034 1.00110.97 C ANISOU 587 CA PHE A 110 15740 18284 8142 -130 -229 -411 C ATOM 588 C PHE A 110 -101.193 -21.820 213.045 1.00107.98 C ANISOU 588 C PHE A 110 15601 17517 7910 93 -220 -328 C ATOM 589 O PHE A 110 -100.460 -21.975 214.029 1.00106.88 O ANISOU 589 O PHE A 110 15568 17267 7776 -13 -169 -263 O ATOM 590 CB PHE A 110 -102.546 -23.909 212.564 1.00116.36 C ANISOU 590 CB PHE A 110 16584 18846 8781 -452 -293 -300 C ATOM 591 CG PHE A 110 -103.627 -24.747 213.184 1.00123.35 C ANISOU 591 CG PHE A 110 17291 20082 9493 -851 -280 -322 C ATOM 592 CD1 PHE A 110 -103.508 -25.200 214.487 1.00127.59 C ANISOU 592 CD1 PHE A 110 17850 20689 9938 -1124 -207 -258 C ATOM 593 CD2 PHE A 110 -104.781 -25.043 212.483 1.00125.84 C ANISOU 593 CD2 PHE A 110 17400 20695 9719 -968 -341 -402 C ATOM 594 CE1 PHE A 110 -104.512 -25.950 215.070 1.00131.96 C ANISOU 594 CE1 PHE A 110 18234 21598 10307 -1535 -187 -254 C ATOM 595 CE2 PHE A 110 -105.786 -25.798 213.057 1.00130.07 C ANISOU 595 CE2 PHE A 110 17743 21600 10077 -1390 -328 -409 C ATOM 596 CZ PHE A 110 -105.652 -26.253 214.352 1.00133.68 C ANISOU 596 CZ PHE A 110 18234 22122 10438 -1686 -246 -326 C ATOM 597 N VAL A 111 -100.826 -21.061 212.009 1.00108.46 N ANISOU 597 N VAL A 111 15738 17398 8076 386 -269 -325 N ATOM 598 CA VAL A 111 -99.597 -20.275 212.079 1.00103.72 C ANISOU 598 CA VAL A 111 15318 16496 7595 566 -258 -250 C ATOM 599 C VAL A 111 -99.742 -19.161 213.109 1.00101.13 C ANISOU 599 C VAL A 111 14901 16261 7264 695 -219 -360 C ATOM 600 O VAL A 111 -98.791 -18.834 213.834 1.00 97.67 O ANISOU 600 O VAL A 111 14585 15647 6877 682 -192 -307 O ATOM 601 CB VAL A 111 -99.237 -19.709 210.690 1.00105.00 C ANISOU 601 CB VAL A 111 15584 16471 7839 811 -321 -201 C ATOM 602 CG1 VAL A 111 -98.079 -18.726 210.795 1.00107.88 C ANISOU 602 CG1 VAL A 111 16105 16576 8310 957 -313 -121 C ATOM 603 CG2 VAL A 111 -98.895 -20.824 209.715 1.00102.93 C ANISOU 603 CG2 VAL A 111 15448 16094 7568 712 -360 -98 C ATOM 604 N THR A 112 -100.934 -18.560 213.187 1.00106.57 N ANISOU 604 N THR A 112 15373 17244 7876 840 -228 -529 N ATOM 605 CA THR A 112 -101.212 -17.585 214.235 1.00110.39 C ANISOU 605 CA THR A 112 15770 17859 8316 991 -199 -673 C ATOM 606 C THR A 112 -101.011 -18.203 215.609 1.00112.11 C ANISOU 606 C THR A 112 15950 18195 8452 722 -110 -658 C ATOM 607 O THR A 112 -100.369 -17.610 216.483 1.00108.35 O ANISOU 607 O THR A 112 15570 17601 7998 773 -92 -678 O ATOM 608 CB THR A 112 -102.642 -17.058 214.098 1.00112.63 C ANISOU 608 CB THR A 112 15781 18529 8484 1204 -222 -874 C ATOM 609 OG1 THR A 112 -102.869 -16.605 212.758 1.00112.42 O ANISOU 609 OG1 THR A 112 15799 18399 8515 1445 -318 -872 O ATOM 610 CG2 THR A 112 -102.884 -15.911 215.067 1.00115.24 C ANISOU 610 CG2 THR A 112 16064 18962 8760 1458 -215 -1053 C ATOM 611 N LEU A 113 -101.559 -19.403 215.811 1.00115.82 N ANISOU 611 N LEU A 113 16300 18892 8813 414 -69 -617 N ATOM 612 CA LEU A 113 -101.381 -20.097 217.084 1.00115.67 C ANISOU 612 CA LEU A 113 16278 18980 8693 125 8 -569 C ATOM 613 C LEU A 113 -99.908 -20.366 217.367 1.00114.08 C ANISOU 613 C LEU A 113 16365 18384 8596 52 -1 -409 C ATOM 614 O LEU A 113 -99.441 -20.169 218.494 1.00116.40 O ANISOU 614 O LEU A 113 16696 18678 8851 6 41 -414 O ATOM 615 CB LEU A 113 -102.176 -21.402 217.087 1.00117.48 C ANISOU 615 CB LEU A 113 16392 19460 8786 -241 27 -513 C ATOM 616 CG LEU A 113 -103.697 -21.263 217.004 1.00120.90 C ANISOU 616 CG LEU A 113 16463 20405 9068 -244 49 -670 C ATOM 617 CD1 LEU A 113 -104.363 -22.630 216.968 1.00124.66 C ANISOU 617 CD1 LEU A 113 16865 21087 9412 -695 50 -579 C ATOM 618 CD2 LEU A 113 -104.223 -20.436 218.166 1.00119.08 C ANISOU 618 CD2 LEU A 113 16005 20537 8705 -107 135 -837 C ATOM 619 N ASP A 114 -99.163 -20.819 216.357 1.00111.93 N ANISOU 619 N ASP A 114 16282 17810 8437 57 -60 -275 N ATOM 620 CA ASP A 114 -97.735 -21.083 216.520 1.00108.76 C ANISOU 620 CA ASP A 114 16117 17089 8119 27 -74 -129 C ATOM 621 C ASP A 114 -97.002 -19.840 217.015 1.00106.40 C ANISOU 621 C ASP A 114 15858 16670 7898 216 -72 -171 C ATOM 622 O ASP A 114 -96.322 -19.865 218.054 1.00105.82 O ANISOU 622 O ASP A 114 15848 16557 7801 129 -50 -140 O ATOM 623 CB ASP A 114 -97.154 -21.565 215.185 1.00108.41 C ANISOU 623 CB ASP A 114 16223 16805 8163 87 -136 -16 C ATOM 624 CG ASP A 114 -95.704 -22.021 215.290 1.00109.75 C ANISOU 624 CG ASP A 114 16600 16714 8384 68 -152 133 C ATOM 625 OD1 ASP A 114 -94.863 -21.280 215.841 1.00110.49 O ANISOU 625 OD1 ASP A 114 16722 16726 8532 145 -138 149 O ATOM 626 OD2 ASP A 114 -95.401 -23.130 214.801 1.00112.17 O ANISOU 626 OD2 ASP A 114 17046 16908 8664 -14 -193 225 O ATOM 627 N VAL A 115 -97.115 -18.745 216.258 1.00105.49 N ANISOU 627 N VAL A 115 15734 16480 7868 466 -112 -236 N ATOM 628 CA VAL A 115 -96.401 -17.520 216.605 1.00102.51 C ANISOU 628 CA VAL A 115 15451 15931 7567 620 -141 -267 C ATOM 629 C VAL A 115 -96.840 -17.009 217.971 1.00106.11 C ANISOU 629 C VAL A 115 15824 16568 7927 628 -110 -422 C ATOM 630 O VAL A 115 -96.010 -16.574 218.780 1.00109.99 O ANISOU 630 O VAL A 115 16417 16938 8438 602 -121 -415 O ATOM 631 CB VAL A 115 -96.604 -16.456 215.509 1.00102.12 C ANISOU 631 CB VAL A 115 15447 15753 7599 876 -210 -302 C ATOM 632 CG1 VAL A 115 -95.880 -15.170 215.875 1.00 98.77 C ANISOU 632 CG1 VAL A 115 15175 15108 7246 990 -266 -325 C ATOM 633 CG2 VAL A 115 -96.123 -16.980 214.165 1.00100.76 C ANISOU 633 CG2 VAL A 115 15354 15436 7494 867 -232 -144 C ATOM 634 N MET A 116 -98.145 -17.064 218.257 1.00107.71 N ANISOU 634 N MET A 116 15822 17098 8004 664 -72 -572 N ATOM 635 CA MET A 116 -98.642 -16.558 219.531 1.00108.87 C ANISOU 635 CA MET A 116 15863 17481 8022 712 -33 -742 C ATOM 636 C MET A 116 -98.099 -17.364 220.699 1.00103.86 C ANISOU 636 C MET A 116 15255 16904 7304 436 30 -659 C ATOM 637 O MET A 116 -97.684 -16.794 221.712 1.00105.81 O ANISOU 637 O MET A 116 15557 17135 7511 473 29 -732 O ATOM 638 CB MET A 116 -100.170 -16.559 219.539 1.00113.63 C ANISOU 638 CB MET A 116 16186 18513 8476 800 7 -911 C ATOM 639 CG MET A 116 -100.777 -16.079 220.845 1.00119.20 C ANISOU 639 CG MET A 116 16739 19547 9003 879 63 -1106 C ATOM 640 SD MET A 116 -102.577 -16.062 220.807 1.00127.10 S ANISOU 640 SD MET A 116 17341 21157 9796 1008 117 -1312 S ATOM 641 CE MET A 116 -102.912 -17.739 220.281 1.00126.99 C ANISOU 641 CE MET A 116 17209 21294 9747 553 173 -1105 C ATOM 642 N MET A 117 -98.074 -18.692 220.573 1.00101.90 N ANISOU 642 N MET A 117 15003 16698 7017 164 66 -506 N ATOM 643 CA MET A 117 -97.605 -19.519 221.678 1.00104.80 C ANISOU 643 CA MET A 117 15429 17109 7281 -92 109 -410 C ATOM 644 C MET A 117 -96.106 -19.354 221.899 1.00103.31 C ANISOU 644 C MET A 117 15458 16593 7203 -77 57 -301 C ATOM 645 O MET A 117 -95.642 -19.331 223.045 1.00105.93 O ANISOU 645 O MET A 117 15830 16963 7455 -154 71 -304 O ATOM 646 CB MET A 117 -97.959 -20.982 221.425 1.00104.49 C ANISOU 646 CB MET A 117 15396 17140 7167 -384 128 -267 C ATOM 647 CG MET A 117 -99.449 -21.269 221.370 1.00108.81 C ANISOU 647 CG MET A 117 15691 18083 7567 -494 182 -359 C ATOM 648 SD MET A 117 -100.354 -20.634 222.792 1.00113.40 S ANISOU 648 SD MET A 117 16012 19150 7926 -475 286 -549 S ATOM 649 CE MET A 117 -102.036 -20.769 222.192 1.00116.23 C ANISOU 649 CE MET A 117 16020 19984 8158 -507 325 -668 C ATOM 650 N CYS A 118 -95.331 -19.210 220.821 1.00102.59 N ANISOU 650 N CYS A 118 15486 16218 7275 22 -5 -206 N ATOM 651 CA CYS A 118 -93.892 -19.022 221.000 1.00102.45 C ANISOU 651 CA CYS A 118 15623 15960 7345 26 -53 -102 C ATOM 652 C CYS A 118 -93.580 -17.651 221.600 1.00105.27 C ANISOU 652 C CYS A 118 16001 16264 7734 155 -89 -227 C ATOM 653 O CYS A 118 -92.725 -17.529 222.495 1.00112.65 O ANISOU 653 O CYS A 118 17004 17154 8646 85 -112 -205 O ATOM 654 CB CYS A 118 -93.173 -19.209 219.667 1.00103.08 C ANISOU 654 CB CYS A 118 15792 15818 7558 93 -97 32 C ATOM 655 SG CYS A 118 -93.357 -20.853 218.932 1.00 99.95 S ANISOU 655 SG CYS A 118 15448 15412 7117 -31 -94 166 S ATOM 656 N THR A 119 -94.261 -16.608 221.116 1.00105.53 N ANISOU 656 N THR A 119 15999 16290 7808 354 -114 -365 N ATOM 657 CA THR A 119 -94.120 -15.284 221.710 1.00107.89 C ANISOU 657 CA THR A 119 16368 16509 8116 494 -174 -515 C ATOM 658 C THR A 119 -94.536 -15.299 223.177 1.00109.84 C ANISOU 658 C THR A 119 16543 16999 8193 454 -130 -657 C ATOM 659 O THR A 119 -93.907 -14.646 224.019 1.00108.84 O ANISOU 659 O THR A 119 16517 16786 8050 459 -183 -722 O ATOM 660 CB THR A 119 -94.953 -14.277 220.914 1.00105.14 C ANISOU 660 CB THR A 119 16022 16115 7810 755 -223 -647 C ATOM 661 OG1 THR A 119 -94.568 -14.327 219.534 1.00101.16 O ANISOU 661 OG1 THR A 119 15587 15409 7440 776 -257 -495 O ATOM 662 CG2 THR A 119 -94.737 -12.871 221.429 1.00106.44 C ANISOU 662 CG2 THR A 119 16343 16112 7989 918 -324 -799 C ATOM 663 N ALA A 120 -95.589 -16.054 223.502 1.00111.00 N ANISOU 663 N ALA A 120 16511 17471 8193 391 -36 -702 N ATOM 664 CA ALA A 120 -96.003 -16.205 224.891 1.00114.13 C ANISOU 664 CA ALA A 120 16815 18159 8389 319 27 -810 C ATOM 665 C ALA A 120 -94.916 -16.873 225.717 1.00116.95 C ANISOU 665 C ALA A 120 17284 18435 8715 96 23 -663 C ATOM 666 O ALA A 120 -94.663 -16.471 226.855 1.00128.58 O ANISOU 666 O ALA A 120 18788 19985 10082 98 14 -757 O ATOM 667 CB ALA A 120 -97.303 -17.004 224.965 1.00115.34 C ANISOU 667 CB ALA A 120 16736 18708 8378 223 134 -839 C ATOM 668 N LYS A 121 -94.270 -17.900 225.163 1.00110.96 N ANISOU 668 N LYS A 121 16598 17532 8031 -69 18 -443 N ATOM 669 CA LYS A 121 -93.187 -18.572 225.877 1.00104.17 C ANISOU 669 CA LYS A 121 15854 16592 7134 -233 -7 -298 C ATOM 670 C LYS A 121 -92.069 -17.593 226.216 1.00107.65 C ANISOU 670 C LYS A 121 16399 16844 7661 -151 -98 -336 C ATOM 671 O LYS A 121 -91.616 -17.515 227.368 1.00118.19 O ANISOU 671 O LYS A 121 17769 18248 8888 -215 -118 -368 O ATOM 672 CB LYS A 121 -92.652 -19.737 225.043 1.00 94.53 C ANISOU 672 CB LYS A 121 14717 15214 5985 -338 -24 -81 C ATOM 673 N ILE A 122 -91.618 -16.822 225.225 1.00101.57 N ANISOU 673 N ILE A 122 15683 15842 7068 -33 -163 -329 N ATOM 674 CA ILE A 122 -90.467 -15.953 225.470 1.00107.59 C ANISOU 674 CA ILE A 122 16552 16418 7910 -28 -263 -331 C ATOM 675 C ILE A 122 -90.846 -14.798 226.399 1.00114.13 C ANISOU 675 C ILE A 122 17420 17281 8663 68 -307 -563 C ATOM 676 O ILE A 122 -90.056 -14.397 227.267 1.00116.86 O ANISOU 676 O ILE A 122 17842 17588 8973 2 -380 -597 O ATOM 677 CB ILE A 122 -89.861 -15.459 224.144 1.00108.76 C ANISOU 677 CB ILE A 122 16756 16324 8243 23 -319 -231 C ATOM 678 CG1 ILE A 122 -88.610 -14.618 224.416 1.00107.69 C ANISOU 678 CG1 ILE A 122 16715 16029 8172 -49 -428 -205 C ATOM 679 CG2 ILE A 122 -90.882 -14.695 223.340 1.00110.85 C ANISOU 679 CG2 ILE A 122 17023 16533 8564 201 -318 -347 C ATOM 680 CD1 ILE A 122 -87.827 -14.257 223.176 1.00109.93 C ANISOU 680 CD1 ILE A 122 17035 16130 8605 -67 -472 -57 C ATOM 681 N TRP A 123 -92.062 -14.257 226.262 1.00115.43 N ANISOU 681 N TRP A 123 17534 17539 8784 246 -276 -741 N ATOM 682 CA TRP A 123 -92.463 -13.178 227.160 1.00118.70 C ANISOU 682 CA TRP A 123 18005 17997 9098 397 -329 -992 C ATOM 683 C TRP A 123 -92.722 -13.690 228.571 1.00124.18 C ANISOU 683 C TRP A 123 18614 19001 9569 317 -260 -1068 C ATOM 684 O TRP A 123 -92.518 -12.952 229.541 1.00126.06 O ANISOU 684 O TRP A 123 18939 19244 9712 375 -326 -1234 O ATOM 685 CB TRP A 123 -93.694 -12.451 226.619 1.00117.86 C ANISOU 685 CB TRP A 123 17860 17939 8982 673 -326 -1178 C ATOM 686 CG TRP A 123 -93.387 -11.440 225.550 1.00117.89 C ANISOU 686 CG TRP A 123 18044 17582 9167 804 -449 -1170 C ATOM 687 CD1 TRP A 123 -93.805 -11.469 224.255 1.00117.82 C ANISOU 687 CD1 TRP A 123 18009 17492 9266 898 -441 -1092 C ATOM 688 CD2 TRP A 123 -92.617 -10.237 225.694 1.00118.20 C ANISOU 688 CD2 TRP A 123 18341 17289 9280 835 -610 -1234 C ATOM 689 NE1 TRP A 123 -93.336 -10.369 223.577 1.00116.72 N ANISOU 689 NE1 TRP A 123 18098 16991 9258 988 -579 -1087 N ATOM 690 CE2 TRP A 123 -92.603 -9.597 224.439 1.00118.36 C ANISOU 690 CE2 TRP A 123 18492 17028 9450 933 -689 -1169 C ATOM 691 CE3 TRP A 123 -91.934 -9.644 226.761 1.00116.84 C ANISOU 691 CE3 TRP A 123 18318 17025 9051 768 -709 -1337 C ATOM 692 CZ2 TRP A 123 -91.939 -8.390 224.222 1.00118.84 C ANISOU 692 CZ2 TRP A 123 18843 16706 9603 938 -862 -1185 C ATOM 693 CZ3 TRP A 123 -91.270 -8.448 226.541 1.00117.32 C ANISOU 693 CZ3 TRP A 123 18659 16705 9213 770 -889 -1370 C ATOM 694 CH2 TRP A 123 -91.277 -7.836 225.282 1.00118.92 C ANISOU 694 CH2 TRP A 123 19003 16618 9563 841 -964 -1286 C ATOM 695 N ASN A 124 -93.166 -14.941 228.714 1.00124.51 N ANISOU 695 N ASN A 124 18510 19293 9506 169 -139 -947 N ATOM 696 CA ASN A 124 -93.254 -15.544 230.038 1.00126.31 C ANISOU 696 CA ASN A 124 18686 19799 9508 35 -76 -957 C ATOM 697 C ASN A 124 -91.873 -15.697 230.657 1.00126.95 C ANISOU 697 C ASN A 124 18906 19724 9607 -105 -164 -845 C ATOM 698 O ASN A 124 -91.701 -15.494 231.863 1.00125.95 O ANISOU 698 O ASN A 124 18806 19734 9314 -126 -182 -943 O ATOM 699 CB ASN A 124 -93.958 -16.898 229.954 1.00123.93 C ANISOU 699 CB ASN A 124 18249 19743 9096 -149 49 -807 C ATOM 700 CG ASN A 124 -95.457 -16.789 230.146 1.00125.69 C ANISOU 700 CG ASN A 124 18262 20350 9147 -68 159 -974 C ATOM 701 OD1 ASN A 124 -95.944 -15.874 230.808 1.00129.28 O ANISOU 701 OD1 ASN A 124 18662 20979 9478 128 162 -1214 O ATOM 702 ND2 ASN A 124 -96.199 -17.725 229.564 1.00124.36 N ANISOU 702 ND2 ASN A 124 17967 20333 8952 -211 241 -856 N ATOM 703 N LEU A 125 -90.876 -16.062 229.847 1.00124.89 N ANISOU 703 N LEU A 125 18715 19213 9526 -187 -222 -646 N ATOM 704 CA LEU A 125 -89.506 -16.103 230.354 1.00120.97 C ANISOU 704 CA LEU A 125 18313 18604 9047 -292 -321 -551 C ATOM 705 C LEU A 125 -89.060 -14.723 230.830 1.00120.95 C ANISOU 705 C LEU A 125 18407 18478 9069 -220 -441 -736 C ATOM 706 O LEU A 125 -88.422 -14.590 231.885 1.00128.48 O ANISOU 706 O LEU A 125 19411 19490 9914 -292 -508 -778 O ATOM 707 CB LEU A 125 -88.561 -16.634 229.275 1.00116.38 C ANISOU 707 CB LEU A 125 17750 17826 8641 -347 -357 -328 C ATOM 708 N CYS A 126 -89.394 -13.683 230.062 1.00116.17 N ANISOU 708 N CYS A 126 17858 17686 8596 -81 -487 -849 N ATOM 709 CA CYS A 126 -89.069 -12.320 230.480 1.00114.46 C ANISOU 709 CA CYS A 126 17800 17295 8395 -15 -628 -1039 C ATOM 710 C CYS A 126 -89.756 -11.960 231.794 1.00116.89 C ANISOU 710 C CYS A 126 18120 17819 8475 96 -619 -1290 C ATOM 711 O CYS A 126 -89.136 -11.373 232.692 1.00120.25 O ANISOU 711 O CYS A 126 18663 18197 8828 54 -734 -1401 O ATOM 712 CB CYS A 126 -89.454 -11.325 229.384 1.00112.38 C ANISOU 712 CB CYS A 126 17639 16771 8290 138 -687 -1106 C ATOM 713 SG CYS A 126 -89.262 -9.589 229.865 1.00115.32 S ANISOU 713 SG CYS A 126 18294 16859 8662 245 -893 -1365 S ATOM 714 N ALA A 127 -91.043 -12.292 231.918 1.00112.97 N ANISOU 714 N ALA A 127 17488 17591 7845 233 -486 -1389 N ATOM 715 CA ALA A 127 -91.770 -12.013 233.152 1.00116.39 C ANISOU 715 CA ALA A 127 17888 18315 8021 356 -450 -1628 C ATOM 716 C ALA A 127 -91.186 -12.775 234.333 1.00120.27 C ANISOU 716 C ALA A 127 18354 19010 8334 157 -427 -1544 C ATOM 717 O ALA A 127 -91.166 -12.256 235.455 1.00125.05 O ANISOU 717 O ALA A 127 19023 19734 8756 220 -476 -1738 O ATOM 718 CB ALA A 127 -93.249 -12.359 232.975 1.00119.49 C ANISOU 718 CB ALA A 127 18074 19042 8286 502 -292 -1713 C ATOM 719 N ILE A 128 -90.698 -13.996 234.102 1.00119.52 N ANISOU 719 N ILE A 128 18190 18947 8275 -61 -367 -1264 N ATOM 720 CA ILE A 128 -90.069 -14.759 235.173 1.00120.42 C ANISOU 720 CA ILE A 128 18315 19222 8219 -235 -368 -1156 C ATOM 721 C ILE A 128 -88.768 -14.095 235.604 1.00120.24 C ANISOU 721 C ILE A 128 18435 18997 8255 -284 -547 -1188 C ATOM 722 O ILE A 128 -88.458 -14.022 236.800 1.00117.64 O ANISOU 722 O ILE A 128 18149 18817 7732 -321 -595 -1271 O ATOM 723 CB ILE A 128 -89.841 -16.213 234.723 1.00119.88 C ANISOU 723 CB ILE A 128 18194 19176 8180 -416 -295 -852 C ATOM 724 CG1 ILE A 128 -91.175 -16.946 234.585 1.00121.35 C ANISOU 724 CG1 ILE A 128 18245 19623 8242 -444 -129 -826 C ATOM 725 CG2 ILE A 128 -88.940 -16.945 235.702 1.00119.99 C ANISOU 725 CG2 ILE A 128 18272 19271 8049 -566 -347 -714 C ATOM 726 CD1 ILE A 128 -91.050 -18.343 234.012 1.00120.86 C ANISOU 726 CD1 ILE A 128 18189 19515 8218 -624 -83 -541 C ATOM 727 N SER A 129 -87.981 -13.609 234.639 1.00121.07 N ANISOU 727 N SER A 129 18605 18788 8609 -307 -651 -1115 N ATOM 728 CA SER A 129 -86.780 -12.850 234.984 1.00123.09 C ANISOU 728 CA SER A 129 18979 18868 8920 -394 -833 -1153 C ATOM 729 C SER A 129 -87.124 -11.613 235.805 1.00125.86 C ANISOU 729 C SER A 129 19475 19188 9158 -273 -934 -1469 C ATOM 730 O SER A 129 -86.432 -11.288 236.780 1.00127.48 O ANISOU 730 O SER A 129 19761 19424 9250 -352 -1055 -1554 O ATOM 731 CB SER A 129 -86.027 -12.454 233.715 1.00122.29 C ANISOU 731 CB SER A 129 18908 18471 9087 -461 -911 -1020 C ATOM 732 OG SER A 129 -86.777 -11.530 232.946 1.00124.26 O ANISOU 732 OG SER A 129 19243 18522 9449 -312 -918 -1153 O ATOM 733 N ILE A 130 -88.200 -10.918 235.433 1.00127.99 N ANISOU 733 N ILE A 130 19786 19405 9440 -55 -897 -1658 N ATOM 734 CA ILE A 130 -88.601 -9.720 236.166 1.00129.77 C ANISOU 734 CA ILE A 130 20184 19582 9541 131 -1007 -1990 C ATOM 735 C ILE A 130 -89.029 -10.077 237.584 1.00135.57 C ANISOU 735 C ILE A 130 20850 20700 9958 182 -938 -2132 C ATOM 736 O ILE A 130 -88.701 -9.370 238.545 1.00141.42 O ANISOU 736 O ILE A 130 21744 21427 10562 216 -1072 -2341 O ATOM 737 CB ILE A 130 -89.710 -8.969 235.408 1.00128.41 C ANISOU 737 CB ILE A 130 20064 19297 9431 415 -987 -2162 C ATOM 738 CG1 ILE A 130 -89.202 -8.501 234.043 1.00128.23 C ANISOU 738 CG1 ILE A 130 20153 18867 9701 350 -1080 -2016 C ATOM 739 CG2 ILE A 130 -90.210 -7.783 236.222 1.00126.86 C ANISOU 739 CG2 ILE A 130 20065 19068 9066 680 -1107 -2537 C ATOM 740 CD1 ILE A 130 -90.275 -7.892 233.168 1.00125.68 C ANISOU 740 CD1 ILE A 130 19878 18431 9444 636 -1063 -2139 C ATOM 741 N ASP A 131 -89.762 -11.182 237.740 1.00135.19 N ANISOU 741 N ASP A 131 20587 21004 9773 167 -736 -2017 N ATOM 742 CA ASP A 131 -90.192 -11.595 239.071 1.00142.94 C ANISOU 742 CA ASP A 131 21493 22393 10424 179 -652 -2113 C ATOM 743 C ASP A 131 -89.006 -12.020 239.927 1.00139.85 C ANISOU 743 C ASP A 131 21167 22018 9952 -39 -748 -1991 C ATOM 744 O ASP A 131 -88.981 -11.756 241.133 1.00141.07 O ANISOU 744 O ASP A 131 21376 22370 9855 0 -790 -2162 O ATOM 745 CB ASP A 131 -91.211 -12.730 238.968 1.00148.47 C ANISOU 745 CB ASP A 131 21960 23456 10995 137 -422 -1971 C ATOM 746 CG ASP A 131 -91.952 -12.970 240.271 1.00152.88 C ANISOU 746 CG ASP A 131 22420 24496 11174 180 -309 -2107 C ATOM 747 OD1 ASP A 131 -91.801 -12.154 241.204 1.00154.94 O ANISOU 747 OD1 ASP A 131 22793 24810 11269 316 -405 -2360 O ATOM 748 OD2 ASP A 131 -92.684 -13.977 240.363 1.00153.59 O ANISOU 748 OD2 ASP A 131 22326 24918 11113 62 -128 -1957 O ATOM 749 N ARG A 132 -88.010 -12.671 239.322 1.00136.96 N ANISOU 749 N ARG A 132 20788 21472 9778 -243 -791 -1707 N ATOM 750 CA ARG A 132 -86.805 -13.019 240.068 1.00132.39 C ANISOU 750 CA ARG A 132 20256 20917 9129 -416 -910 -1597 C ATOM 751 C ARG A 132 -86.048 -11.774 240.513 1.00133.40 C ANISOU 751 C ARG A 132 20555 20852 9280 -413 -1130 -1814 C ATOM 752 O ARG A 132 -85.573 -11.700 241.654 1.00129.57 O ANISOU 752 O ARG A 132 20125 20513 8591 -461 -1223 -1901 O ATOM 753 CB ARG A 132 -85.901 -13.914 239.218 1.00125.01 C ANISOU 753 CB ARG A 132 19257 19848 8392 -577 -920 -1271 C ATOM 754 CG ARG A 132 -86.384 -15.348 239.043 1.00121.23 C ANISOU 754 CG ARG A 132 18677 19544 7839 -630 -754 -1030 C ATOM 755 CD ARG A 132 -86.375 -16.123 240.356 1.00123.08 C ANISOU 755 CD ARG A 132 18925 20079 7761 -703 -728 -976 C ATOM 756 NE ARG A 132 -87.598 -15.937 241.131 1.00128.66 N ANISOU 756 NE ARG A 132 19596 21075 8212 -628 -601 -1159 N ATOM 757 CZ ARG A 132 -87.752 -16.342 242.388 1.00139.41 C ANISOU 757 CZ ARG A 132 20974 22742 9253 -678 -569 -1170 C ATOM 758 NH1 ARG A 132 -88.899 -16.130 243.019 1.00145.09 N ANISOU 758 NH1 ARG A 132 21625 23778 9726 -601 -437 -1344 N ATOM 759 NH2 ARG A 132 -86.759 -16.958 243.014 1.00143.20 N ANISOU 759 NH2 ARG A 132 21528 23245 9637 -790 -672 -1007 N ATOM 760 N TYR A 133 -85.928 -10.781 239.625 1.00136.31 N ANISOU 760 N TYR A 133 21029 20881 9881 -374 -1231 -1899 N ATOM 761 CA TYR A 133 -85.303 -9.520 240.016 1.00139.27 C ANISOU 761 CA TYR A 133 21619 21024 10272 -399 -1463 -2117 C ATOM 762 C TYR A 133 -86.058 -8.861 241.162 1.00142.27 C ANISOU 762 C TYR A 133 22124 21553 10378 -188 -1491 -2465 C ATOM 763 O TYR A 133 -85.444 -8.358 242.110 1.00143.36 O ANISOU 763 O TYR A 133 22398 21692 10380 -250 -1660 -2619 O ATOM 764 CB TYR A 133 -85.214 -8.574 238.816 1.00137.11 C ANISOU 764 CB TYR A 133 21481 20339 10274 -395 -1560 -2134 C ATOM 765 CG TYR A 133 -84.801 -7.160 239.179 1.00138.49 C ANISOU 765 CG TYR A 133 21953 20214 10453 -414 -1814 -2389 C ATOM 766 CD1 TYR A 133 -83.461 -6.798 239.221 1.00139.07 C ANISOU 766 CD1 TYR A 133 22098 20124 10619 -716 -2016 -2302 C ATOM 767 CD2 TYR A 133 -85.751 -6.184 239.462 1.00139.93 C ANISOU 767 CD2 TYR A 133 22352 20281 10535 -127 -1868 -2721 C ATOM 768 CE1 TYR A 133 -83.077 -5.510 239.550 1.00141.53 C ANISOU 768 CE1 TYR A 133 22716 20131 10927 -786 -2273 -2528 C ATOM 769 CE2 TYR A 133 -85.377 -4.895 239.793 1.00142.57 C ANISOU 769 CE2 TYR A 133 23023 20285 10863 -139 -2131 -2964 C ATOM 770 CZ TYR A 133 -84.039 -4.563 239.834 1.00141.67 C ANISOU 770 CZ TYR A 133 23003 19976 10849 -495 -2338 -2860 C ATOM 771 OH TYR A 133 -83.663 -3.280 240.160 1.00141.10 O ANISOU 771 OH TYR A 133 23300 19547 10766 -558 -2622 -3096 O ATOM 772 N THR A 134 -87.391 -8.846 241.090 1.00140.90 N ANISOU 772 N THR A 134 21894 21538 10102 72 -1332 -2605 N ATOM 773 CA THR A 134 -88.181 -8.249 242.162 1.00141.07 C ANISOU 773 CA THR A 134 22000 21773 9825 325 -1338 -2952 C ATOM 774 C THR A 134 -87.984 -8.996 243.475 1.00142.77 C ANISOU 774 C THR A 134 22121 22394 9733 232 -1281 -2926 C ATOM 775 O THR A 134 -87.832 -8.378 244.534 1.00144.44 O ANISOU 775 O THR A 134 22478 22678 9724 311 -1406 -3182 O ATOM 776 CB THR A 134 -89.661 -8.225 241.778 1.00138.51 C ANISOU 776 CB THR A 134 21555 21642 9432 625 -1154 -3079 C ATOM 777 OG1 THR A 134 -89.822 -7.527 240.536 1.00136.22 O ANISOU 777 OG1 THR A 134 21375 20963 9421 728 -1224 -3093 O ATOM 778 CG2 THR A 134 -90.480 -7.526 242.854 1.00140.12 C ANISOU 778 CG2 THR A 134 21831 22105 9304 943 -1164 -3471 C ATOM 779 N ALA A 135 -87.971 -10.329 243.421 1.00145.20 N ANISOU 779 N ALA A 135 22214 22948 10007 64 -1110 -2616 N ATOM 780 CA ALA A 135 -87.860 -11.125 244.638 1.00143.21 C ANISOU 780 CA ALA A 135 21891 23082 9440 -29 -1049 -2553 C ATOM 781 C ALA A 135 -86.486 -10.981 245.279 1.00141.22 C ANISOU 781 C ALA A 135 21765 22719 9175 -204 -1268 -2523 C ATOM 782 O ALA A 135 -86.371 -10.959 246.510 1.00145.32 O ANISOU 782 O ALA A 135 22333 23488 9395 -190 -1314 -2650 O ATOM 783 CB ALA A 135 -88.163 -12.591 244.330 1.00136.64 C ANISOU 783 CB ALA A 135 20862 22464 8589 -182 -844 -2207 C ATOM 784 N VAL A 136 -85.434 -10.864 244.468 1.00137.34 N ANISOU 784 N VAL A 136 21309 21892 8983 -372 -1407 -2363 N ATOM 785 CA VAL A 136 -84.084 -10.773 245.019 1.00135.16 C ANISOU 785 CA VAL A 136 21097 21564 8693 -561 -1620 -2318 C ATOM 786 C VAL A 136 -83.788 -9.356 245.493 1.00146.19 C ANISOU 786 C VAL A 136 22725 22759 10061 -523 -1853 -2657 C ATOM 787 O VAL A 136 -83.277 -9.150 246.600 1.00151.32 O ANISOU 787 O VAL A 136 23458 23547 10492 -569 -1994 -2789 O ATOM 788 CB VAL A 136 -83.048 -11.256 243.988 1.00122.85 C ANISOU 788 CB VAL A 136 19439 19808 7429 -761 -1670 -2008 C ATOM 789 CG1 VAL A 136 -81.638 -11.045 244.516 1.00128.63 C ANISOU 789 CG1 VAL A 136 20198 20532 8144 -955 -1906 -1984 C ATOM 790 CG2 VAL A 136 -83.275 -12.723 243.660 1.00127.31 C ANISOU 790 CG2 VAL A 136 19835 20558 7981 -782 -1476 -1691 C ATOM 791 N ALA A 137 -84.106 -8.358 244.668 1.00149.38 N ANISOU 791 N ALA A 137 23268 22816 10674 -438 -1916 -2804 N ATOM 792 CA ALA A 137 -83.775 -6.978 245.006 1.00156.61 C ANISOU 792 CA ALA A 137 24474 23446 11584 -426 -2176 -3113 C ATOM 793 C ALA A 137 -84.695 -6.446 246.098 1.00160.80 C ANISOU 793 C ALA A 137 25145 24165 11788 -129 -2172 -3489 C ATOM 794 O ALA A 137 -84.229 -5.892 247.101 1.00168.09 O ANISOU 794 O ALA A 137 26242 25106 12521 -154 -2366 -3710 O ATOM 795 CB ALA A 137 -83.850 -6.100 243.758 1.00158.59 C ANISOU 795 CB ALA A 137 24877 23235 12144 -423 -2257 -3131 C ATOM 796 N MET A 138 -86.010 -6.604 245.922 1.00160.56 N ANISOU 796 N MET A 138 25027 24311 11667 163 -1957 -3577 N ATOM 797 CA MET A 138 -87.013 -6.043 246.826 1.00162.36 C ANISOU 797 CA MET A 138 25354 24765 11572 510 -1931 -3956 C ATOM 798 C MET A 138 -87.849 -7.194 247.378 1.00159.85 C ANISOU 798 C MET A 138 24734 25022 10979 582 -1635 -3841 C ATOM 799 O MET A 138 -88.943 -7.481 246.868 1.00154.03 O ANISOU 799 O MET A 138 23829 24459 10238 759 -1422 -3824 O ATOM 800 CB MET A 138 -87.900 -5.030 246.103 1.00163.44 C ANISOU 800 CB MET A 138 25660 24625 11817 831 -1963 -4208 C ATOM 801 CG MET A 138 -87.153 -3.872 245.457 1.00168.33 C ANISOU 801 CG MET A 138 26627 24623 12708 733 -2262 -4293 C ATOM 802 SD MET A 138 -86.322 -2.784 246.627 1.00179.69 S ANISOU 802 SD MET A 138 28460 25852 13964 676 -2619 -4635 S ATOM 803 CE MET A 138 -85.565 -1.610 245.504 1.00177.38 C ANISOU 803 CE MET A 138 28541 24807 14048 468 -2925 -4615 C ATOM 804 N PRO A 139 -87.377 -7.866 248.433 1.00163.18 N ANISOU 804 N PRO A 139 25086 25763 11150 433 -1623 -3754 N ATOM 805 CA PRO A 139 -88.147 -8.983 249.001 1.00166.61 C ANISOU 805 CA PRO A 139 25267 26708 11330 438 -1346 -3595 C ATOM 806 C PRO A 139 -89.363 -8.553 249.806 1.00180.86 C ANISOU 806 C PRO A 139 27021 28740 12959 712 -1197 -3842 C ATOM 807 O PRO A 139 -90.085 -9.423 250.307 1.00178.89 O ANISOU 807 O PRO A 139 26548 28839 12583 677 -952 -3669 O ATOM 808 CB PRO A 139 -87.123 -9.695 249.905 1.00159.23 C ANISOU 808 CB PRO A 139 24333 25890 10278 178 -1420 -3390 C ATOM 809 CG PRO A 139 -85.783 -9.082 249.573 1.00155.88 C ANISOU 809 CG PRO A 139 24087 25091 10048 16 -1721 -3416 C ATOM 810 CD PRO A 139 -86.080 -7.698 249.105 1.00159.80 C ANISOU 810 CD PRO A 139 24801 25224 10692 210 -1864 -3747 C ATOM 811 N MET A 140 -89.607 -7.255 249.952 1.00193.60 N ANISOU 811 N MET A 140 28840 30163 14556 983 -1347 -4232 N ATOM 812 CA MET A 140 -90.729 -6.762 250.743 1.00203.04 C ANISOU 812 CA MET A 140 29973 31601 15572 1290 -1221 -4496 C ATOM 813 C MET A 140 -92.069 -7.189 250.147 1.00204.11 C ANISOU 813 C MET A 140 29809 32004 15740 1451 -940 -4419 C ATOM 814 O MET A 140 -92.154 -7.531 248.967 1.00200.37 O ANISOU 814 O MET A 140 29257 31412 15464 1389 -892 -4249 O ATOM 815 CB MET A 140 -90.660 -5.239 250.872 1.00211.71 C ANISOU 815 CB MET A 140 31396 32359 16687 1572 -1476 -4930 C ATOM 816 CG MET A 140 -90.853 -4.487 249.568 1.00216.94 C ANISOU 816 CG MET A 140 32214 32620 17592 1753 -1593 -5047 C ATOM 817 SD MET A 140 -90.371 -2.756 249.719 1.00224.30 S ANISOU 817 SD MET A 140 33662 32980 18583 1963 -1988 -5486 S ATOM 818 CE MET A 140 -88.593 -2.914 249.873 1.00221.95 C ANISOU 818 CE MET A 140 33581 32411 18338 1480 -2273 -5327 C ATOM 819 N SER A 148 -100.763 -9.353 246.838 1.00211.30 N ANISOU 819 N SER A 148 28379 35277 16630 2295 537 -4181 N ATOM 820 CA SER A 148 -99.484 -9.622 246.193 1.00201.97 C ANISOU 820 CA SER A 148 27527 33555 15659 2018 390 -3983 C ATOM 821 C SER A 148 -99.672 -10.388 244.886 1.00189.30 C ANISOU 821 C SER A 148 25784 31890 14251 1803 466 -3715 C ATOM 822 O SER A 148 -98.801 -10.366 244.016 1.00187.29 O ANISOU 822 O SER A 148 25773 31187 14201 1702 328 -3616 O ATOM 823 CB SER A 148 -98.563 -10.403 247.133 1.00207.14 C ANISOU 823 CB SER A 148 28306 34188 16212 1634 394 -3747 C ATOM 824 OG SER A 148 -99.148 -11.635 247.514 1.00211.69 O ANISOU 824 OG SER A 148 28580 35190 16665 1316 621 -3451 O ATOM 825 N LYS A 149 -100.813 -11.066 244.750 1.00181.33 N ANISOU 825 N LYS A 149 24374 31354 13168 1723 678 -3600 N ATOM 826 CA LYS A 149 -101.089 -11.832 243.541 1.00164.68 C ANISOU 826 CA LYS A 149 22120 29224 11227 1504 752 -3354 C ATOM 827 C LYS A 149 -101.637 -10.970 242.411 1.00165.56 C ANISOU 827 C LYS A 149 22199 29225 11480 1894 676 -3578 C ATOM 828 O LYS A 149 -101.734 -11.450 241.273 1.00164.48 O ANISOU 828 O LYS A 149 22002 28988 11505 1754 696 -3405 O ATOM 829 CB LYS A 149 -102.074 -12.961 243.858 1.00156.09 C ANISOU 829 CB LYS A 149 20625 28688 9994 1199 989 -3124 C ATOM 830 CG LYS A 149 -102.034 -14.128 242.883 1.00148.76 C ANISOU 830 CG LYS A 149 19634 27671 9216 787 1052 -2766 C ATOM 831 N ARG A 150 -101.988 -9.712 242.694 1.00169.68 N ANISOU 831 N ARG A 150 22787 29740 11942 2393 574 -3959 N ATOM 832 CA ARG A 150 -102.492 -8.836 241.643 1.00174.94 C ANISOU 832 CA ARG A 150 23475 30255 12739 2812 470 -4177 C ATOM 833 C ARG A 150 -101.425 -8.600 240.584 1.00178.24 C ANISOU 833 C ARG A 150 24286 30033 13402 2748 279 -4097 C ATOM 834 O ARG A 150 -101.717 -8.606 239.383 1.00176.68 O ANISOU 834 O ARG A 150 24047 29730 13353 2822 261 -4049 O ATOM 835 CB ARG A 150 -102.963 -7.511 242.242 1.00175.65 C ANISOU 835 CB ARG A 150 23639 30386 12714 3380 357 -4600 C ATOM 836 N ARG A 151 -100.178 -8.401 241.017 1.00182.21 N ANISOU 836 N ARG A 151 25159 30134 13938 2603 130 -4076 N ATOM 837 CA ARG A 151 -99.069 -8.255 240.079 1.00180.14 C ANISOU 837 CA ARG A 151 25247 29312 13886 2489 -54 -3969 C ATOM 838 C ARG A 151 -98.899 -9.503 239.222 1.00177.95 C ANISOU 838 C ARG A 151 24807 29083 13721 2083 70 -3586 C ATOM 839 O ARG A 151 -98.602 -9.410 238.026 1.00176.52 O ANISOU 839 O ARG A 151 24736 28479 13856 2053 -14 -3452 O ATOM 840 CB ARG A 151 -97.787 -7.948 240.853 1.00181.03 C ANISOU 840 CB ARG A 151 25712 29098 13974 2350 -225 -3997 C ATOM 841 CG ARG A 151 -96.563 -7.686 239.997 1.00178.38 C ANISOU 841 CG ARG A 151 25709 28084 13983 2169 -430 -3832 C ATOM 842 CD ARG A 151 -95.360 -7.393 240.878 1.00178.57 C ANISOU 842 CD ARG A 151 26016 27846 13985 2001 -598 -3857 C ATOM 843 NE ARG A 151 -95.070 -8.501 241.784 1.00177.62 N ANISOU 843 NE ARG A 151 25718 28103 13666 1677 -454 -3657 N ATOM 844 CZ ARG A 151 -94.223 -9.489 241.515 1.00174.17 C ANISOU 844 CZ ARG A 151 25250 27532 13396 1265 -424 -3282 C ATOM 845 NH1 ARG A 151 -94.026 -10.454 242.403 1.00175.33 N ANISOU 845 NH1 ARG A 151 25276 28015 13325 1016 -314 -3118 N ATOM 846 NH2 ARG A 151 -93.573 -9.514 240.360 1.00169.62 N ANISOU 846 NH2 ARG A 151 24771 26493 13183 1122 -511 -3073 N ATOM 847 N VAL A 152 -99.101 -10.682 239.814 1.00177.00 N ANISOU 847 N VAL A 152 24432 29322 13498 1717 264 -3335 N ATOM 848 CA VAL A 152 -98.951 -11.928 239.069 1.00168.69 C ANISOU 848 CA VAL A 152 23264 28280 12549 1316 365 -2966 C ATOM 849 C VAL A 152 -100.024 -12.038 237.994 1.00169.20 C ANISOU 849 C VAL A 152 23074 28530 12684 1432 453 -2969 C ATOM 850 O VAL A 152 -99.738 -12.367 236.833 1.00166.78 O ANISOU 850 O VAL A 152 22824 27899 12645 1304 412 -2773 O ATOM 851 CB VAL A 152 -98.997 -13.127 240.032 1.00162.52 C ANISOU 851 CB VAL A 152 22325 27798 11629 914 525 -2706 C ATOM 852 CG1 VAL A 152 -98.523 -14.395 239.338 1.00157.62 C ANISOU 852 CG1 VAL A 152 21721 27034 11132 491 564 -2316 C ATOM 853 CG2 VAL A 152 -98.179 -12.831 241.274 1.00160.63 C ANISOU 853 CG2 VAL A 152 22291 27472 11267 901 441 -2778 C ATOM 854 N THR A 153 -101.278 -11.772 238.371 1.00172.31 N ANISOU 854 N THR A 153 23159 29371 12940 1656 568 -3153 N ATOM 855 CA THR A 153 -102.363 -11.775 237.394 1.00176.42 C ANISOU 855 CA THR A 153 23403 30122 13505 1810 633 -3194 C ATOM 856 C THR A 153 -102.102 -10.761 236.287 1.00177.13 C ANISOU 856 C THR A 153 23747 29788 13765 2190 442 -3371 C ATOM 857 O THR A 153 -102.325 -11.046 235.102 1.00174.40 O ANISOU 857 O THR A 153 23338 29338 13587 2144 440 -3243 O ATOM 858 CB THR A 153 -103.694 -11.485 238.089 1.00179.07 C ANISOU 858 CB THR A 153 23353 31045 13641 2057 758 -3407 C ATOM 859 OG1 THR A 153 -103.984 -12.530 239.026 1.00177.39 O ANISOU 859 OG1 THR A 153 22895 31242 13262 1653 940 -3199 O ATOM 860 CG2 THR A 153 -104.824 -11.397 237.073 1.00179.96 C ANISOU 860 CG2 THR A 153 23155 31432 13789 2261 800 -3478 C ATOM 861 N VAL A 154 -101.604 -9.578 236.658 1.00179.17 N ANISOU 861 N VAL A 154 24326 29724 14025 2537 262 -3639 N ATOM 862 CA VAL A 154 -101.328 -8.532 235.678 1.00178.86 C ANISOU 862 CA VAL A 154 24592 29132 14235 2860 49 -3762 C ATOM 863 C VAL A 154 -100.276 -8.999 234.681 1.00174.69 C ANISOU 863 C VAL A 154 24267 28016 14092 2488 -25 -3404 C ATOM 864 O VAL A 154 -100.443 -8.846 233.467 1.00173.32 O ANISOU 864 O VAL A 154 24118 27595 14140 2569 -79 -3328 O ATOM 865 CB VAL A 154 -100.901 -7.231 236.382 1.00182.47 C ANISOU 865 CB VAL A 154 25416 29292 14621 3224 -155 -4092 C ATOM 866 CG1 VAL A 154 -100.245 -6.282 235.394 1.00181.99 C ANISOU 866 CG1 VAL A 154 25774 28479 14894 3369 -406 -4096 C ATOM 867 CG2 VAL A 154 -102.105 -6.561 237.026 1.00186.86 C ANISOU 867 CG2 VAL A 154 25760 30286 14953 3696 -113 -4437 C ATOM 868 N MET A 155 -99.173 -9.567 235.175 1.00172.90 N ANISOU 868 N MET A 155 24180 27585 13930 2100 -32 -3186 N ATOM 869 CA MET A 155 -98.114 -10.004 234.268 1.00157.91 C ANISOU 869 CA MET A 155 22454 25176 12367 1781 -103 -2863 C ATOM 870 C MET A 155 -98.584 -11.136 233.359 1.00143.98 C ANISOU 870 C MET A 155 20435 23581 10691 1547 42 -2598 C ATOM 871 O MET A 155 -98.275 -11.142 232.161 1.00144.99 O ANISOU 871 O MET A 155 20653 23350 11087 1510 -22 -2446 O ATOM 872 CB MET A 155 -96.879 -10.429 235.064 1.00156.19 C ANISOU 872 CB MET A 155 22396 24791 12156 1451 -141 -2703 C ATOM 873 CG MET A 155 -96.292 -9.325 235.929 1.00159.41 C ANISOU 873 CG MET A 155 23087 24988 12493 1628 -314 -2954 C ATOM 874 SD MET A 155 -94.858 -9.851 236.886 1.00158.04 S ANISOU 874 SD MET A 155 23057 24687 12303 1244 -370 -2771 S ATOM 875 CE MET A 155 -93.590 -9.861 235.622 1.00155.21 C ANISOU 875 CE MET A 155 22894 23722 12357 1008 -509 -2481 C ATOM 876 N ILE A 156 -99.335 -12.099 233.903 1.00136.31 N ANISOU 876 N ILE A 156 19157 23155 9480 1369 231 -2536 N ATOM 877 CA ILE A 156 -99.830 -13.205 233.081 1.00126.72 C ANISOU 877 CA ILE A 156 17723 22098 8326 1111 350 -2293 C ATOM 878 C ILE A 156 -100.730 -12.680 231.965 1.00129.41 C ANISOU 878 C ILE A 156 17938 22471 8760 1408 327 -2418 C ATOM 879 O ILE A 156 -100.561 -13.019 230.777 1.00127.21 O ANISOU 879 O ILE A 156 17697 21917 8718 1309 292 -2236 O ATOM 880 CB ILE A 156 -100.561 -14.240 233.957 1.00121.15 C ANISOU 880 CB ILE A 156 16727 22000 7304 840 543 -2218 C ATOM 881 CG1 ILE A 156 -99.562 -15.006 234.827 1.00121.48 C ANISOU 881 CG1 ILE A 156 16935 21927 7293 488 550 -2002 C ATOM 882 CG2 ILE A 156 -101.362 -15.202 233.091 1.00116.65 C ANISOU 882 CG2 ILE A 156 15910 21654 6756 615 648 -2038 C ATOM 883 CD1 ILE A 156 -100.187 -16.118 235.642 1.00111.58 C ANISOU 883 CD1 ILE A 156 15458 21206 5729 153 726 -1864 C ATOM 884 N SER A 157 -101.671 -11.800 232.326 1.00132.37 N ANISOU 884 N SER A 157 18176 23182 8937 1817 330 -2746 N ATOM 885 CA SER A 157 -102.572 -11.256 231.321 1.00137.37 C ANISOU 885 CA SER A 157 18683 23884 9626 2157 291 -2886 C ATOM 886 C SER A 157 -101.811 -10.414 230.311 1.00140.84 C ANISOU 886 C SER A 157 19491 23634 10388 2336 88 -2864 C ATOM 887 O SER A 157 -102.136 -10.431 229.121 1.00141.14 O ANISOU 887 O SER A 157 19489 23554 10582 2406 54 -2790 O ATOM 888 CB SER A 157 -103.673 -10.435 231.991 1.00139.89 C ANISOU 888 CB SER A 157 18796 24716 9638 2625 317 -3269 C ATOM 889 OG SER A 157 -104.557 -11.269 232.721 1.00140.05 O ANISOU 889 OG SER A 157 18394 25477 9340 2436 529 -3264 O ATOM 890 N ILE A 158 -100.802 -9.663 230.760 1.00141.00 N ANISOU 890 N ILE A 158 19872 23207 10493 2392 -56 -2922 N ATOM 891 CA ILE A 158 -100.059 -8.825 229.827 1.00140.35 C ANISOU 891 CA ILE A 158 20152 22480 10694 2510 -253 -2882 C ATOM 892 C ILE A 158 -99.339 -9.706 228.818 1.00138.29 C ANISOU 892 C ILE A 158 19912 21942 10690 2128 -226 -2516 C ATOM 893 O ILE A 158 -99.310 -9.409 227.618 1.00136.75 O ANISOU 893 O ILE A 158 19817 21455 10689 2219 -307 -2437 O ATOM 894 CB ILE A 158 -99.084 -7.906 230.587 1.00139.37 C ANISOU 894 CB ILE A 158 20404 21959 10590 2564 -419 -3003 C ATOM 895 CG1 ILE A 158 -99.832 -6.717 231.193 1.00142.96 C ANISOU 895 CG1 ILE A 158 20952 22529 10836 3083 -521 -3411 C ATOM 896 CG2 ILE A 158 -97.966 -7.424 229.672 1.00136.38 C ANISOU 896 CG2 ILE A 158 20380 20917 10521 2438 -592 -2821 C ATOM 897 CD1 ILE A 158 -98.937 -5.751 231.938 1.00145.71 C ANISOU 897 CD1 ILE A 158 21713 22462 11189 3143 -716 -3563 C ATOM 898 N VAL A 159 -98.739 -10.801 229.296 1.00138.49 N ANISOU 898 N VAL A 159 19861 22058 10702 1718 -121 -2294 N ATOM 899 CA VAL A 159 -98.039 -11.726 228.408 1.00130.65 C ANISOU 899 CA VAL A 159 18892 20831 9919 1388 -97 -1965 C ATOM 900 C VAL A 159 -98.975 -12.213 227.310 1.00127.38 C ANISOU 900 C VAL A 159 18264 20593 9543 1426 -30 -1904 C ATOM 901 O VAL A 159 -98.677 -12.100 226.112 1.00125.46 O ANISOU 901 O VAL A 159 18129 20031 9508 1447 -100 -1781 O ATOM 902 CB VAL A 159 -97.445 -12.901 229.205 1.00123.58 C ANISOU 902 CB VAL A 159 17941 20071 8944 1001 1 -1766 C ATOM 903 CG1 VAL A 159 -96.970 -13.992 228.258 1.00118.87 C ANISOU 903 CG1 VAL A 159 17340 19311 8515 721 33 -1459 C ATOM 904 CG2 VAL A 159 -96.292 -12.424 230.070 1.00119.33 C ANISOU 904 CG2 VAL A 159 17639 19286 8416 943 -100 -1786 C ATOM 905 N TRP A 160 -100.139 -12.745 227.707 1.00126.94 N ANISOU 905 N TRP A 160 17887 21080 9264 1424 105 -1991 N ATOM 906 CA TRP A 160 -101.033 -13.315 226.696 1.00126.68 C ANISOU 906 CA TRP A 160 17625 21256 9250 1401 163 -1924 C ATOM 907 C TRP A 160 -101.634 -12.243 225.788 1.00128.30 C ANISOU 907 C TRP A 160 17852 21368 9528 1833 55 -2104 C ATOM 908 O TRP A 160 -101.781 -12.463 224.577 1.00126.78 O ANISOU 908 O TRP A 160 17647 21044 9480 1828 23 -1989 O ATOM 909 CB TRP A 160 -102.128 -14.155 227.355 1.00128.40 C ANISOU 909 CB TRP A 160 17473 22120 9193 1234 329 -1957 C ATOM 910 CG TRP A 160 -101.589 -15.321 228.129 1.00126.04 C ANISOU 910 CG TRP A 160 17192 21882 8816 781 421 -1736 C ATOM 911 CD1 TRP A 160 -101.476 -15.432 229.482 1.00131.01 C ANISOU 911 CD1 TRP A 160 17796 22751 9229 681 491 -1784 C ATOM 912 CD2 TRP A 160 -101.074 -16.542 227.583 1.00121.19 C ANISOU 912 CD2 TRP A 160 16660 21065 8322 394 435 -1433 C ATOM 913 NE1 TRP A 160 -100.929 -16.648 229.815 1.00130.86 N ANISOU 913 NE1 TRP A 160 17846 22684 9191 248 543 -1514 N ATOM 914 CE2 TRP A 160 -100.672 -17.348 228.666 1.00124.07 C ANISOU 914 CE2 TRP A 160 17063 21541 8537 78 504 -1302 C ATOM 915 CE3 TRP A 160 -100.916 -17.032 226.283 1.00117.42 C ANISOU 915 CE3 TRP A 160 16246 20321 8048 307 386 -1268 C ATOM 916 CZ2 TRP A 160 -100.124 -18.617 228.490 1.00120.21 C ANISOU 916 CZ2 TRP A 160 16700 20876 8099 -301 511 -1016 C ATOM 917 CZ3 TRP A 160 -100.372 -18.293 226.110 1.00116.47 C ANISOU 917 CZ3 TRP A 160 16237 20043 7974 -64 400 -1001 C ATOM 918 CH2 TRP A 160 -99.982 -19.070 227.207 1.00117.54 C ANISOU 918 CH2 TRP A 160 16433 20265 7962 -355 454 -879 C ATOM 919 N VAL A 161 -101.968 -11.074 226.340 1.00128.68 N ANISOU 919 N VAL A 161 17964 21462 9466 2230 -20 -2392 N ATOM 920 CA VAL A 161 -102.523 -9.989 225.532 1.00121.43 C ANISOU 920 CA VAL A 161 17126 20414 8597 2692 -154 -2573 C ATOM 921 C VAL A 161 -101.517 -9.535 224.484 1.00113.98 C ANISOU 921 C VAL A 161 16554 18808 7946 2666 -306 -2398 C ATOM 922 O VAL A 161 -101.855 -9.364 223.307 1.00108.92 O ANISOU 922 O VAL A 161 15922 18052 7410 2810 -367 -2351 O ATOM 923 CB VAL A 161 -102.973 -8.822 226.428 1.00120.78 C ANISOU 923 CB VAL A 161 17112 20455 8322 3146 -231 -2930 C ATOM 924 CG1 VAL A 161 -103.218 -7.577 225.592 1.00122.73 C ANISOU 924 CG1 VAL A 161 17607 20365 8659 3629 -432 -3088 C ATOM 925 CG2 VAL A 161 -104.238 -9.195 227.182 1.00122.20 C ANISOU 925 CG2 VAL A 161 16840 21412 8180 3260 -73 -3126 C ATOM 926 N LEU A 162 -100.263 -9.331 224.895 1.00113.75 N ANISOU 926 N LEU A 162 16822 18367 8033 2471 -369 -2294 N ATOM 927 CA LEU A 162 -99.239 -8.894 223.953 1.00113.59 C ANISOU 927 CA LEU A 162 17128 17768 8262 2396 -502 -2110 C ATOM 928 C LEU A 162 -98.977 -9.955 222.893 1.00113.87 C ANISOU 928 C LEU A 162 17050 17776 8440 2108 -422 -1818 C ATOM 929 O LEU A 162 -98.774 -9.627 221.718 1.00112.57 O ANISOU 929 O LEU A 162 17026 17318 8426 2176 -506 -1708 O ATOM 930 CB LEU A 162 -97.954 -8.540 224.701 1.00110.46 C ANISOU 930 CB LEU A 162 17009 17030 7930 2199 -578 -2059 C ATOM 931 CG LEU A 162 -96.708 -8.286 223.853 1.00106.74 C ANISOU 931 CG LEU A 162 16817 16043 7696 1996 -685 -1817 C ATOM 932 CD1 LEU A 162 -96.940 -7.139 222.881 1.00104.61 C ANISOU 932 CD1 LEU A 162 16804 15428 7515 2290 -852 -1874 C ATOM 933 CD2 LEU A 162 -95.528 -7.983 224.753 1.00108.75 C ANISOU 933 CD2 LEU A 162 17276 16071 7971 1782 -756 -1794 C ATOM 934 N SER A 163 -98.970 -11.233 223.282 1.00114.66 N ANISOU 934 N SER A 163 16924 18164 8479 1788 -272 -1687 N ATOM 935 CA SER A 163 -98.731 -12.279 222.291 1.00111.77 C ANISOU 935 CA SER A 163 16488 17750 8229 1539 -216 -1433 C ATOM 936 C SER A 163 -99.853 -12.322 221.257 1.00116.24 C ANISOU 936 C SER A 163 16879 18507 8779 1727 -214 -1484 C ATOM 937 O SER A 163 -99.594 -12.402 220.046 1.00112.13 O ANISOU 937 O SER A 163 16446 17755 8403 1722 -263 -1340 O ATOM 938 CB SER A 163 -98.583 -13.632 222.984 1.00102.58 C ANISOU 938 CB SER A 163 15170 16832 6975 1178 -84 -1300 C ATOM 939 OG SER A 163 -97.552 -13.589 223.952 1.00 93.81 O ANISOU 939 OG SER A 163 14212 15570 5862 1030 -97 -1257 O ATOM 940 N PHE A 164 -101.108 -12.248 221.714 1.00119.31 N ANISOU 940 N PHE A 164 17004 19355 8975 1906 -161 -1696 N ATOM 941 CA PHE A 164 -102.229 -12.216 220.779 1.00121.38 C ANISOU 941 CA PHE A 164 17064 19856 9198 2114 -175 -1772 C ATOM 942 C PHE A 164 -102.187 -10.972 219.899 1.00124.68 C ANISOU 942 C PHE A 164 17722 19925 9727 2504 -341 -1847 C ATOM 943 O PHE A 164 -102.515 -11.036 218.710 1.00129.72 O ANISOU 943 O PHE A 164 18337 20516 10436 2588 -388 -1777 O ATOM 944 CB PHE A 164 -103.554 -12.295 221.536 1.00127.58 C ANISOU 944 CB PHE A 164 17480 21272 9722 2246 -86 -2001 C ATOM 945 CG PHE A 164 -104.761 -12.306 220.639 1.00134.14 C ANISOU 945 CG PHE A 164 18042 22440 10486 2452 -102 -2092 C ATOM 946 CD1 PHE A 164 -105.092 -13.440 219.915 1.00131.50 C ANISOU 946 CD1 PHE A 164 17518 22277 10169 2140 -42 -1924 C ATOM 947 CD2 PHE A 164 -105.566 -11.185 220.524 1.00139.48 C ANISOU 947 CD2 PHE A 164 18668 23262 11066 2972 -197 -2356 C ATOM 948 CE1 PHE A 164 -106.201 -13.454 219.089 1.00129.79 C ANISOU 948 CE1 PHE A 164 17037 22397 9880 2313 -71 -2012 C ATOM 949 CE2 PHE A 164 -106.678 -11.194 219.702 1.00140.76 C ANISOU 949 CE2 PHE A 164 18559 23774 11151 3186 -225 -2445 C ATOM 950 CZ PHE A 164 -106.995 -12.330 218.983 1.00134.85 C ANISOU 950 CZ PHE A 164 17592 23220 10424 2839 -159 -2271 C ATOM 951 N THR A 165 -101.788 -9.829 220.464 1.00125.22 N ANISOU 951 N THR A 165 18050 19728 9799 2739 -448 -1987 N ATOM 952 CA THR A 165 -101.671 -8.611 219.667 1.00122.07 C ANISOU 952 CA THR A 165 17962 18922 9499 3080 -633 -2035 C ATOM 953 C THR A 165 -100.616 -8.765 218.579 1.00117.70 C ANISOU 953 C THR A 165 17645 17911 9165 2844 -680 -1738 C ATOM 954 O THR A 165 -100.827 -8.349 217.434 1.00123.84 O ANISOU 954 O THR A 165 18529 18515 10008 3027 -776 -1686 O ATOM 955 CB THR A 165 -101.338 -7.422 220.568 1.00122.85 C ANISOU 955 CB THR A 165 18354 18771 9554 3311 -757 -2231 C ATOM 956 OG1 THR A 165 -102.317 -7.321 221.610 1.00129.95 O ANISOU 956 OG1 THR A 165 19007 20153 10214 3555 -698 -2522 O ATOM 957 CG2 THR A 165 -101.327 -6.130 219.764 1.00119.32 C ANISOU 957 CG2 THR A 165 18276 17878 9181 3674 -977 -2287 C ATOM 958 N ILE A 166 -99.472 -9.359 218.923 1.00111.87 N ANISOU 958 N ILE A 166 16982 17004 8520 2454 -616 -1543 N ATOM 959 CA ILE A 166 -98.405 -9.549 217.945 1.00110.26 C ANISOU 959 CA ILE A 166 16961 16438 8494 2231 -645 -1266 C ATOM 960 C ILE A 166 -98.859 -10.495 216.840 1.00114.19 C ANISOU 960 C ILE A 166 17260 17112 9012 2162 -574 -1135 C ATOM 961 O ILE A 166 -98.554 -10.287 215.659 1.00116.15 O ANISOU 961 O ILE A 166 17646 17127 9360 2196 -637 -990 O ATOM 962 CB ILE A 166 -97.129 -10.058 218.641 1.00104.69 C ANISOU 962 CB ILE A 166 16322 15606 7850 1864 -589 -1111 C ATOM 963 CG1 ILE A 166 -96.529 -8.961 219.524 1.00101.98 C ANISOU 963 CG1 ILE A 166 16239 15002 7507 1916 -703 -1222 C ATOM 964 CG2 ILE A 166 -96.109 -10.536 217.618 1.00101.10 C ANISOU 964 CG2 ILE A 166 15951 14924 7538 1632 -579 -826 C ATOM 965 CD1 ILE A 166 -95.232 -9.357 220.195 1.00 98.22 C ANISOU 965 CD1 ILE A 166 15821 14415 7082 1569 -673 -1076 C ATOM 966 N SER A 167 -99.611 -11.536 217.198 1.00118.37 N ANISOU 966 N SER A 167 17479 18064 9435 2050 -452 -1182 N ATOM 967 CA SER A 167 -99.975 -12.562 216.227 1.00126.30 C ANISOU 967 CA SER A 167 18318 19220 10451 1920 -397 -1057 C ATOM 968 C SER A 167 -101.275 -12.277 215.480 1.00144.74 C ANISOU 968 C SER A 167 20483 21803 12708 2212 -446 -1196 C ATOM 969 O SER A 167 -101.594 -13.010 214.538 1.00145.24 O ANISOU 969 O SER A 167 20437 21966 12783 2126 -431 -1102 O ATOM 970 CB SER A 167 -100.071 -13.922 216.919 1.00116.77 C ANISOU 970 CB SER A 167 16903 18302 9164 1583 -264 -1002 C ATOM 971 OG SER A 167 -98.828 -14.256 217.505 1.00108.87 O ANISOU 971 OG SER A 167 16062 17074 8230 1340 -235 -859 O ATOM 972 N CYS A 168 -102.029 -11.250 215.878 1.00152.13 N ANISOU 972 N CYS A 168 21399 22854 13550 2574 -516 -1429 N ATOM 973 CA CYS A 168 -103.279 -10.899 215.201 1.00155.82 C ANISOU 973 CA CYS A 168 21689 23593 13921 2915 -581 -1582 C ATOM 974 C CYS A 168 -103.193 -10.822 213.678 1.00155.87 C ANISOU 974 C CYS A 168 21821 23375 14026 2996 -671 -1437 C ATOM 975 O CYS A 168 -104.063 -11.407 213.013 1.00158.19 O ANISOU 975 O CYS A 168 21862 23992 14252 3013 -658 -1459 O ATOM 976 CB CYS A 168 -103.796 -9.569 215.767 1.00161.97 C ANISOU 976 CB CYS A 168 22559 24378 14604 3375 -689 -1845 C ATOM 977 SG CYS A 168 -104.983 -9.731 217.115 1.00168.53 S ANISOU 977 SG CYS A 168 22977 25882 15175 3504 -583 -2144 S ATOM 978 N PRO A 169 -102.223 -10.125 213.066 1.00150.36 N ANISOU 978 N PRO A 169 21492 22171 13467 3035 -768 -1287 N ATOM 979 CA PRO A 169 -102.296 -9.910 211.606 1.00143.46 C ANISOU 979 CA PRO A 169 20734 21134 12642 3174 -863 -1169 C ATOM 980 C PRO A 169 -102.421 -11.182 210.780 1.00144.26 C ANISOU 980 C PRO A 169 20632 21432 12750 2925 -782 -1033 C ATOM 981 O PRO A 169 -102.974 -11.136 209.675 1.00143.61 O ANISOU 981 O PRO A 169 20516 21410 12639 3096 -855 -1019 O ATOM 982 CB PRO A 169 -100.986 -9.171 211.300 1.00134.45 C ANISOU 982 CB PRO A 169 20005 19442 11636 3098 -936 -977 C ATOM 983 CG PRO A 169 -100.633 -8.497 212.566 1.00135.12 C ANISOU 983 CG PRO A 169 20225 19397 11717 3117 -956 -1099 C ATOM 984 CD PRO A 169 -101.050 -9.445 213.647 1.00141.77 C ANISOU 984 CD PRO A 169 20731 20661 12476 2945 -806 -1217 C ATOM 985 N LEU A 170 -101.930 -12.316 211.283 1.00142.56 N ANISOU 985 N LEU A 170 20307 21303 12557 2540 -650 -938 N ATOM 986 CA LEU A 170 -101.938 -13.546 210.496 1.00141.36 C ANISOU 986 CA LEU A 170 20040 21261 12409 2298 -599 -809 C ATOM 987 C LEU A 170 -103.353 -14.061 210.250 1.00140.57 C ANISOU 987 C LEU A 170 19610 21626 12176 2356 -603 -957 C ATOM 988 O LEU A 170 -103.655 -14.552 209.157 1.00142.67 O ANISOU 988 O LEU A 170 19831 21948 12430 2342 -644 -898 O ATOM 989 CB LEU A 170 -101.087 -14.612 211.184 1.00142.28 C ANISOU 989 CB LEU A 170 20165 21331 12564 1907 -484 -685 C ATOM 990 CG LEU A 170 -99.591 -14.312 211.265 1.00143.71 C ANISOU 990 CG LEU A 170 20624 21111 12868 1806 -478 -511 C ATOM 991 CD1 LEU A 170 -98.890 -15.304 212.178 1.00145.82 C ANISOU 991 CD1 LEU A 170 20870 21396 13140 1484 -379 -435 C ATOM 992 CD2 LEU A 170 -98.977 -14.331 209.873 1.00140.43 C ANISOU 992 CD2 LEU A 170 20368 20472 12518 1835 -522 -333 C ATOM 993 N LEU A 171 -104.236 -13.961 211.247 1.00133.61 N ANISOU 993 N LEU A 171 18478 21116 11172 2412 -564 -1152 N ATOM 994 CA LEU A 171 -105.598 -14.452 211.065 1.00127.37 C ANISOU 994 CA LEU A 171 17317 20847 10230 2429 -563 -1292 C ATOM 995 C LEU A 171 -106.436 -13.543 210.175 1.00135.55 C ANISOU 995 C LEU A 171 18299 21992 11211 2881 -700 -1419 C ATOM 996 O LEU A 171 -107.487 -13.974 209.688 1.00135.53 O ANISOU 996 O LEU A 171 17998 22404 11094 2900 -728 -1505 O ATOM 997 CB LEU A 171 -106.282 -14.627 212.424 1.00115.69 C ANISOU 997 CB LEU A 171 15547 19808 8601 2343 -464 -1455 C ATOM 998 CG LEU A 171 -106.645 -13.369 213.220 1.00111.44 C ANISOU 998 CG LEU A 171 14989 19367 7985 2753 -495 -1674 C ATOM 999 CD1 LEU A 171 -108.107 -12.982 213.021 1.00108.56 C ANISOU 999 CD1 LEU A 171 14266 19546 7436 3094 -549 -1909 C ATOM 1000 CD2 LEU A 171 -106.336 -13.560 214.697 1.00112.97 C ANISOU 1000 CD2 LEU A 171 15143 19659 8120 2553 -374 -1714 C ATOM 1001 N PHE A 172 -106.002 -12.303 209.952 1.00139.80 N ANISOU 1001 N PHE A 172 19132 22168 11818 3233 -802 -1427 N ATOM 1002 CA PHE A 172 -106.727 -11.360 209.111 1.00144.26 C ANISOU 1002 CA PHE A 172 19722 22768 12324 3705 -960 -1533 C ATOM 1003 C PHE A 172 -106.356 -11.474 207.636 1.00145.86 C ANISOU 1003 C PHE A 172 20117 22703 12602 3705 -1043 -1344 C ATOM 1004 O PHE A 172 -106.579 -10.525 206.876 1.00148.96 O ANISOU 1004 O PHE A 172 20682 22941 12977 4089 -1192 -1363 O ATOM 1005 CB PHE A 172 -106.505 -9.930 209.608 1.00149.34 C ANISOU 1005 CB PHE A 172 20646 23119 12977 4098 -1061 -1640 C ATOM 1006 CG PHE A 172 -107.140 -9.650 210.940 1.00152.34 C ANISOU 1006 CG PHE A 172 20806 23849 13225 4244 -1011 -1892 C ATOM 1007 CD1 PHE A 172 -108.519 -9.656 211.076 1.00155.73 C ANISOU 1007 CD1 PHE A 172 20828 24882 13459 4511 -1025 -2131 C ATOM 1008 CD2 PHE A 172 -106.363 -9.381 212.053 1.00151.16 C ANISOU 1008 CD2 PHE A 172 20837 23469 13127 4120 -952 -1898 C ATOM 1009 CE1 PHE A 172 -109.111 -9.400 212.297 1.00160.07 C ANISOU 1009 CE1 PHE A 172 21148 25817 13854 4664 -966 -2371 C ATOM 1010 CE2 PHE A 172 -106.949 -9.124 213.279 1.00154.80 C ANISOU 1010 CE2 PHE A 172 21100 24278 13440 4271 -903 -2140 C ATOM 1011 CZ PHE A 172 -108.325 -9.133 213.401 1.00159.98 C ANISOU 1011 CZ PHE A 172 21343 25552 13889 4550 -904 -2376 C ATOM 1012 N GLY A 173 -105.802 -12.609 207.214 1.00142.94 N ANISOU 1012 N GLY A 173 19741 22274 12294 3303 -960 -1167 N ATOM 1013 CA GLY A 173 -105.462 -12.806 205.821 1.00138.26 C ANISOU 1013 CA GLY A 173 19309 21481 11742 3303 -1027 -1002 C ATOM 1014 C GLY A 173 -104.192 -12.133 205.352 1.00131.32 C ANISOU 1014 C GLY A 173 18846 20066 10985 3331 -1056 -795 C ATOM 1015 O GLY A 173 -103.913 -12.151 204.148 1.00127.61 O ANISOU 1015 O GLY A 173 18520 19445 10520 3374 -1114 -654 O ATOM 1016 N LEU A 174 -103.412 -11.537 206.257 1.00127.13 N ANISOU 1016 N LEU A 174 18505 19265 10533 3290 -1021 -768 N ATOM 1017 CA LEU A 174 -102.144 -10.938 205.857 1.00123.50 C ANISOU 1017 CA LEU A 174 18417 18330 10179 3237 -1044 -552 C ATOM 1018 C LEU A 174 -101.119 -11.983 205.434 1.00119.87 C ANISOU 1018 C LEU A 174 17986 17778 9782 2877 -935 -341 C ATOM 1019 O LEU A 174 -100.185 -11.655 204.694 1.00120.88 O ANISOU 1019 O LEU A 174 18354 17619 9955 2838 -953 -140 O ATOM 1020 CB LEU A 174 -101.583 -10.082 206.995 1.00124.46 C ANISOU 1020 CB LEU A 174 18720 18211 10360 3246 -1048 -593 C ATOM 1021 CG LEU A 174 -100.314 -9.276 206.705 1.00124.64 C ANISOU 1021 CG LEU A 174 19129 17752 10476 3166 -1096 -379 C ATOM 1022 CD1 LEU A 174 -100.528 -8.345 205.522 1.00128.48 C ANISOU 1022 CD1 LEU A 174 19865 18028 10926 3450 -1253 -298 C ATOM 1023 CD2 LEU A 174 -99.872 -8.495 207.931 1.00125.21 C ANISOU 1023 CD2 LEU A 174 19362 17619 10591 3151 -1119 -458 C ATOM 1024 N ASN A 175 -101.280 -13.231 205.865 1.00116.13 N ANISOU 1024 N ASN A 175 17282 17550 9292 2620 -832 -382 N ATOM 1025 CA ASN A 175 -100.418 -14.320 205.412 1.00106.89 C ANISOU 1025 CA ASN A 175 16151 16309 8154 2341 -753 -215 C ATOM 1026 C ASN A 175 -100.957 -14.822 204.079 1.00108.16 C ANISOU 1026 C ASN A 175 16260 16596 8239 2420 -813 -197 C ATOM 1027 O ASN A 175 -101.910 -15.603 204.034 1.00108.01 O ANISOU 1027 O ASN A 175 16020 16874 8146 2363 -823 -319 O ATOM 1028 CB ASN A 175 -100.369 -15.438 206.447 1.00 96.65 C ANISOU 1028 CB ASN A 175 14699 15167 6855 2044 -649 -262 C ATOM 1029 CG ASN A 175 -99.331 -16.492 206.115 1.00 93.32 C ANISOU 1029 CG ASN A 175 14377 14618 6464 1806 -586 -98 C ATOM 1030 OD1 ASN A 175 -98.193 -16.174 205.772 1.00 94.48 O ANISOU 1030 OD1 ASN A 175 14705 14525 6667 1803 -569 61 O ATOM 1031 ND2 ASN A 175 -99.723 -17.757 206.210 1.00 93.07 N ANISOU 1031 ND2 ASN A 175 14230 14754 6377 1606 -562 -138 N ATOM 1032 N ASN A 176 -100.344 -14.375 202.983 1.00108.24 N ANISOU 1032 N ASN A 176 16475 16398 8254 2529 -856 -37 N ATOM 1033 CA ASN A 176 -100.778 -14.758 201.641 1.00113.78 C ANISOU 1033 CA ASN A 176 17160 17205 8866 2632 -923 -13 C ATOM 1034 C ASN A 176 -99.911 -15.919 201.163 1.00115.80 C ANISOU 1034 C ASN A 176 17465 17417 9115 2408 -848 110 C ATOM 1035 O ASN A 176 -98.965 -15.759 200.391 1.00116.54 O ANISOU 1035 O ASN A 176 17733 17346 9201 2425 -829 285 O ATOM 1036 CB ASN A 176 -100.706 -13.564 200.693 1.00111.97 C ANISOU 1036 CB ASN A 176 17136 16800 8606 2909 -1025 89 C ATOM 1037 CG ASN A 176 -101.675 -13.681 199.533 1.00110.38 C ANISOU 1037 CG ASN A 176 16858 16796 8284 3119 -1136 29 C ATOM 1038 OD1 ASN A 176 -102.055 -14.783 199.136 1.00110.33 O ANISOU 1038 OD1 ASN A 176 16698 17003 8220 3002 -1128 -31 O ATOM 1039 ND2 ASN A 176 -102.081 -12.543 198.983 1.00110.02 N ANISOU 1039 ND2 ASN A 176 16945 16666 8190 3431 -1262 43 N ATOM 1040 N ALA A 177 -100.254 -17.111 201.641 1.00112.57 N ANISOU 1040 N ALA A 177 16910 17174 8690 2198 -811 13 N ATOM 1041 CA ALA A 177 -99.526 -18.318 201.283 1.00107.75 C ANISOU 1041 CA ALA A 177 16375 16510 8056 2017 -767 91 C ATOM 1042 C ALA A 177 -100.006 -18.838 199.936 1.00104.63 C ANISOU 1042 C ALA A 177 15989 16217 7549 2108 -854 70 C ATOM 1043 O ALA A 177 -101.203 -18.809 199.634 1.00108.58 O ANISOU 1043 O ALA A 177 16342 16928 7985 2180 -944 -62 O ATOM 1044 CB ALA A 177 -99.703 -19.392 202.356 1.00109.00 C ANISOU 1044 CB ALA A 177 16439 16749 8227 1743 -721 8 C ATOM 1045 N ASP A 178 -99.066 -19.313 199.123 1.00100.73 N ANISOU 1045 N ASP A 178 15654 15607 7012 2116 -830 191 N ATOM 1046 CA ASP A 178 -99.425 -19.890 197.837 1.00100.98 C ANISOU 1046 CA ASP A 178 15723 15729 6917 2204 -916 162 C ATOM 1047 C ASP A 178 -100.161 -21.213 198.048 1.00 95.45 C ANISOU 1047 C ASP A 178 14951 15147 6168 1998 -976 10 C ATOM 1048 O ASP A 178 -100.311 -21.706 199.170 1.00 90.42 O ANISOU 1048 O ASP A 178 14248 14519 5589 1776 -940 -46 O ATOM 1049 CB ASP A 178 -98.182 -20.084 196.972 1.00104.34 C ANISOU 1049 CB ASP A 178 16330 16035 7280 2283 -865 319 C ATOM 1050 CG ASP A 178 -98.465 -19.883 195.495 1.00103.96 C ANISOU 1050 CG ASP A 178 16340 16070 7092 2491 -945 344 C ATOM 1051 OD1 ASP A 178 -99.640 -20.013 195.091 1.00102.21 O ANISOU 1051 OD1 ASP A 178 16026 15998 6810 2540 -1062 208 O ATOM 1052 OD2 ASP A 178 -97.513 -19.600 194.737 1.00103.85 O ANISOU 1052 OD2 ASP A 178 16447 16002 7008 2600 -893 501 O ATOM 1053 N GLN A 179 -100.631 -21.792 196.948 1.00 98.64 N ANISOU 1053 N GLN A 179 15387 15642 6450 2050 -1081 -52 N ATOM 1054 CA GLN A 179 -101.404 -23.022 197.026 1.00 99.04 C ANISOU 1054 CA GLN A 179 15400 15794 6437 1819 -1174 -197 C ATOM 1055 C GLN A 179 -100.541 -24.179 197.515 1.00 97.47 C ANISOU 1055 C GLN A 179 15392 15393 6248 1628 -1136 -166 C ATOM 1056 O GLN A 179 -99.396 -24.348 197.085 1.00100.63 O ANISOU 1056 O GLN A 179 15976 15630 6626 1757 -1087 -68 O ATOM 1057 CB GLN A 179 -102.009 -23.357 195.663 1.00103.11 C ANISOU 1057 CB GLN A 179 15942 16429 6806 1928 -1314 -273 C ATOM 1058 CG GLN A 179 -102.888 -22.258 195.088 1.00109.05 C ANISOU 1058 CG GLN A 179 16522 17390 7520 2159 -1380 -304 C ATOM 1059 CD GLN A 179 -103.373 -22.573 193.687 1.00116.02 C ANISOU 1059 CD GLN A 179 17447 18393 8241 2286 -1524 -367 C ATOM 1060 OE1 GLN A 179 -102.768 -23.373 192.973 1.00117.16 O ANISOU 1060 OE1 GLN A 179 17797 18419 8299 2284 -1549 -352 O ATOM 1061 NE2 GLN A 179 -104.474 -21.947 193.287 1.00118.68 N ANISOU 1061 NE2 GLN A 179 17590 18984 8519 2426 -1629 -451 N ATOM 1062 N ASN A 180 -101.106 -24.976 198.424 1.00 95.95 N ANISOU 1062 N ASN A 180 15152 15234 6071 1323 -1164 -248 N ATOM 1063 CA ASN A 180 -100.461 -26.174 198.963 1.00 94.94 C ANISOU 1063 CA ASN A 180 15241 14897 5936 1122 -1167 -230 C ATOM 1064 C ASN A 180 -99.127 -25.870 199.643 1.00 95.44 C ANISOU 1064 C ASN A 180 15398 14777 6089 1214 -1030 -95 C ATOM 1065 O ASN A 180 -98.229 -26.716 199.675 1.00 97.91 O ANISOU 1065 O ASN A 180 15934 14898 6368 1215 -1035 -57 O ATOM 1066 CB ASN A 180 -100.284 -27.243 197.881 1.00 94.65 C ANISOU 1066 CB ASN A 180 15454 14742 5766 1157 -1297 -285 C ATOM 1067 CG ASN A 180 -101.601 -27.869 197.465 1.00 96.36 C ANISOU 1067 CG ASN A 180 15615 15112 5887 939 -1461 -431 C ATOM 1068 OD1 ASN A 180 -102.631 -27.195 197.404 1.00 94.80 O ANISOU 1068 OD1 ASN A 180 15139 15189 5692 922 -1480 -489 O ATOM 1069 ND2 ASN A 180 -101.576 -29.166 197.180 1.00 97.65 N ANISOU 1069 ND2 ASN A 180 16047 15104 5952 776 -1597 -497 N ATOM 1070 N GLU A 181 -98.985 -24.668 200.196 1.00 95.02 N ANISOU 1070 N GLU A 181 15181 14786 6138 1302 -923 -31 N ATOM 1071 CA GLU A 181 -97.854 -24.329 201.047 1.00 95.63 C ANISOU 1071 CA GLU A 181 15303 14727 6304 1319 -804 84 C ATOM 1072 C GLU A 181 -98.371 -23.608 202.283 1.00 99.12 C ANISOU 1072 C GLU A 181 15558 15264 6839 1198 -743 59 C ATOM 1073 O GLU A 181 -99.405 -22.933 202.240 1.00102.40 O ANISOU 1073 O GLU A 181 15791 15861 7256 1232 -769 -23 O ATOM 1074 CB GLU A 181 -96.808 -23.466 200.318 1.00 93.77 C ANISOU 1074 CB GLU A 181 15113 14438 6079 1580 -736 215 C ATOM 1075 CG GLU A 181 -97.225 -22.030 200.050 1.00 90.18 C ANISOU 1075 CG GLU A 181 14530 14066 5670 1723 -719 245 C ATOM 1076 CD GLU A 181 -96.038 -21.136 199.736 1.00 87.24 C ANISOU 1076 CD GLU A 181 14219 13607 5322 1866 -636 416 C ATOM 1077 OE1 GLU A 181 -94.909 -21.660 199.629 1.00 84.32 O ANISOU 1077 OE1 GLU A 181 13942 13177 4918 1876 -582 502 O ATOM 1078 OE2 GLU A 181 -96.230 -19.909 199.601 1.00 85.09 O ANISOU 1078 OE2 GLU A 181 13908 13334 5088 1967 -634 466 O ATOM 1079 N CYS A 182 -97.650 -23.771 203.394 1.00 99.78 N ANISOU 1079 N CYS A 182 15686 15245 6982 1083 -668 117 N ATOM 1080 CA CYS A 182 -98.049 -23.186 204.675 1.00102.79 C ANISOU 1080 CA CYS A 182 15912 15717 7429 966 -607 84 C ATOM 1081 C CYS A 182 -96.800 -22.714 205.410 1.00101.94 C ANISOU 1081 C CYS A 182 15868 15464 7400 1004 -518 194 C ATOM 1082 O CYS A 182 -96.109 -23.514 206.048 1.00100.65 O ANISOU 1082 O CYS A 182 15815 15198 7228 884 -500 243 O ATOM 1083 CB CYS A 182 -98.840 -24.177 205.516 1.00105.51 C ANISOU 1083 CB CYS A 182 16216 16157 7717 661 -636 9 C ATOM 1084 SG CYS A 182 -99.457 -23.483 207.061 1.00110.37 S ANISOU 1084 SG CYS A 182 16605 16968 8363 532 -552 -52 S ATOM 1085 N ILE A 183 -96.529 -21.413 205.322 1.00105.10 N ANISOU 1085 N ILE A 183 16214 15852 7867 1166 -480 234 N ATOM 1086 CA ILE A 183 -95.395 -20.789 205.997 1.00105.96 C ANISOU 1086 CA ILE A 183 16365 15844 8049 1174 -410 335 C ATOM 1087 C ILE A 183 -95.808 -19.379 206.395 1.00105.75 C ANISOU 1087 C ILE A 183 16259 15836 8086 1260 -406 294 C ATOM 1088 O ILE A 183 -96.958 -18.976 206.179 1.00110.62 O ANISOU 1088 O ILE A 183 16777 16575 8680 1344 -452 182 O ATOM 1089 CB ILE A 183 -94.158 -20.748 205.083 1.00104.46 C ANISOU 1089 CB ILE A 183 16287 15558 7846 1296 -390 481 C ATOM 1090 CG1 ILE A 183 -94.584 -20.363 203.671 1.00 99.26 C ANISOU 1090 CG1 ILE A 183 15642 14936 7137 1470 -436 491 C ATOM 1091 CG2 ILE A 183 -93.424 -22.075 205.078 1.00104.72 C ANISOU 1091 CG2 ILE A 183 16424 15550 7816 1250 -390 515 C ATOM 1092 CD1 ILE A 183 -93.457 -20.333 202.688 1.00 99.49 C ANISOU 1092 CD1 ILE A 183 15756 14934 7112 1587 -405 636 C ATOM 1093 N ILE A 184 -94.880 -18.620 206.976 1.00102.79 N ANISOU 1093 N ILE A 184 15933 15345 7778 1252 -366 374 N ATOM 1094 CA ILE A 184 -95.033 -17.173 207.049 1.00103.93 C ANISOU 1094 CA ILE A 184 16096 15419 7974 1370 -394 362 C ATOM 1095 C ILE A 184 -94.534 -16.635 205.712 1.00111.87 C ANISOU 1095 C ILE A 184 17208 16330 8968 1500 -420 501 C ATOM 1096 O ILE A 184 -93.333 -16.462 205.509 1.00109.04 O ANISOU 1096 O ILE A 184 16925 15884 8623 1445 -384 656 O ATOM 1097 CB ILE A 184 -94.276 -16.568 208.232 1.00 97.34 C ANISOU 1097 CB ILE A 184 15297 14485 7204 1270 -364 384 C ATOM 1098 CG1 ILE A 184 -94.883 -17.025 209.560 1.00 95.00 C ANISOU 1098 CG1 ILE A 184 14892 14313 6888 1158 -336 243 C ATOM 1099 CG2 ILE A 184 -94.307 -15.043 208.156 1.00 96.14 C ANISOU 1099 CG2 ILE A 184 15245 14186 7097 1394 -425 387 C ATOM 1100 CD1 ILE A 184 -94.237 -18.269 210.139 1.00 93.49 C ANISOU 1100 CD1 ILE A 184 14700 14151 6672 970 -285 299 C ATOM 1101 N ALA A 185 -95.460 -16.379 204.790 1.00120.52 N ANISOU 1101 N ALA A 185 18294 17481 10018 1666 -485 450 N ATOM 1102 CA ALA A 185 -95.116 -16.094 203.403 1.00124.87 C ANISOU 1102 CA ALA A 185 18944 17984 10517 1787 -511 582 C ATOM 1103 C ALA A 185 -94.671 -14.656 203.172 1.00128.35 C ANISOU 1103 C ALA A 185 19533 18243 10990 1856 -549 702 C ATOM 1104 O ALA A 185 -94.501 -14.260 202.014 1.00136.91 O ANISOU 1104 O ALA A 185 20716 19291 12014 1956 -580 826 O ATOM 1105 CB ALA A 185 -96.304 -16.420 202.492 1.00127.90 C ANISOU 1105 CB ALA A 185 19267 18508 10821 1937 -584 480 C ATOM 1106 N ASN A 186 -94.482 -13.869 204.226 1.00124.24 N ANISOU 1106 N ASN A 186 19060 17599 10548 1795 -559 673 N ATOM 1107 CA ASN A 186 -94.110 -12.468 204.086 1.00122.21 C ANISOU 1107 CA ASN A 186 19002 17115 10318 1832 -628 778 C ATOM 1108 C ASN A 186 -92.786 -12.219 204.795 1.00123.87 C ANISOU 1108 C ASN A 186 19265 17215 10586 1592 -576 904 C ATOM 1109 O ASN A 186 -92.709 -12.387 206.025 1.00131.88 O ANISOU 1109 O ASN A 186 20213 18240 11655 1492 -552 797 O ATOM 1110 CB ASN A 186 -95.204 -11.560 204.653 1.00123.34 C ANISOU 1110 CB ASN A 186 19198 17184 10482 2024 -735 596 C ATOM 1111 CG ASN A 186 -95.089 -10.131 204.163 1.00128.24 C ANISOU 1111 CG ASN A 186 20100 17528 11099 2139 -858 697 C ATOM 1112 OD1 ASN A 186 -94.007 -9.669 203.801 1.00128.39 O ANISOU 1112 OD1 ASN A 186 20278 17378 11125 1972 -852 914 O ATOM 1113 ND2 ASN A 186 -96.212 -9.422 204.144 1.00131.31 N ANISOU 1113 ND2 ASN A 186 20554 17878 11458 2426 -981 544 N ATOM 1114 N PRO A 187 -91.726 -11.832 204.082 1.00120.04 N ANISOU 1114 N PRO A 187 18878 16659 10071 1478 -559 1132 N ATOM 1115 CA PRO A 187 -90.452 -11.549 204.764 1.00123.60 C ANISOU 1115 CA PRO A 187 19345 17052 10563 1222 -520 1253 C ATOM 1116 C PRO A 187 -90.531 -10.360 205.704 1.00132.21 C ANISOU 1116 C PRO A 187 20610 17894 11730 1164 -622 1194 C ATOM 1117 O PRO A 187 -89.852 -10.350 206.740 1.00130.51 O ANISOU 1117 O PRO A 187 20357 17666 11564 978 -602 1178 O ATOM 1118 CB PRO A 187 -89.481 -11.291 203.601 1.00122.76 C ANISOU 1118 CB PRO A 187 19292 16978 10374 1122 -487 1517 C ATOM 1119 CG PRO A 187 -90.124 -11.937 202.409 1.00121.04 C ANISOU 1119 CG PRO A 187 19028 16899 10064 1334 -468 1507 C ATOM 1120 CD PRO A 187 -91.597 -11.774 202.617 1.00119.52 C ANISOU 1120 CD PRO A 187 18874 16631 9908 1556 -560 1293 C ATOM 1121 N ALA A 188 -91.338 -9.349 205.369 1.00137.76 N ANISOU 1121 N ALA A 188 21522 18390 12429 1339 -749 1151 N ATOM 1122 CA ALA A 188 -91.483 -8.195 206.250 1.00141.47 C ANISOU 1122 CA ALA A 188 22211 18588 12955 1336 -875 1062 C ATOM 1123 C ALA A 188 -92.080 -8.604 207.590 1.00140.78 C ANISOU 1123 C ALA A 188 21978 18603 12909 1406 -853 800 C ATOM 1124 O ALA A 188 -91.631 -8.143 208.647 1.00146.83 O ANISOU 1124 O ALA A 188 22819 19249 13719 1271 -889 746 O ATOM 1125 CB ALA A 188 -92.343 -7.125 205.579 1.00144.70 C ANISOU 1125 CB ALA A 188 22892 18759 13328 1593 -1034 1043 C ATOM 1126 N PHE A 189 -93.098 -9.469 207.567 1.00129.50 N ANISOU 1126 N PHE A 189 20340 17415 11450 1592 -799 638 N ATOM 1127 CA PHE A 189 -93.649 -9.969 208.820 1.00120.59 C ANISOU 1127 CA PHE A 189 19043 16445 10330 1613 -756 417 C ATOM 1128 C PHE A 189 -92.649 -10.852 209.552 1.00113.70 C ANISOU 1128 C PHE A 189 18030 15686 9484 1338 -644 483 C ATOM 1129 O PHE A 189 -92.644 -10.879 210.785 1.00114.25 O ANISOU 1129 O PHE A 189 18057 15786 9566 1274 -634 358 O ATOM 1130 CB PHE A 189 -94.950 -10.732 208.573 1.00121.33 C ANISOU 1130 CB PHE A 189 18928 16805 10365 1811 -726 258 C ATOM 1131 CG PHE A 189 -95.638 -11.176 209.836 1.00122.86 C ANISOU 1131 CG PHE A 189 18942 17204 10536 1819 -681 40 C ATOM 1132 CD1 PHE A 189 -96.407 -10.286 210.569 1.00124.65 C ANISOU 1132 CD1 PHE A 189 19219 17408 10735 2025 -762 -163 C ATOM 1133 CD2 PHE A 189 -95.512 -12.478 210.292 1.00120.15 C ANISOU 1133 CD2 PHE A 189 18396 17080 10176 1630 -564 40 C ATOM 1134 CE1 PHE A 189 -97.039 -10.688 211.732 1.00121.86 C ANISOU 1134 CE1 PHE A 189 18675 17300 10327 2029 -706 -358 C ATOM 1135 CE2 PHE A 189 -96.142 -12.886 211.453 1.00116.85 C ANISOU 1135 CE2 PHE A 189 17820 16866 9712 1601 -519 -132 C ATOM 1136 CZ PHE A 189 -96.906 -11.990 212.174 1.00117.82 C ANISOU 1136 CZ PHE A 189 17952 17018 9796 1793 -578 -330 C ATOM 1137 N VAL A 190 -91.796 -11.571 208.817 1.00110.35 N ANISOU 1137 N VAL A 190 17538 15342 9050 1204 -567 671 N ATOM 1138 CA VAL A 190 -90.720 -12.327 209.455 1.00111.12 C ANISOU 1138 CA VAL A 190 17523 15541 9156 984 -483 745 C ATOM 1139 C VAL A 190 -89.818 -11.391 210.249 1.00114.91 C ANISOU 1139 C VAL A 190 18122 15857 9682 802 -537 793 C ATOM 1140 O VAL A 190 -89.478 -11.658 211.408 1.00114.19 O ANISOU 1140 O VAL A 190 17964 15820 9603 689 -518 720 O ATOM 1141 CB VAL A 190 -89.922 -13.122 208.406 1.00109.59 C ANISOU 1141 CB VAL A 190 17251 15472 8916 934 -407 930 C ATOM 1142 CG1 VAL A 190 -88.628 -13.645 209.008 1.00106.63 C ANISOU 1142 CG1 VAL A 190 16781 15196 8538 740 -347 1024 C ATOM 1143 CG2 VAL A 190 -90.756 -14.267 207.858 1.00107.19 C ANISOU 1143 CG2 VAL A 190 16839 15327 8561 1077 -365 849 C ATOM 1144 N VAL A 191 -89.433 -10.267 209.639 1.00120.18 N ANISOU 1144 N VAL A 191 18986 16314 10361 754 -620 922 N ATOM 1145 CA VAL A 191 -88.562 -9.307 210.314 1.00123.07 C ANISOU 1145 CA VAL A 191 19501 16496 10764 532 -700 979 C ATOM 1146 C VAL A 191 -89.267 -8.715 211.530 1.00122.47 C ANISOU 1146 C VAL A 191 19536 16281 10715 626 -790 739 C ATOM 1147 O VAL A 191 -88.692 -8.624 212.623 1.00120.95 O ANISOU 1147 O VAL A 191 19333 16083 10538 463 -806 687 O ATOM 1148 CB VAL A 191 -88.107 -8.211 209.334 1.00120.66 C ANISOU 1148 CB VAL A 191 19432 15966 10449 432 -789 1183 C ATOM 1149 CG1 VAL A 191 -87.238 -7.188 210.050 1.00121.76 C ANISOU 1149 CG1 VAL A 191 19756 15887 10619 151 -899 1241 C ATOM 1150 CG2 VAL A 191 -87.355 -8.825 208.165 1.00115.33 C ANISOU 1150 CG2 VAL A 191 18611 15499 9712 340 -681 1419 C ATOM 1151 N TYR A 192 -90.522 -8.294 211.351 1.00121.29 N ANISOU 1151 N TYR A 192 19486 16048 10552 914 -856 578 N ATOM 1152 CA TYR A 192 -91.268 -7.691 212.453 1.00123.85 C ANISOU 1152 CA TYR A 192 19907 16282 10869 1069 -942 324 C ATOM 1153 C TYR A 192 -91.430 -8.664 213.616 1.00124.25 C ANISOU 1153 C TYR A 192 19706 16607 10894 1030 -834 177 C ATOM 1154 O TYR A 192 -91.296 -8.276 214.785 1.00128.52 O ANISOU 1154 O TYR A 192 20306 17099 11426 984 -880 44 O ATOM 1155 CB TYR A 192 -92.634 -7.216 211.953 1.00127.07 C ANISOU 1155 CB TYR A 192 20399 16645 11237 1439 -1019 173 C ATOM 1156 CG TYR A 192 -93.722 -7.216 213.007 1.00132.48 C ANISOU 1156 CG TYR A 192 20991 17478 11867 1678 -1028 -130 C ATOM 1157 CD1 TYR A 192 -93.865 -6.154 213.890 1.00137.22 C ANISOU 1157 CD1 TYR A 192 21823 17866 12449 1790 -1163 -306 C ATOM 1158 CD2 TYR A 192 -94.618 -8.274 213.106 1.00133.75 C ANISOU 1158 CD2 TYR A 192 20838 18008 11974 1785 -906 -243 C ATOM 1159 CE1 TYR A 192 -94.861 -6.153 214.850 1.00139.78 C ANISOU 1159 CE1 TYR A 192 22035 18386 12689 2037 -1159 -595 C ATOM 1160 CE2 TYR A 192 -95.615 -8.282 214.062 1.00136.33 C ANISOU 1160 CE2 TYR A 192 21039 18542 12219 1978 -898 -507 C ATOM 1161 CZ TYR A 192 -95.733 -7.219 214.931 1.00137.96 C ANISOU 1161 CZ TYR A 192 21447 18576 12395 2122 -1016 -686 C ATOM 1162 OH TYR A 192 -96.726 -7.221 215.884 1.00136.68 O ANISOU 1162 OH TYR A 192 21136 18676 12120 2342 -997 -960 O ATOM 1163 N SER A 193 -91.718 -9.933 213.316 1.00119.33 N ANISOU 1163 N SER A 193 18830 16262 10246 1040 -702 202 N ATOM 1164 CA SER A 193 -91.895 -10.925 214.368 1.00116.75 C ANISOU 1164 CA SER A 193 18299 16182 9878 976 -606 95 C ATOM 1165 C SER A 193 -90.576 -11.234 215.060 1.00117.47 C ANISOU 1165 C SER A 193 18368 16277 9989 709 -579 206 C ATOM 1166 O SER A 193 -90.538 -11.381 216.285 1.00118.65 O ANISOU 1166 O SER A 193 18475 16505 10103 648 -570 93 O ATOM 1167 CB SER A 193 -92.510 -12.197 213.790 1.00118.59 C ANISOU 1167 CB SER A 193 18329 16659 10072 1022 -503 112 C ATOM 1168 OG SER A 193 -93.738 -11.915 213.142 1.00123.16 O ANISOU 1168 OG SER A 193 18893 17281 10620 1263 -538 3 O ATOM 1169 N SER A 194 -89.484 -11.336 214.299 1.00119.46 N ANISOU 1169 N SER A 194 18630 16484 10276 558 -566 426 N ATOM 1170 CA SER A 194 -88.181 -11.522 214.926 1.00125.37 C ANISOU 1170 CA SER A 194 19333 17274 11029 319 -558 529 C ATOM 1171 C SER A 194 -87.831 -10.354 215.837 1.00129.26 C ANISOU 1171 C SER A 194 19996 17577 11542 209 -676 453 C ATOM 1172 O SER A 194 -87.190 -10.547 216.877 1.00125.34 O ANISOU 1172 O SER A 194 19443 17156 11025 62 -681 424 O ATOM 1173 CB SER A 194 -87.103 -11.707 213.858 1.00125.38 C ANISOU 1173 CB SER A 194 19286 17314 11036 197 -524 773 C ATOM 1174 OG SER A 194 -86.921 -10.519 213.105 1.00123.45 O ANISOU 1174 OG SER A 194 19227 16855 10823 147 -609 873 O ATOM 1175 N ILE A 195 -88.240 -9.138 215.468 1.00134.44 N ANISOU 1175 N ILE A 195 20886 17968 12226 286 -791 413 N ATOM 1176 CA ILE A 195 -87.881 -7.970 216.267 1.00131.84 C ANISOU 1176 CA ILE A 195 20786 17397 11909 176 -938 335 C ATOM 1177 C ILE A 195 -88.704 -7.914 217.549 1.00128.07 C ANISOU 1177 C ILE A 195 20316 16966 11379 340 -959 54 C ATOM 1178 O ILE A 195 -88.155 -7.813 218.652 1.00130.27 O ANISOU 1178 O ILE A 195 20602 17262 11633 195 -996 -15 O ATOM 1179 CB ILE A 195 -88.039 -6.681 215.440 1.00136.11 C ANISOU 1179 CB ILE A 195 21645 17590 12482 214 -1083 390 C ATOM 1180 CG1 ILE A 195 -86.939 -6.585 214.382 1.00136.37 C ANISOU 1180 CG1 ILE A 195 21680 17597 12537 -54 -1070 697 C ATOM 1181 CG2 ILE A 195 -88.017 -5.459 216.348 1.00140.25 C ANISOU 1181 CG2 ILE A 195 22477 17810 13003 184 -1268 235 C ATOM 1182 CD1 ILE A 195 -87.093 -5.404 213.450 1.00139.11 C ANISOU 1182 CD1 ILE A 195 22359 17602 12895 -45 -1208 801 C ATOM 1183 N VAL A 196 -90.032 -7.986 217.430 1.00122.57 N ANISOU 1183 N VAL A 196 19595 16333 10645 646 -935 -115 N ATOM 1184 CA VAL A 196 -90.864 -7.758 218.611 1.00116.36 C ANISOU 1184 CA VAL A 196 18815 15620 9776 826 -960 -394 C ATOM 1185 C VAL A 196 -91.031 -9.018 219.458 1.00113.78 C ANISOU 1185 C VAL A 196 18201 15655 9376 768 -810 -442 C ATOM 1186 O VAL A 196 -91.214 -8.925 220.677 1.00112.23 O ANISOU 1186 O VAL A 196 17994 15552 9096 787 -819 -616 O ATOM 1187 CB VAL A 196 -92.231 -7.179 218.207 1.00111.31 C ANISOU 1187 CB VAL A 196 18256 14942 9095 1200 -1014 -576 C ATOM 1188 CG1 VAL A 196 -92.045 -5.899 217.413 1.00111.54 C ANISOU 1188 CG1 VAL A 196 18638 14560 9180 1266 -1191 -516 C ATOM 1189 CG2 VAL A 196 -93.046 -8.197 217.422 1.00110.46 C ANISOU 1189 CG2 VAL A 196 17885 15117 8969 1316 -878 -534 C ATOM 1190 N SER A 197 -90.974 -10.202 218.851 1.00111.94 N ANISOU 1190 N SER A 197 17760 15618 9156 696 -682 -291 N ATOM 1191 CA SER A 197 -91.249 -11.436 219.571 1.00113.88 C ANISOU 1191 CA SER A 197 17784 16166 9318 639 -558 -321 C ATOM 1192 C SER A 197 -90.000 -12.100 220.124 1.00113.89 C ANISOU 1192 C SER A 197 17735 16216 9321 389 -532 -179 C ATOM 1193 O SER A 197 -90.085 -12.810 221.130 1.00115.56 O ANISOU 1193 O SER A 197 17848 16618 9441 328 -477 -234 O ATOM 1194 CB SER A 197 -91.980 -12.427 218.660 1.00118.10 C ANISOU 1194 CB SER A 197 18160 16868 9844 708 -461 -259 C ATOM 1195 OG SER A 197 -93.262 -11.943 218.300 1.00123.41 O ANISOU 1195 OG SER A 197 18819 17588 10483 954 -481 -416 O ATOM 1196 N PHE A 198 -88.841 -11.900 219.500 1.00115.49 N ANISOU 1196 N PHE A 198 17992 16285 9604 247 -572 6 N ATOM 1197 CA PHE A 198 -87.621 -12.557 219.955 1.00112.92 C ANISOU 1197 CA PHE A 198 17580 16060 9264 47 -554 139 C ATOM 1198 C PHE A 198 -86.580 -11.571 220.463 1.00119.43 C ANISOU 1198 C PHE A 198 18515 16748 10116 -130 -671 157 C ATOM 1199 O PHE A 198 -86.131 -11.698 221.606 1.00117.35 O ANISOU 1199 O PHE A 198 18225 16571 9791 -230 -698 99 O ATOM 1200 CB PHE A 198 -87.037 -13.429 218.836 1.00104.91 C ANISOU 1200 CB PHE A 198 16461 15120 8280 22 -487 348 C ATOM 1201 CG PHE A 198 -85.780 -14.152 219.229 1.00102.19 C ANISOU 1201 CG PHE A 198 16010 14916 7900 -118 -476 476 C ATOM 1202 CD1 PHE A 198 -85.834 -15.244 220.080 1.00100.82 C ANISOU 1202 CD1 PHE A 198 15765 14902 7640 -113 -433 448 C ATOM 1203 CD2 PHE A 198 -84.547 -13.742 218.751 1.00101.90 C ANISOU 1203 CD2 PHE A 198 15944 14876 7896 -255 -516 632 C ATOM 1204 CE1 PHE A 198 -84.682 -15.912 220.449 1.00101.75 C ANISOU 1204 CE1 PHE A 198 15799 15152 7710 -191 -443 558 C ATOM 1205 CE2 PHE A 198 -83.391 -14.407 219.116 1.00103.14 C ANISOU 1205 CE2 PHE A 198 15966 15221 8001 -345 -512 736 C ATOM 1206 CZ PHE A 198 -83.459 -15.494 219.966 1.00103.70 C ANISOU 1206 CZ PHE A 198 15982 15429 7990 -287 -483 692 C ATOM 1207 N TYR A 199 -86.182 -10.587 219.653 1.00126.89 N ANISOU 1207 N TYR A 199 19594 17482 11135 -196 -752 244 N ATOM 1208 CA TYR A 199 -85.015 -9.776 219.990 1.00134.72 C ANISOU 1208 CA TYR A 199 20673 18366 12147 -450 -868 315 C ATOM 1209 C TYR A 199 -85.275 -8.891 221.205 1.00137.76 C ANISOU 1209 C TYR A 199 21242 18604 12496 -459 -993 96 C ATOM 1210 O TYR A 199 -84.457 -8.841 222.131 1.00144.75 O ANISOU 1210 O TYR A 199 22101 19554 13342 -643 -1053 81 O ATOM 1211 CB TYR A 199 -84.610 -8.933 218.781 1.00141.64 C ANISOU 1211 CB TYR A 199 21678 19045 13092 -556 -928 483 C ATOM 1212 CG TYR A 199 -83.815 -9.707 217.755 1.00144.08 C ANISOU 1212 CG TYR A 199 21780 19560 13403 -638 -825 726 C ATOM 1213 CD1 TYR A 199 -83.000 -10.765 218.135 1.00142.18 C ANISOU 1213 CD1 TYR A 199 21294 19616 13111 -701 -750 798 C ATOM 1214 CD2 TYR A 199 -83.893 -9.392 216.405 1.00149.29 C ANISOU 1214 CD2 TYR A 199 22498 20131 14094 -617 -808 874 C ATOM 1215 CE1 TYR A 199 -82.277 -11.481 217.202 1.00143.89 C ANISOU 1215 CE1 TYR A 199 21323 20044 13304 -716 -662 993 C ATOM 1216 CE2 TYR A 199 -83.172 -10.103 215.463 1.00151.62 C ANISOU 1216 CE2 TYR A 199 22596 20652 14361 -661 -707 1079 C ATOM 1217 CZ TYR A 199 -82.366 -11.146 215.868 1.00149.66 C ANISOU 1217 CZ TYR A 199 22098 20707 14058 -698 -634 1128 C ATOM 1218 OH TYR A 199 -81.647 -11.857 214.935 1.00151.27 O ANISOU 1218 OH TYR A 199 22108 21158 14211 -686 -542 1305 O ATOM 1219 N VAL A 200 -86.413 -8.195 221.229 1.00131.74 N ANISOU 1219 N VAL A 200 20662 17663 11729 -233 -1043 -91 N ATOM 1220 CA VAL A 200 -86.733 -7.337 222.373 1.00129.57 C ANISOU 1220 CA VAL A 200 20583 17253 11394 -177 -1169 -336 C ATOM 1221 C VAL A 200 -86.869 -8.136 223.667 1.00125.40 C ANISOU 1221 C VAL A 200 19883 17011 10753 -154 -1093 -466 C ATOM 1222 O VAL A 200 -86.215 -7.775 224.660 1.00125.38 O ANISOU 1222 O VAL A 200 19950 16988 10702 -305 -1190 -538 O ATOM 1223 CB VAL A 200 -87.977 -6.483 222.066 1.00128.37 C ANISOU 1223 CB VAL A 200 20648 16891 11235 137 -1238 -524 C ATOM 1224 CG1 VAL A 200 -88.408 -5.710 223.302 1.00129.82 C ANISOU 1224 CG1 VAL A 200 21020 16984 11321 271 -1358 -819 C ATOM 1225 CG2 VAL A 200 -87.695 -5.534 220.912 1.00126.66 C ANISOU 1225 CG2 VAL A 200 20683 16329 11112 76 -1358 -381 C ATOM 1226 N PRO A 201 -87.683 -9.202 223.737 1.00120.52 N ANISOU 1226 N PRO A 201 19056 16661 10075 4 -935 -496 N ATOM 1227 CA PRO A 201 -87.773 -9.942 225.008 1.00120.23 C ANISOU 1227 CA PRO A 201 18887 16889 9905 -13 -872 -591 C ATOM 1228 C PRO A 201 -86.456 -10.568 225.417 1.00122.06 C ANISOU 1228 C PRO A 201 19015 17230 10130 -265 -877 -426 C ATOM 1229 O PRO A 201 -86.118 -10.562 226.606 1.00124.20 O ANISOU 1229 O PRO A 201 19293 17596 10301 -339 -923 -519 O ATOM 1230 CB PRO A 201 -88.842 -11.011 224.729 1.00116.07 C ANISOU 1230 CB PRO A 201 18170 16604 9325 137 -708 -590 C ATOM 1231 CG PRO A 201 -89.504 -10.609 223.469 1.00115.22 C ANISOU 1231 CG PRO A 201 18110 16357 9310 295 -708 -573 C ATOM 1232 CD PRO A 201 -88.517 -9.821 222.692 1.00116.24 C ANISOU 1232 CD PRO A 201 18397 16202 9565 166 -819 -430 C ATOM 1233 N PHE A 202 -85.696 -11.106 224.460 1.00121.03 N ANISOU 1233 N PHE A 202 18782 17118 10086 -374 -837 -190 N ATOM 1234 CA PHE A 202 -84.421 -11.732 224.793 1.00121.79 C ANISOU 1234 CA PHE A 202 18749 17367 10158 -564 -848 -38 C ATOM 1235 C PHE A 202 -83.434 -10.715 225.350 1.00120.70 C ANISOU 1235 C PHE A 202 18710 17122 10026 -778 -1008 -63 C ATOM 1236 O PHE A 202 -82.758 -10.983 226.350 1.00122.97 O ANISOU 1236 O PHE A 202 18934 17560 10228 -888 -1054 -81 O ATOM 1237 CB PHE A 202 -83.850 -12.427 223.555 1.00125.55 C ANISOU 1237 CB PHE A 202 19092 17908 10704 -585 -776 195 C ATOM 1238 CG PHE A 202 -82.431 -12.895 223.711 1.00129.78 C ANISOU 1238 CG PHE A 202 19479 18619 11211 -745 -805 352 C ATOM 1239 CD1 PHE A 202 -82.039 -13.627 224.820 1.00131.41 C ANISOU 1239 CD1 PHE A 202 19607 19016 11306 -761 -814 328 C ATOM 1240 CD2 PHE A 202 -81.489 -12.611 222.736 1.00131.69 C ANISOU 1240 CD2 PHE A 202 19647 18874 11517 -869 -824 530 C ATOM 1241 CE1 PHE A 202 -80.733 -14.059 224.956 1.00133.25 C ANISOU 1241 CE1 PHE A 202 19686 19446 11498 -864 -855 463 C ATOM 1242 CE2 PHE A 202 -80.183 -13.040 222.866 1.00132.72 C ANISOU 1242 CE2 PHE A 202 19592 19240 11597 -991 -849 665 C ATOM 1243 CZ PHE A 202 -79.804 -13.765 223.977 1.00132.86 C ANISOU 1243 CZ PHE A 202 19526 19444 11509 -972 -871 624 C ATOM 1244 N ILE A 203 -83.351 -9.533 224.735 1.00115.45 N ANISOU 1244 N ILE A 203 18225 16188 9451 -854 -1111 -64 N ATOM 1245 CA ILE A 203 -82.419 -8.520 225.223 1.00112.95 C ANISOU 1245 CA ILE A 203 18040 15738 9138 -1114 -1288 -81 C ATOM 1246 C ILE A 203 -82.847 -8.012 226.596 1.00116.78 C ANISOU 1246 C ILE A 203 18684 16164 9522 -1055 -1386 -349 C ATOM 1247 O ILE A 203 -82.013 -7.844 227.497 1.00122.63 O ANISOU 1247 O ILE A 203 19417 16978 10200 -1249 -1492 -382 O ATOM 1248 CB ILE A 203 -82.289 -7.374 224.202 1.00110.56 C ANISOU 1248 CB ILE A 203 17950 15117 8940 -1234 -1391 1 C ATOM 1249 CG1 ILE A 203 -81.581 -7.865 222.938 1.00101.91 C ANISOU 1249 CG1 ILE A 203 16661 14154 7906 -1352 -1298 288 C ATOM 1250 CG2 ILE A 203 -81.533 -6.200 224.805 1.00116.68 C ANISOU 1250 CG2 ILE A 203 18943 15682 9706 -1522 -1608 -56 C ATOM 1251 CD1 ILE A 203 -81.551 -6.847 221.818 1.00 98.99 C ANISOU 1251 CD1 ILE A 203 16498 13495 7617 -1465 -1374 405 C ATOM 1252 N VAL A 204 -84.150 -7.783 226.791 1.00116.81 N ANISOU 1252 N VAL A 204 18813 16080 9488 -773 -1354 -555 N ATOM 1253 CA VAL A 204 -84.621 -7.300 228.088 1.00118.08 C ANISOU 1253 CA VAL A 204 19117 16228 9521 -669 -1437 -833 C ATOM 1254 C VAL A 204 -84.378 -8.345 229.173 1.00117.30 C ANISOU 1254 C VAL A 204 18805 16480 9284 -698 -1353 -841 C ATOM 1255 O VAL A 204 -83.961 -8.015 230.291 1.00113.63 O ANISOU 1255 O VAL A 204 18411 16049 8714 -787 -1462 -972 O ATOM 1256 CB VAL A 204 -86.106 -6.897 228.005 1.00115.36 C ANISOU 1256 CB VAL A 204 18896 15798 9136 -316 -1403 -1054 C ATOM 1257 CG1 VAL A 204 -86.658 -6.602 229.390 1.00112.70 C ANISOU 1257 CG1 VAL A 204 18643 15558 8621 -160 -1447 -1351 C ATOM 1258 CG2 VAL A 204 -86.272 -5.685 227.101 1.00118.87 C ANISOU 1258 CG2 VAL A 204 19636 15839 9692 -271 -1544 -1071 C ATOM 1259 N THR A 205 -84.611 -9.621 228.856 1.00119.00 N ANISOU 1259 N THR A 205 18785 16942 9488 -632 -1175 -697 N ATOM 1260 CA THR A 205 -84.391 -10.684 229.831 1.00121.88 C ANISOU 1260 CA THR A 205 18990 17609 9711 -659 -1106 -672 C ATOM 1261 C THR A 205 -82.912 -10.839 230.156 1.00130.27 C ANISOU 1261 C THR A 205 19975 18751 10771 -901 -1205 -534 C ATOM 1262 O THR A 205 -82.545 -11.062 231.316 1.00128.50 O ANISOU 1262 O THR A 205 19730 18689 10407 -955 -1255 -601 O ATOM 1263 CB THR A 205 -84.959 -11.999 229.299 1.00113.81 C ANISOU 1263 CB THR A 205 17796 16767 8682 -554 -924 -533 C ATOM 1264 OG1 THR A 205 -86.324 -11.808 228.908 1.00112.95 O ANISOU 1264 OG1 THR A 205 17720 16622 8575 -351 -841 -657 O ATOM 1265 CG2 THR A 205 -84.889 -13.084 230.361 1.00110.91 C ANISOU 1265 CG2 THR A 205 17328 16671 8141 -575 -866 -508 C ATOM 1266 N LEU A 206 -82.048 -10.719 229.145 1.00137.30 N ANISOU 1266 N LEU A 206 20804 19569 11794 -1046 -1235 -341 N ATOM 1267 CA LEU A 206 -80.613 -10.775 229.392 1.00140.36 C ANISOU 1267 CA LEU A 206 21073 20090 12167 -1282 -1336 -215 C ATOM 1268 C LEU A 206 -80.170 -9.629 230.291 1.00144.78 C ANISOU 1268 C LEU A 206 21799 20530 12682 -1466 -1533 -378 C ATOM 1269 O LEU A 206 -79.353 -9.823 231.196 1.00146.41 O ANISOU 1269 O LEU A 206 21919 20925 12783 -1594 -1619 -385 O ATOM 1270 CB LEU A 206 -79.850 -10.754 228.068 1.00139.81 C ANISOU 1270 CB LEU A 206 20888 20008 12227 -1405 -1320 15 C ATOM 1271 CG LEU A 206 -78.324 -10.810 228.159 1.00141.24 C ANISOU 1271 CG LEU A 206 20877 20405 12381 -1652 -1413 164 C ATOM 1272 CD1 LEU A 206 -77.881 -12.017 228.972 1.00140.13 C ANISOU 1272 CD1 LEU A 206 20551 20587 12105 -1552 -1381 199 C ATOM 1273 CD2 LEU A 206 -77.706 -10.841 226.770 1.00141.20 C ANISOU 1273 CD2 LEU A 206 20728 20447 12473 -1742 -1362 390 C ATOM 1274 N LEU A 207 -80.718 -8.430 230.074 1.00145.10 N ANISOU 1274 N LEU A 207 22100 20245 12784 -1466 -1624 -522 N ATOM 1275 CA LEU A 207 -80.366 -7.298 230.928 1.00146.42 C ANISOU 1275 CA LEU A 207 22495 20239 12900 -1632 -1839 -705 C ATOM 1276 C LEU A 207 -80.869 -7.498 232.355 1.00143.95 C ANISOU 1276 C LEU A 207 22227 20066 12402 -1475 -1849 -942 C ATOM 1277 O LEU A 207 -80.168 -7.163 233.319 1.00147.77 O ANISOU 1277 O LEU A 207 22754 20605 12786 -1643 -2002 -1033 O ATOM 1278 CB LEU A 207 -80.912 -6.001 230.335 1.00151.28 C ANISOU 1278 CB LEU A 207 23444 20426 13611 -1617 -1952 -811 C ATOM 1279 CG LEU A 207 -80.260 -5.567 229.020 1.00155.04 C ANISOU 1279 CG LEU A 207 23931 20736 14242 -1856 -1988 -568 C ATOM 1280 CD1 LEU A 207 -80.743 -4.187 228.602 1.00158.96 C ANISOU 1280 CD1 LEU A 207 24839 20754 14803 -1862 -2151 -680 C ATOM 1281 CD2 LEU A 207 -78.742 -5.598 229.134 1.00157.31 C ANISOU 1281 CD2 LEU A 207 24038 21210 14521 -2258 -2084 -390 C ATOM 1282 N VAL A 208 -82.079 -8.040 232.513 1.00140.88 N ANISOU 1282 N VAL A 208 21816 19767 11945 -1171 -1689 -1042 N ATOM 1283 CA VAL A 208 -82.610 -8.285 233.853 1.00133.09 C ANISOU 1283 CA VAL A 208 20848 18973 10749 -1027 -1672 -1249 C ATOM 1284 C VAL A 208 -81.762 -9.322 234.583 1.00134.56 C ANISOU 1284 C VAL A 208 20819 19486 10820 -1150 -1649 -1114 C ATOM 1285 O VAL A 208 -81.468 -9.180 235.777 1.00130.60 O ANISOU 1285 O VAL A 208 20365 19103 10153 -1195 -1748 -1250 O ATOM 1286 CB VAL A 208 -84.089 -8.707 233.776 1.00120.45 C ANISOU 1286 CB VAL A 208 19216 17465 9083 -715 -1488 -1351 C ATOM 1287 CG1 VAL A 208 -84.574 -9.195 235.130 1.00116.05 C ANISOU 1287 CG1 VAL A 208 18610 17206 8276 -605 -1429 -1504 C ATOM 1288 CG2 VAL A 208 -84.945 -7.546 233.297 1.00118.18 C ANISOU 1288 CG2 VAL A 208 19166 16877 8859 -530 -1553 -1548 C ATOM 1289 N TYR A 209 -81.334 -10.369 233.876 1.00137.24 N ANISOU 1289 N TYR A 209 20940 19972 11232 -1184 -1536 -850 N ATOM 1290 CA TYR A 209 -80.508 -11.383 234.525 1.00138.03 C ANISOU 1290 CA TYR A 209 20865 20367 11214 -1251 -1535 -717 C ATOM 1291 C TYR A 209 -79.096 -10.871 234.786 1.00136.35 C ANISOU 1291 C TYR A 209 20604 20192 11010 -1510 -1729 -675 C ATOM 1292 O TYR A 209 -78.446 -11.316 235.737 1.00137.92 O ANISOU 1292 O TYR A 209 20720 20626 11057 -1561 -1800 -669 O ATOM 1293 CB TYR A 209 -80.485 -12.665 233.696 1.00143.55 C ANISOU 1293 CB TYR A 209 21384 21191 11967 -1164 -1380 -472 C ATOM 1294 CG TYR A 209 -81.415 -13.724 234.244 1.00148.30 C ANISOU 1294 CG TYR A 209 21978 21950 12418 -996 -1236 -476 C ATOM 1295 CD1 TYR A 209 -81.012 -14.560 235.277 1.00150.54 C ANISOU 1295 CD1 TYR A 209 22220 22469 12511 -1001 -1258 -426 C ATOM 1296 CD2 TYR A 209 -82.701 -13.874 233.744 1.00150.02 C ANISOU 1296 CD2 TYR A 209 22235 22098 12668 -853 -1089 -521 C ATOM 1297 CE1 TYR A 209 -81.860 -15.523 235.789 1.00152.64 C ANISOU 1297 CE1 TYR A 209 22508 22870 12619 -900 -1134 -402 C ATOM 1298 CE2 TYR A 209 -83.556 -14.836 234.249 1.00150.49 C ANISOU 1298 CE2 TYR A 209 22278 22330 12573 -763 -961 -508 C ATOM 1299 CZ TYR A 209 -83.131 -15.656 235.271 1.00152.23 C ANISOU 1299 CZ TYR A 209 22482 22757 12602 -803 -983 -440 C ATOM 1300 OH TYR A 209 -83.979 -16.613 235.776 1.00152.86 O ANISOU 1300 OH TYR A 209 22572 22999 12510 -764 -862 -399 O ATOM 1301 N ILE A 210 -78.614 -9.929 233.973 1.00131.66 N ANISOU 1301 N ILE A 210 20063 19387 10574 -1694 -1826 -640 N ATOM 1302 CA ILE A 210 -77.368 -9.236 234.293 1.00128.40 C ANISOU 1302 CA ILE A 210 19628 19004 10154 -2004 -2035 -630 C ATOM 1303 C ILE A 210 -77.523 -8.457 235.594 1.00126.16 C ANISOU 1303 C ILE A 210 19564 18645 9726 -2047 -2200 -906 C ATOM 1304 O ILE A 210 -76.651 -8.494 236.471 1.00124.54 O ANISOU 1304 O ILE A 210 19281 18640 9398 -2202 -2338 -930 O ATOM 1305 CB ILE A 210 -76.945 -8.323 233.128 1.00126.59 C ANISOU 1305 CB ILE A 210 19453 18537 10108 -2235 -2104 -525 C ATOM 1306 CG1 ILE A 210 -76.394 -9.155 231.969 1.00118.92 C ANISOU 1306 CG1 ILE A 210 18195 17761 9229 -2238 -1968 -237 C ATOM 1307 CG2 ILE A 210 -75.915 -7.302 233.590 1.00131.50 C ANISOU 1307 CG2 ILE A 210 20148 19108 10706 -2610 -2354 -577 C ATOM 1308 CD1 ILE A 210 -76.187 -8.366 230.694 1.00116.41 C ANISOU 1308 CD1 ILE A 210 17931 17228 9072 -2428 -1987 -109 C ATOM 1309 N LYS A 211 -78.643 -7.740 235.736 1.00126.16 N ANISOU 1309 N LYS A 211 19839 18375 9722 -1882 -2197 -1131 N ATOM 1310 CA LYS A 211 -78.917 -7.031 236.984 1.00133.19 C ANISOU 1310 CA LYS A 211 20959 19203 10444 -1851 -2344 -1429 C ATOM 1311 C LYS A 211 -78.967 -7.994 238.164 1.00138.99 C ANISOU 1311 C LYS A 211 21551 20306 10952 -1724 -2277 -1466 C ATOM 1312 O LYS A 211 -78.521 -7.661 239.269 1.00139.34 O ANISOU 1312 O LYS A 211 21669 20439 10833 -1815 -2436 -1620 O ATOM 1313 CB LYS A 211 -80.238 -6.268 236.885 1.00131.23 C ANISOU 1313 CB LYS A 211 20994 18666 10200 -1591 -2320 -1671 C ATOM 1314 CG LYS A 211 -80.197 -4.984 236.080 1.00132.18 C ANISOU 1314 CG LYS A 211 21401 18338 10485 -1712 -2480 -1720 C ATOM 1315 CD LYS A 211 -81.524 -4.249 236.213 1.00132.21 C ANISOU 1315 CD LYS A 211 21702 18095 10436 -1370 -2485 -2011 C ATOM 1316 CE LYS A 211 -81.512 -2.915 235.489 1.00133.83 C ANISOU 1316 CE LYS A 211 22276 17792 10780 -1460 -2684 -2075 C ATOM 1317 NZ LYS A 211 -82.798 -2.186 235.677 1.00133.49 N ANISOU 1317 NZ LYS A 211 22536 17523 10659 -1057 -2714 -2389 N ATOM 1318 N ILE A 212 -79.515 -9.190 237.948 1.00141.29 N ANISOU 1318 N ILE A 212 21663 20804 11216 -1529 -2053 -1322 N ATOM 1319 CA ILE A 212 -79.586 -10.180 239.020 1.00144.65 C ANISOU 1319 CA ILE A 212 21985 21564 11413 -1428 -1987 -1314 C ATOM 1320 C ILE A 212 -78.190 -10.673 239.387 1.00148.90 C ANISOU 1320 C ILE A 212 22346 22331 11898 -1615 -2110 -1154 C ATOM 1321 O ILE A 212 -77.847 -10.789 240.570 1.00148.63 O ANISOU 1321 O ILE A 212 22324 22494 11654 -1637 -2208 -1244 O ATOM 1322 CB ILE A 212 -80.511 -11.342 238.616 1.00141.26 C ANISOU 1322 CB ILE A 212 21446 21257 10970 -1222 -1739 -1174 C ATOM 1323 CG1 ILE A 212 -81.958 -10.858 238.504 1.00142.25 C ANISOU 1323 CG1 ILE A 212 21706 21261 11082 -1018 -1627 -1373 C ATOM 1324 CG2 ILE A 212 -80.407 -12.485 239.616 1.00137.94 C ANISOU 1324 CG2 ILE A 212 20936 21160 10315 -1174 -1688 -1091 C ATOM 1325 CD1 ILE A 212 -82.920 -11.917 238.011 1.00140.07 C ANISOU 1325 CD1 ILE A 212 21312 21107 10802 -869 -1394 -1239 C ATOM 1326 N TYR A 213 -77.363 -10.968 238.380 1.00154.18 N ANISOU 1326 N TYR A 213 22834 23011 12735 -1733 -2107 -919 N ATOM 1327 CA TYR A 213 -75.993 -11.407 238.634 1.00162.94 C ANISOU 1327 CA TYR A 213 23729 24391 13788 -1883 -2229 -771 C ATOM 1328 C TYR A 213 -75.164 -10.315 239.300 1.00168.63 C ANISOU 1328 C TYR A 213 24514 25098 14460 -2157 -2483 -924 C ATOM 1329 O TYR A 213 -74.185 -10.618 239.993 1.00167.85 O ANISOU 1329 O TYR A 213 24265 25284 14228 -2256 -2614 -884 O ATOM 1330 CB TYR A 213 -75.340 -11.848 237.323 1.00166.47 C ANISOU 1330 CB TYR A 213 23955 24884 14414 -1928 -2164 -512 C ATOM 1331 CG TYR A 213 -73.902 -12.302 237.456 1.00172.62 C ANISOU 1331 CG TYR A 213 24460 26001 15128 -2044 -2283 -358 C ATOM 1332 CD1 TYR A 213 -73.593 -13.575 237.917 1.00174.11 C ANISOU 1332 CD1 TYR A 213 24514 26476 15163 -1841 -2249 -238 C ATOM 1333 CD2 TYR A 213 -72.853 -11.458 237.110 1.00175.92 C ANISOU 1333 CD2 TYR A 213 24754 26465 15621 -2357 -2441 -328 C ATOM 1334 CE1 TYR A 213 -72.279 -13.993 238.036 1.00175.62 C ANISOU 1334 CE1 TYR A 213 24440 27012 15276 -1889 -2370 -112 C ATOM 1335 CE2 TYR A 213 -71.538 -11.867 237.226 1.00177.18 C ANISOU 1335 CE2 TYR A 213 24608 27010 15701 -2454 -2550 -195 C ATOM 1336 CZ TYR A 213 -71.256 -13.134 237.689 1.00176.74 C ANISOU 1336 CZ TYR A 213 24406 27256 15490 -2190 -2514 -97 C ATOM 1337 OH TYR A 213 -69.948 -13.544 237.805 1.00178.12 O ANISOU 1337 OH TYR A 213 24263 27847 15567 -2232 -2634 21 O ATOM 1338 N ILE A 214 -75.530 -9.046 239.098 1.00171.72 N ANISOU 1338 N ILE A 214 25145 25154 14948 -2282 -2574 -1101 N ATOM 1339 CA ILE A 214 -74.876 -7.958 239.821 1.00173.55 C ANISOU 1339 CA ILE A 214 25518 25310 15112 -2554 -2841 -1283 C ATOM 1340 C ILE A 214 -75.049 -8.123 241.326 1.00170.04 C ANISOU 1340 C ILE A 214 25159 25047 14400 -2439 -2916 -1488 C ATOM 1341 O ILE A 214 -74.139 -7.808 242.104 1.00176.78 O ANISOU 1341 O ILE A 214 25984 26050 15135 -2649 -3130 -1556 O ATOM 1342 CB ILE A 214 -75.412 -6.596 239.331 1.00178.27 C ANISOU 1342 CB ILE A 214 26449 25439 15846 -2652 -2934 -1451 C ATOM 1343 CG1 ILE A 214 -74.913 -6.302 237.915 1.00179.86 C ANISOU 1343 CG1 ILE A 214 26560 25496 16282 -2875 -2920 -1220 C ATOM 1344 CG2 ILE A 214 -75.005 -5.473 240.275 1.00183.23 C ANISOU 1344 CG2 ILE A 214 27332 25924 16364 -2877 -3224 -1707 C ATOM 1345 CD1 ILE A 214 -75.437 -5.005 237.340 1.00182.26 C ANISOU 1345 CD1 ILE A 214 27231 25301 16717 -2966 -3021 -1346 C ATOM 1346 N VAL A 215 -76.195 -8.645 241.760 1.00158.63 N ANISOU 1346 N VAL A 215 22229 25199 12845 -1741 -5243 -956 N ATOM 1347 CA VAL A 215 -76.456 -8.858 243.180 1.00136.02 C ANISOU 1347 CA VAL A 215 18942 21880 10860 -1545 -5099 -888 C ATOM 1348 C VAL A 215 -75.740 -10.118 243.648 1.00131.15 C ANISOU 1348 C VAL A 215 18282 21145 10403 -1392 -4860 -1493 C ATOM 1349 O VAL A 215 -76.301 -11.219 243.608 1.00132.04 O ANISOU 1349 O VAL A 215 18379 21023 10769 -1391 -5234 -1793 O ATOM 1350 CB VAL A 215 -77.968 -8.946 243.461 1.00125.77 C ANISOU 1350 CB VAL A 215 17383 20237 10165 -1579 -5648 -603 C ATOM 1351 CG1 VAL A 215 -78.228 -9.055 244.957 1.00122.49 C ANISOU 1351 CG1 VAL A 215 16519 19472 10551 -1436 -5409 -489 C ATOM 1352 CG2 VAL A 215 -78.688 -7.742 242.873 1.00123.61 C ANISOU 1352 CG2 VAL A 215 17156 20032 9777 -1694 -6016 -64 C ATOM 1353 N LEU A 216 -74.496 -9.962 244.091 1.00124.70 N ANISOU 1353 N LEU A 216 17436 20447 9498 -1269 -4300 -1668 N ATOM 1354 CA LEU A 216 -73.696 -11.082 244.576 1.00120.71 C ANISOU 1354 CA LEU A 216 16872 19784 9210 -1085 -4110 -2245 C ATOM 1355 C LEU A 216 -72.513 -10.579 245.396 1.00116.43 C ANISOU 1355 C LEU A 216 16177 19272 8789 -945 -3532 -2228 C ATOM 1356 O LEU A 216 -72.583 -9.520 246.020 1.00111.41 O ANISOU 1356 O LEU A 216 15403 18591 8336 -966 -3342 -1724 O ATOM 1357 CB LEU A 216 -73.199 -11.942 243.411 1.00125.14 C ANISOU 1357 CB LEU A 216 17704 20646 9197 -1073 -4202 -2928 C ATOM 1358 CG LEU A 216 -72.537 -13.268 243.795 1.00124.36 C ANISOU 1358 CG LEU A 216 17540 20272 9439 -839 -4203 -3624 C ATOM 1359 CD1 LEU A 216 -73.567 -14.249 244.335 1.00121.74 C ANISOU 1359 CD1 LEU A 216 17129 19354 9771 -858 -4772 -3600 C ATOM 1360 CD2 LEU A 216 -71.790 -13.864 242.611 1.00130.48 C ANISOU 1360 CD2 LEU A 216 18534 21477 9565 -764 -4138 -4402 C ATOM 1361 N LEU A1003 -69.947 -13.257 256.896 1.00131.23 N ANISOU 1361 N LEU A1003 17212 18266 14382 -450 -3112 -1409 N ATOM 1362 CA LEU A1003 -70.286 -11.978 257.509 1.00130.26 C ANISOU 1362 CA LEU A1003 16964 18428 14102 -466 -2728 -1058 C ATOM 1363 C LEU A1003 -70.868 -12.167 258.905 1.00143.07 C ANISOU 1363 C LEU A1003 18577 19944 15838 -679 -2753 -670 C ATOM 1364 O LEU A1003 -71.343 -11.212 259.518 1.00145.27 O ANISOU 1364 O LEU A1003 18722 20470 16003 -700 -2455 -424 O ATOM 1365 CB LEU A1003 -71.281 -11.211 256.634 1.00120.81 C ANISOU 1365 CB LEU A1003 15630 17560 12711 -520 -2612 -921 C ATOM 1366 CG LEU A1003 -70.773 -10.656 255.302 1.00115.81 C ANISOU 1366 CG LEU A1003 15029 17167 11806 -378 -2502 -1173 C ATOM 1367 CD1 LEU A1003 -71.922 -10.077 254.491 1.00115.80 C ANISOU 1367 CD1 LEU A1003 14943 17402 11652 -484 -2556 -964 C ATOM 1368 CD2 LEU A1003 -69.701 -9.608 255.534 1.00110.87 C ANISOU 1368 CD2 LEU A1003 14379 16666 11081 -207 -2156 -1202 C ATOM 1369 N GLU A1004 -70.824 -13.405 259.405 1.00154.19 N ANISOU 1369 N GLU A1004 20134 20989 17462 -849 -3128 -629 N ATOM 1370 CA GLU A1004 -71.419 -13.706 260.704 1.00161.53 C ANISOU 1370 CA GLU A1004 21090 21866 18417 -1159 -3169 -196 C ATOM 1371 C GLU A1004 -70.726 -12.935 261.823 1.00159.97 C ANISOU 1371 C GLU A1004 20950 21759 18071 -1050 -2898 -106 C ATOM 1372 O GLU A1004 -71.385 -12.331 262.681 1.00158.39 O ANISOU 1372 O GLU A1004 20648 21849 17683 -1195 -2615 180 O ATOM 1373 CB GLU A1004 -71.358 -15.213 260.961 1.00171.71 C ANISOU 1373 CB GLU A1004 22589 22662 19991 -1395 -3729 -131 C ATOM 1374 CG GLU A1004 -70.011 -15.843 260.623 1.00175.83 C ANISOU 1374 CG GLU A1004 23295 22758 20755 -1102 -4062 -578 C ATOM 1375 CD GLU A1004 -69.958 -17.326 260.929 1.00184.08 C ANISOU 1375 CD GLU A1004 24559 23206 22178 -1313 -4731 -516 C ATOM 1376 OE1 GLU A1004 -70.918 -17.846 261.534 1.00188.50 O ANISOU 1376 OE1 GLU A1004 25163 23696 22764 -1760 -4913 -26 O ATOM 1377 OE2 GLU A1004 -68.953 -17.972 260.564 1.00187.43 O ANISOU 1377 OE2 GLU A1004 25086 23224 22905 -1041 -5094 -963 O ATOM 1378 N ASP A1005 -69.390 -12.957 261.835 1.00159.24 N ANISOU 1378 N ASP A1005 20994 21436 18075 -788 -2991 -394 N ATOM 1379 CA ASP A1005 -68.647 -12.183 262.823 1.00157.59 C ANISOU 1379 CA ASP A1005 20843 21282 17753 -663 -2793 -352 C ATOM 1380 C ASP A1005 -68.968 -10.698 262.720 1.00157.98 C ANISOU 1380 C ASP A1005 20689 21752 17582 -521 -2312 -340 C ATOM 1381 O ASP A1005 -68.957 -9.989 263.732 1.00162.90 O ANISOU 1381 O ASP A1005 21326 22516 18051 -518 -2114 -208 O ATOM 1382 CB ASP A1005 -67.146 -12.419 262.652 1.00157.24 C ANISOU 1382 CB ASP A1005 20886 20924 17934 -380 -2992 -722 C ATOM 1383 CG ASP A1005 -66.452 -12.733 263.963 1.00156.29 C ANISOU 1383 CG ASP A1005 20987 20515 17881 -430 -3252 -580 C ATOM 1384 OD1 ASP A1005 -66.902 -12.227 265.012 1.00154.72 O ANISOU 1384 OD1 ASP A1005 20862 20514 17410 -600 -3080 -256 O ATOM 1385 OD2 ASP A1005 -65.458 -13.489 263.944 1.00156.50 O ANISOU 1385 OD2 ASP A1005 21107 20125 18232 -290 -3651 -822 O ATOM 1386 N ASN A1006 -69.297 -10.221 261.516 1.00149.36 N ANISOU 1386 N ASN A1006 19431 20849 16472 -413 -2171 -475 N ATOM 1387 CA ASN A1006 -69.666 -8.818 261.356 1.00140.91 C ANISOU 1387 CA ASN A1006 18179 20091 15270 -289 -1828 -427 C ATOM 1388 C ASN A1006 -70.985 -8.508 262.051 1.00144.00 C ANISOU 1388 C ASN A1006 18410 20726 15579 -454 -1676 -161 C ATOM 1389 O ASN A1006 -71.101 -7.486 262.737 1.00145.83 O ANISOU 1389 O ASN A1006 18546 21130 15731 -345 -1431 -136 O ATOM 1390 CB ASN A1006 -69.737 -8.462 259.871 1.00132.27 C ANISOU 1390 CB ASN A1006 16992 19120 14144 -197 -1801 -567 C ATOM 1391 CG ASN A1006 -68.373 -8.455 259.209 1.00124.09 C ANISOU 1391 CG ASN A1006 16028 18002 13119 -26 -1796 -871 C ATOM 1392 OD1 ASN A1006 -68.091 -9.272 258.333 1.00121.69 O ANISOU 1392 OD1 ASN A1006 15771 17640 12824 -24 -1953 -1110 O ATOM 1393 ND2 ASN A1006 -67.518 -7.529 259.627 1.00121.31 N ANISOU 1393 ND2 ASN A1006 15652 17660 12778 117 -1614 -904 N ATOM 1394 N TRP A1007 -71.988 -9.380 261.902 1.00143.57 N ANISOU 1394 N TRP A1007 18287 20695 15568 -716 -1823 3 N ATOM 1395 CA TRP A1007 -73.248 -9.159 262.606 1.00145.99 C ANISOU 1395 CA TRP A1007 18354 21299 15815 -911 -1633 235 C ATOM 1396 C TRP A1007 -73.061 -9.263 264.113 1.00145.09 C ANISOU 1396 C TRP A1007 18358 21256 15515 -1054 -1504 378 C ATOM 1397 O TRP A1007 -73.660 -8.490 264.872 1.00148.27 O ANISOU 1397 O TRP A1007 18562 22002 15772 -1043 -1181 407 O ATOM 1398 CB TRP A1007 -74.319 -10.146 262.135 1.00152.37 C ANISOU 1398 CB TRP A1007 19036 22107 16750 -1225 -1848 408 C ATOM 1399 CG TRP A1007 -74.312 -10.443 260.666 1.00156.36 C ANISOU 1399 CG TRP A1007 19565 22462 17384 -1140 -2113 243 C ATOM 1400 CD1 TRP A1007 -74.191 -11.668 260.080 1.00160.34 C ANISOU 1400 CD1 TRP A1007 20237 22672 18014 -1288 -2503 188 C ATOM 1401 CD2 TRP A1007 -74.466 -9.500 259.597 1.00158.57 C ANISOU 1401 CD2 TRP A1007 19717 22883 17648 -908 -2050 107 C ATOM 1402 NE1 TRP A1007 -74.241 -11.546 258.712 1.00162.66 N ANISOU 1402 NE1 TRP A1007 20519 22976 18310 -1147 -2638 -26 N ATOM 1403 CE2 TRP A1007 -74.412 -10.225 258.390 1.00160.85 C ANISOU 1403 CE2 TRP A1007 20126 23022 17968 -944 -2368 -33 C ATOM 1404 CE3 TRP A1007 -74.638 -8.113 259.543 1.00159.68 C ANISOU 1404 CE3 TRP A1007 19679 23233 17758 -683 -1808 92 C ATOM 1405 CZ2 TRP A1007 -74.522 -9.611 257.145 1.00161.19 C ANISOU 1405 CZ2 TRP A1007 20143 23182 17918 -806 -2420 -142 C ATOM 1406 CZ3 TRP A1007 -74.747 -7.505 258.306 1.00160.11 C ANISOU 1406 CZ3 TRP A1007 19705 23327 17801 -552 -1916 31 C ATOM 1407 CH2 TRP A1007 -74.690 -8.254 257.124 1.00160.60 C ANISOU 1407 CH2 TRP A1007 19917 23301 17803 -636 -2203 -63 C ATOM 1408 N GLU A1008 -72.251 -10.225 264.567 1.00140.46 N ANISOU 1408 N GLU A1008 18094 20352 14924 -1187 -1786 446 N ATOM 1409 CA GLU A1008 -71.974 -10.330 265.997 1.00133.51 C ANISOU 1409 CA GLU A1008 17406 19522 13798 -1352 -1738 619 C ATOM 1410 C GLU A1008 -71.332 -9.055 266.536 1.00127.18 C ANISOU 1410 C GLU A1008 16613 18862 12849 -1025 -1468 400 C ATOM 1411 O GLU A1008 -71.735 -8.545 267.589 1.00130.02 O ANISOU 1411 O GLU A1008 16931 19549 12921 -1099 -1199 458 O ATOM 1412 CB GLU A1008 -71.080 -11.540 266.268 1.00132.00 C ANISOU 1412 CB GLU A1008 17587 18849 13718 -1498 -2223 717 C ATOM 1413 CG GLU A1008 -70.768 -11.768 267.738 1.00134.71 C ANISOU 1413 CG GLU A1008 18213 19201 13771 -1733 -2292 973 C ATOM 1414 CD GLU A1008 -69.822 -12.933 267.958 1.00137.95 C ANISOU 1414 CD GLU A1008 18996 19032 14387 -1836 -2897 1068 C ATOM 1415 OE1 GLU A1008 -69.636 -13.736 267.020 1.00139.01 O ANISOU 1415 OE1 GLU A1008 19130 18783 14902 -1784 -3251 944 O ATOM 1416 OE2 GLU A1008 -69.264 -13.046 269.070 1.00139.87 O ANISOU 1416 OE2 GLU A1008 19536 19185 14422 -1954 -3063 1238 O ATOM 1417 N THR A1009 -70.345 -8.517 265.813 1.00119.74 N ANISOU 1417 N THR A1009 15705 17699 12091 -680 -1530 125 N ATOM 1418 CA THR A1009 -69.695 -7.276 266.228 1.00112.21 C ANISOU 1418 CA THR A1009 14747 16806 11080 -386 -1342 -75 C ATOM 1419 C THR A1009 -70.683 -6.116 266.249 1.00107.91 C ANISOU 1419 C THR A1009 13897 16625 10478 -265 -999 -139 C ATOM 1420 O THR A1009 -70.707 -5.318 267.197 1.00110.25 O ANISOU 1420 O THR A1009 14182 17099 10609 -161 -811 -243 O ATOM 1421 CB THR A1009 -68.521 -6.968 265.297 1.00106.82 C ANISOU 1421 CB THR A1009 14094 15852 10642 -121 -1463 -308 C ATOM 1422 OG1 THR A1009 -67.540 -8.008 265.400 1.00103.05 O ANISOU 1422 OG1 THR A1009 13840 15030 10287 -166 -1797 -346 O ATOM 1423 CG2 THR A1009 -67.880 -5.637 265.662 1.00107.08 C ANISOU 1423 CG2 THR A1009 14096 15904 10683 137 -1315 -476 C ATOM 1424 N LEU A1010 -71.501 -6.002 265.199 1.00101.56 N ANISOU 1424 N LEU A1010 12841 15914 9834 -253 -962 -120 N ATOM 1425 CA LEU A1010 -72.489 -4.931 265.130 1.00100.76 C ANISOU 1425 CA LEU A1010 12401 16092 9791 -104 -730 -200 C ATOM 1426 C LEU A1010 -73.447 -4.988 266.313 1.00108.95 C ANISOU 1426 C LEU A1010 13267 17519 10610 -268 -464 -160 C ATOM 1427 O LEU A1010 -73.706 -3.971 266.963 1.00110.87 O ANISOU 1427 O LEU A1010 13347 17976 10803 -59 -236 -375 O ATOM 1428 CB LEU A1010 -73.255 -5.003 263.807 1.00 94.91 C ANISOU 1428 CB LEU A1010 11444 15359 9259 -120 -837 -135 C ATOM 1429 CG LEU A1010 -72.475 -4.664 262.533 1.00 86.07 C ANISOU 1429 CG LEU A1010 10442 13998 8263 37 -1019 -196 C ATOM 1430 CD1 LEU A1010 -73.325 -4.912 261.294 1.00 79.63 C ANISOU 1430 CD1 LEU A1010 9474 13231 7550 -46 -1176 -105 C ATOM 1431 CD2 LEU A1010 -71.978 -3.228 262.567 1.00 81.75 C ANISOU 1431 CD2 LEU A1010 9863 13388 7810 324 -949 -323 C ATOM 1432 N ASN A1011 -73.973 -6.177 266.618 1.00112.91 N ANISOU 1432 N ASN A1011 13794 18130 10976 -661 -495 98 N ATOM 1433 CA ASN A1011 -74.938 -6.294 267.709 1.00119.31 C ANISOU 1433 CA ASN A1011 14401 19415 11516 -914 -182 183 C ATOM 1434 C ASN A1011 -74.282 -6.038 269.062 1.00118.89 C ANISOU 1434 C ASN A1011 14624 19487 11062 -916 -47 109 C ATOM 1435 O ASN A1011 -74.884 -5.405 269.943 1.00123.12 O ANISOU 1435 O ASN A1011 14947 20486 11348 -885 319 -64 O ATOM 1436 CB ASN A1011 -75.597 -7.672 267.678 1.00123.45 C ANISOU 1436 CB ASN A1011 14914 19986 12004 -1423 -303 563 C ATOM 1437 CG ASN A1011 -76.808 -7.719 266.764 1.00120.32 C ANISOU 1437 CG ASN A1011 14060 19736 11919 -1481 -282 594 C ATOM 1438 OD1 ASN A1011 -77.917 -7.364 267.164 1.00123.36 O ANISOU 1438 OD1 ASN A1011 13993 20592 12284 -1562 48 555 O ATOM 1439 ND2 ASN A1011 -76.599 -8.159 265.528 1.00113.23 N ANISOU 1439 ND2 ASN A1011 13253 18459 11309 -1432 -644 627 N ATOM 1440 N ASP A1012 -73.047 -6.516 269.249 1.00116.83 N ANISOU 1440 N ASP A1012 14822 18832 10737 -936 -357 192 N ATOM 1441 CA ASP A1012 -72.353 -6.268 270.508 1.00120.91 C ANISOU 1441 CA ASP A1012 15646 19419 10876 -935 -325 128 C ATOM 1442 C ASP A1012 -72.121 -4.778 270.723 1.00120.72 C ANISOU 1442 C ASP A1012 15493 19488 10888 -479 -127 -306 C ATOM 1443 O ASP A1012 -72.370 -4.254 271.815 1.00125.33 O ANISOU 1443 O ASP A1012 16073 20447 11100 -463 130 -484 O ATOM 1444 CB ASP A1012 -71.026 -7.027 270.537 1.00121.77 C ANISOU 1444 CB ASP A1012 16214 19004 11049 -986 -792 265 C ATOM 1445 CG ASP A1012 -71.199 -8.488 270.903 1.00127.06 C ANISOU 1445 CG ASP A1012 17126 19580 11571 -1488 -1057 705 C ATOM 1446 OD1 ASP A1012 -72.054 -8.790 271.762 1.00132.80 O ANISOU 1446 OD1 ASP A1012 17825 20743 11889 -1877 -834 948 O ATOM 1447 OD2 ASP A1012 -70.478 -9.335 270.333 1.00125.66 O ANISOU 1447 OD2 ASP A1012 17151 18897 11698 -1508 -1499 798 O ATOM 1448 N ASN A1013 -71.671 -4.070 269.684 1.00117.30 N ANISOU 1448 N ASN A1013 14957 18728 10886 -127 -256 -488 N ATOM 1449 CA ASN A1013 -71.466 -2.634 269.837 1.00116.46 C ANISOU 1449 CA ASN A1013 14732 18616 10902 281 -159 -862 C ATOM 1450 C ASN A1013 -72.787 -1.882 269.963 1.00117.45 C ANISOU 1450 C ASN A1013 14403 19160 11062 418 171 -1088 C ATOM 1451 O ASN A1013 -72.840 -0.836 270.619 1.00118.29 O ANISOU 1451 O ASN A1013 14418 19396 11129 703 304 -1462 O ATOM 1452 CB ASN A1013 -70.645 -2.094 268.669 1.00110.42 C ANISOU 1452 CB ASN A1013 13981 17400 10576 530 -406 -908 C ATOM 1453 CG ASN A1013 -69.198 -2.543 268.720 1.00105.66 C ANISOU 1453 CG ASN A1013 13733 16421 9991 497 -688 -845 C ATOM 1454 OD1 ASN A1013 -68.566 -2.520 269.776 1.00103.97 O ANISOU 1454 OD1 ASN A1013 13767 16179 9559 492 -759 -923 O ATOM 1455 ND2 ASN A1013 -68.666 -2.958 267.577 1.00104.47 N ANISOU 1455 ND2 ASN A1013 13591 16005 10098 480 -861 -739 N ATOM 1456 N LEU A1014 -73.865 -2.406 269.372 1.00115.23 N ANISOU 1456 N LEU A1014 13806 19084 10890 235 276 -914 N ATOM 1457 CA LEU A1014 -75.182 -1.812 269.578 1.00116.13 C ANISOU 1457 CA LEU A1014 13406 19644 11074 346 595 -1151 C ATOM 1458 C LEU A1014 -75.587 -1.879 271.044 1.00123.09 C ANISOU 1458 C LEU A1014 14248 21092 11427 190 985 -1311 C ATOM 1459 O LEU A1014 -76.046 -0.886 271.620 1.00131.11 O ANISOU 1459 O LEU A1014 14979 22406 12430 494 1237 -1774 O ATOM 1460 CB LEU A1014 -76.222 -2.508 268.700 1.00111.72 C ANISOU 1460 CB LEU A1014 12512 19195 10742 116 587 -895 C ATOM 1461 CG LEU A1014 -76.252 -2.116 267.223 1.00104.41 C ANISOU 1461 CG LEU A1014 11475 17878 10317 333 268 -853 C ATOM 1462 CD1 LEU A1014 -77.250 -2.978 266.471 1.00107.73 C ANISOU 1462 CD1 LEU A1014 11625 18415 10891 46 209 -591 C ATOM 1463 CD2 LEU A1014 -76.590 -0.641 267.070 1.00 99.66 C ANISOU 1463 CD2 LEU A1014 10562 17234 10072 805 262 -1230 C ATOM 1464 N LYS A1015 -75.423 -3.047 271.669 1.00120.95 N ANISOU 1464 N LYS A1015 14273 20979 10702 -295 1015 -944 N ATOM 1465 CA LYS A1015 -75.766 -3.147 273.086 1.00125.31 C ANISOU 1465 CA LYS A1015 14855 22136 10621 -533 1391 -1030 C ATOM 1466 C LYS A1015 -74.803 -2.338 273.951 1.00129.32 C ANISOU 1466 C LYS A1015 15720 22560 10856 -238 1336 -1386 C ATOM 1467 O LYS A1015 -75.197 -1.830 275.011 1.00139.67 O ANISOU 1467 O LYS A1015 16928 24417 11724 -194 1700 -1741 O ATOM 1468 CB LYS A1015 -75.815 -4.614 273.523 1.00126.79 C ANISOU 1468 CB LYS A1015 15327 22457 10391 -1197 1344 -448 C ATOM 1469 CG LYS A1015 -74.493 -5.225 273.946 1.00128.27 C ANISOU 1469 CG LYS A1015 16197 22205 10333 -1354 921 -176 C ATOM 1470 CD LYS A1015 -74.694 -6.669 274.382 1.00137.55 C ANISOU 1470 CD LYS A1015 17628 23476 11160 -2037 802 432 C ATOM 1471 CE LYS A1015 -73.397 -7.302 274.855 1.00140.19 C ANISOU 1471 CE LYS A1015 18632 23324 11309 -2177 290 698 C ATOM 1472 NZ LYS A1015 -73.615 -8.690 275.350 1.00145.73 N ANISOU 1472 NZ LYS A1015 19620 24059 11690 -2872 82 1334 N ATOM 1473 N VAL A1016 -73.556 -2.172 273.499 1.00123.28 N ANISOU 1473 N VAL A1016 15336 21146 10360 -29 892 -1345 N ATOM 1474 CA VAL A1016 -72.612 -1.308 274.208 1.00116.62 C ANISOU 1474 CA VAL A1016 14788 20139 9383 278 762 -1703 C ATOM 1475 C VAL A1016 -73.111 0.132 274.206 1.00118.46 C ANISOU 1475 C VAL A1016 14627 20489 9891 789 945 -2306 C ATOM 1476 O VAL A1016 -73.111 0.811 275.240 1.00120.24 O ANISOU 1476 O VAL A1016 14896 21011 9777 965 1110 -2751 O ATOM 1477 CB VAL A1016 -71.207 -1.420 273.587 1.00102.53 C ANISOU 1477 CB VAL A1016 13372 17638 7948 382 256 -1532 C ATOM 1478 CG1 VAL A1016 -70.330 -0.263 274.039 1.00 99.15 C ANISOU 1478 CG1 VAL A1016 13105 16961 7608 773 84 -1951 C ATOM 1479 CG2 VAL A1016 -70.566 -2.746 273.962 1.00100.94 C ANISOU 1479 CG2 VAL A1016 13612 17301 7440 -48 1 -1077 C ATOM 1480 N ILE A1017 -73.541 0.618 273.039 1.00119.56 N ANISOU 1480 N ILE A1017 14397 20372 10658 1039 862 -2345 N ATOM 1481 CA ILE A1017 -74.120 1.958 272.953 1.00129.35 C ANISOU 1481 CA ILE A1017 15226 21641 12281 1530 936 -2891 C ATOM 1482 C ILE A1017 -75.375 2.048 273.811 1.00139.67 C ANISOU 1482 C ILE A1017 16097 23711 13259 1521 1456 -3260 C ATOM 1483 O ILE A1017 -75.628 3.067 274.466 1.00143.68 O ANISOU 1483 O ILE A1017 16408 24412 13772 1910 1594 -3889 O ATOM 1484 CB ILE A1017 -74.412 2.325 271.486 1.00129.28 C ANISOU 1484 CB ILE A1017 14935 21211 12976 1713 679 -2746 C ATOM 1485 CG1 ILE A1017 -73.125 2.306 270.663 1.00125.26 C ANISOU 1485 CG1 ILE A1017 14824 20053 12717 1699 245 -2430 C ATOM 1486 CG2 ILE A1017 -75.077 3.691 271.395 1.00131.22 C ANISOU 1486 CG2 ILE A1017 14746 21411 13703 2223 652 -3284 C ATOM 1487 CD1 ILE A1017 -73.356 2.367 269.172 1.00124.33 C ANISOU 1487 CD1 ILE A1017 14531 19616 13092 1719 14 -2154 C ATOM 1488 N GLU A1018 -76.178 0.981 273.823 1.00143.31 N ANISOU 1488 N GLU A1018 16372 24631 13449 1070 1751 -2907 N ATOM 1489 CA GLU A1018 -77.420 0.994 274.590 1.00151.89 C ANISOU 1489 CA GLU A1018 16952 26540 14218 983 2317 -3223 C ATOM 1490 C GLU A1018 -77.152 1.142 276.082 1.00160.22 C ANISOU 1490 C GLU A1018 18268 28120 14489 912 2626 -3557 C ATOM 1491 O GLU A1018 -77.894 1.839 276.785 1.00168.98 O ANISOU 1491 O GLU A1018 18959 29813 15434 1156 3044 -4190 O ATOM 1492 CB GLU A1018 -78.225 -0.277 274.316 1.00152.21 C ANISOU 1492 CB GLU A1018 16786 26932 14115 401 2524 -2671 C ATOM 1493 CG GLU A1018 -79.602 -0.278 274.963 1.00159.67 C ANISOU 1493 CG GLU A1018 17070 28777 14821 261 3150 -2964 C ATOM 1494 CD GLU A1018 -80.471 -1.428 274.494 1.00159.10 C ANISOU 1494 CD GLU A1018 16694 28954 14803 -299 3275 -2407 C ATOM 1495 OE1 GLU A1018 -80.100 -2.090 273.502 1.00152.21 O ANISOU 1495 OE1 GLU A1018 16075 27488 14272 -462 2825 -1891 O ATOM 1496 OE2 GLU A1018 -81.525 -1.669 275.119 1.00164.98 O ANISOU 1496 OE2 GLU A1018 16926 30510 15250 -589 3827 -2512 O ATOM 1497 N LYS A1019 -76.098 0.503 276.589 1.00159.19 N ANISOU 1497 N LYS A1019 18816 27803 13865 594 2404 -3182 N ATOM 1498 CA LYS A1019 -75.769 0.638 278.003 1.00167.08 C ANISOU 1498 CA LYS A1019 20154 29275 14053 498 2611 -3462 C ATOM 1499 C LYS A1019 -74.772 1.759 278.280 1.00163.61 C ANISOU 1499 C LYS A1019 20023 28367 13775 1030 2259 -3978 C ATOM 1500 O LYS A1019 -74.409 1.970 279.442 1.00170.50 O ANISOU 1500 O LYS A1019 21226 29571 13984 1006 2348 -4278 O ATOM 1501 CB LYS A1019 -75.219 -0.680 278.562 1.00166.56 C ANISOU 1501 CB LYS A1019 20681 29287 13316 -180 2494 -2763 C ATOM 1502 CG LYS A1019 -73.743 -0.921 278.292 1.00159.13 C ANISOU 1502 CG LYS A1019 20379 27514 12568 -145 1831 -2443 C ATOM 1503 CD LYS A1019 -73.229 -2.080 279.132 1.00159.62 C ANISOU 1503 CD LYS A1019 21038 27698 11910 -758 1670 -1879 C ATOM 1504 CE LYS A1019 -71.730 -2.265 278.974 1.00153.01 C ANISOU 1504 CE LYS A1019 20775 26053 11309 -666 988 -1665 C ATOM 1505 NZ LYS A1019 -71.207 -3.328 279.877 1.00153.92 N ANISOU 1505 NZ LYS A1019 21496 26229 10757 -1224 722 -1146 N ATOM 1506 N ALA A1020 -74.334 2.484 277.255 1.00147.21 N ANISOU 1506 N ALA A1020 17856 25543 12534 1468 1842 -4070 N ATOM 1507 CA ALA A1020 -73.359 3.548 277.446 1.00138.25 C ANISOU 1507 CA ALA A1020 16994 23887 11648 1920 1446 -4494 C ATOM 1508 C ALA A1020 -73.984 4.750 278.148 1.00139.09 C ANISOU 1508 C ALA A1020 16755 24353 11739 2413 1689 -5391 C ATOM 1509 O ALA A1020 -75.193 4.986 278.075 1.00141.41 O ANISOU 1509 O ALA A1020 16447 25123 12159 2557 2093 -5726 O ATOM 1510 CB ALA A1020 -72.770 3.981 276.104 1.00130.37 C ANISOU 1510 CB ALA A1020 15965 22033 11535 2164 953 -4272 C ATOM 1511 N ASP A1021 -73.134 5.515 278.838 1.00137.69 N ANISOU 1511 N ASP A1021 16939 23926 11450 2694 1405 -5830 N ATOM 1512 CA ASP A1021 -73.563 6.699 279.567 1.00141.26 C ANISOU 1512 CA ASP A1021 17142 24632 11900 3216 1537 -6784 C ATOM 1513 C ASP A1021 -72.731 7.936 279.255 1.00140.50 C ANISOU 1513 C ASP A1021 17176 23667 12542 3739 908 -7159 C ATOM 1514 O ASP A1021 -72.956 8.982 279.874 1.00142.14 O ANISOU 1514 O ASP A1021 17233 23946 12827 4222 888 -8009 O ATOM 1515 CB ASP A1021 -73.525 6.445 281.083 1.00142.26 C ANISOU 1515 CB ASP A1021 17598 25450 11004 2977 1863 -7047 C ATOM 1516 CG ASP A1021 -72.152 6.018 281.569 1.00138.20 C ANISOU 1516 CG ASP A1021 17863 24593 10054 2703 1421 -6678 C ATOM 1517 OD1 ASP A1021 -71.261 5.783 280.726 1.00131.74 O ANISOU 1517 OD1 ASP A1021 17274 23053 9727 2649 931 -6173 O ATOM 1518 OD2 ASP A1021 -71.958 5.937 282.799 1.00144.43 O ANISOU 1518 OD2 ASP A1021 19023 25663 10192 2486 1517 -6761 O ATOM 1519 N ASN A1022 -71.784 7.850 278.325 1.00135.20 N ANISOU 1519 N ASN A1022 16758 22194 12416 3643 395 -6575 N ATOM 1520 CA ASN A1022 -70.960 8.987 277.936 1.00135.59 C ANISOU 1520 CA ASN A1022 16916 21394 13208 4031 -222 -6798 C ATOM 1521 C ASN A1022 -70.863 9.009 276.414 1.00135.71 C ANISOU 1521 C ASN A1022 16743 20796 14025 3983 -507 -6211 C ATOM 1522 O ASN A1022 -71.577 8.283 275.715 1.00134.62 O ANISOU 1522 O ASN A1022 16342 20910 13897 3757 -229 -5794 O ATOM 1523 CB ASN A1022 -69.583 8.913 278.609 1.00130.15 C ANISOU 1523 CB ASN A1022 16842 20406 12205 3888 -598 -6720 C ATOM 1524 CG ASN A1022 -68.778 7.714 278.154 1.00123.04 C ANISOU 1524 CG ASN A1022 16269 19350 11132 3367 -692 -5861 C ATOM 1525 OD1 ASN A1022 -68.023 7.788 277.185 1.00116.99 O ANISOU 1525 OD1 ASN A1022 15538 17942 10971 3319 -1062 -5440 O ATOM 1526 ND2 ASN A1022 -68.936 6.597 278.855 1.00125.65 N ANISOU 1526 ND2 ASN A1022 16830 20276 10636 2962 -368 -5608 N ATOM 1527 N ALA A1023 -69.969 9.850 275.895 1.00137.08 N ANISOU 1527 N ALA A1023 17061 20175 14850 4159 -1081 -6166 N ATOM 1528 CA ALA A1023 -69.797 10.005 274.455 1.00139.17 C ANISOU 1528 CA ALA A1023 17189 19872 15817 4084 -1379 -5616 C ATOM 1529 C ALA A1023 -68.623 9.220 273.888 1.00127.88 C ANISOU 1529 C ALA A1023 16106 18166 14318 3649 -1536 -4907 C ATOM 1530 O ALA A1023 -68.667 8.827 272.718 1.00123.06 O ANISOU 1530 O ALA A1023 15383 17404 13968 3440 -1551 -4366 O ATOM 1531 CB ALA A1023 -69.623 11.486 274.100 1.00146.30 C ANISOU 1531 CB ALA A1023 17974 20059 17553 4497 -1935 -5946 C ATOM 1532 N ALA A1024 -67.572 8.988 274.679 1.00127.39 N ANISOU 1532 N ALA A1024 16441 18039 13922 3524 -1676 -4938 N ATOM 1533 CA ALA A1024 -66.406 8.271 274.169 1.00114.65 C ANISOU 1533 CA ALA A1024 15082 16145 12336 3165 -1855 -4356 C ATOM 1534 C ALA A1024 -66.743 6.823 273.833 1.00111.84 C ANISOU 1534 C ALA A1024 14734 16211 11548 2794 -1494 -3871 C ATOM 1535 O ALA A1024 -66.336 6.313 272.779 1.00104.18 O ANISOU 1535 O ALA A1024 13731 15032 10820 2573 -1553 -3383 O ATOM 1536 CB ALA A1024 -65.266 8.336 275.185 1.00112.46 C ANISOU 1536 CB ALA A1024 15193 15702 11835 3143 -2144 -4547 C ATOM 1537 N GLN A1025 -67.476 6.144 274.719 1.00119.67 N ANISOU 1537 N GLN A1025 15772 17810 11888 2697 -1128 -4009 N ATOM 1538 CA GLN A1025 -67.877 4.765 274.454 1.00127.30 C ANISOU 1538 CA GLN A1025 16747 19139 12482 2313 -841 -3537 C ATOM 1539 C GLN A1025 -68.711 4.664 273.184 1.00134.27 C ANISOU 1539 C GLN A1025 17246 20016 13753 2298 -698 -3279 C ATOM 1540 O GLN A1025 -68.501 3.760 272.365 1.00136.77 O ANISOU 1540 O GLN A1025 17596 20251 14121 2024 -712 -2804 O ATOM 1541 CB GLN A1025 -68.655 4.206 275.645 1.00135.93 C ANISOU 1541 CB GLN A1025 17911 20925 12810 2166 -459 -3714 C ATOM 1542 CG GLN A1025 -67.841 4.065 276.919 1.00140.74 C ANISOU 1542 CG GLN A1025 18995 21608 12872 2076 -627 -3865 C ATOM 1543 CD GLN A1025 -68.659 3.511 278.070 1.00149.99 C ANISOU 1543 CD GLN A1025 20256 23558 13176 1847 -210 -3983 C ATOM 1544 OE1 GLN A1025 -69.840 3.199 277.913 1.00151.69 O ANISOU 1544 OE1 GLN A1025 20122 24274 13239 1742 240 -3951 O ATOM 1545 NE2 GLN A1025 -68.034 3.385 279.235 1.00155.63 N ANISOU 1545 NE2 GLN A1025 21432 24405 13297 1733 -368 -4103 N ATOM 1546 N VAL A1026 -69.660 5.585 272.999 1.00131.04 N ANISOU 1546 N VAL A1026 16469 19675 13644 2612 -610 -3625 N ATOM 1547 CA VAL A1026 -70.511 5.542 271.815 1.00127.71 C ANISOU 1547 CA VAL A1026 15685 19235 13604 2609 -551 -3388 C ATOM 1548 C VAL A1026 -69.687 5.784 270.556 1.00126.20 C ANISOU 1548 C VAL A1026 15577 18466 13906 2551 -916 -2996 C ATOM 1549 O VAL A1026 -69.882 5.114 269.534 1.00122.31 O ANISOU 1549 O VAL A1026 15014 17981 13477 2328 -883 -2579 O ATOM 1550 CB VAL A1026 -71.658 6.561 271.946 1.00126.54 C ANISOU 1550 CB VAL A1026 15098 19220 13763 3011 -472 -3899 C ATOM 1551 CG1 VAL A1026 -72.570 6.498 270.729 1.00122.74 C ANISOU 1551 CG1 VAL A1026 14242 18699 13695 3001 -489 -3633 C ATOM 1552 CG2 VAL A1026 -72.446 6.314 273.222 1.00130.84 C ANISOU 1552 CG2 VAL A1026 15511 20464 13739 3041 -15 -4344 C ATOM 1553 N LYS A1027 -68.752 6.736 270.609 1.00126.35 N ANISOU 1553 N LYS A1027 15745 18005 14256 2719 -1268 -3129 N ATOM 1554 CA LYS A1027 -67.903 7.009 269.454 1.00121.66 C ANISOU 1554 CA LYS A1027 15213 16931 14080 2592 -1572 -2734 C ATOM 1555 C LYS A1027 -67.066 5.789 269.087 1.00118.56 C ANISOU 1555 C LYS A1027 15024 16606 13416 2229 -1485 -2329 C ATOM 1556 O LYS A1027 -66.971 5.419 267.911 1.00119.40 O ANISOU 1556 O LYS A1027 15070 16651 13644 2038 -1492 -1956 O ATOM 1557 CB LYS A1027 -67.005 8.214 269.736 1.00124.58 C ANISOU 1557 CB LYS A1027 15695 16788 14851 2777 -1971 -2943 C ATOM 1558 CG LYS A1027 -66.037 8.538 268.611 1.00122.43 C ANISOU 1558 CG LYS A1027 15467 16075 14976 2564 -2252 -2502 C ATOM 1559 N ASP A1028 -66.453 5.149 270.086 1.00112.94 N ANISOU 1559 N ASP A1028 14561 16018 12334 2141 -1440 -2427 N ATOM 1560 CA ASP A1028 -65.619 3.982 269.810 1.00104.53 C ANISOU 1560 CA ASP A1028 13669 14944 11105 1851 -1443 -2109 C ATOM 1561 C ASP A1028 -66.449 2.822 269.268 1.00 98.38 C ANISOU 1561 C ASP A1028 12804 14490 10084 1640 -1194 -1846 C ATOM 1562 O ASP A1028 -66.030 2.131 268.326 1.00 91.85 O ANISOU 1562 O ASP A1028 11975 13579 9345 1459 -1222 -1570 O ATOM 1563 CB ASP A1028 -64.869 3.568 271.078 1.00105.13 C ANISOU 1563 CB ASP A1028 14048 15035 10864 1813 -1552 -2262 C ATOM 1564 CG ASP A1028 -63.878 2.446 270.834 1.00101.71 C ANISOU 1564 CG ASP A1028 13766 14476 10402 1576 -1676 -1994 C ATOM 1565 OD1 ASP A1028 -63.131 2.515 269.835 1.00100.82 O ANISOU 1565 OD1 ASP A1028 13533 14113 10661 1526 -1774 -1841 O ATOM 1566 OD2 ASP A1028 -63.837 1.499 271.648 1.00100.61 O ANISOU 1566 OD2 ASP A1028 13858 14495 9874 1431 -1692 -1947 O ATOM 1567 N ALA A1029 -67.640 2.605 269.838 1.00102.99 N ANISOU 1567 N ALA A1029 13288 15468 10378 1654 -946 -1959 N ATOM 1568 CA ALA A1029 -68.498 1.526 269.366 1.00104.25 C ANISOU 1568 CA ALA A1029 13337 15919 10354 1419 -746 -1698 C ATOM 1569 C ALA A1029 -68.961 1.768 267.937 1.00103.32 C ANISOU 1569 C ALA A1029 12975 15694 10588 1439 -783 -1520 C ATOM 1570 O ALA A1029 -68.989 0.837 267.125 1.00107.44 O ANISOU 1570 O ALA A1029 13509 16235 11078 1223 -784 -1248 O ATOM 1571 CB ALA A1029 -69.700 1.365 270.295 1.00108.44 C ANISOU 1571 CB ALA A1029 13731 16945 10526 1396 -439 -1863 C ATOM 1572 N LEU A1030 -69.314 3.014 267.603 1.00 96.63 N ANISOU 1572 N LEU A1030 11930 14700 10085 1696 -874 -1675 N ATOM 1573 CA LEU A1030 -69.722 3.326 266.236 1.00 91.66 C ANISOU 1573 CA LEU A1030 11122 13938 9765 1687 -997 -1452 C ATOM 1574 C LEU A1030 -68.550 3.226 265.268 1.00 89.49 C ANISOU 1574 C LEU A1030 11024 13385 9593 1523 -1166 -1182 C ATOM 1575 O LEU A1030 -68.740 2.842 264.109 1.00 86.63 O ANISOU 1575 O LEU A1030 10619 13054 9241 1364 -1193 -925 O ATOM 1576 CB LEU A1030 -70.363 4.714 266.180 1.00 90.08 C ANISOU 1576 CB LEU A1030 10689 13574 9965 2003 -1157 -1668 C ATOM 1577 CG LEU A1030 -71.759 4.816 266.803 1.00 92.49 C ANISOU 1577 CG LEU A1030 10660 14229 10253 2189 -955 -1974 C ATOM 1578 CD1 LEU A1030 -72.153 6.266 266.967 1.00 96.24 C ANISOU 1578 CD1 LEU A1030 10918 14450 11197 2593 -1185 -2330 C ATOM 1579 CD2 LEU A1030 -72.793 4.078 265.954 1.00 83.14 C ANISOU 1579 CD2 LEU A1030 9243 13282 9063 2018 -872 -1722 C ATOM 1580 N THR A1031 -67.335 3.549 265.724 1.00 87.98 N ANISOU 1580 N THR A1031 11007 12960 9460 1544 -1275 -1263 N ATOM 1581 CA THR A1031 -66.148 3.334 264.899 1.00 84.82 C ANISOU 1581 CA THR A1031 10700 12388 9138 1360 -1359 -1056 C ATOM 1582 C THR A1031 -65.989 1.856 264.558 1.00 84.09 C ANISOU 1582 C THR A1031 10678 12495 8778 1153 -1225 -946 C ATOM 1583 O THR A1031 -65.795 1.488 263.391 1.00 80.94 O ANISOU 1583 O THR A1031 10243 12139 8372 1000 -1206 -771 O ATOM 1584 CB THR A1031 -64.903 3.861 265.618 1.00 82.71 C ANISOU 1584 CB THR A1031 10549 11852 9025 1419 -1511 -1204 C ATOM 1585 OG1 THR A1031 -65.103 5.235 265.971 1.00 89.06 O ANISOU 1585 OG1 THR A1031 11302 12413 10122 1628 -1701 -1351 O ATOM 1586 CG2 THR A1031 -63.673 3.742 264.726 1.00 76.25 C ANISOU 1586 CG2 THR A1031 9718 10908 8346 1218 -1556 -1018 C ATOM 1587 N LYS A1032 -66.047 0.994 265.577 1.00 84.21 N ANISOU 1587 N LYS A1032 10815 12623 8558 1135 -1166 -1057 N ATOM 1588 CA LYS A1032 -65.949 -0.442 265.327 1.00 85.92 C ANISOU 1588 CA LYS A1032 11114 12936 8596 946 -1138 -957 C ATOM 1589 C LYS A1032 -67.100 -0.936 264.454 1.00 93.54 C ANISOU 1589 C LYS A1032 11950 14108 9482 838 -1046 -805 C ATOM 1590 O LYS A1032 -66.912 -1.838 263.627 1.00 91.12 O ANISOU 1590 O LYS A1032 11667 13812 9141 701 -1078 -728 O ATOM 1591 CB LYS A1032 -65.899 -1.202 266.653 1.00 78.45 C ANISOU 1591 CB LYS A1032 10363 12035 7410 894 -1172 -1020 C ATOM 1592 CG LYS A1032 -64.715 -0.812 267.524 1.00 74.74 C ANISOU 1592 CG LYS A1032 10052 11336 7010 991 -1347 -1176 C ATOM 1593 CD LYS A1032 -64.692 -1.571 268.840 1.00 72.55 C ANISOU 1593 CD LYS A1032 10034 11115 6418 895 -1443 -1183 C ATOM 1594 CE LYS A1032 -63.556 -1.079 269.724 1.00 72.11 C ANISOU 1594 CE LYS A1032 10150 10821 6430 1008 -1684 -1356 C ATOM 1595 NZ LYS A1032 -63.504 -1.793 271.028 1.00 74.57 N ANISOU 1595 NZ LYS A1032 10779 11190 6363 879 -1841 -1322 N ATOM 1596 N MET A1033 -68.287 -0.343 264.606 1.00 96.74 N ANISOU 1596 N MET A1033 12191 14671 9893 920 -960 -808 N ATOM 1597 CA MET A1033 -69.427 -0.738 263.784 1.00 92.93 C ANISOU 1597 CA MET A1033 11544 14369 9398 822 -928 -667 C ATOM 1598 C MET A1033 -69.211 -0.369 262.324 1.00 95.69 C ANISOU 1598 C MET A1033 11863 14622 9873 791 -1047 -526 C ATOM 1599 O MET A1033 -69.564 -1.141 261.428 1.00 93.20 O ANISOU 1599 O MET A1033 11544 14404 9466 638 -1084 -414 O ATOM 1600 CB MET A1033 -70.709 -0.092 264.307 1.00 87.15 C ANISOU 1600 CB MET A1033 10557 13829 8726 954 -824 -761 C ATOM 1601 CG MET A1033 -71.299 -0.773 265.522 1.00 85.42 C ANISOU 1601 CG MET A1033 10315 13895 8245 853 -623 -833 C ATOM 1602 SD MET A1033 -72.904 -0.090 265.972 1.00 89.45 S ANISOU 1602 SD MET A1033 10384 14755 8849 1004 -419 -1020 S ATOM 1603 CE MET A1033 -73.879 -0.570 264.548 1.00 90.06 C ANISOU 1603 CE MET A1033 10224 14862 9132 863 -553 -770 C ATOM 1604 N ARG A1034 -68.655 0.815 262.063 1.00 99.35 N ANISOU 1604 N ARG A1034 12322 14902 10524 902 -1136 -516 N ATOM 1605 CA ARG A1034 -68.353 1.194 260.687 1.00 98.07 C ANISOU 1605 CA ARG A1034 12175 14691 10395 787 -1244 -312 C ATOM 1606 C ARG A1034 -67.263 0.305 260.106 1.00 96.58 C ANISOU 1606 C ARG A1034 12109 14560 10027 614 -1164 -324 C ATOM 1607 O ARG A1034 -67.306 -0.048 258.922 1.00 93.93 O ANISOU 1607 O ARG A1034 11794 14362 9532 459 -1174 -215 O ATOM 1608 CB ARG A1034 -67.935 2.662 260.615 1.00 99.47 C ANISOU 1608 CB ARG A1034 12335 14618 10840 877 -1400 -238 C ATOM 1609 CG ARG A1034 -67.850 3.199 259.192 1.00105.22 C ANISOU 1609 CG ARG A1034 13093 15324 11560 690 -1553 78 C ATOM 1610 CD ARG A1034 -67.121 4.533 259.131 1.00109.31 C ANISOU 1610 CD ARG A1034 13638 15544 12351 676 -1737 220 C ATOM 1611 NE ARG A1034 -67.319 5.205 257.848 1.00111.31 N ANISOU 1611 NE ARG A1034 13939 15757 12595 464 -1962 612 N ATOM 1612 CZ ARG A1034 -66.630 4.933 256.744 1.00111.61 C ANISOU 1612 CZ ARG A1034 14079 16007 12323 132 -1864 847 C ATOM 1613 NH1 ARG A1034 -65.696 3.992 256.754 1.00111.95 N ANISOU 1613 NH1 ARG A1034 14125 16290 12121 34 -1544 658 N ATOM 1614 NH2 ARG A1034 -66.882 5.598 255.625 1.00112.26 N ANISOU 1614 NH2 ARG A1034 14251 16073 12329 -105 -2106 1256 N ATOM 1615 N ALA A1035 -66.272 -0.060 260.924 1.00102.26 N ANISOU 1615 N ALA A1035 12898 15182 10773 654 -1108 -498 N ATOM 1616 CA ALA A1035 -65.227 -0.962 260.449 1.00101.11 C ANISOU 1616 CA ALA A1035 12796 15073 10549 551 -1056 -606 C ATOM 1617 C ALA A1035 -65.800 -2.325 260.079 1.00100.36 C ANISOU 1617 C ALA A1035 12744 15107 10282 472 -1069 -661 C ATOM 1618 O ALA A1035 -65.404 -2.921 259.070 1.00 96.08 O ANISOU 1618 O ALA A1035 12198 14678 9630 381 -1041 -741 O ATOM 1619 CB ALA A1035 -64.135 -1.109 261.509 1.00 97.59 C ANISOU 1619 CB ALA A1035 12393 14438 10248 641 -1091 -792 C ATOM 1620 N ALA A1036 -66.736 -2.835 260.883 1.00103.34 N ANISOU 1620 N ALA A1036 13152 15486 10628 484 -1113 -636 N ATOM 1621 CA ALA A1036 -67.336 -4.134 260.598 1.00101.60 C ANISOU 1621 CA ALA A1036 12971 15325 10306 363 -1192 -645 C ATOM 1622 C ALA A1036 -68.375 -4.072 259.484 1.00101.74 C ANISOU 1622 C ALA A1036 12907 15516 10233 275 -1223 -517 C ATOM 1623 O ALA A1036 -68.622 -5.085 258.819 1.00101.12 O ANISOU 1623 O ALA A1036 12871 15476 10073 167 -1327 -572 O ATOM 1624 CB ALA A1036 -67.970 -4.708 261.866 1.00101.64 C ANISOU 1624 CB ALA A1036 13027 15304 10287 313 -1227 -588 C ATOM 1625 N ALA A1037 -68.991 -2.911 259.262 1.00106.72 N ANISOU 1625 N ALA A1037 13428 16210 10911 329 -1204 -366 N ATOM 1626 CA ALA A1037 -70.072 -2.784 258.296 1.00112.35 C ANISOU 1626 CA ALA A1037 14057 17051 11582 256 -1320 -216 C ATOM 1627 C ALA A1037 -69.589 -2.544 256.874 1.00117.12 C ANISOU 1627 C ALA A1037 14756 17743 12003 154 -1377 -154 C ATOM 1628 O ALA A1037 -70.413 -2.533 255.953 1.00123.99 O ANISOU 1628 O ALA A1037 15615 18719 12777 64 -1539 -23 O ATOM 1629 CB ALA A1037 -71.016 -1.648 258.707 1.00115.12 C ANISOU 1629 CB ALA A1037 14216 17389 12134 388 -1355 -105 C ATOM 1630 N LEU A1038 -68.286 -2.345 256.669 1.00113.78 N ANISOU 1630 N LEU A1038 14411 17313 11509 140 -1251 -241 N ATOM 1631 CA LEU A1038 -67.775 -2.225 255.309 1.00113.38 C ANISOU 1631 CA LEU A1038 14437 17462 11179 -22 -1227 -200 C ATOM 1632 C LEU A1038 -67.890 -3.551 254.570 1.00122.26 C ANISOU 1632 C LEU A1038 15636 18749 12068 -99 -1263 -430 C ATOM 1633 O LEU A1038 -68.152 -3.577 253.362 1.00126.76 O ANISOU 1633 O LEU A1038 16292 19543 12330 -246 -1333 -375 O ATOM 1634 CB LEU A1038 -66.328 -1.735 255.327 1.00104.37 C ANISOU 1634 CB LEU A1038 13277 16332 10047 -49 -1030 -267 C ATOM 1635 CG LEU A1038 -66.155 -0.219 255.432 1.00 99.30 C ANISOU 1635 CG LEU A1038 12608 15561 9559 -83 -1075 37 C ATOM 1636 CD1 LEU A1038 -64.683 0.157 255.486 1.00 98.06 C ANISOU 1636 CD1 LEU A1038 12385 15417 9455 -159 -884 -30 C ATOM 1637 CD2 LEU A1038 -66.853 0.483 254.276 1.00100.76 C ANISOU 1637 CD2 LEU A1038 12878 15863 9544 -271 -1254 390 C ATOM 1638 N ASP A1039 -67.691 -4.662 255.283 1.00123.58 N ANISOU 1638 N ASP A1039 15799 18781 12376 -11 -1272 -692 N ATOM 1639 CA ASP A1039 -67.684 -5.971 254.641 1.00133.85 C ANISOU 1639 CA ASP A1039 17171 20142 13546 -50 -1376 -982 C ATOM 1640 C ASP A1039 -69.067 -6.349 254.124 1.00146.09 C ANISOU 1640 C ASP A1039 18756 21734 15018 -156 -1621 -848 C ATOM 1641 O ASP A1039 -69.179 -7.131 253.174 1.00151.06 O ANISOU 1641 O ASP A1039 19476 22478 15442 -224 -1751 -1057 O ATOM 1642 CB ASP A1039 -67.178 -7.029 255.621 1.00129.92 C ANISOU 1642 CB ASP A1039 16676 19374 13313 58 -1446 -1232 C ATOM 1643 CG ASP A1039 -65.787 -6.725 256.140 1.00130.06 C ANISOU 1643 CG ASP A1039 16628 19320 13470 179 -1275 -1398 C ATOM 1644 OD1 ASP A1039 -65.053 -5.967 255.472 1.00131.87 O ANISOU 1644 OD1 ASP A1039 16786 19768 13552 150 -1060 -1422 O ATOM 1645 OD2 ASP A1039 -65.428 -7.243 257.220 1.00129.34 O ANISOU 1645 OD2 ASP A1039 16555 18954 13635 269 -1383 -1476 O ATOM 1646 N ALA A1040 -70.123 -5.808 254.732 1.00149.53 N ANISOU 1646 N ALA A1040 19090 22091 15632 -159 -1698 -552 N ATOM 1647 CA ALA A1040 -71.488 -6.181 254.386 1.00155.16 C ANISOU 1647 CA ALA A1040 19748 22828 16378 -262 -1948 -425 C ATOM 1648 C ALA A1040 -72.057 -5.335 253.254 1.00163.38 C ANISOU 1648 C ALA A1040 20809 24039 17228 -333 -2094 -217 C ATOM 1649 O ALA A1040 -72.697 -5.872 252.343 1.00168.96 O ANISOU 1649 O ALA A1040 21582 24835 17781 -449 -2345 -242 O ATOM 1650 CB ALA A1040 -72.390 -6.069 255.618 1.00153.40 C ANISOU 1650 CB ALA A1040 19323 22500 16461 -239 -1934 -254 C ATOM 1651 N GLY A1041 -71.840 -4.024 253.294 1.00164.63 N ANISOU 1651 N GLY A1041 20935 24204 17411 -279 -2012 2 N ATOM 1652 CA GLY A1041 -72.448 -3.116 252.346 1.00161.56 C ANISOU 1652 CA GLY A1041 20580 23892 16913 -360 -2251 288 C ATOM 1653 C GLY A1041 -71.727 -3.088 251.014 1.00160.57 C ANISOU 1653 C GLY A1041 20714 24019 16278 -550 -2251 293 C ATOM 1654 O GLY A1041 -70.991 -4.008 250.647 1.00159.73 O ANISOU 1654 O GLY A1041 20718 24073 15898 -598 -2094 -27 O ATOM 1655 N SER A1042 -71.948 -2.002 250.280 1.00157.78 N ANISOU 1655 N SER A1042 20451 23707 15791 -668 -2448 652 N ATOM 1656 CA SER A1042 -71.333 -1.820 248.971 1.00151.04 C ANISOU 1656 CA SER A1042 19867 23172 14349 -935 -2444 753 C ATOM 1657 C SER A1042 -70.179 -0.826 249.044 1.00147.55 C ANISOU 1657 C SER A1042 19458 22767 13838 -1034 -2186 942 C ATOM 1658 O SER A1042 -69.862 -0.306 250.114 1.00140.89 O ANISOU 1658 O SER A1042 18445 21653 13433 -860 -2060 953 O ATOM 1659 CB SER A1042 -72.371 -1.349 247.951 1.00148.59 C ANISOU 1659 CB SER A1042 19705 22898 13855 -1100 -2934 1112 C ATOM 1660 OG SER A1042 -73.051 -0.194 248.412 1.00145.95 O ANISOU 1660 OG SER A1042 19227 22225 14003 -992 -3225 1476 O ATOM 1661 N ASP A1066 -73.477 2.780 250.758 1.00126.44 N ANISOU 1661 N ASP A1066 16224 18774 13045 -428 -3479 1860 N ATOM 1662 CA ASP A1066 -74.210 1.909 251.669 1.00123.81 C ANISOU 1662 CA ASP A1066 15592 18464 12985 -183 -3313 1485 C ATOM 1663 C ASP A1066 -75.004 2.726 252.684 1.00123.90 C ANISOU 1663 C ASP A1066 15248 18177 13652 154 -3452 1406 C ATOM 1664 O ASP A1066 -74.473 3.643 253.309 1.00125.26 O ANISOU 1664 O ASP A1066 15394 18120 14079 293 -3403 1406 O ATOM 1665 CB ASP A1066 -73.255 0.955 252.386 1.00119.82 C ANISOU 1665 CB ASP A1066 15110 18124 12292 -172 -2787 1144 C ATOM 1666 CG ASP A1066 -73.984 -0.124 253.162 1.00118.24 C ANISOU 1666 CG ASP A1066 14685 17985 12256 -50 -2657 854 C ATOM 1667 OD1 ASP A1066 -74.796 -0.850 252.551 1.00119.23 O ANISOU 1667 OD1 ASP A1066 14791 18221 12289 -152 -2862 855 O ATOM 1668 OD2 ASP A1066 -73.741 -0.249 254.380 1.00116.26 O ANISOU 1668 OD2 ASP A1066 14291 17672 12209 108 -2378 649 O ATOM 1669 N ILE A1067 -76.285 2.383 252.838 1.00124.54 N ANISOU 1669 N ILE A1067 15023 18276 14021 285 -3630 1298 N ATOM 1670 CA ILE A1067 -77.158 3.135 253.735 1.00126.44 C ANISOU 1670 CA ILE A1067 14838 18313 14891 630 -3742 1135 C ATOM 1671 C ILE A1067 -76.728 2.950 255.186 1.00121.41 C ANISOU 1671 C ILE A1067 14041 17746 14343 815 -3225 776 C ATOM 1672 O ILE A1067 -76.745 3.900 255.980 1.00122.46 O ANISOU 1672 O ILE A1067 13994 17678 14857 1094 -3229 617 O ATOM 1673 CB ILE A1067 -78.623 2.713 253.520 1.00130.53 C ANISOU 1673 CB ILE A1067 14989 18913 15692 687 -4010 1080 C ATOM 1674 CG1 ILE A1067 -79.011 2.865 252.047 1.00134.08 C ANISOU 1674 CG1 ILE A1067 15664 19285 15995 481 -4599 1452 C ATOM 1675 CG2 ILE A1067 -79.553 3.527 254.407 1.00134.08 C ANISOU 1675 CG2 ILE A1067 14908 19211 16826 1075 -4100 831 C ATOM 1676 CD1 ILE A1067 -80.445 2.483 251.750 1.00137.01 C ANISOU 1676 CD1 ILE A1067 15660 19697 16701 528 -4961 1412 C ATOM 1677 N LEU A1068 -76.329 1.729 255.552 1.00116.20 N ANISOU 1677 N LEU A1068 13469 17347 13334 661 -2828 633 N ATOM 1678 CA LEU A1068 -75.856 1.474 256.909 1.00107.55 C ANISOU 1678 CA LEU A1068 12301 16326 12237 775 -2390 353 C ATOM 1679 C LEU A1068 -74.630 2.317 257.236 1.00 97.08 C ANISOU 1679 C LEU A1068 11200 14794 10894 856 -2311 349 C ATOM 1680 O LEU A1068 -74.526 2.873 258.335 1.00 93.90 O ANISOU 1680 O LEU A1068 10664 14311 10704 1085 -2165 118 O ATOM 1681 CB LEU A1068 -75.549 -0.014 257.082 1.00106.30 C ANISOU 1681 CB LEU A1068 12274 16391 11725 548 -2119 283 C ATOM 1682 CG LEU A1068 -75.046 -0.492 258.444 1.00104.08 C ANISOU 1682 CG LEU A1068 11993 16191 11363 583 -1735 69 C ATOM 1683 CD1 LEU A1068 -76.089 -0.243 259.521 1.00106.16 C ANISOU 1683 CD1 LEU A1068 11853 16603 11878 738 -1584 -109 C ATOM 1684 CD2 LEU A1068 -74.681 -1.967 258.381 1.00100.37 C ANISOU 1684 CD2 LEU A1068 11712 15822 10602 334 -1633 66 C ATOM 1685 N VAL A1069 -73.708 2.452 256.281 1.00 92.85 N ANISOU 1685 N VAL A1069 10986 14195 10098 652 -2410 588 N ATOM 1686 CA VAL A1069 -72.488 3.212 256.532 1.00 91.65 C ANISOU 1686 CA VAL A1069 11010 13858 9955 660 -2339 622 C ATOM 1687 C VAL A1069 -72.799 4.699 256.672 1.00 97.49 C ANISOU 1687 C VAL A1069 11642 14240 11159 865 -2684 704 C ATOM 1688 O VAL A1069 -72.234 5.387 257.532 1.00101.20 O ANISOU 1688 O VAL A1069 12096 14504 11852 1034 -2627 545 O ATOM 1689 CB VAL A1069 -71.463 2.944 255.413 1.00 89.85 C ANISOU 1689 CB VAL A1069 11083 13746 9310 337 -2307 854 C ATOM 1690 CG1 VAL A1069 -70.254 3.855 255.559 1.00 90.18 C ANISOU 1690 CG1 VAL A1069 11242 13598 9425 285 -2273 955 C ATOM 1691 CG2 VAL A1069 -71.044 1.480 255.416 1.00 86.97 C ANISOU 1691 CG2 VAL A1069 10796 13662 8588 220 -1996 642 C ATOM 1692 N GLY A1070 -73.717 5.214 255.853 1.00103.40 N ANISOU 1692 N GLY A1070 12317 14865 12104 871 -3114 932 N ATOM 1693 CA GLY A1070 -74.108 6.609 255.983 1.00112.38 C ANISOU 1693 CA GLY A1070 13328 15576 13794 1107 -3553 982 C ATOM 1694 C GLY A1070 -74.812 6.902 257.294 1.00117.08 C ANISOU 1694 C GLY A1070 13535 16117 14834 1541 -3443 489 C ATOM 1695 O GLY A1070 -74.581 7.943 257.919 1.00116.00 O ANISOU 1695 O GLY A1070 13339 15642 15093 1792 -3602 321 O ATOM 1696 N GLN A1071 -75.686 5.992 257.729 1.00119.72 N ANISOU 1696 N GLN A1071 13589 16802 15098 1616 -3170 234 N ATOM 1697 CA GLN A1071 -76.344 6.171 259.018 1.00123.39 C ANISOU 1697 CA GLN A1071 13656 17366 15861 1972 -2946 -263 C ATOM 1698 C GLN A1071 -75.338 6.096 260.162 1.00123.03 C ANISOU 1698 C GLN A1071 13772 17382 15592 2016 -2545 -522 C ATOM 1699 O GLN A1071 -75.458 6.829 261.154 1.00125.96 O ANISOU 1699 O GLN A1071 13959 17659 16243 2345 -2506 -917 O ATOM 1700 CB GLN A1071 -77.442 5.127 259.199 1.00125.26 C ANISOU 1700 CB GLN A1071 13552 18030 16009 1922 -2701 -398 C ATOM 1701 CG GLN A1071 -78.605 5.226 258.234 1.00130.44 C ANISOU 1701 CG GLN A1071 13946 18629 16985 1936 -3137 -233 C ATOM 1702 CD GLN A1071 -79.605 4.105 258.441 1.00132.03 C ANISOU 1702 CD GLN A1071 13795 19264 17106 1817 -2876 -345 C ATOM 1703 OE1 GLN A1071 -79.274 3.064 259.010 1.00126.30 O ANISOU 1703 OE1 GLN A1071 13169 18855 15965 1602 -2421 -392 O ATOM 1704 NE2 GLN A1071 -80.833 4.311 257.981 1.00139.73 N ANISOU 1704 NE2 GLN A1071 14344 20223 18524 1937 -3218 -365 N ATOM 1705 N ILE A1072 -74.334 5.222 260.041 1.00124.36 N ANISOU 1705 N ILE A1072 14278 17698 15276 1710 -2282 -346 N ATOM 1706 CA ILE A1072 -73.282 5.166 261.054 1.00122.77 C ANISOU 1706 CA ILE A1072 14258 17495 14894 1737 -2004 -548 C ATOM 1707 C ILE A1072 -72.494 6.471 261.077 1.00129.25 C ANISOU 1707 C ILE A1072 15212 17871 16027 1868 -2295 -533 C ATOM 1708 O ILE A1072 -72.127 6.971 262.145 1.00131.56 O ANISOU 1708 O ILE A1072 15495 18059 16434 2086 -2225 -864 O ATOM 1709 CB ILE A1072 -72.366 3.952 260.807 1.00114.83 C ANISOU 1709 CB ILE A1072 13540 16678 13410 1408 -1755 -376 C ATOM 1710 CG1 ILE A1072 -73.105 2.648 261.120 1.00114.77 C ANISOU 1710 CG1 ILE A1072 13414 17041 13152 1288 -1497 -443 C ATOM 1711 CG2 ILE A1072 -71.109 4.042 261.651 1.00112.03 C ANISOU 1711 CG2 ILE A1072 13394 16220 12954 1425 -1607 -520 C ATOM 1712 CD1 ILE A1072 -72.288 1.398 260.842 1.00112.20 C ANISOU 1712 CD1 ILE A1072 13357 16822 12453 1006 -1354 -321 C ATOM 1713 N ASP A1073 -72.269 7.072 259.907 1.00134.68 N ANISOU 1713 N ASP A1073 16033 18285 16854 1714 -2668 -138 N ATOM 1714 CA ASP A1073 -71.560 8.352 259.856 1.00138.70 C ANISOU 1714 CA ASP A1073 16666 18317 17716 1765 -3021 -34 C ATOM 1715 C ASP A1073 -72.375 9.467 260.505 1.00139.81 C ANISOU 1715 C ASP A1073 16541 18127 18455 2210 -3348 -384 C ATOM 1716 O ASP A1073 -71.827 10.309 261.238 1.00141.68 O ANISOU 1716 O ASP A1073 16816 18038 18978 2403 -3484 -623 O ATOM 1717 CB ASP A1073 -71.225 8.709 258.409 1.00145.39 C ANISOU 1717 CB ASP A1073 17728 18997 18514 1413 -3357 548 C ATOM 1718 CG ASP A1073 -70.208 7.772 257.799 1.00146.36 C ANISOU 1718 CG ASP A1073 18089 19448 18071 1006 -3015 788 C ATOM 1719 OD1 ASP A1073 -69.805 6.816 258.488 1.00144.27 O ANISOU 1719 OD1 ASP A1073 17818 19463 17534 1027 -2590 509 O ATOM 1720 OD2 ASP A1073 -69.815 7.987 256.632 1.00149.32 O ANISOU 1720 OD2 ASP A1073 18651 19813 18269 660 -3186 1241 O ATOM 1721 N ASP A1074 -73.688 9.474 260.264 1.00139.22 N ANISOU 1721 N ASP A1074 16162 18124 18612 2399 -3500 -477 N ATOM 1722 CA ASP A1074 -74.544 10.461 260.907 1.00140.36 C ANISOU 1722 CA ASP A1074 15956 18001 19374 2889 -3785 -933 C ATOM 1723 C ASP A1074 -74.523 10.289 262.422 1.00137.99 C ANISOU 1723 C ASP A1074 15492 17980 18958 3176 -3325 -1577 C ATOM 1724 O ASP A1074 -74.401 11.270 263.166 1.00143.19 O ANISOU 1724 O ASP A1074 16078 18322 20007 3526 -3523 -1994 O ATOM 1725 CB ASP A1074 -75.974 10.354 260.348 1.00140.92 C ANISOU 1725 CB ASP A1074 15650 18169 19724 3027 -3998 -938 C ATOM 1726 CG ASP A1074 -76.051 10.694 258.871 1.00140.57 C ANISOU 1726 CG ASP A1074 15809 17794 19807 2764 -4582 -304 C ATOM 1727 OD1 ASP A1074 -75.193 11.469 258.392 1.00140.61 O ANISOU 1727 OD1 ASP A1074 16153 17359 19914 2591 -4955 64 O ATOM 1728 OD2 ASP A1074 -76.962 10.190 258.184 1.00140.38 O ANISOU 1728 OD2 ASP A1074 15617 17961 19761 2691 -4690 -147 O ATOM 1729 N ALA A1075 -74.639 9.045 262.896 1.00130.85 N ANISOU 1729 N ALA A1075 14557 17658 17502 3010 -2749 -1662 N ATOM 1730 CA ALA A1075 -74.549 8.785 264.333 1.00129.17 C ANISOU 1730 CA ALA A1075 14271 17778 17029 3178 -2301 -2184 C ATOM 1731 C ALA A1075 -73.191 9.171 264.920 1.00122.51 C ANISOU 1731 C ALA A1075 13801 16673 16073 3154 -2333 -2244 C ATOM 1732 O ALA A1075 -73.116 9.569 266.092 1.00128.15 O ANISOU 1732 O ALA A1075 14468 17441 16783 3428 -2214 -2766 O ATOM 1733 CB ALA A1075 -74.852 7.306 264.613 1.00129.48 C ANISOU 1733 CB ALA A1075 14281 18432 16483 2888 -1766 -2103 C ATOM 1734 N LEU A1076 -72.128 9.051 264.118 1.00110.53 N ANISOU 1734 N LEU A1076 12631 14913 14454 2820 -2487 -1744 N ATOM 1735 CA LEU A1076 -70.754 9.387 264.500 1.00107.51 C ANISOU 1735 CA LEU A1076 12560 14259 14031 2732 -2560 -1723 C ATOM 1736 C LEU A1076 -70.505 10.884 264.649 1.00118.39 C ANISOU 1736 C LEU A1076 13936 15035 16012 2996 -3071 -1893 C ATOM 1737 O LEU A1076 -69.748 11.298 265.533 1.00117.66 O ANISOU 1737 O LEU A1076 13978 14769 15960 3111 -3113 -2188 O ATOM 1738 CB LEU A1076 -69.804 8.820 263.456 1.00 98.78 C ANISOU 1738 CB LEU A1076 11711 13137 12686 2284 -2546 -1157 C ATOM 1739 CG LEU A1076 -69.272 7.421 263.761 1.00 92.56 C ANISOU 1739 CG LEU A1076 11062 12766 11340 2048 -2105 -1126 C ATOM 1740 CD1 LEU A1076 -68.624 6.788 262.515 1.00 91.38 C ANISOU 1740 CD1 LEU A1076 11061 12680 10978 1660 -2073 -655 C ATOM 1741 CD2 LEU A1076 -68.306 7.442 264.966 1.00 81.15 C ANISOU 1741 CD2 LEU A1076 9778 11264 9789 2123 -2017 -1423 C ATOM 1742 N LYS A1077 -71.139 11.701 263.810 1.00124.19 N ANISOU 1742 N LYS A1077 14535 15407 17245 3089 -3530 -1709 N ATOM 1743 CA LYS A1077 -71.077 13.152 264.000 1.00130.45 C ANISOU 1743 CA LYS A1077 15295 15546 18722 3387 -4117 -1915 C ATOM 1744 C LYS A1077 -71.657 13.562 265.345 1.00139.99 C ANISOU 1744 C LYS A1077 16259 16825 20106 3926 -4029 -2757 C ATOM 1745 O LYS A1077 -71.154 14.485 265.997 1.00146.13 O ANISOU 1745 O LYS A1077 17117 17169 21235 4162 -4345 -3109 O ATOM 1746 CB LYS A1077 -71.773 13.919 262.879 1.00131.90 C ANISOU 1746 CB LYS A1077 15376 15290 19449 3404 -4715 -1557 C ATOM 1747 CG LYS A1077 -70.754 14.794 262.161 1.00133.92 C ANISOU 1747 CG LYS A1077 15943 14930 20009 3084 -5249 -1006 C ATOM 1748 CD LYS A1077 -71.317 15.594 261.028 1.00140.80 C ANISOU 1748 CD LYS A1077 16812 15307 21379 3010 -5940 -529 C ATOM 1749 CE LYS A1077 -70.182 16.370 260.397 1.00145.14 C ANISOU 1749 CE LYS A1077 17698 15331 22117 2569 -6388 88 C ATOM 1750 NZ LYS A1077 -70.601 17.122 259.194 1.00151.90 N ANISOU 1750 NZ LYS A1077 18653 15702 23359 2354 -7111 723 N ATOM 1751 N LEU A1078 -72.744 12.915 265.746 1.00146.32 N ANISOU 1751 N LEU A1078 16738 18182 20676 4114 -3614 -3106 N ATOM 1752 CA LEU A1078 -73.370 13.174 267.039 1.00152.09 C ANISOU 1752 CA LEU A1078 17185 19174 21428 4585 -3388 -3948 C ATOM 1753 C LEU A1078 -72.380 13.016 268.193 1.00157.35 C ANISOU 1753 C LEU A1078 18153 19981 21650 4558 -3131 -4254 C ATOM 1754 O LEU A1078 -72.307 13.872 269.083 1.00160.96 O ANISOU 1754 O LEU A1078 18576 20228 22354 4950 -3316 -4890 O ATOM 1755 CB LEU A1078 -74.538 12.225 267.256 1.00146.23 C ANISOU 1755 CB LEU A1078 16064 19169 20329 4602 -2836 -4130 C ATOM 1756 CG LEU A1078 -75.828 12.653 266.551 1.00148.20 C ANISOU 1756 CG LEU A1078 15830 19300 21178 4865 -3132 -4198 C ATOM 1757 CD1 LEU A1078 -76.913 11.623 266.816 1.00147.54 C ANISOU 1757 CD1 LEU A1078 15339 19999 20722 4804 -2537 -4352 C ATOM 1758 CD2 LEU A1078 -76.249 14.061 266.962 1.00156.03 C ANISOU 1758 CD2 LEU A1078 16535 19792 22956 5475 -3632 -4868 C ATOM 1759 N ALA A1079 -71.578 11.956 268.182 1.00156.58 N ANISOU 1759 N ALA A1079 18366 20191 20936 4116 -2779 -3837 N ATOM 1760 CA ALA A1079 -70.662 11.699 269.295 1.00161.40 C ANISOU 1760 CA ALA A1079 19270 20949 21106 4070 -2582 -4094 C ATOM 1761 C ALA A1079 -69.541 12.727 269.438 1.00165.96 C ANISOU 1761 C ALA A1079 20103 20857 22097 4140 -3100 -4150 C ATOM 1762 O ALA A1079 -69.059 12.932 270.555 1.00170.47 O ANISOU 1762 O ALA A1079 20832 21456 22482 4298 -3087 -4621 O ATOM 1763 CB ALA A1079 -70.078 10.295 269.138 1.00159.72 C ANISOU 1763 CB ALA A1079 19299 21131 20257 3592 -2190 -3603 C ATOM 1764 N ASN A1080 -69.045 13.322 268.350 1.00163.32 N ANISOU 1764 N ASN A1080 19842 19947 22263 3961 -3562 -3640 N ATOM 1765 CA ASN A1080 -68.048 14.368 268.555 1.00158.11 C ANISOU 1765 CA ASN A1080 19378 18631 22066 4005 -4088 -3706 C ATOM 1766 C ASN A1080 -68.638 15.565 269.289 1.00161.22 C ANISOU 1766 C ASN A1080 19609 18656 22991 4570 -4483 -4448 C ATOM 1767 O ASN A1080 -67.969 16.165 270.134 1.00165.61 O ANISOU 1767 O ASN A1080 20330 18914 23680 4737 -4738 -4865 O ATOM 1768 CB ASN A1080 -67.503 14.863 267.215 1.00154.06 C ANISOU 1768 CB ASN A1080 18947 17592 21998 3648 -4521 -2971 C ATOM 1769 CG ASN A1080 -66.574 13.875 266.548 1.00146.60 C ANISOU 1769 CG ASN A1080 18176 16929 20597 3102 -4197 -2344 C ATOM 1770 OD1 ASN A1080 -66.048 12.970 267.195 1.00145.62 O ANISOU 1770 OD1 ASN A1080 18162 17201 19965 3006 -3799 -2468 O ATOM 1771 ND2 ASN A1080 -66.333 14.067 265.258 1.00143.71 N ANISOU 1771 ND2 ASN A1080 17838 16351 20413 2738 -4400 -1683 N ATOM 1772 N GLU A1081 -69.902 15.896 269.026 1.00164.98 N ANISOU 1772 N GLU A1081 19738 19160 23788 4901 -4552 -4695 N ATOM 1773 CA GLU A1081 -70.612 16.939 269.749 1.00178.67 C ANISOU 1773 CA GLU A1081 21221 20624 26041 5523 -4874 -5542 C ATOM 1774 C GLU A1081 -71.090 16.495 271.115 1.00195.69 C ANISOU 1774 C GLU A1081 23249 23497 27608 5835 -4297 -6370 C ATOM 1775 O GLU A1081 -71.665 17.304 271.847 1.00195.73 O ANISOU 1775 O GLU A1081 23020 23403 27946 6388 -4468 -7224 O ATOM 1776 CB GLU A1081 -71.803 17.422 268.923 1.00176.46 C ANISOU 1776 CB GLU A1081 20552 20113 26382 5775 -5190 -5514 C ATOM 1777 N GLY A1082 -70.899 15.233 271.473 1.00200.40 N ANISOU 1777 N GLY A1082 23984 24823 27335 5489 -3633 -6154 N ATOM 1778 CA GLY A1082 -71.337 14.797 272.773 1.00202.53 C ANISOU 1778 CA GLY A1082 24179 25819 26955 5688 -3089 -6848 C ATOM 1779 C GLY A1082 -72.821 14.554 272.908 1.00204.56 C ANISOU 1779 C GLY A1082 23903 26687 27132 5947 -2650 -7264 C ATOM 1780 O GLY A1082 -73.325 14.570 274.037 1.00213.79 O ANISOU 1780 O GLY A1082 24908 28415 27906 6227 -2270 -8032 O ATOM 1781 N LYS A1083 -73.556 14.321 271.817 1.00195.68 N ANISOU 1781 N LYS A1083 22480 25529 26340 5848 -2677 -6808 N ATOM 1782 CA LYS A1083 -75.005 14.126 271.953 1.00183.25 C ANISOU 1782 CA LYS A1083 20310 24529 24787 6106 -2290 -7241 C ATOM 1783 C LYS A1083 -75.286 12.632 272.096 1.00165.03 C ANISOU 1783 C LYS A1083 18006 23078 21620 5619 -1553 -6844 C ATOM 1784 O LYS A1083 -75.453 11.903 271.118 1.00164.18 O ANISOU 1784 O LYS A1083 17888 22995 21499 5254 -1514 -6143 O ATOM 1785 CB LYS A1083 -75.715 14.718 270.733 1.00180.17 C ANISOU 1785 CB LYS A1083 19575 23601 25280 6282 -2815 -6995 C ATOM 1786 CG LYS A1083 -75.355 16.171 270.438 1.00181.77 C ANISOU 1786 CG LYS A1083 19848 22807 26408 6666 -3690 -7200 C ATOM 1787 CD LYS A1083 -76.015 16.665 269.156 1.00182.21 C ANISOU 1787 CD LYS A1083 19645 22305 27283 6743 -4288 -6796 C ATOM 1788 CE LYS A1083 -75.603 18.081 268.808 1.00186.73 C ANISOU 1788 CE LYS A1083 20352 21803 28794 7029 -5254 -6856 C ATOM 1789 NZ LYS A1083 -76.247 18.530 267.543 1.00189.47 N ANISOU 1789 NZ LYS A1083 20505 21594 29890 7047 -5906 -6372 N ATOM 1790 N VAL A1084 -75.340 12.197 273.353 1.00182.00 N ANISOU 1790 N VAL A1084 23293 29200 16660 3485 -6427 -7428 N ATOM 1791 CA VAL A1084 -75.436 10.781 273.674 1.00169.54 C ANISOU 1791 CA VAL A1084 21794 27903 14721 3503 -6059 -7307 C ATOM 1792 C VAL A1084 -76.839 10.241 273.413 1.00165.90 C ANISOU 1792 C VAL A1084 21330 27627 14077 3447 -5789 -7303 C ATOM 1793 O VAL A1084 -77.000 9.175 272.812 1.00162.96 O ANISOU 1793 O VAL A1084 21039 27359 13520 3279 -5526 -7123 O ATOM 1794 CB VAL A1084 -74.993 10.539 275.130 1.00165.97 C ANISOU 1794 CB VAL A1084 21386 27600 14076 3778 -6021 -7386 C ATOM 1795 CG1 VAL A1084 -75.114 9.067 275.498 1.00156.48 C ANISOU 1795 CG1 VAL A1084 20349 26631 12476 3770 -5666 -7233 C ATOM 1796 CG2 VAL A1084 -73.558 11.010 275.306 1.00162.68 C ANISOU 1796 CG2 VAL A1084 20950 27003 13857 3824 -6281 -7405 C ATOM 1797 N LYS A1085 -77.874 10.955 273.862 1.00166.76 N ANISOU 1797 N LYS A1085 21329 27792 14239 3591 -5849 -7518 N ATOM 1798 CA LYS A1085 -79.240 10.477 273.647 1.00162.77 C ANISOU 1798 CA LYS A1085 20772 27502 13572 3534 -5586 -7569 C ATOM 1799 C LYS A1085 -79.602 10.397 272.167 1.00157.10 C ANISOU 1799 C LYS A1085 20062 26617 13011 3287 -5591 -7456 C ATOM 1800 O LYS A1085 -80.197 9.407 271.716 1.00157.17 O ANISOU 1800 O LYS A1085 20105 26798 12814 3141 -5282 -7345 O ATOM 1801 CB LYS A1085 -80.239 11.386 274.365 1.00163.99 C ANISOU 1801 CB LYS A1085 20753 27753 13804 3756 -5695 -7884 C ATOM 1802 CG LYS A1085 -80.620 10.922 275.751 1.00161.15 C ANISOU 1802 CG LYS A1085 20366 27761 13104 3919 -5455 -8003 C ATOM 1803 CD LYS A1085 -80.959 9.443 275.724 1.00160.23 C ANISOU 1803 CD LYS A1085 20381 27915 12586 3718 -5011 -7810 C ATOM 1804 CE LYS A1085 -82.197 9.129 274.897 1.00159.97 C ANISOU 1804 CE LYS A1085 20242 28005 12534 3543 -4807 -7853 C ATOM 1805 NZ LYS A1085 -82.249 7.679 274.541 1.00158.70 N ANISOU 1805 NZ LYS A1085 20265 27987 12049 3290 -4426 -7575 N ATOM 1806 N GLU A1086 -79.235 11.420 271.396 1.00159.09 N ANISOU 1806 N GLU A1086 20311 26518 13617 3217 -5943 -7468 N ATOM 1807 CA GLU A1086 -79.495 11.405 269.966 1.00160.83 C ANISOU 1807 CA GLU A1086 20581 26537 13990 2966 -5983 -7348 C ATOM 1808 C GLU A1086 -78.714 10.288 269.285 1.00159.49 C ANISOU 1808 C GLU A1086 20505 26343 13754 2706 -5690 -6980 C ATOM 1809 O GLU A1086 -79.218 9.628 268.361 1.00156.63 O ANISOU 1809 O GLU A1086 20168 25939 13404 2504 -5448 -6784 O ATOM 1810 CB GLU A1086 -79.167 12.777 269.373 1.00164.99 C ANISOU 1810 CB GLU A1086 21152 26638 14898 2902 -6428 -7393 C ATOM 1811 CG GLU A1086 -80.144 13.869 269.848 1.00170.13 C ANISOU 1811 CG GLU A1086 21716 27194 15731 3139 -6658 -7669 C ATOM 1812 CD GLU A1086 -79.914 14.307 271.291 1.00176.27 C ANISOU 1812 CD GLU A1086 22397 28117 16462 3439 -6726 -7851 C ATOM 1813 OE1 GLU A1086 -78.744 14.320 271.743 1.00177.53 O ANISOU 1813 OE1 GLU A1086 22604 28245 16603 3440 -6791 -7762 O ATOM 1814 OE2 GLU A1086 -80.911 14.550 272.002 1.00179.33 O ANISOU 1814 OE2 GLU A1086 22639 28691 16807 3679 -6687 -8100 O ATOM 1815 N ALA A1087 -77.477 10.059 269.730 1.00161.15 N ANISOU 1815 N ALA A1087 20752 26555 13922 2720 -5704 -6882 N ATOM 1816 CA ALA A1087 -76.689 8.954 269.195 1.00157.82 C ANISOU 1816 CA ALA A1087 20394 26124 13446 2519 -5430 -6564 C ATOM 1817 C ALA A1087 -77.319 7.608 269.536 1.00158.11 C ANISOU 1817 C ALA A1087 20497 26412 13165 2545 -5024 -6436 C ATOM 1818 O ALA A1087 -77.267 6.671 268.736 1.00145.43 O ANISOU 1818 O ALA A1087 18950 24770 11538 2347 -4777 -6172 O ATOM 1819 CB ALA A1087 -75.258 9.030 269.718 1.00154.74 C ANISOU 1819 CB ALA A1087 20005 25720 13071 2583 -5574 -6575 C ATOM 1820 N GLN A1088 -77.925 7.494 270.718 1.00157.04 N ANISOU 1820 N GLN A1088 20368 26537 12764 2768 -4958 -6622 N ATOM 1821 CA GLN A1088 -78.564 6.240 271.109 1.00157.29 C ANISOU 1821 CA GLN A1088 20506 26811 12446 2738 -4577 -6501 C ATOM 1822 C GLN A1088 -79.824 5.981 270.290 1.00163.61 C ANISOU 1822 C GLN A1088 21247 27643 13274 2565 -4366 -6456 C ATOM 1823 O GLN A1088 -80.111 4.834 269.922 1.00165.37 O ANISOU 1823 O GLN A1088 21574 27922 13338 2398 -4050 -6218 O ATOM 1824 CB GLN A1088 -78.875 6.255 272.604 1.00155.50 C ANISOU 1824 CB GLN A1088 20314 26877 11894 2975 -4560 -6729 C ATOM 1825 CG GLN A1088 -77.642 6.204 273.505 1.00155.15 C ANISOU 1825 CG GLN A1088 20382 26817 11749 3160 -4719 -6744 C ATOM 1826 CD GLN A1088 -77.976 6.487 274.955 1.00160.24 C ANISOU 1826 CD GLN A1088 21040 27670 12174 3387 -4728 -6958 C ATOM 1827 OE1 GLN A1088 -79.118 6.787 275.293 1.00164.64 O ANISOU 1827 OE1 GLN A1088 21484 28411 12661 3403 -4619 -7124 O ATOM 1828 NE2 GLN A1088 -76.973 6.384 275.826 1.00156.21 N ANISOU 1828 NE2 GLN A1088 20648 27109 11595 3553 -4835 -6943 N ATOM 1829 N ALA A1089 -80.599 7.031 270.004 1.00165.31 N ANISOU 1829 N ALA A1089 21307 27812 13691 2618 -4565 -6704 N ATOM 1830 CA ALA A1089 -81.746 6.866 269.110 1.00166.39 C ANISOU 1830 CA ALA A1089 21374 27940 13906 2472 -4417 -6697 C ATOM 1831 C ALA A1089 -81.303 6.468 267.706 1.00167.15 C ANISOU 1831 C ALA A1089 21549 27739 14222 2215 -4359 -6364 C ATOM 1832 O ALA A1089 -81.895 5.571 267.085 1.00167.92 O ANISOU 1832 O ALA A1089 21676 27874 14252 2048 -4066 -6184 O ATOM 1833 CB ALA A1089 -82.578 8.147 269.066 1.00168.16 C ANISOU 1833 CB ALA A1089 21436 28133 14323 2629 -4734 -7079 C ATOM 1834 N ALA A1090 -80.241 7.109 267.199 1.00168.02 N ANISOU 1834 N ALA A1090 21689 27570 14579 2159 -4628 -6286 N ATOM 1835 CA ALA A1090 -79.698 6.720 265.901 1.00165.57 C ANISOU 1835 CA ALA A1090 21444 27023 14444 1892 -4559 -5983 C ATOM 1836 C ALA A1090 -79.193 5.284 265.919 1.00163.75 C ANISOU 1836 C ALA A1090 21303 26913 14002 1809 -4228 -5703 C ATOM 1837 O ALA A1090 -79.328 4.563 264.926 1.00158.53 O ANISOU 1837 O ALA A1090 20682 26170 13384 1616 -4037 -5468 O ATOM 1838 CB ALA A1090 -78.582 7.681 265.490 1.00165.19 C ANISOU 1838 CB ALA A1090 21405 26715 14647 1806 -4893 -5982 C ATOM 1839 N ALA A1091 -78.642 4.835 267.046 1.00166.55 N ANISOU 1839 N ALA A1091 21714 27449 14116 1971 -4184 -5735 N ATOM 1840 CA ALA A1091 -78.194 3.448 267.154 1.00165.63 C ANISOU 1840 CA ALA A1091 21742 27423 13768 1930 -3935 -5499 C ATOM 1841 C ALA A1091 -79.367 2.477 267.176 1.00160.86 C ANISOU 1841 C ALA A1091 21221 26972 12925 1852 -3610 -5398 C ATOM 1842 O ALA A1091 -79.285 1.382 266.603 1.00159.29 O ANISOU 1842 O ALA A1091 21137 26740 12647 1716 -3409 -5142 O ATOM 1843 CB ALA A1091 -77.332 3.261 268.399 1.00168.81 C ANISOU 1843 CB ALA A1091 22235 27946 13959 2143 -4026 -5587 C ATOM 1844 N GLU A1092 -80.485 2.882 267.786 1.00160.09 N ANISOU 1844 N GLU A1092 21052 27059 12718 1925 -3563 -5619 N ATOM 1845 CA GLU A1092 -81.668 2.028 267.770 1.00158.66 C ANISOU 1845 CA GLU A1092 20912 27059 12313 1801 -3238 -5561 C ATOM 1846 C GLU A1092 -82.209 1.879 266.355 1.00151.46 C ANISOU 1846 C GLU A1092 19933 25972 11642 1608 -3150 -5417 C ATOM 1847 O GLU A1092 -82.621 0.783 265.960 1.00139.76 O ANISOU 1847 O GLU A1092 18554 24526 10023 1448 -2879 -5201 O ATOM 1848 CB GLU A1092 -82.730 2.631 268.696 1.00162.05 C ANISOU 1848 CB GLU A1092 21207 27772 12592 1918 -3224 -5909 C ATOM 1849 CG GLU A1092 -83.711 1.637 269.309 1.00162.07 C ANISOU 1849 CG GLU A1092 21292 28095 12192 1793 -2860 -5897 C ATOM 1850 CD GLU A1092 -83.010 0.542 270.089 1.00159.50 C ANISOU 1850 CD GLU A1092 21280 27826 11498 1761 -2729 -5665 C ATOM 1851 OE1 GLU A1092 -82.014 0.820 270.789 1.00159.13 O ANISOU 1851 OE1 GLU A1092 21322 27730 11410 1945 -2934 -5701 O ATOM 1852 OE2 GLU A1092 -83.474 -0.614 270.003 1.00158.99 O ANISOU 1852 OE2 GLU A1092 21395 27840 11175 1551 -2442 -5456 O ATOM 1853 N GLN A1093 -82.231 2.969 265.587 1.00145.06 N ANISOU 1853 N GLN A1093 18985 24955 11178 1616 -3397 -5534 N ATOM 1854 CA GLN A1093 -82.625 2.859 264.182 1.00149.47 C ANISOU 1854 CA GLN A1093 19521 25303 11970 1434 -3350 -5383 C ATOM 1855 C GLN A1093 -81.589 2.082 263.352 1.00145.14 C ANISOU 1855 C GLN A1093 19088 24579 11480 1281 -3279 -5038 C ATOM 1856 O GLN A1093 -81.937 1.411 262.362 1.00134.90 O ANISOU 1856 O GLN A1093 17824 23191 10240 1119 -3111 -4836 O ATOM 1857 CB GLN A1093 -82.906 4.251 263.594 1.00156.64 C ANISOU 1857 CB GLN A1093 20322 25995 13199 1474 -3683 -5602 C ATOM 1858 CG GLN A1093 -81.759 5.072 263.071 1.00159.88 C ANISOU 1858 CG GLN A1093 20773 26120 13853 1418 -3988 -5539 C ATOM 1859 CD GLN A1093 -82.268 6.377 262.476 1.00160.30 C ANISOU 1859 CD GLN A1093 20801 25930 14178 1430 -4335 -5750 C ATOM 1860 OE1 GLN A1093 -83.473 6.528 262.203 1.00159.80 O ANISOU 1860 OE1 GLN A1093 20682 25880 14156 1478 -4331 -5916 O ATOM 1861 NE2 GLN A1093 -81.365 7.310 262.218 1.00160.06 N ANISOU 1861 NE2 GLN A1093 20827 25659 14328 1370 -4655 -5754 N ATOM 1862 N LEU A1094 -80.314 2.162 263.742 1.00150.97 N ANISOU 1862 N LEU A1094 19868 25288 12206 1342 -3417 -5000 N ATOM 1863 CA LEU A1094 -79.275 1.350 263.111 1.00145.93 C ANISOU 1863 CA LEU A1094 19303 24562 11583 1236 -3356 -4744 C ATOM 1864 C LEU A1094 -79.530 -0.134 263.314 1.00142.67 C ANISOU 1864 C LEU A1094 19049 24272 10886 1219 -3080 -4547 C ATOM 1865 O LEU A1094 -79.269 -0.946 262.418 1.00136.81 O ANISOU 1865 O LEU A1094 18359 23442 10181 1097 -2974 -4323 O ATOM 1866 CB LEU A1094 -77.894 1.713 263.654 1.00148.86 C ANISOU 1866 CB LEU A1094 19656 24932 11971 1340 -3567 -4821 C ATOM 1867 CG LEU A1094 -77.274 3.002 263.129 1.00135.85 C ANISOU 1867 CG LEU A1094 17886 23110 10623 1256 -3845 -4930 C ATOM 1868 CD1 LEU A1094 -75.967 3.323 263.848 1.00137.17 C ANISOU 1868 CD1 LEU A1094 18014 23326 10779 1369 -4038 -5049 C ATOM 1869 CD2 LEU A1094 -77.050 2.823 261.640 1.00139.74 C ANISOU 1869 CD2 LEU A1094 18357 23434 11304 990 -3787 -4732 C ATOM 1870 N LYS A1095 -80.023 -0.509 264.490 1.00154.43 N ANISOU 1870 N LYS A1095 20641 25964 12072 1326 -2978 -4628 N ATOM 1871 CA LYS A1095 -80.363 -1.908 264.724 1.00155.46 C ANISOU 1871 CA LYS A1095 20988 26189 11892 1261 -2735 -4430 C ATOM 1872 C LYS A1095 -81.466 -2.362 263.775 1.00159.54 C ANISOU 1872 C LYS A1095 21475 26673 12472 1068 -2513 -4303 C ATOM 1873 O LYS A1095 -81.421 -3.484 263.250 1.00162.63 O ANISOU 1873 O LYS A1095 22014 27004 12773 963 -2374 -4056 O ATOM 1874 CB LYS A1095 -80.783 -2.089 266.180 1.00153.88 C ANISOU 1874 CB LYS A1095 20922 26223 11324 1354 -2662 -4559 C ATOM 1875 CG LYS A1095 -81.173 -3.500 266.569 1.00151.75 C ANISOU 1875 CG LYS A1095 20950 26043 10666 1241 -2432 -4355 C ATOM 1876 CD LYS A1095 -81.456 -3.577 268.062 1.00153.51 C ANISOU 1876 CD LYS A1095 21335 26500 10492 1303 -2382 -4492 C ATOM 1877 CE LYS A1095 -81.802 -4.996 268.485 1.00154.26 C ANISOU 1877 CE LYS A1095 21808 26654 10150 1137 -2179 -4267 C ATOM 1878 NZ LYS A1095 -81.982 -5.118 269.960 1.00156.03 N ANISOU 1878 NZ LYS A1095 22254 27097 9934 1161 -2138 -4379 N ATOM 1879 N THR A1096 -82.458 -1.497 263.536 1.00156.20 N ANISOU 1879 N THR A1096 20861 26277 12209 1042 -2510 -4493 N ATOM 1880 CA THR A1096 -83.487 -1.778 262.537 1.00146.42 C ANISOU 1880 CA THR A1096 19559 24983 11089 883 -2345 -4421 C ATOM 1881 C THR A1096 -82.865 -2.031 261.168 1.00141.60 C ANISOU 1881 C THR A1096 18963 24111 10729 782 -2392 -4183 C ATOM 1882 O THR A1096 -83.214 -3.005 260.484 1.00130.02 O ANISOU 1882 O THR A1096 17577 22599 9226 655 -2208 -3969 O ATOM 1883 CB THR A1096 -84.467 -0.605 262.457 1.00141.27 C ANISOU 1883 CB THR A1096 18689 24364 10623 935 -2444 -4736 C ATOM 1884 OG1 THR A1096 -85.213 -0.513 263.684 1.00137.10 O ANISOU 1884 OG1 THR A1096 18112 24152 9828 1008 -2346 -4985 O ATOM 1885 CG2 THR A1096 -85.426 -0.792 261.293 1.00138.57 C ANISOU 1885 CG2 THR A1096 18276 23914 10458 801 -2333 -4688 C ATOM 1886 N THR A1097 -81.942 -1.156 260.750 1.00136.99 N ANISOU 1886 N THR A1097 18298 23364 10387 816 -2637 -4226 N ATOM 1887 CA THR A1097 -81.315 -1.320 259.438 1.00131.25 C ANISOU 1887 CA THR A1097 17565 22429 9874 682 -2673 -4028 C ATOM 1888 C THR A1097 -80.537 -2.629 259.354 1.00128.05 C ANISOU 1888 C THR A1097 17291 22060 9303 672 -2561 -3796 C ATOM 1889 O THR A1097 -80.559 -3.314 258.323 1.00126.47 O ANISOU 1889 O THR A1097 17118 21762 9172 558 -2461 -3599 O ATOM 1890 CB THR A1097 -80.405 -0.130 259.138 1.00129.80 C ANISOU 1890 CB THR A1097 17289 22106 9925 667 -2949 -4134 C ATOM 1891 OG1 THR A1097 -81.055 1.087 259.532 1.00130.20 O ANISOU 1891 OG1 THR A1097 17266 22127 10077 741 -3126 -4391 O ATOM 1892 CG2 THR A1097 -80.013 -0.082 257.649 1.00127.52 C ANISOU 1892 CG2 THR A1097 16981 21611 9861 460 -2974 -3966 C ATOM 1893 N ILE A1098 -79.835 -2.988 260.427 1.00136.54 N ANISOU 1893 N ILE A1098 18463 23262 10155 814 -2610 -3835 N ATOM 1894 CA ILE A1098 -79.042 -4.218 260.433 1.00137.23 C ANISOU 1894 CA ILE A1098 18708 23363 10069 855 -2583 -3664 C ATOM 1895 C ILE A1098 -79.947 -5.444 260.334 1.00142.07 C ANISOU 1895 C ILE A1098 19513 23993 10473 775 -2359 -3468 C ATOM 1896 O ILE A1098 -79.662 -6.391 259.585 1.00142.82 O ANISOU 1896 O ILE A1098 19692 24008 10564 732 -2320 -3278 O ATOM 1897 CB ILE A1098 -78.148 -4.275 261.687 1.00136.06 C ANISOU 1897 CB ILE A1098 18660 23321 9715 1054 -2733 -3787 C ATOM 1898 CG1 ILE A1098 -77.066 -3.196 261.618 1.00134.87 C ANISOU 1898 CG1 ILE A1098 18306 23145 9792 1108 -2964 -3964 C ATOM 1899 CG2 ILE A1098 -77.531 -5.652 261.849 1.00135.56 C ANISOU 1899 CG2 ILE A1098 18833 23257 9415 1136 -2744 -3642 C ATOM 1900 CD1 ILE A1098 -76.230 -3.100 262.868 1.00133.48 C ANISOU 1900 CD1 ILE A1098 18200 23068 9450 1325 -3134 -4128 C ATOM 1901 N ASN A1099 -81.053 -5.447 261.086 1.00146.52 N ANISOU 1901 N ASN A1099 20140 24679 10851 741 -2212 -3530 N ATOM 1902 CA ASN A1099 -81.999 -6.556 260.995 1.00150.56 C ANISOU 1902 CA ASN A1099 20828 25223 11155 603 -1980 -3356 C ATOM 1903 C ASN A1099 -82.605 -6.653 259.599 1.00147.90 C ANISOU 1903 C ASN A1099 20367 24752 11076 463 -1877 -3240 C ATOM 1904 O ASN A1099 -82.809 -7.758 259.076 1.00146.73 O ANISOU 1904 O ASN A1099 20369 24538 10843 374 -1766 -3021 O ATOM 1905 CB ASN A1099 -83.102 -6.390 262.042 1.00156.02 C ANISOU 1905 CB ASN A1099 21547 26132 11602 547 -1820 -3504 C ATOM 1906 CG ASN A1099 -82.620 -6.677 263.451 1.00163.16 C ANISOU 1906 CG ASN A1099 22682 27167 12144 645 -1876 -3550 C ATOM 1907 OD1 ASN A1099 -81.683 -7.446 263.654 1.00166.89 O ANISOU 1907 OD1 ASN A1099 23395 27547 12467 727 -1997 -3409 O ATOM 1908 ND2 ASN A1099 -83.269 -6.062 264.435 1.00166.23 N ANISOU 1908 ND2 ASN A1099 23004 27775 12382 652 -1810 -3775 N ATOM 1909 N ALA A1100 -82.870 -5.506 258.967 1.00147.09 N ANISOU 1909 N ALA A1100 20023 24580 11285 450 -1946 -3385 N ATOM 1910 CA ALA A1100 -83.361 -5.525 257.593 1.00148.43 C ANISOU 1910 CA ALA A1100 20102 24586 11707 332 -1889 -3283 C ATOM 1911 C ALA A1100 -82.337 -6.131 256.642 1.00150.32 C ANISOU 1911 C ALA A1100 20387 24685 12042 313 -1952 -3072 C ATOM 1912 O ALA A1100 -82.696 -6.893 255.736 1.00150.17 O ANISOU 1912 O ALA A1100 20415 24575 12070 224 -1842 -2891 O ATOM 1913 CB ALA A1100 -83.734 -4.110 257.150 1.00148.94 C ANISOU 1913 CB ALA A1100 19967 24560 12064 334 -2026 -3495 C ATOM 1914 N TYR A1101 -81.056 -5.800 256.829 1.00150.41 N ANISOU 1914 N TYR A1101 20364 24700 12084 400 -2134 -3121 N ATOM 1915 CA TYR A1101 -80.005 -6.412 256.016 1.00148.31 C ANISOU 1915 CA TYR A1101 20100 24375 11877 396 -2197 -2986 C ATOM 1916 C TYR A1101 -79.971 -7.928 256.190 1.00145.96 C ANISOU 1916 C TYR A1101 20025 24101 11330 452 -2125 -2807 C ATOM 1917 O TYR A1101 -79.833 -8.674 255.209 1.00143.99 O ANISOU 1917 O TYR A1101 19794 23774 11142 411 -2094 -2651 O ATOM 1918 CB TYR A1101 -78.649 -5.804 256.374 1.00150.49 C ANISOU 1918 CB TYR A1101 20273 24711 12195 482 -2401 -3136 C ATOM 1919 CG TYR A1101 -78.272 -4.609 255.530 1.00153.61 C ANISOU 1919 CG TYR A1101 20469 25019 12877 340 -2502 -3219 C ATOM 1920 CD1 TYR A1101 -78.653 -4.529 254.197 1.00153.50 C ANISOU 1920 CD1 TYR A1101 20406 24866 13050 162 -2435 -3100 C ATOM 1921 CD2 TYR A1101 -77.542 -3.558 256.067 1.00157.16 C ANISOU 1921 CD2 TYR A1101 20814 25508 13393 364 -2679 -3411 C ATOM 1922 CE1 TYR A1101 -78.311 -3.437 253.421 1.00154.21 C ANISOU 1922 CE1 TYR A1101 20384 24849 13359 -13 -2546 -3158 C ATOM 1923 CE2 TYR A1101 -77.197 -2.463 255.300 1.00156.75 C ANISOU 1923 CE2 TYR A1101 20635 25353 13572 182 -2790 -3471 C ATOM 1924 CZ TYR A1101 -77.584 -2.407 253.978 1.00154.22 C ANISOU 1924 CZ TYR A1101 20305 24884 13407 -20 -2725 -3338 C ATOM 1925 OH TYR A1101 -77.242 -1.316 253.212 1.00152.58 O ANISOU 1925 OH TYR A1101 20037 24548 13388 -245 -2853 -3381 O ATOM 1926 N ILE A1102 -80.093 -8.398 257.435 1.00147.06 N ANISOU 1926 N ILE A1102 20367 24338 11173 542 -2120 -2829 N ATOM 1927 CA ILE A1102 -80.097 -9.839 257.696 1.00147.81 C ANISOU 1927 CA ILE A1102 20762 24414 10986 576 -2099 -2652 C ATOM 1928 C ILE A1102 -81.253 -10.509 256.959 1.00151.25 C ANISOU 1928 C ILE A1102 21264 24773 11431 405 -1893 -2463 C ATOM 1929 O ILE A1102 -81.072 -11.519 256.262 1.00152.63 O ANISOU 1929 O ILE A1102 21558 24850 11586 406 -1912 -2288 O ATOM 1930 CB ILE A1102 -80.150 -10.119 259.209 1.00145.48 C ANISOU 1930 CB ILE A1102 20726 24218 10332 649 -2126 -2706 C ATOM 1931 CG1 ILE A1102 -78.943 -9.494 259.911 1.00143.98 C ANISOU 1931 CG1 ILE A1102 20470 24089 10149 850 -2357 -2906 C ATOM 1932 CG2 ILE A1102 -80.208 -11.617 259.471 1.00145.25 C ANISOU 1932 CG2 ILE A1102 21091 24119 9977 645 -2142 -2503 C ATOM 1933 CD1 ILE A1102 -78.861 -9.812 261.389 1.00145.68 C ANISOU 1933 CD1 ILE A1102 20978 24379 9995 950 -2423 -2959 C ATOM 1934 N GLN A1103 -82.455 -9.941 257.088 1.00151.44 N ANISOU 1934 N GLN A1103 21192 24852 11497 273 -1712 -2529 N ATOM 1935 CA GLN A1103 -83.624 -10.527 256.436 1.00149.93 C ANISOU 1935 CA GLN A1103 21033 24610 11322 106 -1510 -2394 C ATOM 1936 C GLN A1103 -83.463 -10.536 254.920 1.00145.66 C ANISOU 1936 C GLN A1103 20347 23904 11094 87 -1534 -2292 C ATOM 1937 O GLN A1103 -83.818 -11.519 254.255 1.00143.92 O ANISOU 1937 O GLN A1103 20241 23592 10850 22 -1459 -2101 O ATOM 1938 CB GLN A1103 -84.896 -9.773 256.831 1.00151.58 C ANISOU 1938 CB GLN A1103 21094 24948 11550 -2 -1340 -2576 C ATOM 1939 CG GLN A1103 -85.120 -9.633 258.328 1.00156.08 C ANISOU 1939 CG GLN A1103 21766 25732 11805 -2 -1294 -2717 C ATOM 1940 CD GLN A1103 -85.359 -10.961 259.020 1.00157.88 C ANISOU 1940 CD GLN A1103 22354 26013 11620 -126 -1184 -2531 C ATOM 1941 OE1 GLN A1103 -85.733 -11.948 258.386 1.00161.63 O ANISOU 1941 OE1 GLN A1103 22972 26384 12055 -248 -1098 -2321 O ATOM 1942 NE2 GLN A1103 -85.146 -10.990 260.330 1.00155.27 N ANISOU 1942 NE2 GLN A1103 22205 25827 10965 -105 -1207 -2604 N ATOM 1943 N LYS A1104 -82.951 -9.441 254.354 1.00145.26 N ANISOU 1943 N LYS A1104 20064 23806 11320 121 -1645 -2416 N ATOM 1944 CA LYS A1104 -82.808 -9.358 252.906 1.00143.19 C ANISOU 1944 CA LYS A1104 19682 23395 11328 64 -1662 -2326 C ATOM 1945 C LYS A1104 -81.820 -10.397 252.386 1.00146.61 C ANISOU 1945 C LYS A1104 20202 23800 11702 134 -1745 -2171 C ATOM 1946 O LYS A1104 -82.103 -11.095 251.404 1.00151.00 O ANISOU 1946 O LYS A1104 20787 24257 12331 88 -1686 -2013 O ATOM 1947 CB LYS A1104 -82.368 -7.950 252.504 1.00140.63 C ANISOU 1947 CB LYS A1104 19154 23023 11256 40 -1790 -2487 C ATOM 1948 N TYR A1105 -80.658 -10.529 253.032 1.00146.65 N ANISOU 1948 N TYR A1105 20244 23899 11579 269 -1904 -2244 N ATOM 1949 CA TYR A1105 -79.709 -11.519 252.534 1.00146.54 C ANISOU 1949 CA TYR A1105 20287 23882 11511 376 -2024 -2164 C ATOM 1950 C TYR A1105 -80.102 -12.952 252.874 1.00150.64 C ANISOU 1950 C TYR A1105 21122 24346 11769 433 -2019 -1990 C ATOM 1951 O TYR A1105 -79.691 -13.874 252.151 1.00152.10 O ANISOU 1951 O TYR A1105 21364 24476 11951 505 -2105 -1891 O ATOM 1952 CB TYR A1105 -78.311 -11.231 253.089 1.00144.43 C ANISOU 1952 CB TYR A1105 19939 23742 11196 527 -2231 -2351 C ATOM 1953 N GLY A1106 -81.070 -13.145 253.767 1.00149.84 N ANISOU 1953 N GLY A1106 21218 24248 11467 354 -1897 -1939 N ATOM 1954 CA GLY A1106 -81.629 -14.472 253.921 1.00149.95 C ANISOU 1954 CA GLY A1106 21559 24178 11236 315 -1865 -1738 C ATOM 1955 C GLY A1106 -82.612 -14.804 252.823 1.00149.97 C ANISOU 1955 C GLY A1106 21505 24075 11401 167 -1694 -1585 C ATOM 1956 O GLY A1106 -82.577 -15.911 252.271 1.00149.02 O ANISOU 1956 O GLY A1106 21557 23843 11221 194 -1755 -1415 O ATOM 1957 N SER A 364 -83.507 -13.868 252.501 1.00151.58 N ANISOU 1957 N SER A 364 21482 24300 11810 33 -1511 -1662 N ATOM 1958 CA SER A 364 -84.407 -14.107 251.378 1.00145.28 C ANISOU 1958 CA SER A 364 20611 23388 11202 -80 -1373 -1550 C ATOM 1959 C SER A 364 -83.617 -14.315 250.090 1.00146.97 C ANISOU 1959 C SER A 364 20719 23499 11626 10 -1493 -1477 C ATOM 1960 O SER A 364 -83.984 -15.148 249.250 1.00147.40 O ANISOU 1960 O SER A 364 20843 23438 11723 -12 -1462 -1315 O ATOM 1961 CB SER A 364 -85.384 -12.941 251.228 1.00137.41 C ANISOU 1961 CB SER A 364 19379 22419 10412 -186 -1228 -1713 C ATOM 1962 OG SER A 364 -86.345 -12.941 252.269 1.00136.43 O ANISOU 1962 OG SER A 364 19325 22430 10084 -296 -1074 -1794 O ATOM 1963 N GLN A 365 -82.513 -13.578 249.929 1.00150.34 N ANISOU 1963 N GLN A 365 20968 23985 12168 98 -1628 -1609 N ATOM 1964 CA GLN A 365 -81.686 -13.732 248.737 1.00155.12 C ANISOU 1964 CA GLN A 365 21441 24560 12939 149 -1724 -1580 C ATOM 1965 C GLN A 365 -81.060 -15.119 248.665 1.00160.16 C ANISOU 1965 C GLN A 365 22260 25193 13402 306 -1872 -1478 C ATOM 1966 O GLN A 365 -81.088 -15.772 247.611 1.00164.76 O ANISOU 1966 O GLN A 365 22831 25699 14073 325 -1883 -1367 O ATOM 1967 CB GLN A 365 -80.598 -12.656 248.708 1.00156.19 C ANISOU 1967 CB GLN A 365 21349 24806 13188 160 -1828 -1770 C ATOM 1968 CG GLN A 365 -81.096 -11.260 248.379 1.00154.41 C ANISOU 1968 CG GLN A 365 20961 24525 13184 -1 -1752 -1859 C ATOM 1969 CD GLN A 365 -79.962 -10.293 248.100 1.00155.26 C ANISOU 1969 CD GLN A 365 20871 24716 13404 -53 -1865 -2009 C ATOM 1970 OE1 GLN A 365 -78.788 -10.637 248.244 1.00156.67 O ANISOU 1970 OE1 GLN A 365 20986 25042 13497 41 -1980 -2085 O ATOM 1971 NE2 GLN A 365 -80.307 -9.076 247.697 1.00155.78 N ANISOU 1971 NE2 GLN A 365 20848 24687 13654 -211 -1855 -2074 N ATOM 1972 N GLN A 366 -80.488 -15.594 249.781 1.00162.86 N ANISOU 1972 N GLN A 366 22793 25600 13488 440 -2020 -1530 N ATOM 1973 CA GLN A 366 -79.939 -16.945 249.771 1.00166.01 C ANISOU 1973 CA GLN A 366 23426 25951 13699 618 -2230 -1455 C ATOM 1974 C GLN A 366 -81.013 -18.002 249.539 1.00173.29 C ANISOU 1974 C GLN A 366 24624 26701 14520 531 -2154 -1210 C ATOM 1975 O GLN A 366 -80.740 -19.031 248.910 1.00172.82 O ANISOU 1975 O GLN A 366 24681 26555 14429 649 -2307 -1120 O ATOM 1976 CB GLN A 366 -79.195 -17.222 251.078 1.00163.51 C ANISOU 1976 CB GLN A 366 23328 25694 13106 782 -2441 -1566 C ATOM 1977 CG GLN A 366 -78.589 -18.619 251.172 1.00163.37 C ANISOU 1977 CG GLN A 366 23618 25590 12867 1005 -2744 -1526 C ATOM 1978 CD GLN A 366 -77.591 -18.905 250.064 1.00160.59 C ANISOU 1978 CD GLN A 366 23019 25315 12681 1190 -2918 -1651 C ATOM 1979 OE1 GLN A 366 -76.411 -18.573 250.174 1.00162.83 O ANISOU 1979 OE1 GLN A 366 23102 25770 12997 1359 -3089 -1908 O ATOM 1980 NE2 GLN A 366 -78.061 -19.534 248.991 1.00155.24 N ANISOU 1980 NE2 GLN A 366 22341 24538 12105 1155 -2872 -1495 N ATOM 1981 N LYS A 367 -82.235 -17.771 250.025 1.00177.04 N ANISOU 1981 N LYS A 367 25188 27139 14938 323 -1927 -1126 N ATOM 1982 CA LYS A 367 -83.315 -18.712 249.740 1.00178.94 C ANISOU 1982 CA LYS A 367 25651 27238 15099 188 -1823 -911 C ATOM 1983 C LYS A 367 -83.667 -18.757 248.255 1.00179.63 C ANISOU 1983 C LYS A 367 25536 27234 15484 169 -1747 -835 C ATOM 1984 O LYS A 367 -83.868 -19.841 247.693 1.00181.29 O ANISOU 1984 O LYS A 367 25921 27309 15651 198 -1821 -671 O ATOM 1985 CB LYS A 367 -84.549 -18.354 250.568 1.00181.38 C ANISOU 1985 CB LYS A 367 26025 27599 15291 -57 -1570 -905 C ATOM 1986 N GLU A 368 -83.744 -17.595 247.602 1.00172.60 N ANISOU 1986 N GLU A 368 24308 26392 14882 119 -1626 -952 N ATOM 1987 CA GLU A 368 -84.209 -17.542 246.215 1.00160.82 C ANISOU 1987 CA GLU A 368 22656 24791 13657 75 -1542 -881 C ATOM 1988 C GLU A 368 -83.133 -17.832 245.170 1.00148.80 C ANISOU 1988 C GLU A 368 21013 23278 12245 228 -1707 -887 C ATOM 1989 O GLU A 368 -83.484 -18.078 244.004 1.00145.69 O ANISOU 1989 O GLU A 368 20552 22782 12023 212 -1664 -796 O ATOM 1990 CB GLU A 368 -84.875 -16.196 245.947 1.00164.42 C ANISOU 1990 CB GLU A 368 22874 25251 14349 -60 -1375 -1004 C ATOM 1991 CG GLU A 368 -85.975 -15.892 246.950 1.00170.97 C ANISOU 1991 CG GLU A 368 23762 26126 15072 -194 -1213 -1065 C ATOM 1992 CD GLU A 368 -86.559 -14.518 246.769 1.00174.69 C ANISOU 1992 CD GLU A 368 24004 26602 15769 -269 -1124 -1249 C ATOM 1993 OE1 GLU A 368 -85.839 -13.651 246.239 1.00175.79 O ANISOU 1993 OE1 GLU A 368 23989 26724 16079 -232 -1221 -1333 O ATOM 1994 OE2 GLU A 368 -87.729 -14.305 247.151 1.00176.36 O ANISOU 1994 OE2 GLU A 368 24194 26840 15976 -374 -975 -1331 O ATOM 1995 N LYS A 369 -81.848 -17.787 245.541 1.00147.09 N ANISOU 1995 N LYS A 369 20748 23206 11936 376 -1891 -1022 N ATOM 1996 CA LYS A 369 -80.786 -17.916 244.540 1.00142.72 C ANISOU 1996 CA LYS A 369 19998 22742 11487 495 -2024 -1102 C ATOM 1997 C LYS A 369 -80.879 -19.231 243.768 1.00144.21 C ANISOU 1997 C LYS A 369 20321 22826 11645 625 -2138 -963 C ATOM 1998 O LYS A 369 -80.560 -19.277 242.575 1.00142.27 O ANISOU 1998 O LYS A 369 19891 22613 11553 651 -2146 -978 O ATOM 1999 CB LYS A 369 -79.411 -17.759 245.189 1.00139.30 C ANISOU 1999 CB LYS A 369 19480 22513 10936 649 -2220 -1322 C ATOM 2000 CG LYS A 369 -79.014 -16.307 245.422 1.00137.26 C ANISOU 2000 CG LYS A 369 18972 22385 10794 513 -2129 -1493 C ATOM 2001 CD LYS A 369 -77.745 -15.951 244.660 1.00136.16 C ANISOU 2001 CD LYS A 369 18529 22458 10746 533 -2214 -1686 C ATOM 2002 CE LYS A 369 -77.259 -14.550 245.001 1.00133.67 C ANISOU 2002 CE LYS A 369 18010 22265 10514 375 -2160 -1857 C ATOM 2003 NZ LYS A 369 -78.096 -13.502 244.349 1.00127.35 N ANISOU 2003 NZ LYS A 369 17153 21324 9911 110 -1973 -1764 N ATOM 2004 N LYS A 370 -81.285 -20.317 244.429 1.00148.17 N ANISOU 2004 N LYS A 370 21165 23202 11931 696 -2243 -831 N ATOM 2005 CA LYS A 370 -81.292 -21.622 243.769 1.00149.06 C ANISOU 2005 CA LYS A 370 21447 23193 11994 844 -2419 -708 C ATOM 2006 C LYS A 370 -82.343 -21.673 242.662 1.00157.91 C ANISOU 2006 C LYS A 370 22504 24168 13326 710 -2225 -541 C ATOM 2007 O LYS A 370 -82.062 -22.123 241.541 1.00154.78 O ANISOU 2007 O LYS A 370 22004 23760 13046 823 -2308 -527 O ATOM 2008 CB LYS A 370 -81.533 -22.728 244.796 1.00144.35 C ANISOU 2008 CB LYS A 370 21307 22453 11087 901 -2601 -587 C ATOM 2009 N ALA A 371 -83.567 -21.228 242.961 1.00164.32 N ANISOU 2009 N ALA A 371 23366 24882 14187 483 -1978 -442 N ATOM 2010 CA ALA A 371 -84.591 -21.140 241.925 1.00159.81 C ANISOU 2010 CA ALA A 371 22706 24173 13842 367 -1800 -333 C ATOM 2011 C ALA A 371 -84.178 -20.165 240.831 1.00155.08 C ANISOU 2011 C ALA A 371 21782 23640 13502 358 -1736 -442 C ATOM 2012 O ALA A 371 -84.478 -20.389 239.649 1.00157.92 O ANISOU 2012 O ALA A 371 22075 23900 14028 372 -1712 -367 O ATOM 2013 CB ALA A 371 -85.929 -20.726 242.536 1.00162.79 C ANISOU 2013 CB ALA A 371 23144 24489 14221 138 -1560 -295 C ATOM 2014 N THR A 372 -83.475 -19.090 241.203 1.00144.29 N ANISOU 2014 N THR A 372 20237 22432 12154 317 -1720 -615 N ATOM 2015 CA THR A 372 -82.969 -18.156 240.203 1.00129.68 C ANISOU 2015 CA THR A 372 18126 20647 10499 252 -1680 -713 C ATOM 2016 C THR A 372 -82.021 -18.861 239.240 1.00126.06 C ANISOU 2016 C THR A 372 17570 20289 10037 400 -1825 -733 C ATOM 2017 O THR A 372 -82.106 -18.675 238.021 1.00125.87 O ANISOU 2017 O THR A 372 17430 20227 10170 344 -1770 -703 O ATOM 2018 CB THR A 372 -82.273 -16.978 240.885 1.00120.92 C ANISOU 2018 CB THR A 372 16874 19697 9372 169 -1673 -897 C ATOM 2019 OG1 THR A 372 -83.210 -16.293 241.727 1.00119.67 O ANISOU 2019 OG1 THR A 372 16786 19458 9225 52 -1551 -908 O ATOM 2020 CG2 THR A 372 -81.729 -16.006 239.849 1.00115.67 C ANISOU 2020 CG2 THR A 372 15989 19091 8870 34 -1640 -984 C ATOM 2021 N GLN A 373 -81.116 -19.681 239.775 1.00122.26 N ANISOU 2021 N GLN A 373 17143 19942 9367 604 -2033 -809 N ATOM 2022 CA GLN A 373 -80.164 -20.414 238.944 1.00124.80 C ANISOU 2022 CA GLN A 373 17344 20407 9667 793 -2213 -898 C ATOM 2023 C GLN A 373 -80.879 -21.424 238.050 1.00126.37 C ANISOU 2023 C GLN A 373 17674 20416 9927 880 -2245 -712 C ATOM 2024 O GLN A 373 -80.513 -21.598 236.878 1.00127.32 O ANISOU 2024 O GLN A 373 17624 20613 10138 930 -2270 -750 O ATOM 2025 CB GLN A 373 -79.138 -21.112 239.838 1.00129.05 C ANISOU 2025 CB GLN A 373 17952 21097 9983 1040 -2488 -1059 C ATOM 2026 CG GLN A 373 -78.138 -21.995 239.112 1.00130.89 C ANISOU 2026 CG GLN A 373 18059 21504 10169 1301 -2739 -1220 C ATOM 2027 CD GLN A 373 -77.191 -22.699 240.069 1.00130.46 C ANISOU 2027 CD GLN A 373 18117 21559 9892 1588 -3072 -1416 C ATOM 2028 OE1 GLN A 373 -77.128 -22.367 241.254 1.00127.26 O ANISOU 2028 OE1 GLN A 373 17846 21134 9371 1562 -3090 -1446 O ATOM 2029 NE2 GLN A 373 -76.454 -23.679 239.560 1.00130.97 N ANISOU 2029 NE2 GLN A 373 18136 21734 9892 1883 -3367 -1574 N ATOM 2030 N MET A 374 -81.891 -22.108 238.589 1.00125.97 N ANISOU 2030 N MET A 374 17923 20129 9811 880 -2244 -518 N ATOM 2031 CA MET A 374 -82.649 -23.059 237.778 1.00125.70 C ANISOU 2031 CA MET A 374 18027 19890 9842 941 -2276 -334 C ATOM 2032 C MET A 374 -83.323 -22.360 236.601 1.00123.38 C ANISOU 2032 C MET A 374 17560 19513 9806 787 -2056 -277 C ATOM 2033 O MET A 374 -83.266 -22.836 235.459 1.00124.00 O ANISOU 2033 O MET A 374 17573 19561 9980 883 -2111 -240 O ATOM 2034 CB MET A 374 -83.693 -23.773 238.637 1.00128.51 C ANISOU 2034 CB MET A 374 18734 20025 10070 877 -2269 -143 C ATOM 2035 CG MET A 374 -84.530 -24.784 237.866 1.00129.05 C ANISOU 2035 CG MET A 374 18965 19865 10201 915 -2309 52 C ATOM 2036 SD MET A 374 -85.964 -25.367 238.789 1.00130.19 S ANISOU 2036 SD MET A 374 19472 19782 10213 697 -2198 267 S ATOM 2037 CE MET A 374 -86.886 -23.842 238.969 1.00126.28 C ANISOU 2037 CE MET A 374 18735 19338 9908 418 -1813 185 C ATOM 2038 N LEU A 375 -83.948 -21.208 236.858 1.00120.38 N ANISOU 2038 N LEU A 375 17116 19087 9535 564 -1837 -291 N ATOM 2039 CA LEU A 375 -84.591 -20.471 235.774 1.00118.08 C ANISOU 2039 CA LEU A 375 16711 18674 9478 429 -1680 -260 C ATOM 2040 C LEU A 375 -83.566 -19.892 234.808 1.00115.03 C ANISOU 2040 C LEU A 375 16098 18460 9147 403 -1702 -379 C ATOM 2041 O LEU A 375 -83.846 -19.762 233.610 1.00111.97 O ANISOU 2041 O LEU A 375 15662 17978 8902 360 -1653 -328 O ATOM 2042 CB LEU A 375 -85.487 -19.376 236.345 1.00124.40 C ANISOU 2042 CB LEU A 375 17520 19380 10368 231 -1505 -295 C ATOM 2043 CG LEU A 375 -86.617 -19.931 237.210 1.00129.38 C ANISOU 2043 CG LEU A 375 18337 19888 10934 202 -1437 -206 C ATOM 2044 CD1 LEU A 375 -87.136 -18.886 238.176 1.00132.54 C ANISOU 2044 CD1 LEU A 375 18705 20321 11333 49 -1308 -326 C ATOM 2045 CD2 LEU A 375 -87.733 -20.448 236.320 1.00128.70 C ANISOU 2045 CD2 LEU A 375 18311 19579 11009 199 -1377 -84 C ATOM 2046 N ALA A 376 -82.369 -19.572 235.301 1.00121.27 N ANISOU 2046 N ALA A 376 16752 19515 9811 416 -1775 -548 N ATOM 2047 CA ALA A 376 -81.305 -19.100 234.423 1.00119.40 C ANISOU 2047 CA ALA A 376 16274 19509 9583 349 -1783 -692 C ATOM 2048 C ALA A 376 -80.890 -20.192 233.447 1.00125.79 C ANISOU 2048 C ALA A 376 17021 20405 10369 548 -1908 -691 C ATOM 2049 O ALA A 376 -80.697 -19.932 232.254 1.00122.93 O ANISOU 2049 O ALA A 376 16529 20099 10078 454 -1847 -708 O ATOM 2050 CB ALA A 376 -80.107 -18.630 235.248 1.00114.76 C ANISOU 2050 CB ALA A 376 15530 19216 8858 333 -1846 -910 C ATOM 2051 N ILE A 377 -80.754 -21.426 233.936 1.00134.61 N ANISOU 2051 N ILE A 377 18254 21524 11368 822 -2106 -679 N ATOM 2052 CA ILE A 377 -80.374 -22.510 233.035 1.00133.99 C ANISOU 2052 CA ILE A 377 18126 21518 11267 1056 -2277 -704 C ATOM 2053 C ILE A 377 -81.529 -22.870 232.103 1.00129.62 C ANISOU 2053 C ILE A 377 17707 20668 10874 1041 -2199 -476 C ATOM 2054 O ILE A 377 -81.303 -23.264 230.950 1.00131.74 O ANISOU 2054 O ILE A 377 17865 21000 11189 1128 -2244 -496 O ATOM 2055 CB ILE A 377 -79.893 -23.728 233.847 1.00139.66 C ANISOU 2055 CB ILE A 377 18988 22274 11801 1372 -2585 -770 C ATOM 2056 CG1 ILE A 377 -78.614 -23.383 234.612 1.00147.25 C ANISOU 2056 CG1 ILE A 377 19772 23562 12616 1430 -2696 -1058 C ATOM 2057 CG2 ILE A 377 -79.658 -24.933 232.946 1.00138.76 C ANISOU 2057 CG2 ILE A 377 18868 22180 11673 1655 -2816 -792 C ATOM 2058 CD1 ILE A 377 -77.469 -22.957 233.718 1.00151.06 C ANISOU 2058 CD1 ILE A 377 19855 24437 13105 1400 -2676 -1334 C ATOM 2059 N VAL A 378 -82.777 -22.699 232.552 1.00123.79 N ANISOU 2059 N VAL A 378 17182 19628 10224 926 -2074 -286 N ATOM 2060 CA VAL A 378 -83.915 -22.871 231.646 1.00120.30 C ANISOU 2060 CA VAL A 378 16836 18910 9963 891 -1983 -110 C ATOM 2061 C VAL A 378 -83.844 -21.866 230.499 1.00124.35 C ANISOU 2061 C VAL A 378 17188 19446 10615 714 -1838 -153 C ATOM 2062 O VAL A 378 -84.008 -22.218 229.322 1.00124.27 O ANISOU 2062 O VAL A 378 17156 19370 10693 776 -1854 -99 O ATOM 2063 CB VAL A 378 -85.241 -22.742 232.419 1.00114.61 C ANISOU 2063 CB VAL A 378 16319 17926 9304 771 -1859 27 C ATOM 2064 CG1 VAL A 378 -86.402 -22.550 231.456 1.00 94.74 C ANISOU 2064 CG1 VAL A 378 13837 15147 7012 699 -1737 136 C ATOM 2065 CG2 VAL A 378 -85.474 -23.961 233.287 1.00114.33 C ANISOU 2065 CG2 VAL A 378 16517 17813 9110 906 -2009 127 C ATOM 2066 N LEU A 379 -83.595 -20.596 230.834 1.00125.94 N ANISOU 2066 N LEU A 379 17307 19723 10820 482 -1714 -247 N ATOM 2067 CA LEU A 379 -83.435 -19.560 229.817 1.00133.02 C ANISOU 2067 CA LEU A 379 18116 20626 11800 260 -1608 -287 C ATOM 2068 C LEU A 379 -82.282 -19.879 228.872 1.00139.29 C ANISOU 2068 C LEU A 379 18708 21722 12494 293 -1664 -399 C ATOM 2069 O LEU A 379 -82.392 -19.688 227.653 1.00142.67 O ANISOU 2069 O LEU A 379 19125 22099 12983 201 -1614 -361 O ATOM 2070 CB LEU A 379 -83.226 -18.204 230.492 1.00135.29 C ANISOU 2070 CB LEU A 379 18378 20954 12073 9 -1522 -383 C ATOM 2071 CG LEU A 379 -82.717 -17.047 229.633 1.00137.10 C ANISOU 2071 CG LEU A 379 18542 21242 12307 -284 -1454 -451 C ATOM 2072 CD1 LEU A 379 -83.759 -16.653 228.598 1.00137.84 C ANISOU 2072 CD1 LEU A 379 18816 20987 12568 -374 -1416 -327 C ATOM 2073 CD2 LEU A 379 -82.351 -15.860 230.509 1.00138.39 C ANISOU 2073 CD2 LEU A 379 18684 21472 12425 -498 -1423 -562 C ATOM 2074 N GLY A 380 -81.161 -20.349 229.424 1.00135.81 N ANISOU 2074 N GLY A 380 18100 21614 11887 423 -1776 -569 N ATOM 2075 CA GLY A 380 -80.033 -20.726 228.588 1.00127.18 C ANISOU 2075 CA GLY A 380 16758 20880 10685 481 -1841 -748 C ATOM 2076 C GLY A 380 -80.387 -21.814 227.594 1.00115.99 C ANISOU 2076 C GLY A 380 15377 19377 9318 717 -1940 -663 C ATOM 2077 O GLY A 380 -80.037 -21.732 226.414 1.00117.56 O ANISOU 2077 O GLY A 380 15440 19722 9505 641 -1892 -719 O ATOM 2078 N VAL A 381 -81.059 -22.867 228.067 1.00108.23 N ANISOU 2078 N VAL A 381 14588 18164 8372 991 -2089 -531 N ATOM 2079 CA VAL A 381 -81.440 -23.960 227.177 1.00108.84 C ANISOU 2079 CA VAL A 381 14724 18124 8505 1234 -2218 -442 C ATOM 2080 C VAL A 381 -82.393 -23.457 226.099 1.00107.17 C ANISOU 2080 C VAL A 381 14604 17643 8471 1067 -2048 -270 C ATOM 2081 O VAL A 381 -82.293 -23.848 224.929 1.00106.96 O ANISOU 2081 O VAL A 381 14508 17664 8469 1150 -2082 -277 O ATOM 2082 CB VAL A 381 -82.050 -25.124 227.979 1.00 97.85 C ANISOU 2082 CB VAL A 381 13584 16492 7102 1496 -2418 -308 C ATOM 2083 CG1 VAL A 381 -82.585 -26.187 227.037 1.00 96.97 C ANISOU 2083 CG1 VAL A 381 13568 16201 7075 1722 -2555 -189 C ATOM 2084 CG2 VAL A 381 -81.011 -25.723 228.912 1.00100.09 C ANISOU 2084 CG2 VAL A 381 13821 17023 7185 1708 -2660 -503 C ATOM 2085 N PHE A 382 -83.324 -22.574 226.472 1.00107.64 N ANISOU 2085 N PHE A 382 14824 17422 8654 848 -1888 -143 N ATOM 2086 CA PHE A 382 -84.248 -22.009 225.491 1.00111.37 C ANISOU 2086 CA PHE A 382 15411 17605 9298 705 -1769 -18 C ATOM 2087 C PHE A 382 -83.496 -21.249 224.404 1.00113.20 C ANISOU 2087 C PHE A 382 15511 18035 9465 490 -1686 -114 C ATOM 2088 O PHE A 382 -83.766 -21.415 223.205 1.00107.67 O ANISOU 2088 O PHE A 382 14848 17237 8824 506 -1682 -54 O ATOM 2089 CB PHE A 382 -85.255 -21.096 226.195 1.00109.75 C ANISOU 2089 CB PHE A 382 15370 17114 9216 525 -1653 51 C ATOM 2090 CG PHE A 382 -86.073 -20.245 225.261 1.00106.93 C ANISOU 2090 CG PHE A 382 15140 16466 9021 362 -1571 111 C ATOM 2091 CD1 PHE A 382 -87.208 -20.752 224.650 1.00105.41 C ANISOU 2091 CD1 PHE A 382 15086 15956 9009 498 -1596 229 C ATOM 2092 CD2 PHE A 382 -85.714 -18.930 225.008 1.00107.49 C ANISOU 2092 CD2 PHE A 382 15222 16560 9060 69 -1499 39 C ATOM 2093 CE1 PHE A 382 -87.963 -19.966 223.797 1.00105.48 C ANISOU 2093 CE1 PHE A 382 15236 15673 9169 381 -1564 253 C ATOM 2094 CE2 PHE A 382 -86.463 -18.141 224.155 1.00107.18 C ANISOU 2094 CE2 PHE A 382 15367 16207 9151 -71 -1483 84 C ATOM 2095 CZ PHE A 382 -87.589 -18.660 223.549 1.00105.31 C ANISOU 2095 CZ PHE A 382 15262 15651 9099 104 -1523 181 C ATOM 2096 N ILE A 383 -82.543 -20.405 224.810 1.00119.10 N ANISOU 2096 N ILE A 383 16116 19064 10074 260 -1618 -266 N ATOM 2097 CA ILE A 383 -81.785 -19.619 223.840 1.00121.61 C ANISOU 2097 CA ILE A 383 16324 19599 10285 -34 -1519 -362 C ATOM 2098 C ILE A 383 -80.950 -20.529 222.948 1.00122.48 C ANISOU 2098 C ILE A 383 16206 20060 10273 125 -1583 -488 C ATOM 2099 O ILE A 383 -80.876 -20.327 221.730 1.00119.10 O ANISOU 2099 O ILE A 383 15776 19666 9809 -20 -1517 -477 O ATOM 2100 CB ILE A 383 -80.915 -18.574 224.562 1.00121.50 C ANISOU 2100 CB ILE A 383 16193 19832 10138 -330 -1441 -513 C ATOM 2101 CG1 ILE A 383 -81.801 -17.524 225.233 1.00120.10 C ANISOU 2101 CG1 ILE A 383 16259 19286 10087 -505 -1394 -403 C ATOM 2102 CG2 ILE A 383 -79.950 -17.913 223.589 1.00121.79 C ANISOU 2102 CG2 ILE A 383 16086 20184 10006 -675 -1336 -640 C ATOM 2103 CD1 ILE A 383 -82.864 -16.958 224.318 1.00119.56 C ANISOU 2103 CD1 ILE A 383 16467 18798 10164 -632 -1369 -247 C ATOM 2104 N ILE A 384 -80.322 -21.552 223.533 1.00124.93 N ANISOU 2104 N ILE A 384 16336 20630 10503 438 -1738 -628 N ATOM 2105 CA ILE A 384 -79.524 -22.486 222.741 1.00124.86 C ANISOU 2105 CA ILE A 384 16086 20976 10381 655 -1852 -807 C ATOM 2106 C ILE A 384 -80.395 -23.196 221.714 1.00126.78 C ANISOU 2106 C ILE A 384 16482 20935 10753 846 -1910 -629 C ATOM 2107 O ILE A 384 -80.002 -23.365 220.553 1.00131.81 O ANISOU 2107 O ILE A 384 16984 21780 11318 829 -1890 -714 O ATOM 2108 CB ILE A 384 -78.799 -23.487 223.661 1.00123.36 C ANISOU 2108 CB ILE A 384 15741 21036 10096 1015 -2090 -1004 C ATOM 2109 CG1 ILE A 384 -77.709 -22.777 224.465 1.00126.67 C ANISOU 2109 CG1 ILE A 384 15934 21831 10365 830 -2037 -1255 C ATOM 2110 CG2 ILE A 384 -78.209 -24.633 222.853 1.00122.52 C ANISOU 2110 CG2 ILE A 384 15431 21212 9910 1346 -2289 -1191 C ATOM 2111 CD1 ILE A 384 -76.704 -22.040 223.607 1.00131.02 C ANISOU 2111 CD1 ILE A 384 16180 22839 10763 498 -1867 -1486 C ATOM 2112 N CYS A 385 -81.595 -23.614 222.121 1.00126.56 N ANISOU 2112 N CYS A 385 16730 20448 10910 1015 -1975 -394 N ATOM 2113 CA CYS A 385 -82.474 -24.335 221.209 1.00122.72 C ANISOU 2113 CA CYS A 385 16391 19670 10566 1214 -2047 -230 C ATOM 2114 C CYS A 385 -82.956 -23.442 220.072 1.00116.03 C ANISOU 2114 C CYS A 385 15654 18645 9789 940 -1876 -132 C ATOM 2115 O CYS A 385 -82.982 -23.870 218.912 1.00110.07 O ANISOU 2115 O CYS A 385 14876 17909 9038 1035 -1910 -125 O ATOM 2116 CB CYS A 385 -83.661 -24.919 221.975 1.00120.07 C ANISOU 2116 CB CYS A 385 16314 18908 10400 1393 -2133 -23 C ATOM 2117 SG CYS A 385 -83.227 -26.259 223.110 1.00121.77 S ANISOU 2117 SG CYS A 385 16528 19234 10505 1750 -2415 -88 S ATOM 2118 N TRP A 386 -83.342 -22.203 220.376 1.00115.45 N ANISOU 2118 N TRP A 386 15724 18381 9759 610 -1722 -67 N ATOM 2119 CA TRP A 386 -83.999 -21.360 219.383 1.00113.37 C ANISOU 2119 CA TRP A 386 15672 17826 9577 377 -1626 45 C ATOM 2120 C TRP A 386 -83.051 -20.424 218.639 1.00114.00 C ANISOU 2120 C TRP A 386 15675 18194 9445 -11 -1500 -66 C ATOM 2121 O TRP A 386 -83.500 -19.713 217.734 1.00113.10 O ANISOU 2121 O TRP A 386 15787 17834 9351 -234 -1449 27 O ATOM 2122 CB TRP A 386 -85.114 -20.543 220.043 1.00110.87 C ANISOU 2122 CB TRP A 386 15612 17072 9440 263 -1589 161 C ATOM 2123 CG TRP A 386 -86.405 -21.295 220.156 1.00109.80 C ANISOU 2123 CG TRP A 386 15627 16555 9538 550 -1671 296 C ATOM 2124 CD1 TRP A 386 -86.931 -21.851 221.284 1.00111.85 C ANISOU 2124 CD1 TRP A 386 15895 16726 9878 719 -1712 331 C ATOM 2125 CD2 TRP A 386 -87.320 -21.599 219.095 1.00112.96 C ANISOU 2125 CD2 TRP A 386 16189 16628 10103 676 -1721 401 C ATOM 2126 NE1 TRP A 386 -88.124 -22.468 220.997 1.00112.77 N ANISOU 2126 NE1 TRP A 386 16153 16498 10197 910 -1767 447 N ATOM 2127 CE2 TRP A 386 -88.385 -22.330 219.659 1.00113.61 C ANISOU 2127 CE2 TRP A 386 16345 16446 10374 911 -1782 484 C ATOM 2128 CE3 TRP A 386 -87.345 -21.320 217.725 1.00117.59 C ANISOU 2128 CE3 TRP A 386 16878 17119 10681 597 -1720 428 C ATOM 2129 CZ2 TRP A 386 -89.463 -22.785 218.903 1.00114.90 C ANISOU 2129 CZ2 TRP A 386 16651 16263 10744 1083 -1844 576 C ATOM 2130 CZ3 TRP A 386 -88.417 -21.773 216.975 1.00117.92 C ANISOU 2130 CZ3 TRP A 386 17084 16792 10927 799 -1798 528 C ATOM 2131 CH2 TRP A 386 -89.460 -22.497 217.566 1.00115.98 C ANISOU 2131 CH2 TRP A 386 16878 16295 10893 1047 -1861 592 C ATOM 2132 N LEU A 387 -81.758 -20.399 218.986 1.00114.41 N ANISOU 2132 N LEU A 387 15430 18758 9283 -116 -1460 -274 N ATOM 2133 CA LEU A 387 -80.847 -19.473 218.314 1.00115.25 C ANISOU 2133 CA LEU A 387 15455 19175 9161 -562 -1313 -392 C ATOM 2134 C LEU A 387 -80.576 -19.840 216.857 1.00115.06 C ANISOU 2134 C LEU A 387 15376 19324 9017 -595 -1282 -425 C ATOM 2135 O LEU A 387 -80.620 -18.936 216.003 1.00121.97 O ANISOU 2135 O LEU A 387 16450 20103 9788 -992 -1174 -359 O ATOM 2136 CB LEU A 387 -79.546 -19.363 219.115 1.00116.76 C ANISOU 2136 CB LEU A 387 15301 19900 9162 -664 -1274 -651 C ATOM 2137 CG LEU A 387 -78.784 -18.041 219.027 1.00116.21 C ANISOU 2137 CG LEU A 387 15213 20048 8894 -1227 -1106 -743 C ATOM 2138 CD1 LEU A 387 -79.714 -16.869 219.296 1.00114.23 C ANISOU 2138 CD1 LEU A 387 15373 19260 8768 -1486 -1089 -524 C ATOM 2139 CD2 LEU A 387 -77.616 -18.034 220.001 1.00117.40 C ANISOU 2139 CD2 LEU A 387 15006 20691 8908 -1252 -1095 -1015 C ATOM 2140 N PRO A 388 -80.281 -21.099 216.497 1.00110.46 N ANISOU 2140 N PRO A 388 14557 18990 8422 -211 -1391 -533 N ATOM 2141 CA PRO A 388 -79.957 -21.385 215.087 1.00110.22 C ANISOU 2141 CA PRO A 388 14448 19181 8250 -262 -1351 -598 C ATOM 2142 C PRO A 388 -81.072 -21.027 214.121 1.00109.92 C ANISOU 2142 C PRO A 388 14813 18615 8336 -346 -1338 -338 C ATOM 2143 O PRO A 388 -80.792 -20.654 212.975 1.00108.08 O ANISOU 2143 O PRO A 388 14634 18506 7925 -625 -1238 -354 O ATOM 2144 CB PRO A 388 -79.671 -22.893 215.091 1.00108.18 C ANISOU 2144 CB PRO A 388 13912 19168 8023 279 -1551 -747 C ATOM 2145 CG PRO A 388 -79.288 -23.201 216.488 1.00108.84 C ANISOU 2145 CG PRO A 388 13841 19376 8135 470 -1657 -861 C ATOM 2146 CD PRO A 388 -80.131 -22.304 217.334 1.00107.30 C ANISOU 2146 CD PRO A 388 13962 18710 8096 270 -1581 -628 C ATOM 2147 N PHE A 389 -82.328 -21.118 214.559 1.00110.78 N ANISOU 2147 N PHE A 389 15208 18151 8732 -123 -1441 -120 N ATOM 2148 CA PHE A 389 -83.457 -20.755 213.709 1.00114.40 C ANISOU 2148 CA PHE A 389 16053 18075 9338 -161 -1465 88 C ATOM 2149 C PHE A 389 -83.357 -19.301 213.261 1.00118.09 C ANISOU 2149 C PHE A 389 16796 18419 9655 -705 -1349 132 C ATOM 2150 O PHE A 389 -83.360 -18.999 212.060 1.00118.86 O ANISOU 2150 O PHE A 389 17075 18460 9624 -910 -1315 176 O ATOM 2151 CB PHE A 389 -84.764 -21.012 214.465 1.00116.56 C ANISOU 2151 CB PHE A 389 16524 17825 9937 134 -1581 244 C ATOM 2152 CG PHE A 389 -85.998 -20.874 213.621 1.00121.52 C ANISOU 2152 CG PHE A 389 17498 17912 10764 212 -1653 404 C ATOM 2153 CD1 PHE A 389 -86.495 -21.954 212.914 1.00123.51 C ANISOU 2153 CD1 PHE A 389 17738 18046 11144 579 -1762 459 C ATOM 2154 CD2 PHE A 389 -86.681 -19.671 213.565 1.00122.83 C ANISOU 2154 CD2 PHE A 389 18008 17663 10997 -53 -1649 476 C ATOM 2155 CE1 PHE A 389 -87.637 -21.829 212.145 1.00123.35 C ANISOU 2155 CE1 PHE A 389 18025 17523 11319 669 -1841 581 C ATOM 2156 CE2 PHE A 389 -87.826 -19.542 212.802 1.00121.81 C ANISOU 2156 CE2 PHE A 389 18200 17024 11059 55 -1755 579 C ATOM 2157 CZ PHE A 389 -88.303 -20.622 212.090 1.00122.09 C ANISOU 2157 CZ PHE A 389 18200 16962 11226 414 -1839 630 C ATOM 2158 N PHE A 390 -83.251 -18.381 214.221 1.00121.38 N ANISOU 2158 N PHE A 390 17274 18781 10063 -955 -1306 121 N ATOM 2159 CA PHE A 390 -83.157 -16.970 213.870 1.00124.16 C ANISOU 2159 CA PHE A 390 17939 18972 10264 -1483 -1247 166 C ATOM 2160 C PHE A 390 -81.827 -16.640 213.205 1.00131.02 C ANISOU 2160 C PHE A 390 18634 20390 10758 -1926 -1082 28 C ATOM 2161 O PHE A 390 -81.764 -15.720 212.384 1.00134.16 O ANISOU 2161 O PHE A 390 19350 20657 10969 -2380 -1041 96 O ATOM 2162 CB PHE A 390 -83.364 -16.108 215.114 1.00123.52 C ANISOU 2162 CB PHE A 390 17950 18707 10275 -1607 -1271 168 C ATOM 2163 CG PHE A 390 -84.767 -16.150 215.648 1.00122.32 C ANISOU 2163 CG PHE A 390 18023 17998 10455 -1286 -1415 277 C ATOM 2164 CD1 PHE A 390 -85.129 -17.081 216.607 1.00119.44 C ANISOU 2164 CD1 PHE A 390 17433 17669 10282 -871 -1448 260 C ATOM 2165 CD2 PHE A 390 -85.727 -15.268 215.180 1.00122.95 C ANISOU 2165 CD2 PHE A 390 18549 17526 10640 -1408 -1534 372 C ATOM 2166 CE1 PHE A 390 -86.420 -17.126 217.098 1.00117.08 C ANISOU 2166 CE1 PHE A 390 17306 16917 10264 -624 -1549 329 C ATOM 2167 CE2 PHE A 390 -87.021 -15.309 215.666 1.00120.85 C ANISOU 2167 CE2 PHE A 390 18435 16803 10681 -1106 -1666 406 C ATOM 2168 CZ PHE A 390 -87.367 -16.239 216.626 1.00117.58 C ANISOU 2168 CZ PHE A 390 17748 16481 10446 -732 -1650 382 C ATOM 2169 N ILE A 391 -80.760 -17.376 213.531 1.00133.75 N ANISOU 2169 N ILE A 391 18490 21356 10972 -1816 -1003 -187 N ATOM 2170 CA ILE A 391 -79.485 -17.164 212.847 1.00143.14 C ANISOU 2170 CA ILE A 391 19436 23155 11796 -2226 -831 -383 C ATOM 2171 C ILE A 391 -79.633 -17.450 211.356 1.00148.30 C ANISOU 2171 C ILE A 391 20222 23805 12322 -2283 -804 -331 C ATOM 2172 O ILE A 391 -79.213 -16.654 210.504 1.00152.01 O ANISOU 2172 O ILE A 391 20869 24386 12500 -2827 -675 -325 O ATOM 2173 CB ILE A 391 -78.376 -18.020 213.490 1.00145.95 C ANISOU 2173 CB ILE A 391 19206 24182 12068 -1994 -803 -690 C ATOM 2174 CG1 ILE A 391 -77.605 -17.211 214.540 1.00147.92 C ANISOU 2174 CG1 ILE A 391 19308 24681 12215 -2314 -719 -826 C ATOM 2175 CG2 ILE A 391 -77.405 -18.544 212.439 1.00148.87 C ANISOU 2175 CG2 ILE A 391 19232 25178 12152 -2091 -697 -934 C ATOM 2176 CD1 ILE A 391 -78.464 -16.571 215.609 1.00144.38 C ANISOU 2176 CD1 ILE A 391 19171 23678 12008 -2267 -813 -628 C ATOM 2177 N THR A 392 -80.261 -18.580 211.017 1.00147.17 N ANISOU 2177 N THR A 392 20026 23509 12382 -1741 -936 -283 N ATOM 2178 CA THR A 392 -80.483 -18.907 209.614 1.00146.09 C ANISOU 2178 CA THR A 392 20024 23333 12151 -1734 -934 -230 C ATOM 2179 C THR A 392 -81.475 -17.954 208.964 1.00140.97 C ANISOU 2179 C THR A 392 19993 22021 11550 -1999 -983 35 C ATOM 2180 O THR A 392 -81.352 -17.659 207.772 1.00141.67 O ANISOU 2180 O THR A 392 20291 22130 11408 -2298 -921 72 O ATOM 2181 CB THR A 392 -80.965 -20.350 209.473 1.00148.87 C ANISOU 2181 CB THR A 392 20192 23636 12737 -1064 -1101 -240 C ATOM 2182 OG1 THR A 392 -81.995 -20.612 210.435 1.00150.08 O ANISOU 2182 OG1 THR A 392 20494 23279 13253 -688 -1260 -81 O ATOM 2183 CG2 THR A 392 -79.811 -21.314 209.687 1.00150.87 C ANISOU 2183 CG2 THR A 392 19865 24612 12845 -838 -1094 -560 C ATOM 2184 N HIS A 393 -82.458 -17.462 209.721 1.00138.34 N ANISOU 2184 N HIS A 393 19965 21103 11494 -1891 -1112 196 N ATOM 2185 CA HIS A 393 -83.378 -16.469 209.172 1.00138.77 C ANISOU 2185 CA HIS A 393 20620 20512 11592 -2125 -1215 392 C ATOM 2186 C HIS A 393 -82.637 -15.193 208.783 1.00133.95 C ANISOU 2186 C HIS A 393 20264 20022 10610 -2849 -1104 390 C ATOM 2187 O HIS A 393 -82.835 -14.651 207.686 1.00133.96 O ANISOU 2187 O HIS A 393 20693 19777 10429 -3162 -1133 497 O ATOM 2188 CB HIS A 393 -84.485 -16.167 210.181 1.00145.33 C ANISOU 2188 CB HIS A 393 21650 20786 12781 -1865 -1380 483 C ATOM 2189 CG HIS A 393 -85.756 -16.913 209.923 1.00148.83 C ANISOU 2189 CG HIS A 393 22221 20762 13566 -1343 -1548 579 C ATOM 2190 ND1 HIS A 393 -86.771 -16.406 209.141 1.00149.62 N ANISOU 2190 ND1 HIS A 393 22814 20264 13772 -1347 -1710 694 N ATOM 2191 CD2 HIS A 393 -86.173 -18.133 210.336 1.00147.65 C ANISOU 2191 CD2 HIS A 393 21784 20650 13666 -814 -1596 564 C ATOM 2192 CE1 HIS A 393 -87.761 -17.278 209.089 1.00147.58 C ANISOU 2192 CE1 HIS A 393 22522 19721 13831 -839 -1828 729 C ATOM 2193 NE2 HIS A 393 -87.424 -18.335 209.805 1.00145.90 N ANISOU 2193 NE2 HIS A 393 21850 19882 13703 -530 -1756 667 N ATOM 2194 N ILE A 394 -81.782 -14.695 209.679 1.00130.50 N ANISOU 2194 N ILE A 394 19596 19945 10043 -3140 -989 272 N ATOM 2195 CA ILE A 394 -81.023 -13.480 209.393 1.00128.30 C ANISOU 2195 CA ILE A 394 19546 19805 9398 -3875 -881 266 C ATOM 2196 C ILE A 394 -80.060 -13.715 208.236 1.00129.56 C ANISOU 2196 C ILE A 394 19545 20524 9156 -4240 -677 160 C ATOM 2197 O ILE A 394 -79.839 -12.827 207.403 1.00130.97 O ANISOU 2197 O ILE A 394 20132 20621 9011 -4844 -630 243 O ATOM 2198 CB ILE A 394 -80.290 -12.994 210.658 1.00122.77 C ANISOU 2198 CB ILE A 394 18571 19407 8668 -4064 -803 135 C ATOM 2199 CG1 ILE A 394 -81.293 -12.687 211.771 1.00118.25 C ANISOU 2199 CG1 ILE A 394 18186 18278 8465 -3733 -1003 232 C ATOM 2200 CG2 ILE A 394 -79.445 -11.765 210.355 1.00123.87 C ANISOU 2200 CG2 ILE A 394 18932 19721 8412 -4867 -688 120 C ATOM 2201 CD1 ILE A 394 -82.336 -11.659 211.388 1.00112.90 C ANISOU 2201 CD1 ILE A 394 18192 16844 7863 -3898 -1225 422 C ATOM 2202 N LEU A 395 -79.479 -14.916 208.157 1.00127.73 N ANISOU 2202 N LEU A 395 18739 20874 8919 -3889 -572 -40 N ATOM 2203 CA LEU A 395 -78.644 -15.253 207.008 1.00132.77 C ANISOU 2203 CA LEU A 395 19176 22080 9190 -4161 -389 -187 C ATOM 2204 C LEU A 395 -79.446 -15.187 205.714 1.00137.07 C ANISOU 2204 C LEU A 395 20231 22160 9688 -4195 -478 24 C ATOM 2205 O LEU A 395 -79.019 -14.565 204.736 1.00145.13 O ANISOU 2205 O LEU A 395 21514 23312 10316 -4790 -354 48 O ATOM 2206 CB LEU A 395 -78.031 -16.642 207.191 1.00131.70 C ANISOU 2206 CB LEU A 395 18347 22576 9116 -3642 -348 -468 C ATOM 2207 CG LEU A 395 -76.766 -16.737 208.045 1.00134.36 C ANISOU 2207 CG LEU A 395 18094 23648 9310 -3761 -206 -799 C ATOM 2208 CD1 LEU A 395 -76.239 -18.164 208.058 1.00135.17 C ANISOU 2208 CD1 LEU A 395 17582 24312 9463 -3191 -246 -1101 C ATOM 2209 CD2 LEU A 395 -75.705 -15.775 207.535 1.00137.82 C ANISOU 2209 CD2 LEU A 395 18511 24582 9273 -4596 54 -937 C ATOM 2210 N ASN A 396 -80.627 -15.810 205.703 1.00131.60 N ANISOU 2210 N ASN A 396 19708 20911 9383 -3581 -698 175 N ATOM 2211 CA ASN A 396 -81.462 -15.828 204.507 1.00127.71 C ANISOU 2211 CA ASN A 396 19690 19941 8894 -3523 -818 355 C ATOM 2212 C ASN A 396 -81.856 -14.416 204.090 1.00128.08 C ANISOU 2212 C ASN A 396 20467 19432 8765 -4098 -902 556 C ATOM 2213 O ASN A 396 -81.923 -14.109 202.893 1.00133.10 O ANISOU 2213 O ASN A 396 21505 19933 9135 -4413 -903 649 O ATOM 2214 CB ASN A 396 -82.701 -16.691 204.764 1.00122.55 C ANISOU 2214 CB ASN A 396 19062 18770 8731 -2762 -1051 457 C ATOM 2215 CG ASN A 396 -83.459 -17.036 203.493 1.00122.87 C ANISOU 2215 CG ASN A 396 19443 18438 8802 -2572 -1172 580 C ATOM 2216 OD1 ASN A 396 -83.705 -16.181 202.645 1.00126.85 O ANISOU 2216 OD1 ASN A 396 20499 18597 9100 -2978 -1217 711 O ATOM 2217 ND2 ASN A 396 -83.837 -18.302 203.362 1.00120.57 N ANISOU 2217 ND2 ASN A 396 18855 18193 8763 -1949 -1253 539 N ATOM 2218 N ILE A 397 -82.106 -13.538 205.060 1.00125.10 N ANISOU 2218 N ILE A 397 20297 18722 8514 -4243 -998 617 N ATOM 2219 CA ILE A 397 -82.562 -12.187 204.738 1.00125.43 C ANISOU 2219 CA ILE A 397 21086 18154 8419 -4730 -1165 795 C ATOM 2220 C ILE A 397 -81.404 -11.311 204.267 1.00132.67 C ANISOU 2220 C ILE A 397 22138 19483 8787 -5599 -963 767 C ATOM 2221 O ILE A 397 -81.416 -10.791 203.145 1.00133.91 O ANISOU 2221 O ILE A 397 22813 19450 8617 -6052 -988 885 O ATOM 2222 CB ILE A 397 -83.282 -11.557 205.944 1.00125.05 C ANISOU 2222 CB ILE A 397 21209 17598 8705 -4543 -1378 839 C ATOM 2223 CG1 ILE A 397 -84.582 -12.304 206.237 1.00118.17 C ANISOU 2223 CG1 ILE A 397 20314 16248 8337 -3773 -1588 873 C ATOM 2224 CG2 ILE A 397 -83.564 -10.085 205.686 1.00129.03 C ANISOU 2224 CG2 ILE A 397 22473 17532 9023 -5088 -1586 975 C ATOM 2225 CD1 ILE A 397 -85.602 -12.175 205.131 1.00114.28 C ANISOU 2225 CD1 ILE A 397 20398 15117 7905 -3651 -1824 1005 C ATOM 2226 N HIS A 398 -80.390 -11.132 205.112 1.00140.74 N ANISOU 2226 N HIS A 398 22714 21075 9685 -5869 -762 605 N ATOM 2227 CA HIS A 398 -79.323 -10.171 204.859 1.00150.20 C ANISOU 2227 CA HIS A 398 24043 22642 10386 -6748 -577 567 C ATOM 2228 C HIS A 398 -78.108 -10.773 204.162 1.00158.36 C ANISOU 2228 C HIS A 398 24552 24593 11022 -7056 -227 343 C ATOM 2229 O HIS A 398 -77.073 -10.105 204.067 1.00158.57 O ANISOU 2229 O HIS A 398 24527 25094 10629 -7794 -12 243 O ATOM 2230 CB HIS A 398 -78.895 -9.514 206.173 1.00151.02 C ANISOU 2230 CB HIS A 398 23975 22838 10566 -6918 -569 491 C ATOM 2231 CG HIS A 398 -79.982 -8.725 206.834 1.00146.65 C ANISOU 2231 CG HIS A 398 23960 21434 10325 -6735 -913 671 C ATOM 2232 ND1 HIS A 398 -80.784 -9.247 207.826 1.00140.70 N ANISOU 2232 ND1 HIS A 398 22981 20412 10068 -6008 -1064 649 N ATOM 2233 CD2 HIS A 398 -80.405 -7.453 206.640 1.00148.20 C ANISOU 2233 CD2 HIS A 398 24916 20999 10394 -7184 -1155 846 C ATOM 2234 CE1 HIS A 398 -81.652 -8.331 208.216 1.00140.19 C ANISOU 2234 CE1 HIS A 398 23460 19631 10175 -6003 -1366 775 C ATOM 2235 NE2 HIS A 398 -81.443 -7.233 207.513 1.00144.69 N ANISOU 2235 NE2 HIS A 398 24643 19947 10383 -6685 -1452 892 N ATOM 2236 N CYS A 399 -78.201 -12.005 203.673 1.00168.44 N ANISOU 2236 N CYS A 399 25434 26151 12414 -6520 -174 238 N ATOM 2237 CA CYS A 399 -77.134 -12.616 202.895 1.00179.27 C ANISOU 2237 CA CYS A 399 26316 28388 13409 -6756 120 -13 C ATOM 2238 C CYS A 399 -77.527 -12.951 201.468 1.00176.47 C ANISOU 2238 C CYS A 399 26277 27899 12874 -6763 106 90 C ATOM 2239 O CYS A 399 -76.664 -12.920 200.586 1.00184.11 O ANISOU 2239 O CYS A 399 27119 29471 13364 -7294 358 -54 O ATOM 2240 CB CYS A 399 -76.646 -13.910 203.573 1.00188.93 C ANISOU 2240 CB CYS A 399 26674 30238 14874 -6096 192 -324 C ATOM 2241 SG CYS A 399 -75.834 -15.075 202.438 1.00202.19 S ANISOU 2241 SG CYS A 399 27774 32792 16259 -5986 402 -644 S ATOM 2242 N ASP A 400 -78.808 -13.230 201.217 1.00166.76 N ANISOU 2242 N ASP A 400 25460 25901 11998 -6217 -180 320 N ATOM 2243 CA ASP A 400 -79.259 -13.911 200.005 1.00166.55 C ANISOU 2243 CA ASP A 400 25576 25775 11928 -5959 -227 372 C ATOM 2244 C ASP A 400 -78.671 -15.317 199.935 1.00168.19 C ANISOU 2244 C ASP A 400 24967 26739 12197 -5448 -85 74 C ATOM 2245 O ASP A 400 -78.449 -15.865 198.852 1.00170.17 O ANISOU 2245 O ASP A 400 25128 27310 12218 -5448 5 -10 O ATOM 2246 CB ASP A 400 -78.926 -13.113 198.739 1.00170.19 C ANISOU 2246 CB ASP A 400 26585 26256 11823 -6766 -114 474 C ATOM 2247 CG ASP A 400 -79.549 -11.731 198.739 1.00167.04 C ANISOU 2247 CG ASP A 400 27089 25030 11348 -7249 -338 770 C ATOM 2248 OD1 ASP A 400 -80.563 -11.534 199.440 1.00161.51 O ANISOU 2248 OD1 ASP A 400 26661 23605 11102 -6793 -640 912 O ATOM 2249 OD2 ASP A 400 -79.027 -10.842 198.033 1.00169.76 O ANISOU 2249 OD2 ASP A 400 27884 25453 11163 -8095 -228 842 O ATOM 2250 N CYS A 401 -78.417 -15.896 201.109 1.00167.26 N ANISOU 2250 N CYS A 401 24276 26894 12380 -5002 -94 -99 N ATOM 2251 CA CYS A 401 -77.916 -17.260 201.211 1.00167.10 C ANISOU 2251 CA CYS A 401 23513 27508 12468 -4429 -52 -398 C ATOM 2252 C CYS A 401 -78.958 -18.244 200.695 1.00156.02 C ANISOU 2252 C CYS A 401 22224 25655 11403 -3704 -287 -270 C ATOM 2253 O CYS A 401 -80.112 -18.228 201.133 1.00152.44 O ANISOU 2253 O CYS A 401 22119 24441 11360 -3308 -525 -27 O ATOM 2254 CB CYS A 401 -77.566 -17.586 202.664 1.00173.89 C ANISOU 2254 CB CYS A 401 23878 28595 13598 -4096 -83 -564 C ATOM 2255 SG CYS A 401 -76.010 -16.901 203.304 1.00188.46 S ANISOU 2255 SG CYS A 401 25264 31285 15058 -4772 211 -887 S ATOM 2256 N ASN A 402 -78.552 -19.106 199.762 1.00152.59 N ANISOU 2256 N ASN A 402 21475 25710 10792 -3530 -223 -459 N ATOM 2257 CA ASN A 402 -79.423 -20.176 199.278 1.00144.56 C ANISOU 2257 CA ASN A 402 20481 24353 10093 -2803 -453 -381 C ATOM 2258 C ASN A 402 -79.442 -21.274 200.339 1.00141.73 C ANISOU 2258 C ASN A 402 19596 24130 10127 -2081 -613 -532 C ATOM 2259 O ASN A 402 -78.741 -22.286 200.256 1.00142.88 O ANISOU 2259 O ASN A 402 19166 24908 10216 -1743 -615 -842 O ATOM 2260 CB ASN A 402 -78.948 -20.694 197.927 1.00143.25 C ANISOU 2260 CB ASN A 402 20164 24681 9585 -2870 -347 -548 C ATOM 2261 CG ASN A 402 -78.956 -19.619 196.855 1.00143.60 C ANISOU 2261 CG ASN A 402 20803 24559 9198 -3622 -201 -376 C ATOM 2262 OD1 ASN A 402 -79.764 -18.691 196.897 1.00141.95 O ANISOU 2262 OD1 ASN A 402 21274 23585 9074 -3864 -313 -55 O ATOM 2263 ND2 ASN A 402 -78.055 -19.742 195.887 1.00144.84 N ANISOU 2263 ND2 ASN A 402 20723 25438 8872 -4001 30 -608 N ATOM 2264 N ILE A 403 -80.265 -21.060 201.356 1.00135.78 N ANISOU 2264 N ILE A 403 19065 22764 9759 -1847 -771 -324 N ATOM 2265 CA ILE A 403 -80.312 -21.970 202.502 1.00132.22 C ANISOU 2265 CA ILE A 403 18207 22380 9650 -1254 -922 -428 C ATOM 2266 C ILE A 403 -81.223 -23.147 202.162 1.00130.81 C ANISOU 2266 C ILE A 403 18050 21841 9811 -540 -1178 -340 C ATOM 2267 O ILE A 403 -82.367 -22.929 201.734 1.00133.75 O ANISOU 2267 O ILE A 403 18912 21518 10391 -440 -1298 -68 O ATOM 2268 CB ILE A 403 -80.805 -21.238 203.746 1.00132.37 C ANISOU 2268 CB ILE A 403 18451 21938 9907 -1343 -963 -256 C ATOM 2269 CG1 ILE A 403 -79.806 -20.156 204.162 1.00138.61 C ANISOU 2269 CG1 ILE A 403 19165 23132 10368 -2020 -731 -372 C ATOM 2270 CG2 ILE A 403 -81.038 -22.217 204.887 1.00129.96 C ANISOU 2270 CG2 ILE A 403 17828 21597 9954 -725 -1142 -312 C ATOM 2271 CD1 ILE A 403 -78.451 -20.695 204.563 1.00143.85 C ANISOU 2271 CD1 ILE A 403 19148 24683 10824 -2012 -609 -762 C ATOM 2272 N PRO A 404 -80.763 -24.389 202.331 1.00127.37 N ANISOU 2272 N PRO A 404 17116 21840 9440 -29 -1297 -578 N ATOM 2273 CA PRO A 404 -81.630 -25.529 202.052 1.00122.85 C ANISOU 2273 CA PRO A 404 16584 20900 9192 638 -1569 -484 C ATOM 2274 C PRO A 404 -82.730 -25.639 203.097 1.00113.47 C ANISOU 2274 C PRO A 404 15636 19036 8442 947 -1743 -239 C ATOM 2275 O PRO A 404 -82.536 -25.254 204.262 1.00112.21 O ANISOU 2275 O PRO A 404 15403 18895 8336 823 -1698 -246 O ATOM 2276 CB PRO A 404 -80.671 -26.730 202.118 1.00121.67 C ANISOU 2276 CB PRO A 404 15831 21449 8950 1048 -1680 -851 C ATOM 2277 CG PRO A 404 -79.572 -26.275 203.015 1.00121.13 C ANISOU 2277 CG PRO A 404 15415 21932 8676 731 -1524 -1094 C ATOM 2278 CD PRO A 404 -79.412 -24.804 202.751 1.00125.04 C ANISOU 2278 CD PRO A 404 16206 22390 8914 -36 -1222 -973 C ATOM 2279 N PRO A 405 -83.904 -26.153 202.720 1.00106.26 N ANISOU 2279 N PRO A 405 15001 17534 7838 1339 -1937 -34 N ATOM 2280 CA PRO A 405 -84.984 -26.309 203.709 1.00106.24 C ANISOU 2280 CA PRO A 405 15192 16936 8239 1611 -2085 165 C ATOM 2281 C PRO A 405 -84.684 -27.334 204.791 1.00114.81 C ANISOU 2281 C PRO A 405 15924 18242 9457 2013 -2237 50 C ATOM 2282 O PRO A 405 -85.338 -27.304 205.843 1.00116.43 O ANISOU 2282 O PRO A 405 16244 18085 9907 2101 -2295 181 O ATOM 2283 CB PRO A 405 -86.184 -26.743 202.856 1.00102.36 C ANISOU 2283 CB PRO A 405 15014 15872 8007 1939 -2256 345 C ATOM 2284 CG PRO A 405 -85.855 -26.289 201.468 1.00106.58 C ANISOU 2284 CG PRO A 405 15695 16549 8252 1665 -2151 315 C ATOM 2285 CD PRO A 405 -84.366 -26.414 201.348 1.00109.17 C ANISOU 2285 CD PRO A 405 15577 17715 8186 1461 -2000 33 C ATOM 2286 N VAL A 406 -83.737 -28.249 204.561 1.00123.99 N ANISOU 2286 N VAL A 406 16679 19977 10454 2264 -2327 -209 N ATOM 2287 CA VAL A 406 -83.405 -29.240 205.581 1.00132.98 C ANISOU 2287 CA VAL A 406 17537 21297 11691 2661 -2536 -337 C ATOM 2288 C VAL A 406 -82.895 -28.557 206.844 1.00138.91 C ANISOU 2288 C VAL A 406 18197 22212 12370 2365 -2404 -389 C ATOM 2289 O VAL A 406 -83.233 -28.961 207.963 1.00139.60 O ANISOU 2289 O VAL A 406 18314 22084 12644 2575 -2539 -318 O ATOM 2290 CB VAL A 406 -82.390 -30.261 205.032 1.00139.88 C ANISOU 2290 CB VAL A 406 17986 22794 12369 2989 -2698 -675 C ATOM 2291 CG1 VAL A 406 -83.065 -31.195 204.040 1.00139.72 C ANISOU 2291 CG1 VAL A 406 18072 22511 12505 3427 -2923 -598 C ATOM 2292 CG2 VAL A 406 -81.212 -29.553 204.377 1.00145.38 C ANISOU 2292 CG2 VAL A 406 18409 24165 12662 2555 -2436 -947 C ATOM 2293 N LEU A 407 -82.091 -27.501 206.687 1.00144.32 N ANISOU 2293 N LEU A 407 18793 23270 12771 1848 -2137 -508 N ATOM 2294 CA LEU A 407 -81.628 -26.750 207.849 1.00147.70 C ANISOU 2294 CA LEU A 407 19154 23829 13136 1540 -2006 -551 C ATOM 2295 C LEU A 407 -82.787 -26.052 208.548 1.00143.77 C ANISOU 2295 C LEU A 407 19070 22655 12900 1414 -1973 -237 C ATOM 2296 O LEU A 407 -82.833 -25.998 209.783 1.00144.72 O ANISOU 2296 O LEU A 407 19165 22702 13122 1448 -2002 -219 O ATOM 2297 CB LEU A 407 -80.564 -25.734 207.435 1.00154.55 C ANISOU 2297 CB LEU A 407 19865 25221 13635 965 -1726 -738 C ATOM 2298 CG LEU A 407 -79.206 -26.288 207.003 1.00158.97 C ANISOU 2298 CG LEU A 407 19899 26612 13890 1016 -1715 -1156 C ATOM 2299 CD1 LEU A 407 -78.282 -25.160 206.572 1.00165.05 C ANISOU 2299 CD1 LEU A 407 20562 27863 14285 336 -1393 -1310 C ATOM 2300 CD2 LEU A 407 -78.579 -27.099 208.127 1.00156.89 C ANISOU 2300 CD2 LEU A 407 19277 26656 13680 1402 -1918 -1404 C ATOM 2301 N TYR A 408 -83.736 -25.523 207.771 1.00138.97 N ANISOU 2301 N TYR A 408 18845 21557 12400 1285 -1932 -16 N ATOM 2302 CA TYR A 408 -84.908 -24.882 208.357 1.00127.51 C ANISOU 2302 CA TYR A 408 17767 19470 11212 1212 -1936 224 C ATOM 2303 C TYR A 408 -85.689 -25.858 209.226 1.00116.28 C ANISOU 2303 C TYR A 408 16332 17754 10097 1669 -2128 310 C ATOM 2304 O TYR A 408 -86.034 -25.548 210.371 1.00119.30 O ANISOU 2304 O TYR A 408 16772 17959 10598 1614 -2110 369 O ATOM 2305 CB TYR A 408 -85.799 -24.311 207.254 1.00127.18 C ANISOU 2305 CB TYR A 408 18132 18950 11239 1089 -1930 392 C ATOM 2306 CG TYR A 408 -85.677 -22.815 207.081 1.00133.60 C ANISOU 2306 CG TYR A 408 19231 19655 11875 521 -1770 438 C ATOM 2307 CD1 TYR A 408 -86.355 -21.942 207.921 1.00134.38 C ANISOU 2307 CD1 TYR A 408 19583 19340 12136 364 -1772 541 C ATOM 2308 CD2 TYR A 408 -84.883 -22.275 206.077 1.00142.46 C ANISOU 2308 CD2 TYR A 408 20387 21093 12648 125 -1633 368 C ATOM 2309 CE1 TYR A 408 -86.246 -20.573 207.767 1.00140.76 C ANISOU 2309 CE1 TYR A 408 20695 20008 12777 -141 -1685 578 C ATOM 2310 CE2 TYR A 408 -84.768 -20.908 205.915 1.00148.32 C ANISOU 2310 CE2 TYR A 408 21456 21699 13200 -435 -1520 429 C ATOM 2311 CZ TYR A 408 -85.451 -20.062 206.763 1.00146.94 C ANISOU 2311 CZ TYR A 408 21556 21067 13206 -551 -1568 538 C ATOM 2312 OH TYR A 408 -85.340 -18.699 206.605 1.00148.62 O ANISOU 2312 OH TYR A 408 22136 21107 13227 -1094 -1512 593 O ATOM 2313 N SER A 409 -85.958 -27.058 208.704 1.00106.22 N ANISOU 2313 N SER A 409 14989 16438 8934 2105 -2319 313 N ATOM 2314 CA SER A 409 -86.706 -28.041 209.483 1.00 99.80 C ANISOU 2314 CA SER A 409 14206 15334 8382 2494 -2517 409 C ATOM 2315 C SER A 409 -85.905 -28.527 210.687 1.00105.20 C ANISOU 2315 C SER A 409 14639 16369 8964 2588 -2588 277 C ATOM 2316 O SER A 409 -86.455 -28.675 211.788 1.00107.47 O ANISOU 2316 O SER A 409 15026 16411 9398 2641 -2633 378 O ATOM 2317 CB SER A 409 -87.107 -29.219 208.595 1.00 96.57 C ANISOU 2317 CB SER A 409 13798 14801 8094 2927 -2738 437 C ATOM 2318 OG SER A 409 -85.967 -29.934 208.150 1.00102.22 O ANISOU 2318 OG SER A 409 14196 16060 8585 3112 -2840 211 O ATOM 2319 N ALA A 410 -84.603 -28.768 210.502 1.00108.08 N ANISOU 2319 N ALA A 410 14680 17322 9065 2603 -2603 25 N ATOM 2320 CA ALA A 410 -83.773 -29.243 211.602 1.00108.73 C ANISOU 2320 CA ALA A 410 14528 17745 9040 2731 -2717 -149 C ATOM 2321 C ALA A 410 -83.734 -28.234 212.740 1.00110.45 C ANISOU 2321 C ALA A 410 14808 17918 9239 2378 -2531 -104 C ATOM 2322 O ALA A 410 -83.836 -28.607 213.912 1.00114.81 O ANISOU 2322 O ALA A 410 15386 18385 9853 2505 -2639 -78 O ATOM 2323 CB ALA A 410 -82.361 -29.545 211.102 1.00111.17 C ANISOU 2323 CB ALA A 410 14436 18739 9063 2790 -2757 -500 C ATOM 2324 N PHE A 411 -83.620 -26.945 212.417 1.00108.77 N ANISOU 2324 N PHE A 411 14660 17734 8935 1925 -2270 -85 N ATOM 2325 CA PHE A 411 -83.558 -25.938 213.468 1.00108.15 C ANISOU 2325 CA PHE A 411 14642 17614 8837 1595 -2116 -58 C ATOM 2326 C PHE A 411 -84.933 -25.637 214.051 1.00103.69 C ANISOU 2326 C PHE A 411 14409 16444 8545 1592 -2111 192 C ATOM 2327 O PHE A 411 -85.037 -25.320 215.243 1.00105.03 O ANISOU 2327 O PHE A 411 14604 16551 8750 1510 -2080 211 O ATOM 2328 CB PHE A 411 -82.896 -24.672 212.929 1.00111.96 C ANISOU 2328 CB PHE A 411 15099 18343 9099 1090 -1877 -140 C ATOM 2329 CG PHE A 411 -81.433 -24.847 212.637 1.00114.72 C ANISOU 2329 CG PHE A 411 15048 19393 9148 1014 -1836 -450 C ATOM 2330 CD1 PHE A 411 -80.665 -25.707 213.405 1.00116.27 C ANISOU 2330 CD1 PHE A 411 14932 19958 9287 1319 -1996 -673 C ATOM 2331 CD2 PHE A 411 -80.829 -24.169 211.593 1.00116.30 C ANISOU 2331 CD2 PHE A 411 15191 19890 9106 632 -1653 -547 C ATOM 2332 CE1 PHE A 411 -79.320 -25.881 213.144 1.00121.94 C ANISOU 2332 CE1 PHE A 411 15238 21357 9739 1282 -1980 -1029 C ATOM 2333 CE2 PHE A 411 -79.482 -24.341 211.326 1.00121.01 C ANISOU 2333 CE2 PHE A 411 15367 21199 9414 540 -1595 -885 C ATOM 2334 CZ PHE A 411 -78.728 -25.197 212.103 1.00124.34 C ANISOU 2334 CZ PHE A 411 15429 22009 9807 884 -1761 -1148 C ATOM 2335 N THR A 412 -85.994 -25.765 213.250 1.00103.08 N ANISOU 2335 N THR A 412 14566 15941 8660 1697 -2151 353 N ATOM 2336 CA THR A 412 -87.347 -25.718 213.792 1.00106.32 C ANISOU 2336 CA THR A 412 15228 15821 9346 1769 -2180 529 C ATOM 2337 C THR A 412 -87.532 -26.773 214.874 1.00112.39 C ANISOU 2337 C THR A 412 15934 16577 10193 2050 -2324 555 C ATOM 2338 O THR A 412 -88.032 -26.483 215.968 1.00116.27 O ANISOU 2338 O THR A 412 16509 16905 10764 1959 -2276 608 O ATOM 2339 CB THR A 412 -88.368 -25.919 212.670 1.00100.99 C ANISOU 2339 CB THR A 412 14766 14741 8866 1914 -2245 647 C ATOM 2340 OG1 THR A 412 -88.286 -24.832 211.741 1.00 99.23 O ANISOU 2340 OG1 THR A 412 14695 14455 8553 1612 -2131 642 O ATOM 2341 CG2 THR A 412 -89.776 -25.998 213.234 1.00 96.73 C ANISOU 2341 CG2 THR A 412 14426 13708 8620 2015 -2284 771 C ATOM 2342 N TRP A 413 -87.111 -28.007 214.593 1.00113.89 N ANISOU 2342 N TRP A 413 15994 16944 10336 2385 -2522 505 N ATOM 2343 CA TRP A 413 -87.287 -29.059 215.586 1.00114.45 C ANISOU 2343 CA TRP A 413 16084 16953 10449 2637 -2712 546 C ATOM 2344 C TRP A 413 -86.290 -28.931 216.733 1.00119.68 C ANISOU 2344 C TRP A 413 16595 17969 10911 2557 -2714 406 C ATOM 2345 O TRP A 413 -86.605 -29.318 217.863 1.00124.42 O ANISOU 2345 O TRP A 413 17300 18441 11534 2605 -2789 474 O ATOM 2346 CB TRP A 413 -87.204 -30.429 214.914 1.00118.01 C ANISOU 2346 CB TRP A 413 16500 17420 10919 3044 -2990 534 C ATOM 2347 CG TRP A 413 -88.373 -30.643 214.006 1.00122.57 C ANISOU 2347 CG TRP A 413 17263 17573 11734 3145 -3008 696 C ATOM 2348 CD1 TRP A 413 -88.349 -30.751 212.646 1.00130.95 C ANISOU 2348 CD1 TRP A 413 18294 18643 12817 3261 -3039 671 C ATOM 2349 CD2 TRP A 413 -89.752 -30.707 214.388 1.00119.52 C ANISOU 2349 CD2 TRP A 413 17110 16709 11595 3121 -2983 879 C ATOM 2350 NE1 TRP A 413 -89.624 -30.907 212.160 1.00129.65 N ANISOU 2350 NE1 TRP A 413 18345 18003 12913 3342 -3060 834 N ATOM 2351 CE2 TRP A 413 -90.504 -30.879 213.210 1.00123.74 C ANISOU 2351 CE2 TRP A 413 17741 16963 12310 3254 -3022 949 C ATOM 2352 CE3 TRP A 413 -90.423 -30.648 215.613 1.00118.08 C ANISOU 2352 CE3 TRP A 413 17046 16334 11483 2993 -2928 967 C ATOM 2353 CZ2 TRP A 413 -91.893 -30.997 213.222 1.00121.07 C ANISOU 2353 CZ2 TRP A 413 17595 16166 12241 3275 -3017 1081 C ATOM 2354 CZ3 TRP A 413 -91.799 -30.764 215.622 1.00120.11 C ANISOU 2354 CZ3 TRP A 413 17480 16170 11987 2985 -2901 1093 C ATOM 2355 CH2 TRP A 413 -92.519 -30.938 214.435 1.00120.98 C ANISOU 2355 CH2 TRP A 413 17662 16012 12293 3131 -2949 1139 C ATOM 2356 N LEU A 414 -85.102 -28.378 216.478 1.00120.05 N ANISOU 2356 N LEU A 414 16402 18464 10747 2412 -2628 202 N ATOM 2357 CA LEU A 414 -84.175 -28.095 217.569 1.00120.97 C ANISOU 2357 CA LEU A 414 16366 18908 10690 2310 -2612 45 C ATOM 2358 C LEU A 414 -84.768 -27.077 218.536 1.00125.28 C ANISOU 2358 C LEU A 414 17072 19220 11310 2002 -2416 165 C ATOM 2359 O LEU A 414 -84.568 -27.172 219.752 1.00125.48 O ANISOU 2359 O LEU A 414 17102 19296 11277 2009 -2460 138 O ATOM 2360 CB LEU A 414 -82.838 -27.599 217.016 1.00115.67 C ANISOU 2360 CB LEU A 414 15380 18782 9785 2158 -2523 -223 C ATOM 2361 CG LEU A 414 -81.794 -27.198 218.063 1.00114.17 C ANISOU 2361 CG LEU A 414 14992 18971 9416 2032 -2495 -430 C ATOM 2362 CD1 LEU A 414 -81.343 -28.407 218.868 1.00112.64 C ANISOU 2362 CD1 LEU A 414 14737 18897 9163 2435 -2816 -558 C ATOM 2363 CD2 LEU A 414 -80.606 -26.509 217.412 1.00117.54 C ANISOU 2363 CD2 LEU A 414 15107 19931 9621 1772 -2339 -694 C ATOM 2364 N GLY A 415 -85.509 -26.098 218.010 1.00127.07 N ANISOU 2364 N GLY A 415 17445 19179 11657 1746 -2228 278 N ATOM 2365 CA GLY A 415 -86.195 -25.153 218.872 1.00124.92 C ANISOU 2365 CA GLY A 415 17328 18657 11478 1500 -2084 362 C ATOM 2366 C GLY A 415 -87.422 -25.736 219.544 1.00118.75 C ANISOU 2366 C GLY A 415 16736 17495 10889 1650 -2147 515 C ATOM 2367 O GLY A 415 -87.770 -25.337 220.659 1.00122.60 O ANISOU 2367 O GLY A 415 17285 17905 11393 1526 -2077 532 O ATOM 2368 N TYR A 416 -88.096 -26.679 218.881 1.00115.72 N ANISOU 2368 N TYR A 416 16439 16889 10640 1898 -2274 616 N ATOM 2369 CA TYR A 416 -89.249 -27.328 219.501 1.00115.04 C ANISOU 2369 CA TYR A 416 16522 16474 10714 2002 -2330 751 C ATOM 2370 C TYR A 416 -88.834 -28.298 220.602 1.00128.46 C ANISOU 2370 C TYR A 416 18227 18309 12274 2140 -2485 757 C ATOM 2371 O TYR A 416 -89.628 -28.576 221.509 1.00131.93 O ANISOU 2371 O TYR A 416 18812 18552 12764 2093 -2474 852 O ATOM 2372 CB TYR A 416 -90.084 -28.053 218.446 1.00107.00 C ANISOU 2372 CB TYR A 416 15603 15168 9883 2213 -2433 852 C ATOM 2373 CG TYR A 416 -91.079 -27.163 217.741 1.00103.23 C ANISOU 2373 CG TYR A 416 15237 14372 9612 2082 -2303 876 C ATOM 2374 CD1 TYR A 416 -91.759 -26.169 218.433 1.00100.81 C ANISOU 2374 CD1 TYR A 416 15001 13911 9392 1852 -2152 847 C ATOM 2375 CD2 TYR A 416 -91.347 -27.320 216.388 1.00 99.30 C ANISOU 2375 CD2 TYR A 416 14786 13722 9220 2214 -2363 903 C ATOM 2376 CE1 TYR A 416 -92.673 -25.353 217.798 1.00 95.73 C ANISOU 2376 CE1 TYR A 416 14478 12956 8938 1773 -2096 823 C ATOM 2377 CE2 TYR A 416 -92.262 -26.508 215.743 1.00 93.06 C ANISOU 2377 CE2 TYR A 416 14139 12605 8614 2120 -2292 905 C ATOM 2378 CZ TYR A 416 -92.921 -25.527 216.454 1.00 90.73 C ANISOU 2378 CZ TYR A 416 13920 12147 8406 1908 -2174 855 C ATOM 2379 OH TYR A 416 -93.832 -24.715 215.819 1.00 92.96 O ANISOU 2379 OH TYR A 416 14363 12086 8872 1854 -2163 811 O ATOM 2380 N VAL A 417 -87.614 -28.836 220.529 1.00135.61 N ANISOU 2380 N VAL A 417 18988 19551 12989 2307 -2648 637 N ATOM 2381 CA VAL A 417 -87.124 -29.744 221.565 1.00141.90 C ANISOU 2381 CA VAL A 417 19833 20456 13628 2466 -2862 613 C ATOM 2382 C VAL A 417 -87.160 -29.077 222.935 1.00143.12 C ANISOU 2382 C VAL A 417 20039 20637 13704 2227 -2722 611 C ATOM 2383 O VAL A 417 -87.419 -29.736 223.950 1.00145.37 O ANISOU 2383 O VAL A 417 20502 20817 13915 2266 -2839 688 O ATOM 2384 CB VAL A 417 -85.707 -30.241 221.206 1.00148.87 C ANISOU 2384 CB VAL A 417 20500 21745 14318 2698 -3073 394 C ATOM 2385 CG1 VAL A 417 -84.978 -30.765 222.435 1.00153.20 C ANISOU 2385 CG1 VAL A 417 21084 22456 14670 2808 -3279 296 C ATOM 2386 CG2 VAL A 417 -85.782 -31.327 220.146 1.00150.87 C ANISOU 2386 CG2 VAL A 417 20762 21934 14628 3027 -3316 406 C ATOM 2387 N ASN A 418 -86.928 -27.761 222.986 1.00138.49 N ANISOU 2387 N ASN A 418 19327 20174 13117 1962 -2484 528 N ATOM 2388 CA ASN A 418 -86.956 -27.032 224.250 1.00137.14 C ANISOU 2388 CA ASN A 418 19188 20038 12880 1744 -2352 506 C ATOM 2389 C ASN A 418 -88.282 -27.178 224.988 1.00129.33 C ANISOU 2389 C ASN A 418 18412 18724 12001 1653 -2279 658 C ATOM 2390 O ASN A 418 -88.312 -27.044 226.217 1.00130.31 O ANISOU 2390 O ASN A 418 18604 18886 12021 1543 -2242 654 O ATOM 2391 CB ASN A 418 -86.660 -25.551 223.995 1.00140.66 C ANISOU 2391 CB ASN A 418 19503 20598 13343 1466 -2131 407 C ATOM 2392 CG ASN A 418 -86.811 -24.701 225.240 1.00142.11 C ANISOU 2392 CG ASN A 418 19721 20786 13490 1249 -1999 378 C ATOM 2393 OD1 ASN A 418 -85.957 -24.720 226.126 1.00145.33 O ANISOU 2393 OD1 ASN A 418 20056 21437 13724 1252 -2049 280 O ATOM 2394 ND2 ASN A 418 -87.901 -23.945 225.313 1.00137.57 N ANISOU 2394 ND2 ASN A 418 19248 19944 13077 1081 -1850 434 N ATOM 2395 N SER A 419 -89.374 -27.464 224.277 1.00119.57 N ANISOU 2395 N SER A 419 17274 17194 10964 1690 -2257 771 N ATOM 2396 CA SER A 419 -90.669 -27.637 224.924 1.00114.89 C ANISOU 2396 CA SER A 419 16840 16339 10473 1581 -2173 872 C ATOM 2397 C SER A 419 -90.747 -28.893 225.785 1.00121.12 C ANISOU 2397 C SER A 419 17817 17089 11115 1661 -2344 981 C ATOM 2398 O SER A 419 -91.761 -29.091 226.463 1.00122.54 O ANISOU 2398 O SER A 419 18132 17104 11322 1510 -2257 1058 O ATOM 2399 CB SER A 419 -91.779 -27.663 223.872 1.00107.26 C ANISOU 2399 CB SER A 419 15909 15079 9766 1619 -2129 927 C ATOM 2400 OG SER A 419 -91.778 -26.474 223.102 1.00106.20 O ANISOU 2400 OG SER A 419 15680 14923 9748 1527 -2006 832 O ATOM 2401 N ALA A 420 -89.713 -29.738 225.784 1.00122.97 N ANISOU 2401 N ALA A 420 18075 17474 11176 1880 -2602 969 N ATOM 2402 CA ALA A 420 -89.705 -30.957 226.579 1.00128.14 C ANISOU 2402 CA ALA A 420 18984 18048 11657 1968 -2842 1073 C ATOM 2403 C ALA A 420 -88.643 -30.985 227.668 1.00133.81 C ANISOU 2403 C ALA A 420 19738 18997 12108 1988 -2968 978 C ATOM 2404 O ALA A 420 -88.712 -31.852 228.547 1.00139.36 O ANISOU 2404 O ALA A 420 20722 19599 12630 1999 -3157 1069 O ATOM 2405 CB ALA A 420 -89.511 -32.185 225.676 1.00128.92 C ANISOU 2405 CB ALA A 420 19164 18046 11775 2284 -3159 1128 C ATOM 2406 N VAL A 421 -87.669 -30.072 227.641 1.00134.17 N ANISOU 2406 N VAL A 421 19532 19334 12111 1979 -2882 793 N ATOM 2407 CA VAL A 421 -86.553 -30.120 228.583 1.00132.86 C ANISOU 2407 CA VAL A 421 19366 19408 11705 2046 -3034 657 C ATOM 2408 C VAL A 421 -86.817 -29.366 229.878 1.00129.08 C ANISOU 2408 C VAL A 421 18955 18950 11138 1775 -2834 665 C ATOM 2409 O VAL A 421 -86.046 -29.522 230.838 1.00129.70 O ANISOU 2409 O VAL A 421 19108 19168 11002 1825 -2980 580 O ATOM 2410 CB VAL A 421 -85.271 -29.561 227.936 1.00129.50 C ANISOU 2410 CB VAL A 421 18605 19341 11256 2159 -3052 414 C ATOM 2411 CG1 VAL A 421 -84.837 -30.440 226.773 1.00127.76 C ANISOU 2411 CG1 VAL A 421 18305 19174 11064 2468 -3298 354 C ATOM 2412 CG2 VAL A 421 -85.505 -28.137 227.472 1.00127.80 C ANISOU 2412 CG2 VAL A 421 18175 19188 11193 1890 -2702 379 C ATOM 2413 N ASN A 422 -87.872 -28.559 229.944 1.00123.47 N ANISOU 2413 N ASN A 422 18220 18110 10582 1513 -2530 734 N ATOM 2414 CA ASN A 422 -88.145 -27.772 231.142 1.00121.38 C ANISOU 2414 CA ASN A 422 17984 17897 10239 1267 -2336 704 C ATOM 2415 C ASN A 422 -88.578 -28.639 232.325 1.00121.62 C ANISOU 2415 C ASN A 422 18339 17811 10058 1193 -2432 830 C ATOM 2416 O ASN A 422 -88.116 -28.398 233.449 1.00128.24 O ANISOU 2416 O ASN A 422 19247 18777 10699 1120 -2442 771 O ATOM 2417 CB ASN A 422 -89.200 -26.701 230.849 1.00120.81 C ANISOU 2417 CB ASN A 422 17791 17721 10392 1044 -2032 693 C ATOM 2418 CG ASN A 422 -88.656 -25.565 230.007 1.00118.62 C ANISOU 2418 CG ASN A 422 17260 17564 10246 1029 -1934 558 C ATOM 2419 OD1 ASN A 422 -87.461 -25.272 230.039 1.00118.68 O ANISOU 2419 OD1 ASN A 422 17139 17812 10143 1085 -2006 442 O ATOM 2420 ND2 ASN A 422 -89.532 -24.918 229.248 1.00115.96 N ANISOU 2420 ND2 ASN A 422 16867 17057 10135 938 -1786 559 N ATOM 2421 N PRO A 423 -89.452 -29.640 232.142 1.00118.21 N ANISOU 2421 N PRO A 423 18136 17137 9640 1181 -2509 1003 N ATOM 2422 CA PRO A 423 -89.712 -30.563 233.260 1.00119.32 C ANISOU 2422 CA PRO A 423 18653 17168 9514 1077 -2647 1136 C ATOM 2423 C PRO A 423 -88.471 -31.288 233.748 1.00127.67 C ANISOU 2423 C PRO A 423 19899 18297 10311 1315 -3024 1096 C ATOM 2424 O PRO A 423 -88.342 -31.530 234.955 1.00130.35 O ANISOU 2424 O PRO A 423 20507 18634 10386 1203 -3102 1129 O ATOM 2425 CB PRO A 423 -90.742 -31.538 232.675 1.00114.40 C ANISOU 2425 CB PRO A 423 18217 16269 8980 1045 -2702 1319 C ATOM 2426 CG PRO A 423 -91.443 -30.750 231.639 1.00113.49 C ANISOU 2426 CG PRO A 423 17793 16130 9197 1013 -2443 1260 C ATOM 2427 CD PRO A 423 -90.381 -29.887 231.022 1.00114.44 C ANISOU 2427 CD PRO A 423 17613 16458 9410 1199 -2444 1090 C ATOM 2428 N ILE A 424 -87.542 -31.628 232.852 1.00133.37 N ANISOU 2428 N ILE A 424 20487 19097 11091 1648 -3276 993 N ATOM 2429 CA ILE A 424 -86.305 -32.275 233.280 1.00138.06 C ANISOU 2429 CA ILE A 424 21214 19792 11452 1927 -3674 873 C ATOM 2430 C ILE A 424 -85.476 -31.332 234.145 1.00138.64 C ANISOU 2430 C ILE A 424 21128 20135 11415 1874 -3576 683 C ATOM 2431 O ILE A 424 -84.894 -31.746 235.156 1.00139.26 O ANISOU 2431 O ILE A 424 21456 20224 11234 1946 -3820 638 O ATOM 2432 CB ILE A 424 -85.512 -32.767 232.055 1.00139.85 C ANISOU 2432 CB ILE A 424 21247 20112 11779 2301 -3941 736 C ATOM 2433 CG1 ILE A 424 -86.367 -33.716 231.214 1.00140.81 C ANISOU 2433 CG1 ILE A 424 21542 19942 12016 2367 -4058 930 C ATOM 2434 CG2 ILE A 424 -84.225 -33.450 232.490 1.00140.14 C ANISOU 2434 CG2 ILE A 424 21389 20275 11581 2634 -4398 538 C ATOM 2435 CD1 ILE A 424 -85.673 -34.222 229.969 1.00137.30 C ANISOU 2435 CD1 ILE A 424 20902 19595 11670 2743 -4317 790 C ATOM 2436 N ILE A 425 -85.409 -30.053 233.767 1.00137.40 N ANISOU 2436 N ILE A 425 20585 20177 11443 1748 -3244 568 N ATOM 2437 CA ILE A 425 -84.678 -29.084 234.578 1.00138.45 C ANISOU 2437 CA ILE A 425 20560 20555 11489 1670 -3137 392 C ATOM 2438 C ILE A 425 -85.351 -28.906 235.933 1.00137.97 C ANISOU 2438 C ILE A 425 20759 20394 11269 1411 -3004 503 C ATOM 2439 O ILE A 425 -84.678 -28.810 236.966 1.00138.44 O ANISOU 2439 O ILE A 425 20918 20563 11121 1437 -3117 406 O ATOM 2440 CB ILE A 425 -84.543 -27.746 233.831 1.00135.21 C ANISOU 2440 CB ILE A 425 19737 20334 11304 1549 -2832 268 C ATOM 2441 CG1 ILE A 425 -83.794 -27.945 232.513 1.00134.23 C ANISOU 2441 CG1 ILE A 425 19362 20358 11280 1770 -2955 143 C ATOM 2442 CG2 ILE A 425 -83.805 -26.738 234.694 1.00136.34 C ANISOU 2442 CG2 ILE A 425 19730 20714 11358 1452 -2738 92 C ATOM 2443 CD1 ILE A 425 -82.386 -28.468 232.683 1.00135.76 C ANISOU 2443 CD1 ILE A 425 19478 20806 11296 2060 -3284 -95 C ATOM 2444 N TYR A 426 -86.687 -28.855 235.954 1.00133.85 N ANISOU 2444 N TYR A 426 20337 19685 10834 1156 -2763 680 N ATOM 2445 CA TYR A 426 -87.396 -28.743 237.225 1.00126.57 C ANISOU 2445 CA TYR A 426 19646 18712 9733 877 -2615 763 C ATOM 2446 C TYR A 426 -87.147 -29.960 238.106 1.00122.31 C ANISOU 2446 C TYR A 426 19579 18036 8858 925 -2942 876 C ATOM 2447 O TYR A 426 -87.075 -29.836 239.334 1.00125.24 O ANISOU 2447 O TYR A 426 20151 18450 8985 782 -2929 872 O ATOM 2448 CB TYR A 426 -88.896 -28.558 236.988 1.00123.42 C ANISOU 2448 CB TYR A 426 19227 18176 9490 602 -2310 880 C ATOM 2449 CG TYR A 426 -89.253 -27.383 236.101 1.00120.13 C ANISOU 2449 CG TYR A 426 18418 17827 9400 566 -2043 763 C ATOM 2450 CD1 TYR A 426 -88.446 -26.254 236.046 1.00117.94 C ANISOU 2450 CD1 TYR A 426 17864 17750 9196 616 -1976 582 C ATOM 2451 CD2 TYR A 426 -90.403 -27.404 235.321 1.00122.06 C ANISOU 2451 CD2 TYR A 426 18597 17914 9868 472 -1884 827 C ATOM 2452 CE1 TYR A 426 -88.772 -25.180 235.237 1.00116.43 C ANISOU 2452 CE1 TYR A 426 17394 17574 9272 560 -1780 489 C ATOM 2453 CE2 TYR A 426 -90.736 -26.337 234.509 1.00118.59 C ANISOU 2453 CE2 TYR A 426 17860 17489 9709 455 -1695 710 C ATOM 2454 CZ TYR A 426 -89.918 -25.228 234.471 1.00114.28 C ANISOU 2454 CZ TYR A 426 17095 17116 9210 492 -1654 552 C ATOM 2455 OH TYR A 426 -90.249 -24.164 233.664 1.00108.40 O ANISOU 2455 OH TYR A 426 16131 16342 8715 452 -1510 449 O ATOM 2456 N THR A 427 -87.019 -31.141 237.498 1.00120.83 N ANISOU 2456 N THR A 427 19604 17666 8639 1127 -3263 975 N ATOM 2457 CA THR A 427 -86.745 -32.352 238.264 1.00122.59 C ANISOU 2457 CA THR A 427 20349 17702 8529 1194 -3659 1082 C ATOM 2458 C THR A 427 -85.327 -32.341 238.824 1.00129.40 C ANISOU 2458 C THR A 427 21238 18716 9212 1484 -3981 868 C ATOM 2459 O THR A 427 -85.105 -32.719 239.981 1.00135.00 O ANISOU 2459 O THR A 427 22340 19347 9606 1430 -4172 900 O ATOM 2460 CB THR A 427 -86.955 -33.586 237.385 1.00122.20 C ANISOU 2460 CB THR A 427 20515 17400 8515 1371 -3968 1217 C ATOM 2461 OG1 THR A 427 -88.318 -33.642 236.949 1.00110.34 O ANISOU 2461 OG1 THR A 427 19008 15748 7168 1084 -3677 1406 O ATOM 2462 CG2 THR A 427 -86.626 -34.858 238.155 1.00115.25 C ANISOU 2462 CG2 THR A 427 20241 16278 7271 1455 -4458 1322 C ATOM 2463 N THR A 428 -84.358 -31.900 238.020 1.00130.71 N ANISOU 2463 N THR A 428 20990 19112 9562 1778 -4044 630 N ATOM 2464 CA THR A 428 -82.956 -32.012 238.406 1.00140.25 C ANISOU 2464 CA THR A 428 22177 20493 10620 2100 -4396 366 C ATOM 2465 C THR A 428 -82.507 -30.896 239.345 1.00152.94 C ANISOU 2465 C THR A 428 23611 22332 12169 1972 -4184 214 C ATOM 2466 O THR A 428 -81.688 -31.141 240.238 1.00158.07 O ANISOU 2466 O THR A 428 24460 23015 12582 2132 -4478 76 O ATOM 2467 CB THR A 428 -82.074 -32.026 237.154 1.00135.30 C ANISOU 2467 CB THR A 428 21141 20078 10187 2438 -4539 130 C ATOM 2468 OG1 THR A 428 -82.527 -33.053 236.263 1.00134.71 O ANISOU 2468 OG1 THR A 428 21222 19784 10176 2575 -4743 268 O ATOM 2469 CG2 THR A 428 -80.620 -32.292 237.519 1.00135.37 C ANISOU 2469 CG2 THR A 428 21112 20289 10034 2806 -4955 -203 C ATOM 2470 N PHE A 429 -83.033 -29.682 239.185 1.00159.07 N ANISOU 2470 N PHE A 429 24046 23244 13148 1704 -3716 225 N ATOM 2471 CA PHE A 429 -82.536 -28.523 239.916 1.00159.32 C ANISOU 2471 CA PHE A 429 23856 23512 13168 1609 -3528 53 C ATOM 2472 C PHE A 429 -83.469 -28.057 241.029 1.00152.66 C ANISOU 2472 C PHE A 429 23208 22589 12206 1266 -3256 197 C ATOM 2473 O PHE A 429 -83.198 -27.026 241.654 1.00153.35 O ANISOU 2473 O PHE A 429 23111 22856 12297 1170 -3079 65 O ATOM 2474 CB PHE A 429 -82.267 -27.367 238.950 1.00167.15 C ANISOU 2474 CB PHE A 429 24315 24740 14454 1570 -3253 -97 C ATOM 2475 CG PHE A 429 -80.957 -27.477 238.222 1.00174.69 C ANISOU 2475 CG PHE A 429 24986 25937 15451 1871 -3485 -362 C ATOM 2476 CD1 PHE A 429 -80.002 -28.398 238.619 1.00181.58 C ANISOU 2476 CD1 PHE A 429 26030 26844 16116 2196 -3927 -522 C ATOM 2477 CD2 PHE A 429 -80.680 -26.656 237.141 1.00175.25 C ANISOU 2477 CD2 PHE A 429 24627 26212 15750 1819 -3277 -477 C ATOM 2478 CE1 PHE A 429 -78.796 -28.499 237.952 1.00185.00 C ANISOU 2478 CE1 PHE A 429 26147 27560 16586 2482 -4141 -834 C ATOM 2479 CE2 PHE A 429 -79.476 -26.752 236.470 1.00179.20 C ANISOU 2479 CE2 PHE A 429 24831 26996 16260 2048 -3458 -752 C ATOM 2480 CZ PHE A 429 -78.533 -27.675 236.875 1.00183.99 C ANISOU 2480 CZ PHE A 429 25548 27685 16675 2390 -3882 -951 C ATOM 2481 N ASN A 430 -84.554 -28.779 241.298 1.00143.59 N ANISOU 2481 N ASN A 430 22416 21199 10943 1066 -3218 444 N ATOM 2482 CA ASN A 430 -85.459 -28.419 242.379 1.00140.10 C ANISOU 2482 CA ASN A 430 22151 20732 10347 716 -2953 548 C ATOM 2483 C ASN A 430 -85.783 -29.650 243.214 1.00143.59 C ANISOU 2483 C ASN A 430 23196 20939 10424 614 -3195 746 C ATOM 2484 O ASN A 430 -85.816 -30.775 242.707 1.00143.52 O ANISOU 2484 O ASN A 430 23457 20713 10362 733 -3480 875 O ATOM 2485 CB ASN A 430 -86.754 -27.788 241.847 1.00136.93 C ANISOU 2485 CB ASN A 430 21509 20328 10192 436 -2533 623 C ATOM 2486 CG ASN A 430 -87.588 -27.155 242.945 1.00134.52 C ANISOU 2486 CG ASN A 430 21249 20106 9758 98 -2227 624 C ATOM 2487 OD1 ASN A 430 -88.382 -27.827 243.604 1.00135.69 O ANISOU 2487 OD1 ASN A 430 21740 20147 9670 -153 -2186 779 O ATOM 2488 ND2 ASN A 430 -87.408 -25.855 243.150 1.00130.92 N ANISOU 2488 ND2 ASN A 430 20450 19855 9440 73 -2019 436 N ATOM 2489 N ILE A 431 -86.026 -29.419 244.501 1.00145.10 N ANISOU 2489 N ILE A 431 23619 21167 10346 380 -3093 769 N ATOM 2490 CA ILE A 431 -86.306 -30.499 245.445 1.00142.55 C ANISOU 2490 CA ILE A 431 23933 20624 9606 212 -3313 962 C ATOM 2491 C ILE A 431 -87.801 -30.758 245.569 1.00145.26 C ANISOU 2491 C ILE A 431 24429 20884 9881 -247 -2993 1175 C ATOM 2492 O ILE A 431 -88.264 -31.889 245.392 1.00145.59 O ANISOU 2492 O ILE A 431 24874 20672 9772 -356 -3173 1389 O ATOM 2493 CB ILE A 431 -85.676 -30.172 246.817 1.00137.95 C ANISOU 2493 CB ILE A 431 23565 20133 8715 202 -3406 860 C ATOM 2494 CG1 ILE A 431 -84.169 -29.944 246.675 1.00132.96 C ANISOU 2494 CG1 ILE A 431 22751 19605 8161 666 -3739 602 C ATOM 2495 CG2 ILE A 431 -85.962 -31.284 247.814 1.00142.11 C ANISOU 2495 CG2 ILE A 431 24826 20407 8763 -10 -3653 1073 C ATOM 2496 CD1 ILE A 431 -83.449 -31.037 245.912 1.00130.82 C ANISOU 2496 CD1 ILE A 431 22654 19153 7897 1037 -4230 587 C ATOM 2497 N GLU A 432 -88.574 -29.716 245.887 1.00149.02 N ANISOU 2497 N GLU A 432 24580 21582 10458 -524 -2532 1094 N ATOM 2498 CA GLU A 432 -90.014 -29.885 246.054 1.00160.27 C ANISOU 2498 CA GLU A 432 26078 23002 11817 -973 -2200 1221 C ATOM 2499 C GLU A 432 -90.686 -30.310 244.756 1.00162.62 C ANISOU 2499 C GLU A 432 26217 23158 12411 -954 -2153 1313 C ATOM 2500 O GLU A 432 -91.675 -31.051 244.785 1.00165.08 O ANISOU 2500 O GLU A 432 26777 23349 12596 -1273 -2068 1483 O ATOM 2501 CB GLU A 432 -90.644 -28.595 246.582 1.00162.84 C ANISOU 2501 CB GLU A 432 26011 23631 12230 -1196 -1753 1030 C ATOM 2502 CG GLU A 432 -90.209 -28.204 247.986 1.00169.04 C ANISOU 2502 CG GLU A 432 26978 24566 12683 -1288 -1750 951 C ATOM 2503 CD GLU A 432 -88.883 -27.471 248.007 1.00171.67 C ANISOU 2503 CD GLU A 432 27094 24988 13147 -890 -1941 767 C ATOM 2504 OE1 GLU A 432 -88.408 -27.065 246.925 1.00169.02 O ANISOU 2504 OE1 GLU A 432 26388 24656 13175 -601 -1991 673 O ATOM 2505 OE2 GLU A 432 -88.315 -27.300 249.106 1.00175.59 O ANISOU 2505 OE2 GLU A 432 27792 25557 13368 -884 -2036 708 O ATOM 2506 N PHE A 433 -90.160 -29.871 243.610 1.00159.78 N ANISOU 2506 N PHE A 433 25463 22817 12431 -603 -2210 1201 N ATOM 2507 CA PHE A 433 -90.719 -30.309 242.335 1.00158.72 C ANISOU 2507 CA PHE A 433 25202 22531 12573 -543 -2203 1287 C ATOM 2508 C PHE A 433 -90.523 -31.807 242.138 1.00161.16 C ANISOU 2508 C PHE A 433 26004 22544 12685 -462 -2606 1506 C ATOM 2509 O PHE A 433 -91.453 -32.514 241.730 1.00165.04 O ANISOU 2509 O PHE A 433 26644 22867 13195 -657 -2562 1668 O ATOM 2510 CB PHE A 433 -90.086 -29.525 241.186 1.00157.08 C ANISOU 2510 CB PHE A 433 24515 22412 12758 -198 -2202 1121 C ATOM 2511 N ARG A 434 -89.323 -32.311 242.436 1.00161.92 N ANISOU 2511 N ARG A 434 26366 22567 12591 -167 -3031 1491 N ATOM 2512 CA ARG A 434 -89.066 -33.742 242.308 1.00163.44 C ANISOU 2512 CA ARG A 434 27078 22450 12573 -46 -3502 1669 C ATOM 2513 C ARG A 434 -89.897 -34.541 243.304 1.00165.18 C ANISOU 2513 C ARG A 434 27886 22487 12387 -501 -3505 1906 C ATOM 2514 O ARG A 434 -90.381 -35.635 242.986 1.00164.98 O ANISOU 2514 O ARG A 434 28237 22184 12263 -605 -3710 2116 O ATOM 2515 CB ARG A 434 -87.577 -34.022 242.506 1.00164.43 C ANISOU 2515 CB ARG A 434 27343 22564 12570 395 -3985 1526 C ATOM 2516 CG ARG A 434 -87.199 -35.494 242.484 1.00167.71 C ANISOU 2516 CG ARG A 434 28180 22644 12899 568 -4475 1632 C ATOM 2517 CD ARG A 434 -85.723 -35.665 242.166 1.00168.70 C ANISOU 2517 CD ARG A 434 28067 22822 13209 1091 -4840 1367 C ATOM 2518 NE ARG A 434 -84.904 -34.696 242.889 1.00169.94 N ANISOU 2518 NE ARG A 434 28062 23250 13257 1188 -4792 1148 N ATOM 2519 CZ ARG A 434 -83.639 -34.417 242.595 1.00169.47 C ANISOU 2519 CZ ARG A 434 27671 23371 13348 1590 -4995 854 C ATOM 2520 NH1 ARG A 434 -82.972 -33.519 243.308 1.00167.96 N ANISOU 2520 NH1 ARG A 434 27346 23421 13049 1641 -4936 659 N ATOM 2521 NH2 ARG A 434 -83.040 -35.033 241.585 1.00169.52 N ANISOU 2521 NH2 ARG A 434 27463 23334 13615 1928 -5243 733 N ATOM 2522 N LYS A 435 -90.086 -34.002 244.512 1.00164.23 N ANISOU 2522 N LYS A 435 27861 22527 12013 -802 -3276 1875 N ATOM 2523 CA LYS A 435 -90.933 -34.670 245.494 1.00169.40 C ANISOU 2523 CA LYS A 435 29056 23064 12243 -1319 -3210 2089 C ATOM 2524 C LYS A 435 -92.375 -34.757 245.007 1.00167.89 C ANISOU 2524 C LYS A 435 28703 22895 12194 -1722 -2821 2187 C ATOM 2525 O LYS A 435 -93.009 -35.815 245.097 1.00173.45 O ANISOU 2525 O LYS A 435 29878 23364 12661 -2032 -2936 2420 O ATOM 2526 CB LYS A 435 -90.858 -33.938 246.835 1.00171.76 C ANISOU 2526 CB LYS A 435 29403 23595 12263 -1553 -2992 1993 C ATOM 2527 N ALA A 436 -92.919 -33.641 244.511 1.00160.67 N ANISOU 2527 N ALA A 436 27138 22253 11655 -1733 -2376 1992 N ATOM 2528 CA ALA A 436 -94.284 -33.648 243.995 1.00152.70 C ANISOU 2528 CA ALA A 436 25910 21286 10822 -2063 -2018 2015 C ATOM 2529 C ALA A 436 -94.423 -34.599 242.815 1.00151.88 C ANISOU 2529 C ALA A 436 25913 20882 10912 -1890 -2275 2174 C ATOM 2530 O ALA A 436 -95.442 -35.288 242.679 1.00152.25 O ANISOU 2530 O ALA A 436 26140 20816 10893 -2244 -2178 2317 O ATOM 2531 CB ALA A 436 -94.695 -32.233 243.591 1.00145.27 C ANISOU 2531 CB ALA A 436 24266 20651 10277 -1996 -1596 1731 C ATOM 2532 N PHE A 437 -93.400 -34.659 241.957 1.00152.09 N ANISOU 2532 N PHE A 437 25822 20797 11169 -1358 -2608 2133 N ATOM 2533 CA PHE A 437 -93.401 -35.613 240.853 1.00156.37 C ANISOU 2533 CA PHE A 437 26487 21055 11871 -1136 -2913 2269 C ATOM 2534 C PHE A 437 -93.490 -37.044 241.366 1.00161.79 C ANISOU 2534 C PHE A 437 27912 21414 12148 -1341 -3294 2542 C ATOM 2535 O PHE A 437 -94.373 -37.808 240.961 1.00168.08 O ANISOU 2535 O PHE A 437 28892 22019 12950 -1581 -3291 2712 O ATOM 2536 CB PHE A 437 -92.153 -35.420 239.991 1.00157.30 C ANISOU 2536 CB PHE A 437 26359 21174 12235 -538 -3219 2134 C ATOM 2537 CG PHE A 437 -92.199 -34.196 239.120 1.00155.01 C ANISOU 2537 CG PHE A 437 25395 21118 12384 -361 -2889 1919 C ATOM 2538 CD1 PHE A 437 -93.374 -33.480 238.966 1.00154.34 C ANISOU 2538 CD1 PHE A 437 24986 21157 12501 -656 -2426 1857 C ATOM 2539 CD2 PHE A 437 -91.067 -33.762 238.451 1.00152.52 C ANISOU 2539 CD2 PHE A 437 24788 20901 12263 87 -3061 1756 C ATOM 2540 CE1 PHE A 437 -93.418 -32.355 238.163 1.00149.59 C ANISOU 2540 CE1 PHE A 437 23839 20716 12282 -489 -2184 1659 C ATOM 2541 CE2 PHE A 437 -91.107 -32.637 237.648 1.00147.87 C ANISOU 2541 CE2 PHE A 437 23651 20497 12037 198 -2777 1581 C ATOM 2542 CZ PHE A 437 -92.284 -31.934 237.504 1.00146.56 C ANISOU 2542 CZ PHE A 437 23226 20395 12064 -81 -2360 1544 C ATOM 2543 N LEU A 438 -92.577 -37.424 242.263 1.00159.44 N ANISOU 2543 N LEU A 438 28056 21026 11499 -1249 -3647 2577 N ATOM 2544 CA LEU A 438 -92.559 -38.795 242.763 1.00159.12 C ANISOU 2544 CA LEU A 438 28483 20618 11358 -1357 -3950 2737 C ATOM 2545 C LEU A 438 -93.838 -39.137 243.516 1.00164.89 C ANISOU 2545 C LEU A 438 29542 21320 11790 -2056 -3652 2925 C ATOM 2546 O LEU A 438 -94.278 -40.293 243.498 1.00166.12 O ANISOU 2546 O LEU A 438 30055 21151 11911 -2254 -3830 3101 O ATOM 2547 CB LEU A 438 -91.338 -39.016 243.656 1.00152.42 C ANISOU 2547 CB LEU A 438 27814 19691 10406 -1090 -4270 2630 C ATOM 2548 CG LEU A 438 -89.978 -38.899 242.967 1.00144.45 C ANISOU 2548 CG LEU A 438 26491 18712 9681 -423 -4608 2407 C ATOM 2549 CD1 LEU A 438 -88.849 -39.176 243.947 1.00146.18 C ANISOU 2549 CD1 LEU A 438 26920 18848 9773 -216 -4921 2284 C ATOM 2550 CD2 LEU A 438 -89.899 -39.837 241.772 1.00143.54 C ANISOU 2550 CD2 LEU A 438 26320 18347 9873 -125 -4897 2434 C ATOM 2551 N LYS A 439 -94.451 -38.154 244.177 1.00164.88 N ANISOU 2551 N LYS A 439 29405 21674 11569 -2455 -3191 2863 N ATOM 2552 CA LYS A 439 -95.656 -38.419 244.956 1.00168.98 C ANISOU 2552 CA LYS A 439 30162 22256 11786 -3162 -2852 2983 C ATOM 2553 C LYS A 439 -96.878 -38.585 244.059 1.00166.24 C ANISOU 2553 C LYS A 439 29676 21939 11550 -3461 -2608 3058 C ATOM 2554 O LYS A 439 -97.669 -39.517 244.244 1.00169.04 O ANISOU 2554 O LYS A 439 30357 22109 11763 -3898 -2596 3232 O ATOM 2555 CB LYS A 439 -95.881 -37.296 245.970 1.00170.44 C ANISOU 2555 CB LYS A 439 30168 22869 11722 -3469 -2420 2824 C ATOM 2556 N ILE A 440 -97.054 -37.690 243.082 1.00164.19 N ANISOU 2556 N ILE A 440 28689 21873 11824 -3143 -2343 2829 N ATOM 2557 CA ILE A 440 -98.176 -37.816 242.158 1.00169.00 C ANISOU 2557 CA ILE A 440 28988 22477 12747 -3298 -2098 2810 C ATOM 2558 C ILE A 440 -98.044 -39.050 241.272 1.00179.74 C ANISOU 2558 C ILE A 440 30716 23411 14167 -3108 -2557 3049 C ATOM 2559 O ILE A 440 -99.055 -39.563 240.776 1.00180.46 O ANISOU 2559 O ILE A 440 30803 23412 14352 -3388 -2435 3127 O ATOM 2560 CB ILE A 440 -98.323 -36.539 241.306 1.00158.12 C ANISOU 2560 CB ILE A 440 26806 21358 11913 -2960 -1773 2500 C ATOM 2561 CG1 ILE A 440 -99.684 -36.508 240.605 1.00153.20 C ANISOU 2561 CG1 ILE A 440 25840 20799 11570 -3210 -1438 2412 C ATOM 2562 CG2 ILE A 440 -97.211 -36.442 240.275 1.00152.87 C ANISOU 2562 CG2 ILE A 440 25981 20532 11570 -2285 -2129 2478 C ATOM 2563 CD1 ILE A 440 -100.863 -36.557 241.548 1.00153.48 C ANISOU 2563 CD1 ILE A 440 25932 21075 11307 -3907 -1035 2364 C ATOM 2564 N LEU A 441 -96.824 -39.557 241.071 1.00183.17 N ANISOU 2564 N LEU A 441 31463 23590 14544 -2630 -3102 3140 N ATOM 2565 CA LEU A 441 -96.650 -40.817 240.356 1.00181.08 C ANISOU 2565 CA LEU A 441 31524 22905 14374 -2415 -3572 3317 C ATOM 2566 C LEU A 441 -97.154 -42.020 241.143 1.00181.95 C ANISOU 2566 C LEU A 441 32168 22724 14240 -2887 -3683 3509 C ATOM 2567 O LEU A 441 -97.447 -43.056 240.537 1.00190.38 O ANISOU 2567 O LEU A 441 33427 23461 15446 -2869 -3933 3635 O ATOM 2568 CB LEU A 441 -95.178 -41.017 239.994 1.00181.55 C ANISOU 2568 CB LEU A 441 31483 22821 14675 -1706 -4023 3192 C ATOM 2569 CG LEU A 441 -94.635 -40.157 238.849 1.00176.82 C ANISOU 2569 CG LEU A 441 30372 22410 14400 -1180 -4022 3018 C ATOM 2570 CD1 LEU A 441 -93.121 -40.270 238.761 1.00176.37 C ANISOU 2570 CD1 LEU A 441 30187 22324 14503 -585 -4396 2840 C ATOM 2571 CD2 LEU A 441 -95.284 -40.548 237.531 1.00174.65 C ANISOU 2571 CD2 LEU A 441 29959 21986 14415 -1071 -4060 3091 C ATOM 2572 N HIS A 442 -97.260 -41.918 242.464 1.00173.71 N ANISOU 2572 N HIS A 442 31379 21785 12838 -3315 -3514 3526 N ATOM 2573 CA HIS A 442 -97.736 -43.044 243.263 1.00165.27 C ANISOU 2573 CA HIS A 442 30860 20430 11504 -3817 -3622 3706 C ATOM 2574 C HIS A 442 -98.890 -42.624 244.168 1.00162.16 C ANISOU 2574 C HIS A 442 30504 20361 10748 -4607 -3079 3727 C ATOM 2575 O HIS A 442 -99.704 -41.777 243.801 1.00152.70 O ANISOU 2575 O HIS A 442 28906 19542 9570 -4830 -2624 3631 O ATOM 2576 CB HIS A 442 -96.598 -43.636 244.098 1.00165.25 C ANISOU 2576 CB HIS A 442 31243 20147 11396 -3566 -4055 3698 C ATOM 2577 CG HIS A 442 -97.054 -44.629 245.122 1.00172.45 C ANISOU 2577 CG HIS A 442 32770 20786 11966 -4145 -4142 3867 C ATOM 2578 ND1 HIS A 442 -97.407 -44.269 246.405 1.00176.69 N ANISOU 2578 ND1 HIS A 442 33490 21526 12117 -4680 -3834 3878 N ATOM 2579 CD2 HIS A 442 -97.216 -45.971 245.050 1.00176.95 C ANISOU 2579 CD2 HIS A 442 33828 20891 12514 -4291 -4509 4019 C ATOM 2580 CE1 HIS A 442 -97.766 -45.348 247.079 1.00182.48 C ANISOU 2580 CE1 HIS A 442 34811 21930 12595 -5150 -4006 4041 C ATOM 2581 NE2 HIS A 442 -97.659 -46.394 246.280 1.00182.64 N ANISOU 2581 NE2 HIS A 442 35042 21528 12824 -4931 -4425 4131 N TER 2582 HIS A 442 ATOM 2583 N ASP B 1 -106.287 -34.126 188.770 1.00119.34 N ANISOU 2583 N ASP B 1 12349 17411 15582 -1600 2759 2933 N ATOM 2584 CA ASP B 1 -106.067 -33.815 187.364 1.00113.12 C ANISOU 2584 CA ASP B 1 11832 16152 14995 -1848 2666 2590 C ATOM 2585 C ASP B 1 -107.370 -33.422 186.674 1.00109.79 C ANISOU 2585 C ASP B 1 11043 16089 14582 -1798 2624 2735 C ATOM 2586 O ASP B 1 -108.075 -34.268 186.123 1.00108.80 O ANISOU 2586 O ASP B 1 10663 15820 14856 -2160 2385 2916 O ATOM 2587 CB ASP B 1 -105.427 -35.007 186.648 1.00116.60 C ANISOU 2587 CB ASP B 1 12529 15847 15928 -2369 2411 2411 C ATOM 2588 CG ASP B 1 -104.001 -35.259 187.099 1.00119.43 C ANISOU 2588 CG ASP B 1 13318 15847 16211 -2400 2422 2192 C ATOM 2589 OD1 ASP B 1 -103.179 -34.321 187.021 1.00116.82 O ANISOU 2589 OD1 ASP B 1 13330 15439 15618 -2236 2501 1963 O ATOM 2590 OD2 ASP B 1 -103.703 -36.391 187.533 1.00123.52 O ANISOU 2590 OD2 ASP B 1 13818 16196 16918 -2571 2323 2286 O ATOM 2591 N ILE B 2 -107.683 -32.130 186.709 1.00106.65 N ANISOU 2591 N ILE B 2 10656 16163 13702 -1304 2835 2624 N ATOM 2592 CA ILE B 2 -108.888 -31.595 186.084 1.00101.05 C ANISOU 2592 CA ILE B 2 9612 15869 12915 -1153 2816 2727 C ATOM 2593 C ILE B 2 -108.556 -31.256 184.636 1.00 93.94 C ANISOU 2593 C ILE B 2 9183 14308 12201 -1378 2547 2177 C ATOM 2594 O ILE B 2 -107.779 -30.336 184.367 1.00 85.73 O ANISOU 2594 O ILE B 2 8745 12938 10892 -1089 2535 1622 O ATOM 2595 CB ILE B 2 -109.415 -30.366 186.834 1.00 97.99 C ANISOU 2595 CB ILE B 2 9198 16175 11859 -356 3070 2675 C ATOM 2596 CG1 ILE B 2 -109.736 -30.718 188.287 1.00 96.80 C ANISOU 2596 CG1 ILE B 2 8809 16467 11502 -76 3147 3036 C ATOM 2597 CG2 ILE B 2 -110.640 -29.797 186.134 1.00102.91 C ANISOU 2597 CG2 ILE B 2 9498 17187 12416 -162 3038 2764 C ATOM 2598 CD1 ILE B 2 -110.111 -29.522 189.133 1.00 96.37 C ANISOU 2598 CD1 ILE B 2 8876 16971 10770 742 3339 2900 C ATOM 2599 N VAL B 3 -109.145 -31.996 183.701 1.00 96.33 N ANISOU 2599 N VAL B 3 9241 14398 12963 -1890 2282 2328 N ATOM 2600 CA VAL B 3 -108.879 -31.782 182.283 1.00 92.68 C ANISOU 2600 CA VAL B 3 9232 13326 12656 -2107 1992 1808 C ATOM 2601 C VAL B 3 -109.743 -30.625 181.799 1.00 87.34 C ANISOU 2601 C VAL B 3 8503 13032 11649 -1692 1973 1654 C ATOM 2602 O VAL B 3 -110.969 -30.648 181.943 1.00 88.60 O ANISOU 2602 O VAL B 3 8076 13783 11806 -1638 1985 2101 O ATOM 2603 CB VAL B 3 -109.153 -33.054 181.469 1.00100.74 C ANISOU 2603 CB VAL B 3 10080 13931 14264 -2812 1663 1983 C ATOM 2604 CG1 VAL B 3 -108.878 -32.809 179.992 1.00 96.21 C ANISOU 2604 CG1 VAL B 3 10009 12788 13758 -2972 1373 1419 C ATOM 2605 CG2 VAL B 3 -108.311 -34.210 181.990 1.00104.93 C ANISOU 2605 CG2 VAL B 3 10698 14043 15128 -3144 1683 2116 C ATOM 2606 N MET B 4 -109.104 -29.610 181.227 1.00 81.50 N ANISOU 2606 N MET B 4 8344 11968 10656 -1397 1941 1078 N ATOM 2607 CA MET B 4 -109.802 -28.473 180.648 1.00 79.63 C ANISOU 2607 CA MET B 4 8126 11983 10147 -1010 1897 887 C ATOM 2608 C MET B 4 -109.976 -28.681 179.150 1.00 78.16 C ANISOU 2608 C MET B 4 8067 11400 10232 -1415 1558 666 C ATOM 2609 O MET B 4 -109.040 -29.092 178.458 1.00 73.99 O ANISOU 2609 O MET B 4 7980 10237 9896 -1731 1404 338 O ATOM 2610 CB MET B 4 -109.036 -27.176 180.913 1.00 74.11 C ANISOU 2610 CB MET B 4 7975 11155 9029 -440 2017 424 C ATOM 2611 CG MET B 4 -108.817 -26.889 182.390 1.00 75.94 C ANISOU 2611 CG MET B 4 8182 11760 8911 6 2307 558 C ATOM 2612 SD MET B 4 -110.343 -26.936 183.350 1.00 84.51 S ANISOU 2612 SD MET B 4 8488 13855 9766 378 2572 1183 S ATOM 2613 CE MET B 4 -111.105 -25.397 182.850 1.00 82.58 C ANISOU 2613 CE MET B 4 8361 13864 9150 1036 2574 903 C ATOM 2614 N THR B 5 -111.176 -28.393 178.653 1.00 81.95 N ANISOU 2614 N THR B 5 8153 12287 10697 -1377 1448 868 N ATOM 2615 CA THR B 5 -111.494 -28.547 177.241 1.00 79.59 C ANISOU 2615 CA THR B 5 7930 11711 10598 -1746 1095 693 C ATOM 2616 C THR B 5 -111.934 -27.207 176.673 1.00 84.84 C ANISOU 2616 C THR B 5 8680 12603 10952 -1282 1094 481 C ATOM 2617 O THR B 5 -112.840 -26.564 177.214 1.00 83.94 O ANISOU 2617 O THR B 5 8170 13100 10622 -856 1270 774 O ATOM 2618 CB THR B 5 -112.592 -29.596 177.030 1.00 76.95 C ANISOU 2618 CB THR B 5 6993 11616 10627 -2271 854 1209 C ATOM 2619 OG1 THR B 5 -112.038 -30.908 177.185 1.00 80.72 O ANISOU 2619 OG1 THR B 5 7532 11647 11489 -2806 735 1291 O ATOM 2620 CG2 THR B 5 -113.196 -29.469 175.639 1.00 71.17 C ANISOU 2620 CG2 THR B 5 6275 10788 9980 -2529 478 1065 C ATOM 2621 N GLN B 6 -111.292 -26.792 175.584 1.00 87.40 N ANISOU 2621 N GLN B 6 9503 12452 11251 -1333 911 8 N ATOM 2622 CA GLN B 6 -111.715 -25.645 174.794 1.00 89.67 C ANISOU 2622 CA GLN B 6 9858 12882 11330 -1008 831 -169 C ATOM 2623 C GLN B 6 -112.356 -26.172 173.517 1.00106.04 C ANISOU 2623 C GLN B 6 11777 14906 13607 -1492 462 -130 C ATOM 2624 O GLN B 6 -111.717 -26.913 172.762 1.00110.73 O ANISOU 2624 O GLN B 6 12702 14998 14374 -1920 242 -383 O ATOM 2625 CB GLN B 6 -110.534 -24.725 174.489 1.00 79.67 C ANISOU 2625 CB GLN B 6 9225 11163 9881 -702 868 -661 C ATOM 2626 CG GLN B 6 -109.785 -24.278 175.737 1.00 75.86 C ANISOU 2626 CG GLN B 6 8971 10639 9212 -302 1144 -733 C ATOM 2627 CD GLN B 6 -109.066 -22.957 175.556 1.00 75.01 C ANISOU 2627 CD GLN B 6 9342 10271 8887 146 1142 -1096 C ATOM 2628 OE1 GLN B 6 -108.184 -22.605 176.340 1.00 77.80 O ANISOU 2628 OE1 GLN B 6 10025 10413 9123 373 1255 -1242 O ATOM 2629 NE2 GLN B 6 -109.441 -22.216 174.520 1.00 72.55 N ANISOU 2629 NE2 GLN B 6 9059 9969 8540 252 979 -1209 N ATOM 2630 N THR B 7 -113.615 -25.792 173.284 1.00119.66 N ANISOU 2630 N THR B 7 13010 17164 15291 -1400 388 194 N ATOM 2631 CA THR B 7 -114.448 -26.514 172.325 1.00136.18 C ANISOU 2631 CA THR B 7 14805 19322 17616 -1949 -4 390 C ATOM 2632 C THR B 7 -113.871 -26.450 170.915 1.00138.86 C ANISOU 2632 C THR B 7 15652 19182 17928 -2172 -306 -95 C ATOM 2633 O THR B 7 -113.801 -27.468 170.216 1.00143.05 O ANISOU 2633 O THR B 7 16302 19384 18667 -2726 -640 -188 O ATOM 2634 CB THR B 7 -115.873 -25.958 172.349 1.00148.21 C ANISOU 2634 CB THR B 7 15682 21557 19072 -1743 -5 877 C ATOM 2635 OG1 THR B 7 -115.832 -24.526 172.287 1.00152.50 O ANISOU 2635 OG1 THR B 7 16385 22266 19292 -1084 206 682 O ATOM 2636 CG2 THR B 7 -116.589 -26.388 173.621 1.00151.90 C ANISOU 2636 CG2 THR B 7 15534 22560 19620 -1659 231 1487 C ATOM 2637 N THR B 8 -113.450 -25.267 170.477 1.00127.67 N ANISOU 2637 N THR B 8 14548 17715 16248 -1727 -209 -399 N ATOM 2638 CA THR B 8 -112.914 -25.078 169.136 1.00112.40 C ANISOU 2638 CA THR B 8 13046 15430 14230 -1852 -455 -796 C ATOM 2639 C THR B 8 -111.466 -24.618 169.221 1.00 97.19 C ANISOU 2639 C THR B 8 11710 13035 12182 -1572 -258 -1195 C ATOM 2640 O THR B 8 -111.166 -23.616 169.878 1.00 96.82 O ANISOU 2640 O THR B 8 11736 13061 11992 -1077 -6 -1215 O ATOM 2641 CB THR B 8 -113.741 -24.058 168.346 1.00110.90 C ANISOU 2641 CB THR B 8 12633 15626 13877 -1622 -576 -705 C ATOM 2642 OG1 THR B 8 -113.639 -22.771 168.969 1.00105.94 O ANISOU 2642 OG1 THR B 8 12015 15172 13066 -976 -267 -696 O ATOM 2643 CG2 THR B 8 -115.203 -24.479 168.300 1.00118.32 C ANISOU 2643 CG2 THR B 8 12922 17083 14952 -1901 -777 -217 C ATOM 2644 N SER B 9 -110.572 -25.354 168.556 1.00 86.74 N ANISOU 2644 N SER B 9 10814 11227 10916 -1876 -392 -1495 N ATOM 2645 CA SER B 9 -109.166 -24.964 168.536 1.00 75.14 C ANISOU 2645 CA SER B 9 9860 9338 9351 -1637 -223 -1793 C ATOM 2646 C SER B 9 -108.954 -23.728 167.671 1.00 72.15 C ANISOU 2646 C SER B 9 9652 9006 8756 -1297 -270 -1934 C ATOM 2647 O SER B 9 -108.165 -22.844 168.022 1.00 63.13 O ANISOU 2647 O SER B 9 8734 7716 7536 -930 -100 -2007 O ATOM 2648 CB SER B 9 -108.304 -26.124 168.040 1.00 68.59 C ANISOU 2648 CB SER B 9 9411 8022 8630 -1997 -321 -2026 C ATOM 2649 OG SER B 9 -108.533 -26.380 166.666 1.00 75.40 O ANISOU 2649 OG SER B 9 10414 8836 9397 -2206 -627 -2214 O ATOM 2650 N SER B 10 -109.644 -23.653 166.537 1.00 79.56 N ANISOU 2650 N SER B 10 10477 10141 9611 -1436 -534 -1945 N ATOM 2651 CA SER B 10 -109.600 -22.500 165.653 1.00 84.61 C ANISOU 2651 CA SER B 10 11189 10897 10061 -1137 -604 -2002 C ATOM 2652 C SER B 10 -110.966 -21.828 165.616 1.00 86.80 C ANISOU 2652 C SER B 10 10975 11696 10308 -1006 -683 -1725 C ATOM 2653 O SER B 10 -112.000 -22.474 165.807 1.00 91.58 O ANISOU 2653 O SER B 10 11192 12588 11014 -1282 -796 -1503 O ATOM 2654 CB SER B 10 -109.176 -22.905 164.238 1.00 87.16 C ANISOU 2654 CB SER B 10 11813 11058 10247 -1351 -839 -2236 C ATOM 2655 OG SER B 10 -109.126 -21.780 163.378 1.00 90.78 O ANISOU 2655 OG SER B 10 12293 11674 10524 -1061 -900 -2225 O ATOM 2656 N LEU B 11 -110.961 -20.520 165.368 1.00 81.60 N ANISOU 2656 N LEU B 11 10312 11154 9539 -581 -635 -1691 N ATOM 2657 CA LEU B 11 -112.190 -19.733 165.426 1.00 76.70 C ANISOU 2657 CA LEU B 11 9232 11017 8892 -341 -651 -1404 C ATOM 2658 C LEU B 11 -111.996 -18.460 164.620 1.00 76.39 C ANISOU 2658 C LEU B 11 9291 10990 8742 8 -713 -1428 C ATOM 2659 O LEU B 11 -111.082 -17.680 164.906 1.00 75.15 O ANISOU 2659 O LEU B 11 9447 10522 8586 339 -590 -1551 O ATOM 2660 CB LEU B 11 -112.558 -19.405 166.873 1.00 74.79 C ANISOU 2660 CB LEU B 11 8782 10936 8700 7 -365 -1230 C ATOM 2661 CG LEU B 11 -113.903 -18.711 167.094 1.00 75.87 C ANISOU 2661 CG LEU B 11 8397 11626 8802 320 -315 -880 C ATOM 2662 CD1 LEU B 11 -115.051 -19.626 166.698 1.00 82.02 C ANISOU 2662 CD1 LEU B 11 8681 12816 9665 -141 -519 -568 C ATOM 2663 CD2 LEU B 11 -114.045 -18.259 168.539 1.00 73.15 C ANISOU 2663 CD2 LEU B 11 7975 11401 8418 809 13 -784 C ATOM 2664 N SER B 12 -112.850 -18.249 163.623 1.00 75.89 N ANISOU 2664 N SER B 12 8945 11280 8607 -88 -936 -1272 N ATOM 2665 CA SER B 12 -112.730 -17.121 162.711 1.00 79.91 C ANISOU 2665 CA SER B 12 9494 11844 9023 189 -1030 -1237 C ATOM 2666 C SER B 12 -113.751 -16.054 163.079 1.00 79.75 C ANISOU 2666 C SER B 12 9070 12188 9046 619 -946 -936 C ATOM 2667 O SER B 12 -114.903 -16.365 163.396 1.00 88.48 O ANISOU 2667 O SER B 12 9725 13710 10183 545 -945 -673 O ATOM 2668 CB SER B 12 -112.934 -17.566 161.261 1.00 92.43 C ANISOU 2668 CB SER B 12 11063 13602 10455 -175 -1346 -1265 C ATOM 2669 OG SER B 12 -114.140 -18.294 161.116 1.00104.20 O ANISOU 2669 OG SER B 12 12156 15476 11961 -533 -1541 -1078 O ATOM 2670 N ALA B 13 -113.325 -14.794 163.034 1.00 74.73 N ANISOU 2670 N ALA B 13 8583 11385 8428 1079 -887 -938 N ATOM 2671 CA ALA B 13 -114.181 -13.691 163.441 1.00 64.65 C ANISOU 2671 CA ALA B 13 7008 10359 7199 1588 -787 -697 C ATOM 2672 C ALA B 13 -113.892 -12.472 162.579 1.00 71.66 C ANISOU 2672 C ALA B 13 7974 11142 8111 1874 -918 -629 C ATOM 2673 O ALA B 13 -112.731 -12.162 162.300 1.00 70.22 O ANISOU 2673 O ALA B 13 8186 10533 7960 1889 -974 -798 O ATOM 2674 CB ALA B 13 -113.983 -13.348 164.921 1.00 63.97 C ANISOU 2674 CB ALA B 13 7077 10070 7158 2013 -512 -793 C ATOM 2675 N SER B 14 -114.954 -11.788 162.164 1.00 77.48 N ANISOU 2675 N SER B 14 8294 12286 8858 2098 -970 -320 N ATOM 2676 CA SER B 14 -114.797 -10.524 161.461 1.00 82.77 C ANISOU 2676 CA SER B 14 8979 12868 9600 2433 -1082 -187 C ATOM 2677 C SER B 14 -114.336 -9.441 162.429 1.00 83.06 C ANISOU 2677 C SER B 14 9308 12463 9789 3016 -943 -294 C ATOM 2678 O SER B 14 -114.582 -9.509 163.637 1.00 80.02 O ANISOU 2678 O SER B 14 8971 12038 9395 3282 -729 -393 O ATOM 2679 CB SER B 14 -116.111 -10.112 160.798 1.00 89.30 C ANISOU 2679 CB SER B 14 9250 14269 10412 2524 -1169 211 C ATOM 2680 OG SER B 14 -116.604 -11.140 159.956 1.00 94.18 O ANISOU 2680 OG SER B 14 9614 15288 10881 1954 -1363 302 O ATOM 2681 N LEU B 15 -113.647 -8.440 161.889 1.00 84.75 N ANISOU 2681 N LEU B 15 9729 12337 10134 3214 -1095 -264 N ATOM 2682 CA LEU B 15 -113.111 -7.374 162.723 1.00 86.06 C ANISOU 2682 CA LEU B 15 10244 11975 10479 3721 -1069 -385 C ATOM 2683 C LEU B 15 -114.240 -6.559 163.343 1.00 85.44 C ANISOU 2683 C LEU B 15 9932 12094 10437 4316 -933 -250 C ATOM 2684 O LEU B 15 -115.266 -6.301 162.707 1.00 86.84 O ANISOU 2684 O LEU B 15 9647 12743 10606 4404 -944 71 O ATOM 2685 CB LEU B 15 -112.195 -6.468 161.903 1.00 89.70 C ANISOU 2685 CB LEU B 15 10903 12047 11132 3758 -1320 -278 C ATOM 2686 CG LEU B 15 -110.721 -6.875 161.869 1.00 84.70 C ANISOU 2686 CG LEU B 15 10688 10964 10531 3439 -1405 -452 C ATOM 2687 CD1 LEU B 15 -109.972 -6.097 160.798 1.00 86.63 C ANISOU 2687 CD1 LEU B 15 10958 11017 10940 3414 -1655 -189 C ATOM 2688 CD2 LEU B 15 -110.080 -6.670 163.233 1.00 80.98 C ANISOU 2688 CD2 LEU B 15 10657 9958 10156 3666 -1344 -735 C ATOM 2689 N GLY B 16 -114.043 -6.154 164.595 1.00 78.64 N ANISOU 2689 N GLY B 16 9400 10887 9594 4755 -803 -488 N ATOM 2690 CA GLY B 16 -115.067 -5.419 165.312 1.00 80.15 C ANISOU 2690 CA GLY B 16 9437 11257 9758 5425 -625 -407 C ATOM 2691 C GLY B 16 -116.304 -6.221 165.645 1.00 79.96 C ANISOU 2691 C GLY B 16 8895 11957 9528 5411 -351 -198 C ATOM 2692 O GLY B 16 -117.396 -5.651 165.737 1.00100.49 O ANISOU 2692 O GLY B 16 11140 14929 12113 5893 -215 68 O ATOM 2693 N ASP B 17 -116.168 -7.530 165.829 1.00 77.38 N ANISOU 2693 N ASP B 17 8492 11838 9069 4877 -275 -264 N ATOM 2694 CA ASP B 17 -117.288 -8.401 166.153 1.00 84.99 C ANISOU 2694 CA ASP B 17 8932 13472 9888 4765 -68 0 C ATOM 2695 C ASP B 17 -117.191 -8.889 167.593 1.00 85.98 C ANISOU 2695 C ASP B 17 9226 13583 9860 4972 207 -188 C ATOM 2696 O ASP B 17 -116.185 -8.699 168.281 1.00 84.26 O ANISOU 2696 O ASP B 17 9560 12827 9628 5100 208 -565 O ATOM 2697 CB ASP B 17 -117.346 -9.598 165.197 1.00 90.83 C ANISOU 2697 CB ASP B 17 9400 14492 10617 3955 -247 128 C ATOM 2698 CG ASP B 17 -118.080 -9.282 163.912 1.00105.94 C ANISOU 2698 CG ASP B 17 10884 16787 12582 3814 -449 483 C ATOM 2699 OD1 ASP B 17 -118.420 -8.100 163.694 1.00113.07 O ANISOU 2699 OD1 ASP B 17 11707 17686 13569 4323 -449 641 O ATOM 2700 OD2 ASP B 17 -118.325 -10.218 163.123 1.00111.30 O ANISOU 2700 OD2 ASP B 17 11317 17758 13213 3199 -631 604 O ATOM 2701 N ARG B 18 -118.267 -9.530 168.038 1.00 93.56 N ANISOU 2701 N ARG B 18 9664 15179 10705 4992 425 134 N ATOM 2702 CA ARG B 18 -118.336 -10.122 169.367 1.00 96.68 C ANISOU 2702 CA ARG B 18 10082 15725 10929 5163 712 76 C ATOM 2703 C ARG B 18 -117.835 -11.558 169.293 1.00 98.73 C ANISOU 2703 C ARG B 18 10333 15954 11227 4362 623 18 C ATOM 2704 O ARG B 18 -118.430 -12.392 168.602 1.00101.86 O ANISOU 2704 O ARG B 18 10275 16726 11699 3818 498 322 O ATOM 2705 CB ARG B 18 -119.764 -10.071 169.907 1.00102.54 C ANISOU 2705 CB ARG B 18 10202 17220 11540 5630 1012 553 C ATOM 2706 CG ARG B 18 -119.997 -10.930 171.137 1.00100.75 C ANISOU 2706 CG ARG B 18 9811 17338 11132 5683 1308 655 C ATOM 2707 CD ARG B 18 -121.482 -11.082 171.420 1.00107.58 C ANISOU 2707 CD ARG B 18 9892 19073 11912 5985 1567 1298 C ATOM 2708 NE ARG B 18 -121.739 -11.445 172.810 1.00114.99 N ANISOU 2708 NE ARG B 18 10760 20331 12598 6352 1927 1402 N ATOM 2709 CZ ARG B 18 -122.012 -10.568 173.772 1.00120.99 C ANISOU 2709 CZ ARG B 18 11915 20969 13087 6947 2120 1308 C ATOM 2710 NH1 ARG B 18 -122.072 -9.273 173.493 1.00125.04 N ANISOU 2710 NH1 ARG B 18 12791 21131 13587 7370 2046 1120 N ATOM 2711 NH2 ARG B 18 -122.232 -10.987 175.011 1.00122.25 N ANISOU 2711 NH2 ARG B 18 12087 21375 12988 7108 2363 1424 N ATOM 2712 N VAL B 19 -116.748 -11.846 170.002 1.00 86.77 N ANISOU 2712 N VAL B 19 9070 12555 11344 4020 772 -480 N ATOM 2713 CA VAL B 19 -116.138 -13.170 170.003 1.00 88.40 C ANISOU 2713 CA VAL B 19 9239 12744 11603 3567 784 -308 C ATOM 2714 C VAL B 19 -116.348 -13.799 171.372 1.00 87.09 C ANISOU 2714 C VAL B 19 8965 12874 11251 3449 959 -302 C ATOM 2715 O VAL B 19 -116.205 -13.129 172.400 1.00 88.96 O ANISOU 2715 O VAL B 19 9345 13119 11339 3639 1018 -441 O ATOM 2716 CB VAL B 19 -114.638 -13.101 169.654 1.00 92.20 C ANISOU 2716 CB VAL B 19 10081 12741 12208 3385 641 -270 C ATOM 2717 CG1 VAL B 19 -114.069 -14.499 169.453 1.00 92.10 C ANISOU 2717 CG1 VAL B 19 10015 12705 12274 2960 639 -88 C ATOM 2718 CG2 VAL B 19 -114.422 -12.246 168.416 1.00 92.59 C ANISOU 2718 CG2 VAL B 19 10285 12489 12406 3543 483 -295 C ATOM 2719 N THR B 20 -116.684 -15.087 171.383 1.00 84.53 N ANISOU 2719 N THR B 20 8407 12783 10927 3126 1045 -142 N ATOM 2720 CA THR B 20 -116.898 -15.823 172.621 1.00 85.07 C ANISOU 2720 CA THR B 20 8376 13134 10814 2966 1220 -91 C ATOM 2721 C THR B 20 -116.151 -17.146 172.550 1.00 88.13 C ANISOU 2721 C THR B 20 8831 13378 11276 2536 1207 113 C ATOM 2722 O THR B 20 -116.328 -17.916 171.600 1.00 88.48 O ANISOU 2722 O THR B 20 8745 13404 11467 2313 1168 232 O ATOM 2723 CB THR B 20 -118.390 -16.068 172.877 1.00 86.16 C ANISOU 2723 CB THR B 20 8102 13805 10829 3029 1392 -104 C ATOM 2724 OG1 THR B 20 -119.043 -14.821 173.144 1.00 90.47 O ANISOU 2724 OG1 THR B 20 8600 14499 11274 3478 1419 -310 O ATOM 2725 CG2 THR B 20 -118.584 -16.998 174.067 1.00 82.55 C ANISOU 2725 CG2 THR B 20 7546 13633 10185 2786 1584 -7 C ATOM 2726 N ILE B 21 -115.320 -17.398 173.557 1.00 88.14 N ANISOU 2726 N ILE B 21 9043 13280 11167 2436 1236 146 N ATOM 2727 CA ILE B 21 -114.470 -18.580 173.630 1.00 82.22 C ANISOU 2727 CA ILE B 21 8411 12358 10470 2085 1214 337 C ATOM 2728 C ILE B 21 -114.901 -19.381 174.847 1.00 86.95 C ANISOU 2728 C ILE B 21 8909 13272 10856 1934 1404 442 C ATOM 2729 O ILE B 21 -114.807 -18.894 175.981 1.00 85.46 O ANISOU 2729 O ILE B 21 8806 13206 10460 2085 1473 357 O ATOM 2730 CB ILE B 21 -112.981 -18.210 173.714 1.00 79.10 C ANISOU 2730 CB ILE B 21 8365 11564 10126 2098 1059 305 C ATOM 2731 CG1 ILE B 21 -112.624 -17.193 172.628 1.00 75.95 C ANISOU 2731 CG1 ILE B 21 8082 10878 9899 2276 895 181 C ATOM 2732 CG2 ILE B 21 -112.116 -19.455 173.597 1.00 80.10 C ANISOU 2732 CG2 ILE B 21 8592 11507 10335 1772 1018 505 C ATOM 2733 CD1 ILE B 21 -111.237 -16.606 172.773 1.00 76.90 C ANISOU 2733 CD1 ILE B 21 8526 10645 10046 2306 756 108 C ATOM 2734 N SER B 22 -115.374 -20.601 174.615 1.00 93.44 N ANISOU 2734 N SER B 22 9563 14221 11719 1626 1492 623 N ATOM 2735 CA SER B 22 -115.864 -21.457 175.683 1.00 96.78 C ANISOU 2735 CA SER B 22 9886 14941 11943 1436 1688 756 C ATOM 2736 C SER B 22 -114.744 -22.326 176.245 1.00 90.15 C ANISOU 2736 C SER B 22 9321 13856 11074 1221 1656 935 C ATOM 2737 O SER B 22 -113.723 -22.572 175.598 1.00 88.61 O ANISOU 2737 O SER B 22 9324 13287 11055 1145 1495 984 O ATOM 2738 CB SER B 22 -117.011 -22.336 175.183 1.00105.15 C ANISOU 2738 CB SER B 22 10628 16273 13051 1185 1813 861 C ATOM 2739 OG SER B 22 -116.584 -23.180 174.130 1.00108.97 O ANISOU 2739 OG SER B 22 11171 16468 13765 922 1708 982 O ATOM 2740 N CYS B 23 -114.954 -22.791 177.475 1.00 89.32 N ANISOU 2740 N CYS B 23 9219 13988 10729 1136 1815 1035 N ATOM 2741 CA CYS B 23 -113.942 -23.552 178.202 1.00 80.57 C ANISOU 2741 CA CYS B 23 8376 12699 9538 986 1792 1211 C ATOM 2742 C CYS B 23 -114.677 -24.404 179.228 1.00 82.66 C ANISOU 2742 C CYS B 23 8542 13297 9569 786 2021 1387 C ATOM 2743 O CYS B 23 -115.301 -23.863 180.149 1.00 83.29 O ANISOU 2743 O CYS B 23 8513 13730 9405 932 2160 1296 O ATOM 2744 CB CYS B 23 -112.938 -22.614 178.864 1.00 77.70 C ANISOU 2744 CB CYS B 23 8250 12210 9062 1243 1672 1070 C ATOM 2745 SG CYS B 23 -111.807 -23.370 180.056 1.00 77.23 S ANISOU 2745 SG CYS B 23 8475 12062 8806 1134 1652 1261 S ATOM 2746 N ARG B 24 -114.633 -25.722 179.051 1.00 88.43 N ANISOU 2746 N ARG B 24 9316 13915 10371 453 2069 1632 N ATOM 2747 CA ARG B 24 -115.383 -26.651 179.886 1.00 93.96 C ANISOU 2747 CA ARG B 24 9931 14897 10872 198 2298 1833 C ATOM 2748 C ARG B 24 -114.420 -27.419 180.781 1.00 91.70 C ANISOU 2748 C ARG B 24 9960 14434 10447 100 2285 2058 C ATOM 2749 O ARG B 24 -113.544 -28.137 180.287 1.00 90.64 O ANISOU 2749 O ARG B 24 10038 13916 10485 -18 2156 2193 O ATOM 2750 CB ARG B 24 -116.204 -27.618 179.033 1.00102.41 C ANISOU 2750 CB ARG B 24 10814 15986 12113 -142 2387 1950 C ATOM 2751 CG ARG B 24 -116.985 -28.637 179.847 1.00111.29 C ANISOU 2751 CG ARG B 24 11863 17380 13043 -466 2636 2173 C ATOM 2752 CD ARG B 24 -117.849 -29.518 178.961 1.00116.88 C ANISOU 2752 CD ARG B 24 12366 18118 13924 -827 2722 2251 C ATOM 2753 NE ARG B 24 -118.578 -30.520 179.733 1.00122.77 N ANISOU 2753 NE ARG B 24 13059 19101 14487 -1183 2971 2475 N ATOM 2754 N ALA B 25 -114.587 -27.263 182.090 1.00 94.56 N ANISOU 2754 N ALA B 25 10351 15090 10487 167 2417 2095 N ATOM 2755 CA ALA B 25 -113.819 -28.025 183.060 1.00 96.12 C ANISOU 2755 CA ALA B 25 10830 15194 10498 77 2425 2334 C ATOM 2756 C ALA B 25 -114.411 -29.417 183.238 1.00100.82 C ANISOU 2756 C ALA B 25 11426 15827 11054 -310 2612 2641 C ATOM 2757 O ALA B 25 -115.627 -29.614 183.154 1.00104.38 O ANISOU 2757 O ALA B 25 11611 16575 11473 -494 2810 2646 O ATOM 2758 CB ALA B 25 -113.781 -27.300 184.404 1.00 97.33 C ANISOU 2758 CB ALA B 25 11020 15670 10292 297 2493 2250 C ATOM 2759 N SER B 26 -113.534 -30.394 183.478 1.00100.77 N ANISOU 2759 N SER B 26 11724 15514 11051 -436 2548 2898 N ATOM 2760 CA SER B 26 -113.983 -31.771 183.650 1.00103.12 C ANISOU 2760 CA SER B 26 12096 15764 11320 -813 2717 3212 C ATOM 2761 C SER B 26 -114.785 -31.970 184.930 1.00111.16 C ANISOU 2761 C SER B 26 13054 17216 11968 -930 2976 3353 C ATOM 2762 O SER B 26 -115.400 -33.029 185.095 1.00121.47 O ANISOU 2762 O SER B 26 14374 18551 13228 -1285 3162 3601 O ATOM 2763 CB SER B 26 -112.786 -32.723 183.636 1.00104.69 C ANISOU 2763 CB SER B 26 12670 15507 11602 -860 2574 3453 C ATOM 2764 OG SER B 26 -111.876 -32.416 184.676 1.00107.32 O ANISOU 2764 OG SER B 26 13213 15876 11686 -618 2484 3500 O ATOM 2765 N GLN B 27 -114.788 -30.990 185.831 1.00110.92 N ANISOU 2765 N GLN B 27 12964 17516 11666 -656 2998 3198 N ATOM 2766 CA GLN B 27 -115.620 -31.025 187.024 1.00108.17 C ANISOU 2766 CA GLN B 27 12514 17644 10942 -736 3256 3284 C ATOM 2767 C GLN B 27 -115.882 -29.592 187.468 1.00112.63 C ANISOU 2767 C GLN B 27 12885 18573 11335 -381 3258 2950 C ATOM 2768 O GLN B 27 -115.404 -28.633 186.855 1.00109.93 O ANISOU 2768 O GLN B 27 12519 18076 11172 -100 3059 2680 O ATOM 2769 CB GLN B 27 -114.957 -31.837 188.142 1.00102.54 C ANISOU 2769 CB GLN B 27 12140 16868 9953 -813 3287 3607 C ATOM 2770 CG GLN B 27 -113.747 -31.155 188.760 1.00 99.65 C ANISOU 2770 CG GLN B 27 11996 16426 9440 -456 3074 3514 C ATOM 2771 CD GLN B 27 -113.097 -31.991 189.844 1.00103.24 C ANISOU 2771 CD GLN B 27 12780 16841 9608 -514 3089 3849 C ATOM 2772 OE1 GLN B 27 -112.460 -33.006 189.564 1.00105.58 O ANISOU 2772 OE1 GLN B 27 13329 16748 10039 -647 3002 4112 O ATOM 2773 NE2 GLN B 27 -113.257 -31.568 191.093 1.00106.28 N ANISOU 2773 NE2 GLN B 27 13170 17631 9582 -397 3198 3840 N ATOM 2774 N ASP B 28 -116.653 -29.449 188.542 1.00118.83 N ANISOU 2774 N ASP B 28 13545 19840 11765 -400 3493 2968 N ATOM 2775 CA ASP B 28 -117.011 -28.134 189.069 1.00121.33 C ANISOU 2775 CA ASP B 28 13682 20537 11883 -62 3532 2646 C ATOM 2776 C ASP B 28 -115.766 -27.496 189.672 1.00121.82 C ANISOU 2776 C ASP B 28 14033 20441 11813 244 3322 2548 C ATOM 2777 O ASP B 28 -115.339 -27.855 190.771 1.00127.06 O ANISOU 2777 O ASP B 28 14903 21212 12160 226 3364 2722 O ATOM 2778 CB ASP B 28 -118.128 -28.260 190.099 1.00126.68 C ANISOU 2778 CB ASP B 28 14156 21786 12190 -181 3855 2708 C ATOM 2779 CG ASP B 28 -118.862 -26.952 190.328 1.00131.18 C ANISOU 2779 CG ASP B 28 14434 22779 12630 143 3938 2337 C ATOM 2780 OD1 ASP B 28 -118.286 -25.883 190.038 1.00129.71 O ANISOU 2780 OD1 ASP B 28 14308 22427 12550 497 3734 2051 O ATOM 2781 OD2 ASP B 28 -120.019 -26.994 190.796 1.00136.65 O ANISOU 2781 OD2 ASP B 28 14839 23968 13112 43 4213 2330 O ATOM 2782 N ILE B 29 -115.175 -26.542 188.954 1.00117.52 N ANISOU 2782 N ILE B 29 13505 19650 11498 516 3092 2269 N ATOM 2783 CA ILE B 29 -113.994 -25.841 189.446 1.00116.74 C ANISOU 2783 CA ILE B 29 13653 19409 11293 789 2882 2132 C ATOM 2784 C ILE B 29 -114.404 -24.587 190.208 1.00114.19 C ANISOU 2784 C ILE B 29 13222 19460 10705 1087 2957 1812 C ATOM 2785 O ILE B 29 -113.550 -23.779 190.588 1.00114.28 O ANISOU 2785 O ILE B 29 13405 19389 10627 1330 2790 1617 O ATOM 2786 CB ILE B 29 -113.019 -25.500 188.304 1.00118.07 C ANISOU 2786 CB ILE B 29 13933 19090 11837 894 2592 2011 C ATOM 2787 CG1 ILE B 29 -113.722 -24.700 187.208 1.00120.17 C ANISOU 2787 CG1 ILE B 29 13947 19334 12378 1002 2583 1750 C ATOM 2788 CG2 ILE B 29 -112.392 -26.768 187.741 1.00114.57 C ANISOU 2788 CG2 ILE B 29 13660 18269 11604 640 2502 2325 C ATOM 2789 CD1 ILE B 29 -112.778 -24.144 186.162 1.00116.60 C ANISOU 2789 CD1 ILE B 29 13608 18446 12249 1138 2310 1593 C ATOM 2790 N SER B 30 -115.711 -24.416 190.427 1.00114.78 N ANISOU 2790 N SER B 30 13007 19954 10652 1068 3210 1741 N ATOM 2791 CA SER B 30 -116.242 -23.393 191.335 1.00110.78 C ANISOU 2791 CA SER B 30 12390 19876 9827 1336 3341 1468 C ATOM 2792 C SER B 30 -115.708 -21.998 191.011 1.00109.67 C ANISOU 2792 C SER B 30 12320 19547 9802 1708 3137 1082 C ATOM 2793 O SER B 30 -115.329 -21.234 191.901 1.00106.48 O ANISOU 2793 O SER B 30 12047 19278 9131 1933 3110 884 O ATOM 2794 CB SER B 30 -115.947 -23.760 192.790 1.00106.78 C ANISOU 2794 CB SER B 30 12060 19640 8870 1293 3443 1621 C ATOM 2795 OG SER B 30 -116.205 -25.132 193.028 1.00108.11 O ANISOU 2795 OG SER B 30 12253 19863 8960 926 3592 2028 O ATOM 2796 N ASN B 31 -115.665 -21.676 189.717 1.00109.51 N ANISOU 2796 N ASN B 31 12230 19203 10177 1756 2991 976 N ATOM 2797 CA ASN B 31 -115.269 -20.353 189.228 1.00110.22 C ANISOU 2797 CA ASN B 31 12383 19074 10420 2083 2810 625 C ATOM 2798 C ASN B 31 -113.828 -20.014 189.598 1.00113.00 C ANISOU 2798 C ASN B 31 13076 19133 10725 2167 2574 563 C ATOM 2799 O ASN B 31 -113.485 -18.847 189.800 1.00117.14 O ANISOU 2799 O ASN B 31 13705 19604 11198 2437 2478 250 O ATOM 2800 CB ASN B 31 -116.215 -19.261 189.737 1.00111.83 C ANISOU 2800 CB ASN B 31 12407 19661 10424 2390 2969 308 C ATOM 2801 CG ASN B 31 -117.669 -19.575 189.463 1.00115.38 C ANISOU 2801 CG ASN B 31 12472 20484 10882 2320 3212 356 C ATOM 2802 OD1 ASN B 31 -118.161 -19.367 188.357 1.00118.72 O ANISOU 2802 OD1 ASN B 31 12713 20798 11600 2363 3170 291 O ATOM 2803 ND2 ASN B 31 -118.366 -20.079 190.474 1.00117.78 N ANISOU 2803 ND2 ASN B 31 12643 21259 10850 2205 3468 470 N ATOM 2804 N TYR B 32 -112.974 -21.030 189.685 1.00113.55 N ANISOU 2804 N TYR B 32 13324 19010 10811 1936 2478 853 N ATOM 2805 CA TYR B 32 -111.539 -20.840 189.891 1.00108.24 C ANISOU 2805 CA TYR B 32 12940 18056 10130 1989 2230 822 C ATOM 2806 C TYR B 32 -110.884 -21.030 188.526 1.00 99.19 C ANISOU 2806 C TYR B 32 11839 16435 9413 1908 2025 870 C ATOM 2807 O TYR B 32 -110.425 -22.120 188.182 1.00 95.95 O ANISOU 2807 O TYR B 32 11497 15830 9128 1692 1969 1158 O ATOM 2808 CB TYR B 32 -110.989 -21.809 190.933 1.00112.03 C ANISOU 2808 CB TYR B 32 13585 18666 10317 1837 2249 1108 C ATOM 2809 CG TYR B 32 -111.501 -21.573 192.340 1.00120.60 C ANISOU 2809 CG TYR B 32 14656 20230 10936 1922 2437 1053 C ATOM 2810 CD1 TYR B 32 -111.197 -20.405 193.025 1.00122.53 C ANISOU 2810 CD1 TYR B 32 14987 20604 10964 2181 2378 716 C ATOM 2811 CD2 TYR B 32 -112.270 -22.530 192.990 1.00122.95 C ANISOU 2811 CD2 TYR B 32 14868 20848 10999 1728 2679 1336 C ATOM 2812 CE1 TYR B 32 -111.658 -20.189 194.311 1.00124.52 C ANISOU 2812 CE1 TYR B 32 15230 21311 10772 2265 2553 648 C ATOM 2813 CE2 TYR B 32 -112.734 -22.324 194.274 1.00125.43 C ANISOU 2813 CE2 TYR B 32 15166 21626 10866 1800 2862 1290 C ATOM 2814 CZ TYR B 32 -112.425 -21.152 194.931 1.00127.35 C ANISOU 2814 CZ TYR B 32 15487 22008 10894 2079 2797 940 C ATOM 2815 OH TYR B 32 -112.886 -20.944 196.211 1.00132.37 O ANISOU 2815 OH TYR B 32 16109 23121 11066 2157 2984 878 O ATOM 2816 N LEU B 33 -110.840 -19.954 187.743 1.00 98.57 N ANISOU 2816 N LEU B 33 11736 16162 9553 2092 1916 587 N ATOM 2817 CA LEU B 33 -110.358 -20.040 186.373 1.00 96.17 C ANISOU 2817 CA LEU B 33 11448 15444 9647 2023 1745 612 C ATOM 2818 C LEU B 33 -109.764 -18.705 185.949 1.00 94.23 C ANISOU 2818 C LEU B 33 11317 14959 9526 2244 1568 289 C ATOM 2819 O LEU B 33 -110.252 -17.642 186.344 1.00 94.40 O ANISOU 2819 O LEU B 33 11318 15132 9418 2472 1630 18 O ATOM 2820 CB LEU B 33 -111.489 -20.437 185.416 1.00 93.60 C ANISOU 2820 CB LEU B 33 10868 15154 9542 1925 1873 697 C ATOM 2821 CG LEU B 33 -111.182 -20.378 183.918 1.00 90.14 C ANISOU 2821 CG LEU B 33 10416 14330 9501 1885 1714 682 C ATOM 2822 CD1 LEU B 33 -110.709 -21.732 183.412 1.00 92.60 C ANISOU 2822 CD1 LEU B 33 10777 14433 9975 1597 1666 991 C ATOM 2823 CD2 LEU B 33 -112.383 -19.887 183.133 1.00 88.97 C ANISOU 2823 CD2 LEU B 33 10015 14295 9495 1982 1810 557 C ATOM 2824 N ASN B 34 -108.708 -18.776 185.142 1.00 89.45 N ANISOU 2824 N ASN B 34 10842 13976 9169 2170 1357 318 N ATOM 2825 CA ASN B 34 -108.022 -17.609 184.615 1.00 87.13 C ANISOU 2825 CA ASN B 34 10678 13404 9024 2316 1180 48 C ATOM 2826 C ASN B 34 -107.885 -17.741 183.103 1.00 79.31 C ANISOU 2826 C ASN B 34 9640 12076 8416 2234 1078 105 C ATOM 2827 O ASN B 34 -107.893 -18.843 182.550 1.00 77.70 O ANISOU 2827 O ASN B 34 9363 11802 8358 2038 1087 357 O ATOM 2828 CB ASN B 34 -106.636 -17.441 185.255 1.00 91.32 C ANISOU 2828 CB ASN B 34 11432 13839 9425 2298 1001 -9 C ATOM 2829 CG ASN B 34 -106.662 -17.624 186.762 1.00 98.94 C ANISOU 2829 CG ASN B 34 12448 15158 9987 2331 1088 8 C ATOM 2830 OD1 ASN B 34 -107.561 -17.134 187.444 1.00103.92 O ANISOU 2830 OD1 ASN B 34 13012 16070 10402 2470 1252 -128 O ATOM 2831 ND2 ASN B 34 -105.672 -18.335 187.288 1.00 99.15 N ANISOU 2831 ND2 ASN B 34 12588 15189 9895 2218 979 176 N ATOM 2832 N TRP B 35 -107.759 -16.593 182.441 1.00 76.06 N ANISOU 2832 N TRP B 35 9291 11449 8158 2384 983 -136 N ATOM 2833 CA TRP B 35 -107.624 -16.512 180.990 1.00 70.33 C ANISOU 2833 CA TRP B 35 8540 10410 7773 2335 881 -115 C ATOM 2834 C TRP B 35 -106.334 -15.782 180.648 1.00 74.28 C ANISOU 2834 C TRP B 35 9258 10586 8380 2338 674 -263 C ATOM 2835 O TRP B 35 -106.143 -14.632 181.067 1.00 75.38 O ANISOU 2835 O TRP B 35 9536 10684 8422 2496 635 -519 O ATOM 2836 CB TRP B 35 -108.816 -15.791 180.356 1.00 69.59 C ANISOU 2836 CB TRP B 35 8304 10362 7776 2518 972 -244 C ATOM 2837 CG TRP B 35 -110.095 -16.564 180.361 1.00 75.02 C ANISOU 2837 CG TRP B 35 8722 11356 8425 2471 1161 -91 C ATOM 2838 CD1 TRP B 35 -111.107 -16.475 181.271 1.00 80.33 C ANISOU 2838 CD1 TRP B 35 9255 12412 8856 2586 1352 -140 C ATOM 2839 CD2 TRP B 35 -110.513 -17.528 179.389 1.00 72.51 C ANISOU 2839 CD2 TRP B 35 8234 11004 8312 2280 1184 120 C ATOM 2840 NE1 TRP B 35 -112.125 -17.333 180.932 1.00 78.68 N ANISOU 2840 NE1 TRP B 35 8783 12421 8691 2459 1494 36 N ATOM 2841 CE2 TRP B 35 -111.785 -17.992 179.780 1.00 74.71 C ANISOU 2841 CE2 TRP B 35 8265 11659 8463 2265 1390 194 C ATOM 2842 CE3 TRP B 35 -109.933 -18.049 178.228 1.00 70.45 C ANISOU 2842 CE3 TRP B 35 8002 10445 8321 2111 1055 243 C ATOM 2843 CZ2 TRP B 35 -112.485 -18.951 179.052 1.00 75.45 C ANISOU 2843 CZ2 TRP B 35 8145 11826 8695 2065 1462 380 C ATOM 2844 CZ3 TRP B 35 -110.630 -19.000 177.507 1.00 73.70 C ANISOU 2844 CZ3 TRP B 35 8217 10921 8866 1934 1126 421 C ATOM 2845 CH2 TRP B 35 -111.892 -19.441 177.921 1.00 73.43 C ANISOU 2845 CH2 TRP B 35 7943 11252 8705 1903 1324 486 C ATOM 2846 N TYR B 36 -105.467 -16.449 179.885 1.00 74.99 N ANISOU 2846 N TYR B 36 9376 10451 8666 2155 549 -111 N ATOM 2847 CA TYR B 36 -104.222 -15.900 179.371 1.00 73.67 C ANISOU 2847 CA TYR B 36 9372 9987 8633 2109 358 -219 C ATOM 2848 C TYR B 36 -104.290 -15.744 177.857 1.00 68.21 C ANISOU 2848 C TYR B 36 8643 9022 8251 2070 301 -199 C ATOM 2849 O TYR B 36 -105.041 -16.441 177.167 1.00 69.60 O ANISOU 2849 O TYR B 36 8661 9229 8554 2018 377 -42 O ATOM 2850 CB TYR B 36 -103.028 -16.796 179.721 1.00 69.85 C ANISOU 2850 CB TYR B 36 8942 9490 8107 1945 249 -66 C ATOM 2851 CG TYR B 36 -102.834 -17.064 181.192 1.00 67.69 C ANISOU 2851 CG TYR B 36 8714 9493 7511 1971 281 -49 C ATOM 2852 CD1 TYR B 36 -101.929 -16.323 181.937 1.00 67.31 C ANISOU 2852 CD1 TYR B 36 8813 9464 7299 2010 165 -244 C ATOM 2853 CD2 TYR B 36 -103.539 -18.073 181.833 1.00 66.83 C ANISOU 2853 CD2 TYR B 36 8508 9634 7251 1937 426 167 C ATOM 2854 CE1 TYR B 36 -101.743 -16.567 183.281 1.00 73.04 C ANISOU 2854 CE1 TYR B 36 9580 10468 7705 2038 183 -229 C ATOM 2855 CE2 TYR B 36 -103.359 -18.325 183.175 1.00 72.47 C ANISOU 2855 CE2 TYR B 36 9277 10612 7647 1962 457 202 C ATOM 2856 CZ TYR B 36 -102.460 -17.570 183.896 1.00 77.56 C ANISOU 2856 CZ TYR B 36 10062 11288 8121 2024 330 2 C ATOM 2857 OH TYR B 36 -102.275 -17.820 185.236 1.00 84.06 O ANISOU 2857 OH TYR B 36 10938 12399 8603 2054 351 35 O ATOM 2858 N GLN B 37 -103.453 -14.844 177.347 1.00 62.63 N ANISOU 2858 N GLN B 37 8089 8054 7654 2073 164 -359 N ATOM 2859 CA GLN B 37 -103.311 -14.590 175.921 1.00 65.16 C ANISOU 2859 CA GLN B 37 8416 8099 8245 2026 92 -349 C ATOM 2860 C GLN B 37 -101.868 -14.838 175.504 1.00 63.14 C ANISOU 2860 C GLN B 37 8244 7651 8095 1843 -63 -316 C ATOM 2861 O GLN B 37 -100.936 -14.449 176.213 1.00 67.91 O ANISOU 2861 O GLN B 37 8969 8255 8580 1812 -149 -432 O ATOM 2862 CB GLN B 37 -103.712 -13.152 175.580 1.00 73.51 C ANISOU 2862 CB GLN B 37 9594 8996 9340 2207 84 -572 C ATOM 2863 CG GLN B 37 -103.592 -12.791 174.112 1.00 76.79 C ANISOU 2863 CG GLN B 37 10041 9129 10009 2172 10 -554 C ATOM 2864 CD GLN B 37 -103.547 -11.293 173.889 1.00 84.18 C ANISOU 2864 CD GLN B 37 11189 9828 10967 2317 -37 -777 C ATOM 2865 OE1 GLN B 37 -102.716 -10.594 174.469 1.00 85.66 O ANISOU 2865 OE1 GLN B 37 11568 9909 11070 2285 -106 -944 O ATOM 2866 NE2 GLN B 37 -104.444 -10.790 173.049 1.00 87.63 N ANISOU 2866 NE2 GLN B 37 11603 10180 11513 2476 -3 -782 N ATOM 2867 N GLN B 38 -101.684 -15.481 174.352 1.00 58.91 N ANISOU 2867 N GLN B 38 7632 6976 7774 1722 -99 -170 N ATOM 2868 CA GLN B 38 -100.363 -15.693 173.773 1.00 55.91 C ANISOU 2868 CA GLN B 38 7304 6421 7516 1562 -234 -146 C ATOM 2869 C GLN B 38 -100.369 -15.185 172.340 1.00 57.89 C ANISOU 2869 C GLN B 38 7578 6425 7991 1529 -276 -173 C ATOM 2870 O GLN B 38 -101.125 -15.689 171.500 1.00 54.90 O ANISOU 2870 O GLN B 38 7084 6036 7737 1527 -220 -54 O ATOM 2871 CB GLN B 38 -99.954 -17.168 173.810 1.00 51.08 C ANISOU 2871 CB GLN B 38 6589 5893 6929 1441 -240 75 C ATOM 2872 CG GLN B 38 -98.535 -17.407 173.313 1.00 46.61 C ANISOU 2872 CG GLN B 38 6054 5189 6466 1309 -378 85 C ATOM 2873 CD GLN B 38 -98.125 -18.862 173.373 1.00 52.01 C ANISOU 2873 CD GLN B 38 6656 5934 7171 1234 -385 299 C ATOM 2874 OE1 GLN B 38 -96.974 -19.184 173.671 1.00 53.91 O ANISOU 2874 OE1 GLN B 38 6914 6194 7376 1189 -489 312 O ATOM 2875 NE2 GLN B 38 -99.068 -19.753 173.096 1.00 58.45 N ANISOU 2875 NE2 GLN B 38 7385 6783 8042 1222 -276 464 N ATOM 2876 N LYS B 39 -99.530 -14.187 172.072 1.00 63.89 N ANISOU 2876 N LYS B 39 8490 6997 8789 1489 -373 -330 N ATOM 2877 CA LYS B 39 -99.397 -13.579 170.760 1.00 59.41 C ANISOU 2877 CA LYS B 39 7985 6181 8408 1445 -418 -357 C ATOM 2878 C LYS B 39 -98.532 -14.447 169.850 1.00 53.19 C ANISOU 2878 C LYS B 39 7114 5327 7770 1260 -481 -226 C ATOM 2879 O LYS B 39 -97.833 -15.348 170.321 1.00 48.11 O ANISOU 2879 O LYS B 39 6397 4798 7085 1176 -513 -149 O ATOM 2880 CB LYS B 39 -98.791 -12.185 170.893 1.00 63.93 C ANISOU 2880 CB LYS B 39 8776 6565 8948 1440 -486 -571 C ATOM 2881 CG LYS B 39 -99.612 -11.228 171.739 1.00 71.57 C ANISOU 2881 CG LYS B 39 9860 7560 9772 1646 -425 -734 C ATOM 2882 CD LYS B 39 -98.985 -9.845 171.768 1.00 77.56 C ANISOU 2882 CD LYS B 39 10876 8073 10521 1618 -494 -952 C ATOM 2883 CE LYS B 39 -99.974 -8.792 172.235 1.00 78.93 C ANISOU 2883 CE LYS B 39 11195 8191 10605 1869 -424 -1112 C ATOM 2884 NZ LYS B 39 -99.339 -7.450 172.343 1.00 82.15 N ANISOU 2884 NZ LYS B 39 11894 8322 10996 1826 -488 -1338 N ATOM 2885 N PRO B 40 -98.584 -14.213 168.534 1.00 55.77 N ANISOU 2885 N PRO B 40 7451 5477 8263 1212 -499 -196 N ATOM 2886 CA PRO B 40 -97.751 -15.006 167.611 1.00 52.90 C ANISOU 2886 CA PRO B 40 7008 5056 8034 1044 -550 -93 C ATOM 2887 C PRO B 40 -96.274 -15.039 167.978 1.00 57.95 C ANISOU 2887 C PRO B 40 7676 5699 8642 905 -644 -154 C ATOM 2888 O PRO B 40 -95.600 -16.037 167.693 1.00 62.11 O ANISOU 2888 O PRO B 40 8095 6277 9228 814 -673 -55 O ATOM 2889 CB PRO B 40 -97.967 -14.312 166.258 1.00 47.50 C ANISOU 2889 CB PRO B 40 6389 4172 7484 1026 -562 -104 C ATOM 2890 CG PRO B 40 -99.210 -13.476 166.409 1.00 47.50 C ANISOU 2890 CG PRO B 40 6455 4156 7437 1224 -504 -159 C ATOM 2891 CD PRO B 40 -99.681 -13.526 167.831 1.00 51.62 C ANISOU 2891 CD PRO B 40 6958 4860 7794 1347 -450 -211 C ATOM 2892 N ASP B 41 -95.746 -13.984 168.599 1.00 62.70 N ANISOU 2892 N ASP B 41 8417 6256 9150 888 -694 -324 N ATOM 2893 CA ASP B 41 -94.351 -13.967 169.026 1.00 64.20 C ANISOU 2893 CA ASP B 41 8606 6497 9289 745 -791 -403 C ATOM 2894 C ASP B 41 -94.108 -14.762 170.308 1.00 71.28 C ANISOU 2894 C ASP B 41 9418 7639 10027 800 -809 -366 C ATOM 2895 O ASP B 41 -93.023 -14.656 170.890 1.00 72.40 O ANISOU 2895 O ASP B 41 9555 7874 10082 714 -901 -452 O ATOM 2896 CB ASP B 41 -93.868 -12.523 169.202 1.00 61.95 C ANISOU 2896 CB ASP B 41 8511 6068 8958 670 -841 -614 C ATOM 2897 CG ASP B 41 -94.545 -11.808 170.359 1.00 76.08 C ANISOU 2897 CG ASP B 41 10426 7899 10583 816 -808 -747 C ATOM 2898 OD1 ASP B 41 -95.561 -12.318 170.876 1.00 82.67 O ANISOU 2898 OD1 ASP B 41 11195 8867 11349 989 -729 -666 O ATOM 2899 OD2 ASP B 41 -94.054 -10.729 170.753 1.00 83.78 O ANISOU 2899 OD2 ASP B 41 11567 8776 11490 747 -856 -942 O ATOM 2900 N GLY B 42 -95.086 -15.551 170.756 1.00 76.45 N ANISOU 2900 N GLY B 42 10003 8413 10630 931 -725 -235 N ATOM 2901 CA GLY B 42 -94.946 -16.372 171.939 1.00 73.52 C ANISOU 2901 CA GLY B 42 9570 8266 10096 987 -729 -160 C ATOM 2902 C GLY B 42 -95.150 -15.676 173.268 1.00 70.05 C ANISOU 2902 C GLY B 42 9222 7961 9431 1072 -726 -298 C ATOM 2903 O GLY B 42 -95.194 -16.359 174.299 1.00 70.16 O ANISOU 2903 O GLY B 42 9194 8182 9280 1135 -714 -219 O ATOM 2904 N THR B 43 -95.278 -14.350 173.291 1.00 67.92 N ANISOU 2904 N THR B 43 9094 7574 9139 1082 -732 -502 N ATOM 2905 CA THR B 43 -95.419 -13.646 174.559 1.00 70.59 C ANISOU 2905 CA THR B 43 9536 8033 9253 1162 -731 -668 C ATOM 2906 C THR B 43 -96.768 -13.972 175.188 1.00 70.44 C ANISOU 2906 C THR B 43 9481 8160 9122 1344 -595 -592 C ATOM 2907 O THR B 43 -97.801 -13.951 174.513 1.00 67.22 O ANISOU 2907 O THR B 43 9044 7670 8827 1424 -500 -529 O ATOM 2908 CB THR B 43 -95.281 -12.137 174.357 1.00 73.02 C ANISOU 2908 CB THR B 43 10036 8128 9579 1131 -761 -912 C ATOM 2909 OG1 THR B 43 -96.221 -11.694 173.370 1.00 80.02 O ANISOU 2909 OG1 THR B 43 10973 8808 10625 1212 -682 -885 O ATOM 2910 CG2 THR B 43 -93.870 -11.784 173.910 1.00 73.15 C ANISOU 2910 CG2 THR B 43 10080 8046 9668 909 -890 -1003 C ATOM 2911 N VAL B 44 -96.759 -14.262 176.487 1.00 71.16 N ANISOU 2911 N VAL B 44 9565 8496 8977 1404 -586 -600 N ATOM 2912 CA VAL B 44 -97.961 -14.625 177.226 1.00 63.77 C ANISOU 2912 CA VAL B 44 8583 7753 7896 1554 -446 -525 C ATOM 2913 C VAL B 44 -98.350 -13.474 178.143 1.00 67.42 C ANISOU 2913 C VAL B 44 9179 8276 8162 1677 -412 -772 C ATOM 2914 O VAL B 44 -97.493 -12.863 178.793 1.00 72.90 O ANISOU 2914 O VAL B 44 9981 8994 8723 1628 -512 -952 O ATOM 2915 CB VAL B 44 -97.757 -15.925 178.028 1.00 56.46 C ANISOU 2915 CB VAL B 44 7559 7070 6824 1538 -437 -316 C ATOM 2916 CG1 VAL B 44 -99.046 -16.331 178.729 1.00 53.80 C ANISOU 2916 CG1 VAL B 44 7166 6938 6337 1656 -270 -220 C ATOM 2917 CG2 VAL B 44 -97.272 -17.037 177.114 1.00 58.02 C ANISOU 2917 CG2 VAL B 44 7655 7168 7222 1429 -479 -97 C ATOM 2918 N LYS B 45 -99.647 -13.180 178.189 1.00 64.91 N ANISOU 2918 N LYS B 45 8845 7997 7820 1839 -272 -792 N ATOM 2919 CA LYS B 45 -100.193 -12.072 178.958 1.00 67.88 C ANISOU 2919 CA LYS B 45 9349 8417 8026 2002 -216 -1036 C ATOM 2920 C LYS B 45 -101.341 -12.584 179.814 1.00 66.34 C ANISOU 2920 C LYS B 45 9038 8530 7638 2150 -52 -955 C ATOM 2921 O LYS B 45 -102.178 -13.359 179.340 1.00 66.78 O ANISOU 2921 O LYS B 45 8931 8657 7786 2165 49 -756 O ATOM 2922 CB LYS B 45 -100.677 -10.939 178.044 1.00 71.06 C ANISOU 2922 CB LYS B 45 9866 8531 8602 2100 -202 -1183 C ATOM 2923 CG LYS B 45 -100.752 -9.581 178.722 1.00 78.15 C ANISOU 2923 CG LYS B 45 10981 9353 9359 2230 -201 -1493 C ATOM 2924 N LEU B 46 -101.384 -12.149 181.071 1.00 63.46 N ANISOU 2924 N LEU B 46 8753 8363 6995 2241 -23 -1118 N ATOM 2925 CA LEU B 46 -102.503 -12.482 181.942 1.00 67.74 C ANISOU 2925 CA LEU B 46 9193 9222 7322 2387 150 -1074 C ATOM 2926 C LEU B 46 -103.641 -11.501 181.697 1.00 73.23 C ANISOU 2926 C LEU B 46 9910 9864 8052 2615 264 -1251 C ATOM 2927 O LEU B 46 -103.472 -10.288 181.868 1.00 74.22 O ANISOU 2927 O LEU B 46 10224 9836 8140 2721 223 -1529 O ATOM 2928 CB LEU B 46 -102.079 -12.451 183.409 1.00 73.38 C ANISOU 2928 CB LEU B 46 9983 10204 7695 2401 138 -1174 C ATOM 2929 CG LEU B 46 -103.228 -12.577 184.416 1.00 79.48 C ANISOU 2929 CG LEU B 46 10676 11324 8200 2564 332 -1180 C ATOM 2930 CD1 LEU B 46 -103.967 -13.898 184.241 1.00 83.70 C ANISOU 2930 CD1 LEU B 46 10996 12039 8766 2502 461 -847 C ATOM 2931 CD2 LEU B 46 -102.736 -12.417 185.847 1.00 77.72 C ANISOU 2931 CD2 LEU B 46 10554 11359 7616 2582 306 -1310 C ATOM 2932 N LEU B 47 -104.800 -12.024 181.298 1.00 74.33 N ANISOU 2932 N LEU B 47 9854 10130 8257 2691 406 -1096 N ATOM 2933 CA LEU B 47 -105.967 -11.198 181.015 1.00 73.64 C ANISOU 2933 CA LEU B 47 9736 10040 8203 2939 517 -1239 C ATOM 2934 C LEU B 47 -106.968 -11.219 182.165 1.00 77.49 C ANISOU 2934 C LEU B 47 10122 10918 8405 3113 700 -1303 C ATOM 2935 O LEU B 47 -107.308 -10.167 182.714 1.00 78.31 O ANISOU 2935 O LEU B 47 10342 11042 8372 3337 745 -1571 O ATOM 2936 CB LEU B 47 -106.646 -11.656 179.717 1.00 69.45 C ANISOU 2936 CB LEU B 47 9028 9424 7936 2921 545 -1054 C ATOM 2937 CG LEU B 47 -105.822 -11.607 178.432 1.00 70.69 C ANISOU 2937 CG LEU B 47 9268 9212 8379 2772 387 -989 C ATOM 2938 CD1 LEU B 47 -106.670 -12.066 177.259 1.00 70.71 C ANISOU 2938 CD1 LEU B 47 9077 9200 8591 2779 434 -823 C ATOM 2939 CD2 LEU B 47 -105.273 -10.209 178.189 1.00 69.69 C ANISOU 2939 CD2 LEU B 47 9407 8764 8310 2865 282 -1243 C ATOM 2940 N LEU B 48 -107.450 -12.401 182.543 1.00 79.84 N ANISOU 2940 N LEU B 48 10212 11522 8602 3010 816 -1065 N ATOM 2941 CA LEU B 48 -108.493 -12.490 183.553 1.00 82.10 C ANISOU 2941 CA LEU B 48 10365 12213 8616 3153 1015 -1099 C ATOM 2942 C LEU B 48 -108.104 -13.473 184.645 1.00 83.86 C ANISOU 2942 C LEU B 48 10571 12710 8582 2986 1056 -931 C ATOM 2943 O LEU B 48 -107.466 -14.493 184.382 1.00 83.22 O ANISOU 2943 O LEU B 48 10473 12558 8588 2756 982 -680 O ATOM 2944 CB LEU B 48 -109.828 -12.927 182.936 1.00 78.92 C ANISOU 2944 CB LEU B 48 9682 11987 8318 3209 1170 -966 C ATOM 2945 CG LEU B 48 -110.514 -11.939 181.993 1.00 74.35 C ANISOU 2945 CG LEU B 48 9077 11240 7932 3449 1164 -1130 C ATOM 2946 CD1 LEU B 48 -111.846 -12.494 181.534 1.00 74.56 C ANISOU 2946 CD1 LEU B 48 8778 11540 8013 3487 1319 -992 C ATOM 2947 CD2 LEU B 48 -110.703 -10.600 182.673 1.00 74.52 C ANISOU 2947 CD2 LEU B 48 9263 11261 7788 3755 1192 -1467 C ATOM 2948 N TYR B 49 -108.520 -13.166 185.873 1.00 85.77 N ANISOU 2948 N TYR B 49 10824 13270 8494 3120 1179 -1066 N ATOM 2949 CA TYR B 49 -108.422 -14.084 186.998 1.00 89.80 C ANISOU 2949 CA TYR B 49 11299 14114 8707 2996 1261 -892 C ATOM 2950 C TYR B 49 -109.751 -14.091 187.738 1.00 97.77 C ANISOU 2950 C TYR B 49 12128 15550 9471 3139 1515 -925 C ATOM 2951 O TYR B 49 -110.523 -13.133 187.669 1.00104.75 O ANISOU 2951 O TYR B 49 12969 16481 10350 3389 1599 -1172 O ATOM 2952 CB TYR B 49 -107.282 -13.708 187.961 1.00 91.32 C ANISOU 2952 CB TYR B 49 11723 14308 8666 2983 1125 -1038 C ATOM 2953 CG TYR B 49 -107.387 -12.320 188.546 1.00 89.02 C ANISOU 2953 CG TYR B 49 11579 14034 8210 3220 1133 -1436 C ATOM 2954 CD1 TYR B 49 -106.917 -11.212 187.856 1.00 90.90 C ANISOU 2954 CD1 TYR B 49 11986 13891 8659 3302 991 -1688 C ATOM 2955 CD2 TYR B 49 -107.950 -12.121 189.801 1.00 90.43 C ANISOU 2955 CD2 TYR B 49 11746 14601 8012 3356 1288 -1562 C ATOM 2956 CE1 TYR B 49 -107.011 -9.943 188.394 1.00 94.07 C ANISOU 2956 CE1 TYR B 49 12560 14265 8916 3516 1001 -2060 C ATOM 2957 CE2 TYR B 49 -108.048 -10.856 190.347 1.00 95.92 C ANISOU 2957 CE2 TYR B 49 12594 15299 8552 3583 1299 -1948 C ATOM 2958 CZ TYR B 49 -107.577 -9.772 189.641 1.00 99.16 C ANISOU 2958 CZ TYR B 49 13191 15295 9192 3663 1153 -2199 C ATOM 2959 OH TYR B 49 -107.673 -8.511 190.182 1.00106.69 O ANISOU 2959 OH TYR B 49 14333 16208 9997 3886 1166 -2593 O ATOM 2960 N TYR B 50 -110.021 -15.194 188.436 1.00 99.65 N ANISOU 2960 N TYR B 50 12258 16100 9503 2982 1643 -665 N ATOM 2961 CA TYR B 50 -111.272 -15.391 189.178 1.00103.92 C ANISOU 2961 CA TYR B 50 12598 17099 9787 3057 1908 -647 C ATOM 2962 C TYR B 50 -112.499 -15.333 188.268 1.00104.08 C ANISOU 2962 C TYR B 50 12351 17173 10022 3130 2039 -641 C ATOM 2963 O TYR B 50 -113.595 -14.989 188.719 1.00107.80 O ANISOU 2963 O TYR B 50 12643 17995 10320 3300 2241 -762 O ATOM 2964 CB TYR B 50 -111.405 -14.381 190.324 1.00109.54 C ANISOU 2964 CB TYR B 50 13410 18052 10158 3304 1977 -969 C ATOM 2965 CG TYR B 50 -112.165 -14.903 191.526 1.00115.83 C ANISOU 2965 CG TYR B 50 14077 19374 10559 3290 2220 -878 C ATOM 2966 CD1 TYR B 50 -112.712 -16.181 191.530 1.00114.58 C ANISOU 2966 CD1 TYR B 50 13731 19428 10376 3052 2368 -518 C ATOM 2967 CD2 TYR B 50 -112.325 -14.120 192.660 1.00118.50 C ANISOU 2967 CD2 TYR B 50 14494 19991 10539 3500 2306 -1155 C ATOM 2968 CE1 TYR B 50 -113.404 -16.659 192.630 1.00114.59 C ANISOU 2968 CE1 TYR B 50 13622 19915 10003 3013 2603 -418 C ATOM 2969 CE2 TYR B 50 -113.014 -14.587 193.762 1.00117.03 C ANISOU 2969 CE2 TYR B 50 14188 20309 9969 3483 2539 -1070 C ATOM 2970 CZ TYR B 50 -113.551 -15.857 193.743 1.00118.90 C ANISOU 2970 CZ TYR B 50 14234 20758 10185 3233 2690 -692 C ATOM 2971 OH TYR B 50 -114.239 -16.325 194.840 1.00130.71 O ANISOU 2971 OH TYR B 50 15617 22763 11286 3191 2935 -592 O ATOM 2972 N THR B 51 -112.299 -15.635 186.981 1.00105.79 N ANISOU 2972 N THR B 51 12532 17060 10604 3014 1918 -517 N ATOM 2973 CA THR B 51 -113.346 -15.821 185.976 1.00111.89 C ANISOU 2973 CA THR B 51 13039 17871 11604 3017 2007 -451 C ATOM 2974 C THR B 51 -114.023 -14.521 185.547 1.00114.63 C ANISOU 2974 C THR B 51 13328 18196 12030 3362 2019 -760 C ATOM 2975 O THR B 51 -114.750 -14.509 184.549 1.00115.79 O ANISOU 2975 O THR B 51 13278 18318 12398 3404 2038 -732 O ATOM 2976 CB THR B 51 -114.405 -16.807 186.495 1.00116.41 C ANISOU 2976 CB THR B 51 13343 18892 11995 2864 2257 -240 C ATOM 2977 OG1 THR B 51 -113.762 -17.894 187.172 1.00117.89 O ANISOU 2977 OG1 THR B 51 13646 19115 12032 2592 2261 28 O ATOM 2978 CG2 THR B 51 -115.236 -17.362 185.354 1.00118.26 C ANISOU 2978 CG2 THR B 51 13310 19129 12496 2740 2307 -96 C ATOM 2979 N SER B 52 -113.780 -13.418 186.246 1.00114.82 N ANISOU 2979 N SER B 52 13534 18210 11881 3619 1998 -1056 N ATOM 2980 CA SER B 52 -114.393 -12.165 185.819 1.00115.29 C ANISOU 2980 CA SER B 52 13582 18197 12026 3975 2004 -1347 C ATOM 2981 C SER B 52 -113.560 -10.923 186.095 1.00111.54 C ANISOU 2981 C SER B 52 13450 17410 11519 4172 1859 -1655 C ATOM 2982 O SER B 52 -114.022 -9.824 185.774 1.00111.30 O ANISOU 2982 O SER B 52 13465 17269 11557 4488 1859 -1905 O ATOM 2983 CB SER B 52 -115.775 -12.010 186.484 1.00122.18 C ANISOU 2983 CB SER B 52 14180 19583 12661 4192 2262 -1448 C ATOM 2984 OG SER B 52 -116.658 -13.037 186.072 1.00127.90 O ANISOU 2984 OG SER B 52 14561 20588 13448 4008 2397 -1192 O ATOM 2985 N ARG B 53 -112.363 -11.039 186.659 1.00109.92 N ANISOU 2985 N ARG B 53 13491 17057 11215 4002 1732 -1654 N ATOM 2986 CA ARG B 53 -111.634 -9.882 187.162 1.00104.39 C ANISOU 2986 CA ARG B 53 13103 16145 10415 4158 1624 -1976 C ATOM 2987 C ARG B 53 -110.520 -9.500 186.194 1.00 94.34 C ANISOU 2987 C ARG B 53 12060 14344 9441 4041 1379 -1991 C ATOM 2988 O ARG B 53 -109.610 -10.296 185.939 1.00 87.79 O ANISOU 2988 O ARG B 53 11262 13390 8705 3752 1254 -1774 O ATOM 2989 CB ARG B 53 -111.078 -10.177 188.554 1.00104.86 C ANISOU 2989 CB ARG B 53 13267 16465 10110 4056 1650 -2003 C ATOM 2990 CG ARG B 53 -112.131 -10.769 189.482 1.00108.83 C ANISOU 2990 CG ARG B 53 13526 17518 10307 4103 1906 -1918 C ATOM 2991 CD ARG B 53 -111.701 -10.784 190.935 1.00118.82 C ANISOU 2991 CD ARG B 53 14923 19064 11160 4083 1946 -2014 C ATOM 2992 NE ARG B 53 -111.532 -9.442 191.482 1.00128.44 N ANISOU 2992 NE ARG B 53 16369 20201 12232 4348 1915 -2436 N ATOM 2993 CZ ARG B 53 -111.289 -9.190 192.764 1.00136.96 C ANISOU 2993 CZ ARG B 53 17572 21541 12927 4397 1959 -2613 C ATOM 2994 NH1 ARG B 53 -111.150 -7.939 193.182 1.00142.90 N ANISOU 2994 NH1 ARG B 53 18548 22178 13568 4634 1928 -3022 N ATOM 2995 NH2 ARG B 53 -111.193 -10.189 193.630 1.00137.25 N ANISOU 2995 NH2 ARG B 53 17524 21946 12678 4210 2037 -2381 N ATOM 2996 N LEU B 54 -110.603 -8.284 185.657 1.00 96.59 N ANISOU 2996 N LEU B 54 12508 14322 9868 4274 1317 -2243 N ATOM 2997 CA LEU B 54 -109.621 -7.806 184.694 1.00 99.10 C ANISOU 2997 CA LEU B 54 13052 14136 10465 4166 1104 -2269 C ATOM 2998 C LEU B 54 -108.275 -7.593 185.376 1.00 99.65 C ANISOU 2998 C LEU B 54 13383 14070 10409 3983 958 -2389 C ATOM 2999 O LEU B 54 -108.199 -6.979 186.445 1.00104.53 O ANISOU 2999 O LEU B 54 14145 14811 10760 4101 995 -2644 O ATOM 3000 CB LEU B 54 -110.098 -6.508 184.044 1.00103.75 C ANISOU 3000 CB LEU B 54 13785 14430 11205 4476 1089 -2508 C ATOM 3001 CG LEU B 54 -111.289 -6.603 183.088 1.00106.00 C ANISOU 3001 CG LEU B 54 13823 14781 11672 4665 1176 -2389 C ATOM 3002 CD1 LEU B 54 -111.993 -5.260 182.979 1.00114.16 C ANISOU 3002 CD1 LEU B 54 14991 15672 12712 5085 1218 -2678 C ATOM 3003 CD2 LEU B 54 -110.849 -7.087 181.715 1.00 99.87 C ANISOU 3003 CD2 LEU B 54 13009 13715 11220 4447 1037 -2145 C ATOM 3004 N HIS B 55 -107.214 -8.104 184.760 1.00 94.54 N ANISOU 3004 N HIS B 55 12785 13194 9944 3698 791 -2216 N ATOM 3005 CA HIS B 55 -105.872 -7.785 185.218 1.00 96.42 C ANISOU 3005 CA HIS B 55 13258 13275 10104 3523 624 -2349 C ATOM 3006 C HIS B 55 -105.571 -6.311 184.948 1.00102.40 C ANISOU 3006 C HIS B 55 14314 13646 10947 3648 540 -2681 C ATOM 3007 O HIS B 55 -106.268 -5.636 184.186 1.00105.39 O ANISOU 3007 O HIS B 55 14730 13813 11502 3852 582 -2750 O ATOM 3008 CB HIS B 55 -104.850 -8.690 184.523 1.00 88.90 C ANISOU 3008 CB HIS B 55 12253 12182 9343 3211 473 -2083 C ATOM 3009 CG HIS B 55 -103.431 -8.438 184.930 1.00 84.45 C ANISOU 3009 CG HIS B 55 11879 11500 8707 3017 292 -2203 C ATOM 3010 ND1 HIS B 55 -103.036 -8.363 186.248 1.00 87.53 N ANISOU 3010 ND1 HIS B 55 12345 12147 8766 3008 281 -2347 N ATOM 3011 CD2 HIS B 55 -102.313 -8.241 184.191 1.00 81.55 C ANISOU 3011 CD2 HIS B 55 11623 10819 8543 2816 113 -2208 C ATOM 3012 CE1 HIS B 55 -101.737 -8.132 186.304 1.00 87.68 C ANISOU 3012 CE1 HIS B 55 12503 12021 8790 2810 94 -2439 C ATOM 3013 NE2 HIS B 55 -101.274 -8.053 185.070 1.00 83.57 N ANISOU 3013 NE2 HIS B 55 12001 11157 8596 2687 -5 -2358 N ATOM 3014 N SER B 56 -104.523 -5.807 185.594 1.00103.15 N ANISOU 3014 N SER B 56 14632 13653 10907 3522 418 -2889 N ATOM 3015 CA SER B 56 -104.095 -4.435 185.357 1.00110.97 C ANISOU 3015 CA SER B 56 15944 14238 11981 3574 329 -3206 C ATOM 3016 C SER B 56 -103.562 -4.282 183.938 1.00112.15 C ANISOU 3016 C SER B 56 16159 13963 12490 3421 204 -3083 C ATOM 3017 O SER B 56 -102.705 -5.054 183.497 1.00113.09 O ANISOU 3017 O SER B 56 16180 14066 12721 3143 92 -2871 O ATOM 3018 CB SER B 56 -103.028 -4.030 186.373 1.00121.20 C ANISOU 3018 CB SER B 56 17439 15569 13041 3413 216 -3451 C ATOM 3019 OG SER B 56 -103.557 -4.005 187.687 1.00128.21 O ANISOU 3019 OG SER B 56 18306 16835 13572 3580 336 -3607 O ATOM 3020 N GLY B 57 -104.073 -3.282 183.224 1.00114.06 N ANISOU 3020 N GLY B 57 16571 13865 12901 3619 226 -3215 N ATOM 3021 CA GLY B 57 -103.561 -2.950 181.910 1.00104.43 C ANISOU 3021 CA GLY B 57 15469 12218 11994 3485 112 -3130 C ATOM 3022 C GLY B 57 -104.183 -3.695 180.752 1.00 97.42 C ANISOU 3022 C GLY B 57 14336 11342 11338 3516 148 -2810 C ATOM 3023 O GLY B 57 -103.580 -3.742 179.674 1.00 94.90 O ANISOU 3023 O GLY B 57 14057 10745 11254 3330 42 -2679 O ATOM 3024 N VAL B 58 -105.367 -4.274 180.928 1.00 96.27 N ANISOU 3024 N VAL B 58 13931 11523 11122 3729 295 -2690 N ATOM 3025 CA VAL B 58 -106.071 -4.932 179.828 1.00 92.44 C ANISOU 3025 CA VAL B 58 13207 11070 10846 3766 333 -2415 C ATOM 3026 C VAL B 58 -107.358 -4.168 179.539 1.00 89.08 C ANISOU 3026 C VAL B 58 12781 10616 10447 4161 440 -2519 C ATOM 3027 O VAL B 58 -107.997 -3.653 180.470 1.00 89.24 O ANISOU 3027 O VAL B 58 12838 10809 10262 4419 549 -2731 O ATOM 3028 CB VAL B 58 -106.344 -6.414 180.140 1.00 96.20 C ANISOU 3028 CB VAL B 58 13341 11967 11243 3629 407 -2147 C ATOM 3029 CG1 VAL B 58 -105.036 -7.154 180.383 1.00 92.32 C ANISOU 3029 CG1 VAL B 58 12864 11482 10731 3282 287 -2038 C ATOM 3030 CG2 VAL B 58 -107.268 -6.557 181.336 1.00105.69 C ANISOU 3030 CG2 VAL B 58 14410 13585 12163 3831 577 -2232 C ATOM 3031 N PRO B 59 -107.766 -4.048 178.278 1.00 88.57 N ANISOU 3031 N PRO B 59 12678 10355 10618 4238 409 -2384 N ATOM 3032 CA PRO B 59 -108.916 -3.199 177.946 1.00 94.60 C ANISOU 3032 CA PRO B 59 13470 11062 11413 4649 483 -2493 C ATOM 3033 C PRO B 59 -110.231 -3.849 178.349 1.00 94.14 C ANISOU 3033 C PRO B 59 13040 11503 11228 4860 652 -2418 C ATOM 3034 O PRO B 59 -110.317 -5.043 178.643 1.00 93.74 O ANISOU 3034 O PRO B 59 12705 11803 11112 4657 710 -2228 O ATOM 3035 CB PRO B 59 -108.812 -3.039 176.427 1.00 92.84 C ANISOU 3035 CB PRO B 59 13276 10523 11475 4551 374 -2298 C ATOM 3036 CG PRO B 59 -108.096 -4.264 175.974 1.00 84.50 C ANISOU 3036 CG PRO B 59 12052 9544 10510 4214 312 -2064 C ATOM 3037 CD PRO B 59 -107.142 -4.634 177.078 1.00 84.08 C ANISOU 3037 CD PRO B 59 12055 9601 10291 3965 295 -2139 C ATOM 3038 N SER B 60 -111.277 -3.023 178.358 1.00 92.77 N ANISOU 3038 N SER B 60 12839 11365 11044 5108 715 -2491 N ATOM 3039 CA SER B 60 -112.602 -3.447 178.794 1.00 92.05 C ANISOU 3039 CA SER B 60 12398 11756 10820 5309 877 -2454 C ATOM 3040 C SER B 60 -113.363 -4.234 177.736 1.00 92.12 C ANISOU 3040 C SER B 60 12069 11947 10985 5291 888 -2194 C ATOM 3041 O SER B 60 -114.485 -4.675 178.011 1.00 92.51 O ANISOU 3041 O SER B 60 11789 12425 10936 5412 1021 -2146 O ATOM 3042 CB SER B 60 -113.427 -2.227 179.215 1.00 94.72 C ANISOU 3042 CB SER B 60 12832 12066 11092 5577 927 -2639 C ATOM 3043 OG SER B 60 -114.688 -2.616 179.732 1.00 98.27 O ANISOU 3043 OG SER B 60 12937 13009 11393 5760 1087 -2625 O ATOM 3044 N ARG B 61 -112.800 -4.409 176.537 1.00 90.43 N ANISOU 3044 N ARG B 61 11922 11437 11002 5123 752 -2032 N ATOM 3045 CA ARG B 61 -113.421 -5.294 175.557 1.00 90.05 C ANISOU 3045 CA ARG B 61 11547 11582 11086 5063 757 -1790 C ATOM 3046 C ARG B 61 -113.557 -6.713 176.091 1.00 91.20 C ANISOU 3046 C ARG B 61 11372 12162 11119 4927 878 -1668 C ATOM 3047 O ARG B 61 -114.494 -7.430 175.721 1.00 93.47 O ANISOU 3047 O ARG B 61 11306 12783 11426 4931 956 -1523 O ATOM 3048 CB ARG B 61 -112.611 -5.302 174.261 1.00 86.59 C ANISOU 3048 CB ARG B 61 11262 10749 10891 4863 590 -1645 C ATOM 3049 CG ARG B 61 -112.292 -3.927 173.710 1.00 91.65 C ANISOU 3049 CG ARG B 61 12248 10935 11640 4903 477 -1725 C ATOM 3050 CD ARG B 61 -111.675 -4.034 172.329 1.00 93.21 C ANISOU 3050 CD ARG B 61 12527 10831 12060 4690 339 -1543 C ATOM 3051 NE ARG B 61 -110.429 -4.795 172.350 1.00 91.03 N ANISOU 3051 NE ARG B 61 12329 10432 11826 4421 279 -1495 N ATOM 3052 CZ ARG B 61 -109.227 -4.254 172.508 1.00 90.21 C ANISOU 3052 CZ ARG B 61 12554 9978 11744 4260 194 -1596 C ATOM 3053 NH1 ARG B 61 -109.104 -2.943 172.665 1.00 93.19 N ANISOU 3053 NH1 ARG B 61 13218 10081 12110 4327 170 -1746 N ATOM 3054 NH2 ARG B 61 -108.146 -5.022 172.515 1.00 85.74 N ANISOU 3054 NH2 ARG B 61 12015 9350 11213 3999 132 -1538 N ATOM 3055 N PHE B 62 -112.645 -7.129 176.964 1.00 91.41 N ANISOU 3055 N PHE B 62 11515 12184 11031 4668 876 -1676 N ATOM 3056 CA PHE B 62 -112.639 -8.482 177.498 1.00 92.92 C ANISOU 3056 CA PHE B 62 11461 12719 11126 4375 960 -1486 C ATOM 3057 C PHE B 62 -113.551 -8.586 178.712 1.00 94.27 C ANISOU 3057 C PHE B 62 11444 13352 11024 4542 1158 -1582 C ATOM 3058 O PHE B 62 -113.651 -7.654 179.515 1.00 95.21 O ANISOU 3058 O PHE B 62 11725 13474 10978 4799 1205 -1834 O ATOM 3059 CB PHE B 62 -111.218 -8.910 177.869 1.00 91.54 C ANISOU 3059 CB PHE B 62 11492 12348 10942 4044 856 -1432 C ATOM 3060 CG PHE B 62 -110.260 -8.886 176.714 1.00 88.49 C ANISOU 3060 CG PHE B 62 11264 11550 10809 3850 677 -1336 C ATOM 3061 CD1 PHE B 62 -109.484 -7.768 176.461 1.00 91.65 C ANISOU 3061 CD1 PHE B 62 11997 11544 11280 3913 554 -1508 C ATOM 3062 CD2 PHE B 62 -110.142 -9.982 175.876 1.00 82.00 C ANISOU 3062 CD2 PHE B 62 10263 10747 10145 3595 641 -1080 C ATOM 3063 CE1 PHE B 62 -108.604 -7.745 175.395 1.00 90.19 C ANISOU 3063 CE1 PHE B 62 11946 11009 11313 3718 405 -1415 C ATOM 3064 CE2 PHE B 62 -109.264 -9.966 174.809 1.00 81.88 C ANISOU 3064 CE2 PHE B 62 10383 10382 10346 3425 489 -1001 C ATOM 3065 CZ PHE B 62 -108.494 -8.846 174.568 1.00 85.71 C ANISOU 3065 CZ PHE B 62 11181 10493 10893 3484 374 -1163 C ATOM 3066 N SER B 63 -114.217 -9.730 178.834 1.00 94.16 N ANISOU 3066 N SER B 63 11095 13726 10956 4381 1280 -1385 N ATOM 3067 CA SER B 63 -115.081 -9.995 179.974 1.00 95.92 C ANISOU 3067 CA SER B 63 11105 14435 10905 4476 1489 -1434 C ATOM 3068 C SER B 63 -115.218 -11.500 180.139 1.00 93.20 C ANISOU 3068 C SER B 63 10513 14376 10522 4114 1578 -1151 C ATOM 3069 O SER B 63 -115.375 -12.225 179.156 1.00 91.90 O ANISOU 3069 O SER B 63 10190 14170 10556 3925 1534 -952 O ATOM 3070 CB SER B 63 -116.460 -9.349 179.795 1.00 94.10 C ANISOU 3070 CB SER B 63 10644 14469 10641 4864 1605 -1571 C ATOM 3071 OG SER B 63 -117.084 -9.799 178.604 1.00 85.69 O ANISOU 3071 OG SER B 63 9323 13452 9781 4817 1574 -1404 O ATOM 3072 N GLY B 64 -115.156 -11.965 181.381 1.00 94.11 N ANISOU 3072 N GLY B 64 10614 14769 10373 4015 1702 -1134 N ATOM 3073 CA GLY B 64 -115.333 -13.382 181.619 1.00 95.21 C ANISOU 3073 CA GLY B 64 10552 15168 10456 3677 1804 -856 C ATOM 3074 C GLY B 64 -116.658 -13.702 182.273 1.00103.15 C ANISOU 3074 C GLY B 64 11224 16721 11246 3746 2052 -848 C ATOM 3075 O GLY B 64 -117.257 -12.848 182.934 1.00105.05 O ANISOU 3075 O GLY B 64 11429 17186 11300 4062 2160 -1080 O ATOM 3076 N SER B 65 -117.127 -14.933 182.092 1.00104.17 N ANISOU 3076 N SER B 65 11109 17071 11399 3443 2151 -589 N ATOM 3077 CA SER B 65 -118.339 -15.391 182.753 1.00109.76 C ANISOU 3077 CA SER B 65 11485 18329 11889 3425 2404 -547 C ATOM 3078 C SER B 65 -118.275 -16.904 182.885 1.00112.09 C ANISOU 3078 C SER B 65 11692 18729 12167 2974 2483 -221 C ATOM 3079 O SER B 65 -117.394 -17.559 182.326 1.00112.18 O ANISOU 3079 O SER B 65 11873 18384 12364 2723 2336 -43 O ATOM 3080 CB SER B 65 -119.594 -14.962 181.986 1.00110.91 C ANISOU 3080 CB SER B 65 11292 18711 12137 3646 2468 -648 C ATOM 3081 OG SER B 65 -119.576 -15.461 180.660 1.00107.56 O ANISOU 3081 OG SER B 65 10782 18074 12013 3464 2342 -497 O ATOM 3082 N GLY B 66 -119.225 -17.456 183.631 1.00117.13 N ANISOU 3082 N GLY B 66 12070 19859 12576 2875 2727 -145 N ATOM 3083 CA GLY B 66 -119.309 -18.896 183.749 1.00114.92 C ANISOU 3083 CA GLY B 66 11706 19684 12275 2436 2827 172 C ATOM 3084 C GLY B 66 -119.609 -19.390 185.147 1.00120.65 C ANISOU 3084 C GLY B 66 12397 20809 12634 2318 3055 266 C ATOM 3085 O GLY B 66 -119.544 -18.631 186.117 1.00124.23 O ANISOU 3085 O GLY B 66 12940 21430 12831 2573 3113 80 O ATOM 3086 N SER B 67 -119.949 -20.671 185.248 1.00122.63 N ANISOU 3086 N SER B 67 12532 21212 12852 1922 3190 554 N ATOM 3087 CA SER B 67 -120.237 -21.308 186.525 1.00124.56 C ANISOU 3087 CA SER B 67 12756 21824 12746 1745 3418 705 C ATOM 3088 C SER B 67 -120.127 -22.814 186.340 1.00121.79 C ANISOU 3088 C SER B 67 12440 21366 12470 1262 3467 1073 C ATOM 3089 O SER B 67 -120.086 -23.322 185.215 1.00124.21 O ANISOU 3089 O SER B 67 12704 21405 13086 1077 3361 1170 O ATOM 3090 CB SER B 67 -121.621 -20.915 187.053 1.00134.05 C ANISOU 3090 CB SER B 67 13575 23643 13715 1882 3685 559 C ATOM 3091 OG SER B 67 -122.644 -21.334 186.167 1.00139.77 O ANISOU 3091 OG SER B 67 13930 24559 14619 1720 3767 610 O ATOM 3092 N GLY B 68 -120.070 -23.523 187.467 1.00122.64 N ANISOU 3092 N GLY B 68 12647 21674 12278 1062 3628 1278 N ATOM 3093 CA GLY B 68 -119.971 -24.968 187.444 1.00118.97 C ANISOU 3093 CA GLY B 68 12263 21096 11845 608 3696 1644 C ATOM 3094 C GLY B 68 -118.777 -25.449 186.650 1.00115.15 C ANISOU 3094 C GLY B 68 12087 20005 11659 509 3432 1776 C ATOM 3095 O GLY B 68 -117.629 -25.307 187.081 1.00117.12 O ANISOU 3095 O GLY B 68 12662 19990 11849 629 3274 1796 O ATOM 3096 N THR B 69 -119.044 -26.024 185.478 1.00110.44 N ANISOU 3096 N THR B 69 11376 19209 11376 289 3384 1854 N ATOM 3097 CA THR B 69 -117.997 -26.514 184.596 1.00105.18 C ANISOU 3097 CA THR B 69 10967 17986 11012 192 3148 1962 C ATOM 3098 C THR B 69 -117.845 -25.692 183.325 1.00 98.46 C ANISOU 3098 C THR B 69 10035 16898 10477 407 2943 1723 C ATOM 3099 O THR B 69 -116.854 -25.874 182.610 1.00 98.46 O ANISOU 3099 O THR B 69 10258 16442 10712 394 2729 1762 O ATOM 3100 CB THR B 69 -118.266 -27.977 184.209 1.00108.26 C ANISOU 3100 CB THR B 69 11363 18254 11517 -269 3240 2267 C ATOM 3101 OG1 THR B 69 -119.373 -28.036 183.302 1.00108.54 O ANISOU 3101 OG1 THR B 69 11042 18477 11722 -409 3322 2184 O ATOM 3102 CG2 THR B 69 -118.588 -28.804 185.443 1.00113.19 C ANISOU 3102 CG2 THR B 69 12051 19141 11814 -513 3476 2527 C ATOM 3103 N ASP B 70 -118.780 -24.793 183.028 1.00 94.30 N ANISOU 3103 N ASP B 70 9203 16673 9955 618 3001 1482 N ATOM 3104 CA ASP B 70 -118.800 -24.070 181.763 1.00 91.76 C ANISOU 3104 CA ASP B 70 8783 16157 9923 806 2824 1284 C ATOM 3105 C ASP B 70 -118.413 -22.619 181.999 1.00 88.27 C ANISOU 3105 C ASP B 70 8436 15680 9422 1258 2711 999 C ATOM 3106 O ASP B 70 -119.040 -21.935 182.814 1.00 84.07 O ANISOU 3106 O ASP B 70 7773 15522 8649 1477 2852 846 O ATOM 3107 CB ASP B 70 -120.185 -24.144 181.115 1.00 99.99 C ANISOU 3107 CB ASP B 70 9401 17556 11035 721 2955 1229 C ATOM 3108 CG ASP B 70 -120.621 -25.566 180.834 1.00106.15 C ANISOU 3108 CG ASP B 70 10084 18367 11881 234 3071 1488 C ATOM 3109 OD1 ASP B 70 -119.778 -26.369 180.380 1.00105.59 O ANISOU 3109 OD1 ASP B 70 10270 17865 11983 12 2950 1660 O ATOM 3110 OD2 ASP B 70 -121.806 -25.882 181.071 1.00109.88 O ANISOU 3110 OD2 ASP B 70 10223 19296 12230 68 3289 1511 O ATOM 3111 N TYR B 71 -117.398 -22.145 181.277 1.00 91.36 N ANISOU 3111 N TYR B 71 9059 15624 10031 1391 2466 919 N ATOM 3112 CA TYR B 71 -116.951 -20.767 181.406 1.00 89.82 C ANISOU 3112 CA TYR B 71 8997 15323 9809 1783 2344 649 C ATOM 3113 C TYR B 71 -116.650 -20.219 180.020 1.00 84.95 C ANISOU 3113 C TYR B 71 8406 14362 9510 1896 2138 541 C ATOM 3114 O TYR B 71 -116.533 -20.967 179.047 1.00 78.15 O ANISOU 3114 O TYR B 71 7514 13304 8876 1664 2066 684 O ATOM 3115 CB TYR B 71 -115.726 -20.665 182.322 1.00 87.00 C ANISOU 3115 CB TYR B 71 8985 14774 9300 1821 2256 663 C ATOM 3116 CG TYR B 71 -115.954 -21.263 183.694 1.00 93.32 C ANISOU 3116 CG TYR B 71 9788 15907 9761 1701 2449 799 C ATOM 3117 CD1 TYR B 71 -115.787 -22.623 183.919 1.00 92.80 C ANISOU 3117 CD1 TYR B 71 9776 15816 9666 1349 2516 1114 C ATOM 3118 CD2 TYR B 71 -116.362 -20.472 184.757 1.00 98.72 C ANISOU 3118 CD2 TYR B 71 10435 16928 10146 1942 2573 615 C ATOM 3119 CE1 TYR B 71 -116.011 -23.172 185.164 1.00 94.07 C ANISOU 3119 CE1 TYR B 71 9959 16280 9503 1234 2697 1262 C ATOM 3120 CE2 TYR B 71 -116.582 -21.011 186.008 1.00 95.94 C ANISOU 3120 CE2 TYR B 71 10087 16907 9460 1829 2757 744 C ATOM 3121 CZ TYR B 71 -116.404 -22.361 186.207 1.00 92.08 C ANISOU 3121 CZ TYR B 71 9656 16388 8941 1470 2818 1080 C ATOM 3122 OH TYR B 71 -116.620 -22.904 187.453 1.00 91.48 O ANISOU 3122 OH TYR B 71 9605 16635 8516 1351 3005 1234 O ATOM 3123 N SER B 72 -116.526 -18.897 179.930 1.00 85.13 N ANISOU 3123 N SER B 72 8502 14303 9539 2254 2047 285 N ATOM 3124 CA SER B 72 -116.403 -18.268 178.625 1.00 84.07 C ANISOU 3124 CA SER B 72 8378 13886 9678 2390 1874 183 C ATOM 3125 C SER B 72 -115.725 -16.911 178.750 1.00 85.50 C ANISOU 3125 C SER B 72 8815 13821 9852 2720 1740 -57 C ATOM 3126 O SER B 72 -115.960 -16.167 179.708 1.00 90.65 O ANISOU 3126 O SER B 72 9499 14659 10283 2957 1825 -230 O ATOM 3127 CB SER B 72 -117.773 -18.105 177.958 1.00 86.09 C ANISOU 3127 CB SER B 72 8268 14450 9990 2488 1963 126 C ATOM 3128 OG SER B 72 -118.511 -17.056 178.561 1.00 89.65 O ANISOU 3128 OG SER B 72 8611 15188 10265 2854 2061 -97 O ATOM 3129 N LEU B 73 -114.884 -16.610 177.767 1.00 81.68 N ANISOU 3129 N LEU B 73 8517 12914 9603 2716 1538 -71 N ATOM 3130 CA LEU B 73 -114.285 -15.300 177.573 1.00 87.20 C ANISOU 3130 CA LEU B 73 9457 13322 10355 2992 1396 -290 C ATOM 3131 C LEU B 73 -115.008 -14.609 176.424 1.00 90.41 C ANISOU 3131 C LEU B 73 9735 13682 10934 3204 1343 -378 C ATOM 3132 O LEU B 73 -115.452 -15.258 175.475 1.00 97.23 O ANISOU 3132 O LEU B 73 10402 14585 11954 3056 1330 -242 O ATOM 3133 CB LEU B 73 -112.789 -15.424 177.273 1.00 90.11 C ANISOU 3133 CB LEU B 73 10124 13262 10852 2823 1209 -236 C ATOM 3134 CG LEU B 73 -111.993 -14.171 176.900 1.00 89.18 C ANISOU 3134 CG LEU B 73 10281 12777 10825 3014 1045 -433 C ATOM 3135 CD1 LEU B 73 -112.133 -13.099 177.966 1.00 97.40 C ANISOU 3135 CD1 LEU B 73 11446 13915 11647 3292 1102 -678 C ATOM 3136 CD2 LEU B 73 -110.530 -14.521 176.676 1.00 76.00 C ANISOU 3136 CD2 LEU B 73 8842 10774 9262 2786 885 -352 C ATOM 3137 N THR B 74 -115.125 -13.286 176.507 1.00 87.43 N ANISOU 3137 N THR B 74 9483 13215 10523 3559 1307 -609 N ATOM 3138 CA THR B 74 -115.913 -12.538 175.536 1.00 89.30 C ANISOU 3138 CA THR B 74 9604 13442 10885 3831 1266 -696 C ATOM 3139 C THR B 74 -115.216 -11.231 175.201 1.00 94.38 C ANISOU 3139 C THR B 74 10590 13658 11611 4074 1115 -873 C ATOM 3140 O THR B 74 -114.917 -10.433 176.096 1.00 96.74 O ANISOU 3140 O THR B 74 11098 13894 11765 4254 1137 -1062 O ATOM 3141 CB THR B 74 -117.324 -12.266 176.069 1.00 87.37 C ANISOU 3141 CB THR B 74 9054 13676 10468 4100 1447 -802 C ATOM 3142 OG1 THR B 74 -118.093 -13.474 176.026 1.00 89.95 O ANISOU 3142 OG1 THR B 74 9022 14385 10768 3840 1574 -619 O ATOM 3143 CG2 THR B 74 -118.017 -11.199 175.235 1.00 84.07 C ANISOU 3143 CG2 THR B 74 8587 13210 10147 4492 1382 -940 C ATOM 3144 N ILE B 75 -114.951 -11.031 173.915 1.00 93.41 N ANISOU 3144 N ILE B 75 10536 13244 11712 4058 966 -813 N ATOM 3145 CA ILE B 75 -114.439 -9.775 173.385 1.00 90.21 C ANISOU 3145 CA ILE B 75 10443 12426 11406 4283 828 -953 C ATOM 3146 C ILE B 75 -115.607 -9.055 172.725 1.00105.10 C ANISOU 3146 C ILE B 75 12176 14432 13326 4657 837 -1021 C ATOM 3147 O ILE B 75 -116.211 -9.578 171.779 1.00107.70 O ANISOU 3147 O ILE B 75 12257 14900 13763 4584 811 -880 O ATOM 3148 CB ILE B 75 -113.296 -10.009 172.386 1.00 78.94 C ANISOU 3148 CB ILE B 75 9213 10594 10186 4013 657 -828 C ATOM 3149 CG1 ILE B 75 -112.273 -10.990 172.961 1.00 77.55 C ANISOU 3149 CG1 ILE B 75 9095 10389 9979 3640 654 -721 C ATOM 3150 CG2 ILE B 75 -112.624 -8.692 172.028 1.00 79.78 C ANISOU 3150 CG2 ILE B 75 9691 10256 10365 4192 532 -975 C ATOM 3151 CD1 ILE B 75 -111.156 -11.339 172.000 1.00 73.45 C ANISOU 3151 CD1 ILE B 75 8724 9528 9656 3370 502 -599 C ATOM 3152 N SER B 76 -115.934 -7.865 173.234 1.00113.60 N ANISOU 3152 N SER B 76 13429 15423 14311 4902 845 -1208 N ATOM 3153 CA SER B 76 -117.075 -7.113 172.718 1.00115.80 C ANISOU 3153 CA SER B 76 13610 15778 14612 5108 827 -1236 C ATOM 3154 C SER B 76 -116.877 -6.768 171.247 1.00116.17 C ANISOU 3154 C SER B 76 13770 15501 14868 5054 657 -1120 C ATOM 3155 O SER B 76 -117.663 -7.177 170.385 1.00122.42 O ANISOU 3155 O SER B 76 14298 16490 15726 5034 635 -1000 O ATOM 3156 CB SER B 76 -117.285 -5.848 173.550 1.00121.38 C ANISOU 3156 CB SER B 76 14543 16382 15194 5374 858 -1455 C ATOM 3157 OG SER B 76 -116.112 -5.054 173.573 1.00124.64 O ANISOU 3157 OG SER B 76 15388 16305 15665 5339 753 -1546 O ATOM 3158 N ASN B 77 -115.833 -6.005 170.944 1.00109.99 N ANISOU 3158 N ASN B 77 13377 14236 14176 5012 540 -1159 N ATOM 3159 CA ASN B 77 -115.437 -5.718 169.575 1.00102.24 C ANISOU 3159 CA ASN B 77 12536 12930 13378 4909 390 -1036 C ATOM 3160 C ASN B 77 -114.017 -6.223 169.364 1.00 93.94 C ANISOU 3160 C ASN B 77 11675 11593 12425 4625 316 -970 C ATOM 3161 O ASN B 77 -113.141 -6.016 170.209 1.00 96.87 O ANISOU 3161 O ASN B 77 12273 11798 12736 4578 328 -1085 O ATOM 3162 CB ASN B 77 -115.538 -4.219 169.268 1.00108.19 C ANISOU 3162 CB ASN B 77 13587 13364 14157 5103 321 -1122 C ATOM 3163 CG ASN B 77 -114.636 -3.379 170.148 1.00114.10 C ANISOU 3163 CG ASN B 77 14706 13796 14851 5114 324 -1296 C ATOM 3164 OD1 ASN B 77 -113.470 -3.158 169.830 1.00112.43 O ANISOU 3164 OD1 ASN B 77 14770 13216 14730 4912 239 -1280 O ATOM 3165 ND2 ASN B 77 -115.176 -2.901 171.263 1.00118.33 N ANISOU 3165 ND2 ASN B 77 15242 14488 15230 5335 425 -1474 N ATOM 3166 N LEU B 78 -113.798 -6.894 168.237 1.00 86.90 N ANISOU 3166 N LEU B 78 10685 10659 11673 4436 236 -796 N ATOM 3167 CA LEU B 78 -112.506 -7.492 167.927 1.00 82.94 C ANISOU 3167 CA LEU B 78 10322 9919 11272 4161 163 -716 C ATOM 3168 C LEU B 78 -111.601 -6.473 167.246 1.00 84.64 C ANISOU 3168 C LEU B 78 10907 9666 11588 4071 45 -727 C ATOM 3169 O LEU B 78 -111.915 -5.983 166.155 1.00 86.78 O ANISOU 3169 O LEU B 78 11205 9826 11941 4091 -23 -644 O ATOM 3170 CB LEU B 78 -112.681 -8.725 167.043 1.00 86.08 C ANISOU 3170 CB LEU B 78 10438 10500 11767 3990 141 -530 C ATOM 3171 CG LEU B 78 -111.389 -9.470 166.707 1.00 87.78 C ANISOU 3171 CG LEU B 78 10765 10501 12086 3658 71 -432 C ATOM 3172 CD1 LEU B 78 -110.821 -10.142 167.949 1.00 83.74 C ANISOU 3172 CD1 LEU B 78 10245 10096 11478 3451 150 -457 C ATOM 3173 CD2 LEU B 78 -111.621 -10.485 165.600 1.00 91.16 C ANISOU 3173 CD2 LEU B 78 10957 11054 12624 3450 34 -253 C ATOM 3174 N GLU B 79 -110.483 -6.159 167.888 1.00 84.91 N ANISOU 3174 N GLU B 79 11213 9449 11602 3963 25 -829 N ATOM 3175 CA GLU B 79 -109.424 -5.352 167.308 1.00 86.22 C ANISOU 3175 CA GLU B 79 11707 9192 11858 3793 -72 -833 C ATOM 3176 C GLU B 79 -108.319 -6.250 166.772 1.00 87.99 C ANISOU 3176 C GLU B 79 11934 9312 12187 3484 -142 -717 C ATOM 3177 O GLU B 79 -108.193 -7.408 167.181 1.00 89.65 O ANISOU 3177 O GLU B 79 11960 9724 12378 3422 -117 -676 O ATOM 3178 CB GLU B 79 -108.859 -4.387 168.358 1.00 88.41 C ANISOU 3178 CB GLU B 79 12283 9268 12043 3841 -55 -1042 C ATOM 3179 CG GLU B 79 -109.878 -3.405 168.917 1.00 95.53 C ANISOU 3179 CG GLU B 79 13219 10235 12841 4152 12 -1176 C ATOM 3180 CD GLU B 79 -110.511 -2.547 167.836 1.00104.06 C ANISOU 3180 CD GLU B 79 14350 11184 14005 4265 -30 -1091 C ATOM 3181 OE1 GLU B 79 -109.802 -2.180 166.874 1.00106.72 O ANISOU 3181 OE1 GLU B 79 14861 11231 14456 4081 -111 -997 O ATOM 3182 OE2 GLU B 79 -111.715 -2.235 167.945 1.00107.54 O ANISOU 3182 OE2 GLU B 79 14649 11826 14384 4543 20 -1117 O ATOM 3183 N PRO B 80 -107.498 -5.756 165.839 1.00 89.95 N ANISOU 3183 N PRO B 80 12380 9258 12540 3286 -222 -654 N ATOM 3184 CA PRO B 80 -106.449 -6.621 165.270 1.00 86.19 C ANISOU 3184 CA PRO B 80 11886 8704 12159 2987 -285 -546 C ATOM 3185 C PRO B 80 -105.414 -7.075 166.285 1.00 81.61 C ANISOU 3185 C PRO B 80 11388 8084 11535 2854 -302 -647 C ATOM 3186 O PRO B 80 -104.838 -8.158 166.121 1.00 76.07 O ANISOU 3186 O PRO B 80 10539 7482 10882 2616 -322 -543 O ATOM 3187 CB PRO B 80 -105.826 -5.740 164.177 1.00 88.25 C ANISOU 3187 CB PRO B 80 12360 8668 12502 2828 -338 -486 C ATOM 3188 CG PRO B 80 -106.148 -4.342 164.586 1.00 94.14 C ANISOU 3188 CG PRO B 80 13327 9254 13189 3003 -314 -614 C ATOM 3189 CD PRO B 80 -107.507 -4.423 165.211 1.00 95.52 C ANISOU 3189 CD PRO B 80 13318 9699 13277 3324 -250 -666 C ATOM 3190 N GLU B 81 -105.153 -6.280 167.326 1.00 84.33 N ANISOU 3190 N GLU B 81 11935 8332 11776 2935 -284 -836 N ATOM 3191 CA GLU B 81 -104.220 -6.699 168.366 1.00 80.78 C ANISOU 3191 CA GLU B 81 11510 7937 11246 2747 -290 -922 C ATOM 3192 C GLU B 81 -104.697 -7.944 169.103 1.00 79.28 C ANISOU 3192 C GLU B 81 11005 8149 10967 2721 -208 -841 C ATOM 3193 O GLU B 81 -103.874 -8.660 169.684 1.00 83.32 O ANISOU 3193 O GLU B 81 11464 8757 11435 2499 -223 -819 O ATOM 3194 CB GLU B 81 -103.990 -5.562 169.365 1.00 92.30 C ANISOU 3194 CB GLU B 81 13247 9237 12586 2864 -284 -1167 C ATOM 3195 CG GLU B 81 -103.278 -4.343 168.792 1.00105.98 C ANISOU 3195 CG GLU B 81 15297 10580 14390 2746 -346 -1234 C ATOM 3196 CD GLU B 81 -104.195 -3.450 167.977 1.00117.26 C ANISOU 3196 CD GLU B 81 16754 11928 15870 2897 -304 -1161 C ATOM 3197 OE1 GLU B 81 -105.424 -3.671 168.005 1.00120.54 O ANISOU 3197 OE1 GLU B 81 16978 12568 16252 3156 -243 -1116 O ATOM 3198 OE2 GLU B 81 -103.686 -2.525 167.308 1.00121.35 O ANISOU 3198 OE2 GLU B 81 17478 12174 16458 2758 -332 -1148 O ATOM 3199 N ASP B 82 -106.001 -8.216 169.093 1.00 79.17 N ANISOU 3199 N ASP B 82 10782 8378 10920 2940 -123 -789 N ATOM 3200 CA ASP B 82 -106.571 -9.343 169.821 1.00 76.59 C ANISOU 3200 CA ASP B 82 10170 8434 10497 2908 -25 -709 C ATOM 3201 C ASP B 82 -106.477 -10.662 169.064 1.00 66.14 C ANISOU 3201 C ASP B 82 8621 7223 9286 2671 -36 -492 C ATOM 3202 O ASP B 82 -106.965 -11.679 169.569 1.00 65.52 O ANISOU 3202 O ASP B 82 8317 7436 9143 2611 50 -401 O ATOM 3203 CB ASP B 82 -108.034 -9.052 170.168 1.00 82.77 C ANISOU 3203 CB ASP B 82 10801 9463 11184 3229 85 -763 C ATOM 3204 CG ASP B 82 -108.212 -7.720 170.868 1.00 92.77 C ANISOU 3204 CG ASP B 82 12303 10603 12341 3509 104 -996 C ATOM 3205 OD1 ASP B 82 -107.216 -7.193 171.406 1.00 95.52 O ANISOU 3205 OD1 ASP B 82 12908 10739 12647 3411 52 -1125 O ATOM 3206 OD2 ASP B 82 -109.347 -7.199 170.881 1.00 99.41 O ANISOU 3206 OD2 ASP B 82 13071 11564 13136 3831 169 -1061 O ATOM 3207 N ILE B 83 -105.869 -10.678 167.881 1.00 57.02 N ANISOU 3207 N ILE B 83 7534 5844 8289 2528 -131 -412 N ATOM 3208 CA ILE B 83 -105.668 -11.920 167.140 1.00 56.95 C ANISOU 3208 CA ILE B 83 7341 5911 8386 2298 -146 -232 C ATOM 3209 C ILE B 83 -104.510 -12.669 167.793 1.00 58.87 C ANISOU 3209 C ILE B 83 7610 6154 8602 2059 -168 -205 C ATOM 3210 O ILE B 83 -103.345 -12.302 167.625 1.00 64.08 O ANISOU 3210 O ILE B 83 8442 6600 9304 1931 -254 -254 O ATOM 3211 CB ILE B 83 -105.398 -11.655 165.656 1.00 53.80 C ANISOU 3211 CB ILE B 83 7008 5292 8142 2239 -236 -168 C ATOM 3212 CG1 ILE B 83 -106.597 -10.952 165.019 1.00 57.60 C ANISOU 3212 CG1 ILE B 83 7451 5802 8632 2508 -226 -177 C ATOM 3213 CG2 ILE B 83 -105.107 -12.958 164.926 1.00 53.94 C ANISOU 3213 CG2 ILE B 83 6854 5381 8261 1995 -249 -11 C ATOM 3214 CD1 ILE B 83 -107.849 -11.800 164.973 1.00 62.34 C ANISOU 3214 CD1 ILE B 83 7731 6748 9208 2569 -147 -92 C ATOM 3215 N ALA B 84 -104.832 -13.724 168.532 1.00 49.22 N ANISOU 3215 N ALA B 84 6215 5184 7303 1998 -89 -121 N ATOM 3216 CA ALA B 84 -103.858 -14.462 169.329 1.00 48.45 C ANISOU 3216 CA ALA B 84 6139 5126 7144 1828 -106 -83 C ATOM 3217 C ALA B 84 -104.507 -15.771 169.759 1.00 53.14 C ANISOU 3217 C ALA B 84 6526 5976 7689 1759 -5 71 C ATOM 3218 O ALA B 84 -105.637 -16.082 169.370 1.00 52.22 O ANISOU 3218 O ALA B 84 6240 6001 7598 1807 72 133 O ATOM 3219 CB ALA B 84 -103.387 -13.644 170.533 1.00 50.29 C ANISOU 3219 CB ALA B 84 6537 5357 7214 1912 -116 -248 C ATOM 3220 N THR B 85 -103.786 -16.538 170.574 1.00 52.83 N ANISOU 3220 N THR B 85 6502 6000 7571 1640 -8 136 N ATOM 3221 CA THR B 85 -104.296 -17.789 171.121 1.00 54.10 C ANISOU 3221 CA THR B 85 6518 6372 7665 1557 92 297 C ATOM 3222 C THR B 85 -104.630 -17.597 172.593 1.00 58.93 C ANISOU 3222 C THR B 85 7144 7207 8040 1662 176 247 C ATOM 3223 O THR B 85 -103.795 -17.123 173.367 1.00 64.32 O ANISOU 3223 O THR B 85 7969 7861 8609 1693 115 151 O ATOM 3224 CB THR B 85 -103.277 -18.918 170.952 1.00 53.05 C ANISOU 3224 CB THR B 85 6405 6146 7606 1366 32 438 C ATOM 3225 OG1 THR B 85 -102.714 -18.862 169.635 1.00 66.40 O ANISOU 3225 OG1 THR B 85 8119 7617 9494 1284 -60 434 O ATOM 3226 CG2 THR B 85 -103.944 -20.270 171.152 1.00 44.77 C ANISOU 3226 CG2 THR B 85 5226 5242 6543 1255 140 628 C ATOM 3227 N TYR B 86 -105.843 -17.974 172.980 1.00 57.94 N ANISOU 3227 N TYR B 86 6861 7326 7826 1705 318 307 N ATOM 3228 CA TYR B 86 -106.337 -17.747 174.331 1.00 61.41 C ANISOU 3228 CA TYR B 86 7291 8019 8022 1819 424 253 C ATOM 3229 C TYR B 86 -106.432 -19.071 175.075 1.00 61.07 C ANISOU 3229 C TYR B 86 7178 8156 7869 1663 515 458 C ATOM 3230 O TYR B 86 -106.997 -20.041 174.559 1.00 56.28 O ANISOU 3230 O TYR B 86 6435 7592 7356 1520 583 619 O ATOM 3231 CB TYR B 86 -107.691 -17.038 174.294 1.00 62.16 C ANISOU 3231 CB TYR B 86 7253 8296 8071 2014 532 147 C ATOM 3232 CG TYR B 86 -107.605 -15.661 173.673 1.00 65.48 C ANISOU 3232 CG TYR B 86 7790 8513 8576 2206 443 -50 C ATOM 3233 CD1 TYR B 86 -107.764 -15.483 172.305 1.00 68.71 C ANISOU 3233 CD1 TYR B 86 8163 8749 9194 2200 375 -29 C ATOM 3234 CD2 TYR B 86 -107.335 -14.543 174.451 1.00 72.43 C ANISOU 3234 CD2 TYR B 86 8842 9359 9319 2384 425 -254 C ATOM 3235 CE1 TYR B 86 -107.671 -14.229 171.732 1.00 74.79 C ANISOU 3235 CE1 TYR B 86 9074 9309 10033 2375 295 -182 C ATOM 3236 CE2 TYR B 86 -107.243 -13.284 173.887 1.00 73.42 C ANISOU 3236 CE2 TYR B 86 9118 9254 9527 2550 348 -426 C ATOM 3237 CZ TYR B 86 -107.411 -13.133 172.528 1.00 76.14 C ANISOU 3237 CZ TYR B 86 9433 9418 10079 2547 284 -377 C ATOM 3238 OH TYR B 86 -107.322 -11.881 171.962 1.00 79.72 O ANISOU 3238 OH TYR B 86 10065 9622 10605 2713 210 -522 O ATOM 3239 N TYR B 87 -105.873 -19.107 176.283 1.00 66.15 N ANISOU 3239 N TYR B 87 7929 8900 8306 1683 515 452 N ATOM 3240 CA TYR B 87 -105.826 -20.313 177.098 1.00 66.79 C ANISOU 3240 CA TYR B 87 7996 9131 8252 1552 590 664 C ATOM 3241 C TYR B 87 -106.571 -20.091 178.406 1.00 69.03 C ANISOU 3241 C TYR B 87 8240 9743 8245 1653 735 628 C ATOM 3242 O TYR B 87 -106.434 -19.039 179.038 1.00 73.06 O ANISOU 3242 O TYR B 87 8831 10318 8610 1824 713 423 O ATOM 3243 CB TYR B 87 -104.378 -20.720 177.405 1.00 63.16 C ANISOU 3243 CB TYR B 87 7697 8526 7773 1485 446 727 C ATOM 3244 CG TYR B 87 -103.551 -21.091 176.195 1.00 56.89 C ANISOU 3244 CG TYR B 87 6932 7440 7243 1379 316 777 C ATOM 3245 CD1 TYR B 87 -102.797 -20.136 175.526 1.00 58.64 C ANISOU 3245 CD1 TYR B 87 7228 7464 7587 1429 178 599 C ATOM 3246 CD2 TYR B 87 -103.510 -22.399 175.732 1.00 52.35 C ANISOU 3246 CD2 TYR B 87 6324 6782 6785 1220 338 996 C ATOM 3247 CE1 TYR B 87 -102.035 -20.471 174.423 1.00 64.38 C ANISOU 3247 CE1 TYR B 87 7969 7956 8536 1328 72 640 C ATOM 3248 CE2 TYR B 87 -102.750 -22.744 174.629 1.00 54.58 C ANISOU 3248 CE2 TYR B 87 6631 6812 7296 1139 227 1022 C ATOM 3249 CZ TYR B 87 -102.015 -21.776 173.979 1.00 63.74 C ANISOU 3249 CZ TYR B 87 7839 7815 8562 1195 97 845 C ATOM 3250 OH TYR B 87 -101.257 -22.113 172.881 1.00 72.91 O ANISOU 3250 OH TYR B 87 9013 8756 9932 1110 0 868 O ATOM 3251 N CYS B 88 -107.357 -21.084 178.812 1.00 64.70 N ANISOU 3251 N CYS B 88 7577 9401 7605 1534 891 821 N ATOM 3252 CA CYS B 88 -108.032 -21.059 180.101 1.00 62.82 C ANISOU 3252 CA CYS B 88 7296 9507 7066 1594 1050 826 C ATOM 3253 C CYS B 88 -107.364 -22.055 181.039 1.00 67.11 C ANISOU 3253 C CYS B 88 7965 10100 7432 1472 1051 1042 C ATOM 3254 O CYS B 88 -107.021 -23.170 180.635 1.00 69.65 O ANISOU 3254 O CYS B 88 8320 10266 7877 1293 1026 1266 O ATOM 3255 CB CYS B 88 -109.528 -21.371 179.959 1.00 63.55 C ANISOU 3255 CB CYS B 88 7144 9856 7145 1544 1251 882 C ATOM 3256 SG CYS B 88 -109.947 -23.012 179.315 1.00 68.83 S ANISOU 3256 SG CYS B 88 7710 10473 7971 1215 1335 1192 S ATOM 3257 N GLN B 89 -107.181 -21.643 182.291 1.00 71.47 N ANISOU 3257 N GLN B 89 8601 10868 7688 1585 1077 971 N ATOM 3258 CA GLN B 89 -106.465 -22.432 183.284 1.00 71.05 C ANISOU 3258 CA GLN B 89 8688 10886 7421 1517 1054 1162 C ATOM 3259 C GLN B 89 -107.293 -22.518 184.556 1.00 74.22 C ANISOU 3259 C GLN B 89 9043 11680 7476 1543 1250 1206 C ATOM 3260 O GLN B 89 -107.815 -21.503 185.025 1.00 76.02 O ANISOU 3260 O GLN B 89 9217 12113 7553 1711 1317 972 O ATOM 3261 CB GLN B 89 -105.095 -21.821 183.595 1.00 68.73 C ANISOU 3261 CB GLN B 89 8570 10472 7074 1624 841 1020 C ATOM 3262 CG GLN B 89 -104.482 -22.303 184.900 1.00 73.23 C ANISOU 3262 CG GLN B 89 9269 11231 7326 1631 820 1149 C ATOM 3263 CD GLN B 89 -104.319 -21.193 185.917 1.00 81.52 C ANISOU 3263 CD GLN B 89 10381 12500 8092 1801 797 890 C ATOM 3264 OE1 GLN B 89 -104.022 -20.052 185.566 1.00 79.38 O ANISOU 3264 OE1 GLN B 89 10135 12114 7910 1907 698 604 O ATOM 3265 NE2 GLN B 89 -104.514 -21.522 187.188 1.00 87.00 N ANISOU 3265 NE2 GLN B 89 11118 13505 8434 1818 891 988 N ATOM 3266 N GLN B 90 -107.407 -23.716 185.117 1.00 77.68 N ANISOU 3266 N GLN B 90 9518 12217 7780 1382 1347 1505 N ATOM 3267 CA GLN B 90 -108.093 -23.907 186.386 1.00 80.08 C ANISOU 3267 CA GLN B 90 9798 12905 7722 1378 1538 1587 C ATOM 3268 C GLN B 90 -107.076 -24.014 187.515 1.00 78.89 C ANISOU 3268 C GLN B 90 9855 12836 7283 1448 1434 1650 C ATOM 3269 O GLN B 90 -106.029 -24.653 187.368 1.00 75.62 O ANISOU 3269 O GLN B 90 9590 12197 6946 1401 1273 1809 O ATOM 3270 CB GLN B 90 -108.987 -25.151 186.352 1.00 84.32 C ANISOU 3270 CB GLN B 90 10248 13529 8260 1129 1740 1892 C ATOM 3271 CG GLN B 90 -108.249 -26.474 186.200 1.00 86.08 C ANISOU 3271 CG GLN B 90 10647 13490 8571 949 1666 2218 C ATOM 3272 CD GLN B 90 -107.881 -27.101 187.533 1.00 90.36 C ANISOU 3272 CD GLN B 90 11367 14211 8755 933 1708 2448 C ATOM 3273 OE1 GLN B 90 -108.367 -26.684 188.584 1.00 93.70 O ANISOU 3273 OE1 GLN B 90 11755 14998 8849 1003 1837 2391 O ATOM 3274 NE2 GLN B 90 -107.012 -28.104 187.495 1.00 91.60 N ANISOU 3274 NE2 GLN B 90 11720 14118 8964 858 1598 2708 N ATOM 3275 N TYR B 91 -107.379 -23.359 188.636 1.00 84.27 N ANISOU 3275 N TYR B 91 10538 13858 7622 1578 1520 1509 N ATOM 3276 CA TYR B 91 -106.583 -23.480 189.851 1.00 89.91 C ANISOU 3276 CA TYR B 91 11430 14740 7993 1640 1447 1573 C ATOM 3277 C TYR B 91 -107.417 -23.994 191.019 1.00 96.29 C ANISOU 3277 C TYR B 91 12217 15947 8422 1579 1683 1751 C ATOM 3278 O TYR B 91 -107.075 -23.748 192.180 1.00100.05 O ANISOU 3278 O TYR B 91 12800 16684 8533 1677 1671 1714 O ATOM 3279 CB TYR B 91 -105.920 -22.145 190.203 1.00 91.94 C ANISOU 3279 CB TYR B 91 11753 15034 8145 1852 1292 1207 C ATOM 3280 CG TYR B 91 -106.882 -21.012 190.486 1.00 99.76 C ANISOU 3280 CG TYR B 91 12630 16257 9018 2003 1438 895 C ATOM 3281 CD1 TYR B 91 -107.444 -20.277 189.450 1.00102.12 C ANISOU 3281 CD1 TYR B 91 12801 16387 9613 2069 1455 687 C ATOM 3282 CD2 TYR B 91 -107.221 -20.670 191.789 1.00105.74 C ANISOU 3282 CD2 TYR B 91 13413 17408 9357 2102 1557 806 C ATOM 3283 CE1 TYR B 91 -108.319 -19.238 189.702 1.00105.31 C ANISOU 3283 CE1 TYR B 91 13109 16992 9912 2250 1584 402 C ATOM 3284 CE2 TYR B 91 -108.097 -19.633 192.051 1.00111.09 C ANISOU 3284 CE2 TYR B 91 13988 18296 9924 2271 1696 504 C ATOM 3285 CZ TYR B 91 -108.643 -18.921 191.003 1.00110.46 C ANISOU 3285 CZ TYR B 91 13786 18027 10157 2355 1707 303 C ATOM 3286 OH TYR B 91 -109.516 -17.888 191.257 1.00111.85 O ANISOU 3286 OH TYR B 91 13868 18403 10226 2563 1842 3 O ATOM 3287 N SER B 92 -108.506 -24.711 190.728 1.00 99.89 N ANISOU 3287 N SER B 92 12534 16474 8948 1400 1902 1942 N ATOM 3288 CA SER B 92 -109.370 -25.227 191.785 1.00106.00 C ANISOU 3288 CA SER B 92 13270 17641 9364 1303 2155 2125 C ATOM 3289 C SER B 92 -108.643 -26.258 192.639 1.00112.84 C ANISOU 3289 C SER B 92 14372 18517 9984 1214 2113 2470 C ATOM 3290 O SER B 92 -108.859 -26.330 193.854 1.00117.66 O ANISOU 3290 O SER B 92 15039 19486 10182 1234 2234 2549 O ATOM 3291 CB SER B 92 -110.637 -25.827 191.176 1.00107.97 C ANISOU 3291 CB SER B 92 13306 17942 9775 1085 2386 2260 C ATOM 3292 OG SER B 92 -111.521 -26.285 192.184 1.00118.10 O ANISOU 3292 OG SER B 92 14529 19634 10708 966 2653 2427 O ATOM 3293 N LYS B 93 -107.783 -27.065 192.023 1.00114.81 N ANISOU 3293 N LYS B 93 14767 18386 10470 1134 1943 2681 N ATOM 3294 CA LYS B 93 -106.962 -28.017 192.754 1.00115.44 C ANISOU 3294 CA LYS B 93 15092 18429 10341 1104 1862 3007 C ATOM 3295 C LYS B 93 -105.673 -28.246 191.980 1.00108.32 C ANISOU 3295 C LYS B 93 14315 17114 9727 1172 1576 3027 C ATOM 3296 O LYS B 93 -105.637 -28.123 190.753 1.00 99.33 O ANISOU 3296 O LYS B 93 13085 15671 8985 1135 1506 2914 O ATOM 3297 CB LYS B 93 -107.695 -29.346 192.985 1.00119.31 C ANISOU 3297 CB LYS B 93 15640 18940 10755 838 2086 3418 C ATOM 3298 CG LYS B 93 -107.721 -30.268 191.776 1.00123.96 C ANISOU 3298 CG LYS B 93 16243 19096 11759 643 2068 3600 C ATOM 3299 CD LYS B 93 -108.337 -31.618 192.115 1.00132.45 C ANISOU 3299 CD LYS B 93 17433 20161 12731 361 2279 4019 C ATOM 3300 CE LYS B 93 -108.205 -32.588 190.951 1.00129.50 C ANISOU 3300 CE LYS B 93 17129 19314 12762 176 2234 4192 C ATOM 3301 NZ LYS B 93 -108.819 -33.914 191.239 1.00129.83 N ANISOU 3301 NZ LYS B 93 17312 19296 12722 -130 2446 4594 N ATOM 3302 N LEU B 94 -104.612 -28.564 192.713 1.00109.72 N ANISOU 3302 N LEU B 94 14689 17312 9687 1281 1408 3164 N ATOM 3303 CA LEU B 94 -103.349 -28.881 192.071 1.00101.35 C ANISOU 3303 CA LEU B 94 13736 15907 8866 1358 1142 3208 C ATOM 3304 C LEU B 94 -103.384 -30.292 191.482 1.00 99.18 C ANISOU 3304 C LEU B 94 13576 15300 8808 1192 1187 3579 C ATOM 3305 O LEU B 94 -104.031 -31.186 192.033 1.00104.16 O ANISOU 3305 O LEU B 94 14303 16012 9263 1043 1377 3890 O ATOM 3306 CB LEU B 94 -102.201 -28.764 193.070 1.00102.80 C ANISOU 3306 CB LEU B 94 14067 16262 8729 1548 938 3228 C ATOM 3307 CG LEU B 94 -101.759 -27.340 193.418 1.00 96.83 C ANISOU 3307 CG LEU B 94 13228 15721 7841 1718 804 2810 C ATOM 3308 CD1 LEU B 94 -100.439 -27.359 194.171 1.00 96.94 C ANISOU 3308 CD1 LEU B 94 13372 15852 7607 1881 551 2837 C ATOM 3309 CD2 LEU B 94 -101.651 -26.485 192.164 1.00 91.30 C ANISOU 3309 CD2 LEU B 94 12382 14756 7552 1725 716 2484 C ATOM 3310 N PRO B 95 -102.694 -30.518 190.351 1.00 93.40 N ANISOU 3310 N PRO B 95 12848 14185 8455 1205 1022 3549 N ATOM 3311 CA PRO B 95 -101.892 -29.522 189.632 1.00 88.22 C ANISOU 3311 CA PRO B 95 12087 13416 8017 1349 806 3206 C ATOM 3312 C PRO B 95 -102.742 -28.526 188.850 1.00 87.31 C ANISOU 3312 C PRO B 95 11755 13306 8113 1297 901 2888 C ATOM 3313 O PRO B 95 -103.854 -28.857 188.436 1.00 90.67 O ANISOU 3313 O PRO B 95 12089 13710 8652 1128 1104 2959 O ATOM 3314 CB PRO B 95 -101.054 -30.374 188.680 1.00 85.43 C ANISOU 3314 CB PRO B 95 11819 12656 7983 1342 656 3356 C ATOM 3315 CG PRO B 95 -101.904 -31.564 188.416 1.00 88.33 C ANISOU 3315 CG PRO B 95 12261 12854 8447 1128 856 3666 C ATOM 3316 CD PRO B 95 -102.638 -31.839 189.701 1.00 94.42 C ANISOU 3316 CD PRO B 95 13107 13952 8818 1066 1046 3863 C ATOM 3317 N ARG B 96 -102.220 -27.317 188.658 1.00 85.32 N ANISOU 3317 N ARG B 96 11426 13085 7905 1438 753 2543 N ATOM 3318 CA ARG B 96 -102.853 -26.371 187.751 1.00 78.74 C ANISOU 3318 CA ARG B 96 10421 12180 7318 1424 802 2251 C ATOM 3319 C ARG B 96 -102.806 -26.922 186.332 1.00 69.02 C ANISOU 3319 C ARG B 96 9147 10575 6504 1309 768 2320 C ATOM 3320 O ARG B 96 -101.755 -27.364 185.860 1.00 75.40 O ANISOU 3320 O ARG B 96 10038 11144 7468 1334 592 2392 O ATOM 3321 CB ARG B 96 -102.152 -25.014 187.824 1.00 77.72 C ANISOU 3321 CB ARG B 96 10273 12101 7157 1587 633 1888 C ATOM 3322 CG ARG B 96 -102.248 -24.334 189.182 1.00 79.27 C ANISOU 3322 CG ARG B 96 10509 12672 6939 1703 667 1754 C ATOM 3323 CD ARG B 96 -101.112 -23.341 189.380 1.00 82.46 C ANISOU 3323 CD ARG B 96 10965 13082 7286 1833 436 1469 C ATOM 3324 NE ARG B 96 -101.210 -22.636 190.656 1.00 87.82 N ANISOU 3324 NE ARG B 96 11688 14116 7562 1939 464 1301 N ATOM 3325 CZ ARG B 96 -100.208 -21.968 191.219 1.00 85.58 C ANISOU 3325 CZ ARG B 96 11477 13935 7106 2031 271 1099 C ATOM 3326 NH1 ARG B 96 -99.024 -21.916 190.625 1.00 81.50 N ANISOU 3326 NH1 ARG B 96 10977 13207 6783 2025 41 1048 N ATOM 3327 NH2 ARG B 96 -100.388 -21.355 192.381 1.00 88.81 N ANISOU 3327 NH2 ARG B 96 11932 14678 7135 2118 312 936 N ATOM 3328 N THR B 97 -103.946 -26.898 185.651 1.00 66.63 N ANISOU 3328 N THR B 97 8701 10245 6371 1190 935 2289 N ATOM 3329 CA THR B 97 -104.029 -27.384 184.285 1.00 71.77 C ANISOU 3329 CA THR B 97 9298 10573 7399 1067 915 2332 C ATOM 3330 C THR B 97 -104.582 -26.295 183.376 1.00 66.94 C ANISOU 3330 C THR B 97 8510 9934 6990 1105 923 2036 C ATOM 3331 O THR B 97 -105.261 -25.366 183.822 1.00 64.91 O ANISOU 3331 O THR B 97 8158 9920 6585 1195 1011 1846 O ATOM 3332 CB THR B 97 -104.902 -28.643 184.191 1.00 75.04 C ANISOU 3332 CB THR B 97 9716 10948 7846 842 1105 2628 C ATOM 3333 OG1 THR B 97 -106.140 -28.423 184.878 1.00 82.40 O ANISOU 3333 OG1 THR B 97 10529 12217 8561 782 1330 2623 O ATOM 3334 CG2 THR B 97 -104.188 -29.830 184.820 1.00 73.19 C ANISOU 3334 CG2 THR B 97 9708 10616 7487 813 1064 2950 C ATOM 3335 N PHE B 98 -104.284 -26.427 182.089 1.00 61.29 N ANISOU 3335 N PHE B 98 7764 8919 6607 1050 830 2001 N ATOM 3336 CA PHE B 98 -104.677 -25.463 181.075 1.00 61.01 C ANISOU 3336 CA PHE B 98 7589 8807 6786 1091 808 1750 C ATOM 3337 C PHE B 98 -105.630 -26.108 180.078 1.00 63.35 C ANISOU 3337 C PHE B 98 7756 9009 7305 914 925 1844 C ATOM 3338 O PHE B 98 -105.806 -27.328 180.043 1.00 69.28 O ANISOU 3338 O PHE B 98 8550 9684 8089 740 999 2090 O ATOM 3339 CB PHE B 98 -103.448 -24.912 180.339 1.00 60.24 C ANISOU 3339 CB PHE B 98 7556 8459 6874 1175 585 1596 C ATOM 3340 CG PHE B 98 -102.592 -24.005 181.175 1.00 61.20 C ANISOU 3340 CG PHE B 98 7767 8689 6798 1333 461 1425 C ATOM 3341 CD1 PHE B 98 -101.578 -24.521 181.965 1.00 63.13 C ANISOU 3341 CD1 PHE B 98 8139 8970 6879 1366 356 1547 C ATOM 3342 CD2 PHE B 98 -102.783 -22.634 181.147 1.00 61.55 C ANISOU 3342 CD2 PHE B 98 7774 8791 6820 1452 441 1135 C ATOM 3343 CE1 PHE B 98 -100.785 -23.687 182.730 1.00 65.59 C ANISOU 3343 CE1 PHE B 98 8516 9410 6997 1490 232 1372 C ATOM 3344 CE2 PHE B 98 -101.992 -21.795 181.908 1.00 66.49 C ANISOU 3344 CE2 PHE B 98 8495 9504 7265 1568 326 955 C ATOM 3345 CZ PHE B 98 -100.992 -22.322 182.701 1.00 68.82 C ANISOU 3345 CZ PHE B 98 8893 9868 7389 1575 220 1067 C ATOM 3346 N GLY B 99 -106.243 -25.260 179.256 1.00 62.69 N ANISOU 3346 N GLY B 99 7523 8927 7371 960 935 1641 N ATOM 3347 CA GLY B 99 -107.039 -25.731 178.145 1.00 66.70 C ANISOU 3347 CA GLY B 99 7890 9346 8108 807 1003 1685 C ATOM 3348 C GLY B 99 -106.202 -25.922 176.895 1.00 69.86 C ANISOU 3348 C GLY B 99 8347 9402 8795 768 841 1664 C ATOM 3349 O GLY B 99 -105.052 -25.493 176.817 1.00 70.36 O ANISOU 3349 O GLY B 99 8529 9313 8893 877 678 1581 O ATOM 3350 N GLY B 100 -106.804 -26.586 175.906 1.00 69.54 N ANISOU 3350 N GLY B 100 8210 9263 8950 597 893 1733 N ATOM 3351 CA GLY B 100 -106.079 -26.881 174.682 1.00 65.75 C ANISOU 3351 CA GLY B 100 7780 8472 8731 545 759 1719 C ATOM 3352 C GLY B 100 -105.643 -25.635 173.939 1.00 61.69 C ANISOU 3352 C GLY B 100 7240 7873 8327 705 623 1485 C ATOM 3353 O GLY B 100 -104.664 -25.666 173.188 1.00 59.73 O ANISOU 3353 O GLY B 100 7072 7385 8236 710 485 1453 O ATOM 3354 N GLY B 101 -106.353 -24.528 174.136 1.00 60.29 N ANISOU 3354 N GLY B 101 6958 7886 8064 841 665 1321 N ATOM 3355 CA GLY B 101 -106.060 -23.309 173.413 1.00 58.16 C ANISOU 3355 CA GLY B 101 6688 7514 7897 989 550 1111 C ATOM 3356 C GLY B 101 -106.989 -23.076 172.244 1.00 59.93 C ANISOU 3356 C GLY B 101 6749 7743 8280 967 576 1050 C ATOM 3357 O GLY B 101 -107.362 -24.016 171.537 1.00 61.75 O ANISOU 3357 O GLY B 101 6900 7927 8636 787 612 1162 O ATOM 3358 N THR B 102 -107.374 -21.819 172.035 1.00 59.67 N ANISOU 3358 N THR B 102 6672 7763 8235 1154 552 869 N ATOM 3359 CA THR B 102 -108.227 -21.430 170.920 1.00 59.19 C ANISOU 3359 CA THR B 102 6460 7723 8305 1186 552 801 C ATOM 3360 C THR B 102 -107.577 -20.248 170.223 1.00 56.27 C ANISOU 3360 C THR B 102 6211 7140 8028 1339 411 645 C ATOM 3361 O THR B 102 -107.423 -19.179 170.823 1.00 60.33 O ANISOU 3361 O THR B 102 6820 7666 8437 1527 391 506 O ATOM 3362 CB THR B 102 -109.638 -21.068 171.392 1.00 65.70 C ANISOU 3362 CB THR B 102 7084 8879 8998 1295 694 752 C ATOM 3363 OG1 THR B 102 -110.334 -22.258 171.785 1.00 67.87 O ANISOU 3363 OG1 THR B 102 7222 9349 9216 1089 836 913 O ATOM 3364 CG2 THR B 102 -110.414 -20.381 170.277 1.00 64.63 C ANISOU 3364 CG2 THR B 102 6807 8772 8977 1410 659 652 C ATOM 3365 N LYS B 103 -107.196 -20.439 168.966 1.00 54.54 N ANISOU 3365 N LYS B 103 6003 6722 7997 1248 318 665 N ATOM 3366 CA LYS B 103 -106.470 -19.429 168.212 1.00 59.54 C ANISOU 3366 CA LYS B 103 6770 7129 8723 1343 187 548 C ATOM 3367 C LYS B 103 -107.441 -18.665 167.324 1.00 63.58 C ANISOU 3367 C LYS B 103 7178 7691 9290 1479 182 474 C ATOM 3368 O LYS B 103 -108.341 -19.254 166.717 1.00 64.43 O ANISOU 3368 O LYS B 103 7096 7934 9449 1407 230 540 O ATOM 3369 CB LYS B 103 -105.370 -20.083 167.372 1.00 63.68 C ANISOU 3369 CB LYS B 103 7375 7420 9400 1169 90 614 C ATOM 3370 CG LYS B 103 -104.424 -19.128 166.666 1.00 70.18 C ANISOU 3370 CG LYS B 103 8348 8012 10305 1217 -36 509 C ATOM 3371 CD LYS B 103 -104.172 -19.593 165.239 1.00 80.23 C ANISOU 3371 CD LYS B 103 9588 9147 11748 1088 -95 558 C ATOM 3372 CE LYS B 103 -102.945 -18.926 164.639 1.00 90.13 C ANISOU 3372 CE LYS B 103 10998 10174 13072 1069 -208 487 C ATOM 3373 NZ LYS B 103 -103.306 -17.823 163.707 1.00 96.11 N ANISOU 3373 NZ LYS B 103 11796 10846 13874 1169 -253 413 N ATOM 3374 N LEU B 104 -107.259 -17.352 167.257 1.00 67.64 N ANISOU 3374 N LEU B 104 7821 8093 9785 1674 120 338 N ATOM 3375 CA LEU B 104 -108.156 -16.483 166.511 1.00 61.90 C ANISOU 3375 CA LEU B 104 7030 7400 9089 1865 106 270 C ATOM 3376 C LEU B 104 -107.621 -16.234 165.109 1.00 57.69 C ANISOU 3376 C LEU B 104 6582 6629 8710 1808 -13 285 C ATOM 3377 O LEU B 104 -106.418 -16.039 164.914 1.00 70.22 O ANISOU 3377 O LEU B 104 8356 7974 10351 1716 -95 269 O ATOM 3378 CB LEU B 104 -108.357 -15.150 167.233 1.00 60.80 C ANISOU 3378 CB LEU B 104 7016 7251 8834 2139 116 113 C ATOM 3379 CG LEU B 104 -109.217 -15.168 168.498 1.00 61.98 C ANISOU 3379 CG LEU B 104 7046 7699 8806 2268 250 68 C ATOM 3380 CD1 LEU B 104 -109.722 -13.771 168.814 1.00 66.56 C ANISOU 3380 CD1 LEU B 104 7716 8273 9302 2597 258 -105 C ATOM 3381 CD2 LEU B 104 -110.382 -16.134 168.345 1.00 60.03 C ANISOU 3381 CD2 LEU B 104 6493 7767 8550 2191 356 177 C ATOM 3382 N GLU B 105 -108.525 -16.240 164.137 1.00 46.19 N ANISOU 3382 N GLU B 105 4973 5270 7308 1858 -22 315 N ATOM 3383 CA GLU B 105 -108.204 -15.879 162.768 1.00 47.87 C ANISOU 3383 CA GLU B 105 5259 5295 7633 1842 -130 329 C ATOM 3384 C GLU B 105 -109.201 -14.826 162.309 1.00 50.82 C ANISOU 3384 C GLU B 105 5597 5738 7974 2126 -153 275 C ATOM 3385 O GLU B 105 -110.332 -14.767 162.799 1.00 62.29 O ANISOU 3385 O GLU B 105 6866 7460 9343 2286 -78 248 O ATOM 3386 CB GLU B 105 -108.221 -17.111 161.845 1.00 57.04 C ANISOU 3386 CB GLU B 105 6274 6505 8894 1597 -141 435 C ATOM 3387 CG GLU B 105 -109.397 -17.187 160.889 1.00 71.92 C ANISOU 3387 CG GLU B 105 7948 8583 10794 1653 -152 459 C ATOM 3388 CD GLU B 105 -109.386 -18.459 160.063 1.00 77.89 C ANISOU 3388 CD GLU B 105 8574 9383 11638 1381 -158 538 C ATOM 3389 OE1 GLU B 105 -108.523 -19.326 160.317 1.00 81.40 O ANISOU 3389 OE1 GLU B 105 9093 9703 12132 1172 -139 580 O ATOM 3390 OE2 GLU B 105 -110.245 -18.598 159.169 1.00 77.70 O ANISOU 3390 OE2 GLU B 105 8376 9521 11627 1385 -184 549 O ATOM 3391 N ILE B 106 -108.774 -13.990 161.372 1.00 47.65 N ANISOU 3391 N ILE B 106 5372 5102 7629 2197 -255 264 N ATOM 3392 CA ILE B 106 -109.662 -12.989 160.796 1.00 47.66 C ANISOU 3392 CA ILE B 106 5371 5134 7603 2488 -296 236 C ATOM 3393 C ILE B 106 -110.509 -13.630 159.706 1.00 45.31 C ANISOU 3393 C ILE B 106 4820 5054 7340 2445 -325 321 C ATOM 3394 O ILE B 106 -109.987 -14.291 158.801 1.00 51.10 O ANISOU 3394 O ILE B 106 5548 5714 8154 2214 -376 392 O ATOM 3395 CB ILE B 106 -108.858 -11.797 160.252 1.00 46.12 C ANISOU 3395 CB ILE B 106 5506 4576 7443 2574 -390 207 C ATOM 3396 CG1 ILE B 106 -108.421 -10.885 161.400 1.00 53.47 C ANISOU 3396 CG1 ILE B 106 6667 5341 8308 2704 -359 80 C ATOM 3397 CG2 ILE B 106 -109.678 -11.013 159.241 1.00 46.59 C ANISOU 3397 CG2 ILE B 106 5565 4645 7494 2813 -455 240 C ATOM 3398 CD1 ILE B 106 -107.366 -9.875 161.011 1.00 67.15 C ANISOU 3398 CD1 ILE B 106 8733 6711 10068 2619 -413 58 C ATOM 3399 N LYS B 107 -111.823 -13.449 159.801 1.00 45.04 N ANISOU 3399 N LYS B 107 4563 5315 7236 2668 -291 300 N ATOM 3400 CA LYS B 107 -112.716 -13.916 158.752 1.00 50.56 C ANISOU 3400 CA LYS B 107 5004 6258 7947 2654 -335 360 C ATOM 3401 C LYS B 107 -112.612 -12.991 157.548 1.00 50.81 C ANISOU 3401 C LYS B 107 5199 6109 7998 2824 -467 393 C ATOM 3402 O LYS B 107 -112.590 -11.765 157.687 1.00 49.66 O ANISOU 3402 O LYS B 107 5267 5784 7817 3086 -497 351 O ATOM 3403 CB LYS B 107 -114.160 -13.972 159.253 1.00 48.28 C ANISOU 3403 CB LYS B 107 4394 6386 7564 2846 -259 320 C ATOM 3404 CG LYS B 107 -115.056 -14.885 158.430 1.00 48.86 C ANISOU 3404 CG LYS B 107 4125 6794 7645 2701 -274 373 C ATOM 3405 CD LYS B 107 -116.398 -15.122 159.103 1.00 57.12 C ANISOU 3405 CD LYS B 107 4813 8295 8594 2812 -170 328 C ATOM 3406 CE LYS B 107 -116.251 -15.997 160.334 1.00 63.34 C ANISOU 3406 CE LYS B 107 5540 9167 9358 2576 -15 325 C ATOM 3407 NZ LYS B 107 -117.573 -16.414 160.881 1.00 72.12 N ANISOU 3407 NZ LYS B 107 6267 10762 10372 2601 103 297 N ATOM 3408 N ARG B 108 -112.555 -13.582 156.358 1.00 45.21 N ANISOU 3408 N ARG B 108 4407 5436 7336 2645 -540 468 N ATOM 3409 CA ARG B 108 -112.462 -12.794 155.140 1.00 53.67 C ANISOU 3409 CA ARG B 108 5627 6361 8404 2783 -666 522 C ATOM 3410 C ARG B 108 -113.150 -13.538 154.006 1.00 46.10 C ANISOU 3410 C ARG B 108 4402 5680 7436 2678 -728 577 C ATOM 3411 O ARG B 108 -113.586 -14.682 154.155 1.00 50.39 O ANISOU 3411 O ARG B 108 4672 6482 7991 2460 -671 564 O ATOM 3412 CB ARG B 108 -111.005 -12.494 154.777 1.00 52.76 C ANISOU 3412 CB ARG B 108 5856 5836 8355 2612 -705 551 C ATOM 3413 CG ARG B 108 -110.185 -13.727 154.442 1.00 41.25 C ANISOU 3413 CG ARG B 108 4347 4351 6974 2219 -686 579 C ATOM 3414 CD ARG B 108 -109.143 -13.406 153.390 1.00 44.52 C ANISOU 3414 CD ARG B 108 5000 4491 7423 2098 -764 633 C ATOM 3415 NE ARG B 108 -109.759 -13.210 152.080 1.00 46.47 N ANISOU 3415 NE ARG B 108 5180 4854 7623 2188 -859 701 N ATOM 3416 CZ ARG B 108 -109.157 -12.631 151.048 1.00 44.16 C ANISOU 3416 CZ ARG B 108 5101 4361 7316 2174 -936 767 C ATOM 3417 NH1 ARG B 108 -107.917 -12.180 151.168 1.00 44.07 N ANISOU 3417 NH1 ARG B 108 5377 4038 7330 2047 -911 764 N ATOM 3418 NH2 ARG B 108 -109.798 -12.497 149.895 1.00 42.61 N ANISOU 3418 NH2 ARG B 108 4829 4310 7052 2270 -1027 836 N ATOM 3419 N ALA B 109 -113.245 -12.861 152.864 1.00 47.05 N ANISOU 3419 N ALA B 109 4619 5738 7522 2829 -848 638 N ATOM 3420 CA ALA B 109 -113.902 -13.433 151.699 1.00 56.92 C ANISOU 3420 CA ALA B 109 5630 7262 8734 2757 -931 683 C ATOM 3421 C ALA B 109 -113.193 -14.703 151.245 1.00 57.11 C ANISOU 3421 C ALA B 109 5610 7256 8832 2325 -909 688 C ATOM 3422 O ALA B 109 -111.972 -14.836 151.360 1.00 60.40 O ANISOU 3422 O ALA B 109 6266 7364 9322 2133 -879 694 O ATOM 3423 CB ALA B 109 -113.942 -12.416 150.558 1.00 57.20 C ANISOU 3423 CB ALA B 109 5846 7183 8705 2977 -1064 766 C ATOM 3424 N ASP B 110 -113.982 -15.646 150.734 1.00 62.77 N ANISOU 3424 N ASP B 110 6013 8309 9526 2176 -924 673 N ATOM 3425 CA ASP B 110 -113.427 -16.862 150.159 1.00 53.74 C ANISOU 3425 CA ASP B 110 4831 7141 8444 1789 -913 664 C ATOM 3426 C ASP B 110 -112.457 -16.530 149.031 1.00 46.42 C ANISOU 3426 C ASP B 110 4160 5960 7518 1730 -1001 716 C ATOM 3427 O ASP B 110 -112.587 -15.512 148.345 1.00 44.35 O ANISOU 3427 O ASP B 110 4017 5656 7179 1969 -1099 777 O ATOM 3428 CB ASP B 110 -114.545 -17.767 149.642 1.00 45.77 C ANISOU 3428 CB ASP B 110 3455 6543 7391 1656 -936 626 C ATOM 3429 CG ASP B 110 -115.548 -18.127 150.719 1.00 59.24 C ANISOU 3429 CG ASP B 110 4881 8543 9084 1680 -835 578 C ATOM 3430 OD1 ASP B 110 -115.141 -18.275 151.890 1.00 57.52 O ANISOU 3430 OD1 ASP B 110 4751 8182 8920 1633 -717 567 O ATOM 3431 OD2 ASP B 110 -116.746 -18.264 150.391 1.00 64.67 O ANISOU 3431 OD2 ASP B 110 5248 9630 9694 1740 -873 551 O ATOM 3432 N ALA B 111 -111.475 -17.407 148.842 1.00 40.96 N ANISOU 3432 N ALA B 111 3556 5098 6906 1416 -959 697 N ATOM 3433 CA ALA B 111 -110.427 -17.191 147.855 1.00 39.84 C ANISOU 3433 CA ALA B 111 3647 4726 6766 1322 -1014 735 C ATOM 3434 C ALA B 111 -109.954 -18.544 147.351 1.00 40.69 C ANISOU 3434 C ALA B 111 3681 4850 6931 977 -983 682 C ATOM 3435 O ALA B 111 -109.628 -19.426 148.151 1.00 37.35 O ANISOU 3435 O ALA B 111 3223 4370 6600 798 -888 636 O ATOM 3436 CB ALA B 111 -109.257 -16.398 148.447 1.00 38.54 C ANISOU 3436 CB ALA B 111 3795 4198 6650 1372 -975 760 C ATOM 3437 N ALA B 112 -109.929 -18.703 146.034 1.00 43.42 N ANISOU 3437 N ALA B 112 4016 5271 7212 897 -1064 687 N ATOM 3438 CA ALA B 112 -109.484 -19.960 145.454 1.00 38.08 C ANISOU 3438 CA ALA B 112 3287 4601 6579 586 -1038 615 C ATOM 3439 C ALA B 112 -107.958 -20.025 145.449 1.00 50.18 C ANISOU 3439 C ALA B 112 5070 5813 8185 461 -986 615 C ATOM 3440 O ALA B 112 -107.293 -19.002 145.258 1.00 58.27 O ANISOU 3440 O ALA B 112 6303 6661 9176 581 -1011 680 O ATOM 3441 CB ALA B 112 -110.017 -20.116 144.031 1.00 40.27 C ANISOU 3441 CB ALA B 112 3457 5105 6739 544 -1144 601 C ATOM 3442 N PRO B 113 -107.380 -21.206 145.652 1.00 42.19 N ANISOU 3442 N PRO B 113 4041 4721 7268 223 -911 542 N ATOM 3443 CA PRO B 113 -105.919 -21.311 145.694 1.00 33.85 C ANISOU 3443 CA PRO B 113 3184 3399 6278 126 -861 533 C ATOM 3444 C PRO B 113 -105.312 -21.311 144.301 1.00 40.83 C ANISOU 3444 C PRO B 113 4148 4271 7094 34 -906 515 C ATOM 3445 O PRO B 113 -105.875 -21.862 143.352 1.00 47.96 O ANISOU 3445 O PRO B 113 4934 5354 7933 -58 -951 466 O ATOM 3446 CB PRO B 113 -105.691 -22.653 146.399 1.00 33.02 C ANISOU 3446 CB PRO B 113 3015 3242 6290 -58 -772 465 C ATOM 3447 CG PRO B 113 -106.869 -23.469 145.987 1.00 38.14 C ANISOU 3447 CG PRO B 113 3452 4127 6913 -166 -790 413 C ATOM 3448 CD PRO B 113 -108.032 -22.502 145.915 1.00 43.47 C ANISOU 3448 CD PRO B 113 4007 5026 7484 36 -864 468 C ATOM 3449 N THR B 114 -104.143 -20.687 144.190 1.00 41.13 N ANISOU 3449 N THR B 114 4382 4113 7135 43 -888 549 N ATOM 3450 CA THR B 114 -103.341 -20.759 142.977 1.00 33.62 C ANISOU 3450 CA THR B 114 3515 3138 6120 -73 -899 528 C ATOM 3451 C THR B 114 -102.412 -21.958 143.103 1.00 33.77 C ANISOU 3451 C THR B 114 3523 3065 6242 -258 -817 422 C ATOM 3452 O THR B 114 -101.575 -22.005 144.011 1.00 46.13 O ANISOU 3452 O THR B 114 5156 4468 7903 -262 -756 418 O ATOM 3453 CB THR B 114 -102.542 -19.475 142.761 1.00 35.98 C ANISOU 3453 CB THR B 114 4026 3286 6361 5 -910 619 C ATOM 3454 OG1 THR B 114 -103.389 -18.339 142.984 1.00 46.78 O ANISOU 3454 OG1 THR B 114 5439 4672 7664 223 -975 720 O ATOM 3455 CG2 THR B 114 -101.999 -19.423 141.342 1.00 33.09 C ANISOU 3455 CG2 THR B 114 3727 2965 5880 -100 -927 620 C ATOM 3456 N VAL B 115 -102.581 -22.932 142.214 1.00 33.40 N ANISOU 3456 N VAL B 115 3392 3128 6170 -399 -821 328 N ATOM 3457 CA VAL B 115 -101.909 -24.221 142.313 1.00 33.02 C ANISOU 3457 CA VAL B 115 3330 2994 6224 -551 -746 213 C ATOM 3458 C VAL B 115 -100.809 -24.290 141.267 1.00 33.29 C ANISOU 3458 C VAL B 115 3449 2999 6202 -634 -723 155 C ATOM 3459 O VAL B 115 -101.053 -24.068 140.074 1.00 32.39 O ANISOU 3459 O VAL B 115 3330 3024 5952 -668 -771 142 O ATOM 3460 CB VAL B 115 -102.900 -25.386 142.139 1.00 36.12 C ANISOU 3460 CB VAL B 115 3579 3506 6640 -672 -751 121 C ATOM 3461 CG1 VAL B 115 -102.178 -26.722 142.245 1.00 32.02 C ANISOU 3461 CG1 VAL B 115 3091 2844 6232 -812 -671 4 C ATOM 3462 CG2 VAL B 115 -104.017 -25.286 143.166 1.00 32.55 C ANISOU 3462 CG2 VAL B 115 3016 3126 6227 -604 -761 182 C ATOM 3463 N SER B 116 -99.600 -24.591 141.724 1.00 32.84 N ANISOU 3463 N SER B 116 3457 2787 6234 -659 -649 119 N ATOM 3464 CA SER B 116 -98.435 -24.770 140.870 1.00 30.54 C ANISOU 3464 CA SER B 116 3220 2482 5902 -736 -604 46 C ATOM 3465 C SER B 116 -97.794 -26.103 141.217 1.00 33.48 C ANISOU 3465 C SER B 116 3569 2753 6400 -792 -532 -78 C ATOM 3466 O SER B 116 -97.785 -26.500 142.384 1.00 32.71 O ANISOU 3466 O SER B 116 3464 2540 6425 -746 -509 -56 O ATOM 3467 CB SER B 116 -97.426 -23.632 141.046 1.00 31.21 C ANISOU 3467 CB SER B 116 3405 2496 5956 -694 -585 129 C ATOM 3468 OG SER B 116 -98.065 -22.370 140.989 1.00 32.80 O ANISOU 3468 OG SER B 116 3670 2725 6068 -612 -650 261 O ATOM 3469 N ILE B 117 -97.271 -26.802 140.214 1.00 43.63 N ANISOU 3469 N ILE B 117 4852 4079 7645 -877 -495 -207 N ATOM 3470 CA ILE B 117 -96.597 -28.076 140.434 1.00 31.29 C ANISOU 3470 CA ILE B 117 3291 2401 6196 -899 -425 -335 C ATOM 3471 C ILE B 117 -95.210 -28.010 139.813 1.00 46.59 C ANISOU 3471 C ILE B 117 5249 4361 8091 -899 -363 -409 C ATOM 3472 O ILE B 117 -95.005 -27.360 138.781 1.00 52.19 O ANISOU 3472 O ILE B 117 5968 5207 8656 -949 -367 -410 O ATOM 3473 CB ILE B 117 -97.410 -29.264 139.871 1.00 32.52 C ANISOU 3473 CB ILE B 117 3422 2572 6362 -1004 -428 -467 C ATOM 3474 CG1 ILE B 117 -96.814 -30.593 140.345 1.00 43.35 C ANISOU 3474 CG1 ILE B 117 4838 3756 7879 -999 -356 -576 C ATOM 3475 CG2 ILE B 117 -97.488 -29.209 138.353 1.00 33.75 C ANISOU 3475 CG2 ILE B 117 3567 2900 6356 -1093 -445 -566 C ATOM 3476 CD1 ILE B 117 -97.615 -31.807 139.931 1.00 46.58 C ANISOU 3476 CD1 ILE B 117 5257 4124 8319 -1127 -350 -710 C ATOM 3477 N PHE B 118 -94.249 -28.667 140.464 1.00 42.58 N ANISOU 3477 N PHE B 118 4743 3735 7699 -836 -305 -464 N ATOM 3478 CA PHE B 118 -92.853 -28.616 140.071 1.00 37.31 C ANISOU 3478 CA PHE B 118 4057 3113 7004 -815 -240 -537 C ATOM 3479 C PHE B 118 -92.277 -30.026 140.113 1.00 37.62 C ANISOU 3479 C PHE B 118 4096 3052 7146 -758 -179 -691 C ATOM 3480 O PHE B 118 -92.408 -30.721 141.146 1.00 35.97 O ANISOU 3480 O PHE B 118 3913 2679 7073 -681 -183 -668 O ATOM 3481 CB PHE B 118 -92.052 -27.686 140.986 1.00 36.70 C ANISOU 3481 CB PHE B 118 3966 3021 6955 -755 -241 -426 C ATOM 3482 CG PHE B 118 -92.610 -26.296 141.071 1.00 40.50 C ANISOU 3482 CG PHE B 118 4489 3545 7355 -790 -298 -276 C ATOM 3483 CD1 PHE B 118 -92.160 -25.300 140.222 1.00 41.42 C ANISOU 3483 CD1 PHE B 118 4630 3775 7335 -869 -284 -242 C ATOM 3484 CD2 PHE B 118 -93.595 -25.989 141.993 1.00 42.28 C ANISOU 3484 CD2 PHE B 118 4740 3691 7631 -739 -358 -168 C ATOM 3485 CE1 PHE B 118 -92.677 -24.022 140.297 1.00 46.17 C ANISOU 3485 CE1 PHE B 118 5307 4373 7863 -883 -337 -96 C ATOM 3486 CE2 PHE B 118 -94.117 -24.718 142.070 1.00 44.28 C ANISOU 3486 CE2 PHE B 118 5046 3966 7811 -737 -410 -41 C ATOM 3487 CZ PHE B 118 -93.659 -23.732 141.225 1.00 48.01 C ANISOU 3487 CZ PHE B 118 5569 4515 8158 -802 -403 -3 C ATOM 3488 N PRO B 119 -91.634 -30.465 139.034 1.00 41.81 N ANISOU 3488 N PRO B 119 4609 3671 7605 -783 -119 -845 N ATOM 3489 CA PRO B 119 -90.999 -31.786 139.015 1.00 37.80 C ANISOU 3489 CA PRO B 119 4115 3055 7191 -695 -55 -1010 C ATOM 3490 C PRO B 119 -89.690 -31.766 139.783 1.00 39.46 C ANISOU 3490 C PRO B 119 4265 3253 7475 -546 -17 -998 C ATOM 3491 O PRO B 119 -89.210 -30.692 140.176 1.00 44.24 O ANISOU 3491 O PRO B 119 4808 3959 8041 -552 -34 -885 O ATOM 3492 CB PRO B 119 -90.762 -32.047 137.516 1.00 41.44 C ANISOU 3492 CB PRO B 119 4566 3666 7514 -770 -2 -1185 C ATOM 3493 CG PRO B 119 -91.517 -30.964 136.783 1.00 49.20 C ANISOU 3493 CG PRO B 119 5543 4821 8331 -911 -55 -1090 C ATOM 3494 CD PRO B 119 -91.569 -29.805 137.721 1.00 43.71 C ANISOU 3494 CD PRO B 119 4832 4114 7661 -889 -106 -878 C ATOM 3495 N PRO B 120 -89.083 -32.929 140.026 1.00 41.15 N ANISOU 3495 N PRO B 120 4497 3344 7792 -406 28 -1114 N ATOM 3496 CA PRO B 120 -87.792 -32.945 140.724 1.00 40.02 C ANISOU 3496 CA PRO B 120 4268 3232 7706 -237 53 -1111 C ATOM 3497 C PRO B 120 -86.688 -32.312 139.890 1.00 39.42 C ANISOU 3497 C PRO B 120 4055 3418 7505 -262 116 -1193 C ATOM 3498 O PRO B 120 -86.604 -32.514 138.676 1.00 42.56 O ANISOU 3498 O PRO B 120 4446 3925 7802 -326 176 -1332 O ATOM 3499 CB PRO B 120 -87.528 -34.438 140.951 1.00 38.28 C ANISOU 3499 CB PRO B 120 4126 2810 7610 -65 88 -1231 C ATOM 3500 CG PRO B 120 -88.876 -35.071 140.912 1.00 38.25 C ANISOU 3500 CG PRO B 120 4274 2604 7655 -173 61 -1224 C ATOM 3501 CD PRO B 120 -89.673 -34.275 139.925 1.00 37.56 C ANISOU 3501 CD PRO B 120 4163 2681 7428 -387 42 -1225 C ATOM 3502 N SER B 121 -85.845 -31.528 140.559 1.00 40.34 N ANISOU 3502 N SER B 121 4059 3650 7617 -228 104 -1108 N ATOM 3503 CA SER B 121 -84.635 -31.008 139.939 1.00 47.78 C ANISOU 3503 CA SER B 121 4845 4853 8454 -254 176 -1187 C ATOM 3504 C SER B 121 -83.699 -32.148 139.547 1.00 57.86 C ANISOU 3504 C SER B 121 6046 6177 9762 -68 255 -1388 C ATOM 3505 O SER B 121 -83.705 -33.224 140.151 1.00 56.21 O ANISOU 3505 O SER B 121 5896 5777 9683 128 238 -1428 O ATOM 3506 CB SER B 121 -83.924 -30.046 140.891 1.00 51.86 C ANISOU 3506 CB SER B 121 5255 5472 8979 -264 140 -1070 C ATOM 3507 OG SER B 121 -82.718 -29.562 140.325 1.00 65.48 O ANISOU 3507 OG SER B 121 6808 7469 10603 -318 217 -1151 O ATOM 3508 N SER B 122 -82.893 -31.906 138.508 1.00 59.10 N ANISOU 3508 N SER B 122 6079 6588 9789 -124 350 -1512 N ATOM 3509 CA SER B 122 -81.831 -32.848 138.165 1.00 63.40 C ANISOU 3509 CA SER B 122 6509 7234 10348 79 436 -1714 C ATOM 3510 C SER B 122 -80.869 -33.044 139.331 1.00 59.00 C ANISOU 3510 C SER B 122 5816 6704 9896 294 402 -1686 C ATOM 3511 O SER B 122 -80.385 -34.159 139.571 1.00 62.44 O ANISOU 3511 O SER B 122 6242 7058 10424 561 419 -1801 O ATOM 3512 CB SER B 122 -81.076 -32.362 136.928 1.00 72.77 C ANISOU 3512 CB SER B 122 7551 8749 11351 -43 552 -1833 C ATOM 3513 OG SER B 122 -81.968 -31.943 135.911 1.00 80.21 O ANISOU 3513 OG SER B 122 8614 9702 12160 -262 565 -1815 O ATOM 3514 N GLU B 123 -80.575 -31.964 140.063 1.00 51.23 N ANISOU 3514 N GLU B 123 4736 5834 8894 189 350 -1538 N ATOM 3515 CA GLU B 123 -79.640 -32.051 141.179 1.00 54.94 C ANISOU 3515 CA GLU B 123 5054 6382 9438 373 304 -1513 C ATOM 3516 C GLU B 123 -80.123 -33.043 142.227 1.00 61.04 C ANISOU 3516 C GLU B 123 5972 6852 10367 608 220 -1452 C ATOM 3517 O GLU B 123 -79.315 -33.741 142.851 1.00 67.38 O ANISOU 3517 O GLU B 123 6684 7680 11238 876 202 -1498 O ATOM 3518 CB GLU B 123 -79.444 -30.673 141.808 1.00 57.97 C ANISOU 3518 CB GLU B 123 5355 6901 9770 173 251 -1366 C ATOM 3519 CG GLU B 123 -79.454 -29.523 140.821 1.00 66.59 C ANISOU 3519 CG GLU B 123 6421 8171 10709 -135 319 -1351 C ATOM 3520 CD GLU B 123 -78.797 -28.285 141.385 1.00 81.13 C ANISOU 3520 CD GLU B 123 8135 10195 12498 -309 294 -1264 C ATOM 3521 OE1 GLU B 123 -78.200 -28.384 142.477 1.00 86.51 O ANISOU 3521 OE1 GLU B 123 8700 10922 13248 -176 228 -1251 O ATOM 3522 OE2 GLU B 123 -78.884 -27.216 140.744 1.00 84.86 O ANISOU 3522 OE2 GLU B 123 8634 10757 12852 -581 338 -1209 O ATOM 3523 N GLN B 124 -81.439 -33.122 142.431 1.00 56.96 N ANISOU 3523 N GLN B 124 5682 6060 9902 514 169 -1343 N ATOM 3524 CA GLN B 124 -81.976 -34.066 143.402 1.00 53.01 C ANISOU 3524 CA GLN B 124 5340 5262 9539 696 104 -1269 C ATOM 3525 C GLN B 124 -81.970 -35.484 142.848 1.00 53.78 C ANISOU 3525 C GLN B 124 5547 5182 9704 881 163 -1427 C ATOM 3526 O GLN B 124 -81.703 -36.440 143.585 1.00 49.60 O ANISOU 3526 O GLN B 124 5083 4481 9281 1136 136 -1418 O ATOM 3527 CB GLN B 124 -83.390 -33.655 143.811 1.00 39.46 C ANISOU 3527 CB GLN B 124 3804 3345 7846 515 43 -1106 C ATOM 3528 CG GLN B 124 -83.971 -34.487 144.941 1.00 40.81 C ANISOU 3528 CG GLN B 124 4132 3232 8140 658 -18 -997 C ATOM 3529 CD GLN B 124 -85.356 -34.026 145.351 1.00 39.17 C ANISOU 3529 CD GLN B 124 4062 2881 7941 473 -66 -844 C ATOM 3530 OE1 GLN B 124 -85.977 -33.209 144.672 1.00 37.72 O ANISOU 3530 OE1 GLN B 124 3875 2779 7678 260 -60 -835 O ATOM 3531 NE2 GLN B 124 -85.845 -34.546 146.470 1.00 43.34 N ANISOU 3531 NE2 GLN B 124 4706 3207 8552 563 -114 -719 N ATOM 3532 N LEU B 125 -82.268 -35.639 141.554 1.00 54.68 N ANISOU 3532 N LEU B 125 5700 5326 9750 760 242 -1572 N ATOM 3533 CA LEU B 125 -82.226 -36.961 140.941 1.00 52.21 C ANISOU 3533 CA LEU B 125 5502 4845 9492 923 306 -1758 C ATOM 3534 C LEU B 125 -80.826 -37.555 140.983 1.00 53.54 C ANISOU 3534 C LEU B 125 5517 5148 9678 1233 354 -1897 C ATOM 3535 O LEU B 125 -80.676 -38.779 141.070 1.00 57.51 O ANISOU 3535 O LEU B 125 6146 5428 10279 1482 373 -1995 O ATOM 3536 CB LEU B 125 -82.734 -36.895 139.501 1.00 52.05 C ANISOU 3536 CB LEU B 125 5525 4893 9358 719 378 -1905 C ATOM 3537 CG LEU B 125 -84.201 -36.494 139.332 1.00 44.71 C ANISOU 3537 CG LEU B 125 4748 3834 8407 445 326 -1797 C ATOM 3538 CD1 LEU B 125 -84.489 -36.101 137.894 1.00 45.80 C ANISOU 3538 CD1 LEU B 125 4865 4157 8380 240 384 -1918 C ATOM 3539 CD2 LEU B 125 -85.113 -37.627 139.775 1.00 45.19 C ANISOU 3539 CD2 LEU B 125 5042 3522 8606 491 296 -1794 C ATOM 3540 N THR B 126 -79.791 -36.714 140.928 1.00 57.83 N ANISOU 3540 N THR B 126 5791 6054 10127 1226 374 -1908 N ATOM 3541 CA THR B 126 -78.438 -37.234 141.097 1.00 61.80 C ANISOU 3541 CA THR B 126 6101 6735 10644 1541 407 -2030 C ATOM 3542 C THR B 126 -78.153 -37.671 142.528 1.00 57.69 C ANISOU 3542 C THR B 126 5601 6077 10244 1806 302 -1894 C ATOM 3543 O THR B 126 -77.159 -38.368 142.757 1.00 65.75 O ANISOU 3543 O THR B 126 6508 7174 11298 2140 311 -1988 O ATOM 3544 CB THR B 126 -77.403 -36.192 140.665 1.00 66.05 C ANISOU 3544 CB THR B 126 6319 7737 11040 1424 462 -2081 C ATOM 3545 OG1 THR B 126 -77.531 -35.018 141.479 1.00 75.79 O ANISOU 3545 OG1 THR B 126 7484 9063 12251 1222 376 -1880 O ATOM 3546 CG2 THR B 126 -77.591 -35.825 139.200 1.00 59.83 C ANISOU 3546 CG2 THR B 126 5519 7106 10109 1186 578 -2213 C ATOM 3547 N SER B 127 -78.992 -37.286 143.487 1.00 52.73 N ANISOU 3547 N SER B 127 5107 5264 9665 1682 203 -1677 N ATOM 3548 CA SER B 127 -78.943 -37.815 144.843 1.00 56.08 C ANISOU 3548 CA SER B 127 5613 5505 10191 1919 103 -1529 C ATOM 3549 C SER B 127 -79.792 -39.068 145.022 1.00 59.22 C ANISOU 3549 C SER B 127 6337 5451 10713 2038 102 -1506 C ATOM 3550 O SER B 127 -79.860 -39.599 146.135 1.00 58.17 O ANISOU 3550 O SER B 127 6357 5181 10563 2174 31 -1322 O ATOM 3551 CB SER B 127 -79.391 -36.745 145.844 1.00 59.76 C ANISOU 3551 CB SER B 127 6056 6020 10630 1724 6 -1312 C ATOM 3552 OG SER B 127 -78.602 -35.574 145.728 1.00 72.74 O ANISOU 3552 OG SER B 127 7426 8049 12164 1586 6 -1334 O ATOM 3553 N GLY B 128 -80.434 -39.551 143.960 1.00 56.87 N ANISOU 3553 N GLY B 128 6194 4990 10423 1919 184 -1644 N ATOM 3554 CA GLY B 128 -81.353 -40.665 144.055 1.00 52.16 C ANISOU 3554 CA GLY B 128 5948 4030 9842 1901 188 -1586 C ATOM 3555 C GLY B 128 -82.712 -40.327 144.624 1.00 54.44 C ANISOU 3555 C GLY B 128 6404 4148 10133 1623 132 -1385 C ATOM 3556 O GLY B 128 -83.559 -41.222 144.737 1.00 55.49 O ANISOU 3556 O GLY B 128 6815 4029 10240 1555 140 -1322 O ATOM 3557 N GLY B 129 -82.950 -39.067 144.990 1.00 50.81 N ANISOU 3557 N GLY B 129 4268 6792 8245 1422 -1655 -1900 N ATOM 3558 CA GLY B 129 -84.235 -38.634 145.490 1.00 47.95 C ANISOU 3558 CA GLY B 129 4210 6361 7650 1392 -1597 -1494 C ATOM 3559 C GLY B 129 -85.032 -37.905 144.418 1.00 43.95 C ANISOU 3559 C GLY B 129 3772 5570 7358 802 -1261 -1227 C ATOM 3560 O GLY B 129 -84.513 -37.504 143.380 1.00 41.24 O ANISOU 3560 O GLY B 129 3250 5091 7329 443 -1048 -1391 O ATOM 3561 N ALA B 130 -86.325 -37.739 144.689 1.00 43.09 N ANISOU 3561 N ALA B 130 3955 5361 7057 757 -1193 -814 N ATOM 3562 CA ALA B 130 -87.218 -37.085 143.738 1.00 46.42 C ANISOU 3562 CA ALA B 130 4487 5547 7603 319 -945 -560 C ATOM 3563 C ALA B 130 -88.372 -36.484 144.525 1.00 41.97 C ANISOU 3563 C ALA B 130 4073 4982 6891 366 -972 -348 C ATOM 3564 O ALA B 130 -89.230 -37.217 145.023 1.00 42.34 O ANISOU 3564 O ALA B 130 4368 4988 6729 544 -973 -32 O ATOM 3565 CB ALA B 130 -87.722 -38.069 142.685 1.00 34.87 C ANISOU 3565 CB ALA B 130 3246 3897 6106 174 -805 -241 C ATOM 3566 N SER B 131 -88.401 -35.162 144.634 1.00 38.27 N ANISOU 3566 N SER B 131 3451 4514 6575 200 -934 -530 N ATOM 3567 CA SER B 131 -89.503 -34.463 145.279 1.00 34.80 C ANISOU 3567 CA SER B 131 3132 4059 6030 207 -941 -352 C ATOM 3568 C SER B 131 -90.329 -33.748 144.220 1.00 34.40 C ANISOU 3568 C SER B 131 3197 3773 6103 -149 -728 -137 C ATOM 3569 O SER B 131 -89.824 -32.855 143.530 1.00 46.50 O ANISOU 3569 O SER B 131 4618 5192 7857 -373 -556 -305 O ATOM 3570 CB SER B 131 -88.988 -33.470 146.321 1.00 37.00 C ANISOU 3570 CB SER B 131 3160 4529 6370 360 -1091 -755 C ATOM 3571 OG SER B 131 -88.445 -34.143 147.444 1.00 39.41 O ANISOU 3571 OG SER B 131 3443 5107 6425 848 -1362 -936 O ATOM 3572 N VAL B 132 -91.592 -34.138 144.099 1.00 31.23 N ANISOU 3572 N VAL B 132 3019 3274 5572 -161 -709 204 N ATOM 3573 CA VAL B 132 -92.579 -33.356 143.368 1.00 36.45 C ANISOU 3573 CA VAL B 132 3793 3776 6280 -361 -607 364 C ATOM 3574 C VAL B 132 -93.218 -32.385 144.346 1.00 36.77 C ANISOU 3574 C VAL B 132 3804 3857 6311 -317 -645 354 C ATOM 3575 O VAL B 132 -93.630 -32.779 145.443 1.00 41.25 O ANISOU 3575 O VAL B 132 4396 4523 6753 -119 -729 414 O ATOM 3576 CB VAL B 132 -93.634 -34.264 142.717 1.00 37.55 C ANISOU 3576 CB VAL B 132 4091 3810 6365 -377 -614 598 C ATOM 3577 CG1 VAL B 132 -94.467 -33.476 141.725 1.00 36.12 C ANISOU 3577 CG1 VAL B 132 4024 3512 6189 -489 -579 673 C ATOM 3578 CG2 VAL B 132 -92.959 -35.442 142.031 1.00 36.18 C ANISOU 3578 CG2 VAL B 132 3927 3627 6193 -364 -604 575 C ATOM 3579 N VAL B 133 -93.311 -31.117 143.961 1.00 37.19 N ANISOU 3579 N VAL B 133 3841 3805 6483 -471 -536 296 N ATOM 3580 CA VAL B 133 -93.788 -30.090 144.880 1.00 37.79 C ANISOU 3580 CA VAL B 133 3854 3913 6592 -443 -564 230 C ATOM 3581 C VAL B 133 -95.045 -29.446 144.317 1.00 42.14 C ANISOU 3581 C VAL B 133 4576 4305 7130 -526 -504 453 C ATOM 3582 O VAL B 133 -95.167 -29.248 143.105 1.00 51.25 O ANISOU 3582 O VAL B 133 5883 5308 8283 -603 -396 556 O ATOM 3583 CB VAL B 133 -92.698 -29.030 145.151 1.00 37.51 C ANISOU 3583 CB VAL B 133 3579 3876 6797 -520 -472 -143 C ATOM 3584 CG1 VAL B 133 -93.178 -28.007 146.174 1.00 33.25 C ANISOU 3584 CG1 VAL B 133 2946 3386 6300 -469 -526 -266 C ATOM 3585 CG2 VAL B 133 -91.418 -29.699 145.632 1.00 39.63 C ANISOU 3585 CG2 VAL B 133 3616 4339 7104 -383 -598 -470 C ATOM 3586 N CYS B 134 -95.983 -29.130 145.208 1.00 39.92 N ANISOU 3586 N CYS B 134 4290 4071 6808 -449 -579 510 N ATOM 3587 CA CYS B 134 -97.229 -28.460 144.866 1.00 35.21 C ANISOU 3587 CA CYS B 134 3800 3354 6223 -481 -569 655 C ATOM 3588 C CYS B 134 -97.418 -27.273 145.793 1.00 37.76 C ANISOU 3588 C CYS B 134 4037 3690 6619 -474 -547 544 C ATOM 3589 O CYS B 134 -97.443 -27.437 147.016 1.00 29.83 O ANISOU 3589 O CYS B 134 2940 2838 5555 -356 -620 465 O ATOM 3590 CB CYS B 134 -98.422 -29.411 144.984 1.00 35.11 C ANISOU 3590 CB CYS B 134 3819 3349 6173 -413 -651 800 C ATOM 3591 SG CYS B 134 -99.759 -29.061 143.834 1.00 57.01 S ANISOU 3591 SG CYS B 134 6684 5995 8982 -405 -729 866 S ATOM 3592 N PHE B 135 -97.554 -26.088 145.216 1.00 30.30 N ANISOU 3592 N PHE B 135 3163 2573 5778 -554 -422 544 N ATOM 3593 CA PHE B 135 -97.855 -24.882 145.971 1.00 38.62 C ANISOU 3593 CA PHE B 135 4139 3589 6946 -563 -378 434 C ATOM 3594 C PHE B 135 -99.323 -24.546 145.773 1.00 39.41 C ANISOU 3594 C PHE B 135 4369 3617 6988 -494 -443 624 C ATOM 3595 O PHE B 135 -99.795 -24.473 144.633 1.00 49.30 O ANISOU 3595 O PHE B 135 5815 4742 8177 -448 -432 772 O ATOM 3596 CB PHE B 135 -96.981 -23.710 145.522 1.00 34.88 C ANISOU 3596 CB PHE B 135 3646 2894 6713 -695 -106 275 C ATOM 3597 CG PHE B 135 -95.545 -23.822 145.944 1.00 34.43 C ANISOU 3597 CG PHE B 135 3320 2912 6850 -772 -48 -79 C ATOM 3598 CD1 PHE B 135 -95.208 -24.333 147.186 1.00 41.21 C ANISOU 3598 CD1 PHE B 135 3948 4073 7636 -636 -299 -321 C ATOM 3599 CD2 PHE B 135 -94.531 -23.407 145.101 1.00 36.42 C ANISOU 3599 CD2 PHE B 135 3557 2923 7357 -931 279 -203 C ATOM 3600 CE1 PHE B 135 -93.885 -24.433 147.574 1.00 48.47 C ANISOU 3600 CE1 PHE B 135 4577 5108 8733 -628 -325 -744 C ATOM 3601 CE2 PHE B 135 -93.208 -23.506 145.481 1.00 43.28 C ANISOU 3601 CE2 PHE B 135 4088 3859 8497 -1007 326 -634 C ATOM 3602 CZ PHE B 135 -92.884 -24.018 146.718 1.00 46.93 C ANISOU 3602 CZ PHE B 135 4270 4678 8884 -841 -27 -938 C ATOM 3603 N LEU B 136 -100.038 -24.335 146.875 1.00 34.89 N ANISOU 3603 N LEU B 136 3693 3140 6422 -437 -520 583 N ATOM 3604 CA LEU B 136 -101.410 -23.841 146.849 1.00 35.54 C ANISOU 3604 CA LEU B 136 3824 3153 6528 -378 -569 677 C ATOM 3605 C LEU B 136 -101.364 -22.513 147.594 1.00 34.80 C ANISOU 3605 C LEU B 136 3661 3010 6551 -396 -487 541 C ATOM 3606 O LEU B 136 -101.270 -22.487 148.825 1.00 39.07 O ANISOU 3606 O LEU B 136 4062 3701 7081 -356 -517 402 O ATOM 3607 CB LEU B 136 -102.376 -24.833 147.498 1.00 44.28 C ANISOU 3607 CB LEU B 136 4851 4363 7612 -314 -643 731 C ATOM 3608 CG LEU B 136 -102.173 -26.336 147.254 1.00 47.31 C ANISOU 3608 CG LEU B 136 5234 4795 7946 -313 -653 796 C ATOM 3609 CD1 LEU B 136 -103.358 -27.120 147.768 1.00 48.70 C ANISOU 3609 CD1 LEU B 136 5330 4940 8236 -278 -594 833 C ATOM 3610 CD2 LEU B 136 -101.951 -26.663 145.790 1.00 48.51 C ANISOU 3610 CD2 LEU B 136 5477 4877 8077 -338 -725 831 C ATOM 3611 N ASN B 137 -101.419 -21.412 146.852 1.00 32.63 N ANISOU 3611 N ASN B 137 3517 2510 6370 -411 -360 575 N ATOM 3612 CA ASN B 137 -101.160 -20.094 147.409 1.00 39.95 C ANISOU 3612 CA ASN B 137 4371 3312 7497 -467 -203 408 C ATOM 3613 C ASN B 137 -102.433 -19.266 147.514 1.00 39.87 C ANISOU 3613 C ASN B 137 4432 3209 7509 -361 -241 490 C ATOM 3614 O ASN B 137 -103.285 -19.294 146.618 1.00 48.56 O ANISOU 3614 O ASN B 137 5724 4225 8500 -219 -316 678 O ATOM 3615 CB ASN B 137 -100.127 -19.349 146.560 1.00 50.85 C ANISOU 3615 CB ASN B 137 5858 4401 9060 -572 119 368 C ATOM 3616 CG ASN B 137 -98.748 -19.970 146.647 1.00 51.33 C ANISOU 3616 CG ASN B 137 5741 4548 9212 -701 178 159 C ATOM 3617 OD1 ASN B 137 -98.371 -20.526 147.678 1.00 44.89 O ANISOU 3617 OD1 ASN B 137 4675 4012 8370 -686 -19 -66 O ATOM 3618 ND2 ASN B 137 -97.987 -19.882 145.562 1.00 55.59 N ANISOU 3618 ND2 ASN B 137 6437 4848 9838 -776 465 225 N ATOM 3619 N ASN B 138 -102.538 -18.525 148.622 1.00 42.19 N ANISOU 3619 N ASN B 138 4553 3540 7936 -387 -219 295 N ATOM 3620 CA ASN B 138 -103.478 -17.417 148.801 1.00 46.12 C ANISOU 3620 CA ASN B 138 5090 3894 8538 -316 -183 305 C ATOM 3621 C ASN B 138 -104.932 -17.878 148.650 1.00 45.98 C ANISOU 3621 C ASN B 138 5114 3962 8393 -163 -391 462 C ATOM 3622 O ASN B 138 -105.653 -17.490 147.729 1.00 42.14 O ANISOU 3622 O ASN B 138 4810 3328 7873 -9 -433 596 O ATOM 3623 CB ASN B 138 -103.151 -16.272 147.836 1.00 38.62 C ANISOU 3623 CB ASN B 138 4369 2562 7741 -314 106 383 C ATOM 3624 CG ASN B 138 -101.710 -15.814 147.950 1.00 47.41 C ANISOU 3624 CG ASN B 138 5362 3517 9134 -517 405 142 C ATOM 3625 OD1 ASN B 138 -100.841 -16.275 147.212 1.00 56.87 O ANISOU 3625 OD1 ASN B 138 6640 4638 10328 -588 546 188 O ATOM 3626 ND2 ASN B 138 -101.449 -14.911 148.888 1.00 45.92 N ANISOU 3626 ND2 ASN B 138 4934 3277 9237 -611 508 -182 N ATOM 3627 N PHE B 139 -105.344 -18.721 149.594 1.00 47.30 N ANISOU 3627 N PHE B 139 5109 4360 8504 -167 -498 408 N ATOM 3628 CA PHE B 139 -106.708 -19.224 149.633 1.00 40.80 C ANISOU 3628 CA PHE B 139 4221 3585 7697 -76 -611 458 C ATOM 3629 C PHE B 139 -107.302 -18.988 151.015 1.00 43.74 C ANISOU 3629 C PHE B 139 4442 4051 8126 -61 -546 347 C ATOM 3630 O PHE B 139 -106.586 -18.798 152.002 1.00 38.43 O ANISOU 3630 O PHE B 139 3731 3489 7380 -72 -474 237 O ATOM 3631 CB PHE B 139 -106.775 -20.720 149.286 1.00 35.25 C ANISOU 3631 CB PHE B 139 3485 2976 6931 -95 -670 529 C ATOM 3632 CG PHE B 139 -105.968 -21.598 150.205 1.00 36.92 C ANISOU 3632 CG PHE B 139 3663 3338 7027 -146 -569 529 C ATOM 3633 CD1 PHE B 139 -106.524 -22.105 151.371 1.00 41.99 C ANISOU 3633 CD1 PHE B 139 4234 4058 7660 -92 -445 522 C ATOM 3634 CD2 PHE B 139 -104.656 -21.920 149.902 1.00 38.68 C ANISOU 3634 CD2 PHE B 139 3955 3609 7134 -196 -570 535 C ATOM 3635 CE1 PHE B 139 -105.787 -22.911 152.217 1.00 33.32 C ANISOU 3635 CE1 PHE B 139 3202 3097 6363 -15 -346 553 C ATOM 3636 CE2 PHE B 139 -103.914 -22.729 150.745 1.00 42.23 C ANISOU 3636 CE2 PHE B 139 4389 4222 7434 -149 -529 507 C ATOM 3637 CZ PHE B 139 -104.481 -23.224 151.903 1.00 39.71 C ANISOU 3637 CZ PHE B 139 4066 3992 7030 -22 -429 533 C ATOM 3638 N TYR B 140 -108.635 -18.992 151.069 1.00 46.47 N ANISOU 3638 N TYR B 140 4688 4360 8606 5 -579 327 N ATOM 3639 CA TYR B 140 -109.379 -18.877 152.310 1.00 44.81 C ANISOU 3639 CA TYR B 140 4351 4207 8469 32 -452 241 C ATOM 3640 C TYR B 140 -110.722 -19.548 152.072 1.00 40.30 C ANISOU 3640 C TYR B 140 3610 3575 8126 50 -441 200 C ATOM 3641 O TYR B 140 -111.313 -19.358 150.998 1.00 37.96 O ANISOU 3641 O TYR B 140 3266 3203 7955 118 -645 138 O ATOM 3642 CB TYR B 140 -109.585 -17.424 152.755 1.00 47.18 C ANISOU 3642 CB TYR B 140 4635 4449 8844 75 -449 126 C ATOM 3643 CG TYR B 140 -110.231 -17.300 154.118 1.00 47.33 C ANISOU 3643 CG TYR B 140 4549 4550 8883 127 -296 26 C ATOM 3644 CD1 TYR B 140 -109.456 -17.209 155.266 1.00 51.53 C ANISOU 3644 CD1 TYR B 140 5125 5244 9209 186 -209 -60 C ATOM 3645 CD2 TYR B 140 -111.613 -17.290 154.259 1.00 39.59 C ANISOU 3645 CD2 TYR B 140 3422 3497 8124 163 -240 -26 C ATOM 3646 CE1 TYR B 140 -110.037 -17.105 156.513 1.00 49.35 C ANISOU 3646 CE1 TYR B 140 4826 5056 8870 309 -47 -136 C ATOM 3647 CE2 TYR B 140 -112.203 -17.189 155.504 1.00 40.99 C ANISOU 3647 CE2 TYR B 140 3536 3721 8319 218 -22 -101 C ATOM 3648 CZ TYR B 140 -111.410 -17.095 156.626 1.00 49.55 C ANISOU 3648 CZ TYR B 140 4742 4965 9118 306 85 -125 C ATOM 3649 OH TYR B 140 -111.994 -16.992 157.868 1.00 57.76 O ANISOU 3649 OH TYR B 140 5787 6062 10096 434 322 -185 O ATOM 3650 N PRO B 141 -111.237 -20.329 153.037 1.00 41.22 N ANISOU 3650 N PRO B 141 3636 3704 8321 30 -182 193 N ATOM 3651 CA PRO B 141 -110.655 -20.634 154.349 1.00 43.83 C ANISOU 3651 CA PRO B 141 4104 4142 8409 87 65 276 C ATOM 3652 C PRO B 141 -109.498 -21.621 154.263 1.00 48.69 C ANISOU 3652 C PRO B 141 4883 4846 8770 98 78 414 C ATOM 3653 O PRO B 141 -109.179 -22.094 153.172 1.00 42.95 O ANISOU 3653 O PRO B 141 4143 4079 8096 8 -72 451 O ATOM 3654 CB PRO B 141 -111.829 -21.252 155.124 1.00 46.96 C ANISOU 3654 CB PRO B 141 4396 4423 9025 102 430 262 C ATOM 3655 CG PRO B 141 -113.053 -20.983 154.291 1.00 46.29 C ANISOU 3655 CG PRO B 141 4015 4195 9378 20 307 67 C ATOM 3656 CD PRO B 141 -112.566 -20.940 152.886 1.00 40.09 C ANISOU 3656 CD PRO B 141 3242 3438 8553 0 -75 58 C ATOM 3657 N LYS B 142 -108.872 -21.921 155.403 1.00 58.35 N ANISOU 3657 N LYS B 142 6277 6207 9687 266 236 467 N ATOM 3658 CA LYS B 142 -107.737 -22.835 155.405 1.00 55.47 C ANISOU 3658 CA LYS B 142 6074 5950 9052 350 219 568 C ATOM 3659 C LYS B 142 -108.150 -24.282 155.180 1.00 51.40 C ANISOU 3659 C LYS B 142 5608 5274 8648 318 488 749 C ATOM 3660 O LYS B 142 -107.274 -25.140 155.030 1.00 53.13 O ANISOU 3660 O LYS B 142 5962 5546 8680 383 478 851 O ATOM 3661 CB LYS B 142 -106.968 -22.721 156.723 1.00 57.38 C ANISOU 3661 CB LYS B 142 6502 6424 8875 666 252 513 C ATOM 3662 CG LYS B 142 -107.807 -22.995 157.961 1.00 63.83 C ANISOU 3662 CG LYS B 142 7487 7211 9556 904 629 614 C ATOM 3663 CD LYS B 142 -106.951 -22.983 159.219 1.00 69.08 C ANISOU 3663 CD LYS B 142 8409 8162 9676 1356 602 543 C ATOM 3664 CE LYS B 142 -107.809 -22.979 160.477 1.00 73.43 C ANISOU 3664 CE LYS B 142 9183 8687 10029 1652 994 635 C ATOM 3665 NZ LYS B 142 -108.643 -24.208 160.594 1.00 77.27 N ANISOU 3665 NZ LYS B 142 9869 8863 10628 1662 1569 977 N ATOM 3666 N ASP B 143 -109.449 -24.570 155.149 1.00 51.77 N ANISOU 3666 N ASP B 143 5513 5102 9056 216 747 744 N ATOM 3667 CA ASP B 143 -109.944 -25.931 154.955 1.00 58.42 C ANISOU 3667 CA ASP B 143 6331 5710 10156 144 1093 836 C ATOM 3668 C ASP B 143 -109.722 -26.332 153.502 1.00 54.01 C ANISOU 3668 C ASP B 143 5600 5124 9796 -44 788 748 C ATOM 3669 O ASP B 143 -110.499 -25.965 152.618 1.00 58.44 O ANISOU 3669 O ASP B 143 5890 5623 10691 -174 583 539 O ATOM 3670 CB ASP B 143 -111.418 -26.014 155.333 1.00 73.07 C ANISOU 3670 CB ASP B 143 7986 7310 12467 61 1486 735 C ATOM 3671 CG ASP B 143 -111.675 -25.592 156.767 1.00 86.42 C ANISOU 3671 CG ASP B 143 9892 9020 13925 280 1834 836 C ATOM 3672 OD1 ASP B 143 -110.995 -26.116 157.674 1.00 93.00 O ANISOU 3672 OD1 ASP B 143 11106 9910 14318 560 2088 1068 O ATOM 3673 OD2 ASP B 143 -112.557 -24.735 156.987 1.00 95.30 O ANISOU 3673 OD2 ASP B 143 10825 10115 15271 228 1841 670 O ATOM 3674 N ILE B 144 -108.656 -27.086 153.247 1.00 44.77 N ANISOU 3674 N ILE B 144 4601 4022 8388 -2 736 881 N ATOM 3675 CA ILE B 144 -108.331 -27.546 151.904 1.00 39.56 C ANISOU 3675 CA ILE B 144 3828 3350 7854 -144 474 811 C ATOM 3676 C ILE B 144 -107.877 -28.997 151.984 1.00 44.63 C ANISOU 3676 C ILE B 144 4595 3877 8485 -118 745 958 C ATOM 3677 O ILE B 144 -107.345 -29.444 153.004 1.00 49.28 O ANISOU 3677 O ILE B 144 5460 4484 8781 86 1011 1162 O ATOM 3678 CB ILE B 144 -107.258 -26.653 151.242 1.00 34.62 C ANISOU 3678 CB ILE B 144 3278 2935 6941 -136 57 792 C ATOM 3679 CG1 ILE B 144 -107.245 -26.860 149.728 1.00 33.76 C ANISOU 3679 CG1 ILE B 144 3068 2793 6964 -238 -205 698 C ATOM 3680 CG2 ILE B 144 -105.881 -26.928 151.833 1.00 34.06 C ANISOU 3680 CG2 ILE B 144 3427 3026 6490 0 63 908 C ATOM 3681 CD1 ILE B 144 -106.386 -25.861 148.997 1.00 38.20 C ANISOU 3681 CD1 ILE B 144 3740 3463 7310 -226 -481 698 C ATOM 3682 N ASN B 145 -108.104 -29.743 150.903 1.00 47.48 N ANISOU 3682 N ASN B 145 4774 4119 9149 -271 673 835 N ATOM 3683 CA ASN B 145 -107.715 -31.147 150.850 1.00 43.41 C ANISOU 3683 CA ASN B 145 4347 3446 8700 -273 944 945 C ATOM 3684 C ASN B 145 -106.834 -31.368 149.632 1.00 38.66 C ANISOU 3684 C ASN B 145 3730 2985 7974 -330 553 888 C ATOM 3685 O ASN B 145 -107.151 -30.889 148.539 1.00 43.93 O ANISOU 3685 O ASN B 145 4207 3719 8766 -414 204 674 O ATOM 3686 CB ASN B 145 -108.939 -32.066 150.802 1.00 52.82 C ANISOU 3686 CB ASN B 145 5278 4274 10517 -424 1371 779 C ATOM 3687 CG ASN B 145 -108.582 -33.524 151.012 1.00 63.98 C ANISOU 3687 CG ASN B 145 6847 5445 12017 -396 1813 936 C ATOM 3688 OD1 ASN B 145 -108.209 -34.226 150.072 1.00 67.02 O ANISOU 3688 OD1 ASN B 145 7137 5859 12469 -467 1629 813 O ATOM 3689 ND2 ASN B 145 -108.695 -33.987 152.251 1.00 71.71 N ANISOU 3689 ND2 ASN B 145 8116 6265 12867 -210 2380 1183 N ATOM 3690 N VAL B 146 -105.733 -32.097 149.818 1.00 37.58 N ANISOU 3690 N VAL B 146 3823 2894 7563 -229 622 1076 N ATOM 3691 CA VAL B 146 -104.760 -32.344 148.760 1.00 41.69 C ANISOU 3691 CA VAL B 146 4356 3542 7943 -272 310 1039 C ATOM 3692 C VAL B 146 -104.535 -33.842 148.618 1.00 41.35 C ANISOU 3692 C VAL B 146 4354 3309 8049 -277 570 1103 C ATOM 3693 O VAL B 146 -104.206 -34.524 149.595 1.00 37.55 O ANISOU 3693 O VAL B 146 4109 2732 7428 -101 915 1324 O ATOM 3694 CB VAL B 146 -103.419 -31.638 149.034 1.00 40.05 C ANISOU 3694 CB VAL B 146 4334 3601 7282 -143 83 1124 C ATOM 3695 CG1 VAL B 146 -102.534 -31.682 147.796 1.00 31.83 C ANISOU 3695 CG1 VAL B 146 3270 2652 6170 -230 -193 1049 C ATOM 3696 CG2 VAL B 146 -103.645 -30.210 149.491 1.00 42.83 C ANISOU 3696 CG2 VAL B 146 4663 4075 7536 -120 -47 1065 C ATOM 3697 N LYS B 147 -104.715 -34.346 147.402 1.00 35.91 N ANISOU 3697 N LYS B 147 3466 2562 7617 -424 409 901 N ATOM 3698 CA LYS B 147 -104.426 -35.723 147.041 1.00 40.59 C ANISOU 3698 CA LYS B 147 4054 2975 8391 -459 600 900 C ATOM 3699 C LYS B 147 -103.311 -35.754 146.004 1.00 41.70 C ANISOU 3699 C LYS B 147 4254 3328 8263 -454 229 870 C ATOM 3700 O LYS B 147 -103.196 -34.858 145.159 1.00 33.45 O ANISOU 3700 O LYS B 147 3162 2474 7074 -478 -140 750 O ATOM 3701 CB LYS B 147 -105.671 -36.429 146.488 1.00 39.95 C ANISOU 3701 CB LYS B 147 3628 2661 8892 -612 755 561 C ATOM 3702 CG LYS B 147 -106.700 -36.788 147.548 1.00 58.59 C ANISOU 3702 CG LYS B 147 5949 4809 11503 -584 1284 555 C ATOM 3703 CD LYS B 147 -108.110 -36.809 146.976 1.00 75.52 C ANISOU 3703 CD LYS B 147 7660 6869 14164 -684 1257 80 C ATOM 3704 CE LYS B 147 -108.229 -37.796 145.826 1.00 82.09 C ANISOU 3704 CE LYS B 147 8244 7657 15287 -731 1136 -276 C ATOM 3705 NZ LYS B 147 -109.642 -37.979 145.389 1.00 79.99 N ANISOU 3705 NZ LYS B 147 7543 7276 15572 -748 1160 -814 N ATOM 3706 N TRP B 148 -102.472 -36.782 146.089 1.00 40.32 N ANISOU 3706 N TRP B 148 4221 3090 8007 -391 380 1000 N ATOM 3707 CA TRP B 148 -101.426 -37.031 145.108 1.00 33.82 C ANISOU 3707 CA TRP B 148 3431 2418 7001 -399 111 950 C ATOM 3708 C TRP B 148 -101.768 -38.285 144.320 1.00 36.57 C ANISOU 3708 C TRP B 148 3618 2552 7724 -503 218 773 C ATOM 3709 O TRP B 148 -102.116 -39.316 144.906 1.00 37.93 O ANISOU 3709 O TRP B 148 3797 2430 8186 -502 635 837 O ATOM 3710 CB TRP B 148 -100.062 -37.178 145.781 1.00 33.13 C ANISOU 3710 CB TRP B 148 3590 2470 6527 -210 131 1160 C ATOM 3711 CG TRP B 148 -99.459 -35.871 146.168 1.00 35.57 C ANISOU 3711 CG TRP B 148 3958 3040 6516 -138 -92 1171 C ATOM 3712 CD1 TRP B 148 -99.483 -35.290 147.400 1.00 32.67 C ANISOU 3712 CD1 TRP B 148 3696 2752 5964 32 -17 1264 C ATOM 3713 CD2 TRP B 148 -98.729 -34.981 145.317 1.00 42.94 C ANISOU 3713 CD2 TRP B 148 4846 4152 7318 -225 -372 1051 C ATOM 3714 NE1 TRP B 148 -98.819 -34.088 147.369 1.00 34.87 N ANISOU 3714 NE1 TRP B 148 3932 3253 6062 26 -268 1151 N ATOM 3715 CE2 TRP B 148 -98.345 -33.876 146.101 1.00 37.52 C ANISOU 3715 CE2 TRP B 148 4184 3617 6454 -146 -439 1038 C ATOM 3716 CE3 TRP B 148 -98.363 -35.010 143.968 1.00 29.19 C ANISOU 3716 CE3 TRP B 148 3067 2428 5596 -337 -520 946 C ATOM 3717 CZ2 TRP B 148 -97.613 -32.810 145.582 1.00 29.99 C ANISOU 3717 CZ2 TRP B 148 3187 2772 5436 -226 -585 914 C ATOM 3718 CZ3 TRP B 148 -97.638 -33.952 143.454 1.00 37.09 C ANISOU 3718 CZ3 TRP B 148 4099 3539 6456 -377 -636 887 C ATOM 3719 CH2 TRP B 148 -97.271 -32.867 144.260 1.00 37.79 C ANISOU 3719 CH2 TRP B 148 4180 3717 6461 -347 -638 867 C ATOM 3720 N LYS B 149 -101.675 -38.194 142.997 1.00 39.14 N ANISOU 3720 N LYS B 149 3822 3002 8049 -562 -116 538 N ATOM 3721 CA LYS B 149 -101.951 -39.319 142.117 1.00 46.25 C ANISOU 3721 CA LYS B 149 4527 3752 9293 -637 -101 270 C ATOM 3722 C LYS B 149 -100.720 -39.633 141.281 1.00 49.04 C ANISOU 3722 C LYS B 149 5022 4263 9346 -587 -294 302 C ATOM 3723 O LYS B 149 -100.119 -38.737 140.678 1.00 50.90 O ANISOU 3723 O LYS B 149 5387 4741 9212 -527 -571 335 O ATOM 3724 CB LYS B 149 -103.163 -39.036 141.225 1.00 44.23 C ANISOU 3724 CB LYS B 149 3954 3513 9339 -669 -358 -166 C ATOM 3725 CG LYS B 149 -104.470 -38.968 142.006 1.00 47.51 C ANISOU 3725 CG LYS B 149 4144 3741 10166 -730 -98 -299 C ATOM 3726 CD LYS B 149 -105.662 -38.670 141.115 1.00 51.75 C ANISOU 3726 CD LYS B 149 4335 4359 10970 -674 -417 -820 C ATOM 3727 CE LYS B 149 -106.938 -38.569 141.936 1.00 59.56 C ANISOU 3727 CE LYS B 149 5124 5204 12303 -686 -113 -960 C ATOM 3728 NZ LYS B 149 -108.125 -38.258 141.094 1.00 69.07 N ANISOU 3728 NZ LYS B 149 5984 6495 13764 -562 -450 -1526 N ATOM 3729 N ILE B 150 -100.344 -40.906 141.269 1.00 47.95 N ANISOU 3729 N ILE B 150 4875 3944 9401 -610 -77 301 N ATOM 3730 CA ILE B 150 -99.311 -41.440 140.394 1.00 40.40 C ANISOU 3730 CA ILE B 150 3990 3090 8269 -579 -223 259 C ATOM 3731 C ILE B 150 -99.986 -42.418 139.442 1.00 43.03 C ANISOU 3731 C ILE B 150 4050 3269 9031 -656 -252 -140 C ATOM 3732 O ILE B 150 -100.572 -43.417 139.882 1.00 48.75 O ANISOU 3732 O ILE B 150 4619 3676 10228 -736 99 -232 O ATOM 3733 CB ILE B 150 -98.189 -42.115 141.196 1.00 37.65 C ANISOU 3733 CB ILE B 150 3859 2683 7764 -481 14 554 C ATOM 3734 CG1 ILE B 150 -97.673 -41.166 142.279 1.00 35.11 C ANISOU 3734 CG1 ILE B 150 3733 2527 7080 -351 11 824 C ATOM 3735 CG2 ILE B 150 -97.061 -42.515 140.282 1.00 35.03 C ANISOU 3735 CG2 ILE B 150 3577 2484 7247 -456 -155 489 C ATOM 3736 CD1 ILE B 150 -96.627 -41.780 143.183 1.00 36.35 C ANISOU 3736 CD1 ILE B 150 4105 2678 7029 -126 174 1049 C ATOM 3737 N ASP B 151 -99.929 -42.110 138.145 1.00 43.54 N ANISOU 3737 N ASP B 151 4070 3554 8918 -590 -635 -404 N ATOM 3738 CA ASP B 151 -100.578 -42.906 137.100 1.00 41.78 C ANISOU 3738 CA ASP B 151 3557 3275 9042 -586 -790 -906 C ATOM 3739 C ASP B 151 -102.020 -43.240 137.470 1.00 46.37 C ANISOU 3739 C ASP B 151 3757 3627 10235 -679 -640 -1252 C ATOM 3740 O ASP B 151 -102.498 -44.357 137.264 1.00 60.04 O ANISOU 3740 O ASP B 151 5257 5215 12340 -683 -435 -1548 O ATOM 3741 CB ASP B 151 -99.783 -44.178 136.806 1.00 42.48 C ANISOU 3741 CB ASP B 151 3652 3227 9261 -632 -627 -932 C ATOM 3742 CG ASP B 151 -98.412 -43.887 136.235 1.00 55.10 C ANISOU 3742 CG ASP B 151 5560 5075 10300 -525 -786 -707 C ATOM 3743 OD1 ASP B 151 -98.256 -42.851 135.555 1.00 52.83 O ANISOU 3743 OD1 ASP B 151 5432 5053 9586 -392 -1067 -698 O ATOM 3744 OD2 ASP B 151 -97.491 -44.700 136.460 1.00 58.48 O ANISOU 3744 OD2 ASP B 151 6080 5403 10738 -555 -585 -548 O ATOM 3745 N GLY B 152 -102.719 -42.259 138.035 1.00 44.41 N ANISOU 3745 N GLY B 152 3492 3425 9956 -669 -672 -1179 N ATOM 3746 CA GLY B 152 -104.125 -42.394 138.333 1.00 47.70 C ANISOU 3746 CA GLY B 152 3607 3746 10772 -649 -513 -1493 C ATOM 3747 C GLY B 152 -104.444 -42.913 139.718 1.00 64.72 C ANISOU 3747 C GLY B 152 5794 5624 13171 -748 108 -1218 C ATOM 3748 O GLY B 152 -105.605 -42.828 140.138 1.00 75.73 O ANISOU 3748 O GLY B 152 6962 6914 14897 -745 293 -1427 O ATOM 3749 N SER B 153 -103.462 -43.443 140.444 1.00 56.58 N ANISOU 3749 N SER B 153 5059 4476 11964 -780 437 -777 N ATOM 3750 CA SER B 153 -103.708 -44.063 141.739 1.00 60.11 C ANISOU 3750 CA SER B 153 5616 4669 12555 -774 1046 -513 C ATOM 3751 C SER B 153 -103.256 -43.131 142.855 1.00 54.90 C ANISOU 3751 C SER B 153 5301 4085 11474 -709 1110 -37 C ATOM 3752 O SER B 153 -102.240 -42.446 142.729 1.00 49.95 O ANISOU 3752 O SER B 153 4895 3645 10438 -670 800 196 O ATOM 3753 CB SER B 153 -102.983 -45.405 141.846 1.00 70.52 C ANISOU 3753 CB SER B 153 7063 5801 13931 -747 1388 -379 C ATOM 3754 OG SER B 153 -103.176 -46.181 140.676 1.00 75.60 O ANISOU 3754 OG SER B 153 7397 6422 14907 -798 1240 -829 O ATOM 3755 N GLU B 154 -103.999 -43.128 143.957 1.00 53.66 N ANISOU 3755 N GLU B 154 5179 3772 11438 -672 1536 78 N ATOM 3756 CA GLU B 154 -103.700 -42.222 145.058 1.00 53.24 C ANISOU 3756 CA GLU B 154 5435 3802 10992 -565 1591 468 C ATOM 3757 C GLU B 154 -102.534 -42.726 145.898 1.00 62.86 C ANISOU 3757 C GLU B 154 7087 4992 11804 -353 1817 899 C ATOM 3758 O GLU B 154 -102.368 -43.931 146.105 1.00 73.78 O ANISOU 3758 O GLU B 154 8564 6179 13290 -274 2193 957 O ATOM 3759 CB GLU B 154 -104.926 -42.022 145.945 1.00 53.98 C ANISOU 3759 CB GLU B 154 5433 3740 11337 -562 1978 421 C ATOM 3760 CG GLU B 154 -106.088 -41.350 145.244 1.00 57.51 C ANISOU 3760 CG GLU B 154 5462 4245 12146 -694 1702 -21 C ATOM 3761 CD GLU B 154 -107.232 -41.054 146.188 1.00 66.47 C ANISOU 3761 CD GLU B 154 6507 5219 13530 -681 2090 -61 C ATOM 3762 OE1 GLU B 154 -106.964 -40.801 147.382 1.00 69.33 O ANISOU 3762 OE1 GLU B 154 7205 5543 13594 -564 2396 333 O ATOM 3763 OE2 GLU B 154 -108.397 -41.075 145.738 1.00 73.64 O ANISOU 3763 OE2 GLU B 154 7012 6040 14928 -747 2085 -518 O ATOM 3764 N ARG B 155 -101.726 -41.784 146.380 1.00 63.25 N ANISOU 3764 N ARG B 155 7391 5242 11398 -215 1574 1171 N ATOM 3765 CA ARG B 155 -100.549 -42.075 147.187 1.00 58.59 C ANISOU 3765 CA ARG B 155 7205 4702 10355 101 1660 1518 C ATOM 3766 C ARG B 155 -100.655 -41.328 148.507 1.00 63.26 C ANISOU 3766 C ARG B 155 8060 5369 10607 354 1790 1761 C ATOM 3767 O ARG B 155 -100.926 -40.122 148.523 1.00 64.73 O ANISOU 3767 O ARG B 155 8137 5694 10764 271 1535 1722 O ATOM 3768 CB ARG B 155 -99.266 -41.676 146.454 1.00 51.73 C ANISOU 3768 CB ARG B 155 6346 4044 9265 125 1180 1536 C ATOM 3769 CG ARG B 155 -98.011 -41.807 147.299 1.00 63.01 C ANISOU 3769 CG ARG B 155 8114 5657 10171 534 1136 1768 C ATOM 3770 CD ARG B 155 -97.153 -42.981 146.868 1.00 70.04 C ANISOU 3770 CD ARG B 155 9090 6453 11069 639 1188 1793 C ATOM 3771 NE ARG B 155 -96.058 -43.210 147.805 1.00 72.60 N ANISOU 3771 NE ARG B 155 9750 6940 10894 1136 1159 1982 N ATOM 3772 CZ ARG B 155 -95.043 -44.038 147.583 1.00 70.62 C ANISOU 3772 CZ ARG B 155 9598 6715 10518 1338 1098 1990 C ATOM 3773 NH1 ARG B 155 -94.972 -44.713 146.444 1.00 69.74 N ANISOU 3773 NH1 ARG B 155 9283 6464 10749 1044 1088 1844 N ATOM 3774 NH2 ARG B 155 -94.093 -44.182 148.498 1.00 66.48 N ANISOU 3774 NH2 ARG B 155 9367 6381 9510 1881 1010 2101 N ATOM 3775 N GLN B 156 -100.437 -42.043 149.609 1.00 70.14 N ANISOU 3775 N GLN B 156 9293 6158 11197 699 2185 1999 N ATOM 3776 CA GLN B 156 -100.561 -41.488 150.951 1.00 81.83 C ANISOU 3776 CA GLN B 156 11081 7723 12289 1032 2354 2209 C ATOM 3777 C GLN B 156 -99.221 -41.328 151.652 1.00 84.27 C ANISOU 3777 C GLN B 156 11749 8321 11949 1537 2090 2379 C ATOM 3778 O GLN B 156 -98.910 -40.243 152.155 1.00 82.24 O ANISOU 3778 O GLN B 156 11550 8325 11373 1739 1787 2389 O ATOM 3779 CB GLN B 156 -101.487 -42.372 151.799 1.00 98.31 C ANISOU 3779 CB GLN B 156 13325 9516 14511 1137 3061 2304 C ATOM 3780 CG GLN B 156 -102.873 -42.572 151.207 1.00111.54 C ANISOU 3780 CG GLN B 156 14571 10923 16886 713 3337 2031 C ATOM 3781 CD GLN B 156 -103.807 -41.415 151.504 1.00118.44 C ANISOU 3781 CD GLN B 156 15278 11838 17886 581 3288 1943 C ATOM 3782 OE1 GLN B 156 -103.630 -40.695 152.486 1.00120.28 O ANISOU 3782 OE1 GLN B 156 15802 12203 17695 852 3295 2155 O ATOM 3783 NE2 GLN B 156 -104.812 -41.234 150.654 1.00120.31 N ANISOU 3783 NE2 GLN B 156 15037 11980 18695 209 3212 1590 N ATOM 3784 N ASN B 157 -98.413 -42.384 151.696 1.00 84.59 N ANISOU 3784 N ASN B 157 11996 8348 11798 1782 2167 2452 N ATOM 3785 CA ASN B 157 -97.119 -42.321 152.360 1.00 88.75 C ANISOU 3785 CA ASN B 157 12810 9204 11708 2323 1860 2501 C ATOM 3786 C ASN B 157 -96.108 -41.585 151.491 1.00 80.99 C ANISOU 3786 C ASN B 157 11551 8496 10727 2252 1229 2307 C ATOM 3787 O ASN B 157 -96.069 -41.760 150.269 1.00 77.80 O ANISOU 3787 O ASN B 157 10860 7966 10734 1860 1127 2213 O ATOM 3788 CB ASN B 157 -96.613 -43.728 152.681 1.00103.62 C ANISOU 3788 CB ASN B 157 14995 10974 13404 2630 2167 2624 C ATOM 3789 CG ASN B 157 -96.600 -44.634 151.466 1.00114.64 C ANISOU 3789 CG ASN B 157 16154 12112 15293 2245 2247 2555 C ATOM 3790 OD1 ASN B 157 -97.542 -44.642 150.674 1.00116.73 O ANISOU 3790 OD1 ASN B 157 16098 12139 16113 1749 2398 2445 O ATOM 3791 ND2 ASN B 157 -95.528 -45.403 151.313 1.00119.89 N ANISOU 3791 ND2 ASN B 157 16951 12850 15752 2502 2115 2563 N ATOM 3792 N GLY B 158 -95.290 -40.755 152.131 1.00 73.35 N ANISOU 3792 N GLY B 158 10630 7929 9310 2646 818 2180 N ATOM 3793 CA GLY B 158 -94.336 -39.934 151.417 1.00 58.93 C ANISOU 3793 CA GLY B 158 8408 6466 7517 2453 244 1795 C ATOM 3794 C GLY B 158 -94.844 -38.563 151.049 1.00 53.98 C ANISOU 3794 C GLY B 158 7442 5959 7109 2006 45 1586 C ATOM 3795 O GLY B 158 -94.293 -37.937 150.136 1.00 50.49 O ANISOU 3795 O GLY B 158 6660 5668 6857 1668 -263 1304 O ATOM 3796 N VAL B 159 -95.878 -38.073 151.728 1.00 54.35 N ANISOU 3796 N VAL B 159 7600 5909 7139 2016 262 1728 N ATOM 3797 CA VAL B 159 -96.477 -36.775 151.443 1.00 45.31 C ANISOU 3797 CA VAL B 159 6174 4842 6200 1635 108 1560 C ATOM 3798 C VAL B 159 -96.334 -35.905 152.682 1.00 44.23 C ANISOU 3798 C VAL B 159 6141 4976 5689 2020 -32 1456 C ATOM 3799 O VAL B 159 -96.858 -36.244 153.751 1.00 51.17 O ANISOU 3799 O VAL B 159 7373 5771 6297 2409 265 1695 O ATOM 3800 CB VAL B 159 -97.953 -36.898 151.037 1.00 39.33 C ANISOU 3800 CB VAL B 159 5364 3728 5850 1260 460 1730 C ATOM 3801 CG1 VAL B 159 -98.513 -35.531 150.684 1.00 36.88 C ANISOU 3801 CG1 VAL B 159 4782 3518 5712 934 251 1547 C ATOM 3802 CG2 VAL B 159 -98.108 -37.865 149.872 1.00 38.44 C ANISOU 3802 CG2 VAL B 159 5132 3366 6109 957 576 1749 C ATOM 3803 N LEU B 160 -95.630 -34.791 152.536 1.00 41.73 N ANISOU 3803 N LEU B 160 5527 4954 5376 1926 -436 1080 N ATOM 3804 CA LEU B 160 -95.445 -33.820 153.602 1.00 44.74 C ANISOU 3804 CA LEU B 160 5897 5618 5483 2242 -639 845 C ATOM 3805 C LEU B 160 -96.278 -32.588 153.286 1.00 47.93 C ANISOU 3805 C LEU B 160 6070 5945 6194 1800 -629 773 C ATOM 3806 O LEU B 160 -96.368 -32.173 152.127 1.00 48.12 O ANISOU 3806 O LEU B 160 5849 5845 6591 1312 -666 714 O ATOM 3807 CB LEU B 160 -93.969 -33.442 153.749 1.00 47.55 C ANISOU 3807 CB LEU B 160 6010 6341 5716 2487 -1085 348 C ATOM 3808 CG LEU B 160 -93.460 -33.221 155.171 1.00 58.86 C ANISOU 3808 CG LEU B 160 7582 8138 6644 3199 -1333 86 C ATOM 3809 CD1 LEU B 160 -93.341 -34.548 155.901 1.00 66.87 C ANISOU 3809 CD1 LEU B 160 9111 9152 7144 3864 -1182 405 C ATOM 3810 CD2 LEU B 160 -92.124 -32.497 155.150 1.00 68.02 C ANISOU 3810 CD2 LEU B 160 8282 9646 7917 3278 -1812 -607 C ATOM 3811 N ASN B 161 -96.895 -32.005 154.309 1.00 46.88 N ANISOU 3811 N ASN B 161 6061 5884 5870 2022 -564 788 N ATOM 3812 CA ASN B 161 -97.800 -30.882 154.110 1.00 44.51 C ANISOU 3812 CA ASN B 161 5579 5488 5847 1655 -524 749 C ATOM 3813 C ASN B 161 -97.480 -29.786 155.112 1.00 41.78 C ANISOU 3813 C ASN B 161 5148 5430 5296 1926 -757 408 C ATOM 3814 O ASN B 161 -97.456 -30.034 156.321 1.00 57.70 O ANISOU 3814 O ASN B 161 7435 7619 6870 2470 -738 425 O ATOM 3815 CB ASN B 161 -99.261 -31.324 154.249 1.00 45.04 C ANISOU 3815 CB ASN B 161 5839 5245 6029 1552 -101 1125 C ATOM 3816 CG ASN B 161 -99.758 -32.077 153.031 1.00 43.03 C ANISOU 3816 CG ASN B 161 5499 4692 6159 1154 67 1298 C ATOM 3817 OD1 ASN B 161 -99.213 -31.936 151.938 1.00 37.18 O ANISOU 3817 OD1 ASN B 161 4551 3974 5603 879 -152 1161 O ATOM 3818 ND2 ASN B 161 -100.802 -32.877 153.213 1.00 49.89 N ANISOU 3818 ND2 ASN B 161 6516 5262 7178 1136 489 1558 N ATOM 3819 N SER B 162 -97.248 -28.576 154.605 1.00 44.33 N ANISOU 3819 N SER B 162 5124 5783 5937 1585 -941 92 N ATOM 3820 CA SER B 162 -96.885 -27.437 155.440 1.00 47.05 C ANISOU 3820 CA SER B 162 5287 6370 6219 1770 -1167 -342 C ATOM 3821 C SER B 162 -97.818 -26.275 155.138 1.00 46.51 C ANISOU 3821 C SER B 162 5082 6112 6476 1381 -1051 -319 C ATOM 3822 O SER B 162 -97.919 -25.843 153.986 1.00 42.15 O ANISOU 3822 O SER B 162 4375 5336 6305 931 -987 -278 O ATOM 3823 CB SER B 162 -95.428 -27.027 155.206 1.00 43.67 C ANISOU 3823 CB SER B 162 4498 6138 5957 1776 -1475 -896 C ATOM 3824 OG SER B 162 -95.013 -26.061 156.154 1.00 47.38 O ANISOU 3824 OG SER B 162 4749 6873 6382 2037 -1720 -1428 O ATOM 3825 N TRP B 163 -98.482 -25.768 156.171 1.00 47.28 N ANISOU 3825 N TRP B 163 5277 6300 6388 1610 -1016 -344 N ATOM 3826 CA TRP B 163 -99.336 -24.593 156.074 1.00 47.10 C ANISOU 3826 CA TRP B 163 5121 6131 6645 1322 -936 -377 C ATOM 3827 C TRP B 163 -98.605 -23.368 156.603 1.00 46.14 C ANISOU 3827 C TRP B 163 4701 6202 6628 1397 -1177 -946 C ATOM 3828 O TRP B 163 -97.761 -23.465 157.497 1.00 48.09 O ANISOU 3828 O TRP B 163 4901 6775 6598 1830 -1422 -1323 O ATOM 3829 CB TRP B 163 -100.634 -24.777 156.866 1.00 57.23 C ANISOU 3829 CB TRP B 163 6666 7348 7732 1490 -685 -71 C ATOM 3830 CG TRP B 163 -101.757 -25.419 156.116 1.00 67.27 C ANISOU 3830 CG TRP B 163 8040 8298 9223 1198 -386 356 C ATOM 3831 CD1 TRP B 163 -102.732 -24.783 155.401 1.00 60.02 C ANISOU 3831 CD1 TRP B 163 6979 7153 8672 834 -308 428 C ATOM 3832 CD2 TRP B 163 -102.039 -26.819 156.021 1.00 71.52 C ANISOU 3832 CD2 TRP B 163 8811 8698 9666 1284 -131 694 C ATOM 3833 NE1 TRP B 163 -103.598 -25.702 154.861 1.00 56.39 N ANISOU 3833 NE1 TRP B 163 6590 6462 8373 692 -75 716 N ATOM 3834 CE2 TRP B 163 -103.195 -26.959 155.226 1.00 65.29 C ANISOU 3834 CE2 TRP B 163 7935 7609 9263 925 74 884 C ATOM 3835 CE3 TRP B 163 -101.425 -27.969 156.526 1.00 72.34 C ANISOU 3835 CE3 TRP B 163 9187 8885 9414 1663 -49 827 C ATOM 3836 CZ2 TRP B 163 -103.747 -28.202 154.925 1.00 66.87 C ANISOU 3836 CZ2 TRP B 163 8246 7573 9590 873 381 1142 C ATOM 3837 CZ3 TRP B 163 -101.975 -29.201 156.226 1.00 71.27 C ANISOU 3837 CZ3 TRP B 163 9234 8476 9372 1612 310 1173 C ATOM 3838 CH2 TRP B 163 -103.124 -29.308 155.433 1.00 69.83 C ANISOU 3838 CH2 TRP B 163 8894 7976 9661 1190 534 1300 C ATOM 3839 N THR B 164 -98.941 -22.211 156.050 1.00 41.86 N ANISOU 3839 N THR B 164 3955 5448 6503 1016 -1105 -1045 N ATOM 3840 CA THR B 164 -98.475 -20.958 156.618 1.00 51.65 C ANISOU 3840 CA THR B 164 4896 6788 7940 1046 -1241 -1593 C ATOM 3841 C THR B 164 -99.532 -20.415 157.571 1.00 49.53 C ANISOU 3841 C THR B 164 4744 6574 7500 1221 -1192 -1540 C ATOM 3842 O THR B 164 -100.716 -20.749 157.479 1.00 45.81 O ANISOU 3842 O THR B 164 4518 5951 6938 1158 -982 -1073 O ATOM 3843 CB THR B 164 -98.179 -19.928 155.526 1.00 43.46 C ANISOU 3843 CB THR B 164 3609 5419 7486 565 -1093 -1738 C ATOM 3844 OG1 THR B 164 -99.287 -19.854 154.620 1.00 40.47 O ANISOU 3844 OG1 THR B 164 3443 4726 7208 287 -864 -1223 O ATOM 3845 CG2 THR B 164 -96.923 -20.305 154.759 1.00 43.85 C ANISOU 3845 CG2 THR B 164 3483 5433 7746 430 -1110 -1938 C ATOM 3846 N ASP B 165 -99.094 -19.569 158.496 1.00 58.08 N ANISOU 3846 N ASP B 165 5608 7876 8582 1447 -1383 -2088 N ATOM 3847 CA ASP B 165 -100.057 -18.817 159.280 1.00 66.74 C ANISOU 3847 CA ASP B 165 6765 8986 9609 1547 -1317 -2098 C ATOM 3848 C ASP B 165 -100.789 -17.822 158.385 1.00 64.26 C ANISOU 3848 C ASP B 165 6342 8266 9808 1040 -1090 -1939 C ATOM 3849 O ASP B 165 -100.366 -17.528 157.262 1.00 72.76 O ANISOU 3849 O ASP B 165 7285 9074 11286 671 -994 -1926 O ATOM 3850 CB ASP B 165 -99.370 -18.092 160.436 1.00 81.94 C ANISOU 3850 CB ASP B 165 8444 11254 11437 1929 -1612 -2812 C ATOM 3851 CG ASP B 165 -99.886 -18.539 161.790 1.00 96.48 C ANISOU 3851 CG ASP B 165 10628 13427 12605 2549 -1677 -2738 C ATOM 3852 OD1 ASP B 165 -101.071 -18.924 161.877 1.00 98.54 O ANISOU 3852 OD1 ASP B 165 11236 13528 12676 2529 -1371 -2167 O ATOM 3853 OD2 ASP B 165 -99.105 -18.510 162.765 1.00104.05 O ANISOU 3853 OD2 ASP B 165 11510 14798 13226 3096 -2015 -3283 O ATOM 3854 N GLN B 166 -101.914 -17.320 158.887 1.00 52.47 N ANISOU 3854 N GLN B 166 4949 6719 8267 1077 -976 -1800 N ATOM 3855 CA GLN B 166 -102.712 -16.382 158.111 1.00 49.06 C ANISOU 3855 CA GLN B 166 4459 5923 8259 701 -790 -1642 C ATOM 3856 C GLN B 166 -101.876 -15.160 157.752 1.00 52.07 C ANISOU 3856 C GLN B 166 4520 6130 9134 472 -785 -2106 C ATOM 3857 O GLN B 166 -101.140 -14.624 158.585 1.00 50.12 O ANISOU 3857 O GLN B 166 4012 6080 8950 636 -941 -2688 O ATOM 3858 CB GLN B 166 -103.959 -15.976 158.895 1.00 45.79 C ANISOU 3858 CB GLN B 166 4144 5522 7730 830 -696 -1537 C ATOM 3859 CG GLN B 166 -105.068 -15.396 158.041 1.00 43.84 C ANISOU 3859 CG GLN B 166 3923 4924 7811 537 -521 -1242 C ATOM 3860 CD GLN B 166 -106.306 -15.072 158.849 1.00 44.66 C ANISOU 3860 CD GLN B 166 4084 5049 7836 668 -418 -1177 C ATOM 3861 OE1 GLN B 166 -106.232 -14.863 160.059 1.00 47.07 O ANISOU 3861 OE1 GLN B 166 4384 5594 7907 947 -460 -1434 O ATOM 3862 NE2 GLN B 166 -107.454 -15.029 158.183 1.00 43.17 N ANISOU 3862 NE2 GLN B 166 3942 4622 7838 510 -294 -877 N ATOM 3863 N ASP B 167 -101.991 -14.725 156.501 1.00 46.33 N ANISOU 3863 N ASP B 167 3822 5011 8771 130 -576 -1879 N ATOM 3864 CA ASP B 167 -101.080 -13.717 155.978 1.00 47.45 C ANISOU 3864 CA ASP B 167 3720 4870 9439 -116 -412 -2248 C ATOM 3865 C ASP B 167 -101.352 -12.353 156.598 1.00 59.18 C ANISOU 3865 C ASP B 167 5010 6228 11249 -140 -330 -2623 C ATOM 3866 O ASP B 167 -102.503 -11.961 156.806 1.00 63.77 O ANISOU 3866 O ASP B 167 5740 6748 11744 -91 -294 -2383 O ATOM 3867 CB ASP B 167 -101.194 -13.631 154.457 1.00 52.07 C ANISOU 3867 CB ASP B 167 4518 5034 10233 -380 -132 -1823 C ATOM 3868 CG ASP B 167 -100.064 -12.830 153.831 1.00 71.37 C ANISOU 3868 CG ASP B 167 6770 7124 13223 -629 174 -2153 C ATOM 3869 OD1 ASP B 167 -99.158 -12.387 154.569 1.00 80.49 O ANISOU 3869 OD1 ASP B 167 7532 8373 14676 -639 133 -2793 O ATOM 3870 OD2 ASP B 167 -100.081 -12.644 152.596 1.00 79.44 O ANISOU 3870 OD2 ASP B 167 8032 7760 14392 -786 483 -1808 O ATOM 3871 N SER B 168 -100.270 -11.632 156.898 1.00 69.46 N ANISOU 3871 N SER B 168 5928 7478 12985 -220 -292 -3277 N ATOM 3872 CA SER B 168 -100.399 -10.301 157.474 1.00 74.37 C ANISOU 3872 CA SER B 168 6299 7941 14018 -268 -185 -3737 C ATOM 3873 C SER B 168 -101.042 -9.328 156.496 1.00 74.96 C ANISOU 3873 C SER B 168 6572 7428 14479 -539 249 -3372 C ATOM 3874 O SER B 168 -101.708 -8.375 156.918 1.00 75.43 O ANISOU 3874 O SER B 168 6599 7351 14712 -525 332 -3475 O ATOM 3875 CB SER B 168 -99.027 -9.785 157.910 1.00 83.08 C ANISOU 3875 CB SER B 168 6913 9108 15545 -266 -182 -4542 C ATOM 3876 OG SER B 168 -98.209 -10.846 158.373 1.00 86.56 O ANISOU 3876 OG SER B 168 7233 10002 15654 -15 -556 -4824 O ATOM 3877 N LYS B 169 -100.868 -9.556 155.194 1.00 74.89 N ANISOU 3877 N LYS B 169 6813 7078 14565 -724 530 -2938 N ATOM 3878 CA LYS B 169 -101.327 -8.613 154.179 1.00 79.73 C ANISOU 3878 CA LYS B 169 7714 7221 15358 -814 975 -2521 C ATOM 3879 C LYS B 169 -102.769 -8.882 153.755 1.00 81.66 C ANISOU 3879 C LYS B 169 8364 7374 15291 -695 858 -1941 C ATOM 3880 O LYS B 169 -103.643 -8.026 153.930 1.00 93.86 O ANISOU 3880 O LYS B 169 9988 8746 16929 -628 932 -1876 O ATOM 3881 CB LYS B 169 -100.393 -8.661 152.966 1.00 81.29 C ANISOU 3881 CB LYS B 169 8046 7205 15636 -927 1358 -2313 C ATOM 3882 CG LYS B 169 -98.940 -8.360 153.288 1.00 89.52 C ANISOU 3882 CG LYS B 169 8644 8334 17034 -1002 1530 -2892 C ATOM 3883 N ASP B 170 -103.038 -10.068 153.207 1.00 69.92 N ANISOU 3883 N ASP B 170 7105 6101 13361 -607 658 -1519 N ATOM 3884 CA ASP B 170 -104.340 -10.363 152.622 1.00 58.23 C ANISOU 3884 CA ASP B 170 5957 4613 11554 -440 544 -1000 C ATOM 3885 C ASP B 170 -105.151 -11.367 153.433 1.00 44.97 C ANISOU 3885 C ASP B 170 4214 3396 9478 -292 173 -927 C ATOM 3886 O ASP B 170 -106.218 -11.792 152.976 1.00 54.03 O ANISOU 3886 O ASP B 170 5539 4568 10424 -174 60 -592 O ATOM 3887 CB ASP B 170 -104.176 -10.852 151.179 1.00 52.63 C ANISOU 3887 CB ASP B 170 5583 3701 10713 -426 668 -589 C ATOM 3888 CG ASP B 170 -103.313 -12.101 151.067 1.00 53.66 C ANISOU 3888 CG ASP B 170 5631 4097 10661 -504 532 -609 C ATOM 3889 OD1 ASP B 170 -103.063 -12.768 152.093 1.00 52.63 O ANISOU 3889 OD1 ASP B 170 5247 4351 10399 -494 281 -852 O ATOM 3890 OD2 ASP B 170 -102.886 -12.424 149.939 1.00 57.13 O ANISOU 3890 OD2 ASP B 170 6301 4354 11053 -524 689 -369 O ATOM 3891 N SER B 171 -104.672 -11.758 154.616 1.00 45.13 N ANISOU 3891 N SER B 171 3991 3763 9394 -255 12 -1262 N ATOM 3892 CA SER B 171 -105.377 -12.676 155.515 1.00 43.74 C ANISOU 3892 CA SER B 171 3820 3962 8836 -69 -206 -1179 C ATOM 3893 C SER B 171 -105.697 -14.014 154.856 1.00 44.05 C ANISOU 3893 C SER B 171 4039 4089 8609 -48 -280 -785 C ATOM 3894 O SER B 171 -106.641 -14.698 155.259 1.00 40.98 O ANISOU 3894 O SER B 171 3704 3841 8027 64 -328 -612 O ATOM 3895 CB SER B 171 -106.659 -12.038 156.066 1.00 44.21 C ANISOU 3895 CB SER B 171 3882 3993 8921 27 -194 -1149 C ATOM 3896 OG SER B 171 -106.361 -10.942 156.913 1.00 46.74 O ANISOU 3896 OG SER B 171 4007 4302 9448 41 -156 -1574 O ATOM 3897 N THR B 172 -104.928 -14.404 153.844 1.00 44.35 N ANISOU 3897 N THR B 172 4156 4013 8683 -160 -241 -671 N ATOM 3898 CA THR B 172 -105.089 -15.695 153.194 1.00 38.40 C ANISOU 3898 CA THR B 172 3539 3343 7707 -145 -321 -367 C ATOM 3899 C THR B 172 -104.166 -16.729 153.827 1.00 44.47 C ANISOU 3899 C THR B 172 4244 4398 8256 -82 -412 -483 C ATOM 3900 O THR B 172 -103.303 -16.417 154.651 1.00 49.82 O ANISOU 3900 O THR B 172 4761 5229 8940 -20 -460 -838 O ATOM 3901 CB THR B 172 -104.799 -15.591 151.698 1.00 48.22 C ANISOU 3901 CB THR B 172 4958 4319 9046 -237 -230 -163 C ATOM 3902 OG1 THR B 172 -103.471 -15.083 151.507 1.00 61.04 O ANISOU 3902 OG1 THR B 172 6514 5808 10871 -371 -62 -378 O ATOM 3903 CG2 THR B 172 -105.792 -14.662 151.021 1.00 48.81 C ANISOU 3903 CG2 THR B 172 5185 4128 9232 -160 -172 -9 C ATOM 3904 N TYR B 173 -104.357 -17.979 153.425 1.00 44.24 N ANISOU 3904 N TYR B 173 4329 4442 8039 -57 -452 -223 N ATOM 3905 CA TYR B 173 -103.467 -19.066 153.796 1.00 43.39 C ANISOU 3905 CA TYR B 173 4228 4555 7705 36 -519 -261 C ATOM 3906 C TYR B 173 -102.771 -19.599 152.552 1.00 45.22 C ANISOU 3906 C TYR B 173 4515 4674 7992 -110 -515 -137 C ATOM 3907 O TYR B 173 -103.233 -19.411 151.424 1.00 49.11 O ANISOU 3907 O TYR B 173 5108 4951 8600 -220 -466 57 O ATOM 3908 CB TYR B 173 -104.226 -20.203 154.494 1.00 41.03 C ANISOU 3908 CB TYR B 173 4047 4391 7150 214 -474 -54 C ATOM 3909 CG TYR B 173 -104.774 -19.845 155.856 1.00 47.32 C ANISOU 3909 CG TYR B 173 4853 5326 7802 431 -419 -164 C ATOM 3910 CD1 TYR B 173 -104.020 -20.044 157.004 1.00 52.00 C ANISOU 3910 CD1 TYR B 173 5485 6196 8074 741 -492 -373 C ATOM 3911 CD2 TYR B 173 -106.049 -19.309 155.992 1.00 45.06 C ANISOU 3911 CD2 TYR B 173 4544 4907 7670 384 -308 -90 C ATOM 3912 CE1 TYR B 173 -104.519 -19.719 158.251 1.00 51.60 C ANISOU 3912 CE1 TYR B 173 5502 6288 7814 1013 -431 -472 C ATOM 3913 CE2 TYR B 173 -106.556 -18.981 157.236 1.00 44.63 C ANISOU 3913 CE2 TYR B 173 4516 4968 7474 591 -214 -187 C ATOM 3914 CZ TYR B 173 -105.787 -19.188 158.361 1.00 45.77 C ANISOU 3914 CZ TYR B 173 4751 5388 7253 912 -263 -361 C ATOM 3915 OH TYR B 173 -106.285 -18.865 159.602 1.00 51.84 O ANISOU 3915 OH TYR B 173 5603 6289 7805 1190 -162 -457 O ATOM 3916 N SER B 174 -101.643 -20.268 152.774 1.00 42.66 N ANISOU 3916 N SER B 174 4142 4518 7550 -50 -582 -274 N ATOM 3917 CA SER B 174 -100.955 -20.985 151.715 1.00 37.93 C ANISOU 3917 CA SER B 174 3598 3849 6966 -162 -568 -158 C ATOM 3918 C SER B 174 -100.401 -22.278 152.288 1.00 35.35 C ANISOU 3918 C SER B 174 3298 3767 6365 27 -669 -154 C ATOM 3919 O SER B 174 -100.182 -22.403 153.495 1.00 36.50 O ANISOU 3919 O SER B 174 3417 4147 6305 286 -757 -329 O ATOM 3920 CB SER B 174 -99.827 -20.148 151.096 1.00 35.99 C ANISOU 3920 CB SER B 174 3226 3440 7007 -335 -461 -408 C ATOM 3921 OG SER B 174 -100.356 -19.085 150.323 1.00 42.83 O ANISOU 3921 OG SER B 174 4191 3992 8088 -467 -278 -293 O ATOM 3922 N MET B 175 -100.176 -23.245 151.405 1.00 35.52 N ANISOU 3922 N MET B 175 3412 3732 6350 -46 -654 45 N ATOM 3923 CA MET B 175 -99.603 -24.511 151.827 1.00 40.51 C ANISOU 3923 CA MET B 175 4104 4546 6741 146 -715 77 C ATOM 3924 C MET B 175 -98.741 -25.081 150.711 1.00 46.07 C ANISOU 3924 C MET B 175 4797 5183 7526 2 -719 100 C ATOM 3925 O MET B 175 -98.922 -24.762 149.532 1.00 39.73 O ANISOU 3925 O MET B 175 4029 4173 6894 -215 -640 210 O ATOM 3926 CB MET B 175 -100.692 -25.510 152.234 1.00 38.25 C ANISOU 3926 CB MET B 175 4001 4236 6295 272 -599 387 C ATOM 3927 CG MET B 175 -101.253 -26.334 151.094 1.00 39.54 C ANISOU 3927 CG MET B 175 4220 4209 6595 90 -522 627 C ATOM 3928 SD MET B 175 -102.074 -27.814 151.707 1.00 46.70 S ANISOU 3928 SD MET B 175 5282 5043 7418 246 -280 879 S ATOM 3929 CE MET B 175 -100.717 -28.594 152.570 1.00 52.74 C ANISOU 3929 CE MET B 175 6202 6032 7805 598 -323 844 C ATOM 3930 N SER B 176 -97.774 -25.896 151.111 1.00 49.92 N ANISOU 3930 N SER B 176 5262 5854 7852 185 -814 -21 N ATOM 3931 CA SER B 176 -96.981 -26.691 150.189 1.00 48.38 C ANISOU 3931 CA SER B 176 5067 5619 7695 94 -813 15 C ATOM 3932 C SER B 176 -97.183 -28.167 150.501 1.00 44.23 C ANISOU 3932 C SER B 176 4727 5160 6916 307 -806 256 C ATOM 3933 O SER B 176 -97.244 -28.566 151.671 1.00 47.89 O ANISOU 3933 O SER B 176 5298 5784 7115 643 -832 261 O ATOM 3934 CB SER B 176 -95.494 -26.326 150.265 1.00 54.01 C ANISOU 3934 CB SER B 176 5531 6450 8540 112 -905 -422 C ATOM 3935 OG SER B 176 -94.991 -26.489 151.578 1.00 73.25 O ANISOU 3935 OG SER B 176 7886 9191 10755 490 -1114 -710 O ATOM 3936 N SER B 177 -97.297 -28.967 149.445 1.00 32.76 N ANISOU 3936 N SER B 177 3346 3563 5540 147 -735 455 N ATOM 3937 CA SER B 177 -97.424 -30.414 149.539 1.00 35.35 C ANISOU 3937 CA SER B 177 3828 3869 5734 291 -661 666 C ATOM 3938 C SER B 177 -96.283 -31.037 148.752 1.00 41.39 C ANISOU 3938 C SER B 177 4539 4663 6523 246 -731 576 C ATOM 3939 O SER B 177 -96.125 -30.762 147.559 1.00 44.82 O ANISOU 3939 O SER B 177 4912 4986 7132 -11 -719 556 O ATOM 3940 CB SER B 177 -98.775 -30.886 148.998 1.00 30.69 C ANISOU 3940 CB SER B 177 3306 3052 5304 132 -499 907 C ATOM 3941 OG SER B 177 -99.027 -32.231 149.360 1.00 31.77 O ANISOU 3941 OG SER B 177 3584 3098 5390 278 -315 1089 O ATOM 3942 N THR B 178 -95.500 -31.885 149.406 1.00 39.05 N ANISOU 3942 N THR B 178 4305 4514 6020 547 -788 530 N ATOM 3943 CA THR B 178 -94.315 -32.470 148.795 1.00 38.53 C ANISOU 3943 CA THR B 178 4153 4506 5983 547 -874 388 C ATOM 3944 C THR B 178 -94.458 -33.983 148.776 1.00 42.98 C ANISOU 3944 C THR B 178 4926 4980 6425 709 -761 648 C ATOM 3945 O THR B 178 -94.650 -34.607 149.825 1.00 43.01 O ANISOU 3945 O THR B 178 5144 5022 6176 1078 -687 788 O ATOM 3946 CB THR B 178 -93.048 -32.063 149.548 1.00 38.14 C ANISOU 3946 CB THR B 178 3916 4731 5845 812 -1100 -31 C ATOM 3947 OG1 THR B 178 -93.007 -30.636 149.676 1.00 38.54 O ANISOU 3947 OG1 THR B 178 3747 4809 6089 649 -1140 -311 O ATOM 3948 CG2 THR B 178 -91.812 -32.534 148.798 1.00 36.14 C ANISOU 3948 CG2 THR B 178 3495 4512 5722 753 -1166 -249 C ATOM 3949 N LEU B 179 -94.355 -34.565 147.586 1.00 43.17 N ANISOU 3949 N LEU B 179 4920 4862 6622 468 -706 711 N ATOM 3950 CA LEU B 179 -94.338 -36.009 147.403 1.00 43.92 C ANISOU 3950 CA LEU B 179 5160 4838 6690 576 -585 890 C ATOM 3951 C LEU B 179 -92.885 -36.415 147.202 1.00 41.75 C ANISOU 3951 C LEU B 179 4798 4721 6344 713 -741 681 C ATOM 3952 O LEU B 179 -92.273 -36.069 146.185 1.00 45.67 O ANISOU 3952 O LEU B 179 5119 5222 7010 458 -801 507 O ATOM 3953 CB LEU B 179 -95.199 -36.427 146.214 1.00 37.61 C ANISOU 3953 CB LEU B 179 4339 3802 6150 254 -463 1006 C ATOM 3954 CG LEU B 179 -95.194 -37.923 145.894 1.00 39.05 C ANISOU 3954 CG LEU B 179 4612 3812 6412 306 -307 1124 C ATOM 3955 CD1 LEU B 179 -95.867 -38.720 147.001 1.00 49.09 C ANISOU 3955 CD1 LEU B 179 6099 4908 7646 554 -8 1360 C ATOM 3956 CD2 LEU B 179 -95.851 -38.194 144.550 1.00 35.23 C ANISOU 3956 CD2 LEU B 179 4018 3170 6199 4 -296 1074 C ATOM 3957 N THR B 180 -92.333 -37.137 148.171 1.00 38.60 N ANISOU 3957 N THR B 180 4543 4440 5682 1161 -783 689 N ATOM 3958 CA THR B 180 -90.930 -37.523 148.155 1.00 42.33 C ANISOU 3958 CA THR B 180 4901 5108 6075 1390 -988 417 C ATOM 3959 C THR B 180 -90.837 -39.006 147.830 1.00 43.14 C ANISOU 3959 C THR B 180 5202 5041 6147 1513 -836 648 C ATOM 3960 O THR B 180 -91.377 -39.845 148.560 1.00 40.41 O ANISOU 3960 O THR B 180 5182 4558 5614 1828 -628 951 O ATOM 3961 CB THR B 180 -90.256 -37.220 149.493 1.00 47.30 C ANISOU 3961 CB THR B 180 5539 6054 6381 1935 -1238 162 C ATOM 3962 OG1 THR B 180 -90.112 -35.802 149.644 1.00 54.67 O ANISOU 3962 OG1 THR B 180 6176 7138 7456 1764 -1396 -186 O ATOM 3963 CG2 THR B 180 -88.883 -37.869 149.554 1.00 49.21 C ANISOU 3963 CG2 THR B 180 5673 6500 6524 2286 -1474 -142 C ATOM 3964 N LEU B 181 -90.158 -39.317 146.732 1.00 44.44 N ANISOU 3964 N LEU B 181 5191 5177 6517 1271 -878 508 N ATOM 3965 CA LEU B 181 -89.980 -40.668 146.241 1.00 40.98 C ANISOU 3965 CA LEU B 181 4880 4572 6118 1327 -748 660 C ATOM 3966 C LEU B 181 -88.495 -40.914 146.029 1.00 45.13 C ANISOU 3966 C LEU B 181 5219 5302 6625 1495 -969 330 C ATOM 3967 O LEU B 181 -87.693 -39.978 145.953 1.00 53.74 O ANISOU 3967 O LEU B 181 6011 6604 7805 1420 -1166 -51 O ATOM 3968 CB LEU B 181 -90.747 -40.896 144.931 1.00 38.28 C ANISOU 3968 CB LEU B 181 4489 3978 6078 850 -575 776 C ATOM 3969 CG LEU B 181 -92.273 -40.902 145.023 1.00 40.83 C ANISOU 3969 CG LEU B 181 4927 4063 6524 691 -352 1020 C ATOM 3970 CD1 LEU B 181 -92.889 -40.570 143.673 1.00 32.90 C ANISOU 3970 CD1 LEU B 181 3770 2961 5767 271 -365 942 C ATOM 3971 CD2 LEU B 181 -92.768 -42.249 145.526 1.00 43.98 C ANISOU 3971 CD2 LEU B 181 5566 4183 6960 904 -38 1277 C ATOM 3972 N THR B 182 -88.129 -42.185 145.944 1.00 54.39 N ANISOU 3972 N THR B 182 6544 6380 7744 1723 -900 441 N ATOM 3973 CA THR B 182 -86.800 -42.490 145.452 1.00 42.02 C ANISOU 3973 CA THR B 182 4752 4963 6251 1789 -1081 112 C ATOM 3974 C THR B 182 -86.784 -42.362 143.932 1.00 47.86 C ANISOU 3974 C THR B 182 5303 5562 7320 1232 -962 50 C ATOM 3975 O THR B 182 -87.820 -42.453 143.266 1.00 51.01 O ANISOU 3975 O THR B 182 5810 5738 7835 916 -771 292 O ATOM 3976 CB THR B 182 -86.373 -43.896 145.876 1.00 44.88 C ANISOU 3976 CB THR B 182 5367 5266 6419 2277 -1050 253 C ATOM 3977 OG1 THR B 182 -87.173 -44.868 145.191 1.00 63.21 O ANISOU 3977 OG1 THR B 182 7882 7219 8918 2035 -715 596 O ATOM 3978 CG2 THR B 182 -86.548 -44.071 147.377 1.00 48.25 C ANISOU 3978 CG2 THR B 182 6134 5788 6411 2935 -1090 413 C ATOM 3979 N LYS B 183 -85.590 -42.124 143.385 1.00 40.11 N ANISOU 3979 N LYS B 183 4031 4719 6492 1155 -1072 -326 N ATOM 3980 CA LYS B 183 -85.458 -42.037 141.934 1.00 38.57 C ANISOU 3980 CA LYS B 183 3730 4386 6538 713 -907 -373 C ATOM 3981 C LYS B 183 -85.937 -43.318 141.266 1.00 37.82 C ANISOU 3981 C LYS B 183 3839 4081 6450 674 -772 -114 C ATOM 3982 O LYS B 183 -86.536 -43.277 140.184 1.00 36.18 O ANISOU 3982 O LYS B 183 3679 3726 6344 353 -637 -20 O ATOM 3983 CB LYS B 183 -84.010 -41.735 141.549 1.00 44.31 C ANISOU 3983 CB LYS B 183 4116 5247 7474 678 -955 -835 C ATOM 3984 CG LYS B 183 -83.803 -41.541 140.053 1.00 48.04 C ANISOU 3984 CG LYS B 183 4542 5557 8154 266 -697 -869 C ATOM 3985 CD LYS B 183 -82.363 -41.181 139.723 1.00 58.79 C ANISOU 3985 CD LYS B 183 5537 6990 9812 200 -631 -1355 C ATOM 3986 CE LYS B 183 -81.440 -42.373 139.898 1.00 71.77 C ANISOU 3986 CE LYS B 183 7066 8744 11461 503 -798 -1548 C ATOM 3987 NZ LYS B 183 -81.860 -43.515 139.039 1.00 81.60 N ANISOU 3987 NZ LYS B 183 8580 9825 12600 443 -687 -1230 N ATOM 3988 N ASP B 184 -85.670 -44.467 141.891 1.00 40.85 N ANISOU 3988 N ASP B 184 4354 4442 6724 1047 -805 -28 N ATOM 3989 CA ASP B 184 -86.048 -45.744 141.295 1.00 39.77 C ANISOU 3989 CA ASP B 184 4376 4056 6679 1010 -630 165 C ATOM 3990 C ASP B 184 -87.556 -45.830 141.093 1.00 38.36 C ANISOU 3990 C ASP B 184 4348 3628 6598 779 -434 434 C ATOM 3991 O ASP B 184 -88.029 -46.138 139.994 1.00 40.15 O ANISOU 3991 O ASP B 184 4534 3714 7009 492 -349 407 O ATOM 3992 CB ASP B 184 -85.555 -46.894 142.173 1.00 42.78 C ANISOU 3992 CB ASP B 184 4942 4401 6912 1523 -632 259 C ATOM 3993 CG ASP B 184 -85.604 -48.236 141.464 1.00 44.56 C ANISOU 3993 CG ASP B 184 5261 4358 7313 1480 -436 358 C ATOM 3994 OD1 ASP B 184 -86.081 -48.293 140.310 1.00 45.37 O ANISOU 3994 OD1 ASP B 184 5265 4332 7643 1063 -338 317 O ATOM 3995 OD2 ASP B 184 -85.166 -49.239 142.064 1.00 49.05 O ANISOU 3995 OD2 ASP B 184 6020 4842 7775 1915 -385 458 O ATOM 3996 N GLU B 185 -88.331 -45.555 142.146 1.00 38.73 N ANISOU 3996 N GLU B 185 4551 3630 6535 934 -368 640 N ATOM 3997 CA GLU B 185 -89.783 -45.556 142.001 1.00 41.49 C ANISOU 3997 CA GLU B 185 4967 3738 7058 701 -169 817 C ATOM 3998 C GLU B 185 -90.246 -44.442 141.071 1.00 41.78 C ANISOU 3998 C GLU B 185 4832 3875 7166 326 -295 675 C ATOM 3999 O GLU B 185 -91.195 -44.626 140.299 1.00 36.76 O ANISOU 3999 O GLU B 185 4155 3085 6729 100 -228 653 O ATOM 4000 CB GLU B 185 -90.450 -45.421 143.369 1.00 39.22 C ANISOU 4000 CB GLU B 185 4895 3376 6631 963 -20 1064 C ATOM 4001 CG GLU B 185 -90.672 -46.740 144.083 1.00 47.78 C ANISOU 4001 CG GLU B 185 6275 4142 7736 1291 331 1328 C ATOM 4002 CD GLU B 185 -91.107 -46.550 145.521 1.00 59.86 C ANISOU 4002 CD GLU B 185 8111 5628 9004 1676 512 1596 C ATOM 4003 OE1 GLU B 185 -91.354 -45.390 145.917 1.00 60.52 O ANISOU 4003 OE1 GLU B 185 8119 5936 8940 1626 332 1539 O ATOM 4004 OE2 GLU B 185 -91.202 -47.558 146.255 1.00 60.53 O ANISOU 4004 OE2 GLU B 185 8549 5433 9018 2059 873 1872 O ATOM 4005 N TYR B 186 -89.588 -43.282 141.133 1.00 38.44 N ANISOU 4005 N TYR B 186 4308 3696 6601 298 -464 541 N ATOM 4006 CA TYR B 186 -90.005 -42.139 140.327 1.00 36.11 C ANISOU 4006 CA TYR B 186 3940 3448 6331 15 -510 466 C ATOM 4007 C TYR B 186 -89.921 -42.452 138.837 1.00 37.32 C ANISOU 4007 C TYR B 186 4077 3547 6557 -166 -490 357 C ATOM 4008 O TYR B 186 -90.846 -42.153 138.074 1.00 37.27 O ANISOU 4008 O TYR B 186 4109 3482 6568 -294 -506 358 O ATOM 4009 CB TYR B 186 -89.152 -40.919 140.680 1.00 36.01 C ANISOU 4009 CB TYR B 186 3811 3630 6242 19 -592 306 C ATOM 4010 CG TYR B 186 -89.431 -39.690 139.842 1.00 40.25 C ANISOU 4010 CG TYR B 186 4339 4152 6802 -230 -541 264 C ATOM 4011 CD1 TYR B 186 -90.653 -39.033 139.916 1.00 40.20 C ANISOU 4011 CD1 TYR B 186 4420 4088 6766 -304 -547 406 C ATOM 4012 CD2 TYR B 186 -88.460 -39.172 138.995 1.00 45.05 C ANISOU 4012 CD2 TYR B 186 4875 4772 7470 -356 -433 85 C ATOM 4013 CE1 TYR B 186 -90.906 -37.904 139.155 1.00 37.56 C ANISOU 4013 CE1 TYR B 186 4147 3722 6403 -444 -487 397 C ATOM 4014 CE2 TYR B 186 -88.700 -38.041 138.235 1.00 46.46 C ANISOU 4014 CE2 TYR B 186 5144 4871 7637 -516 -286 105 C ATOM 4015 CZ TYR B 186 -89.925 -37.413 138.317 1.00 41.19 C ANISOU 4015 CZ TYR B 186 4608 4160 6881 -533 -333 275 C ATOM 4016 OH TYR B 186 -90.169 -36.293 137.556 1.00 39.10 O ANISOU 4016 OH TYR B 186 4500 3800 6556 -609 -175 324 O ATOM 4017 N GLU B 187 -88.818 -43.064 138.408 1.00 38.30 N ANISOU 4017 N GLU B 187 4149 3707 6696 -122 -478 230 N ATOM 4018 CA GLU B 187 -88.601 -43.363 136.997 1.00 38.25 C ANISOU 4018 CA GLU B 187 4158 3668 6708 -246 -439 113 C ATOM 4019 C GLU B 187 -89.410 -44.553 136.499 1.00 40.06 C ANISOU 4019 C GLU B 187 4415 3741 7066 -248 -437 110 C ATOM 4020 O GLU B 187 -89.307 -44.895 135.316 1.00 50.00 O ANISOU 4020 O GLU B 187 5689 4995 8312 -297 -446 -32 O ATOM 4021 CB GLU B 187 -87.113 -43.608 136.736 1.00 44.18 C ANISOU 4021 CB GLU B 187 4807 4497 7483 -209 -391 -63 C ATOM 4022 CG GLU B 187 -86.234 -42.397 136.997 1.00 48.35 C ANISOU 4022 CG GLU B 187 5211 5137 8023 -262 -336 -204 C ATOM 4023 CD GLU B 187 -84.756 -42.721 136.918 1.00 57.63 C ANISOU 4023 CD GLU B 187 6185 6382 9330 -209 -291 -476 C ATOM 4024 OE1 GLU B 187 -84.396 -43.908 137.071 1.00 63.75 O ANISOU 4024 OE1 GLU B 187 6936 7163 10124 -43 -374 -502 O ATOM 4025 OE2 GLU B 187 -83.953 -41.789 136.703 1.00 62.79 O ANISOU 4025 OE2 GLU B 187 6688 7055 10116 -332 -137 -691 O ATOM 4026 N ARG B 188 -90.206 -45.189 137.354 1.00 40.51 N ANISOU 4026 N ARG B 188 4475 3645 7273 -183 -382 229 N ATOM 4027 CA ARG B 188 -91.050 -46.302 136.945 1.00 43.31 C ANISOU 4027 CA ARG B 188 4783 3776 7896 -226 -303 150 C ATOM 4028 C ARG B 188 -92.488 -45.883 136.681 1.00 46.65 C ANISOU 4028 C ARG B 188 5135 4137 8454 -340 -357 65 C ATOM 4029 O ARG B 188 -93.308 -46.727 136.308 1.00 48.34 O ANISOU 4029 O ARG B 188 5218 4158 8991 -396 -301 -120 O ATOM 4030 CB ARG B 188 -91.010 -47.410 138.001 1.00 37.69 C ANISOU 4030 CB ARG B 188 4132 2827 7361 -68 -73 314 C ATOM 4031 CG ARG B 188 -89.650 -48.075 138.099 1.00 39.73 C ANISOU 4031 CG ARG B 188 4442 3138 7516 116 -66 321 C ATOM 4032 CD ARG B 188 -89.604 -49.153 139.161 1.00 40.77 C ANISOU 4032 CD ARG B 188 4737 3017 7738 388 187 534 C ATOM 4033 NE ARG B 188 -88.231 -49.588 139.399 1.00 41.74 N ANISOU 4033 NE ARG B 188 4916 3264 7679 666 108 522 N ATOM 4034 CZ ARG B 188 -87.645 -50.593 138.756 1.00 42.95 C ANISOU 4034 CZ ARG B 188 5035 3317 7968 691 156 406 C ATOM 4035 NH1 ARG B 188 -86.391 -50.918 139.034 1.00 44.11 N ANISOU 4035 NH1 ARG B 188 5206 3602 7952 980 54 362 N ATOM 4036 NH2 ARG B 188 -88.312 -51.269 137.830 1.00 43.41 N ANISOU 4036 NH2 ARG B 188 4998 3152 8345 450 279 274 N ATOM 4037 N HIS B 189 -92.813 -44.606 136.867 1.00 42.74 N ANISOU 4037 N HIS B 189 4684 3789 7768 -364 -462 140 N ATOM 4038 CA HIS B 189 -94.147 -44.089 136.616 1.00 38.50 C ANISOU 4038 CA HIS B 189 4071 3230 7328 -421 -561 30 C ATOM 4039 C HIS B 189 -94.051 -42.838 135.755 1.00 41.35 C ANISOU 4039 C HIS B 189 4551 3808 7352 -389 -751 -7 C ATOM 4040 O HIS B 189 -92.980 -42.246 135.594 1.00 37.78 O ANISOU 4040 O HIS B 189 4229 3469 6656 -377 -710 94 O ATOM 4041 CB HIS B 189 -94.880 -43.798 137.928 1.00 37.19 C ANISOU 4041 CB HIS B 189 3889 2948 7294 -431 -417 212 C ATOM 4042 CG HIS B 189 -95.031 -44.997 138.810 1.00 36.61 C ANISOU 4042 CG HIS B 189 3805 2588 7519 -396 -106 315 C ATOM 4043 ND1 HIS B 189 -95.928 -46.008 138.541 1.00 39.11 N ANISOU 4043 ND1 HIS B 189 3943 2614 8304 -487 67 109 N ATOM 4044 CD2 HIS B 189 -94.403 -45.347 139.957 1.00 36.91 C ANISOU 4044 CD2 HIS B 189 4014 2555 7455 -228 100 588 C ATOM 4045 CE1 HIS B 189 -95.843 -46.931 139.482 1.00 44.60 C ANISOU 4045 CE1 HIS B 189 4740 3011 9195 -409 455 312 C ATOM 4046 NE2 HIS B 189 -94.925 -46.553 140.354 1.00 41.42 N ANISOU 4046 NE2 HIS B 189 4588 2758 8393 -206 458 626 N ATOM 4047 N ASN B 190 -95.190 -42.434 135.196 1.00 41.92 N ANISOU 4047 N ASN B 190 4577 3910 7442 -345 -925 -181 N ATOM 4048 CA ASN B 190 -95.221 -41.404 134.165 1.00 42.47 C ANISOU 4048 CA ASN B 190 4845 4149 7143 -200 -1089 -224 C ATOM 4049 C ASN B 190 -95.929 -40.129 134.599 1.00 45.21 C ANISOU 4049 C ASN B 190 5258 4536 7384 -166 -1144 -105 C ATOM 4050 O ASN B 190 -95.348 -39.043 134.513 1.00 41.30 O ANISOU 4050 O ASN B 190 4987 4095 6611 -133 -1055 87 O ATOM 4051 CB ASN B 190 -95.888 -41.962 132.900 1.00 47.60 C ANISOU 4051 CB ASN B 190 5444 4864 7776 -20 -1338 -600 C ATOM 4052 CG ASN B 190 -95.896 -40.967 131.758 1.00 68.43 C ANISOU 4052 CG ASN B 190 8408 7679 9912 271 -1489 -615 C ATOM 4053 OD1 ASN B 190 -95.068 -40.058 131.706 1.00 68.69 O ANISOU 4053 OD1 ASN B 190 8730 7723 9646 282 -1288 -323 O ATOM 4054 ND2 ASN B 190 -96.837 -41.133 130.836 1.00 84.40 N ANISOU 4054 ND2 ASN B 190 10392 9822 11854 552 -1817 -988 N ATOM 4055 N SER B 191 -97.169 -40.227 135.069 1.00 48.12 N ANISOU 4055 N SER B 191 5417 4843 8024 -184 -1241 -240 N ATOM 4056 CA SER B 191 -97.997 -39.057 135.335 1.00 44.29 C ANISOU 4056 CA SER B 191 4971 4406 7451 -114 -1341 -192 C ATOM 4057 C SER B 191 -98.028 -38.758 136.826 1.00 41.12 C ANISOU 4057 C SER B 191 4495 3906 7223 -288 -1133 49 C ATOM 4058 O SER B 191 -98.309 -39.646 137.638 1.00 52.64 O ANISOU 4058 O SER B 191 5773 5213 9016 -402 -975 40 O ATOM 4059 CB SER B 191 -99.422 -39.276 134.823 1.00 50.76 C ANISOU 4059 CB SER B 191 5564 5247 8477 25 -1618 -593 C ATOM 4060 OG SER B 191 -99.416 -39.770 133.496 1.00 68.41 O ANISOU 4060 OG SER B 191 7832 7600 10559 250 -1857 -907 O ATOM 4061 N TYR B 192 -97.748 -37.506 137.184 1.00 33.57 N ANISOU 4061 N TYR B 192 3705 3012 6039 -275 -1095 256 N ATOM 4062 CA TYR B 192 -97.764 -37.067 138.571 1.00 31.28 C ANISOU 4062 CA TYR B 192 3364 2680 5843 -376 -947 440 C ATOM 4063 C TYR B 192 -98.751 -35.918 138.707 1.00 35.90 C ANISOU 4063 C TYR B 192 3959 3285 6394 -320 -1047 437 C ATOM 4064 O TYR B 192 -98.649 -34.916 137.987 1.00 39.54 O ANISOU 4064 O TYR B 192 4615 3806 6602 -206 -1122 468 O ATOM 4065 CB TYR B 192 -96.360 -36.671 139.034 1.00 33.02 C ANISOU 4065 CB TYR B 192 3691 2954 5899 -420 -805 602 C ATOM 4066 CG TYR B 192 -95.435 -37.865 139.104 1.00 39.36 C ANISOU 4066 CG TYR B 192 4454 3743 6758 -434 -724 590 C ATOM 4067 CD1 TYR B 192 -94.801 -38.346 137.964 1.00 45.08 C ANISOU 4067 CD1 TYR B 192 5238 4487 7405 -422 -746 495 C ATOM 4068 CD2 TYR B 192 -95.224 -38.534 140.302 1.00 30.93 C ANISOU 4068 CD2 TYR B 192 3332 2635 5787 -400 -612 680 C ATOM 4069 CE1 TYR B 192 -93.970 -39.448 138.020 1.00 38.15 C ANISOU 4069 CE1 TYR B 192 4311 3588 6596 -424 -677 470 C ATOM 4070 CE2 TYR B 192 -94.393 -39.635 140.368 1.00 30.48 C ANISOU 4070 CE2 TYR B 192 3273 2551 5756 -345 -542 679 C ATOM 4071 CZ TYR B 192 -93.769 -40.088 139.224 1.00 35.65 C ANISOU 4071 CZ TYR B 192 3934 3225 6387 -382 -585 562 C ATOM 4072 OH TYR B 192 -92.940 -41.185 139.285 1.00 35.84 O ANISOU 4072 OH TYR B 192 3947 3218 6454 -318 -519 548 O ATOM 4073 N THR B 193 -99.697 -36.069 139.636 1.00 38.95 N ANISOU 4073 N THR B 193 4168 3589 7043 -376 -993 413 N ATOM 4074 CA THR B 193 -100.891 -35.239 139.702 1.00 36.40 C ANISOU 4074 CA THR B 193 3769 3270 6791 -316 -1116 317 C ATOM 4075 C THR B 193 -101.099 -34.745 141.124 1.00 37.01 C ANISOU 4075 C THR B 193 3816 3298 6949 -397 -930 491 C ATOM 4076 O THR B 193 -101.011 -35.525 142.078 1.00 37.32 O ANISOU 4076 O THR B 193 3798 3234 7147 -461 -700 579 O ATOM 4077 CB THR B 193 -102.125 -36.028 139.241 1.00 38.91 C ANISOU 4077 CB THR B 193 3800 3516 7468 -287 -1241 -41 C ATOM 4078 OG1 THR B 193 -102.074 -36.208 137.821 1.00 47.93 O ANISOU 4078 OG1 THR B 193 4994 4775 8440 -102 -1520 -273 O ATOM 4079 CG2 THR B 193 -103.410 -35.296 139.607 1.00 36.16 C ANISOU 4079 CG2 THR B 193 3285 3150 7305 -242 -1328 -185 C ATOM 4080 N CYS B 194 -101.392 -33.455 141.252 1.00 44.55 N ANISOU 4080 N CYS B 194 4848 4310 7768 -343 -1008 543 N ATOM 4081 CA CYS B 194 -101.697 -32.795 142.513 1.00 42.27 C ANISOU 4081 CA CYS B 194 4531 4003 7528 -384 -877 658 C ATOM 4082 C CYS B 194 -103.122 -32.266 142.417 1.00 45.34 C ANISOU 4082 C CYS B 194 4774 4355 8098 -331 -994 495 C ATOM 4083 O CYS B 194 -103.409 -31.385 141.596 1.00 43.59 O ANISOU 4083 O CYS B 194 4643 4195 7724 -193 -1206 429 O ATOM 4084 CB CYS B 194 -100.697 -31.673 142.776 1.00 46.86 C ANISOU 4084 CB CYS B 194 5282 4666 7857 -379 -849 796 C ATOM 4085 SG CYS B 194 -101.085 -30.568 144.127 1.00 63.36 S ANISOU 4085 SG CYS B 194 7340 6772 9962 -380 -768 854 S ATOM 4086 N GLU B 195 -104.017 -32.833 143.223 1.00 49.89 N ANISOU 4086 N GLU B 195 5142 4806 9010 -403 -822 418 N ATOM 4087 CA GLU B 195 -105.443 -32.556 143.151 1.00 44.12 C ANISOU 4087 CA GLU B 195 4163 4014 8585 -375 -908 160 C ATOM 4088 C GLU B 195 -105.869 -31.882 144.447 1.00 36.47 C ANISOU 4088 C GLU B 195 3193 2995 7669 -415 -693 299 C ATOM 4089 O GLU B 195 -105.512 -32.342 145.534 1.00 36.58 O ANISOU 4089 O GLU B 195 3289 2928 7682 -469 -370 500 O ATOM 4090 CB GLU B 195 -106.223 -33.851 142.906 1.00 42.84 C ANISOU 4090 CB GLU B 195 3679 3680 8918 -457 -804 -153 C ATOM 4091 CG GLU B 195 -107.686 -33.673 142.555 1.00 52.61 C ANISOU 4091 CG GLU B 195 4543 4874 10571 -406 -968 -602 C ATOM 4092 CD GLU B 195 -108.282 -34.929 141.946 1.00 57.55 C ANISOU 4092 CD GLU B 195 4804 5362 11703 -460 -947 -1056 C ATOM 4093 OE1 GLU B 195 -107.593 -35.571 141.126 1.00 54.02 O ANISOU 4093 OE1 GLU B 195 4421 4974 11130 -429 -1093 -1102 O ATOM 4094 OE2 GLU B 195 -109.429 -35.280 142.292 1.00 63.61 O ANISOU 4094 OE2 GLU B 195 5314 5985 12868 -463 -716 -1357 O ATOM 4095 N ALA B 196 -106.608 -30.782 144.337 1.00 37.60 N ANISOU 4095 N ALA B 196 3285 3194 7809 -330 -875 197 N ATOM 4096 CA ALA B 196 -106.932 -29.942 145.484 1.00 43.65 C ANISOU 4096 CA ALA B 196 4075 3943 8567 -347 -713 321 C ATOM 4097 C ALA B 196 -108.426 -29.663 145.496 1.00 44.35 C ANISOU 4097 C ALA B 196 3862 3953 9034 -321 -763 27 C ATOM 4098 O ALA B 196 -108.960 -29.111 144.531 1.00 43.14 O ANISOU 4098 O ALA B 196 3634 3884 8872 -160 -1116 -200 O ATOM 4099 CB ALA B 196 -106.140 -28.631 145.448 1.00 37.84 C ANISOU 4099 CB ALA B 196 3594 3338 7446 -271 -851 499 C ATOM 4100 N THR B 197 -109.095 -30.030 146.583 1.00 38.34 N ANISOU 4100 N THR B 197 2949 3025 8592 -428 -393 16 N ATOM 4101 CA THR B 197 -110.490 -29.659 146.776 1.00 42.71 C ANISOU 4101 CA THR B 197 3180 3486 9562 -428 -373 -286 C ATOM 4102 C THR B 197 -110.580 -28.537 147.801 1.00 44.71 C ANISOU 4102 C THR B 197 3578 3784 9627 -391 -266 -89 C ATOM 4103 O THR B 197 -109.949 -28.598 148.867 1.00 38.82 O ANISOU 4103 O THR B 197 3068 3025 8656 -412 37 213 O ATOM 4104 CB THR B 197 -111.338 -30.851 147.226 1.00 44.15 C ANISOU 4104 CB THR B 197 3050 3376 10349 -586 76 -506 C ATOM 4105 OG1 THR B 197 -110.941 -31.261 148.540 1.00 45.42 O ANISOU 4105 OG1 THR B 197 3459 3381 10419 -645 626 -136 O ATOM 4106 CG2 THR B 197 -111.189 -32.015 146.259 1.00 46.59 C ANISOU 4106 CG2 THR B 197 3264 3660 10777 -581 1 -728 C ATOM 4107 N HIS B 198 -111.380 -27.526 147.467 1.00 42.12 N ANISOU 4107 N HIS B 198 3108 3520 9374 -280 -541 -297 N ATOM 4108 CA HIS B 198 -111.587 -26.340 148.280 1.00 40.20 C ANISOU 4108 CA HIS B 198 2960 3317 8999 -231 -496 -182 C ATOM 4109 C HIS B 198 -113.013 -25.856 148.068 1.00 44.70 C ANISOU 4109 C HIS B 198 3175 3840 9968 -151 -640 -564 C ATOM 4110 O HIS B 198 -113.600 -26.059 147.002 1.00 48.76 O ANISOU 4110 O HIS B 198 3455 4391 10682 -27 -972 -919 O ATOM 4111 CB HIS B 198 -110.581 -25.237 147.931 1.00 39.28 C ANISOU 4111 CB HIS B 198 3182 3358 8386 -118 -752 47 C ATOM 4112 CG HIS B 198 -110.525 -24.128 148.935 1.00 40.89 C ANISOU 4112 CG HIS B 198 3494 3585 8459 -104 -639 171 C ATOM 4113 ND1 HIS B 198 -110.967 -22.852 148.659 1.00 39.02 N ANISOU 4113 ND1 HIS B 198 3276 3360 8191 28 -844 100 N ATOM 4114 CD2 HIS B 198 -110.080 -24.104 150.213 1.00 36.46 C ANISOU 4114 CD2 HIS B 198 3042 3041 7771 -156 -354 332 C ATOM 4115 CE1 HIS B 198 -110.795 -22.089 149.723 1.00 38.78 C ANISOU 4115 CE1 HIS B 198 3317 3340 8078 -2 -677 193 C ATOM 4116 NE2 HIS B 198 -110.258 -22.824 150.681 1.00 39.63 N ANISOU 4116 NE2 HIS B 198 3477 3475 8105 -94 -404 315 N ATOM 4117 N LYS B 199 -113.571 -25.232 149.108 1.00 46.39 N ANISOU 4117 N LYS B 199 3337 3993 10294 -181 -407 -539 N ATOM 4118 CA LYS B 199 -114.960 -24.784 149.069 1.00 56.37 C ANISOU 4118 CA LYS B 199 4220 5198 12000 -115 -491 -935 C ATOM 4119 C LYS B 199 -115.237 -23.858 147.887 1.00 54.97 C ANISOU 4119 C LYS B 199 4041 5186 11660 184 -1086 -1136 C ATOM 4120 O LYS B 199 -116.354 -23.850 147.355 1.00 55.78 O ANISOU 4120 O LYS B 199 3840 5287 12067 324 -1306 -1595 O ATOM 4121 CB LYS B 199 -115.303 -24.097 150.394 1.00 69.79 C ANISOU 4121 CB LYS B 199 5963 6832 13722 -167 -148 -802 C ATOM 4122 CG LYS B 199 -116.369 -23.017 150.324 1.00 78.01 C ANISOU 4122 CG LYS B 199 6769 7896 14974 -23 -373 -1092 C ATOM 4123 CD LYS B 199 -116.415 -22.233 151.627 1.00 84.89 C ANISOU 4123 CD LYS B 199 7785 8741 15729 -57 -60 -890 C ATOM 4124 CE LYS B 199 -117.472 -21.144 151.588 1.00 92.91 C ANISOU 4124 CE LYS B 199 8566 9766 16971 88 -268 -1177 C ATOM 4125 NZ LYS B 199 -117.418 -20.270 152.794 1.00 94.17 N ANISOU 4125 NZ LYS B 199 8896 9923 16960 77 -11 -986 N ATOM 4126 N THR B 200 -114.234 -23.097 147.442 1.00 55.46 N ANISOU 4126 N THR B 200 4534 5364 11172 318 -1297 -810 N ATOM 4127 CA THR B 200 -114.427 -22.131 146.364 1.00 54.57 C ANISOU 4127 CA THR B 200 4572 5350 10813 682 -1752 -895 C ATOM 4128 C THR B 200 -114.724 -22.770 145.012 1.00 60.65 C ANISOU 4128 C THR B 200 5228 6220 11597 940 -2152 -1216 C ATOM 4129 O THR B 200 -115.020 -22.040 144.060 1.00 65.31 O ANISOU 4129 O THR B 200 6002 6909 11903 1350 -2532 -1321 O ATOM 4130 CB THR B 200 -113.189 -21.241 146.231 1.00 49.60 C ANISOU 4130 CB THR B 200 4455 4723 9666 727 -1716 -455 C ATOM 4131 OG1 THR B 200 -112.029 -22.059 146.031 1.00 41.29 O ANISOU 4131 OG1 THR B 200 3580 3692 8418 558 -1590 -239 O ATOM 4132 CG2 THR B 200 -113.001 -20.401 147.483 1.00 42.04 C ANISOU 4132 CG2 THR B 200 3562 3702 8709 563 -1427 -270 C ATOM 4133 N SER B 201 -114.656 -24.094 144.897 1.00 59.72 N ANISOU 4133 N SER B 201 4872 6079 11741 745 -2050 -1382 N ATOM 4134 CA SER B 201 -114.892 -24.758 143.623 1.00 60.77 C ANISOU 4134 CA SER B 201 4989 6324 11777 952 -2372 -1727 C ATOM 4135 C SER B 201 -115.578 -26.092 143.870 1.00 64.62 C ANISOU 4135 C SER B 201 5087 6671 12794 684 -2111 -2129 C ATOM 4136 O SER B 201 -115.244 -26.800 144.823 1.00 71.82 O ANISOU 4136 O SER B 201 5905 7403 13981 338 -1637 -1929 O ATOM 4137 CB SER B 201 -113.586 -24.970 142.849 1.00 57.65 C ANISOU 4137 CB SER B 201 4944 6006 10954 1058 -2507 -1396 C ATOM 4138 OG SER B 201 -113.833 -25.571 141.590 1.00 61.20 O ANISOU 4138 OG SER B 201 5419 6593 11240 1301 -2813 -1745 O ATOM 4139 N THR B 202 -116.538 -26.431 143.006 1.00 68.25 N ANISOU 4139 N THR B 202 5368 7184 13381 891 -2381 -2700 N ATOM 4140 CA THR B 202 -117.196 -27.725 143.129 1.00 77.38 C ANISOU 4140 CA THR B 202 6166 8132 15104 684 -2101 -3138 C ATOM 4141 C THR B 202 -116.385 -28.831 142.469 1.00 71.40 C ANISOU 4141 C THR B 202 5470 7388 14269 635 -2102 -3105 C ATOM 4142 O THR B 202 -116.468 -29.990 142.889 1.00 70.98 O ANISOU 4142 O THR B 202 5216 7096 14657 380 -1677 -3207 O ATOM 4143 CB THR B 202 -118.598 -27.673 142.516 1.00 85.75 C ANISOU 4143 CB THR B 202 6944 9204 16432 931 -2386 -3874 C ATOM 4144 OG1 THR B 202 -118.505 -27.799 141.091 1.00 85.62 O ANISOU 4144 OG1 THR B 202 7051 9427 16052 1311 -2906 -4174 O ATOM 4145 CG2 THR B 202 -119.283 -26.358 142.859 1.00 86.75 C ANISOU 4145 CG2 THR B 202 7096 9407 16458 1091 -2551 -3890 C ATOM 4146 N SER B 203 -115.590 -28.492 141.455 1.00 59.39 N ANISOU 4146 N SER B 203 4262 6119 12184 905 -2522 -2940 N ATOM 4147 CA SER B 203 -114.681 -29.406 140.774 1.00 58.29 C ANISOU 4147 CA SER B 203 4233 6026 11887 884 -2563 -2860 C ATOM 4148 C SER B 203 -113.288 -29.314 141.389 1.00 64.86 C ANISOU 4148 C SER B 203 5323 6831 12489 651 -2330 -2185 C ATOM 4149 O SER B 203 -112.844 -28.221 141.756 1.00 66.16 O ANISOU 4149 O SER B 203 5722 7055 12361 717 -2380 -1791 O ATOM 4150 CB SER B 203 -114.604 -29.085 139.284 1.00 71.90 C ANISOU 4150 CB SER B 203 6210 8031 13077 1372 -3114 -3070 C ATOM 4151 OG SER B 203 -115.616 -29.761 138.561 1.00 81.43 O ANISOU 4151 OG SER B 203 7129 9248 14564 1553 -3306 -3792 O ATOM 4152 N PRO B 204 -112.585 -30.436 141.518 1.00 60.36 N ANISOU 4152 N PRO B 204 4719 6149 12064 400 -2063 -2064 N ATOM 4153 CA PRO B 204 -111.213 -30.383 142.032 1.00 54.30 C ANISOU 4153 CA PRO B 204 4211 5367 11053 204 -1878 -1476 C ATOM 4154 C PRO B 204 -110.289 -29.619 141.094 1.00 52.81 C ANISOU 4154 C PRO B 204 4519 5381 10163 491 -2189 -1195 C ATOM 4155 O PRO B 204 -110.445 -29.641 139.871 1.00 57.87 O ANISOU 4155 O PRO B 204 5200 6181 10608 833 -2600 -1466 O ATOM 4156 CB PRO B 204 -110.812 -31.861 142.128 1.00 49.57 C ANISOU 4156 CB PRO B 204 3516 4604 10712 -43 -1549 -1505 C ATOM 4157 CG PRO B 204 -112.107 -32.604 142.196 1.00 60.51 C ANISOU 4157 CG PRO B 204 4560 5818 12612 -57 -1347 -2014 C ATOM 4158 CD PRO B 204 -113.054 -31.819 141.337 1.00 64.26 C ANISOU 4158 CD PRO B 204 4937 6476 13004 278 -1843 -2464 C ATOM 4159 N ILE B 205 -109.316 -28.939 141.691 1.00 49.44 N ANISOU 4159 N ILE B 205 4476 4934 9376 377 -1954 -680 N ATOM 4160 CA ILE B 205 -108.287 -28.214 140.955 1.00 47.08 C ANISOU 4160 CA ILE B 205 4654 4720 8512 561 -2052 -371 C ATOM 4161 C ILE B 205 -107.119 -29.166 140.740 1.00 49.82 C ANISOU 4161 C ILE B 205 5124 5058 8747 390 -1893 -206 C ATOM 4162 O ILE B 205 -106.506 -29.633 141.705 1.00 49.03 O ANISOU 4162 O ILE B 205 4994 4878 8756 103 -1577 -4 O ATOM 4163 CB ILE B 205 -107.839 -26.956 141.712 1.00 38.83 C ANISOU 4163 CB ILE B 205 3865 3620 7269 500 -1850 -19 C ATOM 4164 CG1 ILE B 205 -109.013 -25.991 141.898 1.00 40.47 C ANISOU 4164 CG1 ILE B 205 3962 3827 7586 692 -2011 -182 C ATOM 4165 CG2 ILE B 205 -106.701 -26.271 140.971 1.00 38.12 C ANISOU 4165 CG2 ILE B 205 4236 3520 6726 630 -1802 273 C ATOM 4166 CD1 ILE B 205 -108.866 -25.073 143.095 1.00 38.54 C ANISOU 4166 CD1 ILE B 205 3771 3499 7374 515 -1746 50 C ATOM 4167 N VAL B 206 -106.812 -29.462 139.482 1.00 50.74 N ANISOU 4167 N VAL B 206 5399 5268 8610 623 -2121 -305 N ATOM 4168 CA VAL B 206 -105.857 -30.506 139.135 1.00 49.16 C ANISOU 4168 CA VAL B 206 5252 5067 8359 487 -2014 -241 C ATOM 4169 C VAL B 206 -104.658 -29.864 138.455 1.00 53.25 C ANISOU 4169 C VAL B 206 6244 5604 8383 608 -1936 79 C ATOM 4170 O VAL B 206 -104.817 -28.998 137.587 1.00 58.95 O ANISOU 4170 O VAL B 206 7272 6365 8760 964 -2088 107 O ATOM 4171 CB VAL B 206 -106.497 -31.574 138.228 1.00 41.97 C ANISOU 4171 CB VAL B 206 4072 4229 7646 636 -2299 -708 C ATOM 4172 CG1 VAL B 206 -105.475 -32.631 137.836 1.00 55.19 C ANISOU 4172 CG1 VAL B 206 5822 5891 9258 505 -2180 -634 C ATOM 4173 CG2 VAL B 206 -107.691 -32.208 138.922 1.00 43.63 C ANISOU 4173 CG2 VAL B 206 3748 4334 8496 465 -2259 -1089 C ATOM 4174 N LYS B 207 -103.460 -30.283 138.860 1.00 45.19 N ANISOU 4174 N LYS B 207 5295 4531 7343 346 -1660 306 N ATOM 4175 CA LYS B 207 -102.224 -29.838 138.227 1.00 39.73 C ANISOU 4175 CA LYS B 207 4972 3811 6314 394 -1496 542 C ATOM 4176 C LYS B 207 -101.340 -31.060 138.035 1.00 37.56 C ANISOU 4176 C LYS B 207 4629 3557 6083 238 -1416 522 C ATOM 4177 O LYS B 207 -101.041 -31.759 139.005 1.00 38.52 O ANISOU 4177 O LYS B 207 4532 3657 6446 -11 -1286 544 O ATOM 4178 CB LYS B 207 -101.514 -28.785 139.083 1.00 36.78 C ANISOU 4178 CB LYS B 207 4700 3332 5942 220 -1204 781 C ATOM 4179 CG LYS B 207 -101.113 -27.532 138.326 1.00 42.42 C ANISOU 4179 CG LYS B 207 5818 3918 6380 416 -1039 956 C ATOM 4180 CD LYS B 207 -102.333 -26.682 138.010 1.00 39.36 C ANISOU 4180 CD LYS B 207 5554 3528 5873 740 -1241 919 C ATOM 4181 CE LYS B 207 -101.957 -25.438 137.223 1.00 54.15 C ANISOU 4181 CE LYS B 207 7932 5205 7436 1012 -991 1153 C ATOM 4182 NZ LYS B 207 -103.133 -24.547 137.004 1.00 68.77 N ANISOU 4182 NZ LYS B 207 9937 7049 9143 1392 -1195 1132 N ATOM 4183 N SER B 208 -100.906 -31.319 136.805 1.00 41.98 N ANISOU 4183 N SER B 208 5418 4155 6377 434 -1476 493 N ATOM 4184 CA SER B 208 -100.216 -32.569 136.525 1.00 45.64 C ANISOU 4184 CA SER B 208 5788 4647 6908 315 -1445 418 C ATOM 4185 C SER B 208 -99.046 -32.336 135.583 1.00 51.97 C ANISOU 4185 C SER B 208 6945 5418 7382 410 -1257 571 C ATOM 4186 O SER B 208 -98.958 -31.311 134.902 1.00 55.82 O ANISOU 4186 O SER B 208 7802 5847 7562 648 -1159 710 O ATOM 4187 CB SER B 208 -101.164 -33.604 135.905 1.00 44.56 C ANISOU 4187 CB SER B 208 5424 4598 6909 462 -1760 50 C ATOM 4188 OG SER B 208 -102.122 -34.044 136.846 1.00 49.11 O ANISOU 4188 OG SER B 208 5610 5122 7929 292 -1792 -120 O ATOM 4189 N PHE B 209 -98.141 -33.312 135.559 1.00 52.52 N ANISOU 4189 N PHE B 209 6924 5492 7540 239 -1151 553 N ATOM 4190 CA PHE B 209 -97.110 -33.346 134.533 1.00 48.89 C ANISOU 4190 CA PHE B 209 6756 5003 6816 335 -970 626 C ATOM 4191 C PHE B 209 -96.738 -34.793 134.236 1.00 46.14 C ANISOU 4191 C PHE B 209 6233 4722 6574 263 -1059 457 C ATOM 4192 O PHE B 209 -96.770 -35.660 135.116 1.00 38.62 O ANISOU 4192 O PHE B 209 4962 3770 5944 44 -1090 388 O ATOM 4193 CB PHE B 209 -95.865 -32.533 134.928 1.00 41.53 C ANISOU 4193 CB PHE B 209 5931 3922 5926 136 -554 826 C ATOM 4194 CG PHE B 209 -95.008 -33.182 135.976 1.00 39.34 C ANISOU 4194 CG PHE B 209 5325 3666 5957 -171 -471 776 C ATOM 4195 CD1 PHE B 209 -93.950 -34.004 135.616 1.00 46.25 C ANISOU 4195 CD1 PHE B 209 6163 4549 6862 -247 -358 716 C ATOM 4196 CD2 PHE B 209 -95.243 -32.953 137.319 1.00 40.74 C ANISOU 4196 CD2 PHE B 209 5261 3868 6352 -318 -515 778 C ATOM 4197 CE1 PHE B 209 -93.156 -34.598 136.577 1.00 50.12 C ANISOU 4197 CE1 PHE B 209 6375 5081 7587 -429 -328 644 C ATOM 4198 CE2 PHE B 209 -94.451 -33.544 138.283 1.00 50.16 C ANISOU 4198 CE2 PHE B 209 6218 5113 7729 -464 -477 719 C ATOM 4199 CZ PHE B 209 -93.407 -34.368 137.913 1.00 55.22 C ANISOU 4199 CZ PHE B 209 6820 5772 8390 -503 -402 646 C ATOM 4200 N ASN B 210 -96.380 -35.035 132.978 1.00 49.96 N ANISOU 4200 N ASN B 210 6977 5242 6761 491 -1058 406 N ATOM 4201 CA ASN B 210 -95.929 -36.338 132.510 1.00 54.09 C ANISOU 4201 CA ASN B 210 7380 5821 7351 454 -1119 231 C ATOM 4202 C ASN B 210 -94.408 -36.354 132.462 1.00 54.03 C ANISOU 4202 C ASN B 210 7478 5721 7329 279 -746 390 C ATOM 4203 O ASN B 210 -93.789 -35.440 131.908 1.00 55.15 O ANISOU 4203 O ASN B 210 7956 5765 7234 373 -444 558 O ATOM 4204 CB ASN B 210 -96.508 -36.655 131.131 1.00 63.36 C ANISOU 4204 CB ASN B 210 8750 7129 8194 868 -1394 -7 C ATOM 4205 CG ASN B 210 -97.991 -36.951 131.179 1.00 73.15 C ANISOU 4205 CG ASN B 210 9713 8483 9599 1026 -1828 -354 C ATOM 4206 OD1 ASN B 210 -98.465 -37.651 132.073 1.00 75.87 O ANISOU 4206 OD1 ASN B 210 9628 8771 10427 746 -1883 -497 O ATOM 4207 ND2 ASN B 210 -98.734 -36.413 130.220 1.00 82.71 N ANISOU 4207 ND2 ASN B 210 11175 9834 10417 1515 -2109 -514 N ATOM 4208 N ARG B 211 -93.812 -37.389 133.054 1.00 50.55 N ANISOU 4208 N ARG B 211 6750 5281 7176 46 -724 320 N ATOM 4209 CA ARG B 211 -92.361 -37.424 133.194 1.00 43.65 C ANISOU 4209 CA ARG B 211 5868 4342 6375 -122 -416 387 C ATOM 4210 C ARG B 211 -91.656 -37.579 131.852 1.00 48.63 C ANISOU 4210 C ARG B 211 6777 4951 6748 24 -237 359 C ATOM 4211 O ARG B 211 -90.509 -37.142 131.705 1.00 62.31 O ANISOU 4211 O ARG B 211 8590 6572 8511 -78 135 420 O ATOM 4212 CB ARG B 211 -91.954 -38.565 134.122 1.00 44.57 C ANISOU 4212 CB ARG B 211 5656 4482 6797 -292 -484 308 C ATOM 4213 CG ARG B 211 -90.563 -38.424 134.701 1.00 47.39 C ANISOU 4213 CG ARG B 211 5894 4816 7294 -435 -258 308 C ATOM 4214 CD ARG B 211 -90.272 -39.560 135.658 1.00 49.81 C ANISOU 4214 CD ARG B 211 5955 5163 7806 -465 -370 252 C ATOM 4215 NE ARG B 211 -90.710 -40.842 135.118 1.00 52.18 N ANISOU 4215 NE ARG B 211 6243 5442 8142 -408 -487 181 N ATOM 4216 CZ ARG B 211 -90.010 -41.559 134.248 1.00 42.67 C ANISOU 4216 CZ ARG B 211 5066 4237 6908 -386 -433 69 C ATOM 4217 NH1 ARG B 211 -88.839 -41.115 133.814 1.00 40.90 N ANISOU 4217 NH1 ARG B 211 4893 4022 6627 -423 -228 33 N ATOM 4218 NH2 ARG B 211 -90.483 -42.716 133.807 1.00 45.12 N ANISOU 4218 NH2 ARG B 211 5327 4511 7304 -339 -546 -47 N ATOM 4219 N ASN B 212 -92.317 -38.182 130.863 1.00 52.55 N ANISOU 4219 N ASN B 212 7403 5545 7017 280 -474 219 N ATOM 4220 CA ASN B 212 -91.668 -38.434 129.583 1.00 71.76 C ANISOU 4220 CA ASN B 212 10136 7983 9147 480 -313 180 C ATOM 4221 C ASN B 212 -91.690 -37.239 128.638 1.00 86.17 C ANISOU 4221 C ASN B 212 12506 9730 10506 806 -54 371 C ATOM 4222 O ASN B 212 -91.045 -37.297 127.585 1.00 93.22 O ANISOU 4222 O ASN B 212 13744 10579 11098 1007 210 402 O ATOM 4223 CB ASN B 212 -92.312 -39.646 128.899 1.00 78.88 C ANISOU 4223 CB ASN B 212 10938 9041 9991 673 -696 -128 C ATOM 4224 CG ASN B 212 -93.819 -39.512 128.758 1.00 84.09 C ANISOU 4224 CG ASN B 212 11557 9827 10564 931 -1124 -319 C ATOM 4225 OD1 ASN B 212 -94.391 -38.451 129.009 1.00 92.27 O ANISOU 4225 OD1 ASN B 212 12736 10848 11473 1032 -1136 -171 O ATOM 4226 ND2 ASN B 212 -94.470 -40.597 128.354 1.00 80.08 N ANISOU 4226 ND2 ASN B 212 10812 9433 10180 1041 -1474 -708 N ATOM 4227 N GLU B 213 -92.401 -36.165 128.976 1.00 90.22 N ANISOU 4227 N GLU B 213 13149 10195 10934 898 -72 519 N ATOM 4228 CA GLU B 213 -92.414 -34.951 128.160 1.00 98.21 C ANISOU 4228 CA GLU B 213 14748 11063 11503 1250 260 763 C ATOM 4229 C GLU B 213 -91.565 -33.851 128.785 1.00100.90 C ANISOU 4229 C GLU B 213 15118 11103 12116 943 835 998 C ATOM 4230 O GLU B 213 -91.901 -32.666 128.703 1.00 98.55 O ANISOU 4230 O GLU B 213 15153 10636 11655 1115 1066 1211 O ATOM 4231 CB GLU B 213 -93.847 -34.476 127.929 1.00103.41 C ANISOU 4231 CB GLU B 213 15583 11864 11843 1671 -163 723 C ATOM 4232 CG GLU B 213 -94.616 -34.103 129.187 1.00110.59 C ANISOU 4232 CG GLU B 213 16099 12790 13130 1408 -396 705 C ATOM 4233 CD GLU B 213 -95.815 -33.218 128.894 1.00120.92 C ANISOU 4233 CD GLU B 213 17683 14155 14106 1851 -640 733 C ATOM 4234 OE1 GLU B 213 -95.932 -32.737 127.747 1.00125.72 O ANISOU 4234 OE1 GLU B 213 18868 14760 14142 2402 -566 829 O ATOM 4235 OE2 GLU B 213 -96.638 -33.005 129.809 1.00119.71 O ANISOU 4235 OE2 GLU B 213 17199 14049 14237 1698 -896 658 O ATOM 4236 N CYS B 214 -90.439 -34.221 129.390 1.00108.84 N ANISOU 4236 N CYS B 214 15762 12028 13566 518 1079 913 N ATOM 4237 CA CYS B 214 -89.592 -33.296 130.125 1.00117.56 C ANISOU 4237 CA CYS B 214 16714 12878 15074 186 1553 964 C ATOM 4238 C CYS B 214 -88.211 -33.185 129.494 1.00124.59 C ANISOU 4238 C CYS B 214 17726 13512 16100 72 2205 949 C ATOM 4239 O CYS B 214 -87.786 -34.039 128.710 1.00124.47 O ANISOU 4239 O CYS B 214 17813 13565 15917 177 2227 886 O ATOM 4240 CB CYS B 214 -89.472 -33.722 131.593 1.00116.60 C ANISOU 4240 CB CYS B 214 15973 12905 15423 -173 1236 767 C ATOM 4241 SG CYS B 214 -91.072 -33.792 132.418 1.00117.96 S ANISOU 4241 SG CYS B 214 15999 13296 15523 -82 627 792 S ATOM 4242 N ASN B 215 -87.515 -32.112 129.857 1.00128.77 N ANISOU 4242 N ASN B 215 18207 13721 17000 -157 2769 962 N ATOM 4243 CA ASN B 215 -86.168 -31.843 129.369 1.00133.87 C ANISOU 4243 CA ASN B 215 18883 14032 17948 -334 3519 880 C ATOM 4244 C ASN B 215 -85.436 -30.881 130.300 1.00136.76 C ANISOU 4244 C ASN B 215 18835 14129 18997 -726 3932 664 C ATOM 4245 O ASN B 215 -84.241 -31.033 130.557 1.00138.48 O ANISOU 4245 O ASN B 215 18626 14234 19754 -1030 4242 324 O ATOM 4246 CB ASN B 215 -86.214 -31.268 127.952 1.00136.29 C ANISOU 4246 CB ASN B 215 19982 14031 17771 54 4133 1218 C ATOM 4247 CG ASN B 215 -84.940 -30.535 127.580 1.00141.76 C ANISOU 4247 CG ASN B 215 20719 14254 18889 -145 5095 1148 C ATOM 4248 OD1 ASN B 215 -83.905 -31.152 127.332 1.00142.37 O ANISOU 4248 OD1 ASN B 215 20572 14279 19244 -337 5362 927 O ATOM 4249 ND2 ASN B 215 -85.010 -29.209 127.539 1.00147.04 N ANISOU 4249 ND2 ASN B 215 21544 14700 19624 -36 5477 1188 N ATOM 4250 OXT ASN B 215 -86.022 -29.931 130.819 1.00136.25 O ANISOU 4250 OXT ASN B 215 18812 13960 18996 -734 3945 761 O TER 4251 ASN B 215 ATOM 4252 N GLU C 1 -90.093 -1.361 186.543 1.00133.91 N ANISOU 4252 N GLU C 1 18634 12245 20000 -1078 -1540 -5972 N ATOM 4253 CA GLU C 1 -90.596 -2.099 185.390 1.00129.17 C ANISOU 4253 CA GLU C 1 18828 11501 18751 -729 -1474 -4909 C ATOM 4254 C GLU C 1 -90.146 -3.555 185.421 1.00119.62 C ANISOU 4254 C GLU C 1 17432 11119 16898 -665 -1888 -4656 C ATOM 4255 O GLU C 1 -88.949 -3.842 185.449 1.00119.33 O ANISOU 4255 O GLU C 1 16951 11184 17205 -962 -1722 -4932 O ATOM 4256 CB GLU C 1 -90.127 -1.440 184.093 1.00137.78 C ANISOU 4256 CB GLU C 1 20453 11466 20430 -812 -559 -4414 C ATOM 4257 CG GLU C 1 -90.566 -2.166 182.833 1.00136.52 C ANISOU 4257 CG GLU C 1 21085 11214 19572 -388 -477 -3381 C ATOM 4258 CD GLU C 1 -90.107 -1.467 181.570 1.00147.00 C ANISOU 4258 CD GLU C 1 23002 11452 21401 -370 486 -2847 C ATOM 4259 OE1 GLU C 1 -89.561 -0.347 181.673 1.00156.51 O ANISOU 4259 OE1 GLU C 1 24051 11846 23570 -699 1163 -3243 O ATOM 4260 OE2 GLU C 1 -90.285 -2.039 180.474 1.00145.88 O ANISOU 4260 OE2 GLU C 1 23468 11256 20704 -9 614 -2053 O ATOM 4261 N VAL C 2 -91.108 -4.472 185.408 1.00112.77 N ANISOU 4261 N VAL C 2 16881 10808 15157 -273 -2384 -4169 N ATOM 4262 CA VAL C 2 -90.813 -5.882 185.626 1.00104.90 C ANISOU 4262 CA VAL C 2 15674 10618 13564 -177 -2777 -3970 C ATOM 4263 C VAL C 2 -90.384 -6.512 184.307 1.00102.52 C ANISOU 4263 C VAL C 2 15796 9984 13174 -146 -2412 -3271 C ATOM 4264 O VAL C 2 -90.938 -6.207 183.244 1.00103.40 O ANISOU 4264 O VAL C 2 16546 9523 13219 59 -2102 -2734 O ATOM 4265 CB VAL C 2 -92.037 -6.600 186.224 1.00 94.70 C ANISOU 4265 CB VAL C 2 14489 9993 11498 193 -3345 -3817 C ATOM 4266 CG1 VAL C 2 -91.741 -8.077 186.446 1.00 89.93 C ANISOU 4266 CG1 VAL C 2 13704 10120 10346 320 -3623 -3558 C ATOM 4267 CG2 VAL C 2 -92.459 -5.931 187.524 1.00 91.37 C ANISOU 4267 CG2 VAL C 2 13590 9977 11151 168 -3527 -4343 C ATOM 4268 N GLN C 3 -89.394 -7.400 184.373 1.00100.25 N ANISOU 4268 N GLN C 3 15148 10101 12841 -289 -2462 -3289 N ATOM 4269 CA GLN C 3 -88.911 -8.109 183.196 1.00 93.29 C ANISOU 4269 CA GLN C 3 14586 8998 11861 -277 -2148 -2684 C ATOM 4270 C GLN C 3 -88.328 -9.446 183.623 1.00 89.32 C ANISOU 4270 C GLN C 3 13680 9263 10995 -256 -2488 -2671 C ATOM 4271 O GLN C 3 -87.554 -9.510 184.584 1.00 94.59 O ANISOU 4271 O GLN C 3 13720 10390 11831 -402 -2697 -3238 O ATOM 4272 CB GLN C 3 -87.857 -7.289 182.443 1.00 97.54 C ANISOU 4272 CB GLN C 3 15156 8729 13176 -623 -1432 -2750 C ATOM 4273 CG GLN C 3 -87.197 -8.043 181.299 1.00 95.42 C ANISOU 4273 CG GLN C 3 15143 8295 12820 -638 -1089 -2193 C ATOM 4274 CD GLN C 3 -85.955 -7.349 180.778 1.00100.77 C ANISOU 4274 CD GLN C 3 15687 8264 14339 -1052 -350 -2386 C ATOM 4275 OE1 GLN C 3 -85.726 -6.171 181.052 1.00103.40 O ANISOU 4275 OE1 GLN C 3 15874 8032 15383 -1302 38 -2844 O ATOM 4276 NE2 GLN C 3 -85.143 -8.080 180.021 1.00100.21 N ANISOU 4276 NE2 GLN C 3 15638 8180 14257 -1145 -97 -2076 N ATOM 4277 N LEU C 4 -88.702 -10.506 182.908 1.00 83.04 N ANISOU 4277 N LEU C 4 13224 8622 9705 -26 -2537 -2064 N ATOM 4278 CA LEU C 4 -88.166 -11.845 183.127 1.00 81.43 C ANISOU 4278 CA LEU C 4 12727 9017 9196 28 -2743 -1927 C ATOM 4279 C LEU C 4 -87.463 -12.271 181.845 1.00 84.06 C ANISOU 4279 C LEU C 4 13287 8983 9670 -82 -2329 -1500 C ATOM 4280 O LEU C 4 -88.121 -12.581 180.846 1.00 91.83 O ANISOU 4280 O LEU C 4 14770 9749 10374 123 -2201 -1003 O ATOM 4281 CB LEU C 4 -89.271 -12.835 183.497 1.00 73.02 C ANISOU 4281 CB LEU C 4 11789 8459 7494 384 -3108 -1654 C ATOM 4282 CG LEU C 4 -90.253 -12.438 184.601 1.00 71.86 C ANISOU 4282 CG LEU C 4 11564 8617 7122 554 -3457 -1966 C ATOM 4283 CD1 LEU C 4 -91.175 -13.603 184.926 1.00 68.21 C ANISOU 4283 CD1 LEU C 4 10976 8600 6341 805 -3366 -1540 C ATOM 4284 CD2 LEU C 4 -89.518 -11.969 185.844 1.00 71.23 C ANISOU 4284 CD2 LEU C 4 10915 8929 7219 443 -3664 -2590 C ATOM 4285 N GLN C 5 -86.134 -12.288 181.871 1.00 80.25 N ANISOU 4285 N GLN C 5 12403 8477 9611 -375 -2130 -1754 N ATOM 4286 CA GLN C 5 -85.340 -12.664 180.708 1.00 79.39 C ANISOU 4286 CA GLN C 5 12455 8021 9689 -520 -1693 -1405 C ATOM 4287 C GLN C 5 -84.822 -14.085 180.889 1.00 73.88 C ANISOU 4287 C GLN C 5 11443 7929 8698 -434 -1938 -1271 C ATOM 4288 O GLN C 5 -84.136 -14.378 181.873 1.00 78.99 O ANISOU 4288 O GLN C 5 11522 9087 9405 -467 -2210 -1690 O ATOM 4289 CB GLN C 5 -84.182 -11.690 180.491 1.00 93.42 C ANISOU 4289 CB GLN C 5 13997 9241 12256 -940 -1179 -1802 C ATOM 4290 CG GLN C 5 -83.405 -11.944 179.209 1.00100.27 C ANISOU 4290 CG GLN C 5 15106 9649 13343 -1092 -611 -1410 C ATOM 4291 CD GLN C 5 -82.240 -10.992 179.029 1.00108.98 C ANISOU 4291 CD GLN C 5 15935 10134 15339 -1550 13 -1855 C ATOM 4292 OE1 GLN C 5 -82.157 -9.961 179.696 1.00112.95 O ANISOU 4292 OE1 GLN C 5 16162 10399 16356 -1750 106 -2431 O ATOM 4293 NE2 GLN C 5 -81.331 -11.334 178.123 1.00110.67 N ANISOU 4293 NE2 GLN C 5 16187 10061 15802 -1736 494 -1644 N ATOM 4294 N GLN C 6 -85.161 -14.961 179.953 1.00 70.65 N ANISOU 4294 N GLN C 6 11388 7493 7963 -269 -1841 -721 N ATOM 4295 CA GLN C 6 -84.735 -16.351 179.998 1.00 72.18 C ANISOU 4295 CA GLN C 6 11336 8156 7932 -176 -1982 -534 C ATOM 4296 C GLN C 6 -83.518 -16.567 179.106 1.00 67.10 C ANISOU 4296 C GLN C 6 10604 7249 7643 -433 -1584 -452 C ATOM 4297 O GLN C 6 -83.193 -15.747 178.243 1.00 65.31 O ANISOU 4297 O GLN C 6 10639 6426 7749 -634 -1127 -401 O ATOM 4298 CB GLN C 6 -85.875 -17.282 179.576 1.00 75.04 C ANISOU 4298 CB GLN C 6 12031 8675 7804 141 -2100 -102 C ATOM 4299 CG GLN C 6 -87.201 -16.978 180.255 1.00 78.56 C ANISOU 4299 CG GLN C 6 12630 9267 7952 376 -2397 -184 C ATOM 4300 CD GLN C 6 -88.240 -18.056 180.018 1.00 78.63 C ANISOU 4300 CD GLN C 6 12792 9494 7590 658 -2491 86 C ATOM 4301 OE1 GLN C 6 -89.430 -17.848 180.253 1.00 80.27 O ANISOU 4301 OE1 GLN C 6 13152 9735 7614 842 -2626 28 O ATOM 4302 NE2 GLN C 6 -87.793 -19.216 179.553 1.00 76.56 N ANISOU 4302 NE2 GLN C 6 12413 9362 7314 670 -2359 317 N ATOM 4303 N SER C 7 -82.845 -17.693 179.329 1.00 65.30 N ANISOU 4303 N SER C 7 10019 7449 7344 -394 -1710 -416 N ATOM 4304 CA SER C 7 -81.628 -18.008 178.598 1.00 69.70 C ANISOU 4304 CA SER C 7 10400 7837 8246 -638 -1376 -401 C ATOM 4305 C SER C 7 -81.955 -18.343 177.142 1.00 69.12 C ANISOU 4305 C SER C 7 10838 7388 8035 -604 -1015 117 C ATOM 4306 O SER C 7 -83.116 -18.386 176.725 1.00 65.80 O ANISOU 4306 O SER C 7 10856 6908 7239 -352 -1076 409 O ATOM 4307 CB SER C 7 -80.889 -19.158 179.278 1.00 74.25 C ANISOU 4307 CB SER C 7 10462 9015 8735 -515 -1647 -494 C ATOM 4308 OG SER C 7 -81.586 -20.381 179.114 1.00 77.24 O ANISOU 4308 OG SER C 7 11024 9638 8685 -218 -1760 -28 O ATOM 4309 N GLY C 8 -80.909 -18.582 176.358 1.00 71.73 N ANISOU 4309 N GLY C 8 11076 7513 8665 -827 -645 168 N ATOM 4310 CA GLY C 8 -81.070 -18.912 174.959 1.00 62.00 C ANISOU 4310 CA GLY C 8 10286 5997 7274 -761 -285 611 C ATOM 4311 C GLY C 8 -81.608 -20.316 174.744 1.00 57.48 C ANISOU 4311 C GLY C 8 9701 5845 6294 -491 -528 882 C ATOM 4312 O GLY C 8 -81.819 -21.100 175.670 1.00 56.42 O ANISOU 4312 O GLY C 8 9251 6159 6029 -356 -897 807 O ATOM 4313 N ALA C 9 -81.829 -20.633 173.470 1.00 70.59 N ANISOU 4313 N ALA C 9 11714 7341 7766 -379 -255 1189 N ATOM 4314 CA ALA C 9 -82.348 -21.940 173.098 1.00 64.95 C ANISOU 4314 CA ALA C 9 10949 6963 6767 -151 -400 1349 C ATOM 4315 C ALA C 9 -81.287 -23.020 173.276 1.00 68.81 C ANISOU 4315 C ALA C 9 10958 7672 7516 -317 -367 1313 C ATOM 4316 O ALA C 9 -80.083 -22.762 173.207 1.00 74.42 O ANISOU 4316 O ALA C 9 11457 8234 8583 -600 -146 1199 O ATOM 4317 CB ALA C 9 -82.844 -21.927 171.652 1.00 54.09 C ANISOU 4317 CB ALA C 9 10030 5435 5086 74 -145 1578 C ATOM 4318 N GLU C 10 -81.752 -24.245 173.506 1.00 68.51 N ANISOU 4318 N GLU C 10 10728 7958 7346 -129 -546 1381 N ATOM 4319 CA GLU C 10 -80.897 -25.378 173.823 1.00 71.28 C ANISOU 4319 CA GLU C 10 10635 8533 7914 -182 -536 1392 C ATOM 4320 C GLU C 10 -81.094 -26.477 172.788 1.00 70.91 C ANISOU 4320 C GLU C 10 10595 8507 7840 -101 -333 1528 C ATOM 4321 O GLU C 10 -82.224 -26.766 172.380 1.00 76.23 O ANISOU 4321 O GLU C 10 11455 9218 8291 107 -366 1538 O ATOM 4322 CB GLU C 10 -81.203 -25.921 175.222 1.00 72.63 C ANISOU 4322 CB GLU C 10 10537 9044 8016 26 -841 1369 C ATOM 4323 CG GLU C 10 -81.129 -24.878 176.328 1.00 77.03 C ANISOU 4323 CG GLU C 10 11037 9694 8537 14 -1104 1148 C ATOM 4324 CD GLU C 10 -79.706 -24.485 176.677 1.00 80.18 C ANISOU 4324 CD GLU C 10 11061 10158 9245 -192 -1107 876 C ATOM 4325 OE1 GLU C 10 -79.530 -23.502 177.427 1.00 80.61 O ANISOU 4325 OE1 GLU C 10 11004 10260 9363 -256 -1279 556 O ATOM 4326 OE2 GLU C 10 -78.764 -25.161 176.210 1.00 79.24 O ANISOU 4326 OE2 GLU C 10 10707 10058 9345 -289 -935 905 O ATOM 4327 N LEU C 11 -79.988 -27.100 172.382 1.00 66.98 N ANISOU 4327 N LEU C 11 9833 8011 7605 -261 -132 1548 N ATOM 4328 CA LEU C 11 -79.986 -28.199 171.416 1.00 66.19 C ANISOU 4328 CA LEU C 11 9649 7944 7556 -219 84 1613 C ATOM 4329 C LEU C 11 -79.193 -29.333 172.061 1.00 68.88 C ANISOU 4329 C LEU C 11 9518 8456 8196 -220 83 1649 C ATOM 4330 O LEU C 11 -77.964 -29.375 171.964 1.00 73.93 O ANISOU 4330 O LEU C 11 9923 9083 9085 -405 189 1603 O ATOM 4331 CB LEU C 11 -79.393 -27.756 170.080 1.00 61.10 C ANISOU 4331 CB LEU C 11 9218 7091 6906 -376 412 1632 C ATOM 4332 CG LEU C 11 -79.322 -28.800 168.968 1.00 58.16 C ANISOU 4332 CG LEU C 11 8746 6799 6554 -326 637 1629 C ATOM 4333 CD1 LEU C 11 -80.705 -29.353 168.687 1.00 60.28 C ANISOU 4333 CD1 LEU C 11 9086 7240 6579 -21 512 1523 C ATOM 4334 CD2 LEU C 11 -78.724 -28.190 167.710 1.00 54.56 C ANISOU 4334 CD2 LEU C 11 8578 6151 5999 -423 996 1690 C ATOM 4335 N VAL C 12 -79.899 -30.250 172.719 1.00 66.39 N ANISOU 4335 N VAL C 12 9069 8279 7879 20 12 1727 N ATOM 4336 CA VAL C 12 -79.288 -31.235 173.605 1.00 68.58 C ANISOU 4336 CA VAL C 12 8983 8716 8360 168 17 1855 C ATOM 4337 C VAL C 12 -79.442 -32.628 173.007 1.00 65.61 C ANISOU 4337 C VAL C 12 8416 8263 8248 232 331 1923 C ATOM 4338 O VAL C 12 -80.469 -32.944 172.395 1.00 64.22 O ANISOU 4338 O VAL C 12 8343 7992 8067 263 462 1820 O ATOM 4339 CB VAL C 12 -79.910 -31.167 175.014 1.00 78.01 C ANISOU 4339 CB VAL C 12 10200 10082 9358 461 -201 1958 C ATOM 4340 CG1 VAL C 12 -79.121 -32.019 175.991 1.00 86.55 C ANISOU 4340 CG1 VAL C 12 10964 11390 10529 745 -206 2141 C ATOM 4341 CG2 VAL C 12 -79.979 -29.723 175.493 1.00 80.14 C ANISOU 4341 CG2 VAL C 12 10653 10406 9390 376 -504 1792 C ATOM 4342 N LYS C 13 -78.416 -33.459 173.189 1.00 67.68 N ANISOU 4342 N LYS C 13 8355 8582 8778 272 451 2028 N ATOM 4343 CA LYS C 13 -78.513 -34.864 172.829 1.00 67.12 C ANISOU 4343 CA LYS C 13 8056 8398 9050 365 798 2106 C ATOM 4344 C LYS C 13 -79.379 -35.617 173.840 1.00 66.24 C ANISOU 4344 C LYS C 13 7934 8242 8991 707 937 2322 C ATOM 4345 O LYS C 13 -79.397 -35.279 175.027 1.00 76.95 O ANISOU 4345 O LYS C 13 9372 9764 10103 960 738 2508 O ATOM 4346 CB LYS C 13 -77.129 -35.506 172.772 1.00 75.97 C ANISOU 4346 CB LYS C 13 8843 9574 10447 352 897 2176 C ATOM 4347 CG LYS C 13 -76.294 -35.117 171.565 1.00 89.29 C ANISOU 4347 CG LYS C 13 10482 11214 12229 -12 960 1955 C ATOM 4348 CD LYS C 13 -74.853 -35.581 171.729 1.00 98.58 C ANISOU 4348 CD LYS C 13 11290 12490 13676 -17 988 1964 C ATOM 4349 CE LYS C 13 -74.178 -34.897 172.908 1.00102.13 C ANISOU 4349 CE LYS C 13 11640 13203 13963 137 636 1944 C ATOM 4350 NZ LYS C 13 -72.744 -35.281 173.027 1.00102.15 N ANISOU 4350 NZ LYS C 13 11219 13370 14225 164 614 1830 N ATOM 4351 N PRO C 14 -80.106 -36.639 173.393 1.00 60.08 N ANISOU 4351 N PRO C 14 7037 7234 8557 732 1328 2263 N ATOM 4352 CA PRO C 14 -80.993 -37.367 174.308 1.00 60.94 C ANISOU 4352 CA PRO C 14 7148 7186 8822 1029 1621 2459 C ATOM 4353 C PRO C 14 -80.221 -38.110 175.387 1.00 64.76 C ANISOU 4353 C PRO C 14 7526 7703 9378 1418 1785 2924 C ATOM 4354 O PRO C 14 -79.121 -38.620 175.164 1.00 74.76 O ANISOU 4354 O PRO C 14 8576 9008 10822 1446 1844 3023 O ATOM 4355 CB PRO C 14 -81.736 -38.342 173.386 1.00 61.68 C ANISOU 4355 CB PRO C 14 7016 6986 9433 897 2083 2150 C ATOM 4356 CG PRO C 14 -80.881 -38.458 172.170 1.00 61.83 C ANISOU 4356 CG PRO C 14 6855 7063 9573 640 2055 1931 C ATOM 4357 CD PRO C 14 -80.204 -37.133 172.010 1.00 62.16 C ANISOU 4357 CD PRO C 14 7141 7373 9105 496 1560 1942 C ATOM 4358 N GLY C 15 -80.824 -38.165 176.574 1.00 64.92 N ANISOU 4358 N GLY C 15 7716 7733 9218 1782 1869 3215 N ATOM 4359 CA GLY C 15 -80.194 -38.699 177.758 1.00 69.20 C ANISOU 4359 CA GLY C 15 8258 8413 9622 2325 1972 3711 C ATOM 4360 C GLY C 15 -79.496 -37.665 178.618 1.00 71.10 C ANISOU 4360 C GLY C 15 8583 9183 9248 2541 1357 3748 C ATOM 4361 O GLY C 15 -79.407 -37.843 179.837 1.00 75.12 O ANISOU 4361 O GLY C 15 9187 9926 9431 3109 1356 4108 O ATOM 4362 N ALA C 16 -78.998 -36.591 178.011 1.00 67.94 N ANISOU 4362 N ALA C 16 8138 8978 8699 2135 880 3353 N ATOM 4363 CA ALA C 16 -78.267 -35.566 178.739 1.00 65.63 C ANISOU 4363 CA ALA C 16 7814 9154 7968 2260 332 3221 C ATOM 4364 C ALA C 16 -79.220 -34.731 179.597 1.00 76.74 C ANISOU 4364 C ALA C 16 9488 10706 8964 2391 107 3202 C ATOM 4365 O ALA C 16 -80.421 -34.997 179.695 1.00 77.22 O ANISOU 4365 O ALA C 16 9764 10508 9066 2421 391 3332 O ATOM 4366 CB ALA C 16 -77.486 -34.684 177.769 1.00 62.30 C ANISOU 4366 CB ALA C 16 7262 8755 7656 1734 60 2789 C ATOM 4367 N SER C 17 -78.661 -33.700 180.224 1.00 85.65 N ANISOU 4367 N SER C 17 10547 12254 9742 2456 -393 2958 N ATOM 4368 CA SER C 17 -79.400 -32.764 181.056 1.00 90.32 C ANISOU 4368 CA SER C 17 11335 13046 9937 2562 -677 2850 C ATOM 4369 C SER C 17 -79.189 -31.350 180.531 1.00 91.77 C ANISOU 4369 C SER C 17 11505 13223 10142 2051 -1034 2348 C ATOM 4370 O SER C 17 -78.259 -31.083 179.765 1.00 94.80 O ANISOU 4370 O SER C 17 11692 13542 10784 1716 -1078 2100 O ATOM 4371 CB SER C 17 -78.966 -32.855 182.525 1.00 99.52 C ANISOU 4371 CB SER C 17 12402 14761 10649 3217 -903 2955 C ATOM 4372 OG SER C 17 -79.628 -31.882 183.314 1.00107.06 O ANISOU 4372 OG SER C 17 13507 15863 11308 3176 -1160 2674 O ATOM 4373 N VAL C 18 -80.065 -30.436 180.952 1.00 76.69 N ANISOU 4373 N VAL C 18 7373 10480 11286 836 567 2289 N ATOM 4374 CA VAL C 18 -79.959 -29.032 180.570 1.00 75.94 C ANISOU 4374 CA VAL C 18 7540 10369 10945 590 332 1987 C ATOM 4375 C VAL C 18 -80.483 -28.174 181.713 1.00 72.39 C ANISOU 4375 C VAL C 18 7254 10218 10034 573 -147 1870 C ATOM 4376 O VAL C 18 -81.279 -28.621 182.541 1.00 65.57 O ANISOU 4376 O VAL C 18 6430 9538 8946 750 -231 1929 O ATOM 4377 CB VAL C 18 -80.718 -28.732 179.254 1.00 72.88 C ANISOU 4377 CB VAL C 18 7575 9673 10445 489 590 1661 C ATOM 4378 CG1 VAL C 18 -82.209 -28.562 179.511 1.00 64.31 C ANISOU 4378 CG1 VAL C 18 6838 8638 8958 590 460 1465 C ATOM 4379 CG2 VAL C 18 -80.135 -27.506 178.568 1.00 74.78 C ANISOU 4379 CG2 VAL C 18 7958 9803 10654 221 495 1490 C ATOM 4380 N LYS C 19 -80.011 -26.928 181.766 1.00 73.99 N ANISOU 4380 N LYS C 19 7559 10452 10101 339 -428 1689 N ATOM 4381 CA LYS C 19 -80.350 -26.008 182.849 1.00 70.65 C ANISOU 4381 CA LYS C 19 7313 10275 9256 269 -850 1512 C ATOM 4382 C LYS C 19 -80.681 -24.648 182.250 1.00 70.21 C ANISOU 4382 C LYS C 19 7667 9968 9043 86 -927 1133 C ATOM 4383 O LYS C 19 -79.793 -23.954 181.745 1.00 74.64 O ANISOU 4383 O LYS C 19 8181 10397 9780 -161 -970 1094 O ATOM 4384 CB LYS C 19 -79.203 -25.899 183.854 1.00 73.15 C ANISOU 4384 CB LYS C 19 7256 10943 9593 120 -1192 1736 C ATOM 4385 CG LYS C 19 -79.544 -25.131 185.120 1.00 74.62 C ANISOU 4385 CG LYS C 19 7632 11446 9275 20 -1608 1541 C ATOM 4386 CD LYS C 19 -78.473 -25.332 186.182 1.00 79.64 C ANISOU 4386 CD LYS C 19 7842 12538 9881 -127 -1966 1853 C ATOM 4387 CE LYS C 19 -78.846 -24.644 187.485 1.00 80.70 C ANISOU 4387 CE LYS C 19 8208 13034 9420 -268 -2358 1624 C ATOM 4388 NZ LYS C 19 -77.832 -24.893 188.547 1.00 81.27 N ANISOU 4388 NZ LYS C 19 7858 13635 9386 -453 -2760 1968 N ATOM 4389 N ILE C 20 -81.956 -24.273 182.313 1.00 69.64 N ANISOU 4389 N ILE C 20 7965 9818 8678 214 -929 891 N ATOM 4390 CA ILE C 20 -82.457 -23.004 181.801 1.00 68.06 C ANISOU 4390 CA ILE C 20 8157 9345 8356 111 -986 578 C ATOM 4391 C ILE C 20 -82.541 -22.016 182.955 1.00 70.14 C ANISOU 4391 C ILE C 20 8588 9744 8320 26 -1307 334 C ATOM 4392 O ILE C 20 -82.871 -22.395 184.089 1.00 70.10 O ANISOU 4392 O ILE C 20 8527 10054 8055 142 -1428 346 O ATOM 4393 CB ILE C 20 -83.833 -23.193 181.133 1.00 61.60 C ANISOU 4393 CB ILE C 20 7598 8358 7450 319 -782 498 C ATOM 4394 CG1 ILE C 20 -83.749 -24.245 180.027 1.00 58.68 C ANISOU 4394 CG1 ILE C 20 7099 7880 7318 342 -454 686 C ATOM 4395 CG2 ILE C 20 -84.354 -21.879 180.573 1.00 63.42 C ANISOU 4395 CG2 ILE C 20 8192 8292 7611 250 -845 262 C ATOM 4396 CD1 ILE C 20 -85.100 -24.704 179.532 1.00 60.20 C ANISOU 4396 CD1 ILE C 20 7466 8011 7395 511 -292 647 C ATOM 4397 N SER C 21 -82.260 -20.746 182.670 1.00 68.69 N ANISOU 4397 N SER C 21 8632 9308 8158 -194 -1420 100 N ATOM 4398 CA SER C 21 -82.277 -19.696 183.674 1.00 73.47 C ANISOU 4398 CA SER C 21 9454 9954 8506 -336 -1680 -213 C ATOM 4399 C SER C 21 -83.371 -18.681 183.365 1.00 72.33 C ANISOU 4399 C SER C 21 9749 9440 8294 -219 -1593 -510 C ATOM 4400 O SER C 21 -83.883 -18.601 182.245 1.00 71.78 O ANISOU 4400 O SER C 21 9792 9079 8403 -110 -1403 -432 O ATOM 4401 CB SER C 21 -80.920 -18.985 183.755 1.00 79.74 C ANISOU 4401 CB SER C 21 10127 10734 9435 -743 -1901 -252 C ATOM 4402 OG SER C 21 -80.536 -18.472 182.491 1.00 85.29 O ANISOU 4402 OG SER C 21 10892 11051 10463 -882 -1753 -212 O ATOM 4403 N CYS C 22 -83.718 -17.899 184.387 1.00 73.52 N ANISOU 4403 N CYS C 22 10143 9613 8178 -249 -1729 -844 N ATOM 4404 CA CYS C 22 -84.799 -16.919 184.293 1.00 67.28 C ANISOU 4404 CA CYS C 22 9747 8457 7360 -85 -1614 -1133 C ATOM 4405 C CYS C 22 -84.460 -15.790 185.262 1.00 66.89 C ANISOU 4405 C CYS C 22 9958 8326 7132 -337 -1780 -1557 C ATOM 4406 O CYS C 22 -84.659 -15.934 186.472 1.00 71.30 O ANISOU 4406 O CYS C 22 10560 9208 7321 -329 -1860 -1750 O ATOM 4407 CB CYS C 22 -86.138 -17.561 184.626 1.00 66.11 C ANISOU 4407 CB CYS C 22 9621 8465 7033 312 -1445 -1103 C ATOM 4408 SG CYS C 22 -87.512 -16.432 184.924 1.00 66.38 S ANISOU 4408 SG CYS C 22 10059 8147 7015 575 -1286 -1464 S ATOM 4409 N LYS C 23 -83.935 -14.687 184.735 1.00 62.37 N ANISOU 4409 N LYS C 23 9570 7327 6801 -593 -1818 -1704 N ATOM 4410 CA LYS C 23 -83.496 -13.569 185.556 1.00 65.74 C ANISOU 4410 CA LYS C 23 10264 7607 7108 -917 -1965 -2144 C ATOM 4411 C LYS C 23 -84.604 -12.529 185.644 1.00 69.24 C ANISOU 4411 C LYS C 23 11148 7563 7597 -696 -1751 -2494 C ATOM 4412 O LYS C 23 -85.148 -12.102 184.619 1.00 66.42 O ANISOU 4412 O LYS C 23 10902 6759 7577 -497 -1574 -2353 O ATOM 4413 CB LYS C 23 -82.222 -12.935 184.995 1.00 65.06 C ANISOU 4413 CB LYS C 23 10112 7302 7307 -1368 -2116 -2108 C ATOM 4414 CG LYS C 23 -81.516 -12.025 185.988 1.00 72.86 C ANISOU 4414 CG LYS C 23 11282 8283 8117 -1826 -2347 -2546 C ATOM 4415 CD LYS C 23 -80.457 -11.166 185.323 1.00 75.79 C ANISOU 4415 CD LYS C 23 11653 8291 8851 -2267 -2439 -2548 C ATOM 4416 CE LYS C 23 -79.602 -10.458 186.363 1.00 85.95 C ANISOU 4416 CE LYS C 23 13034 9691 9931 -2815 -2732 -2957 C ATOM 4417 NZ LYS C 23 -80.432 -9.807 187.416 1.00 92.42 N ANISOU 4417 NZ LYS C 23 14321 10393 10403 -2768 -2666 -3521 N ATOM 4418 N ALA C 24 -84.936 -12.135 186.869 1.00 73.40 N ANISOU 4418 N ALA C 24 11918 8188 7784 -729 -1753 -2931 N ATOM 4419 CA ALA C 24 -86.016 -11.202 187.144 1.00 78.50 C ANISOU 4419 CA ALA C 24 12968 8384 8472 -482 -1484 -3310 C ATOM 4420 C ALA C 24 -85.448 -9.821 187.449 1.00 83.46 C ANISOU 4420 C ALA C 24 13969 8539 9202 -875 -1518 -3790 C ATOM 4421 O ALA C 24 -84.355 -9.687 188.005 1.00 83.46 O ANISOU 4421 O ALA C 24 13944 8765 9003 -1371 -1790 -3971 O ATOM 4422 CB ALA C 24 -86.870 -11.685 188.318 1.00 81.75 C ANISOU 4422 CB ALA C 24 13442 9190 8428 -240 -1364 -3525 C ATOM 4423 N SER C 25 -86.204 -8.791 187.077 1.00 85.77 N ANISOU 4423 N SER C 25 14591 8159 9837 -658 -1239 -3979 N ATOM 4424 CA SER C 25 -85.827 -7.425 187.412 1.00 94.69 C ANISOU 4424 CA SER C 25 16137 8726 11114 -992 -1188 -4490 C ATOM 4425 C SER C 25 -87.079 -6.580 187.588 1.00103.83 C ANISOU 4425 C SER C 25 17663 9305 12484 -577 -773 -4797 C ATOM 4426 O SER C 25 -88.030 -6.699 186.813 1.00106.61 O ANISOU 4426 O SER C 25 17912 9441 13154 -79 -573 -4436 O ATOM 4427 CB SER C 25 -84.926 -6.814 186.333 1.00 96.29 C ANISOU 4427 CB SER C 25 16310 8493 11784 -1306 -1306 -4258 C ATOM 4428 OG SER C 25 -85.633 -6.635 185.118 1.00 95.23 O ANISOU 4428 OG SER C 25 16149 7925 12109 -907 -1107 -3841 O ATOM 4429 N GLY C 26 -87.076 -5.736 188.616 1.00110.21 N ANISOU 4429 N GLY C 26 18656 10021 13198 -768 -613 -5356 N ATOM 4430 CA GLY C 26 -88.148 -4.788 188.832 1.00114.41 C ANISOU 4430 CA GLY C 26 19366 10035 14071 -394 -184 -5624 C ATOM 4431 C GLY C 26 -89.002 -5.007 190.063 1.00119.70 C ANISOU 4431 C GLY C 26 20079 11062 14341 -157 47 -5999 C ATOM 4432 O GLY C 26 -90.037 -4.344 190.197 1.00125.40 O ANISOU 4432 O GLY C 26 20891 11380 15376 247 416 -6157 O ATOM 4433 N TYR C 27 -88.608 -5.900 190.967 1.00122.35 N ANISOU 4433 N TYR C 27 20326 12151 14013 -384 -168 -6107 N ATOM 4434 CA TYR C 27 -89.381 -6.159 192.177 1.00127.83 C ANISOU 4434 CA TYR C 27 21054 13251 14264 -185 42 -6427 C ATOM 4435 C TYR C 27 -88.505 -6.937 193.148 1.00130.74 C ANISOU 4435 C TYR C 27 21332 14434 13909 -599 -345 -6505 C ATOM 4436 O TYR C 27 -87.393 -7.354 192.815 1.00123.98 O ANISOU 4436 O TYR C 27 20323 13828 12957 -987 -753 -6264 O ATOM 4437 CB TYR C 27 -90.671 -6.929 191.872 1.00118.24 C ANISOU 4437 CB TYR C 27 19676 12137 13114 390 358 -6082 C ATOM 4438 CG TYR C 27 -90.450 -8.316 191.307 1.00103.81 C ANISOU 4438 CG TYR C 27 17609 10789 11045 462 70 -5514 C ATOM 4439 CD1 TYR C 27 -90.316 -8.522 189.940 1.00 97.12 C ANISOU 4439 CD1 TYR C 27 16657 9634 10610 634 -99 -5036 C ATOM 4440 CD2 TYR C 27 -90.384 -9.422 192.143 1.00100.18 C ANISOU 4440 CD2 TYR C 27 16996 11105 9961 394 -67 -5444 C ATOM 4441 CE1 TYR C 27 -90.117 -9.791 189.426 1.00 88.90 C ANISOU 4441 CE1 TYR C 27 15191 9124 9465 700 -355 -4472 C ATOM 4442 CE2 TYR C 27 -90.186 -10.691 191.640 1.00 93.00 C ANISOU 4442 CE2 TYR C 27 15788 10635 8913 524 -357 -4920 C ATOM 4443 CZ TYR C 27 -90.053 -10.871 190.282 1.00 88.54 C ANISOU 4443 CZ TYR C 27 14958 9813 8871 652 -468 -4416 C ATOM 4444 OH TYR C 27 -89.856 -12.137 189.781 1.00 86.46 O ANISOU 4444 OH TYR C 27 14258 10017 8576 719 -669 -3852 O ATOM 4445 N SER C 28 -89.025 -7.128 194.360 1.00138.11 N ANISOU 4445 N SER C 28 22347 15782 14346 -486 -228 -6788 N ATOM 4446 CA SER C 28 -88.341 -7.936 195.364 1.00137.41 C ANISOU 4446 CA SER C 28 22183 16495 13533 -785 -600 -6747 C ATOM 4447 C SER C 28 -88.447 -9.405 194.974 1.00124.68 C ANISOU 4447 C SER C 28 20189 15447 11736 -641 -712 -6189 C ATOM 4448 O SER C 28 -89.529 -9.997 195.047 1.00122.11 O ANISOU 4448 O SER C 28 19753 15289 11354 -273 -361 -6062 O ATOM 4449 CB SER C 28 -88.942 -7.686 196.744 1.00149.43 C ANISOU 4449 CB SER C 28 23983 18233 14560 -681 -401 -7149 C ATOM 4450 OG SER C 28 -90.356 -7.775 196.709 1.00152.01 O ANISOU 4450 OG SER C 28 24286 18417 15054 -123 98 -7177 O ATOM 4451 N PHE C 29 -87.320 -9.992 194.563 1.00113.24 N ANISOU 4451 N PHE C 29 18510 14286 10228 -981 -1163 -5828 N ATOM 4452 CA PHE C 29 -87.329 -11.349 194.024 1.00101.75 C ANISOU 4452 CA PHE C 29 16720 13253 8687 -857 -1284 -5237 C ATOM 4453 C PHE C 29 -87.841 -12.360 195.043 1.00105.75 C ANISOU 4453 C PHE C 29 17068 14469 8644 -700 -1230 -5070 C ATOM 4454 O PHE C 29 -88.600 -13.272 194.695 1.00103.23 O ANISOU 4454 O PHE C 29 16635 14238 8349 -340 -1062 -4657 O ATOM 4455 CB PHE C 29 -85.924 -11.726 193.549 1.00 97.61 C ANISOU 4455 CB PHE C 29 15936 12931 8220 -1262 -1798 -4893 C ATOM 4456 CG PHE C 29 -85.835 -13.092 192.924 1.00 90.21 C ANISOU 4456 CG PHE C 29 14544 12357 7375 -1035 -1940 -4198 C ATOM 4457 CD1 PHE C 29 -86.090 -13.267 191.574 1.00 86.82 C ANISOU 4457 CD1 PHE C 29 13915 11515 7556 -719 -1807 -3813 C ATOM 4458 CD2 PHE C 29 -85.477 -14.197 193.681 1.00 89.75 C ANISOU 4458 CD2 PHE C 29 14185 13058 6858 -1120 -2182 -3884 C ATOM 4459 CE1 PHE C 29 -86.004 -14.518 190.993 1.00 80.54 C ANISOU 4459 CE1 PHE C 29 12665 11029 6908 -508 -1876 -3204 C ATOM 4460 CE2 PHE C 29 -85.389 -15.452 193.105 1.00 85.57 C ANISOU 4460 CE2 PHE C 29 13173 12795 6542 -867 -2244 -3225 C ATOM 4461 CZ PHE C 29 -85.652 -15.612 191.759 1.00 78.73 C ANISOU 4461 CZ PHE C 29 12146 11483 6285 -572 -2074 -2923 C ATOM 4462 N THR C 30 -87.442 -12.215 196.307 1.00112.90 N ANISOU 4462 N THR C 30 18246 15627 9023 -869 -1466 -5229 N ATOM 4463 CA THR C 30 -87.721 -13.232 197.316 1.00113.10 C ANISOU 4463 CA THR C 30 18233 16245 8495 -822 -1481 -4916 C ATOM 4464 C THR C 30 -89.187 -13.296 197.731 1.00119.99 C ANISOU 4464 C THR C 30 19378 16987 9227 -450 -920 -5024 C ATOM 4465 O THR C 30 -89.532 -14.146 198.560 1.00129.06 O ANISOU 4465 O THR C 30 20449 18622 9964 -413 -863 -4769 O ATOM 4466 CB THR C 30 -86.854 -12.990 198.552 1.00114.94 C ANISOU 4466 CB THR C 30 18529 16889 8255 -1224 -1815 -5095 C ATOM 4467 OG1 THR C 30 -87.195 -11.726 199.136 1.00123.32 O ANISOU 4467 OG1 THR C 30 20019 17598 9238 -1270 -1584 -5776 O ATOM 4468 CG2 THR C 30 -85.381 -12.987 198.175 1.00111.30 C ANISOU 4468 CG2 THR C 30 17748 16574 7967 -1664 -2324 -4900 C ATOM 4469 N GLY C 31 -90.054 -12.447 197.186 1.00116.63 N ANISOU 4469 N GLY C 31 19146 15931 9235 -232 -448 -5316 N ATOM 4470 CA GLY C 31 -91.434 -12.412 197.628 1.00119.09 C ANISOU 4470 CA GLY C 31 19514 16198 9536 -23 203 -5474 C ATOM 4471 C GLY C 31 -92.392 -13.177 196.738 1.00110.68 C ANISOU 4471 C GLY C 31 17964 15190 8898 512 411 -5136 C ATOM 4472 O GLY C 31 -93.335 -13.808 197.224 1.00113.16 O ANISOU 4472 O GLY C 31 18168 15761 9066 781 690 -4969 O ATOM 4473 N TYR C 32 -92.157 -13.131 195.431 1.00 99.37 N ANISOU 4473 N TYR C 32 16341 13413 8001 730 221 -4917 N ATOM 4474 CA TYR C 32 -93.064 -13.706 194.447 1.00 91.45 C ANISOU 4474 CA TYR C 32 15050 12254 7443 1299 354 -4502 C ATOM 4475 C TYR C 32 -92.564 -15.084 194.029 1.00 81.54 C ANISOU 4475 C TYR C 32 13413 11498 6070 1327 -10 -3933 C ATOM 4476 O TYR C 32 -91.455 -15.211 193.499 1.00 78.86 O ANISOU 4476 O TYR C 32 12989 11189 5784 1076 -405 -3792 O ATOM 4477 CB TYR C 32 -93.180 -12.793 193.228 1.00 95.35 C ANISOU 4477 CB TYR C 32 15639 12004 8584 1507 401 -4561 C ATOM 4478 CG TYR C 32 -93.722 -11.411 193.512 1.00106.16 C ANISOU 4478 CG TYR C 32 17306 12793 10235 1536 804 -5059 C ATOM 4479 CD1 TYR C 32 -92.912 -10.421 194.051 1.00111.03 C ANISOU 4479 CD1 TYR C 32 18219 13231 10735 1070 750 -5578 C ATOM 4480 CD2 TYR C 32 -95.037 -11.085 193.207 1.00108.89 C ANISOU 4480 CD2 TYR C 32 17561 12782 11031 2026 1225 -4999 C ATOM 4481 CE1 TYR C 32 -93.400 -9.153 194.301 1.00116.64 C ANISOU 4481 CE1 TYR C 32 19117 13418 11781 1148 1101 -6073 C ATOM 4482 CE2 TYR C 32 -95.533 -9.818 193.450 1.00113.84 C ANISOU 4482 CE2 TYR C 32 18375 12871 12009 2092 1596 -5437 C ATOM 4483 CZ TYR C 32 -94.711 -8.858 193.998 1.00119.14 C ANISOU 4483 CZ TYR C 32 19338 13363 12569 1675 1531 -5993 C ATOM 4484 OH TYR C 32 -95.202 -7.596 194.245 1.00130.62 O ANISOU 4484 OH TYR C 32 20936 14290 14405 1839 1819 -6445 O ATOM 4485 N ASN C 33 -93.382 -16.107 194.268 1.00 77.95 N ANISOU 4485 N ASN C 33 12693 11406 5521 1604 157 -3588 N ATOM 4486 CA ASN C 33 -93.013 -17.465 193.892 1.00 74.74 C ANISOU 4486 CA ASN C 33 11898 11428 5072 1643 -101 -3029 C ATOM 4487 C ASN C 33 -92.868 -17.574 192.379 1.00 76.10 C ANISOU 4487 C ASN C 33 11854 11211 5848 1768 -219 -2704 C ATOM 4488 O ASN C 33 -93.611 -16.944 191.621 1.00 76.12 O ANISOU 4488 O ASN C 33 11916 10729 6277 2027 -15 -2771 O ATOM 4489 CB ASN C 33 -94.059 -18.457 194.401 1.00 72.32 C ANISOU 4489 CB ASN C 33 11356 11462 4661 1895 167 -2721 C ATOM 4490 CG ASN C 33 -94.085 -18.545 195.916 1.00 79.97 C ANISOU 4490 CG ASN C 33 12470 12821 5095 1638 262 -2861 C ATOM 4491 OD1 ASN C 33 -93.645 -17.629 196.610 1.00 86.56 O ANISOU 4491 OD1 ASN C 33 13656 13584 5648 1325 250 -3304 O ATOM 4492 ND2 ASN C 33 -94.606 -19.649 196.436 1.00 79.95 N ANISOU 4492 ND2 ASN C 33 12226 13206 4944 1738 364 -2484 N ATOM 4493 N MET C 34 -91.907 -18.381 191.937 1.00 75.92 N ANISOU 4493 N MET C 34 11557 11395 5893 1563 -531 -2311 N ATOM 4494 CA MET C 34 -91.598 -18.513 190.518 1.00 76.34 C ANISOU 4494 CA MET C 34 11421 11110 6476 1581 -633 -2008 C ATOM 4495 C MET C 34 -92.161 -19.830 189.997 1.00 76.19 C ANISOU 4495 C MET C 34 11047 11283 6619 1811 -543 -1525 C ATOM 4496 O MET C 34 -91.779 -20.905 190.472 1.00 75.05 O ANISOU 4496 O MET C 34 10679 11563 6273 1742 -632 -1238 O ATOM 4497 CB MET C 34 -90.091 -18.439 190.275 1.00 77.06 C ANISOU 4497 CB MET C 34 11449 11227 6605 1182 -981 -1938 C ATOM 4498 CG MET C 34 -89.704 -18.310 188.808 1.00 72.99 C ANISOU 4498 CG MET C 34 10823 10304 6605 1153 -1038 -1722 C ATOM 4499 SD MET C 34 -90.238 -16.758 188.058 1.00 74.33 S ANISOU 4499 SD MET C 34 11338 9776 7127 1244 -890 -2048 S ATOM 4500 CE MET C 34 -89.021 -15.620 188.714 1.00 81.45 C ANISOU 4500 CE MET C 34 12527 10556 7866 779 -1111 -2488 C ATOM 4501 N ASN C 35 -93.066 -19.739 189.029 1.00 74.73 N ANISOU 4501 N ASN C 35 10808 10782 6806 2065 -372 -1420 N ATOM 4502 CA ASN C 35 -93.646 -20.896 188.371 1.00 74.55 C ANISOU 4502 CA ASN C 35 10476 10877 6972 2225 -289 -1012 C ATOM 4503 C ASN C 35 -92.881 -21.218 187.095 1.00 78.60 C ANISOU 4503 C ASN C 35 10857 11199 7809 2055 -448 -760 C ATOM 4504 O ASN C 35 -92.328 -20.334 186.437 1.00 82.85 O ANISOU 4504 O ASN C 35 11545 11403 8530 1918 -557 -880 O ATOM 4505 CB ASN C 35 -95.119 -20.653 188.033 1.00 71.47 C ANISOU 4505 CB ASN C 35 10063 10317 6774 2561 -38 -1019 C ATOM 4506 CG ASN C 35 -96.021 -20.743 189.246 1.00 78.59 C ANISOU 4506 CG ASN C 35 10990 11491 7380 2770 212 -1166 C ATOM 4507 OD1 ASN C 35 -96.703 -21.747 189.451 1.00 74.14 O ANISOU 4507 OD1 ASN C 35 10191 11213 6768 2898 346 -915 O ATOM 4508 ND2 ASN C 35 -96.033 -19.691 190.056 1.00 90.79 N ANISOU 4508 ND2 ASN C 35 12836 12935 8726 2784 310 -1592 N ATOM 4509 N TRP C 36 -92.873 -22.498 186.746 1.00 75.71 N ANISOU 4509 N TRP C 36 10221 11026 7520 2057 -418 -416 N ATOM 4510 CA TRP C 36 -92.334 -22.976 185.485 1.00 67.53 C ANISOU 4510 CA TRP C 36 9058 9819 6783 1920 -470 -188 C ATOM 4511 C TRP C 36 -93.403 -23.800 184.788 1.00 69.26 C ANISOU 4511 C TRP C 36 9117 10044 7156 2067 -304 23 C ATOM 4512 O TRP C 36 -94.072 -24.633 185.419 1.00 72.93 O ANISOU 4512 O TRP C 36 9434 10762 7513 2199 -173 142 O ATOM 4513 CB TRP C 36 -91.068 -23.812 185.687 1.00 65.18 C ANISOU 4513 CB TRP C 36 8577 9710 6477 1719 -572 11 C ATOM 4514 CG TRP C 36 -89.878 -23.006 186.101 1.00 72.06 C ANISOU 4514 CG TRP C 36 9550 10572 7258 1491 -792 -153 C ATOM 4515 CD1 TRP C 36 -89.486 -22.720 187.375 1.00 80.93 C ANISOU 4515 CD1 TRP C 36 10731 11971 8047 1411 -930 -292 C ATOM 4516 CD2 TRP C 36 -88.927 -22.374 185.237 1.00 78.69 C ANISOU 4516 CD2 TRP C 36 10442 11133 8323 1267 -904 -196 C ATOM 4517 NE1 TRP C 36 -88.346 -21.954 187.359 1.00 90.32 N ANISOU 4517 NE1 TRP C 36 11990 13071 9256 1132 -1148 -429 N ATOM 4518 CE2 TRP C 36 -87.983 -21.727 186.057 1.00 86.44 C ANISOU 4518 CE2 TRP C 36 11486 12226 9132 1051 -1121 -363 C ATOM 4519 CE3 TRP C 36 -88.782 -22.294 183.848 1.00 79.47 C ANISOU 4519 CE3 TRP C 36 10546 10925 8724 1197 -839 -105 C ATOM 4520 CZ2 TRP C 36 -86.908 -21.010 185.536 1.00 84.08 C ANISOU 4520 CZ2 TRP C 36 11223 11716 9010 776 -1267 -431 C ATOM 4521 CZ3 TRP C 36 -87.716 -21.580 183.333 1.00 78.36 C ANISOU 4521 CZ3 TRP C 36 10460 10580 8732 945 -956 -161 C ATOM 4522 CH2 TRP C 36 -86.792 -20.950 184.175 1.00 79.36 C ANISOU 4522 CH2 TRP C 36 10617 10797 8738 742 -1164 -317 C ATOM 4523 N VAL C 37 -93.540 -23.551 183.484 1.00 68.48 N ANISOU 4523 N VAL C 37 9050 9680 7288 2004 -321 78 N ATOM 4524 CA VAL C 37 -94.631 -24.048 182.654 1.00 63.66 C ANISOU 4524 CA VAL C 37 8326 9055 6806 2084 -224 235 C ATOM 4525 C VAL C 37 -94.042 -24.533 181.335 1.00 59.97 C ANISOU 4525 C VAL C 37 7837 8454 6496 1840 -243 373 C ATOM 4526 O VAL C 37 -93.098 -23.935 180.807 1.00 55.24 O ANISOU 4526 O VAL C 37 7366 7665 5958 1673 -335 320 O ATOM 4527 CB VAL C 37 -95.698 -22.953 182.420 1.00 60.61 C ANISOU 4527 CB VAL C 37 8036 8502 6492 2285 -235 149 C ATOM 4528 CG1 VAL C 37 -96.629 -23.317 181.270 1.00 58.99 C ANISOU 4528 CG1 VAL C 37 7700 8282 6434 2278 -234 360 C ATOM 4529 CG2 VAL C 37 -96.494 -22.702 183.692 1.00 61.56 C ANISOU 4529 CG2 VAL C 37 8144 8775 6473 2553 -106 10 C ATOM 4530 N LYS C 38 -94.585 -25.629 180.812 1.00 59.65 N ANISOU 4530 N LYS C 38 7644 8509 6513 1790 -127 530 N ATOM 4531 CA LYS C 38 -94.134 -26.211 179.557 1.00 56.53 C ANISOU 4531 CA LYS C 38 7254 8001 6223 1532 -79 611 C ATOM 4532 C LYS C 38 -95.186 -25.997 178.475 1.00 52.74 C ANISOU 4532 C LYS C 38 6802 7488 5747 1479 -135 672 C ATOM 4533 O LYS C 38 -96.388 -26.023 178.752 1.00 60.68 O ANISOU 4533 O LYS C 38 7693 8624 6737 1642 -145 724 O ATOM 4534 CB LYS C 38 -93.852 -27.708 179.731 1.00 60.01 C ANISOU 4534 CB LYS C 38 7523 8540 6737 1453 121 721 C ATOM 4535 CG LYS C 38 -93.427 -28.439 178.467 1.00 60.97 C ANISOU 4535 CG LYS C 38 7673 8521 6973 1177 263 746 C ATOM 4536 CD LYS C 38 -93.109 -29.894 178.766 1.00 57.43 C ANISOU 4536 CD LYS C 38 7056 8087 6676 1140 515 846 C ATOM 4537 CE LYS C 38 -92.979 -30.708 177.492 1.00 56.52 C ANISOU 4537 CE LYS C 38 7002 7811 6664 856 730 803 C ATOM 4538 NZ LYS C 38 -92.715 -32.145 177.776 1.00 62.72 N ANISOU 4538 NZ LYS C 38 7633 8525 7674 837 1032 892 N ATOM 4539 N GLN C 39 -94.725 -25.786 177.242 1.00 50.13 N ANISOU 4539 N GLN C 39 6604 7015 5427 1236 -174 690 N ATOM 4540 CA GLN C 39 -95.585 -25.718 176.065 1.00 49.52 C ANISOU 4540 CA GLN C 39 6556 6966 5294 1095 -259 791 C ATOM 4541 C GLN C 39 -94.988 -26.632 175.005 1.00 55.64 C ANISOU 4541 C GLN C 39 7399 7714 6027 738 -111 774 C ATOM 4542 O GLN C 39 -93.933 -26.327 174.437 1.00 48.15 O ANISOU 4542 O GLN C 39 6602 6613 5080 568 -68 732 O ATOM 4543 CB GLN C 39 -95.722 -24.289 175.536 1.00 46.86 C ANISOU 4543 CB GLN C 39 6370 6480 4954 1146 -467 854 C ATOM 4544 CG GLN C 39 -96.769 -24.167 174.427 1.00 50.64 C ANISOU 4544 CG GLN C 39 6823 7061 5357 1035 -620 1047 C ATOM 4545 CD GLN C 39 -96.894 -22.762 173.866 1.00 59.20 C ANISOU 4545 CD GLN C 39 8040 7974 6481 1105 -824 1197 C ATOM 4546 OE1 GLN C 39 -97.775 -22.484 173.053 1.00 69.12 O ANISOU 4546 OE1 GLN C 39 9243 9330 7691 1062 -1002 1429 O ATOM 4547 NE2 GLN C 39 -96.012 -21.875 174.289 1.00 59.22 N ANISOU 4547 NE2 GLN C 39 8202 7718 6581 1194 -812 1094 N ATOM 4548 N SER C 40 -95.657 -27.754 174.755 1.00 69.76 N ANISOU 4548 N SER C 40 9079 9634 7792 607 2 785 N ATOM 4549 CA SER C 40 -95.202 -28.728 173.776 1.00 81.94 C ANISOU 4549 CA SER C 40 10712 11126 9295 248 210 705 C ATOM 4550 C SER C 40 -95.339 -28.169 172.360 1.00 89.70 C ANISOU 4550 C SER C 40 11896 12128 10059 -47 72 735 C ATOM 4551 O SER C 40 -95.911 -27.099 172.131 1.00101.77 O ANISOU 4551 O SER C 40 13449 13715 11504 46 -208 878 O ATOM 4552 CB SER C 40 -95.988 -30.029 173.913 1.00 88.84 C ANISOU 4552 CB SER C 40 11438 12108 10211 156 365 686 C ATOM 4553 OG SER C 40 -97.334 -29.854 173.506 1.00 96.56 O ANISOU 4553 OG SER C 40 12338 13295 11055 90 148 778 O ATOM 4554 N ARG C 41 -94.779 -28.912 171.401 1.00116.67 N ANISOU 4554 N ARG C 41 18088 15612 10630 1334 -1861 192 N ATOM 4555 CA ARG C 41 -94.991 -28.602 169.990 1.00108.11 C ANISOU 4555 CA ARG C 41 17441 14515 9121 1176 -2126 174 C ATOM 4556 C ARG C 41 -96.476 -28.497 169.664 1.00109.39 C ANISOU 4556 C ARG C 41 17438 14868 9260 1385 -2630 165 C ATOM 4557 O ARG C 41 -96.869 -27.716 168.788 1.00112.49 O ANISOU 4557 O ARG C 41 18101 15207 9434 1396 -2956 253 O ATOM 4558 CB ARG C 41 -94.316 -29.673 169.128 1.00102.63 C ANISOU 4558 CB ARG C 41 16852 13816 8326 755 -1828 -41 C ATOM 4559 CG ARG C 41 -94.617 -29.614 167.639 1.00106.95 C ANISOU 4559 CG ARG C 41 17829 14422 8385 510 -2074 -112 C ATOM 4560 CD ARG C 41 -94.180 -28.292 167.028 1.00109.90 C ANISOU 4560 CD ARG C 41 18582 14645 8530 439 -2123 95 C ATOM 4561 NE ARG C 41 -94.150 -28.351 165.569 1.00115.46 N ANISOU 4561 NE ARG C 41 19597 15402 8870 92 -2167 26 N ATOM 4562 CZ ARG C 41 -95.223 -28.264 164.791 1.00121.40 C ANISOU 4562 CZ ARG C 41 20383 16275 9467 128 -2605 60 C ATOM 4563 NH1 ARG C 41 -96.426 -28.115 165.328 1.00123.88 N ANISOU 4563 NH1 ARG C 41 20395 16675 9998 500 -3033 132 N ATOM 4564 NH2 ARG C 41 -95.094 -28.329 163.473 1.00123.64 N ANISOU 4564 NH2 ARG C 41 20979 16616 9381 -205 -2613 -1 N ATOM 4565 N GLY C 42 -97.314 -29.255 170.368 1.00109.35 N ANISOU 4565 N GLY C 42 16854 15069 9623 1488 -2625 60 N ATOM 4566 CA GLY C 42 -98.752 -29.240 170.205 1.00117.07 C ANISOU 4566 CA GLY C 42 17517 16290 10676 1683 -3063 -14 C ATOM 4567 C GLY C 42 -99.465 -28.051 170.809 1.00120.70 C ANISOU 4567 C GLY C 42 17848 16784 11228 2159 -3394 75 C ATOM 4568 O GLY C 42 -100.691 -28.088 170.947 1.00122.59 O ANISOU 4568 O GLY C 42 17647 17274 11656 2373 -3700 -47 O ATOM 4569 N LYS C 43 -98.732 -27.005 171.192 1.00118.07 N ANISOU 4569 N LYS C 43 17851 16204 10805 2328 -3331 240 N ATOM 4570 CA LYS C 43 -99.267 -25.735 171.682 1.00113.21 C ANISOU 4570 CA LYS C 43 17135 15486 10394 2709 -3545 294 C ATOM 4571 C LYS C 43 -100.023 -25.859 173.001 1.00103.85 C ANISOU 4571 C LYS C 43 15366 14600 9494 3077 -3542 151 C ATOM 4572 O LYS C 43 -100.606 -24.872 173.467 1.00106.24 O ANISOU 4572 O LYS C 43 15516 14865 9986 3449 -3735 103 O ATOM 4573 CB LYS C 43 -100.166 -25.060 170.637 1.00113.58 C ANISOU 4573 CB LYS C 43 17289 15466 10399 2812 -4040 313 C ATOM 4574 CG LYS C 43 -99.409 -24.361 169.524 1.00113.29 C ANISOU 4574 CG LYS C 43 17875 15090 10079 2532 -4048 510 C ATOM 4575 CD LYS C 43 -98.913 -22.999 169.984 1.00113.75 C ANISOU 4575 CD LYS C 43 18191 14794 10234 2705 -4005 640 C ATOM 4576 CE LYS C 43 -98.238 -22.248 168.849 1.00120.05 C ANISOU 4576 CE LYS C 43 19604 15277 10734 2413 -4049 837 C ATOM 4577 NZ LYS C 43 -97.878 -20.858 169.246 1.00123.00 N ANISOU 4577 NZ LYS C 43 20260 15274 11202 2587 -4096 946 N ATOM 4578 N SER C 44 -100.032 -27.035 173.619 1.00 91.01 N ANISOU 4578 N SER C 44 13306 13195 8077 2825 -3146 57 N ATOM 4579 CA SER C 44 -100.711 -27.223 174.892 1.00 82.18 C ANISOU 4579 CA SER C 44 11583 12364 7279 2977 -2961 -72 C ATOM 4580 C SER C 44 -99.771 -26.915 176.052 1.00 80.79 C ANISOU 4580 C SER C 44 11495 12063 7139 2997 -2570 31 C ATOM 4581 O SER C 44 -98.565 -27.168 175.986 1.00 86.30 O ANISOU 4581 O SER C 44 12543 12526 7722 2754 -2314 174 O ATOM 4582 CB SER C 44 -101.240 -28.652 175.015 1.00 82.21 C ANISOU 4582 CB SER C 44 11127 12647 7463 2636 -2752 -187 C ATOM 4583 OG SER C 44 -100.248 -29.594 174.647 1.00 77.41 O ANISOU 4583 OG SER C 44 10800 11841 6770 2232 -2470 -88 O ATOM 4584 N LEU C 45 -100.338 -26.366 177.122 1.00 78.88 N ANISOU 4584 N LEU C 45 10903 12007 7063 3288 -2530 -84 N ATOM 4585 CA LEU C 45 -99.569 -25.854 178.246 1.00 71.14 C ANISOU 4585 CA LEU C 45 10022 10931 6077 3363 -2244 -23 C ATOM 4586 C LEU C 45 -99.666 -26.804 179.433 1.00 71.76 C ANISOU 4586 C LEU C 45 9683 11300 6282 3131 -1826 -46 C ATOM 4587 O LEU C 45 -100.691 -27.457 179.648 1.00 80.71 O ANISOU 4587 O LEU C 45 10331 12776 7559 3049 -1783 -186 O ATOM 4588 CB LEU C 45 -100.055 -24.461 178.663 1.00 70.44 C ANISOU 4588 CB LEU C 45 9913 10811 6041 3853 -2485 -165 C ATOM 4589 CG LEU C 45 -99.691 -23.288 177.751 1.00 71.22 C ANISOU 4589 CG LEU C 45 10589 10488 5983 4086 -2887 -62 C ATOM 4590 CD1 LEU C 45 -100.488 -22.051 178.131 1.00 75.25 C ANISOU 4590 CD1 LEU C 45 10973 10968 6651 4632 -3208 -266 C ATOM 4591 CD2 LEU C 45 -98.201 -23.002 177.821 1.00 69.82 C ANISOU 4591 CD2 LEU C 45 10951 9965 5612 3863 -2657 149 C ATOM 4592 N GLU C 46 -98.584 -26.869 180.206 1.00 63.00 N ANISOU 4592 N GLU C 46 8778 10051 5106 2998 -1536 100 N ATOM 4593 CA GLU C 46 -98.516 -27.728 181.380 1.00 67.33 C ANISOU 4593 CA GLU C 46 9061 10813 5709 2754 -1180 153 C ATOM 4594 C GLU C 46 -97.791 -26.989 182.492 1.00 68.32 C ANISOU 4594 C GLU C 46 9334 10890 5735 2878 -1025 189 C ATOM 4595 O GLU C 46 -96.709 -26.438 182.272 1.00 64.21 O ANISOU 4595 O GLU C 46 9216 10052 5129 2919 -1068 290 O ATOM 4596 CB GLU C 46 -97.797 -29.048 181.073 1.00 60.11 C ANISOU 4596 CB GLU C 46 8268 9737 4836 2353 -1021 339 C ATOM 4597 CG GLU C 46 -98.658 -30.078 180.365 1.00 71.45 C ANISOU 4597 CG GLU C 46 9451 11304 6391 2128 -1078 272 C ATOM 4598 CD GLU C 46 -97.930 -31.389 180.144 1.00 73.35 C ANISOU 4598 CD GLU C 46 9826 11326 6720 1758 -920 418 C ATOM 4599 OE1 GLU C 46 -96.727 -31.353 179.812 1.00 77.01 O ANISOU 4599 OE1 GLU C 46 10640 11473 7146 1738 -891 509 O ATOM 4600 OE2 GLU C 46 -98.560 -32.455 180.304 1.00 79.42 O ANISOU 4600 OE2 GLU C 46 10334 12224 7617 1479 -825 415 O ATOM 4601 N TRP C 47 -98.384 -26.990 183.681 1.00 72.66 N ANISOU 4601 N TRP C 47 9553 11778 6275 2892 -827 83 N ATOM 4602 CA TRP C 47 -97.767 -26.383 184.857 1.00 77.50 C ANISOU 4602 CA TRP C 47 10288 12410 6750 2963 -664 88 C ATOM 4603 C TRP C 47 -96.733 -27.356 185.406 1.00 79.77 C ANISOU 4603 C TRP C 47 10747 12591 6969 2605 -469 373 C ATOM 4604 O TRP C 47 -97.076 -28.348 186.052 1.00 79.81 O ANISOU 4604 O TRP C 47 10550 12817 6957 2318 -275 472 O ATOM 4605 CB TRP C 47 -98.826 -26.037 185.898 1.00 75.32 C ANISOU 4605 CB TRP C 47 9594 12580 6443 3082 -502 -178 C ATOM 4606 CG TRP C 47 -98.276 -25.561 187.208 1.00 76.46 C ANISOU 4606 CG TRP C 47 9848 12818 6386 3084 -298 -200 C ATOM 4607 CD1 TRP C 47 -97.749 -24.331 187.476 1.00 79.64 C ANISOU 4607 CD1 TRP C 47 10502 13034 6724 3379 -397 -330 C ATOM 4608 CD2 TRP C 47 -98.224 -26.296 188.438 1.00 89.30 C ANISOU 4608 CD2 TRP C 47 11370 14744 7816 2745 18 -93 C ATOM 4609 NE1 TRP C 47 -97.360 -24.259 188.792 1.00 91.14 N ANISOU 4609 NE1 TRP C 47 11990 14682 7955 3255 -163 -342 N ATOM 4610 CE2 TRP C 47 -97.642 -25.452 189.405 1.00 94.87 C ANISOU 4610 CE2 TRP C 47 12264 15464 8318 2865 86 -181 C ATOM 4611 CE3 TRP C 47 -98.607 -27.587 188.813 1.00 94.26 C ANISOU 4611 CE3 TRP C 47 11810 15606 8397 2319 232 86 C ATOM 4612 CZ2 TRP C 47 -97.434 -25.857 190.722 1.00 94.40 C ANISOU 4612 CZ2 TRP C 47 12216 15682 7970 2580 345 -91 C ATOM 4613 CZ3 TRP C 47 -98.400 -27.988 190.122 1.00 95.12 C ANISOU 4613 CZ3 TRP C 47 11962 15952 8226 2024 490 212 C ATOM 4614 CH2 TRP C 47 -97.818 -27.125 191.060 1.00 93.69 C ANISOU 4614 CH2 TRP C 47 11976 15817 7804 2159 538 126 C ATOM 4615 N ILE C 48 -95.456 -27.077 185.138 1.00 77.46 N ANISOU 4615 N ILE C 48 10833 11947 6652 2612 -540 504 N ATOM 4616 CA ILE C 48 -94.388 -27.918 185.669 1.00 70.06 C ANISOU 4616 CA ILE C 48 10032 10880 5706 2349 -424 742 C ATOM 4617 C ILE C 48 -94.354 -27.823 187.187 1.00 72.53 C ANISOU 4617 C ILE C 48 10284 11442 5832 2296 -272 776 C ATOM 4618 O ILE C 48 -94.358 -28.841 187.889 1.00 77.26 O ANISOU 4618 O ILE C 48 10815 12152 6389 2022 -153 969 O ATOM 4619 CB ILE C 48 -93.032 -27.536 185.048 1.00 63.53 C ANISOU 4619 CB ILE C 48 9543 9675 4920 2378 -521 796 C ATOM 4620 CG1 ILE C 48 -93.026 -27.843 183.549 1.00 65.32 C ANISOU 4620 CG1 ILE C 48 9862 9695 5264 2329 -620 773 C ATOM 4621 CG2 ILE C 48 -91.896 -28.260 185.757 1.00 51.94 C ANISOU 4621 CG2 ILE C 48 8153 8095 3488 2189 -455 987 C ATOM 4622 CD1 ILE C 48 -91.791 -27.348 182.834 1.00 60.53 C ANISOU 4622 CD1 ILE C 48 9573 8773 4655 2313 -659 770 C ATOM 4623 N GLY C 49 -94.323 -26.606 187.717 1.00 71.51 N ANISOU 4623 N GLY C 49 10217 11386 5568 2533 -287 593 N ATOM 4624 CA GLY C 49 -94.326 -26.459 189.159 1.00 70.09 C ANISOU 4624 CA GLY C 49 9997 11486 5149 2465 -131 575 C ATOM 4625 C GLY C 49 -94.001 -25.039 189.569 1.00 71.06 C ANISOU 4625 C GLY C 49 10273 11567 5160 2740 -189 340 C ATOM 4626 O GLY C 49 -94.051 -24.117 188.759 1.00 77.72 O ANISOU 4626 O GLY C 49 11219 12187 6126 3006 -347 179 O ATOM 4627 N TYR C 50 -93.688 -24.878 190.854 1.00 74.67 N ANISOU 4627 N TYR C 50 10782 12228 5362 2650 -77 327 N ATOM 4628 CA TYR C 50 -93.275 -23.567 191.336 1.00 80.23 C ANISOU 4628 CA TYR C 50 11660 12870 5954 2871 -132 82 C ATOM 4629 C TYR C 50 -92.313 -23.726 192.504 1.00 79.81 C ANISOU 4629 C TYR C 50 11787 12897 5638 2661 -110 214 C ATOM 4630 O TYR C 50 -92.237 -24.779 193.141 1.00 71.40 O ANISOU 4630 O TYR C 50 10689 12017 4422 2373 -34 472 O ATOM 4631 CB TYR C 50 -94.477 -22.687 191.729 1.00 79.38 C ANISOU 4631 CB TYR C 50 11321 13048 5790 3139 -20 -331 C ATOM 4632 CG TYR C 50 -95.081 -22.943 193.099 1.00 76.30 C ANISOU 4632 CG TYR C 50 10727 13183 5078 2967 270 -462 C ATOM 4633 CD1 TYR C 50 -94.530 -22.378 194.246 1.00 79.05 C ANISOU 4633 CD1 TYR C 50 11259 13657 5120 2923 333 -586 C ATOM 4634 CD2 TYR C 50 -96.231 -23.709 193.238 1.00 76.33 C ANISOU 4634 CD2 TYR C 50 10358 13584 5058 2812 494 -495 C ATOM 4635 CE1 TYR C 50 -95.084 -22.602 195.491 1.00 84.39 C ANISOU 4635 CE1 TYR C 50 11791 14850 5422 2716 623 -716 C ATOM 4636 CE2 TYR C 50 -96.798 -23.928 194.481 1.00 83.27 C ANISOU 4636 CE2 TYR C 50 11068 14983 5590 2583 815 -627 C ATOM 4637 CZ TYR C 50 -96.218 -23.375 195.604 1.00 86.42 C ANISOU 4637 CZ TYR C 50 11692 15508 5637 2533 884 -731 C ATOM 4638 OH TYR C 50 -96.773 -23.593 196.844 1.00 82.23 O ANISOU 4638 OH TYR C 50 11034 15528 4680 2255 1226 -869 O ATOM 4639 N ILE C 51 -91.568 -22.656 192.763 1.00 80.78 N ANISOU 4639 N ILE C 51 12132 12852 5709 2796 -217 44 N ATOM 4640 CA ILE C 51 -90.604 -22.601 193.853 1.00 83.89 C ANISOU 4640 CA ILE C 51 12689 13300 5885 2612 -259 107 C ATOM 4641 C ILE C 51 -90.801 -21.299 194.616 1.00 92.29 C ANISOU 4641 C ILE C 51 13830 14484 6752 2789 -212 -296 C ATOM 4642 O ILE C 51 -91.024 -20.240 194.017 1.00 99.71 O ANISOU 4642 O ILE C 51 14845 15204 7837 3088 -276 -568 O ATOM 4643 CB ILE C 51 -89.151 -22.729 193.340 1.00 82.43 C ANISOU 4643 CB ILE C 51 12663 12706 5951 2498 -472 300 C ATOM 4644 CG1 ILE C 51 -88.162 -22.698 194.509 1.00 89.84 C ANISOU 4644 CG1 ILE C 51 13698 13706 6730 2292 -572 347 C ATOM 4645 CG2 ILE C 51 -88.831 -21.645 192.317 1.00 74.50 C ANISOU 4645 CG2 ILE C 51 11830 11352 5124 2719 -571 115 C ATOM 4646 CD1 ILE C 51 -86.730 -22.970 194.107 1.00 87.39 C ANISOU 4646 CD1 ILE C 51 13462 13101 6640 2201 -784 508 C ATOM 4647 N ASN C 52 -90.748 -21.388 195.946 1.00 93.03 N ANISOU 4647 N ASN C 52 13917 14876 6554 2569 -112 -336 N ATOM 4648 CA ASN C 52 -90.762 -20.208 196.798 1.00 93.48 C ANISOU 4648 CA ASN C 52 14065 15032 6422 2670 -68 -737 C ATOM 4649 C ASN C 52 -89.332 -19.702 196.918 1.00 97.94 C ANISOU 4649 C ASN C 52 14884 15276 7051 2580 -313 -690 C ATOM 4650 O ASN C 52 -88.493 -20.393 197.518 1.00 98.86 O ANISOU 4650 O ASN C 52 15051 15439 7072 2276 -423 -418 O ATOM 4651 CB ASN C 52 -91.337 -20.537 198.170 1.00 90.31 C ANISOU 4651 CB ASN C 52 13566 15119 5631 2407 167 -817 C ATOM 4652 CG ASN C 52 -91.541 -19.303 199.036 1.00 87.33 C ANISOU 4652 CG ASN C 52 13238 14874 5067 2520 268 -1320 C ATOM 4653 OD1 ASN C 52 -90.644 -18.472 199.186 1.00 82.79 O ANISOU 4653 OD1 ASN C 52 12888 14042 4528 2567 81 -1448 O ATOM 4654 ND2 ASN C 52 -92.733 -19.178 199.609 1.00 89.64 N ANISOU 4654 ND2 ASN C 52 13300 15576 5182 2547 581 -1643 N ATOM 4655 N PRO C 53 -89.002 -18.530 196.370 1.00100.23 N ANISOU 4655 N PRO C 53 15352 15237 7495 2827 -430 -950 N ATOM 4656 CA PRO C 53 -87.597 -18.094 196.384 1.00101.36 C ANISOU 4656 CA PRO C 53 15718 15095 7701 2696 -648 -913 C ATOM 4657 C PRO C 53 -87.067 -17.805 197.775 1.00102.35 C ANISOU 4657 C PRO C 53 15912 15447 7530 2483 -681 -1051 C ATOM 4658 O PRO C 53 -85.866 -17.982 198.011 1.00 98.52 O ANISOU 4658 O PRO C 53 15510 14884 7039 2280 -883 -905 O ATOM 4659 CB PRO C 53 -87.619 -16.831 195.513 1.00101.14 C ANISOU 4659 CB PRO C 53 15923 14657 7848 2986 -732 -1193 C ATOM 4660 CG PRO C 53 -89.010 -16.310 195.664 1.00102.21 C ANISOU 4660 CG PRO C 53 15961 14947 7928 3306 -582 -1527 C ATOM 4661 CD PRO C 53 -89.891 -17.524 195.767 1.00 99.67 C ANISOU 4661 CD PRO C 53 15311 15027 7531 3234 -396 -1314 C ATOM 4662 N PHE C 54 -87.922 -17.369 198.702 1.00105.34 N ANISOU 4662 N PHE C 54 16244 16130 7650 2518 -494 -1358 N ATOM 4663 CA PHE C 54 -87.474 -17.084 200.062 1.00104.87 C ANISOU 4663 CA PHE C 54 16283 16312 7249 2271 -512 -1510 C ATOM 4664 C PHE C 54 -86.956 -18.348 200.743 1.00 99.01 C ANISOU 4664 C PHE C 54 15514 15810 6295 1894 -604 -1074 C ATOM 4665 O PHE C 54 -85.776 -18.440 201.099 1.00103.90 O ANISOU 4665 O PHE C 54 16246 16363 6868 1714 -870 -938 O ATOM 4666 CB PHE C 54 -88.627 -16.458 200.856 1.00111.23 C ANISOU 4666 CB PHE C 54 17016 17419 7826 2366 -229 -1954 C ATOM 4667 CG PHE C 54 -88.237 -15.932 202.218 1.00117.67 C ANISOU 4667 CG PHE C 54 17986 18454 8270 2121 -220 -2211 C ATOM 4668 CD1 PHE C 54 -86.912 -15.886 202.626 1.00117.88 C ANISOU 4668 CD1 PHE C 54 18204 18387 8198 1883 -506 -2077 C ATOM 4669 CD2 PHE C 54 -89.213 -15.485 203.093 1.00121.58 C ANISOU 4669 CD2 PHE C 54 18415 19267 8511 2124 80 -2622 C ATOM 4670 CE1 PHE C 54 -86.574 -15.409 203.878 1.00119.38 C ANISOU 4670 CE1 PHE C 54 18555 18795 8010 1641 -522 -2321 C ATOM 4671 CE2 PHE C 54 -88.880 -15.007 204.345 1.00124.21 C ANISOU 4671 CE2 PHE C 54 18931 19797 8466 1872 107 -2874 C ATOM 4672 CZ PHE C 54 -87.560 -14.970 204.737 1.00122.56 C ANISOU 4672 CZ PHE C 54 18950 19488 8128 1624 -209 -2712 C ATOM 4673 N TYR C 55 -87.825 -19.336 200.930 1.00 92.98 N ANISOU 4673 N TYR C 55 14615 15310 5404 1774 -417 -856 N ATOM 4674 CA TYR C 55 -87.478 -20.529 201.689 1.00 95.48 C ANISOU 4674 CA TYR C 55 14995 15808 5474 1397 -519 -439 C ATOM 4675 C TYR C 55 -86.913 -21.646 200.824 1.00 98.97 C ANISOU 4675 C TYR C 55 15365 15995 6244 1379 -725 28 C ATOM 4676 O TYR C 55 -86.607 -22.720 201.351 1.00105.96 O ANISOU 4676 O TYR C 55 16324 16944 6990 1105 -871 409 O ATOM 4677 CB TYR C 55 -88.701 -21.053 202.448 1.00 97.99 C ANISOU 4677 CB TYR C 55 15283 16520 5430 1197 -193 -447 C ATOM 4678 CG TYR C 55 -89.245 -20.106 203.491 1.00103.89 C ANISOU 4678 CG TYR C 55 16104 17563 5806 1155 46 -922 C ATOM 4679 CD1 TYR C 55 -88.821 -20.177 204.812 1.00 96.26 C ANISOU 4679 CD1 TYR C 55 15426 16782 4367 810 -20 -889 C ATOM 4680 CD2 TYR C 55 -90.188 -19.146 203.157 1.00103.35 C ANISOU 4680 CD2 TYR C 55 15838 17561 5870 1484 315 -1423 C ATOM 4681 CE1 TYR C 55 -89.320 -19.312 205.768 1.00105.17 C ANISOU 4681 CE1 TYR C 55 16645 18165 5151 773 228 -1358 C ATOM 4682 CE2 TYR C 55 -90.695 -18.281 204.105 1.00105.27 C ANISOU 4682 CE2 TYR C 55 16117 18051 5829 1469 549 -1911 C ATOM 4683 CZ TYR C 55 -90.257 -18.365 205.408 1.00104.97 C ANISOU 4683 CZ TYR C 55 16367 18207 5310 1098 530 -1884 C ATOM 4684 OH TYR C 55 -90.764 -17.500 206.349 1.00107.77 O ANISOU 4684 OH TYR C 55 16778 18793 5377 1086 788 -2397 O ATOM 4685 N GLY C 56 -86.772 -21.430 199.518 1.00 94.65 N ANISOU 4685 N GLY C 56 14714 15131 6119 1655 -752 2 N ATOM 4686 CA GLY C 56 -86.267 -22.464 198.641 1.00 87.30 C ANISOU 4686 CA GLY C 56 13703 13953 5516 1647 -905 375 C ATOM 4687 C GLY C 56 -87.194 -23.644 198.463 1.00 84.24 C ANISOU 4687 C GLY C 56 13210 13675 5124 1540 -754 652 C ATOM 4688 O GLY C 56 -86.833 -24.595 197.760 1.00 78.97 O ANISOU 4688 O GLY C 56 12484 12789 4734 1526 -876 950 O ATOM 4689 N THR C 57 -88.374 -23.613 199.078 1.00 85.51 N ANISOU 4689 N THR C 57 13340 14178 4973 1458 -478 528 N ATOM 4690 CA THR C 57 -89.311 -24.721 199.005 1.00 86.75 C ANISOU 4690 CA THR C 57 13408 14492 5061 1300 -304 771 C ATOM 4691 C THR C 57 -89.958 -24.786 197.628 1.00 89.14 C ANISOU 4691 C THR C 57 13498 14664 5706 1570 -193 718 C ATOM 4692 O THR C 57 -90.148 -23.769 196.954 1.00 89.52 O ANISOU 4692 O THR C 57 13480 14619 5914 1889 -155 400 O ATOM 4693 CB THR C 57 -90.390 -24.584 200.077 1.00 87.73 C ANISOU 4693 CB THR C 57 13532 15077 4724 1112 15 586 C ATOM 4694 OG1 THR C 57 -91.220 -23.454 199.778 1.00 87.42 O ANISOU 4694 OG1 THR C 57 13294 15203 4720 1425 254 91 O ATOM 4695 CG2 THR C 57 -89.758 -24.398 201.446 1.00 89.43 C ANISOU 4695 CG2 THR C 57 14034 15405 4541 841 -100 599 C ATOM 4696 N THR C 58 -90.299 -26.002 197.212 1.00 87.36 N ANISOU 4696 N THR C 58 13210 14410 5573 1430 -172 1042 N ATOM 4697 CA THR C 58 -90.818 -26.257 195.880 1.00 80.30 C ANISOU 4697 CA THR C 58 12143 13384 4985 1634 -116 1045 C ATOM 4698 C THR C 58 -92.106 -27.058 195.980 1.00 84.87 C ANISOU 4698 C THR C 58 12552 14320 5376 1467 149 1134 C ATOM 4699 O THR C 58 -92.309 -27.827 196.924 1.00 88.40 O ANISOU 4699 O THR C 58 13083 14965 5541 1107 231 1360 O ATOM 4700 CB THR C 58 -89.806 -27.022 195.014 1.00 75.48 C ANISOU 4700 CB THR C 58 11595 12330 4752 1633 -370 1330 C ATOM 4701 OG1 THR C 58 -89.562 -28.311 195.592 1.00 81.14 O ANISOU 4701 OG1 THR C 58 12412 13022 5396 1336 -473 1725 O ATOM 4702 CG2 THR C 58 -88.493 -26.262 194.919 1.00 73.83 C ANISOU 4702 CG2 THR C 58 11494 11844 4714 1750 -590 1221 C ATOM 4703 N ASN C 59 -92.978 -26.867 194.993 1.00 83.40 N ANISOU 4703 N ASN C 59 12121 14169 5398 1675 267 942 N ATOM 4704 CA ASN C 59 -94.185 -27.669 194.842 1.00 85.36 C ANISOU 4704 CA ASN C 59 12105 14667 5663 1471 495 980 C ATOM 4705 C ASN C 59 -94.297 -28.069 193.380 1.00 82.55 C ANISOU 4705 C ASN C 59 11629 13967 5768 1597 368 1029 C ATOM 4706 O ASN C 59 -94.417 -27.205 192.501 1.00 79.68 O ANISOU 4706 O ASN C 59 11189 13455 5632 1933 282 765 O ATOM 4707 CB ASN C 59 -95.427 -26.901 195.298 1.00 87.26 C ANISOU 4707 CB ASN C 59 12039 15394 5722 1561 799 535 C ATOM 4708 CG ASN C 59 -96.638 -27.797 195.466 1.00 93.21 C ANISOU 4708 CG ASN C 59 12489 16526 6400 1226 1094 567 C ATOM 4709 OD1 ASN C 59 -97.271 -28.195 194.489 1.00 93.98 O ANISOU 4709 OD1 ASN C 59 12334 16542 6832 1266 1082 541 O ATOM 4710 ND2 ASN C 59 -96.968 -28.115 196.712 1.00100.61 N ANISOU 4710 ND2 ASN C 59 13459 17900 6869 850 1366 615 N ATOM 4711 N TYR C 60 -94.243 -29.372 193.126 1.00 84.00 N ANISOU 4711 N TYR C 60 11841 14003 6071 1314 336 1369 N ATOM 4712 CA TYR C 60 -94.163 -29.921 191.783 1.00 80.83 C ANISOU 4712 CA TYR C 60 11386 13247 6077 1374 202 1434 C ATOM 4713 C TYR C 60 -95.499 -30.500 191.341 1.00 81.33 C ANISOU 4713 C TYR C 60 11131 13532 6237 1214 376 1352 C ATOM 4714 O TYR C 60 -96.297 -30.974 192.155 1.00 84.52 O ANISOU 4714 O TYR C 60 11401 14296 6418 907 608 1397 O ATOM 4715 CB TYR C 60 -93.097 -31.016 191.701 1.00 79.33 C ANISOU 4715 CB TYR C 60 11436 12661 6042 1202 9 1812 C ATOM 4716 CG TYR C 60 -91.676 -30.509 191.716 1.00 76.38 C ANISOU 4716 CG TYR C 60 11285 12002 5736 1400 -218 1836 C ATOM 4717 CD1 TYR C 60 -91.026 -30.178 190.535 1.00 72.55 C ANISOU 4717 CD1 TYR C 60 10812 11189 5564 1615 -338 1703 C ATOM 4718 CD2 TYR C 60 -90.981 -30.371 192.909 1.00 75.01 C ANISOU 4718 CD2 TYR C 60 11302 11911 5288 1332 -308 1977 C ATOM 4719 CE1 TYR C 60 -89.725 -29.717 190.541 1.00 71.85 C ANISOU 4719 CE1 TYR C 60 10873 10875 5553 1742 -505 1687 C ATOM 4720 CE2 TYR C 60 -89.679 -29.912 192.925 1.00 75.67 C ANISOU 4720 CE2 TYR C 60 11528 11760 5464 1494 -531 1964 C ATOM 4721 CZ TYR C 60 -89.056 -29.586 191.739 1.00 74.69 C ANISOU 4721 CZ TYR C 60 11365 11324 5692 1692 -610 1807 C ATOM 4722 OH TYR C 60 -87.760 -29.127 191.753 1.00 76.14 O ANISOU 4722 OH TYR C 60 11639 11310 5981 1802 -793 1756 O ATOM 4723 N ASN C 61 -95.731 -30.453 190.034 1.00 77.56 N ANISOU 4723 N ASN C 61 10539 12856 6074 1388 263 1220 N ATOM 4724 CA ASN C 61 -96.696 -31.349 189.418 1.00 79.23 C ANISOU 4724 CA ASN C 61 10502 13144 6457 1172 334 1222 C ATOM 4725 C ASN C 61 -96.149 -32.768 189.497 1.00 88.11 C ANISOU 4725 C ASN C 61 11829 13974 7676 815 293 1603 C ATOM 4726 O ASN C 61 -95.017 -33.028 189.075 1.00 88.34 O ANISOU 4726 O ASN C 61 12111 13579 7873 902 99 1751 O ATOM 4727 CB ASN C 61 -96.943 -30.943 187.965 1.00 74.60 C ANISOU 4727 CB ASN C 61 9818 12387 6140 1443 156 1004 C ATOM 4728 CG ASN C 61 -98.023 -31.774 187.289 1.00 81.13 C ANISOU 4728 CG ASN C 61 10348 13338 7141 1233 194 941 C ATOM 4729 OD1 ASN C 61 -98.477 -32.788 187.819 1.00 88.12 O ANISOU 4729 OD1 ASN C 61 11130 14358 7995 838 363 1093 O ATOM 4730 ND2 ASN C 61 -98.432 -31.346 186.100 1.00 79.85 N ANISOU 4730 ND2 ASN C 61 10076 13117 7148 1465 13 725 N ATOM 4731 N GLN C 62 -96.948 -33.686 190.050 1.00 99.29 N ANISOU 4731 N GLN C 62 13126 15599 8999 404 478 1742 N ATOM 4732 CA GLN C 62 -96.492 -35.059 190.244 1.00105.97 C ANISOU 4732 CA GLN C 62 14219 16111 9935 44 411 2136 C ATOM 4733 C GLN C 62 -96.036 -35.712 188.944 1.00107.87 C ANISOU 4733 C GLN C 62 14521 15871 10595 122 208 2138 C ATOM 4734 O GLN C 62 -95.330 -36.726 188.986 1.00112.65 O ANISOU 4734 O GLN C 62 15375 16060 11366 -36 71 2420 O ATOM 4735 CB GLN C 62 -97.603 -35.893 190.886 1.00114.61 C ANISOU 4735 CB GLN C 62 15169 17510 10868 -472 669 2254 C ATOM 4736 CG GLN C 62 -98.058 -35.388 192.249 1.00123.56 C ANISOU 4736 CG GLN C 62 16260 19165 11522 -648 937 2244 C ATOM 4737 CD GLN C 62 -97.004 -35.560 193.329 1.00128.73 C ANISOU 4737 CD GLN C 62 17375 19652 11885 -741 812 2624 C ATOM 4738 OE1 GLN C 62 -96.062 -36.338 193.177 1.00128.26 O ANISOU 4738 OE1 GLN C 62 17644 19075 12014 -764 531 2961 O ATOM 4739 NE2 GLN C 62 -97.162 -34.832 194.428 1.00133.24 N ANISOU 4739 NE2 GLN C 62 17958 20666 12002 -780 998 2540 N ATOM 4740 N ARG C 63 -96.420 -35.153 187.795 1.00103.79 N ANISOU 4740 N ARG C 63 13800 15393 10244 366 166 1817 N ATOM 4741 CA ARG C 63 -95.999 -35.690 186.508 1.00 93.84 C ANISOU 4741 CA ARG C 63 12612 13732 9312 420 3 1760 C ATOM 4742 C ARG C 63 -94.550 -35.348 186.187 1.00 85.54 C ANISOU 4742 C ARG C 63 11826 12312 8364 696 -163 1785 C ATOM 4743 O ARG C 63 -93.900 -36.076 185.428 1.00 88.02 O ANISOU 4743 O ARG C 63 12255 12237 8951 672 -265 1795 O ATOM 4744 CB ARG C 63 -96.917 -35.164 185.404 1.00 97.33 C ANISOU 4744 CB ARG C 63 12788 14375 9821 560 -21 1424 C ATOM 4745 CG ARG C 63 -97.822 -36.211 184.785 1.00108.71 C ANISOU 4745 CG ARG C 63 14039 15820 11446 237 2 1372 C ATOM 4746 CD ARG C 63 -98.513 -35.660 183.549 1.00115.91 C ANISOU 4746 CD ARG C 63 14744 16873 12425 428 -128 1044 C ATOM 4747 NE ARG C 63 -97.558 -35.108 182.593 1.00119.21 N ANISOU 4747 NE ARG C 63 15429 16992 12874 724 -304 965 N ATOM 4748 CZ ARG C 63 -97.091 -35.765 181.537 1.00121.85 C ANISOU 4748 CZ ARG C 63 15921 17001 13375 641 -397 913 C ATOM 4749 NH1 ARG C 63 -97.497 -37.004 181.292 1.00125.72 N ANISOU 4749 NH1 ARG C 63 16339 17374 14054 304 -369 927 N ATOM 4750 NH2 ARG C 63 -96.224 -35.182 180.721 1.00118.87 N ANISOU 4750 NH2 ARG C 63 15783 16418 12966 861 -497 821 N ATOM 4751 N PHE C 64 -94.028 -34.259 186.748 1.00 80.09 N ANISOU 4751 N PHE C 64 11211 11746 7475 940 -176 1751 N ATOM 4752 CA PHE C 64 -92.681 -33.790 186.449 1.00 75.22 C ANISOU 4752 CA PHE C 64 10790 10841 6948 1172 -308 1725 C ATOM 4753 C PHE C 64 -91.670 -34.124 187.537 1.00 77.82 C ANISOU 4753 C PHE C 64 11296 11025 7246 1132 -398 1983 C ATOM 4754 O PHE C 64 -90.488 -33.805 187.377 1.00 76.63 O ANISOU 4754 O PHE C 64 11252 10654 7209 1303 -515 1944 O ATOM 4755 CB PHE C 64 -92.688 -32.278 186.199 1.00 67.98 C ANISOU 4755 CB PHE C 64 9870 10094 5866 1464 -310 1488 C ATOM 4756 CG PHE C 64 -93.473 -31.871 184.986 1.00 62.46 C ANISOU 4756 CG PHE C 64 9067 9454 5211 1563 -332 1255 C ATOM 4757 CD1 PHE C 64 -92.864 -31.800 183.744 1.00 54.16 C ANISOU 4757 CD1 PHE C 64 8153 8133 4291 1625 -415 1146 C ATOM 4758 CD2 PHE C 64 -94.819 -31.563 185.085 1.00 66.96 C ANISOU 4758 CD2 PHE C 64 9392 10369 5680 1585 -280 1127 C ATOM 4759 CE1 PHE C 64 -93.582 -31.428 182.624 1.00 56.14 C ANISOU 4759 CE1 PHE C 64 8372 8438 4521 1695 -489 966 C ATOM 4760 CE2 PHE C 64 -95.543 -31.190 183.969 1.00 71.39 C ANISOU 4760 CE2 PHE C 64 9856 10976 6293 1706 -386 923 C ATOM 4761 CZ PHE C 64 -94.923 -31.123 182.737 1.00 65.63 C ANISOU 4761 CZ PHE C 64 9338 9955 5644 1756 -512 869 C ATOM 4762 N LYS C 65 -92.107 -34.730 188.641 1.00 82.17 N ANISOU 4762 N LYS C 65 11883 11713 7627 887 -357 2241 N ATOM 4763 CA LYS C 65 -91.194 -35.076 189.723 1.00 82.65 C ANISOU 4763 CA LYS C 65 12161 11636 7607 837 -516 2532 C ATOM 4764 C LYS C 65 -90.060 -35.947 189.197 1.00 79.83 C ANISOU 4764 C LYS C 65 11906 10757 7670 910 -746 2619 C ATOM 4765 O LYS C 65 -90.287 -36.890 188.433 1.00 86.24 O ANISOU 4765 O LYS C 65 12686 11302 8779 802 -749 2613 O ATOM 4766 CB LYS C 65 -91.949 -35.798 190.839 1.00 91.40 C ANISOU 4766 CB LYS C 65 13356 12933 8441 467 -434 2841 C ATOM 4767 CG LYS C 65 -91.465 -35.458 192.238 1.00102.88 C ANISOU 4767 CG LYS C 65 15017 14560 9512 422 -516 3054 C ATOM 4768 CD LYS C 65 -92.599 -34.921 193.098 1.00109.78 C ANISOU 4768 CD LYS C 65 15801 16005 9904 214 -216 2987 C ATOM 4769 CE LYS C 65 -92.128 -34.617 194.511 1.00112.80 C ANISOU 4769 CE LYS C 65 16436 16591 9832 118 -288 3184 C ATOM 4770 NZ LYS C 65 -93.236 -34.120 195.372 1.00115.07 N ANISOU 4770 NZ LYS C 65 16622 17476 9623 -116 65 3056 N ATOM 4771 N GLY C 66 -88.832 -35.621 189.601 1.00 75.26 N ANISOU 4771 N GLY C 66 11417 10039 7140 1100 -944 2651 N ATOM 4772 CA GLY C 66 -87.653 -36.300 189.104 1.00 72.89 C ANISOU 4772 CA GLY C 66 11127 9282 7288 1238 -1162 2637 C ATOM 4773 C GLY C 66 -87.254 -35.946 187.690 1.00 74.91 C ANISOU 4773 C GLY C 66 11224 9413 7824 1405 -1053 2253 C ATOM 4774 O GLY C 66 -86.137 -36.286 187.279 1.00 80.31 O ANISOU 4774 O GLY C 66 11854 9790 8870 1547 -1183 2136 O ATOM 4775 N LYS C 67 -88.121 -35.280 186.927 1.00 70.15 N ANISOU 4775 N LYS C 67 10546 9048 7060 1386 -829 2039 N ATOM 4776 CA LYS C 67 -87.770 -34.777 185.606 1.00 66.35 C ANISOU 4776 CA LYS C 67 9997 8496 6717 1499 -727 1703 C ATOM 4777 C LYS C 67 -87.282 -33.336 185.658 1.00 67.06 C ANISOU 4777 C LYS C 67 10116 8769 6595 1652 -690 1549 C ATOM 4778 O LYS C 67 -86.367 -32.964 184.916 1.00 70.70 O ANISOU 4778 O LYS C 67 10564 9097 7201 1723 -660 1332 O ATOM 4779 CB LYS C 67 -88.969 -34.884 184.661 1.00 67.64 C ANISOU 4779 CB LYS C 67 10110 8770 6821 1390 -585 1577 C ATOM 4780 CG LYS C 67 -88.594 -34.835 183.191 1.00 67.24 C ANISOU 4780 CG LYS C 67 10053 8564 6930 1419 -512 1275 C ATOM 4781 CD LYS C 67 -87.530 -35.867 182.868 1.00 75.95 C ANISOU 4781 CD LYS C 67 11126 9287 8445 1419 -564 1197 C ATOM 4782 CE LYS C 67 -87.358 -36.032 181.371 1.00 75.55 C ANISOU 4782 CE LYS C 67 11066 9124 8515 1369 -433 857 C ATOM 4783 NZ LYS C 67 -87.985 -37.282 180.863 1.00 80.49 N ANISOU 4783 NZ LYS C 67 11669 9560 9355 1212 -438 820 N ATOM 4784 N ALA C 68 -87.875 -32.520 186.524 1.00 67.05 N ANISOU 4784 N ALA C 68 10156 9066 6254 1677 -671 1630 N ATOM 4785 CA ALA C 68 -87.507 -31.121 186.656 1.00 70.06 C ANISOU 4785 CA ALA C 68 10602 9582 6437 1814 -652 1478 C ATOM 4786 C ALA C 68 -86.941 -30.876 188.047 1.00 70.61 C ANISOU 4786 C ALA C 68 10722 9753 6354 1836 -777 1621 C ATOM 4787 O ALA C 68 -87.342 -31.515 189.024 1.00 71.44 O ANISOU 4787 O ALA C 68 10848 9963 6333 1731 -832 1859 O ATOM 4788 CB ALA C 68 -88.706 -30.199 186.406 1.00 72.10 C ANISOU 4788 CB ALA C 68 10868 10087 6440 1879 -547 1358 C ATOM 4789 N THR C 69 -86.004 -29.936 188.123 1.00 69.07 N ANISOU 4789 N THR C 69 10572 9532 6139 1928 -825 1474 N ATOM 4790 CA THR C 69 -85.417 -29.507 189.386 1.00 67.99 C ANISOU 4790 CA THR C 69 10493 9518 5824 1948 -969 1547 C ATOM 4791 C THR C 69 -85.386 -27.988 189.405 1.00 70.47 C ANISOU 4791 C THR C 69 10901 9950 5926 2033 -899 1315 C ATOM 4792 O THR C 69 -84.693 -27.371 188.590 1.00 74.40 O ANISOU 4792 O THR C 69 11419 10286 6566 2052 -865 1124 O ATOM 4793 CB THR C 69 -84.007 -30.072 189.569 1.00 68.96 C ANISOU 4793 CB THR C 69 10536 9422 6242 1963 -1186 1588 C ATOM 4794 OG1 THR C 69 -84.055 -31.505 189.533 1.00 70.79 O ANISOU 4794 OG1 THR C 69 10716 9460 6720 1919 -1292 1800 O ATOM 4795 CG2 THR C 69 -83.423 -29.620 190.898 1.00 73.89 C ANISOU 4795 CG2 THR C 69 11230 10200 6646 1972 -1394 1666 C ATOM 4796 N LEU C 70 -86.143 -27.392 190.320 1.00 71.23 N ANISOU 4796 N LEU C 70 11067 10315 5683 2059 -862 1312 N ATOM 4797 CA LEU C 70 -86.221 -25.943 190.431 1.00 71.38 C ANISOU 4797 CA LEU C 70 11198 10404 5518 2167 -817 1066 C ATOM 4798 C LEU C 70 -85.218 -25.462 191.470 1.00 72.90 C ANISOU 4798 C LEU C 70 11464 10649 5585 2135 -970 1032 C ATOM 4799 O LEU C 70 -85.125 -26.030 192.563 1.00 72.37 O ANISOU 4799 O LEU C 70 11378 10740 5380 2033 -1070 1198 O ATOM 4800 CB LEU C 70 -87.636 -25.507 190.811 1.00 68.28 C ANISOU 4800 CB LEU C 70 10774 10270 4900 2234 -673 972 C ATOM 4801 CG LEU C 70 -88.758 -26.006 189.895 1.00 64.09 C ANISOU 4801 CG LEU C 70 10134 9765 4453 2278 -566 996 C ATOM 4802 CD1 LEU C 70 -90.071 -25.310 190.220 1.00 65.56 C ANISOU 4802 CD1 LEU C 70 10236 10226 4447 2420 -450 802 C ATOM 4803 CD2 LEU C 70 -88.395 -25.823 188.428 1.00 59.74 C ANISOU 4803 CD2 LEU C 70 9645 8905 4147 2322 -595 925 C ATOM 4804 N THR C 71 -84.468 -24.417 191.126 1.00 74.30 N ANISOU 4804 N THR C 71 11729 10677 5826 2161 -994 815 N ATOM 4805 CA THR C 71 -83.496 -23.825 192.035 1.00 73.87 C ANISOU 4805 CA THR C 71 11729 10671 5667 2110 -1152 720 C ATOM 4806 C THR C 71 -83.550 -22.310 191.904 1.00 80.26 C ANISOU 4806 C THR C 71 12724 11403 6367 2162 -1089 430 C ATOM 4807 O THR C 71 -84.084 -21.770 190.934 1.00 76.94 O ANISOU 4807 O THR C 71 12401 10815 6019 2236 -969 337 O ATOM 4808 CB THR C 71 -82.066 -24.322 191.763 1.00 64.95 C ANISOU 4808 CB THR C 71 10451 9369 4857 2015 -1307 744 C ATOM 4809 OG1 THR C 71 -81.734 -24.107 190.385 1.00 68.72 O ANISOU 4809 OG1 THR C 71 10901 9603 5606 1976 -1159 612 O ATOM 4810 CG2 THR C 71 -81.926 -25.801 192.096 1.00 57.62 C ANISOU 4810 CG2 THR C 71 9374 8456 4063 2007 -1459 1028 C ATOM 4811 N VAL C 72 -82.997 -21.623 192.903 1.00 86.50 N ANISOU 4811 N VAL C 72 13597 12293 6976 2118 -1209 291 N ATOM 4812 CA VAL C 72 -82.919 -20.170 192.884 1.00 90.35 C ANISOU 4812 CA VAL C 72 14295 12648 7386 2144 -1185 -6 C ATOM 4813 C VAL C 72 -81.506 -19.734 193.240 1.00 84.04 C ANISOU 4813 C VAL C 72 13494 11775 6663 1962 -1349 -132 C ATOM 4814 O VAL C 72 -80.737 -20.466 193.867 1.00 75.79 O ANISOU 4814 O VAL C 72 12278 10876 5642 1874 -1529 -17 O ATOM 4815 CB VAL C 72 -83.937 -19.511 193.842 1.00 97.70 C ANISOU 4815 CB VAL C 72 15343 13802 7978 2289 -1128 -182 C ATOM 4816 CG1 VAL C 72 -85.351 -19.661 193.306 1.00 96.20 C ANISOU 4816 CG1 VAL C 72 15105 13653 7793 2482 -956 -161 C ATOM 4817 CG2 VAL C 72 -83.820 -20.110 195.236 1.00 99.15 C ANISOU 4817 CG2 VAL C 72 15433 14339 7902 2172 -1212 -87 C ATOM 4818 N ASP C 73 -81.175 -18.517 192.819 1.00 85.70 N ANISOU 4818 N ASP C 73 13901 11735 6925 1899 -1314 -372 N ATOM 4819 CA ASP C 73 -79.975 -17.807 193.255 1.00 85.70 C ANISOU 4819 CA ASP C 73 13929 11675 6959 1692 -1449 -578 C ATOM 4820 C ASP C 73 -80.439 -16.418 193.679 1.00 85.31 C ANISOU 4820 C ASP C 73 14200 11506 6707 1751 -1436 -864 C ATOM 4821 O ASP C 73 -80.720 -15.564 192.829 1.00 83.94 O ANISOU 4821 O ASP C 73 14273 10992 6627 1766 -1340 -957 O ATOM 4822 CB ASP C 73 -78.925 -17.741 192.151 1.00 85.68 C ANISOU 4822 CB ASP C 73 13846 11421 7288 1457 -1385 -611 C ATOM 4823 CG ASP C 73 -77.616 -17.142 192.629 1.00 92.65 C ANISOU 4823 CG ASP C 73 14658 12296 8250 1197 -1525 -842 C ATOM 4824 OD1 ASP C 73 -77.384 -17.117 193.856 1.00 95.61 O ANISOU 4824 OD1 ASP C 73 14980 12904 8445 1216 -1742 -914 O ATOM 4825 OD2 ASP C 73 -76.819 -16.694 191.778 1.00 95.60 O ANISOU 4825 OD2 ASP C 73 15030 12452 8841 935 -1414 -962 O ATOM 4826 N LYS C 74 -80.552 -16.212 194.993 1.00 92.93 N ANISOU 4826 N LYS C 74 11576 15781 7954 613 -3009 -2008 N ATOM 4827 CA LYS C 74 -81.012 -14.927 195.506 1.00 95.97 C ANISOU 4827 CA LYS C 74 11946 16143 8374 532 -3020 -2245 C ATOM 4828 C LYS C 74 -80.036 -13.806 195.176 1.00 95.84 C ANISOU 4828 C LYS C 74 11760 16065 8589 305 -3098 -2612 C ATOM 4829 O LYS C 74 -80.458 -12.667 194.946 1.00 93.85 O ANISOU 4829 O LYS C 74 11583 15615 8462 108 -3098 -2779 O ATOM 4830 CB LYS C 74 -81.210 -15.006 197.019 1.00 98.40 C ANISOU 4830 CB LYS C 74 12290 16715 8381 809 -3042 -2269 C ATOM 4831 CG LYS C 74 -82.296 -15.948 197.495 1.00100.99 C ANISOU 4831 CG LYS C 74 12849 17123 8400 966 -2901 -1978 C ATOM 4832 CD LYS C 74 -82.420 -15.855 199.008 1.00109.67 C ANISOU 4832 CD LYS C 74 14059 18476 9135 1183 -2906 -2063 C ATOM 4833 CE LYS C 74 -83.445 -16.826 199.553 1.00113.26 C ANISOU 4833 CE LYS C 74 14817 19034 9182 1288 -2698 -1802 C ATOM 4834 NZ LYS C 74 -83.006 -18.242 199.414 1.00115.89 N ANISOU 4834 NZ LYS C 74 15378 19313 9344 1415 -2703 -1447 N ATOM 4835 N SER C 75 -78.735 -14.104 195.162 1.00 99.67 N ANISOU 4835 N SER C 75 12019 16715 9137 332 -3169 -2785 N ATOM 4836 CA SER C 75 -77.737 -13.093 194.827 1.00105.42 C ANISOU 4836 CA SER C 75 12539 17422 10093 59 -3188 -3209 C ATOM 4837 C SER C 75 -77.980 -12.530 193.432 1.00106.42 C ANISOU 4837 C SER C 75 12856 17186 10393 -376 -3066 -3236 C ATOM 4838 O SER C 75 -78.126 -11.316 193.252 1.00110.36 O ANISOU 4838 O SER C 75 13489 17456 10988 -635 -3052 -3438 O ATOM 4839 CB SER C 75 -76.332 -13.689 194.939 1.00112.09 C ANISOU 4839 CB SER C 75 13030 18540 11020 176 -3271 -3457 C ATOM 4840 OG SER C 75 -76.153 -14.755 194.023 1.00115.04 O ANISOU 4840 OG SER C 75 13398 18885 11427 158 -3217 -3285 O ATOM 4841 N SER C 76 -78.031 -13.404 192.429 1.00105.70 N ANISOU 4841 N SER C 76 12847 17001 10313 -460 -2991 -3034 N ATOM 4842 CA SER C 76 -78.341 -12.983 191.070 1.00104.55 C ANISOU 4842 CA SER C 76 13000 16468 10258 -863 -2886 -3026 C ATOM 4843 C SER C 76 -79.836 -12.826 190.829 1.00 99.16 C ANISOU 4843 C SER C 76 12687 15485 9502 -797 -2942 -2725 C ATOM 4844 O SER C 76 -80.226 -12.434 189.723 1.00 94.61 O ANISOU 4844 O SER C 76 12461 14519 8969 -1073 -2929 -2706 O ATOM 4845 CB SER C 76 -77.759 -13.981 190.065 1.00105.30 C ANISOU 4845 CB SER C 76 13028 16598 10384 -1000 -2772 -2980 C ATOM 4846 OG SER C 76 -78.424 -15.230 190.144 1.00102.56 O ANISOU 4846 OG SER C 76 12727 16340 9901 -666 -2822 -2568 O ATOM 4847 N SER C 77 -80.668 -13.103 191.836 1.00100.25 N ANISOU 4847 N SER C 77 12770 15785 9534 -453 -2997 -2545 N ATOM 4848 CA SER C 77 -82.125 -13.023 191.722 1.00 97.10 C ANISOU 4848 CA SER C 77 12585 15184 9124 -363 -3031 -2361 C ATOM 4849 C SER C 77 -82.614 -13.754 190.474 1.00 87.34 C ANISOU 4849 C SER C 77 11560 13704 7921 -454 -3016 -2120 C ATOM 4850 O SER C 77 -83.341 -13.206 189.643 1.00 80.26 O ANISOU 4850 O SER C 77 10952 12424 7119 -582 -3105 -2129 O ATOM 4851 CB SER C 77 -82.598 -11.568 191.729 1.00100.32 C ANISOU 4851 CB SER C 77 13166 15316 9634 -494 -3130 -2599 C ATOM 4852 OG SER C 77 -82.239 -10.906 190.528 1.00102.26 O ANISOU 4852 OG SER C 77 13729 15159 9967 -854 -3161 -2710 O ATOM 4853 N THR C 78 -82.206 -15.015 190.347 1.00 85.10 N ANISOU 4853 N THR C 78 11160 13617 7558 -354 -2932 -1910 N ATOM 4854 CA THR C 78 -82.446 -15.781 189.130 1.00 77.12 C ANISOU 4854 CA THR C 78 10328 12398 6577 -458 -2898 -1694 C ATOM 4855 C THR C 78 -82.998 -17.153 189.479 1.00 76.92 C ANISOU 4855 C THR C 78 10225 12542 6459 -188 -2819 -1357 C ATOM 4856 O THR C 78 -82.429 -17.861 190.315 1.00 79.12 O ANISOU 4856 O THR C 78 10331 13141 6589 17 -2784 -1295 O ATOM 4857 CB THR C 78 -81.157 -15.934 188.312 1.00 69.58 C ANISOU 4857 CB THR C 78 9355 11385 5697 -733 -2774 -1784 C ATOM 4858 OG1 THR C 78 -80.490 -14.669 188.222 1.00 73.62 O ANISOU 4858 OG1 THR C 78 9910 11800 6262 -1034 -2776 -2159 O ATOM 4859 CG2 THR C 78 -81.468 -16.440 186.913 1.00 62.78 C ANISOU 4859 CG2 THR C 78 8814 10095 4945 -922 -2662 -1529 C ATOM 4860 N ALA C 79 -84.095 -17.529 188.833 1.00 73.95 N ANISOU 4860 N ALA C 79 10024 11867 6205 -193 -2785 -1142 N ATOM 4861 CA ALA C 79 -84.600 -18.887 188.938 1.00 73.32 C ANISOU 4861 CA ALA C 79 9922 11856 6082 -36 -2648 -824 C ATOM 4862 C ALA C 79 -83.936 -19.776 187.893 1.00 74.69 C ANISOU 4862 C ALA C 79 10185 11863 6332 -142 -2570 -623 C ATOM 4863 O ALA C 79 -83.410 -19.306 186.883 1.00 79.99 O ANISOU 4863 O ALA C 79 10992 12283 7117 -384 -2586 -715 O ATOM 4864 CB ALA C 79 -86.118 -18.917 188.766 1.00 70.10 C ANISOU 4864 CB ALA C 79 9570 11236 5829 -5 -2634 -780 C ATOM 4865 N TYR C 80 -83.966 -21.080 188.151 1.00 71.94 N ANISOU 4865 N TYR C 80 9810 11631 5893 24 -2459 -356 N ATOM 4866 CA TYR C 80 -83.387 -22.063 187.252 1.00 72.23 C ANISOU 4866 CA TYR C 80 9910 11529 6005 -24 -2385 -175 C ATOM 4867 C TYR C 80 -84.259 -23.305 187.251 1.00 72.60 C ANISOU 4867 C TYR C 80 10060 11473 6050 88 -2258 150 C ATOM 4868 O TYR C 80 -84.762 -23.720 188.301 1.00 72.25 O ANISOU 4868 O TYR C 80 10014 11610 5828 255 -2181 251 O ATOM 4869 CB TYR C 80 -81.959 -22.450 187.667 1.00 74.10 C ANISOU 4869 CB TYR C 80 9963 12066 6125 111 -2430 -281 C ATOM 4870 CG TYR C 80 -80.976 -21.304 187.727 1.00 79.80 C ANISOU 4870 CG TYR C 80 10507 12930 6885 -40 -2509 -680 C ATOM 4871 CD1 TYR C 80 -80.826 -20.553 188.885 1.00 82.30 C ANISOU 4871 CD1 TYR C 80 10675 13546 7051 89 -2640 -904 C ATOM 4872 CD2 TYR C 80 -80.184 -20.986 186.632 1.00 81.55 C ANISOU 4872 CD2 TYR C 80 10725 12979 7282 -350 -2413 -864 C ATOM 4873 CE1 TYR C 80 -79.924 -19.508 188.947 1.00 82.91 C ANISOU 4873 CE1 TYR C 80 10569 13741 7193 -81 -2700 -1311 C ATOM 4874 CE2 TYR C 80 -79.278 -19.945 186.686 1.00 83.86 C ANISOU 4874 CE2 TYR C 80 10858 13378 7627 -567 -2412 -1273 C ATOM 4875 CZ TYR C 80 -79.153 -19.209 187.844 1.00 85.65 C ANISOU 4875 CZ TYR C 80 10901 13898 7743 -429 -2568 -1500 C ATOM 4876 OH TYR C 80 -78.251 -18.170 187.899 1.00 91.19 O ANISOU 4876 OH TYR C 80 11426 14694 8529 -677 -2554 -1948 O ATOM 4877 N ILE C 81 -84.416 -23.904 186.075 1.00 69.04 N ANISOU 4877 N ILE C 81 9739 10716 5776 -36 -2205 296 N ATOM 4878 CA ILE C 81 -85.034 -25.216 185.936 1.00 64.71 C ANISOU 4878 CA ILE C 81 9287 10041 5259 35 -2069 585 C ATOM 4879 C ILE C 81 -84.018 -26.138 185.278 1.00 66.06 C ANISOU 4879 C ILE C 81 9500 10158 5442 68 -2047 697 C ATOM 4880 O ILE C 81 -83.367 -25.758 184.300 1.00 67.83 O ANISOU 4880 O ILE C 81 9737 10258 5779 -103 -2075 561 O ATOM 4881 CB ILE C 81 -86.346 -25.154 185.128 1.00 61.29 C ANISOU 4881 CB ILE C 81 8938 9275 5074 -110 -2060 597 C ATOM 4882 CG1 ILE C 81 -87.017 -26.529 185.085 1.00 57.82 C ANISOU 4882 CG1 ILE C 81 8561 8718 4692 -80 -1874 848 C ATOM 4883 CG2 ILE C 81 -86.108 -24.626 183.720 1.00 61.45 C ANISOU 4883 CG2 ILE C 81 9126 8975 5246 -296 -2196 505 C ATOM 4884 CD1 ILE C 81 -88.412 -26.510 184.498 1.00 53.34 C ANISOU 4884 CD1 ILE C 81 7970 7886 4410 -194 -1877 764 C ATOM 4885 N GLN C 82 -83.871 -27.343 185.816 1.00 64.90 N ANISOU 4885 N GLN C 82 9415 10081 5163 278 -1981 920 N ATOM 4886 CA GLN C 82 -82.951 -28.322 185.255 1.00 69.60 C ANISOU 4886 CA GLN C 82 10036 10617 5792 378 -1992 997 C ATOM 4887 C GLN C 82 -83.729 -29.568 184.867 1.00 76.50 C ANISOU 4887 C GLN C 82 11126 11206 6735 378 -1851 1301 C ATOM 4888 O GLN C 82 -84.439 -30.145 185.697 1.00 77.55 O ANISOU 4888 O GLN C 82 11411 11333 6723 465 -1740 1501 O ATOM 4889 CB GLN C 82 -81.835 -28.662 186.244 1.00 73.45 C ANISOU 4889 CB GLN C 82 10439 11414 6056 714 -2146 927 C ATOM 4890 CG GLN C 82 -80.805 -29.635 185.695 1.00 77.82 C ANISOU 4890 CG GLN C 82 10951 11925 6691 881 -2214 904 C ATOM 4891 CD GLN C 82 -79.580 -29.747 186.579 1.00 90.62 C ANISOU 4891 CD GLN C 82 12402 13872 8156 1257 -2479 682 C ATOM 4892 OE1 GLN C 82 -79.644 -30.290 187.682 1.00 95.65 O ANISOU 4892 OE1 GLN C 82 13256 14592 8494 1594 -2621 848 O ATOM 4893 NE2 GLN C 82 -78.455 -29.230 186.099 1.00 95.55 N ANISOU 4893 NE2 GLN C 82 12662 14669 8972 1194 -2546 265 N ATOM 4894 N LEU C 83 -83.604 -29.963 183.605 1.00 75.37 N ANISOU 4894 N LEU C 83 11026 10811 6799 242 -1819 1313 N ATOM 4895 CA LEU C 83 -84.268 -31.139 183.061 1.00 72.75 C ANISOU 4895 CA LEU C 83 10881 10180 6581 215 -1700 1552 C ATOM 4896 C LEU C 83 -83.224 -32.224 182.834 1.00 81.58 C ANISOU 4896 C LEU C 83 12047 11275 7674 422 -1732 1619 C ATOM 4897 O LEU C 83 -82.239 -32.003 182.118 1.00 89.60 O ANISOU 4897 O LEU C 83 12925 12340 8779 392 -1785 1407 O ATOM 4898 CB LEU C 83 -84.996 -30.800 181.762 1.00 64.96 C ANISOU 4898 CB LEU C 83 9947 8895 5839 -57 -1693 1485 C ATOM 4899 CG LEU C 83 -85.890 -29.559 181.822 1.00 66.41 C ANISOU 4899 CG LEU C 83 10075 9072 6087 -203 -1772 1318 C ATOM 4900 CD1 LEU C 83 -86.320 -29.139 180.426 1.00 64.42 C ANISOU 4900 CD1 LEU C 83 9977 8488 6011 -398 -1886 1211 C ATOM 4901 CD2 LEU C 83 -87.101 -29.809 182.709 1.00 70.21 C ANISOU 4901 CD2 LEU C 83 10502 9584 6591 -179 -1658 1388 C ATOM 4902 N ASN C 84 -83.439 -33.385 183.443 1.00 83.75 N ANISOU 4902 N ASN C 84 12539 11453 7827 619 -1683 1879 N ATOM 4903 CA ASN C 84 -82.518 -34.506 183.361 1.00 87.04 C ANISOU 4903 CA ASN C 84 13058 11804 8208 904 -1777 1944 C ATOM 4904 C ASN C 84 -83.142 -35.626 182.539 1.00 85.09 C ANISOU 4904 C ASN C 84 13034 11165 8131 797 -1629 2151 C ATOM 4905 O ASN C 84 -84.366 -35.734 182.429 1.00 84.89 O ANISOU 4905 O ASN C 84 13123 10944 8188 558 -1447 2290 O ATOM 4906 CB ASN C 84 -82.155 -35.019 184.758 1.00 92.47 C ANISOU 4906 CB ASN C 84 13966 12616 8552 1281 -1909 2086 C ATOM 4907 CG ASN C 84 -82.340 -33.963 185.830 1.00 93.28 C ANISOU 4907 CG ASN C 84 13988 13023 8430 1280 -1945 2000 C ATOM 4908 OD1 ASN C 84 -81.486 -33.097 186.020 1.00 93.93 O ANISOU 4908 OD1 ASN C 84 13776 13412 8501 1372 -2134 1704 O ATOM 4909 ND2 ASN C 84 -83.464 -34.026 186.534 1.00 92.59 N ANISOU 4909 ND2 ASN C 84 14146 12854 8178 1146 -1730 2214 N ATOM 4910 N SER C 85 -82.278 -36.470 181.972 1.00 81.05 N ANISOU 4910 N SER C 85 12543 10551 7701 985 -1716 2112 N ATOM 4911 CA SER C 85 -82.697 -37.652 181.219 1.00 77.13 C ANISOU 4911 CA SER C 85 12277 9673 7357 937 -1608 2288 C ATOM 4912 C SER C 85 -83.655 -37.257 180.093 1.00 74.40 C ANISOU 4912 C SER C 85 11874 9140 7254 532 -1456 2242 C ATOM 4913 O SER C 85 -84.815 -37.671 180.042 1.00 79.03 O ANISOU 4913 O SER C 85 12614 9486 7926 354 -1311 2405 O ATOM 4914 CB SER C 85 -83.326 -38.696 182.150 1.00 76.18 C ANISOU 4914 CB SER C 85 12579 9322 7044 1064 -1522 2637 C ATOM 4915 OG SER C 85 -83.430 -39.956 181.513 1.00 76.02 O ANISOU 4915 OG SER C 85 12804 8923 7156 1094 -1463 2778 O ATOM 4916 N LEU C 86 -83.138 -36.435 179.183 1.00 66.77 N ANISOU 4916 N LEU C 86 10708 8271 6390 384 -1499 1977 N ATOM 4917 CA LEU C 86 -83.957 -35.824 178.144 1.00 61.44 C ANISOU 4917 CA LEU C 86 10064 7418 5863 51 -1455 1898 C ATOM 4918 C LEU C 86 -84.294 -36.827 177.047 1.00 63.81 C ANISOU 4918 C LEU C 86 10541 7366 6336 -29 -1399 1957 C ATOM 4919 O LEU C 86 -83.414 -37.532 176.541 1.00 64.62 O ANISOU 4919 O LEU C 86 10662 7420 6469 86 -1383 1897 O ATOM 4920 CB LEU C 86 -83.239 -34.612 177.553 1.00 55.72 C ANISOU 4920 CB LEU C 86 9221 6846 5102 -110 -1493 1615 C ATOM 4921 CG LEU C 86 -83.138 -33.406 178.489 1.00 57.01 C ANISOU 4921 CG LEU C 86 9220 7307 5132 -108 -1559 1516 C ATOM 4922 CD1 LEU C 86 -82.259 -32.318 177.892 1.00 62.48 C ANISOU 4922 CD1 LEU C 86 9841 8109 5789 -308 -1540 1215 C ATOM 4923 CD2 LEU C 86 -84.522 -32.868 178.805 1.00 53.09 C ANISOU 4923 CD2 LEU C 86 8784 6722 4668 -220 -1597 1603 C ATOM 4924 N THR C 87 -85.570 -36.886 176.684 1.00 65.98 N ANISOU 4924 N THR C 87 10911 7406 6752 -212 -1384 2015 N ATOM 4925 CA THR C 87 -86.068 -37.668 175.561 1.00 68.41 C ANISOU 4925 CA THR C 87 11380 7370 7245 -324 -1373 2014 C ATOM 4926 C THR C 87 -86.758 -36.737 174.568 1.00 69.76 C ANISOU 4926 C THR C 87 11617 7405 7483 -540 -1523 1826 C ATOM 4927 O THR C 87 -86.826 -35.522 174.767 1.00 71.26 O ANISOU 4927 O THR C 87 11753 7742 7580 -597 -1625 1715 O ATOM 4928 CB THR C 87 -87.023 -38.768 176.035 1.00 71.91 C ANISOU 4928 CB THR C 87 11896 7599 7827 -329 -1249 2200 C ATOM 4929 OG1 THR C 87 -88.097 -38.184 176.783 1.00 68.52 O ANISOU 4929 OG1 THR C 87 11338 7252 7445 -448 -1208 2181 O ATOM 4930 CG2 THR C 87 -86.287 -39.774 176.909 1.00 72.51 C ANISOU 4930 CG2 THR C 87 12090 7696 7765 -81 -1151 2415 C ATOM 4931 N SER C 88 -87.272 -37.324 173.483 1.00 73.66 N ANISOU 4931 N SER C 88 12280 7584 8123 -632 -1578 1778 N ATOM 4932 CA SER C 88 -87.948 -36.528 172.461 1.00 75.87 C ANISOU 4932 CA SER C 88 12732 7668 8428 -774 -1812 1587 C ATOM 4933 C SER C 88 -89.140 -35.778 173.044 1.00 75.17 C ANISOU 4933 C SER C 88 12471 7620 8471 -788 -1972 1490 C ATOM 4934 O SER C 88 -89.391 -34.621 172.685 1.00 65.98 O ANISOU 4934 O SER C 88 11421 6420 7228 -819 -2213 1328 O ATOM 4935 CB SER C 88 -88.393 -37.425 171.306 1.00 78.23 C ANISOU 4935 CB SER C 88 13233 7620 8869 -828 -1882 1532 C ATOM 4936 OG SER C 88 -87.277 -37.988 170.639 1.00 86.22 O ANISOU 4936 OG SER C 88 14415 8593 9753 -824 -1738 1549 O ATOM 4937 N GLU C 89 -89.886 -36.421 173.945 1.00 82.38 N ANISOU 4937 N GLU C 89 13139 8581 9579 -775 -1823 1558 N ATOM 4938 CA GLU C 89 -91.064 -35.799 174.540 1.00 84.14 C ANISOU 4938 CA GLU C 89 13114 8870 9984 -811 -1908 1382 C ATOM 4939 C GLU C 89 -90.718 -34.547 175.339 1.00 77.07 C ANISOU 4939 C GLU C 89 12124 8266 8894 -751 -1953 1355 C ATOM 4940 O GLU C 89 -91.613 -33.751 175.645 1.00 78.92 O ANISOU 4940 O GLU C 89 12176 8546 9263 -751 -2104 1133 O ATOM 4941 CB GLU C 89 -91.784 -36.816 175.430 1.00 94.31 C ANISOU 4941 CB GLU C 89 14200 10161 11472 -893 -1593 1456 C ATOM 4942 CG GLU C 89 -93.205 -36.438 175.811 1.00112.30 C ANISOU 4942 CG GLU C 89 16148 12456 14063 -999 -1617 1146 C ATOM 4943 CD GLU C 89 -93.826 -37.427 176.779 1.00129.99 C ANISOU 4943 CD GLU C 89 18245 14701 16446 -1178 -1169 1212 C ATOM 4944 OE1 GLU C 89 -93.255 -38.524 176.956 1.00136.64 O ANISOU 4944 OE1 GLU C 89 19331 15428 17159 -1198 -916 1518 O ATOM 4945 OE2 GLU C 89 -94.883 -37.108 177.364 1.00137.35 O ANISOU 4945 OE2 GLU C 89 18849 15726 17611 -1309 -1054 931 O ATOM 4946 N ASP C 90 -89.443 -34.350 175.675 1.00 69.31 N ANISOU 4946 N ASP C 90 11224 7482 7629 -688 -1846 1515 N ATOM 4947 CA ASP C 90 -89.019 -33.203 176.467 1.00 65.45 C ANISOU 4947 CA ASP C 90 10636 7276 6957 -642 -1878 1470 C ATOM 4948 C ASP C 90 -88.741 -31.957 175.638 1.00 65.13 C ANISOU 4948 C ASP C 90 10807 7139 6798 -703 -2131 1295 C ATOM 4949 O ASP C 90 -88.684 -30.859 176.205 1.00 70.42 O ANISOU 4949 O ASP C 90 11411 7973 7374 -688 -2212 1196 O ATOM 4950 CB ASP C 90 -87.765 -33.557 177.269 1.00 67.09 C ANISOU 4950 CB ASP C 90 10800 7750 6942 -530 -1681 1649 C ATOM 4951 CG ASP C 90 -87.992 -34.709 178.220 1.00 72.52 C ANISOU 4951 CG ASP C 90 11437 8479 7640 -443 -1458 1860 C ATOM 4952 OD1 ASP C 90 -89.020 -34.701 178.929 1.00 76.03 O ANISOU 4952 OD1 ASP C 90 11768 8946 8174 -505 -1358 1843 O ATOM 4953 OD2 ASP C 90 -87.150 -35.629 178.248 1.00 76.72 O ANISOU 4953 OD2 ASP C 90 12073 8993 8084 -319 -1373 2015 O ATOM 4954 N SER C 91 -88.569 -32.088 174.325 1.00 61.26 N ANISOU 4954 N SER C 91 10639 6359 6278 -785 -2246 1252 N ATOM 4955 CA SER C 91 -88.317 -30.917 173.495 1.00 56.64 C ANISOU 4955 CA SER C 91 10424 5597 5500 -885 -2457 1108 C ATOM 4956 C SER C 91 -89.586 -30.081 173.408 1.00 50.69 C ANISOU 4956 C SER C 91 9718 4665 4878 -804 -2841 908 C ATOM 4957 O SER C 91 -90.614 -30.551 172.910 1.00 56.44 O ANISOU 4957 O SER C 91 10437 5175 5834 -736 -3051 799 O ATOM 4958 CB SER C 91 -87.852 -31.346 172.105 1.00 54.10 C ANISOU 4958 CB SER C 91 10524 4978 5051 -1010 -2449 1109 C ATOM 4959 OG SER C 91 -88.449 -32.574 171.725 1.00 54.92 O ANISOU 4959 OG SER C 91 10560 4936 5372 -948 -2454 1160 O ATOM 4960 N ALA C 92 -89.511 -28.844 173.884 1.00 41.58 N ANISOU 4960 N ALA C 92 6032 3842 5925 1099 -226 1360 N ATOM 4961 CA ALA C 92 -90.666 -27.948 173.927 1.00 40.50 C ANISOU 4961 CA ALA C 92 5792 3769 5827 910 -232 1232 C ATOM 4962 C ALA C 92 -90.164 -26.551 174.274 1.00 44.88 C ANISOU 4962 C ALA C 92 6177 4514 6362 973 -533 1146 C ATOM 4963 O ALA C 92 -88.954 -26.319 174.376 1.00 44.91 O ANISOU 4963 O ALA C 92 6118 4609 6337 1120 -726 1163 O ATOM 4964 CB ALA C 92 -91.708 -28.442 174.932 1.00 42.03 C ANISOU 4964 CB ALA C 92 6206 3883 5882 908 4 1269 C ATOM 4965 N VAL C 93 -91.089 -25.619 174.493 1.00 39.06 N ANISOU 4965 N VAL C 93 5365 3840 5636 862 -558 1042 N ATOM 4966 CA VAL C 93 -90.751 -24.296 175.003 1.00 49.44 C ANISOU 4966 CA VAL C 93 6572 5303 6911 914 -788 953 C ATOM 4967 C VAL C 93 -91.044 -24.278 176.495 1.00 56.28 C ANISOU 4967 C VAL C 93 7612 6211 7561 1048 -756 983 C ATOM 4968 O VAL C 93 -92.030 -24.865 176.955 1.00 63.66 O ANISOU 4968 O VAL C 93 8696 7059 8431 1014 -535 1022 O ATOM 4969 CB VAL C 93 -91.531 -23.192 174.263 1.00 49.26 C ANISOU 4969 CB VAL C 93 6372 5311 7033 738 -834 823 C ATOM 4970 CG1 VAL C 93 -91.168 -21.818 174.809 1.00 37.14 C ANISOU 4970 CG1 VAL C 93 4763 3889 5458 783 -1031 724 C ATOM 4971 CG2 VAL C 93 -91.258 -23.263 172.769 1.00 52.32 C ANISOU 4971 CG2 VAL C 93 6619 5658 7603 615 -856 804 C ATOM 4972 N TYR C 94 -90.174 -23.631 177.262 1.00 49.74 N ANISOU 4972 N TYR C 94 6766 5523 6611 1190 -962 953 N ATOM 4973 CA TYR C 94 -90.307 -23.573 178.711 1.00 51.10 C ANISOU 4973 CA TYR C 94 7108 5763 6545 1335 -961 977 C ATOM 4974 C TYR C 94 -90.369 -22.115 179.140 1.00 63.33 C ANISOU 4974 C TYR C 94 8542 7441 8080 1283 -1125 817 C ATOM 4975 O TYR C 94 -89.478 -21.326 178.804 1.00 69.92 O ANISOU 4975 O TYR C 94 9211 8380 8978 1268 -1328 719 O ATOM 4976 CB TYR C 94 -89.151 -24.306 179.391 1.00 52.03 C ANISOU 4976 CB TYR C 94 7342 5956 6470 1593 -1050 1092 C ATOM 4977 CG TYR C 94 -89.143 -25.791 179.096 1.00 57.20 C ANISOU 4977 CG TYR C 94 8173 6444 7118 1674 -840 1267 C ATOM 4978 CD1 TYR C 94 -89.865 -26.679 179.883 1.00 57.13 C ANISOU 4978 CD1 TYR C 94 8454 6306 6946 1748 -592 1389 C ATOM 4979 CD2 TYR C 94 -88.430 -26.302 178.020 1.00 64.66 C ANISOU 4979 CD2 TYR C 94 9012 7338 8218 1665 -860 1303 C ATOM 4980 CE1 TYR C 94 -89.866 -28.036 179.614 1.00 61.45 C ANISOU 4980 CE1 TYR C 94 9198 6664 7488 1811 -357 1543 C ATOM 4981 CE2 TYR C 94 -88.427 -27.657 177.742 1.00 69.37 C ANISOU 4981 CE2 TYR C 94 9790 7756 8811 1734 -640 1455 C ATOM 4982 CZ TYR C 94 -89.147 -28.519 178.542 1.00 65.72 C ANISOU 4982 CZ TYR C 94 9631 7154 8188 1805 -383 1575 C ATOM 4983 OH TYR C 94 -89.148 -29.868 178.270 1.00 60.67 O ANISOU 4983 OH TYR C 94 9205 6302 7545 1863 -124 1720 O ATOM 4984 N TYR C 95 -91.428 -21.760 179.864 1.00 65.60 N ANISOU 4984 N TYR C 95 8923 7709 8292 1242 -1010 779 N ATOM 4985 CA TYR C 95 -91.643 -20.410 180.360 1.00 62.71 C ANISOU 4985 CA TYR C 95 8490 7433 7904 1196 -1114 628 C ATOM 4986 C TYR C 95 -91.489 -20.377 181.871 1.00 66.66 C ANISOU 4986 C TYR C 95 9167 8035 8125 1345 -1142 632 C ATOM 4987 O TYR C 95 -91.942 -21.288 182.574 1.00 70.88 O ANISOU 4987 O TYR C 95 9914 8514 8504 1435 -977 749 O ATOM 4988 CB TYR C 95 -93.041 -19.894 180.005 1.00 64.91 C ANISOU 4988 CB TYR C 95 8720 7626 8316 1044 -961 562 C ATOM 4989 CG TYR C 95 -93.339 -19.778 178.531 1.00 75.45 C ANISOU 4989 CG TYR C 95 9877 8893 9898 905 -945 542 C ATOM 4990 CD1 TYR C 95 -93.809 -20.868 177.813 1.00 81.39 C ANISOU 4990 CD1 TYR C 95 10636 9554 10734 841 -786 628 C ATOM 4991 CD2 TYR C 95 -93.182 -18.571 177.864 1.00 77.54 C ANISOU 4991 CD2 TYR C 95 9986 9178 10298 834 -1071 433 C ATOM 4992 CE1 TYR C 95 -94.094 -20.766 176.471 1.00 77.78 C ANISOU 4992 CE1 TYR C 95 10017 9062 10475 716 -782 600 C ATOM 4993 CE2 TYR C 95 -93.467 -18.459 176.518 1.00 76.44 C ANISOU 4993 CE2 TYR C 95 9707 8983 10352 731 -1058 428 C ATOM 4994 CZ TYR C 95 -93.924 -19.560 175.826 1.00 74.72 C ANISOU 4994 CZ TYR C 95 9481 8710 10201 674 -927 508 C ATOM 4995 OH TYR C 95 -94.210 -19.460 174.484 1.00 76.16 O ANISOU 4995 OH TYR C 95 9523 8864 10549 573 -926 493 O ATOM 4996 N CYS C 96 -90.842 -19.331 182.367 1.00 65.83 N ANISOU 4996 N CYS C 96 8989 8077 7948 1361 -1335 494 N ATOM 4997 CA CYS C 96 -90.961 -18.964 183.766 1.00 66.71 C ANISOU 4997 CA CYS C 96 9247 8293 7807 1450 -1353 442 C ATOM 4998 C CYS C 96 -92.015 -17.873 183.895 1.00 69.30 C ANISOU 4998 C CYS C 96 9552 8561 8217 1306 -1259 308 C ATOM 4999 O CYS C 96 -92.274 -17.119 182.953 1.00 67.18 O ANISOU 4999 O CYS C 96 9123 8225 8179 1168 -1265 226 O ATOM 5000 CB CYS C 96 -89.627 -18.490 184.346 1.00 69.04 C ANISOU 5000 CB CYS C 96 9476 8815 7942 1548 -1615 341 C ATOM 5001 SG CYS C 96 -88.908 -17.026 183.572 1.00 71.23 S ANISOU 5001 SG CYS C 96 9480 9157 8426 1363 -1795 105 S ATOM 5002 N ALA C 97 -92.628 -17.801 185.071 1.00 75.94 N ANISOU 5002 N ALA C 97 10571 9423 8859 1357 -1159 295 N ATOM 5003 CA ALA C 97 -93.700 -16.846 185.299 1.00 74.34 C ANISOU 5003 CA ALA C 97 10365 9160 8721 1248 -1039 175 C ATOM 5004 C ALA C 97 -93.748 -16.499 186.778 1.00 79.55 C ANISOU 5004 C ALA C 97 11205 9919 9101 1324 -1035 107 C ATOM 5005 O ALA C 97 -93.280 -17.256 187.630 1.00 83.96 O ANISOU 5005 O ALA C 97 11933 10566 9402 1473 -1064 198 O ATOM 5006 CB ALA C 97 -95.049 -17.393 184.822 1.00 69.79 C ANISOU 5006 CB ALA C 97 9800 8430 8287 1173 -785 250 C ATOM 5007 N ARG C 98 -94.306 -15.334 187.072 1.00 81.21 N ANISOU 5007 N ARG C 98 11392 10115 9351 1236 -995 -52 N ATOM 5008 CA ARG C 98 -94.328 -14.810 188.428 1.00 86.08 C ANISOU 5008 CA ARG C 98 12166 10829 9712 1279 -996 -158 C ATOM 5009 C ARG C 98 -95.715 -14.986 189.030 1.00 89.06 C ANISOU 5009 C ARG C 98 12693 11099 10046 1268 -722 -130 C ATOM 5010 O ARG C 98 -96.725 -14.727 188.372 1.00 91.29 O ANISOU 5010 O ARG C 98 12876 11255 10556 1177 -568 -146 O ATOM 5011 CB ARG C 98 -93.937 -13.333 188.450 1.00 80.83 C ANISOU 5011 CB ARG C 98 11397 10211 9105 1177 -1112 -383 C ATOM 5012 CG ARG C 98 -93.700 -12.809 189.845 1.00 78.80 C ANISOU 5012 CG ARG C 98 11291 10093 8556 1210 -1152 -520 C ATOM 5013 CD ARG C 98 -93.510 -11.308 189.875 1.00 79.35 C ANISOU 5013 CD ARG C 98 11285 10161 8702 1075 -1194 -765 C ATOM 5014 NE ARG C 98 -94.775 -10.602 189.708 1.00 82.68 N ANISOU 5014 NE ARG C 98 11728 10394 9293 1007 -970 -809 N ATOM 5015 CZ ARG C 98 -94.910 -9.284 189.798 1.00 92.04 C ANISOU 5015 CZ ARG C 98 12906 11515 10550 909 -925 -1004 C ATOM 5016 NH1 ARG C 98 -93.854 -8.524 190.055 1.00 95.92 N ANISOU 5016 NH1 ARG C 98 13369 12112 10962 827 -1077 -1194 N ATOM 5017 NH2 ARG C 98 -96.101 -8.725 189.632 1.00 96.04 N ANISOU 5017 NH2 ARG C 98 13429 11854 11207 894 -715 -1021 N ATOM 5018 N ARG C 99 -95.755 -15.419 190.286 1.00 87.90 N ANISOU 5018 N ARG C 99 12782 11020 9596 1368 -662 -95 N ATOM 5019 CA ARG C 99 -97.023 -15.601 190.979 1.00 87.34 C ANISOU 5019 CA ARG C 99 12876 10852 9458 1349 -380 -82 C ATOM 5020 C ARG C 99 -97.728 -14.264 191.165 1.00 91.95 C ANISOU 5020 C ARG C 99 13391 11403 10144 1247 -309 -278 C ATOM 5021 O ARG C 99 -97.191 -13.350 191.798 1.00 96.62 O ANISOU 5021 O ARG C 99 14015 12092 10604 1245 -433 -427 O ATOM 5022 CB ARG C 99 -96.788 -16.275 192.330 1.00 88.26 C ANISOU 5022 CB ARG C 99 13295 11050 9191 1492 -339 -4 C ATOM 5023 CG ARG C 99 -97.932 -16.123 193.317 1.00 88.23 C ANISOU 5023 CG ARG C 99 13485 10978 9060 1461 -67 -53 C ATOM 5024 CD ARG C 99 -97.451 -16.373 194.736 1.00 92.66 C ANISOU 5024 CD ARG C 99 14342 11667 9196 1608 -102 -28 C ATOM 5025 NE ARG C 99 -98.476 -16.077 195.732 1.00 94.58 N ANISOU 5025 NE ARG C 99 14778 11853 9304 1566 154 -103 N ATOM 5026 CZ ARG C 99 -98.273 -16.121 197.045 1.00 99.53 C ANISOU 5026 CZ ARG C 99 15683 12584 9551 1673 164 -111 C ATOM 5027 NH1 ARG C 99 -99.262 -15.841 197.882 1.00101.14 N ANISOU 5027 NH1 ARG C 99 16056 12717 9655 1617 424 -187 N ATOM 5028 NH2 ARG C 99 -97.079 -16.447 197.521 1.00102.45 N ANISOU 5028 NH2 ARG C 99 16155 13144 9627 1846 -88 -49 N ATOM 5029 N TYR C 100 -98.927 -14.149 190.600 1.00 90.83 N ANISOU 5029 N TYR C 100 13146 11132 10233 1167 -103 -288 N ATOM 5030 CA TYR C 100 -99.772 -12.980 190.821 1.00 86.10 C ANISOU 5030 CA TYR C 100 12500 10485 9727 1109 14 -452 C ATOM 5031 C TYR C 100 -100.331 -13.038 192.238 1.00 83.33 C ANISOU 5031 C TYR C 100 12394 10150 9118 1138 198 -495 C ATOM 5032 O TYR C 100 -101.170 -13.890 192.546 1.00 81.49 O ANISOU 5032 O TYR C 100 12262 9862 8841 1136 432 -412 O ATOM 5033 CB TYR C 100 -100.887 -12.940 189.780 1.00 84.84 C ANISOU 5033 CB TYR C 100 12136 10226 9874 1052 165 -443 C ATOM 5034 CG TYR C 100 -101.724 -11.680 189.794 1.00 89.19 C ANISOU 5034 CG TYR C 100 12602 10726 10559 1035 267 -598 C ATOM 5035 CD1 TYR C 100 -101.129 -10.425 189.818 1.00 91.84 C ANISOU 5035 CD1 TYR C 100 12928 11054 10912 1035 134 -728 C ATOM 5036 CD2 TYR C 100 -103.110 -11.745 189.754 1.00 88.82 C ANISOU 5036 CD2 TYR C 100 12479 10638 10630 1022 514 -625 C ATOM 5037 CE1 TYR C 100 -101.892 -9.272 189.822 1.00 93.76 C ANISOU 5037 CE1 TYR C 100 13125 11221 11278 1044 254 -858 C ATOM 5038 CE2 TYR C 100 -103.882 -10.599 189.758 1.00 89.98 C ANISOU 5038 CE2 TYR C 100 12544 10743 10900 1046 611 -758 C ATOM 5039 CZ TYR C 100 -103.268 -9.365 189.791 1.00 94.70 C ANISOU 5039 CZ TYR C 100 13169 11306 11506 1069 485 -863 C ATOM 5040 OH TYR C 100 -104.033 -8.222 189.795 1.00 99.02 O ANISOU 5040 OH TYR C 100 13666 11783 12175 1116 607 -984 O ATOM 5041 N LEU C 101 -99.853 -12.143 193.107 1.00 83.61 N ANISOU 5041 N LEU C 101 12535 10260 8972 1148 111 -638 N ATOM 5042 CA LEU C 101 -100.244 -12.197 194.514 1.00 82.82 C ANISOU 5042 CA LEU C 101 12695 10194 8580 1180 266 -683 C ATOM 5043 C LEU C 101 -101.738 -11.959 194.690 1.00 84.81 C ANISOU 5043 C LEU C 101 12944 10324 8957 1128 584 -740 C ATOM 5044 O LEU C 101 -102.400 -12.669 195.457 1.00 89.51 O ANISOU 5044 O LEU C 101 13725 10892 9392 1142 811 -684 O ATOM 5045 CB LEU C 101 -99.443 -11.177 195.323 1.00 76.18 C ANISOU 5045 CB LEU C 101 11938 9471 7536 1175 104 -864 C ATOM 5046 CG LEU C 101 -97.930 -11.386 195.406 1.00 71.91 C ANISOU 5046 CG LEU C 101 11397 9115 6809 1231 -214 -853 C ATOM 5047 CD1 LEU C 101 -97.327 -10.511 196.494 1.00 67.86 C ANISOU 5047 CD1 LEU C 101 11004 8756 6023 1211 -321 -1061 C ATOM 5048 CD2 LEU C 101 -97.594 -12.847 195.646 1.00 73.01 C ANISOU 5048 CD2 LEU C 101 11678 9317 6745 1369 -239 -626 C ATOM 5049 N THR C 102 -102.285 -10.957 193.997 1.00 81.97 N ANISOU 5049 N THR C 102 12379 9890 8875 1080 619 -855 N ATOM 5050 CA THR C 102 -103.711 -10.665 194.106 1.00 82.87 C ANISOU 5050 CA THR C 102 12443 9919 9126 1056 909 -925 C ATOM 5051 C THR C 102 -104.559 -11.865 193.698 1.00 88.57 C ANISOU 5051 C THR C 102 13099 10609 9946 1030 1099 -799 C ATOM 5052 O THR C 102 -105.540 -12.200 194.372 1.00 89.81 O ANISOU 5052 O THR C 102 13348 10735 10039 1003 1380 -827 O ATOM 5053 CB THR C 102 -104.063 -9.447 193.253 1.00 85.83 C ANISOU 5053 CB THR C 102 12595 10227 9790 1057 884 -1036 C ATOM 5054 OG1 THR C 102 -103.093 -8.414 193.469 1.00 88.17 O ANISOU 5054 OG1 THR C 102 12956 10532 10013 1049 704 -1153 O ATOM 5055 CG2 THR C 102 -105.443 -8.922 193.618 1.00 88.59 C ANISOU 5055 CG2 THR C 102 12911 10517 10232 1071 1172 -1146 C ATOM 5056 N GLY C 103 -104.197 -12.524 192.600 1.00 96.80 N ANISOU 5056 N GLY C 103 13984 11654 11141 1019 972 -677 N ATOM 5057 CA GLY C 103 -104.998 -13.610 192.072 1.00 98.52 C ANISOU 5057 CA GLY C 103 14111 11840 11480 962 1158 -590 C ATOM 5058 C GLY C 103 -104.439 -14.981 192.392 1.00 99.28 C ANISOU 5058 C GLY C 103 14420 11926 11378 966 1179 -424 C ATOM 5059 O GLY C 103 -103.380 -15.360 191.884 1.00 99.59 O ANISOU 5059 O GLY C 103 14453 11989 11397 1007 951 -316 O ATOM 5060 N THR C 104 -105.148 -15.734 193.230 1.00 98.14 N ANISOU 5060 N THR C 104 14476 11731 11083 930 1473 -401 N ATOM 5061 CA THR C 104 -104.687 -17.057 193.631 1.00 97.71 C ANISOU 5061 CA THR C 104 14686 11629 10810 958 1547 -228 C ATOM 5062 C THR C 104 -104.561 -17.973 192.419 1.00 91.02 C ANISOU 5062 C THR C 104 13683 10739 10162 902 1523 -119 C ATOM 5063 O THR C 104 -105.465 -18.045 191.582 1.00 84.18 O ANISOU 5063 O THR C 104 12567 9858 9561 782 1654 -189 O ATOM 5064 CB THR C 104 -105.649 -17.664 194.654 1.00100.08 C ANISOU 5064 CB THR C 104 15232 11847 10946 904 1935 -237 C ATOM 5065 OG1 THR C 104 -105.807 -16.763 195.758 1.00102.18 O ANISOU 5065 OG1 THR C 104 15639 12155 11031 948 1967 -354 O ATOM 5066 CG2 THR C 104 -105.117 -18.994 195.167 1.00 98.57 C ANISOU 5066 CG2 THR C 104 15388 11576 10487 968 2033 -39 C ATOM 5067 N GLY C 105 -103.426 -18.663 192.321 1.00 94.23 N ANISOU 5067 N GLY C 105 14227 11144 10432 998 1350 41 N ATOM 5068 CA GLY C 105 -103.222 -19.616 191.248 1.00 91.78 C ANISOU 5068 CA GLY C 105 13816 10774 10281 950 1346 152 C ATOM 5069 C GLY C 105 -103.025 -19.012 189.878 1.00 85.67 C ANISOU 5069 C GLY C 105 12681 10060 9812 901 1117 93 C ATOM 5070 O GLY C 105 -103.203 -19.708 188.876 1.00 85.53 O ANISOU 5070 O GLY C 105 12525 9997 9973 815 1167 137 O ATOM 5071 N ALA C 106 -102.661 -17.736 189.801 1.00 81.60 N ANISOU 5071 N ALA C 106 12026 9632 9348 948 883 -9 N ATOM 5072 CA ALA C 106 -102.448 -17.056 188.534 1.00 77.70 C ANISOU 5072 CA ALA C 106 11228 9175 9119 918 677 -58 C ATOM 5073 C ALA C 106 -101.017 -16.545 188.452 1.00 78.60 C ANISOU 5073 C ALA C 106 11354 9351 9158 1010 352 -34 C ATOM 5074 O ALA C 106 -100.409 -16.182 189.464 1.00 82.86 O ANISOU 5074 O ALA C 106 12069 9947 9466 1090 264 -58 O ATOM 5075 CB ALA C 106 -103.429 -15.891 188.354 1.00 81.50 C ANISOU 5075 CB ALA C 106 11513 9681 9774 882 736 -222 C ATOM 5076 N MET C 107 -100.483 -16.520 187.234 1.00 76.41 N ANISOU 5076 N MET C 107 10881 9078 9073 988 180 -1 N ATOM 5077 CA MET C 107 -99.172 -15.950 186.953 1.00 76.43 C ANISOU 5077 CA MET C 107 10836 9142 9061 1040 -113 -10 C ATOM 5078 C MET C 107 -99.346 -14.705 186.092 1.00 78.67 C ANISOU 5078 C MET C 107 10902 9415 9575 992 -206 -128 C ATOM 5079 O MET C 107 -99.919 -14.778 185.000 1.00 82.02 O ANISOU 5079 O MET C 107 11143 9800 10218 939 -165 -113 O ATOM 5080 CB MET C 107 -98.270 -16.970 186.261 1.00 79.64 C ANISOU 5080 CB MET C 107 11229 9547 9485 1066 -223 132 C ATOM 5081 CG MET C 107 -97.802 -18.102 187.168 1.00 85.13 C ANISOU 5081 CG MET C 107 12183 10251 9913 1174 -170 267 C ATOM 5082 SD MET C 107 -98.862 -19.559 187.105 1.00 85.09 S ANISOU 5082 SD MET C 107 12306 10102 9922 1114 180 389 S ATOM 5083 CE MET C 107 -98.608 -20.091 185.413 1.00 83.49 C ANISOU 5083 CE MET C 107 11870 9850 10003 1026 114 444 C ATOM 5084 N ASP C 108 -98.845 -13.570 186.580 1.00 79.58 N ANISOU 5084 N ASP C 108 11048 9563 9626 1012 -323 -248 N ATOM 5085 CA ASP C 108 -99.102 -12.288 185.932 1.00 78.79 C ANISOU 5085 CA ASP C 108 10806 9412 9717 982 -355 -362 C ATOM 5086 C ASP C 108 -98.064 -11.929 184.875 1.00 82.39 C ANISOU 5086 C ASP C 108 11139 9859 10305 954 -560 -358 C ATOM 5087 O ASP C 108 -98.420 -11.386 183.824 1.00 88.53 O ANISOU 5087 O ASP C 108 11775 10570 11293 938 -558 -368 O ATOM 5088 CB ASP C 108 -99.172 -11.174 186.980 1.00 80.08 C ANISOU 5088 CB ASP C 108 11090 9577 9759 993 -320 -518 C ATOM 5089 CG ASP C 108 -98.005 -11.206 187.948 1.00 84.47 C ANISOU 5089 CG ASP C 108 11796 10239 10060 1004 -468 -563 C ATOM 5090 OD1 ASP C 108 -97.072 -12.008 187.737 1.00 86.36 O ANISOU 5090 OD1 ASP C 108 12027 10552 10234 1027 -617 -468 O ATOM 5091 OD2 ASP C 108 -98.020 -10.426 188.923 1.00 89.45 O ANISOU 5091 OD2 ASP C 108 12546 10892 10548 999 -436 -701 O ATOM 5092 N TYR C 109 -96.789 -12.217 185.125 1.00 81.60 N ANISOU 5092 N TYR C 109 11088 9838 10079 958 -734 -347 N ATOM 5093 CA TYR C 109 -95.705 -11.818 184.235 1.00 83.85 C ANISOU 5093 CA TYR C 109 11257 10124 10477 913 -916 -375 C ATOM 5094 C TYR C 109 -94.935 -13.056 183.806 1.00 83.81 C ANISOU 5094 C TYR C 109 11216 10178 10450 940 -1018 -235 C ATOM 5095 O TYR C 109 -94.427 -13.797 184.652 1.00 88.00 O ANISOU 5095 O TYR C 109 11858 10808 10770 1013 -1064 -185 O ATOM 5096 CB TYR C 109 -94.774 -10.821 184.927 1.00 88.68 C ANISOU 5096 CB TYR C 109 11922 10800 10973 876 -1034 -549 C ATOM 5097 CG TYR C 109 -95.399 -9.466 185.163 1.00 98.03 C ANISOU 5097 CG TYR C 109 13148 11884 12214 836 -922 -700 C ATOM 5098 CD1 TYR C 109 -96.215 -8.878 184.206 1.00104.19 C ANISOU 5098 CD1 TYR C 109 13849 12517 13219 837 -816 -682 C ATOM 5099 CD2 TYR C 109 -95.183 -8.780 186.351 1.00102.06 C ANISOU 5099 CD2 TYR C 109 13785 12452 12540 814 -915 -862 C ATOM 5100 CE1 TYR C 109 -96.790 -7.639 184.422 1.00107.49 C ANISOU 5100 CE1 TYR C 109 14327 12827 13688 838 -695 -807 C ATOM 5101 CE2 TYR C 109 -95.753 -7.542 186.576 1.00105.03 C ANISOU 5101 CE2 TYR C 109 14222 12712 12972 781 -784 -1004 C ATOM 5102 CZ TYR C 109 -96.555 -6.977 185.610 1.00105.37 C ANISOU 5102 CZ TYR C 109 14197 12587 13250 803 -668 -969 C ATOM 5103 OH TYR C 109 -97.125 -5.745 185.833 1.00104.26 O ANISOU 5103 OH TYR C 109 14136 12315 13164 804 -520 -1097 O ATOM 5104 N TRP C 110 -94.836 -13.270 182.498 1.00 77.39 N ANISOU 5104 N TRP C 110 10263 9303 9840 898 -1049 -169 N ATOM 5105 CA TRP C 110 -94.175 -14.439 181.943 1.00 68.94 C ANISOU 5105 CA TRP C 110 9154 8260 8781 918 -1116 -37 C ATOM 5106 C TRP C 110 -92.867 -14.044 181.270 1.00 69.46 C ANISOU 5106 C TRP C 110 9109 8361 8922 878 -1303 -90 C ATOM 5107 O TRP C 110 -92.642 -12.880 180.927 1.00 71.51 O ANISOU 5107 O TRP C 110 9311 8582 9276 804 -1346 -216 O ATOM 5108 CB TRP C 110 -95.078 -15.154 180.930 1.00 65.04 C ANISOU 5108 CB TRP C 110 8581 7679 8451 881 -986 70 C ATOM 5109 CG TRP C 110 -96.326 -15.735 181.519 1.00 64.75 C ANISOU 5109 CG TRP C 110 8628 7621 8355 894 -778 110 C ATOM 5110 CD1 TRP C 110 -97.246 -15.093 182.296 1.00 68.85 C ANISOU 5110 CD1 TRP C 110 9201 8137 8822 903 -660 26 C ATOM 5111 CD2 TRP C 110 -96.799 -17.079 181.367 1.00 68.96 C ANISOU 5111 CD2 TRP C 110 9202 8121 8880 880 -631 226 C ATOM 5112 NE1 TRP C 110 -98.258 -15.954 182.642 1.00 74.21 N ANISOU 5112 NE1 TRP C 110 9937 8796 9462 891 -452 78 N ATOM 5113 CE2 TRP C 110 -98.008 -17.180 182.083 1.00 73.10 C ANISOU 5113 CE2 TRP C 110 9796 8630 9347 867 -423 197 C ATOM 5114 CE3 TRP C 110 -96.317 -18.206 180.695 1.00 69.29 C ANISOU 5114 CE3 TRP C 110 9236 8132 8960 868 -631 342 C ATOM 5115 CZ2 TRP C 110 -98.741 -18.362 182.148 1.00 74.62 C ANISOU 5115 CZ2 TRP C 110 10053 8777 9521 822 -206 268 C ATOM 5116 CZ3 TRP C 110 -97.046 -19.379 180.761 1.00 75.23 C ANISOU 5116 CZ3 TRP C 110 10068 8825 9690 832 -415 419 C ATOM 5117 CH2 TRP C 110 -98.245 -19.449 181.482 1.00 77.25 C ANISOU 5117 CH2 TRP C 110 10394 9065 9890 799 -201 377 C ATOM 5118 N GLY C 111 -91.996 -15.039 181.089 1.00 68.26 N ANISOU 5118 N GLY C 111 8939 8272 8726 927 -1392 4 N ATOM 5119 CA GLY C 111 -90.788 -14.845 180.318 1.00 67.68 C ANISOU 5119 CA GLY C 111 8732 8235 8747 883 -1546 -39 C ATOM 5120 C GLY C 111 -91.029 -15.041 178.832 1.00 69.21 C ANISOU 5120 C GLY C 111 8818 8306 9173 807 -1498 32 C ATOM 5121 O GLY C 111 -92.113 -15.424 178.396 1.00 67.78 O ANISOU 5121 O GLY C 111 8648 8038 9068 794 -1361 115 O ATOM 5122 N GLN C 112 -89.989 -14.771 178.045 1.00 67.70 N ANISOU 5122 N GLN C 112 8513 8125 9087 747 -1610 -16 N ATOM 5123 CA GLN C 112 -90.106 -14.898 176.599 1.00 63.15 C ANISOU 5123 CA GLN C 112 7846 7437 8711 672 -1573 44 C ATOM 5124 C GLN C 112 -90.001 -16.341 176.125 1.00 66.00 C ANISOU 5124 C GLN C 112 8197 7794 9087 717 -1541 198 C ATOM 5125 O GLN C 112 -90.172 -16.597 174.929 1.00 73.03 O ANISOU 5125 O GLN C 112 9020 8602 10127 650 -1498 251 O ATOM 5126 CB GLN C 112 -89.045 -14.042 175.898 1.00 61.32 C ANISOU 5126 CB GLN C 112 7516 7193 8589 572 -1667 -74 C ATOM 5127 CG GLN C 112 -87.675 -14.690 175.779 1.00 63.18 C ANISOU 5127 CG GLN C 112 7660 7537 8810 588 -1789 -77 C ATOM 5128 CD GLN C 112 -86.849 -14.560 177.044 1.00 70.20 C ANISOU 5128 CD GLN C 112 8546 8614 9514 652 -1914 -187 C ATOM 5129 OE1 GLN C 112 -87.360 -14.188 178.100 1.00 74.66 O ANISOU 5129 OE1 GLN C 112 9208 9222 9937 692 -1899 -235 O ATOM 5130 NE2 GLN C 112 -85.560 -14.865 176.940 1.00 71.05 N ANISOU 5130 NE2 GLN C 112 8529 8852 9613 667 -2041 -238 N ATOM 5131 N GLY C 113 -89.730 -17.281 177.023 1.00 66.80 N ANISOU 5131 N GLY C 113 8383 7973 9026 834 -1548 272 N ATOM 5132 CA GLY C 113 -89.683 -18.681 176.666 1.00 62.23 C ANISOU 5132 CA GLY C 113 7841 7355 8450 889 -1475 423 C ATOM 5133 C GLY C 113 -88.287 -19.138 176.279 1.00 62.54 C ANISOU 5133 C GLY C 113 7797 7458 8508 941 -1600 441 C ATOM 5134 O GLY C 113 -87.423 -18.354 175.890 1.00 66.61 O ANISOU 5134 O GLY C 113 8183 8028 9099 880 -1727 325 O ATOM 5135 N THR C 114 -88.072 -20.446 176.401 1.00 64.96 N ANISOU 5135 N THR C 114 8188 7747 8745 1058 -1539 583 N ATOM 5136 CA THR C 114 -86.798 -21.060 176.047 1.00 66.75 C ANISOU 5136 CA THR C 114 8341 8034 8988 1149 -1634 621 C ATOM 5137 C THR C 114 -87.086 -22.341 175.284 1.00 65.75 C ANISOU 5137 C THR C 114 8286 7757 8940 1152 -1465 771 C ATOM 5138 O THR C 114 -87.704 -23.258 175.829 1.00 69.78 O ANISOU 5138 O THR C 114 8978 8193 9340 1234 -1310 891 O ATOM 5139 CB THR C 114 -85.954 -21.361 177.290 1.00 66.50 C ANISOU 5139 CB THR C 114 8364 8180 8723 1372 -1760 639 C ATOM 5140 OG1 THR C 114 -85.586 -20.133 177.930 1.00 69.46 O ANISOU 5140 OG1 THR C 114 8649 8714 9030 1334 -1922 459 O ATOM 5141 CG2 THR C 114 -84.698 -22.127 176.904 1.00 64.80 C ANISOU 5141 CG2 THR C 114 8062 8035 8523 1506 -1845 694 C ATOM 5142 N SER C 115 -86.659 -22.397 174.026 1.00 62.82 N ANISOU 5142 N SER C 115 7789 7328 8753 1047 -1469 754 N ATOM 5143 CA SER C 115 -86.804 -23.615 173.246 1.00 64.48 C ANISOU 5143 CA SER C 115 8061 7399 9040 1035 -1307 874 C ATOM 5144 C SER C 115 -85.758 -24.633 173.675 1.00 65.11 C ANISOU 5144 C SER C 115 8204 7516 9019 1259 -1327 981 C ATOM 5145 O SER C 115 -84.597 -24.291 173.910 1.00 69.63 O ANISOU 5145 O SER C 115 8654 8243 9559 1368 -1512 926 O ATOM 5146 CB SER C 115 -86.667 -23.320 171.753 1.00 71.30 C ANISOU 5146 CB SER C 115 8779 8196 10115 854 -1305 816 C ATOM 5147 OG SER C 115 -87.706 -22.468 171.303 1.00 85.95 O ANISOU 5147 OG SER C 115 10594 10018 12045 689 -1276 741 O ATOM 5148 N VAL C 116 -86.182 -25.887 173.792 1.00 63.62 N ANISOU 5148 N VAL C 116 8208 7188 8775 1334 -1124 1128 N ATOM 5149 CA VAL C 116 -85.293 -27.011 174.050 1.00 59.09 C ANISOU 5149 CA VAL C 116 7737 6599 8115 1571 -1090 1263 C ATOM 5150 C VAL C 116 -85.600 -28.072 173.008 1.00 54.61 C ANISOU 5150 C VAL C 116 7250 5814 7684 1470 -852 1341 C ATOM 5151 O VAL C 116 -86.753 -28.507 172.883 1.00 47.38 O ANISOU 5151 O VAL C 116 6470 4749 6785 1328 -631 1365 O ATOM 5152 CB VAL C 116 -85.463 -27.574 175.471 1.00 51.21 C ANISOU 5152 CB VAL C 116 6980 5621 6856 1813 -1036 1387 C ATOM 5153 CG1 VAL C 116 -84.824 -28.949 175.580 1.00 46.37 C ANISOU 5153 CG1 VAL C 116 6545 4912 6160 2065 -913 1569 C ATOM 5154 CG2 VAL C 116 -84.852 -26.625 176.484 1.00 53.03 C ANISOU 5154 CG2 VAL C 116 7113 6108 6928 1947 -1303 1300 C ATOM 5155 N THR C 117 -84.576 -28.484 172.262 1.00 51.41 N ANISOU 5155 N THR C 117 6752 5402 7378 1530 -886 1359 N ATOM 5156 CA THR C 117 -84.710 -29.502 171.230 1.00 46.83 C ANISOU 5156 CA THR C 117 6247 4618 6927 1437 -660 1419 C ATOM 5157 C THR C 117 -83.825 -30.685 171.590 1.00 48.98 C ANISOU 5157 C THR C 117 6671 4830 7110 1733 -577 1577 C ATOM 5158 O THR C 117 -82.596 -30.556 171.636 1.00 56.10 O ANISOU 5158 O THR C 117 7431 5879 8007 1921 -758 1572 O ATOM 5159 CB THR C 117 -84.330 -28.948 169.855 1.00 42.15 C ANISOU 5159 CB THR C 117 5425 4041 6548 1230 -737 1298 C ATOM 5160 OG1 THR C 117 -85.043 -27.728 169.615 1.00 39.82 O ANISOU 5160 OG1 THR C 117 5002 3820 6309 1018 -841 1165 O ATOM 5161 CG2 THR C 117 -84.673 -29.952 168.765 1.00 42.77 C ANISOU 5161 CG2 THR C 117 5591 3911 6748 1086 -488 1334 C ATOM 5162 N VAL C 118 -84.451 -31.828 171.839 1.00 48.95 N ANISOU 5162 N VAL C 118 6953 4610 7034 1776 -289 1709 N ATOM 5163 CA VAL C 118 -83.739 -33.079 172.064 1.00 58.93 C ANISOU 5163 CA VAL C 118 8422 5749 8219 2062 -140 1883 C ATOM 5164 C VAL C 118 -83.614 -33.800 170.728 1.00 58.65 C ANISOU 5164 C VAL C 118 8378 5521 8384 1903 57 1869 C ATOM 5165 O VAL C 118 -84.624 -34.142 170.102 1.00 61.57 O ANISOU 5165 O VAL C 118 8835 5714 8845 1621 292 1822 O ATOM 5166 CB VAL C 118 -84.466 -33.950 173.100 1.00 62.58 C ANISOU 5166 CB VAL C 118 9254 6042 8480 2199 113 2038 C ATOM 5167 CG1 VAL C 118 -83.701 -35.232 173.346 1.00 62.71 C ANISOU 5167 CG1 VAL C 118 9503 5926 8397 2509 276 2217 C ATOM 5168 CG2 VAL C 118 -84.650 -33.177 174.399 1.00 68.42 C ANISOU 5168 CG2 VAL C 118 10005 6980 9012 2330 -79 2036 C ATOM 5169 N SER C 119 -82.378 -34.032 170.291 1.00 58.24 N ANISOU 5169 N SER C 119 8210 5522 8397 2079 -35 1894 N ATOM 5170 CA SER C 119 -82.138 -34.718 169.030 1.00 65.82 C ANISOU 5170 CA SER C 119 9164 6302 9541 1948 151 1879 C ATOM 5171 C SER C 119 -80.695 -35.194 168.985 1.00 66.31 C ANISOU 5171 C SER C 119 9165 6422 9610 2275 78 1960 C ATOM 5172 O SER C 119 -79.784 -34.475 169.403 1.00 70.90 O ANISOU 5172 O SER C 119 9517 7272 10148 2453 -221 1915 O ATOM 5173 CB SER C 119 -82.429 -33.806 167.832 1.00 44.00 C ANISOU 5173 CB SER C 119 6140 3603 6974 1578 52 1686 C ATOM 5174 OG SER C 119 -82.036 -34.423 166.618 1.00 43.79 O ANISOU 5174 OG SER C 119 6095 3434 7110 1471 205 1663 O ATOM 5175 N SER C 120 -80.497 -36.406 168.466 1.00 64.77 N ANISOU 5175 N SER C 120 9154 6001 9455 2314 351 2033 N ATOM 5176 CA SER C 120 -79.169 -36.968 168.254 1.00 62.07 C ANISOU 5176 CA SER C 120 8736 5725 9122 2557 307 2055 C ATOM 5177 C SER C 120 -78.693 -36.787 166.817 1.00 56.48 C ANISOU 5177 C SER C 120 7822 4960 8676 2381 332 1962 C ATOM 5178 O SER C 120 -77.956 -37.629 166.294 1.00 62.69 O ANISOU 5178 O SER C 120 8645 5665 9508 2476 462 1979 O ATOM 5179 CB SER C 120 -79.155 -38.447 168.637 1.00 68.78 C ANISOU 5179 CB SER C 120 9910 6395 9830 2704 591 2168 C ATOM 5180 OG SER C 120 -80.069 -39.184 167.844 1.00 75.74 O ANISOU 5180 OG SER C 120 10990 6991 10799 2407 941 2143 O ATOM 5181 N ALA C 121 -79.102 -35.701 166.169 1.00 47.63 N ANISOU 5181 N ALA C 121 6480 3927 7690 2063 195 1810 N ATOM 5182 CA ALA C 121 -78.703 -35.400 164.803 1.00 51.13 C ANISOU 5182 CA ALA C 121 6722 4364 8343 1819 191 1670 C ATOM 5183 C ALA C 121 -77.504 -34.462 164.801 1.00 50.64 C ANISOU 5183 C ALA C 121 6321 4588 8333 1924 -118 1566 C ATOM 5184 O ALA C 121 -77.404 -33.561 165.640 1.00 52.01 O ANISOU 5184 O ALA C 121 6359 4993 8409 1997 -373 1520 O ATOM 5185 CB ALA C 121 -79.858 -34.772 164.021 1.00 43.35 C ANISOU 5185 CB ALA C 121 5705 3331 7434 1387 225 1536 C ATOM 5186 N LYS C 122 -76.600 -34.674 163.851 1.00 53.42 N ANISOU 5186 N LYS C 122 6535 4920 8840 1912 -75 1509 N ATOM 5187 CA LYS C 122 -75.455 -33.792 163.711 1.00 52.19 C ANISOU 5187 CA LYS C 122 6039 5027 8762 1956 -327 1373 C ATOM 5188 C LYS C 122 -75.833 -32.568 162.886 1.00 43.75 C ANISOU 5188 C LYS C 122 4807 4010 7807 1561 -426 1190 C ATOM 5189 O LYS C 122 -76.790 -32.584 162.106 1.00 44.92 O ANISOU 5189 O LYS C 122 5079 3983 8004 1272 -280 1170 O ATOM 5190 CB LYS C 122 -74.287 -34.520 163.045 1.00 59.35 C ANISOU 5190 CB LYS C 122 6857 5898 9795 2116 -223 1379 C ATOM 5191 CG LYS C 122 -73.619 -35.579 163.906 1.00 71.18 C ANISOU 5191 CG LYS C 122 8462 7407 11176 2594 -176 1555 C ATOM 5192 CD LYS C 122 -72.156 -35.750 163.518 1.00 86.77 C ANISOU 5192 CD LYS C 122 10176 9529 13266 2804 -233 1494 C ATOM 5193 CE LYS C 122 -71.979 -35.739 162.006 1.00 88.90 C ANISOU 5193 CE LYS C 122 10370 9644 13766 2484 -65 1370 C ATOM 5194 NZ LYS C 122 -70.546 -35.748 161.607 1.00 91.03 N ANISOU 5194 NZ LYS C 122 10340 10083 14165 2648 -127 1272 N ATOM 5195 N THR C 123 -75.080 -31.487 163.084 1.00 43.78 N ANISOU 5195 N THR C 123 4534 4264 7836 1555 -672 1048 N ATOM 5196 CA THR C 123 -75.251 -30.308 162.247 1.00 43.38 C ANISOU 5196 CA THR C 123 4343 4241 7896 1210 -740 878 C ATOM 5197 C THR C 123 -75.024 -30.679 160.788 1.00 42.50 C ANISOU 5197 C THR C 123 4237 3958 7953 1015 -548 836 C ATOM 5198 O THR C 123 -73.974 -31.223 160.432 1.00 49.16 O ANISOU 5198 O THR C 123 4977 4814 8888 1145 -489 823 O ATOM 5199 CB THR C 123 -74.285 -29.205 162.675 1.00 44.28 C ANISOU 5199 CB THR C 123 4166 4633 8026 1239 -985 713 C ATOM 5200 OG1 THR C 123 -74.579 -28.805 164.019 1.00 46.79 O ANISOU 5200 OG1 THR C 123 4493 5116 8170 1392 -1163 736 O ATOM 5201 CG2 THR C 123 -74.414 -28.000 161.755 1.00 40.58 C ANISOU 5201 CG2 THR C 123 3599 4146 7674 886 -1007 547 C ATOM 5202 N THR C 124 -76.007 -30.382 159.945 1.00 39.49 N ANISOU 5202 N THR C 124 3969 3433 7602 715 -454 810 N ATOM 5203 CA THR C 124 -75.963 -30.771 158.546 1.00 42.36 C ANISOU 5203 CA THR C 124 4377 3630 8089 512 -262 773 C ATOM 5204 C THR C 124 -76.373 -29.584 157.684 1.00 44.65 C ANISOU 5204 C THR C 124 4612 3932 8421 203 -322 651 C ATOM 5205 O THR C 124 -77.454 -29.008 157.900 1.00 48.73 O ANISOU 5205 O THR C 124 5207 4457 8852 92 -386 659 O ATOM 5206 CB THR C 124 -76.874 -31.975 158.276 1.00 41.19 C ANISOU 5206 CB THR C 124 4487 3262 7902 478 -21 886 C ATOM 5207 OG1 THR C 124 -76.341 -33.131 158.934 1.00 49.34 O ANISOU 5207 OG1 THR C 124 5605 4236 8906 783 84 1010 O ATOM 5208 CG2 THR C 124 -76.953 -32.251 156.786 1.00 37.62 C ANISOU 5208 CG2 THR C 124 4081 2660 7554 222 163 820 C ATOM 5209 N PRO C 125 -75.556 -29.183 156.716 1.00 39.88 N ANISOU 5209 N PRO C 125 3888 3327 7940 72 -292 540 N ATOM 5210 CA PRO C 125 -75.950 -28.093 155.824 1.00 37.66 C ANISOU 5210 CA PRO C 125 3606 3024 7678 -204 -316 445 C ATOM 5211 C PRO C 125 -77.088 -28.533 154.923 1.00 40.37 C ANISOU 5211 C PRO C 125 4144 3219 7978 -386 -173 493 C ATOM 5212 O PRO C 125 -77.272 -29.737 154.685 1.00 48.13 O ANISOU 5212 O PRO C 125 5238 4084 8964 -356 -4 558 O ATOM 5213 CB PRO C 125 -74.672 -27.815 155.019 1.00 38.41 C ANISOU 5213 CB PRO C 125 3548 3130 7916 -278 -264 323 C ATOM 5214 CG PRO C 125 -73.918 -29.100 155.061 1.00 42.32 C ANISOU 5214 CG PRO C 125 4016 3588 8476 -88 -140 374 C ATOM 5215 CD PRO C 125 -74.218 -29.710 156.399 1.00 41.05 C ANISOU 5215 CD PRO C 125 3899 3491 8209 186 -220 498 C ATOM 5216 N PRO C 126 -77.865 -27.595 154.391 1.00 34.16 N ANISOU 5216 N PRO C 126 3404 2436 7140 -572 -227 454 N ATOM 5217 CA PRO C 126 -79.024 -27.962 153.576 1.00 33.38 C ANISOU 5217 CA PRO C 126 3460 2271 6952 -727 -124 476 C ATOM 5218 C PRO C 126 -78.691 -28.191 152.111 1.00 38.88 C ANISOU 5218 C PRO C 126 4234 3000 7538 -841 23 395 C ATOM 5219 O PRO C 126 -77.738 -27.639 151.557 1.00 32.33 O ANISOU 5219 O PRO C 126 3343 2185 6757 -877 30 326 O ATOM 5220 CB PRO C 126 -79.936 -26.741 153.736 1.00 30.80 C ANISOU 5220 CB PRO C 126 3152 2060 6490 -773 -273 456 C ATOM 5221 CG PRO C 126 -78.980 -25.608 153.836 1.00 31.01 C ANISOU 5221 CG PRO C 126 3065 2112 6605 -776 -374 389 C ATOM 5222 CD PRO C 126 -77.799 -26.139 154.621 1.00 34.86 C ANISOU 5222 CD PRO C 126 3415 2617 7214 -622 -387 383 C ATOM 5223 N SER C 127 -79.511 -29.029 151.480 1.00 40.68 N ANISOU 5223 N SER C 127 4606 3237 7613 -915 145 392 N ATOM 5224 CA SER C 127 -79.481 -29.212 150.036 1.00 39.64 C ANISOU 5224 CA SER C 127 4583 3147 7333 -1048 250 319 C ATOM 5225 C SER C 127 -80.552 -28.321 149.420 1.00 39.55 C ANISOU 5225 C SER C 127 4647 3251 7128 -1156 163 290 C ATOM 5226 O SER C 127 -81.743 -28.481 149.712 1.00 47.58 O ANISOU 5226 O SER C 127 5694 4309 8074 -1185 132 307 O ATOM 5227 CB SER C 127 -79.706 -30.676 149.660 1.00 32.87 C ANISOU 5227 CB SER C 127 3829 2222 6437 -1086 427 318 C ATOM 5228 OG SER C 127 -78.539 -31.447 149.896 1.00 33.96 O ANISOU 5228 OG SER C 127 3911 2227 6764 -981 548 342 O ATOM 5229 N VAL C 128 -80.122 -27.365 148.601 1.00 31.21 N ANISOU 5229 N VAL C 128 3615 2229 6013 -1212 134 251 N ATOM 5230 CA VAL C 128 -81.016 -26.403 147.968 1.00 30.82 C ANISOU 5230 CA VAL C 128 3640 2245 5826 -1292 62 243 C ATOM 5231 C VAL C 128 -81.337 -26.896 146.564 1.00 35.22 C ANISOU 5231 C VAL C 128 4322 2820 6242 -1442 148 208 C ATOM 5232 O VAL C 128 -80.436 -27.057 145.732 1.00 38.72 O ANISOU 5232 O VAL C 128 4814 3229 6667 -1491 223 183 O ATOM 5233 CB VAL C 128 -80.391 -25.001 147.933 1.00 30.77 C ANISOU 5233 CB VAL C 128 3621 2226 5845 -1269 -2 234 C ATOM 5234 CG1 VAL C 128 -81.277 -24.041 147.149 1.00 40.56 C ANISOU 5234 CG1 VAL C 128 4960 3478 6971 -1340 -50 246 C ATOM 5235 CG2 VAL C 128 -80.153 -24.496 149.345 1.00 30.42 C ANISOU 5235 CG2 VAL C 128 3444 2175 5939 -1146 -114 259 C ATOM 5236 N TYR C 129 -82.620 -27.134 146.299 1.00 35.66 N ANISOU 5236 N TYR C 129 4404 2932 6214 -1525 126 202 N ATOM 5237 CA TYR C 129 -83.092 -27.584 145.004 1.00 36.55 C ANISOU 5237 CA TYR C 129 4604 3076 6208 -1692 171 168 C ATOM 5238 C TYR C 129 -83.976 -26.522 144.373 1.00 45.24 C ANISOU 5238 C TYR C 129 5715 4209 7265 -1761 91 164 C ATOM 5239 O TYR C 129 -84.877 -25.995 145.040 1.00 50.34 O ANISOU 5239 O TYR C 129 6265 4894 7968 -1704 -20 188 O ATOM 5240 CB TYR C 129 -83.862 -28.900 145.142 1.00 40.88 C ANISOU 5240 CB TYR C 129 5137 3660 6735 -1761 222 147 C ATOM 5241 CG TYR C 129 -83.013 -30.032 145.674 1.00 41.41 C ANISOU 5241 CG TYR C 129 5207 3644 6882 -1678 337 158 C ATOM 5242 CD1 TYR C 129 -81.720 -30.228 145.205 1.00 38.37 C ANISOU 5242 CD1 TYR C 129 4846 3189 6546 -1637 409 156 C ATOM 5243 CD2 TYR C 129 -83.493 -30.893 146.653 1.00 32.97 C ANISOU 5243 CD2 TYR C 129 4114 2550 5864 -1636 393 166 C ATOM 5244 CE1 TYR C 129 -80.934 -31.256 145.684 1.00 37.43 C ANISOU 5244 CE1 TYR C 129 4709 2973 6538 -1549 537 159 C ATOM 5245 CE2 TYR C 129 -82.711 -31.924 147.141 1.00 33.51 C ANISOU 5245 CE2 TYR C 129 4198 2504 6030 -1546 526 183 C ATOM 5246 CZ TYR C 129 -81.432 -32.100 146.652 1.00 40.03 C ANISOU 5246 CZ TYR C 129 5031 3258 6919 -1498 598 178 C ATOM 5247 OH TYR C 129 -80.645 -33.122 147.129 1.00 46.04 O ANISOU 5247 OH TYR C 129 5795 3889 7811 -1395 751 196 O ATOM 5248 N PRO C 130 -83.753 -26.181 143.107 1.00 44.88 N ANISOU 5248 N PRO C 130 5769 4133 7150 -1870 112 158 N ATOM 5249 CA PRO C 130 -84.600 -25.181 142.447 1.00 39.57 C ANISOU 5249 CA PRO C 130 5094 3448 6494 -1916 37 170 C ATOM 5250 C PRO C 130 -85.890 -25.793 141.926 1.00 42.10 C ANISOU 5250 C PRO C 130 5340 3895 6760 -2068 -38 128 C ATOM 5251 O PRO C 130 -85.910 -26.918 141.420 1.00 55.89 O ANISOU 5251 O PRO C 130 7055 5676 8505 -2144 72 48 O ATOM 5252 CB PRO C 130 -83.715 -24.687 141.299 1.00 34.56 C ANISOU 5252 CB PRO C 130 4620 2713 5798 -1972 127 177 C ATOM 5253 CG PRO C 130 -82.909 -25.895 140.943 1.00 37.01 C ANISOU 5253 CG PRO C 130 4892 3030 6140 -1985 130 204 C ATOM 5254 CD PRO C 130 -82.630 -26.604 142.250 1.00 39.32 C ANISOU 5254 CD PRO C 130 5135 3373 6432 -1900 162 179 C ATOM 5255 N LEU C 131 -86.979 -25.037 142.053 1.00 37.61 N ANISOU 5255 N LEU C 131 4734 3517 6040 -1958 -231 164 N ATOM 5256 CA LEU C 131 -88.290 -25.421 141.544 1.00 36.32 C ANISOU 5256 CA LEU C 131 4494 3630 5676 -2015 -311 74 C ATOM 5257 C LEU C 131 -88.672 -24.414 140.468 1.00 37.72 C ANISOU 5257 C LEU C 131 4784 3942 5606 -1922 -435 122 C ATOM 5258 O LEU C 131 -89.040 -23.275 140.777 1.00 47.88 O ANISOU 5258 O LEU C 131 6093 5278 6823 -1711 -585 226 O ATOM 5259 CB LEU C 131 -89.325 -25.448 142.667 1.00 35.94 C ANISOU 5259 CB LEU C 131 4274 3736 5646 -1924 -426 61 C ATOM 5260 CG LEU C 131 -89.020 -26.371 143.847 1.00 34.79 C ANISOU 5260 CG LEU C 131 4051 3451 5717 -1976 -304 40 C ATOM 5261 CD1 LEU C 131 -90.156 -26.346 144.851 1.00 34.74 C ANISOU 5261 CD1 LEU C 131 3893 3613 5694 -1899 -406 18 C ATOM 5262 CD2 LEU C 131 -88.754 -27.791 143.369 1.00 48.83 C ANISOU 5262 CD2 LEU C 131 5849 5159 7545 -2208 -88 -79 C ATOM 5263 N ALA C 132 -88.595 -24.840 139.219 1.00 35.63 N ANISOU 5263 N ALA C 132 5130 2770 5639 392 -773 -29 N ATOM 5264 CA ALA C 132 -88.957 -24.049 138.060 1.00 45.77 C ANISOU 5264 CA ALA C 132 6491 4195 6703 600 -863 -3 C ATOM 5265 C ALA C 132 -90.211 -24.619 137.415 1.00 54.03 C ANISOU 5265 C ALA C 132 7742 5282 7504 262 -1440 -123 C ATOM 5266 O ALA C 132 -90.531 -25.798 137.603 1.00 58.20 O ANISOU 5266 O ALA C 132 8551 5595 7968 -88 -1697 -273 O ATOM 5267 CB ALA C 132 -87.807 -24.029 137.042 1.00 55.86 C ANISOU 5267 CB ALA C 132 8319 5215 7692 1104 -534 -11 C ATOM 5268 N PRO C 133 -90.970 -23.801 136.679 1.00 57.09 N ANISOU 5268 N PRO C 133 7970 5947 7775 343 -1668 -58 N ATOM 5269 CA PRO C 133 -92.204 -24.296 136.059 1.00 62.47 C ANISOU 5269 CA PRO C 133 8753 6731 8250 3 -2312 -179 C ATOM 5270 C PRO C 133 -91.955 -25.565 135.258 1.00 66.26 C ANISOU 5270 C PRO C 133 10083 6819 8275 -78 -2560 -439 C ATOM 5271 O PRO C 133 -90.877 -25.774 134.698 1.00 61.64 O ANISOU 5271 O PRO C 133 10104 5929 7388 316 -2231 -478 O ATOM 5272 CB PRO C 133 -92.644 -23.135 135.155 1.00 66.79 C ANISOU 5272 CB PRO C 133 9166 7596 8614 341 -2422 -34 C ATOM 5273 CG PRO C 133 -91.491 -22.175 135.135 1.00 66.04 C ANISOU 5273 CG PRO C 133 9086 7441 8566 876 -1759 130 C ATOM 5274 CD PRO C 133 -90.785 -22.364 136.431 1.00 53.50 C ANISOU 5274 CD PRO C 133 7193 5733 7402 738 -1359 142 C ATOM 5275 N GLY C 134 -92.977 -26.413 135.215 1.00 78.68 N ANISOU 5275 N GLY C 134 11691 8376 9828 -608 -3115 -618 N ATOM 5276 CA GLY C 134 -92.841 -27.763 134.712 1.00 84.14 C ANISOU 5276 CA GLY C 134 13173 8628 10168 -827 -3340 -906 C ATOM 5277 C GLY C 134 -92.438 -27.909 133.262 1.00 83.41 C ANISOU 5277 C GLY C 134 13954 8334 9403 -470 -3471 -1060 C ATOM 5278 O GLY C 134 -92.161 -26.930 132.562 1.00 68.30 O ANISOU 5278 O GLY C 134 12082 6611 7260 23 -3339 -918 O ATOM 5279 N CYS C 135 -92.421 -29.158 132.807 1.00 99.11 N ANISOU 5279 N CYS C 135 16709 9894 11054 -718 -3698 -1354 N ATOM 5280 CA CYS C 135 -91.923 -29.529 131.492 1.00111.17 C ANISOU 5280 CA CYS C 135 19266 11098 11878 -385 -3748 -1542 C ATOM 5281 C CYS C 135 -92.745 -28.883 130.385 1.00111.53 C ANISOU 5281 C CYS C 135 19387 11490 11500 -303 -4340 -1594 C ATOM 5282 O CYS C 135 -92.239 -28.034 129.644 1.00107.21 O ANISOU 5282 O CYS C 135 19076 11036 10621 301 -4092 -1438 O ATOM 5283 CB CYS C 135 -91.926 -31.051 131.375 1.00127.39 C ANISOU 5283 CB CYS C 135 21950 12682 13768 -748 -3816 -1794 C ATOM 5284 SG CYS C 135 -91.416 -31.856 132.921 1.00136.47 S ANISOU 5284 SG CYS C 135 22750 13589 15512 -979 -3285 -1677 S ATOM 5285 N GLY C 136 -94.009 -29.273 130.266 1.00117.79 N ANISOU 5285 N GLY C 136 19866 12507 12382 -867 -5006 -1741 N ATOM 5286 CA GLY C 136 -94.893 -28.667 129.291 1.00120.84 C ANISOU 5286 CA GLY C 136 20111 13318 12487 -786 -5535 -1724 C ATOM 5287 C GLY C 136 -95.952 -27.832 129.977 1.00115.34 C ANISOU 5287 C GLY C 136 18262 13209 12353 -1032 -5817 -1512 C ATOM 5288 O GLY C 136 -97.095 -27.749 129.516 1.00110.70 O ANISOU 5288 O GLY C 136 17263 13004 11796 -1263 -6294 -1535 O ATOM 5289 N ASP C 137 -95.572 -27.204 131.088 1.00114.06 N ANISOU 5289 N ASP C 137 17540 13131 12668 -956 -5451 -1288 N ATOM 5290 CA ASP C 137 -96.512 -26.462 131.917 1.00120.15 C ANISOU 5290 CA ASP C 137 17186 14397 14069 -1186 -5558 -1041 C ATOM 5291 C ASP C 137 -96.796 -25.101 131.291 1.00132.72 C ANISOU 5291 C ASP C 137 18477 16454 15497 -663 -5646 -770 C ATOM 5292 O ASP C 137 -95.893 -24.265 131.166 1.00131.56 O ANISOU 5292 O ASP C 137 18487 16269 15230 -59 -5042 -560 O ATOM 5293 CB ASP C 137 -95.947 -26.300 133.327 1.00110.82 C ANISOU 5293 CB ASP C 137 15502 13122 13483 -1213 -4859 -844 C ATOM 5294 CG ASP C 137 -97.006 -25.924 134.347 1.00111.91 C ANISOU 5294 CG ASP C 137 14599 13630 14291 -1613 -4966 -661 C ATOM 5295 OD1 ASP C 137 -98.032 -25.325 133.962 1.00116.31 O ANISOU 5295 OD1 ASP C 137 14651 14636 14908 -1592 -5209 -540 O ATOM 5296 OD2 ASP C 137 -96.807 -26.230 135.541 1.00108.85 O ANISOU 5296 OD2 ASP C 137 13912 13096 14351 -1841 -4550 -598 O ATOM 5297 N THR C 138 -98.049 -24.882 130.903 1.00146.36 N ANISOU 5297 N THR C 138 19687 18620 17304 -851 -6084 -730 N ATOM 5298 CA THR C 138 -98.467 -23.588 130.383 1.00152.05 C ANISOU 5298 CA THR C 138 20043 19814 17915 -367 -6166 -434 C ATOM 5299 C THR C 138 -98.576 -22.578 131.518 1.00147.04 C ANISOU 5299 C THR C 138 18507 19430 17931 -267 -5728 -76 C ATOM 5300 O THR C 138 -99.198 -22.853 132.549 1.00150.63 O ANISOU 5300 O THR C 138 18285 19971 18975 -733 -5570 -56 O ATOM 5301 CB THR C 138 -99.804 -23.713 129.655 1.00166.78 C ANISOU 5301 CB THR C 138 21588 22102 19680 -596 -6718 -503 C ATOM 5302 OG1 THR C 138 -100.816 -24.132 130.580 1.00171.21 O ANISOU 5302 OG1 THR C 138 21316 22850 20887 -1177 -6731 -528 O ATOM 5303 CG2 THR C 138 -99.703 -24.731 128.530 1.00174.28 C ANISOU 5303 CG2 THR C 138 23435 22782 20001 -718 -7129 -874 C ATOM 5304 N THR C 139 -97.971 -21.409 131.334 1.00141.00 N ANISOU 5304 N THR C 139 17781 18740 17051 382 -5347 208 N ATOM 5305 CA THR C 139 -97.988 -20.362 132.342 1.00127.87 C ANISOU 5305 CA THR C 139 15345 17264 15977 530 -4750 540 C ATOM 5306 C THR C 139 -98.922 -19.237 131.913 1.00122.58 C ANISOU 5306 C THR C 139 14158 17096 15322 864 -4902 853 C ATOM 5307 O THR C 139 -99.204 -19.049 130.726 1.00126.04 O ANISOU 5307 O THR C 139 14965 17707 15217 1168 -5263 865 O ATOM 5308 CB THR C 139 -96.580 -19.807 132.589 1.00121.24 C ANISOU 5308 CB THR C 139 14854 16102 15110 980 -3862 628 C ATOM 5309 OG1 THR C 139 -96.104 -19.160 131.402 1.00124.49 O ANISOU 5309 OG1 THR C 139 15851 16487 14962 1616 -3743 727 O ATOM 5310 CG2 THR C 139 -95.624 -20.929 132.967 1.00117.14 C ANISOU 5310 CG2 THR C 139 14843 15112 14554 722 -3642 348 C ATOM 5311 N GLY C 140 -99.397 -18.489 132.898 1.00109.80 N ANISOU 5311 N GLY C 140 11756 15696 14267 822 -4436 1078 N ATOM 5312 CA GLY C 140 -100.315 -17.380 132.689 1.00103.06 C ANISOU 5312 CA GLY C 140 10419 15271 13469 1170 -4344 1315 C ATOM 5313 C GLY C 140 -99.604 -16.044 132.690 1.00 88.46 C ANISOU 5313 C GLY C 140 8660 13300 11651 1809 -3730 1590 C ATOM 5314 O GLY C 140 -98.518 -15.894 132.118 1.00 81.35 O ANISOU 5314 O GLY C 140 8324 12163 10424 2193 -3569 1707 O ATOM 5315 N SER C 141 -100.225 -15.057 133.339 1.00 81.52 N ANISOU 5315 N SER C 141 7311 12465 11196 1865 -3299 1696 N ATOM 5316 CA SER C 141 -99.588 -13.753 133.481 1.00 70.83 C ANISOU 5316 CA SER C 141 6077 10888 9946 2252 -2551 1911 C ATOM 5317 C SER C 141 -98.505 -13.782 134.549 1.00 66.09 C ANISOU 5317 C SER C 141 5545 9976 9591 2055 -1870 1807 C ATOM 5318 O SER C 141 -97.479 -13.105 134.417 1.00 64.21 O ANISOU 5318 O SER C 141 5639 9490 9266 2334 -1306 1865 O ATOM 5319 CB SER C 141 -100.631 -12.688 133.818 1.00 67.25 C ANISOU 5319 CB SER C 141 5203 10584 9765 2315 -2316 2052 C ATOM 5320 OG SER C 141 -101.066 -12.816 135.160 1.00 64.44 O ANISOU 5320 OG SER C 141 4470 10204 9810 1874 -2004 1932 O ATOM 5321 N SER C 142 -98.717 -14.552 135.611 1.00 55.11 N ANISOU 5321 N SER C 142 3892 8568 8477 1545 -1878 1624 N ATOM 5322 CA SER C 142 -97.746 -14.701 136.681 1.00 52.41 C ANISOU 5322 CA SER C 142 3664 7932 8318 1319 -1344 1491 C ATOM 5323 C SER C 142 -97.103 -16.080 136.620 1.00 50.62 C ANISOU 5323 C SER C 142 3609 7583 8041 1091 -1698 1372 C ATOM 5324 O SER C 142 -97.686 -17.038 136.105 1.00 63.29 O ANISOU 5324 O SER C 142 5213 9309 9525 861 -2370 1308 O ATOM 5325 CB SER C 142 -98.396 -14.492 138.052 1.00 53.77 C ANISOU 5325 CB SER C 142 3603 8077 8750 946 -1021 1405 C ATOM 5326 OG SER C 142 -98.832 -13.153 138.212 1.00 70.77 O ANISOU 5326 OG SER C 142 5705 10247 10938 1136 -662 1533 O ATOM 5327 N VAL C 143 -95.890 -16.165 137.154 1.00 42.91 N ANISOU 5327 N VAL C 143 2849 6312 7144 1103 -1257 1294 N ATOM 5328 CA VAL C 143 -95.139 -17.407 137.252 1.00 41.60 C ANISOU 5328 CA VAL C 143 2937 5896 6972 894 -1472 1142 C ATOM 5329 C VAL C 143 -94.642 -17.525 138.684 1.00 40.99 C ANISOU 5329 C VAL C 143 2752 5654 7167 600 -1004 1017 C ATOM 5330 O VAL C 143 -94.090 -16.564 139.237 1.00 33.64 O ANISOU 5330 O VAL C 143 1941 4652 6189 709 -438 974 O ATOM 5331 CB VAL C 143 -93.966 -17.457 136.252 1.00 41.48 C ANISOU 5331 CB VAL C 143 3635 5609 6516 1295 -1282 1044 C ATOM 5332 CG1 VAL C 143 -93.329 -16.087 136.107 1.00 39.47 C ANISOU 5332 CG1 VAL C 143 3337 5326 6333 1783 -644 1240 C ATOM 5333 CG2 VAL C 143 -92.932 -18.489 136.681 1.00 38.91 C ANISOU 5333 CG2 VAL C 143 3680 4934 6170 1104 -1150 806 C ATOM 5334 N THR C 144 -94.854 -18.693 139.284 1.00 44.83 N ANISOU 5334 N THR C 144 3217 6044 7772 170 -1273 886 N ATOM 5335 CA THR C 144 -94.404 -18.977 140.639 1.00 33.39 C ANISOU 5335 CA THR C 144 1868 4425 6392 -55 -879 765 C ATOM 5336 C THR C 144 -93.156 -19.845 140.564 1.00 38.45 C ANISOU 5336 C THR C 144 2718 4769 7123 -19 -929 668 C ATOM 5337 O THR C 144 -93.183 -20.938 139.990 1.00 49.84 O ANISOU 5337 O THR C 144 4573 6052 8312 -163 -1284 516 O ATOM 5338 CB THR C 144 -95.499 -19.671 141.451 1.00 35.18 C ANISOU 5338 CB THR C 144 2014 4708 6647 -442 -1000 706 C ATOM 5339 OG1 THR C 144 -96.646 -18.817 141.537 1.00 37.15 O ANISOU 5339 OG1 THR C 144 2034 5201 6880 -398 -923 788 O ATOM 5340 CG2 THR C 144 -95.002 -19.985 142.854 1.00 31.89 C ANISOU 5340 CG2 THR C 144 1799 4131 6186 -534 -658 619 C ATOM 5341 N LEU C 145 -92.068 -19.341 141.131 1.00 35.20 N ANISOU 5341 N LEU C 145 2459 4241 6674 167 -432 627 N ATOM 5342 CA LEU C 145 -90.803 -20.041 141.263 1.00 38.88 C ANISOU 5342 CA LEU C 145 3164 4435 7174 270 -317 520 C ATOM 5343 C LEU C 145 -90.615 -20.456 142.715 1.00 44.78 C ANISOU 5343 C LEU C 145 3939 5132 7945 8 -189 454 C ATOM 5344 O LEU C 145 -91.208 -19.872 143.624 1.00 39.36 O ANISOU 5344 O LEU C 145 3297 4596 7063 -94 -70 460 O ATOM 5345 CB LEU C 145 -89.653 -19.137 140.813 1.00 30.70 C ANISOU 5345 CB LEU C 145 2356 3355 5955 623 109 507 C ATOM 5346 CG LEU C 145 -89.777 -18.626 139.378 1.00 33.72 C ANISOU 5346 CG LEU C 145 2879 3736 6198 1014 102 604 C ATOM 5347 CD1 LEU C 145 -88.809 -17.484 139.118 1.00 39.06 C ANISOU 5347 CD1 LEU C 145 3798 4466 6579 1115 512 542 C ATOM 5348 CD2 LEU C 145 -89.546 -19.756 138.402 1.00 36.91 C ANISOU 5348 CD2 LEU C 145 3873 3912 6238 1095 -177 492 C ATOM 5349 N GLY C 146 -89.788 -21.478 142.941 1.00 39.78 N ANISOU 5349 N GLY C 146 3440 4266 7409 6 -226 377 N ATOM 5350 CA GLY C 146 -89.624 -21.969 144.293 1.00 34.81 C ANISOU 5350 CA GLY C 146 2852 3593 6781 -165 -153 351 C ATOM 5351 C GLY C 146 -88.233 -22.491 144.574 1.00 29.38 C ANISOU 5351 C GLY C 146 2280 2712 6173 26 -14 298 C ATOM 5352 O GLY C 146 -87.424 -22.717 143.674 1.00 25.49 O ANISOU 5352 O GLY C 146 2090 2065 5531 300 44 254 O ATOM 5353 N CYS C 147 -87.979 -22.709 145.859 1.00 33.25 N ANISOU 5353 N CYS C 147 2804 3213 6616 -52 48 295 N ATOM 5354 CA CYS C 147 -86.752 -23.347 146.308 1.00 27.30 C ANISOU 5354 CA CYS C 147 2118 2318 5937 118 121 273 C ATOM 5355 C CYS C 147 -87.082 -24.296 147.444 1.00 27.14 C ANISOU 5355 C CYS C 147 2215 2207 5893 -82 22 312 C ATOM 5356 O CYS C 147 -87.726 -23.904 148.423 1.00 26.52 O ANISOU 5356 O CYS C 147 2032 2307 5735 -208 49 337 O ATOM 5357 CB CYS C 147 -85.710 -22.314 146.752 1.00 21.94 C ANISOU 5357 CB CYS C 147 1545 1852 4939 163 277 221 C ATOM 5358 SG CYS C 147 -84.700 -21.714 145.388 1.00 39.50 S ANISOU 5358 SG CYS C 147 3891 4162 6955 349 415 193 S ATOM 5359 N LEU C 148 -86.648 -25.543 147.294 1.00 29.70 N ANISOU 5359 N LEU C 148 2972 2265 6048 -3 -48 308 N ATOM 5360 CA LEU C 148 -86.851 -26.588 148.284 1.00 33.47 C ANISOU 5360 CA LEU C 148 3691 2582 6445 -140 -89 369 C ATOM 5361 C LEU C 148 -85.556 -26.766 149.068 1.00 37.01 C ANISOU 5361 C LEU C 148 4163 3044 6854 199 -13 412 C ATOM 5362 O LEU C 148 -84.499 -27.013 148.478 1.00 41.03 O ANISOU 5362 O LEU C 148 4800 3471 7317 527 36 399 O ATOM 5363 CB LEU C 148 -87.273 -27.885 147.594 1.00 30.66 C ANISOU 5363 CB LEU C 148 3846 1875 5929 -283 -199 338 C ATOM 5364 CG LEU C 148 -87.287 -29.201 148.366 1.00 35.73 C ANISOU 5364 CG LEU C 148 4902 2214 6459 -354 -168 410 C ATOM 5365 CD1 LEU C 148 -88.242 -29.116 149.541 1.00 40.77 C ANISOU 5365 CD1 LEU C 148 5344 2955 7193 -668 -123 498 C ATOM 5366 CD2 LEU C 148 -87.677 -30.334 147.436 1.00 34.17 C ANISOU 5366 CD2 LEU C 148 5230 1646 6105 -521 -254 320 C ATOM 5367 N VAL C 149 -85.632 -26.633 150.387 1.00 32.74 N ANISOU 5367 N VAL C 149 3501 2627 6313 142 -2 470 N ATOM 5368 CA VAL C 149 -84.472 -26.733 151.262 1.00 26.18 C ANISOU 5368 CA VAL C 149 2648 1880 5420 454 -20 508 C ATOM 5369 C VAL C 149 -84.633 -28.033 152.033 1.00 28.85 C ANISOU 5369 C VAL C 149 3441 1977 5544 468 -34 641 C ATOM 5370 O VAL C 149 -85.524 -28.151 152.882 1.00 43.57 O ANISOU 5370 O VAL C 149 5384 3820 7352 220 10 704 O ATOM 5371 CB VAL C 149 -84.376 -25.528 152.207 1.00 34.63 C ANISOU 5371 CB VAL C 149 3310 3270 6578 407 -20 450 C ATOM 5372 CG1 VAL C 149 -83.105 -25.580 153.021 1.00 42.36 C ANISOU 5372 CG1 VAL C 149 4218 4382 7493 723 -138 452 C ATOM 5373 CG2 VAL C 149 -84.468 -24.228 151.423 1.00 26.80 C ANISOU 5373 CG2 VAL C 149 1994 2462 5725 299 73 326 C ATOM 5374 N LYS C 150 -83.779 -29.012 151.747 1.00 30.93 N ANISOU 5374 N LYS C 150 4029 2028 5696 783 -33 710 N ATOM 5375 CA LYS C 150 -83.993 -30.380 152.202 1.00 36.21 C ANISOU 5375 CA LYS C 150 5240 2358 6162 807 22 850 C ATOM 5376 C LYS C 150 -82.804 -30.882 153.007 1.00 38.88 C ANISOU 5376 C LYS C 150 5693 2730 6350 1285 -19 996 C ATOM 5377 O LYS C 150 -81.650 -30.685 152.606 1.00 44.37 O ANISOU 5377 O LYS C 150 6185 3578 7096 1625 -77 965 O ATOM 5378 CB LYS C 150 -84.246 -31.306 151.008 1.00 38.67 C ANISOU 5378 CB LYS C 150 5983 2273 6437 735 95 812 C ATOM 5379 CG LYS C 150 -84.859 -32.644 151.371 1.00 47.90 C ANISOU 5379 CG LYS C 150 7686 3083 7433 557 170 890 C ATOM 5380 CD LYS C 150 -85.382 -33.349 150.133 1.00 53.67 C ANISOU 5380 CD LYS C 150 8663 3581 8149 304 152 744 C ATOM 5381 CE LYS C 150 -86.142 -34.609 150.498 1.00 64.03 C ANISOU 5381 CE LYS C 150 10333 4609 9386 40 250 781 C ATOM 5382 NZ LYS C 150 -85.354 -35.470 151.421 1.00 73.69 N ANISOU 5382 NZ LYS C 150 11826 5755 10416 392 386 956 N ATOM 5383 N GLY C 151 -83.088 -31.522 154.139 1.00 38.66 N ANISOU 5383 N GLY C 151 5975 2602 6111 1303 9 1148 N ATOM 5384 CA GLY C 151 -82.096 -32.351 154.795 1.00 49.55 C ANISOU 5384 CA GLY C 151 7623 3924 7280 1787 -25 1336 C ATOM 5385 C GLY C 151 -81.091 -31.620 155.653 1.00 46.29 C ANISOU 5385 C GLY C 151 6812 3945 6829 2123 -274 1351 C ATOM 5386 O GLY C 151 -79.914 -31.998 155.674 1.00 50.68 O ANISOU 5386 O GLY C 151 7260 4634 7362 2456 -393 1388 O ATOM 5387 N TYR C 152 -81.513 -30.579 156.362 1.00 40.91 N ANISOU 5387 N TYR C 152 5825 3571 6149 1877 -383 1234 N ATOM 5388 CA TYR C 152 -80.604 -29.800 157.187 1.00 41.93 C ANISOU 5388 CA TYR C 152 5579 4122 6231 2106 -674 1175 C ATOM 5389 C TYR C 152 -80.930 -29.994 158.662 1.00 44.65 C ANISOU 5389 C TYR C 152 6257 4523 6184 2157 -751 1286 C ATOM 5390 O TYR C 152 -81.991 -30.502 159.035 1.00 45.00 O ANISOU 5390 O TYR C 152 6737 4295 6067 1943 -506 1395 O ATOM 5391 CB TYR C 152 -80.660 -28.313 156.818 1.00 38.49 C ANISOU 5391 CB TYR C 152 4560 3981 6085 1816 -730 911 C ATOM 5392 CG TYR C 152 -81.987 -27.642 157.089 1.00 36.04 C ANISOU 5392 CG TYR C 152 4273 3655 5765 1352 -567 821 C ATOM 5393 CD1 TYR C 152 -82.994 -27.641 156.133 1.00 37.90 C ANISOU 5393 CD1 TYR C 152 4532 3683 6187 1024 -336 796 C ATOM 5394 CD2 TYR C 152 -82.226 -26.993 158.294 1.00 36.93 C ANISOU 5394 CD2 TYR C 152 4385 3969 5679 1264 -648 764 C ATOM 5395 CE1 TYR C 152 -84.206 -27.023 156.375 1.00 37.51 C ANISOU 5395 CE1 TYR C 152 4426 3643 6183 639 -179 753 C ATOM 5396 CE2 TYR C 152 -83.434 -26.374 158.544 1.00 43.79 C ANISOU 5396 CE2 TYR C 152 5270 4802 6567 887 -426 716 C ATOM 5397 CZ TYR C 152 -84.419 -26.390 157.581 1.00 40.49 C ANISOU 5397 CZ TYR C 152 4794 4195 6396 584 -186 727 C ATOM 5398 OH TYR C 152 -85.622 -25.774 157.827 1.00 39.31 O ANISOU 5398 OH TYR C 152 4587 4032 6317 246 42 716 O ATOM 5399 N PHE C 153 -79.986 -29.570 159.506 1.00 25.16 N ANISOU 5399 N PHE C 153 3854 2867 2840 -696 -720 -1175 N ATOM 5400 CA PHE C 153 -80.150 -29.573 160.950 1.00 29.40 C ANISOU 5400 CA PHE C 153 4132 3469 3568 -786 -532 -1250 C ATOM 5401 C PHE C 153 -79.066 -28.689 161.536 1.00 30.96 C ANISOU 5401 C PHE C 153 4283 3840 3639 -659 -170 -1252 C ATOM 5402 O PHE C 153 -77.914 -28.773 161.089 1.00 34.84 O ANISOU 5402 O PHE C 153 4911 4376 3951 -478 -227 -1192 O ATOM 5403 CB PHE C 153 -80.062 -30.990 161.532 1.00 37.86 C ANISOU 5403 CB PHE C 153 5293 4446 4646 -764 -776 -1201 C ATOM 5404 CG PHE C 153 -80.392 -31.066 162.997 1.00 37.73 C ANISOU 5404 CG PHE C 153 5094 4550 4691 -1044 -450 -1210 C ATOM 5405 CD1 PHE C 153 -79.426 -30.806 163.957 1.00 28.96 C ANISOU 5405 CD1 PHE C 153 4034 3582 3388 -920 -121 -1224 C ATOM 5406 CD2 PHE C 153 -81.675 -31.379 163.414 1.00 43.81 C ANISOU 5406 CD2 PHE C 153 5565 5293 5787 -1453 -493 -1108 C ATOM 5407 CE1 PHE C 153 -79.731 -30.867 165.302 1.00 30.02 C ANISOU 5407 CE1 PHE C 153 4088 3810 3509 -1122 199 -1294 C ATOM 5408 CE2 PHE C 153 -81.985 -31.442 164.759 1.00 45.83 C ANISOU 5408 CE2 PHE C 153 5608 5710 6093 -1711 -91 -1089 C ATOM 5409 CZ PHE C 153 -81.011 -31.187 165.703 1.00 35.11 C ANISOU 5409 CZ PHE C 153 4499 4461 4379 -1525 281 -1324 C ATOM 5410 N PRO C 154 -79.379 -27.841 162.527 1.00 29.21 N ANISOU 5410 N PRO C 154 3904 3687 3506 -785 166 -1336 N ATOM 5411 CA PRO C 154 -80.705 -27.652 163.123 1.00 29.34 C ANISOU 5411 CA PRO C 154 3729 3693 3728 -1016 411 -1516 C ATOM 5412 C PRO C 154 -81.574 -26.630 162.396 1.00 33.58 C ANISOU 5412 C PRO C 154 4057 4174 4526 -1045 504 -1616 C ATOM 5413 O PRO C 154 -81.301 -26.262 161.255 1.00 38.70 O ANISOU 5413 O PRO C 154 4732 4807 5163 -934 290 -1576 O ATOM 5414 CB PRO C 154 -80.373 -27.163 164.530 1.00 27.87 C ANISOU 5414 CB PRO C 154 3664 3525 3401 -958 740 -1568 C ATOM 5415 CG PRO C 154 -79.130 -26.377 164.334 1.00 28.60 C ANISOU 5415 CG PRO C 154 3903 3582 3380 -782 562 -1415 C ATOM 5416 CD PRO C 154 -78.341 -27.124 163.285 1.00 25.33 C ANISOU 5416 CD PRO C 154 3486 3220 2919 -713 285 -1274 C ATOM 5417 N GLU C 155 -82.626 -26.188 163.081 1.00 44.55 N ANISOU 5417 N GLU C 155 5209 5616 6104 -936 833 -1394 N ATOM 5418 CA GLU C 155 -83.599 -25.262 162.525 1.00 51.45 C ANISOU 5418 CA GLU C 155 5812 6497 7240 -782 951 -1203 C ATOM 5419 C GLU C 155 -82.979 -23.860 162.443 1.00 53.63 C ANISOU 5419 C GLU C 155 6379 6674 7325 -582 1098 -1482 C ATOM 5420 O GLU C 155 -81.799 -23.656 162.744 1.00 47.12 O ANISOU 5420 O GLU C 155 5906 5767 6229 -630 1029 -1742 O ATOM 5421 CB GLU C 155 -84.871 -25.303 163.376 1.00 59.94 C ANISOU 5421 CB GLU C 155 6512 7740 8522 -615 1324 -751 C ATOM 5422 CG GLU C 155 -86.098 -24.573 162.835 1.00 73.85 C ANISOU 5422 CG GLU C 155 7852 9583 10624 -440 1459 -376 C ATOM 5423 CD GLU C 155 -86.575 -25.125 161.505 1.00 80.21 C ANISOU 5423 CD GLU C 155 8364 10288 11824 -778 895 -172 C ATOM 5424 OE1 GLU C 155 -87.568 -25.882 161.504 1.00 86.91 O ANISOU 5424 OE1 GLU C 155 8738 11208 13076 -972 708 397 O ATOM 5425 OE2 GLU C 155 -85.968 -24.794 160.463 1.00 75.09 O ANISOU 5425 OE2 GLU C 155 7973 9473 11084 -832 594 -516 O ATOM 5426 N SER C 156 -83.793 -22.880 162.036 1.00 52.38 N ANISOU 5426 N SER C 156 6058 6501 7342 -383 1239 -1359 N ATOM 5427 CA SER C 156 -83.350 -21.543 161.630 1.00 48.05 C ANISOU 5427 CA SER C 156 5752 5799 6707 -253 1218 -1558 C ATOM 5428 C SER C 156 -82.473 -21.610 160.374 1.00 47.67 C ANISOU 5428 C SER C 156 5694 5733 6684 -471 837 -1656 C ATOM 5429 O SER C 156 -81.253 -21.446 160.406 1.00 64.57 O ANISOU 5429 O SER C 156 8069 7833 8631 -569 690 -1783 O ATOM 5430 CB SER C 156 -82.631 -20.815 162.774 1.00 66.21 C ANISOU 5430 CB SER C 156 8588 7908 8661 -87 1334 -1790 C ATOM 5431 OG SER C 156 -83.533 -20.474 163.812 1.00 83.67 O ANISOU 5431 OG SER C 156 10926 10129 10736 348 1745 -1686 O ATOM 5432 N VAL C 157 -83.148 -21.879 159.259 1.00 44.53 N ANISOU 5432 N VAL C 157 5007 5385 6527 -503 664 -1505 N ATOM 5433 CA VAL C 157 -82.664 -21.538 157.925 1.00 40.94 C ANISOU 5433 CA VAL C 157 4553 4923 6079 -501 404 -1533 C ATOM 5434 C VAL C 157 -83.367 -20.262 157.482 1.00 34.77 C ANISOU 5434 C VAL C 157 3642 4069 5501 -364 513 -1472 C ATOM 5435 O VAL C 157 -84.558 -20.072 157.757 1.00 38.42 O ANISOU 5435 O VAL C 157 3892 4531 6176 -263 697 -1319 O ATOM 5436 CB VAL C 157 -82.916 -22.697 156.937 1.00 42.69 C ANISOU 5436 CB VAL C 157 4728 5155 6338 -546 36 -1451 C ATOM 5437 CG1 VAL C 157 -83.276 -22.180 155.554 1.00 42.49 C ANISOU 5437 CG1 VAL C 157 4627 5082 6435 -424 -168 -1383 C ATOM 5438 CG2 VAL C 157 -81.697 -23.606 156.862 1.00 49.28 C ANISOU 5438 CG2 VAL C 157 5845 6064 6814 -527 -133 -1560 C ATOM 5439 N THR C 158 -82.639 -19.379 156.797 1.00 36.42 N ANISOU 5439 N THR C 158 3935 4245 5657 -337 406 -1510 N ATOM 5440 CA THR C 158 -83.207 -18.137 156.285 1.00 37.32 C ANISOU 5440 CA THR C 158 3970 4260 5951 -217 449 -1465 C ATOM 5441 C THR C 158 -83.181 -18.144 154.763 1.00 47.85 C ANISOU 5441 C THR C 158 5139 5669 7372 -184 221 -1362 C ATOM 5442 O THR C 158 -82.133 -18.376 154.159 1.00 56.92 O ANISOU 5442 O THR C 158 6349 6939 8341 -174 70 -1306 O ATOM 5443 CB THR C 158 -82.437 -16.922 156.811 1.00 32.96 C ANISOU 5443 CB THR C 158 3709 3522 5293 -222 423 -1534 C ATOM 5444 OG1 THR C 158 -82.199 -17.074 158.216 1.00 49.97 O ANISOU 5444 OG1 THR C 158 6181 5558 7247 -212 536 -1665 O ATOM 5445 CG2 THR C 158 -83.220 -15.640 156.562 1.00 34.23 C ANISOU 5445 CG2 THR C 158 3899 3508 5599 -39 478 -1526 C ATOM 5446 N VAL C 159 -84.327 -17.874 154.146 1.00 46.90 N ANISOU 5446 N VAL C 159 4813 5503 7503 -104 210 -1277 N ATOM 5447 CA VAL C 159 -84.470 -17.914 152.693 1.00 38.24 C ANISOU 5447 CA VAL C 159 3637 4423 6469 -24 -48 -1194 C ATOM 5448 C VAL C 159 -84.913 -16.538 152.219 1.00 35.92 C ANISOU 5448 C VAL C 159 3225 4055 6367 66 35 -1147 C ATOM 5449 O VAL C 159 -85.940 -16.021 152.675 1.00 45.39 O ANISOU 5449 O VAL C 159 4289 5180 7777 118 219 -1105 O ATOM 5450 CB VAL C 159 -85.457 -19.001 152.241 1.00 36.16 C ANISOU 5450 CB VAL C 159 3283 4090 6366 -70 -328 -1092 C ATOM 5451 CG1 VAL C 159 -85.534 -19.043 150.725 1.00 35.88 C ANISOU 5451 CG1 VAL C 159 3348 3988 6298 87 -686 -1051 C ATOM 5452 CG2 VAL C 159 -85.027 -20.353 152.782 1.00 37.88 C ANISOU 5452 CG2 VAL C 159 3683 4321 6388 -171 -474 -1140 C ATOM 5453 N THR C 160 -84.146 -15.949 151.305 1.00 33.42 N ANISOU 5453 N THR C 160 2942 3793 5962 139 -79 -1086 N ATOM 5454 CA THR C 160 -84.513 -14.675 150.699 1.00 39.73 C ANISOU 5454 CA THR C 160 3640 4507 6947 208 -70 -1020 C ATOM 5455 C THR C 160 -84.416 -14.782 149.185 1.00 39.56 C ANISOU 5455 C THR C 160 3560 4588 6886 378 -273 -891 C ATOM 5456 O THR C 160 -83.737 -15.654 148.647 1.00 36.95 O ANISOU 5456 O THR C 160 3352 4408 6281 523 -399 -834 O ATOM 5457 CB THR C 160 -83.626 -13.519 151.191 1.00 28.58 C ANISOU 5457 CB THR C 160 2352 3006 5502 116 -62 -976 C ATOM 5458 OG1 THR C 160 -82.270 -13.742 150.783 1.00 29.73 O ANISOU 5458 OG1 THR C 160 2467 3352 5477 69 -188 -754 O ATOM 5459 CG2 THR C 160 -83.691 -13.391 152.708 1.00 29.45 C ANISOU 5459 CG2 THR C 160 2714 2932 5542 53 68 -1146 C ATOM 5460 N TRP C 161 -85.133 -13.904 148.494 1.00 43.13 N ANISOU 5460 N TRP C 161 3883 4948 7555 447 -298 -842 N ATOM 5461 CA TRP C 161 -85.195 -13.930 147.038 1.00 37.68 C ANISOU 5461 CA TRP C 161 3188 4315 6813 666 -498 -729 C ATOM 5462 C TRP C 161 -84.560 -12.661 146.492 1.00 29.88 C ANISOU 5462 C TRP C 161 2092 3402 5856 718 -446 -537 C ATOM 5463 O TRP C 161 -84.978 -11.553 146.845 1.00 30.95 O ANISOU 5463 O TRP C 161 2151 3374 6235 594 -380 -563 O ATOM 5464 CB TRP C 161 -86.636 -14.090 146.557 1.00 30.67 C ANISOU 5464 CB TRP C 161 2209 3243 6200 671 -665 -757 C ATOM 5465 CG TRP C 161 -87.183 -15.437 146.901 1.00 36.75 C ANISOU 5465 CG TRP C 161 3055 3920 6987 570 -880 -787 C ATOM 5466 CD1 TRP C 161 -87.742 -15.815 148.086 1.00 31.71 C ANISOU 5466 CD1 TRP C 161 2254 3258 6535 360 -733 -771 C ATOM 5467 CD2 TRP C 161 -87.189 -16.600 146.066 1.00 37.58 C ANISOU 5467 CD2 TRP C 161 3479 3911 6886 705 -1345 -790 C ATOM 5468 NE1 TRP C 161 -88.110 -17.137 148.036 1.00 32.91 N ANISOU 5468 NE1 TRP C 161 2504 3299 6700 255 -1102 -709 N ATOM 5469 CE2 TRP C 161 -87.782 -17.642 146.806 1.00 33.51 C ANISOU 5469 CE2 TRP C 161 2943 3263 6524 458 -1540 -757 C ATOM 5470 CE3 TRP C 161 -86.759 -16.859 144.762 1.00 42.15 C ANISOU 5470 CE3 TRP C 161 4432 4463 7119 1081 -1649 -791 C ATOM 5471 CZ2 TRP C 161 -87.957 -18.922 146.285 1.00 35.60 C ANISOU 5471 CZ2 TRP C 161 3594 3282 6649 489 -2144 -749 C ATOM 5472 CZ3 TRP C 161 -86.935 -18.131 144.247 1.00 49.16 C ANISOU 5472 CZ3 TRP C 161 5804 5105 7771 1230 -2206 -838 C ATOM 5473 CH2 TRP C 161 -87.527 -19.146 145.007 1.00 52.15 C ANISOU 5473 CH2 TRP C 161 6196 5268 8348 894 -2506 -830 C ATOM 5474 N ASN C 162 -83.557 -12.830 145.629 1.00 40.70 N ANISOU 5474 N ASN C 162 3476 5029 6958 956 -490 -282 N ATOM 5475 CA ASN C 162 -82.760 -11.723 145.104 1.00 36.99 C ANISOU 5475 CA ASN C 162 2801 4714 6541 982 -465 93 C ATOM 5476 C ASN C 162 -82.230 -10.847 146.235 1.00 40.77 C ANISOU 5476 C ASN C 162 3212 5048 7230 582 -480 170 C ATOM 5477 O ASN C 162 -82.421 -9.629 146.259 1.00 43.24 O ANISOU 5477 O ASN C 162 3477 5155 7799 418 -586 240 O ATOM 5478 CB ASN C 162 -83.559 -10.902 144.091 1.00 32.45 C ANISOU 5478 CB ASN C 162 2144 4035 6150 1105 -536 114 C ATOM 5479 CG ASN C 162 -83.757 -11.635 142.781 1.00 33.36 C ANISOU 5479 CG ASN C 162 2472 4295 5907 1546 -610 155 C ATOM 5480 OD1 ASN C 162 -83.093 -12.636 142.511 1.00 34.00 O ANISOU 5480 OD1 ASN C 162 2731 4569 5619 1875 -611 254 O ATOM 5481 ND2 ASN C 162 -84.671 -11.139 141.957 1.00 37.23 N ANISOU 5481 ND2 ASN C 162 3026 4651 6468 1586 -688 100 N ATOM 5482 N SER C 163 -81.567 -11.495 147.195 1.00 42.78 N ANISOU 5482 N SER C 163 3554 5351 7351 439 -447 142 N ATOM 5483 CA SER C 163 -80.900 -10.838 148.318 1.00 41.55 C ANISOU 5483 CA SER C 163 3461 5004 7324 75 -583 235 C ATOM 5484 C SER C 163 -81.850 -9.980 149.146 1.00 40.15 C ANISOU 5484 C SER C 163 3561 4364 7331 -63 -643 -128 C ATOM 5485 O SER C 163 -81.407 -9.099 149.889 1.00 53.48 O ANISOU 5485 O SER C 163 5464 5745 9113 -300 -904 -57 O ATOM 5486 CB SER C 163 -79.714 -9.994 147.837 1.00 53.88 C ANISOU 5486 CB SER C 163 4737 6722 9014 -63 -798 888 C ATOM 5487 OG SER C 163 -78.763 -10.794 147.157 1.00 65.77 O ANISOU 5487 OG SER C 163 5966 8748 10275 209 -647 1342 O ATOM 5488 N GLY C 164 -83.154 -10.217 149.033 1.00 31.96 N ANISOU 5488 N GLY C 164 2561 3253 6328 128 -453 -455 N ATOM 5489 CA GLY C 164 -84.149 -9.452 149.754 1.00 33.34 C ANISOU 5489 CA GLY C 164 2968 3092 6606 184 -394 -712 C ATOM 5490 C GLY C 164 -84.968 -8.518 148.892 1.00 34.36 C ANISOU 5490 C GLY C 164 2997 3126 6934 324 -415 -682 C ATOM 5491 O GLY C 164 -85.965 -7.969 149.379 1.00 39.80 O ANISOU 5491 O GLY C 164 3847 3603 7672 504 -289 -860 O ATOM 5492 N SER C 165 -84.580 -8.315 147.632 1.00 37.54 N ANISOU 5492 N SER C 165 5763 1864 6636 -135 -593 -704 N ATOM 5493 CA SER C 165 -85.293 -7.371 146.778 1.00 46.78 C ANISOU 5493 CA SER C 165 7117 2868 7789 -29 -585 -636 C ATOM 5494 C SER C 165 -86.708 -7.848 146.476 1.00 48.08 C ANISOU 5494 C SER C 165 7153 3150 7966 323 -451 -633 C ATOM 5495 O SER C 165 -87.639 -7.038 146.412 1.00 57.35 O ANISOU 5495 O SER C 165 8515 4186 9090 542 -398 -627 O ATOM 5496 CB SER C 165 -84.514 -7.150 145.483 1.00 47.48 C ANISOU 5496 CB SER C 165 7132 2948 7962 -293 -690 -467 C ATOM 5497 OG SER C 165 -83.198 -6.701 145.750 1.00 56.07 O ANISOU 5497 OG SER C 165 8294 3988 9023 -669 -839 -406 O ATOM 5498 N LEU C 166 -86.892 -9.153 146.288 1.00 43.63 N ANISOU 5498 N LEU C 166 6257 2845 7476 374 -398 -619 N ATOM 5499 CA LEU C 166 -88.220 -9.732 146.117 1.00 41.61 C ANISOU 5499 CA LEU C 166 5839 2741 7230 638 -307 -590 C ATOM 5500 C LEU C 166 -88.762 -10.098 147.493 1.00 41.46 C ANISOU 5500 C LEU C 166 5799 2805 7147 817 -232 -678 C ATOM 5501 O LEU C 166 -88.292 -11.053 148.120 1.00 42.54 O ANISOU 5501 O LEU C 166 5762 3083 7317 732 -225 -724 O ATOM 5502 CB LEU C 166 -88.166 -10.953 145.202 1.00 40.21 C ANISOU 5502 CB LEU C 166 5355 2766 7155 564 -308 -524 C ATOM 5503 CG LEU C 166 -87.768 -10.713 143.744 1.00 38.04 C ANISOU 5503 CG LEU C 166 5068 2438 6948 444 -367 -427 C ATOM 5504 CD1 LEU C 166 -87.684 -12.036 143.001 1.00 32.95 C ANISOU 5504 CD1 LEU C 166 4177 1971 6370 413 -360 -402 C ATOM 5505 CD2 LEU C 166 -88.741 -9.766 143.057 1.00 37.83 C ANISOU 5505 CD2 LEU C 166 5176 2291 6907 589 -377 -346 C ATOM 5506 N SER C 167 -89.751 -9.340 147.963 1.00 45.46 N ANISOU 5506 N SER C 167 6478 3229 7566 1095 -162 -689 N ATOM 5507 CA SER C 167 -90.336 -9.575 149.277 1.00 48.79 C ANISOU 5507 CA SER C 167 6882 3741 7916 1321 -70 -758 C ATOM 5508 C SER C 167 -91.855 -9.671 149.200 1.00 48.60 C ANISOU 5508 C SER C 167 6709 3878 7878 1670 34 -648 C ATOM 5509 O SER C 167 -92.482 -10.358 150.013 1.00 43.87 O ANISOU 5509 O SER C 167 5907 3497 7264 1839 103 -631 O ATOM 5510 CB SER C 167 -89.925 -8.464 150.245 1.00 61.18 C ANISOU 5510 CB SER C 167 8808 5059 9379 1353 -51 -891 C ATOM 5511 OG SER C 167 -90.231 -7.187 149.712 1.00 69.77 O ANISOU 5511 OG SER C 167 10133 5906 10471 1428 -40 -870 O ATOM 5512 N SER C 168 -92.447 -8.981 148.223 1.00 52.69 N ANISOU 5512 N SER C 168 7298 4316 8408 1782 41 -546 N ATOM 5513 CA SER C 168 -93.898 -8.826 148.183 1.00 51.73 C ANISOU 5513 CA SER C 168 7038 4347 8270 2154 157 -405 C ATOM 5514 C SER C 168 -94.601 -10.164 147.984 1.00 53.75 C ANISOU 5514 C SER C 168 6870 4963 8589 2156 94 -298 C ATOM 5515 O SER C 168 -95.480 -10.540 148.769 1.00 61.00 O ANISOU 5515 O SER C 168 7586 6144 9446 2408 160 -235 O ATOM 5516 CB SER C 168 -94.284 -7.846 147.075 1.00 50.85 C ANISOU 5516 CB SER C 168 7044 4067 8211 2227 162 -300 C ATOM 5517 OG SER C 168 -93.689 -6.578 147.288 1.00 52.40 O ANISOU 5517 OG SER C 168 7533 3910 8468 2148 150 -423 O ATOM 5518 N SER C 169 -94.230 -10.898 146.935 1.00 43.29 N ANISOU 5518 N SER C 169 5378 3653 7418 1850 -15 -254 N ATOM 5519 CA SER C 169 -94.926 -12.118 146.543 1.00 39.90 C ANISOU 5519 CA SER C 169 4564 3472 7125 1773 -60 -108 C ATOM 5520 C SER C 169 -94.244 -13.376 147.069 1.00 43.31 C ANISOU 5520 C SER C 169 4855 3961 7642 1522 -92 -168 C ATOM 5521 O SER C 169 -94.258 -14.413 146.398 1.00 48.19 O ANISOU 5521 O SER C 169 5289 4625 8394 1325 -186 -95 O ATOM 5522 CB SER C 169 -95.052 -12.188 145.022 1.00 49.57 C ANISOU 5522 CB SER C 169 5730 4645 8459 1635 -160 -6 C ATOM 5523 OG SER C 169 -93.827 -12.590 144.435 1.00 60.97 O ANISOU 5523 OG SER C 169 7268 5941 9957 1326 -230 -113 O ATOM 5524 N VAL C 170 -93.644 -13.310 148.254 1.00 43.46 N ANISOU 5524 N VAL C 170 4981 3955 7578 1542 -31 -298 N ATOM 5525 CA VAL C 170 -92.892 -14.430 148.807 1.00 37.07 C ANISOU 5525 CA VAL C 170 4062 3188 6836 1327 -60 -356 C ATOM 5526 C VAL C 170 -93.731 -15.133 149.865 1.00 37.61 C ANISOU 5526 C VAL C 170 3872 3505 6915 1468 -7 -255 C ATOM 5527 O VAL C 170 -94.358 -14.490 150.716 1.00 39.18 O ANISOU 5527 O VAL C 170 4084 3821 6982 1756 96 -244 O ATOM 5528 CB VAL C 170 -91.548 -13.957 149.394 1.00 31.37 C ANISOU 5528 CB VAL C 170 3584 2304 6031 1211 -52 -535 C ATOM 5529 CG1 VAL C 170 -90.823 -15.107 150.077 1.00 29.88 C ANISOU 5529 CG1 VAL C 170 3260 2192 5899 1048 -69 -577 C ATOM 5530 CG2 VAL C 170 -90.679 -13.346 148.307 1.00 35.50 C ANISOU 5530 CG2 VAL C 170 4285 2653 6549 1036 -115 -568 C ATOM 5531 N HIS C 171 -93.738 -16.462 149.805 1.00 41.09 N ANISOU 5531 N HIS C 171 4085 4036 7492 1278 -86 -164 N ATOM 5532 CA HIS C 171 -94.301 -17.328 150.831 1.00 32.25 C ANISOU 5532 CA HIS C 171 2695 3167 6391 1308 -66 -27 C ATOM 5533 C HIS C 171 -93.195 -18.241 151.337 1.00 36.42 C ANISOU 5533 C HIS C 171 3278 3610 6951 1090 -111 -134 C ATOM 5534 O HIS C 171 -92.490 -18.864 150.538 1.00 41.43 O ANISOU 5534 O HIS C 171 3996 4081 7663 883 -213 -183 O ATOM 5535 CB HIS C 171 -95.466 -18.165 150.291 1.00 33.23 C ANISOU 5535 CB HIS C 171 2537 3532 6556 1195 -172 264 C ATOM 5536 CG HIS C 171 -96.666 -17.360 149.898 1.00 41.10 C ANISOU 5536 CG HIS C 171 3396 4719 7503 1434 -122 436 C ATOM 5537 ND1 HIS C 171 -97.435 -16.676 150.813 1.00 37.70 N ANISOU 5537 ND1 HIS C 171 2879 4563 6880 1760 33 504 N ATOM 5538 CD2 HIS C 171 -97.238 -17.143 148.690 1.00 47.75 C ANISOU 5538 CD2 HIS C 171 4200 5554 8388 1401 -208 554 C ATOM 5539 CE1 HIS C 171 -98.424 -16.065 150.186 1.00 59.56 C ANISOU 5539 CE1 HIS C 171 5569 7489 9572 1924 43 648 C ATOM 5540 NE2 HIS C 171 -98.328 -16.332 148.896 1.00 38.47 N ANISOU 5540 NE2 HIS C 171 2902 4654 7062 1705 -99 702 N ATOM 5541 N THR C 172 -93.039 -18.319 152.654 1.00 34.93 N ANISOU 5541 N THR C 172 3045 3551 6677 1172 -28 -162 N ATOM 5542 CA THR C 172 -92.055 -19.200 153.271 1.00 36.29 C ANISOU 5542 CA THR C 172 3235 3689 6865 995 -64 -227 C ATOM 5543 C THR C 172 -92.794 -20.215 154.126 1.00 35.38 C ANISOU 5543 C THR C 172 2860 3857 6725 952 -79 -6 C ATOM 5544 O THR C 172 -93.558 -19.836 155.021 1.00 44.81 O ANISOU 5544 O THR C 172 3912 5313 7802 1151 28 87 O ATOM 5545 CB THR C 172 -91.052 -18.409 154.115 1.00 42.18 C ANISOU 5545 CB THR C 172 4173 4338 7517 1072 17 -445 C ATOM 5546 OG1 THR C 172 -90.133 -17.726 153.254 1.00 49.67 O ANISOU 5546 OG1 THR C 172 5345 5026 8504 992 -20 -598 O ATOM 5547 CG2 THR C 172 -90.275 -19.343 155.031 1.00 29.08 C ANISOU 5547 CG2 THR C 172 2452 2756 5840 941 -1 -449 C ATOM 5548 N PHE C 173 -92.581 -21.500 153.844 1.00 32.67 N ANISOU 5548 N PHE C 173 2474 3467 6471 708 -218 94 N ATOM 5549 CA PHE C 173 -93.385 -22.436 154.610 1.00 35.83 C ANISOU 5549 CA PHE C 173 2630 4133 6851 620 -266 360 C ATOM 5550 C PHE C 173 -92.568 -23.025 155.752 1.00 38.62 C ANISOU 5550 C PHE C 173 2992 4516 7164 578 -241 317 C ATOM 5551 O PHE C 173 -91.374 -23.298 155.583 1.00 38.20 O ANISOU 5551 O PHE C 173 3127 4235 7153 511 -272 145 O ATOM 5552 CB PHE C 173 -93.903 -23.557 153.709 1.00 32.10 C ANISOU 5552 CB PHE C 173 2123 3592 6482 346 -486 557 C ATOM 5553 CG PHE C 173 -94.689 -23.062 152.525 1.00 35.18 C ANISOU 5553 CG PHE C 173 2495 3970 6902 350 -540 618 C ATOM 5554 CD1 PHE C 173 -94.047 -22.725 151.343 1.00 31.16 C ANISOU 5554 CD1 PHE C 173 2230 3165 6444 344 -577 414 C ATOM 5555 CD2 PHE C 173 -96.063 -22.916 152.599 1.00 34.86 C ANISOU 5555 CD2 PHE C 173 2163 4265 6817 372 -549 910 C ATOM 5556 CE1 PHE C 173 -94.764 -22.262 150.256 1.00 31.76 C ANISOU 5556 CE1 PHE C 173 2287 3243 6536 346 -632 481 C ATOM 5557 CE2 PHE C 173 -96.784 -22.450 151.516 1.00 35.55 C ANISOU 5557 CE2 PHE C 173 2212 4372 6924 381 -605 990 C ATOM 5558 CZ PHE C 173 -96.135 -22.125 150.343 1.00 33.91 C ANISOU 5558 CZ PHE C 173 2277 3832 6776 362 -651 766 C ATOM 5559 N PRO C 174 -93.187 -23.209 156.918 1.00 32.91 N ANISOU 5559 N PRO C 174 2047 4116 6340 639 -176 496 N ATOM 5560 CA PRO C 174 -92.450 -23.747 158.067 1.00 40.93 C ANISOU 5560 CA PRO C 174 3057 5195 7300 605 -151 477 C ATOM 5561 C PRO C 174 -91.902 -25.137 157.784 1.00 43.74 C ANISOU 5561 C PRO C 174 3484 5356 7779 341 -334 561 C ATOM 5562 O PRO C 174 -92.464 -25.909 157.004 1.00 43.45 O ANISOU 5562 O PRO C 174 3442 5228 7839 150 -505 728 O ATOM 5563 CB PRO C 174 -93.500 -23.781 159.186 1.00 39.79 C ANISOU 5563 CB PRO C 174 2612 5494 7011 709 -62 731 C ATOM 5564 CG PRO C 174 -94.815 -23.598 158.514 1.00 36.77 C ANISOU 5564 CG PRO C 174 2036 5294 6642 729 -86 956 C ATOM 5565 CD PRO C 174 -94.564 -22.826 157.266 1.00 35.27 C ANISOU 5565 CD PRO C 174 2070 4792 6538 786 -98 733 C ATOM 5566 N ALA C 175 -90.787 -25.447 158.436 1.00 42.90 N ANISOU 5566 N ALA C 175 3472 5180 7649 342 -313 446 N ATOM 5567 CA ALA C 175 -90.084 -26.691 158.184 1.00 40.78 C ANISOU 5567 CA ALA C 175 3329 4691 7473 181 -467 488 C ATOM 5568 C ALA C 175 -90.722 -27.834 158.964 1.00 44.12 C ANISOU 5568 C ALA C 175 3597 5267 7898 14 -582 804 C ATOM 5569 O ALA C 175 -91.390 -27.635 159.982 1.00 48.56 O ANISOU 5569 O ALA C 175 3916 6175 8358 49 -496 971 O ATOM 5570 CB ALA C 175 -88.609 -26.563 158.561 1.00 36.15 C ANISOU 5570 CB ALA C 175 2867 4019 6847 268 -397 282 C ATOM 5571 N LEU C 176 -90.504 -29.049 158.468 1.00 40.30 N ANISOU 5571 N LEU C 176 3280 4519 7514 -158 -787 897 N ATOM 5572 CA LEU C 176 -91.022 -30.249 159.101 1.00 41.44 C ANISOU 5572 CA LEU C 176 3347 4721 7676 -375 -956 1220 C ATOM 5573 C LEU C 176 -89.931 -31.306 159.117 1.00 41.15 C ANISOU 5573 C LEU C 176 3579 4372 7685 -385 -1074 1169 C ATOM 5574 O LEU C 176 -89.015 -31.289 158.288 1.00 40.31 O ANISOU 5574 O LEU C 176 3726 3984 7606 -255 -1072 925 O ATOM 5575 CB LEU C 176 -92.261 -30.789 158.377 1.00 40.85 C ANISOU 5575 CB LEU C 176 3245 4607 7668 -644 -1178 1482 C ATOM 5576 CG LEU C 176 -93.446 -29.834 158.242 1.00 44.13 C ANISOU 5576 CG LEU C 176 3366 5370 8032 -614 -1077 1594 C ATOM 5577 CD1 LEU C 176 -94.494 -30.436 157.331 1.00 45.67 C ANISOU 5577 CD1 LEU C 176 3565 5492 8296 -920 -1341 1848 C ATOM 5578 CD2 LEU C 176 -94.036 -29.512 159.606 1.00 39.49 C ANISOU 5578 CD2 LEU C 176 2405 5290 7312 -535 -917 1815 C ATOM 5579 N LEU C 177 -90.036 -32.220 160.076 1.00 44.97 N ANISOU 5579 N LEU C 177 3991 4937 8157 -514 -1170 1425 N ATOM 5580 CA LEU C 177 -89.089 -33.316 160.177 1.00 38.08 C ANISOU 5580 CA LEU C 177 3383 3766 7318 -497 -1298 1425 C ATOM 5581 C LEU C 177 -89.368 -34.372 159.116 1.00 49.80 C ANISOU 5581 C LEU C 177 5227 4801 8893 -668 -1596 1491 C ATOM 5582 O LEU C 177 -90.522 -34.658 158.782 1.00 59.13 O ANISOU 5582 O LEU C 177 6376 5976 10115 -951 -1783 1714 O ATOM 5583 CB LEU C 177 -89.139 -33.938 161.571 1.00 39.73 C ANISOU 5583 CB LEU C 177 3414 4202 7480 -586 -1317 1701 C ATOM 5584 CG LEU C 177 -88.257 -33.235 162.606 1.00 38.34 C ANISOU 5584 CG LEU C 177 3055 4326 7187 -357 -1069 1560 C ATOM 5585 CD1 LEU C 177 -88.380 -33.901 163.967 1.00 40.27 C ANISOU 5585 CD1 LEU C 177 3118 4817 7366 -455 -1100 1860 C ATOM 5586 CD2 LEU C 177 -86.805 -33.181 162.148 1.00 36.84 C ANISOU 5586 CD2 LEU C 177 3088 3909 7001 -123 -1007 1275 C ATOM 5587 N GLN C 178 -88.292 -34.948 158.590 1.00 48.44 N ANISOU 5587 N GLN C 178 5408 4270 8726 -482 -1649 1306 N ATOM 5588 CA GLN C 178 -88.344 -35.945 157.528 1.00 65.17 C ANISOU 5588 CA GLN C 178 7986 5892 10883 -552 -1928 1289 C ATOM 5589 C GLN C 178 -87.019 -36.683 157.575 1.00 74.46 C ANISOU 5589 C GLN C 178 9466 6808 12017 -251 -1926 1164 C ATOM 5590 O GLN C 178 -85.963 -36.057 157.421 1.00 79.55 O ANISOU 5590 O GLN C 178 10053 7571 12602 70 -1691 924 O ATOM 5591 CB GLN C 178 -88.569 -35.295 156.162 1.00 71.01 C ANISOU 5591 CB GLN C 178 8845 6515 11621 -509 -1915 1064 C ATOM 5592 CG GLN C 178 -88.624 -36.278 155.004 1.00 80.60 C ANISOU 5592 CG GLN C 178 10553 7330 12743 -542 -2159 972 C ATOM 5593 CD GLN C 178 -88.941 -35.603 153.682 1.00 81.81 C ANISOU 5593 CD GLN C 178 10768 7492 12823 -513 -2117 768 C ATOM 5594 OE1 GLN C 178 -88.568 -34.452 153.453 1.00 72.33 O ANISOU 5594 OE1 GLN C 178 9370 6435 11675 -336 -1896 605 O ATOM 5595 NE2 GLN C 178 -89.638 -36.317 152.805 1.00 86.79 N ANISOU 5595 NE2 GLN C 178 11675 7974 13327 -693 -2343 788 N ATOM 5596 N SER C 179 -87.066 -37.992 157.828 1.00 76.36 N ANISOU 5596 N SER C 179 10015 6725 12273 -354 -2188 1354 N ATOM 5597 CA SER C 179 -85.859 -38.810 157.962 1.00 73.90 C ANISOU 5597 CA SER C 179 9984 6250 11843 -27 -2153 1246 C ATOM 5598 C SER C 179 -84.917 -38.236 159.018 1.00 67.65 C ANISOU 5598 C SER C 179 8837 5795 11070 209 -1905 1263 C ATOM 5599 O SER C 179 -83.694 -38.356 158.916 1.00 73.78 O ANISOU 5599 O SER C 179 9716 6547 11771 585 -1783 1117 O ATOM 5600 CB SER C 179 -85.138 -38.960 156.619 1.00 80.38 C ANISOU 5600 CB SER C 179 11166 6904 12472 283 -2065 901 C ATOM 5601 OG SER C 179 -85.999 -39.507 155.636 1.00 88.05 O ANISOU 5601 OG SER C 179 12440 7665 13351 65 -2265 859 O ATOM 5602 N GLY C 180 -85.488 -37.602 160.040 1.00 51.13 N ANISOU 5602 N GLY C 180 6300 4131 8996 -5 -1791 1421 N ATOM 5603 CA GLY C 180 -84.714 -37.026 161.119 1.00 42.17 C ANISOU 5603 CA GLY C 180 4821 3410 7792 153 -1547 1410 C ATOM 5604 C GLY C 180 -84.078 -35.685 160.829 1.00 49.53 C ANISOU 5604 C GLY C 180 5537 4620 8662 342 -1273 1127 C ATOM 5605 O GLY C 180 -83.334 -35.180 161.677 1.00 63.29 O ANISOU 5605 O GLY C 180 7035 6688 10326 453 -1100 1104 O ATOM 5606 N LEU C 181 -84.352 -35.082 159.674 1.00 45.39 N ANISOU 5606 N LEU C 181 5105 3980 8161 353 -1250 932 N ATOM 5607 CA LEU C 181 -83.785 -33.788 159.320 1.00 42.11 C ANISOU 5607 CA LEU C 181 4517 3792 7692 492 -1022 690 C ATOM 5608 C LEU C 181 -84.902 -32.862 158.865 1.00 44.69 C ANISOU 5608 C LEU C 181 4729 4189 8061 310 -996 638 C ATOM 5609 O LEU C 181 -85.996 -33.305 158.520 1.00 44.68 O ANISOU 5609 O LEU C 181 4812 4037 8128 109 -1163 768 O ATOM 5610 CB LEU C 181 -82.715 -33.919 158.226 1.00 36.70 C ANISOU 5610 CB LEU C 181 4062 2925 6959 781 -988 498 C ATOM 5611 CG LEU C 181 -81.501 -34.784 158.576 1.00 37.28 C ANISOU 5611 CG LEU C 181 4235 2973 6958 1060 -983 552 C ATOM 5612 CD1 LEU C 181 -80.500 -34.793 157.435 1.00 37.68 C ANISOU 5612 CD1 LEU C 181 4461 2938 6918 1395 -911 380 C ATOM 5613 CD2 LEU C 181 -80.845 -34.281 159.851 1.00 36.61 C ANISOU 5613 CD2 LEU C 181 3798 3302 6811 1058 -835 628 C ATOM 5614 N TYR C 182 -84.620 -31.567 158.838 1.00 44.00 N ANISOU 5614 N TYR C 182 4461 4331 7926 373 -804 466 N ATOM 5615 CA TYR C 182 -85.666 -30.608 158.522 1.00 36.71 C ANISOU 5615 CA TYR C 182 3425 3498 7027 256 -760 428 C ATOM 5616 C TYR C 182 -85.766 -30.364 157.023 1.00 36.93 C ANISOU 5616 C TYR C 182 3644 3292 7097 291 -800 278 C ATOM 5617 O TYR C 182 -84.782 -30.452 156.280 1.00 35.80 O ANISOU 5617 O TYR C 182 3659 3020 6924 457 -775 135 O ATOM 5618 CB TYR C 182 -85.423 -29.281 159.244 1.00 35.26 C ANISOU 5618 CB TYR C 182 3026 3618 6754 308 -564 313 C ATOM 5619 CG TYR C 182 -85.625 -29.348 160.739 1.00 36.66 C ANISOU 5619 CG TYR C 182 3001 4076 6851 265 -518 456 C ATOM 5620 CD1 TYR C 182 -86.902 -29.378 161.284 1.00 38.55 C ANISOU 5620 CD1 TYR C 182 3084 4484 7080 158 -535 641 C ATOM 5621 CD2 TYR C 182 -84.542 -29.385 161.606 1.00 38.34 C ANISOU 5621 CD2 TYR C 182 3156 4436 6974 336 -459 434 C ATOM 5622 CE1 TYR C 182 -87.095 -29.442 162.650 1.00 41.99 C ANISOU 5622 CE1 TYR C 182 3325 5224 7406 145 -479 786 C ATOM 5623 CE2 TYR C 182 -84.725 -29.448 162.974 1.00 43.38 C ANISOU 5623 CE2 TYR C 182 3621 5348 7512 301 -421 563 C ATOM 5624 CZ TYR C 182 -86.003 -29.476 163.490 1.00 45.53 C ANISOU 5624 CZ TYR C 182 3755 5780 7764 216 -425 731 C ATOM 5625 OH TYR C 182 -86.190 -29.537 164.852 1.00 54.34 O ANISOU 5625 OH TYR C 182 4688 7214 8745 207 -373 872 O ATOM 5626 N THR C 183 -86.978 -30.032 156.588 1.00 42.93 N ANISOU 5626 N THR C 183 4360 4048 7904 148 -854 336 N ATOM 5627 CA THR C 183 -87.228 -29.664 155.206 1.00 41.10 C ANISOU 5627 CA THR C 183 4276 3641 7700 158 -892 212 C ATOM 5628 C THR C 183 -88.205 -28.500 155.189 1.00 38.03 C ANISOU 5628 C THR C 183 3682 3452 7316 105 -800 221 C ATOM 5629 O THR C 183 -89.138 -28.449 155.994 1.00 45.17 O ANISOU 5629 O THR C 183 4378 4569 8215 9 -798 404 O ATOM 5630 CB THR C 183 -87.787 -30.850 154.406 1.00 52.33 C ANISOU 5630 CB THR C 183 5963 4753 9168 25 -1150 313 C ATOM 5631 OG1 THR C 183 -86.906 -31.971 154.537 1.00 68.89 O ANISOU 5631 OG1 THR C 183 8299 6635 11239 130 -1239 309 O ATOM 5632 CG2 THR C 183 -87.919 -30.496 152.933 1.00 31.84 C ANISOU 5632 CG2 THR C 183 3548 1984 6566 57 -1192 163 C ATOM 5633 N MET C 184 -87.984 -27.570 154.266 1.00 28.76 N ANISOU 5633 N MET C 184 2564 2229 6134 194 -720 45 N ATOM 5634 CA MET C 184 -88.859 -26.422 154.098 1.00 34.53 C ANISOU 5634 CA MET C 184 3156 3101 6864 198 -637 40 C ATOM 5635 C MET C 184 -88.846 -26.019 152.631 1.00 36.61 C ANISOU 5635 C MET C 184 3572 3189 7148 219 -671 -76 C ATOM 5636 O MET C 184 -88.129 -26.600 151.812 1.00 30.55 O ANISOU 5636 O MET C 184 3010 2224 6375 249 -741 -164 O ATOM 5637 CB MET C 184 -88.428 -25.261 154.997 1.00 36.22 C ANISOU 5637 CB MET C 184 3256 3504 7003 324 -446 -71 C ATOM 5638 CG MET C 184 -87.095 -24.651 154.616 1.00 46.13 C ANISOU 5638 CG MET C 184 4630 4674 8223 404 -369 -275 C ATOM 5639 SD MET C 184 -87.055 -22.889 154.974 1.00 61.42 S ANISOU 5639 SD MET C 184 6553 6702 10084 484 -227 -418 S ATOM 5640 CE MET C 184 -87.975 -22.262 153.575 1.00 62.22 C ANISOU 5640 CE MET C 184 6716 6676 10248 503 -254 -423 C ATOM 5641 N SER C 185 -89.652 -25.016 152.300 1.00 40.16 N ANISOU 5641 N SER C 185 3927 3730 7603 240 -616 -68 N ATOM 5642 CA SER C 185 -89.707 -24.535 150.930 1.00 31.90 C ANISOU 5642 CA SER C 185 3003 2548 6568 256 -644 -155 C ATOM 5643 C SER C 185 -90.114 -23.071 150.925 1.00 33.28 C ANISOU 5643 C SER C 185 3087 2832 6726 365 -509 -200 C ATOM 5644 O SER C 185 -90.654 -22.543 151.903 1.00 33.31 O ANISOU 5644 O SER C 185 2941 3018 6698 440 -417 -141 O ATOM 5645 CB SER C 185 -90.674 -25.365 150.077 1.00 29.85 C ANISOU 5645 CB SER C 185 2802 2195 6344 95 -852 -11 C ATOM 5646 OG SER C 185 -91.933 -25.495 150.712 1.00 50.62 O ANISOU 5646 OG SER C 185 5207 5034 8994 -14 -903 230 O ATOM 5647 N SER C 186 -89.832 -22.420 149.804 1.00 32.48 N ANISOU 5647 N SER C 186 3104 2613 6625 400 -500 -302 N ATOM 5648 CA SER C 186 -90.162 -21.018 149.622 1.00 26.38 C ANISOU 5648 CA SER C 186 2315 1870 5838 508 -401 -344 C ATOM 5649 C SER C 186 -90.642 -20.828 148.195 1.00 30.43 C ANISOU 5649 C SER C 186 2890 2298 6373 479 -480 -312 C ATOM 5650 O SER C 186 -90.176 -21.501 147.275 1.00 33.96 O ANISOU 5650 O SER C 186 3461 2628 6814 405 -572 -351 O ATOM 5651 CB SER C 186 -88.963 -20.107 149.913 1.00 32.00 C ANISOU 5651 CB SER C 186 3146 2571 6442 533 -292 -498 C ATOM 5652 OG SER C 186 -89.385 -18.798 150.253 1.00 35.73 O ANISOU 5652 OG SER C 186 3654 3062 6861 639 -211 -527 O ATOM 5653 N SER C 187 -91.582 -19.907 148.023 1.00 27.38 N ANISOU 5653 N SER C 187 2430 1984 5988 571 -443 -240 N ATOM 5654 CA SER C 187 -92.119 -19.580 146.714 1.00 27.81 C ANISOU 5654 CA SER C 187 2520 1991 6054 555 -514 -186 C ATOM 5655 C SER C 187 -92.138 -18.071 146.534 1.00 34.62 C ANISOU 5655 C SER C 187 3451 2821 6884 710 -403 -238 C ATOM 5656 O SER C 187 -92.296 -17.314 147.493 1.00 31.18 O ANISOU 5656 O SER C 187 3016 2455 6375 845 -292 -261 O ATOM 5657 CB SER C 187 -93.535 -20.147 146.524 1.00 33.40 C ANISOU 5657 CB SER C 187 3048 2865 6778 480 -633 47 C ATOM 5658 OG SER C 187 -94.497 -19.388 147.236 1.00 35.63 O ANISOU 5658 OG SER C 187 3137 3362 7038 656 -530 177 O ATOM 5659 N VAL C 188 -91.950 -17.648 145.290 1.00 37.55 N ANISOU 5659 N VAL C 188 3932 3108 7226 669 -441 -253 N ATOM 5660 CA VAL C 188 -92.051 -16.251 144.896 1.00 38.37 C ANISOU 5660 CA VAL C 188 4142 3178 7256 770 -373 -258 C ATOM 5661 C VAL C 188 -92.842 -16.216 143.598 1.00 37.68 C ANISOU 5661 C VAL C 188 4001 3066 7252 783 -473 -136 C ATOM 5662 O VAL C 188 -92.894 -17.202 142.859 1.00 31.31 O ANISOU 5662 O VAL C 188 3168 2259 6470 648 -597 -103 O ATOM 5663 CB VAL C 188 -90.659 -15.596 144.731 1.00 36.48 C ANISOU 5663 CB VAL C 188 4097 2860 6905 679 -325 -378 C ATOM 5664 CG1 VAL C 188 -89.951 -16.145 143.499 1.00 34.20 C ANISOU 5664 CG1 VAL C 188 3836 2545 6612 559 -389 -388 C ATOM 5665 CG2 VAL C 188 -90.772 -14.077 144.677 1.00 37.37 C ANISOU 5665 CG2 VAL C 188 4368 2872 6957 780 -280 -377 C ATOM 5666 N THR C 189 -93.496 -15.090 143.333 1.00 38.58 N ANISOU 5666 N THR C 189 4134 3183 7339 939 -430 -62 N ATOM 5667 CA THR C 189 -94.294 -14.949 142.124 1.00 42.06 C ANISOU 5667 CA THR C 189 4504 3645 7833 960 -527 89 C ATOM 5668 C THR C 189 -93.891 -13.667 141.414 1.00 48.87 C ANISOU 5668 C THR C 189 5563 4366 8639 1020 -484 60 C ATOM 5669 O THR C 189 -93.778 -12.614 142.047 1.00 52.73 O ANISOU 5669 O THR C 189 6202 4800 9032 1149 -383 11 O ATOM 5670 CB THR C 189 -95.792 -14.934 142.449 1.00 33.49 C ANISOU 5670 CB THR C 189 3176 2808 6742 1107 -532 308 C ATOM 5671 OG1 THR C 189 -96.188 -16.225 142.928 1.00 33.38 O ANISOU 5671 OG1 THR C 189 2979 2973 6732 943 -613 393 O ATOM 5672 CG2 THR C 189 -96.605 -14.603 141.211 1.00 34.85 C ANISOU 5672 CG2 THR C 189 3281 3064 6898 1117 -623 488 C ATOM 5673 N VAL C 190 -93.680 -13.758 140.105 1.00 43.86 N ANISOU 5673 N VAL C 190 4961 3673 8029 917 -579 100 N ATOM 5674 CA VAL C 190 -93.318 -12.583 139.315 1.00 40.40 C ANISOU 5674 CA VAL C 190 4686 3103 7560 949 -564 123 C ATOM 5675 C VAL C 190 -94.156 -12.578 138.045 1.00 40.33 C ANISOU 5675 C VAL C 190 4594 3191 7538 951 -665 294 C ATOM 5676 O VAL C 190 -94.705 -13.614 137.643 1.00 48.74 O ANISOU 5676 O VAL C 190 5526 4420 8573 843 -767 354 O ATOM 5677 CB VAL C 190 -91.806 -12.561 138.983 1.00 40.25 C ANISOU 5677 CB VAL C 190 4812 2988 7492 769 -550 6 C ATOM 5678 CG1 VAL C 190 -90.980 -12.335 140.242 1.00 38.40 C ANISOU 5678 CG1 VAL C 190 4668 2739 7185 727 -457 -121 C ATOM 5679 CG2 VAL C 190 -91.394 -13.852 138.293 1.00 38.03 C ANISOU 5679 CG2 VAL C 190 4470 2805 7176 635 -618 -34 C ATOM 5680 N PRO C 191 -94.298 -11.421 137.397 1.00 38.00 N ANISOU 5680 N PRO C 191 4399 2799 7239 1051 -662 390 N ATOM 5681 CA PRO C 191 -94.919 -11.411 136.068 1.00 36.33 C ANISOU 5681 CA PRO C 191 4121 2706 6978 1017 -764 556 C ATOM 5682 C PRO C 191 -94.175 -12.341 135.121 1.00 35.32 C ANISOU 5682 C PRO C 191 4024 2636 6759 783 -844 483 C ATOM 5683 O PRO C 191 -92.951 -12.472 135.189 1.00 34.24 O ANISOU 5683 O PRO C 191 3999 2418 6594 687 -793 347 O ATOM 5684 CB PRO C 191 -94.812 -9.945 135.633 1.00 41.32 C ANISOU 5684 CB PRO C 191 4922 3157 7622 1144 -736 643 C ATOM 5685 CG PRO C 191 -94.699 -9.179 136.905 1.00 38.35 C ANISOU 5685 CG PRO C 191 4688 2607 7276 1318 -629 549 C ATOM 5686 CD PRO C 191 -93.973 -10.064 137.871 1.00 36.36 C ANISOU 5686 CD PRO C 191 4409 2390 7015 1179 -579 359 C ATOM 5687 N SER C 192 -94.929 -13.001 134.237 1.00 45.33 N ANISOU 5687 N SER C 192 5197 4069 7955 704 -978 587 N ATOM 5688 CA SER C 192 -94.317 -13.957 133.319 1.00 45.22 C ANISOU 5688 CA SER C 192 5276 4100 7808 534 -1069 494 C ATOM 5689 C SER C 192 -93.315 -13.272 132.399 1.00 45.10 C ANISOU 5689 C SER C 192 5390 4041 7703 523 -1016 486 C ATOM 5690 O SER C 192 -92.268 -13.844 132.074 1.00 55.29 O ANISOU 5690 O SER C 192 6775 5349 8882 461 -992 359 O ATOM 5691 CB SER C 192 -95.390 -14.675 132.501 1.00 54.50 C ANISOU 5691 CB SER C 192 6378 5434 8896 428 -1266 616 C ATOM 5692 OG SER C 192 -96.311 -15.348 133.341 1.00 62.17 O ANISOU 5692 OG SER C 192 7192 6493 9938 384 -1338 682 O ATOM 5693 N SER C 193 -93.623 -12.049 131.963 1.00 43.24 N ANISOU 5693 N SER C 193 5157 3772 7500 599 -999 648 N ATOM 5694 CA SER C 193 -92.738 -11.333 131.052 1.00 44.41 C ANISOU 5694 CA SER C 193 5408 3904 7561 551 -969 704 C ATOM 5695 C SER C 193 -91.389 -11.007 131.679 1.00 50.23 C ANISOU 5695 C SER C 193 6227 4536 8324 495 -855 607 C ATOM 5696 O SER C 193 -90.433 -10.722 130.948 1.00 58.42 O ANISOU 5696 O SER C 193 7305 5643 9250 407 -830 659 O ATOM 5697 CB SER C 193 -93.412 -10.046 130.581 1.00 45.73 C ANISOU 5697 CB SER C 193 5587 4010 7777 645 -993 923 C ATOM 5698 OG SER C 193 -94.097 -9.416 131.648 1.00 49.29 O ANISOU 5698 OG SER C 193 6029 4318 8380 817 -946 948 O ATOM 5699 N THR C 194 -91.283 -11.046 133.006 1.00 48.27 N ANISOU 5699 N THR C 194 5980 4163 8197 531 -792 493 N ATOM 5700 CA THR C 194 -90.061 -10.642 133.690 1.00 46.82 C ANISOU 5700 CA THR C 194 5870 3882 8037 446 -713 427 C ATOM 5701 C THR C 194 -89.092 -11.792 133.940 1.00 34.15 C ANISOU 5701 C THR C 194 4209 2418 6348 380 -664 280 C ATOM 5702 O THR C 194 -87.931 -11.536 134.274 1.00 34.49 O ANISOU 5702 O THR C 194 4262 2474 6366 283 -607 272 O ATOM 5703 CB THR C 194 -90.397 -9.975 135.028 1.00 52.35 C ANISOU 5703 CB THR C 194 6645 4364 8880 535 -679 377 C ATOM 5704 OG1 THR C 194 -91.036 -10.923 135.894 1.00 49.25 O ANISOU 5704 OG1 THR C 194 6144 4036 8535 626 -658 261 O ATOM 5705 CG2 THR C 194 -91.325 -8.789 134.812 1.00 51.09 C ANISOU 5705 CG2 THR C 194 6586 4046 8780 681 -716 521 C ATOM 5706 N TRP C 195 -89.525 -13.041 133.781 1.00 34.13 N ANISOU 5706 N TRP C 195 4160 2518 6289 426 -703 184 N ATOM 5707 CA TRP C 195 -88.666 -14.188 134.029 1.00 41.24 C ANISOU 5707 CA TRP C 195 5056 3513 7098 423 -665 39 C ATOM 5708 C TRP C 195 -88.667 -15.093 132.805 1.00 52.89 C ANISOU 5708 C TRP C 195 6593 5128 8374 460 -731 9 C ATOM 5709 O TRP C 195 -89.733 -15.363 132.238 1.00 62.97 O ANISOU 5709 O TRP C 195 7898 6393 9633 455 -854 42 O ATOM 5710 CB TRP C 195 -89.134 -14.971 135.265 1.00 36.30 C ANISOU 5710 CB TRP C 195 4400 2808 6586 451 -673 -79 C ATOM 5711 CG TRP C 195 -88.230 -16.100 135.614 1.00 37.69 C ANISOU 5711 CG TRP C 195 4596 3045 6680 473 -637 -216 C ATOM 5712 CD1 TRP C 195 -87.042 -16.024 136.277 1.00 38.48 C ANISOU 5712 CD1 TRP C 195 4657 3194 6771 465 -532 -255 C ATOM 5713 CD2 TRP C 195 -88.424 -17.484 135.298 1.00 36.74 C ANISOU 5713 CD2 TRP C 195 4564 2937 6457 515 -725 -316 C ATOM 5714 NE1 TRP C 195 -86.488 -17.274 136.405 1.00 36.53 N ANISOU 5714 NE1 TRP C 195 4443 3012 6426 546 -522 -368 N ATOM 5715 CE2 TRP C 195 -87.317 -18.188 135.811 1.00 35.37 C ANISOU 5715 CE2 TRP C 195 4410 2810 6220 584 -645 -421 C ATOM 5716 CE3 TRP C 195 -89.428 -18.196 134.637 1.00 31.84 C ANISOU 5716 CE3 TRP C 195 4033 2281 5782 486 -889 -316 C ATOM 5717 CZ2 TRP C 195 -87.186 -19.569 135.684 1.00 37.74 C ANISOU 5717 CZ2 TRP C 195 4857 3078 6404 672 -714 -543 C ATOM 5718 CZ3 TRP C 195 -89.296 -19.566 134.510 1.00 35.43 C ANISOU 5718 CZ3 TRP C 195 4656 2686 6120 515 -986 -442 C ATOM 5719 CH2 TRP C 195 -88.184 -20.238 135.032 1.00 38.72 C ANISOU 5719 CH2 TRP C 195 5130 3105 6476 630 -894 -563 C ATOM 5720 N PRO C 196 -87.494 -15.583 132.367 1.00 52.84 N ANISOU 5720 N PRO C 196 6613 5276 8186 513 -660 -43 N ATOM 5721 CA PRO C 196 -86.185 -15.488 133.016 1.00 55.49 C ANISOU 5721 CA PRO C 196 6871 5706 8507 514 -530 -53 C ATOM 5722 C PRO C 196 -85.380 -14.260 132.611 1.00 52.33 C ANISOU 5722 C PRO C 196 6384 5428 8072 406 -465 142 C ATOM 5723 O PRO C 196 -84.182 -14.201 132.889 1.00 52.36 O ANISOU 5723 O PRO C 196 6288 5602 8005 376 -374 192 O ATOM 5724 CB PRO C 196 -85.484 -16.756 132.534 1.00 58.24 C ANISOU 5724 CB PRO C 196 7292 6214 8624 685 -499 -172 C ATOM 5725 CG PRO C 196 -85.992 -16.907 131.136 1.00 54.91 C ANISOU 5725 CG PRO C 196 6986 5857 8019 741 -582 -153 C ATOM 5726 CD PRO C 196 -87.435 -16.432 131.161 1.00 53.05 C ANISOU 5726 CD PRO C 196 6763 5429 7964 610 -718 -99 C ATOM 5727 N SER C 197 -86.033 -13.298 131.957 1.00 51.69 N ANISOU 5727 N SER C 197 6331 5276 8034 333 -527 282 N ATOM 5728 CA SER C 197 -85.319 -12.132 131.448 1.00 50.61 C ANISOU 5728 CA SER C 197 6144 5234 7853 193 -503 505 C ATOM 5729 C SER C 197 -84.657 -11.351 132.573 1.00 52.81 C ANISOU 5729 C SER C 197 6402 5392 8271 25 -485 556 C ATOM 5730 O SER C 197 -83.540 -10.846 132.414 1.00 63.60 O ANISOU 5730 O SER C 197 7678 6935 9550 -129 -456 727 O ATOM 5731 CB SER C 197 -86.286 -11.241 130.678 1.00 57.88 C ANISOU 5731 CB SER C 197 7136 6034 8823 163 -593 645 C ATOM 5732 OG SER C 197 -87.097 -12.033 129.835 1.00 70.57 O ANISOU 5732 OG SER C 197 8778 7716 10320 291 -648 575 O ATOM 5733 N GLN C 198 -85.328 -11.239 133.713 1.00 50.09 N ANISOU 5733 N GLN C 198 6138 4775 8119 41 -516 429 N ATOM 5734 CA GLN C 198 -84.769 -10.611 134.902 1.00 36.57 C ANISOU 5734 CA GLN C 198 4464 2918 6514 -101 -520 425 C ATOM 5735 C GLN C 198 -84.511 -11.697 135.938 1.00 34.05 C ANISOU 5735 C GLN C 198 4072 2655 6213 -19 -458 235 C ATOM 5736 O GLN C 198 -85.448 -12.373 136.376 1.00 36.84 O ANISOU 5736 O GLN C 198 4450 2905 6641 128 -461 86 O ATOM 5737 CB GLN C 198 -85.709 -9.532 135.438 1.00 36.16 C ANISOU 5737 CB GLN C 198 4604 2508 6627 -96 -598 427 C ATOM 5738 CG GLN C 198 -86.207 -8.588 134.349 1.00 42.16 C ANISOU 5738 CG GLN C 198 5454 3187 7377 -113 -667 613 C ATOM 5739 CD GLN C 198 -86.935 -7.379 134.897 1.00 47.48 C ANISOU 5739 CD GLN C 198 6370 3484 8185 -73 -744 638 C ATOM 5740 OE1 GLN C 198 -86.725 -6.979 136.042 1.00 52.63 O ANISOU 5740 OE1 GLN C 198 7164 3926 8905 -110 -764 545 O ATOM 5741 NE2 GLN C 198 -87.799 -6.787 134.079 1.00 52.49 N ANISOU 5741 NE2 GLN C 198 7077 4032 8836 32 -792 762 N ATOM 5742 N THR C 199 -83.241 -11.863 136.312 1.00 35.13 N ANISOU 5742 N THR C 199 4096 2983 6269 -127 -411 279 N ATOM 5743 CA THR C 199 -82.814 -12.989 137.136 1.00 33.28 C ANISOU 5743 CA THR C 199 3770 2861 6013 -28 -344 135 C ATOM 5744 C THR C 199 -83.645 -13.089 138.411 1.00 36.08 C ANISOU 5744 C THR C 199 4218 2954 6537 15 -371 -32 C ATOM 5745 O THR C 199 -83.991 -12.079 139.029 1.00 39.10 O ANISOU 5745 O THR C 199 4724 3107 7024 -78 -426 -24 O ATOM 5746 CB THR C 199 -81.326 -12.837 137.479 1.00 34.73 C ANISOU 5746 CB THR C 199 3796 3301 6097 -186 -307 268 C ATOM 5747 OG1 THR C 199 -80.536 -13.105 136.313 1.00 44.80 O ANISOU 5747 OG1 THR C 199 4920 4938 7162 -132 -238 425 O ATOM 5748 CG2 THR C 199 -80.908 -13.786 138.597 1.00 35.40 C ANISOU 5748 CG2 THR C 199 3802 3457 6192 -102 -253 136 C ATOM 5749 N VAL C 200 -83.968 -14.322 138.800 1.00 32.92 N ANISOU 5749 N VAL C 200 3781 2587 6140 173 -338 -176 N ATOM 5750 CA VAL C 200 -84.536 -14.621 140.110 1.00 34.31 C ANISOU 5750 CA VAL C 200 3982 2617 6438 211 -344 -301 C ATOM 5751 C VAL C 200 -83.649 -15.664 140.777 1.00 36.95 C ANISOU 5751 C VAL C 200 4215 3111 6714 249 -289 -362 C ATOM 5752 O VAL C 200 -83.417 -16.741 140.215 1.00 34.53 O ANISOU 5752 O VAL C 200 3883 2929 6308 382 -266 -394 O ATOM 5753 CB VAL C 200 -85.988 -15.113 140.012 1.00 31.90 C ANISOU 5753 CB VAL C 200 3716 2195 6207 337 -387 -361 C ATOM 5754 CG1 VAL C 200 -86.482 -15.570 141.375 1.00 27.58 C ANISOU 5754 CG1 VAL C 200 3143 1585 5751 382 -378 -451 C ATOM 5755 CG2 VAL C 200 -86.883 -14.011 139.463 1.00 29.29 C ANISOU 5755 CG2 VAL C 200 3464 1734 5933 340 -432 -275 C ATOM 5756 N THR C 201 -83.158 -15.341 141.971 1.00 43.47 N ANISOU 5756 N THR C 201 5015 3921 7582 151 -280 -381 N ATOM 5757 CA THR C 201 -82.227 -16.181 142.710 1.00 45.00 C ANISOU 5757 CA THR C 201 5091 4290 7718 173 -232 -404 C ATOM 5758 C THR C 201 -82.715 -16.311 144.145 1.00 42.47 C ANISOU 5758 C THR C 201 4798 3842 7496 171 -244 -507 C ATOM 5759 O THR C 201 -83.115 -15.318 144.761 1.00 46.41 O ANISOU 5759 O THR C 201 5398 4181 8056 83 -281 -529 O ATOM 5760 CB THR C 201 -80.806 -15.591 142.683 1.00 42.47 C ANISOU 5760 CB THR C 201 4649 4195 7293 1 -218 -254 C ATOM 5761 OG1 THR C 201 -80.271 -15.689 141.357 1.00 43.81 O ANISOU 5761 OG1 THR C 201 4739 4581 7327 55 -177 -132 O ATOM 5762 CG2 THR C 201 -79.890 -16.335 143.644 1.00 46.94 C ANISOU 5762 CG2 THR C 201 5070 4959 7804 21 -176 -255 C ATOM 5763 N CYS C 202 -82.689 -17.531 144.676 1.00 31.50 N ANISOU 5763 N CYS C 202 3348 2518 6102 288 -218 -566 N ATOM 5764 CA CYS C 202 -82.983 -17.757 146.084 1.00 31.16 C ANISOU 5764 CA CYS C 202 3292 2427 6121 282 -220 -632 C ATOM 5765 C CYS C 202 -81.696 -18.020 146.856 1.00 35.70 C ANISOU 5765 C CYS C 202 3750 3194 6620 222 -191 -597 C ATOM 5766 O CYS C 202 -80.812 -18.753 146.400 1.00 39.23 O ANISOU 5766 O CYS C 202 4100 3832 6975 304 -151 -540 O ATOM 5767 CB CYS C 202 -83.969 -18.915 146.271 1.00 34.44 C ANISOU 5767 CB CYS C 202 3717 2776 6593 411 -241 -678 C ATOM 5768 SG CYS C 202 -83.263 -20.575 146.253 1.00 54.85 S ANISOU 5768 SG CYS C 202 6272 5461 9107 540 -238 -683 S ATOM 5769 N SER C 203 -81.599 -17.399 148.028 1.00 40.34 N ANISOU 5769 N SER C 203 4356 3750 7221 104 -213 -626 N ATOM 5770 CA SER C 203 -80.441 -17.474 148.909 1.00 39.95 C ANISOU 5770 CA SER C 203 4193 3891 7093 -6 -216 -577 C ATOM 5771 C SER C 203 -80.884 -18.134 150.206 1.00 37.21 C ANISOU 5771 C SER C 203 3833 3528 6777 68 -205 -654 C ATOM 5772 O SER C 203 -81.699 -17.569 150.947 1.00 33.98 O ANISOU 5772 O SER C 203 3540 2971 6401 58 -225 -739 O ATOM 5773 CB SER C 203 -79.871 -16.082 149.171 1.00 48.14 C ANISOU 5773 CB SER C 203 5311 4896 8084 -272 -299 -533 C ATOM 5774 OG SER C 203 -79.423 -15.485 147.966 1.00 62.57 O ANISOU 5774 OG SER C 203 7126 6770 9878 -373 -319 -412 O ATOM 5775 N VAL C 204 -80.366 -19.335 150.459 1.00 34.99 N ANISOU 5775 N VAL C 204 3421 3409 6466 177 -169 -613 N ATOM 5776 CA VAL C 204 -80.601 -20.065 151.698 1.00 26.94 C ANISOU 5776 CA VAL C 204 2359 2418 5460 229 -165 -639 C ATOM 5777 C VAL C 204 -79.376 -19.902 152.586 1.00 34.16 C ANISOU 5777 C VAL C 204 3149 3558 6271 104 -178 -573 C ATOM 5778 O VAL C 204 -78.238 -20.038 152.121 1.00 47.95 O ANISOU 5778 O VAL C 204 4760 5522 7937 88 -163 -457 O ATOM 5779 CB VAL C 204 -80.891 -21.549 151.419 1.00 31.55 C ANISOU 5779 CB VAL C 204 2927 2983 6077 423 -152 -619 C ATOM 5780 CG1 VAL C 204 -81.061 -22.316 152.717 1.00 43.95 C ANISOU 5780 CG1 VAL C 204 4442 4598 7658 449 -161 -602 C ATOM 5781 CG2 VAL C 204 -82.127 -21.681 150.543 1.00 34.08 C ANISOU 5781 CG2 VAL C 204 3371 3095 6482 481 -184 -662 C ATOM 5782 N ALA C 205 -79.608 -19.608 153.862 1.00 33.91 N ANISOU 5782 N ALA C 205 3148 3516 6219 25 -207 -626 N ATOM 5783 CA ALA C 205 -78.552 -19.299 154.815 1.00 29.08 C ANISOU 5783 CA ALA C 205 2451 3105 5492 -146 -256 -571 C ATOM 5784 C ALA C 205 -78.745 -20.138 156.067 1.00 38.74 C ANISOU 5784 C ALA C 205 3606 4417 6696 -61 -238 -577 C ATOM 5785 O ALA C 205 -79.768 -20.012 156.750 1.00 41.59 O ANISOU 5785 O ALA C 205 4072 4653 7078 -10 -230 -673 O ATOM 5786 CB ALA C 205 -78.544 -17.808 155.166 1.00 30.34 C ANISOU 5786 CB ALA C 205 2800 3137 5591 -382 -354 -644 C ATOM 5787 N HIS C 206 -77.774 -21.007 156.350 1.00 39.48 N ANISOU 5787 N HIS C 206 3507 4757 6735 -18 -225 -448 N ATOM 5788 CA HIS C 206 -77.771 -21.878 157.519 1.00 34.70 C ANISOU 5788 CA HIS C 206 2815 4269 6102 54 -218 -408 C ATOM 5789 C HIS C 206 -76.608 -21.429 158.393 1.00 39.48 C ANISOU 5789 C HIS C 206 3296 5145 6558 -146 -285 -325 C ATOM 5790 O HIS C 206 -75.454 -21.837 158.164 1.00 46.63 O ANISOU 5790 O HIS C 206 3998 6321 7398 -135 -280 -159 O ATOM 5791 CB HIS C 206 -77.620 -23.347 157.119 1.00 29.27 C ANISOU 5791 CB HIS C 206 2040 3616 5463 300 -168 -309 C ATOM 5792 CG HIS C 206 -78.081 -24.309 158.169 1.00 29.19 C ANISOU 5792 CG HIS C 206 2009 3609 5473 386 -174 -270 C ATOM 5793 ND1 HIS C 206 -77.488 -25.538 158.364 1.00 39.69 N ANISOU 5793 ND1 HIS C 206 3250 5045 6784 558 -167 -139 N ATOM 5794 CD2 HIS C 206 -79.083 -24.227 159.076 1.00 39.31 C ANISOU 5794 CD2 HIS C 206 3343 4819 6773 338 -186 -320 C ATOM 5795 CE1 HIS C 206 -78.102 -26.169 159.349 1.00 42.72 C ANISOU 5795 CE1 HIS C 206 3639 5398 7193 568 -192 -102 C ATOM 5796 NE2 HIS C 206 -79.074 -25.395 159.797 1.00 38.87 N ANISOU 5796 NE2 HIS C 206 3214 4834 6721 434 -196 -202 N ATOM 5797 N PRO C 207 -76.844 -20.522 159.347 1.00 40.01 N ANISOU 5797 N PRO C 207 3493 5167 6541 -330 -359 -426 N ATOM 5798 CA PRO C 207 -75.767 -20.102 160.261 1.00 40.96 C ANISOU 5798 CA PRO C 207 3529 5538 6495 -571 -468 -347 C ATOM 5799 C PRO C 207 -75.076 -21.266 160.946 1.00 34.54 C ANISOU 5799 C PRO C 207 2458 5033 5633 -468 -439 -179 C ATOM 5800 O PRO C 207 -73.850 -21.253 161.107 1.00 46.64 O ANISOU 5800 O PRO C 207 3786 6881 7055 -608 -500 -3 O ATOM 5801 CB PRO C 207 -76.495 -19.201 161.268 1.00 34.78 C ANISOU 5801 CB PRO C 207 3017 4579 5618 -672 -537 -540 C ATOM 5802 CG PRO C 207 -77.718 -18.732 160.555 1.00 33.93 C ANISOU 5802 CG PRO C 207 3127 4142 5624 -531 -474 -695 C ATOM 5803 CD PRO C 207 -78.118 -19.840 159.630 1.00 33.86 C ANISOU 5803 CD PRO C 207 2960 4119 5786 -298 -354 -614 C ATOM 5804 N ALA C 208 -75.849 -22.270 161.369 1.00 34.15 N ANISOU 5804 N ALA C 208 2405 4915 5656 -235 -360 -197 N ATOM 5805 CA ALA C 208 -75.307 -23.343 162.196 1.00 36.55 C ANISOU 5805 CA ALA C 208 2513 5469 5908 -135 -350 -39 C ATOM 5806 C ALA C 208 -74.216 -24.115 161.468 1.00 34.83 C ANISOU 5806 C ALA C 208 2078 5465 5691 13 -310 159 C ATOM 5807 O ALA C 208 -73.216 -24.512 162.078 1.00 50.32 O ANISOU 5807 O ALA C 208 3822 7756 7540 7 -336 339 O ATOM 5808 CB ALA C 208 -76.429 -24.283 162.631 1.00 33.16 C ANISOU 5808 CB ALA C 208 2144 4885 5570 62 -292 -62 C ATOM 5809 N SER C 209 -74.385 -24.341 160.167 1.00 33.97 N ANISOU 5809 N SER C 209 2023 5203 5682 178 -244 138 N ATOM 5810 CA SER C 209 -73.343 -24.962 159.366 1.00 40.35 C ANISOU 5810 CA SER C 209 2650 6237 6443 382 -186 312 C ATOM 5811 C SER C 209 -72.473 -23.938 158.653 1.00 40.46 C ANISOU 5811 C SER C 209 2535 6471 6367 185 -209 394 C ATOM 5812 O SER C 209 -71.700 -24.312 157.765 1.00 50.95 O ANISOU 5812 O SER C 209 3707 8015 7637 380 -136 540 O ATOM 5813 CB SER C 209 -73.956 -25.926 158.347 1.00 39.45 C ANISOU 5813 CB SER C 209 2699 5849 6441 712 -111 253 C ATOM 5814 OG SER C 209 -74.963 -25.290 157.579 1.00 32.53 O ANISOU 5814 OG SER C 209 2029 4658 5672 624 -115 74 O ATOM 5815 N SER C 210 -72.576 -22.661 159.030 1.00 39.43 N ANISOU 5815 N SER C 210 2483 6296 6202 -188 -318 318 N ATOM 5816 CA SER C 210 -71.783 -21.588 158.428 1.00 43.01 C ANISOU 5816 CA SER C 210 2845 6928 6570 -471 -391 427 C ATOM 5817 C SER C 210 -71.885 -21.594 156.906 1.00 45.33 C ANISOU 5817 C SER C 210 3155 7143 6926 -302 -296 434 C ATOM 5818 O SER C 210 -70.918 -21.304 156.199 1.00 55.36 O ANISOU 5818 O SER C 210 4204 8734 8095 -368 -290 644 O ATOM 5819 CB SER C 210 -70.321 -21.673 158.871 1.00 47.74 C ANISOU 5819 CB SER C 210 3084 8063 6991 -601 -448 728 C ATOM 5820 OG SER C 210 -70.199 -21.475 160.267 1.00 67.01 O ANISOU 5820 OG SER C 210 5533 10581 9346 -829 -573 719 O ATOM 5821 N THR C 211 -73.062 -21.931 156.385 1.00 35.32 N ANISOU 5821 N THR C 211 2131 5486 5804 -93 -226 230 N ATOM 5822 CA THR C 211 -73.202 -22.171 154.955 1.00 34.87 C ANISOU 5822 CA THR C 211 2108 5355 5785 124 -133 226 C ATOM 5823 C THR C 211 -74.265 -21.265 154.354 1.00 42.06 C ANISOU 5823 C THR C 211 3280 5893 6810 -13 -168 42 C ATOM 5824 O THR C 211 -75.282 -20.974 154.986 1.00 32.02 O ANISOU 5824 O THR C 211 2208 4332 5625 -86 -211 -129 O ATOM 5825 CB THR C 211 -73.561 -23.636 154.673 1.00 34.17 C ANISOU 5825 CB THR C 211 2084 5156 5742 549 -36 185 C ATOM 5826 OG1 THR C 211 -72.796 -24.491 155.529 1.00 46.73 O ANISOU 5826 OG1 THR C 211 3492 7014 7248 691 -20 331 O ATOM 5827 CG2 THR C 211 -73.267 -23.989 153.224 1.00 34.85 C ANISOU 5827 CG2 THR C 211 2168 5300 5774 817 56 227 C ATOM 5828 N THR C 212 -74.003 -20.784 153.145 1.00 37.42 N ANISOU 5828 N THR C 212 2669 5353 6196 -32 -144 104 N ATOM 5829 CA THR C 212 -75.021 -20.137 152.334 1.00 35.82 C ANISOU 5829 CA THR C 212 2703 4808 6100 -71 -156 -45 C ATOM 5830 C THR C 212 -74.967 -20.730 150.936 1.00 35.40 C ANISOU 5830 C THR C 212 2628 4799 6022 202 -56 -9 C ATOM 5831 O THR C 212 -73.885 -20.915 150.371 1.00 35.34 O ANISOU 5831 O THR C 212 2402 5154 5874 288 3 180 O ATOM 5832 CB THR C 212 -74.832 -18.612 152.284 1.00 38.87 C ANISOU 5832 CB THR C 212 3157 5149 6464 -453 -274 -10 C ATOM 5833 OG1 THR C 212 -75.239 -18.042 153.534 1.00 39.69 O ANISOU 5833 OG1 THR C 212 3422 5076 6583 -645 -377 -132 O ATOM 5834 CG2 THR C 212 -75.661 -17.995 151.164 1.00 41.76 C ANISOU 5834 CG2 THR C 212 3717 5236 6914 -442 -268 -97 C ATOM 5835 N VAL C 213 -76.138 -21.033 150.389 1.00 30.86 N ANISOU 5835 N VAL C 213 2276 3891 5559 348 -41 -176 N ATOM 5836 CA VAL C 213 -76.267 -21.539 149.030 1.00 38.07 C ANISOU 5836 CA VAL C 213 3251 4779 6435 591 22 -187 C ATOM 5837 C VAL C 213 -77.160 -20.580 148.261 1.00 32.02 C ANISOU 5837 C VAL C 213 2647 3767 5754 444 -21 -267 C ATOM 5838 O VAL C 213 -78.296 -20.312 148.673 1.00 37.71 O ANISOU 5838 O VAL C 213 3528 4192 6606 367 -75 -399 O ATOM 5839 CB VAL C 213 -76.830 -22.970 148.998 1.00 36.32 C ANISOU 5839 CB VAL C 213 3180 4376 6242 901 39 -290 C ATOM 5840 CG1 VAL C 213 -76.767 -23.528 147.587 1.00 31.31 C ANISOU 5840 CG1 VAL C 213 2653 3738 5507 1176 88 -308 C ATOM 5841 CG2 VAL C 213 -76.055 -23.865 149.954 1.00 31.38 C ANISOU 5841 CG2 VAL C 213 2426 3942 5554 1043 66 -207 C ATOM 5842 N ASP C 214 -76.653 -20.068 147.146 1.00 31.23 N ANISOU 5842 N ASP C 214 2481 3823 5560 425 9 -162 N ATOM 5843 CA ASP C 214 -77.445 -19.282 146.215 1.00 32.01 C ANISOU 5843 CA ASP C 214 2731 3710 5720 338 -25 -212 C ATOM 5844 C ASP C 214 -77.744 -20.147 145.004 1.00 36.23 C ANISOU 5844 C ASP C 214 3356 4222 6186 633 30 -262 C ATOM 5845 O ASP C 214 -76.826 -20.709 144.396 1.00 33.11 O ANISOU 5845 O ASP C 214 2846 4117 5617 844 115 -165 O ATOM 5846 CB ASP C 214 -76.705 -18.012 145.790 1.00 32.29 C ANISOU 5846 CB ASP C 214 2658 3922 5688 61 -60 -32 C ATOM 5847 CG ASP C 214 -76.415 -17.092 146.955 1.00 40.62 C ANISOU 5847 CG ASP C 214 3709 4940 6783 -271 -167 3 C ATOM 5848 OD1 ASP C 214 -77.308 -16.925 147.808 1.00 32.14 O ANISOU 5848 OD1 ASP C 214 2819 3566 5827 -302 -217 -168 O ATOM 5849 OD2 ASP C 214 -75.296 -16.536 147.020 1.00 51.28 O ANISOU 5849 OD2 ASP C 214 4878 6580 8024 -504 -212 215 O ATOM 5850 N LYS C 215 -79.021 -20.253 144.656 1.00 29.40 N ANISOU 5850 N LYS C 215 2701 3036 5432 662 -25 -403 N ATOM 5851 CA LYS C 215 -79.437 -20.978 143.469 1.00 32.02 C ANISOU 5851 CA LYS C 215 3180 3295 5690 885 -22 -466 C ATOM 5852 C LYS C 215 -80.232 -20.035 142.582 1.00 40.04 C ANISOU 5852 C LYS C 215 4282 4174 6758 752 -68 -467 C ATOM 5853 O LYS C 215 -81.210 -19.428 143.033 1.00 50.04 O ANISOU 5853 O LYS C 215 5615 5218 8181 596 -134 -514 O ATOM 5854 CB LYS C 215 -80.275 -22.201 143.849 1.00 35.11 C ANISOU 5854 CB LYS C 215 3756 3436 6149 1022 -90 -600 C ATOM 5855 CG LYS C 215 -79.834 -23.477 143.169 1.00 42.60 C ANISOU 5855 CG LYS C 215 4845 4415 6926 1346 -74 -645 C ATOM 5856 CD LYS C 215 -78.793 -24.180 144.026 1.00 35.62 C ANISOU 5856 CD LYS C 215 3846 3716 5970 1510 -4 -591 C ATOM 5857 CE LYS C 215 -78.199 -25.377 143.313 1.00 34.45 C ANISOU 5857 CE LYS C 215 3866 3617 5607 1920 33 -630 C ATOM 5858 NZ LYS C 215 -77.338 -26.199 144.213 1.00 34.85 N ANISOU 5858 NZ LYS C 215 3838 3803 5599 2126 86 -574 N ATOM 5859 N LYS C 216 -79.813 -19.913 141.328 1.00 30.68 N ANISOU 5859 N LYS C 216 3088 3149 5419 845 -26 -400 N ATOM 5860 CA LYS C 216 -80.480 -19.041 140.374 1.00 30.65 C ANISOU 5860 CA LYS C 216 3157 3049 5441 734 -70 -371 C ATOM 5861 C LYS C 216 -81.415 -19.885 139.519 1.00 38.96 C ANISOU 5861 C LYS C 216 4423 3926 6456 904 -133 -496 C ATOM 5862 O LYS C 216 -80.972 -20.821 138.843 1.00 44.92 O ANISOU 5862 O LYS C 216 5262 4784 7023 1153 -102 -539 O ATOM 5863 CB LYS C 216 -79.466 -18.299 139.503 1.00 32.50 C ANISOU 5863 CB LYS C 216 3236 3599 5514 686 -2 -180 C ATOM 5864 CG LYS C 216 -80.022 -17.833 138.174 1.00 33.06 C ANISOU 5864 CG LYS C 216 3400 3632 5528 688 -30 -147 C ATOM 5865 CD LYS C 216 -78.942 -17.215 137.314 1.00 52.93 C ANISOU 5865 CD LYS C 216 5731 6527 7854 649 46 84 C ATOM 5866 CE LYS C 216 -79.461 -16.933 135.919 1.00 59.11 C ANISOU 5866 CE LYS C 216 6611 7309 8538 700 27 116 C ATOM 5867 NZ LYS C 216 -79.018 -17.974 134.953 1.00 62.48 N ANISOU 5867 NZ LYS C 216 7071 7987 8681 1058 118 74 N ATOM 5868 N LEU C 217 -82.701 -19.560 139.563 1.00 31.43 N ANISOU 5868 N LEU C 217 3568 2718 5655 783 -232 -544 N ATOM 5869 CA LEU C 217 -83.706 -20.369 138.890 1.00 34.58 C ANISOU 5869 CA LEU C 217 4161 2945 6032 864 -343 -635 C ATOM 5870 C LEU C 217 -83.637 -20.167 137.382 1.00 38.51 C ANISOU 5870 C LEU C 217 4736 3540 6357 939 -348 -604 C ATOM 5871 O LEU C 217 -83.539 -19.035 136.898 1.00 31.19 O ANISOU 5871 O LEU C 217 3712 2705 5436 831 -311 -487 O ATOM 5872 CB LEU C 217 -85.098 -20.052 139.428 1.00 36.67 C ANISOU 5872 CB LEU C 217 4437 3003 6495 708 -443 -635 C ATOM 5873 CG LEU C 217 -85.294 -20.591 140.849 1.00 43.20 C ANISOU 5873 CG LEU C 217 5218 3753 7444 678 -453 -673 C ATOM 5874 CD1 LEU C 217 -84.880 -19.583 141.913 1.00 49.68 C ANISOU 5874 CD1 LEU C 217 5889 4629 8358 584 -362 -634 C ATOM 5875 CD2 LEU C 217 -86.721 -21.056 141.059 1.00 53.52 C ANISOU 5875 CD2 LEU C 217 6575 4986 8774 574 -570 -638 C ATOM 5876 N GLU C 218 -83.687 -21.270 136.645 1.00 44.90 N ANISOU 5876 N GLU C 218 5755 4311 6993 1126 -408 -707 N ATOM 5877 CA GLU C 218 -83.590 -21.276 135.197 1.00 43.21 C ANISOU 5877 CA GLU C 218 5659 4205 6554 1250 -416 -706 C ATOM 5878 C GLU C 218 -84.677 -22.172 134.624 1.00 47.49 C ANISOU 5878 C GLU C 218 6501 4497 7047 1257 -619 -829 C ATOM 5879 O GLU C 218 -85.125 -23.113 135.287 1.00 55.29 O ANISOU 5879 O GLU C 218 7634 5265 8107 1239 -735 -919 O ATOM 5880 CB GLU C 218 -82.207 -21.768 134.743 1.00 51.63 C ANISOU 5880 CB GLU C 218 6719 5556 7343 1554 -270 -708 C ATOM 5881 CG GLU C 218 -81.142 -20.681 134.740 1.00 63.80 C ANISOU 5881 CG GLU C 218 7937 7454 8850 1492 -102 -502 C ATOM 5882 CD GLU C 218 -79.795 -21.181 134.261 1.00 77.23 C ANISOU 5882 CD GLU C 218 9562 9540 10242 1822 58 -446 C ATOM 5883 OE1 GLU C 218 -79.583 -22.411 134.257 1.00 83.72 O ANISOU 5883 OE1 GLU C 218 10594 10306 10910 2140 59 -599 O ATOM 5884 OE2 GLU C 218 -78.947 -20.342 133.887 1.00 80.39 O ANISOU 5884 OE2 GLU C 218 9696 10310 10539 1771 176 -228 O ATOM 5885 N PRO C 219 -85.131 -21.890 133.402 1.00 51.23 N ANISOU 5885 N PRO C 219 7074 5001 7389 1246 -688 -811 N ATOM 5886 CA PRO C 219 -86.287 -22.605 132.846 1.00 50.48 C ANISOU 5886 CA PRO C 219 7253 4675 7252 1165 -929 -893 C ATOM 5887 C PRO C 219 -86.059 -24.105 132.716 1.00 62.65 C ANISOU 5887 C PRO C 219 9170 6036 8598 1361 -1047 -1082 C ATOM 5888 O PRO C 219 -84.968 -24.634 132.940 1.00 57.25 O ANISOU 5888 O PRO C 219 8543 5432 7779 1638 -916 -1158 O ATOM 5889 CB PRO C 219 -86.459 -21.954 131.472 1.00 44.79 C ANISOU 5889 CB PRO C 219 6552 4105 6363 1171 -941 -829 C ATOM 5890 CG PRO C 219 -85.997 -20.557 131.685 1.00 50.05 C ANISOU 5890 CG PRO C 219 6882 4979 7158 1092 -756 -650 C ATOM 5891 CD PRO C 219 -84.819 -20.677 132.626 1.00 52.47 C ANISOU 5891 CD PRO C 219 7050 5394 7491 1205 -583 -660 C ATOM 5892 N SER C 220 -87.137 -24.789 132.335 1.00 82.86 N ANISOU 5892 N SER C 220 12006 8346 11131 1208 -1321 -1138 N ATOM 5893 CA SER C 220 -87.136 -26.222 132.044 1.00 97.75 C ANISOU 5893 CA SER C 220 14373 9960 12807 1340 -1522 -1325 C ATOM 5894 C SER C 220 -86.736 -27.043 133.266 1.00112.33 C ANISOU 5894 C SER C 220 16222 11707 14752 1373 -1479 -1340 C ATOM 5895 O SER C 220 -85.885 -27.929 133.186 1.00122.28 O ANISOU 5895 O SER C 220 17685 12988 15789 1636 -1407 -1430 O ATOM 5896 CB SER C 220 -86.207 -26.537 130.867 1.00100.28 C ANISOU 5896 CB SER C 220 14968 10402 12732 1734 -1437 -1470 C ATOM 5897 OG SER C 220 -86.643 -25.888 129.686 1.00100.86 O ANISOU 5897 OG SER C 220 15034 10617 12670 1660 -1482 -1422 O ATOM 5898 OXT SER C 220 -87.265 -26.846 134.361 1.00116.85 O ANISOU 5898 OXT SER C 220 16538 12265 15595 1118 -1481 -1212 O TER 5899 SER C 220 HETATM 5900 C1 SIP A1201 -93.995 -21.801 211.052 1.00101.04 C HETATM 5901 C2 SIP A1201 -92.957 -21.248 212.043 1.00102.43 C HETATM 5902 C4 SIP A1201 -92.322 -23.470 212.767 1.00102.24 C HETATM 5903 C5 SIP A1201 -93.404 -24.096 211.916 1.00100.74 C HETATM 5904 C6 SIP A1201 -93.697 -23.266 210.667 1.00100.04 C HETATM 5905 C7 SIP A1201 -92.459 -23.279 209.715 1.00 97.08 C HETATM 5906 C10 SIP A1201 -94.115 -24.541 208.722 1.00 94.58 C HETATM 5907 C12 SIP A1201 -96.086 -24.226 210.288 1.00103.35 C HETATM 5908 C13 SIP A1201 -96.620 -25.447 209.930 1.00105.96 C HETATM 5909 C14 SIP A1201 -97.898 -25.786 210.326 1.00104.83 C HETATM 5910 C15 SIP A1201 -98.641 -24.901 211.080 1.00103.42 C HETATM 5911 C16 SIP A1201 -98.110 -23.683 211.440 1.00104.04 C HETATM 5912 C17 SIP A1201 -96.837 -23.343 211.043 1.00104.24 C HETATM 5913 C18 SIP A1201 -91.583 -21.602 213.959 1.00103.63 C HETATM 5914 C19 SIP A1201 -92.038 -20.241 214.426 1.00106.72 C HETATM 5915 C20 SIP A1201 -91.572 -19.986 215.827 1.00109.96 C HETATM 5916 C21 SIP A1201 -91.823 -18.593 216.346 1.00111.05 C HETATM 5917 C23 SIP A1201 -91.002 -18.117 217.497 1.00115.82 C HETATM 5918 C24 SIP A1201 -90.064 -18.954 218.066 1.00116.05 C HETATM 5919 C25 SIP A1201 -89.297 -18.550 219.137 1.00114.29 C HETATM 5920 C26 SIP A1201 -89.485 -17.281 219.646 1.00114.41 C HETATM 5921 C27 SIP A1201 -90.421 -16.428 219.099 1.00115.14 C HETATM 5922 C28 SIP A1201 -91.171 -16.861 218.028 1.00116.46 C HETATM 5923 F29 SIP A1201 -88.738 -16.863 220.702 1.00114.28 F HETATM 5924 N3 SIP A1201 -92.703 -22.132 213.209 1.00103.38 N HETATM 5925 N9 SIP A1201 -92.758 -24.010 208.651 1.00 96.66 N HETATM 5926 N11 SIP A1201 -94.793 -23.906 209.872 1.00 98.31 N HETATM 5927 O8 SIP A1201 -91.387 -22.714 209.899 1.00 93.50 O HETATM 5928 O22 SIP A1201 -92.678 -17.887 215.856 1.00112.51 O CONECT 569 1084 CONECT 1084 569 CONECT 2241 2255 CONECT 2255 2241 CONECT 2745 3256 CONECT 3256 2745 CONECT 3591 4085 CONECT 4085 3591 CONECT 4241 5284 CONECT 4408 5001 CONECT 5001 4408 CONECT 5284 4241 CONECT 5358 5768 CONECT 5768 5358 CONECT 5900 5901 5904 CONECT 5901 5900 5924 CONECT 5902 5903 5924 CONECT 5903 5902 5904 CONECT 5904 5900 5903 5905 5926 CONECT 5905 5904 5925 5927 CONECT 5906 5925 5926 CONECT 5907 5908 5912 5926 CONECT 5908 5907 5909 CONECT 5909 5908 5910 CONECT 5910 5909 5911 CONECT 5911 5910 5912 CONECT 5912 5907 5911 CONECT 5913 5914 5924 CONECT 5914 5913 5915 CONECT 5915 5914 5916 CONECT 5916 5915 5917 5928 CONECT 5917 5916 5918 5922 CONECT 5918 5917 5919 CONECT 5919 5918 5920 CONECT 5920 5919 5921 5923 CONECT 5921 5920 5922 CONECT 5922 5917 5921 CONECT 5923 5920 CONECT 5924 5901 5902 5913 CONECT 5925 5905 5906 CONECT 5926 5904 5906 5907 CONECT 5927 5905 CONECT 5928 5916 MASTER 487 0 1 21 43 0 0 6 5925 3 43 62 END