HEADER SIGNALING PROTEIN 20-JUN-19 6PEL TITLE CRYSTAL STRUCTURE OF BOVINE OPSIN WITH CITRONELLOL BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: ILENLKDVGLF G ALPHA PEPTIDE CT2; COMPND 6 CHAIN: B; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 8 ORGANISM_TAXID: 9913 KEYWDS OLFACTORY RECEPTOR, ODORANT, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.T.EGER,T.MORIZUMI,O.P.ERNST REVDAT 2 29-JUL-20 6PEL 1 COMPND REMARK HETNAM LINK REVDAT 2 2 1 SITE ATOM REVDAT 1 24-JUN-20 6PEL 0 JRNL AUTH T.MORIZUMI,K.KUROI,B.T.EGER,W.L.OU,N.VAN EPS,H.TSUKAMOTO, JRNL AUTH 2 Y.FURUTANI,O.P.ERNST JRNL TITL ODORANT-BINDING SITE IN VISUAL OPSIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.19 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10_2155) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 20585 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 1047 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 39.7587 - 6.0889 1.00 2862 154 0.2291 0.2626 REMARK 3 2 6.0889 - 4.8356 1.00 2805 144 0.2251 0.2347 REMARK 3 3 4.8356 - 4.2252 1.00 2790 156 0.1703 0.2256 REMARK 3 4 4.2252 - 3.8392 1.00 2767 153 0.1874 0.2305 REMARK 3 5 3.8392 - 3.5642 1.00 2776 154 0.1967 0.2395 REMARK 3 6 3.5642 - 3.3542 1.00 2760 140 0.2282 0.2661 REMARK 3 7 3.3542 - 3.1863 1.00 2778 146 0.2816 0.3140 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.720 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 2872 REMARK 3 ANGLE : 0.834 3907 REMARK 3 CHIRALITY : 0.045 445 REMARK 3 PLANARITY : 0.006 473 REMARK 3 DIHEDRAL : 14.358 1730 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 2:139 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.0328 41.5946 39.3316 REMARK 3 T TENSOR REMARK 3 T11: 0.6758 T22: 0.6556 REMARK 3 T33: 0.7215 T12: 0.0589 REMARK 3 T13: -0.0429 T23: 0.0657 REMARK 3 L TENSOR REMARK 3 L11: 1.9082 L22: 3.5676 REMARK 3 L33: 1.2172 L12: 1.4161 REMARK 3 L13: 0.1584 L23: -0.0025 REMARK 3 S TENSOR REMARK 3 S11: -0.0464 S12: 0.0282 S13: 0.0553 REMARK 3 S21: -0.2596 S22: 0.0231 S23: -0.6726 REMARK 3 S31: -0.1055 S32: 0.0485 S33: 0.0004 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 140:168 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1196 26.0406 24.1755 REMARK 3 T TENSOR REMARK 3 T11: 1.1207 T22: 0.5848 REMARK 3 T33: 1.2664 T12: -0.1102 REMARK 3 T13: 0.0758 T23: 0.0288 REMARK 3 L TENSOR REMARK 3 L11: 0.8397 L22: 0.4098 REMARK 3 L33: 0.0512 L12: 1.0035 REMARK 3 L13: -0.2981 L23: 0.1583 REMARK 3 S TENSOR REMARK 3 S11: -0.4074 S12: 1.2914 S13: -2.0890 REMARK 3 S21: -0.8880 S22: 0.2683 S23: 0.1185 REMARK 3 S31: 1.2988 S32: -0.3528 S33: 0.0217 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN A AND RESID 169:222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5645 49.5548 29.7779 REMARK 3 T TENSOR REMARK 3 T11: 0.8645 T22: 0.6475 REMARK 3 T33: 0.7968 T12: 0.0614 REMARK 3 T13: -0.1184 T23: 0.1543 REMARK 3 L TENSOR REMARK 3 L11: 3.0353 L22: 0.3723 REMARK 3 L33: 2.7884 L12: 0.7759 REMARK 3 L13: -0.0946 L23: -0.1831 REMARK 3 S TENSOR REMARK 3 S11: -0.2175 S12: 0.4133 S13: 1.6918 REMARK 3 S21: -0.6463 S22: 0.2140 S23: -0.6318 REMARK 3 S31: -0.8885 S32: 0.5008 S33: 0.1396 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN A AND RESID 223:287 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.8218 35.0181 41.2007 REMARK 3 T TENSOR REMARK 3 T11: 0.5912 T22: 0.7102 REMARK 3 T33: 0.7108 T12: 0.0534 REMARK 3 T13: -0.1297 T23: 0.0174 REMARK 3 L TENSOR REMARK 3 L11: 4.7967 L22: 2.1766 REMARK 3 L33: 3.7553 L12: -2.4273 REMARK 3 L13: -1.0324 L23: -1.1448 REMARK 3 S TENSOR REMARK 3 S11: 0.1026 S12: 0.0079 S13: 0.5178 REMARK 3 S21: 0.5064 S22: -0.3118 S23: 0.7086 REMARK 3 S31: 0.0112 S32: -0.2334 S33: -0.0016 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN A AND RESID 288:326 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.2361 27.4544 46.0492 REMARK 3 T TENSOR REMARK 3 T11: 1.0378 T22: 0.8448 REMARK 3 T33: 1.2963 T12: 0.0178 REMARK 3 T13: -0.0762 T23: -0.0237 REMARK 3 L TENSOR REMARK 3 L11: 1.6620 L22: -0.0248 REMARK 3 L33: 1.2128 L12: 0.1655 REMARK 3 L13: 2.2452 L23: 0.1521 REMARK 3 S TENSOR REMARK 3 S11: -0.1607 S12: 0.0135 S13: 0.0853 REMARK 3 S21: 0.4704 S22: 0.1803 S23: 0.5187 REMARK 3 S31: -0.2089 S32: -0.3419 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN B AND RESID 340:344 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.7716 13.8745 36.6946 REMARK 3 T TENSOR REMARK 3 T11: 1.5376 T22: 1.3625 REMARK 3 T33: 2.0462 T12: -0.0136 REMARK 3 T13: 0.0560 T23: 0.2894 REMARK 3 L TENSOR REMARK 3 L11: 0.0059 L22: 0.0055 REMARK 3 L33: 0.0933 L12: 0.0041 REMARK 3 L13: -0.0375 L23: -0.0446 REMARK 3 S TENSOR REMARK 3 S11: -0.4648 S12: 1.7841 S13: -1.1236 REMARK 3 S21: -0.8885 S22: 0.0037 S23: -0.7892 REMARK 3 S31: 0.6185 S32: 1.8265 S33: -0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN B AND RESID 345:350 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.5441 16.8390 39.4239 REMARK 3 T TENSOR REMARK 3 T11: 1.3309 T22: 1.1893 REMARK 3 T33: 1.3909 T12: -0.1635 REMARK 3 T13: -0.0590 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 0.0410 L22: 0.0376 REMARK 3 L33: 0.0366 L12: 0.0299 REMARK 3 L13: 0.0113 L23: -0.0515 REMARK 3 S TENSOR REMARK 3 S11: 0.1416 S12: -0.8594 S13: -0.4425 REMARK 3 S21: 0.0552 S22: 0.8034 S23: -0.0576 REMARK 3 S31: 1.2176 S32: 0.5963 S33: -0.0000 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 6PEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1000242412. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-OCT-16 REMARK 200 TEMPERATURE (KELVIN) : 173 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER R 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20603 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.186 REMARK 200 RESOLUTION RANGE LOW (A) : 39.756 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.08100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.70 REMARK 200 R MERGE FOR SHELL (I) : 0.54900 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: 3CAP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 84.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.1-3.3M AMMONIUM SULFATE, 0.1M SODIUM REMARK 280 ACETATE BUFFER, PH 5.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 121.70600 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.26699 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.14667 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.70600 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.26699 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.14667 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.70600 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.26699 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.14667 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.70600 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.26699 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.14667 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.70600 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.26699 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.14667 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.70600 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.26699 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.14667 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.53398 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 72.29333 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.53398 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 72.29333 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.53398 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 72.29333 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.53398 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 72.29333 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.53398 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 72.29333 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.53398 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 72.29333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL 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 1 REMARK 465 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ALA A 166 OH TYR A 206 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 10 108.56 -161.58 REMARK 500 GLU A 25 -30.91 -133.60 REMARK 500 GLN A 28 39.61 -99.41 REMARK 500 ALA A 32 137.48 -174.08 REMARK 500 ARG A 69 48.20 -93.84 REMARK 500 LEU A 72 5.78 -64.99 REMARK 500 CYS A 167 -19.34 -148.48 REMARK 500 SER A 176 -164.44 57.38 REMARK 500 TYR A 191 22.08 -140.99 REMARK 500 HIS A 195 85.90 -26.25 REMARK 500 ASN A 199 61.58 60.92 REMARK 500 PHE A 212 -54.79 -144.58 REMARK 500 GLN A 237 46.58 -144.60 REMARK 500 THR A 277 -40.04 -139.74 REMARK 500 HIS A 278 50.35 -108.25 REMARK 500 SER A 281 -158.61 -73.39 REMARK 500 ILE A 307 -50.48 -127.84 REMARK 500 CYS A 323 57.28 39.93 REMARK 500 LYS A 325 -157.99 -111.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6NWE RELATED DB: PDB REMARK 900 THIS IS THE SAME BOVINE OPSIN PROTEIN AND G ALPHA CT2 PEPTIDE WITH REMARK 900 A DIFFERENT COMPOUND (CITRONELLOL) BOUND REMARK 900 RELATED ID: 6PGS RELATED DB: PDB REMARK 900 RELATED ID: 6PH7 RELATED DB: PDB DBREF 6PEL A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 6PEL B 340 350 PDB 6PEL 6PEL 340 350 SEQRES 1 A 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE SEQRES 2 A 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA SEQRES 3 A 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET SEQRES 4 A 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE SEQRES 5 A 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS SEQRES 6 A 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN SEQRES 7 A 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE SEQRES 8 A 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL SEQRES 9 A 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA SEQRES 10 A 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL SEQRES 11 A 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET SEQRES 12 A 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY SEQRES 13 A 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA SEQRES 14 A 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY SEQRES 15 A 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS SEQRES 16 A 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE SEQRES 17 A 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE SEQRES 18 A 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA SEQRES 19 A 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU SEQRES 20 A 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA SEQRES 21 A 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE SEQRES 22 A 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE SEQRES 23 A 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA SEQRES 24 A 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN SEQRES 25 A 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS SEQRES 26 A 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER SEQRES 27 A 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA SEQRES 1 B 11 ILE LEU GLU ASN LEU LYS ASP VAL GLY LEU PHE HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET BMA C 4 11 HET ODM A 401 11 HET BOG A 406 20 HET PLM A 407 17 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM ODM (3R)-3,7-DIMETHYLOCT-6-EN-1-OL HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM PLM PALMITIC ACID HETSYN ODM CITRONELLOL FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 3 BMA 2(C6 H12 O6) FORMUL 4 ODM C10 H20 O FORMUL 5 BOG C14 H28 O6 FORMUL 6 PLM C16 H32 O2 HELIX 1 AA1 SER A 14 GLY A 18 5 5 HELIX 2 AA2 GLU A 33 HIS A 65 1 33 HELIX 3 AA3 LYS A 66 ARG A 69 5 4 HELIX 4 AA4 THR A 70 LEU A 72 5 3 HELIX 5 AA5 ASN A 73 GLY A 89 1 17 HELIX 6 AA6 GLY A 90 GLY A 101 1 12 HELIX 7 AA7 PHE A 105 LYS A 141 1 37 HELIX 8 AA8 GLY A 149 ALA A 169 1 21 HELIX 9 AA9 PRO A 170 VAL A 173 5 4 HELIX 10 AB1 HIS A 195 THR A 198 5 4 HELIX 11 AB2 ASN A 199 HIS A 211 1 13 HELIX 12 AB3 PHE A 212 GLN A 236 1 25 HELIX 13 AB4 SER A 240 ILE A 275 1 36 HELIX 14 AB5 GLY A 284 THR A 289 1 6 HELIX 15 AB6 THR A 289 ILE A 307 1 19 HELIX 16 AB7 ASN A 310 CYS A 322 1 13 HELIX 17 AB8 LEU B 341 VAL B 347 1 7 SHEET 1 AA1 2 THR A 4 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.03 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.43 LINK SG CYS A 323 C1 PLM A 407 1555 1555 1.62 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.43 LINK O3 BMA C 3 C1 BMA C 4 1555 1555 1.44 CRYST1 243.412 243.412 108.440 90.00 90.00 120.00 H 3 2 18 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 0.004108 0.002372 0.000000 0.00000 SCALE2 0.000000 0.004744 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009222 0.00000 ATOM 1 N ASN A 2 13.947 69.172 40.359 1.00103.74 N ANISOU 1 N ASN A 2 13753 9834 15831 1111 -1336 510 N ATOM 2 CA ASN A 2 14.282 68.238 41.430 1.00108.65 C ANISOU 2 CA ASN A 2 14319 10687 16276 1071 -1228 317 C ATOM 3 C ASN A 2 15.437 67.294 41.099 1.00109.42 C ANISOU 3 C ASN A 2 14448 10986 16140 924 -1190 410 C ATOM 4 O ASN A 2 16.025 66.708 42.002 1.00109.68 O ANISOU 4 O ASN A 2 14449 11165 16059 857 -1127 270 O ATOM 5 CB ASN A 2 13.056 67.407 41.809 1.00117.13 C ANISOU 5 CB ASN A 2 15290 11915 17299 1201 -1206 227 C ATOM 6 CG ASN A 2 12.016 68.213 42.555 1.00130.13 C ANISOU 6 CG ASN A 2 16867 13393 19185 1338 -1183 44 C ATOM 7 OD1 ASN A 2 12.335 68.940 43.497 1.00139.40 O ANISOU 7 OD1 ASN A 2 18062 14449 20455 1311 -1118 -150 O ATOM 8 ND2 ASN A 2 10.763 68.099 42.129 1.00122.30 N ANISOU 8 ND2 ASN A 2 15787 12377 18303 1482 -1235 100 N ATOM 9 N GLY A 3 15.764 67.135 39.817 1.00100.36 N ANISOU 9 N GLY A 3 13365 9840 14926 866 -1227 644 N ATOM 10 CA GLY A 3 16.813 66.240 39.396 1.00 89.73 C ANISOU 10 CA GLY A 3 12039 8667 13390 735 -1165 729 C ATOM 11 C GLY A 3 18.035 66.974 38.880 1.00 99.56 C ANISOU 11 C GLY A 3 13357 9776 14694 587 -1144 832 C ATOM 12 O GLY A 3 18.207 68.180 39.064 1.00 99.51 O ANISOU 12 O GLY A 3 13390 9548 14871 571 -1180 810 O ATOM 13 N THR A 4 18.892 66.214 38.210 1.00101.78 N ANISOU 13 N THR A 4 13655 10187 14830 473 -1073 942 N ATOM 14 CA THR A 4 20.148 66.756 37.707 1.00 74.17 C ANISOU 14 CA THR A 4 10207 6590 11383 312 -1018 1035 C ATOM 15 C THR A 4 20.545 65.891 36.524 1.00 73.57 C ANISOU 15 C THR A 4 10180 6641 11131 227 -935 1200 C ATOM 16 O THR A 4 21.051 64.783 36.719 1.00100.96 O ANISOU 16 O THR A 4 13571 10300 14490 196 -850 1149 O ATOM 17 CB THR A 4 21.231 66.728 38.767 1.00 73.90 C ANISOU 17 CB THR A 4 10080 6590 11409 227 -972 880 C ATOM 18 OG1 THR A 4 20.998 67.750 39.739 1.00 95.31 O ANISOU 18 OG1 THR A 4 12790 9140 14283 266 -1039 734 O ATOM 19 CG2 THR A 4 22.563 66.947 38.111 1.00 74.74 C ANISOU 19 CG2 THR A 4 10201 6646 11550 54 -889 991 C ATOM 20 N GLU A 5 20.335 66.385 35.318 1.00 74.89 N ANISOU 20 N GLU A 5 10487 6696 11273 180 -958 1395 N ATOM 21 CA GLU A 5 20.624 65.509 34.204 1.00 78.61 C ANISOU 21 CA GLU A 5 11030 7296 11544 88 -863 1531 C ATOM 22 C GLU A 5 22.018 65.713 33.640 1.00102.21 C ANISOU 22 C GLU A 5 14051 10242 14540 -104 -714 1603 C ATOM 23 O GLU A 5 22.799 66.583 34.042 1.00116.08 O ANISOU 23 O GLU A 5 15777 11862 16465 -178 -699 1570 O ATOM 24 CB GLU A 5 19.619 65.674 33.078 1.00 84.67 C ANISOU 24 CB GLU A 5 11954 8006 12211 112 -963 1718 C ATOM 25 CG GLU A 5 18.630 66.771 33.287 1.00107.13 C ANISOU 25 CG GLU A 5 14825 10651 15230 228 -1143 1744 C ATOM 26 CD GLU A 5 17.724 66.854 32.130 1.00107.16 C ANISOU 26 CD GLU A 5 14976 10602 15139 235 -1268 1952 C ATOM 27 OE1 GLU A 5 17.570 65.778 31.563 1.00110.90 O ANISOU 27 OE1 GLU A 5 15485 11257 15394 205 -1222 1997 O ATOM 28 OE2 GLU A 5 17.191 67.934 31.798 1.00122.62 O ANISOU 28 OE2 GLU A 5 17014 12339 17240 264 -1416 2069 O ATOM 29 N GLY A 6 22.292 64.874 32.661 1.00104.94 N ANISOU 29 N GLY A 6 14464 10707 14701 -192 -594 1699 N ATOM 30 CA GLY A 6 23.533 64.841 31.959 1.00105.43 C ANISOU 30 CA GLY A 6 14558 10758 14742 -380 -407 1767 C ATOM 31 C GLY A 6 23.409 63.916 30.772 1.00111.46 C ANISOU 31 C GLY A 6 15447 11644 15259 -454 -293 1872 C ATOM 32 O GLY A 6 22.365 63.306 30.507 1.00108.85 O ANISOU 32 O GLY A 6 15178 11405 14774 -361 -382 1899 O ATOM 33 N PRO A 7 24.519 63.772 30.066 1.00113.69 N ANISOU 33 N PRO A 7 15760 11930 15508 -632 -80 1919 N ATOM 34 CA PRO A 7 24.539 62.993 28.817 1.00112.53 C ANISOU 34 CA PRO A 7 15769 11874 15111 -745 73 2014 C ATOM 35 C PRO A 7 23.985 61.582 28.922 1.00116.66 C ANISOU 35 C PRO A 7 16240 12600 15486 -640 86 1926 C ATOM 36 O PRO A 7 23.238 61.160 28.032 1.00125.68 O ANISOU 36 O PRO A 7 17562 13793 16397 -663 60 2022 O ATOM 37 CB PRO A 7 26.032 62.975 28.465 1.00101.41 C ANISOU 37 CB PRO A 7 14305 10447 13778 -931 344 1999 C ATOM 38 CG PRO A 7 26.639 64.079 29.270 1.00100.35 C ANISOU 38 CG PRO A 7 14051 10164 13914 -941 280 1965 C ATOM 39 CD PRO A 7 25.861 64.153 30.516 1.00102.61 C ANISOU 39 CD PRO A 7 14212 10465 14308 -735 50 1851 C ATOM 40 N ASN A 8 24.342 60.825 29.954 1.00100.59 N ANISOU 40 N ASN A 8 13976 10676 13570 -540 116 1756 N ATOM 41 CA ASN A 8 23.942 59.424 30.010 1.00 81.88 C ANISOU 41 CA ASN A 8 11557 8488 11067 -460 151 1677 C ATOM 42 C ASN A 8 23.410 59.045 31.383 1.00 81.64 C ANISOU 42 C ASN A 8 11343 8536 11139 -275 -8 1539 C ATOM 43 O ASN A 8 23.626 57.925 31.854 1.00 95.54 O ANISOU 43 O ASN A 8 12972 10430 12899 -224 50 1432 O ATOM 44 CB ASN A 8 25.100 58.504 29.629 1.00 87.73 C ANISOU 44 CB ASN A 8 12218 9305 11811 -568 422 1617 C ATOM 45 CG ASN A 8 25.351 58.466 28.136 1.00102.48 C ANISOU 45 CG ASN A 8 14310 11149 13478 -752 616 1733 C ATOM 46 OD1 ASN A 8 24.457 58.742 27.336 1.00120.31 O ANISOU 46 OD1 ASN A 8 16801 13383 15526 -784 519 1861 O ATOM 47 ND2 ASN A 8 26.570 58.110 27.752 1.00 95.93 N ANISOU 47 ND2 ASN A 8 13411 10322 12717 -882 891 1688 N ATOM 48 N PHE A 9 22.696 59.948 32.046 1.00 86.66 N ANISOU 48 N PHE A 9 11975 9084 11866 -178 -205 1535 N ATOM 49 CA PHE A 9 22.166 59.632 33.370 1.00 96.05 C ANISOU 49 CA PHE A 9 13014 10347 13133 -23 -334 1392 C ATOM 50 C PHE A 9 21.110 60.659 33.761 1.00109.08 C ANISOU 50 C PHE A 9 14713 11885 14849 79 -526 1406 C ATOM 51 O PHE A 9 20.751 61.554 32.988 1.00100.64 O ANISOU 51 O PHE A 9 13787 10678 13773 42 -583 1540 O ATOM 52 CB PHE A 9 23.277 59.571 34.424 1.00110.61 C ANISOU 52 CB PHE A 9 14669 12199 15159 -45 -288 1265 C ATOM 53 CG PHE A 9 24.134 60.809 34.489 1.00112.34 C ANISOU 53 CG PHE A 9 14883 12247 15554 -146 -272 1292 C ATOM 54 CD1 PHE A 9 23.713 61.931 35.188 1.00106.45 C ANISOU 54 CD1 PHE A 9 14150 11373 14926 -93 -420 1258 C ATOM 55 CD2 PHE A 9 25.372 60.841 33.869 1.00 99.89 C ANISOU 55 CD2 PHE A 9 13282 10631 14040 -299 -95 1340 C ATOM 56 CE1 PHE A 9 24.503 63.062 35.253 1.00 95.04 C ANISOU 56 CE1 PHE A 9 12706 9760 13646 -194 -411 1279 C ATOM 57 CE2 PHE A 9 26.167 61.970 33.932 1.00 79.44 C ANISOU 57 CE2 PHE A 9 10680 7882 11620 -404 -80 1367 C ATOM 58 CZ PHE A 9 25.732 63.080 34.626 1.00 89.22 C ANISOU 58 CZ PHE A 9 11944 8992 12965 -353 -247 1340 C ATOM 59 N TYR A 10 20.618 60.505 34.989 1.00103.74 N ANISOU 59 N TYR A 10 13915 11259 14242 203 -621 1264 N ATOM 60 CA TYR A 10 19.662 61.426 35.595 1.00 84.72 C ANISOU 60 CA TYR A 10 11510 8742 11936 314 -772 1224 C ATOM 61 C TYR A 10 19.715 61.177 37.095 1.00 77.99 C ANISOU 61 C TYR A 10 10515 7959 11160 382 -800 1030 C ATOM 62 O TYR A 10 19.246 60.134 37.560 1.00 96.55 O ANISOU 62 O TYR A 10 12801 10472 13411 450 -804 955 O ATOM 63 CB TYR A 10 18.255 61.204 35.049 1.00 82.85 C ANISOU 63 CB TYR A 10 11345 8533 11600 413 -875 1299 C ATOM 64 CG TYR A 10 17.199 62.031 35.756 1.00 99.13 C ANISOU 64 CG TYR A 10 13369 10486 13807 549 -1012 1233 C ATOM 65 CD1 TYR A 10 16.560 61.555 36.898 1.00 67.58 C ANISOU 65 CD1 TYR A 10 9254 6592 9830 662 -1036 1064 C ATOM 66 CD2 TYR A 10 16.849 63.292 35.287 1.00 84.33 C ANISOU 66 CD2 TYR A 10 11580 8397 12064 558 -1107 1335 C ATOM 67 CE1 TYR A 10 15.611 62.307 37.550 1.00 76.83 C ANISOU 67 CE1 TYR A 10 10383 7659 11150 781 -1123 980 C ATOM 68 CE2 TYR A 10 15.897 64.051 35.932 1.00 83.45 C ANISOU 68 CE2 TYR A 10 11416 8166 12125 691 -1215 1260 C ATOM 69 CZ TYR A 10 15.280 63.555 37.063 1.00 90.89 C ANISOU 69 CZ TYR A 10 12230 9216 13087 804 -1209 1073 C ATOM 70 OH TYR A 10 14.328 64.310 37.711 1.00 74.15 O ANISOU 70 OH TYR A 10 10051 6971 11154 933 -1280 976 O ATOM 71 N VAL A 11 20.281 62.114 37.844 1.00 68.15 N ANISOU 71 N VAL A 11 9233 6588 10073 349 -823 951 N ATOM 72 CA VAL A 11 20.424 61.980 39.290 1.00 73.48 C ANISOU 72 CA VAL A 11 9805 7315 10800 379 -858 766 C ATOM 73 C VAL A 11 19.194 62.603 39.945 1.00 97.36 C ANISOU 73 C VAL A 11 12846 10270 13878 504 -945 669 C ATOM 74 O VAL A 11 18.999 63.823 39.827 1.00110.20 O ANISOU 74 O VAL A 11 14527 11701 15644 515 -989 684 O ATOM 75 CB VAL A 11 21.710 62.646 39.793 1.00 84.54 C ANISOU 75 CB VAL A 11 11162 8617 12343 258 -843 720 C ATOM 76 CG1 VAL A 11 21.817 62.515 41.307 1.00 68.19 C ANISOU 76 CG1 VAL A 11 9015 6598 10294 268 -905 534 C ATOM 77 CG2 VAL A 11 22.926 62.035 39.107 1.00 68.48 C ANISOU 77 CG2 VAL A 11 9081 6639 10298 138 -734 812 C ATOM 78 N PRO A 12 18.359 61.825 40.639 1.00 93.93 N ANISOU 78 N PRO A 12 12359 9976 13353 595 -963 564 N ATOM 79 CA PRO A 12 17.167 62.403 41.272 1.00 78.41 C ANISOU 79 CA PRO A 12 10391 7942 11460 714 -1013 453 C ATOM 80 C PRO A 12 17.510 63.276 42.469 1.00 90.41 C ANISOU 80 C PRO A 12 11904 9352 13096 683 -1022 278 C ATOM 81 O PRO A 12 17.089 62.994 43.595 1.00100.81 O ANISOU 81 O PRO A 12 13188 10746 14368 713 -1013 106 O ATOM 82 CB PRO A 12 16.368 61.167 41.693 1.00 65.88 C ANISOU 82 CB PRO A 12 8746 6561 9724 784 -1001 390 C ATOM 83 CG PRO A 12 17.420 60.143 41.964 1.00 88.94 C ANISOU 83 CG PRO A 12 11630 9634 12528 685 -962 386 C ATOM 84 CD PRO A 12 18.496 60.388 40.935 1.00 90.11 C ANISOU 84 CD PRO A 12 11812 9710 12715 588 -928 534 C ATOM 85 N PHE A 13 18.278 64.337 42.234 1.00 80.71 N ANISOU 85 N PHE A 13 10721 7942 12005 607 -1034 316 N ATOM 86 CA PHE A 13 18.679 65.251 43.295 1.00 84.58 C ANISOU 86 CA PHE A 13 11224 8304 12610 558 -1050 152 C ATOM 87 C PHE A 13 19.070 66.575 42.656 1.00 95.00 C ANISOU 87 C PHE A 13 12608 9374 14112 517 -1074 240 C ATOM 88 O PHE A 13 19.822 66.590 41.678 1.00 97.58 O ANISOU 88 O PHE A 13 12958 9677 14441 434 -1060 412 O ATOM 89 CB PHE A 13 19.836 64.668 44.107 1.00 80.49 C ANISOU 89 CB PHE A 13 10663 7905 12013 427 -1050 78 C ATOM 90 CG PHE A 13 20.132 65.417 45.372 1.00 81.89 C ANISOU 90 CG PHE A 13 10870 7989 12256 362 -1082 -117 C ATOM 91 CD1 PHE A 13 19.413 65.161 46.527 1.00 83.53 C ANISOU 91 CD1 PHE A 13 11090 8274 12375 401 -1076 -308 C ATOM 92 CD2 PHE A 13 21.140 66.365 45.413 1.00 80.73 C ANISOU 92 CD2 PHE A 13 10749 7679 12247 244 -1113 -113 C ATOM 93 CE1 PHE A 13 19.688 65.843 47.698 1.00 82.52 C ANISOU 93 CE1 PHE A 13 11018 8060 12275 318 -1098 -500 C ATOM 94 CE2 PHE A 13 21.422 67.048 46.581 1.00 85.54 C ANISOU 94 CE2 PHE A 13 11402 8199 12902 167 -1152 -300 C ATOM 95 CZ PHE A 13 20.693 66.786 47.725 1.00 84.89 C ANISOU 95 CZ PHE A 13 11351 8195 12710 202 -1145 -497 C ATOM 96 N SER A 14 18.555 67.676 43.203 1.00 93.62 N ANISOU 96 N SER A 14 12468 9008 14095 569 -1097 118 N ATOM 97 CA SER A 14 18.707 68.984 42.578 1.00 95.61 C ANISOU 97 CA SER A 14 12790 8994 14545 553 -1134 208 C ATOM 98 C SER A 14 20.111 69.539 42.790 1.00113.82 C ANISOU 98 C SER A 14 15120 11212 16913 380 -1133 202 C ATOM 99 O SER A 14 20.634 69.533 43.910 1.00106.59 O ANISOU 99 O SER A 14 14185 10331 15981 306 -1133 27 O ATOM 100 CB SER A 14 17.671 69.958 43.133 1.00104.59 C ANISOU 100 CB SER A 14 13940 9933 15864 677 -1152 62 C ATOM 101 OG SER A 14 17.862 71.254 42.596 1.00118.98 O ANISOU 101 OG SER A 14 15834 11475 17899 657 -1200 147 O ATOM 102 N ASN A 15 20.711 70.044 41.711 1.00114.77 N ANISOU 102 N ASN A 15 15290 11214 17103 301 -1139 397 N ATOM 103 CA ASN A 15 22.063 70.584 41.744 1.00104.46 C ANISOU 103 CA ASN A 15 13993 9817 15879 126 -1130 419 C ATOM 104 C ASN A 15 22.102 72.049 42.170 1.00 95.97 C ANISOU 104 C ASN A 15 12987 8457 15019 101 -1177 333 C ATOM 105 O ASN A 15 23.078 72.747 41.870 1.00 93.64 O ANISOU 105 O ASN A 15 12722 8025 14832 -41 -1179 405 O ATOM 106 CB ASN A 15 22.734 70.415 40.379 1.00104.43 C ANISOU 106 CB ASN A 15 14016 9822 15841 29 -1081 663 C ATOM 107 CG ASN A 15 24.235 70.358 40.485 1.00 97.16 C ANISOU 107 CG ASN A 15 13036 8926 14956 -156 -1033 674 C ATOM 108 OD1 ASN A 15 24.785 70.568 41.560 1.00 82.76 O ANISOU 108 OD1 ASN A 15 11161 7088 13198 -218 -1070 515 O ATOM 109 ND2 ASN A 15 24.909 70.075 39.381 1.00123.96 N ANISOU 109 ND2 ASN A 15 16436 12352 18311 -256 -949 857 N ATOM 110 N LYS A 16 21.062 72.526 42.860 1.00104.50 N ANISOU 110 N LYS A 16 14088 9438 16178 232 -1203 172 N ATOM 111 CA LYS A 16 21.033 73.911 43.323 1.00 84.58 C ANISOU 111 CA LYS A 16 11633 6626 13876 219 -1236 61 C ATOM 112 C LYS A 16 22.196 74.222 44.248 1.00 85.27 C ANISOU 112 C LYS A 16 11726 6692 13983 44 -1242 -82 C ATOM 113 O LYS A 16 22.612 75.379 44.354 1.00 99.95 O ANISOU 113 O LYS A 16 13650 8304 16023 -34 -1272 -113 O ATOM 114 CB LYS A 16 19.723 74.203 44.054 1.00 85.26 C ANISOU 114 CB LYS A 16 11718 6636 14040 392 -1226 -134 C ATOM 115 CG LYS A 16 18.568 74.392 43.161 1.00118.55 C ANISOU 115 CG LYS A 16 15931 10756 18358 560 -1259 4 C ATOM 116 CD LYS A 16 17.240 74.658 43.876 1.00152.76 C ANISOU 116 CD LYS A 16 20223 15005 22813 742 -1231 -197 C ATOM 117 CE LYS A 16 16.057 74.940 42.929 1.00161.27 C ANISOU 117 CE LYS A 16 21274 15950 24053 917 -1299 -37 C ATOM 118 NZ LYS A 16 14.805 75.291 43.601 1.00145.88 N ANISOU 118 NZ LYS A 16 19254 13887 22287 1096 -1260 -236 N ATOM 119 N THR A 17 22.712 73.215 44.944 1.00101.35 N ANISOU 119 N THR A 17 13696 8971 15843 -24 -1231 -167 N ATOM 120 CA THR A 17 23.824 73.384 45.866 1.00109.90 C ANISOU 120 CA THR A 17 14772 10055 16931 -202 -1272 -292 C ATOM 121 C THR A 17 25.168 73.018 45.248 1.00114.82 C ANISOU 121 C THR A 17 15318 10751 17556 -360 -1278 -117 C ATOM 122 O THR A 17 26.186 73.059 45.946 1.00115.21 O ANISOU 122 O THR A 17 15332 10816 17628 -517 -1332 -192 O ATOM 123 CB THR A 17 23.586 72.551 47.131 1.00109.29 C ANISOU 123 CB THR A 17 14674 10179 16671 -198 -1282 -497 C ATOM 124 OG1 THR A 17 23.019 71.284 46.774 1.00127.03 O ANISOU 124 OG1 THR A 17 16852 12669 18746 -88 -1242 -414 O ATOM 125 CG2 THR A 17 22.638 73.277 48.075 1.00 93.19 C ANISOU 125 CG2 THR A 17 12729 8002 14675 -123 -1259 -743 C ATOM 126 N GLY A 18 25.198 72.664 43.965 1.00103.85 N ANISOU 126 N GLY A 18 13903 9405 16150 -331 -1222 109 N ATOM 127 CA GLY A 18 26.452 72.413 43.282 1.00 89.44 C ANISOU 127 CA GLY A 18 12005 7622 14356 -484 -1186 268 C ATOM 128 C GLY A 18 27.137 71.118 43.644 1.00 93.52 C ANISOU 128 C GLY A 18 12386 8395 14754 -536 -1178 254 C ATOM 129 O GLY A 18 28.314 70.944 43.322 1.00115.22 O ANISOU 129 O GLY A 18 15039 11165 17574 -677 -1150 343 O ATOM 130 N VAL A 19 26.429 70.194 44.293 1.00 93.55 N ANISOU 130 N VAL A 19 12368 8584 14593 -427 -1198 151 N ATOM 131 CA VAL A 19 27.054 69.001 44.851 1.00 88.74 C ANISOU 131 CA VAL A 19 11637 8195 13885 -478 -1224 120 C ATOM 132 C VAL A 19 26.924 67.772 43.955 1.00 96.20 C ANISOU 132 C VAL A 19 12510 9329 14714 -406 -1133 263 C ATOM 133 O VAL A 19 27.752 66.854 44.064 1.00 96.04 O ANISOU 133 O VAL A 19 12363 9449 14681 -472 -1132 293 O ATOM 134 CB VAL A 19 26.465 68.699 46.244 1.00 82.34 C ANISOU 134 CB VAL A 19 10862 7472 12951 -438 -1309 -89 C ATOM 135 CG1 VAL A 19 26.831 69.803 47.221 1.00 80.58 C ANISOU 135 CG1 VAL A 19 10712 7075 12828 -552 -1398 -250 C ATOM 136 CG2 VAL A 19 24.953 68.547 46.153 1.00 77.55 C ANISOU 136 CG2 VAL A 19 10334 6900 12232 -251 -1257 -136 C ATOM 137 N VAL A 20 25.924 67.732 43.072 1.00 86.83 N ANISOU 137 N VAL A 20 11399 8139 13454 -280 -1067 351 N ATOM 138 CA VAL A 20 25.653 66.529 42.296 1.00 90.61 C ANISOU 138 CA VAL A 20 11837 8802 13791 -212 -988 461 C ATOM 139 C VAL A 20 26.812 66.221 41.358 1.00 94.13 C ANISOU 139 C VAL A 20 12205 9262 14296 -333 -886 609 C ATOM 140 O VAL A 20 27.352 67.109 40.684 1.00 85.32 O ANISOU 140 O VAL A 20 11130 7987 13302 -429 -840 702 O ATOM 141 CB VAL A 20 24.338 66.691 41.518 1.00 87.56 C ANISOU 141 CB VAL A 20 11559 8382 13327 -71 -965 534 C ATOM 142 CG1 VAL A 20 24.010 65.408 40.785 1.00 72.54 C ANISOU 142 CG1 VAL A 20 9629 6675 11259 -12 -896 630 C ATOM 143 CG2 VAL A 20 23.212 67.077 42.460 1.00 85.42 C ANISOU 143 CG2 VAL A 20 11337 8073 13048 48 -1040 371 C ATOM 144 N ARG A 21 27.195 64.944 41.310 1.00 86.17 N ANISOU 144 N ARG A 21 11086 8441 13214 -331 -839 627 N ATOM 145 CA ARG A 21 28.285 64.467 40.472 1.00 93.46 C ANISOU 145 CA ARG A 21 11910 9394 14205 -436 -710 739 C ATOM 146 C ARG A 21 27.814 63.279 39.643 1.00 95.77 C ANISOU 146 C ARG A 21 12211 9846 14334 -357 -601 814 C ATOM 147 O ARG A 21 26.832 62.612 39.977 1.00104.43 O ANISOU 147 O ARG A 21 13341 11060 15279 -232 -655 764 O ATOM 148 CB ARG A 21 29.503 64.061 41.311 1.00 74.61 C ANISOU 148 CB ARG A 21 9336 7050 11961 -536 -762 674 C ATOM 149 CG ARG A 21 30.017 65.146 42.239 1.00 78.22 C ANISOU 149 CG ARG A 21 9787 7363 12568 -634 -893 586 C ATOM 150 CD ARG A 21 30.774 66.210 41.473 1.00101.25 C ANISOU 150 CD ARG A 21 12717 10099 15656 -766 -809 679 C ATOM 151 NE ARG A 21 31.252 67.279 42.345 1.00109.36 N ANISOU 151 NE ARG A 21 13746 10973 16831 -869 -940 591 N ATOM 152 CZ ARG A 21 30.573 68.392 42.599 1.00 96.36 C ANISOU 152 CZ ARG A 21 12259 9173 15181 -844 -1005 534 C ATOM 153 NH1 ARG A 21 29.381 68.580 42.048 1.00100.84 N ANISOU 153 NH1 ARG A 21 12974 9718 15624 -711 -965 570 N ATOM 154 NH2 ARG A 21 31.082 69.314 43.403 1.00 95.00 N ANISOU 154 NH2 ARG A 21 12090 8859 15145 -953 -1118 441 N ATOM 155 N SER A 22 28.541 63.021 38.559 1.00 92.28 N ANISOU 155 N SER A 22 11740 9401 13923 -445 -436 926 N ATOM 156 CA SER A 22 28.201 61.935 37.651 1.00 79.88 C ANISOU 156 CA SER A 22 10196 7961 12195 -399 -307 994 C ATOM 157 C SER A 22 28.186 60.605 38.399 1.00 91.96 C ANISOU 157 C SER A 22 11593 9663 13683 -320 -350 905 C ATOM 158 O SER A 22 29.162 60.277 39.089 1.00104.89 O ANISOU 158 O SER A 22 13057 11319 15476 -375 -379 851 O ATOM 159 CB SER A 22 29.207 61.881 36.499 1.00 91.55 C ANISOU 159 CB SER A 22 11649 9398 13737 -538 -92 1097 C ATOM 160 OG SER A 22 28.920 60.840 35.581 1.00 72.88 O ANISOU 160 OG SER A 22 9331 7150 11209 -513 51 1147 O ATOM 161 N PRO A 23 27.109 59.819 38.298 1.00 93.82 N ANISOU 161 N PRO A 23 11901 10020 13725 -200 -371 897 N ATOM 162 CA PRO A 23 27.089 58.506 38.965 1.00 94.59 C ANISOU 162 CA PRO A 23 11884 10276 13781 -135 -409 827 C ATOM 163 C PRO A 23 28.150 57.547 38.453 1.00 97.81 C ANISOU 163 C PRO A 23 12151 10732 14281 -196 -258 858 C ATOM 164 O PRO A 23 28.382 56.511 39.091 1.00 90.94 O ANISOU 164 O PRO A 23 11154 9960 13439 -158 -305 806 O ATOM 165 CB PRO A 23 25.677 57.984 38.672 1.00 83.12 C ANISOU 165 CB PRO A 23 10559 8920 12104 -12 -431 836 C ATOM 166 CG PRO A 23 25.233 58.739 37.462 1.00 85.97 C ANISOU 166 CG PRO A 23 11082 9188 12396 -36 -357 947 C ATOM 167 CD PRO A 23 25.855 60.094 37.578 1.00 94.49 C ANISOU 167 CD PRO A 23 12170 10095 13637 -124 -379 962 C ATOM 168 N PHE A 24 28.790 57.850 37.328 1.00 87.56 N ANISOU 168 N PHE A 24 10872 9360 13037 -295 -72 939 N ATOM 169 CA PHE A 24 29.895 57.054 36.817 1.00 80.78 C ANISOU 169 CA PHE A 24 9860 8520 12311 -365 111 951 C ATOM 170 C PHE A 24 31.247 57.507 37.350 1.00 83.02 C ANISOU 170 C PHE A 24 9940 8712 12890 -470 101 929 C ATOM 171 O PHE A 24 32.257 56.870 37.036 1.00 87.75 O ANISOU 171 O PHE A 24 10365 9313 13664 -525 249 929 O ATOM 172 CB PHE A 24 29.924 57.107 35.285 1.00 74.67 C ANISOU 172 CB PHE A 24 9221 7717 11431 -443 353 1040 C ATOM 173 CG PHE A 24 28.658 56.637 34.630 1.00 80.13 C ANISOU 173 CG PHE A 24 10118 8494 11836 -365 357 1076 C ATOM 174 CD1 PHE A 24 28.038 55.467 35.040 1.00 85.67 C ANISOU 174 CD1 PHE A 24 10786 9328 12435 -248 292 1019 C ATOM 175 CD2 PHE A 24 28.088 57.368 33.599 1.00 70.61 C ANISOU 175 CD2 PHE A 24 9136 7225 10466 -419 408 1178 C ATOM 176 CE1 PHE A 24 26.876 55.035 34.432 1.00 82.80 C ANISOU 176 CE1 PHE A 24 10600 9039 11820 -186 286 1054 C ATOM 177 CE2 PHE A 24 26.926 56.946 32.989 1.00 71.58 C ANISOU 177 CE2 PHE A 24 9440 7420 10335 -357 382 1223 C ATOM 178 CZ PHE A 24 26.317 55.777 33.406 1.00 96.13 C ANISOU 178 CZ PHE A 24 12504 10668 13354 -241 324 1155 C ATOM 179 N GLU A 25 31.300 58.583 38.141 1.00 84.30 N ANISOU 179 N GLU A 25 10113 8787 13130 -502 -67 905 N ATOM 180 CA GLU A 25 32.583 59.216 38.428 1.00 83.35 C ANISOU 180 CA GLU A 25 9827 8556 13288 -633 -65 904 C ATOM 181 C GLU A 25 32.821 59.550 39.899 1.00 83.78 C ANISOU 181 C GLU A 25 9788 8589 13455 -640 -326 824 C ATOM 182 O GLU A 25 33.971 59.545 40.348 1.00 92.13 O ANISOU 182 O GLU A 25 10639 9601 14765 -731 -367 813 O ATOM 183 CB GLU A 25 32.730 60.486 37.584 1.00106.34 C ANISOU 183 CB GLU A 25 12866 11323 16216 -744 47 980 C ATOM 184 CG GLU A 25 32.691 60.260 36.069 1.00124.88 C ANISOU 184 CG GLU A 25 15323 13674 18451 -793 317 1072 C ATOM 185 CD GLU A 25 33.937 59.571 35.518 1.00131.12 C ANISOU 185 CD GLU A 25 15910 14471 19438 -888 553 1074 C ATOM 186 OE1 GLU A 25 34.803 59.139 36.309 1.00127.65 O ANISOU 186 OE1 GLU A 25 15217 14040 19245 -894 488 1015 O ATOM 187 OE2 GLU A 25 34.051 59.467 34.278 1.00133.22 O ANISOU 187 OE2 GLU A 25 16273 14727 19620 -964 807 1136 O ATOM 188 N ALA A 26 31.776 59.852 40.663 1.00 83.46 N ANISOU 188 N ALA A 26 9895 8578 13240 -557 -502 765 N ATOM 189 CA ALA A 26 31.976 60.215 42.059 1.00 76.24 C ANISOU 189 CA ALA A 26 8933 7641 12394 -588 -738 676 C ATOM 190 C ALA A 26 30.882 59.616 42.929 1.00 92.51 C ANISOU 190 C ALA A 26 11088 9825 14237 -470 -881 598 C ATOM 191 O ALA A 26 29.777 59.345 42.444 1.00108.22 O ANISOU 191 O ALA A 26 13214 11879 16026 -360 -813 608 O ATOM 192 CB ALA A 26 32.001 61.739 42.249 1.00 83.98 C ANISOU 192 CB ALA A 26 10016 8460 13432 -669 -797 655 C ATOM 193 N PRO A 27 31.167 59.386 44.212 1.00 83.94 N ANISOU 193 N PRO A 27 9937 8775 13183 -503 -1083 524 N ATOM 194 CA PRO A 27 30.139 58.860 45.118 1.00 97.05 C ANISOU 194 CA PRO A 27 11703 10551 14621 -417 -1209 443 C ATOM 195 C PRO A 27 28.941 59.792 45.238 1.00 95.10 C ANISOU 195 C PRO A 27 11666 10259 14210 -358 -1208 371 C ATOM 196 O PRO A 27 29.075 61.018 45.237 1.00 96.30 O ANISOU 196 O PRO A 27 11880 10268 14441 -417 -1217 345 O ATOM 197 CB PRO A 27 30.882 58.732 46.451 1.00 71.55 C ANISOU 197 CB PRO A 27 8385 7326 11475 -519 -1437 388 C ATOM 198 CG PRO A 27 32.289 58.509 46.060 1.00 77.24 C ANISOU 198 CG PRO A 27 8879 7991 12479 -608 -1413 471 C ATOM 199 CD PRO A 27 32.505 59.343 44.825 1.00 86.60 C ANISOU 199 CD PRO A 27 10077 9065 13763 -629 -1202 528 C ATOM 200 N GLN A 28 27.760 59.188 45.353 1.00 86.11 N ANISOU 200 N GLN A 28 10622 9233 12862 -239 -1198 337 N ATOM 201 CA GLN A 28 26.487 59.899 45.445 1.00 90.12 C ANISOU 201 CA GLN A 28 11299 9710 13235 -156 -1185 265 C ATOM 202 C GLN A 28 26.001 60.005 46.884 1.00 87.86 C ANISOU 202 C GLN A 28 11086 9459 12837 -172 -1323 114 C ATOM 203 O GLN A 28 24.803 59.869 47.147 1.00 75.21 O ANISOU 203 O GLN A 28 9581 7918 11078 -77 -1303 45 O ATOM 204 CB GLN A 28 25.433 59.205 44.586 1.00 87.90 C ANISOU 204 CB GLN A 28 11068 9523 12808 -23 -1074 324 C ATOM 205 CG GLN A 28 25.910 58.791 43.203 1.00 96.85 C ANISOU 205 CG GLN A 28 12147 10657 13996 -25 -929 465 C ATOM 206 CD GLN A 28 26.042 59.964 42.254 1.00110.25 C ANISOU 206 CD GLN A 28 13914 12195 15781 -62 -845 537 C ATOM 207 OE1 GLN A 28 25.052 60.606 41.899 1.00115.32 O ANISOU 207 OE1 GLN A 28 14682 12780 16356 8 -838 544 O ATOM 208 NE2 GLN A 28 27.268 60.253 41.838 1.00108.35 N ANISOU 208 NE2 GLN A 28 13585 11875 15709 -177 -786 597 N ATOM 209 N TYR A 29 26.901 60.248 47.839 1.00 71.16 N ANISOU 209 N TYR A 29 8932 7307 10797 -303 -1462 59 N ATOM 210 CA TYR A 29 26.484 60.274 49.243 1.00 83.47 C ANISOU 210 CA TYR A 29 10592 8912 12211 -349 -1592 -88 C ATOM 211 C TYR A 29 25.614 61.487 49.601 1.00 96.08 C ANISOU 211 C TYR A 29 12349 10395 13763 -326 -1556 -230 C ATOM 212 O TYR A 29 25.308 61.675 50.787 1.00104.59 O ANISOU 212 O TYR A 29 13531 11488 14721 -387 -1638 -380 O ATOM 213 CB TYR A 29 27.709 60.215 50.157 1.00 94.32 C ANISOU 213 CB TYR A 29 11896 10270 13670 -518 -1780 -99 C ATOM 214 CG TYR A 29 28.438 58.890 50.096 1.00 94.17 C ANISOU 214 CG TYR A 29 11715 10366 13700 -531 -1847 17 C ATOM 215 CD1 TYR A 29 27.777 57.702 50.372 1.00107.30 C ANISOU 215 CD1 TYR A 29 13398 12185 15186 -459 -1857 26 C ATOM 216 CD2 TYR A 29 29.786 58.827 49.768 1.00 82.69 C ANISOU 216 CD2 TYR A 29 10078 8850 12491 -617 -1896 117 C ATOM 217 CE1 TYR A 29 28.434 56.490 50.315 1.00128.07 C ANISOU 217 CE1 TYR A 29 15880 14897 17885 -465 -1923 132 C ATOM 218 CE2 TYR A 29 30.453 57.619 49.713 1.00 83.96 C ANISOU 218 CE2 TYR A 29 10070 9092 12739 -617 -1953 217 C ATOM 219 CZ TYR A 29 29.772 56.453 49.986 1.00118.83 C ANISOU 219 CZ TYR A 29 14518 13652 16978 -538 -1971 225 C ATOM 220 OH TYR A 29 30.429 55.245 49.931 1.00130.93 O ANISOU 220 OH TYR A 29 15883 15244 18621 -531 -2032 326 O ATOM 221 N TYR A 30 25.206 62.298 48.625 1.00 96.46 N ANISOU 221 N TYR A 30 12424 10323 13903 -246 -1437 -190 N ATOM 222 CA TYR A 30 24.281 63.397 48.864 1.00105.47 C ANISOU 222 CA TYR A 30 13697 11337 15040 -194 -1394 -316 C ATOM 223 C TYR A 30 22.821 62.999 48.682 1.00108.87 C ANISOU 223 C TYR A 30 14176 11849 15341 -32 -1301 -350 C ATOM 224 O TYR A 30 21.940 63.673 49.226 1.00120.35 O ANISOU 224 O TYR A 30 15723 13230 16773 14 -1270 -498 O ATOM 225 CB TYR A 30 24.607 64.568 47.934 1.00 91.74 C ANISOU 225 CB TYR A 30 11965 9395 13497 -199 -1341 -241 C ATOM 226 CG TYR A 30 24.856 64.136 46.512 1.00 80.42 C ANISOU 226 CG TYR A 30 10451 7987 12118 -151 -1251 -40 C ATOM 227 CD1 TYR A 30 23.799 63.878 45.647 1.00 81.19 C ANISOU 227 CD1 TYR A 30 10583 8119 12146 -8 -1162 31 C ATOM 228 CD2 TYR A 30 26.147 63.971 46.037 1.00 72.36 C ANISOU 228 CD2 TYR A 30 9321 6954 11219 -261 -1251 74 C ATOM 229 CE1 TYR A 30 24.025 63.473 44.348 1.00 89.75 C ANISOU 229 CE1 TYR A 30 11627 9228 13244 11 -1078 207 C ATOM 230 CE2 TYR A 30 26.383 63.569 44.742 1.00 79.96 C ANISOU 230 CE2 TYR A 30 10229 7938 12213 -235 -1137 238 C ATOM 231 CZ TYR A 30 25.321 63.321 43.901 1.00100.97 C ANISOU 231 CZ TYR A 30 12958 10639 14768 -105 -1052 303 C ATOM 232 OH TYR A 30 25.561 62.919 42.608 1.00116.63 O ANISOU 232 OH TYR A 30 14919 12645 16752 -103 -938 460 O ATOM 233 N LEU A 31 22.539 61.938 47.924 1.00 91.14 N ANISOU 233 N LEU A 31 11863 9741 13026 51 -1251 -224 N ATOM 234 CA LEU A 31 21.178 61.439 47.785 1.00 91.97 C ANISOU 234 CA LEU A 31 11997 9939 13010 191 -1182 -249 C ATOM 235 C LEU A 31 20.882 60.271 48.714 1.00 93.39 C ANISOU 235 C LEU A 31 12174 10311 12999 175 -1218 -318 C ATOM 236 O LEU A 31 19.789 59.701 48.641 1.00108.73 O ANISOU 236 O LEU A 31 14126 12351 14836 277 -1159 -335 O ATOM 237 CB LEU A 31 20.887 61.040 46.330 1.00 77.25 C ANISOU 237 CB LEU A 31 10089 8096 11166 286 -1108 -72 C ATOM 238 CG LEU A 31 21.794 60.151 45.476 1.00 82.31 C ANISOU 238 CG LEU A 31 10645 8818 11812 245 -1088 89 C ATOM 239 CD1 LEU A 31 22.001 58.767 46.066 1.00116.85 C ANISOU 239 CD1 LEU A 31 14958 13378 16063 224 -1126 78 C ATOM 240 CD2 LEU A 31 21.191 60.032 44.086 1.00 85.85 C ANISOU 240 CD2 LEU A 31 11113 9259 12248 335 -1004 226 C ATOM 241 N ALA A 32 21.829 59.904 49.574 1.00 84.24 N ANISOU 241 N ALA A 32 11002 9202 11802 41 -1325 -346 N ATOM 242 CA ALA A 32 21.659 58.850 50.562 1.00 87.89 C ANISOU 242 CA ALA A 32 11485 9831 12079 -6 -1389 -401 C ATOM 243 C ALA A 32 22.893 58.824 51.447 1.00 92.72 C ANISOU 243 C ALA A 32 12091 10433 12706 -178 -1550 -415 C ATOM 244 O ALA A 32 24.014 58.942 50.949 1.00 97.77 O ANISOU 244 O ALA A 32 12630 11008 13510 -232 -1602 -308 O ATOM 245 CB ALA A 32 21.455 57.477 49.906 1.00 95.44 C ANISOU 245 CB ALA A 32 12357 10938 12968 71 -1359 -267 C ATOM 246 N GLU A 33 22.679 58.674 52.755 1.00 88.03 N ANISOU 246 N GLU A 33 11607 9901 11941 -276 -1630 -546 N ATOM 247 CA GLU A 33 23.791 58.513 53.671 1.00 81.73 C ANISOU 247 CA GLU A 33 10816 9109 11128 -456 -1825 -545 C ATOM 248 C GLU A 33 24.621 57.301 53.257 1.00 93.16 C ANISOU 248 C GLU A 33 12106 10647 12643 -458 -1917 -361 C ATOM 249 O GLU A 33 24.138 56.425 52.535 1.00108.71 O ANISOU 249 O GLU A 33 14008 12707 14589 -336 -1824 -272 O ATOM 250 CB GLU A 33 23.287 58.336 55.102 1.00 88.42 C ANISOU 250 CB GLU A 33 11837 10037 11722 -569 -1890 -700 C ATOM 251 CG GLU A 33 22.275 59.363 55.558 1.00104.83 C ANISOU 251 CG GLU A 33 14069 12040 13722 -551 -1752 -912 C ATOM 252 CD GLU A 33 22.617 59.932 56.918 1.00124.64 C ANISOU 252 CD GLU A 33 16754 14507 16096 -755 -1864 -1078 C ATOM 253 OE1 GLU A 33 23.756 60.417 57.082 1.00125.97 O ANISOU 253 OE1 GLU A 33 16904 14582 16376 -882 -2021 -1045 O ATOM 254 OE2 GLU A 33 21.757 59.886 57.824 1.00135.32 O ANISOU 254 OE2 GLU A 33 18268 15922 17228 -802 -1792 -1245 O ATOM 255 N PRO A 34 25.882 57.230 53.689 1.00 92.85 N ANISOU 255 N PRO A 34 11997 10572 12708 -598 -2102 -303 N ATOM 256 CA PRO A 34 26.677 56.040 53.364 1.00 88.87 C ANISOU 256 CA PRO A 34 11323 10137 12306 -594 -2190 -137 C ATOM 257 C PRO A 34 26.105 54.762 53.947 1.00102.25 C ANISOU 257 C PRO A 34 13067 11989 13795 -583 -2248 -116 C ATOM 258 O PRO A 34 26.197 53.709 53.305 1.00109.70 O ANISOU 258 O PRO A 34 13887 12997 14799 -496 -2214 6 O ATOM 259 CB PRO A 34 28.054 56.371 53.956 1.00 79.90 C ANISOU 259 CB PRO A 34 10114 8917 11329 -765 -2410 -104 C ATOM 260 CG PRO A 34 28.089 57.841 54.011 1.00 73.18 C ANISOU 260 CG PRO A 34 9350 7927 10530 -819 -2369 -217 C ATOM 261 CD PRO A 34 26.697 58.248 54.369 1.00 72.74 C ANISOU 261 CD PRO A 34 9498 7903 10238 -759 -2238 -376 C ATOM 262 N TRP A 35 25.500 54.821 55.139 1.00 93.24 N ANISOU 262 N TRP A 35 12113 10907 12406 -678 -2319 -238 N ATOM 263 CA TRP A 35 24.979 53.602 55.746 1.00 85.85 C ANISOU 263 CA TRP A 35 11239 10118 11261 -693 -2379 -209 C ATOM 264 C TRP A 35 23.854 53.005 54.915 1.00 81.23 C ANISOU 264 C TRP A 35 10633 9618 10614 -513 -2167 -193 C ATOM 265 O TRP A 35 23.631 51.790 54.955 1.00107.01 O ANISOU 265 O TRP A 35 13871 12989 13798 -487 -2198 -109 O ATOM 266 CB TRP A 35 24.517 53.866 57.183 1.00 80.47 C ANISOU 266 CB TRP A 35 10793 9482 10300 -855 -2468 -356 C ATOM 267 CG TRP A 35 23.270 54.682 57.322 1.00 76.91 C ANISOU 267 CG TRP A 35 10494 9027 9700 -803 -2253 -549 C ATOM 268 CD1 TRP A 35 23.192 56.020 57.558 1.00 79.25 C ANISOU 268 CD1 TRP A 35 10886 9205 10022 -846 -2193 -706 C ATOM 269 CD2 TRP A 35 21.918 54.204 57.266 1.00103.75 C ANISOU 269 CD2 TRP A 35 13956 12533 12930 -702 -2070 -611 C ATOM 270 NE1 TRP A 35 21.876 56.412 57.636 1.00100.99 N ANISOU 270 NE1 TRP A 35 13745 11976 12652 -764 -1977 -864 N ATOM 271 CE2 TRP A 35 21.075 55.315 57.460 1.00 96.40 C ANISOU 271 CE2 TRP A 35 13139 11537 11952 -677 -1899 -808 C ATOM 272 CE3 TRP A 35 21.341 52.947 57.062 1.00103.28 C ANISOU 272 CE3 TRP A 35 13859 12608 12774 -630 -2035 -521 C ATOM 273 CZ2 TRP A 35 19.686 55.207 57.456 1.00 78.07 C ANISOU 273 CZ2 TRP A 35 10871 9282 9509 -581 -1694 -914 C ATOM 274 CZ3 TRP A 35 19.964 52.842 57.060 1.00 80.91 C ANISOU 274 CZ3 TRP A 35 11093 9849 9798 -547 -1837 -623 C ATOM 275 CH2 TRP A 35 19.151 53.965 57.255 1.00 70.97 C ANISOU 275 CH2 TRP A 35 9926 8526 8514 -520 -1668 -817 C ATOM 276 N GLN A 36 23.146 53.833 54.146 1.00 75.31 N ANISOU 276 N GLN A 36 9892 8813 9912 -393 -1967 -262 N ATOM 277 CA GLN A 36 22.113 53.307 53.263 1.00 71.29 C ANISOU 277 CA GLN A 36 9349 8373 9366 -229 -1789 -231 C ATOM 278 C GLN A 36 22.718 52.582 52.069 1.00 80.85 C ANISOU 278 C GLN A 36 10389 9581 10751 -141 -1762 -63 C ATOM 279 O GLN A 36 22.135 51.610 51.578 1.00 87.86 O ANISOU 279 O GLN A 36 11246 10560 11577 -52 -1692 -3 O ATOM 280 CB GLN A 36 21.189 54.438 52.818 1.00 68.77 C ANISOU 280 CB GLN A 36 9087 7978 9067 -134 -1617 -342 C ATOM 281 CG GLN A 36 20.360 54.988 53.970 1.00 83.41 C ANISOU 281 CG GLN A 36 11106 9844 10741 -199 -1588 -535 C ATOM 282 CD GLN A 36 19.697 56.306 53.654 1.00100.23 C ANISOU 282 CD GLN A 36 13275 11846 12960 -120 -1447 -657 C ATOM 283 OE1 GLN A 36 20.227 57.117 52.899 1.00107.61 O ANISOU 283 OE1 GLN A 36 14151 12648 14089 -85 -1437 -609 O ATOM 284 NE2 GLN A 36 18.528 56.531 54.237 1.00125.08 N ANISOU 284 NE2 GLN A 36 16520 15023 15983 -96 -1331 -815 N ATOM 285 N PHE A 37 23.885 53.029 51.595 1.00 77.88 N ANISOU 285 N PHE A 37 9900 9096 10593 -175 -1804 5 N ATOM 286 CA PHE A 37 24.616 52.245 50.606 1.00 80.16 C ANISOU 286 CA PHE A 37 10023 9381 11054 -121 -1772 149 C ATOM 287 C PHE A 37 25.138 50.948 51.209 1.00 80.72 C ANISOU 287 C PHE A 37 10028 9527 11117 -173 -1927 228 C ATOM 288 O PHE A 37 25.204 49.924 50.518 1.00 87.27 O ANISOU 288 O PHE A 37 10760 10395 12003 -96 -1869 319 O ATOM 289 CB PHE A 37 25.769 53.065 50.026 1.00 69.25 C ANISOU 289 CB PHE A 37 8528 7860 9922 -163 -1765 194 C ATOM 290 CG PHE A 37 25.331 54.147 49.085 1.00 68.45 C ANISOU 290 CG PHE A 37 8471 7672 9863 -95 -1596 168 C ATOM 291 CD1 PHE A 37 25.023 55.412 49.557 1.00 81.83 C ANISOU 291 CD1 PHE A 37 10278 9283 11531 -135 -1608 59 C ATOM 292 CD2 PHE A 37 25.236 53.903 47.725 1.00 71.42 C ANISOU 292 CD2 PHE A 37 8790 8040 10307 -1 -1430 256 C ATOM 293 CE1 PHE A 37 24.619 56.414 48.690 1.00 87.73 C ANISOU 293 CE1 PHE A 37 11065 9929 12338 -71 -1474 52 C ATOM 294 CE2 PHE A 37 24.835 54.901 46.853 1.00 80.53 C ANISOU 294 CE2 PHE A 37 10002 9106 11490 46 -1302 255 C ATOM 295 CZ PHE A 37 24.524 56.157 47.337 1.00 80.06 C ANISOU 295 CZ PHE A 37 10041 8954 11426 17 -1332 161 C ATOM 296 N SER A 38 25.510 50.972 52.491 1.00 72.95 N ANISOU 296 N SER A 38 9105 8552 10060 -310 -2133 195 N ATOM 297 CA SER A 38 25.913 49.748 53.172 1.00 65.58 C ANISOU 297 CA SER A 38 8134 7683 9101 -371 -2316 282 C ATOM 298 C SER A 38 24.753 48.767 53.270 1.00 83.34 C ANISOU 298 C SER A 38 10478 10063 11126 -305 -2247 277 C ATOM 299 O SER A 38 24.943 47.554 53.124 1.00 78.93 O ANISOU 299 O SER A 38 9838 9544 10609 -275 -2296 382 O ATOM 300 CB SER A 38 26.455 50.073 54.564 1.00 67.60 C ANISOU 300 CB SER A 38 8479 7922 9283 -557 -2570 250 C ATOM 301 OG SER A 38 27.724 50.695 54.491 1.00 69.63 O ANISOU 301 OG SER A 38 8604 8058 9795 -631 -2683 291 O ATOM 302 N MET A 39 23.541 49.274 53.518 1.00 87.19 N ANISOU 302 N MET A 39 11127 10608 11395 -284 -2128 153 N ATOM 303 CA MET A 39 22.376 48.399 53.588 1.00 62.67 C ANISOU 303 CA MET A 39 8098 7625 8088 -228 -2046 141 C ATOM 304 C MET A 39 21.975 47.894 52.212 1.00 76.76 C ANISOU 304 C MET A 39 9779 9422 9964 -66 -1870 206 C ATOM 305 O MET A 39 21.487 46.765 52.086 1.00 88.54 O ANISOU 305 O MET A 39 11267 10998 11377 -25 -1853 260 O ATOM 306 CB MET A 39 21.207 49.125 54.251 1.00 62.98 C ANISOU 306 CB MET A 39 8314 7711 7904 -254 -1951 -23 C ATOM 307 CG MET A 39 21.407 49.377 55.732 1.00 76.45 C ANISOU 307 CG MET A 39 10176 9435 9437 -442 -2110 -102 C ATOM 308 SD MET A 39 21.986 47.904 56.601 1.00 80.39 S ANISOU 308 SD MET A 39 10693 10012 9840 -571 -2360 40 S ATOM 309 CE MET A 39 20.663 46.747 56.251 1.00 95.60 C ANISOU 309 CE MET A 39 12642 12073 11610 -466 -2201 60 C ATOM 310 N LEU A 40 22.157 48.714 51.177 1.00 75.00 N ANISOU 310 N LEU A 40 9489 9113 9893 12 -1743 204 N ATOM 311 CA LEU A 40 22.015 48.226 49.811 1.00 80.82 C ANISOU 311 CA LEU A 40 10138 9848 10722 134 -1597 281 C ATOM 312 C LEU A 40 22.933 47.033 49.571 1.00102.00 C ANISOU 312 C LEU A 40 12690 12527 13538 130 -1662 397 C ATOM 313 O LEU A 40 22.494 45.980 49.092 1.00106.13 O ANISOU 313 O LEU A 40 13197 13110 14017 194 -1602 445 O ATOM 314 CB LEU A 40 22.314 49.363 48.832 1.00 72.84 C ANISOU 314 CB LEU A 40 9091 8727 9857 177 -1481 277 C ATOM 315 CG LEU A 40 22.212 49.153 47.321 1.00 81.79 C ANISOU 315 CG LEU A 40 10171 9839 11067 274 -1316 349 C ATOM 316 CD1 LEU A 40 20.940 48.421 46.960 1.00 57.22 C ANISOU 316 CD1 LEU A 40 7124 6831 7786 358 -1239 347 C ATOM 317 CD2 LEU A 40 22.262 50.502 46.614 1.00 96.84 C ANISOU 317 CD2 LEU A 40 12101 11637 13058 290 -1226 333 C ATOM 318 N ALA A 41 24.211 47.174 49.934 1.00 91.76 N ANISOU 318 N ALA A 41 11291 11149 12424 50 -1793 441 N ATOM 319 CA ALA A 41 25.164 46.080 49.772 1.00 75.52 C ANISOU 319 CA ALA A 41 9078 9062 10552 50 -1866 549 C ATOM 320 C ALA A 41 24.774 44.874 50.615 1.00 92.67 C ANISOU 320 C ALA A 41 11303 11320 12587 21 -2005 588 C ATOM 321 O ALA A 41 24.952 43.726 50.190 1.00 97.60 O ANISOU 321 O ALA A 41 11840 11945 13299 75 -1989 664 O ATOM 322 CB ALA A 41 26.568 46.557 50.138 1.00 80.68 C ANISOU 322 CB ALA A 41 9599 9606 11450 -41 -2010 586 C ATOM 323 N ALA A 42 24.245 45.114 51.818 1.00 96.18 N ANISOU 323 N ALA A 42 11901 11830 12813 -74 -2134 533 N ATOM 324 CA ALA A 42 23.826 44.012 52.676 1.00 76.65 C ANISOU 324 CA ALA A 42 9507 9441 10175 -127 -2266 576 C ATOM 325 C ALA A 42 22.701 43.217 52.030 1.00 76.92 C ANISOU 325 C ALA A 42 9583 9561 10082 -22 -2099 571 C ATOM 326 O ALA A 42 22.727 41.981 52.013 1.00 93.48 O ANISOU 326 O ALA A 42 11643 11678 12198 -6 -2150 656 O ATOM 327 CB ALA A 42 23.396 44.541 54.045 1.00 62.61 C ANISOU 327 CB ALA A 42 7918 7721 8149 -270 -2394 496 C ATOM 328 N TYR A 43 21.701 43.910 51.482 1.00 75.82 N ANISOU 328 N TYR A 43 9516 9463 9829 48 -1909 477 N ATOM 329 CA TYR A 43 20.602 43.198 50.845 1.00 76.59 C ANISOU 329 CA TYR A 43 9647 9641 9813 138 -1767 475 C ATOM 330 C TYR A 43 21.079 42.427 49.620 1.00 82.56 C ANISOU 330 C TYR A 43 10273 10346 10749 232 -1679 559 C ATOM 331 O TYR A 43 20.608 41.314 49.361 1.00100.41 O ANISOU 331 O TYR A 43 12539 12655 12957 268 -1651 600 O ATOM 332 CB TYR A 43 19.474 44.157 50.470 1.00 67.51 C ANISOU 332 CB TYR A 43 8577 8526 8548 197 -1605 369 C ATOM 333 CG TYR A 43 18.197 43.404 50.189 1.00 88.98 C ANISOU 333 CG TYR A 43 11347 11348 11116 253 -1508 359 C ATOM 334 CD1 TYR A 43 17.543 42.721 51.207 1.00 92.54 C ANISOU 334 CD1 TYR A 43 11888 11895 11378 178 -1571 341 C ATOM 335 CD2 TYR A 43 17.663 43.343 48.908 1.00 84.29 C ANISOU 335 CD2 TYR A 43 10715 10750 10560 362 -1364 376 C ATOM 336 CE1 TYR A 43 16.386 42.015 50.965 1.00 86.98 C ANISOU 336 CE1 TYR A 43 11216 11282 10551 218 -1482 335 C ATOM 337 CE2 TYR A 43 16.503 42.638 48.655 1.00 76.59 C ANISOU 337 CE2 TYR A 43 9778 9866 9457 402 -1296 372 C ATOM 338 CZ TYR A 43 15.870 41.975 49.688 1.00 94.56 C ANISOU 338 CZ TYR A 43 12123 12236 11571 333 -1352 349 C ATOM 339 OH TYR A 43 14.717 41.265 49.446 1.00117.21 O ANISOU 339 OH TYR A 43 15015 15192 14327 363 -1283 346 O ATOM 340 N MET A 44 22.012 42.997 48.854 1.00 81.08 N ANISOU 340 N MET A 44 9976 10056 10773 261 -1622 577 N ATOM 341 CA MET A 44 22.597 42.241 47.751 1.00 79.40 C ANISOU 341 CA MET A 44 9643 9784 10741 329 -1520 641 C ATOM 342 C MET A 44 23.301 40.992 48.266 1.00 87.78 C ANISOU 342 C MET A 44 10613 10817 11924 302 -1663 724 C ATOM 343 O MET A 44 23.212 39.922 47.653 1.00 79.05 O ANISOU 343 O MET A 44 9467 9705 10863 360 -1590 761 O ATOM 344 CB MET A 44 23.566 43.118 46.957 1.00 87.04 C ANISOU 344 CB MET A 44 10508 10644 11921 338 -1426 642 C ATOM 345 CG MET A 44 22.928 44.329 46.293 1.00 71.31 C ANISOU 345 CG MET A 44 8605 8653 9837 368 -1288 584 C ATOM 346 SD MET A 44 21.523 43.917 45.238 1.00 84.06 S ANISOU 346 SD MET A 44 10330 10349 11258 457 -1122 571 S ATOM 347 CE MET A 44 20.159 44.394 46.296 1.00 68.17 C ANISOU 347 CE MET A 44 8454 8439 9009 446 -1204 494 C ATOM 348 N PHE A 45 23.996 41.109 49.401 1.00 87.93 N ANISOU 348 N PHE A 45 10604 10807 11998 209 -1880 757 N ATOM 349 CA PHE A 45 24.630 39.945 50.011 1.00 80.45 C ANISOU 349 CA PHE A 45 9575 9820 11170 175 -2065 857 C ATOM 350 C PHE A 45 23.600 38.879 50.353 1.00 84.47 C ANISOU 350 C PHE A 45 10206 10423 11464 177 -2088 876 C ATOM 351 O PHE A 45 23.814 37.690 50.090 1.00 95.25 O ANISOU 351 O PHE A 45 11499 11747 12945 218 -2103 947 O ATOM 352 CB PHE A 45 25.404 40.370 51.260 1.00 78.79 C ANISOU 352 CB PHE A 45 9356 9575 11004 48 -2330 894 C ATOM 353 CG PHE A 45 26.323 39.312 51.797 1.00 78.24 C ANISOU 353 CG PHE A 45 9161 9424 11142 12 -2556 1023 C ATOM 354 CD1 PHE A 45 27.259 38.708 50.973 1.00 80.88 C ANISOU 354 CD1 PHE A 45 9272 9636 11823 97 -2496 1079 C ATOM 355 CD2 PHE A 45 26.271 38.939 53.131 1.00 80.28 C ANISOU 355 CD2 PHE A 45 9527 9717 11258 -114 -2830 1088 C ATOM 356 CE1 PHE A 45 28.112 37.738 51.463 1.00 76.14 C ANISOU 356 CE1 PHE A 45 8530 8936 11462 77 -2713 1201 C ATOM 357 CE2 PHE A 45 27.127 37.969 53.630 1.00 78.40 C ANISOU 357 CE2 PHE A 45 9173 9387 11230 -150 -3074 1228 C ATOM 358 CZ PHE A 45 28.046 37.368 52.793 1.00 66.51 C ANISOU 358 CZ PHE A 45 7417 7747 10108 -44 -3020 1287 C ATOM 359 N LEU A 46 22.471 39.290 50.935 1.00 82.99 N ANISOU 359 N LEU A 46 10198 10354 10980 131 -2077 809 N ATOM 360 CA LEU A 46 21.389 38.355 51.230 1.00 70.99 C ANISOU 360 CA LEU A 46 8794 8933 9246 123 -2071 818 C ATOM 361 C LEU A 46 20.921 37.644 49.966 1.00 84.34 C ANISOU 361 C LEU A 46 10440 10623 10982 240 -1880 818 C ATOM 362 O LEU A 46 20.827 36.412 49.930 1.00 83.43 O ANISOU 362 O LEU A 46 10313 10500 10887 251 -1915 883 O ATOM 363 CB LEU A 46 20.231 39.107 51.891 1.00 72.71 C ANISOU 363 CB LEU A 46 9184 9270 9173 65 -2028 716 C ATOM 364 CG LEU A 46 19.137 38.319 52.615 1.00 77.58 C ANISOU 364 CG LEU A 46 9940 10000 9537 1 -2052 716 C ATOM 365 CD1 LEU A 46 19.734 37.504 53.740 1.00 77.29 C ANISOU 365 CD1 LEU A 46 9943 9945 9478 -125 -2299 823 C ATOM 366 CD2 LEU A 46 18.073 39.253 53.157 1.00 71.67 C ANISOU 366 CD2 LEU A 46 9326 9349 8554 -44 -1960 586 C ATOM 367 N LEU A 47 20.641 38.408 48.907 1.00 89.38 N ANISOU 367 N LEU A 47 11066 11260 11635 318 -1686 751 N ATOM 368 CA LEU A 47 20.126 37.816 47.676 1.00 77.79 C ANISOU 368 CA LEU A 47 9591 9799 10169 406 -1509 744 C ATOM 369 C LEU A 47 21.134 36.878 47.025 1.00 80.88 C ANISOU 369 C LEU A 47 9849 10076 10806 448 -1484 805 C ATOM 370 O LEU A 47 20.739 35.965 46.293 1.00 90.88 O ANISOU 370 O LEU A 47 11127 11343 12060 495 -1383 809 O ATOM 371 CB LEU A 47 19.722 38.914 46.693 1.00 83.02 C ANISOU 371 CB LEU A 47 10279 10468 10798 460 -1338 678 C ATOM 372 CG LEU A 47 18.615 39.871 47.137 1.00 81.59 C ANISOU 372 CG LEU A 47 10208 10376 10415 446 -1327 605 C ATOM 373 CD1 LEU A 47 18.464 40.995 46.127 1.00 86.17 C ANISOU 373 CD1 LEU A 47 10793 10921 11026 501 -1192 567 C ATOM 374 CD2 LEU A 47 17.299 39.130 47.317 1.00 88.36 C ANISOU 374 CD2 LEU A 47 11152 11344 11077 448 -1310 591 C ATOM 375 N ILE A 48 22.430 37.086 47.258 1.00 92.76 N ANISOU 375 N ILE A 48 11218 11474 12551 431 -1566 843 N ATOM 376 CA ILE A 48 23.429 36.173 46.709 1.00 94.50 C ANISOU 376 CA ILE A 48 11281 11568 13055 476 -1534 891 C ATOM 377 C ILE A 48 23.525 34.914 47.558 1.00 83.16 C ANISOU 377 C ILE A 48 9828 10107 11661 449 -1725 977 C ATOM 378 O ILE A 48 23.517 33.792 47.040 1.00 89.01 O ANISOU 378 O ILE A 48 10533 10794 12493 500 -1661 997 O ATOM 379 CB ILE A 48 24.798 36.869 46.591 1.00 91.45 C ANISOU 379 CB ILE A 48 10724 11066 12956 469 -1542 902 C ATOM 380 CG1 ILE A 48 24.738 38.021 45.585 1.00 80.54 C ANISOU 380 CG1 ILE A 48 9366 9690 11545 491 -1328 828 C ATOM 381 CG2 ILE A 48 25.868 35.861 46.194 1.00 63.22 C ANISOU 381 CG2 ILE A 48 6955 7346 9721 515 -1520 948 C ATOM 382 CD1 ILE A 48 25.789 39.087 45.819 1.00 60.15 C ANISOU 382 CD1 ILE A 48 6670 7033 9151 447 -1378 831 C ATOM 383 N MET A 49 23.612 35.088 48.880 1.00 91.63 N ANISOU 383 N MET A 49 10944 11212 12660 357 -1968 1030 N ATOM 384 CA MET A 49 23.769 33.949 49.777 1.00 77.35 C ANISOU 384 CA MET A 49 9134 9368 10885 308 -2189 1138 C ATOM 385 C MET A 49 22.565 33.020 49.721 1.00 71.51 C ANISOU 385 C MET A 49 8537 8715 9920 313 -2135 1136 C ATOM 386 O MET A 49 22.716 31.799 49.843 1.00 89.39 O ANISOU 386 O MET A 49 10768 10909 12287 321 -2219 1215 O ATOM 387 CB MET A 49 24.002 34.444 51.206 1.00 75.39 C ANISOU 387 CB MET A 49 8954 9155 10537 176 -2459 1191 C ATOM 388 CG MET A 49 25.317 35.187 51.408 1.00 75.70 C ANISOU 388 CG MET A 49 8836 9089 10838 151 -2576 1218 C ATOM 389 SD MET A 49 26.770 34.123 51.259 1.00106.25 S ANISOU 389 SD MET A 49 12435 12752 15185 202 -2717 1346 S ATOM 390 CE MET A 49 27.242 34.362 49.545 1.00 97.70 C ANISOU 390 CE MET A 49 11172 11585 14366 348 -2357 1245 C ATOM 391 N LEU A 50 21.367 33.569 49.538 1.00 68.17 N ANISOU 391 N LEU A 50 8259 8430 9212 307 -2001 1049 N ATOM 392 CA LEU A 50 20.183 32.727 49.414 1.00 70.26 C ANISOU 392 CA LEU A 50 8641 8778 9276 307 -1938 1042 C ATOM 393 C LEU A 50 19.899 32.336 47.968 1.00 78.55 C ANISOU 393 C LEU A 50 9658 9800 10389 410 -1710 989 C ATOM 394 O LEU A 50 19.450 31.216 47.710 1.00112.02 O ANISOU 394 O LEU A 50 13928 14029 14606 422 -1686 1013 O ATOM 395 CB LEU A 50 18.959 33.432 50.008 1.00 70.13 C ANISOU 395 CB LEU A 50 8784 8921 8939 241 -1915 975 C ATOM 396 CG LEU A 50 19.025 33.862 51.477 1.00 79.96 C ANISOU 396 CG LEU A 50 10120 10217 10045 110 -2107 999 C ATOM 397 CD1 LEU A 50 17.629 34.197 51.997 1.00 57.20 C ANISOU 397 CD1 LEU A 50 7396 7488 6849 46 -2034 920 C ATOM 398 CD2 LEU A 50 19.709 32.811 52.355 1.00 58.40 C ANISOU 398 CD2 LEU A 50 7382 7413 7394 30 -2350 1136 C ATOM 399 N GLY A 51 20.167 33.228 47.014 1.00 77.37 N ANISOU 399 N GLY A 51 9459 9631 10307 469 -1545 919 N ATOM 400 CA GLY A 51 19.772 32.971 45.641 1.00 70.79 C ANISOU 400 CA GLY A 51 8642 8789 9467 537 -1329 864 C ATOM 401 C GLY A 51 20.705 32.069 44.862 1.00 80.59 C ANISOU 401 C GLY A 51 9768 9883 10971 591 -1243 876 C ATOM 402 O GLY A 51 20.264 31.376 43.941 1.00 82.90 O ANISOU 402 O GLY A 51 10107 10164 11226 621 -1100 840 O ATOM 403 N PHE A 52 21.993 32.064 45.194 1.00 79.59 N ANISOU 403 N PHE A 52 9485 9635 11122 599 -1322 919 N ATOM 404 CA PHE A 52 22.907 31.247 44.403 1.00 82.85 C ANISOU 404 CA PHE A 52 9762 9890 11828 659 -1204 911 C ATOM 405 C PHE A 52 22.817 29.772 44.789 1.00101.18 C ANISOU 405 C PHE A 52 12074 12143 14227 666 -1310 971 C ATOM 406 O PHE A 52 22.717 28.921 43.896 1.00111.04 O ANISOU 406 O PHE A 52 13330 13324 15537 710 -1149 924 O ATOM 407 CB PHE A 52 24.352 31.742 44.522 1.00 82.16 C ANISOU 407 CB PHE A 52 9472 9678 12068 672 -1233 932 C ATOM 408 CG PHE A 52 25.365 30.762 44.001 1.00 83.27 C ANISOU 408 CG PHE A 52 9432 9634 12572 735 -1148 933 C ATOM 409 CD1 PHE A 52 25.612 30.661 42.643 1.00 89.16 C ANISOU 409 CD1 PHE A 52 10153 10316 13409 780 -846 832 C ATOM 410 CD2 PHE A 52 26.058 29.931 44.867 1.00 84.54 C ANISOU 410 CD2 PHE A 52 9456 9677 12988 741 -1370 1032 C ATOM 411 CE1 PHE A 52 26.537 29.758 42.156 1.00 86.42 C ANISOU 411 CE1 PHE A 52 9635 9787 13415 838 -732 809 C ATOM 412 CE2 PHE A 52 26.982 29.023 44.386 1.00 90.93 C ANISOU 412 CE2 PHE A 52 10076 10294 14177 811 -1286 1026 C ATOM 413 CZ PHE A 52 27.222 28.937 43.028 1.00 91.94 C ANISOU 413 CZ PHE A 52 10169 10357 14407 864 -950 902 C ATOM 414 N PRO A 53 22.873 29.413 46.080 1.00 96.58 N ANISOU 414 N PRO A 53 11490 11562 13643 614 -1578 1076 N ATOM 415 CA PRO A 53 22.716 27.988 46.423 1.00 85.72 C ANISOU 415 CA PRO A 53 10125 10112 12331 612 -1686 1147 C ATOM 416 C PRO A 53 21.414 27.381 45.927 1.00 83.84 C ANISOU 416 C PRO A 53 10057 9966 11830 604 -1568 1098 C ATOM 417 O PRO A 53 21.435 26.327 45.281 1.00101.02 O ANISOU 417 O PRO A 53 12218 12040 14124 647 -1473 1078 O ATOM 418 CB PRO A 53 22.805 27.998 47.954 1.00 83.03 C ANISOU 418 CB PRO A 53 9814 9802 11933 520 -2004 1274 C ATOM 419 CG PRO A 53 23.684 29.138 48.251 1.00 85.50 C ANISOU 419 CG PRO A 53 10021 10103 12363 507 -2066 1274 C ATOM 420 CD PRO A 53 23.284 30.195 47.261 1.00 93.65 C ANISOU 420 CD PRO A 53 11096 11226 13261 544 -1806 1143 C ATOM 421 N ILE A 54 20.278 28.025 46.200 1.00 83.00 N ANISOU 421 N ILE A 54 10107 10043 11387 546 -1568 1072 N ATOM 422 CA ILE A 54 18.986 27.431 45.865 1.00 93.68 C ANISOU 422 CA ILE A 54 11605 11488 12501 524 -1493 1040 C ATOM 423 C ILE A 54 18.850 27.200 44.365 1.00 84.76 C ANISOU 423 C ILE A 54 10486 10317 11404 586 -1246 941 C ATOM 424 O ILE A 54 18.250 26.208 43.934 1.00 95.41 O ANISOU 424 O ILE A 54 11906 11648 12698 581 -1193 926 O ATOM 425 CB ILE A 54 17.848 28.314 46.414 1.00100.22 C ANISOU 425 CB ILE A 54 12561 12510 13009 458 -1520 1017 C ATOM 426 CG1 ILE A 54 17.986 28.468 47.930 1.00111.07 C ANISOU 426 CG1 ILE A 54 13959 13922 14319 369 -1750 1103 C ATOM 427 CG2 ILE A 54 16.492 27.721 46.074 1.00104.52 C ANISOU 427 CG2 ILE A 54 13228 13150 13333 430 -1449 988 C ATOM 428 CD1 ILE A 54 16.925 29.348 48.559 1.00117.89 C ANISOU 428 CD1 ILE A 54 14941 14962 14888 299 -1752 1059 C ATOM 429 N ASN A 55 19.415 28.086 43.547 1.00 86.49 N ANISOU 429 N ASN A 55 10648 10512 11702 631 -1093 874 N ATOM 430 CA ASN A 55 19.256 27.983 42.101 1.00 88.74 C ANISOU 430 CA ASN A 55 10980 10770 11967 661 -852 778 C ATOM 431 C ASN A 55 20.299 27.083 41.454 1.00 94.04 C ANISOU 431 C ASN A 55 11543 11248 12938 713 -730 745 C ATOM 432 O ASN A 55 19.981 26.342 40.519 1.00106.50 O ANISOU 432 O ASN A 55 13197 12783 14485 716 -575 676 O ATOM 433 CB ASN A 55 19.308 29.374 41.469 1.00 94.12 C ANISOU 433 CB ASN A 55 11679 11515 12568 666 -732 726 C ATOM 434 CG ASN A 55 18.010 30.122 41.622 1.00 94.00 C ANISOU 434 CG ASN A 55 11794 11671 12250 630 -776 723 C ATOM 435 OD1 ASN A 55 17.088 29.939 40.830 1.00103.63 O ANISOU 435 OD1 ASN A 55 13130 12950 13295 615 -689 684 O ATOM 436 ND2 ASN A 55 17.922 30.962 42.648 1.00 79.67 N ANISOU 436 ND2 ASN A 55 9960 9931 10382 610 -915 758 N ATOM 437 N PHE A 56 21.547 27.148 41.920 1.00 84.89 N ANISOU 437 N PHE A 56 10203 9966 12084 749 -793 785 N ATOM 438 CA PHE A 56 22.569 26.241 41.413 1.00 91.42 C ANISOU 438 CA PHE A 56 10890 10588 13256 808 -680 751 C ATOM 439 C PHE A 56 22.252 24.798 41.789 1.00102.64 C ANISOU 439 C PHE A 56 12337 11927 14736 812 -786 796 C ATOM 440 O PHE A 56 22.375 23.889 40.959 1.00105.33 O ANISOU 440 O PHE A 56 12682 12145 15195 844 -615 718 O ATOM 441 CB PHE A 56 23.938 26.657 41.951 1.00 91.36 C ANISOU 441 CB PHE A 56 10655 10466 13592 843 -765 802 C ATOM 442 CG PHE A 56 25.059 25.767 41.511 1.00 91.57 C ANISOU 442 CG PHE A 56 10490 10263 14039 914 -652 768 C ATOM 443 CD1 PHE A 56 25.662 25.953 40.278 1.00 88.97 C ANISOU 443 CD1 PHE A 56 10103 9850 13850 944 -334 638 C ATOM 444 CD2 PHE A 56 25.516 24.749 42.332 1.00 83.44 C ANISOU 444 CD2 PHE A 56 9339 9091 13274 946 -861 866 C ATOM 445 CE1 PHE A 56 26.694 25.138 39.868 1.00 82.01 C ANISOU 445 CE1 PHE A 56 9030 8746 13383 1013 -197 585 C ATOM 446 CE2 PHE A 56 26.549 23.926 41.927 1.00 79.58 C ANISOU 446 CE2 PHE A 56 8649 8368 13219 1025 -755 830 C ATOM 447 CZ PHE A 56 27.138 24.121 40.694 1.00 85.98 C ANISOU 447 CZ PHE A 56 9387 9096 14184 1063 -408 679 C ATOM 448 N LEU A 57 21.830 24.578 43.038 1.00 95.25 N ANISOU 448 N LEU A 57 11432 11051 13706 768 -1059 918 N ATOM 449 CA LEU A 57 21.470 23.240 43.497 1.00 83.59 C ANISOU 449 CA LEU A 57 9998 9499 12263 754 -1187 984 C ATOM 450 C LEU A 57 20.389 22.612 42.628 1.00 87.57 C ANISOU 450 C LEU A 57 10673 10052 12546 731 -1025 897 C ATOM 451 O LEU A 57 20.363 21.388 42.460 1.00102.52 O ANISOU 451 O LEU A 57 12577 11815 14562 744 -1016 896 O ATOM 452 CB LEU A 57 21.007 23.303 44.953 1.00 82.41 C ANISOU 452 CB LEU A 57 9909 9451 11952 674 -1486 1126 C ATOM 453 CG LEU A 57 20.437 22.036 45.588 1.00 83.33 C ANISOU 453 CG LEU A 57 10111 9526 12024 624 -1647 1219 C ATOM 454 CD1 LEU A 57 21.521 20.985 45.763 1.00 77.90 C ANISOU 454 CD1 LEU A 57 9265 8584 11750 685 -1746 1291 C ATOM 455 CD2 LEU A 57 19.769 22.355 46.916 1.00 84.69 C ANISOU 455 CD2 LEU A 57 10396 9853 11929 511 -1883 1331 C ATOM 456 N THR A 58 19.491 23.425 42.072 1.00 87.76 N ANISOU 456 N THR A 58 10831 10252 12260 693 -912 829 N ATOM 457 CA THR A 58 18.463 22.893 41.185 1.00 86.48 C ANISOU 457 CA THR A 58 10831 10140 11888 658 -777 750 C ATOM 458 C THR A 58 19.086 22.229 39.963 1.00 88.96 C ANISOU 458 C THR A 58 11125 10283 12393 702 -538 633 C ATOM 459 O THR A 58 18.760 21.084 39.628 1.00103.71 O ANISOU 459 O THR A 58 13060 12062 14281 689 -497 600 O ATOM 460 CB THR A 58 17.513 24.009 40.763 1.00 77.99 C ANISOU 460 CB THR A 58 9875 9265 10494 616 -716 709 C ATOM 461 OG1 THR A 58 16.799 24.497 41.909 1.00 67.44 O ANISOU 461 OG1 THR A 58 8567 8078 8978 570 -911 795 O ATOM 462 CG2 THR A 58 16.558 23.482 39.726 1.00 78.43 C ANISOU 462 CG2 THR A 58 10087 9355 10359 573 -587 630 C ATOM 463 N LEU A 59 19.992 22.938 39.288 1.00 86.07 N ANISOU 463 N LEU A 59 10672 9862 12168 745 -363 561 N ATOM 464 CA LEU A 59 20.711 22.352 38.164 1.00 89.21 C ANISOU 464 CA LEU A 59 11040 10087 12770 778 -100 433 C ATOM 465 C LEU A 59 21.522 21.140 38.604 1.00 87.96 C ANISOU 465 C LEU A 59 10729 9702 12990 844 -153 458 C ATOM 466 O LEU A 59 21.623 20.149 37.870 1.00 82.05 O ANISOU 466 O LEU A 59 10014 8807 12354 856 14 357 O ATOM 467 CB LEU A 59 21.616 23.406 37.527 1.00 90.17 C ANISOU 467 CB LEU A 59 11074 10192 12994 800 89 368 C ATOM 468 CG LEU A 59 20.929 24.730 37.180 1.00101.20 C ANISOU 468 CG LEU A 59 12603 11791 14058 743 110 368 C ATOM 469 CD1 LEU A 59 21.944 25.854 37.061 1.00 97.45 C ANISOU 469 CD1 LEU A 59 11996 11295 13736 766 198 361 C ATOM 470 CD2 LEU A 59 20.122 24.605 35.897 1.00 99.06 C ANISOU 470 CD2 LEU A 59 12554 11572 13510 672 301 265 C ATOM 471 N TYR A 60 22.091 21.194 39.809 1.00 83.21 N ANISOU 471 N TYR A 60 9966 9060 12589 879 -397 593 N ATOM 472 CA TYR A 60 22.906 20.089 40.301 1.00 98.17 C ANISOU 472 CA TYR A 60 11697 10723 14880 945 -494 645 C ATOM 473 C TYR A 60 22.078 18.816 40.455 1.00100.91 C ANISOU 473 C TYR A 60 12177 11023 15142 913 -576 670 C ATOM 474 O TYR A 60 22.382 17.786 39.842 1.00103.36 O ANISOU 474 O TYR A 60 12465 11137 15670 954 -431 584 O ATOM 475 CB TYR A 60 23.567 20.477 41.625 1.00 92.13 C ANISOU 475 CB TYR A 60 10767 9947 14293 961 -793 812 C ATOM 476 CG TYR A 60 24.546 19.444 42.127 1.00104.44 C ANISOU 476 CG TYR A 60 12124 11246 16314 1034 -923 888 C ATOM 477 CD1 TYR A 60 25.858 19.421 41.669 1.00104.38 C ANISOU 477 CD1 TYR A 60 11870 11035 16754 1128 -777 824 C ATOM 478 CD2 TYR A 60 24.157 18.485 43.051 1.00109.83 C ANISOU 478 CD2 TYR A 60 12854 11873 17004 1006 -1192 1028 C ATOM 479 CE1 TYR A 60 26.755 18.472 42.124 1.00104.70 C ANISOU 479 CE1 TYR A 60 11699 10816 17266 1206 -910 898 C ATOM 480 CE2 TYR A 60 25.044 17.537 43.510 1.00118.41 C ANISOU 480 CE2 TYR A 60 13756 12703 18532 1074 -1339 1115 C ATOM 481 CZ TYR A 60 26.341 17.531 43.046 1.00116.86 C ANISOU 481 CZ TYR A 60 13297 12298 18806 1181 -1205 1051 C ATOM 482 OH TYR A 60 27.221 16.577 43.508 1.00119.51 O ANISOU 482 OH TYR A 60 13423 12357 19627 1260 -1367 1144 O ATOM 483 N VAL A 61 21.020 18.867 41.272 1.00 93.75 N ANISOU 483 N VAL A 61 11410 10287 13924 832 -796 780 N ATOM 484 CA VAL A 61 20.189 17.680 41.470 1.00 81.33 C ANISOU 484 CA VAL A 61 9966 8677 12260 784 -882 816 C ATOM 485 C VAL A 61 19.571 17.229 40.155 1.00 89.95 C ANISOU 485 C VAL A 61 11209 9760 13207 759 -619 650 C ATOM 486 O VAL A 61 19.338 16.032 39.953 1.00 98.03 O ANISOU 486 O VAL A 61 12290 10646 14312 750 -602 624 O ATOM 487 CB VAL A 61 19.110 17.930 42.545 1.00 83.62 C ANISOU 487 CB VAL A 61 10381 9174 12216 683 -1126 949 C ATOM 488 CG1 VAL A 61 19.740 18.478 43.814 1.00 73.53 C ANISOU 488 CG1 VAL A 61 8987 7915 11038 683 -1378 1100 C ATOM 489 CG2 VAL A 61 18.015 18.860 42.027 1.00 78.23 C ANISOU 489 CG2 VAL A 61 9851 8738 11135 620 -1015 874 C ATOM 490 N THR A 62 19.305 18.161 39.237 1.00 95.32 N ANISOU 490 N THR A 62 11969 10577 13672 737 -422 538 N ATOM 491 CA THR A 62 18.879 17.753 37.904 1.00 94.77 C ANISOU 491 CA THR A 62 12052 10478 13477 700 -169 376 C ATOM 492 C THR A 62 19.956 16.918 37.222 1.00103.10 C ANISOU 492 C THR A 62 13007 11262 14904 772 44 255 C ATOM 493 O THR A 62 19.640 15.968 36.496 1.00109.47 O ANISOU 493 O THR A 62 13933 11962 15698 742 182 146 O ATOM 494 CB THR A 62 18.520 18.978 37.061 1.00 95.44 C ANISOU 494 CB THR A 62 12239 10743 13281 656 -19 301 C ATOM 495 OG1 THR A 62 17.374 19.628 37.626 1.00117.19 O ANISOU 495 OG1 THR A 62 15088 13730 15708 592 -203 395 O ATOM 496 CG2 THR A 62 18.204 18.574 35.629 1.00 81.18 C ANISOU 496 CG2 THR A 62 10608 8895 11342 598 241 134 C ATOM 497 N VAL A 63 21.230 17.228 37.474 1.00101.62 N ANISOU 497 N VAL A 63 12594 10947 15069 866 73 268 N ATOM 498 CA VAL A 63 22.309 16.425 36.907 1.00103.28 C ANISOU 498 CA VAL A 63 12665 10878 15697 947 283 151 C ATOM 499 C VAL A 63 22.422 15.079 37.623 1.00110.61 C ANISOU 499 C VAL A 63 13521 11601 16905 993 103 232 C ATOM 500 O VAL A 63 22.849 14.085 37.023 1.00116.36 O ANISOU 500 O VAL A 63 14219 12093 17899 1037 284 110 O ATOM 501 CB VAL A 63 23.632 17.221 36.942 1.00 90.95 C ANISOU 501 CB VAL A 63 10857 9245 14455 1029 370 142 C ATOM 502 CG1 VAL A 63 24.815 16.352 36.555 1.00 74.16 C ANISOU 502 CG1 VAL A 63 8527 6807 12844 1129 561 37 C ATOM 503 CG2 VAL A 63 23.553 18.413 36.006 1.00 70.49 C ANISOU 503 CG2 VAL A 63 8365 6816 11602 972 604 37 C ATOM 504 N GLN A 64 22.017 15.003 38.895 1.00113.62 N ANISOU 504 N GLN A 64 13890 12059 17223 972 -246 434 N ATOM 505 CA GLN A 64 22.157 13.750 39.635 1.00 94.27 C ANISOU 505 CA GLN A 64 11377 9403 15039 1004 -447 541 C ATOM 506 C GLN A 64 21.009 12.783 39.362 1.00100.04 C ANISOU 506 C GLN A 64 12338 10142 15532 919 -442 507 C ATOM 507 O GLN A 64 21.232 11.573 39.250 1.00114.95 O ANISOU 507 O GLN A 64 14204 11785 17684 954 -423 478 O ATOM 508 CB GLN A 64 22.241 14.019 41.138 1.00 78.30 C ANISOU 508 CB GLN A 64 9269 7445 13036 991 -830 781 C ATOM 509 CG GLN A 64 23.297 15.015 41.547 1.00 91.28 C ANISOU 509 CG GLN A 64 10697 9098 14886 1053 -891 837 C ATOM 510 CD GLN A 64 24.503 14.353 42.167 1.00105.64 C ANISOU 510 CD GLN A 64 12259 10636 17243 1151 -1056 941 C ATOM 511 OE1 GLN A 64 25.393 13.878 41.463 1.00114.87 O ANISOU 511 OE1 GLN A 64 13260 11567 18817 1253 -848 821 O ATOM 512 NE2 GLN A 64 24.542 14.318 43.495 1.00107.23 N ANISOU 512 NE2 GLN A 64 12427 10855 17460 1114 -1434 1165 N ATOM 513 N HIS A 65 19.781 13.287 39.269 1.00 87.60 N ANISOU 513 N HIS A 65 10970 8831 13484 807 -468 512 N ATOM 514 CA HIS A 65 18.583 12.454 39.271 1.00 90.85 C ANISOU 514 CA HIS A 65 11584 9285 13651 706 -537 525 C ATOM 515 C HIS A 65 17.973 12.420 37.877 1.00100.43 C ANISOU 515 C HIS A 65 12982 10548 14630 645 -257 323 C ATOM 516 O HIS A 65 17.538 13.455 37.362 1.00 97.90 O ANISOU 516 O HIS A 65 12744 10439 14016 599 -165 271 O ATOM 517 CB HIS A 65 17.574 12.975 40.294 1.00 77.64 C ANISOU 517 CB HIS A 65 9995 7867 11637 610 -794 691 C ATOM 518 CG HIS A 65 18.109 13.020 41.691 1.00 93.57 C ANISOU 518 CG HIS A 65 11878 9850 13823 634 -1081 893 C ATOM 519 ND1 HIS A 65 19.063 13.928 42.095 1.00105.41 N ANISOU 519 ND1 HIS A 65 13208 11362 15481 705 -1131 940 N ATOM 520 CD2 HIS A 65 17.835 12.257 42.775 1.00 95.16 C ANISOU 520 CD2 HIS A 65 12104 9999 14052 580 -1345 1065 C ATOM 521 CE1 HIS A 65 19.348 13.728 43.369 1.00112.23 C ANISOU 521 CE1 HIS A 65 14003 12186 16453 691 -1425 1132 C ATOM 522 NE2 HIS A 65 18.616 12.719 43.806 1.00104.26 N ANISOU 522 NE2 HIS A 65 13116 11138 15360 613 -1558 1215 N ATOM 523 N LYS A 66 17.931 11.228 37.274 1.00106.74 N ANISOU 523 N LYS A 66 13856 11142 15557 635 -136 214 N ATOM 524 CA LYS A 66 17.387 11.115 35.925 1.00109.56 C ANISOU 524 CA LYS A 66 14415 11528 15684 555 123 14 C ATOM 525 C LYS A 66 15.889 11.364 35.896 1.00104.61 C ANISOU 525 C LYS A 66 13993 11157 14595 414 6 60 C ATOM 526 O LYS A 66 15.365 11.892 34.908 1.00100.60 O ANISOU 526 O LYS A 66 13638 10783 13802 337 156 -54 O ATOM 527 CB LYS A 66 17.683 9.739 35.336 1.00121.56 C ANISOU 527 CB LYS A 66 15978 12754 17455 568 278 -124 C ATOM 528 CG LYS A 66 16.962 9.487 34.019 1.00137.26 C ANISOU 528 CG LYS A 66 18223 14774 19153 448 506 -323 C ATOM 529 CD LYS A 66 17.814 8.666 33.076 1.00150.05 C ANISOU 529 CD LYS A 66 19846 16098 21070 492 819 -547 C ATOM 530 CE LYS A 66 18.161 9.445 31.813 1.00155.71 C ANISOU 530 CE LYS A 66 20655 16875 21631 454 1150 -744 C ATOM 531 NZ LYS A 66 19.466 9.012 31.235 1.00146.68 N ANISOU 531 NZ LYS A 66 19382 15442 20906 553 1468 -930 N ATOM 532 N LYS A 67 15.185 10.999 36.960 1.00103.21 N ANISOU 532 N LYS A 67 13822 11049 14346 369 -263 229 N ATOM 533 CA LYS A 67 13.742 11.179 36.997 1.00 96.20 C ANISOU 533 CA LYS A 67 13096 10393 13064 235 -371 273 C ATOM 534 C LYS A 67 13.346 12.652 36.963 1.00 97.24 C ANISOU 534 C LYS A 67 13225 10800 12922 219 -384 301 C ATOM 535 O LYS A 67 12.153 12.968 36.930 1.00116.80 O ANISOU 535 O LYS A 67 15810 13478 15091 119 -462 331 O ATOM 536 CB LYS A 67 13.165 10.498 38.237 1.00101.65 C ANISOU 536 CB LYS A 67 13775 11089 13757 185 -637 453 C ATOM 537 CG LYS A 67 13.237 8.976 38.193 1.00111.52 C ANISOU 537 CG LYS A 67 15074 12078 15219 167 -645 432 C ATOM 538 CD LYS A 67 12.202 8.399 37.235 1.00117.62 C ANISOU 538 CD LYS A 67 16055 12877 15760 39 -546 306 C ATOM 539 CE LYS A 67 12.839 7.521 36.165 1.00121.42 C ANISOU 539 CE LYS A 67 16595 13084 16455 71 -313 110 C ATOM 540 NZ LYS A 67 13.438 6.278 36.721 1.00115.05 N ANISOU 540 NZ LYS A 67 15716 11977 16021 129 -385 160 N ATOM 541 N LEU A 68 14.327 13.560 36.971 1.00 84.54 N ANISOU 541 N LEU A 68 11484 9192 11445 317 -311 293 N ATOM 542 CA LEU A 68 14.078 14.993 36.865 1.00 83.57 C ANISOU 542 CA LEU A 68 11357 9296 11099 312 -305 309 C ATOM 543 C LEU A 68 14.304 15.543 35.463 1.00 82.88 C ANISOU 543 C LEU A 68 11361 9216 10912 298 -52 148 C ATOM 544 O LEU A 68 13.921 16.688 35.196 1.00 70.19 O ANISOU 544 O LEU A 68 9790 7794 9085 273 -48 158 O ATOM 545 CB LEU A 68 14.969 15.763 37.848 1.00 83.27 C ANISOU 545 CB LEU A 68 11125 9271 11241 407 -409 417 C ATOM 546 CG LEU A 68 14.677 15.620 39.341 1.00 81.53 C ANISOU 546 CG LEU A 68 10840 9110 11028 391 -684 598 C ATOM 547 CD1 LEU A 68 15.780 16.267 40.157 1.00 85.39 C ANISOU 547 CD1 LEU A 68 11147 9561 11734 479 -773 683 C ATOM 548 CD2 LEU A 68 13.334 16.243 39.678 1.00 77.32 C ANISOU 548 CD2 LEU A 68 10404 8836 10138 297 -789 652 C ATOM 549 N ARG A 69 14.906 14.765 34.567 1.00 77.81 N ANISOU 549 N ARG A 69 10768 8371 10425 306 162 0 N ATOM 550 CA ARG A 69 15.276 15.251 33.237 1.00 85.05 C ANISOU 550 CA ARG A 69 11785 9274 11254 278 433 -161 C ATOM 551 C ARG A 69 14.200 14.956 32.196 1.00 98.39 C ANISOU 551 C ARG A 69 13737 11036 12611 131 493 -255 C ATOM 552 O ARG A 69 14.478 14.464 31.102 1.00 87.58 O ANISOU 552 O ARG A 69 12505 9539 11233 77 725 -425 O ATOM 553 CB ARG A 69 16.616 14.656 32.828 1.00 79.98 C ANISOU 553 CB ARG A 69 11044 8365 10979 362 671 -291 C ATOM 554 CG ARG A 69 17.769 15.119 33.702 1.00 76.73 C ANISOU 554 CG ARG A 69 10361 7887 10908 499 617 -201 C ATOM 555 CD ARG A 69 19.109 14.819 33.062 1.00 73.82 C ANISOU 555 CD ARG A 69 9877 7277 10893 576 906 -353 C ATOM 556 NE ARG A 69 19.323 13.389 32.872 1.00102.17 N ANISOU 556 NE ARG A 69 13478 10615 14728 596 992 -449 N ATOM 557 CZ ARG A 69 19.816 12.579 33.803 1.00107.17 C ANISOU 557 CZ ARG A 69 13929 11066 15726 694 836 -356 C ATOM 558 NH1 ARG A 69 20.142 13.056 34.996 1.00 72.34 N ANISOU 558 NH1 ARG A 69 9326 6710 11451 766 578 -164 N ATOM 559 NH2 ARG A 69 19.985 11.293 33.544 1.00118.64 N ANISOU 559 NH2 ARG A 69 15401 12270 17407 711 927 -454 N ATOM 560 N THR A 70 12.944 15.280 32.539 1.00105.72 N ANISOU 560 N THR A 70 14735 12171 13264 55 279 -148 N ATOM 561 CA THR A 70 11.735 15.191 31.740 1.00101.09 C ANISOU 561 CA THR A 70 14366 11698 12346 -92 249 -187 C ATOM 562 C THR A 70 11.423 16.543 31.102 1.00110.67 C ANISOU 562 C THR A 70 15650 13094 13305 -133 267 -175 C ATOM 563 O THR A 70 11.819 17.586 31.631 1.00126.09 O ANISOU 563 O THR A 70 17463 15134 15312 -48 225 -93 O ATOM 564 CB THR A 70 10.556 14.741 32.608 1.00102.74 C ANISOU 564 CB THR A 70 14563 12014 12461 -143 -6 -61 C ATOM 565 OG1 THR A 70 10.247 15.764 33.562 1.00103.73 O ANISOU 565 OG1 THR A 70 14549 12323 12539 -92 -175 86 O ATOM 566 CG2 THR A 70 10.912 13.461 33.352 1.00109.51 C ANISOU 566 CG2 THR A 70 15348 12682 13580 -103 -49 -42 C ATOM 567 N PRO A 71 10.724 16.569 29.959 1.00 96.95 N ANISOU 567 N PRO A 71 14137 11409 11289 -272 314 -250 N ATOM 568 CA PRO A 71 10.537 17.852 29.256 1.00102.56 C ANISOU 568 CA PRO A 71 14930 12263 11775 -317 331 -231 C ATOM 569 C PRO A 71 9.739 18.873 30.045 1.00 97.23 C ANISOU 569 C PRO A 71 14136 11794 11013 -280 92 -66 C ATOM 570 O PRO A 71 10.075 20.064 30.020 1.00111.95 O ANISOU 570 O PRO A 71 15946 13734 12856 -232 107 -20 O ATOM 571 CB PRO A 71 9.811 17.442 27.966 1.00105.31 C ANISOU 571 CB PRO A 71 15562 12614 11838 -497 374 -327 C ATOM 572 CG PRO A 71 10.096 15.990 27.807 1.00 95.67 C ANISOU 572 CG PRO A 71 14406 11198 10745 -526 495 -455 C ATOM 573 CD PRO A 71 10.156 15.445 29.198 1.00 94.58 C ANISOU 573 CD PRO A 71 14042 11024 10871 -404 355 -357 C ATOM 574 N LEU A 72 8.696 18.444 30.758 1.00 91.22 N ANISOU 574 N LEU A 72 13330 11117 10213 -306 -115 19 N ATOM 575 CA LEU A 72 7.889 19.348 31.580 1.00 92.92 C ANISOU 575 CA LEU A 72 13418 11518 10369 -272 -318 157 C ATOM 576 C LEU A 72 8.668 19.954 32.739 1.00 95.15 C ANISOU 576 C LEU A 72 13490 11809 10854 -130 -333 228 C ATOM 577 O LEU A 72 8.074 20.641 33.580 1.00105.66 O ANISOU 577 O LEU A 72 14708 13278 12159 -98 -482 328 O ATOM 578 CB LEU A 72 6.654 18.621 32.113 1.00100.87 C ANISOU 578 CB LEU A 72 14415 12597 11315 -343 -499 216 C ATOM 579 CG LEU A 72 5.490 18.422 31.141 1.00 94.62 C ANISOU 579 CG LEU A 72 13792 11872 10288 -495 -582 197 C ATOM 580 CD1 LEU A 72 4.364 17.667 31.824 1.00 94.02 C ANISOU 580 CD1 LEU A 72 13663 11858 10204 -559 -749 258 C ATOM 581 CD2 LEU A 72 4.996 19.759 30.613 1.00 96.88 C ANISOU 581 CD2 LEU A 72 14097 12298 10416 -510 -657 253 C ATOM 582 N ASN A 73 9.976 19.700 32.801 1.00 87.12 N ANISOU 582 N ASN A 73 12416 10639 10046 -52 -181 171 N ATOM 583 CA ASN A 73 10.860 20.326 33.771 1.00 87.04 C ANISOU 583 CA ASN A 73 12216 10620 10234 70 -197 233 C ATOM 584 C ASN A 73 11.824 21.331 33.161 1.00 89.45 C ANISOU 584 C ASN A 73 12507 10899 10579 116 -40 189 C ATOM 585 O ASN A 73 12.402 22.128 33.906 1.00 89.79 O ANISOU 585 O ASN A 73 12402 10970 10745 201 -79 250 O ATOM 586 CB ASN A 73 11.676 19.260 34.514 1.00 84.32 C ANISOU 586 CB ASN A 73 11767 10108 10161 133 -186 232 C ATOM 587 CG ASN A 73 10.915 18.644 35.658 1.00 76.79 C ANISOU 587 CG ASN A 73 10762 9208 9206 113 -388 336 C ATOM 588 OD1 ASN A 73 9.716 18.869 35.810 1.00 94.07 O ANISOU 588 OD1 ASN A 73 12995 11552 11194 44 -507 385 O ATOM 589 ND2 ASN A 73 11.608 17.860 36.476 1.00 82.36 N ANISOU 589 ND2 ASN A 73 11369 9777 10148 166 -429 375 N ATOM 590 N TYR A 74 12.013 21.310 31.836 1.00 85.97 N ANISOU 590 N TYR A 74 12231 10404 10030 45 137 84 N ATOM 591 CA TYR A 74 12.992 22.184 31.194 1.00 79.00 C ANISOU 591 CA TYR A 74 11349 9480 9186 67 319 35 C ATOM 592 C TYR A 74 12.793 23.639 31.600 1.00 83.78 C ANISOU 592 C TYR A 74 11878 10231 9724 107 203 141 C ATOM 593 O TYR A 74 13.743 24.320 32.006 1.00 84.16 O ANISOU 593 O TYR A 74 11788 10247 9943 188 257 159 O ATOM 594 CB TYR A 74 12.906 22.053 29.671 1.00 72.03 C ANISOU 594 CB TYR A 74 10711 8559 8099 -60 501 -79 C ATOM 595 CG TYR A 74 13.389 20.738 29.095 1.00 75.53 C ANISOU 595 CG TYR A 74 11242 8821 8635 -100 696 -227 C ATOM 596 CD1 TYR A 74 13.833 19.708 29.915 1.00 82.71 C ANISOU 596 CD1 TYR A 74 12003 9601 9824 -13 684 -240 C ATOM 597 CD2 TYR A 74 13.410 20.535 27.719 1.00 79.70 C ANISOU 597 CD2 TYR A 74 12014 9296 8971 -233 894 -357 C ATOM 598 CE1 TYR A 74 14.275 18.507 29.379 1.00 86.36 C ANISOU 598 CE1 TYR A 74 12539 9873 10402 -40 869 -384 C ATOM 599 CE2 TYR A 74 13.850 19.343 27.175 1.00 78.13 C ANISOU 599 CE2 TYR A 74 11906 8920 8861 -274 1099 -517 C ATOM 600 CZ TYR A 74 14.281 18.333 28.009 1.00 81.58 C ANISOU 600 CZ TYR A 74 12173 9217 9608 -168 1089 -533 C ATOM 601 OH TYR A 74 14.717 17.147 27.465 1.00 85.49 O ANISOU 601 OH TYR A 74 12750 9512 10221 -200 1297 -700 O ATOM 602 N ILE A 75 11.554 24.129 31.506 1.00 89.18 N ANISOU 602 N ILE A 75 12639 11065 10181 50 38 210 N ATOM 603 CA ILE A 75 11.278 25.530 31.817 1.00 78.34 C ANISOU 603 CA ILE A 75 11202 9813 8751 88 -68 301 C ATOM 604 C ILE A 75 11.708 25.855 33.244 1.00 73.30 C ANISOU 604 C ILE A 75 10346 9192 8313 202 -158 364 C ATOM 605 O ILE A 75 12.250 26.933 33.511 1.00 86.81 O ANISOU 605 O ILE A 75 11973 10921 10089 257 -149 396 O ATOM 606 CB ILE A 75 9.788 25.850 31.564 1.00 75.03 C ANISOU 606 CB ILE A 75 10869 9532 8106 17 -248 365 C ATOM 607 CG1 ILE A 75 9.594 27.337 31.275 1.00 67.82 C ANISOU 607 CG1 ILE A 75 9963 8698 7110 27 -300 432 C ATOM 608 CG2 ILE A 75 8.897 25.406 32.721 1.00 77.76 C ANISOU 608 CG2 ILE A 75 11094 9961 8489 45 -427 425 C ATOM 609 CD1 ILE A 75 10.136 27.760 29.930 1.00 82.37 C ANISOU 609 CD1 ILE A 75 11984 10480 8832 -53 -149 392 C ATOM 610 N LEU A 76 11.511 24.916 34.174 1.00 67.99 N ANISOU 610 N LEU A 76 9594 8506 7734 224 -249 383 N ATOM 611 CA LEU A 76 11.982 25.116 35.541 1.00 80.59 C ANISOU 611 CA LEU A 76 11013 10106 9500 307 -342 446 C ATOM 612 C LEU A 76 13.490 25.320 35.569 1.00 85.42 C ANISOU 612 C LEU A 76 11526 10590 10341 375 -218 415 C ATOM 613 O LEU A 76 13.989 26.275 36.176 1.00 82.57 O ANISOU 613 O LEU A 76 11056 10258 10060 428 -259 458 O ATOM 614 CB LEU A 76 11.591 23.925 36.412 1.00 83.72 C ANISOU 614 CB LEU A 76 11377 10486 9948 293 -451 477 C ATOM 615 CG LEU A 76 10.104 23.633 36.564 1.00 80.50 C ANISOU 615 CG LEU A 76 11033 10204 9350 220 -576 512 C ATOM 616 CD1 LEU A 76 9.925 22.441 37.477 1.00102.91 C ANISOU 616 CD1 LEU A 76 13836 13002 12262 199 -665 549 C ATOM 617 CD2 LEU A 76 9.380 24.847 37.113 1.00 83.17 C ANISOU 617 CD2 LEU A 76 11311 10699 9590 235 -680 569 C ATOM 618 N LEU A 77 14.235 24.419 34.923 1.00 78.26 N ANISOU 618 N LEU A 77 10647 9530 9559 371 -59 334 N ATOM 619 CA LEU A 77 15.667 24.629 34.751 1.00 82.94 C ANISOU 619 CA LEU A 77 11132 9988 10391 429 96 288 C ATOM 620 C LEU A 77 15.935 26.012 34.182 1.00 76.21 C ANISOU 620 C LEU A 77 10302 9196 9457 421 179 286 C ATOM 621 O LEU A 77 16.774 26.758 34.697 1.00 82.65 O ANISOU 621 O LEU A 77 10977 9991 10436 479 174 318 O ATOM 622 CB LEU A 77 16.255 23.551 33.839 1.00 94.26 C ANISOU 622 CB LEU A 77 12625 11252 11937 409 309 168 C ATOM 623 CG LEU A 77 16.445 22.162 34.446 1.00 90.32 C ANISOU 623 CG LEU A 77 12055 10622 11640 444 255 166 C ATOM 624 CD1 LEU A 77 17.003 21.209 33.405 1.00 89.95 C ANISOU 624 CD1 LEU A 77 12079 10394 11703 423 503 19 C ATOM 625 CD2 LEU A 77 17.363 22.237 35.657 1.00 83.68 C ANISOU 625 CD2 LEU A 77 10986 9713 11095 542 136 251 C ATOM 626 N ASN A 78 15.198 26.378 33.131 1.00 73.96 N ANISOU 626 N ASN A 78 10203 8982 8917 338 234 259 N ATOM 627 CA ASN A 78 15.323 27.708 32.548 1.00 81.30 C ANISOU 627 CA ASN A 78 11181 9965 9742 315 289 276 C ATOM 628 C ASN A 78 15.204 28.785 33.618 1.00 83.77 C ANISOU 628 C ASN A 78 11359 10372 10099 382 115 373 C ATOM 629 O ASN A 78 16.068 29.661 33.731 1.00 89.69 O ANISOU 629 O ASN A 78 12021 11088 10969 416 172 383 O ATOM 630 CB ASN A 78 14.264 27.894 31.461 1.00 78.22 C ANISOU 630 CB ASN A 78 11017 9656 9047 207 281 273 C ATOM 631 CG ASN A 78 14.498 29.123 30.626 1.00 79.41 C ANISOU 631 CG ASN A 78 11260 9826 9086 160 363 290 C ATOM 632 OD1 ASN A 78 15.492 29.215 29.908 1.00 88.77 O ANISOU 632 OD1 ASN A 78 12482 10915 10331 127 586 221 O ATOM 633 ND2 ASN A 78 13.573 30.071 30.695 1.00 82.89 N ANISOU 633 ND2 ASN A 78 11737 10383 9376 150 191 382 N ATOM 634 N LEU A 79 14.151 28.706 34.438 1.00 78.51 N ANISOU 634 N LEU A 79 10674 9814 9342 393 -85 435 N ATOM 635 CA LEU A 79 13.964 29.656 35.530 1.00 73.39 C ANISOU 635 CA LEU A 79 9910 9251 8725 446 -236 506 C ATOM 636 C LEU A 79 15.223 29.777 36.378 1.00 86.57 C ANISOU 636 C LEU A 79 11414 10837 10641 510 -228 513 C ATOM 637 O LEU A 79 15.702 30.884 36.646 1.00 97.13 O ANISOU 637 O LEU A 79 12685 12184 12036 537 -237 536 O ATOM 638 CB LEU A 79 12.776 29.229 36.394 1.00 68.20 C ANISOU 638 CB LEU A 79 9242 8700 7972 439 -412 549 C ATOM 639 CG LEU A 79 12.444 30.111 37.598 1.00 69.20 C ANISOU 639 CG LEU A 79 9268 8918 8107 478 -551 601 C ATOM 640 CD1 LEU A 79 12.005 31.490 37.130 1.00 80.80 C ANISOU 640 CD1 LEU A 79 10770 10446 9483 484 -557 615 C ATOM 641 CD2 LEU A 79 11.374 29.463 38.467 1.00 50.92 C ANISOU 641 CD2 LEU A 79 6943 6693 5712 453 -680 628 C ATOM 642 N ALA A 80 15.783 28.638 36.792 1.00 77.90 N ANISOU 642 N ALA A 80 10247 9646 9707 530 -222 500 N ATOM 643 CA ALA A 80 17.000 28.659 37.597 1.00 81.41 C ANISOU 643 CA ALA A 80 10521 9997 10416 585 -247 521 C ATOM 644 C ALA A 80 18.106 29.435 36.893 1.00 91.02 C ANISOU 644 C ALA A 80 11684 11132 11766 599 -76 480 C ATOM 645 O ALA A 80 18.718 30.335 37.479 1.00 92.51 O ANISOU 645 O ALA A 80 11765 11322 12063 626 -132 516 O ATOM 646 CB ALA A 80 17.448 27.231 37.909 1.00 73.01 C ANISOU 646 CB ALA A 80 9396 8810 9533 604 -256 515 C ATOM 647 N VAL A 81 18.360 29.112 35.622 1.00 83.11 N ANISOU 647 N VAL A 81 10772 10059 10747 566 140 399 N ATOM 648 CA VAL A 81 19.359 29.845 34.850 1.00 86.50 C ANISOU 648 CA VAL A 81 11172 10414 11279 556 338 353 C ATOM 649 C VAL A 81 19.039 31.334 34.843 1.00 83.14 C ANISOU 649 C VAL A 81 10788 10091 10709 537 277 406 C ATOM 650 O VAL A 81 19.923 32.175 35.053 1.00 72.71 O ANISOU 650 O VAL A 81 9354 8730 9541 555 309 420 O ATOM 651 CB VAL A 81 19.453 29.278 33.422 1.00 80.17 C ANISOU 651 CB VAL A 81 10519 9542 10401 490 592 249 C ATOM 652 CG1 VAL A 81 20.306 30.182 32.543 1.00 75.40 C ANISOU 652 CG1 VAL A 81 9927 8887 9833 448 811 207 C ATOM 653 CG2 VAL A 81 20.022 27.869 33.456 1.00 77.76 C ANISOU 653 CG2 VAL A 81 10137 9091 10318 523 684 178 C ATOM 654 N ALA A 82 17.769 31.680 34.617 1.00 69.76 N ANISOU 654 N ALA A 82 9244 8520 8743 501 181 439 N ATOM 655 CA ALA A 82 17.357 33.077 34.671 1.00 71.54 C ANISOU 655 CA ALA A 82 9501 8826 8854 495 101 494 C ATOM 656 C ALA A 82 17.798 33.718 35.976 1.00 74.80 C ANISOU 656 C ALA A 82 9747 9251 9424 555 -38 538 C ATOM 657 O ALA A 82 18.441 34.773 35.977 1.00 83.14 O ANISOU 657 O ALA A 82 10752 10278 10560 557 -6 551 O ATOM 658 CB ALA A 82 15.840 33.189 34.501 1.00 69.97 C ANISOU 658 CB ALA A 82 9437 8749 8401 467 -29 531 C ATOM 659 N ASP A 83 17.490 33.072 37.102 1.00 65.89 N ANISOU 659 N ASP A 83 8544 8157 8333 588 -193 561 N ATOM 660 CA ASP A 83 17.846 33.652 38.390 1.00 74.51 C ANISOU 660 CA ASP A 83 9511 9266 9533 620 -341 601 C ATOM 661 C ASP A 83 19.353 33.804 38.535 1.00 78.25 C ANISOU 661 C ASP A 83 9836 9618 10278 638 -280 595 C ATOM 662 O ASP A 83 19.819 34.767 39.154 1.00 79.50 O ANISOU 662 O ASP A 83 9917 9776 10513 643 -352 619 O ATOM 663 CB ASP A 83 17.271 32.804 39.522 1.00 87.74 C ANISOU 663 CB ASP A 83 11163 10995 11178 625 -508 631 C ATOM 664 CG ASP A 83 15.758 32.713 39.466 1.00 92.67 C ANISOU 664 CG ASP A 83 11904 11743 11562 603 -567 635 C ATOM 665 OD1 ASP A 83 15.133 33.614 38.868 1.00 94.44 O ANISOU 665 OD1 ASP A 83 12200 12022 11660 597 -539 630 O ATOM 666 OD2 ASP A 83 15.190 31.746 40.016 1.00 96.27 O ANISOU 666 OD2 ASP A 83 12373 12235 11970 588 -649 650 O ATOM 667 N LEU A 84 20.132 32.889 37.956 1.00 77.60 N ANISOU 667 N LEU A 84 9703 9422 10358 645 -140 557 N ATOM 668 CA LEU A 84 21.582 33.035 38.013 1.00 65.70 C ANISOU 668 CA LEU A 84 8025 7788 9152 664 -64 547 C ATOM 669 C LEU A 84 22.041 34.242 37.206 1.00 75.26 C ANISOU 669 C LEU A 84 9256 8983 10356 631 89 525 C ATOM 670 O LEU A 84 22.955 34.962 37.624 1.00 87.36 O ANISOU 670 O LEU A 84 10652 10464 12077 635 67 544 O ATOM 671 CB LEU A 84 22.264 31.758 37.527 1.00 87.77 C ANISOU 671 CB LEU A 84 10749 10448 12150 685 78 495 C ATOM 672 CG LEU A 84 22.071 30.523 38.412 1.00 84.86 C ANISOU 672 CG LEU A 84 10328 10052 11862 719 -88 533 C ATOM 673 CD1 LEU A 84 22.843 29.348 37.840 1.00 80.42 C ANISOU 673 CD1 LEU A 84 9681 9323 11551 750 75 471 C ATOM 674 CD2 LEU A 84 22.493 30.794 39.853 1.00 73.38 C ANISOU 674 CD2 LEU A 84 8735 8602 10543 736 -341 624 C ATOM 675 N PHE A 85 21.413 34.490 36.053 1.00 91.84 N ANISOU 675 N PHE A 85 11535 11123 12238 585 231 494 N ATOM 676 CA PHE A 85 21.666 35.739 35.341 1.00 81.08 C ANISOU 676 CA PHE A 85 10229 9756 10821 538 340 498 C ATOM 677 C PHE A 85 21.287 36.942 36.194 1.00 75.85 C ANISOU 677 C PHE A 85 9549 9166 10104 553 149 560 C ATOM 678 O PHE A 85 21.952 37.981 36.130 1.00 87.88 O ANISOU 678 O PHE A 85 11023 10647 11719 532 189 573 O ATOM 679 CB PHE A 85 20.903 35.764 34.015 1.00 87.24 C ANISOU 679 CB PHE A 85 11238 10574 11336 470 474 477 C ATOM 680 CG PHE A 85 21.561 34.976 32.913 1.00 93.44 C ANISOU 680 CG PHE A 85 12066 11263 12173 419 743 392 C ATOM 681 CD1 PHE A 85 22.063 33.708 33.148 1.00106.25 C ANISOU 681 CD1 PHE A 85 13578 12804 13987 461 802 333 C ATOM 682 CD2 PHE A 85 21.659 35.500 31.634 1.00 95.60 C ANISOU 682 CD2 PHE A 85 12505 11518 12301 321 943 370 C ATOM 683 CE1 PHE A 85 22.663 32.984 32.136 1.00110.70 C ANISOU 683 CE1 PHE A 85 14180 13265 14616 417 1077 232 C ATOM 684 CE2 PHE A 85 22.254 34.779 30.616 1.00 90.24 C ANISOU 684 CE2 PHE A 85 11887 10750 11651 257 1222 272 C ATOM 685 CZ PHE A 85 22.757 33.520 30.868 1.00100.04 C ANISOU 685 CZ PHE A 85 13003 11906 13102 310 1301 192 C ATOM 686 N MET A 86 20.231 36.822 37.002 1.00 73.92 N ANISOU 686 N MET A 86 9344 9022 9718 583 -46 589 N ATOM 687 CA MET A 86 19.891 37.886 37.938 1.00 66.12 C ANISOU 687 CA MET A 86 8333 8092 8699 598 -213 623 C ATOM 688 C MET A 86 20.917 38.023 39.054 1.00 79.25 C ANISOU 688 C MET A 86 9823 9701 10587 611 -312 634 C ATOM 689 O MET A 86 21.038 39.103 39.639 1.00 97.84 O ANISOU 689 O MET A 86 12151 12063 12960 604 -398 647 O ATOM 690 CB MET A 86 18.510 37.641 38.548 1.00 56.16 C ANISOU 690 CB MET A 86 7146 6948 7244 617 -365 635 C ATOM 691 CG MET A 86 17.352 37.907 37.606 1.00 89.30 C ANISOU 691 CG MET A 86 11500 11206 11225 602 -332 643 C ATOM 692 SD MET A 86 15.755 37.487 38.333 1.00102.89 S ANISOU 692 SD MET A 86 13265 13057 12771 623 -492 650 S ATOM 693 CE MET A 86 15.760 38.493 39.814 1.00 79.70 C ANISOU 693 CE MET A 86 10239 10151 9893 649 -630 643 C ATOM 694 N VAL A 87 21.656 36.963 39.358 1.00 73.37 N ANISOU 694 N VAL A 87 8962 8891 10022 626 -313 631 N ATOM 695 CA VAL A 87 22.573 36.976 40.490 1.00 89.25 C ANISOU 695 CA VAL A 87 10810 10851 12251 630 -459 661 C ATOM 696 C VAL A 87 23.937 37.521 40.094 1.00 93.48 C ANISOU 696 C VAL A 87 11202 11268 13048 616 -345 653 C ATOM 697 O VAL A 87 24.454 38.444 40.728 1.00 88.81 O ANISOU 697 O VAL A 87 10537 10659 12546 592 -445 674 O ATOM 698 CB VAL A 87 22.676 35.558 41.094 1.00 96.82 C ANISOU 698 CB VAL A 87 11702 11781 13302 653 -556 685 C ATOM 699 CG1 VAL A 87 23.930 35.423 41.946 1.00 99.07 C ANISOU 699 CG1 VAL A 87 11791 11965 13887 653 -682 728 C ATOM 700 CG2 VAL A 87 21.435 35.249 41.920 1.00 72.06 C ANISOU 700 CG2 VAL A 87 8684 8770 9926 644 -721 708 C ATOM 701 N PHE A 88 24.532 36.974 39.036 1.00 95.80 N ANISOU 701 N PHE A 88 11457 11474 13468 619 -124 614 N ATOM 702 CA PHE A 88 25.883 37.348 38.641 1.00 85.52 C ANISOU 702 CA PHE A 88 9991 10050 12452 600 17 597 C ATOM 703 C PHE A 88 25.924 38.503 37.654 1.00 92.28 C ANISOU 703 C PHE A 88 10944 10909 13210 544 198 577 C ATOM 704 O PHE A 88 26.956 39.176 37.553 1.00116.26 O ANISOU 704 O PHE A 88 13851 13864 16458 511 273 577 O ATOM 705 CB PHE A 88 26.605 36.138 38.049 1.00 61.23 C ANISOU 705 CB PHE A 88 6801 6858 9605 628 194 549 C ATOM 706 CG PHE A 88 26.815 35.035 39.034 1.00 85.88 C ANISOU 706 CG PHE A 88 9792 9935 12903 681 3 587 C ATOM 707 CD1 PHE A 88 27.902 35.058 39.890 1.00 77.06 C ANISOU 707 CD1 PHE A 88 8442 8725 12115 694 -142 636 C ATOM 708 CD2 PHE A 88 25.916 33.984 39.122 1.00 95.01 C ANISOU 708 CD2 PHE A 88 11062 11138 13899 709 -52 586 C ATOM 709 CE1 PHE A 88 28.099 34.049 40.809 1.00 74.16 C ANISOU 709 CE1 PHE A 88 7965 8305 11910 733 -349 693 C ATOM 710 CE2 PHE A 88 26.107 32.969 40.039 1.00 96.30 C ANISOU 710 CE2 PHE A 88 11118 11249 14221 748 -240 637 C ATOM 711 CZ PHE A 88 27.202 33.002 40.883 1.00 87.98 C ANISOU 711 CZ PHE A 88 9840 10096 13491 760 -395 696 C ATOM 712 N GLY A 89 24.838 38.749 36.930 1.00 85.46 N ANISOU 712 N GLY A 89 10301 10129 12042 525 257 570 N ATOM 713 CA GLY A 89 24.779 39.893 36.046 1.00 92.17 C ANISOU 713 CA GLY A 89 11269 10978 12775 462 385 577 C ATOM 714 C GLY A 89 24.283 41.137 36.750 1.00 94.55 C ANISOU 714 C GLY A 89 11611 11333 12981 462 197 625 C ATOM 715 O GLY A 89 24.534 42.257 36.296 1.00 99.70 O ANISOU 715 O GLY A 89 12305 11950 13628 412 263 644 O ATOM 716 N GLY A 90 23.584 40.955 37.869 1.00 92.51 N ANISOU 716 N GLY A 90 11348 11151 12652 511 -28 639 N ATOM 717 CA GLY A 90 22.983 42.074 38.566 1.00 80.94 C ANISOU 717 CA GLY A 90 9935 9735 11084 513 -188 660 C ATOM 718 C GLY A 90 23.381 42.222 40.021 1.00 85.82 C ANISOU 718 C GLY A 90 10430 10353 11824 521 -389 662 C ATOM 719 O GLY A 90 23.940 43.252 40.409 1.00104.78 O ANISOU 719 O GLY A 90 12780 12707 14326 488 -438 666 O ATOM 720 N PHE A 91 23.106 41.200 40.834 1.00 77.70 N ANISOU 720 N PHE A 91 9369 9374 10779 548 -514 664 N ATOM 721 CA PHE A 91 23.227 41.348 42.283 1.00 84.26 C ANISOU 721 CA PHE A 91 10143 10228 11645 533 -733 672 C ATOM 722 C PHE A 91 24.674 41.575 42.714 1.00 88.65 C ANISOU 722 C PHE A 91 10520 10678 12484 495 -786 693 C ATOM 723 O PHE A 91 24.942 42.425 43.573 1.00 88.56 O ANISOU 723 O PHE A 91 10489 10659 12501 452 -925 692 O ATOM 724 CB PHE A 91 22.646 40.120 42.989 1.00 95.36 C ANISOU 724 CB PHE A 91 11568 11701 12962 552 -850 685 C ATOM 725 CG PHE A 91 21.173 39.908 42.741 1.00 99.63 C ANISOU 725 CG PHE A 91 12265 12352 13239 578 -825 665 C ATOM 726 CD1 PHE A 91 20.359 40.953 42.331 1.00108.43 C ANISOU 726 CD1 PHE A 91 13484 13507 14207 586 -777 640 C ATOM 727 CD2 PHE A 91 20.603 38.660 42.927 1.00 96.18 C ANISOU 727 CD2 PHE A 91 11857 11966 12721 592 -861 677 C ATOM 728 CE1 PHE A 91 19.006 40.753 42.105 1.00 89.89 C ANISOU 728 CE1 PHE A 91 11250 11251 11654 611 -770 628 C ATOM 729 CE2 PHE A 91 19.253 38.457 42.703 1.00 99.67 C ANISOU 729 CE2 PHE A 91 12423 12507 12940 607 -843 660 C ATOM 730 CZ PHE A 91 18.455 39.505 42.291 1.00 74.37 C ANISOU 730 CZ PHE A 91 9305 9346 9609 619 -800 636 C ATOM 731 N THR A 92 25.618 40.822 42.142 1.00 83.05 N ANISOU 731 N THR A 92 9673 9880 12002 507 -676 705 N ATOM 732 CA THR A 92 27.017 40.955 42.545 1.00 81.80 C ANISOU 732 CA THR A 92 9306 9612 12163 476 -734 730 C ATOM 733 C THR A 92 27.593 42.286 42.085 1.00 86.69 C ANISOU 733 C THR A 92 9899 10174 12863 426 -636 716 C ATOM 734 O THR A 92 28.289 42.969 42.846 1.00 90.07 O ANISOU 734 O THR A 92 10231 10558 13433 375 -779 733 O ATOM 735 CB THR A 92 27.848 39.797 41.989 1.00 84.78 C ANISOU 735 CB THR A 92 9521 9892 12800 512 -612 734 C ATOM 736 OG1 THR A 92 27.928 39.901 40.561 1.00 84.45 O ANISOU 736 OG1 THR A 92 9519 9816 12753 515 -310 685 O ATOM 737 CG2 THR A 92 27.226 38.461 42.368 1.00 70.32 C ANISOU 737 CG2 THR A 92 7732 8101 10886 559 -704 752 C ATOM 738 N THR A 93 27.326 42.660 40.831 1.00 90.20 N ANISOU 738 N THR A 93 10441 10616 13217 426 -400 690 N ATOM 739 CA THR A 93 27.725 43.974 40.338 1.00 78.23 C ANISOU 739 CA THR A 93 8939 9047 11738 368 -304 688 C ATOM 740 C THR A 93 27.241 45.074 41.275 1.00 74.15 C ANISOU 740 C THR A 93 8505 8569 11102 344 -501 689 C ATOM 741 O THR A 93 28.031 45.902 41.742 1.00 85.93 O ANISOU 741 O THR A 93 9903 9993 12755 286 -575 695 O ATOM 742 CB THR A 93 27.177 44.192 38.925 1.00 74.85 C ANISOU 742 CB THR A 93 8675 8632 11134 360 -65 677 C ATOM 743 OG1 THR A 93 27.648 43.153 38.057 1.00 82.88 O ANISOU 743 OG1 THR A 93 9634 9608 12251 368 143 653 O ATOM 744 CG2 THR A 93 27.627 45.533 38.382 1.00 86.20 C ANISOU 744 CG2 THR A 93 10137 10001 12614 288 34 691 C ATOM 745 N THR A 94 25.941 45.073 41.588 1.00 66.39 N ANISOU 745 N THR A 94 7689 7688 9849 384 -585 675 N ATOM 746 CA THR A 94 25.379 46.099 42.460 1.00 76.43 C ANISOU 746 CA THR A 94 9048 8988 11003 365 -739 651 C ATOM 747 C THR A 94 25.981 46.049 43.859 1.00 88.62 C ANISOU 747 C THR A 94 10495 10523 12655 319 -960 647 C ATOM 748 O THR A 94 26.084 47.085 44.520 1.00108.81 O ANISOU 748 O THR A 94 13078 13053 15212 268 -1063 620 O ATOM 749 CB THR A 94 23.857 45.960 42.524 1.00 89.45 C ANISOU 749 CB THR A 94 10865 10745 12377 421 -765 628 C ATOM 750 OG1 THR A 94 23.304 46.215 41.226 1.00107.00 O ANISOU 750 OG1 THR A 94 13192 12965 14500 445 -599 645 O ATOM 751 CG2 THR A 94 23.259 46.945 43.523 1.00 66.60 C ANISOU 751 CG2 THR A 94 8049 7874 9383 406 -904 579 C ATOM 752 N LEU A 95 26.392 44.870 44.329 1.00 83.24 N ANISOU 752 N LEU A 95 9710 9852 12066 327 -1047 677 N ATOM 753 CA LEU A 95 27.123 44.806 45.592 1.00 82.84 C ANISOU 753 CA LEU A 95 9562 9774 12140 263 -1282 699 C ATOM 754 C LEU A 95 28.425 45.590 45.499 1.00 92.12 C ANISOU 754 C LEU A 95 10580 10831 13592 198 -1285 714 C ATOM 755 O LEU A 95 28.691 46.479 46.316 1.00105.53 O ANISOU 755 O LEU A 95 12293 12506 15299 122 -1437 697 O ATOM 756 CB LEU A 95 27.391 43.348 45.974 1.00 87.15 C ANISOU 756 CB LEU A 95 10014 10328 12773 286 -1379 752 C ATOM 757 CG LEU A 95 28.378 43.066 47.113 1.00 73.25 C ANISOU 757 CG LEU A 95 8115 8510 11208 215 -1639 809 C ATOM 758 CD1 LEU A 95 27.928 43.697 48.417 1.00 84.92 C ANISOU 758 CD1 LEU A 95 9736 10053 12479 127 -1862 787 C ATOM 759 CD2 LEU A 95 28.566 41.573 47.290 1.00 62.98 C ANISOU 759 CD2 LEU A 95 6724 7195 10011 255 -1715 875 C ATOM 760 N TYR A 96 29.239 45.285 44.488 1.00 91.45 N ANISOU 760 N TYR A 96 10347 10665 13735 219 -1102 737 N ATOM 761 CA TYR A 96 30.524 45.953 44.323 1.00 82.01 C ANISOU 761 CA TYR A 96 8971 9351 12838 152 -1077 753 C ATOM 762 C TYR A 96 30.348 47.460 44.162 1.00 93.48 C ANISOU 762 C TYR A 96 10534 10782 14201 96 -1036 720 C ATOM 763 O TYR A 96 30.931 48.249 44.918 1.00 97.41 O ANISOU 763 O TYR A 96 10979 11227 14803 14 -1194 719 O ATOM 764 CB TYR A 96 31.251 45.350 43.121 1.00 67.36 C ANISOU 764 CB TYR A 96 6963 7420 11210 185 -818 761 C ATOM 765 CG TYR A 96 32.680 45.798 42.979 1.00 79.22 C ANISOU 765 CG TYR A 96 8226 8794 13081 117 -779 780 C ATOM 766 CD1 TYR A 96 33.638 45.417 43.909 1.00 80.25 C ANISOU 766 CD1 TYR A 96 8134 8857 13499 86 -1005 825 C ATOM 767 CD2 TYR A 96 33.075 46.597 41.915 1.00 73.63 C ANISOU 767 CD2 TYR A 96 7510 8025 12441 73 -524 760 C ATOM 768 CE1 TYR A 96 34.949 45.825 43.789 1.00 79.45 C ANISOU 768 CE1 TYR A 96 7786 8634 13769 21 -978 845 C ATOM 769 CE2 TYR A 96 34.385 47.007 41.782 1.00 83.36 C ANISOU 769 CE2 TYR A 96 8508 9139 14027 1 -471 774 C ATOM 770 CZ TYR A 96 35.318 46.617 42.723 1.00 90.98 C ANISOU 770 CZ TYR A 96 9229 10040 15299 -20 -698 813 C ATOM 771 OH TYR A 96 36.626 47.025 42.599 1.00103.18 O ANISOU 771 OH TYR A 96 10514 11462 17228 -95 -654 829 O ATOM 772 N THR A 97 29.527 47.879 43.193 1.00 80.49 N ANISOU 772 N THR A 97 9052 9168 12363 134 -841 698 N ATOM 773 CA THR A 97 29.355 49.306 42.933 1.00 81.74 C ANISOU 773 CA THR A 97 9316 9282 12461 86 -797 679 C ATOM 774 C THR A 97 28.735 50.017 44.128 1.00 68.47 C ANISOU 774 C THR A 97 7752 7635 10628 64 -1014 634 C ATOM 775 O THR A 97 29.093 51.161 44.429 1.00 76.37 O ANISOU 775 O THR A 97 8762 8561 11694 -7 -1069 613 O ATOM 776 CB THR A 97 28.500 49.528 41.685 1.00 79.41 C ANISOU 776 CB THR A 97 9186 9011 11977 130 -584 684 C ATOM 777 OG1 THR A 97 27.158 49.104 41.942 1.00 64.92 O ANISOU 777 OG1 THR A 97 7506 7286 9875 207 -648 661 O ATOM 778 CG2 THR A 97 29.061 48.750 40.506 1.00 75.43 C ANISOU 778 CG2 THR A 97 8601 8478 11579 135 -348 710 C ATOM 779 N SER A 98 27.803 49.362 44.824 1.00 62.55 N ANISOU 779 N SER A 98 7098 6992 9675 113 -1125 608 N ATOM 780 CA SER A 98 27.244 49.978 46.022 1.00 78.11 C ANISOU 780 CA SER A 98 9185 8995 11498 76 -1306 546 C ATOM 781 C SER A 98 28.317 50.198 47.077 1.00 79.06 C ANISOU 781 C SER A 98 9197 9058 11784 -34 -1513 549 C ATOM 782 O SER A 98 28.245 51.167 47.839 1.00 87.28 O ANISOU 782 O SER A 98 10322 10070 12771 -105 -1624 489 O ATOM 783 CB SER A 98 26.099 49.137 46.593 1.00 73.02 C ANISOU 783 CB SER A 98 8653 8479 10611 130 -1368 518 C ATOM 784 OG SER A 98 26.574 47.952 47.207 1.00 82.55 O ANISOU 784 OG SER A 98 9765 9722 11877 112 -1498 564 O ATOM 785 N LEU A 99 29.328 49.328 47.125 1.00 81.46 N ANISOU 785 N LEU A 99 9312 9333 12306 -53 -1573 618 N ATOM 786 CA LEU A 99 30.422 49.518 48.069 1.00 93.26 C ANISOU 786 CA LEU A 99 10680 10761 13993 -165 -1799 642 C ATOM 787 C LEU A 99 31.334 50.678 47.696 1.00 91.91 C ANISOU 787 C LEU A 99 10416 10468 14039 -241 -1749 638 C ATOM 788 O LEU A 99 32.123 51.116 48.540 1.00 73.83 O ANISOU 788 O LEU A 99 8053 8118 11880 -354 -1954 643 O ATOM 789 CB LEU A 99 31.239 48.233 48.198 1.00100.18 C ANISOU 789 CB LEU A 99 11353 11621 15089 -153 -1890 728 C ATOM 790 CG LEU A 99 30.500 47.139 48.962 1.00 98.91 C ANISOU 790 CG LEU A 99 11291 11565 14727 -124 -2033 745 C ATOM 791 CD1 LEU A 99 31.369 45.910 49.108 1.00 95.55 C ANISOU 791 CD1 LEU A 99 10655 11093 14558 -112 -2147 842 C ATOM 792 CD2 LEU A 99 30.063 47.667 50.319 1.00 89.64 C ANISOU 792 CD2 LEU A 99 10291 10442 13325 -229 -2266 699 C ATOM 793 N HIS A 100 31.252 51.190 46.469 1.00101.10 N ANISOU 793 N HIS A 100 11588 11589 15236 -199 -1495 636 N ATOM 794 CA HIS A 100 31.967 52.409 46.118 1.00 83.90 C ANISOU 794 CA HIS A 100 9360 9293 13223 -282 -1437 631 C ATOM 795 C HIS A 100 31.114 53.664 46.233 1.00 90.16 C ANISOU 795 C HIS A 100 10372 10070 13813 -295 -1426 561 C ATOM 796 O HIS A 100 31.670 54.766 46.226 1.00104.59 O ANISOU 796 O HIS A 100 12184 11792 15764 -383 -1436 549 O ATOM 797 CB HIS A 100 32.520 52.325 44.695 1.00 69.39 C ANISOU 797 CB HIS A 100 7407 7395 11561 -260 -1159 679 C ATOM 798 CG HIS A 100 33.494 51.212 44.493 1.00 70.88 C ANISOU 798 CG HIS A 100 7348 7563 12021 -249 -1128 730 C ATOM 799 ND1 HIS A 100 34.856 51.377 44.628 1.00 91.89 N ANISOU 799 ND1 HIS A 100 9758 10117 15037 -337 -1174 764 N ATOM 800 CD2 HIS A 100 33.302 49.912 44.171 1.00 80.02 C ANISOU 800 CD2 HIS A 100 8455 8778 13172 -158 -1055 749 C ATOM 801 CE1 HIS A 100 35.461 50.227 44.392 1.00 98.32 C ANISOU 801 CE1 HIS A 100 10368 10920 16071 -291 -1125 800 C ATOM 802 NE2 HIS A 100 34.541 49.322 44.113 1.00110.09 N ANISOU 802 NE2 HIS A 100 11983 12505 17341 -183 -1051 789 N ATOM 803 N GLY A 101 29.792 53.532 46.329 1.00 98.07 N ANISOU 803 N GLY A 101 11564 11163 14534 -210 -1404 514 N ATOM 804 CA GLY A 101 28.909 54.677 46.361 1.00100.03 C ANISOU 804 CA GLY A 101 12001 11382 14626 -200 -1375 445 C ATOM 805 C GLY A 101 28.397 55.134 45.010 1.00 92.73 C ANISOU 805 C GLY A 101 11149 10419 13664 -133 -1154 482 C ATOM 806 O GLY A 101 27.553 56.039 44.962 1.00100.01 O ANISOU 806 O GLY A 101 12222 11304 14472 -104 -1135 437 O ATOM 807 N TYR A 102 28.869 54.538 43.917 1.00 93.13 N ANISOU 807 N TYR A 102 11105 10469 13810 -114 -990 562 N ATOM 808 CA TYR A 102 28.456 54.939 42.578 1.00 82.02 C ANISOU 808 CA TYR A 102 9791 9025 12347 -81 -787 612 C ATOM 809 C TYR A 102 28.818 53.826 41.603 1.00 85.74 C ANISOU 809 C TYR A 102 10177 9543 12858 -56 -616 673 C ATOM 810 O TYR A 102 29.515 52.870 41.951 1.00102.62 O ANISOU 810 O TYR A 102 12155 11713 15125 -61 -648 675 O ATOM 811 CB TYR A 102 29.103 56.267 42.170 1.00 95.57 C ANISOU 811 CB TYR A 102 11511 10592 14208 -176 -734 636 C ATOM 812 CG TYR A 102 30.597 56.187 41.938 1.00101.65 C ANISOU 812 CG TYR A 102 12079 11292 15253 -280 -672 677 C ATOM 813 CD1 TYR A 102 31.491 56.280 42.996 1.00 88.94 C ANISOU 813 CD1 TYR A 102 10321 9647 13825 -358 -847 645 C ATOM 814 CD2 TYR A 102 31.111 56.024 40.657 1.00101.25 C ANISOU 814 CD2 TYR A 102 11983 11204 15282 -312 -436 746 C ATOM 815 CE1 TYR A 102 32.853 56.209 42.784 1.00 83.09 C ANISOU 815 CE1 TYR A 102 9362 8832 13375 -451 -798 685 C ATOM 816 CE2 TYR A 102 32.469 55.950 40.438 1.00 71.16 C ANISOU 816 CE2 TYR A 102 7964 7323 11750 -408 -351 772 C ATOM 817 CZ TYR A 102 33.336 56.044 41.503 1.00 89.31 C ANISOU 817 CZ TYR A 102 10086 9583 14263 -470 -537 744 C ATOM 818 OH TYR A 102 34.692 55.971 41.284 1.00110.07 O ANISOU 818 OH TYR A 102 12476 12134 17210 -564 -459 773 O ATOM 819 N PHE A 103 28.346 53.972 40.366 1.00 78.43 N ANISOU 819 N PHE A 103 9367 8608 11826 -36 -437 721 N ATOM 820 CA PHE A 103 28.497 52.930 39.350 1.00 91.99 C ANISOU 820 CA PHE A 103 11057 10371 13525 -18 -248 759 C ATOM 821 C PHE A 103 29.864 53.065 38.684 1.00 87.58 C ANISOU 821 C PHE A 103 10352 9717 13207 -121 -74 791 C ATOM 822 O PHE A 103 30.039 53.839 37.740 1.00 96.98 O ANISOU 822 O PHE A 103 11625 10831 14392 -193 79 837 O ATOM 823 CB PHE A 103 27.369 53.013 38.329 1.00 80.25 C ANISOU 823 CB PHE A 103 9779 8919 11794 25 -150 799 C ATOM 824 CG PHE A 103 27.263 51.799 37.463 1.00 89.44 C ANISOU 824 CG PHE A 103 10955 10152 12874 49 8 814 C ATOM 825 CD1 PHE A 103 26.549 50.693 37.887 1.00 94.05 C ANISOU 825 CD1 PHE A 103 11544 10850 13342 139 -69 781 C ATOM 826 CD2 PHE A 103 27.899 51.751 36.236 1.00107.64 C ANISOU 826 CD2 PHE A 103 13276 12406 15218 -32 246 854 C ATOM 827 CE1 PHE A 103 26.463 49.565 37.097 1.00104.56 C ANISOU 827 CE1 PHE A 103 12892 12232 14603 156 77 785 C ATOM 828 CE2 PHE A 103 27.817 50.626 35.445 1.00101.68 C ANISOU 828 CE2 PHE A 103 12546 11705 14381 -21 408 847 C ATOM 829 CZ PHE A 103 27.097 49.533 35.873 1.00 93.34 C ANISOU 829 CZ PHE A 103 11493 10754 13218 77 317 811 C ATOM 830 N VAL A 104 30.831 52.270 39.150 1.00 74.71 N ANISOU 830 N VAL A 104 8500 8085 11801 -131 -91 771 N ATOM 831 CA VAL A 104 32.228 52.472 38.777 1.00 95.46 C ANISOU 831 CA VAL A 104 10932 10609 14729 -231 46 787 C ATOM 832 C VAL A 104 32.542 52.048 37.348 1.00101.80 C ANISOU 832 C VAL A 104 11748 11393 15539 -266 371 806 C ATOM 833 O VAL A 104 33.567 52.468 36.798 1.00104.98 O ANISOU 833 O VAL A 104 12036 11700 16151 -369 546 820 O ATOM 834 CB VAL A 104 33.153 51.716 39.749 1.00 82.25 C ANISOU 834 CB VAL A 104 8994 8928 13330 -224 -98 768 C ATOM 835 CG1 VAL A 104 33.035 52.286 41.147 1.00 82.83 C ANISOU 835 CG1 VAL A 104 9070 9004 13399 -239 -411 750 C ATOM 836 CG2 VAL A 104 32.813 50.237 39.746 1.00 90.61 C ANISOU 836 CG2 VAL A 104 10019 10071 14340 -123 -82 752 C ATOM 837 N PHE A 105 31.705 51.225 36.726 1.00104.41 N ANISOU 837 N PHE A 105 12219 11807 15645 -197 466 800 N ATOM 838 CA PHE A 105 32.048 50.619 35.446 1.00100.72 C ANISOU 838 CA PHE A 105 11768 11326 15176 -240 778 795 C ATOM 839 C PHE A 105 31.635 51.468 34.247 1.00 99.20 C ANISOU 839 C PHE A 105 11820 11105 14766 -330 951 849 C ATOM 840 O PHE A 105 31.762 51.011 33.106 1.00 87.44 O ANISOU 840 O PHE A 105 10409 9614 13200 -387 1216 844 O ATOM 841 CB PHE A 105 31.433 49.222 35.355 1.00 92.34 C ANISOU 841 CB PHE A 105 10738 10357 13990 -139 795 757 C ATOM 842 CG PHE A 105 31.843 48.314 36.483 1.00102.11 C ANISOU 842 CG PHE A 105 11748 11610 15440 -58 620 723 C ATOM 843 CD1 PHE A 105 33.169 47.923 36.627 1.00103.08 C ANISOU 843 CD1 PHE A 105 11586 11644 15934 -87 700 702 C ATOM 844 CD2 PHE A 105 30.909 47.857 37.401 1.00 86.82 C ANISOU 844 CD2 PHE A 105 9877 9768 13343 38 371 720 C ATOM 845 CE1 PHE A 105 33.557 47.092 37.665 1.00 70.51 C ANISOU 845 CE1 PHE A 105 7253 7518 12018 -19 503 694 C ATOM 846 CE2 PHE A 105 31.289 47.024 38.441 1.00 80.41 C ANISOU 846 CE2 PHE A 105 8881 8964 12708 93 194 708 C ATOM 847 CZ PHE A 105 32.616 46.643 38.573 1.00 78.64 C ANISOU 847 CZ PHE A 105 8381 8644 12855 65 244 702 C ATOM 848 N GLY A 106 31.154 52.687 34.474 1.00 95.80 N ANISOU 848 N GLY A 106 11520 10642 14237 -354 805 899 N ATOM 849 CA GLY A 106 30.897 53.616 33.400 1.00112.05 C ANISOU 849 CA GLY A 106 13796 12644 16135 -455 936 974 C ATOM 850 C GLY A 106 29.683 53.267 32.563 1.00116.37 C ANISOU 850 C GLY A 106 14608 13266 16343 -423 964 1013 C ATOM 851 O GLY A 106 28.956 52.309 32.843 1.00131.81 O ANISOU 851 O GLY A 106 16579 15323 18181 -314 881 974 O ATOM 852 N PRO A 107 29.439 54.062 31.516 1.00105.98 N ANISOU 852 N PRO A 107 13511 11893 14864 -529 1066 1101 N ATOM 853 CA PRO A 107 28.257 53.822 30.667 1.00100.13 C ANISOU 853 CA PRO A 107 13039 11213 13795 -518 1057 1159 C ATOM 854 C PRO A 107 28.195 52.433 30.049 1.00106.14 C ANISOU 854 C PRO A 107 13825 12063 14440 -514 1231 1101 C ATOM 855 O PRO A 107 27.114 51.832 30.018 1.00125.69 O ANISOU 855 O PRO A 107 16416 14629 16711 -430 1116 1103 O ATOM 856 CB PRO A 107 28.382 54.916 29.599 1.00106.16 C ANISOU 856 CB PRO A 107 14008 11873 14454 -679 1168 1274 C ATOM 857 CG PRO A 107 29.088 56.032 30.306 1.00 84.44 C ANISOU 857 CG PRO A 107 11120 9011 11951 -708 1090 1284 C ATOM 858 CD PRO A 107 30.073 55.362 31.231 1.00 86.67 C ANISOU 858 CD PRO A 107 11092 9318 12521 -660 1120 1168 C ATOM 859 N THR A 108 29.312 51.908 29.539 1.00110.56 N ANISOU 859 N THR A 108 14277 12591 15138 -605 1516 1044 N ATOM 860 CA THR A 108 29.291 50.571 28.949 1.00109.47 C ANISOU 860 CA THR A 108 14164 12518 14911 -601 1704 969 C ATOM 861 C THR A 108 28.925 49.519 29.990 1.00102.90 C ANISOU 861 C THR A 108 13167 11770 14162 -428 1527 893 C ATOM 862 O THR A 108 28.058 48.669 29.752 1.00105.39 O ANISOU 862 O THR A 108 13604 12168 14272 -374 1492 875 O ATOM 863 CB THR A 108 30.643 50.251 28.309 1.00100.17 C ANISOU 863 CB THR A 108 12861 11270 13929 -723 2063 902 C ATOM 864 OG1 THR A 108 31.695 50.572 29.227 1.00112.05 O ANISOU 864 OG1 THR A 108 14054 12707 15812 -696 2027 870 O ATOM 865 CG2 THR A 108 30.825 51.047 27.025 1.00102.03 C ANISOU 865 CG2 THR A 108 13342 11445 13981 -926 2288 976 C ATOM 866 N GLY A 109 29.578 49.563 31.155 1.00 89.79 N ANISOU 866 N GLY A 109 11237 10083 12796 -355 1403 855 N ATOM 867 CA GLY A 109 29.184 48.690 32.247 1.00 82.42 C ANISOU 867 CA GLY A 109 10170 9223 11921 -207 1195 805 C ATOM 868 C GLY A 109 27.724 48.843 32.620 1.00 97.18 C ANISOU 868 C GLY A 109 12215 11182 13527 -120 945 845 C ATOM 869 O GLY A 109 27.085 47.881 33.053 1.00111.32 O ANISOU 869 O GLY A 109 13997 13058 15244 -24 843 809 O ATOM 870 N CYS A 110 27.176 50.049 32.454 1.00 98.27 N ANISOU 870 N CYS A 110 12507 11293 13540 -153 848 921 N ATOM 871 CA CYS A 110 25.747 50.252 32.668 1.00101.79 C ANISOU 871 CA CYS A 110 13111 11805 13758 -73 636 959 C ATOM 872 C CYS A 110 24.929 49.463 31.656 1.00109.97 C ANISOU 872 C CYS A 110 14340 12910 14532 -87 716 978 C ATOM 873 O CYS A 110 23.924 48.834 32.010 1.00112.01 O ANISOU 873 O CYS A 110 14634 13259 14664 6 575 962 O ATOM 874 CB CYS A 110 25.420 51.741 32.582 1.00104.05 C ANISOU 874 CB CYS A 110 13511 12013 14010 -110 534 1040 C ATOM 875 SG CYS A 110 23.828 52.211 33.248 1.00121.72 S ANISOU 875 SG CYS A 110 15847 14299 16103 15 246 1063 S ATOM 876 N ASN A 111 25.350 49.479 30.390 1.00108.32 N ANISOU 876 N ASN A 111 14266 12659 14232 -218 948 1007 N ATOM 877 CA ASN A 111 24.644 48.722 29.364 1.00 96.92 C ANISOU 877 CA ASN A 111 13032 11274 12519 -262 1032 1019 C ATOM 878 C ASN A 111 24.734 47.225 29.618 1.00 99.93 C ANISOU 878 C ASN A 111 13305 11723 12940 -194 1101 912 C ATOM 879 O ASN A 111 23.773 46.493 29.365 1.00 93.40 O ANISOU 879 O ASN A 111 12601 10975 11913 -162 1034 909 O ATOM 880 CB ASN A 111 25.199 49.068 27.986 1.00 90.76 C ANISOU 880 CB ASN A 111 12435 10428 11623 -446 1290 1062 C ATOM 881 CG ASN A 111 24.714 50.407 27.492 1.00 93.24 C ANISOU 881 CG ASN A 111 12946 10682 11799 -523 1181 1202 C ATOM 882 OD1 ASN A 111 23.869 50.483 26.601 1.00100.19 O ANISOU 882 OD1 ASN A 111 14083 11582 12404 -591 1136 1287 O ATOM 883 ND2 ASN A 111 25.236 51.477 28.078 1.00113.98 N ANISOU 883 ND2 ASN A 111 15457 13226 14624 -517 1117 1233 N ATOM 884 N LEU A 112 25.878 46.749 30.117 1.00101.81 N ANISOU 884 N LEU A 112 13307 11922 13456 -175 1223 830 N ATOM 885 CA LEU A 112 26.028 45.324 30.400 1.00 86.71 C ANISOU 885 CA LEU A 112 11275 10047 11626 -104 1277 736 C ATOM 886 C LEU A 112 25.171 44.904 31.587 1.00 80.82 C ANISOU 886 C LEU A 112 10454 9385 10869 38 990 734 C ATOM 887 O LEU A 112 24.363 43.974 31.484 1.00 85.05 O ANISOU 887 O LEU A 112 11072 9993 11251 81 946 712 O ATOM 888 CB LEU A 112 27.494 44.988 30.663 1.00 86.89 C ANISOU 888 CB LEU A 112 11036 9982 11994 -114 1456 662 C ATOM 889 CG LEU A 112 28.428 44.917 29.459 1.00 92.32 C ANISOU 889 CG LEU A 112 11762 10590 12726 -253 1824 616 C ATOM 890 CD1 LEU A 112 29.800 44.446 29.903 1.00 72.37 C ANISOU 890 CD1 LEU A 112 8915 7975 10608 -229 1967 536 C ATOM 891 CD2 LEU A 112 27.858 43.996 28.394 1.00105.14 C ANISOU 891 CD2 LEU A 112 13610 12253 14087 -306 1995 568 C ATOM 892 N GLU A 113 25.343 45.576 32.728 1.00 83.46 N ANISOU 892 N GLU A 113 10641 9709 11361 98 799 753 N ATOM 893 CA GLU A 113 24.614 45.191 33.931 1.00 80.79 C ANISOU 893 CA GLU A 113 10235 9449 11012 212 548 741 C ATOM 894 C GLU A 113 23.111 45.333 33.734 1.00 89.55 C ANISOU 894 C GLU A 113 11541 10644 11841 245 413 783 C ATOM 895 O GLU A 113 22.333 44.496 34.205 1.00110.47 O ANISOU 895 O GLU A 113 14192 13376 14406 315 302 760 O ATOM 896 CB GLU A 113 25.092 46.027 35.117 1.00 71.02 C ANISOU 896 CB GLU A 113 8844 8178 9963 238 383 747 C ATOM 897 CG GLU A 113 24.488 45.633 36.449 1.00 77.09 C ANISOU 897 CG GLU A 113 9547 9023 10723 330 144 726 C ATOM 898 CD GLU A 113 23.380 46.565 36.876 1.00 96.42 C ANISOU 898 CD GLU A 113 12112 11513 13010 362 -24 749 C ATOM 899 OE1 GLU A 113 22.202 46.153 36.854 1.00 92.00 O ANISOU 899 OE1 GLU A 113 11656 11038 12261 412 -95 751 O ATOM 900 OE2 GLU A 113 23.692 47.721 37.226 1.00127.92 O ANISOU 900 OE2 GLU A 113 16081 15441 17082 336 -80 760 O ATOM 901 N GLY A 114 22.683 46.376 33.023 1.00 85.22 N ANISOU 901 N GLY A 114 11153 10067 11159 190 414 851 N ATOM 902 CA GLY A 114 21.267 46.520 32.729 1.00 95.06 C ANISOU 902 CA GLY A 114 12568 11377 12172 218 279 902 C ATOM 903 C GLY A 114 20.770 45.495 31.727 1.00 86.96 C ANISOU 903 C GLY A 114 11690 10402 10948 176 376 899 C ATOM 904 O GLY A 114 19.636 45.020 31.826 1.00 87.63 O ANISOU 904 O GLY A 114 11839 10568 10889 226 244 908 O ATOM 905 N PHE A 115 21.608 45.139 30.749 1.00 71.30 N ANISOU 905 N PHE A 115 9765 8370 8957 73 617 879 N ATOM 906 CA PHE A 115 21.189 44.159 29.751 1.00 79.54 C ANISOU 906 CA PHE A 115 10975 9452 9796 11 729 859 C ATOM 907 C PHE A 115 21.019 42.779 30.370 1.00 91.92 C ANISOU 907 C PHE A 115 12430 11079 11416 96 703 774 C ATOM 908 O PHE A 115 20.059 42.069 30.057 1.00103.33 O ANISOU 908 O PHE A 115 13995 12592 12675 99 639 774 O ATOM 909 CB PHE A 115 22.191 44.101 28.598 1.00 81.02 C ANISOU 909 CB PHE A 115 11254 9563 9966 -132 1031 832 C ATOM 910 CG PHE A 115 21.918 42.999 27.615 1.00103.28 C ANISOU 910 CG PHE A 115 14245 12410 12586 -210 1183 779 C ATOM 911 CD1 PHE A 115 20.933 43.140 26.653 1.00116.10 C ANISOU 911 CD1 PHE A 115 16147 14072 13895 -303 1120 852 C ATOM 912 CD2 PHE A 115 22.645 41.820 27.653 1.00100.92 C ANISOU 912 CD2 PHE A 115 13832 12088 12427 -194 1378 655 C ATOM 913 CE1 PHE A 115 20.676 42.126 25.749 1.00109.89 C ANISOU 913 CE1 PHE A 115 15540 13309 12905 -393 1252 795 C ATOM 914 CE2 PHE A 115 22.391 40.804 26.750 1.00 99.11 C ANISOU 914 CE2 PHE A 115 13772 11870 12014 -271 1530 588 C ATOM 915 CZ PHE A 115 21.406 40.958 25.797 1.00 94.38 C ANISOU 915 CZ PHE A 115 13469 11318 11071 -378 1469 654 C ATOM 916 N PHE A 116 21.939 42.379 31.247 1.00 91.68 N ANISOU 916 N PHE A 116 12172 11016 11648 159 737 710 N ATOM 917 CA PHE A 116 21.852 41.049 31.836 1.00 97.15 C ANISOU 917 CA PHE A 116 12760 11744 12409 232 706 644 C ATOM 918 C PHE A 116 20.847 40.992 32.979 1.00 91.88 C ANISOU 918 C PHE A 116 12044 11167 11701 331 434 671 C ATOM 919 O PHE A 116 20.219 39.948 33.188 1.00 93.50 O ANISOU 919 O PHE A 116 12263 11429 11834 368 376 644 O ATOM 920 CB PHE A 116 23.239 40.594 32.293 1.00 84.35 C ANISOU 920 CB PHE A 116 10910 10037 11103 255 830 580 C ATOM 921 CG PHE A 116 24.120 40.149 31.161 1.00 93.00 C ANISOU 921 CG PHE A 116 12037 11047 12250 167 1146 513 C ATOM 922 CD1 PHE A 116 23.634 39.280 30.196 1.00101.71 C ANISOU 922 CD1 PHE A 116 13323 12167 13155 113 1281 465 C ATOM 923 CD2 PHE A 116 25.417 40.617 31.040 1.00 97.84 C ANISOU 923 CD2 PHE A 116 12506 11561 13108 125 1320 490 C ATOM 924 CE1 PHE A 116 24.429 38.871 29.142 1.00 97.25 C ANISOU 924 CE1 PHE A 116 12809 11521 12622 18 1603 382 C ATOM 925 CE2 PHE A 116 26.218 40.212 29.985 1.00 96.12 C ANISOU 925 CE2 PHE A 116 12315 11262 12945 35 1649 412 C ATOM 926 CZ PHE A 116 25.722 39.338 29.036 1.00 88.14 C ANISOU 926 CZ PHE A 116 11500 10268 11720 -20 1800 352 C ATOM 927 N ALA A 117 20.667 42.090 33.716 1.00 74.86 N ANISOU 927 N ALA A 117 9838 9020 9586 366 280 715 N ATOM 928 CA ALA A 117 19.625 42.119 34.737 1.00 80.41 C ANISOU 928 CA ALA A 117 10516 9808 10227 445 55 726 C ATOM 929 C ALA A 117 18.243 42.064 34.099 1.00 85.29 C ANISOU 929 C ALA A 117 11305 10496 10604 438 -14 764 C ATOM 930 O ALA A 117 17.396 41.253 34.491 1.00 79.57 O ANISOU 930 O ALA A 117 10581 9851 9800 478 -107 748 O ATOM 931 CB ALA A 117 19.770 43.366 35.608 1.00 78.76 C ANISOU 931 CB ALA A 117 10231 9576 10119 472 -65 744 C ATOM 932 N THR A 118 18.002 42.922 33.105 1.00 87.52 N ANISOU 932 N THR A 118 11733 10746 10776 378 20 825 N ATOM 933 CA THR A 118 16.731 42.897 32.391 1.00 90.37 C ANISOU 933 CA THR A 118 12256 11158 10922 358 -68 880 C ATOM 934 C THR A 118 16.510 41.552 31.712 1.00 95.63 C ANISOU 934 C THR A 118 13014 11865 11457 311 16 844 C ATOM 935 O THR A 118 15.415 40.981 31.792 1.00 98.85 O ANISOU 935 O THR A 118 13459 12349 11750 334 -104 852 O ATOM 936 CB THR A 118 16.687 44.032 31.369 1.00 81.77 C ANISOU 936 CB THR A 118 11321 10003 9744 280 -51 970 C ATOM 937 OG1 THR A 118 16.865 45.285 32.043 1.00 80.66 O ANISOU 937 OG1 THR A 118 11094 9810 9744 329 -135 996 O ATOM 938 CG2 THR A 118 15.356 44.041 30.620 1.00 77.60 C ANISOU 938 CG2 THR A 118 10957 9519 9009 253 -185 1047 C ATOM 939 N LEU A 119 17.543 41.028 31.046 1.00 92.29 N ANISOU 939 N LEU A 119 12620 11383 11062 240 234 797 N ATOM 940 CA LEU A 119 17.446 39.721 30.405 1.00 87.61 C ANISOU 940 CA LEU A 119 12118 10807 10363 190 344 739 C ATOM 941 C LEU A 119 17.002 38.656 31.401 1.00 93.02 C ANISOU 941 C LEU A 119 12677 11552 11113 280 236 692 C ATOM 942 O LEU A 119 15.968 38.007 31.215 1.00 99.03 O ANISOU 942 O LEU A 119 13526 12380 11720 271 144 698 O ATOM 943 CB LEU A 119 18.789 39.344 29.775 1.00 85.50 C ANISOU 943 CB LEU A 119 11844 10446 10194 121 625 666 C ATOM 944 CG LEU A 119 18.844 38.078 28.918 1.00 67.23 C ANISOU 944 CG LEU A 119 9652 8117 7774 48 800 583 C ATOM 945 CD1 LEU A 119 18.067 38.262 27.624 1.00 76.88 C ANISOU 945 CD1 LEU A 119 11166 9366 8678 -86 810 629 C ATOM 946 CD2 LEU A 119 20.281 37.688 28.627 1.00 78.87 C ANISOU 946 CD2 LEU A 119 11037 9485 9446 17 1089 486 C ATOM 947 N GLY A 120 17.766 38.484 32.483 1.00 95.93 N ANISOU 947 N GLY A 120 12845 11897 11709 356 229 654 N ATOM 948 CA GLY A 120 17.434 37.459 33.461 1.00 87.76 C ANISOU 948 CA GLY A 120 11703 10908 10732 424 124 623 C ATOM 949 C GLY A 120 16.023 37.592 34.004 1.00 86.90 C ANISOU 949 C GLY A 120 11624 10907 10488 460 -84 665 C ATOM 950 O GLY A 120 15.281 36.610 34.085 1.00109.91 O ANISOU 950 O GLY A 120 14569 13875 13316 461 -138 650 O ATOM 951 N GLY A 121 15.631 38.812 34.376 1.00 81.74 N ANISOU 951 N GLY A 121 10952 10275 9829 488 -194 711 N ATOM 952 CA GLY A 121 14.294 39.014 34.911 1.00 81.86 C ANISOU 952 CA GLY A 121 10968 10381 9754 529 -368 738 C ATOM 953 C GLY A 121 13.201 38.670 33.915 1.00 82.80 C ANISOU 953 C GLY A 121 11234 10544 9682 480 -405 772 C ATOM 954 O GLY A 121 12.159 38.126 34.286 1.00 80.07 O ANISOU 954 O GLY A 121 10874 10277 9273 499 -513 772 O ATOM 955 N GLU A 122 13.426 38.978 32.636 1.00 92.98 N ANISOU 955 N GLU A 122 12674 11783 10872 402 -319 806 N ATOM 956 CA GLU A 122 12.415 38.690 31.622 1.00 91.11 C ANISOU 956 CA GLU A 122 12602 11582 10434 332 -379 851 C ATOM 957 C GLU A 122 12.356 37.207 31.295 1.00 87.23 C ANISOU 957 C GLU A 122 12170 11112 9862 283 -308 791 C ATOM 958 O GLU A 122 11.274 36.673 31.023 1.00 88.96 O ANISOU 958 O GLU A 122 12456 11391 9952 253 -417 811 O ATOM 959 CB GLU A 122 12.689 39.487 30.352 1.00 89.51 C ANISOU 959 CB GLU A 122 12577 11315 10119 236 -319 916 C ATOM 960 CG GLU A 122 12.386 40.941 30.468 1.00 79.41 C ANISOU 960 CG GLU A 122 11277 10007 8886 272 -438 1001 C ATOM 961 CD GLU A 122 10.934 41.207 30.731 1.00 97.44 C ANISOU 961 CD GLU A 122 13530 12350 11144 324 -663 1059 C ATOM 962 OE1 GLU A 122 10.050 40.610 30.073 1.00122.58 O ANISOU 962 OE1 GLU A 122 16818 15579 14178 266 -748 1093 O ATOM 963 OE2 GLU A 122 10.692 42.029 31.621 1.00 92.97 O ANISOU 963 OE2 GLU A 122 12825 11779 10720 420 -749 1062 O ATOM 964 N ILE A 123 13.510 36.531 31.283 1.00 94.32 N ANISOU 964 N ILE A 123 13039 11947 10851 272 -125 716 N ATOM 965 CA ILE A 123 13.512 35.079 31.124 1.00 80.23 C ANISOU 965 CA ILE A 123 11288 10160 9037 242 -53 645 C ATOM 966 C ILE A 123 12.721 34.428 32.248 1.00 72.68 C ANISOU 966 C ILE A 123 10210 9279 8125 312 -210 644 C ATOM 967 O ILE A 123 11.938 33.500 32.017 1.00 87.31 O ANISOU 967 O ILE A 123 12132 11172 9870 272 -258 631 O ATOM 968 CB ILE A 123 14.952 34.534 31.074 1.00 81.64 C ANISOU 968 CB ILE A 123 11405 10235 9379 243 168 562 C ATOM 969 CG1 ILE A 123 15.752 35.188 29.953 1.00 90.90 C ANISOU 969 CG1 ILE A 123 12698 11334 10504 156 359 553 C ATOM 970 CG2 ILE A 123 14.937 33.032 30.870 1.00 89.44 C ANISOU 970 CG2 ILE A 123 12431 11195 10356 217 246 483 C ATOM 971 CD1 ILE A 123 17.246 35.002 30.106 1.00 98.18 C ANISOU 971 CD1 ILE A 123 13491 12151 11664 178 570 480 C ATOM 972 N ALA A 124 12.911 34.903 33.481 1.00 72.31 N ANISOU 972 N ALA A 124 9994 9254 8228 400 -289 656 N ATOM 973 CA ALA A 124 12.148 34.366 34.603 1.00 72.68 C ANISOU 973 CA ALA A 124 9941 9377 8295 446 -426 657 C ATOM 974 C ALA A 124 10.650 34.574 34.398 1.00 76.76 C ANISOU 974 C ALA A 124 10511 9986 8669 428 -567 701 C ATOM 975 O ALA A 124 9.866 33.622 34.481 1.00 93.12 O ANISOU 975 O ALA A 124 12600 12109 10672 401 -623 692 O ATOM 976 CB ALA A 124 12.617 35.004 35.912 1.00 59.02 C ANISOU 976 CB ALA A 124 8055 7653 6717 519 -483 660 C ATOM 977 N LEU A 125 10.239 35.812 34.108 1.00 68.79 N ANISOU 977 N LEU A 125 9518 8986 7631 441 -631 752 N ATOM 978 CA LEU A 125 8.819 36.114 33.933 1.00 83.94 C ANISOU 978 CA LEU A 125 11453 10975 9466 436 -782 802 C ATOM 979 C LEU A 125 8.202 35.272 32.820 1.00 86.26 C ANISOU 979 C LEU A 125 11896 11283 9595 340 -803 819 C ATOM 980 O LEU A 125 7.149 34.650 33.006 1.00 82.88 O ANISOU 980 O LEU A 125 11444 10924 9123 324 -906 824 O ATOM 981 CB LEU A 125 8.635 37.607 33.647 1.00 95.78 C ANISOU 981 CB LEU A 125 12955 12445 10993 466 -844 863 C ATOM 982 CG LEU A 125 7.275 38.091 33.130 1.00101.54 C ANISOU 982 CG LEU A 125 13710 13208 11662 456 -1008 937 C ATOM 983 CD1 LEU A 125 6.869 39.383 33.818 1.00 89.84 C ANISOU 983 CD1 LEU A 125 12102 11714 10319 549 -1090 957 C ATOM 984 CD2 LEU A 125 7.304 38.292 31.619 1.00 99.62 C ANISOU 984 CD2 LEU A 125 13668 12914 11269 357 -1022 1012 C ATOM 985 N TRP A 126 8.841 35.246 31.650 1.00 82.53 N ANISOU 985 N TRP A 126 11588 10744 9024 260 -701 822 N ATOM 986 CA TRP A 126 8.285 34.494 30.534 1.00 86.91 C ANISOU 986 CA TRP A 126 12322 11305 9393 145 -721 831 C ATOM 987 C TRP A 126 8.368 32.990 30.750 1.00 96.69 C ANISOU 987 C TRP A 126 13564 12549 10623 117 -651 749 C ATOM 988 O TRP A 126 7.580 32.248 30.155 1.00103.52 O ANISOU 988 O TRP A 126 14538 13442 11352 32 -717 751 O ATOM 989 CB TRP A 126 8.979 34.898 29.234 1.00 96.05 C ANISOU 989 CB TRP A 126 13684 12389 10423 44 -606 847 C ATOM 990 CG TRP A 126 8.485 36.217 28.726 1.00101.92 C ANISOU 990 CG TRP A 126 14484 13128 11114 29 -741 961 C ATOM 991 CD1 TRP A 126 9.165 37.398 28.703 1.00 94.92 C ANISOU 991 CD1 TRP A 126 13584 12184 10299 60 -694 1001 C ATOM 992 CD2 TRP A 126 7.184 36.492 28.193 1.00106.10 C ANISOU 992 CD2 TRP A 126 15080 13698 11535 -18 -964 1059 C ATOM 993 NE1 TRP A 126 8.373 38.390 28.174 1.00 89.98 N ANISOU 993 NE1 TRP A 126 13024 11552 9612 36 -873 1121 N ATOM 994 CE2 TRP A 126 7.151 37.858 27.854 1.00 99.27 C ANISOU 994 CE2 TRP A 126 14243 12788 10687 -9 -1048 1162 C ATOM 995 CE3 TRP A 126 6.045 35.712 27.965 1.00107.63 C ANISOU 995 CE3 TRP A 126 15305 13955 11636 -73 -1113 1076 C ATOM 996 CZ2 TRP A 126 6.026 38.462 27.298 1.00107.51 C ANISOU 996 CZ2 TRP A 126 15339 13839 11672 -43 -1287 1288 C ATOM 997 CZ3 TRP A 126 4.930 36.313 27.414 1.00 99.95 C ANISOU 997 CZ3 TRP A 126 14374 12998 10603 -112 -1348 1197 C ATOM 998 CH2 TRP A 126 4.928 37.674 27.087 1.00106.06 C ANISOU 998 CH2 TRP A 126 15169 13719 11410 -93 -1439 1305 C ATOM 999 N SER A 127 9.294 32.525 31.591 1.00 98.03 N ANISOU 999 N SER A 127 13618 12682 10945 183 -537 685 N ATOM 1000 CA SER A 127 9.266 31.125 32.003 1.00 89.04 C ANISOU 1000 CA SER A 127 12455 11539 9837 174 -509 626 C ATOM 1001 C SER A 127 8.034 30.833 32.850 1.00 81.85 C ANISOU 1001 C SER A 127 11446 10730 8924 195 -682 660 C ATOM 1002 O SER A 127 7.424 29.766 32.718 1.00 82.02 O ANISOU 1002 O SER A 127 11515 10769 8879 136 -717 641 O ATOM 1003 CB SER A 127 10.539 30.767 32.767 1.00 79.60 C ANISOU 1003 CB SER A 127 11141 10268 8834 242 -385 573 C ATOM 1004 OG SER A 127 11.669 30.807 31.915 1.00 92.24 O ANISOU 1004 OG SER A 127 12822 11766 10460 211 -192 522 O ATOM 1005 N LEU A 128 7.653 31.765 33.727 1.00 65.51 N ANISOU 1005 N LEU A 128 9239 8720 6931 271 -776 702 N ATOM 1006 CA LEU A 128 6.416 31.592 34.481 1.00 84.46 C ANISOU 1006 CA LEU A 128 11541 11218 9331 282 -912 725 C ATOM 1007 C LEU A 128 5.210 31.522 33.550 1.00 93.19 C ANISOU 1007 C LEU A 128 12731 12368 10309 207 -1029 768 C ATOM 1008 O LEU A 128 4.318 30.686 33.738 1.00 87.53 O ANISOU 1008 O LEU A 128 11993 11706 9560 161 -1102 766 O ATOM 1009 CB LEU A 128 6.248 32.724 35.494 1.00 72.15 C ANISOU 1009 CB LEU A 128 9834 9702 7877 370 -962 741 C ATOM 1010 CG LEU A 128 7.232 32.772 36.662 1.00 64.62 C ANISOU 1010 CG LEU A 128 8785 8726 7042 428 -896 705 C ATOM 1011 CD1 LEU A 128 6.642 33.593 37.799 1.00 91.85 C ANISOU 1011 CD1 LEU A 128 12105 12243 10553 483 -960 703 C ATOM 1012 CD2 LEU A 128 7.591 31.377 37.136 1.00 59.16 C ANISOU 1012 CD2 LEU A 128 8096 8018 6364 396 -862 678 C ATOM 1013 N VAL A 129 5.171 32.386 32.535 1.00 92.88 N ANISOU 1013 N VAL A 129 12791 12301 10200 181 -1062 817 N ATOM 1014 CA VAL A 129 4.063 32.366 31.583 1.00 94.66 C ANISOU 1014 CA VAL A 129 13109 12557 10302 95 -1209 877 C ATOM 1015 C VAL A 129 4.038 31.046 30.825 1.00 93.69 C ANISOU 1015 C VAL A 129 13149 12415 10036 -26 -1173 836 C ATOM 1016 O VAL A 129 3.004 30.369 30.757 1.00 95.18 O ANISOU 1016 O VAL A 129 13331 12656 10177 -87 -1291 849 O ATOM 1017 CB VAL A 129 4.160 33.564 30.623 1.00 94.22 C ANISOU 1017 CB VAL A 129 13157 12456 10188 76 -1260 955 C ATOM 1018 CG1 VAL A 129 3.089 33.474 29.548 1.00 86.08 C ANISOU 1018 CG1 VAL A 129 12249 11444 9014 -35 -1441 1033 C ATOM 1019 CG2 VAL A 129 4.037 34.856 31.395 1.00 84.30 C ANISOU 1019 CG2 VAL A 129 11732 11205 9094 198 -1311 991 C ATOM 1020 N VAL A 130 5.179 30.659 30.247 1.00 91.55 N ANISOU 1020 N VAL A 130 13018 12060 9706 -67 -999 775 N ATOM 1021 CA VAL A 130 5.246 29.430 29.458 1.00 91.33 C ANISOU 1021 CA VAL A 130 13166 11991 9544 -186 -933 712 C ATOM 1022 C VAL A 130 4.865 28.225 30.307 1.00 86.90 C ANISOU 1022 C VAL A 130 12505 11455 9058 -174 -949 667 C ATOM 1023 O VAL A 130 4.157 27.320 29.845 1.00 83.74 O ANISOU 1023 O VAL A 130 12200 11066 8553 -277 -1013 652 O ATOM 1024 CB VAL A 130 6.647 29.271 28.838 1.00 87.97 C ANISOU 1024 CB VAL A 130 12871 11456 9096 -213 -697 633 C ATOM 1025 CG1 VAL A 130 6.851 27.853 28.331 1.00 84.93 C ANISOU 1025 CG1 VAL A 130 12624 11007 8636 -307 -584 531 C ATOM 1026 CG2 VAL A 130 6.835 30.266 27.708 1.00 91.24 C ANISOU 1026 CG2 VAL A 130 13457 11848 9364 -288 -687 683 C ATOM 1027 N LEU A 131 5.318 28.195 31.561 1.00 80.11 N ANISOU 1027 N LEU A 131 11466 10601 8372 -63 -902 651 N ATOM 1028 CA LEU A 131 4.934 27.110 32.458 1.00 70.30 C ANISOU 1028 CA LEU A 131 10134 9382 7195 -61 -931 628 C ATOM 1029 C LEU A 131 3.420 27.055 32.627 1.00 72.82 C ANISOU 1029 C LEU A 131 10394 9808 7468 -107 -1111 682 C ATOM 1030 O LEU A 131 2.816 25.979 32.545 1.00 84.60 O ANISOU 1030 O LEU A 131 11925 11307 8912 -190 -1155 666 O ATOM 1031 CB LEU A 131 5.629 27.275 33.810 1.00 68.53 C ANISOU 1031 CB LEU A 131 9742 9155 7143 50 -883 624 C ATOM 1032 CG LEU A 131 5.376 26.177 34.844 1.00 82.55 C ANISOU 1032 CG LEU A 131 11439 10943 8984 43 -911 617 C ATOM 1033 CD1 LEU A 131 5.729 24.812 34.279 1.00107.03 C ANISOU 1033 CD1 LEU A 131 14662 13942 12064 -27 -837 559 C ATOM 1034 CD2 LEU A 131 6.165 26.446 36.112 1.00 72.13 C ANISOU 1034 CD2 LEU A 131 9986 9613 7808 133 -882 625 C ATOM 1035 N ALA A 132 2.787 28.211 32.848 1.00 82.10 N ANISOU 1035 N ALA A 132 11463 11055 8678 -55 -1215 745 N ATOM 1036 CA ALA A 132 1.331 28.245 32.953 1.00 74.21 C ANISOU 1036 CA ALA A 132 10375 10147 7676 -92 -1382 795 C ATOM 1037 C ALA A 132 0.674 27.696 31.692 1.00 87.48 C ANISOU 1037 C ALA A 132 12218 11817 9203 -229 -1484 816 C ATOM 1038 O ALA A 132 -0.297 26.935 31.772 1.00 93.28 O ANISOU 1038 O ALA A 132 12919 12599 9925 -304 -1582 823 O ATOM 1039 CB ALA A 132 0.853 29.670 33.228 1.00 74.02 C ANISOU 1039 CB ALA A 132 10214 10168 7742 -6 -1465 852 C ATOM 1040 N ILE A 133 1.200 28.057 30.519 1.00 95.03 N ANISOU 1040 N ILE A 133 13364 12711 10033 -281 -1462 823 N ATOM 1041 CA ILE A 133 0.635 27.568 29.263 1.00 93.90 C ANISOU 1041 CA ILE A 133 13418 12554 9707 -437 -1565 841 C ATOM 1042 C ILE A 133 0.770 26.053 29.172 1.00106.14 C ANISOU 1042 C ILE A 133 15073 14064 11193 -529 -1484 752 C ATOM 1043 O ILE A 133 -0.183 25.347 28.819 1.00123.09 O ANISOU 1043 O ILE A 133 17263 16239 13266 -643 -1616 764 O ATOM 1044 CB ILE A 133 1.304 28.264 28.064 1.00 84.37 C ANISOU 1044 CB ILE A 133 12426 11282 8349 -493 -1525 860 C ATOM 1045 CG1 ILE A 133 1.049 29.770 28.110 1.00 81.02 C ANISOU 1045 CG1 ILE A 133 11903 10883 7997 -411 -1640 966 C ATOM 1046 CG2 ILE A 133 0.803 27.674 26.756 1.00 68.25 C ANISOU 1046 CG2 ILE A 133 10635 9221 6077 -684 -1623 867 C ATOM 1047 CD1 ILE A 133 1.741 30.542 27.007 1.00 74.29 C ANISOU 1047 CD1 ILE A 133 11263 9964 6999 -471 -1599 1002 C ATOM 1048 N GLU A 134 1.960 25.531 29.486 1.00 98.92 N ANISOU 1048 N GLU A 134 14190 13069 10326 -481 -1275 664 N ATOM 1049 CA GLU A 134 2.181 24.089 29.415 1.00 98.46 C ANISOU 1049 CA GLU A 134 14227 12942 10242 -555 -1186 574 C ATOM 1050 C GLU A 134 1.227 23.334 30.331 1.00 90.28 C ANISOU 1050 C GLU A 134 13043 11968 9289 -564 -1296 597 C ATOM 1051 O GLU A 134 0.670 22.301 29.944 1.00 82.85 O ANISOU 1051 O GLU A 134 12199 11008 8271 -685 -1346 567 O ATOM 1052 CB GLU A 134 3.633 23.759 29.767 1.00 97.46 C ANISOU 1052 CB GLU A 134 14100 12707 10225 -472 -957 490 C ATOM 1053 CG GLU A 134 4.643 24.149 28.699 1.00112.12 C ANISOU 1053 CG GLU A 134 16136 14475 11989 -504 -793 433 C ATOM 1054 CD GLU A 134 6.078 23.906 29.135 1.00127.71 C ANISOU 1054 CD GLU A 134 18052 16339 14132 -406 -570 354 C ATOM 1055 OE1 GLU A 134 6.282 23.372 30.247 1.00138.72 O ANISOU 1055 OE1 GLU A 134 19286 17718 15703 -320 -569 354 O ATOM 1056 OE2 GLU A 134 7.001 24.252 28.367 1.00117.62 O ANISOU 1056 OE2 GLU A 134 16889 14986 12816 -423 -401 299 O ATOM 1057 N ARG A 135 1.019 23.834 31.548 1.00 83.44 N ANISOU 1057 N ARG A 135 11955 11177 8573 -453 -1327 645 N ATOM 1058 CA ARG A 135 0.126 23.144 32.472 1.00 70.86 C ANISOU 1058 CA ARG A 135 10225 9647 7051 -476 -1406 666 C ATOM 1059 C ARG A 135 -1.325 23.245 32.018 1.00 88.88 C ANISOU 1059 C ARG A 135 12475 12016 9278 -572 -1599 723 C ATOM 1060 O ARG A 135 -2.103 22.301 32.197 1.00 74.24 O ANISOU 1060 O ARG A 135 10601 10184 7421 -665 -1665 722 O ATOM 1061 CB ARG A 135 0.309 23.704 33.878 1.00 66.28 C ANISOU 1061 CB ARG A 135 9440 9123 6618 -353 -1370 691 C ATOM 1062 CG ARG A 135 1.726 23.530 34.383 1.00 58.22 C ANISOU 1062 CG ARG A 135 8437 8012 5673 -271 -1217 649 C ATOM 1063 CD ARG A 135 1.939 24.200 35.718 1.00 76.52 C ANISOU 1063 CD ARG A 135 10582 10385 8105 -168 -1201 677 C ATOM 1064 NE ARG A 135 3.067 23.601 36.421 1.00 90.55 N ANISOU 1064 NE ARG A 135 12361 12075 9969 -125 -1106 654 N ATOM 1065 CZ ARG A 135 3.563 24.056 37.564 1.00 95.51 C ANISOU 1065 CZ ARG A 135 12880 12723 10686 -51 -1087 674 C ATOM 1066 NH1 ARG A 135 3.037 25.130 38.138 1.00 82.25 N ANISOU 1066 NH1 ARG A 135 11088 11147 9015 -8 -1127 698 N ATOM 1067 NH2 ARG A 135 4.590 23.439 38.130 1.00104.03 N ANISOU 1067 NH2 ARG A 135 13963 13708 11855 -23 -1035 669 N ATOM 1068 N TYR A 136 -1.708 24.376 31.424 1.00103.33 N ANISOU 1068 N TYR A 136 14293 13888 11081 -554 -1703 783 N ATOM 1069 CA TYR A 136 -3.038 24.473 30.832 1.00 94.49 C ANISOU 1069 CA TYR A 136 13148 12829 9924 -652 -1916 849 C ATOM 1070 C TYR A 136 -3.221 23.431 29.737 1.00 96.64 C ANISOU 1070 C TYR A 136 13651 13048 10021 -826 -1971 817 C ATOM 1071 O TYR A 136 -4.238 22.735 29.687 1.00108.89 O ANISOU 1071 O TYR A 136 15167 14637 11570 -934 -2101 835 O ATOM 1072 CB TYR A 136 -3.272 25.878 30.275 1.00 82.65 C ANISOU 1072 CB TYR A 136 11622 11350 8431 -604 -2032 931 C ATOM 1073 CG TYR A 136 -4.480 25.966 29.369 1.00 83.24 C ANISOU 1073 CG TYR A 136 11719 11456 8451 -724 -2283 1014 C ATOM 1074 CD1 TYR A 136 -5.763 26.002 29.898 1.00 82.53 C ANISOU 1074 CD1 TYR A 136 11394 11447 8517 -725 -2431 1065 C ATOM 1075 CD2 TYR A 136 -4.339 26.004 27.985 1.00 78.11 C ANISOU 1075 CD2 TYR A 136 11330 10754 7597 -849 -2374 1042 C ATOM 1076 CE1 TYR A 136 -6.871 26.075 29.078 1.00 85.32 C ANISOU 1076 CE1 TYR A 136 11744 11821 8854 -836 -2686 1151 C ATOM 1077 CE2 TYR A 136 -5.445 26.078 27.156 1.00 81.61 C ANISOU 1077 CE2 TYR A 136 11803 11221 7984 -975 -2641 1134 C ATOM 1078 CZ TYR A 136 -6.708 26.114 27.710 1.00 86.71 C ANISOU 1078 CZ TYR A 136 12187 11941 8817 -962 -2808 1193 C ATOM 1079 OH TYR A 136 -7.815 26.187 26.896 1.00102.83 O ANISOU 1079 OH TYR A 136 14233 13999 10837 -1087 -3098 1294 O ATOM 1080 N VAL A 137 -2.234 23.304 28.852 1.00 94.25 N ANISOU 1080 N VAL A 137 13588 12651 9571 -867 -1859 761 N ATOM 1081 CA VAL A 137 -2.353 22.381 27.728 1.00 97.93 C ANISOU 1081 CA VAL A 137 14310 13055 9842 -1047 -1890 710 C ATOM 1082 C VAL A 137 -2.381 20.937 28.217 1.00106.56 C ANISOU 1082 C VAL A 137 15409 14103 10976 -1099 -1815 630 C ATOM 1083 O VAL A 137 -3.244 20.144 27.822 1.00115.43 O ANISOU 1083 O VAL A 137 16598 15233 12029 -1246 -1944 628 O ATOM 1084 CB VAL A 137 -1.206 22.620 26.730 1.00 88.94 C ANISOU 1084 CB VAL A 137 13429 11821 8544 -1078 -1735 648 C ATOM 1085 CG1 VAL A 137 -1.052 21.435 25.801 1.00 95.43 C ANISOU 1085 CG1 VAL A 137 14524 12551 9184 -1253 -1674 542 C ATOM 1086 CG2 VAL A 137 -1.452 23.894 25.940 1.00 78.67 C ANISOU 1086 CG2 VAL A 137 12191 10558 7143 -1100 -1873 749 C ATOM 1087 N VAL A 138 -1.443 20.580 29.096 1.00105.31 N ANISOU 1087 N VAL A 138 15181 13891 10943 -985 -1622 571 N ATOM 1088 CA VAL A 138 -1.291 19.190 29.514 1.00 94.72 C ANISOU 1088 CA VAL A 138 13869 12470 9648 -1031 -1542 500 C ATOM 1089 C VAL A 138 -2.463 18.745 30.384 1.00 84.47 C ANISOU 1089 C VAL A 138 12388 11263 8444 -1066 -1681 562 C ATOM 1090 O VAL A 138 -2.972 17.628 30.235 1.00 73.90 O ANISOU 1090 O VAL A 138 11120 9885 7073 -1193 -1727 532 O ATOM 1091 CB VAL A 138 0.059 19.010 30.232 1.00 82.58 C ANISOU 1091 CB VAL A 138 12291 10839 8245 -895 -1329 444 C ATOM 1092 CG1 VAL A 138 0.038 17.781 31.124 1.00 82.86 C ANISOU 1092 CG1 VAL A 138 12267 10819 8399 -904 -1299 423 C ATOM 1093 CG2 VAL A 138 1.185 18.918 29.213 1.00 69.42 C ANISOU 1093 CG2 VAL A 138 10840 9043 6492 -912 -1153 341 C ATOM 1094 N VAL A 139 -2.915 19.603 31.293 1.00 90.70 N ANISOU 1094 N VAL A 139 12943 12166 9352 -966 -1737 642 N ATOM 1095 CA VAL A 139 -3.957 19.210 32.238 1.00 82.16 C ANISOU 1095 CA VAL A 139 11672 11171 8373 -999 -1821 690 C ATOM 1096 C VAL A 139 -5.353 19.435 31.667 1.00 87.69 C ANISOU 1096 C VAL A 139 12313 11960 9047 -1108 -2033 750 C ATOM 1097 O VAL A 139 -6.223 18.568 31.789 1.00 95.11 O ANISOU 1097 O VAL A 139 13217 12919 10001 -1229 -2117 758 O ATOM 1098 CB VAL A 139 -3.760 19.956 33.573 1.00 69.64 C ANISOU 1098 CB VAL A 139 9870 9659 6932 -853 -1749 725 C ATOM 1099 CG1 VAL A 139 -5.030 19.916 34.406 1.00 72.27 C ANISOU 1099 CG1 VAL A 139 9990 10108 7360 -895 -1834 776 C ATOM 1100 CG2 VAL A 139 -2.601 19.346 34.343 1.00 63.36 C ANISOU 1100 CG2 VAL A 139 9113 8773 6187 -788 -1589 684 C ATOM 1101 N CYS A 140 -5.593 20.583 31.031 1.00113.03 N ANISOU 1101 N CYS A 140 15112 8728 19107 -3172 -293 1212 N ATOM 1102 CA CYS A 140 -6.926 20.906 30.534 1.00106.34 C ANISOU 1102 CA CYS A 140 14177 8067 18160 -3487 -467 1118 C ATOM 1103 C CYS A 140 -7.271 20.199 29.230 1.00127.78 C ANISOU 1103 C CYS A 140 16968 10525 21057 -3857 -538 666 C ATOM 1104 O CYS A 140 -8.450 20.174 28.861 1.00151.65 O ANISOU 1104 O CYS A 140 19939 13668 24013 -4139 -675 528 O ATOM 1105 CB CYS A 140 -7.074 22.418 30.347 1.00109.64 C ANISOU 1105 CB CYS A 140 14432 8960 18265 -3454 -611 1358 C ATOM 1106 SG CYS A 140 -6.975 23.368 31.879 1.00128.27 S ANISOU 1106 SG CYS A 140 16670 11727 20340 -3043 -554 1797 S ATOM 1107 N LYS A 141 -6.288 19.628 28.537 1.00122.00 N ANISOU 1107 N LYS A 141 16348 9473 20535 -3847 -439 394 N ATOM 1108 CA LYS A 141 -6.504 18.891 27.298 1.00129.86 C ANISOU 1108 CA LYS A 141 17417 10235 21690 -4166 -472 -136 C ATOM 1109 C LYS A 141 -7.341 19.686 26.286 1.00141.07 C ANISOU 1109 C LYS A 141 18730 11995 22874 -4516 -733 -295 C ATOM 1110 O LYS A 141 -8.445 19.285 25.939 1.00160.53 O ANISOU 1110 O LYS A 141 21191 14504 25299 -4803 -842 -508 O ATOM 1111 CB LYS A 141 -7.158 17.544 27.582 1.00121.67 C ANISOU 1111 CB LYS A 141 16486 8902 20843 -4272 -406 -331 C ATOM 1112 CG LYS A 141 -6.569 16.780 28.762 1.00107.43 C ANISOU 1112 CG LYS A 141 14762 6856 19201 -3950 -231 -106 C ATOM 1113 CD LYS A 141 -7.215 15.409 28.909 1.00125.78 C ANISOU 1113 CD LYS A 141 17190 8882 21719 -4085 -196 -325 C ATOM 1114 CE LYS A 141 -6.720 14.688 30.156 1.00136.09 C ANISOU 1114 CE LYS A 141 18551 10007 23150 -3787 -67 -78 C ATOM 1115 NZ LYS A 141 -7.076 13.238 30.157 1.00130.70 N ANISOU 1115 NZ LYS A 141 17978 8972 22710 -3894 -16 -329 N ATOM 1116 N PRO A 142 -6.823 20.822 25.799 1.00133.40 N ANISOU 1116 N PRO A 142 17704 11448 21532 -4415 -810 -189 N ATOM 1117 CA PRO A 142 -7.618 21.669 24.905 1.00137.96 C ANISOU 1117 CA PRO A 142 18207 12587 21624 -4640 -1042 -287 C ATOM 1118 C PRO A 142 -7.468 21.365 23.423 1.00154.82 C ANISOU 1118 C PRO A 142 20442 14919 23462 -4796 -1023 -851 C ATOM 1119 O PRO A 142 -8.185 21.974 22.616 1.00162.31 O ANISOU 1119 O PRO A 142 21332 16321 24015 -5017 -1224 -965 O ATOM 1120 CB PRO A 142 -7.077 23.068 25.221 1.00138.54 C ANISOU 1120 CB PRO A 142 18181 13078 21380 -4394 -1100 147 C ATOM 1121 CG PRO A 142 -5.628 22.823 25.484 1.00136.10 C ANISOU 1121 CG PRO A 142 17968 12527 21216 -4051 -847 172 C ATOM 1122 CD PRO A 142 -5.518 21.437 26.100 1.00141.54 C ANISOU 1122 CD PRO A 142 18746 12559 22473 -4047 -672 55 C ATOM 1123 N MET A 143 -6.568 20.463 23.039 1.00162.80 N ANISOU 1123 N MET A 143 21595 15613 24650 -4696 -790 -1203 N ATOM 1124 CA MET A 143 -6.366 20.094 21.646 1.00169.97 C ANISOU 1124 CA MET A 143 22604 16674 25303 -4853 -743 -1765 C ATOM 1125 C MET A 143 -6.555 18.593 21.481 1.00183.07 C ANISOU 1125 C MET A 143 24373 17817 27369 -5017 -592 -2186 C ATOM 1126 O MET A 143 -6.069 17.803 22.297 1.00181.16 O ANISOU 1126 O MET A 143 24179 17056 27598 -4850 -409 -2102 O ATOM 1127 CB MET A 143 -4.971 20.507 21.155 1.00170.04 C ANISOU 1127 CB MET A 143 22683 16842 25082 -4576 -585 -1850 C ATOM 1128 CG MET A 143 -4.673 21.991 21.307 1.00170.39 C ANISOU 1128 CG MET A 143 22628 17392 24722 -4389 -712 -1441 C ATOM 1129 SD MET A 143 -3.246 22.539 20.345 1.00174.30 S ANISOU 1129 SD MET A 143 23213 18201 24813 -4163 -574 -1662 S ATOM 1130 CE MET A 143 -1.936 21.555 21.067 1.00176.60 C ANISOU 1130 CE MET A 143 23614 17861 25623 -3833 -237 -1678 C ATOM 1131 N SER A 144 -7.264 18.206 20.424 1.00194.74 N ANISOU 1131 N SER A 144 25886 19442 28664 -5349 -669 -2634 N ATOM 1132 CA SER A 144 -7.522 16.795 20.169 1.00206.32 C ANISOU 1132 CA SER A 144 27454 20454 30486 -5538 -530 -3068 C ATOM 1133 C SER A 144 -6.232 16.074 19.800 1.00209.50 C ANISOU 1133 C SER A 144 27989 20557 31056 -5349 -237 -3392 C ATOM 1134 O SER A 144 -5.493 16.517 18.915 1.00208.40 O ANISOU 1134 O SER A 144 27893 20726 30563 -5285 -187 -3603 O ATOM 1135 CB SER A 144 -8.553 16.634 19.052 1.00216.43 C ANISOU 1135 CB SER A 144 28736 22015 31480 -5946 -682 -3477 C ATOM 1136 OG SER A 144 -9.852 16.985 19.494 1.00217.93 O ANISOU 1136 OG SER A 144 28812 22343 31648 -6150 -927 -3221 O ATOM 1137 N ASN A 145 -5.968 14.963 20.485 1.00213.22 N ANISOU 1137 N ASN A 145 28518 20421 32073 -5264 -45 -3430 N ATOM 1138 CA ASN A 145 -4.827 14.089 20.212 1.00214.83 C ANISOU 1138 CA ASN A 145 28842 20246 32536 -5104 248 -3756 C ATOM 1139 C ASN A 145 -3.515 14.879 20.203 1.00211.72 C ANISOU 1139 C ASN A 145 28458 20046 31940 -4755 345 -3583 C ATOM 1140 O ASN A 145 -2.875 15.079 19.171 1.00219.80 O ANISOU 1140 O ASN A 145 29542 21322 32650 -4752 418 -3917 O ATOM 1141 CB ASN A 145 -5.022 13.340 18.890 1.00215.88 C ANISOU 1141 CB ASN A 145 29068 20406 32551 -5399 324 -4414 C ATOM 1142 CG ASN A 145 -6.398 12.720 18.768 1.00214.11 C ANISOU 1142 CG ASN A 145 28828 20097 32428 -5772 198 -4594 C ATOM 1143 OD1 ASN A 145 -7.114 12.565 19.757 1.00212.74 O ANISOU 1143 OD1 ASN A 145 28594 19759 32477 -5745 85 -4223 O ATOM 1144 ND2 ASN A 145 -6.775 12.357 17.547 1.00218.99 N ANISOU 1144 ND2 ASN A 145 29500 20895 32813 -6078 196 -5116 N ATOM 1145 N PHE A 146 -3.130 15.326 21.396 1.00196.01 N ANISOU 1145 N PHE A 146 26406 17932 30135 -4467 346 -3049 N ATOM 1146 CA PHE A 146 -1.874 16.041 21.569 1.00174.90 C ANISOU 1146 CA PHE A 146 23736 15392 27323 -4111 448 -2829 C ATOM 1147 C PHE A 146 -1.251 15.671 22.904 1.00178.59 C ANISOU 1147 C PHE A 146 24194 15372 28289 -3813 590 -2438 C ATOM 1148 O PHE A 146 -1.906 15.769 23.945 1.00175.00 O ANISOU 1148 O PHE A 146 23659 14789 28042 -3823 479 -2031 O ATOM 1149 CB PHE A 146 -2.071 17.559 21.496 1.00155.92 C ANISOU 1149 CB PHE A 146 21233 13616 24394 -4066 228 -2488 C ATOM 1150 CG PHE A 146 -0.828 18.338 21.815 1.00157.02 C ANISOU 1150 CG PHE A 146 21368 13888 24405 -3690 327 -2204 C ATOM 1151 CD1 PHE A 146 0.137 18.551 20.846 1.00160.36 C ANISOU 1151 CD1 PHE A 146 21871 14524 24536 -3592 444 -2520 C ATOM 1152 CD2 PHE A 146 -0.615 18.845 23.088 1.00147.96 C ANISOU 1152 CD2 PHE A 146 20139 12650 23428 -3442 310 -1630 C ATOM 1153 CE1 PHE A 146 1.284 19.258 21.136 1.00146.32 C ANISOU 1153 CE1 PHE A 146 20092 12866 22638 -3245 539 -2268 C ATOM 1154 CE2 PHE A 146 0.535 19.550 23.382 1.00132.42 C ANISOU 1154 CE2 PHE A 146 18168 10805 21340 -3099 408 -1372 C ATOM 1155 CZ PHE A 146 1.483 19.758 22.406 1.00136.46 C ANISOU 1155 CZ PHE A 146 18761 11528 21560 -2996 521 -1692 C ATOM 1156 N ARG A 147 0.013 15.255 22.868 1.00187.95 N ANISOU 1156 N ARG A 147 25458 16291 29663 -3557 832 -2561 N ATOM 1157 CA ARG A 147 0.816 15.089 24.069 1.00190.05 C ANISOU 1157 CA ARG A 147 25711 16168 30333 -3229 968 -2160 C ATOM 1158 C ARG A 147 2.073 15.941 23.952 1.00184.81 C ANISOU 1158 C ARG A 147 25054 15761 29403 -2904 1057 -2017 C ATOM 1159 O ARG A 147 2.555 16.223 22.851 1.00185.23 O ANISOU 1159 O ARG A 147 25164 16116 29100 -2919 1100 -2370 O ATOM 1160 CB ARG A 147 1.197 13.625 24.315 1.00200.80 C ANISOU 1160 CB ARG A 147 27149 17097 32049 -3120 1132 -2325 C ATOM 1161 CG ARG A 147 1.471 13.317 25.785 1.00207.30 C ANISOU 1161 CG ARG A 147 27929 17817 33018 -2805 1111 -1770 C ATOM 1162 CD ARG A 147 2.161 11.975 25.968 1.00220.34 C ANISOU 1162 CD ARG A 147 29645 19122 34954 -2639 1285 -1922 C ATOM 1163 NE ARG A 147 3.602 12.062 25.745 1.00224.43 N ANISOU 1163 NE ARG A 147 30191 19576 35504 -2354 1479 -1992 N ATOM 1164 CZ ARG A 147 4.517 11.954 26.704 1.00218.74 C ANISOU 1164 CZ ARG A 147 29440 18822 34851 -2012 1534 -1626 C ATOM 1165 NH1 ARG A 147 4.147 11.743 27.960 1.00215.54 N ANISOU 1165 NH1 ARG A 147 28977 18451 34466 -1921 1418 -1189 N ATOM 1166 NH2 ARG A 147 5.805 12.048 26.405 1.00215.74 N ANISOU 1166 NH2 ARG A 147 29085 18405 34482 -1772 1705 -1719 N ATOM 1167 N PHE A 148 2.600 16.340 25.104 1.00174.85 N ANISOU 1167 N PHE A 148 23737 14379 28318 -2617 1086 -1497 N ATOM 1168 CA PHE A 148 3.660 17.337 25.181 1.00151.63 C ANISOU 1168 CA PHE A 148 20780 11736 25095 -2305 1133 -1250 C ATOM 1169 C PHE A 148 5.022 16.653 25.138 1.00155.89 C ANISOU 1169 C PHE A 148 21410 11894 25929 -2041 1412 -1433 C ATOM 1170 O PHE A 148 5.363 15.878 26.039 1.00161.34 O ANISOU 1170 O PHE A 148 22087 12376 26838 -1837 1452 -1206 O ATOM 1171 CB PHE A 148 3.497 18.160 26.457 1.00123.19 C ANISOU 1171 CB PHE A 148 17065 8224 21519 -2147 1021 -586 C ATOM 1172 CG PHE A 148 4.448 19.307 26.565 1.00113.34 C ANISOU 1172 CG PHE A 148 15786 7341 19936 -1849 1044 -296 C ATOM 1173 CD1 PHE A 148 4.145 20.530 25.991 1.00112.49 C ANISOU 1173 CD1 PHE A 148 15624 7859 19256 -1908 871 -235 C ATOM 1174 CD2 PHE A 148 5.642 19.166 27.249 1.00105.17 C ANISOU 1174 CD2 PHE A 148 14770 6125 19067 -1493 1210 -75 C ATOM 1175 CE1 PHE A 148 5.016 21.592 26.094 1.00105.70 C ANISOU 1175 CE1 PHE A 148 14737 7337 18086 -1633 897 31 C ATOM 1176 CE2 PHE A 148 6.519 20.220 27.354 1.00115.50 C ANISOU 1176 CE2 PHE A 148 16055 7685 20145 -1235 1260 187 C ATOM 1177 CZ PHE A 148 6.205 21.438 26.776 1.00121.05 C ANISOU 1177 CZ PHE A 148 16709 8999 20285 -1298 1096 238 C ATOM 1178 N GLY A 149 5.804 16.951 24.100 1.00150.52 N ANISOU 1178 N GLY A 149 20796 11477 24919 -1971 1502 -1771 N ATOM 1179 CA GLY A 149 7.070 16.300 23.868 1.00144.46 C ANISOU 1179 CA GLY A 149 20116 10378 24393 -1752 1768 -2026 C ATOM 1180 C GLY A 149 8.265 17.173 24.201 1.00136.43 C ANISOU 1180 C GLY A 149 19085 9549 23201 -1383 1847 -1718 C ATOM 1181 O GLY A 149 8.147 18.273 24.745 1.00148.95 O ANISOU 1181 O GLY A 149 20590 11490 24513 -1275 1706 -1258 O ATOM 1182 N GLU A 150 9.445 16.649 23.862 1.00122.69 N ANISOU 1182 N GLU A 150 17426 7555 21634 -1190 2087 -1988 N ATOM 1183 CA GLU A 150 10.684 17.380 24.107 1.00124.03 C ANISOU 1183 CA GLU A 150 17597 7872 21659 -831 2190 -1750 C ATOM 1184 C GLU A 150 10.789 18.605 23.207 1.00134.16 C ANISOU 1184 C GLU A 150 18883 9832 22261 -849 2079 -1835 C ATOM 1185 O GLU A 150 11.233 19.671 23.649 1.00143.82 O ANISOU 1185 O GLU A 150 20056 11373 23218 -625 2029 -1432 O ATOM 1186 CB GLU A 150 11.882 16.452 23.899 1.00130.71 C ANISOU 1186 CB GLU A 150 18493 8461 22710 -624 2401 -2010 C ATOM 1187 CG GLU A 150 13.236 17.088 24.175 1.00152.05 C ANISOU 1187 CG GLU A 150 21182 11344 25245 -246 2494 -1769 C ATOM 1188 CD GLU A 150 14.390 16.256 23.642 1.00157.18 C ANISOU 1188 CD GLU A 150 21883 11832 26006 -104 2686 -2131 C ATOM 1189 OE1 GLU A 150 14.155 15.413 22.750 1.00150.52 O ANISOU 1189 OE1 GLU A 150 21111 10787 25293 -320 2778 -2663 O ATOM 1190 OE2 GLU A 150 15.530 16.445 24.114 1.00160.36 O ANISOU 1190 OE2 GLU A 150 22244 12341 26346 209 2735 -1882 O ATOM 1191 N ASN A 151 10.376 18.473 21.944 1.00129.30 N ANISOU 1191 N ASN A 151 18324 9450 21353 -1123 2039 -2353 N ATOM 1192 CA ASN A 151 10.479 19.587 21.007 1.00118.61 C ANISOU 1192 CA ASN A 151 16980 8736 19349 -1162 1931 -2468 C ATOM 1193 C ASN A 151 9.583 20.748 21.422 1.00110.90 C ANISOU 1193 C ASN A 151 15894 8228 18014 -1232 1659 -2013 C ATOM 1194 O ASN A 151 9.952 21.915 21.245 1.00125.37 O ANISOU 1194 O ASN A 151 17701 10542 19394 -1099 1587 -1824 O ATOM 1195 CB ASN A 151 10.134 19.116 19.594 1.00141.05 C ANISOU 1195 CB ASN A 151 19904 11706 21984 -1482 1938 -3120 C ATOM 1196 CG ASN A 151 11.085 18.046 19.088 1.00157.03 C ANISOU 1196 CG ASN A 151 22033 13306 24327 -1416 2222 -3602 C ATOM 1197 OD1 ASN A 151 12.216 17.934 19.560 1.00164.52 O ANISOU 1197 OD1 ASN A 151 23001 14004 25505 -1094 2409 -3479 O ATOM 1198 ND2 ASN A 151 10.631 17.256 18.121 1.00158.82 N ANISOU 1198 ND2 ASN A 151 22321 13450 24573 -1727 2259 -4157 N ATOM 1199 N HIS A 152 8.406 20.453 21.977 1.00112.43 N ANISOU 1199 N HIS A 152 16020 8287 18411 -1440 1510 -1836 N ATOM 1200 CA HIS A 152 7.538 21.521 22.461 1.00114.30 C ANISOU 1200 CA HIS A 152 16140 8929 18359 -1504 1260 -1385 C ATOM 1201 C HIS A 152 8.180 22.263 23.627 1.00115.09 C ANISOU 1201 C HIS A 152 16170 9044 18516 -1161 1289 -791 C ATOM 1202 O HIS A 152 8.132 23.498 23.686 1.00124.46 O ANISOU 1202 O HIS A 152 17286 10718 19284 -1088 1156 -489 O ATOM 1203 CB HIS A 152 6.177 20.956 22.872 1.00124.70 C ANISOU 1203 CB HIS A 152 17402 10044 19934 -1794 1114 -1330 C ATOM 1204 CG HIS A 152 5.428 20.302 21.753 1.00119.55 C ANISOU 1204 CG HIS A 152 16808 9420 19196 -2155 1065 -1884 C ATOM 1205 ND1 HIS A 152 5.162 18.949 21.727 1.00120.12 N ANISOU 1205 ND1 HIS A 152 16939 8976 19724 -2305 1179 -2203 N ATOM 1206 CD2 HIS A 152 4.887 20.813 20.622 1.00116.77 C ANISOU 1206 CD2 HIS A 152 16461 9553 18353 -2402 914 -2172 C ATOM 1207 CE1 HIS A 152 4.491 18.656 20.628 1.00137.91 C ANISOU 1207 CE1 HIS A 152 19233 11400 21766 -2632 1109 -2670 C ATOM 1208 NE2 HIS A 152 4.312 19.769 19.940 1.00146.20 N ANISOU 1208 NE2 HIS A 152 20251 13057 22241 -2700 944 -2658 N ATOM 1209 N ALA A 153 8.789 21.526 24.559 1.00123.17 N ANISOU 1209 N ALA A 153 17207 9538 20055 -953 1464 -615 N ATOM 1210 CA ALA A 153 9.455 22.159 25.694 1.00128.66 C ANISOU 1210 CA ALA A 153 17837 10219 20828 -631 1508 -54 C ATOM 1211 C ALA A 153 10.594 23.057 25.229 1.00121.73 C ANISOU 1211 C ALA A 153 16992 9710 19550 -371 1591 -56 C ATOM 1212 O ALA A 153 10.699 24.216 25.649 1.00122.19 O ANISOU 1212 O ALA A 153 16975 10151 19302 -230 1502 356 O ATOM 1213 CB ALA A 153 9.967 21.091 26.662 1.00119.42 C ANISOU 1213 CB ALA A 153 16686 8389 20297 -470 1691 77 C ATOM 1214 N ILE A 154 11.458 22.530 24.357 1.00112.59 N ANISOU 1214 N ILE A 154 15947 8438 18394 -310 1770 -526 N ATOM 1215 CA ILE A 154 12.549 23.321 23.793 1.00105.79 C ANISOU 1215 CA ILE A 154 15131 7925 17141 -84 1856 -596 C ATOM 1216 C ILE A 154 12.009 24.577 23.122 1.00114.51 C ANISOU 1216 C ILE A 154 16193 9713 17603 -214 1643 -561 C ATOM 1217 O ILE A 154 12.551 25.676 23.298 1.00104.19 O ANISOU 1217 O ILE A 154 14850 8777 15959 -1 1622 -264 O ATOM 1218 CB ILE A 154 13.368 22.461 22.813 1.00108.75 C ANISOU 1218 CB ILE A 154 15634 8070 17616 -77 2066 -1193 C ATOM 1219 CG1 ILE A 154 14.173 21.405 23.576 1.00 91.63 C ANISOU 1219 CG1 ILE A 154 13496 5250 16069 140 2298 -1149 C ATOM 1220 CG2 ILE A 154 14.259 23.334 21.941 1.00 88.53 C ANISOU 1220 CG2 ILE A 154 13128 5968 14542 61 2112 -1369 C ATOM 1221 CD1 ILE A 154 14.872 20.414 22.682 1.00 98.89 C ANISOU 1221 CD1 ILE A 154 14529 5869 17177 120 2513 -1745 C ATOM 1222 N MET A 155 10.930 24.434 22.346 1.00119.43 N ANISOU 1222 N MET A 155 16815 10512 18051 -568 1481 -857 N ATOM 1223 CA MET A 155 10.283 25.598 21.749 1.00111.72 C ANISOU 1223 CA MET A 155 15783 10171 16494 -720 1252 -797 C ATOM 1224 C MET A 155 9.891 26.617 22.811 1.00109.00 C ANISOU 1224 C MET A 155 15303 10052 16061 -606 1107 -157 C ATOM 1225 O MET A 155 10.105 27.822 22.633 1.00117.73 O ANISOU 1225 O MET A 155 16365 11656 16709 -505 1021 44 O ATOM 1226 CB MET A 155 9.055 25.167 20.947 1.00119.71 C ANISOU 1226 CB MET A 155 16798 11264 17421 -1135 1090 -1156 C ATOM 1227 CG MET A 155 9.368 24.546 19.596 1.00139.58 C ANISOU 1227 CG MET A 155 19440 13787 19808 -1299 1188 -1817 C ATOM 1228 SD MET A 155 7.883 23.957 18.759 1.00154.41 S ANISOU 1228 SD MET A 155 21315 15721 21631 -1798 1005 -2214 S ATOM 1229 CE MET A 155 8.598 22.997 17.427 1.00161.80 C ANISOU 1229 CE MET A 155 22409 16499 22568 -1912 1219 -2972 C ATOM 1230 N GLY A 156 9.322 26.152 23.926 1.00 90.83 N ANISOU 1230 N GLY A 156 12932 7387 14194 -625 1084 169 N ATOM 1231 CA GLY A 156 8.910 27.073 24.974 1.00 98.89 C ANISOU 1231 CA GLY A 156 13818 8599 15159 -541 956 771 C ATOM 1232 C GLY A 156 10.071 27.841 25.575 1.00109.71 C ANISOU 1232 C GLY A 156 15172 10082 16430 -164 1080 1135 C ATOM 1233 O GLY A 156 9.977 29.051 25.797 1.00106.21 O ANISOU 1233 O GLY A 156 14641 10083 15633 -89 968 1484 O ATOM 1234 N VAL A 157 11.181 27.148 25.846 1.00107.97 N ANISOU 1234 N VAL A 157 15033 9461 16528 76 1316 1059 N ATOM 1235 CA VAL A 157 12.368 27.815 26.377 1.00 82.29 C ANISOU 1235 CA VAL A 157 11776 6299 13191 443 1452 1376 C ATOM 1236 C VAL A 157 12.864 28.869 25.395 1.00 88.77 C ANISOU 1236 C VAL A 157 12628 7694 13407 511 1420 1223 C ATOM 1237 O VAL A 157 13.116 30.020 25.768 1.00 95.30 O ANISOU 1237 O VAL A 157 13384 8897 13928 678 1374 1605 O ATOM 1238 CB VAL A 157 13.465 26.784 26.703 1.00 84.26 C ANISOU 1238 CB VAL A 157 12113 5999 13902 666 1711 1255 C ATOM 1239 CG1 VAL A 157 14.746 27.486 27.119 1.00 81.63 C ANISOU 1239 CG1 VAL A 157 11784 5791 13442 1042 1855 1535 C ATOM 1240 CG2 VAL A 157 12.999 25.831 27.800 1.00 78.00 C ANISOU 1240 CG2 VAL A 157 11258 4750 13630 604 1694 1452 C ATOM 1241 N ALA A 158 12.994 28.495 24.118 1.00 90.87 N ANISOU 1241 N ALA A 158 12999 8041 13487 372 1445 658 N ATOM 1242 CA ALA A 158 13.425 29.458 23.109 1.00 80.87 C ANISOU 1242 CA ALA A 158 11770 7324 11634 405 1405 478 C ATOM 1243 C ALA A 158 12.471 30.641 23.022 1.00 83.88 C ANISOU 1243 C ALA A 158 12039 8255 11577 252 1147 742 C ATOM 1244 O ALA A 158 12.903 31.767 22.754 1.00 74.77 O ANISOU 1244 O ALA A 158 10866 7571 9971 386 1109 880 O ATOM 1245 CB ALA A 158 13.550 28.775 21.748 1.00 93.23 C ANISOU 1245 CB ALA A 158 13461 8870 13093 216 1458 -192 C ATOM 1246 N PHE A 159 11.176 30.408 23.247 1.00105.69 N ANISOU 1246 N PHE A 159 14722 10964 14472 -26 969 818 N ATOM 1247 CA PHE A 159 10.222 31.510 23.264 1.00101.45 C ANISOU 1247 CA PHE A 159 14060 10915 13571 -171 721 1103 C ATOM 1248 C PHE A 159 10.497 32.457 24.425 1.00 94.88 C ANISOU 1248 C PHE A 159 13116 10213 12722 84 726 1723 C ATOM 1249 O PHE A 159 10.390 33.679 24.272 1.00 92.16 O ANISOU 1249 O PHE A 159 12696 10378 11942 117 605 1943 O ATOM 1250 CB PHE A 159 8.793 30.969 23.329 1.00 83.93 C ANISOU 1250 CB PHE A 159 11779 8558 11551 -519 544 1050 C ATOM 1251 CG PHE A 159 7.744 32.036 23.451 1.00 76.58 C ANISOU 1251 CG PHE A 159 10703 8078 10315 -675 289 1367 C ATOM 1252 CD1 PHE A 159 7.415 32.832 22.366 1.00 74.91 C ANISOU 1252 CD1 PHE A 159 10482 8405 9575 -829 124 1180 C ATOM 1253 CD2 PHE A 159 7.080 32.238 24.650 1.00 82.99 C ANISOU 1253 CD2 PHE A 159 11385 8771 11377 -677 214 1852 C ATOM 1254 CE1 PHE A 159 6.447 33.815 22.477 1.00 83.86 C ANISOU 1254 CE1 PHE A 159 11472 9943 10447 -971 -113 1478 C ATOM 1255 CE2 PHE A 159 6.110 33.218 24.769 1.00 88.56 C ANISOU 1255 CE2 PHE A 159 11948 9879 11823 -823 -14 2138 C ATOM 1256 CZ PHE A 159 5.792 34.006 23.681 1.00 82.86 C ANISOU 1256 CZ PHE A 159 11211 9685 10587 -966 -179 1954 C ATOM 1257 N THR A 160 10.856 31.917 25.594 1.00 92.99 N ANISOU 1257 N THR A 160 12859 9521 12951 260 866 2014 N ATOM 1258 CA THR A 160 11.242 32.785 26.702 1.00 86.97 C ANISOU 1258 CA THR A 160 11998 8872 12175 512 899 2591 C ATOM 1259 C THR A 160 12.463 33.620 26.340 1.00 96.16 C ANISOU 1259 C THR A 160 13211 10364 12962 801 1015 2608 C ATOM 1260 O THR A 160 12.521 34.814 26.656 1.00104.01 O ANISOU 1260 O THR A 160 14060 11854 13605 847 877 2774 O ATOM 1261 CB THR A 160 11.513 31.967 27.968 1.00 87.70 C ANISOU 1261 CB THR A 160 12043 8531 12747 607 977 2718 C ATOM 1262 OG1 THR A 160 12.559 31.019 27.721 1.00105.87 O ANISOU 1262 OG1 THR A 160 14499 10354 15372 794 1243 2518 O ATOM 1263 CG2 THR A 160 10.261 31.231 28.414 1.00 86.85 C ANISOU 1263 CG2 THR A 160 11888 8143 12968 332 855 2737 C ATOM 1264 N TRP A 161 13.443 33.016 25.659 1.00 92.67 N ANISOU 1264 N TRP A 161 12910 9755 12545 918 1188 2202 N ATOM 1265 CA ATRP A 161 14.643 33.757 25.279 0.66 78.91 C ANISOU 1265 CA ATRP A 161 11225 8307 10449 1193 1308 2184 C ATOM 1266 CA BTRP A 161 14.641 33.762 25.284 0.34 79.12 C ANISOU 1266 CA BTRP A 161 11251 8335 10476 1193 1308 2187 C ATOM 1267 C TRP A 161 14.324 34.845 24.261 1.00 89.87 C ANISOU 1267 C TRP A 161 12599 10330 11219 1073 1139 2059 C ATOM 1268 O TRP A 161 14.874 35.950 24.332 1.00 98.49 O ANISOU 1268 O TRP A 161 13658 11812 11952 1272 1147 2305 O ATOM 1269 CB ATRP A 161 15.702 32.804 24.725 0.66 74.84 C ANISOU 1269 CB ATRP A 161 10863 7453 10120 1314 1529 1736 C ATOM 1270 CB BTRP A 161 15.713 32.813 24.747 0.34 77.08 C ANISOU 1270 CB BTRP A 161 11145 7735 10405 1319 1531 1746 C ATOM 1271 CG ATRP A 161 16.195 31.800 25.720 0.66 83.23 C ANISOU 1271 CG ATRP A 161 11940 7902 11780 1475 1712 1878 C ATOM 1272 CG BTRP A 161 16.322 31.932 25.795 0.34 82.31 C ANISOU 1272 CG BTRP A 161 11819 7817 11636 1520 1724 1930 C ATOM 1273 CD1ATRP A 161 15.861 31.720 27.042 0.66 79.42 C ANISOU 1273 CD1ATRP A 161 11289 7318 11570 1458 1626 2253 C ATOM 1274 CD1BTRP A 161 15.913 30.682 26.148 0.34 90.43 C ANISOU 1274 CD1BTRP A 161 12865 8303 13192 1392 1764 1811 C ATOM 1275 CD2ATRP A 161 17.113 30.727 25.473 0.66 91.37 C ANISOU 1275 CD2ATRP A 161 13092 8488 13139 1593 1931 1526 C ATOM 1276 CD2BTRP A 161 17.452 32.233 26.625 0.34 82.91 C ANISOU 1276 CD2BTRP A 161 11785 8001 11716 1756 1797 2117 C ATOM 1277 NE1ATRP A 161 16.514 30.665 27.632 0.66 88.80 N ANISOU 1277 NE1ATRP A 161 12435 8185 13118 1492 1697 2092 N ATOM 1278 NE1BTRP A 161 16.713 30.184 27.147 0.34 92.34 N ANISOU 1278 NE1BTRP A 161 13019 8335 13729 1549 1839 1940 N ATOM 1279 CE2ATRP A 161 17.288 30.039 26.690 0.66 97.69 C ANISOU 1279 CE2ATRP A 161 13803 8894 14418 1669 1979 1785 C ATOM 1280 CE2BTRP A 161 17.666 31.116 27.458 0.34 89.51 C ANISOU 1280 CE2BTRP A 161 12524 8508 12979 1681 1793 2027 C ATOM 1281 CE3ATRP A 161 17.803 30.283 24.340 0.66 73.54 C ANISOU 1281 CE3ATRP A 161 10965 6209 10770 1594 2050 971 C ATOM 1282 CE3BTRP A 161 18.303 33.337 26.745 0.34 68.16 C ANISOU 1282 CE3BTRP A 161 9772 6706 9419 1844 1751 2138 C ATOM 1283 CZ2ATRP A 161 18.125 28.928 26.807 0.66 93.16 C ANISOU 1283 CZ2ATRP A 161 13249 7968 14179 1731 2106 1520 C ATOM 1284 CZ2BTRP A 161 18.696 31.071 28.397 0.34 87.19 C ANISOU 1284 CZ2BTRP A 161 12045 8432 12652 1704 1749 2011 C ATOM 1285 CZ3ATRP A 161 18.632 29.180 24.458 0.66 84.08 C ANISOU 1285 CZ3ATRP A 161 12382 7014 12552 1730 2273 750 C ATOM 1286 CZ3BTRP A 161 19.325 33.290 27.678 0.34 56.22 C ANISOU 1286 CZ3BTRP A 161 8059 5351 7951 1829 1740 2066 C ATOM 1287 CH2ATRP A 161 18.786 28.516 25.682 0.66 86.61 C ANISOU 1287 CH2ATRP A 161 12656 6829 13423 1867 2370 1085 C ATOM 1288 CH2BTRP A 161 19.512 32.165 28.492 0.34 72.54 C ANISOU 1288 CH2BTRP A 161 10077 7082 10402 1764 1736 2027 C ATOM 1289 N VAL A 162 13.443 34.551 23.303 1.00 99.56 N ANISOU 1289 N VAL A 162 13847 11669 12311 746 984 1680 N ATOM 1290 CA VAL A 162 13.082 35.546 22.296 1.00 94.75 C ANISOU 1290 CA VAL A 162 13220 11659 11119 605 805 1554 C ATOM 1291 C VAL A 162 12.335 36.708 22.940 1.00 99.88 C ANISOU 1291 C VAL A 162 13703 12676 11570 587 621 2075 C ATOM 1292 O VAL A 162 12.635 37.879 22.679 1.00103.55 O ANISOU 1292 O VAL A 162 14132 13625 11586 696 567 2233 O ATOM 1293 CB VAL A 162 12.259 34.898 21.167 1.00 92.38 C ANISOU 1293 CB VAL A 162 12976 11373 10750 236 678 1039 C ATOM 1294 CG1 VAL A 162 11.530 35.963 20.364 1.00 90.24 C ANISOU 1294 CG1 VAL A 162 12641 11714 9935 35 432 1032 C ATOM 1295 CG2 VAL A 162 13.162 34.082 20.259 1.00 85.47 C ANISOU 1295 CG2 VAL A 162 12270 10307 9899 264 861 483 C ATOM 1296 N MET A 163 11.352 36.406 23.792 1.00103.89 N ANISOU 1296 N MET A 163 14103 12955 12415 446 525 2346 N ATOM 1297 CA MET A 163 10.637 37.468 24.493 1.00102.67 C ANISOU 1297 CA MET A 163 13773 13102 12134 415 357 2797 C ATOM 1298 C MET A 163 11.568 38.276 25.386 1.00110.05 C ANISOU 1298 C MET A 163 14567 14048 13201 544 341 2468 C ATOM 1299 O MET A 163 11.338 39.471 25.601 1.00114.11 O ANISOU 1299 O MET A 163 14946 14766 13644 452 199 2196 O ATOM 1300 CB MET A 163 9.492 36.885 25.321 1.00107.84 C ANISOU 1300 CB MET A 163 14332 13437 13205 210 256 2944 C ATOM 1301 CG MET A 163 8.355 36.290 24.510 1.00105.44 C ANISOU 1301 CG MET A 163 14041 13118 12904 -156 90 2673 C ATOM 1302 SD MET A 163 7.554 37.484 23.425 1.00110.41 S ANISOU 1302 SD MET A 163 14590 14443 12915 -382 -187 2601 S ATOM 1303 CE MET A 163 8.244 37.011 21.842 1.00112.33 C ANISOU 1303 CE MET A 163 15024 14787 12868 -443 -123 1930 C ATOM 1304 N ALA A 164 12.621 37.650 25.914 1.00101.68 N ANISOU 1304 N ALA A 164 13525 12722 12387 743 525 2470 N ATOM 1305 CA ALA A 164 13.563 38.375 26.760 1.00107.78 C ANISOU 1305 CA ALA A 164 14087 13606 13258 821 538 2209 C ATOM 1306 C ALA A 164 14.429 39.321 25.936 1.00107.10 C ANISOU 1306 C ALA A 164 13948 13832 12913 952 596 2066 C ATOM 1307 O ALA A 164 14.550 40.508 26.262 1.00112.02 O ANISOU 1307 O ALA A 164 14224 14762 13579 1065 661 1994 O ATOM 1308 CB ALA A 164 14.430 37.392 27.543 1.00108.18 C ANISOU 1308 CB ALA A 164 14149 13346 13608 969 711 2236 C ATOM 1309 N LEU A 165 15.048 38.810 24.867 1.00102.92 N ANISOU 1309 N LEU A 165 13677 13285 12144 1076 704 2107 N ATOM 1310 CA LEU A 165 15.851 39.666 23.996 1.00 91.06 C ANISOU 1310 CA LEU A 165 12165 12066 10368 1135 698 1889 C ATOM 1311 C LEU A 165 15.016 40.781 23.383 1.00 93.89 C ANISOU 1311 C LEU A 165 12426 12712 10535 900 475 1765 C ATOM 1312 O LEU A 165 15.510 41.900 23.204 1.00 88.49 O ANISOU 1312 O LEU A 165 11490 12262 9870 1059 514 1655 O ATOM 1313 CB LEU A 165 16.509 38.832 22.897 1.00 80.51 C ANISOU 1313 CB LEU A 165 11190 10735 8665 1412 967 1931 C ATOM 1314 CG LEU A 165 17.659 37.931 23.345 1.00100.26 C ANISOU 1314 CG LEU A 165 13859 12837 11399 1757 1296 1989 C ATOM 1315 CD1 LEU A 165 18.101 37.011 22.218 1.00 98.60 C ANISOU 1315 CD1 LEU A 165 13978 12461 11025 1811 1501 1621 C ATOM 1316 CD2 LEU A 165 18.822 38.779 23.836 1.00115.09 C ANISOU 1316 CD2 LEU A 165 15434 14838 13457 1826 1252 1768 C ATOM 1317 N ALA A 166 13.746 40.507 23.084 1.00 94.00 N ANISOU 1317 N ALA A 166 12556 12760 10400 685 339 1871 N ATOM 1318 CA ALA A 166 12.837 41.505 22.533 1.00 95.85 C ANISOU 1318 CA ALA A 166 12709 13207 10500 506 163 1753 C ATOM 1319 C ALA A 166 12.431 42.523 23.594 1.00118.83 C ANISOU 1319 C ALA A 166 15128 16247 13775 618 200 1827 C ATOM 1320 O ALA A 166 11.431 43.230 23.437 1.00115.47 O ANISOU 1320 O ALA A 166 14521 16003 13351 491 98 1836 O ATOM 1321 CB ALA A 166 11.597 40.825 21.949 1.00 70.79 C ANISOU 1321 CB ALA A 166 9698 10154 7045 338 62 1895 C ATOM 1322 N CYS A 167 13.210 42.611 24.670 1.00129.71 N ANISOU 1322 N CYS A 167 16261 17572 15451 836 378 1861 N ATOM 1323 CA CYS A 167 12.867 43.444 25.813 1.00132.38 C ANISOU 1323 CA CYS A 167 16131 18064 16105 896 468 1910 C ATOM 1324 C CYS A 167 14.125 43.981 26.486 1.00130.33 C ANISOU 1324 C CYS A 167 15592 17895 16034 1181 706 1845 C ATOM 1325 O CYS A 167 14.069 44.965 27.231 1.00135.87 O ANISOU 1325 O CYS A 167 16149 18598 16879 1086 680 1718 O ATOM 1326 CB CYS A 167 12.023 42.640 26.802 1.00133.90 C ANISOU 1326 CB CYS A 167 16328 18063 16485 778 437 2049 C ATOM 1327 SG CYS A 167 11.462 43.555 28.235 1.00132.99 S ANISOU 1327 SG CYS A 167 15635 18170 16725 779 534 2108 S ATOM 1328 N ALA A 168 15.267 43.339 26.231 1.00119.80 N ANISOU 1328 N ALA A 168 14490 16405 14625 1347 806 1787 N ATOM 1329 CA ALA A 168 16.538 43.772 26.791 1.00110.50 C ANISOU 1329 CA ALA A 168 13275 15157 13555 1459 914 1624 C ATOM 1330 C ALA A 168 17.488 44.365 25.762 1.00105.56 C ANISOU 1330 C ALA A 168 12750 14579 12781 1546 874 1469 C ATOM 1331 O ALA A 168 18.402 45.103 26.143 1.00115.21 O ANISOU 1331 O ALA A 168 14004 15678 14091 1436 814 1270 O ATOM 1332 CB ALA A 168 17.240 42.601 27.496 1.00105.04 C ANISOU 1332 CB ALA A 168 12716 14242 12954 1554 1075 1673 C ATOM 1333 N ALA A 169 17.292 44.071 24.481 1.00119.48 N ANISOU 1333 N ALA A 169 15520 16099 13778 -90 509 2148 N ATOM 1334 CA ALA A 169 18.151 44.540 23.400 1.00105.59 C ANISOU 1334 CA ALA A 169 13684 14418 12017 -360 728 2419 C ATOM 1335 C ALA A 169 17.798 45.932 22.866 1.00111.40 C ANISOU 1335 C ALA A 169 14518 14838 12972 -581 668 2744 C ATOM 1336 O ALA A 169 18.714 46.665 22.471 1.00113.51 O ANISOU 1336 O ALA A 169 14645 15070 13415 -847 786 2901 O ATOM 1337 CB ALA A 169 18.135 43.531 22.249 1.00 94.94 C ANISOU 1337 CB ALA A 169 12437 13401 10235 -328 940 2545 C ATOM 1338 N PRO A 170 16.524 46.333 22.798 1.00100.95 N ANISOU 1338 N PRO A 170 13425 13288 11642 -490 496 2872 N ATOM 1339 CA PRO A 170 16.195 47.669 22.260 1.00 98.34 C ANISOU 1339 CA PRO A 170 13190 12635 11539 -684 441 3210 C ATOM 1340 C PRO A 170 16.957 48.798 22.940 1.00 91.43 C ANISOU 1340 C PRO A 170 12145 11461 11134 -873 385 3146 C ATOM 1341 O PRO A 170 17.421 49.715 22.247 1.00 89.62 O ANISOU 1341 O PRO A 170 11895 11093 11062 -1145 469 3442 O ATOM 1342 CB PRO A 170 14.682 47.780 22.498 1.00103.51 C ANISOU 1342 CB PRO A 170 14077 13101 12150 -468 221 3235 C ATOM 1343 CG PRO A 170 14.210 46.397 22.366 1.00101.16 C ANISOU 1343 CG PRO A 170 13867 13143 11425 -257 262 3101 C ATOM 1344 CD PRO A 170 15.298 45.518 22.937 1.00 98.43 C ANISOU 1344 CD PRO A 170 13310 13045 11045 -221 377 2784 C ATOM 1345 N PRO A 171 17.108 48.805 24.274 1.00 87.46 N ANISOU 1345 N PRO A 171 11515 10853 10863 -761 244 2776 N ATOM 1346 CA PRO A 171 17.891 49.893 24.890 1.00 80.62 C ANISOU 1346 CA PRO A 171 10479 9718 10434 -977 204 2702 C ATOM 1347 C PRO A 171 19.351 49.922 24.468 1.00100.19 C ANISOU 1347 C PRO A 171 12726 12405 12935 -1248 425 2765 C ATOM 1348 O PRO A 171 19.987 50.979 24.573 1.00111.47 O ANISOU 1348 O PRO A 171 14054 13602 14696 -1512 429 2835 O ATOM 1349 CB PRO A 171 17.748 49.626 26.395 1.00 73.98 C ANISOU 1349 CB PRO A 171 9532 8838 9739 -779 24 2257 C ATOM 1350 CG PRO A 171 16.479 48.890 26.514 1.00 94.09 C ANISOU 1350 CG PRO A 171 12276 11447 12025 -473 -102 2197 C ATOM 1351 CD PRO A 171 16.456 47.989 25.318 1.00 96.56 C ANISOU 1351 CD PRO A 171 12687 12082 11918 -455 85 2426 C ATOM 1352 N LEU A 172 19.907 48.807 23.995 1.00 97.15 N ANISOU 1352 N LEU A 172 12252 12449 12211 -1196 612 2737 N ATOM 1353 CA LEU A 172 21.280 48.809 23.510 1.00 94.96 C ANISOU 1353 CA LEU A 172 11742 12413 11924 -1444 837 2811 C ATOM 1354 C LEU A 172 21.417 49.395 22.111 1.00 97.98 C ANISOU 1354 C LEU A 172 12210 12792 12226 -1711 990 3255 C ATOM 1355 O LEU A 172 22.546 49.645 21.676 1.00111.98 O ANISOU 1355 O LEU A 172 13789 14723 14036 -1972 1165 3359 O ATOM 1356 CB LEU A 172 21.858 47.389 23.507 1.00 84.90 C ANISOU 1356 CB LEU A 172 10329 11602 10325 -1270 992 2609 C ATOM 1357 CG LEU A 172 22.068 46.634 24.822 1.00 82.84 C ANISOU 1357 CG LEU A 172 9911 11457 10106 -1033 893 2188 C ATOM 1358 CD1 LEU A 172 23.001 45.459 24.587 1.00 95.42 C ANISOU 1358 CD1 LEU A 172 11317 13498 11438 -949 1106 2076 C ATOM 1359 CD2 LEU A 172 22.613 47.532 25.917 1.00 76.80 C ANISOU 1359 CD2 LEU A 172 8949 10482 9748 -1173 765 2001 C ATOM 1360 N VAL A 173 20.311 49.619 21.396 1.00101.69 N ANISOU 1360 N VAL A 173 12949 13112 12575 -1660 928 3530 N ATOM 1361 CA VAL A 173 20.367 50.016 19.995 1.00110.22 C ANISOU 1361 CA VAL A 173 14113 14259 13505 -1893 1078 3973 C ATOM 1362 C VAL A 173 19.522 51.241 19.679 1.00111.23 C ANISOU 1362 C VAL A 173 14446 13950 13865 -1997 930 4302 C ATOM 1363 O VAL A 173 19.487 51.667 18.524 1.00114.88 O ANISOU 1363 O VAL A 173 14987 14441 14219 -2199 1031 4713 O ATOM 1364 CB VAL A 173 19.973 48.850 19.065 1.00 98.09 C ANISOU 1364 CB VAL A 173 12686 13120 11463 -1751 1222 4053 C ATOM 1365 CG1 VAL A 173 21.075 47.801 19.036 1.00100.33 C ANISOU 1365 CG1 VAL A 173 12744 13843 11532 -1730 1438 3829 C ATOM 1366 CG2 VAL A 173 18.656 48.236 19.512 1.00 83.36 C ANISOU 1366 CG2 VAL A 173 11036 11188 9449 -1415 1044 3900 C ATOM 1367 N GLY A 174 18.831 51.826 20.655 1.00 92.66 N ANISOU 1367 N GLY A 174 12180 11201 11827 -1862 695 4143 N ATOM 1368 CA GLY A 174 18.185 53.095 20.386 1.00 93.12 C ANISOU 1368 CA GLY A 174 12407 10806 12169 -1973 566 4455 C ATOM 1369 C GLY A 174 16.743 53.257 20.819 1.00118.89 C ANISOU 1369 C GLY A 174 15893 13791 15487 -1686 334 4420 C ATOM 1370 O GLY A 174 16.215 54.371 20.768 1.00135.81 O ANISOU 1370 O GLY A 174 18163 15506 17931 -1744 208 4635 O ATOM 1371 N TRP A 175 16.082 52.177 21.226 1.00116.77 N ANISOU 1371 N TRP A 175 15677 13754 14936 -1378 275 4164 N ATOM 1372 CA TRP A 175 14.730 52.260 21.769 1.00114.33 C ANISOU 1372 CA TRP A 175 15548 13227 14665 -1094 47 4078 C ATOM 1373 C TRP A 175 14.840 52.188 23.288 1.00108.60 C ANISOU 1373 C TRP A 175 14702 12376 14186 -943 -101 3592 C ATOM 1374 O TRP A 175 15.197 51.144 23.842 1.00 87.66 O ANISOU 1374 O TRP A 175 11929 10035 11343 -818 -62 3272 O ATOM 1375 CB TRP A 175 13.831 51.157 21.217 1.00111.78 C ANISOU 1375 CB TRP A 175 15373 13244 13856 -876 64 4132 C ATOM 1376 CG TRP A 175 12.373 51.468 21.388 1.00119.65 C ANISOU 1376 CG TRP A 175 16574 14021 14867 -648 -150 4206 C ATOM 1377 CD1 TRP A 175 11.833 52.666 21.754 1.00117.39 C ANISOU 1377 CD1 TRP A 175 16361 13271 14971 -632 -323 4297 C ATOM 1378 CD2 TRP A 175 11.271 50.569 21.208 1.00128.68 C ANISOU 1378 CD2 TRP A 175 17866 15405 15620 -404 -212 4187 C ATOM 1379 NE1 TRP A 175 10.464 52.572 21.811 1.00109.27 N ANISOU 1379 NE1 TRP A 175 15504 12198 13816 -375 -488 4341 N ATOM 1380 CE2 TRP A 175 10.093 51.295 21.481 1.00121.63 C ANISOU 1380 CE2 TRP A 175 17117 14203 14896 -244 -426 4279 C ATOM 1381 CE3 TRP A 175 11.165 49.222 20.844 1.00118.39 C ANISOU 1381 CE3 TRP A 175 16591 14546 13845 -308 -105 4095 C ATOM 1382 CZ2 TRP A 175 8.826 50.719 21.401 1.00122.07 C ANISOU 1382 CZ2 TRP A 175 17325 14411 14646 -3 -539 4291 C ATOM 1383 CZ3 TRP A 175 9.907 48.653 20.765 1.00105.85 C ANISOU 1383 CZ3 TRP A 175 15172 13084 11961 -87 -217 4103 C ATOM 1384 CH2 TRP A 175 8.754 49.401 21.043 1.00115.29 C ANISOU 1384 CH2 TRP A 175 16492 13997 13316 58 -434 4205 C ATOM 1385 N SER A 176 14.532 53.306 23.952 1.00112.47 N ANISOU 1385 N SER A 176 15223 12410 15102 -955 -268 3541 N ATOM 1386 CA SER A 176 14.861 53.545 25.355 1.00112.01 C ANISOU 1386 CA SER A 176 15015 12188 15356 -911 -390 3103 C ATOM 1387 C SER A 176 16.366 53.425 25.585 1.00120.74 C ANISOU 1387 C SER A 176 15862 13470 16545 -1154 -235 2952 C ATOM 1388 O SER A 176 17.153 53.451 24.631 1.00107.76 O ANISOU 1388 O SER A 176 14164 11977 14803 -1392 -42 3224 O ATOM 1389 CB SER A 176 14.095 52.596 26.280 1.00 94.14 C ANISOU 1389 CB SER A 176 12762 10113 12895 -573 -532 2739 C ATOM 1390 OG SER A 176 14.145 53.056 27.621 1.00 90.20 O ANISOU 1390 OG SER A 176 12152 9393 12727 -521 -690 2356 O ATOM 1391 N ARG A 177 16.777 53.301 26.844 1.00120.44 N ANISOU 1391 N ARG A 177 15645 13441 16674 -1103 -318 2525 N ATOM 1392 CA ARG A 177 18.195 53.300 27.180 1.00105.67 C ANISOU 1392 CA ARG A 177 13505 11726 14919 -1337 -194 2368 C ATOM 1393 C ARG A 177 18.366 52.853 28.625 1.00106.04 C ANISOU 1393 C ARG A 177 13370 11882 15037 -1187 -314 1876 C ATOM 1394 O ARG A 177 17.456 52.990 29.447 1.00 94.00 O ANISOU 1394 O ARG A 177 11929 10175 13612 -980 -512 1661 O ATOM 1395 CB ARG A 177 18.812 54.684 26.975 1.00 96.42 C ANISOU 1395 CB ARG A 177 12304 10177 14155 -1685 -166 2542 C ATOM 1396 CG ARG A 177 18.010 55.784 27.634 1.00 92.73 C ANISOU 1396 CG ARG A 177 11971 9181 14082 -1639 -376 2456 C ATOM 1397 CD ARG A 177 18.835 57.032 27.851 1.00 99.15 C ANISOU 1397 CD ARG A 177 12694 9637 15342 -1988 -361 2464 C ATOM 1398 NE ARG A 177 18.276 57.838 28.930 1.00105.45 N ANISOU 1398 NE ARG A 177 13538 10011 16517 -1908 -565 2172 N ATOM 1399 CZ ARG A 177 18.803 58.975 29.366 1.00101.10 C ANISOU 1399 CZ ARG A 177 12934 9076 16403 -2175 -595 2085 C ATOM 1400 NH1 ARG A 177 19.909 59.450 28.810 1.00107.00 N ANISOU 1400 NH1 ARG A 177 13577 9816 17262 -2553 -441 2289 N ATOM 1401 NH2 ARG A 177 18.223 59.635 30.358 1.00 99.67 N ANISOU 1401 NH2 ARG A 177 12802 8525 16542 -2072 -778 1785 N ATOM 1402 N TYR A 178 19.552 52.325 28.922 1.00106.71 N ANISOU 1402 N TYR A 178 13192 12289 15062 -1295 -191 1707 N ATOM 1403 CA TYR A 178 19.906 51.911 30.274 1.00101.30 C ANISOU 1403 CA TYR A 178 12288 11758 14441 -1194 -289 1266 C ATOM 1404 C TYR A 178 20.615 53.051 30.992 1.00 94.20 C ANISOU 1404 C TYR A 178 11226 10596 13971 -1469 -339 1104 C ATOM 1405 O TYR A 178 21.602 53.592 30.483 1.00103.73 O ANISOU 1405 O TYR A 178 12321 11787 15305 -1782 -195 1268 O ATOM 1406 CB TYR A 178 20.805 50.673 30.246 1.00106.17 C ANISOU 1406 CB TYR A 178 12693 12888 14758 -1137 -134 1171 C ATOM 1407 CG TYR A 178 20.112 49.408 29.797 1.00 99.77 C ANISOU 1407 CG TYR A 178 12029 12350 13531 -841 -103 1228 C ATOM 1408 CD1 TYR A 178 18.882 49.041 30.322 1.00100.64 C ANISOU 1408 CD1 TYR A 178 12309 12387 13544 -557 -289 1093 C ATOM 1409 CD2 TYR A 178 20.688 48.583 28.842 1.00 99.56 C ANISOU 1409 CD2 TYR A 178 11969 12658 13203 -855 117 1407 C ATOM 1410 CE1 TYR A 178 18.248 47.886 29.911 1.00102.68 C ANISOU 1410 CE1 TYR A 178 12708 12888 13417 -313 -261 1143 C ATOM 1411 CE2 TYR A 178 20.061 47.429 28.424 1.00101.50 C ANISOU 1411 CE2 TYR A 178 12361 13133 13073 -602 153 1440 C ATOM 1412 CZ TYR A 178 18.842 47.084 28.961 1.00103.16 C ANISOU 1412 CZ TYR A 178 12748 13254 13195 -340 -39 1312 C ATOM 1413 OH TYR A 178 18.218 45.931 28.546 1.00105.80 O ANISOU 1413 OH TYR A 178 13234 13814 13152 -113 -4 1342 O ATOM 1414 N ILE A 179 20.108 53.425 32.163 1.00 83.25 N ANISOU 1414 N ILE A 179 9823 9010 12797 -1367 -540 776 N ATOM 1415 CA ILE A 179 20.769 54.431 32.993 1.00 91.02 C ANISOU 1415 CA ILE A 179 10638 9769 14176 -1622 -597 547 C ATOM 1416 C ILE A 179 20.731 53.987 34.448 1.00 81.01 C ANISOU 1416 C ILE A 179 9181 8685 12913 -1465 -747 76 C ATOM 1417 O ILE A 179 19.867 53.197 34.854 1.00 95.39 O ANISOU 1417 O ILE A 179 11076 10654 14515 -1145 -860 -55 O ATOM 1418 CB ILE A 179 20.128 55.832 32.851 1.00103.71 C ANISOU 1418 CB ILE A 179 12461 10780 16164 -1741 -696 662 C ATOM 1419 CG1 ILE A 179 18.764 55.906 33.536 1.00 95.71 C ANISOU 1419 CG1 ILE A 179 11618 9552 15196 -1430 -914 465 C ATOM 1420 CG2 ILE A 179 19.998 56.247 31.388 1.00 88.56 C ANISOU 1420 CG2 ILE A 179 10752 8680 14217 -1867 -570 1172 C ATOM 1421 CD1 ILE A 179 18.166 57.296 33.479 1.00 87.45 C ANISOU 1421 CD1 ILE A 179 10767 7904 14557 -1519 -1013 547 C ATOM 1422 N PRO A 180 21.680 54.466 35.252 1.00 83.21 N ANISOU 1422 N PRO A 180 9202 8990 13424 -1703 -752 -178 N ATOM 1423 CA PRO A 180 21.656 54.163 36.689 1.00 81.49 C ANISOU 1423 CA PRO A 180 8785 8947 13229 -1587 -907 -632 C ATOM 1424 C PRO A 180 20.368 54.640 37.345 1.00105.70 C ANISOU 1424 C PRO A 180 12038 11681 16441 -1392 -1122 -825 C ATOM 1425 O PRO A 180 19.994 55.811 37.246 1.00115.62 O ANISOU 1425 O PRO A 180 13447 12456 18025 -1519 -1176 -790 O ATOM 1426 CB PRO A 180 22.875 54.918 37.229 1.00 85.17 C ANISOU 1426 CB PRO A 180 8979 9405 13976 -1958 -862 -809 C ATOM 1427 CG PRO A 180 23.795 55.013 36.072 1.00 87.58 C ANISOU 1427 CG PRO A 180 9254 9781 14241 -2204 -641 -451 C ATOM 1428 CD PRO A 180 22.920 55.160 34.859 1.00 87.80 C ANISOU 1428 CD PRO A 180 9625 9534 14200 -2102 -600 -56 C ATOM 1429 N GLU A 181 19.699 53.716 38.027 1.00 87.09 N ANISOU 1429 N GLU A 181 9663 9589 13840 -1081 -1244 -1031 N ATOM 1430 CA GLU A 181 18.448 53.974 38.720 1.00 76.11 C ANISOU 1430 CA GLU A 181 8414 7986 12518 -857 -1451 -1242 C ATOM 1431 C GLU A 181 18.704 54.307 40.187 1.00 87.02 C ANISOU 1431 C GLU A 181 9554 9424 14084 -926 -1591 -1718 C ATOM 1432 O GLU A 181 19.772 54.024 40.736 1.00 88.55 O ANISOU 1432 O GLU A 181 9456 9929 14261 -1083 -1542 -1887 O ATOM 1433 CB GLU A 181 17.523 52.761 38.615 1.00 70.74 C ANISOU 1433 CB GLU A 181 7853 7585 11440 -496 -1509 -1186 C ATOM 1434 CG GLU A 181 18.062 51.522 39.332 1.00122.94 C ANISOU 1434 CG GLU A 181 14215 14728 17771 -388 -1511 -1389 C ATOM 1435 CD GLU A 181 17.262 50.264 39.040 1.00134.24 C ANISOU 1435 CD GLU A 181 15786 16421 18798 -69 -1534 -1277 C ATOM 1436 OE1 GLU A 181 16.307 50.336 38.238 1.00147.40 O ANISOU 1436 OE1 GLU A 181 17735 17890 20380 56 -1541 -1038 O ATOM 1437 OE2 GLU A 181 17.592 49.201 39.612 1.00120.49 O ANISOU 1437 OE2 GLU A 181 13870 15085 16824 51 -1547 -1420 O ATOM 1438 N GLY A 182 17.702 54.926 40.812 1.00 81.26 N ANISOU 1438 N GLY A 182 8941 8406 13528 -806 -1765 -1934 N ATOM 1439 CA GLY A 182 17.671 55.158 42.246 1.00 76.14 C ANISOU 1439 CA GLY A 182 8091 7836 13003 -814 -1922 -2415 C ATOM 1440 C GLY A 182 18.933 55.731 42.851 1.00 83.36 C ANISOU 1440 C GLY A 182 8724 8795 14154 -1166 -1871 -2642 C ATOM 1441 O GLY A 182 19.310 56.871 42.565 1.00116.71 O ANISOU 1441 O GLY A 182 13003 12614 18726 -1438 -1816 -2602 O ATOM 1442 N MET A 183 19.595 54.945 43.696 1.00 84.76 N ANISOU 1442 N MET A 183 8595 9470 14141 -1173 -1892 -2874 N ATOM 1443 CA MET A 183 20.849 55.352 44.315 1.00101.70 C ANISOU 1443 CA MET A 183 10428 11760 16454 -1507 -1844 -3093 C ATOM 1444 C MET A 183 22.035 55.261 43.363 1.00 98.93 C ANISOU 1444 C MET A 183 9997 11509 16083 -1742 -1629 -2771 C ATOM 1445 O MET A 183 23.182 55.306 43.821 1.00 99.10 O ANISOU 1445 O MET A 183 9714 11791 16149 -1993 -1572 -2912 O ATOM 1446 CB MET A 183 21.111 54.514 45.568 1.00121.76 C ANISOU 1446 CB MET A 183 12649 14836 18778 -1415 -1952 -3432 C ATOM 1447 CG MET A 183 20.187 54.851 46.723 1.00117.74 C ANISOU 1447 CG MET A 183 12135 14254 18347 -1294 -2164 -3839 C ATOM 1448 SD MET A 183 20.071 53.532 47.942 1.00110.15 S ANISOU 1448 SD MET A 183 10891 13955 17004 -1058 -2309 -4103 S ATOM 1449 CE MET A 183 21.695 53.599 48.695 1.00 99.77 C ANISOU 1449 CE MET A 183 9122 13035 15750 -1409 -2249 -4313 C ATOM 1450 N GLN A 184 21.780 55.122 42.061 1.00 95.61 N ANISOU 1450 N GLN A 184 9827 10922 15578 -1670 -1508 -2348 N ATOM 1451 CA GLN A 184 22.764 55.225 40.988 1.00105.93 C ANISOU 1451 CA GLN A 184 11110 12244 16895 -1909 -1297 -2007 C ATOM 1452 C GLN A 184 23.789 54.100 40.998 1.00102.22 C ANISOU 1452 C GLN A 184 10353 12358 16128 -1895 -1180 -1968 C ATOM 1453 O GLN A 184 24.792 54.188 40.280 1.00103.77 O ANISOU 1453 O GLN A 184 10448 12646 16332 -2125 -1001 -1749 O ATOM 1454 CB GLN A 184 23.499 56.572 41.020 1.00122.19 C ANISOU 1454 CB GLN A 184 13109 13962 19355 -2332 -1250 -2063 C ATOM 1455 CG GLN A 184 22.591 57.799 41.079 1.00 91.39 C ANISOU 1455 CG GLN A 184 9478 9435 15812 -2367 -1361 -2128 C ATOM 1456 CD GLN A 184 21.591 57.845 39.941 1.00 96.64 C ANISOU 1456 CD GLN A 184 10510 9780 16428 -2163 -1340 -1737 C ATOM 1457 OE1 GLN A 184 21.957 57.806 38.767 1.00103.22 O ANISOU 1457 OE1 GLN A 184 11438 10587 17194 -2265 -1182 -1332 O ATOM 1458 NE2 GLN A 184 20.317 57.921 40.287 1.00103.69 N ANISOU 1458 NE2 GLN A 184 11596 10461 17338 -1875 -1499 -1855 N ATOM 1459 N CYS A 185 23.572 53.043 41.782 1.00114.92 N ANISOU 1459 N CYS A 185 11822 14367 17476 -1629 -1275 -2164 N ATOM 1460 CA CYS A 185 24.520 51.938 41.861 1.00 99.65 C ANISOU 1460 CA CYS A 185 9610 12978 15275 -1579 -1174 -2134 C ATOM 1461 C CYS A 185 24.165 50.771 40.954 1.00 86.77 C ANISOU 1461 C CYS A 185 8142 11526 13302 -1284 -1078 -1836 C ATOM 1462 O CYS A 185 25.045 49.963 40.639 1.00 96.80 O ANISOU 1462 O CYS A 185 9229 13170 14382 -1267 -935 -1720 O ATOM 1463 CB CYS A 185 24.637 51.435 43.304 1.00 81.40 C ANISOU 1463 CB CYS A 185 7010 11035 12882 -1485 -1330 -2514 C ATOM 1464 SG CYS A 185 25.488 52.583 44.410 1.00118.01 S ANISOU 1464 SG CYS A 185 11335 15651 17852 -1887 -1396 -2889 S ATOM 1465 N SER A 186 22.907 50.662 40.536 1.00 81.53 N ANISOU 1465 N SER A 186 7808 10613 12555 -1054 -1150 -1722 N ATOM 1466 CA SER A 186 22.464 49.642 39.599 1.00 91.41 C ANISOU 1466 CA SER A 186 9255 11989 13488 -802 -1059 -1440 C ATOM 1467 C SER A 186 21.848 50.315 38.381 1.00 91.34 C ANISOU 1467 C SER A 186 9578 11570 13557 -858 -988 -1119 C ATOM 1468 O SER A 186 21.314 51.424 38.470 1.00 99.14 O ANISOU 1468 O SER A 186 10706 12143 14819 -968 -1080 -1154 O ATOM 1469 CB SER A 186 21.453 48.692 40.250 1.00 89.20 C ANISOU 1469 CB SER A 186 9055 11873 12964 -451 -1222 -1589 C ATOM 1470 OG SER A 186 20.563 49.410 41.085 1.00109.72 O ANISOU 1470 OG SER A 186 11725 14221 15741 -425 -1429 -1834 O ATOM 1471 N CYS A 187 21.923 49.637 37.241 1.00 85.98 N ANISOU 1471 N CYS A 187 9021 11014 12634 -780 -824 -805 N ATOM 1472 CA CYS A 187 21.474 50.187 35.971 1.00 79.61 C ANISOU 1472 CA CYS A 187 8497 9895 11855 -855 -732 -452 C ATOM 1473 C CYS A 187 20.199 49.500 35.502 1.00 77.85 C ANISOU 1473 C CYS A 187 8567 9650 11362 -548 -789 -319 C ATOM 1474 O CYS A 187 20.062 48.277 35.611 1.00 96.15 O ANISOU 1474 O CYS A 187 10866 12296 13372 -314 -780 -366 O ATOM 1475 CB CYS A 187 22.566 50.051 34.913 1.00 81.11 C ANISOU 1475 CB CYS A 187 8596 10256 11966 -1052 -483 -177 C ATOM 1476 SG CYS A 187 23.807 51.330 35.075 1.00108.40 S ANISOU 1476 SG CYS A 187 11819 13565 15803 -1504 -412 -209 S ATOM 1477 N GLY A 188 19.269 50.291 34.973 1.00 69.19 N ANISOU 1477 N GLY A 188 7741 8166 10383 -554 -849 -145 N ATOM 1478 CA GLY A 188 17.999 49.760 34.533 1.00 66.41 C ANISOU 1478 CA GLY A 188 7663 7787 9784 -285 -916 -14 C ATOM 1479 C GLY A 188 17.446 50.517 33.344 1.00 91.33 C ANISOU 1479 C GLY A 188 11084 10616 13003 -370 -861 358 C ATOM 1480 O GLY A 188 18.064 51.447 32.823 1.00 95.89 O ANISOU 1480 O GLY A 188 11642 10973 13819 -642 -766 533 O ATOM 1481 N ILE A 189 16.254 50.094 32.920 1.00 98.38 N ANISOU 1481 N ILE A 189 12220 11494 13667 -139 -927 489 N ATOM 1482 CA ILE A 189 15.564 50.731 31.807 1.00102.14 C ANISOU 1482 CA ILE A 189 12953 11694 14161 -177 -898 860 C ATOM 1483 C ILE A 189 15.129 52.133 32.210 1.00104.39 C ANISOU 1483 C ILE A 189 13303 11497 14863 -258 -1039 820 C ATOM 1484 O ILE A 189 14.730 52.375 33.357 1.00 99.67 O ANISOU 1484 O ILE A 189 12644 10799 14428 -150 -1215 485 O ATOM 1485 CB ILE A 189 14.370 49.864 31.369 1.00102.27 C ANISOU 1485 CB ILE A 189 13189 11863 13804 97 -948 974 C ATOM 1486 CG1 ILE A 189 14.816 48.847 30.316 1.00 98.78 C ANISOU 1486 CG1 ILE A 189 12774 11764 12993 81 -738 1197 C ATOM 1487 CG2 ILE A 189 13.202 50.718 30.873 1.00 79.96 C ANISOU 1487 CG2 ILE A 189 10611 8688 11081 155 -1053 1205 C ATOM 1488 CD1 ILE A 189 13.723 47.914 29.868 1.00 98.55 C ANISOU 1488 CD1 ILE A 189 12956 11917 12574 318 -771 1292 C ATOM 1489 N ASP A 190 15.222 53.072 31.268 1.00113.31 N ANISOU 1489 N ASP A 190 14554 12324 16174 -453 -959 1162 N ATOM 1490 CA ASP A 190 14.888 54.469 31.526 1.00101.14 C ANISOU 1490 CA ASP A 190 13093 10270 15067 -549 -1072 1166 C ATOM 1491 C ASP A 190 13.381 54.664 31.408 1.00109.54 C ANISOU 1491 C ASP A 190 14399 11130 16092 -280 -1229 1261 C ATOM 1492 O ASP A 190 12.808 54.529 30.322 1.00109.11 O ANISOU 1492 O ASP A 190 14533 11089 15836 -225 -1177 1637 O ATOM 1493 CB ASP A 190 15.639 55.380 30.560 1.00 97.42 C ANISOU 1493 CB ASP A 190 12649 9556 14811 -880 -923 1519 C ATOM 1494 CG ASP A 190 15.366 56.850 30.814 1.00109.91 C ANISOU 1494 CG ASP A 190 14324 10562 16876 -995 -1030 1532 C ATOM 1495 OD1 ASP A 190 14.872 57.182 31.912 1.00116.70 O ANISOU 1495 OD1 ASP A 190 15161 11240 17941 -860 -1201 1177 O ATOM 1496 OD2 ASP A 190 15.650 57.675 29.917 1.00 97.98 O ANISOU 1496 OD2 ASP A 190 12907 8778 15542 -1226 -941 1895 O ATOM 1497 N TYR A 191 12.738 54.984 32.536 1.00108.62 N ANISOU 1497 N TYR A 191 14263 10851 16156 -116 -1422 916 N ATOM 1498 CA TYR A 191 11.320 55.322 32.559 1.00108.61 C ANISOU 1498 CA TYR A 191 14462 10630 16175 141 -1585 966 C ATOM 1499 C TYR A 191 11.046 56.463 33.534 1.00109.73 C ANISOU 1499 C TYR A 191 14581 10342 16770 148 -1739 679 C ATOM 1500 O TYR A 191 9.913 56.605 34.008 1.00111.03 O ANISOU 1500 O TYR A 191 14835 10401 16952 407 -1905 546 O ATOM 1501 CB TYR A 191 10.460 54.099 32.920 1.00114.26 C ANISOU 1501 CB TYR A 191 15197 11744 16471 446 -1677 815 C ATOM 1502 CG TYR A 191 10.867 53.428 34.210 1.00110.52 C ANISOU 1502 CG TYR A 191 14499 11556 15939 500 -1745 347 C ATOM 1503 CD1 TYR A 191 11.846 52.447 34.222 1.00115.29 C ANISOU 1503 CD1 TYR A 191 14940 12550 16313 412 -1617 287 C ATOM 1504 CD2 TYR A 191 10.278 53.778 35.415 1.00113.08 C ANISOU 1504 CD2 TYR A 191 14762 11770 16434 643 -1937 -30 C ATOM 1505 CE1 TYR A 191 12.230 51.836 35.396 1.00122.97 C ANISOU 1505 CE1 TYR A 191 15697 13794 17233 463 -1684 -108 C ATOM 1506 CE2 TYR A 191 10.654 53.170 36.596 1.00112.39 C ANISOU 1506 CE2 TYR A 191 14454 11972 16277 677 -2004 -439 C ATOM 1507 CZ TYR A 191 11.630 52.200 36.581 1.00117.60 C ANISOU 1507 CZ TYR A 191 14956 13015 16711 587 -1881 -463 C ATOM 1508 OH TYR A 191 12.008 51.592 37.756 1.00128.08 O ANISOU 1508 OH TYR A 191 16055 14641 17968 626 -1954 -841 O ATOM 1509 N TYR A 192 12.062 57.265 33.856 1.00137.47 N ANISOU 1509 N TYR A 192 17969 13619 20643 -135 -1684 562 N ATOM 1510 CA TYR A 192 11.906 58.433 34.711 1.00154.12 C ANISOU 1510 CA TYR A 192 20066 15276 23215 -174 -1807 286 C ATOM 1511 C TYR A 192 12.463 59.689 34.051 1.00141.39 C ANISOU 1511 C TYR A 192 18541 13170 22010 -468 -1720 558 C ATOM 1512 O TYR A 192 12.578 60.727 34.713 1.00135.34 O ANISOU 1512 O TYR A 192 17757 11992 21674 -573 -1789 328 O ATOM 1513 CB TYR A 192 12.562 58.205 36.083 1.00171.82 C ANISOU 1513 CB TYR A 192 22041 17717 25525 -241 -1861 -245 C ATOM 1514 CG TYR A 192 13.754 57.273 36.069 1.00184.39 C ANISOU 1514 CG TYR A 192 23414 19779 26865 -409 -1720 -277 C ATOM 1515 CD1 TYR A 192 13.584 55.893 36.042 1.00187.92 C ANISOU 1515 CD1 TYR A 192 23813 20735 26853 -214 -1705 -283 C ATOM 1516 CD2 TYR A 192 15.046 57.772 36.103 1.00204.40 C ANISOU 1516 CD2 TYR A 192 25788 22248 29627 -761 -1603 -309 C ATOM 1517 CE1 TYR A 192 14.667 55.040 36.028 1.00197.73 C ANISOU 1517 CE1 TYR A 192 24855 22390 27884 -339 -1574 -310 C ATOM 1518 CE2 TYR A 192 16.135 56.925 36.099 1.00214.30 C ANISOU 1518 CE2 TYR A 192 26823 23950 30652 -894 -1474 -338 C ATOM 1519 CZ TYR A 192 15.940 55.560 36.056 1.00211.73 C ANISOU 1519 CZ TYR A 192 26454 24108 29884 -669 -1458 -337 C ATOM 1520 OH TYR A 192 17.019 54.708 36.044 1.00212.50 O ANISOU 1520 OH TYR A 192 26334 24637 29768 -773 -1326 -361 O ATOM 1521 N THR A 193 12.829 59.611 32.772 1.00126.87 N ANISOU 1521 N THR A 193 16793 11371 20042 -618 -1567 1036 N ATOM 1522 CA THR A 193 13.105 60.758 31.922 1.00119.03 C ANISOU 1522 CA THR A 193 15936 9912 19379 -860 -1495 1411 C ATOM 1523 C THR A 193 12.372 60.566 30.602 1.00114.72 C ANISOU 1523 C THR A 193 15604 9396 18589 -741 -1452 1944 C ATOM 1524 O THR A 193 12.254 59.434 30.114 1.00 96.89 O ANISOU 1524 O THR A 193 13333 7614 15868 -630 -1385 2062 O ATOM 1525 CB THR A 193 14.609 60.941 31.658 1.00117.18 C ANISOU 1525 CB THR A 193 15539 9744 19241 -1277 -1321 1477 C ATOM 1526 OG1 THR A 193 15.103 59.848 30.874 1.00105.51 O ANISOU 1526 OG1 THR A 193 13990 8785 17316 -1313 -1164 1701 O ATOM 1527 CG2 THR A 193 15.376 61.013 32.962 1.00126.31 C ANISOU 1527 CG2 THR A 193 16452 10960 20579 -1405 -1358 949 C ATOM 1528 N PRO A 194 11.859 61.645 30.005 1.00123.02 N ANISOU 1528 N PRO A 194 16855 9950 19939 -761 -1490 2273 N ATOM 1529 CA PRO A 194 11.079 61.508 28.769 1.00115.75 C ANISOU 1529 CA PRO A 194 16129 9070 18781 -638 -1466 2793 C ATOM 1530 C PRO A 194 11.944 61.531 27.526 1.00124.51 C ANISOU 1530 C PRO A 194 17244 10286 19778 -959 -1270 3260 C ATOM 1531 O PRO A 194 11.458 61.814 26.429 1.00137.60 O ANISOU 1531 O PRO A 194 19069 11846 21367 -955 -1243 3754 O ATOM 1532 CB PRO A 194 10.165 62.733 28.813 1.00121.08 C ANISOU 1532 CB PRO A 194 16994 9137 19875 -503 -1608 2914 C ATOM 1533 CG PRO A 194 11.038 63.768 29.452 1.00120.17 C ANISOU 1533 CG PRO A 194 16808 8578 20273 -782 -1599 2688 C ATOM 1534 CD PRO A 194 11.877 63.039 30.483 1.00124.32 C ANISOU 1534 CD PRO A 194 17081 9480 20677 -870 -1570 2170 C ATOM 1535 N HIS A 195 13.232 61.268 27.706 1.00134.51 N ANISOU 1535 N HIS A 195 18315 11764 21029 -1245 -1135 3108 N ATOM 1536 CA HIS A 195 14.226 61.240 26.639 1.00145.81 C ANISOU 1536 CA HIS A 195 19700 13359 22344 -1582 -934 3486 C ATOM 1537 C HIS A 195 13.752 60.922 25.230 1.00137.17 C ANISOU 1537 C HIS A 195 18753 12451 20913 -1550 -850 4028 C ATOM 1538 O HIS A 195 13.898 59.784 24.781 1.00100.93 O ANISOU 1538 O HIS A 195 14101 8390 15859 -1498 -742 4064 O ATOM 1539 CB HIS A 195 15.270 60.198 26.958 1.00136.03 C ANISOU 1539 CB HIS A 195 18213 12652 20820 -1687 -804 3215 C ATOM 1540 CG HIS A 195 16.594 60.497 26.354 1.00139.03 C ANISOU 1540 CG HIS A 195 18466 13095 21263 -2101 -616 3421 C ATOM 1541 ND1 HIS A 195 17.154 59.740 25.348 1.00139.37 N ANISOU 1541 ND1 HIS A 195 18446 13589 20917 -2219 -426 3697 N ATOM 1542 CD2 HIS A 195 17.471 61.490 26.617 1.00131.03 C ANISOU 1542 CD2 HIS A 195 17373 11758 20655 -2439 -586 3384 C ATOM 1543 CE1 HIS A 195 18.332 60.246 25.032 1.00140.39 C ANISOU 1543 CE1 HIS A 195 18446 13692 21202 -2606 -288 3823 C ATOM 1544 NE2 HIS A 195 18.547 61.308 25.787 1.00134.12 N ANISOU 1544 NE2 HIS A 195 17642 12429 20888 -2755 -384 3643 N ATOM 1545 N GLU A 196 13.301 61.932 24.491 1.00148.81 N ANISOU 1545 N GLU A 196 20413 13506 22622 -1617 -883 4462 N ATOM 1546 CA GLU A 196 12.757 61.726 23.152 1.00138.56 C ANISOU 1546 CA GLU A 196 19257 12377 21013 -1588 -822 5004 C ATOM 1547 C GLU A 196 13.746 61.163 22.117 1.00130.67 C ANISOU 1547 C GLU A 196 18154 11819 19676 -1884 -592 5286 C ATOM 1548 O GLU A 196 13.298 60.587 21.119 1.00136.79 O ANISOU 1548 O GLU A 196 19006 12919 20051 -1819 -527 5618 O ATOM 1549 CB GLU A 196 12.191 63.049 22.656 1.00150.21 C ANISOU 1549 CB GLU A 196 20930 13268 22875 -1626 -909 5416 C ATOM 1550 CG GLU A 196 10.816 63.334 23.208 1.00153.50 C ANISOU 1550 CG GLU A 196 21494 13398 23432 -1229 -1122 5300 C ATOM 1551 CD GLU A 196 10.832 64.121 24.505 1.00152.73 C ANISOU 1551 CD GLU A 196 21374 12813 23846 -1174 -1255 4847 C ATOM 1552 OE1 GLU A 196 11.929 64.492 24.977 1.00163.96 O ANISOU 1552 OE1 GLU A 196 22670 14100 25527 -1468 -1186 4631 O ATOM 1553 OE2 GLU A 196 9.733 64.377 25.045 1.00131.06 O ANISOU 1553 OE2 GLU A 196 18728 9833 21234 -840 -1428 4702 O ATOM 1554 N GLU A 197 15.062 61.344 22.281 1.00129.17 N ANISOU 1554 N GLU A 197 17787 11664 19628 -2218 -465 5176 N ATOM 1555 CA GLU A 197 15.985 60.857 21.249 1.00131.48 C ANISOU 1555 CA GLU A 197 17971 12385 19599 -2496 -241 5459 C ATOM 1556 C GLU A 197 15.946 59.338 21.097 1.00127.46 C ANISOU 1556 C GLU A 197 17375 12518 18535 -2304 -147 5290 C ATOM 1557 O GLU A 197 16.330 58.814 20.043 1.00132.70 O ANISOU 1557 O GLU A 197 18005 13571 18843 -2443 28 5578 O ATOM 1558 CB GLU A 197 17.422 61.301 21.539 1.00137.58 C ANISOU 1558 CB GLU A 197 18542 13112 20620 -2882 -125 5336 C ATOM 1559 CG GLU A 197 17.627 62.805 21.559 1.00147.78 C ANISOU 1559 CG GLU A 197 19920 13775 22453 -3149 -185 5537 C ATOM 1560 CD GLU A 197 17.728 63.357 22.966 1.00157.44 C ANISOU 1560 CD GLU A 197 21093 14612 24116 -3112 -324 5041 C ATOM 1561 OE1 GLU A 197 16.690 63.427 23.659 1.00147.09 O ANISOU 1561 OE1 GLU A 197 19901 13063 22922 -2774 -503 4818 O ATOM 1562 OE2 GLU A 197 18.852 63.711 23.383 1.00170.65 O ANISOU 1562 OE2 GLU A 197 22594 16246 26000 -3428 -252 4864 O ATOM 1563 N THR A 198 15.489 58.623 22.124 1.00120.40 N ANISOU 1563 N THR A 198 16446 11740 17560 -1996 -257 4830 N ATOM 1564 CA THR A 198 15.373 57.174 22.084 1.00127.25 C ANISOU 1564 CA THR A 198 17253 13163 17932 -1791 -187 4645 C ATOM 1565 C THR A 198 13.937 56.682 22.226 1.00134.46 C ANISOU 1565 C THR A 198 18342 14110 18636 -1410 -343 4600 C ATOM 1566 O THR A 198 13.719 55.464 22.272 1.00126.41 O ANISOU 1566 O THR A 198 17298 13517 17216 -1223 -307 4425 O ATOM 1567 CB THR A 198 16.247 56.544 23.177 1.00111.55 C ANISOU 1567 CB THR A 198 15029 11390 15963 -1781 -159 4132 C ATOM 1568 OG1 THR A 198 15.831 57.022 24.462 1.00119.83 O ANISOU 1568 OG1 THR A 198 16077 12099 17356 -1630 -360 3763 O ATOM 1569 CG2 THR A 198 17.702 56.910 22.961 1.00102.29 C ANISOU 1569 CG2 THR A 198 13657 10277 14932 -2163 12 4187 C ATOM 1570 N ASN A 199 12.958 57.588 22.302 1.00119.21 N ANISOU 1570 N ASN A 199 16583 11742 16967 -1291 -513 4753 N ATOM 1571 CA ASN A 199 11.532 57.251 22.313 1.00108.56 C ANISOU 1571 CA ASN A 199 15401 10423 15422 -946 -663 4780 C ATOM 1572 C ASN A 199 11.174 56.375 23.516 1.00105.04 C ANISOU 1572 C ASN A 199 14883 10167 14859 -662 -773 4247 C ATOM 1573 O ASN A 199 10.705 55.243 23.384 1.00102.45 O ANISOU 1573 O ASN A 199 14580 10247 14101 -479 -758 4171 O ATOM 1574 CB ASN A 199 11.121 56.580 20.997 1.00 99.49 C ANISOU 1574 CB ASN A 199 14352 9662 13788 -943 -552 5180 C ATOM 1575 CG ASN A 199 11.546 57.378 19.783 1.00119.76 C ANISOU 1575 CG ASN A 199 16966 12109 16429 -1248 -433 5721 C ATOM 1576 OD1 ASN A 199 12.581 57.102 19.178 1.00126.25 O ANISOU 1576 OD1 ASN A 199 17673 13192 17103 -1517 -236 5831 O ATOM 1577 ND2 ASN A 199 10.751 58.379 19.425 1.00133.22 N ANISOU 1577 ND2 ASN A 199 18830 13423 18364 -1206 -554 6070 N ATOM 1578 N ASN A 200 11.389 56.936 24.707 1.00115.95 N ANISOU 1578 N ASN A 200 16178 11242 16635 -641 -888 3878 N ATOM 1579 CA ASN A 200 11.133 56.192 25.936 1.00114.24 C ANISOU 1579 CA ASN A 200 15868 11202 16338 -402 -999 3366 C ATOM 1580 C ASN A 200 9.650 55.908 26.132 1.00117.25 C ANISOU 1580 C ASN A 200 16399 11603 16549 -52 -1174 3336 C ATOM 1581 O ASN A 200 9.290 54.847 26.656 1.00122.50 O ANISOU 1581 O ASN A 200 17024 12611 16908 150 -1219 3059 O ATOM 1582 CB ASN A 200 11.685 56.962 27.136 1.00114.82 C ANISOU 1582 CB ASN A 200 15807 10943 16876 -486 -1084 2989 C ATOM 1583 CG ASN A 200 13.197 57.026 27.138 1.00110.29 C ANISOU 1583 CG ASN A 200 15038 10455 16412 -820 -918 2929 C ATOM 1584 OD1 ASN A 200 13.848 56.626 26.174 1.00 92.05 O ANISOU 1584 OD1 ASN A 200 12698 8410 13868 -999 -734 3204 O ATOM 1585 ND2 ASN A 200 13.765 57.534 28.224 1.00124.27 N ANISOU 1585 ND2 ASN A 200 16662 12027 18528 -913 -979 2562 N ATOM 1586 N GLU A 201 8.783 56.828 25.710 1.00122.37 N ANISOU 1586 N GLU A 201 17214 11895 17385 23 -1272 3631 N ATOM 1587 CA GLU A 201 7.357 56.691 25.987 1.00121.36 C ANISOU 1587 CA GLU A 201 17208 11764 17141 363 -1453 3586 C ATOM 1588 C GLU A 201 6.770 55.471 25.297 1.00123.15 C ANISOU 1588 C GLU A 201 17503 12497 16792 489 -1405 3732 C ATOM 1589 O GLU A 201 6.069 54.664 25.922 1.00126.84 O ANISOU 1589 O GLU A 201 17965 13213 17016 730 -1509 3457 O ATOM 1590 CB GLU A 201 6.619 57.962 25.571 1.00126.04 C ANISOU 1590 CB GLU A 201 17955 11871 18063 415 -1553 3922 C ATOM 1591 CG GLU A 201 5.141 57.964 25.912 1.00132.94 C ANISOU 1591 CG GLU A 201 18933 12711 18867 778 -1748 3871 C ATOM 1592 CD GLU A 201 4.416 59.140 25.299 1.00154.02 C ANISOU 1592 CD GLU A 201 21759 14944 21819 842 -1827 4283 C ATOM 1593 OE1 GLU A 201 5.078 60.159 25.009 1.00161.19 O ANISOU 1593 OE1 GLU A 201 22686 15437 23121 619 -1770 4481 O ATOM 1594 OE2 GLU A 201 3.189 59.040 25.095 1.00161.50 O ANISOU 1594 OE2 GLU A 201 22798 15996 22570 1111 -1925 4396 O ATOM 1595 N SER A 202 7.043 55.323 24.001 1.00112.93 N ANISOU 1595 N SER A 202 16271 11369 15266 313 -1247 4164 N ATOM 1596 CA SER A 202 6.538 54.169 23.270 1.00 95.35 C ANISOU 1596 CA SER A 202 14115 9630 12484 396 -1182 4300 C ATOM 1597 C SER A 202 7.099 52.868 23.826 1.00 95.96 C ANISOU 1597 C SER A 202 14072 10114 12275 421 -1107 3908 C ATOM 1598 O SER A 202 6.408 51.844 23.823 1.00109.75 O ANISOU 1598 O SER A 202 15874 12203 13622 597 -1138 3817 O ATOM 1599 CB SER A 202 6.876 54.304 21.786 1.00 93.62 C ANISOU 1599 CB SER A 202 13961 9525 12085 161 -1009 4814 C ATOM 1600 OG SER A 202 8.256 54.084 21.560 1.00111.98 O ANISOU 1600 OG SER A 202 16153 11978 14418 -114 -810 4776 O ATOM 1601 N PHE A 203 8.341 52.887 24.316 1.00 93.65 N ANISOU 1601 N PHE A 203 13610 9791 12180 247 -1010 3680 N ATOM 1602 CA PHE A 203 8.922 51.666 24.864 1.00 98.40 C ANISOU 1602 CA PHE A 203 14083 10769 12535 285 -939 3324 C ATOM 1603 C PHE A 203 8.285 51.301 26.196 1.00 89.63 C ANISOU 1603 C PHE A 203 12934 9666 11455 546 -1134 2892 C ATOM 1604 O PHE A 203 8.050 50.123 26.480 1.00 87.34 O ANISOU 1604 O PHE A 203 12635 9727 10822 688 -1139 2691 O ATOM 1605 CB PHE A 203 10.433 51.814 25.028 1.00 91.04 C ANISOU 1605 CB PHE A 203 12958 9830 11805 31 -786 3215 C ATOM 1606 CG PHE A 203 11.116 50.538 25.422 1.00 90.79 C ANISOU 1606 CG PHE A 203 12786 10205 11505 68 -687 2914 C ATOM 1607 CD1 PHE A 203 11.284 50.207 26.756 1.00 91.29 C ANISOU 1607 CD1 PHE A 203 12709 10293 11683 194 -797 2470 C ATOM 1608 CD2 PHE A 203 11.570 49.656 24.457 1.00 97.40 C ANISOU 1608 CD2 PHE A 203 13630 11407 11972 -16 -483 3078 C ATOM 1609 CE1 PHE A 203 11.904 49.029 27.118 1.00 89.33 C ANISOU 1609 CE1 PHE A 203 12332 10410 11199 243 -711 2222 C ATOM 1610 CE2 PHE A 203 12.191 48.476 24.813 1.00 89.37 C ANISOU 1610 CE2 PHE A 203 12490 10738 10728 42 -388 2805 C ATOM 1611 CZ PHE A 203 12.359 48.162 26.145 1.00 84.36 C ANISOU 1611 CZ PHE A 203 11719 10108 10224 176 -506 2390 C ATOM 1612 N VAL A 204 8.015 52.297 27.030 1.00 89.15 N ANISOU 1612 N VAL A 204 12848 9223 11803 602 -1294 2738 N ATOM 1613 CA VAL A 204 7.366 52.036 28.302 1.00 94.78 C ANISOU 1613 CA VAL A 204 13512 9952 12548 842 -1485 2329 C ATOM 1614 C VAL A 204 5.949 51.509 28.086 1.00105.54 C ANISOU 1614 C VAL A 204 15033 11493 13575 1098 -1604 2417 C ATOM 1615 O VAL A 204 5.492 50.597 28.789 1.00 97.58 O ANISOU 1615 O VAL A 204 13995 10756 12323 1275 -1692 2134 O ATOM 1616 CB VAL A 204 7.395 53.325 29.128 1.00106.21 C ANISOU 1616 CB VAL A 204 14905 10931 14521 827 -1612 2160 C ATOM 1617 CG1 VAL A 204 6.509 53.198 30.216 1.00115.04 C ANISOU 1617 CG1 VAL A 204 16004 12057 15650 1083 -1812 1820 C ATOM 1618 CG2 VAL A 204 8.806 53.614 29.618 1.00108.00 C ANISOU 1618 CG2 VAL A 204 14936 11074 15024 580 -1514 1958 C ATOM 1619 N ILE A 205 5.238 52.064 27.103 1.00113.46 N ANISOU 1619 N ILE A 205 16199 12363 14547 1110 -1609 2825 N ATOM 1620 CA ILE A 205 3.923 51.535 26.749 1.00109.82 C ANISOU 1620 CA ILE A 205 15880 12123 13722 1323 -1704 2956 C ATOM 1621 C ILE A 205 4.042 50.096 26.264 1.00109.02 C ANISOU 1621 C ILE A 205 15805 12515 13101 1302 -1581 2956 C ATOM 1622 O ILE A 205 3.254 49.226 26.655 1.00103.81 O ANISOU 1622 O ILE A 205 15183 12127 12134 1485 -1676 2784 O ATOM 1623 CB ILE A 205 3.251 52.437 25.696 1.00 97.65 C ANISOU 1623 CB ILE A 205 14490 10365 12248 1315 -1717 3440 C ATOM 1624 CG1 ILE A 205 2.796 53.751 26.334 1.00 94.02 C ANISOU 1624 CG1 ILE A 205 14032 9413 12280 1430 -1883 3388 C ATOM 1625 CG2 ILE A 205 2.075 51.720 25.054 1.00 90.70 C ANISOU 1625 CG2 ILE A 205 13685 9871 10905 1462 -1700 3587 C ATOM 1626 CD1 ILE A 205 2.646 54.887 25.350 1.00 78.74 C ANISOU 1626 CD1 ILE A 205 12206 7135 10576 1342 -1858 3875 C ATOM 1627 N TYR A 206 5.039 49.818 25.421 1.00 97.89 N ANISOU 1627 N TYR A 206 14373 11229 11590 1074 -1366 3137 N ATOM 1628 CA TYR A 206 5.212 48.470 24.887 1.00 76.48 C ANISOU 1628 CA TYR A 206 11694 8963 8402 1048 -1226 3133 C ATOM 1629 C TYR A 206 5.605 47.480 25.976 1.00 89.31 C ANISOU 1629 C TYR A 206 13199 10788 9946 1144 -1251 2681 C ATOM 1630 O TYR A 206 5.238 46.302 25.904 1.00 92.13 O ANISOU 1630 O TYR A 206 13618 11481 9907 1235 -1232 2591 O ATOM 1631 CB TYR A 206 6.244 48.503 23.759 1.00 69.42 C ANISOU 1631 CB TYR A 206 10782 8144 7452 782 -984 3416 C ATOM 1632 CG TYR A 206 7.062 47.245 23.592 1.00109.40 C ANISOU 1632 CG TYR A 206 15781 13578 12209 718 -801 3255 C ATOM 1633 CD1 TYR A 206 6.572 46.160 22.878 1.00110.93 C ANISOU 1633 CD1 TYR A 206 16098 14135 11915 760 -722 3336 C ATOM 1634 CD2 TYR A 206 8.340 47.154 24.129 1.00121.17 C ANISOU 1634 CD2 TYR A 206 17084 15054 13902 611 -703 3025 C ATOM 1635 CE1 TYR A 206 7.327 45.014 22.717 1.00110.73 C ANISOU 1635 CE1 TYR A 206 16024 14417 11632 716 -548 3179 C ATOM 1636 CE2 TYR A 206 9.100 46.014 23.975 1.00115.25 C ANISOU 1636 CE2 TYR A 206 16266 14633 12890 579 -533 2885 C ATOM 1637 CZ TYR A 206 8.590 44.948 23.267 1.00108.91 C ANISOU 1637 CZ TYR A 206 15602 14156 11625 639 -454 2959 C ATOM 1638 OH TYR A 206 9.346 43.811 23.111 1.00105.74 O ANISOU 1638 OH TYR A 206 15142 14053 10982 623 -278 2806 O ATOM 1639 N MET A 207 6.348 47.938 26.986 1.00101.93 N ANISOU 1639 N MET A 207 14627 12188 11913 1115 -1295 2400 N ATOM 1640 CA MET A 207 6.610 47.119 28.165 1.00104.94 C ANISOU 1640 CA MET A 207 14878 12743 12251 1226 -1360 1974 C ATOM 1641 C MET A 207 5.315 46.778 28.886 1.00109.53 C ANISOU 1641 C MET A 207 15531 13407 12681 1474 -1576 1799 C ATOM 1642 O MET A 207 4.975 45.604 29.069 1.00103.10 O ANISOU 1642 O MET A 207 14752 12908 11513 1581 -1589 1668 O ATOM 1643 CB MET A 207 7.552 47.859 29.113 1.00108.78 C ANISOU 1643 CB MET A 207 15160 12991 13179 1133 -1386 1726 C ATOM 1644 CG MET A 207 8.962 47.967 28.614 1.00119.02 C ANISOU 1644 CG MET A 207 16338 14296 14589 887 -1173 1819 C ATOM 1645 SD MET A 207 9.715 46.343 28.555 1.00121.76 S ANISOU 1645 SD MET A 207 16603 15108 14552 906 -1011 1670 S ATOM 1646 CE MET A 207 10.012 46.055 30.298 1.00113.59 C ANISOU 1646 CE MET A 207 15353 14116 13692 1028 -1170 1173 C ATOM 1647 N PHE A 208 4.585 47.811 29.311 1.00102.10 N ANISOU 1647 N PHE A 208 14608 12175 12010 1567 -1746 1791 N ATOM 1648 CA PHE A 208 3.385 47.604 30.109 1.00 87.13 C ANISOU 1648 CA PHE A 208 12743 10355 10006 1805 -1960 1594 C ATOM 1649 C PHE A 208 2.379 46.727 29.377 1.00 98.21 C ANISOU 1649 C PHE A 208 14159 12114 11041 1759 -1835 1707 C ATOM 1650 O PHE A 208 1.756 45.850 29.984 1.00112.33 O ANISOU 1650 O PHE A 208 15797 14166 12716 1726 -1790 1420 O ATOM 1651 CB PHE A 208 2.769 48.955 30.468 1.00 96.65 C ANISOU 1651 CB PHE A 208 13954 11177 11592 1889 -2113 1606 C ATOM 1652 CG PHE A 208 1.657 48.873 31.471 1.00105.05 C ANISOU 1652 CG PHE A 208 14978 12320 12617 2109 -2311 1328 C ATOM 1653 CD1 PHE A 208 1.923 48.967 32.828 1.00107.69 C ANISOU 1653 CD1 PHE A 208 15160 12603 13153 2185 -2449 912 C ATOM 1654 CD2 PHE A 208 0.343 48.717 31.057 1.00 96.63 C ANISOU 1654 CD2 PHE A 208 13862 11471 11381 2073 -2197 1410 C ATOM 1655 CE1 PHE A 208 0.899 48.899 33.754 1.00112.38 C ANISOU 1655 CE1 PHE A 208 15651 13333 13714 2282 -2523 624 C ATOM 1656 CE2 PHE A 208 -0.683 48.647 31.977 1.00 98.86 C ANISOU 1656 CE2 PHE A 208 14024 11875 11664 2140 -2246 1121 C ATOM 1657 CZ PHE A 208 -0.406 48.738 33.328 1.00111.17 C ANISOU 1657 CZ PHE A 208 15499 13368 13373 2242 -2397 733 C ATOM 1658 N VAL A 209 2.229 46.924 28.069 1.00 89.98 N ANISOU 1658 N VAL A 209 13188 11091 9910 1629 -1703 2075 N ATOM 1659 CA VAL A 209 1.231 46.172 27.313 1.00 91.68 C ANISOU 1659 CA VAL A 209 13283 11632 9920 1454 -1567 2118 C ATOM 1660 C VAL A 209 1.718 44.752 27.022 1.00 97.51 C ANISOU 1660 C VAL A 209 13966 12664 10420 1284 -1411 1976 C ATOM 1661 O VAL A 209 1.055 43.773 27.383 1.00104.82 O ANISOU 1661 O VAL A 209 14765 13779 11284 1194 -1366 1725 O ATOM 1662 CB VAL A 209 0.850 46.923 26.022 1.00 92.66 C ANISOU 1662 CB VAL A 209 13456 11687 10064 1352 -1527 2542 C ATOM 1663 CG1 VAL A 209 -0.099 46.085 25.186 1.00 80.53 C ANISOU 1663 CG1 VAL A 209 11809 10461 8328 1113 -1458 2551 C ATOM 1664 CG2 VAL A 209 0.214 48.273 26.355 1.00 86.09 C ANISOU 1664 CG2 VAL A 209 12656 10539 9517 1532 -1664 2662 C ATOM 1665 N VAL A 210 2.892 44.616 26.389 1.00 94.06 N ANISOU 1665 N VAL A 210 13632 12227 9879 1228 -1310 2134 N ATOM 1666 CA VAL A 210 3.343 43.314 25.876 1.00 72.69 C ANISOU 1666 CA VAL A 210 10890 9773 6957 1056 -1144 2025 C ATOM 1667 C VAL A 210 4.020 42.469 26.946 1.00 82.67 C ANISOU 1667 C VAL A 210 12089 11112 8210 1158 -1132 1696 C ATOM 1668 O VAL A 210 3.926 41.236 26.929 1.00 86.04 O ANISOU 1668 O VAL A 210 12432 11704 8557 1040 -1030 1497 O ATOM 1669 CB VAL A 210 4.305 43.492 24.693 1.00 72.30 C ANISOU 1669 CB VAL A 210 10971 9728 6774 937 -1001 2323 C ATOM 1670 CG1 VAL A 210 4.995 42.165 24.387 1.00 62.74 C ANISOU 1670 CG1 VAL A 210 9734 8736 5367 828 -832 2142 C ATOM 1671 CG2 VAL A 210 3.588 43.999 23.486 1.00 70.97 C ANISOU 1671 CG2 VAL A 210 10860 9532 6574 750 -1008 2597 C ATOM 1672 N HIS A 211 4.814 43.089 27.814 1.00 92.19 N ANISOU 1672 N HIS A 211 13341 12169 9517 1362 -1243 1650 N ATOM 1673 CA HIS A 211 5.594 42.343 28.791 1.00 85.71 C ANISOU 1673 CA HIS A 211 12434 11452 8680 1454 -1253 1354 C ATOM 1674 C HIS A 211 5.032 42.506 30.191 1.00 85.54 C ANISOU 1674 C HIS A 211 12290 11366 8846 1567 -1433 1048 C ATOM 1675 O HIS A 211 5.750 42.305 31.175 1.00 81.67 O ANISOU 1675 O HIS A 211 11711 10907 8414 1671 -1516 817 O ATOM 1676 CB HIS A 211 7.067 42.756 28.753 1.00 84.83 C ANISOU 1676 CB HIS A 211 12310 11268 8652 1465 -1190 1428 C ATOM 1677 CG HIS A 211 7.752 42.455 27.454 1.00 87.50 C ANISOU 1677 CG HIS A 211 12704 11723 8819 1305 -936 1682 C ATOM 1678 ND1 HIS A 211 8.515 41.325 27.254 1.00 81.13 N ANISOU 1678 ND1 HIS A 211 11859 11170 7798 1294 -766 1588 N ATOM 1679 CD2 HIS A 211 7.795 43.147 26.291 1.00 97.10 C ANISOU 1679 CD2 HIS A 211 14001 12847 10047 1150 -821 2028 C ATOM 1680 CE1 HIS A 211 8.991 41.330 26.021 1.00 90.56 C ANISOU 1680 CE1 HIS A 211 13105 12435 8869 1138 -551 1843 C ATOM 1681 NE2 HIS A 211 8.570 42.425 25.416 1.00 93.85 N ANISOU 1681 NE2 HIS A 211 13592 12656 9411 1038 -582 2121 N ATOM 1682 N PHE A 212 3.761 42.886 30.299 1.00 92.51 N ANISOU 1682 N PHE A 212 13142 12185 9822 1538 -1484 1039 N ATOM 1683 CA PHE A 212 3.102 42.883 31.595 1.00 98.61 C ANISOU 1683 CA PHE A 212 13787 12942 10739 1600 -1580 738 C ATOM 1684 C PHE A 212 1.634 42.491 31.482 1.00114.31 C ANISOU 1684 C PHE A 212 15703 15007 12722 1467 -1488 716 C ATOM 1685 O PHE A 212 1.194 41.556 32.158 1.00127.94 O ANISOU 1685 O PHE A 212 17310 16826 14477 1378 -1397 513 O ATOM 1686 CB PHE A 212 3.231 44.240 32.282 1.00 86.79 C ANISOU 1686 CB PHE A 212 12329 11190 9458 1795 -1834 699 C ATOM 1687 CG PHE A 212 2.557 44.288 33.616 1.00 92.06 C ANISOU 1687 CG PHE A 212 12858 11864 10257 1843 -1917 368 C ATOM 1688 CD1 PHE A 212 2.929 43.408 34.620 1.00 80.54 C ANISOU 1688 CD1 PHE A 212 11251 10556 8795 1802 -1853 85 C ATOM 1689 CD2 PHE A 212 1.538 45.192 33.864 1.00104.57 C ANISOU 1689 CD2 PHE A 212 14460 13300 11970 1919 -2026 358 C ATOM 1690 CE1 PHE A 212 2.303 43.435 35.853 1.00 88.92 C ANISOU 1690 CE1 PHE A 212 12195 11619 9970 1817 -1879 -182 C ATOM 1691 CE2 PHE A 212 0.907 45.224 35.096 1.00101.95 C ANISOU 1691 CE2 PHE A 212 14015 12993 11730 1955 -2074 52 C ATOM 1692 CZ PHE A 212 1.291 44.345 36.092 1.00 85.81 C ANISOU 1692 CZ PHE A 212 11834 11099 9672 1894 -1989 -210 C ATOM 1693 N ILE A 213 0.862 43.187 30.644 1.00107.81 N ANISOU 1693 N ILE A 213 14942 14131 11890 1445 -1510 952 N ATOM 1694 CA ILE A 213 -0.561 42.874 30.529 1.00101.19 C ANISOU 1694 CA ILE A 213 14016 13382 11049 1321 -1451 937 C ATOM 1695 C ILE A 213 -0.755 41.504 29.888 1.00 97.54 C ANISOU 1695 C ILE A 213 13600 13057 10404 1238 -1296 877 C ATOM 1696 O ILE A 213 -1.495 40.660 30.408 1.00 93.69 O ANISOU 1696 O ILE A 213 13101 12609 9889 1301 -1241 662 O ATOM 1697 CB ILE A 213 -1.303 43.972 29.745 1.00 99.99 C ANISOU 1697 CB ILE A 213 13924 13146 10920 1359 -1529 1209 C ATOM 1698 CG1 ILE A 213 -1.271 45.300 30.504 1.00 94.72 C ANISOU 1698 CG1 ILE A 213 13320 12236 10435 1608 -1716 1179 C ATOM 1699 CG2 ILE A 213 -2.745 43.561 29.495 1.00 86.80 C ANISOU 1699 CG2 ILE A 213 12257 11574 9149 1333 -1488 1160 C ATOM 1700 CD1 ILE A 213 -1.956 45.255 31.849 1.00 92.44 C ANISOU 1700 CD1 ILE A 213 12939 11956 10230 1684 -1773 851 C ATOM 1701 N ILE A 214 -0.100 41.265 28.747 1.00 97.66 N ANISOU 1701 N ILE A 214 13663 13131 10313 1105 -1223 1077 N ATOM 1702 CA ILE A 214 -0.191 39.958 28.092 1.00 93.35 C ANISOU 1702 CA ILE A 214 13159 12697 9614 1038 -1082 1012 C ATOM 1703 C ILE A 214 0.179 38.817 29.041 1.00100.18 C ANISOU 1703 C ILE A 214 13972 13575 10516 1122 -1015 734 C ATOM 1704 O ILE A 214 -0.622 37.885 29.188 1.00101.87 O ANISOU 1704 O ILE A 214 14178 13820 10708 1164 -958 604 O ATOM 1705 CB ILE A 214 0.634 39.950 26.800 1.00 80.24 C ANISOU 1705 CB ILE A 214 11562 11092 7833 878 -1015 1244 C ATOM 1706 CG1 ILE A 214 0.186 41.067 25.851 1.00 70.84 C ANISOU 1706 CG1 ILE A 214 10418 9871 6628 790 -1087 1556 C ATOM 1707 CG2 ILE A 214 0.574 38.585 26.127 1.00 65.67 C ANISOU 1707 CG2 ILE A 214 9758 9354 5842 819 -876 1157 C ATOM 1708 CD1 ILE A 214 -1.285 41.087 25.575 1.00 79.72 C ANISOU 1708 CD1 ILE A 214 11557 11029 7705 814 -1116 1561 C ATOM 1709 N PRO A 215 1.341 38.826 29.711 1.00103.42 N ANISOU 1709 N PRO A 215 14335 13962 10996 1147 -1027 658 N ATOM 1710 CA PRO A 215 1.628 37.737 30.660 1.00103.10 C ANISOU 1710 CA PRO A 215 14231 13933 11011 1240 -970 416 C ATOM 1711 C PRO A 215 0.588 37.607 31.756 1.00 95.86 C ANISOU 1711 C PRO A 215 13259 12969 10193 1362 -1008 227 C ATOM 1712 O PRO A 215 0.199 36.488 32.109 1.00 99.90 O ANISOU 1712 O PRO A 215 13740 13498 10718 1419 -939 106 O ATOM 1713 CB PRO A 215 3.001 38.128 31.227 1.00102.80 C ANISOU 1713 CB PRO A 215 14134 13889 11035 1239 -1017 396 C ATOM 1714 CG PRO A 215 3.606 38.993 30.191 1.00101.08 C ANISOU 1714 CG PRO A 215 13984 13680 10742 1132 -1044 659 C ATOM 1715 CD PRO A 215 2.465 39.779 29.639 1.00101.61 C ANISOU 1715 CD PRO A 215 14092 13702 10812 1092 -1100 813 C ATOM 1716 N LEU A 216 0.127 38.733 32.303 1.00 91.74 N ANISOU 1716 N LEU A 216 12724 12385 9749 1405 -1123 213 N ATOM 1717 CA LEU A 216 -0.874 38.700 33.364 1.00 90.92 C ANISOU 1717 CA LEU A 216 12573 12246 9727 1521 -1153 29 C ATOM 1718 C LEU A 216 -2.134 37.981 32.903 1.00 90.71 C ANISOU 1718 C LEU A 216 12575 12264 9627 1526 -1086 44 C ATOM 1719 O LEU A 216 -2.657 37.104 33.602 1.00 99.20 O ANISOU 1719 O LEU A 216 13595 13354 10743 1599 -1039 -93 O ATOM 1720 CB LEU A 216 -1.189 40.129 33.806 1.00101.57 C ANISOU 1720 CB LEU A 216 13920 13518 11155 1561 -1295 33 C ATOM 1721 CG LEU A 216 -1.959 40.377 35.099 1.00101.68 C ANISOU 1721 CG LEU A 216 13876 13488 11268 1688 -1349 -188 C ATOM 1722 CD1 LEU A 216 -1.436 39.487 36.207 1.00 96.30 C ANISOU 1722 CD1 LEU A 216 13098 12831 10659 1749 -1291 -389 C ATOM 1723 CD2 LEU A 216 -1.824 41.841 35.483 1.00102.84 C ANISOU 1723 CD2 LEU A 216 14015 13541 11519 1715 -1512 -182 C ATOM 1724 N ILE A 217 -2.624 38.328 31.711 1.00 89.48 N ANISOU 1724 N ILE A 217 12492 12143 9364 1440 -1087 234 N ATOM 1725 CA ILE A 217 -3.843 37.716 31.193 1.00 84.83 C ANISOU 1725 CA ILE A 217 11920 11618 8694 1422 -1042 263 C ATOM 1726 C ILE A 217 -3.624 36.236 30.903 1.00 85.04 C ANISOU 1726 C ILE A 217 11939 11694 8678 1383 -937 225 C ATOM 1727 O ILE A 217 -4.480 35.399 31.214 1.00100.82 O ANISOU 1727 O ILE A 217 13904 13721 10682 1416 -908 148 O ATOM 1728 CB ILE A 217 -4.328 38.475 29.943 1.00 79.69 C ANISOU 1728 CB ILE A 217 11338 11007 7932 1326 -1076 494 C ATOM 1729 CG1 ILE A 217 -4.777 39.888 30.316 1.00 86.93 C ANISOU 1729 CG1 ILE A 217 12255 11860 8914 1393 -1199 542 C ATOM 1730 CG2 ILE A 217 -5.461 37.729 29.265 1.00 76.06 C ANISOU 1730 CG2 ILE A 217 10891 10642 7365 1275 -1029 535 C ATOM 1731 CD1 ILE A 217 -5.095 40.757 29.120 1.00 84.27 C ANISOU 1731 CD1 ILE A 217 11972 11546 8501 1308 -1250 823 C ATOM 1732 N VAL A 218 -2.480 35.886 30.310 1.00 75.66 N ANISOU 1732 N VAL A 218 10782 10521 7447 1313 -885 287 N ATOM 1733 CA VAL A 218 -2.216 34.488 29.974 1.00 74.36 C ANISOU 1733 CA VAL A 218 10621 10393 7238 1282 -795 255 C ATOM 1734 C VAL A 218 -2.169 33.635 31.237 1.00 80.69 C ANISOU 1734 C VAL A 218 11340 11155 8163 1400 -784 78 C ATOM 1735 O VAL A 218 -2.760 32.550 31.297 1.00 93.09 O ANISOU 1735 O VAL A 218 12900 12745 9725 1404 -751 39 O ATOM 1736 CB VAL A 218 -0.916 34.363 29.160 1.00 64.80 C ANISOU 1736 CB VAL A 218 9457 9211 5953 1200 -739 345 C ATOM 1737 CG1 VAL A 218 -0.531 32.910 29.009 1.00 53.01 C ANISOU 1737 CG1 VAL A 218 7967 7739 4435 1202 -656 283 C ATOM 1738 CG2 VAL A 218 -1.083 35.007 27.794 1.00 64.19 C ANISOU 1738 CG2 VAL A 218 9461 9194 5734 1061 -736 549 C ATOM 1739 N ILE A 219 -1.477 34.118 32.270 1.00 91.55 N ANISOU 1739 N ILE A 219 12653 12483 9648 1485 -821 -20 N ATOM 1740 CA ILE A 219 -1.379 33.368 33.520 1.00 92.56 C ANISOU 1740 CA ILE A 219 12687 12591 9889 1594 -813 -173 C ATOM 1741 C ILE A 219 -2.752 33.211 34.160 1.00 86.13 C ANISOU 1741 C ILE A 219 11833 11780 9113 1648 -834 -238 C ATOM 1742 O ILE A 219 -3.158 32.105 34.534 1.00103.07 O ANISOU 1742 O ILE A 219 13941 13943 11278 1672 -803 -281 O ATOM 1743 CB ILE A 219 -0.389 34.049 34.481 1.00 96.25 C ANISOU 1743 CB ILE A 219 13086 13032 10454 1656 -857 -263 C ATOM 1744 CG1 ILE A 219 1.020 34.039 33.895 1.00 76.02 C ANISOU 1744 CG1 ILE A 219 10546 10493 7844 1599 -829 -195 C ATOM 1745 CG2 ILE A 219 -0.400 33.369 35.842 1.00 84.14 C ANISOU 1745 CG2 ILE A 219 11439 11499 9031 1766 -851 -414 C ATOM 1746 CD1 ILE A 219 2.006 34.769 34.747 1.00 76.64 C ANISOU 1746 CD1 ILE A 219 10551 10566 8002 1630 -889 -270 C ATOM 1747 N PHE A 220 -3.486 34.319 34.304 1.00 88.84 N ANISOU 1747 N PHE A 220 12183 12112 9460 1666 -895 -239 N ATOM 1748 CA PHE A 220 -4.798 34.257 34.945 1.00103.10 C ANISOU 1748 CA PHE A 220 13941 13941 11291 1726 -913 -305 C ATOM 1749 C PHE A 220 -5.742 33.333 34.185 1.00 96.82 C ANISOU 1749 C PHE A 220 13177 13209 10404 1651 -875 -224 C ATOM 1750 O PHE A 220 -6.472 32.542 34.794 1.00 85.58 O ANISOU 1750 O PHE A 220 11695 11819 9004 1680 -862 -280 O ATOM 1751 CB PHE A 220 -5.398 35.659 35.065 1.00 93.04 C ANISOU 1751 CB PHE A 220 12686 12646 10017 1763 -990 -309 C ATOM 1752 CG PHE A 220 -5.236 36.270 36.428 1.00 99.79 C ANISOU 1752 CG PHE A 220 13467 13461 10989 1878 -1040 -471 C ATOM 1753 CD1 PHE A 220 -6.147 35.996 37.433 1.00 94.96 C ANISOU 1753 CD1 PHE A 220 12770 12887 10424 1970 -1036 -586 C ATOM 1754 CD2 PHE A 220 -4.172 37.114 36.706 1.00114.69 C ANISOU 1754 CD2 PHE A 220 15359 15286 12930 1882 -1096 -507 C ATOM 1755 CE1 PHE A 220 -6.002 36.551 38.693 1.00102.46 C ANISOU 1755 CE1 PHE A 220 13642 13816 11471 2074 -1078 -744 C ATOM 1756 CE2 PHE A 220 -4.022 37.675 37.964 1.00113.92 C ANISOU 1756 CE2 PHE A 220 15187 15158 12938 1977 -1152 -670 C ATOM 1757 CZ PHE A 220 -4.939 37.392 38.958 1.00106.53 C ANISOU 1757 CZ PHE A 220 14168 14263 12046 2077 -1138 -793 C ATOM 1758 N PHE A 221 -5.730 33.410 32.854 1.00 85.10 N ANISOU 1758 N PHE A 221 11779 11752 8803 1538 -861 -85 N ATOM 1759 CA PHE A 221 -6.573 32.537 32.046 1.00 81.56 C ANISOU 1759 CA PHE A 221 11365 11375 8249 1440 -834 -8 C ATOM 1760 C PHE A 221 -6.198 31.073 32.245 1.00 92.72 C ANISOU 1760 C PHE A 221 12769 12782 9680 1423 -786 -52 C ATOM 1761 O PHE A 221 -7.040 30.247 32.616 1.00113.33 O ANISOU 1761 O PHE A 221 15348 15426 12287 1413 -786 -82 O ATOM 1762 CB PHE A 221 -6.463 32.927 30.573 1.00 88.54 C ANISOU 1762 CB PHE A 221 12341 12304 8995 1312 -826 150 C ATOM 1763 CG PHE A 221 -7.142 31.967 29.638 1.00 95.50 C ANISOU 1763 CG PHE A 221 13268 13269 9749 1184 -797 224 C ATOM 1764 CD1 PHE A 221 -8.521 31.976 29.496 1.00 76.63 C ANISOU 1764 CD1 PHE A 221 10864 10957 7296 1146 -830 257 C ATOM 1765 CD2 PHE A 221 -6.401 31.061 28.894 1.00 98.59 C ANISOU 1765 CD2 PHE A 221 13718 13669 10071 1095 -740 257 C ATOM 1766 CE1 PHE A 221 -9.149 31.098 28.634 1.00 64.85 C ANISOU 1766 CE1 PHE A 221 9420 9549 5672 1004 -813 323 C ATOM 1767 CE2 PHE A 221 -7.024 30.179 28.029 1.00 89.74 C ANISOU 1767 CE2 PHE A 221 12652 12628 8818 959 -720 314 C ATOM 1768 CZ PHE A 221 -8.399 30.199 27.899 1.00 83.75 C ANISOU 1768 CZ PHE A 221 11881 11944 7994 904 -760 348 C ATOM 1769 N CYS A 222 -4.928 30.734 32.005 1.00 89.13 N ANISOU 1769 N CYS A 222 12343 12288 9234 1419 -748 -49 N ATOM 1770 CA CYS A 222 -4.497 29.340 32.065 1.00 86.09 C ANISOU 1770 CA CYS A 222 11969 11891 8850 1408 -707 -77 C ATOM 1771 C CYS A 222 -4.767 28.725 33.434 1.00 84.59 C ANISOU 1771 C CYS A 222 11689 11679 8771 1504 -724 -185 C ATOM 1772 O CYS A 222 -5.286 27.608 33.533 1.00107.71 O ANISOU 1772 O CYS A 222 14629 14623 11675 1466 -717 -188 O ATOM 1773 CB CYS A 222 -3.014 29.235 31.712 1.00 84.73 C ANISOU 1773 CB CYS A 222 11828 11689 8676 1418 -666 -66 C ATOM 1774 SG CYS A 222 -2.654 29.498 29.964 1.00101.96 S ANISOU 1774 SG CYS A 222 14126 13928 10686 1270 -622 76 S ATOM 1775 N TYR A 223 -4.425 29.439 34.506 1.00 99.59 N ANISOU 1775 N TYR A 223 11178 13688 12972 773 -2135 -162 N ATOM 1776 CA TYR A 223 -4.602 28.865 35.834 1.00 90.73 C ANISOU 1776 CA TYR A 223 10223 12327 11922 528 -1884 -222 C ATOM 1777 C TYR A 223 -6.060 28.864 36.276 1.00 90.69 C ANISOU 1777 C TYR A 223 9982 12263 12213 344 -1751 -391 C ATOM 1778 O TYR A 223 -6.475 27.950 36.996 1.00108.47 O ANISOU 1778 O TYR A 223 12311 14341 14561 134 -1581 -485 O ATOM 1779 CB TYR A 223 -3.727 29.603 36.844 1.00 95.97 C ANISOU 1779 CB TYR A 223 11066 12917 12483 544 -1740 -38 C ATOM 1780 CG TYR A 223 -2.280 29.180 36.769 1.00 96.77 C ANISOU 1780 CG TYR A 223 11437 13039 12291 642 -1803 124 C ATOM 1781 CD1 TYR A 223 -1.934 27.835 36.715 1.00116.47 C ANISOU 1781 CD1 TYR A 223 14140 15465 14648 602 -1790 83 C ATOM 1782 CD2 TYR A 223 -1.263 30.119 36.725 1.00 92.05 C ANISOU 1782 CD2 TYR A 223 10876 12525 11573 779 -1869 331 C ATOM 1783 CE1 TYR A 223 -0.611 27.439 36.637 1.00109.98 C ANISOU 1783 CE1 TYR A 223 13558 14689 13539 728 -1834 256 C ATOM 1784 CE2 TYR A 223 0.061 29.734 36.646 1.00101.83 C ANISOU 1784 CE2 TYR A 223 12325 13823 12544 874 -1927 505 C ATOM 1785 CZ TYR A 223 0.382 28.395 36.601 1.00 99.35 C ANISOU 1785 CZ TYR A 223 12216 13473 12060 864 -1906 474 C ATOM 1786 OH TYR A 223 1.701 28.015 36.523 1.00103.73 O ANISOU 1786 OH TYR A 223 12973 14111 12331 993 -1949 672 O ATOM 1787 N GLY A 224 -6.850 29.857 35.866 1.00 68.77 N ANISOU 1787 N GLY A 224 6906 9632 9591 434 -1804 -402 N ATOM 1788 CA GLY A 224 -8.283 29.772 36.096 1.00 76.72 C ANISOU 1788 CA GLY A 224 7637 10641 10871 283 -1708 -555 C ATOM 1789 C GLY A 224 -8.898 28.567 35.410 1.00 94.51 C ANISOU 1789 C GLY A 224 9778 12920 13213 142 -1844 -772 C ATOM 1790 O GLY A 224 -9.708 27.847 36.001 1.00 95.31 O ANISOU 1790 O GLY A 224 9808 12883 13522 -104 -1693 -892 O ATOM 1791 N GLN A 225 -8.509 28.325 34.155 1.00 97.67 N ANISOU 1791 N GLN A 225 10157 13493 13459 301 -2129 -828 N ATOM 1792 CA GLN A 225 -8.980 27.145 33.437 1.00105.15 C ANISOU 1792 CA GLN A 225 11036 14453 14465 176 -2300 -1088 C ATOM 1793 C GLN A 225 -8.561 25.864 34.145 1.00117.53 C ANISOU 1793 C GLN A 225 12920 15697 16039 -48 -2148 -1144 C ATOM 1794 O GLN A 225 -9.333 24.899 34.211 1.00127.74 O ANISOU 1794 O GLN A 225 14130 16848 17557 -301 -2123 -1355 O ATOM 1795 CB GLN A 225 -8.441 27.160 32.006 1.00 98.35 C ANISOU 1795 CB GLN A 225 10158 13855 13357 457 -2628 -1124 C ATOM 1796 CG GLN A 225 -9.079 28.202 31.106 1.00 91.14 C ANISOU 1796 CG GLN A 225 8869 13301 12458 688 -2798 -1102 C ATOM 1797 CD GLN A 225 -10.491 27.834 30.708 1.00107.09 C ANISOU 1797 CD GLN A 225 10515 15461 14711 531 -2910 -1383 C ATOM 1798 OE1 GLN A 225 -10.823 26.656 30.573 1.00129.51 O ANISOU 1798 OE1 GLN A 225 13379 18188 17640 306 -2994 -1655 O ATOM 1799 NE2 GLN A 225 -11.334 28.841 30.523 1.00111.27 N ANISOU 1799 NE2 GLN A 225 10688 16233 15358 646 -2908 -1318 N ATOM 1800 N LEU A 226 -7.339 25.836 34.677 1.00114.88 N ANISOU 1800 N LEU A 226 12935 15242 15472 43 -2038 -945 N ATOM 1801 CA LEU A 226 -6.856 24.637 35.351 1.00104.77 C ANISOU 1801 CA LEU A 226 11971 13673 14162 -114 -1870 -950 C ATOM 1802 C LEU A 226 -7.624 24.387 36.641 1.00108.42 C ANISOU 1802 C LEU A 226 12392 13918 14884 -377 -1544 -936 C ATOM 1803 O LEU A 226 -8.018 23.250 36.922 1.00116.88 O ANISOU 1803 O LEU A 226 13521 14754 16133 -597 -1426 -1046 O ATOM 1804 CB LEU A 226 -5.358 24.761 35.623 1.00 82.27 C ANISOU 1804 CB LEU A 226 9466 10818 10976 79 -1833 -709 C ATOM 1805 CG LEU A 226 -4.590 23.467 35.882 1.00 88.89 C ANISOU 1805 CG LEU A 226 10660 11436 11679 42 -1739 -693 C ATOM 1806 CD1 LEU A 226 -3.303 23.454 35.079 1.00 99.45 C ANISOU 1806 CD1 LEU A 226 12201 12923 12661 330 -1931 -571 C ATOM 1807 CD2 LEU A 226 -4.291 23.324 37.358 1.00 89.14 C ANISOU 1807 CD2 LEU A 226 10882 11287 11699 -65 -1402 -515 C ATOM 1808 N VAL A 227 -7.856 25.434 37.435 1.00 99.39 N ANISOU 1808 N VAL A 227 11149 12839 13776 -345 -1381 -797 N ATOM 1809 CA VAL A 227 -8.626 25.243 38.657 1.00 86.32 C ANISOU 1809 CA VAL A 227 9437 11023 12338 -545 -1058 -767 C ATOM 1810 C VAL A 227 -10.055 24.840 38.320 1.00 88.01 C ANISOU 1810 C VAL A 227 9293 11233 12913 -760 -1077 -959 C ATOM 1811 O VAL A 227 -10.644 24.000 38.999 1.00111.49 O ANISOU 1811 O VAL A 227 12246 14000 16116 -993 -850 -976 O ATOM 1812 CB VAL A 227 -8.566 26.495 39.551 1.00 78.41 C ANISOU 1812 CB VAL A 227 8419 10105 11268 -427 -896 -611 C ATOM 1813 CG1 VAL A 227 -9.336 26.262 40.841 1.00 70.21 C ANISOU 1813 CG1 VAL A 227 7337 8935 10407 -582 -544 -564 C ATOM 1814 CG2 VAL A 227 -7.123 26.827 39.878 1.00 91.85 C ANISOU 1814 CG2 VAL A 227 10451 11815 12634 -256 -907 -448 C ATOM 1815 N PHE A 228 -10.615 25.375 37.234 1.00 90.69 N ANISOU 1815 N PHE A 228 9332 11812 13315 -684 -1348 -1094 N ATOM 1816 CA PHE A 228 -11.943 24.929 36.817 1.00 94.16 C ANISOU 1816 CA PHE A 228 9398 12291 14086 -899 -1414 -1302 C ATOM 1817 C PHE A 228 -11.944 23.439 36.487 1.00 90.38 C ANISOU 1817 C PHE A 228 9028 11579 13733 -1131 -1477 -1498 C ATOM 1818 O PHE A 228 -12.773 22.680 37.002 1.00 95.95 O ANISOU 1818 O PHE A 228 9601 12088 14768 -1425 -1299 -1563 O ATOM 1819 CB PHE A 228 -12.431 25.744 35.622 1.00 82.97 C ANISOU 1819 CB PHE A 228 7647 11231 12649 -725 -1724 -1409 C ATOM 1820 CG PHE A 228 -13.863 25.479 35.262 1.00 89.55 C ANISOU 1820 CG PHE A 228 8029 12183 13812 -929 -1797 -1609 C ATOM 1821 CD1 PHE A 228 -14.885 25.861 36.117 1.00 83.57 C ANISOU 1821 CD1 PHE A 228 7008 11431 13313 -1052 -1539 -1519 C ATOM 1822 CD2 PHE A 228 -14.190 24.851 34.071 1.00 99.35 C ANISOU 1822 CD2 PHE A 228 9096 13557 15094 -986 -2130 -1893 C ATOM 1823 CE1 PHE A 228 -16.204 25.619 35.792 1.00 89.30 C ANISOU 1823 CE1 PHE A 228 7277 12297 14354 -1247 -1605 -1679 C ATOM 1824 CE2 PHE A 228 -15.509 24.610 33.739 1.00 93.40 C ANISOU 1824 CE2 PHE A 228 7891 12945 14652 -1195 -2224 -2095 C ATOM 1825 CZ PHE A 228 -16.518 24.993 34.601 1.00 90.08 C ANISOU 1825 CZ PHE A 228 7184 12534 14510 -1335 -1958 -1973 C ATOM 1826 N THR A 229 -11.009 23.003 35.635 1.00 89.32 N ANISOU 1826 N THR A 229 9139 11446 13351 -993 -1714 -1583 N ATOM 1827 CA THR A 229 -10.926 21.595 35.249 1.00 95.03 C ANISOU 1827 CA THR A 229 10016 11917 14174 -1176 -1788 -1798 C ATOM 1828 C THR A 229 -10.789 20.687 36.466 1.00 77.99 C ANISOU 1828 C THR A 229 8102 9360 12171 -1390 -1409 -1662 C ATOM 1829 O THR A 229 -11.485 19.671 36.582 1.00106.41 O ANISOU 1829 O THR A 229 11621 12698 16113 -1693 -1325 -1815 O ATOM 1830 CB THR A 229 -9.748 21.387 34.292 1.00 94.09 C ANISOU 1830 CB THR A 229 10191 11876 13683 -907 -2049 -1842 C ATOM 1831 OG1 THR A 229 -10.141 21.734 32.959 1.00112.18 O ANISOU 1831 OG1 THR A 229 12216 14495 15913 -772 -2428 -2069 O ATOM 1832 CG2 THR A 229 -9.268 19.943 34.320 1.00 98.45 C ANISOU 1832 CG2 THR A 229 11080 12064 14262 -1036 -1993 -1956 C ATOM 1833 N VAL A 230 -9.893 21.040 37.386 1.00 87.10 N ANISOU 1833 N VAL A 230 9544 10470 13082 -1233 -1172 -1368 N ATOM 1834 CA VAL A 230 -9.646 20.185 38.542 1.00 99.57 C ANISOU 1834 CA VAL A 230 11376 11719 14737 -1365 -801 -1199 C ATOM 1835 C VAL A 230 -10.869 20.147 39.445 1.00104.26 C ANISOU 1835 C VAL A 230 11683 12217 15714 -1616 -510 -1147 C ATOM 1836 O VAL A 230 -11.263 19.084 39.942 1.00106.43 O ANISOU 1836 O VAL A 230 11990 12175 16272 -1856 -275 -1136 O ATOM 1837 CB VAL A 230 -8.395 20.668 39.295 1.00 91.68 C ANISOU 1837 CB VAL A 230 10712 10779 13341 -1107 -651 -909 C ATOM 1838 CG1 VAL A 230 -8.189 19.857 40.554 1.00 93.63 C ANISOU 1838 CG1 VAL A 230 11191 10752 13632 -1195 -246 -703 C ATOM 1839 CG2 VAL A 230 -7.179 20.565 38.397 1.00 88.89 C ANISOU 1839 CG2 VAL A 230 10625 10512 12637 -870 -914 -926 C ATOM 1840 N LYS A 231 -11.491 21.306 39.664 1.00 97.03 N ANISOU 1840 N LYS A 231 10481 11565 14823 -1549 -503 -1094 N ATOM 1841 CA LYS A 231 -12.688 21.372 40.493 1.00 95.40 C ANISOU 1841 CA LYS A 231 9970 11324 14955 -1741 -224 -1021 C ATOM 1842 C LYS A 231 -13.797 20.518 39.912 1.00 97.97 C ANISOU 1842 C LYS A 231 9972 11528 15725 -2073 -313 -1251 C ATOM 1843 O LYS A 231 -14.498 19.801 40.638 1.00 87.91 O ANISOU 1843 O LYS A 231 8583 10024 14795 -2326 -18 -1173 O ATOM 1844 CB LYS A 231 -13.157 22.818 40.601 1.00 97.05 C ANISOU 1844 CB LYS A 231 9923 11859 15093 -1568 -256 -963 C ATOM 1845 CG LYS A 231 -12.227 23.718 41.364 1.00106.05 C ANISOU 1845 CG LYS A 231 11340 13084 15869 -1291 -130 -755 C ATOM 1846 CD LYS A 231 -12.201 23.349 42.812 1.00124.21 C ANISOU 1846 CD LYS A 231 13799 15221 18174 -1327 293 -538 C ATOM 1847 CE LYS A 231 -11.748 24.511 43.668 1.00111.28 C ANISOU 1847 CE LYS A 231 12288 13743 16250 -1073 419 -390 C ATOM 1848 NZ LYS A 231 -12.913 25.275 44.185 1.00132.09 N ANISOU 1848 NZ LYS A 231 14604 16511 19075 -1064 590 -359 N ATOM 1849 N GLU A 232 -13.967 20.596 38.597 1.00 97.71 N ANISOU 1849 N GLU A 232 9772 11662 15691 -2071 -721 -1534 N ATOM 1850 CA GLU A 232 -15.029 19.876 37.915 1.00 97.38 C ANISOU 1850 CA GLU A 232 9382 11564 16053 -2386 -886 -1819 C ATOM 1851 C GLU A 232 -14.813 18.372 38.001 1.00112.52 C ANISOU 1851 C GLU A 232 11535 13025 18193 -2648 -787 -1918 C ATOM 1852 O GLU A 232 -15.739 17.620 38.329 1.00128.50 O ANISOU 1852 O GLU A 232 13325 14818 20680 -2999 -625 -1967 O ATOM 1853 CB GLU A 232 -15.081 20.348 36.465 1.00114.89 C ANISOU 1853 CB GLU A 232 11419 14120 18114 -2243 -1369 -2101 C ATOM 1854 CG GLU A 232 -16.297 19.916 35.698 1.00157.22 C ANISOU 1854 CG GLU A 232 16321 19570 23847 -2527 -1605 -2425 C ATOM 1855 CD GLU A 232 -16.429 20.663 34.389 1.00164.69 C ANISOU 1855 CD GLU A 232 17029 20974 24572 -2296 -2047 -2638 C ATOM 1856 OE1 GLU A 232 -15.443 21.311 33.974 1.00170.36 O ANISOU 1856 OE1 GLU A 232 18002 21864 24864 -1932 -2177 -2545 O ATOM 1857 OE2 GLU A 232 -17.518 20.608 33.781 1.00148.45 O ANISOU 1857 OE2 GLU A 232 14511 19125 22767 -2469 -2258 -2878 O ATOM 1858 N ALA A 233 -13.591 17.915 37.714 1.00108.69 N ANISOU 1858 N ALA A 233 11507 12392 17398 -2477 -865 -1929 N ATOM 1859 CA ALA A 233 -13.284 16.492 37.814 1.00116.57 C ANISOU 1859 CA ALA A 233 12787 12922 18583 -2675 -741 -2001 C ATOM 1860 C ALA A 233 -13.493 15.983 39.235 1.00111.37 C ANISOU 1860 C ALA A 233 12200 11948 18168 -2832 -218 -1676 C ATOM 1861 O ALA A 233 -14.130 14.945 39.449 1.00 99.09 O ANISOU 1861 O ALA A 233 10556 10023 17070 -3170 -50 -1736 O ATOM 1862 CB ALA A 233 -11.850 16.235 37.351 1.00 90.23 C ANISOU 1862 CB ALA A 233 9944 9539 14801 -2379 -875 -1999 C ATOM 1863 N ALA A 234 -12.968 16.711 40.224 1.00 99.82 N ANISOU 1863 N ALA A 234 10890 10630 16409 -2584 46 -1326 N ATOM 1864 CA ALA A 234 -13.169 16.321 41.616 1.00 97.08 C ANISOU 1864 CA ALA A 234 10596 10063 16227 -2664 553 -991 C ATOM 1865 C ALA A 234 -14.646 16.299 41.984 1.00117.70 C ANISOU 1865 C ALA A 234 12720 12658 19344 -2970 721 -981 C ATOM 1866 O ALA A 234 -15.059 15.507 42.838 1.00132.16 O ANISOU 1866 O ALA A 234 14528 14184 21501 -3164 1115 -778 O ATOM 1867 CB ALA A 234 -12.400 17.262 42.542 1.00 88.14 C ANISOU 1867 CB ALA A 234 9671 9177 14642 -2318 741 -681 C ATOM 1868 N ALA A 235 -15.454 17.158 41.355 1.00125.52 N ANISOU 1868 N ALA A 235 13300 13986 20406 -3000 448 -1166 N ATOM 1869 CA ALA A 235 -16.897 17.099 41.558 1.00115.50 C ANISOU 1869 CA ALA A 235 11515 12737 19632 -3301 564 -1177 C ATOM 1870 C ALA A 235 -17.475 15.804 41.005 1.00123.10 C ANISOU 1870 C ALA A 235 12334 13333 21106 -3728 484 -1427 C ATOM 1871 O ALA A 235 -18.305 15.161 41.655 1.00145.58 O ANISOU 1871 O ALA A 235 14948 15937 24429 -4028 801 -1288 O ATOM 1872 CB ALA A 235 -17.574 18.306 40.911 1.00115.81 C ANISOU 1872 CB ALA A 235 11152 13251 19599 -3198 265 -1322 C ATOM 1873 N GLN A 236 -17.045 15.398 39.814 1.00113.87 N ANISOU 1873 N GLN A 236 11301 12109 19857 -3756 70 -1796 N ATOM 1874 CA GLN A 236 -17.478 14.121 39.267 1.00113.75 C ANISOU 1874 CA GLN A 236 11216 11694 20310 -4156 -31 -2092 C ATOM 1875 C GLN A 236 -16.768 12.923 39.900 1.00129.68 C ANISOU 1875 C GLN A 236 13689 13150 22434 -4224 316 -1921 C ATOM 1876 O GLN A 236 -16.951 11.802 39.415 1.00117.33 O ANISOU 1876 O GLN A 236 12163 11175 21242 -4531 236 -2184 O ATOM 1877 CB GLN A 236 -17.276 14.096 37.748 1.00111.85 C ANISOU 1877 CB GLN A 236 10974 11613 19911 -4122 -608 -2582 C ATOM 1878 CG GLN A 236 -18.289 14.913 36.959 1.00117.52 C ANISOU 1878 CG GLN A 236 11134 12815 20703 -4176 -969 -2826 C ATOM 1879 CD GLN A 236 -19.638 14.226 36.837 1.00129.07 C ANISOU 1879 CD GLN A 236 12091 14129 22821 -4685 -994 -3039 C ATOM 1880 OE1 GLN A 236 -19.747 13.145 36.258 1.00129.54 O ANISOU 1880 OE1 GLN A 236 12190 13844 23185 -4988 -1167 -3386 O ATOM 1881 NE2 GLN A 236 -20.673 14.854 37.383 1.00137.10 N ANISOU 1881 NE2 GLN A 236 12622 15401 24067 -4781 -821 -2836 N ATOM 1882 N GLN A 237 -15.980 13.106 40.960 1.00136.80 N ANISOU 1882 N GLN A 237 14931 14018 23029 -3946 699 -1501 N ATOM 1883 CA GLN A 237 -15.264 11.981 41.565 1.00123.00 C ANISOU 1883 CA GLN A 237 13620 11775 21341 -3955 1048 -1298 C ATOM 1884 C GLN A 237 -15.171 12.129 43.083 1.00110.00 C ANISOU 1884 C GLN A 237 12050 10117 19628 -3806 1609 -765 C ATOM 1885 O GLN A 237 -14.121 11.910 43.687 1.00108.58 O ANISOU 1885 O GLN A 237 12309 9845 19101 -3529 1843 -501 O ATOM 1886 CB GLN A 237 -13.874 11.837 40.952 1.00120.87 C ANISOU 1886 CB GLN A 237 13869 11489 20569 -3640 822 -1409 C ATOM 1887 CG GLN A 237 -13.333 10.424 40.990 1.00134.93 C ANISOU 1887 CG GLN A 237 16045 12691 22532 -3738 1012 -1409 C ATOM 1888 CD GLN A 237 -12.551 10.087 39.744 1.00132.16 C ANISOU 1888 CD GLN A 237 15997 12294 21925 -3610 585 -1790 C ATOM 1889 OE1 GLN A 237 -12.368 10.933 38.869 1.00126.62 O ANISOU 1889 OE1 GLN A 237 15206 12023 20882 -3427 155 -2021 O ATOM 1890 NE2 GLN A 237 -12.089 8.845 39.651 1.00121.21 N ANISOU 1890 NE2 GLN A 237 14973 10382 20698 -3679 717 -1843 N ATOM 1891 N GLN A 238 -16.288 12.466 43.731 1.00115.21 N ANISOU 1891 N GLN A 238 12270 10891 20614 -3973 1840 -593 N ATOM 1892 CA GLN A 238 -16.261 12.640 45.180 1.00116.80 C ANISOU 1892 CA GLN A 238 12524 11131 20722 -3792 2375 -92 C ATOM 1893 C GLN A 238 -16.036 11.337 45.936 1.00123.88 C ANISOU 1893 C GLN A 238 13666 11505 21898 -3898 2851 203 C ATOM 1894 O GLN A 238 -15.812 11.382 47.150 1.00133.24 O ANISOU 1894 O GLN A 238 14973 12731 22920 -3675 3311 645 O ATOM 1895 CB GLN A 238 -17.556 13.281 45.669 1.00126.07 C ANISOU 1895 CB GLN A 238 13155 12561 22183 -3920 2528 36 C ATOM 1896 CG GLN A 238 -18.167 14.248 44.690 1.00138.83 C ANISOU 1896 CG GLN A 238 14399 14579 23772 -3963 2053 -311 C ATOM 1897 CD GLN A 238 -18.962 15.333 45.375 1.00142.21 C ANISOU 1897 CD GLN A 238 14465 15415 24152 -3826 2225 -95 C ATOM 1898 OE1 GLN A 238 -19.779 15.061 46.259 1.00141.05 O ANISOU 1898 OE1 GLN A 238 14054 15190 24348 -3956 2638 201 O ATOM 1899 NE2 GLN A 238 -18.717 16.578 44.981 1.00123.85 N ANISOU 1899 NE2 GLN A 238 12131 13521 21403 -3540 1929 -223 N ATOM 1900 N GLU A 239 -16.105 10.185 45.266 1.00121.88 N ANISOU 1900 N GLU A 239 13486 10763 22060 -4215 2764 -26 N ATOM 1901 CA GLU A 239 -15.767 8.933 45.930 1.00126.94 C ANISOU 1901 CA GLU A 239 14420 10860 22952 -4276 3227 267 C ATOM 1902 C GLU A 239 -14.261 8.753 46.080 1.00133.96 C ANISOU 1902 C GLU A 239 15917 11722 23260 -3860 3275 400 C ATOM 1903 O GLU A 239 -13.825 7.949 46.911 1.00150.33 O ANISOU 1903 O GLU A 239 18268 13478 25372 -3756 3742 775 O ATOM 1904 CB GLU A 239 -16.375 7.743 45.176 1.00129.14 C ANISOU 1904 CB GLU A 239 14580 10567 23922 -4774 3129 -44 C ATOM 1905 CG GLU A 239 -15.696 7.376 43.857 1.00133.28 C ANISOU 1905 CG GLU A 239 15404 10938 24296 -4787 2625 -555 C ATOM 1906 CD GLU A 239 -16.216 8.170 42.672 1.00131.73 C ANISOU 1906 CD GLU A 239 14866 11143 24041 -4901 2008 -1064 C ATOM 1907 OE1 GLU A 239 -16.701 9.299 42.877 1.00135.54 O ANISOU 1907 OE1 GLU A 239 15010 12142 24348 -4798 1934 -983 O ATOM 1908 OE2 GLU A 239 -16.136 7.666 41.531 1.00128.81 O ANISOU 1908 OE2 GLU A 239 14573 10583 23785 -5065 1603 -1545 O ATOM 1909 N SER A 240 -13.463 9.493 45.313 1.00113.95 N ANISOU 1909 N SER A 240 13572 9535 20187 -3603 2822 135 N ATOM 1910 CA SER A 240 -12.005 9.433 45.388 1.00110.04 C ANISOU 1910 CA SER A 240 13609 9094 19108 -3196 2822 258 C ATOM 1911 C SER A 240 -11.526 10.557 46.300 1.00114.31 C ANISOU 1911 C SER A 240 14185 10153 19094 -2808 2951 568 C ATOM 1912 O SER A 240 -11.513 11.726 45.908 1.00121.41 O ANISOU 1912 O SER A 240 14935 11501 19695 -2689 2607 393 O ATOM 1913 CB SER A 240 -11.387 9.546 43.998 1.00129.26 C ANISOU 1913 CB SER A 240 16217 11600 21294 -3136 2263 -192 C ATOM 1914 OG SER A 240 -9.970 9.566 44.063 1.00110.77 O ANISOU 1914 OG SER A 240 14349 9366 18371 -2727 2258 -44 O ATOM 1915 N ALA A 241 -11.129 10.197 47.523 1.00106.09 N ANISOU 1915 N ALA A 241 13344 9048 17916 -2601 3452 1026 N ATOM 1916 CA ALA A 241 -10.583 11.189 48.444 1.00106.10 C ANISOU 1916 CA ALA A 241 13420 9536 17356 -2214 3571 1293 C ATOM 1917 C ALA A 241 -9.264 11.763 47.936 1.00100.35 C ANISOU 1917 C ALA A 241 13020 9102 16006 -1892 3214 1165 C ATOM 1918 O ALA A 241 -8.935 12.918 48.233 1.00 93.15 O ANISOU 1918 O ALA A 241 12073 8649 14671 -1658 3081 1184 O ATOM 1919 CB ALA A 241 -10.398 10.570 49.829 1.00106.88 C ANISOU 1919 CB ALA A 241 13673 9522 17414 -2029 4182 1808 C ATOM 1920 N THR A 242 -8.503 10.974 47.173 1.00 97.00 N ANISOU 1920 N THR A 242 12910 8411 15534 -1873 3064 1038 N ATOM 1921 CA THR A 242 -7.254 11.464 46.598 1.00 92.40 C ANISOU 1921 CA THR A 242 12611 8108 14389 -1573 2722 935 C ATOM 1922 C THR A 242 -7.508 12.576 45.588 1.00106.68 C ANISOU 1922 C THR A 242 14174 10244 16116 -1629 2198 564 C ATOM 1923 O THR A 242 -6.754 13.555 45.532 1.00102.50 O ANISOU 1923 O THR A 242 13714 10117 15114 -1369 1982 573 O ATOM 1924 CB THR A 242 -6.493 10.305 45.953 1.00 93.82 C ANISOU 1924 CB THR A 242 13166 7909 14573 -1532 2697 879 C ATOM 1925 OG1 THR A 242 -5.824 9.549 46.971 1.00115.45 O ANISOU 1925 OG1 THR A 242 16213 10502 17152 -1306 3169 1307 O ATOM 1926 CG2 THR A 242 -5.476 10.808 44.940 1.00 89.73 C ANISOU 1926 CG2 THR A 242 12834 7660 13598 -1306 2234 663 C ATOM 1927 N THR A 243 -8.569 12.450 44.786 1.00114.83 N ANISOU 1927 N THR A 243 14900 11117 17613 -1966 1992 247 N ATOM 1928 CA THR A 243 -8.925 13.530 43.873 1.00104.62 C ANISOU 1928 CA THR A 243 13330 10168 16253 -1995 1531 -67 C ATOM 1929 C THR A 243 -9.338 14.783 44.635 1.00 90.81 C ANISOU 1929 C THR A 243 11326 8812 14367 -1897 1611 78 C ATOM 1930 O THR A 243 -9.104 15.903 44.166 1.00 85.29 O ANISOU 1930 O THR A 243 10541 8474 13391 -1747 1295 -47 O ATOM 1931 CB THR A 243 -10.047 13.083 42.933 1.00107.37 C ANISOU 1931 CB THR A 243 13367 10299 17129 -2373 1312 -431 C ATOM 1932 OG1 THR A 243 -9.711 11.816 42.351 1.00 95.94 O ANISOU 1932 OG1 THR A 243 12187 8416 15852 -2478 1287 -580 O ATOM 1933 CG2 THR A 243 -10.243 14.100 41.820 1.00 90.72 C ANISOU 1933 CG2 THR A 243 11021 8571 14879 -2333 805 -755 C ATOM 1934 N GLN A 244 -9.938 14.615 45.817 1.00 89.56 N ANISOU 1934 N GLN A 244 11054 8580 14396 -1957 2047 353 N ATOM 1935 CA GLN A 244 -10.302 15.765 46.637 1.00100.09 C ANISOU 1935 CA GLN A 244 12187 10275 15566 -1819 2159 493 C ATOM 1936 C GLN A 244 -9.060 16.464 47.176 1.00108.92 C ANISOU 1936 C GLN A 244 13612 11694 16079 -1441 2148 651 C ATOM 1937 O GLN A 244 -8.926 17.687 47.055 1.00114.63 O ANISOU 1937 O GLN A 244 14246 12757 16553 -1300 1919 554 O ATOM 1938 CB GLN A 244 -11.219 15.323 47.778 1.00118.36 C ANISOU 1938 CB GLN A 244 14317 12448 18208 -1937 2655 774 C ATOM 1939 CG GLN A 244 -12.454 14.555 47.317 1.00121.17 C ANISOU 1939 CG GLN A 244 14336 12480 19223 -2354 2695 646 C ATOM 1940 CD GLN A 244 -13.149 15.213 46.136 1.00118.75 C ANISOU 1940 CD GLN A 244 13688 12343 19090 -2536 2228 255 C ATOM 1941 OE1 GLN A 244 -13.174 14.663 45.034 1.00109.29 O ANISOU 1941 OE1 GLN A 244 12485 10955 18086 -2732 1922 -48 O ATOM 1942 NE2 GLN A 244 -13.719 16.393 46.362 1.00111.98 N ANISOU 1942 NE2 GLN A 244 12548 11856 18145 -2442 2175 256 N ATOM 1943 N LYS A 245 -8.145 15.698 47.784 1.00115.45 N ANISOU 1943 N LYS A 245 14792 12398 16677 -1273 2400 899 N ATOM 1944 CA LYS A 245 -6.835 16.230 48.149 1.00 94.75 C ANISOU 1944 CA LYS A 245 12463 10067 13471 -932 2333 1021 C ATOM 1945 C LYS A 245 -6.223 17.002 46.988 1.00 88.93 C ANISOU 1945 C LYS A 245 11745 9527 12516 -870 1827 756 C ATOM 1946 O LYS A 245 -5.829 18.165 47.137 1.00 97.17 O ANISOU 1946 O LYS A 245 12758 10906 13254 -704 1660 732 O ATOM 1947 CB LYS A 245 -5.895 15.096 48.571 1.00 82.55 C ANISOU 1947 CB LYS A 245 11290 8329 11746 -779 2595 1281 C ATOM 1948 CG LYS A 245 -6.292 14.332 49.827 1.00110.79 C ANISOU 1948 CG LYS A 245 14891 11745 15457 -753 3148 1631 C ATOM 1949 CD LYS A 245 -5.257 13.252 50.147 1.00139.05 C ANISOU 1949 CD LYS A 245 18858 15155 18818 -550 3391 1902 C ATOM 1950 CE LYS A 245 -5.909 11.894 50.399 1.00148.32 C ANISOU 1950 CE LYS A 245 20046 15824 20485 -737 3806 2087 C ATOM 1951 NZ LYS A 245 -4.910 10.784 50.477 1.00140.19 N ANISOU 1951 NZ LYS A 245 19415 14561 19291 -543 4012 2316 N ATOM 1952 N ALA A 246 -6.160 16.366 45.814 1.00 80.21 N ANISOU 1952 N ALA A 246 10687 8209 11581 -996 1585 554 N ATOM 1953 CA ALA A 246 -5.548 16.993 44.646 1.00 89.57 C ANISOU 1953 CA ALA A 246 11896 9590 12547 -897 1126 339 C ATOM 1954 C ALA A 246 -6.204 18.326 44.317 1.00 98.95 C ANISOU 1954 C ALA A 246 12749 11058 13788 -933 883 169 C ATOM 1955 O ALA A 246 -5.512 19.311 44.037 1.00 99.74 O ANISOU 1955 O ALA A 246 12880 11442 13575 -745 645 154 O ATOM 1956 CB ALA A 246 -5.626 16.052 43.446 1.00 75.97 C ANISOU 1956 CB ALA A 246 10234 7591 11040 -1033 921 108 C ATOM 1957 N GLU A 247 -7.536 18.378 44.344 1.00110.76 N ANISOU 1957 N GLU A 247 13913 12476 15695 -1170 951 60 N ATOM 1958 CA GLU A 247 -8.234 19.630 44.072 1.00113.63 C ANISOU 1958 CA GLU A 247 13950 13106 16119 -1177 761 -74 C ATOM 1959 C GLU A 247 -7.812 20.717 45.055 1.00101.42 C ANISOU 1959 C GLU A 247 12460 11819 14256 -955 880 93 C ATOM 1960 O GLU A 247 -7.507 21.846 44.655 1.00106.78 O ANISOU 1960 O GLU A 247 13082 12737 14752 -820 629 14 O ATOM 1961 CB GLU A 247 -9.745 19.401 44.115 1.00121.36 C ANISOU 1961 CB GLU A 247 14551 13970 17589 -1457 879 -165 C ATOM 1962 CG GLU A 247 -10.575 20.664 44.115 1.00131.40 C ANISOU 1962 CG GLU A 247 15478 15520 18929 -1432 792 -233 C ATOM 1963 CD GLU A 247 -11.119 21.002 45.489 1.00146.77 C ANISOU 1963 CD GLU A 247 17339 17518 20909 -1392 1188 -13 C ATOM 1964 OE1 GLU A 247 -10.663 20.383 46.472 1.00151.56 O ANISOU 1964 OE1 GLU A 247 18185 18003 21399 -1330 1510 211 O ATOM 1965 OE2 GLU A 247 -12.006 21.876 45.590 1.00154.86 O ANISOU 1965 OE2 GLU A 247 18057 18724 22060 -1390 1190 -52 O ATOM 1966 N LYS A 248 -7.765 20.384 46.347 1.00 93.92 N ANISOU 1966 N LYS A 248 11630 10821 13234 -901 1267 325 N ATOM 1967 CA LYS A 248 -7.357 21.360 47.353 1.00 86.61 C ANISOU 1967 CA LYS A 248 10777 10150 11981 -680 1377 445 C ATOM 1968 C LYS A 248 -5.936 21.856 47.101 1.00100.09 C ANISOU 1968 C LYS A 248 12741 12034 13255 -470 1132 452 C ATOM 1969 O LYS A 248 -5.697 23.065 47.004 1.00102.06 O ANISOU 1969 O LYS A 248 12931 12497 13352 -364 936 368 O ATOM 1970 CB LYS A 248 -7.475 20.752 48.752 1.00 78.01 C ANISOU 1970 CB LYS A 248 9792 9007 10841 -618 1840 706 C ATOM 1971 CG LYS A 248 -8.862 20.870 49.368 1.00 89.13 C ANISOU 1971 CG LYS A 248 10896 10392 12578 -729 2117 750 C ATOM 1972 CD LYS A 248 -8.960 20.072 50.662 1.00120.63 C ANISOU 1972 CD LYS A 248 14990 14308 16537 -651 2606 1057 C ATOM 1973 CE LYS A 248 -10.375 20.078 51.224 1.00129.77 C ANISOU 1973 CE LYS A 248 15815 15435 18058 -765 2909 1145 C ATOM 1974 NZ LYS A 248 -10.779 21.424 51.720 1.00133.99 N ANISOU 1974 NZ LYS A 248 16205 16275 18430 -594 2887 1074 N ATOM 1975 N GLU A 249 -4.979 20.931 46.983 1.00102.68 N ANISOU 1975 N GLU A 249 13347 12266 13401 -406 1152 565 N ATOM 1976 CA GLU A 249 -3.581 21.327 46.839 1.00 98.80 C ANISOU 1976 CA GLU A 249 13081 11970 12487 -198 953 622 C ATOM 1977 C GLU A 249 -3.352 22.125 45.561 1.00 90.46 C ANISOU 1977 C GLU A 249 11912 11021 11436 -194 531 440 C ATOM 1978 O GLU A 249 -2.596 23.104 45.560 1.00 99.42 O ANISOU 1978 O GLU A 249 13077 12377 12322 -58 353 451 O ATOM 1979 CB GLU A 249 -2.681 20.090 46.874 1.00110.76 C ANISOU 1979 CB GLU A 249 14898 13358 13827 -111 1073 799 C ATOM 1980 CG GLU A 249 -1.282 20.289 46.284 1.00140.20 C ANISOU 1980 CG GLU A 249 18820 17263 17188 75 803 844 C ATOM 1981 CD GLU A 249 -0.361 21.137 47.154 1.00149.63 C ANISOU 1981 CD GLU A 249 20095 18777 17982 265 799 965 C ATOM 1982 OE1 GLU A 249 -0.806 21.640 48.208 1.00153.86 O ANISOU 1982 OE1 GLU A 249 20557 19409 18495 273 985 979 O ATOM 1983 OE2 GLU A 249 0.821 21.296 46.778 1.00141.01 O ANISOU 1983 OE2 GLU A 249 19134 17854 16592 411 601 1040 O ATOM 1984 N VAL A 250 -3.999 21.730 44.465 1.00 83.43 N ANISOU 1984 N VAL A 250 10879 9985 10834 -338 369 275 N ATOM 1985 CA VAL A 250 -3.819 22.449 43.208 1.00 78.11 C ANISOU 1985 CA VAL A 250 10083 9448 10146 -291 -16 127 C ATOM 1986 C VAL A 250 -4.385 23.861 43.312 1.00 88.02 C ANISOU 1986 C VAL A 250 11085 10878 11478 -279 -100 52 C ATOM 1987 O VAL A 250 -3.782 24.822 42.819 1.00 84.28 O ANISOU 1987 O VAL A 250 10591 10581 10852 -148 -333 51 O ATOM 1988 CB VAL A 250 -4.450 21.662 42.045 1.00 78.25 C ANISOU 1988 CB VAL A 250 9996 9305 10432 -429 -175 -64 C ATOM 1989 CG1 VAL A 250 -4.500 22.511 40.795 1.00 67.99 C ANISOU 1989 CG1 VAL A 250 8504 8202 9128 -353 -547 -212 C ATOM 1990 CG2 VAL A 250 -3.654 20.395 41.777 1.00 85.65 C ANISOU 1990 CG2 VAL A 250 11238 10064 11239 -381 -143 -6 C ATOM 1991 N THR A 251 -5.540 24.018 43.962 1.00 87.73 N ANISOU 1991 N THR A 251 10853 10789 11691 -401 109 11 N ATOM 1992 CA THR A 251 -6.095 25.355 44.143 1.00 84.46 C ANISOU 1992 CA THR A 251 10224 10525 11342 -356 68 -51 C ATOM 1993 C THR A 251 -5.168 26.220 44.989 1.00 90.96 C ANISOU 1993 C THR A 251 11227 11485 11849 -186 102 43 C ATOM 1994 O THR A 251 -4.849 27.355 44.617 1.00 91.29 O ANISOU 1994 O THR A 251 11209 11646 11831 -92 -98 -2 O ATOM 1995 CB THR A 251 -7.486 25.275 44.771 1.00 86.58 C ANISOU 1995 CB THR A 251 10257 10728 11913 -489 324 -81 C ATOM 1996 OG1 THR A 251 -8.364 24.554 43.898 1.00107.12 O ANISOU 1996 OG1 THR A 251 12641 13220 14839 -679 241 -202 O ATOM 1997 CG2 THR A 251 -8.047 26.672 44.994 1.00 87.00 C ANISOU 1997 CG2 THR A 251 10114 10932 12010 -398 306 -137 C ATOM 1998 N ARG A 252 -4.705 25.688 46.125 1.00 96.03 N ANISOU 1998 N ARG A 252 12084 12113 12289 -142 354 175 N ATOM 1999 CA ARG A 252 -3.810 26.449 46.993 1.00 91.63 C ANISOU 1999 CA ARG A 252 11691 11717 11408 12 370 229 C ATOM 2000 C ARG A 252 -2.533 26.850 46.262 1.00 89.89 C ANISOU 2000 C ARG A 252 11582 11602 10971 100 63 255 C ATOM 2001 O ARG A 252 -2.055 27.982 46.408 1.00 95.18 O ANISOU 2001 O ARG A 252 12242 12388 11534 172 -72 212 O ATOM 2002 CB ARG A 252 -3.480 25.638 48.248 1.00 86.15 C ANISOU 2002 CB ARG A 252 11204 11037 10492 77 685 387 C ATOM 2003 CG ARG A 252 -2.898 26.458 49.395 1.00 96.27 C ANISOU 2003 CG ARG A 252 12603 12520 11457 233 746 390 C ATOM 2004 CD ARG A 252 -2.434 25.567 50.542 1.00110.28 C ANISOU 2004 CD ARG A 252 14586 14370 12946 349 1040 577 C ATOM 2005 NE ARG A 252 -1.316 24.711 50.149 1.00142.57 N ANISOU 2005 NE ARG A 252 18870 18470 16830 394 961 729 N ATOM 2006 CZ ARG A 252 -0.049 24.916 50.501 1.00143.13 C ANISOU 2006 CZ ARG A 252 19106 18761 16517 536 853 799 C ATOM 2007 NH1 ARG A 252 0.272 25.948 51.269 1.00150.21 N ANISOU 2007 NH1 ARG A 252 20003 19867 17201 621 792 696 N ATOM 2008 NH2 ARG A 252 0.899 24.083 50.090 1.00124.72 N ANISOU 2008 NH2 ARG A 252 16935 16442 14011 597 804 964 N ATOM 2009 N MET A 253 -1.970 25.942 45.460 1.00 78.73 N ANISOU 2009 N MET A 253 10270 10140 9505 99 -44 329 N ATOM 2010 CA MET A 253 -0.760 26.278 44.714 1.00 75.54 C ANISOU 2010 CA MET A 253 9947 9861 8891 207 -319 396 C ATOM 2011 C MET A 253 -1.026 27.357 43.670 1.00 84.04 C ANISOU 2011 C MET A 253 10803 10984 10143 213 -587 296 C ATOM 2012 O MET A 253 -0.213 28.273 43.503 1.00103.17 O ANISOU 2012 O MET A 253 13225 13528 12446 295 -758 346 O ATOM 2013 CB MET A 253 -0.170 25.030 44.058 1.00 63.40 C ANISOU 2013 CB MET A 253 8576 8263 7250 246 -353 496 C ATOM 2014 CG MET A 253 0.836 24.289 44.929 1.00 90.47 C ANISOU 2014 CG MET A 253 12274 11752 10350 353 -179 690 C ATOM 2015 SD MET A 253 2.168 25.352 45.536 1.00112.12 S ANISOU 2015 SD MET A 253 15076 14790 12734 486 -310 793 S ATOM 2016 CE MET A 253 2.835 25.999 44.001 1.00 99.01 C ANISOU 2016 CE MET A 253 13306 13217 11095 546 -692 813 C ATOM 2017 N VAL A 254 -2.150 27.272 42.955 1.00 77.67 N ANISOU 2017 N VAL A 254 9790 10092 9630 130 -623 171 N ATOM 2018 CA VAL A 254 -2.445 28.286 41.945 1.00 87.28 C ANISOU 2018 CA VAL A 254 10782 11385 10997 178 -856 106 C ATOM 2019 C VAL A 254 -2.609 29.653 42.596 1.00 96.20 C ANISOU 2019 C VAL A 254 11826 12547 12177 207 -816 76 C ATOM 2020 O VAL A 254 -2.147 30.671 42.066 1.00101.69 O ANISOU 2020 O VAL A 254 12451 13310 12875 296 -996 114 O ATOM 2021 CB VAL A 254 -3.687 27.887 41.125 1.00 84.91 C ANISOU 2021 CB VAL A 254 10249 11032 10981 91 -900 -37 C ATOM 2022 CG1 VAL A 254 -4.209 29.077 40.337 1.00 75.02 C ANISOU 2022 CG1 VAL A 254 8727 9888 9888 170 -1072 -88 C ATOM 2023 CG2 VAL A 254 -3.344 26.748 40.183 1.00 86.33 C ANISOU 2023 CG2 VAL A 254 10519 11186 11097 100 -1036 -49 C ATOM 2024 N ILE A 255 -3.253 29.699 43.763 1.00 90.54 N ANISOU 2024 N ILE A 255 11123 11773 11505 147 -567 15 N ATOM 2025 CA ILE A 255 -3.387 30.961 44.484 1.00 75.70 C ANISOU 2025 CA ILE A 255 9209 9907 9646 195 -515 -49 C ATOM 2026 C ILE A 255 -2.017 31.490 44.892 1.00 85.96 C ANISOU 2026 C ILE A 255 10695 11278 10686 260 -620 12 C ATOM 2027 O ILE A 255 -1.730 32.685 44.754 1.00 85.11 O ANISOU 2027 O ILE A 255 10533 11167 10636 303 -745 -22 O ATOM 2028 CB ILE A 255 -4.319 30.780 45.696 1.00 77.88 C ANISOU 2028 CB ILE A 255 9480 10139 9971 159 -206 -115 C ATOM 2029 CG1 ILE A 255 -5.752 30.523 45.220 1.00 68.69 C ANISOU 2029 CG1 ILE A 255 8051 8923 9125 82 -128 -173 C ATOM 2030 CG2 ILE A 255 -4.247 31.991 46.616 1.00 78.63 C ANISOU 2030 CG2 ILE A 255 9623 10254 9999 245 -145 -206 C ATOM 2031 CD1 ILE A 255 -6.716 30.179 46.327 1.00 67.29 C ANISOU 2031 CD1 ILE A 255 7832 8712 9021 46 201 -183 C ATOM 2032 N ILE A 256 -1.143 30.606 45.380 1.00 93.44 N ANISOU 2032 N ILE A 256 11853 12288 11361 265 -569 112 N ATOM 2033 CA ILE A 256 0.199 31.021 45.784 1.00 84.20 C ANISOU 2033 CA ILE A 256 10831 11235 9926 317 -682 177 C ATOM 2034 C ILE A 256 0.974 31.577 44.594 1.00 79.92 C ANISOU 2034 C ILE A 256 10206 10732 9427 353 -966 275 C ATOM 2035 O ILE A 256 1.632 32.619 44.697 1.00 89.59 O ANISOU 2035 O ILE A 256 11411 11985 10644 360 -1096 270 O ATOM 2036 CB ILE A 256 0.941 29.845 46.447 1.00 70.69 C ANISOU 2036 CB ILE A 256 9337 9621 7899 351 -557 305 C ATOM 2037 CG1 ILE A 256 0.547 29.734 47.922 1.00 69.51 C ANISOU 2037 CG1 ILE A 256 9283 9506 7619 371 -288 235 C ATOM 2038 CG2 ILE A 256 2.445 29.999 46.292 1.00 65.43 C ANISOU 2038 CG2 ILE A 256 8768 9119 6973 411 -752 439 C ATOM 2039 CD1 ILE A 256 0.804 28.370 48.525 1.00 67.27 C ANISOU 2039 CD1 ILE A 256 9175 9272 7112 421 -67 390 C ATOM 2040 N MET A 257 0.900 30.900 43.446 1.00 76.06 N ANISOU 2040 N MET A 257 9660 10243 8994 383 -1063 364 N ATOM 2041 CA MET A 257 1.677 31.328 42.287 1.00 87.58 C ANISOU 2041 CA MET A 257 11041 11782 10452 468 -1311 503 C ATOM 2042 C MET A 257 1.157 32.642 41.719 1.00 75.83 C ANISOU 2042 C MET A 257 9334 10236 9242 487 -1410 455 C ATOM 2043 O MET A 257 1.947 33.506 41.321 1.00 82.54 O ANISOU 2043 O MET A 257 10128 11124 10110 536 -1561 571 O ATOM 2044 CB MET A 257 1.664 30.237 41.217 1.00 86.52 C ANISOU 2044 CB MET A 257 10918 11681 10274 536 -1384 579 C ATOM 2045 CG MET A 257 2.347 28.950 41.647 1.00 88.81 C ANISOU 2045 CG MET A 257 11449 12005 10291 556 -1285 671 C ATOM 2046 SD MET A 257 2.341 27.702 40.348 1.00115.89 S ANISOU 2046 SD MET A 257 14926 15427 13679 653 -1382 711 S ATOM 2047 CE MET A 257 0.589 27.582 40.003 1.00111.16 C ANISOU 2047 CE MET A 257 14126 14670 13442 521 -1330 460 C ATOM 2048 N VAL A 258 -0.165 32.809 41.670 1.00 83.78 N ANISOU 2048 N VAL A 258 10200 11151 10481 458 -1313 310 N ATOM 2049 CA VAL A 258 -0.740 34.045 41.148 1.00 86.28 C ANISOU 2049 CA VAL A 258 10307 11416 11060 513 -1374 283 C ATOM 2050 C VAL A 258 -0.410 35.215 42.067 1.00 86.10 C ANISOU 2050 C VAL A 258 10339 11294 11081 480 -1328 219 C ATOM 2051 O VAL A 258 0.052 36.269 41.614 1.00 91.33 O ANISOU 2051 O VAL A 258 10919 11912 11868 529 -1447 301 O ATOM 2052 CB VAL A 258 -2.259 33.886 40.951 1.00 85.08 C ANISOU 2052 CB VAL A 258 9975 11227 11125 499 -1269 150 C ATOM 2053 CG1 VAL A 258 -2.948 35.238 40.982 1.00 91.05 C ANISOU 2053 CG1 VAL A 258 10566 11904 12125 559 -1229 96 C ATOM 2054 CG2 VAL A 258 -2.543 33.176 39.638 1.00 88.14 C ANISOU 2054 CG2 VAL A 258 10228 11724 11537 561 -1415 195 C ATOM 2055 N ILE A 259 -0.629 35.044 43.373 1.00 80.69 N ANISOU 2055 N ILE A 259 9795 10567 10295 406 -1152 72 N ATOM 2056 CA ILE A 259 -0.340 36.117 44.320 1.00 84.41 C ANISOU 2056 CA ILE A 259 10342 10950 10778 383 -1120 -53 C ATOM 2057 C ILE A 259 1.145 36.459 44.310 1.00 88.27 C ANISOU 2057 C ILE A 259 10917 11494 11129 350 -1304 49 C ATOM 2058 O ILE A 259 1.527 37.631 44.415 1.00 83.75 O ANISOU 2058 O ILE A 259 10316 10808 10697 327 -1386 1 O ATOM 2059 CB ILE A 259 -0.831 35.733 45.728 1.00 71.72 C ANISOU 2059 CB ILE A 259 8877 9351 9021 356 -892 -223 C ATOM 2060 CG1 ILE A 259 -2.351 35.880 45.807 1.00 64.46 C ANISOU 2060 CG1 ILE A 259 7820 8350 8321 393 -706 -326 C ATOM 2061 CG2 ILE A 259 -0.145 36.579 46.796 1.00 63.96 C ANISOU 2061 CG2 ILE A 259 8039 8346 7916 338 -910 -372 C ATOM 2062 CD1 ILE A 259 -2.907 35.678 47.195 1.00 85.39 C ANISOU 2062 CD1 ILE A 259 10584 11016 10844 410 -454 -468 C ATOM 2063 N ALA A 260 2.007 35.449 44.164 1.00 88.52 N ANISOU 2063 N ALA A 260 11042 11688 10902 348 -1366 199 N ATOM 2064 CA ALA A 260 3.440 35.716 44.091 1.00 89.20 C ANISOU 2064 CA ALA A 260 11168 11873 10851 324 -1544 336 C ATOM 2065 C ALA A 260 3.793 36.499 42.833 1.00 79.50 C ANISOU 2065 C ALA A 260 9756 10599 9853 373 -1719 520 C ATOM 2066 O ALA A 260 4.629 37.408 42.877 1.00 85.14 O ANISOU 2066 O ALA A 260 10427 11273 10648 317 -1841 571 O ATOM 2067 CB ALA A 260 4.228 34.408 44.150 1.00 69.18 C ANISOU 2067 CB ALA A 260 8767 9541 7977 358 -1546 491 C ATOM 2068 N PHE A 261 3.166 36.163 41.703 1.00 78.54 N ANISOU 2068 N PHE A 261 9509 10490 9842 480 -1733 626 N ATOM 2069 CA PHE A 261 3.393 36.923 40.477 1.00 81.40 C ANISOU 2069 CA PHE A 261 9678 10840 10409 582 -1871 828 C ATOM 2070 C PHE A 261 3.004 38.384 40.664 1.00 89.93 C ANISOU 2070 C PHE A 261 10655 11697 11816 551 -1843 742 C ATOM 2071 O PHE A 261 3.742 39.292 40.265 1.00 88.25 O ANISOU 2071 O PHE A 261 10350 11418 11761 552 -1945 901 O ATOM 2072 CB PHE A 261 2.610 36.304 39.319 1.00 87.37 C ANISOU 2072 CB PHE A 261 10315 11685 11198 729 -1887 897 C ATOM 2073 CG PHE A 261 2.898 36.937 37.987 1.00 84.00 C ANISOU 2073 CG PHE A 261 9688 11320 10907 899 -2021 1148 C ATOM 2074 CD1 PHE A 261 3.973 36.509 37.221 1.00 84.57 C ANISOU 2074 CD1 PHE A 261 9760 11579 10795 1012 -2155 1410 C ATOM 2075 CD2 PHE A 261 2.098 37.960 37.501 1.00 79.87 C ANISOU 2075 CD2 PHE A 261 8973 10690 10682 984 -1992 1153 C ATOM 2076 CE1 PHE A 261 4.247 37.089 35.995 1.00 86.85 C ANISOU 2076 CE1 PHE A 261 9853 11955 11189 1208 -2257 1680 C ATOM 2077 CE2 PHE A 261 2.363 38.545 36.274 1.00 93.53 C ANISOU 2077 CE2 PHE A 261 10510 12500 12527 1180 -2089 1426 C ATOM 2078 CZ PHE A 261 3.438 38.108 35.520 1.00104.97 C ANISOU 2078 CZ PHE A 261 11954 14146 13786 1294 -2220 1693 C ATOM 2079 N LEU A 262 1.844 38.628 41.276 1.00 86.73 N ANISOU 2079 N LEU A 262 10264 11160 11531 530 -1688 505 N ATOM 2080 CA LEU A 262 1.396 39.999 41.492 1.00 76.37 C ANISOU 2080 CA LEU A 262 8883 9609 10526 532 -1633 405 C ATOM 2081 C LEU A 262 2.324 40.736 42.451 1.00 81.93 C ANISOU 2081 C LEU A 262 9716 10184 11230 385 -1682 289 C ATOM 2082 O LEU A 262 2.727 41.872 42.186 1.00100.22 O ANISOU 2082 O LEU A 262 11956 12313 13812 365 -1745 351 O ATOM 2083 CB LEU A 262 -0.044 40.004 42.004 1.00 81.67 C ANISOU 2083 CB LEU A 262 9546 10204 11280 569 -1439 184 C ATOM 2084 CG LEU A 262 -1.082 39.571 40.966 1.00 88.24 C ANISOU 2084 CG LEU A 262 10180 11145 12201 704 -1413 277 C ATOM 2085 CD1 LEU A 262 -2.468 39.486 41.582 1.00 83.35 C ANISOU 2085 CD1 LEU A 262 9530 10486 11655 717 -1214 75 C ATOM 2086 CD2 LEU A 262 -1.076 40.523 39.777 1.00 83.08 C ANISOU 2086 CD2 LEU A 262 9318 10448 11800 859 -1495 490 C ATOM 2087 N ILE A 263 2.689 40.101 43.567 1.00 74.57 N ANISOU 2087 N ILE A 263 8971 9354 10007 283 -1656 122 N ATOM 2088 CA ILE A 263 3.634 40.721 44.493 1.00 86.98 C ANISOU 2088 CA ILE A 263 10653 10866 11529 142 -1742 -20 C ATOM 2089 C ILE A 263 4.936 41.074 43.784 1.00 95.38 C ANISOU 2089 C ILE A 263 11609 11965 12667 79 -1946 237 C ATOM 2090 O ILE A 263 5.576 42.083 44.105 1.00104.66 O ANISOU 2090 O ILE A 263 12768 12976 14021 -48 -2042 163 O ATOM 2091 CB ILE A 263 3.886 39.793 45.701 1.00 92.15 C ANISOU 2091 CB ILE A 263 11504 11725 11782 95 -1686 -183 C ATOM 2092 CG1 ILE A 263 2.613 39.620 46.530 1.00 95.25 C ANISOU 2092 CG1 ILE A 263 11988 12065 12136 162 -1458 -426 C ATOM 2093 CG2 ILE A 263 5.006 40.329 46.582 1.00 81.23 C ANISOU 2093 CG2 ILE A 263 10207 10369 10288 -44 -1826 -324 C ATOM 2094 CD1 ILE A 263 2.800 38.746 47.754 1.00 80.60 C ANISOU 2094 CD1 ILE A 263 10318 10418 9887 159 -1362 -553 C ATOM 2095 N CYS A 264 5.336 40.273 42.796 1.00 98.89 N ANISOU 2095 N CYS A 264 11969 12613 12991 169 -2012 542 N ATOM 2096 CA CYS A 264 6.626 40.478 42.147 1.00 91.67 C ANISOU 2096 CA CYS A 264 10942 11792 12098 140 -2186 834 C ATOM 2097 C CYS A 264 6.579 41.610 41.127 1.00104.17 C ANISOU 2097 C CYS A 264 12317 13171 14094 195 -2220 1038 C ATOM 2098 O CYS A 264 7.393 42.538 41.184 1.00116.83 O ANISOU 2098 O CYS A 264 13839 14635 15916 68 -2315 1106 O ATOM 2099 CB CYS A 264 7.088 39.183 41.480 1.00 93.95 C ANISOU 2099 CB CYS A 264 11239 12387 12072 265 -2227 1090 C ATOM 2100 SG CYS A 264 8.585 39.355 40.494 1.00 92.81 S ANISOU 2100 SG CYS A 264 10921 12410 11933 305 -2411 1526 S ATOM 2101 N TRP A 265 5.645 41.553 40.180 1.00106.36 N ANISOU 2101 N TRP A 265 12487 13433 14490 386 -2140 1150 N ATOM 2102 CA TRP A 265 5.670 42.477 39.053 1.00107.28 C ANISOU 2102 CA TRP A 265 12387 13434 14943 510 -2158 1433 C ATOM 2103 C TRP A 265 4.691 43.636 39.178 1.00104.10 C ANISOU 2103 C TRP A 265 11938 12701 14914 534 -2029 1285 C ATOM 2104 O TRP A 265 4.781 44.580 38.385 1.00106.41 O ANISOU 2104 O TRP A 265 12059 12840 15533 626 -2017 1527 O ATOM 2105 CB TRP A 265 5.405 41.723 37.744 1.00108.34 C ANISOU 2105 CB TRP A 265 12395 13826 14941 766 -2178 1706 C ATOM 2106 CG TRP A 265 6.506 40.774 37.394 1.00112.39 C ANISOU 2106 CG TRP A 265 12933 14633 15135 799 -2301 1929 C ATOM 2107 CD1 TRP A 265 6.427 39.415 37.323 1.00 97.72 C ANISOU 2107 CD1 TRP A 265 11193 13019 12915 872 -2315 1890 C ATOM 2108 CD2 TRP A 265 7.866 41.114 37.092 1.00125.04 C ANISOU 2108 CD2 TRP A 265 14438 16307 16766 766 -2414 2237 C ATOM 2109 NE1 TRP A 265 7.650 38.887 36.984 1.00104.43 N ANISOU 2109 NE1 TRP A 265 12045 14095 13539 918 -2423 2154 N ATOM 2110 CE2 TRP A 265 8.550 39.909 36.836 1.00127.80 C ANISOU 2110 CE2 TRP A 265 14857 16977 16724 855 -2488 2381 C ATOM 2111 CE3 TRP A 265 8.569 42.320 37.007 1.00116.15 C ANISOU 2111 CE3 TRP A 265 13161 14990 15981 666 -2451 2416 C ATOM 2112 CZ2 TRP A 265 9.903 39.876 36.502 1.00131.60 C ANISOU 2112 CZ2 TRP A 265 15309 17604 17091 852 -2503 2603 C ATOM 2113 CZ3 TRP A 265 9.910 42.285 36.676 1.00110.65 C ANISOU 2113 CZ3 TRP A 265 12355 14459 15226 645 -2564 2745 C ATOM 2114 CH2 TRP A 265 10.563 41.071 36.427 1.00115.32 C ANISOU 2114 CH2 TRP A 265 13045 15398 15373 746 -2576 2830 C ATOM 2115 N LEU A 266 3.769 43.605 40.146 1.00 96.48 N ANISOU 2115 N LEU A 266 11119 11626 13912 479 -1911 924 N ATOM 2116 CA LEU A 266 2.808 44.702 40.245 1.00 92.74 C ANISOU 2116 CA LEU A 266 10609 10848 13779 546 -1768 797 C ATOM 2117 C LEU A 266 3.448 45.984 40.763 1.00 97.60 C ANISOU 2117 C LEU A 266 11264 11109 14712 387 -1793 711 C ATOM 2118 O LEU A 266 3.218 47.045 40.156 1.00101.56 O ANISOU 2118 O LEU A 266 11639 11352 15598 482 -1724 864 O ATOM 2119 CB LEU A 266 1.603 44.284 41.093 1.00 95.46 C ANISOU 2119 CB LEU A 266 11081 11204 13986 568 -1616 467 C ATOM 2120 CG LEU A 266 0.306 45.034 40.803 1.00 92.64 C ANISOU 2120 CG LEU A 266 10621 10676 13901 748 -1444 431 C ATOM 2121 CD1 LEU A 266 -0.122 44.781 39.367 1.00 82.30 C ANISOU 2121 CD1 LEU A 266 9068 9562 12641 970 -1460 751 C ATOM 2122 CD2 LEU A 266 -0.790 44.631 41.777 1.00 85.18 C ANISOU 2122 CD2 LEU A 266 9794 9756 12814 756 -1284 117 C ATOM 2123 N PRO A 267 4.234 45.982 41.851 1.00111.08 N ANISOU 2123 N PRO A 267 13132 12778 16294 153 -1888 467 N ATOM 2124 CA PRO A 267 4.870 47.245 42.270 1.00108.29 C ANISOU 2124 CA PRO A 267 12796 12062 16288 -25 -1943 358 C ATOM 2125 C PRO A 267 5.715 47.897 41.188 1.00106.90 C ANISOU 2125 C PRO A 267 12395 11776 16447 -35 -2019 775 C ATOM 2126 O PRO A 267 5.685 49.126 41.052 1.00112.39 O ANISOU 2126 O PRO A 267 13036 12072 17593 -66 -1961 793 O ATOM 2127 CB PRO A 267 5.713 46.819 43.479 1.00102.91 C ANISOU 2127 CB PRO A 267 12283 11514 15303 -258 -2085 69 C ATOM 2128 CG PRO A 267 4.963 45.683 44.053 1.00108.29 C ANISOU 2128 CG PRO A 267 13108 12475 15562 -155 -1990 -106 C ATOM 2129 CD PRO A 267 4.436 44.925 42.862 1.00109.91 C ANISOU 2129 CD PRO A 267 13167 12886 15707 53 -1927 231 C ATOM 2130 N TYR A 268 6.471 47.113 40.414 1.00112.48 N ANISOU 2130 N TYR A 268 12969 12815 16952 10 -2128 1128 N ATOM 2131 CA TYR A 268 7.265 47.695 39.336 1.00120.56 C ANISOU 2131 CA TYR A 268 13753 13779 18275 45 -2175 1583 C ATOM 2132 C TYR A 268 6.372 48.368 38.306 1.00121.77 C ANISOU 2132 C TYR A 268 13756 13767 18745 319 -2005 1830 C ATOM 2133 O TYR A 268 6.648 49.490 37.877 1.00129.12 O ANISOU 2133 O TYR A 268 14553 14377 20129 310 -1952 2041 O ATOM 2134 CB TYR A 268 8.139 46.622 38.682 1.00132.65 C ANISOU 2134 CB TYR A 268 15186 15753 19463 113 -2302 1919 C ATOM 2135 CG TYR A 268 9.519 47.106 38.282 1.00145.07 C ANISOU 2135 CG TYR A 268 16568 17311 21240 -19 -2423 2264 C ATOM 2136 CD1 TYR A 268 10.423 47.545 39.240 1.00157.91 C ANISOU 2136 CD1 TYR A 268 18233 18797 22966 -355 -2555 2059 C ATOM 2137 CD2 TYR A 268 9.922 47.109 36.952 1.00149.75 C ANISOU 2137 CD2 TYR A 268 16924 18060 21916 202 -2410 2797 C ATOM 2138 CE1 TYR A 268 11.685 47.986 38.887 1.00165.01 C ANISOU 2138 CE1 TYR A 268 18918 19692 24084 -504 -2671 2385 C ATOM 2139 CE2 TYR A 268 11.185 47.548 36.588 1.00156.30 C ANISOU 2139 CE2 TYR A 268 17548 18890 22948 88 -2499 3157 C ATOM 2140 CZ TYR A 268 12.061 47.985 37.561 1.00164.13 C ANISOU 2140 CZ TYR A 268 18562 19723 24077 -284 -2630 2953 C ATOM 2141 OH TYR A 268 13.319 48.423 37.211 1.00165.31 O ANISOU 2141 OH TYR A 268 18470 19881 24460 -427 -2724 3320 O ATOM 2142 N ALA A 269 5.276 47.711 37.925 1.00119.58 N ANISOU 2142 N ALA A 269 13487 13699 18247 563 -1911 1805 N ATOM 2143 CA ALA A 269 4.385 48.275 36.917 1.00113.11 C ANISOU 2143 CA ALA A 269 12499 12809 17669 862 -1760 2046 C ATOM 2144 C ALA A 269 3.670 49.512 37.434 1.00118.16 C ANISOU 2144 C ALA A 269 13201 12982 18711 846 -1594 1840 C ATOM 2145 O ALA A 269 3.512 50.491 36.698 1.00139.40 O ANISOU 2145 O ALA A 269 15735 15443 21785 1010 -1473 2123 O ATOM 2146 CB ALA A 269 3.370 47.226 36.469 1.00100.18 C ANISOU 2146 CB ALA A 269 10840 11535 15687 1092 -1730 2011 C ATOM 2147 N GLY A 270 3.230 49.492 38.691 1.00100.82 N ANISOU 2147 N GLY A 270 11238 10643 16428 684 -1566 1364 N ATOM 2148 CA GLY A 270 2.460 50.598 39.225 1.00 99.96 C ANISOU 2148 CA GLY A 270 11222 10105 16653 712 -1395 1130 C ATOM 2149 C GLY A 270 3.309 51.815 39.534 1.00116.02 C ANISOU 2149 C GLY A 270 13288 11662 19133 502 -1418 1108 C ATOM 2150 O GLY A 270 2.945 52.942 39.187 1.00109.47 O ANISOU 2150 O GLY A 270 12403 10445 18744 619 -1257 1224 O ATOM 2151 N VAL A 271 4.447 51.599 40.194 1.00113.94 N ANISOU 2151 N VAL A 271 13105 11419 18770 188 -1616 959 N ATOM 2152 CA VAL A 271 5.350 52.706 40.496 1.00106.47 C ANISOU 2152 CA VAL A 271 12160 10030 18266 -71 -1680 915 C ATOM 2153 C VAL A 271 5.933 53.281 39.212 1.00119.92 C ANISOU 2153 C VAL A 271 13579 11626 20360 15 -1642 1494 C ATOM 2154 O VAL A 271 5.956 54.500 39.015 1.00132.25 O ANISOU 2154 O VAL A 271 15093 12696 22461 -4 -1524 1588 O ATOM 2155 CB VAL A 271 6.454 52.250 41.466 1.00 99.94 C ANISOU 2155 CB VAL A 271 11437 9341 17194 -419 -1928 634 C ATOM 2156 CG1 VAL A 271 7.616 53.224 41.440 1.00111.96 C ANISOU 2156 CG1 VAL A 271 12849 10510 19183 -709 -2044 726 C ATOM 2157 CG2 VAL A 271 5.896 52.124 42.875 1.00 88.77 C ANISOU 2157 CG2 VAL A 271 10319 7884 15526 -499 -1928 27 C ATOM 2158 N ALA A 272 6.401 52.414 38.313 1.00116.80 N ANISOU 2158 N ALA A 272 12997 11682 19700 134 -1722 1903 N ATOM 2159 CA ALA A 272 6.923 52.895 37.040 1.00125.62 C ANISOU 2159 CA ALA A 272 13827 12768 21134 281 -1666 2501 C ATOM 2160 C ALA A 272 5.853 53.631 36.245 1.00141.86 C ANISOU 2160 C ALA A 272 15790 14628 23484 636 -1409 2731 C ATOM 2161 O ALA A 272 6.133 54.660 35.617 1.00158.95 O ANISOU 2161 O ALA A 272 17792 16458 26146 697 -1282 3090 O ATOM 2162 CB ALA A 272 7.481 51.732 36.235 1.00134.39 C ANISOU 2162 CB ALA A 272 14787 14455 21821 419 -1788 2860 C ATOM 2163 N PHE A 273 4.619 53.121 36.263 1.00130.96 N ANISOU 2163 N PHE A 273 14491 13457 21811 880 -1318 2551 N ATOM 2164 CA PHE A 273 3.524 53.784 35.561 1.00134.10 C ANISOU 2164 CA PHE A 273 14786 13727 22439 1243 -1076 2750 C ATOM 2165 C PHE A 273 3.194 55.131 36.186 1.00148.06 C ANISOU 2165 C PHE A 273 16685 14852 24720 1163 -901 2542 C ATOM 2166 O PHE A 273 2.782 56.053 35.477 1.00156.81 O ANISOU 2166 O PHE A 273 17663 15704 26215 1420 -684 2863 O ATOM 2167 CB PHE A 273 2.297 52.872 35.548 1.00132.55 C ANISOU 2167 CB PHE A 273 14629 13929 21806 1472 -1045 2559 C ATOM 2168 CG PHE A 273 1.057 53.511 35.012 1.00139.80 C ANISOU 2168 CG PHE A 273 15447 14760 22911 1837 -806 2687 C ATOM 2169 CD1 PHE A 273 0.922 53.771 33.660 1.00145.81 C ANISOU 2169 CD1 PHE A 273 15928 15695 23777 2198 -711 3215 C ATOM 2170 CD2 PHE A 273 0.006 53.821 35.859 1.00148.32 C ANISOU 2170 CD2 PHE A 273 16699 15633 24022 1858 -669 2293 C ATOM 2171 CE1 PHE A 273 -0.231 54.350 33.164 1.00157.42 C ANISOU 2171 CE1 PHE A 273 17285 17136 25390 2565 -489 3349 C ATOM 2172 CE2 PHE A 273 -1.149 54.399 35.371 1.00158.07 C ANISOU 2172 CE2 PHE A 273 17823 16824 25412 2218 -441 2430 C ATOM 2173 CZ PHE A 273 -1.268 54.665 34.022 1.00161.04 C ANISOU 2173 CZ PHE A 273 17911 17380 25897 2569 -354 2958 C ATOM 2174 N TYR A 274 3.372 55.265 37.502 1.00148.88 N ANISOU 2174 N TYR A 274 17053 14693 24823 838 -986 2009 N ATOM 2175 CA TYR A 274 3.194 56.561 38.150 1.00147.69 C ANISOU 2175 CA TYR A 274 17061 13889 25167 735 -848 1758 C ATOM 2176 C TYR A 274 4.312 57.525 37.765 1.00155.80 C ANISOU 2176 C TYR A 274 17955 14487 26756 537 -859 2056 C ATOM 2177 O TYR A 274 4.061 58.714 37.533 1.00159.19 O ANISOU 2177 O TYR A 274 18373 14385 27727 630 -646 2185 O ATOM 2178 CB TYR A 274 3.132 56.374 39.666 1.00141.27 C ANISOU 2178 CB TYR A 274 16565 12973 24138 462 -963 1081 C ATOM 2179 CG TYR A 274 2.829 57.632 40.447 1.00143.64 C ANISOU 2179 CG TYR A 274 17084 12618 24875 386 -831 716 C ATOM 2180 CD1 TYR A 274 1.519 58.051 40.643 1.00139.57 C ANISOU 2180 CD1 TYR A 274 16693 11940 24397 689 -582 559 C ATOM 2181 CD2 TYR A 274 3.851 58.390 41.004 1.00154.31 C ANISOU 2181 CD2 TYR A 274 18516 13515 26599 14 -960 511 C ATOM 2182 CE1 TYR A 274 1.236 59.198 41.362 1.00151.38 C ANISOU 2182 CE1 TYR A 274 18418 12820 26277 654 -448 211 C ATOM 2183 CE2 TYR A 274 3.579 59.537 41.725 1.00164.18 C ANISOU 2183 CE2 TYR A 274 19994 14132 28257 -57 -850 128 C ATOM 2184 CZ TYR A 274 2.270 59.937 41.902 1.00161.68 C ANISOU 2184 CZ TYR A 274 19830 13646 27955 279 -586 -21 C ATOM 2185 OH TYR A 274 1.996 61.080 42.619 1.00156.35 O ANISOU 2185 OH TYR A 274 19408 12323 27673 243 -464 -413 O ATOM 2186 N ILE A 275 5.547 57.026 37.671 1.00148.24 N ANISOU 2186 N ILE A 275 16881 13748 25696 273 -1089 2201 N ATOM 2187 CA ILE A 275 6.699 57.824 37.258 1.00141.94 C ANISOU 2187 CA ILE A 275 15897 12610 25423 57 -1116 2542 C ATOM 2188 C ILE A 275 6.605 58.068 35.755 1.00153.12 C ANISOU 2188 C ILE A 275 17004 14133 27042 436 -918 3275 C ATOM 2189 O ILE A 275 7.461 58.726 35.154 1.00147.57 O ANISOU 2189 O ILE A 275 16083 13190 26796 355 -874 3716 O ATOM 2190 CB ILE A 275 8.020 57.130 37.651 1.00143.18 C ANISOU 2190 CB ILE A 275 16000 13055 25348 -316 -1426 2480 C ATOM 2191 CG1 ILE A 275 8.027 56.807 39.144 1.00139.39 C ANISOU 2191 CG1 ILE A 275 15823 12563 24578 -622 -1617 1754 C ATOM 2192 CG2 ILE A 275 9.227 58.007 37.361 1.00144.22 C ANISOU 2192 CG2 ILE A 275 15921 12808 26068 -601 -1466 2788 C ATOM 2193 CD1 ILE A 275 9.277 56.079 39.608 1.00102.07 C ANISOU 2193 CD1 ILE A 275 11044 8176 19563 -959 -1921 1672 C ATOM 2194 N PHE A 276 5.547 57.552 35.135 1.00182.29 N ANISOU 2194 N PHE A 276 20658 18203 30400 864 -793 3419 N ATOM 2195 CA PHE A 276 5.299 57.782 33.719 1.00199.93 C ANISOU 2195 CA PHE A 276 22606 20599 32761 1298 -598 4079 C ATOM 2196 C PHE A 276 3.852 58.205 33.483 1.00191.18 C ANISOU 2196 C PHE A 276 21537 19407 31694 1699 -339 4057 C ATOM 2197 O PHE A 276 3.314 58.012 32.389 1.00180.64 O ANISOU 2197 O PHE A 276 19989 18439 30205 2133 -218 4480 O ATOM 2198 CB PHE A 276 5.651 56.535 32.906 1.00204.83 C ANISOU 2198 CB PHE A 276 23044 21945 32837 1472 -757 4389 C ATOM 2199 CG PHE A 276 6.074 56.836 31.505 1.00214.59 C ANISOU 2199 CG PHE A 276 23981 23418 34136 1736 -609 5035 C ATOM 2200 CD1 PHE A 276 5.135 56.938 30.497 1.00228.05 C ANISOU 2200 CD1 PHE A 276 25634 25525 35489 2088 -367 5139 C ATOM 2201 CD2 PHE A 276 7.409 57.025 31.196 1.00210.46 C ANISOU 2201 CD2 PHE A 276 23290 22883 33792 1518 -668 5357 C ATOM 2202 CE1 PHE A 276 5.513 57.222 29.223 1.00231.75 C ANISOU 2202 CE1 PHE A 276 25930 26342 35783 2221 -189 5520 C ATOM 2203 CE2 PHE A 276 7.788 57.305 29.912 1.00214.17 C ANISOU 2203 CE2 PHE A 276 23549 23729 34099 1670 -460 5764 C ATOM 2204 CZ PHE A 276 6.838 57.413 28.940 1.00224.34 C ANISOU 2204 CZ PHE A 276 24829 25373 35036 2020 -219 5828 C ATOM 2205 N THR A 277 3.211 58.763 34.503 1.00187.33 N ANISOU 2205 N THR A 277 21316 18487 31372 1578 -256 3556 N ATOM 2206 CA THR A 277 1.860 59.291 34.394 1.00202.19 C ANISOU 2206 CA THR A 277 23247 20234 33343 1950 14 3524 C ATOM 2207 C THR A 277 1.799 60.589 35.183 1.00207.23 C ANISOU 2207 C THR A 277 24106 20077 34555 1787 179 3247 C ATOM 2208 O THR A 277 1.165 61.560 34.760 1.00213.43 O ANISOU 2208 O THR A 277 24854 20506 35735 2092 480 3487 O ATOM 2209 CB THR A 277 0.835 58.281 34.912 1.00202.66 C ANISOU 2209 CB THR A 277 23435 20749 32817 2046 -63 3108 C ATOM 2210 OG1 THR A 277 0.961 57.057 34.176 1.00197.49 O ANISOU 2210 OG1 THR A 277 22591 20784 31662 2164 -233 3333 O ATOM 2211 CG2 THR A 277 -0.573 58.820 34.759 1.00201.34 C ANISOU 2211 CG2 THR A 277 23270 20495 32733 2450 219 3115 C ATOM 2212 N HIS A 278 2.455 60.597 36.343 1.00191.21 N ANISOU 2212 N HIS A 278 22314 17777 32559 1323 -19 2727 N ATOM 2213 CA HIS A 278 2.776 61.826 37.054 1.00169.12 C ANISOU 2213 CA HIS A 278 19711 14189 30358 1069 64 2456 C ATOM 2214 C HIS A 278 4.277 62.049 36.927 1.00161.74 C ANISOU 2214 C HIS A 278 18637 13058 29759 660 -117 2644 C ATOM 2215 O HIS A 278 4.971 62.274 37.925 1.00140.02 O ANISOU 2215 O HIS A 278 16063 9993 27144 215 -311 2174 O ATOM 2216 CB HIS A 278 2.344 61.746 38.521 1.00156.26 C ANISOU 2216 CB HIS A 278 18456 12405 28511 869 -32 1672 C ATOM 2217 CG HIS A 278 0.859 61.769 38.719 1.00159.76 C ANISOU 2217 CG HIS A 278 19034 12922 28746 1266 197 1498 C ATOM 2218 ND1 HIS A 278 -0.019 61.146 37.858 1.00158.01 N ANISOU 2218 ND1 HIS A 278 18607 13240 28191 1684 313 1861 N ATOM 2219 CD2 HIS A 278 0.098 62.336 39.685 1.00170.82 C ANISOU 2219 CD2 HIS A 278 20741 13948 30216 1318 327 998 C ATOM 2220 CE1 HIS A 278 -1.256 61.332 38.283 1.00166.14 C ANISOU 2220 CE1 HIS A 278 19783 14230 29112 1959 507 1615 C ATOM 2221 NE2 HIS A 278 -1.213 62.051 39.390 1.00172.81 N ANISOU 2221 NE2 HIS A 278 20948 14524 30189 1762 533 1104 N ATOM 2222 N GLN A 279 4.782 61.978 35.698 1.00178.08 N ANISOU 2222 N GLN A 279 20370 15348 31946 824 -60 3338 N ATOM 2223 CA GLN A 279 6.216 61.925 35.461 1.00190.37 C ANISOU 2223 CA GLN A 279 21728 16905 33701 478 -247 3604 C ATOM 2224 C GLN A 279 6.869 63.286 35.670 1.00185.69 C ANISOU 2224 C GLN A 279 21138 15479 33939 178 -144 3635 C ATOM 2225 O GLN A 279 6.265 64.338 35.436 1.00217.26 O ANISOU 2225 O GLN A 279 25184 19096 38270 380 164 3703 O ATOM 2226 CB GLN A 279 6.512 61.421 34.046 1.00207.40 C ANISOU 2226 CB GLN A 279 23518 19588 35697 808 -192 4367 C ATOM 2227 CG GLN A 279 6.247 62.416 32.926 1.00222.15 C ANISOU 2227 CG GLN A 279 25172 21376 37859 1136 171 4897 C ATOM 2228 CD GLN A 279 7.024 62.081 31.665 1.00224.58 C ANISOU 2228 CD GLN A 279 25113 22281 37935 1267 190 5507 C ATOM 2229 OE1 GLN A 279 8.247 61.939 31.696 1.00223.14 O ANISOU 2229 OE1 GLN A 279 24785 22085 37912 959 15 5669 O ATOM 2230 NE2 GLN A 279 6.316 61.946 30.550 1.00225.49 N ANISOU 2230 NE2 GLN A 279 25088 22960 37627 1708 403 5809 N ATOM 2231 N GLY A 280 8.124 63.252 36.120 1.00145.34 N ANISOU 2231 N GLY A 280 15969 10272 28983 -322 -406 3509 N ATOM 2232 CA GLY A 280 8.942 64.437 36.262 1.00159.51 C ANISOU 2232 CA GLY A 280 17703 11463 31440 -674 -359 3512 C ATOM 2233 C GLY A 280 9.068 64.973 37.673 1.00177.47 C ANISOU 2233 C GLY A 280 20310 13207 33914 -1118 -527 2699 C ATOM 2234 O GLY A 280 9.934 65.824 37.916 1.00139.46 O ANISOU 2234 O GLY A 280 15444 8027 29518 -1489 -576 2599 O ATOM 2235 N SER A 281 8.249 64.492 38.610 1.00181.96 N ANISOU 2235 N SER A 281 21210 13805 34121 -1072 -621 2094 N ATOM 2236 CA SER A 281 8.156 65.086 39.941 1.00191.31 C ANISOU 2236 CA SER A 281 22752 14499 35439 -1382 -731 1284 C ATOM 2237 C SER A 281 9.365 64.788 40.819 1.00176.37 C ANISOU 2237 C SER A 281 20854 12671 33486 -1960 -1148 853 C ATOM 2238 O SER A 281 10.453 64.478 40.322 1.00184.76 O ANISOU 2238 O SER A 281 21599 13986 34617 -2187 -1306 1256 O ATOM 2239 CB SER A 281 6.884 64.605 40.646 1.00188.99 C ANISOU 2239 CB SER A 281 22789 14424 34594 -1079 -677 787 C ATOM 2240 OG SER A 281 5.769 65.413 40.309 1.00187.45 O ANISOU 2240 OG SER A 281 22711 13805 34708 -673 -297 909 O ATOM 2241 N ASP A 282 9.178 64.899 42.132 1.00149.43 N ANISOU 2241 N ASP A 282 17788 9087 29903 -2169 -1320 38 N ATOM 2242 CA ASP A 282 10.217 64.599 43.108 1.00139.55 C ANISOU 2242 CA ASP A 282 16562 7987 28474 -2675 -1732 -470 C ATOM 2243 C ASP A 282 10.086 63.139 43.523 1.00153.47 C ANISOU 2243 C ASP A 282 18373 10623 29315 -2557 -1932 -631 C ATOM 2244 O ASP A 282 9.045 62.727 44.047 1.00152.47 O ANISOU 2244 O ASP A 282 18522 10700 28711 -2262 -1844 -972 O ATOM 2245 CB ASP A 282 10.096 65.531 44.316 1.00145.92 C ANISOU 2245 CB ASP A 282 17736 8356 29350 -2874 -1781 -1263 C ATOM 2246 CG ASP A 282 11.212 65.336 45.330 1.00167.16 C ANISOU 2246 CG ASP A 282 20438 11242 31834 -3381 -2205 -1796 C ATOM 2247 OD1 ASP A 282 11.369 64.209 45.848 1.00173.01 O ANISOU 2247 OD1 ASP A 282 21183 12512 32042 -3441 -2480 -2026 O ATOM 2248 OD2 ASP A 282 11.930 66.321 45.617 1.00155.21 O ANISOU 2248 OD2 ASP A 282 18929 9367 30679 -3712 -2263 -1985 O ATOM 2249 N PHE A 283 11.143 62.361 43.292 1.00150.50 N ANISOU 2249 N PHE A 283 17724 10765 28694 -2775 -2180 -362 N ATOM 2250 CA PHE A 283 11.142 60.917 43.525 1.00128.26 C ANISOU 2250 CA PHE A 283 14913 8793 25027 -2649 -2343 -393 C ATOM 2251 C PHE A 283 12.391 60.554 44.317 1.00156.92 C ANISOU 2251 C PHE A 283 18466 12691 28467 -3108 -2740 -707 C ATOM 2252 O PHE A 283 13.486 60.485 43.751 1.00174.69 O ANISOU 2252 O PHE A 283 20380 15071 30922 -3334 -2867 -275 O ATOM 2253 CB PHE A 283 11.103 60.153 42.208 1.00118.57 C ANISOU 2253 CB PHE A 283 13402 8054 23597 -2323 -2202 388 C ATOM 2254 CG PHE A 283 9.805 60.272 41.477 1.00116.55 C ANISOU 2254 CG PHE A 283 13207 7721 23354 -1826 -1851 664 C ATOM 2255 CD1 PHE A 283 8.602 60.129 42.146 1.00162.47 C ANISOU 2255 CD1 PHE A 283 19340 13543 28848 -1587 -1739 208 C ATOM 2256 CD2 PHE A 283 9.786 60.526 40.118 1.00134.82 C ANISOU 2256 CD2 PHE A 283 15239 9998 25987 -1573 -1630 1398 C ATOM 2257 CE1 PHE A 283 7.401 60.233 41.472 1.00169.70 C ANISOU 2257 CE1 PHE A 283 20276 14433 29771 -1130 -1426 470 C ATOM 2258 CE2 PHE A 283 8.588 60.638 39.440 1.00164.44 C ANISOU 2258 CE2 PHE A 283 19022 13735 29724 -1096 -1322 1650 C ATOM 2259 CZ PHE A 283 7.394 60.488 40.117 1.00175.21 C ANISOU 2259 CZ PHE A 283 20686 15109 30775 -886 -1227 1181 C ATOM 2260 N GLY A 284 12.232 60.318 45.616 1.00168.04 N ANISOU 2260 N GLY A 284 20164 14219 29465 -3218 -2928 -1432 N ATOM 2261 CA GLY A 284 13.330 59.860 46.430 1.00172.83 C ANISOU 2261 CA GLY A 284 20702 15193 29772 -3591 -3309 -1753 C ATOM 2262 C GLY A 284 13.940 58.603 45.847 1.00174.03 C ANISOU 2262 C GLY A 284 20593 16104 29426 -3503 -3397 -1225 C ATOM 2263 O GLY A 284 13.230 57.695 45.408 1.00180.09 O ANISOU 2263 O GLY A 284 21410 17290 29725 -3111 -3227 -951 O ATOM 2264 N PRO A 285 15.272 58.547 45.782 1.00170.73 N ANISOU 2264 N PRO A 285 19877 15861 29131 -3863 -3657 -1053 N ATOM 2265 CA PRO A 285 15.926 57.300 45.348 1.00167.26 C ANISOU 2265 CA PRO A 285 19215 16181 28156 -3767 -3756 -595 C ATOM 2266 C PRO A 285 15.460 56.090 46.138 1.00165.03 C ANISOU 2266 C PRO A 285 19185 16506 27012 -3541 -3814 -926 C ATOM 2267 O PRO A 285 15.310 54.996 45.579 1.00174.63 O ANISOU 2267 O PRO A 285 20350 18242 27760 -3245 -3723 -521 O ATOM 2268 CB PRO A 285 17.420 57.593 45.563 1.00167.42 C ANISOU 2268 CB PRO A 285 18923 16249 28439 -4254 -4074 -573 C ATOM 2269 CG PRO A 285 17.475 58.865 46.386 1.00165.10 C ANISOU 2269 CG PRO A 285 18755 15271 28703 -4634 -4199 -1201 C ATOM 2270 CD PRO A 285 16.243 59.622 46.038 1.00164.75 C ANISOU 2270 CD PRO A 285 18949 14609 29038 -4368 -3858 -1231 C ATOM 2271 N ILE A 286 15.205 56.275 47.433 1.00149.57 N ANISOU 2271 N ILE A 286 17509 14477 24843 -3657 -3951 -1659 N ATOM 2272 CA ILE A 286 14.642 55.208 48.252 1.00128.35 C ANISOU 2272 CA ILE A 286 15081 12315 21371 -3408 -3955 -1976 C ATOM 2273 C ILE A 286 13.224 54.875 47.792 1.00122.94 C ANISOU 2273 C ILE A 286 14590 11585 20536 -2958 -3608 -1821 C ATOM 2274 O ILE A 286 12.813 53.709 47.800 1.00126.88 O ANISOU 2274 O ILE A 286 15163 12598 20449 -2684 -3529 -1695 O ATOM 2275 CB ILE A 286 14.701 55.610 49.740 1.00117.09 C ANISOU 2275 CB ILE A 286 13901 10808 19780 -3610 -4173 -2797 C ATOM 2276 CG1 ILE A 286 16.035 55.185 50.365 1.00118.95 C ANISOU 2276 CG1 ILE A 286 13951 11526 19719 -3923 -4545 -2933 C ATOM 2277 CG2 ILE A 286 13.540 55.012 50.523 1.00142.96 C ANISOU 2277 CG2 ILE A 286 17539 14303 22478 -3252 -4015 -3168 C ATOM 2278 CD1 ILE A 286 17.276 55.722 49.669 1.00141.04 C ANISOU 2278 CD1 ILE A 286 16345 14175 23071 -4306 -4722 -2555 C ATOM 2279 N PHE A 287 12.460 55.887 47.368 1.00126.53 N ANISOU 2279 N PHE A 287 15115 11427 21534 -2874 -3390 -1813 N ATOM 2280 CA PHE A 287 11.157 55.630 46.761 1.00131.81 C ANISOU 2280 CA PHE A 287 15891 12074 22117 -2446 -3062 -1581 C ATOM 2281 C PHE A 287 11.308 54.820 45.476 1.00130.44 C ANISOU 2281 C PHE A 287 15455 12280 21825 -2243 -2968 -859 C ATOM 2282 O PHE A 287 10.485 53.943 45.185 1.00127.17 O ANISOU 2282 O PHE A 287 15110 12201 21007 -1914 -2812 -709 O ATOM 2283 CB PHE A 287 10.433 56.960 46.507 1.00169.90 C ANISOU 2283 CB PHE A 287 20806 16163 27586 -2392 -2847 -1664 C ATOM 2284 CG PHE A 287 9.298 56.878 45.511 1.00175.49 C ANISOU 2284 CG PHE A 287 21490 16826 28360 -1972 -2512 -1238 C ATOM 2285 CD1 PHE A 287 9.540 56.986 44.148 1.00167.92 C ANISOU 2285 CD1 PHE A 287 20235 15840 27725 -1873 -2399 -557 C ATOM 2286 CD2 PHE A 287 7.988 56.732 45.940 1.00171.67 C ANISOU 2286 CD2 PHE A 287 21260 16346 27619 -1661 -2311 -1513 C ATOM 2287 CE1 PHE A 287 8.508 56.915 43.236 1.00158.10 C ANISOU 2287 CE1 PHE A 287 18951 14610 26511 -1471 -2115 -186 C ATOM 2288 CE2 PHE A 287 6.950 56.668 45.028 1.00163.78 C ANISOU 2288 CE2 PHE A 287 20204 15345 26682 -1285 -2025 -1132 C ATOM 2289 CZ PHE A 287 7.212 56.761 43.675 1.00159.35 C ANISOU 2289 CZ PHE A 287 19347 14782 26416 -1190 -1938 -482 C ATOM 2290 N MET A 288 12.365 55.097 44.701 1.00144.24 N ANISOU 2290 N MET A 288 19491 13016 22298 1612 -6749 -97 N ATOM 2291 CA MET A 288 12.673 54.353 43.479 1.00165.07 C ANISOU 2291 CA MET A 288 21980 15868 24870 1231 -6601 132 C ATOM 2292 C MET A 288 13.093 52.913 43.713 1.00155.78 C ANISOU 2292 C MET A 288 20753 14952 23485 1167 -6053 139 C ATOM 2293 O MET A 288 13.129 52.142 42.750 1.00141.15 O ANISOU 2293 O MET A 288 18741 13305 21584 906 -5870 269 O ATOM 2294 CB MET A 288 13.839 54.973 42.716 1.00173.34 C ANISOU 2294 CB MET A 288 23111 16869 25882 904 -7009 433 C ATOM 2295 CG MET A 288 13.640 56.352 42.195 1.00176.49 C ANISOU 2295 CG MET A 288 23551 17027 26478 845 -7618 517 C ATOM 2296 SD MET A 288 12.852 56.372 40.577 1.00182.80 S ANISOU 2296 SD MET A 288 24105 17927 27422 536 -7742 652 S ATOM 2297 CE MET A 288 14.011 55.417 39.599 1.00177.58 C ANISOU 2297 CE MET A 288 23345 17601 26526 97 -7527 957 C ATOM 2298 N THR A 289 13.542 52.547 44.909 1.00158.34 N ANISOU 2298 N THR A 289 21215 15270 23677 1371 -5825 26 N ATOM 2299 CA THR A 289 14.042 51.190 45.086 1.00148.21 C ANISOU 2299 CA THR A 289 19897 14218 22200 1279 -5355 51 C ATOM 2300 C THR A 289 13.014 50.298 45.793 1.00127.74 C ANISOU 2300 C THR A 289 17200 11740 19595 1512 -4904 -176 C ATOM 2301 O THR A 289 13.333 49.189 46.227 1.00132.96 O ANISOU 2301 O THR A 289 17856 12558 20104 1500 -4517 -197 O ATOM 2302 CB THR A 289 15.413 51.208 45.789 1.00145.27 C ANISOU 2302 CB THR A 289 19739 13797 21662 1266 -5387 130 C ATOM 2303 OG1 THR A 289 16.308 52.071 45.068 1.00118.67 O ANISOU 2303 OG1 THR A 289 16446 10340 18304 1030 -5831 362 O ATOM 2304 CG2 THR A 289 16.058 49.825 45.776 1.00163.00 C ANISOU 2304 CG2 THR A 289 21944 16278 23712 1118 -4966 180 C ATOM 2305 N ILE A 290 11.755 50.715 45.811 1.00123.76 N ANISOU 2305 N ILE A 290 16591 11182 19250 1695 -4954 -335 N ATOM 2306 CA ILE A 290 10.692 49.965 46.478 1.00139.78 C ANISOU 2306 CA ILE A 290 18503 13339 21267 1916 -4556 -546 C ATOM 2307 C ILE A 290 10.114 48.831 45.624 1.00137.50 C ANISOU 2307 C ILE A 290 17995 13273 20977 1727 -4231 -486 C ATOM 2308 O ILE A 290 9.892 47.731 46.153 1.00131.26 O ANISOU 2308 O ILE A 290 17146 12649 20077 1780 -3819 -554 O ATOM 2309 CB ILE A 290 9.597 50.935 46.937 1.00134.99 C ANISOU 2309 CB ILE A 290 17874 12596 20818 2221 -4761 -766 C ATOM 2310 CG1 ILE A 290 10.194 51.947 47.912 1.00128.87 C ANISOU 2310 CG1 ILE A 290 17322 11610 20033 2444 -5061 -848 C ATOM 2311 CG2 ILE A 290 8.442 50.191 47.546 1.00127.37 C ANISOU 2311 CG2 ILE A 290 16757 11805 19831 2429 -4362 -970 C ATOM 2312 CD1 ILE A 290 9.169 52.825 48.566 1.00120.44 C ANISOU 2312 CD1 ILE A 290 16237 10432 19094 2799 -5244 -1114 C ATOM 2313 N PRO A 291 9.813 49.034 44.334 1.00134.99 N ANISOU 2313 N PRO A 291 17546 12964 20778 1509 -4405 -361 N ATOM 2314 CA PRO A 291 9.437 47.872 43.509 1.00131.14 C ANISOU 2314 CA PRO A 291 16863 12692 20272 1316 -4095 -288 C ATOM 2315 C PRO A 291 10.611 46.970 43.178 1.00126.54 C ANISOU 2315 C PRO A 291 16306 12257 19517 1072 -3943 -123 C ATOM 2316 O PRO A 291 10.447 45.745 43.112 1.00132.24 O ANISOU 2316 O PRO A 291 16921 13161 20163 1016 -3587 -129 O ATOM 2317 CB PRO A 291 8.845 48.519 42.252 1.00132.31 C ANISOU 2317 CB PRO A 291 16883 12786 20604 1164 -4381 -206 C ATOM 2318 CG PRO A 291 9.434 49.870 42.201 1.00133.01 C ANISOU 2318 CG PRO A 291 17124 12657 20756 1149 -4868 -139 C ATOM 2319 CD PRO A 291 9.546 50.298 43.625 1.00146.78 C ANISOU 2319 CD PRO A 291 19041 14274 22454 1465 -4876 -316 C ATOM 2320 N ALA A 292 11.796 47.549 42.963 1.00127.77 N ANISOU 2320 N ALA A 292 16597 12342 19608 925 -4224 24 N ATOM 2321 CA ALA A 292 12.978 46.751 42.651 1.00124.01 C ANISOU 2321 CA ALA A 292 16143 12022 18955 701 -4106 167 C ATOM 2322 C ALA A 292 13.288 45.752 43.756 1.00119.19 C ANISOU 2322 C ALA A 292 15612 11482 18193 838 -3735 58 C ATOM 2323 O ALA A 292 13.871 44.696 43.491 1.00112.98 O ANISOU 2323 O ALA A 292 14779 10867 17281 685 -3521 117 O ATOM 2324 CB ALA A 292 14.175 47.669 42.407 1.00123.82 C ANISOU 2324 CB ALA A 292 16264 11904 18878 551 -4490 333 C ATOM 2325 N PHE A 293 12.911 46.069 44.995 1.00122.72 N ANISOU 2325 N PHE A 293 16172 11805 18649 1125 -3671 -108 N ATOM 2326 CA PHE A 293 13.040 45.118 46.094 1.00119.55 C ANISOU 2326 CA PHE A 293 15832 11478 18114 1260 -3312 -217 C ATOM 2327 C PHE A 293 12.227 43.858 45.818 1.00122.82 C ANISOU 2327 C PHE A 293 16050 12087 18530 1215 -2954 -254 C ATOM 2328 O PHE A 293 12.770 42.748 45.771 1.00120.70 O ANISOU 2328 O PHE A 293 15765 11954 18143 1088 -2730 -208 O ATOM 2329 CB PHE A 293 12.603 45.797 47.395 1.00120.17 C ANISOU 2329 CB PHE A 293 16031 11414 18213 1586 -3334 -397 C ATOM 2330 CG PHE A 293 12.258 44.848 48.508 1.00118.43 C ANISOU 2330 CG PHE A 293 15809 11301 17888 1749 -2943 -533 C ATOM 2331 CD1 PHE A 293 13.244 44.329 49.326 1.00126.63 C ANISOU 2331 CD1 PHE A 293 17005 12344 18764 1752 -2801 -525 C ATOM 2332 CD2 PHE A 293 10.940 44.507 48.760 1.00129.84 C ANISOU 2332 CD2 PHE A 293 17093 12847 19394 1894 -2732 -664 C ATOM 2333 CE1 PHE A 293 12.922 43.470 50.361 1.00137.47 C ANISOU 2333 CE1 PHE A 293 18376 13818 20040 1882 -2462 -637 C ATOM 2334 CE2 PHE A 293 10.615 43.646 49.788 1.00143.13 C ANISOU 2334 CE2 PHE A 293 18763 14653 20968 2021 -2390 -768 C ATOM 2335 CZ PHE A 293 11.608 43.126 50.589 1.00141.55 C ANISOU 2335 CZ PHE A 293 18722 14452 20609 2009 -2259 -750 C ATOM 2336 N PHE A 294 10.916 44.020 45.608 1.00136.14 N ANISOU 2336 N PHE A 294 17586 13786 20356 1317 -2917 -338 N ATOM 2337 CA PHE A 294 10.044 42.872 45.370 1.00125.81 C ANISOU 2337 CA PHE A 294 16088 12652 19062 1285 -2595 -366 C ATOM 2338 C PHE A 294 10.460 42.098 44.126 1.00 98.72 C ANISOU 2338 C PHE A 294 12538 9353 15618 996 -2568 -213 C ATOM 2339 O PHE A 294 10.490 40.862 44.139 1.00 92.89 O ANISOU 2339 O PHE A 294 11730 8759 14806 926 -2299 -204 O ATOM 2340 CB PHE A 294 8.590 43.332 45.245 1.00129.40 C ANISOU 2340 CB PHE A 294 16399 13090 19678 1433 -2609 -473 C ATOM 2341 CG PHE A 294 7.938 43.648 46.560 1.00119.49 C ANISOU 2341 CG PHE A 294 15190 11807 18403 1740 -2509 -664 C ATOM 2342 CD1 PHE A 294 7.611 42.632 47.445 1.00106.18 C ANISOU 2342 CD1 PHE A 294 13467 10269 16606 1827 -2152 -735 C ATOM 2343 CD2 PHE A 294 7.640 44.957 46.906 1.00103.27 C ANISOU 2343 CD2 PHE A 294 13208 9592 16440 1939 -2789 -776 C ATOM 2344 CE1 PHE A 294 7.009 42.915 48.657 1.00100.57 C ANISOU 2344 CE1 PHE A 294 12779 9579 15855 2103 -2056 -911 C ATOM 2345 CE2 PHE A 294 7.035 45.248 48.116 1.00102.63 C ANISOU 2345 CE2 PHE A 294 13150 9517 16327 2239 -2703 -974 C ATOM 2346 CZ PHE A 294 6.720 44.225 48.992 1.00103.91 C ANISOU 2346 CZ PHE A 294 13262 9860 16358 2319 -2324 -1040 C ATOM 2347 N ALA A 295 10.782 42.802 43.039 1.00 94.04 N ANISOU 2347 N ALA A 295 11915 8722 15095 826 -2862 -93 N ATOM 2348 CA ALA A 295 11.145 42.116 41.803 1.00 92.65 C ANISOU 2348 CA ALA A 295 11600 8704 14897 559 -2851 42 C ATOM 2349 C ALA A 295 12.461 41.360 41.950 1.00111.35 C ANISOU 2349 C ALA A 295 14056 11175 17078 435 -2768 100 C ATOM 2350 O ALA A 295 12.585 40.222 41.482 1.00 89.81 O ANISOU 2350 O ALA A 295 11214 8614 14295 314 -2584 124 O ATOM 2351 CB ALA A 295 11.226 43.115 40.650 1.00 93.19 C ANISOU 2351 CB ALA A 295 11616 8728 15066 392 -3205 167 C ATOM 2352 N LYS A 296 13.454 41.970 42.599 1.00117.31 N ANISOU 2352 N LYS A 296 15010 11826 17736 470 -2914 116 N ATOM 2353 CA LYS A 296 14.752 41.314 42.721 1.00106.48 C ANISOU 2353 CA LYS A 296 13725 10548 16184 350 -2857 166 C ATOM 2354 C LYS A 296 14.699 40.120 43.665 1.00100.31 C ANISOU 2354 C LYS A 296 12979 9818 15317 459 -2514 54 C ATOM 2355 O LYS A 296 15.416 39.135 43.452 1.00100.13 O ANISOU 2355 O LYS A 296 12935 9929 15181 333 -2401 76 O ATOM 2356 CB LYS A 296 15.812 42.320 43.176 1.00106.97 C ANISOU 2356 CB LYS A 296 13998 10474 16171 359 -3115 222 C ATOM 2357 CG LYS A 296 16.300 43.240 42.061 1.00119.05 C ANISOU 2357 CG LYS A 296 15487 12019 17726 148 -3478 392 C ATOM 2358 CD LYS A 296 17.155 44.379 42.597 1.00134.77 C ANISOU 2358 CD LYS A 296 17694 13836 19677 182 -3772 453 C ATOM 2359 CE LYS A 296 17.698 45.246 41.468 1.00140.30 C ANISOU 2359 CE LYS A 296 18347 14577 20386 -67 -4152 654 C ATOM 2360 NZ LYS A 296 18.686 44.509 40.630 1.00149.84 N ANISOU 2360 NZ LYS A 296 19455 16051 21426 -330 -4115 769 N ATOM 2361 N THR A 297 13.859 40.172 44.701 1.00 89.85 N ANISOU 2361 N THR A 297 11697 8402 14040 686 -2360 -68 N ATOM 2362 CA THR A 297 13.751 39.036 45.609 1.00 89.31 C ANISOU 2362 CA THR A 297 11650 8394 13888 767 -2047 -155 C ATOM 2363 C THR A 297 13.115 37.817 44.945 1.00115.12 C ANISOU 2363 C THR A 297 14717 11829 17195 661 -1848 -142 C ATOM 2364 O THR A 297 13.206 36.712 45.493 1.00 87.95 O ANISOU 2364 O THR A 297 11283 8456 13678 664 -1627 -182 O ATOM 2365 CB THR A 297 12.964 39.442 46.860 1.00 90.78 C ANISOU 2365 CB THR A 297 11907 8483 14100 1029 -1941 -283 C ATOM 2366 OG1 THR A 297 13.463 40.693 47.345 1.00100.79 O ANISOU 2366 OG1 THR A 297 13351 9583 15364 1142 -2178 -299 O ATOM 2367 CG2 THR A 297 13.124 38.409 47.965 1.00 90.29 C ANISOU 2367 CG2 THR A 297 11915 8474 13918 1095 -1660 -350 C ATOM 2368 N SER A 298 12.506 37.978 43.768 1.00115.27 N ANISOU 2368 N SER A 298 14557 11907 17333 559 -1941 -83 N ATOM 2369 CA SER A 298 11.920 36.845 43.059 1.00 88.12 C ANISOU 2369 CA SER A 298 10923 8617 13940 459 -1779 -65 C ATOM 2370 C SER A 298 12.958 35.869 42.534 1.00 94.18 C ANISOU 2370 C SER A 298 11672 9517 14594 281 -1765 -21 C ATOM 2371 O SER A 298 12.575 34.851 41.954 1.00103.33 O ANISOU 2371 O SER A 298 12676 10798 15787 203 -1652 -14 O ATOM 2372 CB SER A 298 11.058 37.330 41.896 1.00 88.66 C ANISOU 2372 CB SER A 298 10813 8709 14167 394 -1899 -13 C ATOM 2373 OG SER A 298 11.861 37.673 40.782 1.00 94.77 O ANISOU 2373 OG SER A 298 11550 9543 14917 197 -2125 93 O ATOM 2374 N ALA A 299 14.250 36.154 42.688 1.00 97.32 N ANISOU 2374 N ALA A 299 12215 9899 14861 220 -1892 4 N ATOM 2375 CA ALA A 299 15.264 35.148 42.415 1.00 85.24 C ANISOU 2375 CA ALA A 299 10681 8502 13204 88 -1859 7 C ATOM 2376 C ALA A 299 15.385 34.138 43.544 1.00 84.69 C ANISOU 2376 C ALA A 299 10712 8404 13062 176 -1637 -81 C ATOM 2377 O ALA A 299 16.059 33.116 43.373 1.00100.87 O ANISOU 2377 O ALA A 299 12744 10554 15027 84 -1595 -104 O ATOM 2378 CB ALA A 299 16.621 35.810 42.166 1.00 84.01 C ANISOU 2378 CB ALA A 299 10637 8361 12923 -18 -2079 68 C ATOM 2379 N VAL A 300 14.740 34.392 44.678 1.00 85.00 N ANISOU 2379 N VAL A 300 10845 8321 13130 350 -1510 -135 N ATOM 2380 CA VAL A 300 14.819 33.533 45.850 1.00 89.62 C ANISOU 2380 CA VAL A 300 11531 8879 13640 427 -1309 -204 C ATOM 2381 C VAL A 300 13.517 32.769 46.075 1.00 92.98 C ANISOU 2381 C VAL A 300 11817 9358 14155 481 -1106 -225 C ATOM 2382 O VAL A 300 13.529 31.548 46.235 1.00 91.64 O ANISOU 2382 O VAL A 300 11609 9253 13957 423 -984 -236 O ATOM 2383 CB VAL A 300 15.211 34.346 47.104 1.00 92.90 C ANISOU 2383 CB VAL A 300 12169 9146 13984 579 -1313 -250 C ATOM 2384 CG1 VAL A 300 15.032 33.511 48.360 1.00 92.88 C ANISOU 2384 CG1 VAL A 300 12245 9129 13916 666 -1088 -316 C ATOM 2385 CG2 VAL A 300 16.649 34.825 46.985 1.00 93.08 C ANISOU 2385 CG2 VAL A 300 12347 9124 13897 504 -1495 -219 C ATOM 2386 N TYR A 301 12.381 33.468 46.085 1.00 99.36 N ANISOU 2386 N TYR A 301 12541 10139 15071 590 -1086 -230 N ATOM 2387 CA TYR A 301 11.120 32.793 46.366 1.00 99.61 C ANISOU 2387 CA TYR A 301 12436 10239 15174 645 -890 -243 C ATOM 2388 C TYR A 301 10.484 32.158 45.135 1.00109.01 C ANISOU 2388 C TYR A 301 13410 11532 16479 523 -894 -185 C ATOM 2389 O TYR A 301 9.552 31.362 45.286 1.00115.91 O ANISOU 2389 O TYR A 301 14163 12473 17404 534 -737 -176 O ATOM 2390 CB TYR A 301 10.121 33.747 47.043 1.00 89.41 C ANISOU 2390 CB TYR A 301 11140 8898 13934 839 -848 -300 C ATOM 2391 CG TYR A 301 9.699 34.963 46.244 1.00 95.48 C ANISOU 2391 CG TYR A 301 11848 9608 14821 874 -1036 -294 C ATOM 2392 CD1 TYR A 301 8.697 34.880 45.286 1.00109.40 C ANISOU 2392 CD1 TYR A 301 13410 11432 16724 828 -1037 -259 C ATOM 2393 CD2 TYR A 301 10.270 36.205 46.482 1.00108.42 C ANISOU 2393 CD2 TYR A 301 13634 11119 16442 955 -1229 -321 C ATOM 2394 CE1 TYR A 301 8.301 35.992 44.568 1.00111.87 C ANISOU 2394 CE1 TYR A 301 13672 11679 17154 850 -1225 -254 C ATOM 2395 CE2 TYR A 301 9.876 37.322 45.774 1.00 91.29 C ANISOU 2395 CE2 TYR A 301 11415 8880 14391 977 -1437 -310 C ATOM 2396 CZ TYR A 301 8.895 37.209 44.816 1.00 91.56 C ANISOU 2396 CZ TYR A 301 11249 8976 14562 920 -1433 -279 C ATOM 2397 OH TYR A 301 8.504 38.316 44.104 1.00 92.37 O ANISOU 2397 OH TYR A 301 11306 8998 14791 930 -1658 -268 O ATOM 2398 N ASN A 302 10.956 32.473 43.929 1.00 98.68 N ANISOU 2398 N ASN A 302 12041 10248 15206 404 -1073 -138 N ATOM 2399 CA ASN A 302 10.471 31.740 42.764 1.00 97.67 C ANISOU 2399 CA ASN A 302 11708 10229 15172 285 -1076 -90 C ATOM 2400 C ASN A 302 11.025 30.317 42.753 1.00 97.70 C ANISOU 2400 C ASN A 302 11697 10315 15110 190 -1013 -98 C ATOM 2401 O ASN A 302 10.285 29.383 42.424 1.00105.62 O ANISOU 2401 O ASN A 302 12556 11383 16192 156 -926 -78 O ATOM 2402 CB ASN A 302 10.818 32.462 41.459 1.00 87.47 C ANISOU 2402 CB ASN A 302 10339 8972 13925 174 -1290 -36 C ATOM 2403 CG ASN A 302 9.722 33.401 41.005 1.00 96.65 C ANISOU 2403 CG ASN A 302 11401 10085 15237 228 -1342 -13 C ATOM 2404 OD1 ASN A 302 8.794 33.698 41.755 1.00101.30 O ANISOU 2404 OD1 ASN A 302 11999 10608 15881 375 -1231 -57 O ATOM 2405 ND2 ASN A 302 9.820 33.872 39.768 1.00106.18 N ANISOU 2405 ND2 ASN A 302 12503 11337 16504 107 -1519 51 N ATOM 2406 N PRO A 303 12.305 30.091 43.080 1.00 97.34 N ANISOU 2406 N PRO A 303 11795 10263 14927 145 -1072 -130 N ATOM 2407 CA PRO A 303 12.743 28.701 43.277 1.00 88.95 C ANISOU 2407 CA PRO A 303 10733 9253 13809 80 -1016 -162 C ATOM 2408 C PRO A 303 12.096 28.034 44.477 1.00 93.03 C ANISOU 2408 C PRO A 303 11300 9721 14325 156 -828 -172 C ATOM 2409 O PRO A 303 11.920 26.811 44.468 1.00 83.85 O ANISOU 2409 O PRO A 303 10072 8603 13183 97 -783 -168 O ATOM 2410 CB PRO A 303 14.262 28.829 43.452 1.00 82.38 C ANISOU 2410 CB PRO A 303 10062 8413 12826 33 -1130 -205 C ATOM 2411 CG PRO A 303 14.607 30.093 42.762 1.00 93.30 C ANISOU 2411 CG PRO A 303 11443 9803 14204 9 -1288 -164 C ATOM 2412 CD PRO A 303 13.459 31.009 43.025 1.00 99.11 C ANISOU 2412 CD PRO A 303 12155 10450 15051 120 -1233 -132 C ATOM 2413 N VAL A 304 11.731 28.793 45.511 1.00 97.27 N ANISOU 2413 N VAL A 304 11944 10179 14836 283 -734 -184 N ATOM 2414 CA VAL A 304 11.076 28.194 46.669 1.00 85.95 C ANISOU 2414 CA VAL A 304 10535 8741 13380 346 -551 -185 C ATOM 2415 C VAL A 304 9.682 27.703 46.297 1.00 89.17 C ANISOU 2415 C VAL A 304 10737 9230 13914 340 -455 -129 C ATOM 2416 O VAL A 304 9.284 26.587 46.647 1.00106.90 O ANISOU 2416 O VAL A 304 12930 11523 16166 288 -366 -92 O ATOM 2417 CB VAL A 304 11.031 29.192 47.839 1.00 86.93 C ANISOU 2417 CB VAL A 304 10807 8791 13433 500 -483 -229 C ATOM 2418 CG1 VAL A 304 10.058 28.718 48.899 1.00 88.28 C ANISOU 2418 CG1 VAL A 304 10940 9016 13587 570 -286 -220 C ATOM 2419 CG2 VAL A 304 12.418 29.364 48.435 1.00109.62 C ANISOU 2419 CG2 VAL A 304 13901 11576 16171 497 -549 -274 C ATOM 2420 N ILE A 305 8.924 28.524 45.573 1.00103.07 N ANISOU 2420 N ILE A 305 12379 11003 15781 385 -488 -113 N ATOM 2421 CA ILE A 305 7.571 28.135 45.188 1.00 88.13 C ANISOU 2421 CA ILE A 305 10288 9184 14013 386 -397 -61 C ATOM 2422 C ILE A 305 7.609 27.065 44.104 1.00 87.15 C ANISOU 2422 C ILE A 305 10030 9115 13966 244 -465 -11 C ATOM 2423 O ILE A 305 6.957 26.021 44.216 1.00 98.59 O ANISOU 2423 O ILE A 305 11383 10617 15461 200 -385 42 O ATOM 2424 CB ILE A 305 6.767 29.371 44.740 1.00 98.43 C ANISOU 2424 CB ILE A 305 11514 10469 15415 482 -428 -74 C ATOM 2425 CG1 ILE A 305 6.314 30.179 45.959 1.00 90.49 C ANISOU 2425 CG1 ILE A 305 10590 9443 14350 656 -329 -137 C ATOM 2426 CG2 ILE A 305 5.572 28.962 43.894 1.00 93.38 C ANISOU 2426 CG2 ILE A 305 10656 9898 14925 445 -386 -15 C ATOM 2427 CD1 ILE A 305 6.388 31.668 45.770 1.00 90.97 C ANISOU 2427 CD1 ILE A 305 10706 9414 14444 762 -464 -196 C ATOM 2428 N TYR A 306 8.387 27.296 43.050 1.00 86.01 N ANISOU 2428 N TYR A 306 9873 8974 13834 169 -630 -24 N ATOM 2429 CA TYR A 306 8.310 26.482 41.845 1.00 89.34 C ANISOU 2429 CA TYR A 306 10134 9470 14343 60 -715 7 C ATOM 2430 C TYR A 306 9.214 25.260 41.876 1.00 88.48 C ANISOU 2430 C TYR A 306 10065 9390 14164 -26 -779 -25 C ATOM 2431 O TYR A 306 9.053 24.370 41.033 1.00100.21 O ANISOU 2431 O TYR A 306 11411 10939 15725 -97 -847 -11 O ATOM 2432 CB TYR A 306 8.643 27.337 40.620 1.00 91.46 C ANISOU 2432 CB TYR A 306 10335 9767 14648 14 -871 7 C ATOM 2433 CG TYR A 306 7.532 28.287 40.248 1.00 89.90 C ANISOU 2433 CG TYR A 306 10040 9543 14575 73 -846 44 C ATOM 2434 CD1 TYR A 306 7.342 29.474 40.943 1.00 88.72 C ANISOU 2434 CD1 TYR A 306 9995 9310 14406 183 -827 19 C ATOM 2435 CD2 TYR A 306 6.665 27.992 39.207 1.00 97.45 C ANISOU 2435 CD2 TYR A 306 10799 10551 15675 27 -857 93 C ATOM 2436 CE1 TYR A 306 6.320 30.342 40.607 1.00 93.78 C ANISOU 2436 CE1 TYR A 306 10546 9919 15168 247 -829 32 C ATOM 2437 CE2 TYR A 306 5.643 28.853 38.861 1.00105.31 C ANISOU 2437 CE2 TYR A 306 11708 11512 16791 80 -843 117 C ATOM 2438 CZ TYR A 306 5.474 30.025 39.564 1.00103.29 C ANISOU 2438 CZ TYR A 306 11558 11173 16515 190 -834 82 C ATOM 2439 OH TYR A 306 4.456 30.882 39.219 1.00125.35 O ANISOU 2439 OH TYR A 306 14265 13926 19436 251 -846 86 O ATOM 2440 N ILE A 307 10.138 25.178 42.828 1.00 90.00 N ANISOU 2440 N ILE A 307 10442 9532 14222 -13 -771 -75 N ATOM 2441 CA ILE A 307 11.062 24.053 42.861 1.00 95.56 C ANISOU 2441 CA ILE A 307 11194 10253 14862 -91 -858 -125 C ATOM 2442 C ILE A 307 11.085 23.379 44.221 1.00 95.86 C ANISOU 2442 C ILE A 307 11364 10223 14835 -77 -756 -122 C ATOM 2443 O ILE A 307 10.985 22.152 44.316 1.00 98.43 O ANISOU 2443 O ILE A 307 11652 10555 15192 -141 -785 -110 O ATOM 2444 CB ILE A 307 12.473 24.498 42.469 1.00 86.20 C ANISOU 2444 CB ILE A 307 10102 9091 13560 -125 -1004 -201 C ATOM 2445 CG1 ILE A 307 12.462 24.927 41.009 1.00 81.79 C ANISOU 2445 CG1 ILE A 307 9376 8642 13058 -176 -1129 -190 C ATOM 2446 CG2 ILE A 307 13.453 23.383 42.763 1.00 96.79 C ANISOU 2446 CG2 ILE A 307 11522 10435 14819 -180 -1084 -279 C ATOM 2447 CD1 ILE A 307 13.506 24.331 40.213 1.00 90.01 C ANISOU 2447 CD1 ILE A 307 10370 9799 14032 -256 -1294 -266 C ATOM 2448 N MET A 308 11.255 24.164 45.281 1.00 84.24 N ANISOU 2448 N MET A 308 10050 8685 13272 1 -658 -133 N ATOM 2449 CA MET A 308 11.317 23.558 46.604 1.00 84.77 C ANISOU 2449 CA MET A 308 10243 8704 13263 5 -560 -128 C ATOM 2450 C MET A 308 9.963 23.013 47.037 1.00 89.30 C ANISOU 2450 C MET A 308 10695 9325 13909 5 -425 -33 C ATOM 2451 O MET A 308 9.906 22.074 47.835 1.00101.36 O ANISOU 2451 O MET A 308 12265 10846 15403 -52 -390 3 O ATOM 2452 CB MET A 308 11.848 24.564 47.622 1.00 97.68 C ANISOU 2452 CB MET A 308 12071 10267 14777 101 -492 -170 C ATOM 2453 CG MET A 308 13.278 24.286 48.060 1.00106.34 C ANISOU 2453 CG MET A 308 13359 11292 15751 62 -577 -244 C ATOM 2454 SD MET A 308 13.963 25.614 49.071 1.00131.23 S ANISOU 2454 SD MET A 308 16738 14347 18776 184 -529 -292 S ATOM 2455 CE MET A 308 12.627 25.876 50.236 1.00136.14 C ANISOU 2455 CE MET A 308 17331 14993 19404 296 -314 -243 C ATOM 2456 N MET A 309 8.867 23.575 46.529 1.00 91.35 N ANISOU 2456 N MET A 309 10803 9640 14268 58 -361 15 N ATOM 2457 CA MET A 309 7.535 23.054 46.803 1.00 98.41 C ANISOU 2457 CA MET A 309 11554 10606 15233 50 -240 112 C ATOM 2458 C MET A 309 7.069 22.071 45.736 1.00 99.37 C ANISOU 2458 C MET A 309 11502 10763 15492 -48 -333 172 C ATOM 2459 O MET A 309 5.863 21.834 45.600 1.00 88.80 O ANISOU 2459 O MET A 309 10009 9487 14245 -50 -254 261 O ATOM 2460 CB MET A 309 6.538 24.204 46.951 1.00 98.78 C ANISOU 2460 CB MET A 309 11531 10696 15307 178 -115 116 C ATOM 2461 CG MET A 309 6.703 24.981 48.248 1.00 98.96 C ANISOU 2461 CG MET A 309 11697 10707 15195 293 -4 63 C ATOM 2462 SD MET A 309 5.468 26.272 48.476 1.00105.52 S ANISOU 2462 SD MET A 309 12428 11605 16058 470 116 35 S ATOM 2463 CE MET A 309 5.065 26.047 50.209 1.00103.42 C ANISOU 2463 CE MET A 309 12213 11446 15637 532 306 43 C ATOM 2464 N ASN A 310 8.005 21.505 44.980 1.00 95.52 N ANISOU 2464 N ASN A 310 11031 10245 15016 -120 -507 118 N ATOM 2465 CA ASN A 310 7.744 20.499 43.959 1.00 90.35 C ANISOU 2465 CA ASN A 310 10223 9620 14484 -200 -634 149 C ATOM 2466 C ASN A 310 8.275 19.180 44.509 1.00 96.03 C ANISOU 2466 C ASN A 310 11016 10299 15171 -289 -733 148 C ATOM 2467 O ASN A 310 9.483 19.039 44.724 1.00107.50 O ANISOU 2467 O ASN A 310 12609 11707 16529 -305 -830 49 O ATOM 2468 CB ASN A 310 8.424 20.893 42.647 1.00 85.05 C ANISOU 2468 CB ASN A 310 9497 8977 13842 -203 -781 67 C ATOM 2469 CG ASN A 310 8.003 20.031 41.477 1.00 92.17 C ANISOU 2469 CG ASN A 310 10210 9928 14881 -257 -904 90 C ATOM 2470 OD1 ASN A 310 7.077 20.373 40.743 1.00100.43 O ANISOU 2470 OD1 ASN A 310 11106 11011 16041 -239 -864 147 O ATOM 2471 ND2 ASN A 310 8.700 18.920 41.278 1.00 85.98 N ANISOU 2471 ND2 ASN A 310 9435 9141 14092 -316 -1070 32 N ATOM 2472 N LYS A 311 7.369 18.225 44.750 1.00103.33 N ANISOU 2472 N LYS A 311 11846 11237 16176 -352 -722 263 N ATOM 2473 CA LYS A 311 7.717 17.038 45.531 1.00111.02 C ANISOU 2473 CA LYS A 311 12906 12161 17118 -448 -812 292 C ATOM 2474 C LYS A 311 8.915 16.303 44.940 1.00102.86 C ANISOU 2474 C LYS A 311 11924 11072 16086 -488 -1055 165 C ATOM 2475 O LYS A 311 9.790 15.839 45.680 1.00102.15 O ANISOU 2475 O LYS A 311 11990 10913 15908 -530 -1129 109 O ATOM 2476 CB LYS A 311 6.510 16.105 45.629 1.00126.38 C ANISOU 2476 CB LYS A 311 14709 14138 19170 -528 -811 456 C ATOM 2477 CG LYS A 311 6.554 15.142 46.809 1.00130.62 C ANISOU 2477 CG LYS A 311 15337 14643 19650 -639 -845 543 C ATOM 2478 CD LYS A 311 5.308 14.266 46.854 1.00138.35 C ANISOU 2478 CD LYS A 311 16159 15672 20735 -734 -861 733 C ATOM 2479 CE LYS A 311 5.311 13.357 48.074 1.00149.45 C ANISOU 2479 CE LYS A 311 17649 17063 22073 -872 -904 848 C ATOM 2480 NZ LYS A 311 4.245 12.318 48.001 1.00151.31 N ANISOU 2480 NZ LYS A 311 17733 17335 22422 -996 -995 1046 N ATOM 2481 N GLN A 312 8.975 16.194 43.611 1.00104.37 N ANISOU 2481 N GLN A 312 11980 11304 16372 -472 -1186 108 N ATOM 2482 CA GLN A 312 10.120 15.567 42.957 1.00110.30 C ANISOU 2482 CA GLN A 312 12751 12048 17111 -488 -1424 -43 C ATOM 2483 C GLN A 312 11.421 16.263 43.336 1.00112.34 C ANISOU 2483 C GLN A 312 13185 12294 17206 -454 -1415 -173 C ATOM 2484 O GLN A 312 12.317 15.656 43.935 1.00118.51 O ANISOU 2484 O GLN A 312 14104 13010 17914 -489 -1522 -253 O ATOM 2485 CB GLN A 312 9.934 15.590 41.440 1.00121.57 C ANISOU 2485 CB GLN A 312 13986 13566 18642 -459 -1532 -87 C ATOM 2486 CG GLN A 312 9.220 14.385 40.868 1.00139.70 C ANISOU 2486 CG GLN A 312 16128 15851 21099 -499 -1688 -31 C ATOM 2487 CD GLN A 312 9.818 13.947 39.546 1.00148.15 C ANISOU 2487 CD GLN A 312 17074 17000 22215 -471 -1918 -176 C ATOM 2488 OE1 GLN A 312 10.266 14.774 38.749 1.00133.24 O ANISOU 2488 OE1 GLN A 312 15134 15218 20273 -428 -1901 -259 O ATOM 2489 NE2 GLN A 312 9.844 12.638 39.313 1.00152.97 N ANISOU 2489 NE2 GLN A 312 17632 17570 22921 -499 -2155 -208 N ATOM 2490 N PHE A 313 11.539 17.546 42.977 1.00 99.39 N ANISOU 2490 N PHE A 313 11542 10709 15512 -391 -1305 -193 N ATOM 2491 CA PHE A 313 12.766 18.294 43.232 1.00 93.30 C ANISOU 2491 CA PHE A 313 10926 9934 14589 -362 -1312 -301 C ATOM 2492 C PHE A 313 13.122 18.290 44.705 1.00 87.38 C ANISOU 2492 C PHE A 313 10389 9076 13736 -365 -1216 -290 C ATOM 2493 O PHE A 313 14.288 18.108 45.069 1.00 91.14 O ANISOU 2493 O PHE A 313 11010 9511 14107 -379 -1304 -396 O ATOM 2494 CB PHE A 313 12.621 19.732 42.745 1.00 96.79 C ANISOU 2494 CB PHE A 313 11334 10432 15007 -305 -1213 -280 C ATOM 2495 CG PHE A 313 12.873 19.901 41.282 1.00102.72 C ANISOU 2495 CG PHE A 313 11924 11310 15794 -318 -1349 -334 C ATOM 2496 CD1 PHE A 313 14.167 20.027 40.804 1.00 94.99 C ANISOU 2496 CD1 PHE A 313 10981 10411 14699 -336 -1492 -456 C ATOM 2497 CD2 PHE A 313 11.820 19.938 40.383 1.00100.53 C ANISOU 2497 CD2 PHE A 313 11452 11090 15656 -317 -1333 -261 C ATOM 2498 CE1 PHE A 313 14.409 20.182 39.452 1.00 90.89 C ANISOU 2498 CE1 PHE A 313 10292 10051 14190 -357 -1619 -502 C ATOM 2499 CE2 PHE A 313 12.054 20.094 39.029 1.00 98.67 C ANISOU 2499 CE2 PHE A 313 11059 10985 15445 -336 -1459 -307 C ATOM 2500 CZ PHE A 313 13.351 20.215 38.563 1.00 99.61 C ANISOU 2500 CZ PHE A 313 11203 11208 15435 -359 -1603 -427 C ATOM 2501 N ARG A 314 12.137 18.523 45.562 1.00 83.71 N ANISOU 2501 N ARG A 314 9937 8580 13290 -351 -1035 -168 N ATOM 2502 CA ARG A 314 12.368 18.438 46.990 1.00 86.63 C ANISOU 2502 CA ARG A 314 10486 8869 13558 -360 -940 -146 C ATOM 2503 C ARG A 314 13.078 17.134 47.294 1.00 91.41 C ANISOU 2503 C ARG A 314 11170 9407 14157 -453 -1117 -198 C ATOM 2504 O ARG A 314 14.255 17.133 47.669 1.00 97.12 O ANISOU 2504 O ARG A 314 12056 10069 14777 -455 -1187 -308 O ATOM 2505 CB ARG A 314 11.049 18.512 47.739 1.00103.92 C ANISOU 2505 CB ARG A 314 12617 11088 15782 -354 -755 -1 C ATOM 2506 CG ARG A 314 11.171 18.997 49.144 1.00 86.37 C ANISOU 2506 CG ARG A 314 10557 8832 13429 -319 -599 16 C ATOM 2507 CD ARG A 314 9.846 19.563 49.586 1.00 90.00 C ANISOU 2507 CD ARG A 314 10913 9381 13904 -261 -398 123 C ATOM 2508 NE ARG A 314 8.796 18.551 49.683 1.00110.09 N ANISOU 2508 NE ARG A 314 13314 11988 16528 -357 -391 260 N ATOM 2509 CZ ARG A 314 7.679 18.545 48.959 1.00116.03 C ANISOU 2509 CZ ARG A 314 13867 12820 17398 -350 -357 340 C ATOM 2510 NH1 ARG A 314 7.448 19.499 48.069 1.00122.12 N ANISOU 2510 NH1 ARG A 314 14558 13614 18226 -253 -329 291 N ATOM 2511 NH2 ARG A 314 6.783 17.583 49.135 1.00128.57 N ANISOU 2511 NH2 ARG A 314 15338 14463 19048 -450 -364 480 N ATOM 2512 N ASN A 315 12.373 16.023 47.071 1.00 90.60 N ANISOU 2512 N ASN A 315 10946 9306 14170 -529 -1212 -123 N ATOM 2513 CA ASN A 315 12.905 14.703 47.383 1.00 88.92 C ANISOU 2513 CA ASN A 315 10798 9011 13976 -625 -1419 -161 C ATOM 2514 C ASN A 315 14.353 14.562 46.938 1.00 95.52 C ANISOU 2514 C ASN A 315 11723 9821 14748 -605 -1605 -360 C ATOM 2515 O ASN A 315 15.217 14.159 47.722 1.00105.19 O ANISOU 2515 O ASN A 315 13121 10951 15894 -643 -1678 -430 O ATOM 2516 CB ASN A 315 12.037 13.630 46.728 1.00 98.69 C ANISOU 2516 CB ASN A 315 11854 10265 15377 -689 -1566 -78 C ATOM 2517 CG ASN A 315 10.659 13.531 47.350 1.00104.46 C ANISOU 2517 CG ASN A 315 12507 11026 16157 -741 -1408 133 C ATOM 2518 OD1 ASN A 315 10.306 14.299 48.249 1.00116.33 O ANISOU 2518 OD1 ASN A 315 14074 12560 17566 -715 -1179 204 O ATOM 2519 ND2 ASN A 315 9.863 12.588 46.862 1.00 90.60 N ANISOU 2519 ND2 ASN A 315 10602 9277 14546 -808 -1540 231 N ATOM 2520 N CYS A 316 14.645 14.936 45.692 1.00 91.51 N ANISOU 2520 N CYS A 316 11097 9413 14262 -546 -1680 -455 N ATOM 2521 CA CYS A 316 16.008 14.808 45.190 1.00 88.44 C ANISOU 2521 CA CYS A 316 10759 9050 13793 -527 -1861 -650 C ATOM 2522 C CYS A 316 16.975 15.732 45.920 1.00 90.87 C ANISOU 2522 C CYS A 316 11268 9321 13936 -494 -1752 -707 C ATOM 2523 O CYS A 316 18.168 15.425 46.014 1.00112.35 O ANISOU 2523 O CYS A 316 14097 12020 16570 -500 -1891 -856 O ATOM 2524 CB CYS A 316 16.036 15.084 43.690 1.00100.46 C ANISOU 2524 CB CYS A 316 12085 10731 15355 -481 -1949 -720 C ATOM 2525 SG CYS A 316 14.990 13.967 42.740 1.00 95.07 S ANISOU 2525 SG CYS A 316 11165 10085 14872 -504 -2107 -673 S ATOM 2526 N MET A 317 16.490 16.858 46.444 1.00 96.95 N ANISOU 2526 N MET A 317 12091 10082 14663 -450 -1518 -600 N ATOM 2527 CA MET A 317 17.373 17.777 47.153 1.00 97.83 C ANISOU 2527 CA MET A 317 12398 10145 14628 -409 -1428 -646 C ATOM 2528 C MET A 317 17.652 17.311 48.575 1.00103.80 C ANISOU 2528 C MET A 317 13356 10760 15325 -446 -1383 -633 C ATOM 2529 O MET A 317 18.786 17.426 49.051 1.00 99.16 O ANISOU 2529 O MET A 317 12943 10108 14627 -442 -1427 -733 O ATOM 2530 CB MET A 317 16.778 19.183 47.158 1.00 96.12 C ANISOU 2530 CB MET A 317 12163 9964 14395 -332 -1235 -554 C ATOM 2531 CG MET A 317 17.062 19.953 45.889 1.00103.19 C ANISOU 2531 CG MET A 317 12939 10983 15287 -305 -1304 -595 C ATOM 2532 SD MET A 317 16.227 21.543 45.836 1.00123.14 S ANISOU 2532 SD MET A 317 15431 13526 17831 -223 -1128 -484 S ATOM 2533 CE MET A 317 16.907 22.205 44.322 1.00122.95 C ANISOU 2533 CE MET A 317 15285 13650 17780 -243 -1284 -539 C ATOM 2534 N VAL A 318 16.641 16.791 49.274 1.00107.80 N ANISOU 2534 N VAL A 318 13836 11227 15896 -492 -1298 -503 N ATOM 2535 CA VAL A 318 16.908 16.204 50.583 1.00 96.11 C ANISOU 2535 CA VAL A 318 12530 9629 14359 -557 -1285 -481 C ATOM 2536 C VAL A 318 17.802 14.985 50.428 1.00106.25 C ANISOU 2536 C VAL A 318 13867 10839 15664 -636 -1549 -603 C ATOM 2537 O VAL A 318 18.628 14.690 51.301 1.00108.48 O ANISOU 2537 O VAL A 318 14340 11008 15867 -673 -1593 -664 O ATOM 2538 CB VAL A 318 15.590 15.864 51.307 1.00 91.26 C ANISOU 2538 CB VAL A 318 11846 9033 13797 -611 -1155 -299 C ATOM 2539 CG1 VAL A 318 15.875 15.241 52.663 1.00 98.84 C ANISOU 2539 CG1 VAL A 318 12975 9890 14688 -701 -1154 -262 C ATOM 2540 CG2 VAL A 318 14.745 17.118 51.472 1.00 91.72 C ANISOU 2540 CG2 VAL A 318 11848 9176 13827 -508 -906 -214 C ATOM 2541 N THR A 319 17.676 14.276 49.304 1.00116.81 N ANISOU 2541 N THR A 319 15038 12237 17109 -653 -1743 -656 N ATOM 2542 CA THR A 319 18.576 13.165 49.015 1.00107.55 C ANISOU 2542 CA THR A 319 13896 11010 15959 -698 -2032 -814 C ATOM 2543 C THR A 319 20.006 13.649 48.795 1.00102.82 C ANISOU 2543 C THR A 319 13409 10428 15229 -639 -2094 -1006 C ATOM 2544 O THR A 319 20.954 13.061 49.328 1.00104.53 O ANISOU 2544 O THR A 319 13778 10543 15396 -674 -2235 -1125 O ATOM 2545 CB THR A 319 18.072 12.396 47.793 1.00101.10 C ANISOU 2545 CB THR A 319 12854 10275 15284 -702 -2228 -839 C ATOM 2546 OG1 THR A 319 17.036 11.489 48.190 1.00109.05 O ANISOU 2546 OG1 THR A 319 13804 11215 16415 -794 -2275 -683 O ATOM 2547 CG2 THR A 319 19.201 11.624 47.133 1.00111.97 C ANISOU 2547 CG2 THR A 319 14226 11663 16656 -686 -2530 -1071 C ATOM 2548 N THR A 320 20.183 14.728 48.028 1.00101.77 N ANISOU 2548 N THR A 320 13203 10427 15038 -559 -2000 -1031 N ATOM 2549 CA THR A 320 21.524 15.182 47.671 1.00 98.23 C ANISOU 2549 CA THR A 320 12826 10037 14459 -516 -2080 -1199 C ATOM 2550 C THR A 320 22.220 15.875 48.838 1.00 99.91 C ANISOU 2550 C THR A 320 13289 10130 14541 -504 -1942 -1192 C ATOM 2551 O THR A 320 23.391 15.599 49.122 1.00 98.81 O ANISOU 2551 O THR A 320 13287 9941 14313 -512 -2059 -1336 O ATOM 2552 CB THR A 320 21.455 16.111 46.455 1.00 92.45 C ANISOU 2552 CB THR A 320 11925 9498 13705 -460 -2046 -1200 C ATOM 2553 OG1 THR A 320 21.321 15.326 45.262 1.00107.54 O ANISOU 2553 OG1 THR A 320 13621 11541 15699 -463 -2246 -1288 O ATOM 2554 CG2 THR A 320 22.707 16.974 46.356 1.00 79.08 C ANISOU 2554 CG2 THR A 320 10333 7868 11845 -429 -2052 -1299 C ATOM 2555 N LEU A 321 21.515 16.777 49.526 1.00108.03 N ANISOU 2555 N LEU A 321 14375 11115 15557 -475 -1701 -1037 N ATOM 2556 CA LEU A 321 22.132 17.520 50.621 1.00100.42 C ANISOU 2556 CA LEU A 321 13642 10040 14472 -443 -1570 -1029 C ATOM 2557 C LEU A 321 22.506 16.600 51.776 1.00109.23 C ANISOU 2557 C LEU A 321 14937 10992 15573 -513 -1617 -1058 C ATOM 2558 O LEU A 321 23.551 16.785 52.410 1.00101.28 O ANISOU 2558 O LEU A 321 14129 9892 14461 -504 -1629 -1142 O ATOM 2559 CB LEU A 321 21.192 18.627 51.096 1.00101.21 C ANISOU 2559 CB LEU A 321 13742 10140 14572 -378 -1326 -874 C ATOM 2560 CG LEU A 321 20.822 19.672 50.041 1.00 96.70 C ANISOU 2560 CG LEU A 321 13018 9704 14020 -314 -1287 -837 C ATOM 2561 CD1 LEU A 321 19.682 20.552 50.526 1.00 99.68 C ANISOU 2561 CD1 LEU A 321 13369 10074 14429 -247 -1076 -697 C ATOM 2562 CD2 LEU A 321 22.030 20.511 49.673 1.00 78.82 C ANISOU 2562 CD2 LEU A 321 10840 7471 11637 -280 -1353 -924 C ATOM 2563 N CYS A 322 21.671 15.604 52.066 1.00122.55 N ANISOU 2563 N CYS A 322 16559 12640 17364 -592 -1657 -979 N ATOM 2564 CA CYS A 322 21.998 14.601 53.066 1.00120.56 C ANISOU 2564 CA CYS A 322 16458 12236 17112 -688 -1753 -996 C ATOM 2565 C CYS A 322 22.837 13.466 52.488 1.00132.42 C ANISOU 2565 C CYS A 322 17949 13708 18658 -736 -2064 -1175 C ATOM 2566 O CYS A 322 22.907 12.388 53.091 1.00142.20 O ANISOU 2566 O CYS A 322 19262 14820 19946 -836 -2216 -1183 O ATOM 2567 CB CYS A 322 20.720 14.075 53.719 1.00121.30 C ANISOU 2567 CB CYS A 322 16488 12313 17287 -772 -1671 -806 C ATOM 2568 SG CYS A 322 19.869 15.342 54.702 1.00131.56 S ANISOU 2568 SG CYS A 322 17830 13654 18503 -703 -1314 -636 S ATOM 2569 N CYS A 323 23.464 13.704 51.336 1.00139.14 N ANISOU 2569 N CYS A 323 18700 14683 19485 -668 -2176 -1320 N ATOM 2570 CA CYS A 323 24.518 12.876 50.742 1.00135.97 C ANISOU 2570 CA CYS A 323 18291 14296 19077 -671 -2465 -1546 C ATOM 2571 C CYS A 323 24.253 11.379 50.898 1.00130.11 C ANISOU 2571 C CYS A 323 17526 13446 18466 -761 -2717 -1577 C ATOM 2572 O CYS A 323 25.059 10.626 51.444 1.00136.74 O ANISOU 2572 O CYS A 323 18513 14151 19292 -808 -2900 -1703 O ATOM 2573 CB CYS A 323 25.894 13.253 51.306 1.00144.81 C ANISOU 2573 CB CYS A 323 19628 15345 20048 -648 -2471 -1682 C ATOM 2574 SG CYS A 323 25.980 13.697 53.078 1.00165.84 S ANISOU 2574 SG CYS A 323 22584 17789 22638 -687 -2251 -1558 S ATOM 2575 N GLY A 324 23.101 10.950 50.389 1.00129.52 N ANISOU 2575 N GLY A 324 17263 13425 18526 -787 -2744 -1459 N ATOM 2576 CA GLY A 324 22.807 9.532 50.370 1.00131.58 C ANISOU 2576 CA GLY A 324 17476 13591 18927 -870 -3028 -1480 C ATOM 2577 C GLY A 324 21.346 9.145 50.468 1.00139.48 C ANISOU 2577 C GLY A 324 18352 14583 20062 -946 -2977 -1247 C ATOM 2578 O GLY A 324 20.757 8.688 49.483 1.00148.96 O ANISOU 2578 O GLY A 324 19350 15867 21380 -925 -3111 -1247 O ATOM 2579 N LYS A 325 20.749 9.315 51.647 1.00145.10 N ANISOU 2579 N LYS A 325 19172 15208 20752 -1033 -2787 -1048 N ATOM 2580 CA LYS A 325 19.458 8.722 51.953 1.00167.68 C ANISOU 2580 CA LYS A 325 21934 18051 23726 -1142 -2784 -823 C ATOM 2581 C LYS A 325 18.374 9.800 52.073 1.00155.25 C ANISOU 2581 C LYS A 325 20268 16605 22115 -1101 -2429 -626 C ATOM 2582 O LYS A 325 18.518 10.908 51.535 1.00131.41 O ANISOU 2582 O LYS A 325 17208 13694 19029 -975 -2248 -678 O ATOM 2583 CB LYS A 325 19.595 7.882 53.227 1.00178.37 C ANISOU 2583 CB LYS A 325 23460 19231 25080 -1301 -2897 -747 C ATOM 2584 CG LYS A 325 21.032 7.520 53.588 1.00172.92 C ANISOU 2584 CG LYS A 325 22973 18399 24330 -1303 -3090 -969 C ATOM 2585 CD LYS A 325 21.402 6.110 53.152 1.00167.12 C ANISOU 2585 CD LYS A 325 22213 17554 23731 -1363 -3533 -1104 C ATOM 2586 CE LYS A 325 22.853 5.800 53.499 1.00164.93 C ANISOU 2586 CE LYS A 325 22135 17143 23389 -1351 -3724 -1349 C ATOM 2587 NZ LYS A 325 23.152 4.339 53.480 1.00161.47 N ANISOU 2587 NZ LYS A 325 21720 16544 23086 -1443 -4176 -1454 N ATOM 2588 N ASN A 326 17.291 9.465 52.775 1.00166.07 N ANISOU 2588 N ASN A 326 21598 17973 23527 -1212 -2349 -401 N ATOM 2589 CA ASN A 326 16.133 10.344 52.958 1.00173.78 C ANISOU 2589 CA ASN A 326 22467 19084 24475 -1178 -2037 -216 C ATOM 2590 C ASN A 326 15.510 10.760 51.628 1.00167.72 C ANISOU 2590 C ASN A 326 21484 18447 23796 -1076 -2003 -223 C ATOM 2591 O ASN A 326 14.324 11.088 51.565 1.00156.68 O ANISOU 2591 O ASN A 326 19944 17151 22435 -1075 -1834 -58 O ATOM 2592 CB ASN A 326 16.516 11.588 53.767 1.00177.72 C ANISOU 2592 CB ASN A 326 23114 19602 24809 -1093 -1748 -232 C ATOM 2593 CG ASN A 326 16.295 11.406 55.257 1.00181.14 C ANISOU 2593 CG ASN A 326 23675 19992 25157 -1203 -1641 -96 C ATOM 2594 OD1 ASN A 326 17.216 11.563 56.057 1.00178.43 O ANISOU 2594 OD1 ASN A 326 23536 19548 24711 -1206 -1625 -177 O ATOM 2595 ND2 ASN A 326 15.065 11.075 55.636 1.00183.40 N ANISOU 2595 ND2 ASN A 326 23834 20369 25479 -1297 -1568 115 N TER 2596 ASN A 326 ATOM 2597 N ILE B 340 -6.916 13.027 35.849 1.00123.67 N ANISOU 2597 N ILE B 340 15821 11515 19653 -384 170 2135 N ATOM 2598 CA ILE B 340 -5.908 14.058 35.648 1.00128.54 C ANISOU 2598 CA ILE B 340 16118 12738 19983 -620 188 2497 C ATOM 2599 C ILE B 340 -4.814 13.976 36.704 1.00133.35 C ANISOU 2599 C ILE B 340 16397 13364 20906 -389 225 2765 C ATOM 2600 O ILE B 340 -3.849 14.736 36.654 1.00150.14 O ANISOU 2600 O ILE B 340 18220 15982 22846 -530 259 3068 O ATOM 2601 CB ILE B 340 -6.539 15.459 35.648 1.00130.29 C ANISOU 2601 CB ILE B 340 16513 13034 19957 -1133 -135 2884 C ATOM 2602 CG1 ILE B 340 -7.602 15.563 36.743 1.00116.21 C ANISOU 2602 CG1 ILE B 340 15053 10577 18526 -1190 -467 3047 C ATOM 2603 CG2 ILE B 340 -7.106 15.797 34.273 1.00138.20 C ANISOU 2603 CG2 ILE B 340 17680 14346 20483 -1414 -88 2675 C ATOM 2604 CD1 ILE B 340 -8.203 16.945 36.873 1.00121.78 C ANISOU 2604 CD1 ILE B 340 15923 11322 19025 -1682 -800 3457 C ATOM 2605 N LEU B 341 -4.974 13.057 37.661 1.00123.83 N ANISOU 2605 N LEU B 341 15253 11621 20176 -35 217 2653 N ATOM 2606 CA LEU B 341 -3.970 12.894 38.710 1.00123.92 C ANISOU 2606 CA LEU B 341 14962 11606 20516 212 255 2888 C ATOM 2607 C LEU B 341 -2.596 12.607 38.120 1.00132.57 C ANISOU 2607 C LEU B 341 15643 13285 21443 403 596 2793 C ATOM 2608 O LEU B 341 -1.579 13.100 38.622 1.00138.31 O ANISOU 2608 O LEU B 341 16053 14294 22203 397 605 3126 O ATOM 2609 CB LEU B 341 -4.391 11.780 39.667 1.00122.34 C ANISOU 2609 CB LEU B 341 14906 10742 20838 600 238 2695 C ATOM 2610 CG LEU B 341 -5.420 12.164 40.728 1.00116.65 C ANISOU 2610 CG LEU B 341 14493 9424 20403 453 -130 2941 C ATOM 2611 CD1 LEU B 341 -6.021 10.933 41.373 1.00115.59 C ANISOU 2611 CD1 LEU B 341 14559 8640 20721 834 -113 2636 C ATOM 2612 CD2 LEU B 341 -4.768 13.038 41.774 1.00124.84 C ANISOU 2612 CD2 LEU B 341 15322 10530 21582 331 -314 3470 C ATOM 2613 N GLU B 342 -2.548 11.817 37.047 1.00133.15 N ANISOU 2613 N GLU B 342 15712 13548 21331 572 879 2340 N ATOM 2614 CA GLU B 342 -1.288 11.591 36.350 1.00138.25 C ANISOU 2614 CA GLU B 342 15977 14786 21766 724 1207 2234 C ATOM 2615 C GLU B 342 -0.754 12.891 35.763 1.00138.89 C ANISOU 2615 C GLU B 342 15877 15492 21404 319 1160 2566 C ATOM 2616 O GLU B 342 0.417 13.236 35.954 1.00140.69 O ANISOU 2616 O GLU B 342 15743 16121 21591 351 1260 2806 O ATOM 2617 CB GLU B 342 -1.481 10.537 35.259 1.00144.02 C ANISOU 2617 CB GLU B 342 16781 15578 22362 950 1499 1677 C ATOM 2618 CG GLU B 342 -0.212 9.799 34.860 1.00148.84 C ANISOU 2618 CG GLU B 342 17016 16586 22951 1292 1872 1471 C ATOM 2619 CD GLU B 342 0.269 8.822 35.923 1.00154.87 C ANISOU 2619 CD GLU B 342 17648 16980 24216 1744 1959 1415 C ATOM 2620 OE1 GLU B 342 -0.297 8.801 37.037 1.00143.43 O ANISOU 2620 OE1 GLU B 342 16372 14991 23134 1780 1721 1581 O ATOM 2621 OE2 GLU B 342 1.221 8.065 35.639 1.00169.35 O ANISOU 2621 OE2 GLU B 342 19204 19066 26077 2067 2270 1201 O ATOM 2622 N ASN B 343 -1.610 13.634 35.054 1.00137.39 N ANISOU 2622 N ASN B 343 15937 15387 20876 -68 1005 2590 N ATOM 2623 CA ASN B 343 -1.200 14.924 34.507 1.00137.65 C ANISOU 2623 CA ASN B 343 15827 15989 20483 -480 935 2917 C ATOM 2624 C ASN B 343 -0.788 15.888 35.612 1.00134.39 C ANISOU 2624 C ASN B 343 15277 15564 20219 -653 691 3467 C ATOM 2625 O ASN B 343 0.163 16.659 35.449 1.00135.84 O ANISOU 2625 O ASN B 343 15162 16274 20178 -811 736 3751 O ATOM 2626 CB ASN B 343 -2.330 15.529 33.674 1.00136.01 C ANISOU 2626 CB ASN B 343 15955 15788 19935 -863 777 2852 C ATOM 2627 CG ASN B 343 -2.705 14.669 32.489 1.00139.39 C ANISOU 2627 CG ASN B 343 16508 16287 20169 -726 1021 2322 C ATOM 2628 OD1 ASN B 343 -1.854 14.022 31.879 1.00143.97 O ANISOU 2628 OD1 ASN B 343 16838 17209 20657 -478 1342 2068 O ATOM 2629 ND2 ASN B 343 -3.990 14.659 32.152 1.00137.15 N ANISOU 2629 ND2 ASN B 343 16615 15679 19819 -890 870 2150 N ATOM 2630 N LEU B 344 -1.495 15.862 36.745 1.00129.95 N ANISOU 2630 N LEU B 344 14932 14408 20034 -629 430 3624 N ATOM 2631 CA LEU B 344 -1.134 16.743 37.850 1.00126.70 C ANISOU 2631 CA LEU B 344 14401 13951 19788 -782 191 4144 C ATOM 2632 C LEU B 344 0.256 16.420 38.381 1.00129.26 C ANISOU 2632 C LEU B 344 14306 14510 20298 -487 385 4259 C ATOM 2633 O LEU B 344 1.024 17.328 38.719 1.00133.16 O ANISOU 2633 O LEU B 344 14555 15338 20701 -668 311 4669 O ATOM 2634 CB LEU B 344 -2.175 16.649 38.964 1.00121.61 C ANISOU 2634 CB LEU B 344 14077 12592 19538 -773 -108 4250 C ATOM 2635 CG LEU B 344 -3.562 17.188 38.604 1.00118.30 C ANISOU 2635 CG LEU B 344 14073 11932 18945 -1122 -359 4237 C ATOM 2636 CD1 LEU B 344 -4.413 17.379 39.849 1.00121.30 C ANISOU 2636 CD1 LEU B 344 14711 11677 19699 -1172 -693 4473 C ATOM 2637 CD2 LEU B 344 -3.459 18.481 37.810 1.00118.44 C ANISOU 2637 CD2 LEU B 344 14043 12492 18467 -1588 -442 4492 C ATOM 2638 N LYS B 345 0.608 15.135 38.450 1.00122.10 N ANISOU 2638 N LYS B 345 16287 13678 16426 -1769 -895 488 N ATOM 2639 CA LYS B 345 1.953 14.781 38.890 1.00109.54 C ANISOU 2639 CA LYS B 345 14638 12281 14700 -1395 -979 164 C ATOM 2640 C LYS B 345 2.994 15.101 37.825 1.00105.12 C ANISOU 2640 C LYS B 345 14018 11715 14208 -1330 -917 -284 C ATOM 2641 O LYS B 345 4.125 15.467 38.164 1.00105.53 O ANISOU 2641 O LYS B 345 13869 12053 14175 -1088 -862 -657 O ATOM 2642 CB LYS B 345 2.008 13.304 39.280 1.00108.49 C ANISOU 2642 CB LYS B 345 14810 11946 14467 -1185 -1264 399 C ATOM 2643 CG LYS B 345 1.175 12.977 40.512 1.00129.99 C ANISOU 2643 CG LYS B 345 17564 14735 17092 -1186 -1331 798 C ATOM 2644 CD LYS B 345 1.023 11.480 40.720 1.00137.55 C ANISOU 2644 CD LYS B 345 18861 15422 17978 -1039 -1617 1086 C ATOM 2645 CE LYS B 345 0.031 11.183 41.835 1.00134.17 C ANISOU 2645 CE LYS B 345 18480 15022 17476 -1090 -1676 1520 C ATOM 2646 NZ LYS B 345 -0.227 9.724 41.978 1.00136.71 N ANISOU 2646 NZ LYS B 345 19146 15055 17741 -977 -1953 1829 N ATOM 2647 N ASP B 346 2.634 14.986 36.542 1.00107.25 N ANISOU 2647 N ASP B 346 14455 11667 14629 -1543 -922 -256 N ATOM 2648 CA ASP B 346 3.570 15.319 35.469 1.00103.32 C ANISOU 2648 CA ASP B 346 13901 11149 14205 -1502 -857 -675 C ATOM 2649 C ASP B 346 4.002 16.776 35.551 1.00101.27 C ANISOU 2649 C ASP B 346 13263 11245 13969 -1553 -586 -1018 C ATOM 2650 O ASP B 346 5.192 17.093 35.437 1.00110.79 O ANISOU 2650 O ASP B 346 14314 12649 15133 -1346 -536 -1437 O ATOM 2651 CB ASP B 346 2.939 15.041 34.103 1.00102.08 C ANISOU 2651 CB ASP B 346 13977 10591 14216 -1766 -890 -547 C ATOM 2652 CG ASP B 346 2.545 13.595 33.924 1.00122.88 C ANISOU 2652 CG ASP B 346 16995 12858 16835 -1721 -1158 -225 C ATOM 2653 OD1 ASP B 346 3.242 12.715 34.469 1.00127.42 O ANISOU 2653 OD1 ASP B 346 17674 13460 17280 -1416 -1336 -264 O ATOM 2654 OD2 ASP B 346 1.531 13.340 33.240 1.00138.54 O ANISOU 2654 OD2 ASP B 346 19175 14525 18937 -1990 -1190 70 O ATOM 2655 N VAL B 347 3.039 17.684 35.737 1.00 99.46 N ANISOU 2655 N VAL B 347 12880 11100 13809 -1831 -407 -846 N ATOM 2656 CA VAL B 347 3.341 19.111 35.813 1.00 97.52 C ANISOU 2656 CA VAL B 347 12273 11185 13595 -1907 -141 -1145 C ATOM 2657 C VAL B 347 3.784 19.541 37.200 1.00101.37 C ANISOU 2657 C VAL B 347 12506 12082 13926 -1697 -79 -1238 C ATOM 2658 O VAL B 347 4.034 20.733 37.421 1.00 96.82 O ANISOU 2658 O VAL B 347 11615 11811 13359 -1743 142 -1475 O ATOM 2659 CB VAL B 347 2.116 19.924 35.349 1.00 95.16 C ANISOU 2659 CB VAL B 347 11918 10791 13445 -2307 29 -929 C ATOM 2660 CG1 VAL B 347 1.741 19.537 33.925 1.00 94.33 C ANISOU 2660 CG1 VAL B 347 12056 10288 13497 -2512 -27 -866 C ATOM 2661 CG2 VAL B 347 0.949 19.704 36.290 1.00 95.58 C ANISOU 2661 CG2 VAL B 347 12030 10830 13456 -2423 -11 -467 C ATOM 2662 N GLY B 348 3.900 18.608 38.141 1.00110.42 N ANISOU 2662 N GLY B 348 13778 13245 14930 -1466 -265 -1061 N ATOM 2663 CA GLY B 348 4.439 18.925 39.446 1.00106.44 C ANISOU 2663 CA GLY B 348 13047 13127 14270 -1235 -224 -1171 C ATOM 2664 C GLY B 348 3.510 19.685 40.358 1.00100.57 C ANISOU 2664 C GLY B 348 12119 12583 13510 -1406 -80 -932 C ATOM 2665 O GLY B 348 3.974 20.290 41.329 1.00100.75 O ANISOU 2665 O GLY B 348 11883 12971 13426 -1259 20 -1090 O ATOM 2666 N LEU B 349 2.208 19.671 40.081 1.00108.64 N ANISOU 2666 N LEU B 349 13268 13377 14635 -1713 -67 -555 N ATOM 2667 CA LEU B 349 1.237 20.366 40.915 1.00112.75 C ANISOU 2667 CA LEU B 349 13629 14063 15147 -1895 67 -299 C ATOM 2668 C LEU B 349 0.636 19.480 41.996 1.00100.54 C ANISOU 2668 C LEU B 349 12240 12476 13485 -1805 -106 100 C ATOM 2669 O LEU B 349 0.125 20.004 42.993 1.00111.24 O ANISOU 2669 O LEU B 349 13426 14057 14782 -1853 -10 254 O ATOM 2670 CB LEU B 349 0.120 20.946 40.044 1.00106.45 C ANISOU 2670 CB LEU B 349 12857 13062 14529 -2292 197 -112 C ATOM 2671 CG LEU B 349 0.497 22.227 39.299 1.00 94.01 C ANISOU 2671 CG LEU B 349 11020 11637 13061 -2432 442 -476 C ATOM 2672 CD1 LEU B 349 -0.439 22.466 38.129 1.00110.21 C ANISOU 2672 CD1 LEU B 349 13188 13386 15301 -2791 508 -316 C ATOM 2673 CD2 LEU B 349 0.471 23.404 40.254 1.00 93.01 C ANISOU 2673 CD2 LEU B 349 10541 11919 12881 -2449 657 -572 C ATOM 2674 N PHE B 350 0.685 18.163 41.828 1.00105.46 N ANISOU 2674 N PHE B 350 13178 12819 14072 -1677 -355 270 N ATOM 2675 CA PHE B 350 0.230 17.237 42.859 1.00114.81 C ANISOU 2675 CA PHE B 350 14522 13965 15136 -1559 -536 628 C ATOM 2676 C PHE B 350 1.214 16.077 42.999 1.00126.82 C ANISOU 2676 C PHE B 350 16224 15420 16542 -1214 -768 513 C ATOM 2677 O PHE B 350 1.156 15.293 43.948 1.00112.30 O ANISOU 2677 O PHE B 350 14488 13606 14575 -1036 -926 722 O ATOM 2678 CB PHE B 350 -1.172 16.712 42.541 1.00120.55 C ANISOU 2678 CB PHE B 350 15503 14344 15954 -1838 -619 1111 C ATOM 2679 CG PHE B 350 -1.716 15.776 43.582 1.00116.35 C ANISOU 2679 CG PHE B 350 15139 13763 15307 -1737 -802 1498 C ATOM 2680 CD1 PHE B 350 -2.120 16.254 44.818 1.00115.76 C ANISOU 2680 CD1 PHE B 350 14876 13967 15139 -1729 -719 1645 C ATOM 2681 CD2 PHE B 350 -1.818 14.419 43.328 1.00113.32 C ANISOU 2681 CD2 PHE B 350 15099 13055 14903 -1647 -1057 1714 C ATOM 2682 CE1 PHE B 350 -2.618 15.397 45.781 1.00108.01 C ANISOU 2682 CE1 PHE B 350 14046 12942 14050 -1635 -887 2001 C ATOM 2683 CE2 PHE B 350 -2.316 13.558 44.288 1.00117.00 C ANISOU 2683 CE2 PHE B 350 15718 13476 15261 -1553 -1226 2070 C ATOM 2684 CZ PHE B 350 -2.717 14.049 45.516 1.00112.41 C ANISOU 2684 CZ PHE B 350 14946 13175 14589 -1547 -1141 2214 C ATOM 2685 OXT PHE B 350 2.099 15.899 42.162 1.00141.32 O ANISOU 2685 OXT PHE B 350 18107 17176 18411 -1104 -802 205 O TER 2686 PHE B 350 HETATM 2687 C1 NAG C 1 26.326 70.052 39.571 1.00 83.22 C HETATM 2688 C2 NAG C 1 26.903 69.588 38.251 1.00 72.21 C HETATM 2689 C3 NAG C 1 28.405 69.797 38.275 1.00 72.35 C HETATM 2690 C4 NAG C 1 28.771 71.227 38.624 1.00 72.50 C HETATM 2691 C5 NAG C 1 28.096 71.607 39.932 1.00 81.01 C HETATM 2692 C6 NAG C 1 28.361 73.079 40.262 1.00 83.08 C HETATM 2693 C7 NAG C 1 26.271 67.552 36.971 1.00 73.10 C HETATM 2694 C8 NAG C 1 26.017 66.048 37.094 1.00 63.59 C HETATM 2695 N2 NAG C 1 26.618 68.150 38.120 1.00 61.85 N HETATM 2696 O3 NAG C 1 28.954 69.485 36.989 1.00 68.98 O HETATM 2697 O4 NAG C 1 30.188 71.235 38.821 1.00 84.80 O HETATM 2698 O5 NAG C 1 26.675 71.431 39.816 1.00103.91 O HETATM 2699 O6 NAG C 1 27.500 73.907 39.469 1.00 94.20 O HETATM 2700 O7 NAG C 1 26.149 68.127 35.890 1.00 76.94 O HETATM 2701 C1 NAG C 2 31.016 72.184 38.134 1.00 72.03 C HETATM 2702 C2 NAG C 2 32.202 72.389 39.045 1.00 65.83 C HETATM 2703 C3 NAG C 2 33.137 73.411 38.436 1.00 62.51 C HETATM 2704 C4 NAG C 2 33.569 72.922 37.049 1.00 63.14 C HETATM 2705 C5 NAG C 2 32.325 72.653 36.203 1.00 55.72 C HETATM 2706 C6 NAG C 2 32.772 72.142 34.826 1.00 72.86 C HETATM 2707 C7 NAG C 2 32.035 72.277 41.513 1.00 85.20 C HETATM 2708 C8 NAG C 2 31.328 72.847 42.743 1.00 70.51 C HETATM 2709 N2 NAG C 2 31.670 72.827 40.347 1.00 70.09 N HETATM 2710 O3 NAG C 2 34.274 73.581 39.302 1.00 69.41 O HETATM 2711 O4 NAG C 2 34.332 73.926 36.347 1.00 83.13 O HETATM 2712 O5 NAG C 2 31.471 71.701 36.853 1.00 59.09 O HETATM 2713 O6 NAG C 2 31.647 71.949 33.962 1.00 64.15 O HETATM 2714 O7 NAG C 2 32.870 71.383 41.625 1.00114.90 O HETATM 2715 C1 BMA C 3 35.743 74.041 36.573 1.00106.14 C HETATM 2716 C2 BMA C 3 36.349 74.593 35.294 1.00123.60 C HETATM 2717 C3 BMA C 3 37.838 74.820 35.474 1.00132.40 C HETATM 2718 C4 BMA C 3 38.027 75.776 36.642 1.00145.12 C HETATM 2719 C5 BMA C 3 37.363 75.222 37.900 1.00129.89 C HETATM 2720 C6 BMA C 3 37.528 76.251 39.027 1.00124.88 C HETATM 2721 O2 BMA C 3 35.712 75.844 34.995 1.00141.09 O HETATM 2722 O3 BMA C 3 38.428 75.421 34.286 1.00150.64 O HETATM 2723 O4 BMA C 3 39.430 75.985 36.882 1.00163.67 O HETATM 2724 O5 BMA C 3 35.961 74.978 37.651 1.00112.00 O HETATM 2725 O6 BMA C 3 36.653 75.950 40.120 1.00109.07 O HETATM 2726 C1 BMA C 4 38.008 74.865 33.021 1.00165.08 C HETATM 2727 C2 BMA C 4 37.385 75.958 32.122 1.00173.98 C HETATM 2728 C3 BMA C 4 38.503 76.705 31.449 1.00164.96 C HETATM 2729 C4 BMA C 4 39.164 75.748 30.455 1.00164.97 C HETATM 2730 C5 BMA C 4 39.084 74.299 30.967 1.00174.34 C HETATM 2731 C6 BMA C 4 40.144 73.455 30.244 1.00176.05 C HETATM 2732 O2 BMA C 4 36.574 76.839 32.917 1.00181.19 O HETATM 2733 O3 BMA C 4 39.439 77.108 32.457 1.00158.58 O HETATM 2734 O4 BMA C 4 38.496 75.795 29.186 1.00154.05 O HETATM 2735 O5 BMA C 4 39.200 74.295 32.400 1.00173.92 O HETATM 2736 O6 BMA C 4 41.433 74.059 30.394 1.00169.78 O HETATM 2737 CAA ODM A 401 5.978 52.341 33.069 1.00197.62 C HETATM 2738 CAB ODM A 401 6.742 51.026 33.019 1.00196.01 C HETATM 2739 CAE ODM A 401 8.276 51.001 33.095 1.00204.51 C HETATM 2740 CAC ODM A 401 6.042 49.879 32.996 1.00180.15 C HETATM 2741 CAF ODM A 401 6.881 48.605 33.060 1.00161.76 C HETATM 2742 CAG ODM A 401 6.017 47.471 33.621 1.00149.51 C HETATM 2743 CAH ODM A 401 6.922 46.369 34.181 1.00134.15 C HETATM 2744 CAD ODM A 401 6.326 45.797 35.464 1.00124.94 C HETATM 2745 CAI ODM A 401 7.059 45.239 33.160 1.00120.40 C HETATM 2746 CAJ ODM A 401 8.151 44.269 33.617 1.00109.25 C HETATM 2747 OAK ODM A 401 8.371 43.294 32.603 1.00110.15 O HETATM 2748 C1 BOG A 406 -11.857 27.847 46.027 1.00150.60 C HETATM 2749 O1 BOG A 406 -11.297 29.125 46.124 1.00146.61 O HETATM 2750 C2 BOG A 406 -11.324 26.983 47.181 1.00147.01 C HETATM 2751 O2 BOG A 406 -11.299 25.635 46.774 1.00132.69 O HETATM 2752 C3 BOG A 406 -12.092 27.104 48.433 1.00154.84 C HETATM 2753 O3 BOG A 406 -11.607 28.234 49.111 1.00162.81 O HETATM 2754 C4 BOG A 406 -13.553 27.230 48.271 1.00156.95 C HETATM 2755 O4 BOG A 406 -14.199 26.293 49.088 1.00154.54 O HETATM 2756 C5 BOG A 406 -13.978 27.009 46.820 1.00158.05 C HETATM 2757 O5 BOG A 406 -13.312 28.010 45.998 1.00151.72 O HETATM 2758 C6 BOG A 406 -15.489 27.072 46.609 1.00157.43 C HETATM 2759 O6 BOG A 406 -15.812 26.181 45.573 1.00152.63 O HETATM 2760 C1' BOG A 406 -11.366 29.852 44.933 1.00130.20 C HETATM 2761 C2' BOG A 406 -10.025 29.694 44.227 1.00112.39 C HETATM 2762 C3' BOG A 406 -9.865 30.665 43.065 1.00 90.84 C HETATM 2763 C4' BOG A 406 -8.419 30.707 42.592 1.00 89.47 C HETATM 2764 C5' BOG A 406 -8.339 30.785 41.075 1.00 85.32 C HETATM 2765 C6' BOG A 406 -7.258 31.762 40.635 1.00 79.40 C HETATM 2766 C7' BOG A 406 -6.791 31.455 39.218 1.00 87.26 C HETATM 2767 C8' BOG A 406 -6.767 32.708 38.353 1.00 85.31 C HETATM 2768 C1 PLM A 407 25.581 14.038 54.612 1.00112.33 C1+ HETATM 2769 O2 PLM A 407 25.079 13.207 55.293 1.00136.78 O HETATM 2770 C2 PLM A 407 25.470 15.500 55.070 1.00108.95 C HETATM 2771 C3 PLM A 407 24.508 15.723 56.247 1.00107.90 C HETATM 2772 C4 PLM A 407 23.984 17.159 56.414 1.00111.60 C HETATM 2773 C5 PLM A 407 24.830 18.040 57.344 1.00 91.04 C HETATM 2774 C6 PLM A 407 24.032 19.010 58.228 1.00 81.64 C HETATM 2775 C7 PLM A 407 23.969 20.447 57.691 1.00 85.84 C HETATM 2776 C8 PLM A 407 24.091 21.541 58.760 1.00 87.45 C HETATM 2777 C9 PLM A 407 23.313 22.820 58.417 1.00 94.19 C HETATM 2778 CA PLM A 407 24.167 23.950 57.830 1.00103.71 C HETATM 2779 CB PLM A 407 23.354 25.111 57.244 1.00104.52 C HETATM 2780 CC PLM A 407 23.615 26.451 57.942 1.00 98.95 C HETATM 2781 CD PLM A 407 24.711 27.294 57.284 1.00105.35 C HETATM 2782 CE PLM A 407 24.968 28.629 57.990 1.00100.41 C HETATM 2783 CF PLM A 407 24.253 29.805 57.322 1.00 96.30 C HETATM 2784 CG PLM A 407 25.129 31.049 57.172 1.00104.26 C CONECT 109 2687 CONECT 875 1476 CONECT 1476 875 CONECT 2574 2768 CONECT 2687 109 2688 2698 CONECT 2688 2687 2689 2695 CONECT 2689 2688 2690 2696 CONECT 2690 2689 2691 2697 CONECT 2691 2690 2692 2698 CONECT 2692 2691 2699 CONECT 2693 2694 2695 2700 CONECT 2694 2693 CONECT 2695 2688 2693 CONECT 2696 2689 CONECT 2697 2690 2701 CONECT 2698 2687 2691 CONECT 2699 2692 CONECT 2700 2693 CONECT 2701 2697 2702 2712 CONECT 2702 2701 2703 2709 CONECT 2703 2702 2704 2710 CONECT 2704 2703 2705 2711 CONECT 2705 2704 2706 2712 CONECT 2706 2705 2713 CONECT 2707 2708 2709 2714 CONECT 2708 2707 CONECT 2709 2702 2707 CONECT 2710 2703 CONECT 2711 2704 2715 CONECT 2712 2701 2705 CONECT 2713 2706 CONECT 2714 2707 CONECT 2715 2711 2716 2724 CONECT 2716 2715 2717 2721 CONECT 2717 2716 2718 2722 CONECT 2718 2717 2719 2723 CONECT 2719 2718 2720 2724 CONECT 2720 2719 2725 CONECT 2721 2716 CONECT 2722 2717 2726 CONECT 2723 2718 CONECT 2724 2715 2719 CONECT 2725 2720 CONECT 2726 2722 2727 2735 CONECT 2727 2726 2728 2732 CONECT 2728 2727 2729 2733 CONECT 2729 2728 2730 2734 CONECT 2730 2729 2731 2735 CONECT 2731 2730 2736 CONECT 2732 2727 CONECT 2733 2728 CONECT 2734 2729 CONECT 2735 2726 2730 CONECT 2736 2731 CONECT 2737 2738 CONECT 2738 2737 2739 2740 CONECT 2739 2738 CONECT 2740 2738 2741 CONECT 2741 2740 2742 CONECT 2742 2741 2743 CONECT 2743 2742 2744 2745 CONECT 2744 2743 CONECT 2745 2743 2746 CONECT 2746 2745 2747 CONECT 2747 2746 CONECT 2748 2749 2750 2757 CONECT 2749 2748 2760 CONECT 2750 2748 2751 2752 CONECT 2751 2750 CONECT 2752 2750 2753 2754 CONECT 2753 2752 CONECT 2754 2752 2755 2756 CONECT 2755 2754 CONECT 2756 2754 2757 2758 CONECT 2757 2748 2756 CONECT 2758 2756 2759 CONECT 2759 2758 CONECT 2760 2749 2761 CONECT 2761 2760 2762 CONECT 2762 2761 2763 CONECT 2763 2762 2764 CONECT 2764 2763 2765 CONECT 2765 2764 2766 CONECT 2766 2765 2767 CONECT 2767 2766 CONECT 2768 2574 2769 2770 CONECT 2769 2768 CONECT 2770 2768 2771 CONECT 2771 2770 2772 CONECT 2772 2771 2773 CONECT 2773 2772 2774 CONECT 2774 2773 2775 CONECT 2775 2774 2776 CONECT 2776 2775 2777 CONECT 2777 2776 2778 CONECT 2778 2777 2779 CONECT 2779 2778 2780 CONECT 2780 2779 2781 CONECT 2781 2780 2782 CONECT 2782 2781 2783 CONECT 2783 2782 2784 CONECT 2784 2783 MASTER 443 0 7 17 4 0 0 6 2771 2 102 28 END