HEADER SIGNALING PROTEIN 06-FEB-19 6NWE TITLE CRYSTAL STRUCTURE OF BOVINE OPSIN WITH BETA OCTYL GLUCOSIDE BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: ILENLKDVGLF 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_COMMON: BOVINE; SOURCE 9 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 6NWE 1 COMPND REMARK HETNAM LINK REVDAT 2 2 1 SITE ATOM REVDAT 1 12-FEB-20 6NWE 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. 2.71 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) : 2.71 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.10 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 33684 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 1670 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 40.1047 - 6.1863 0.98 2726 130 0.2066 0.2303 REMARK 3 2 6.1863 - 4.9131 0.99 2689 133 0.2029 0.2286 REMARK 3 3 4.9131 - 4.2928 0.99 2648 140 0.1762 0.1891 REMARK 3 4 4.2928 - 3.9007 0.99 2630 162 0.1795 0.2108 REMARK 3 5 3.9007 - 3.6213 0.99 2640 152 0.1896 0.2018 REMARK 3 6 3.6213 - 3.4079 1.00 2673 144 0.1888 0.2109 REMARK 3 7 3.4079 - 3.2373 1.00 2684 119 0.1996 0.2479 REMARK 3 8 3.2373 - 3.0965 1.00 2647 139 0.1986 0.2338 REMARK 3 9 3.0965 - 2.9773 1.00 2678 147 0.1993 0.2315 REMARK 3 10 2.9773 - 2.8746 1.00 2663 130 0.2048 0.2761 REMARK 3 11 2.8746 - 2.7847 1.00 2662 133 0.2294 0.3036 REMARK 3 12 2.7847 - 2.7051 1.00 2674 141 0.2632 0.3515 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) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.780 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 2965 REMARK 3 ANGLE : 0.842 4028 REMARK 3 CHIRALITY : 0.046 465 REMARK 3 PLANARITY : 0.005 474 REMARK 3 DIHEDRAL : 15.166 1779 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 1:139) REMARK 3 ORIGIN FOR THE GROUP (A): 20.0644 41.6094 40.4035 REMARK 3 T TENSOR REMARK 3 T11: 0.4125 T22: 0.3426 REMARK 3 T33: 0.5064 T12: -0.0019 REMARK 3 T13: -0.0613 T23: 0.0807 REMARK 3 L TENSOR REMARK 3 L11: 1.2550 L22: 0.6211 REMARK 3 L33: 0.9188 L12: 0.0412 REMARK 3 L13: -0.2985 L23: -0.4841 REMARK 3 S TENSOR REMARK 3 S11: -0.0552 S12: 0.2582 S13: 0.1567 REMARK 3 S21: -0.3896 S22: 0.0839 S23: -0.3075 REMARK 3 S31: -0.1602 S32: 0.0629 S33: 0.0011 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 140:168) REMARK 3 ORIGIN FOR THE GROUP (A): 7.2604 25.7618 25.2830 REMARK 3 T TENSOR REMARK 3 T11: 0.7990 T22: 0.4008 REMARK 3 T33: 0.4509 T12: -0.1584 REMARK 3 T13: -0.1220 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 2.1831 L22: 0.4188 REMARK 3 L33: 0.1966 L12: 0.1850 REMARK 3 L13: -0.6290 L23: 0.0159 REMARK 3 S TENSOR REMARK 3 S11: -0.3460 S12: 0.6338 S13: -0.4905 REMARK 3 S21: -0.7106 S22: 0.1460 S23: 0.1634 REMARK 3 S31: 0.4193 S32: -0.2127 S33: -0.1581 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 169:222) REMARK 3 ORIGIN FOR THE GROUP (A): 10.6238 49.2259 30.7158 REMARK 3 T TENSOR REMARK 3 T11: 0.5414 T22: 0.3576 REMARK 3 T33: 0.4272 T12: -0.0711 REMARK 3 T13: -0.1743 T23: 0.1811 REMARK 3 L TENSOR REMARK 3 L11: 0.5901 L22: 0.7170 REMARK 3 L33: 1.3625 L12: -0.5085 REMARK 3 L13: -0.2789 L23: 0.8204 REMARK 3 S TENSOR REMARK 3 S11: -0.1805 S12: 0.0464 S13: 0.4267 REMARK 3 S21: -0.1994 S22: 0.2210 S23: -0.3101 REMARK 3 S31: -0.7705 S32: 0.2873 S33: 0.3878 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 223:287) REMARK 3 ORIGIN FOR THE GROUP (A): -2.0019 35.1037 42.0831 REMARK 3 T TENSOR REMARK 3 T11: 0.4959 T22: 0.4915 REMARK 3 T33: 0.6059 T12: -0.0407 REMARK 3 T13: -0.1163 T23: -0.0267 REMARK 3 L TENSOR REMARK 3 L11: 1.3017 L22: 0.4692 REMARK 3 L33: 1.0843 L12: -0.7318 REMARK 3 L13: 0.0062 L23: 0.2543 REMARK 3 S TENSOR REMARK 3 S11: -0.1366 S12: 0.1862 S13: 0.3033 REMARK 3 S21: -0.2297 S22: 0.1524 S23: 0.5856 REMARK 3 S31: -0.0820 S32: -0.3009 S33: 0.0001 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 288:326) REMARK 3 ORIGIN FOR THE GROUP (A): 13.1779 27.5288 47.1422 REMARK 3 T TENSOR REMARK 3 T11: 0.5215 T22: 0.4195 REMARK 3 T33: 0.5447 T12: -0.0050 REMARK 3 T13: -0.0867 T23: 0.0411 REMARK 3 L TENSOR REMARK 3 L11: 0.4060 L22: 0.0516 REMARK 3 L33: 0.4734 L12: 0.0588 REMARK 3 L13: 0.4401 L23: 0.0324 REMARK 3 S TENSOR REMARK 3 S11: -0.1731 S12: 0.0551 S13: 0.0729 REMARK 3 S21: -0.4244 S22: 0.2769 S23: 0.2277 REMARK 3 S31: -0.1816 S32: -0.2504 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 340:344) REMARK 3 ORIGIN FOR THE GROUP (A): -2.8638 13.7496 37.9456 REMARK 3 T TENSOR REMARK 3 T11: 0.9496 T22: 0.8300 REMARK 3 T33: 1.3127 T12: -0.0913 REMARK 3 T13: -0.0922 T23: 0.1068 REMARK 3 L TENSOR REMARK 3 L11: 0.0198 L22: 0.0217 REMARK 3 L33: 0.0255 L12: -0.0098 REMARK 3 L13: -0.0003 L23: -0.0066 REMARK 3 S TENSOR REMARK 3 S11: -0.1967 S12: 0.1731 S13: -0.2839 REMARK 3 S21: -0.4233 S22: -0.0918 S23: -0.1417 REMARK 3 S31: 0.1134 S32: 0.1395 S33: 0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN B AND RESID 345:350) REMARK 3 ORIGIN FOR THE GROUP (A): 1.8762 16.7574 40.7868 REMARK 3 T TENSOR REMARK 3 T11: 0.7512 T22: 0.7559 REMARK 3 T33: 1.0252 T12: -0.1502 REMARK 3 T13: -0.0783 T23: 0.0535 REMARK 3 L TENSOR REMARK 3 L11: 0.0128 L22: 0.0311 REMARK 3 L33: 0.0159 L12: -0.0099 REMARK 3 L13: 0.0122 L23: -0.0205 REMARK 3 S TENSOR REMARK 3 S11: 0.0733 S12: 0.1354 S13: -0.3344 REMARK 3 S21: -0.0629 S22: 0.2237 S23: 0.1382 REMARK 3 S31: 0.3541 S32: 0.0387 S33: -0.0001 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 6NWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-19. REMARK 100 THE DEPOSITION ID IS D_1000239578. 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 : 33699 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 40.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 0.68900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4J4Q 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 121.08450 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.90817 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.90533 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.08450 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.90817 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.90533 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.08450 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.90817 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.90533 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.08450 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 69.90817 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.90533 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.08450 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 69.90817 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.90533 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.08450 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 69.90817 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.90533 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 139.81634 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.81067 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 139.81634 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.81067 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 139.81634 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.81067 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 139.81634 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.81067 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 139.81634 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.81067 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 139.81634 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.81067 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: 4440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 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 OG1 THR A 118 O2 BOG A 412 1.27 REMARK 500 ND2 ASN A 15 O5 NAG C 1 2.17 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 29 4.33 -68.36 REMARK 500 ARG A 69 57.72 -91.67 REMARK 500 SER A 176 -161.87 60.55 REMARK 500 PHE A 212 -56.56 -126.80 REMARK 500 GLN A 237 48.53 -151.59 REMARK 500 HIS A 278 58.74 -113.36 REMARK 500 ILE A 307 -60.93 -120.64 REMARK 500 CYS A 323 -21.47 68.42 REMARK 500 REMARK 500 REMARK: NULL DBREF 6NWE A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 6NWE B 340 350 PDB 6NWE 6NWE 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 BOG A 405 20 HET BOG A 406 20 HET BOG A 407 20 HET BOG A 408 20 HET PLM A 409 17 HET SO4 A 410 5 HET SO4 A 411 5 HET BOG A 412 20 HET SO4 B 401 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM PLM PALMITIC ACID HETNAM SO4 SULFATE ION FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 3 BMA 2(C6 H12 O6) FORMUL 4 BOG 5(C14 H28 O6) FORMUL 8 PLM C16 H32 O2 FORMUL 9 SO4 3(O4 S 2-) FORMUL 13 HOH *9(H2 O) HELIX 1 AA1 GLU A 33 HIS A 65 1 33 HELIX 2 AA2 LYS A 66 ARG A 69 5 4 HELIX 3 AA3 THR A 70 GLY A 90 1 21 HELIX 4 AA4 GLY A 90 HIS A 100 1 11 HELIX 5 AA5 PHE A 105 LYS A 141 1 37 HELIX 6 AA6 GLY A 149 ALA A 169 1 21 HELIX 7 AA7 PRO A 170 VAL A 173 5 4 HELIX 8 AA8 HIS A 195 THR A 198 5 4 HELIX 9 AA9 ASN A 199 PHE A 212 1 14 HELIX 10 AB1 PHE A 212 GLN A 236 1 25 HELIX 11 AB2 SER A 240 HIS A 278 1 39 HELIX 12 AB3 GLY A 284 THR A 297 1 14 HELIX 13 AB4 THR A 297 ILE A 307 1 11 HELIX 14 AB5 ASN A 310 CYS A 322 1 13 HELIX 15 AB6 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 2.06 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.43 LINK SG CYS A 323 C1 PLM A 409 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 1.42 LINK O3 BMA C 3 C1 BMA C 4 1555 1555 1.43 CRYST1 242.169 242.169 110.716 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 0.004129 0.002384 0.000000 0.00000 SCALE2 0.000000 0.004768 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009032 0.00000 ATOM 1 N MET A 1 12.713 72.182 40.787 1.00104.75 N ANISOU 1 N MET A 1 14538 9613 15649 468 -88 2448 N ATOM 2 CA MET A 1 13.584 71.172 40.184 1.00114.96 C ANISOU 2 CA MET A 1 15757 11018 16903 366 -104 2472 C ATOM 3 C MET A 1 14.099 70.182 41.237 1.00101.05 C ANISOU 3 C MET A 1 13931 9283 15179 317 -189 2301 C ATOM 4 O MET A 1 14.654 70.579 42.261 1.00108.71 O ANISOU 4 O MET A 1 14910 10119 16275 264 -194 2146 O ATOM 5 CB MET A 1 14.750 71.844 39.458 1.00124.15 C ANISOU 5 CB MET A 1 16930 12076 18166 238 -10 2530 C ATOM 6 CG MET A 1 15.511 70.920 38.522 1.00127.32 C ANISOU 6 CG MET A 1 17265 12609 18502 151 -3 2605 C ATOM 7 SD MET A 1 16.393 71.827 37.240 1.00130.83 S ANISOU 7 SD MET A 1 17730 12985 18995 53 123 2755 S ATOM 8 CE MET A 1 15.049 72.766 36.512 1.00142.97 C ANISOU 8 CE MET A 1 19343 14535 20444 191 156 2918 C ATOM 9 N ASN A 2 13.923 68.888 40.978 1.00 86.93 N ANISOU 9 N ASN A 2 12080 7717 13233 328 -255 2289 N ATOM 10 CA ASN A 2 14.091 67.879 42.012 1.00 90.72 C ANISOU 10 CA ASN A 2 12498 8304 13667 314 -344 2096 C ATOM 11 C ASN A 2 15.198 66.863 41.734 1.00 88.58 C ANISOU 11 C ASN A 2 12148 8165 13342 195 -354 2021 C ATOM 12 O ASN A 2 15.371 65.929 42.529 1.00 86.46 O ANISOU 12 O ASN A 2 11821 8000 13031 184 -427 1874 O ATOM 13 CB ASN A 2 12.755 67.153 42.234 1.00 89.47 C ANISOU 13 CB ASN A 2 12330 8293 13374 449 -426 2119 C ATOM 14 CG ASN A 2 11.721 68.031 42.928 1.00109.82 C ANISOU 14 CG ASN A 2 14969 10743 16017 573 -430 2138 C ATOM 15 OD1 ASN A 2 12.026 68.695 43.919 1.00126.63 O ANISOU 15 OD1 ASN A 2 17126 12716 18272 557 -420 2015 O ATOM 16 ND2 ASN A 2 10.494 68.043 42.406 1.00105.30 N ANISOU 16 ND2 ASN A 2 14416 10266 15326 691 -436 2265 N ATOM 17 N GLY A 3 15.958 67.017 40.649 1.00 70.45 N ANISOU 17 N GLY A 3 9849 5870 11050 111 -279 2121 N ATOM 18 CA GLY A 3 17.008 66.079 40.305 1.00 64.34 C ANISOU 18 CA GLY A 3 9001 5219 10226 7 -275 2063 C ATOM 19 C GLY A 3 18.116 66.767 39.532 1.00 65.47 C ANISOU 19 C GLY A 3 9148 5268 10460 -107 -173 2137 C ATOM 20 O GLY A 3 18.077 67.977 39.301 1.00 60.22 O ANISOU 20 O GLY A 3 8543 4433 9903 -109 -109 2229 O ATOM 21 N THR A 4 19.113 65.978 39.133 1.00 62.94 N ANISOU 21 N THR A 4 8760 5055 10098 -199 -154 2099 N ATOM 22 CA THR A 4 20.260 66.450 38.367 1.00 61.84 C ANISOU 22 CA THR A 4 8606 4858 10031 -314 -57 2167 C ATOM 23 C THR A 4 20.490 65.520 37.182 1.00 62.18 C ANISOU 23 C THR A 4 8616 5086 9925 -329 -24 2249 C ATOM 24 O THR A 4 20.614 64.305 37.359 1.00 71.22 O ANISOU 24 O THR A 4 9704 6385 10971 -328 -72 2155 O ATOM 25 CB THR A 4 21.524 66.514 39.233 1.00 67.50 C ANISOU 25 CB THR A 4 9262 5504 10882 -434 -56 2014 C ATOM 26 OG1 THR A 4 21.311 67.403 40.332 1.00 62.26 O ANISOU 26 OG1 THR A 4 8637 4667 10351 -426 -86 1926 O ATOM 27 CG2 THR A 4 22.704 67.018 38.420 1.00 53.62 C ANISOU 27 CG2 THR A 4 7482 3688 9202 -554 47 2095 C ATOM 28 N GLU A 5 20.567 66.096 35.987 1.00 71.38 N ANISOU 28 N GLU A 5 9817 6232 11073 -344 63 2423 N ATOM 29 CA GLU A 5 20.663 65.351 34.739 1.00 55.39 C ANISOU 29 CA GLU A 5 7776 4378 8890 -350 103 2521 C ATOM 30 C GLU A 5 22.099 65.285 34.236 1.00 59.31 C ANISOU 30 C GLU A 5 8219 4881 9437 -473 191 2521 C ATOM 31 O GLU A 5 22.844 66.268 34.303 1.00 81.29 O ANISOU 31 O GLU A 5 11002 7509 12373 -550 255 2552 O ATOM 32 CB GLU A 5 19.792 65.993 33.655 1.00 54.01 C ANISOU 32 CB GLU A 5 7672 4206 8644 -283 144 2731 C ATOM 33 CG GLU A 5 18.306 65.911 33.920 1.00 79.25 C ANISOU 33 CG GLU A 5 10912 7440 11758 -153 62 2761 C ATOM 34 CD GLU A 5 17.489 66.357 32.726 1.00 87.32 C ANISOU 34 CD GLU A 5 11988 8510 12681 -90 99 2979 C ATOM 35 OE1 GLU A 5 17.517 67.565 32.399 1.00 78.25 O ANISOU 35 OE1 GLU A 5 10882 7214 11638 -91 169 3112 O ATOM 36 OE2 GLU A 5 16.836 65.494 32.103 1.00100.22 O ANISOU 36 OE2 GLU A 5 13618 10330 14130 -44 60 3020 O ATOM 37 N GLY A 6 22.469 64.124 33.703 1.00 74.81 N ANISOU 37 N GLY A 6 10134 7020 11269 -492 199 2491 N ATOM 38 CA GLY A 6 23.727 63.965 33.014 1.00 75.54 C ANISOU 38 CA GLY A 6 10176 7150 11377 -592 294 2518 C ATOM 39 C GLY A 6 23.532 63.276 31.682 1.00 79.85 C ANISOU 39 C GLY A 6 10736 7870 11733 -568 341 2621 C ATOM 40 O GLY A 6 22.418 62.883 31.317 1.00 94.34 O ANISOU 40 O GLY A 6 12617 9803 13423 -482 291 2666 O ATOM 41 N PRO A 7 24.617 63.142 30.915 1.00 72.16 N ANISOU 41 N PRO A 7 9722 6942 10755 -649 440 2664 N ATOM 42 CA PRO A 7 24.552 62.330 29.683 1.00 92.97 C ANISOU 42 CA PRO A 7 12368 9760 13197 -634 488 2734 C ATOM 43 C PRO A 7 23.984 60.917 29.849 1.00 93.24 C ANISOU 43 C PRO A 7 12393 9956 13076 -576 411 2616 C ATOM 44 O PRO A 7 23.076 60.539 29.092 1.00 91.02 O ANISOU 44 O PRO A 7 12165 9793 12625 -516 391 2686 O ATOM 45 CB PRO A 7 26.013 62.326 29.227 1.00 83.82 C ANISOU 45 CB PRO A 7 11144 8605 12098 -736 601 2746 C ATOM 46 CG PRO A 7 26.506 63.691 29.639 1.00 59.19 C ANISOU 46 CG PRO A 7 8020 5284 9184 -797 636 2801 C ATOM 47 CD PRO A 7 25.827 63.982 30.961 1.00 61.18 C ANISOU 47 CD PRO A 7 8291 5422 9535 -754 524 2692 C ATOM 48 N ASN A 8 24.478 60.121 30.803 1.00 66.74 N ANISOU 48 N ASN A 8 8972 6614 9774 -594 366 2445 N ATOM 49 CA ASN A 8 24.001 58.744 30.968 1.00 54.80 C ANISOU 49 CA ASN A 8 7448 5247 8128 -544 300 2334 C ATOM 50 C ASN A 8 23.420 58.479 32.356 1.00 57.86 C ANISOU 50 C ASN A 8 7817 5590 8578 -496 179 2202 C ATOM 51 O ASN A 8 23.577 57.376 32.884 1.00 58.32 O ANISOU 51 O ASN A 8 7826 5726 8606 -488 136 2071 O ATOM 52 CB ASN A 8 25.121 57.732 30.707 1.00 50.15 C ANISOU 52 CB ASN A 8 6790 4752 7511 -598 366 2254 C ATOM 53 CG ASN A 8 25.602 57.732 29.275 1.00 70.59 C ANISOU 53 CG ASN A 8 9399 7424 9997 -632 485 2371 C ATOM 54 OD1 ASN A 8 24.808 57.754 28.335 1.00 70.05 O ANISOU 54 OD1 ASN A 8 9402 7435 9779 -592 491 2472 O ATOM 55 ND2 ASN A 8 26.918 57.691 29.102 1.00 69.58 N ANISOU 55 ND2 ASN A 8 9206 7288 9944 -706 582 2360 N ATOM 56 N PHE A 9 22.757 59.454 32.976 1.00 60.18 N ANISOU 56 N PHE A 9 8148 5759 8959 -461 126 2232 N ATOM 57 CA PHE A 9 22.255 59.205 34.323 1.00 63.38 C ANISOU 57 CA PHE A 9 8532 6127 9420 -416 18 2102 C ATOM 58 C PHE A 9 21.225 60.256 34.712 1.00 57.58 C ANISOU 58 C PHE A 9 7863 5279 8734 -352 -31 2167 C ATOM 59 O PHE A 9 21.034 61.263 34.027 1.00 61.48 O ANISOU 59 O PHE A 9 8411 5699 9248 -352 24 2310 O ATOM 60 CB PHE A 9 23.397 59.163 35.356 1.00 56.95 C ANISOU 60 CB PHE A 9 7635 5244 8759 -488 18 1970 C ATOM 61 CG PHE A 9 24.216 60.427 35.423 1.00 63.16 C ANISOU 61 CG PHE A 9 8417 5872 9707 -568 84 2019 C ATOM 62 CD1 PHE A 9 23.773 61.533 36.149 1.00 56.56 C ANISOU 62 CD1 PHE A 9 7623 4879 8987 -553 47 2023 C ATOM 63 CD2 PHE A 9 25.436 60.509 34.761 1.00 56.96 C ANISOU 63 CD2 PHE A 9 7587 5092 8962 -660 187 2061 C ATOM 64 CE1 PHE A 9 24.531 62.700 36.196 1.00 54.56 C ANISOU 64 CE1 PHE A 9 7371 4470 8889 -634 109 2065 C ATOM 65 CE2 PHE A 9 26.200 61.676 34.810 1.00 71.28 C ANISOU 65 CE2 PHE A 9 9394 6758 10931 -742 247 2112 C ATOM 66 CZ PHE A 9 25.753 62.765 35.527 1.00 51.74 C ANISOU 66 CZ PHE A 9 6965 4121 8574 -733 207 2111 C ATOM 67 N TYR A 10 20.560 59.987 35.835 1.00 60.18 N ANISOU 67 N TYR A 10 8183 5597 9084 -293 -131 2063 N ATOM 68 CA TYR A 10 19.655 60.930 36.483 1.00 59.40 C ANISOU 68 CA TYR A 10 8136 5379 9054 -228 -181 2090 C ATOM 69 C TYR A 10 19.804 60.698 37.981 1.00 59.19 C ANISOU 69 C TYR A 10 8062 5307 9120 -225 -257 1920 C ATOM 70 O TYR A 10 19.417 59.643 38.485 1.00 66.11 O ANISOU 70 O TYR A 10 8903 6295 9922 -183 -331 1828 O ATOM 71 CB TYR A 10 18.207 60.728 36.022 1.00 56.47 C ANISOU 71 CB TYR A 10 7819 5095 8541 -122 -233 2183 C ATOM 72 CG TYR A 10 17.187 61.557 36.787 1.00 59.04 C ANISOU 72 CG TYR A 10 8190 5312 8929 -36 -289 2202 C ATOM 73 CD1 TYR A 10 16.974 62.903 36.483 1.00 54.24 C ANISOU 73 CD1 TYR A 10 7642 4559 8406 -21 -235 2329 C ATOM 74 CD2 TYR A 10 16.435 60.990 37.813 1.00 49.25 C ANISOU 74 CD2 TYR A 10 6932 4114 7668 35 -389 2099 C ATOM 75 CE1 TYR A 10 16.045 63.657 37.188 1.00 59.03 C ANISOU 75 CE1 TYR A 10 8292 5061 9076 66 -276 2344 C ATOM 76 CE2 TYR A 10 15.509 61.733 38.518 1.00 54.06 C ANISOU 76 CE2 TYR A 10 7580 4628 8331 120 -432 2115 C ATOM 77 CZ TYR A 10 15.312 63.062 38.205 1.00 71.38 C ANISOU 77 CZ TYR A 10 9837 6675 10610 138 -374 2234 C ATOM 78 OH TYR A 10 14.383 63.784 38.927 1.00 77.80 O ANISOU 78 OH TYR A 10 10690 7388 11480 231 -409 2246 O ATOM 79 N VAL A 11 20.392 61.655 38.686 1.00 67.39 N ANISOU 79 N VAL A 11 9097 6187 10320 -276 -238 1876 N ATOM 80 CA VAL A 11 20.552 61.573 40.133 1.00 67.58 C ANISOU 80 CA VAL A 11 9080 6164 10433 -280 -310 1716 C ATOM 81 C VAL A 11 19.312 62.194 40.771 1.00 79.80 C ANISOU 81 C VAL A 11 10693 7636 11993 -178 -369 1725 C ATOM 82 O VAL A 11 19.011 63.365 40.492 1.00 74.75 O ANISOU 82 O VAL A 11 10121 6859 11420 -163 -325 1820 O ATOM 83 CB VAL A 11 21.828 62.284 40.598 1.00 65.92 C ANISOU 83 CB VAL A 11 8834 5827 10386 -396 -264 1654 C ATOM 84 CG1 VAL A 11 22.001 62.143 42.106 1.00 51.42 C ANISOU 84 CG1 VAL A 11 6950 3962 8624 -405 -344 1483 C ATOM 85 CG2 VAL A 11 23.038 61.736 39.853 1.00 62.16 C ANISOU 85 CG2 VAL A 11 8291 5428 9899 -491 -192 1671 C ATOM 86 N PRO A 12 18.579 61.475 41.576 1.00 88.01 N ANISOU 86 N PRO A 12 11712 8756 12972 -103 -460 1640 N ATOM 87 CA PRO A 12 17.340 62.020 42.168 1.00 66.08 C ANISOU 87 CA PRO A 12 8992 5918 10197 6 -513 1655 C ATOM 88 C PRO A 12 17.614 62.931 43.361 1.00 58.49 C ANISOU 88 C PRO A 12 8044 4796 9384 -14 -525 1549 C ATOM 89 O PRO A 12 17.175 62.677 44.489 1.00 64.26 O ANISOU 89 O PRO A 12 8757 5542 10117 38 -599 1438 O ATOM 90 CB PRO A 12 16.585 60.747 42.565 1.00 57.32 C ANISOU 90 CB PRO A 12 7841 4976 8961 81 -603 1598 C ATOM 91 CG PRO A 12 17.685 59.780 42.913 1.00 57.28 C ANISOU 91 CG PRO A 12 7748 5053 8964 -3 -612 1476 C ATOM 92 CD PRO A 12 18.797 60.059 41.932 1.00 58.37 C ANISOU 92 CD PRO A 12 7879 5160 9138 -106 -515 1537 C ATOM 93 N PHE A 13 18.360 64.009 43.112 1.00 50.07 N ANISOU 93 N PHE A 13 7009 3574 8442 -93 -449 1582 N ATOM 94 CA PHE A 13 18.707 64.968 44.152 1.00 47.73 C ANISOU 94 CA PHE A 13 6734 3108 8294 -131 -451 1480 C ATOM 95 C PHE A 13 19.040 66.291 43.475 1.00 65.81 C ANISOU 95 C PHE A 13 9090 5216 10698 -181 -355 1589 C ATOM 96 O PHE A 13 19.762 66.306 42.471 1.00 67.02 O ANISOU 96 O PHE A 13 9228 5385 10853 -256 -285 1680 O ATOM 97 CB PHE A 13 19.889 64.463 44.987 1.00 64.81 C ANISOU 97 CB PHE A 13 8808 5305 10511 -239 -481 1318 C ATOM 98 CG PHE A 13 20.116 65.234 46.260 1.00 65.14 C ANISOU 98 CG PHE A 13 8864 5210 10675 -271 -510 1180 C ATOM 99 CD1 PHE A 13 20.927 66.357 46.273 1.00 60.23 C ANISOU 99 CD1 PHE A 13 8271 4411 10201 -375 -449 1171 C ATOM 100 CD2 PHE A 13 19.536 64.823 47.448 1.00 59.89 C ANISOU 100 CD2 PHE A 13 8184 4597 9975 -202 -598 1056 C ATOM 101 CE1 PHE A 13 21.146 67.068 47.447 1.00 60.36 C ANISOU 101 CE1 PHE A 13 8307 4301 10326 -415 -478 1032 C ATOM 102 CE2 PHE A 13 19.743 65.533 48.622 1.00 63.70 C ANISOU 102 CE2 PHE A 13 8684 4960 10558 -234 -625 921 C ATOM 103 CZ PHE A 13 20.550 66.657 48.622 1.00 55.00 C ANISOU 103 CZ PHE A 13 7617 3680 9601 -343 -566 904 C ATOM 104 N SER A 14 18.508 67.389 44.011 1.00 66.41 N ANISOU 104 N SER A 14 9243 5121 10871 -136 -346 1584 N ATOM 105 CA SER A 14 18.727 68.690 43.400 1.00 55.95 C ANISOU 105 CA SER A 14 7987 3605 9665 -173 -252 1696 C ATOM 106 C SER A 14 20.175 69.122 43.585 1.00 68.56 C ANISOU 106 C SER A 14 9549 5103 11396 -336 -209 1620 C ATOM 107 O SER A 14 20.790 68.852 44.618 1.00 66.13 O ANISOU 107 O SER A 14 9191 4803 11132 -402 -261 1449 O ATOM 108 CB SER A 14 17.784 69.735 44.002 1.00 54.07 C ANISOU 108 CB SER A 14 7842 3196 9504 -78 -249 1698 C ATOM 109 OG SER A 14 18.159 71.065 43.624 1.00 56.98 O ANISOU 109 OG SER A 14 8277 3347 10024 -132 -156 1776 O ATOM 110 N ASN A 15 20.719 69.801 42.571 1.00 64.59 N ANISOU 110 N ASN A 15 9068 4514 10959 -403 -114 1755 N ATOM 111 CA ASN A 15 22.071 70.340 42.622 1.00 60.07 C ANISOU 111 CA ASN A 15 8463 3834 10526 -563 -63 1712 C ATOM 112 C ASN A 15 22.082 71.807 43.035 1.00 66.05 C ANISOU 112 C ASN A 15 9305 4329 11460 -594 -17 1703 C ATOM 113 O ASN A 15 22.998 72.555 42.666 1.00 68.23 O ANISOU 113 O ASN A 15 9582 4480 11864 -713 55 1745 O ATOM 114 CB ASN A 15 22.768 70.156 41.273 1.00 72.63 C ANISOU 114 CB ASN A 15 10017 5493 12085 -628 18 1862 C ATOM 115 CG ASN A 15 24.275 70.066 41.406 1.00 61.42 C ANISOU 115 CG ASN A 15 8514 4070 10753 -792 43 1787 C ATOM 116 OD1 ASN A 15 24.789 69.782 42.485 1.00 66.48 O ANISOU 116 OD1 ASN A 15 9102 4721 11438 -850 -19 1615 O ATOM 117 ND2 ASN A 15 24.991 70.299 40.311 1.00 65.08 N ANISOU 117 ND2 ASN A 15 8958 4529 11240 -866 135 1922 N ATOM 118 N LYS A 16 21.065 72.231 43.788 1.00 75.65 N ANISOU 118 N LYS A 16 10594 5460 12691 -487 -54 1652 N ATOM 119 CA LYS A 16 20.979 73.623 44.228 1.00 71.75 C ANISOU 119 CA LYS A 16 10191 4705 12365 -503 -6 1633 C ATOM 120 C LYS A 16 22.206 74.021 45.032 1.00 65.96 C ANISOU 120 C LYS A 16 9427 3868 11766 -669 -12 1468 C ATOM 121 O LYS A 16 22.707 75.144 44.902 1.00 78.96 O ANISOU 121 O LYS A 16 11125 5370 13508 -747 59 1472 O ATOM 122 CB LYS A 16 19.719 73.818 45.066 1.00 71.14 C ANISOU 122 CB LYS A 16 10184 4597 12248 -354 -53 1567 C ATOM 123 CG LYS A 16 18.827 74.952 44.632 1.00103.36 C ANISOU 123 CG LYS A 16 14375 8574 16323 -250 22 1677 C ATOM 124 CD LYS A 16 17.385 74.663 45.022 1.00122.60 C ANISOU 124 CD LYS A 16 16847 11078 18657 -68 -27 1686 C ATOM 125 CE LYS A 16 17.305 73.863 46.319 1.00127.90 C ANISOU 125 CE LYS A 16 17474 11800 19323 -56 -133 1500 C ATOM 126 NZ LYS A 16 15.905 73.473 46.636 1.00140.87 N ANISOU 126 NZ LYS A 16 19138 13534 20853 123 -182 1523 N ATOM 127 N THR A 17 22.699 73.111 45.872 1.00 75.97 N ANISOU 127 N THR A 17 10609 5274 12980 -719 -98 1303 N ATOM 128 CA THR A 17 23.865 73.357 46.708 1.00 67.10 C ANISOU 128 CA THR A 17 9439 4087 11969 -880 -121 1139 C ATOM 129 C THR A 17 25.175 72.991 46.021 1.00 74.47 C ANISOU 129 C THR A 17 10273 5098 12924 -1025 -85 1189 C ATOM 130 O THR A 17 26.246 73.291 46.561 1.00 85.97 O ANISOU 130 O THR A 17 11683 6495 14488 -1176 -93 1081 O ATOM 131 CB THR A 17 23.731 72.596 48.034 1.00 81.59 C ANISOU 131 CB THR A 17 11226 6041 13732 -857 -234 938 C ATOM 132 OG1 THR A 17 23.521 71.195 47.784 1.00 80.86 O ANISOU 132 OG1 THR A 17 11049 6201 13473 -790 -286 963 O ATOM 133 CG2 THR A 17 22.557 73.154 48.842 1.00 58.82 C ANISOU 133 CG2 THR A 17 8447 3048 10854 -732 -259 871 C ATOM 134 N GLY A 18 25.118 72.377 44.841 1.00 79.62 N ANISOU 134 N GLY A 18 10891 5884 13478 -984 -43 1349 N ATOM 135 CA GLY A 18 26.310 72.066 44.082 1.00 78.28 C ANISOU 135 CA GLY A 18 10632 5786 13325 -1108 7 1415 C ATOM 136 C GLY A 18 27.050 70.820 44.511 1.00 71.22 C ANISOU 136 C GLY A 18 9610 5098 12352 -1159 -57 1305 C ATOM 137 O GLY A 18 28.184 70.616 44.067 1.00 74.34 O ANISOU 137 O GLY A 18 9921 5542 12783 -1276 -17 1334 O ATOM 138 N VAL A 19 26.442 69.969 45.345 1.00 74.89 N ANISOU 138 N VAL A 19 10054 5689 12711 -1071 -153 1188 N ATOM 139 CA VAL A 19 27.139 68.795 45.880 1.00 68.98 C ANISOU 139 CA VAL A 19 9182 5129 11899 -1116 -217 1077 C ATOM 140 C VAL A 19 26.952 67.532 45.047 1.00 67.10 C ANISOU 140 C VAL A 19 8889 5101 11505 -1042 -211 1164 C ATOM 141 O VAL A 19 27.609 66.518 45.330 1.00 80.26 O ANISOU 141 O VAL A 19 10447 6922 13124 -1079 -247 1095 O ATOM 142 CB VAL A 19 26.685 68.489 47.324 1.00 64.96 C ANISOU 142 CB VAL A 19 8666 4654 11363 -1071 -327 896 C ATOM 143 CG1 VAL A 19 26.941 69.686 48.241 1.00 56.14 C ANISOU 143 CG1 VAL A 19 7601 3336 10393 -1156 -338 782 C ATOM 144 CG2 VAL A 19 25.215 68.076 47.351 1.00 53.30 C ANISOU 144 CG2 VAL A 19 7255 3237 9759 -892 -366 925 C ATOM 145 N VAL A 20 26.082 67.551 44.035 1.00 70.46 N ANISOU 145 N VAL A 20 9385 5539 11848 -940 -166 1312 N ATOM 146 CA VAL A 20 25.771 66.333 43.293 1.00 72.17 C ANISOU 146 CA VAL A 20 9564 5955 11904 -864 -169 1378 C ATOM 147 C VAL A 20 26.929 65.975 42.369 1.00 69.46 C ANISOU 147 C VAL A 20 9144 5684 11564 -962 -90 1452 C ATOM 148 O VAL A 20 27.538 66.846 41.735 1.00 63.36 O ANISOU 148 O VAL A 20 8388 4799 10888 -1045 -6 1544 O ATOM 149 CB VAL A 20 24.456 66.504 42.510 1.00 69.41 C ANISOU 149 CB VAL A 20 9311 5603 11459 -731 -151 1514 C ATOM 150 CG1 VAL A 20 24.141 65.255 41.680 1.00 54.89 C ANISOU 150 CG1 VAL A 20 7439 3970 9448 -666 -153 1579 C ATOM 151 CG2 VAL A 20 23.307 66.806 43.464 1.00 67.39 C ANISOU 151 CG2 VAL A 20 9122 5286 11199 -626 -225 1442 C ATOM 152 N ARG A 21 27.242 64.681 42.296 1.00 63.50 N ANISOU 152 N ARG A 21 8304 5116 10708 -950 -113 1414 N ATOM 153 CA ARG A 21 28.317 64.159 41.464 1.00 64.61 C ANISOU 153 CA ARG A 21 8364 5349 10836 -1027 -38 1472 C ATOM 154 C ARG A 21 27.797 63.033 40.580 1.00 68.69 C ANISOU 154 C ARG A 21 8882 6036 11179 -935 -24 1538 C ATOM 155 O ARG A 21 26.797 62.377 40.892 1.00 61.96 O ANISOU 155 O ARG A 21 8057 5263 10222 -828 -96 1498 O ATOM 156 CB ARG A 21 29.483 63.626 42.312 1.00 62.09 C ANISOU 156 CB ARG A 21 7919 5090 10583 -1123 -70 1345 C ATOM 157 CG ARG A 21 30.055 64.638 43.266 1.00 52.70 C ANISOU 157 CG ARG A 21 6718 3750 9555 -1228 -96 1259 C ATOM 158 CD ARG A 21 30.801 65.719 42.523 1.00 54.57 C ANISOU 158 CD ARG A 21 6971 3852 9911 -1337 2 1366 C ATOM 159 NE ARG A 21 31.303 66.747 43.433 1.00 71.54 N ANISOU 159 NE ARG A 21 9120 5840 12220 -1446 -24 1278 N ATOM 160 CZ ARG A 21 30.663 67.877 43.712 1.00 73.93 C ANISOU 160 CZ ARG A 21 9532 5959 12599 -1434 -30 1276 C ATOM 161 NH1 ARG A 21 29.488 68.138 43.153 1.00 92.21 N ANISOU 161 NH1 ARG A 21 11957 8232 14846 -1311 -11 1370 N ATOM 162 NH2 ARG A 21 31.196 68.747 44.552 1.00 72.17 N ANISOU 162 NH2 ARG A 21 9307 5595 12520 -1545 -53 1181 N ATOM 163 N SER A 22 28.509 62.811 39.477 1.00 61.79 N ANISOU 163 N SER A 22 7977 5222 10278 -982 70 1638 N ATOM 164 CA SER A 22 28.201 61.708 38.575 1.00 54.88 C ANISOU 164 CA SER A 22 7100 4513 9239 -914 95 1690 C ATOM 165 C SER A 22 28.210 60.389 39.347 1.00 60.00 C ANISOU 165 C SER A 22 7674 5299 9826 -876 20 1555 C ATOM 166 O SER A 22 29.191 60.092 40.044 1.00 61.29 O ANISOU 166 O SER A 22 7738 5479 10070 -946 9 1464 O ATOM 167 CB SER A 22 29.227 61.678 37.439 1.00 58.85 C ANISOU 167 CB SER A 22 7562 5056 9741 -989 216 1793 C ATOM 168 OG SER A 22 29.094 60.544 36.599 1.00 64.50 O ANISOU 168 OG SER A 22 8269 5937 10301 -935 248 1822 O ATOM 169 N PRO A 23 27.146 59.581 39.268 1.00 60.04 N ANISOU 169 N PRO A 23 7719 5402 9693 -767 -35 1543 N ATOM 170 CA PRO A 23 27.156 58.287 39.974 1.00 59.09 C ANISOU 170 CA PRO A 23 7526 5408 9518 -730 -101 1424 C ATOM 171 C PRO A 23 28.195 57.310 39.429 1.00 58.69 C ANISOU 171 C PRO A 23 7389 5473 9438 -774 -31 1420 C ATOM 172 O PRO A 23 28.386 56.237 40.021 1.00 53.74 O ANISOU 172 O PRO A 23 6689 4942 8787 -752 -74 1325 O ATOM 173 CB PRO A 23 25.722 57.763 39.779 1.00 51.07 C ANISOU 173 CB PRO A 23 6584 4460 8360 -611 -161 1443 C ATOM 174 CG PRO A 23 25.251 58.423 38.525 1.00 57.73 C ANISOU 174 CG PRO A 23 7518 5272 9143 -595 -94 1594 C ATOM 175 CD PRO A 23 25.909 59.782 38.490 1.00 61.93 C ANISOU 175 CD PRO A 23 8064 5649 9820 -677 -36 1648 C ATOM 176 N PHE A 24 28.874 57.655 38.337 1.00 60.93 N ANISOU 176 N PHE A 24 7677 5749 9726 -830 79 1523 N ATOM 177 CA PHE A 24 29.994 56.880 37.828 1.00 61.33 C ANISOU 177 CA PHE A 24 7641 5893 9768 -878 162 1525 C ATOM 178 C PHE A 24 31.343 57.336 38.381 1.00 65.84 C ANISOU 178 C PHE A 24 8108 6408 10499 -990 193 1494 C ATOM 179 O PHE A 24 32.351 56.678 38.110 1.00 78.68 O ANISOU 179 O PHE A 24 9645 8115 12136 -1029 259 1490 O ATOM 180 CB PHE A 24 30.035 56.956 36.294 1.00 51.24 C ANISOU 180 CB PHE A 24 6419 4655 8396 -878 273 1658 C ATOM 181 CG PHE A 24 28.776 56.488 35.623 1.00 55.32 C ANISOU 181 CG PHE A 24 7033 5244 8743 -781 248 1697 C ATOM 182 CD1 PHE A 24 28.238 55.238 35.908 1.00 54.19 C ANISOU 182 CD1 PHE A 24 6880 5211 8499 -710 188 1610 C ATOM 183 CD2 PHE A 24 28.112 57.310 34.708 1.00 53.44 C ANISOU 183 CD2 PHE A 24 6892 4964 8447 -763 281 1828 C ATOM 184 CE1 PHE A 24 27.053 54.802 35.284 1.00 45.74 C ANISOU 184 CE1 PHE A 24 5897 4212 7271 -630 158 1646 C ATOM 185 CE2 PHE A 24 26.937 56.885 34.086 1.00 65.85 C ANISOU 185 CE2 PHE A 24 8547 6616 9857 -679 250 1870 C ATOM 186 CZ PHE A 24 26.409 55.621 34.380 1.00 61.85 C ANISOU 186 CZ PHE A 24 8029 6222 9248 -616 186 1774 C ATOM 187 N GLU A 25 31.396 58.428 39.152 1.00 67.15 N ANISOU 187 N GLU A 25 8282 6440 10790 -1044 148 1471 N ATOM 188 CA GLU A 25 32.673 59.062 39.481 1.00 66.55 C ANISOU 188 CA GLU A 25 8119 6299 10868 -1169 186 1465 C ATOM 189 C GLU A 25 32.925 59.325 40.960 1.00 63.42 C ANISOU 189 C GLU A 25 7663 5849 10584 -1216 87 1337 C ATOM 190 O GLU A 25 34.090 59.506 41.329 1.00 76.72 O ANISOU 190 O GLU A 25 9245 7525 12380 -1321 107 1312 O ATOM 191 CB GLU A 25 32.819 60.398 38.737 1.00 57.39 C ANISOU 191 CB GLU A 25 7023 5003 9778 -1233 261 1587 C ATOM 192 CG GLU A 25 32.711 60.314 37.214 1.00 92.24 C ANISOU 192 CG GLU A 25 11490 9466 14088 -1204 370 1732 C ATOM 193 CD GLU A 25 33.915 59.663 36.539 1.00109.80 C ANISOU 193 CD GLU A 25 13617 11796 16306 -1257 473 1769 C ATOM 194 OE1 GLU A 25 34.812 59.143 37.239 1.00110.56 O ANISOU 194 OE1 GLU A 25 13596 11940 16472 -1306 458 1685 O ATOM 195 OE2 GLU A 25 33.962 59.676 35.290 1.00115.44 O ANISOU 195 OE2 GLU A 25 14369 12550 16942 -1247 573 1888 O ATOM 196 N ALA A 26 31.908 59.365 41.813 1.00 66.83 N ANISOU 196 N ALA A 26 8151 6253 10989 -1146 -17 1257 N ATOM 197 CA ALA A 26 32.108 59.781 43.196 1.00 61.79 C ANISOU 197 CA ALA A 26 7470 5555 10453 -1196 -107 1137 C ATOM 198 C ALA A 26 30.950 59.256 44.029 1.00 57.55 C ANISOU 198 C ALA A 26 6972 5060 9833 -1084 -215 1049 C ATOM 199 O ALA A 26 29.866 59.007 43.495 1.00 60.72 O ANISOU 199 O ALA A 26 7463 5484 10125 -980 -219 1098 O ATOM 200 CB ALA A 26 32.210 61.314 43.304 1.00 50.52 C ANISOU 200 CB ALA A 26 6104 3940 9149 -1279 -93 1162 C ATOM 201 N PRO A 27 31.148 59.070 45.337 1.00 74.70 N ANISOU 201 N PRO A 27 9077 7254 12052 -1104 -305 923 N ATOM 202 CA PRO A 27 30.071 58.520 46.172 1.00 65.20 C ANISOU 202 CA PRO A 27 7902 6103 10769 -995 -407 842 C ATOM 203 C PRO A 27 28.858 59.442 46.226 1.00 63.20 C ANISOU 203 C PRO A 27 7786 5728 10501 -932 -436 859 C ATOM 204 O PRO A 27 28.939 60.644 45.970 1.00 77.98 O ANISOU 204 O PRO A 27 9723 7452 12455 -986 -396 901 O ATOM 205 CB PRO A 27 30.729 58.373 47.553 1.00 61.16 C ANISOU 205 CB PRO A 27 7285 5626 10329 -1055 -486 713 C ATOM 206 CG PRO A 27 32.201 58.288 47.263 1.00 61.90 C ANISOU 206 CG PRO A 27 7264 5751 10504 -1173 -421 738 C ATOM 207 CD PRO A 27 32.415 59.190 46.082 1.00 47.87 C ANISOU 207 CD PRO A 27 5557 3863 8767 -1225 -318 855 C ATOM 208 N GLN A 28 27.712 58.851 46.551 1.00 71.24 N ANISOU 208 N GLN A 28 8844 6807 11416 -812 -502 832 N ATOM 209 CA GLN A 28 26.429 59.547 46.567 1.00 64.73 C ANISOU 209 CA GLN A 28 8141 5892 10559 -726 -530 859 C ATOM 210 C GLN A 28 25.906 59.714 47.988 1.00 67.61 C ANISOU 210 C GLN A 28 8509 6237 10944 -690 -631 735 C ATOM 211 O GLN A 28 24.706 59.586 48.246 1.00 66.26 O ANISOU 211 O GLN A 28 8398 6080 10698 -578 -681 732 O ATOM 212 CB GLN A 28 25.403 58.807 45.712 1.00 57.27 C ANISOU 212 CB GLN A 28 7249 5037 9473 -613 -523 944 C ATOM 213 CG GLN A 28 25.852 58.544 44.284 1.00 63.37 C ANISOU 213 CG GLN A 28 8024 5850 10202 -641 -424 1062 C ATOM 214 CD GLN A 28 25.853 59.800 43.433 1.00 69.37 C ANISOU 214 CD GLN A 28 8869 6474 11016 -678 -346 1175 C ATOM 215 OE1 GLN A 28 24.833 60.484 43.313 1.00 62.08 O ANISOU 215 OE1 GLN A 28 8042 5472 10073 -612 -360 1227 O ATOM 216 NE2 GLN A 28 27.002 60.113 42.840 1.00 61.01 N ANISOU 216 NE2 GLN A 28 7769 5384 10027 -782 -262 1221 N ATOM 217 N TYR A 29 26.804 60.007 48.927 1.00 66.24 N ANISOU 217 N TYR A 29 8265 6037 10866 -785 -661 632 N ATOM 218 CA TYR A 29 26.455 60.133 50.344 1.00 70.36 C ANISOU 218 CA TYR A 29 8778 6556 11401 -764 -757 500 C ATOM 219 C TYR A 29 25.581 61.348 50.654 1.00 74.06 C ANISOU 219 C TYR A 29 9371 6863 11906 -726 -767 487 C ATOM 220 O TYR A 29 25.296 61.587 51.837 1.00 79.46 O ANISOU 220 O TYR A 29 10058 7528 12603 -711 -839 371 O ATOM 221 CB TYR A 29 27.732 60.175 51.182 1.00 62.77 C ANISOU 221 CB TYR A 29 7706 5615 10530 -892 -783 400 C ATOM 222 CG TYR A 29 28.513 58.888 51.131 1.00 68.22 C ANISOU 222 CG TYR A 29 8260 6477 11184 -909 -786 401 C ATOM 223 CD1 TYR A 29 27.862 57.656 51.136 1.00 68.70 C ANISOU 223 CD1 TYR A 29 8294 6677 11131 -797 -820 411 C ATOM 224 CD2 TYR A 29 29.898 58.898 51.060 1.00 59.55 C ANISOU 224 CD2 TYR A 29 7059 5398 10170 -1036 -750 398 C ATOM 225 CE1 TYR A 29 28.574 56.473 51.086 1.00 54.24 C ANISOU 225 CE1 TYR A 29 6343 4990 9277 -807 -814 413 C ATOM 226 CE2 TYR A 29 30.619 57.723 51.003 1.00 49.07 C ANISOU 226 CE2 TYR A 29 5605 4224 8817 -1043 -743 406 C ATOM 227 CZ TYR A 29 29.957 56.511 51.019 1.00 59.97 C ANISOU 227 CZ TYR A 29 6966 5732 10089 -926 -773 412 C ATOM 228 OH TYR A 29 30.686 55.338 50.966 1.00 67.14 O ANISOU 228 OH TYR A 29 7749 6780 10979 -929 -758 421 O ATOM 229 N TYR A 30 25.151 62.108 49.648 1.00 75.80 N ANISOU 229 N TYR A 30 9691 6969 12141 -705 -695 602 N ATOM 230 CA TYR A 30 24.238 63.223 49.843 1.00 76.17 C ANISOU 230 CA TYR A 30 9859 6859 12222 -650 -693 609 C ATOM 231 C TYR A 30 22.776 62.863 49.593 1.00 75.92 C ANISOU 231 C TYR A 30 9895 6877 12076 -491 -717 675 C ATOM 232 O TYR A 30 21.900 63.688 49.873 1.00 88.29 O ANISOU 232 O TYR A 30 11555 8329 13661 -423 -721 677 O ATOM 233 CB TYR A 30 24.635 64.395 48.937 1.00 70.43 C ANISOU 233 CB TYR A 30 9200 5962 11597 -724 -596 708 C ATOM 234 CG TYR A 30 24.860 63.991 47.501 1.00 69.18 C ANISOU 234 CG TYR A 30 9031 5864 11389 -727 -518 860 C ATOM 235 CD1 TYR A 30 23.783 63.741 46.650 1.00 64.78 C ANISOU 235 CD1 TYR A 30 8540 5348 10726 -609 -500 980 C ATOM 236 CD2 TYR A 30 26.148 63.845 46.996 1.00 53.14 C ANISOU 236 CD2 TYR A 30 6921 3858 9411 -849 -463 885 C ATOM 237 CE1 TYR A 30 23.986 63.356 45.335 1.00 63.34 C ANISOU 237 CE1 TYR A 30 8350 5232 10484 -615 -430 1112 C ATOM 238 CE2 TYR A 30 26.360 63.467 45.677 1.00 61.05 C ANISOU 238 CE2 TYR A 30 7915 4921 10358 -849 -386 1020 C ATOM 239 CZ TYR A 30 25.276 63.224 44.853 1.00 71.51 C ANISOU 239 CZ TYR A 30 9312 6287 11570 -733 -370 1129 C ATOM 240 OH TYR A 30 25.483 62.848 43.545 1.00 72.38 O ANISOU 240 OH TYR A 30 9418 6467 11614 -736 -294 1257 O ATOM 241 N LEU A 31 22.483 61.676 49.059 1.00 61.84 N ANISOU 241 N LEU A 31 8066 5255 10175 -430 -729 730 N ATOM 242 CA LEU A 31 21.102 61.221 48.934 1.00 65.73 C ANISOU 242 CA LEU A 31 8607 5814 10553 -287 -767 781 C ATOM 243 C LEU A 31 20.801 60.008 49.798 1.00 53.68 C ANISOU 243 C LEU A 31 7003 4449 8944 -229 -855 693 C ATOM 244 O LEU A 31 19.657 59.543 49.816 1.00 76.35 O ANISOU 244 O LEU A 31 9901 7388 11721 -114 -897 726 O ATOM 245 CB LEU A 31 20.749 60.922 47.472 1.00 62.89 C ANISOU 245 CB LEU A 31 8281 5501 10114 -252 -707 937 C ATOM 246 CG LEU A 31 21.728 60.183 46.574 1.00 64.92 C ANISOU 246 CG LEU A 31 8472 5849 10347 -330 -654 981 C ATOM 247 CD1 LEU A 31 21.710 58.707 46.863 1.00 56.65 C ANISOU 247 CD1 LEU A 31 7339 4979 9205 -295 -708 926 C ATOM 248 CD2 LEU A 31 21.344 60.433 45.141 1.00 72.36 C ANISOU 248 CD2 LEU A 31 9481 6779 11234 -306 -581 1140 C ATOM 249 N ALA A 32 21.795 59.481 50.501 1.00 60.53 N ANISOU 249 N ALA A 32 7770 5383 9846 -307 -885 590 N ATOM 250 CA ALA A 32 21.577 58.502 51.553 1.00 59.26 C ANISOU 250 CA ALA A 32 7533 5356 9629 -259 -973 495 C ATOM 251 C ALA A 32 22.799 58.528 52.453 1.00 62.54 C ANISOU 251 C ALA A 32 7855 5781 10125 -370 -996 379 C ATOM 252 O ALA A 32 23.915 58.762 51.977 1.00 68.66 O ANISOU 252 O ALA A 32 8594 6522 10973 -481 -941 396 O ATOM 253 CB ALA A 32 21.349 57.097 50.991 1.00 56.04 C ANISOU 253 CB ALA A 32 7069 5108 9115 -206 -982 549 C ATOM 254 N GLU A 33 22.588 58.316 53.752 1.00 43.23 N ANISOU 254 N GLU A 33 5370 3388 7667 -341 -1079 267 N ATOM 255 CA GLU A 33 23.735 58.250 54.645 1.00 59.88 C ANISOU 255 CA GLU A 33 7380 5534 9840 -447 -1112 160 C ATOM 256 C GLU A 33 24.583 57.025 54.307 1.00 68.95 C ANISOU 256 C GLU A 33 8404 6827 10967 -483 -1101 187 C ATOM 257 O GLU A 33 24.090 56.065 53.702 1.00 66.11 O ANISOU 257 O GLU A 33 8035 6558 10526 -405 -1092 258 O ATOM 258 CB GLU A 33 23.279 58.178 56.095 1.00 66.61 C ANISOU 258 CB GLU A 33 8210 6435 10662 -400 -1205 40 C ATOM 259 CG GLU A 33 22.165 59.115 56.448 1.00 75.37 C ANISOU 259 CG GLU A 33 9442 7431 11765 -320 -1216 19 C ATOM 260 CD GLU A 33 22.452 59.841 57.731 1.00100.21 C ANISOU 260 CD GLU A 33 12589 10526 14959 -372 -1265 -126 C ATOM 261 OE1 GLU A 33 23.497 60.524 57.784 1.00101.78 O ANISOU 261 OE1 GLU A 33 12774 10644 15254 -506 -1242 -175 O ATOM 262 OE2 GLU A 33 21.655 59.705 58.687 1.00107.52 O ANISOU 262 OE2 GLU A 33 13526 11502 15825 -284 -1328 -193 O ATOM 263 N PRO A 34 25.866 57.038 54.675 1.00 63.44 N ANISOU 263 N PRO A 34 7609 6152 10343 -602 -1100 134 N ATOM 264 CA PRO A 34 26.687 55.826 54.479 1.00 53.04 C ANISOU 264 CA PRO A 34 6164 4979 9012 -626 -1090 158 C ATOM 265 C PRO A 34 26.094 54.578 55.114 1.00 59.60 C ANISOU 265 C PRO A 34 6931 5961 9752 -522 -1158 134 C ATOM 266 O PRO A 34 26.183 53.494 54.522 1.00 76.50 O ANISOU 266 O PRO A 34 9022 8197 11849 -486 -1130 194 O ATOM 267 CB PRO A 34 28.031 56.207 55.114 1.00 41.31 C ANISOU 267 CB PRO A 34 4580 3493 7624 -765 -1100 87 C ATOM 268 CG PRO A 34 28.107 57.680 54.957 1.00 42.78 C ANISOU 268 CG PRO A 34 4864 3500 7890 -840 -1069 73 C ATOM 269 CD PRO A 34 26.680 58.203 55.063 1.00 45.84 C ANISOU 269 CD PRO A 34 5389 3805 8225 -728 -1091 70 C ATOM 270 N TRP A 35 25.467 54.695 56.291 1.00 53.01 N ANISOU 270 N TRP A 35 6103 5152 8889 -472 -1243 50 N ATOM 271 CA TRP A 35 24.905 53.506 56.927 1.00 49.97 C ANISOU 271 CA TRP A 35 5652 4914 8422 -375 -1308 36 C ATOM 272 C TRP A 35 23.781 52.900 56.096 1.00 54.59 C ANISOU 272 C TRP A 35 6305 5517 8921 -261 -1288 125 C ATOM 273 O TRP A 35 23.559 51.688 56.159 1.00 69.19 O ANISOU 273 O TRP A 35 8089 7486 10714 -199 -1311 147 O ATOM 274 CB TRP A 35 24.423 53.818 58.353 1.00 48.65 C ANISOU 274 CB TRP A 35 5481 4772 8233 -342 -1400 -68 C ATOM 275 CG TRP A 35 23.109 54.576 58.475 1.00 62.49 C ANISOU 275 CG TRP A 35 7366 6432 9945 -253 -1416 -74 C ATOM 276 CD1 TRP A 35 22.962 55.916 58.677 1.00 54.77 C ANISOU 276 CD1 TRP A 35 6485 5308 9015 -286 -1405 -124 C ATOM 277 CD2 TRP A 35 21.777 54.028 58.447 1.00 67.52 C ANISOU 277 CD2 TRP A 35 8046 7118 10489 -114 -1444 -29 C ATOM 278 NE1 TRP A 35 21.632 56.242 58.757 1.00 65.39 N ANISOU 278 NE1 TRP A 35 7932 6609 10306 -170 -1419 -107 N ATOM 279 CE2 TRP A 35 20.881 55.106 58.620 1.00 67.42 C ANISOU 279 CE2 TRP A 35 8154 6988 10473 -65 -1445 -47 C ATOM 280 CE3 TRP A 35 21.255 52.737 58.284 1.00 68.76 C ANISOU 280 CE3 TRP A 35 8151 7403 10571 -29 -1465 28 C ATOM 281 CZ2 TRP A 35 19.488 54.937 58.628 1.00 54.71 C ANISOU 281 CZ2 TRP A 35 6607 5395 8786 68 -1468 -2 C ATOM 282 CZ3 TRP A 35 19.865 52.568 58.296 1.00 56.84 C ANISOU 282 CZ3 TRP A 35 6706 5907 8983 94 -1493 67 C ATOM 283 CH2 TRP A 35 19.004 53.661 58.468 1.00 54.86 C ANISOU 283 CH2 TRP A 35 6567 5549 8729 143 -1496 55 C ATOM 284 N GLN A 36 23.070 53.710 55.306 1.00 63.51 N ANISOU 284 N GLN A 36 7561 6528 10041 -233 -1247 182 N ATOM 285 CA GLN A 36 22.034 53.144 54.444 1.00 61.90 C ANISOU 285 CA GLN A 36 7417 6351 9750 -136 -1230 273 C ATOM 286 C GLN A 36 22.644 52.416 53.255 1.00 55.04 C ANISOU 286 C GLN A 36 6519 5522 8872 -171 -1157 349 C ATOM 287 O GLN A 36 22.123 51.378 52.825 1.00 53.89 O ANISOU 287 O GLN A 36 6362 5463 8650 -105 -1161 394 O ATOM 288 CB GLN A 36 21.074 54.232 53.976 1.00 51.46 C ANISOU 288 CB GLN A 36 6232 4903 8418 -90 -1209 321 C ATOM 289 CG GLN A 36 20.290 54.859 55.114 1.00 57.55 C ANISOU 289 CG GLN A 36 7042 5639 9184 -31 -1275 250 C ATOM 290 CD GLN A 36 19.528 56.094 54.682 1.00 63.32 C ANISOU 290 CD GLN A 36 7905 6222 9932 4 -1240 295 C ATOM 291 OE1 GLN A 36 20.105 57.052 54.154 1.00 64.43 O ANISOU 291 OE1 GLN A 36 8095 6236 10150 -75 -1178 313 O ATOM 292 NE2 GLN A 36 18.226 56.077 54.902 1.00 61.01 N ANISOU 292 NE2 GLN A 36 7666 5944 9573 123 -1276 322 N ATOM 293 N PHE A 37 23.754 52.934 52.716 1.00 57.95 N ANISOU 293 N PHE A 37 6873 5829 9317 -277 -1088 362 N ATOM 294 CA PHE A 37 24.497 52.188 51.705 1.00 56.85 C ANISOU 294 CA PHE A 37 6687 5739 9172 -314 -1014 423 C ATOM 295 C PHE A 37 25.016 50.874 52.275 1.00 56.78 C ANISOU 295 C PHE A 37 6550 5868 9155 -303 -1043 383 C ATOM 296 O PHE A 37 25.024 49.849 51.585 1.00 54.38 O ANISOU 296 O PHE A 37 6224 5635 8803 -272 -1006 428 O ATOM 297 CB PHE A 37 25.650 53.027 51.162 1.00 37.62 C ANISOU 297 CB PHE A 37 4247 3218 6830 -432 -937 443 C ATOM 298 CG PHE A 37 25.233 54.048 50.151 1.00 67.65 C ANISOU 298 CG PHE A 37 8173 6898 10633 -439 -876 523 C ATOM 299 CD1 PHE A 37 25.154 53.716 48.806 1.00 64.59 C ANISOU 299 CD1 PHE A 37 7827 6523 10190 -426 -799 621 C ATOM 300 CD2 PHE A 37 24.916 55.343 50.541 1.00 67.45 C ANISOU 300 CD2 PHE A 37 8223 6743 10661 -457 -893 501 C ATOM 301 CE1 PHE A 37 24.760 54.660 47.865 1.00 70.96 C ANISOU 301 CE1 PHE A 37 8742 7227 10992 -430 -744 707 C ATOM 302 CE2 PHE A 37 24.521 56.291 49.606 1.00 65.60 C ANISOU 302 CE2 PHE A 37 8099 6391 10434 -458 -833 587 C ATOM 303 CZ PHE A 37 24.443 55.949 48.265 1.00 70.83 C ANISOU 303 CZ PHE A 37 8796 7079 11038 -444 -760 696 C ATOM 304 N SER A 38 25.431 50.885 53.543 1.00 54.41 N ANISOU 304 N SER A 38 6164 5608 8899 -327 -1109 300 N ATOM 305 CA SER A 38 25.846 49.655 54.206 1.00 54.73 C ANISOU 305 CA SER A 38 6076 5784 8933 -306 -1144 270 C ATOM 306 C SER A 38 24.681 48.682 54.371 1.00 55.53 C ANISOU 306 C SER A 38 6194 5963 8942 -187 -1193 285 C ATOM 307 O SER A 38 24.871 47.463 54.277 1.00 50.19 O ANISOU 307 O SER A 38 5444 5381 8246 -155 -1184 303 O ATOM 308 CB SER A 38 26.463 49.982 55.559 1.00 42.20 C ANISOU 308 CB SER A 38 4400 4232 7404 -358 -1212 182 C ATOM 309 OG SER A 38 27.753 50.521 55.393 1.00 60.66 O ANISOU 309 OG SER A 38 6682 6533 9831 -479 -1166 176 O ATOM 310 N MET A 39 23.474 49.196 54.632 1.00 52.13 N ANISOU 310 N MET A 39 5855 5491 8459 -119 -1244 279 N ATOM 311 CA MET A 39 22.302 48.328 54.734 1.00 55.10 C ANISOU 311 CA MET A 39 6249 5938 8748 -9 -1290 303 C ATOM 312 C MET A 39 21.905 47.785 53.369 1.00 55.14 C ANISOU 312 C MET A 39 6315 5940 8695 16 -1229 386 C ATOM 313 O MET A 39 21.452 46.638 53.262 1.00 55.00 O ANISOU 313 O MET A 39 6269 6004 8624 74 -1245 406 O ATOM 314 CB MET A 39 21.128 49.072 55.382 1.00 50.62 C ANISOU 314 CB MET A 39 5759 5332 8143 58 -1356 281 C ATOM 315 CG MET A 39 21.258 49.237 56.895 1.00 63.66 C ANISOU 315 CG MET A 39 7341 7029 9816 62 -1434 191 C ATOM 316 SD MET A 39 21.899 47.740 57.695 1.00 67.99 S ANISOU 316 SD MET A 39 7723 7741 10367 71 -1473 167 S ATOM 317 CE MET A 39 20.534 46.621 57.385 1.00 62.52 C ANISOU 317 CE MET A 39 7057 7117 9579 194 -1500 233 C ATOM 318 N LEU A 40 22.062 48.593 52.316 1.00 54.48 N ANISOU 318 N LEU A 40 6316 5763 8621 -29 -1159 434 N ATOM 319 CA LEU A 40 21.912 48.076 50.958 1.00 53.44 C ANISOU 319 CA LEU A 40 6233 5639 8432 -23 -1091 509 C ATOM 320 C LEU A 40 22.856 46.901 50.715 1.00 69.27 C ANISOU 320 C LEU A 40 8142 7721 10454 -51 -1045 501 C ATOM 321 O LEU A 40 22.447 45.858 50.189 1.00 61.44 O ANISOU 321 O LEU A 40 7155 6789 9398 -7 -1033 527 O ATOM 322 CB LEU A 40 22.173 49.192 49.947 1.00 53.25 C ANISOU 322 CB LEU A 40 6297 5508 8429 -81 -1017 564 C ATOM 323 CG LEU A 40 22.245 48.776 48.475 1.00 55.06 C ANISOU 323 CG LEU A 40 6574 5748 8599 -93 -933 640 C ATOM 324 CD1 LEU A 40 20.925 48.194 48.028 1.00 41.60 C ANISOU 324 CD1 LEU A 40 4934 4092 6781 -8 -969 683 C ATOM 325 CD2 LEU A 40 22.619 49.954 47.602 1.00 63.58 C ANISOU 325 CD2 LEU A 40 7725 6724 9710 -155 -859 698 C ATOM 326 N ALA A 41 24.129 47.053 51.102 1.00 67.44 N ANISOU 326 N ALA A 41 7822 7489 10313 -125 -1016 466 N ATOM 327 CA ALA A 41 25.096 45.970 50.946 1.00 58.10 C ANISOU 327 CA ALA A 41 6536 6380 9160 -146 -966 464 C ATOM 328 C ALA A 41 24.709 44.762 51.781 1.00 63.45 C ANISOU 328 C ALA A 41 7137 7157 9814 -74 -1030 434 C ATOM 329 O ALA A 41 24.872 43.616 51.347 1.00 59.95 O ANISOU 329 O ALA A 41 6657 6768 9352 -49 -990 451 O ATOM 330 CB ALA A 41 26.491 46.445 51.344 1.00 38.93 C ANISOU 330 CB ALA A 41 4014 3940 6836 -239 -936 438 C ATOM 331 N ALA A 42 24.222 45.000 52.999 1.00 56.44 N ANISOU 331 N ALA A 42 6221 6293 8930 -41 -1126 389 N ATOM 332 CA ALA A 42 23.803 43.902 53.855 1.00 53.38 C ANISOU 332 CA ALA A 42 5758 6004 8521 30 -1190 370 C ATOM 333 C ALA A 42 22.640 43.142 53.228 1.00 63.53 C ANISOU 333 C ALA A 42 7115 7306 9718 106 -1197 409 C ATOM 334 O ALA A 42 22.582 41.908 53.292 1.00 57.09 O ANISOU 334 O ALA A 42 6243 6559 8891 147 -1196 416 O ATOM 335 CB ALA A 42 23.425 44.435 55.235 1.00 43.65 C ANISOU 335 CB ALA A 42 4495 4793 7296 51 -1289 316 C ATOM 336 N TYR A 43 21.716 43.859 52.594 1.00 53.18 N ANISOU 336 N TYR A 43 5926 5933 8345 123 -1200 440 N ATOM 337 CA TYR A 43 20.596 43.173 51.967 1.00 57.03 C ANISOU 337 CA TYR A 43 6480 6445 8743 186 -1213 482 C ATOM 338 C TYR A 43 21.056 42.344 50.774 1.00 56.83 C ANISOU 338 C TYR A 43 6467 6429 8698 160 -1124 510 C ATOM 339 O TYR A 43 20.589 41.214 50.587 1.00 62.03 O ANISOU 339 O TYR A 43 7116 7140 9314 202 -1132 517 O ATOM 340 CB TYR A 43 19.508 44.165 51.550 1.00 51.50 C ANISOU 340 CB TYR A 43 5901 5685 7982 211 -1237 520 C ATOM 341 CG TYR A 43 18.238 43.429 51.247 1.00 56.91 C ANISOU 341 CG TYR A 43 6630 6418 8575 282 -1279 558 C ATOM 342 CD1 TYR A 43 17.541 42.788 52.264 1.00 63.95 C ANISOU 342 CD1 TYR A 43 7466 7379 9452 349 -1362 540 C ATOM 343 CD2 TYR A 43 17.761 43.320 49.945 1.00 47.01 C ANISOU 343 CD2 TYR A 43 5465 5151 7246 276 -1237 614 C ATOM 344 CE1 TYR A 43 16.388 42.085 52.004 1.00 71.00 C ANISOU 344 CE1 TYR A 43 8390 8318 10267 407 -1403 578 C ATOM 345 CE2 TYR A 43 16.600 42.612 49.675 1.00 61.86 C ANISOU 345 CE2 TYR A 43 7379 7083 9040 330 -1282 648 C ATOM 346 CZ TYR A 43 15.919 41.996 50.713 1.00 73.66 C ANISOU 346 CZ TYR A 43 8815 8640 10531 394 -1366 630 C ATOM 347 OH TYR A 43 14.762 41.282 50.474 1.00 76.52 O ANISOU 347 OH TYR A 43 9204 9055 10814 442 -1414 666 O ATOM 348 N MET A 44 21.963 42.885 49.951 1.00 51.16 N ANISOU 348 N MET A 44 5771 5658 8010 90 -1037 524 N ATOM 349 CA MET A 44 22.515 42.093 48.854 1.00 60.05 C ANISOU 349 CA MET A 44 6902 6797 9117 66 -942 544 C ATOM 350 C MET A 44 23.267 40.870 49.370 1.00 62.37 C ANISOU 350 C MET A 44 7077 7154 9468 78 -924 511 C ATOM 351 O MET A 44 23.243 39.813 48.728 1.00 62.69 O ANISOU 351 O MET A 44 7124 7221 9475 96 -876 516 O ATOM 352 CB MET A 44 23.440 42.941 47.983 1.00 50.07 C ANISOU 352 CB MET A 44 5670 5472 7884 -10 -848 570 C ATOM 353 CG MET A 44 22.767 44.117 47.307 1.00 62.71 C ANISOU 353 CG MET A 44 7390 7004 9432 -22 -848 618 C ATOM 354 SD MET A 44 21.460 43.607 46.186 1.00 58.91 S ANISOU 354 SD MET A 44 7026 6550 8808 27 -852 668 S ATOM 355 CE MET A 44 20.022 44.227 47.051 1.00 53.97 C ANISOU 355 CE MET A 44 6442 5914 8149 95 -975 677 C ATOM 356 N PHE A 45 23.937 40.992 50.521 1.00 51.16 N ANISOU 356 N PHE A 45 5547 5759 8132 67 -960 479 N ATOM 357 CA PHE A 45 24.602 39.835 51.118 1.00 56.52 C ANISOU 357 CA PHE A 45 6101 6506 8869 88 -951 461 C ATOM 358 C PHE A 45 23.589 38.756 51.500 1.00 59.74 C ANISOU 358 C PHE A 45 6505 6965 9229 168 -1011 459 C ATOM 359 O PHE A 45 23.805 37.569 51.229 1.00 55.50 O ANISOU 359 O PHE A 45 5930 6457 8702 192 -965 462 O ATOM 360 CB PHE A 45 25.422 40.277 52.334 1.00 42.03 C ANISOU 360 CB PHE A 45 4148 4701 7121 58 -993 433 C ATOM 361 CG PHE A 45 26.310 39.202 52.906 1.00 50.21 C ANISOU 361 CG PHE A 45 5039 5810 8228 72 -972 429 C ATOM 362 CD1 PHE A 45 27.354 38.671 52.162 1.00 45.78 C ANISOU 362 CD1 PHE A 45 4433 5247 7713 43 -861 450 C ATOM 363 CD2 PHE A 45 26.118 38.740 54.207 1.00 50.94 C ANISOU 363 CD2 PHE A 45 5035 5978 8343 117 -1058 413 C ATOM 364 CE1 PHE A 45 28.182 37.691 52.697 1.00 51.97 C ANISOU 364 CE1 PHE A 45 5079 6097 8570 63 -836 457 C ATOM 365 CE2 PHE A 45 26.947 37.760 54.749 1.00 52.33 C ANISOU 365 CE2 PHE A 45 5070 6226 8589 133 -1038 423 C ATOM 366 CZ PHE A 45 27.976 37.235 53.993 1.00 46.43 C ANISOU 366 CZ PHE A 45 4279 5470 7893 108 -926 447 C ATOM 367 N LEU A 46 22.469 39.151 52.113 1.00 51.98 N ANISOU 367 N LEU A 46 5562 5990 8199 210 -1109 456 N ATOM 368 CA LEU A 46 21.415 38.194 52.437 1.00 53.81 C ANISOU 368 CA LEU A 46 5794 6270 8382 282 -1169 463 C ATOM 369 C LEU A 46 20.930 37.458 51.188 1.00 61.79 C ANISOU 369 C LEU A 46 6890 7264 9325 287 -1116 484 C ATOM 370 O LEU A 46 20.854 36.224 51.174 1.00 62.47 O ANISOU 370 O LEU A 46 6938 7382 9416 318 -1103 481 O ATOM 371 CB LEU A 46 20.252 38.909 53.134 1.00 53.65 C ANISOU 371 CB LEU A 46 5817 6255 8313 324 -1272 465 C ATOM 372 CG LEU A 46 19.095 38.065 53.692 1.00 55.27 C ANISOU 372 CG LEU A 46 6008 6519 8473 400 -1350 479 C ATOM 373 CD1 LEU A 46 19.609 37.089 54.708 1.00 54.11 C ANISOU 373 CD1 LEU A 46 5726 6443 8391 428 -1371 465 C ATOM 374 CD2 LEU A 46 18.003 38.915 54.319 1.00 45.17 C ANISOU 374 CD2 LEU A 46 4775 5243 7147 443 -1439 486 C ATOM 375 N LEU A 47 20.617 38.198 50.120 1.00 57.18 N ANISOU 375 N LEU A 47 6421 6628 8677 255 -1082 506 N ATOM 376 CA LEU A 47 20.089 37.566 48.911 1.00 52.96 C ANISOU 376 CA LEU A 47 5975 6088 8060 254 -1039 523 C ATOM 377 C LEU A 47 21.114 36.661 48.239 1.00 52.38 C ANISOU 377 C LEU A 47 5870 6012 8020 227 -929 504 C ATOM 378 O LEU A 47 20.730 35.737 47.514 1.00 55.37 O ANISOU 378 O LEU A 47 6296 6399 8345 236 -899 499 O ATOM 379 CB LEU A 47 19.607 38.621 47.912 1.00 57.51 C ANISOU 379 CB LEU A 47 6674 6620 8557 224 -1023 560 C ATOM 380 CG LEU A 47 18.466 39.548 48.342 1.00 60.88 C ANISOU 380 CG LEU A 47 7153 7040 8940 258 -1117 590 C ATOM 381 CD1 LEU A 47 18.033 40.448 47.185 1.00 58.59 C ANISOU 381 CD1 LEU A 47 6982 6708 8571 231 -1086 641 C ATOM 382 CD2 LEU A 47 17.300 38.727 48.858 1.00 64.58 C ANISOU 382 CD2 LEU A 47 7610 7564 9363 321 -1204 594 C ATOM 383 N ILE A 48 22.410 36.921 48.437 1.00 53.70 N ANISOU 383 N ILE A 48 5961 6167 8274 192 -867 494 N ATOM 384 CA ILE A 48 23.446 36.052 47.883 1.00 55.65 C ANISOU 384 CA ILE A 48 6165 6415 8565 176 -756 481 C ATOM 385 C ILE A 48 23.581 34.787 48.722 1.00 62.94 C ANISOU 385 C ILE A 48 6982 7381 9551 227 -773 463 C ATOM 386 O ILE A 48 23.615 33.670 48.193 1.00 59.61 O ANISOU 386 O ILE A 48 6570 6958 9122 245 -714 450 O ATOM 387 CB ILE A 48 24.790 36.809 47.784 1.00 61.56 C ANISOU 387 CB ILE A 48 6860 7142 9389 119 -681 489 C ATOM 388 CG1 ILE A 48 24.712 37.957 46.771 1.00 64.44 C ANISOU 388 CG1 ILE A 48 7334 7456 9693 66 -643 516 C ATOM 389 CG2 ILE A 48 25.948 35.850 47.432 1.00 38.46 C ANISOU 389 CG2 ILE A 48 3860 4227 6527 115 -566 481 C ATOM 390 CD1 ILE A 48 25.888 38.936 46.846 1.00 52.23 C ANISOU 390 CD1 ILE A 48 5735 5882 8226 3 -594 530 C ATOM 391 N MET A 49 23.640 34.948 50.047 1.00 62.53 N ANISOU 391 N MET A 49 6829 7366 9561 251 -854 463 N ATOM 392 CA MET A 49 23.823 33.811 50.942 1.00 63.01 C ANISOU 392 CA MET A 49 6775 7475 9689 302 -873 460 C ATOM 393 C MET A 49 22.648 32.835 50.891 1.00 65.43 C ANISOU 393 C MET A 49 7127 7792 9941 354 -919 459 C ATOM 394 O MET A 49 22.838 31.637 51.122 1.00 58.22 O ANISOU 394 O MET A 49 6150 6895 9077 390 -892 458 O ATOM 395 CB MET A 49 24.045 34.316 52.369 1.00 56.58 C ANISOU 395 CB MET A 49 5852 6712 8933 313 -960 462 C ATOM 396 CG MET A 49 25.375 35.023 52.576 1.00 63.72 C ANISOU 396 CG MET A 49 6678 7619 9913 258 -916 460 C ATOM 397 SD MET A 49 26.790 33.903 52.467 1.00 72.13 S ANISOU 397 SD MET A 49 7613 8709 11082 263 -802 477 S ATOM 398 CE MET A 49 27.401 34.276 50.826 1.00 68.36 C ANISOU 398 CE MET A 49 7235 8159 10578 204 -665 477 C ATOM 399 N LEU A 50 21.436 33.316 50.604 1.00 53.42 N ANISOU 399 N LEU A 50 5711 6262 8324 357 -986 465 N ATOM 400 CA LEU A 50 20.289 32.427 50.443 1.00 57.97 C ANISOU 400 CA LEU A 50 6335 6849 8842 393 -1030 469 C ATOM 401 C LEU A 50 20.049 32.073 48.978 1.00 61.35 C ANISOU 401 C LEU A 50 6882 7237 9192 360 -957 455 C ATOM 402 O LEU A 50 19.864 30.901 48.639 1.00 65.37 O ANISOU 402 O LEU A 50 7400 7740 9699 373 -925 438 O ATOM 403 CB LEU A 50 19.022 33.065 51.029 1.00 49.51 C ANISOU 403 CB LEU A 50 5298 5805 7709 422 -1151 491 C ATOM 404 CG LEU A 50 19.036 33.520 52.491 1.00 62.54 C ANISOU 404 CG LEU A 50 6850 7502 9411 458 -1235 498 C ATOM 405 CD1 LEU A 50 17.686 34.126 52.907 1.00 49.72 C ANISOU 405 CD1 LEU A 50 5284 5902 7705 490 -1333 517 C ATOM 406 CD2 LEU A 50 19.442 32.390 53.418 1.00 54.10 C ANISOU 406 CD2 LEU A 50 5666 6483 8406 493 -1226 494 C ATOM 407 N GLY A 51 20.062 33.076 48.099 1.00 57.12 N ANISOU 407 N GLY A 51 6439 6674 8591 314 -928 463 N ATOM 408 CA GLY A 51 19.689 32.853 46.714 1.00 50.38 C ANISOU 408 CA GLY A 51 5706 5799 7639 281 -874 455 C ATOM 409 C GLY A 51 20.652 31.976 45.938 1.00 56.16 C ANISOU 409 C GLY A 51 6435 6504 8398 261 -745 419 C ATOM 410 O GLY A 51 20.244 31.304 44.984 1.00 58.84 O ANISOU 410 O GLY A 51 6859 6834 8662 245 -707 396 O ATOM 411 N PHE A 52 21.938 31.973 46.315 1.00 52.78 N ANISOU 411 N PHE A 52 5910 6067 8074 260 -675 415 N ATOM 412 CA PHE A 52 22.887 31.144 45.574 1.00 66.06 C ANISOU 412 CA PHE A 52 7587 7725 9788 250 -541 385 C ATOM 413 C PHE A 52 22.791 29.666 45.953 1.00 66.62 C ANISOU 413 C PHE A 52 7606 7793 9913 296 -529 359 C ATOM 414 O PHE A 52 22.710 28.826 45.049 1.00 69.68 O ANISOU 414 O PHE A 52 8065 8153 10259 288 -455 321 O ATOM 415 CB PHE A 52 24.329 31.624 45.750 1.00 60.98 C ANISOU 415 CB PHE A 52 6853 7076 9239 232 -460 399 C ATOM 416 CG PHE A 52 25.349 30.659 45.201 1.00 59.81 C ANISOU 416 CG PHE A 52 6672 6908 9145 240 -320 376 C ATOM 417 CD1 PHE A 52 25.536 30.530 43.831 1.00 73.41 C ANISOU 417 CD1 PHE A 52 8498 8604 10791 208 -212 353 C ATOM 418 CD2 PHE A 52 26.109 29.872 46.048 1.00 55.34 C ANISOU 418 CD2 PHE A 52 5970 6354 8703 283 -293 380 C ATOM 419 CE1 PHE A 52 26.473 29.636 43.317 1.00 61.40 C ANISOU 419 CE1 PHE A 52 6950 7061 9318 222 -74 327 C ATOM 420 CE2 PHE A 52 27.048 28.979 45.540 1.00 60.96 C ANISOU 420 CE2 PHE A 52 6649 7042 9470 299 -156 364 C ATOM 421 CZ PHE A 52 27.226 28.863 44.174 1.00 61.58 C ANISOU 421 CZ PHE A 52 6837 7087 9474 270 -44 334 C ATOM 422 N PRO A 53 22.825 29.285 47.240 1.00 70.52 N ANISOU 422 N PRO A 53 7980 8313 10499 344 -593 377 N ATOM 423 CA PRO A 53 22.673 27.845 47.552 1.00 58.16 C ANISOU 423 CA PRO A 53 6371 6738 8988 389 -578 361 C ATOM 424 C PRO A 53 21.355 27.255 47.069 1.00 60.24 C ANISOU 424 C PRO A 53 6741 6990 9159 385 -630 338 C ATOM 425 O PRO A 53 21.356 26.199 46.425 1.00 66.94 O ANISOU 425 O PRO A 53 7633 7797 10004 385 -558 298 O ATOM 426 CB PRO A 53 22.801 27.803 49.082 1.00 55.38 C ANISOU 426 CB PRO A 53 5875 6434 8734 437 -659 400 C ATOM 427 CG PRO A 53 23.584 29.008 49.434 1.00 64.68 C ANISOU 427 CG PRO A 53 7000 7638 9939 411 -664 420 C ATOM 428 CD PRO A 53 23.164 30.067 48.447 1.00 53.49 C ANISOU 428 CD PRO A 53 5717 6197 8411 357 -665 410 C ATOM 429 N ILE A 54 20.227 27.919 47.341 1.00 54.59 N ANISOU 429 N ILE A 54 6068 6306 8366 381 -751 362 N ATOM 430 CA ILE A 54 18.924 27.387 46.941 1.00 56.53 C ANISOU 430 CA ILE A 54 6402 6553 8524 373 -813 351 C ATOM 431 C ILE A 54 18.871 27.132 45.437 1.00 62.14 C ANISOU 431 C ILE A 54 7245 7230 9138 320 -730 304 C ATOM 432 O ILE A 54 18.377 26.091 44.989 1.00 69.29 O ANISOU 432 O ILE A 54 8200 8111 10015 310 -716 267 O ATOM 433 CB ILE A 54 17.797 28.334 47.395 1.00 60.98 C ANISOU 433 CB ILE A 54 6989 7163 9016 378 -946 395 C ATOM 434 CG1 ILE A 54 17.815 28.483 48.916 1.00 76.66 C ANISOU 434 CG1 ILE A 54 8847 9189 11089 433 -1026 432 C ATOM 435 CG2 ILE A 54 16.444 27.804 46.959 1.00 66.06 C ANISOU 435 CG2 ILE A 54 7715 7819 9567 365 -1014 393 C ATOM 436 CD1 ILE A 54 16.710 29.361 49.462 1.00 85.46 C ANISOU 436 CD1 ILE A 54 9980 10349 12142 450 -1151 472 C ATOM 437 N ASN A 55 19.369 28.071 44.631 1.00 62.83 N ANISOU 437 N ASN A 55 7391 7313 9168 280 -673 305 N ATOM 438 CA ASN A 55 19.283 27.898 43.183 1.00 58.38 C ANISOU 438 CA ASN A 55 6956 6732 8494 228 -597 265 C ATOM 439 C ASN A 55 20.385 26.992 42.644 1.00 64.94 C ANISOU 439 C ASN A 55 7777 7515 9380 229 -448 210 C ATOM 440 O ASN A 55 20.163 26.269 41.666 1.00 73.28 O ANISOU 440 O ASN A 55 8930 8550 10365 199 -389 154 O ATOM 441 CB ASN A 55 19.325 29.256 42.477 1.00 53.97 C ANISOU 441 CB ASN A 55 6467 6193 7846 187 -592 298 C ATOM 442 CG ASN A 55 18.018 30.034 42.616 1.00 67.13 C ANISOU 442 CG ASN A 55 8183 7901 9423 182 -725 347 C ATOM 443 OD1 ASN A 55 17.018 29.703 41.982 1.00 68.77 O ANISOU 443 OD1 ASN A 55 8478 8130 9523 158 -767 339 O ATOM 444 ND2 ASN A 55 18.032 31.087 43.434 1.00 54.62 N ANISOU 444 ND2 ASN A 55 6543 6328 7881 204 -788 397 N ATOM 445 N PHE A 56 21.572 27.018 43.251 1.00 55.63 N ANISOU 445 N PHE A 56 6486 6323 8327 261 -383 224 N ATOM 446 CA PHE A 56 22.628 26.105 42.826 1.00 60.33 C ANISOU 446 CA PHE A 56 7059 6873 8990 274 -236 182 C ATOM 447 C PHE A 56 22.292 24.668 43.209 1.00 65.46 C ANISOU 447 C PHE A 56 7683 7486 9702 312 -234 147 C ATOM 448 O PHE A 56 22.490 23.740 42.413 1.00 57.21 O ANISOU 448 O PHE A 56 6702 6392 8643 305 -132 85 O ATOM 449 CB PHE A 56 23.969 26.524 43.431 1.00 54.86 C ANISOU 449 CB PHE A 56 6238 6186 8420 299 -174 219 C ATOM 450 CG PHE A 56 25.106 25.629 43.040 1.00 62.60 C ANISOU 450 CG PHE A 56 7181 7125 9480 323 -17 189 C ATOM 451 CD1 PHE A 56 25.778 25.827 41.840 1.00 60.25 C ANISOU 451 CD1 PHE A 56 6957 6811 9126 290 113 162 C ATOM 452 CD2 PHE A 56 25.493 24.577 43.862 1.00 58.76 C ANISOU 452 CD2 PHE A 56 6585 6617 9125 384 7 193 C ATOM 453 CE1 PHE A 56 26.819 24.996 41.468 1.00 63.69 C ANISOU 453 CE1 PHE A 56 7358 7207 9634 320 267 134 C ATOM 454 CE2 PHE A 56 26.530 23.741 43.497 1.00 65.91 C ANISOU 454 CE2 PHE A 56 7454 7478 10109 415 160 170 C ATOM 455 CZ PHE A 56 27.197 23.951 42.299 1.00 68.52 C ANISOU 455 CZ PHE A 56 7861 7792 10383 384 292 138 C ATOM 456 N LEU A 57 21.779 24.466 44.426 1.00 58.36 N ANISOU 456 N LEU A 57 6694 6608 8871 352 -344 186 N ATOM 457 CA LEU A 57 21.365 23.132 44.844 1.00 61.35 C ANISOU 457 CA LEU A 57 7046 6951 9314 387 -352 166 C ATOM 458 C LEU A 57 20.321 22.550 43.893 1.00 62.92 C ANISOU 458 C LEU A 57 7387 7123 9397 340 -367 106 C ATOM 459 O LEU A 57 20.357 21.354 43.583 1.00 70.14 O ANISOU 459 O LEU A 57 8327 7976 10347 345 -298 53 O ATOM 460 CB LEU A 57 20.833 23.180 46.276 1.00 57.20 C ANISOU 460 CB LEU A 57 6408 6470 8857 432 -483 228 C ATOM 461 CG LEU A 57 20.445 21.834 46.888 1.00 69.61 C ANISOU 461 CG LEU A 57 7927 8009 10514 474 -497 228 C ATOM 462 CD1 LEU A 57 21.665 20.897 47.024 1.00 59.27 C ANISOU 462 CD1 LEU A 57 6533 6645 9343 521 -361 220 C ATOM 463 CD2 LEU A 57 19.743 22.051 48.221 1.00 65.26 C ANISOU 463 CD2 LEU A 57 7280 7519 9997 512 -639 296 C ATOM 464 N THR A 58 19.397 23.385 43.404 1.00 56.73 N ANISOU 464 N THR A 58 6696 6385 8475 290 -454 115 N ATOM 465 CA THR A 58 18.411 22.927 42.423 1.00 61.03 C ANISOU 465 CA THR A 58 7375 6921 8893 234 -474 62 C ATOM 466 C THR A 58 19.079 22.343 41.182 1.00 64.07 C ANISOU 466 C THR A 58 7854 7254 9237 201 -323 -22 C ATOM 467 O THR A 58 18.653 21.300 40.673 1.00 75.46 O ANISOU 467 O THR A 58 9367 8651 10651 176 -296 -90 O ATOM 468 CB THR A 58 17.486 24.077 42.018 1.00 53.65 C ANISOU 468 CB THR A 58 6517 6054 7815 190 -576 99 C ATOM 469 OG1 THR A 58 16.827 24.601 43.174 1.00 54.40 O ANISOU 469 OG1 THR A 58 6529 6194 7945 227 -710 172 O ATOM 470 CG2 THR A 58 16.446 23.593 41.016 1.00 36.76 C ANISOU 470 CG2 THR A 58 4508 3922 5537 126 -606 51 C ATOM 471 N LEU A 59 20.112 23.015 40.665 1.00 60.94 N ANISOU 471 N LEU A 59 7462 6862 8832 197 -222 -20 N ATOM 472 CA LEU A 59 20.854 22.462 39.536 1.00 60.12 C ANISOU 472 CA LEU A 59 7436 6712 8695 177 -65 -97 C ATOM 473 C LEU A 59 21.586 21.194 39.938 1.00 59.32 C ANISOU 473 C LEU A 59 7267 6532 8741 231 38 -135 C ATOM 474 O LEU A 59 21.627 20.223 39.174 1.00 64.64 O ANISOU 474 O LEU A 59 8023 7146 9390 215 131 -221 O ATOM 475 CB LEU A 59 21.857 23.483 38.993 1.00 60.75 C ANISOU 475 CB LEU A 59 7516 6818 8749 167 24 -71 C ATOM 476 CG LEU A 59 21.371 24.883 38.616 1.00 70.17 C ANISOU 476 CG LEU A 59 8762 8080 9819 122 -56 -16 C ATOM 477 CD1 LEU A 59 22.498 25.675 37.954 1.00 58.47 C ANISOU 477 CD1 LEU A 59 7284 6608 8325 110 62 2 C ATOM 478 CD2 LEU A 59 20.147 24.806 37.724 1.00 55.84 C ANISOU 478 CD2 LEU A 59 7087 6297 7834 61 -121 -50 C ATOM 479 N TYR A 60 22.161 21.186 41.141 1.00 55.77 N ANISOU 479 N TYR A 60 6666 6081 8444 296 23 -72 N ATOM 480 CA TYR A 60 23.033 20.093 41.556 1.00 56.06 C ANISOU 480 CA TYR A 60 6616 6048 8634 359 133 -87 C ATOM 481 C TYR A 60 22.256 18.785 41.721 1.00 70.53 C ANISOU 481 C TYR A 60 8480 7818 10502 365 110 -133 C ATOM 482 O TYR A 60 22.683 17.734 41.225 1.00 60.42 O ANISOU 482 O TYR A 60 7237 6454 9267 380 236 -201 O ATOM 483 CB TYR A 60 23.755 20.482 42.849 1.00 50.25 C ANISOU 483 CB TYR A 60 5704 5348 8041 421 102 5 C ATOM 484 CG TYR A 60 24.735 19.452 43.355 1.00 69.06 C ANISOU 484 CG TYR A 60 7975 7674 10590 493 214 14 C ATOM 485 CD1 TYR A 60 26.035 19.395 42.862 1.00 73.07 C ANISOU 485 CD1 TYR A 60 8454 8159 11151 516 374 5 C ATOM 486 CD2 TYR A 60 24.365 18.540 44.337 1.00 74.25 C ANISOU 486 CD2 TYR A 60 8549 8305 11356 543 162 41 C ATOM 487 CE1 TYR A 60 26.932 18.450 43.327 1.00 75.19 C ANISOU 487 CE1 TYR A 60 8614 8378 11578 591 480 24 C ATOM 488 CE2 TYR A 60 25.254 17.599 44.810 1.00 74.41 C ANISOU 488 CE2 TYR A 60 8463 8275 11536 616 266 62 C ATOM 489 CZ TYR A 60 26.535 17.555 44.303 1.00 76.79 C ANISOU 489 CZ TYR A 60 8737 8553 11888 641 426 54 C ATOM 490 OH TYR A 60 27.415 16.606 44.773 1.00 82.52 O ANISOU 490 OH TYR A 60 9349 9228 12776 720 534 84 O ATOM 491 N VAL A 61 21.105 18.824 42.405 1.00 52.52 N ANISOU 491 N VAL A 61 6184 5569 8201 355 -46 -98 N ATOM 492 CA VAL A 61 20.366 17.580 42.609 1.00 55.87 C ANISOU 492 CA VAL A 61 6628 5931 8669 357 -71 -133 C ATOM 493 C VAL A 61 19.798 17.066 41.293 1.00 67.40 C ANISOU 493 C VAL A 61 8261 7348 10000 282 -29 -241 C ATOM 494 O VAL A 61 19.663 15.852 41.102 1.00 76.98 O ANISOU 494 O VAL A 61 9512 8473 11264 280 28 -306 O ATOM 495 CB VAL A 61 19.261 17.744 43.673 1.00 46.66 C ANISOU 495 CB VAL A 61 5398 4819 7514 365 -247 -61 C ATOM 496 CG1 VAL A 61 19.869 18.137 45.016 1.00 51.66 C ANISOU 496 CG1 VAL A 61 5859 5496 8275 441 -282 36 C ATOM 497 CG2 VAL A 61 18.188 18.732 43.221 1.00 39.32 C ANISOU 497 CG2 VAL A 61 4559 3967 6414 299 -371 -53 C ATOM 498 N THR A 62 19.465 17.961 40.365 1.00 68.53 N ANISOU 498 N THR A 62 8510 7551 9976 216 -54 -262 N ATOM 499 CA THR A 62 19.039 17.514 39.045 1.00 68.77 C ANISOU 499 CA THR A 62 8705 7556 9869 140 -5 -368 C ATOM 500 C THR A 62 20.139 16.712 38.356 1.00 70.49 C ANISOU 500 C THR A 62 8962 7684 10137 161 191 -454 C ATOM 501 O THR A 62 19.848 15.756 37.628 1.00 66.55 O ANISOU 501 O THR A 62 8571 7118 9597 121 249 -558 O ATOM 502 CB THR A 62 18.610 18.724 38.207 1.00 60.10 C ANISOU 502 CB THR A 62 7698 6552 8585 76 -60 -355 C ATOM 503 OG1 THR A 62 17.471 19.339 38.822 1.00 69.37 O ANISOU 503 OG1 THR A 62 8844 7799 9714 60 -238 -279 O ATOM 504 CG2 THR A 62 18.224 18.315 36.808 1.00 57.54 C ANISOU 504 CG2 THR A 62 7542 6220 8102 -6 -9 -462 C ATOM 505 N VAL A 63 21.406 17.062 38.601 1.00 58.16 N ANISOU 505 N VAL A 63 7309 6119 8669 225 296 -413 N ATOM 506 CA VAL A 63 22.519 16.295 38.047 1.00 56.24 C ANISOU 506 CA VAL A 63 7084 5793 8493 261 491 -481 C ATOM 507 C VAL A 63 22.631 14.930 38.731 1.00 65.71 C ANISOU 507 C VAL A 63 8220 6884 9862 319 537 -500 C ATOM 508 O VAL A 63 23.031 13.946 38.100 1.00 67.06 O ANISOU 508 O VAL A 63 8461 6960 10061 327 679 -592 O ATOM 509 CB VAL A 63 23.830 17.106 38.165 1.00 55.34 C ANISOU 509 CB VAL A 63 6874 5716 8436 311 582 -416 C ATOM 510 CG1 VAL A 63 25.062 16.287 37.696 1.00 48.37 C ANISOU 510 CG1 VAL A 63 5985 4749 7643 365 794 -471 C ATOM 511 CG2 VAL A 63 23.723 18.410 37.389 1.00 53.32 C ANISOU 511 CG2 VAL A 63 6691 5553 8015 250 550 -400 C ATOM 512 N GLN A 64 22.262 14.840 40.013 1.00 67.93 N ANISOU 512 N GLN A 64 8375 7178 10256 361 423 -412 N ATOM 513 CA GLN A 64 22.453 13.628 40.801 1.00 66.01 C ANISOU 513 CA GLN A 64 8047 6842 10192 427 465 -400 C ATOM 514 C GLN A 64 21.222 12.729 40.870 1.00 72.52 C ANISOU 514 C GLN A 64 8939 7611 11005 382 380 -446 C ATOM 515 O GLN A 64 21.357 11.557 41.244 1.00 73.44 O ANISOU 515 O GLN A 64 9021 7624 11261 425 443 -462 O ATOM 516 CB GLN A 64 22.879 13.977 42.239 1.00 59.00 C ANISOU 516 CB GLN A 64 6964 6006 9448 506 401 -267 C ATOM 517 CG GLN A 64 24.041 14.962 42.362 1.00 77.76 C ANISOU 517 CG GLN A 64 9250 8449 11845 542 457 -206 C ATOM 518 CD GLN A 64 25.404 14.359 42.041 1.00 88.85 C ANISOU 518 CD GLN A 64 10614 9785 13360 606 656 -225 C ATOM 519 OE1 GLN A 64 25.505 13.277 41.468 1.00 90.77 O ANISOU 519 OE1 GLN A 64 10931 9921 13637 616 774 -306 O ATOM 520 NE2 GLN A 64 26.463 15.070 42.414 1.00 96.60 N ANISOU 520 NE2 GLN A 64 11477 10826 14400 647 697 -150 N ATOM 521 N HIS A 65 20.032 13.229 40.530 1.00 60.48 N ANISOU 521 N HIS A 65 7503 6151 9325 298 240 -462 N ATOM 522 CA HIS A 65 18.800 12.455 40.673 1.00 57.76 C ANISOU 522 CA HIS A 65 7206 5770 8969 248 140 -491 C ATOM 523 C HIS A 65 18.124 12.298 39.315 1.00 66.91 C ANISOU 523 C HIS A 65 8554 6919 9949 139 147 -614 C ATOM 524 O HIS A 65 17.522 13.246 38.804 1.00 62.14 O ANISOU 524 O HIS A 65 8015 6418 9178 76 55 -607 O ATOM 525 CB HIS A 65 17.868 13.110 41.688 1.00 50.23 C ANISOU 525 CB HIS A 65 6163 4914 8006 249 -52 -380 C ATOM 526 CG HIS A 65 18.397 13.084 43.089 1.00 62.92 C ANISOU 526 CG HIS A 65 7587 6531 9786 349 -69 -266 C ATOM 527 ND1 HIS A 65 17.995 12.147 44.020 1.00 52.01 N ANISOU 527 ND1 HIS A 65 6124 5100 8539 386 -111 -222 N ATOM 528 CD2 HIS A 65 19.301 13.877 43.718 1.00 65.29 C ANISOU 528 CD2 HIS A 65 7770 6893 10145 414 -53 -186 C ATOM 529 CE1 HIS A 65 18.625 12.367 45.161 1.00 68.26 C ANISOU 529 CE1 HIS A 65 8019 7195 10723 474 -119 -117 C ATOM 530 NE2 HIS A 65 19.423 13.411 45.005 1.00 63.95 N ANISOU 530 NE2 HIS A 65 7449 6717 10132 490 -87 -97 N ATOM 531 N LYS A 66 18.205 11.086 38.755 1.00 78.38 N ANISOU 531 N LYS A 66 10094 8249 11439 119 255 -726 N ATOM 532 CA LYS A 66 17.664 10.824 37.422 1.00 79.63 C ANISOU 532 CA LYS A 66 10438 8393 11426 12 278 -861 C ATOM 533 C LYS A 66 16.194 11.228 37.317 1.00 75.22 C ANISOU 533 C LYS A 66 9932 7927 10722 -85 86 -844 C ATOM 534 O LYS A 66 15.757 11.746 36.284 1.00 67.78 O ANISOU 534 O LYS A 66 9111 7056 9585 -171 57 -900 O ATOM 535 CB LYS A 66 17.841 9.339 37.082 1.00 75.42 C ANISOU 535 CB LYS A 66 9976 7697 10985 6 405 -980 C ATOM 536 CG LYS A 66 17.280 8.907 35.731 1.00 90.39 C ANISOU 536 CG LYS A 66 12069 9566 12709 -111 433 -1138 C ATOM 537 CD LYS A 66 17.128 7.386 35.637 1.00 94.90 C ANISOU 537 CD LYS A 66 12703 9968 13387 -130 513 -1248 C ATOM 538 CE LYS A 66 18.481 6.671 35.643 1.00103.07 C ANISOU 538 CE LYS A 66 13711 10869 14583 -27 732 -1288 C ATOM 539 NZ LYS A 66 18.380 5.180 35.488 1.00 82.07 N ANISOU 539 NZ LYS A 66 11124 8026 12034 -41 828 -1403 N ATOM 540 N LYS A 67 15.415 11.006 38.374 1.00 72.15 N ANISOU 540 N LYS A 67 9448 7545 10422 -71 -46 -759 N ATOM 541 CA LYS A 67 13.974 11.197 38.257 1.00 69.80 C ANISOU 541 CA LYS A 67 9199 7323 9999 -164 -219 -747 C ATOM 542 C LYS A 67 13.577 12.660 38.129 1.00 69.79 C ANISOU 542 C LYS A 67 9191 7478 9846 -183 -332 -667 C ATOM 543 O LYS A 67 12.408 12.939 37.839 1.00 68.98 O ANISOU 543 O LYS A 67 9141 7454 9613 -263 -467 -657 O ATOM 544 CB LYS A 67 13.256 10.557 39.450 1.00 52.86 C ANISOU 544 CB LYS A 67 6945 5145 7994 -139 -324 -669 C ATOM 545 CG LYS A 67 13.218 9.022 39.382 1.00 63.59 C ANISOU 545 CG LYS A 67 8345 6346 9470 -160 -245 -760 C ATOM 546 CD LYS A 67 12.383 8.531 38.205 1.00 81.08 C ANISOU 546 CD LYS A 67 10733 8541 11533 -297 -266 -893 C ATOM 547 CE LYS A 67 12.595 7.044 37.914 1.00 96.88 C ANISOU 547 CE LYS A 67 12803 10363 13643 -320 -146 -1015 C ATOM 548 NZ LYS A 67 13.846 6.789 37.133 1.00 97.75 N ANISOU 548 NZ LYS A 67 12989 10387 13763 -283 60 -1123 N ATOM 549 N LEU A 68 14.512 13.591 38.320 1.00 66.00 N ANISOU 549 N LEU A 68 8648 7044 9384 -113 -279 -608 N ATOM 550 CA LEU A 68 14.230 15.010 38.154 1.00 59.52 C ANISOU 550 CA LEU A 68 7828 6357 8431 -127 -368 -534 C ATOM 551 C LEU A 68 14.350 15.475 36.706 1.00 62.27 C ANISOU 551 C LEU A 68 8322 6748 8589 -201 -309 -612 C ATOM 552 O LEU A 68 13.838 16.550 36.376 1.00 66.47 O ANISOU 552 O LEU A 68 8881 7391 8984 -235 -398 -557 O ATOM 553 CB LEU A 68 15.165 15.840 39.038 1.00 58.69 C ANISOU 553 CB LEU A 68 7588 6280 8433 -27 -344 -434 C ATOM 554 CG LEU A 68 14.949 15.719 40.548 1.00 63.05 C ANISOU 554 CG LEU A 68 7984 6833 9138 46 -433 -331 C ATOM 555 CD1 LEU A 68 16.004 16.518 41.317 1.00 50.16 C ANISOU 555 CD1 LEU A 68 6228 5230 7602 134 -395 -250 C ATOM 556 CD2 LEU A 68 13.549 16.181 40.918 1.00 47.47 C ANISOU 556 CD2 LEU A 68 6004 4949 7084 8 -617 -264 C ATOM 557 N ARG A 69 14.973 14.682 35.833 1.00 57.01 N ANISOU 557 N ARG A 69 7752 5999 7910 -224 -160 -736 N ATOM 558 CA ARG A 69 15.292 15.112 34.470 1.00 61.66 C ANISOU 558 CA ARG A 69 8472 6632 8325 -282 -78 -810 C ATOM 559 C ARG A 69 14.174 14.747 33.490 1.00 64.94 C ANISOU 559 C ARG A 69 9032 7084 8558 -405 -149 -897 C ATOM 560 O ARG A 69 14.380 14.069 32.483 1.00 75.52 O ANISOU 560 O ARG A 69 10497 8377 9819 -461 -45 -1029 O ATOM 561 CB ARG A 69 16.630 14.525 34.036 1.00 55.19 C ANISOU 561 CB ARG A 69 7677 5714 7579 -234 131 -896 C ATOM 562 CG ARG A 69 17.796 15.049 34.869 1.00 67.10 C ANISOU 562 CG ARG A 69 9041 7212 9242 -123 201 -802 C ATOM 563 CD ARG A 69 19.140 14.746 34.229 1.00 66.04 C ANISOU 563 CD ARG A 69 8937 7013 9143 -81 410 -872 C ATOM 564 NE ARG A 69 19.468 13.328 34.276 1.00 68.84 N ANISOU 564 NE ARG A 69 9310 7228 9619 -55 524 -965 N ATOM 565 CZ ARG A 69 20.107 12.739 35.283 1.00 73.99 C ANISOU 565 CZ ARG A 69 9833 7795 10484 39 578 -919 C ATOM 566 NH1 ARG A 69 20.486 13.452 36.338 1.00 67.99 N ANISOU 566 NH1 ARG A 69 8917 7087 9829 109 521 -786 N ATOM 567 NH2 ARG A 69 20.369 11.435 35.238 1.00 59.21 N ANISOU 567 NH2 ARG A 69 7989 5787 8720 62 689 -1005 N ATOM 568 N THR A 70 12.942 15.262 33.799 1.00 64.21 N ANISOU 568 N THR A 70 8918 7088 8391 -449 -333 -815 N ATOM 569 CA THR A 70 11.710 15.162 33.026 1.00 72.95 C ANISOU 569 CA THR A 70 10132 8269 9317 -568 -444 -855 C ATOM 570 C THR A 70 11.422 16.474 32.301 1.00 79.86 C ANISOU 570 C THR A 70 11052 9291 10001 -603 -502 -792 C ATOM 571 O THR A 70 11.769 17.551 32.797 1.00 74.39 O ANISOU 571 O THR A 70 10274 8648 9341 -533 -521 -678 O ATOM 572 CB THR A 70 10.521 14.823 33.932 1.00 64.10 C ANISOU 572 CB THR A 70 8939 7159 8258 -584 -610 -789 C ATOM 573 OG1 THR A 70 10.418 15.807 34.970 1.00 87.93 O ANISOU 573 OG1 THR A 70 11823 10241 11345 -503 -701 -636 O ATOM 574 CG2 THR A 70 10.716 13.488 34.573 1.00 54.06 C ANISOU 574 CG2 THR A 70 7630 5742 7168 -560 -556 -848 C ATOM 575 N PRO A 71 10.781 16.408 31.127 1.00 73.94 N ANISOU 575 N PRO A 71 10434 8611 9048 -713 -530 -861 N ATOM 576 CA PRO A 71 10.470 17.643 30.379 1.00 65.18 C ANISOU 576 CA PRO A 71 9367 7648 7749 -747 -585 -790 C ATOM 577 C PRO A 71 9.708 18.700 31.168 1.00 65.96 C ANISOU 577 C PRO A 71 9363 7840 7858 -710 -742 -624 C ATOM 578 O PRO A 71 10.045 19.890 31.075 1.00 89.43 O ANISOU 578 O PRO A 71 12312 10880 10789 -669 -736 -533 O ATOM 579 CB PRO A 71 9.648 17.117 29.197 1.00 58.80 C ANISOU 579 CB PRO A 71 8702 6900 6737 -882 -623 -893 C ATOM 580 CG PRO A 71 10.226 15.753 28.951 1.00 52.21 C ANISOU 580 CG PRO A 71 7936 5925 5975 -902 -490 -1058 C ATOM 581 CD PRO A 71 10.509 15.198 30.331 1.00 57.08 C ANISOU 581 CD PRO A 71 8423 6418 6846 -809 -486 -1020 C ATOM 582 N LEU A 72 8.694 18.310 31.943 1.00 56.09 N ANISOU 582 N LEU A 72 8053 6593 6667 -722 -878 -580 N ATOM 583 CA LEU A 72 7.941 19.278 32.736 1.00 55.28 C ANISOU 583 CA LEU A 72 7850 6575 6577 -679 -1022 -424 C ATOM 584 C LEU A 72 8.784 19.947 33.817 1.00 69.01 C ANISOU 584 C LEU A 72 9468 8270 8483 -554 -982 -338 C ATOM 585 O LEU A 72 8.336 20.939 34.405 1.00 72.38 O ANISOU 585 O LEU A 72 9821 8766 8914 -509 -1079 -213 O ATOM 586 CB LEU A 72 6.725 18.607 33.375 1.00 47.28 C ANISOU 586 CB LEU A 72 6792 5570 5603 -714 -1164 -398 C ATOM 587 CG LEU A 72 5.638 18.151 32.398 1.00 66.14 C ANISOU 587 CG LEU A 72 9284 8034 7811 -849 -1249 -452 C ATOM 588 CD1 LEU A 72 4.687 17.123 33.030 1.00 57.80 C ANISOU 588 CD1 LEU A 72 8187 6943 6834 -891 -1351 -463 C ATOM 589 CD2 LEU A 72 4.879 19.363 31.897 1.00 71.95 C ANISOU 589 CD2 LEU A 72 10032 8930 8375 -874 -1354 -339 C ATOM 590 N ASN A 73 9.980 19.433 34.096 1.00 67.26 N ANISOU 590 N ASN A 73 9220 7938 8398 -498 -842 -402 N ATOM 591 CA ASN A 73 10.891 20.075 35.031 1.00 59.39 C ANISOU 591 CA ASN A 73 8110 6908 7548 -391 -797 -328 C ATOM 592 C ASN A 73 11.895 20.995 34.353 1.00 54.03 C ANISOU 592 C ASN A 73 7466 6252 6812 -373 -688 -322 C ATOM 593 O ASN A 73 12.527 21.799 35.049 1.00 54.08 O ANISOU 593 O ASN A 73 7381 6255 6912 -298 -672 -244 O ATOM 594 CB ASN A 73 11.648 19.019 35.846 1.00 65.03 C ANISOU 594 CB ASN A 73 8752 7498 8461 -331 -712 -378 C ATOM 595 CG ASN A 73 10.849 18.514 37.027 1.00 58.97 C ANISOU 595 CG ASN A 73 7886 6714 7807 -303 -829 -323 C ATOM 596 OD1 ASN A 73 9.722 18.945 37.254 1.00 74.49 O ANISOU 596 OD1 ASN A 73 9837 8762 9705 -327 -973 -249 O ATOM 597 ND2 ASN A 73 11.427 17.588 37.783 1.00 70.93 N ANISOU 597 ND2 ASN A 73 9329 8125 9495 -249 -764 -351 N ATOM 598 N TYR A 74 12.058 20.896 33.024 1.00 53.44 N ANISOU 598 N TYR A 74 7518 6203 6585 -444 -612 -401 N ATOM 599 CA TYR A 74 13.020 21.744 32.318 1.00 55.08 C ANISOU 599 CA TYR A 74 7760 6436 6733 -430 -501 -390 C ATOM 600 C TYR A 74 12.842 23.213 32.681 1.00 59.14 C ANISOU 600 C TYR A 74 8214 7027 7231 -393 -580 -249 C ATOM 601 O TYR A 74 13.826 23.930 32.896 1.00 65.26 O ANISOU 601 O TYR A 74 8937 7782 8075 -338 -502 -207 O ATOM 602 CB TYR A 74 12.878 21.592 30.799 1.00 50.91 C ANISOU 602 CB TYR A 74 7382 5963 5998 -522 -447 -472 C ATOM 603 CG TYR A 74 13.420 20.321 30.183 1.00 66.28 C ANISOU 603 CG TYR A 74 9411 7826 7946 -554 -315 -629 C ATOM 604 CD1 TYR A 74 13.734 19.213 30.960 1.00 62.55 C ANISOU 604 CD1 TYR A 74 8886 7232 7650 -514 -272 -691 C ATOM 605 CD2 TYR A 74 13.620 20.237 28.807 1.00 69.92 C ANISOU 605 CD2 TYR A 74 10007 8331 8229 -623 -227 -715 C ATOM 606 CE1 TYR A 74 14.223 18.055 30.384 1.00 50.52 C ANISOU 606 CE1 TYR A 74 7443 5619 6133 -539 -142 -836 C ATOM 607 CE2 TYR A 74 14.111 19.090 28.222 1.00 65.72 C ANISOU 607 CE2 TYR A 74 9559 7719 7693 -651 -99 -867 C ATOM 608 CZ TYR A 74 14.410 17.998 29.012 1.00 71.75 C ANISOU 608 CZ TYR A 74 10271 8349 8642 -608 -54 -929 C ATOM 609 OH TYR A 74 14.899 16.850 28.420 1.00 77.90 O ANISOU 609 OH TYR A 74 11139 9035 9424 -631 83 -1083 O ATOM 610 N ILE A 75 11.590 23.678 32.752 1.00 63.26 N ANISOU 610 N ILE A 75 8740 7633 7662 -424 -732 -174 N ATOM 611 CA ILE A 75 11.334 25.097 32.963 1.00 65.35 C ANISOU 611 CA ILE A 75 8965 7968 7895 -392 -803 -43 C ATOM 612 C ILE A 75 11.683 25.501 34.392 1.00 63.74 C ANISOU 612 C ILE A 75 8626 7713 7878 -298 -832 27 C ATOM 613 O ILE A 75 12.030 26.661 34.645 1.00 55.21 O ANISOU 613 O ILE A 75 7505 6650 6821 -257 -831 111 O ATOM 614 CB ILE A 75 9.876 25.447 32.596 1.00 65.51 C ANISOU 614 CB ILE A 75 9026 8098 7765 -447 -952 23 C ATOM 615 CG1 ILE A 75 9.737 26.951 32.357 1.00 65.03 C ANISOU 615 CG1 ILE A 75 8964 8114 7631 -426 -985 148 C ATOM 616 CG2 ILE A 75 8.893 25.003 33.674 1.00 52.73 C ANISOU 616 CG2 ILE A 75 7329 6476 6230 -425 -1085 60 C ATOM 617 CD1 ILE A 75 10.464 27.422 31.132 1.00 61.00 C ANISOU 617 CD1 ILE A 75 8542 7634 7003 -463 -872 130 C ATOM 618 N LEU A 76 11.618 24.563 35.342 1.00 54.31 N ANISOU 618 N LEU A 76 7361 6456 6819 -266 -855 -7 N ATOM 619 CA LEU A 76 12.067 24.860 36.701 1.00 56.36 C ANISOU 619 CA LEU A 76 7489 6672 7252 -178 -871 49 C ATOM 620 C LEU A 76 13.586 24.961 36.763 1.00 61.68 C ANISOU 620 C LEU A 76 8127 7281 8028 -137 -725 18 C ATOM 621 O LEU A 76 14.130 25.751 37.542 1.00 63.36 O ANISOU 621 O LEU A 76 8252 7485 8335 -79 -726 82 O ATOM 622 CB LEU A 76 11.561 23.792 37.672 1.00 54.41 C ANISOU 622 CB LEU A 76 7173 6385 7116 -155 -934 31 C ATOM 623 CG LEU A 76 10.043 23.690 37.806 1.00 58.99 C ANISOU 623 CG LEU A 76 7763 7032 7619 -189 -1088 77 C ATOM 624 CD1 LEU A 76 9.658 22.418 38.544 1.00 52.35 C ANISOU 624 CD1 LEU A 76 6869 6138 6882 -183 -1123 41 C ATOM 625 CD2 LEU A 76 9.489 24.917 38.515 1.00 54.29 C ANISOU 625 CD2 LEU A 76 7103 6502 7024 -138 -1194 200 C ATOM 626 N LEU A 77 14.286 24.147 35.972 1.00 63.50 N ANISOU 626 N LEU A 77 8421 7463 8243 -166 -597 -81 N ATOM 627 CA LEU A 77 15.723 24.327 35.813 1.00 59.84 C ANISOU 627 CA LEU A 77 7932 6953 7851 -133 -448 -102 C ATOM 628 C LEU A 77 16.017 25.705 35.244 1.00 66.56 C ANISOU 628 C LEU A 77 8812 7861 8615 -145 -431 -35 C ATOM 629 O LEU A 77 16.906 26.421 35.727 1.00 62.01 O ANISOU 629 O LEU A 77 8159 7267 8134 -101 -386 14 O ATOM 630 CB LEU A 77 16.288 23.236 34.901 1.00 69.81 C ANISOU 630 CB LEU A 77 9277 8162 9084 -166 -311 -223 C ATOM 631 CG LEU A 77 16.932 22.005 35.543 1.00 78.95 C ANISOU 631 CG LEU A 77 10370 9219 10407 -118 -232 -286 C ATOM 632 CD1 LEU A 77 18.392 22.284 35.861 1.00 94.20 C ANISOU 632 CD1 LEU A 77 12217 11110 12464 -54 -104 -267 C ATOM 633 CD2 LEU A 77 16.186 21.601 36.797 1.00 60.08 C ANISOU 633 CD2 LEU A 77 7887 6815 8125 -83 -358 -243 C ATOM 634 N ASN A 78 15.256 26.091 34.216 1.00 53.25 N ANISOU 634 N ASN A 78 7234 6249 6751 -209 -471 -26 N ATOM 635 CA ASN A 78 15.391 27.416 33.626 1.00 64.15 C ANISOU 635 CA ASN A 78 8647 7687 8040 -222 -463 52 C ATOM 636 C ASN A 78 15.192 28.505 34.673 1.00 69.02 C ANISOU 636 C ASN A 78 9169 8311 8743 -170 -557 162 C ATOM 637 O ASN A 78 15.912 29.510 34.682 1.00 64.70 O ANISOU 637 O ASN A 78 8595 7759 8228 -151 -509 218 O ATOM 638 CB ASN A 78 14.379 27.570 32.494 1.00 65.47 C ANISOU 638 CB ASN A 78 8932 7944 7999 -296 -519 58 C ATOM 639 CG ASN A 78 14.722 28.698 31.560 1.00 63.39 C ANISOU 639 CG ASN A 78 8724 7737 7625 -319 -467 120 C ATOM 640 OD1 ASN A 78 15.878 28.863 31.180 1.00 54.02 O ANISOU 640 OD1 ASN A 78 7539 6519 6468 -310 -333 100 O ATOM 641 ND2 ASN A 78 13.719 29.490 31.186 1.00 58.94 N ANISOU 641 ND2 ASN A 78 8200 7258 6936 -346 -570 207 N ATOM 642 N LEU A 79 14.216 28.316 35.565 1.00 57.82 N ANISOU 642 N LEU A 79 7702 6903 7363 -147 -688 192 N ATOM 643 CA LEU A 79 13.986 29.274 36.638 1.00 58.89 C ANISOU 643 CA LEU A 79 7750 7044 7583 -92 -776 285 C ATOM 644 C LEU A 79 15.212 29.409 37.525 1.00 57.29 C ANISOU 644 C LEU A 79 7444 6775 7549 -38 -706 279 C ATOM 645 O LEU A 79 15.577 30.517 37.932 1.00 67.74 O ANISOU 645 O LEU A 79 8725 8096 8918 -13 -713 344 O ATOM 646 CB LEU A 79 12.773 28.847 37.465 1.00 59.10 C ANISOU 646 CB LEU A 79 7736 7093 7626 -73 -917 308 C ATOM 647 CG LEU A 79 12.492 29.682 38.712 1.00 58.24 C ANISOU 647 CG LEU A 79 7532 6987 7609 -7 -1007 391 C ATOM 648 CD1 LEU A 79 12.221 31.134 38.314 1.00 57.10 C ANISOU 648 CD1 LEU A 79 7426 6883 7387 -10 -1035 480 C ATOM 649 CD2 LEU A 79 11.332 29.090 39.508 1.00 51.83 C ANISOU 649 CD2 LEU A 79 6677 6202 6814 13 -1132 410 C ATOM 650 N ALA A 80 15.869 28.289 37.828 1.00 60.92 N ANISOU 650 N ALA A 80 7862 7181 8104 -22 -635 205 N ATOM 651 CA ALA A 80 17.016 28.329 38.726 1.00 58.11 C ANISOU 651 CA ALA A 80 7394 6775 7911 30 -575 206 C ATOM 652 C ALA A 80 18.211 29.008 38.066 1.00 65.67 C ANISOU 652 C ALA A 80 8365 7719 8869 16 -449 211 C ATOM 653 O ALA A 80 18.963 29.726 38.732 1.00 58.94 O ANISOU 653 O ALA A 80 7428 6850 8116 44 -435 253 O ATOM 654 CB ALA A 80 17.369 26.913 39.182 1.00 52.59 C ANISOU 654 CB ALA A 80 6644 6022 7314 56 -528 137 C ATOM 655 N VAL A 81 18.399 28.797 36.759 1.00 70.23 N ANISOU 655 N VAL A 81 9046 8307 9332 -33 -359 169 N ATOM 656 CA VAL A 81 19.484 29.458 36.036 1.00 66.06 C ANISOU 656 CA VAL A 81 8535 7774 8790 -49 -236 181 C ATOM 657 C VAL A 81 19.228 30.959 35.937 1.00 64.72 C ANISOU 657 C VAL A 81 8378 7640 8570 -63 -292 277 C ATOM 658 O VAL A 81 20.142 31.775 36.124 1.00 60.26 O ANISOU 658 O VAL A 81 7761 7057 8079 -55 -237 319 O ATOM 659 CB VAL A 81 19.663 28.815 34.647 1.00 60.78 C ANISOU 659 CB VAL A 81 7981 7117 7996 -96 -126 110 C ATOM 660 CG1 VAL A 81 20.601 29.647 33.777 1.00 56.69 C ANISOU 660 CG1 VAL A 81 7492 6614 7433 -118 -9 141 C ATOM 661 CG2 VAL A 81 20.186 27.388 34.785 1.00 48.46 C ANISOU 661 CG2 VAL A 81 6398 5497 6516 -73 -39 13 C ATOM 662 N ALA A 82 17.984 31.348 35.652 1.00 62.43 N ANISOU 662 N ALA A 82 8157 7402 8163 -85 -400 317 N ATOM 663 CA ALA A 82 17.641 32.764 35.594 1.00 53.94 C ANISOU 663 CA ALA A 82 7095 6354 7047 -89 -456 415 C ATOM 664 C ALA A 82 17.909 33.453 36.923 1.00 61.92 C ANISOU 664 C ALA A 82 7995 7325 8205 -41 -511 460 C ATOM 665 O ALA A 82 18.435 34.571 36.956 1.00 64.18 O ANISOU 665 O ALA A 82 8264 7594 8527 -43 -485 517 O ATOM 666 CB ALA A 82 16.174 32.931 35.197 1.00 45.38 C ANISOU 666 CB ALA A 82 6085 5334 5822 -110 -571 456 C ATOM 667 N ASP A 83 17.548 32.805 38.033 1.00 63.46 N ANISOU 667 N ASP A 83 8117 7507 8488 0 -587 434 N ATOM 668 CA ASP A 83 17.802 33.402 39.339 1.00 57.15 C ANISOU 668 CA ASP A 83 7213 6680 7820 45 -641 468 C ATOM 669 C ASP A 83 19.292 33.565 39.598 1.00 59.05 C ANISOU 669 C ASP A 83 7378 6878 8180 47 -535 452 C ATOM 670 O ASP A 83 19.694 34.447 40.365 1.00 65.93 O ANISOU 670 O ASP A 83 8184 7731 9138 62 -560 489 O ATOM 671 CB ASP A 83 17.164 32.563 40.447 1.00 65.12 C ANISOU 671 CB ASP A 83 8154 7694 8893 90 -734 445 C ATOM 672 CG ASP A 83 15.642 32.667 40.463 1.00 71.62 C ANISOU 672 CG ASP A 83 9027 8565 9621 95 -860 484 C ATOM 673 OD1 ASP A 83 15.087 33.495 39.707 1.00 74.16 O ANISOU 673 OD1 ASP A 83 9428 8916 9834 69 -882 536 O ATOM 674 OD2 ASP A 83 15.003 31.922 41.240 1.00 69.33 O ANISOU 674 OD2 ASP A 83 8690 8286 9366 126 -937 470 O ATOM 675 N LEU A 84 20.127 32.733 38.969 1.00 55.88 N ANISOU 675 N LEU A 84 6984 6462 7785 32 -416 396 N ATOM 676 CA LEU A 84 21.565 32.868 39.156 1.00 57.72 C ANISOU 676 CA LEU A 84 7138 6662 8129 34 -309 391 C ATOM 677 C LEU A 84 22.132 34.025 38.338 1.00 64.20 C ANISOU 677 C LEU A 84 8003 7483 8908 -8 -241 441 C ATOM 678 O LEU A 84 23.071 34.688 38.789 1.00 53.56 O ANISOU 678 O LEU A 84 6577 6111 7661 -11 -205 469 O ATOM 679 CB LEU A 84 22.264 31.549 38.822 1.00 54.74 C ANISOU 679 CB LEU A 84 6746 6267 7785 44 -198 319 C ATOM 680 CG LEU A 84 22.052 30.441 39.865 1.00 59.03 C ANISOU 680 CG LEU A 84 7209 6796 8424 94 -248 282 C ATOM 681 CD1 LEU A 84 22.563 29.107 39.357 1.00 49.58 C ANISOU 681 CD1 LEU A 84 6025 5570 7244 103 -134 210 C ATOM 682 CD2 LEU A 84 22.718 30.782 41.195 1.00 53.56 C ANISOU 682 CD2 LEU A 84 6373 6095 7882 130 -281 314 C ATOM 683 N PHE A 85 21.574 34.297 37.153 1.00 55.46 N ANISOU 683 N PHE A 85 7013 6405 7653 -44 -225 458 N ATOM 684 CA PHE A 85 21.895 35.542 36.460 1.00 65.78 C ANISOU 684 CA PHE A 85 8363 7714 8916 -81 -182 528 C ATOM 685 C PHE A 85 21.598 36.753 37.340 1.00 68.51 C ANISOU 685 C PHE A 85 8666 8037 9327 -69 -278 594 C ATOM 686 O PHE A 85 22.351 37.730 37.334 1.00 69.39 O ANISOU 686 O PHE A 85 8749 8119 9496 -91 -233 640 O ATOM 687 CB PHE A 85 21.113 35.645 35.149 1.00 71.16 C ANISOU 687 CB PHE A 85 9176 8446 9416 -116 -176 548 C ATOM 688 CG PHE A 85 21.744 34.919 33.998 1.00 73.65 C ANISOU 688 CG PHE A 85 9548 8781 9654 -144 -41 497 C ATOM 689 CD1 PHE A 85 21.632 33.544 33.878 1.00 81.25 C ANISOU 689 CD1 PHE A 85 10528 9748 10596 -135 -15 403 C ATOM 690 CD2 PHE A 85 22.427 35.617 33.020 1.00 77.35 C ANISOU 690 CD2 PHE A 85 10056 9263 10069 -180 64 542 C ATOM 691 CE1 PHE A 85 22.202 32.876 32.810 1.00 74.60 C ANISOU 691 CE1 PHE A 85 9746 8919 9679 -158 117 347 C ATOM 692 CE2 PHE A 85 23.000 34.958 31.951 1.00 81.60 C ANISOU 692 CE2 PHE A 85 10650 9826 10528 -202 194 493 C ATOM 693 CZ PHE A 85 22.885 33.585 31.845 1.00 80.56 C ANISOU 693 CZ PHE A 85 10540 9696 10374 -190 222 390 C ATOM 694 N MET A 86 20.498 36.710 38.098 1.00 62.36 N ANISOU 694 N MET A 86 7883 7269 8543 -36 -408 599 N ATOM 695 CA MET A 86 20.198 37.805 39.015 1.00 55.68 C ANISOU 695 CA MET A 86 6997 6396 7761 -18 -496 651 C ATOM 696 C MET A 86 21.230 37.876 40.137 1.00 63.83 C ANISOU 696 C MET A 86 7907 7390 8954 -5 -482 625 C ATOM 697 O MET A 86 21.591 38.971 40.587 1.00 74.48 O ANISOU 697 O MET A 86 9225 8704 10370 -17 -495 662 O ATOM 698 CB MET A 86 18.781 37.650 39.588 1.00 40.17 C ANISOU 698 CB MET A 86 5050 4460 5752 22 -633 661 C ATOM 699 CG MET A 86 17.653 37.699 38.548 1.00 59.56 C ANISOU 699 CG MET A 86 7618 6965 8047 7 -666 701 C ATOM 700 SD MET A 86 15.989 37.218 39.146 1.00 64.44 S ANISOU 700 SD MET A 86 8244 7632 8607 50 -820 711 S ATOM 701 CE MET A 86 15.623 38.446 40.400 1.00 51.95 C ANISOU 701 CE MET A 86 6608 6015 7117 101 -911 768 C ATOM 702 N VAL A 87 21.731 36.722 40.585 1.00 63.03 N ANISOU 702 N VAL A 87 7735 7298 8918 16 -453 564 N ATOM 703 CA VAL A 87 22.651 36.690 41.721 1.00 63.38 C ANISOU 703 CA VAL A 87 7651 7323 9109 31 -451 545 C ATOM 704 C VAL A 87 24.012 37.257 41.330 1.00 64.01 C ANISOU 704 C VAL A 87 7693 7377 9250 -12 -339 562 C ATOM 705 O VAL A 87 24.605 38.052 42.073 1.00 60.03 O ANISOU 705 O VAL A 87 7116 6850 8842 -27 -357 580 O ATOM 706 CB VAL A 87 22.775 35.256 42.273 1.00 59.34 C ANISOU 706 CB VAL A 87 7069 6829 8649 72 -448 488 C ATOM 707 CG1 VAL A 87 24.064 35.095 43.082 1.00 49.59 C ANISOU 707 CG1 VAL A 87 5699 5585 7558 78 -400 477 C ATOM 708 CG2 VAL A 87 21.570 34.915 43.134 1.00 49.78 C ANISOU 708 CG2 VAL A 87 5850 5640 7423 117 -580 484 C ATOM 709 N PHE A 88 24.531 36.854 40.164 1.00 62.66 N ANISOU 709 N PHE A 88 7570 7211 9025 -37 -220 555 N ATOM 710 CA PHE A 88 25.868 37.257 39.736 1.00 69.16 C ANISOU 710 CA PHE A 88 8351 8018 9908 -76 -100 576 C ATOM 711 C PHE A 88 25.871 38.405 38.738 1.00 68.78 C ANISOU 711 C PHE A 88 8390 7958 9787 -125 -58 639 C ATOM 712 O PHE A 88 26.905 39.059 38.576 1.00 79.79 O ANISOU 712 O PHE A 88 9739 9331 11246 -164 18 673 O ATOM 713 CB PHE A 88 26.625 36.061 39.140 1.00 51.71 C ANISOU 713 CB PHE A 88 6125 5823 7701 -64 25 531 C ATOM 714 CG PHE A 88 26.898 34.980 40.137 1.00 73.70 C ANISOU 714 CG PHE A 88 8803 8611 10587 -15 7 484 C ATOM 715 CD1 PHE A 88 27.930 35.115 41.056 1.00 74.91 C ANISOU 715 CD1 PHE A 88 8819 8762 10883 -12 21 496 C ATOM 716 CD2 PHE A 88 26.109 33.838 40.180 1.00 72.73 C ANISOU 716 CD2 PHE A 88 8716 8499 10420 24 -27 433 C ATOM 717 CE1 PHE A 88 28.181 34.123 41.991 1.00 72.77 C ANISOU 717 CE1 PHE A 88 8442 8503 10705 37 3 466 C ATOM 718 CE2 PHE A 88 26.353 32.839 41.113 1.00 65.17 C ANISOU 718 CE2 PHE A 88 7657 7541 9563 72 -40 401 C ATOM 719 CZ PHE A 88 27.388 32.983 42.020 1.00 75.71 C ANISOU 719 CZ PHE A 88 8852 8879 11037 82 -25 421 C ATOM 720 N GLY A 89 24.759 38.665 38.068 1.00 72.13 N ANISOU 720 N GLY A 89 8929 8397 10081 -126 -105 663 N ATOM 721 CA GLY A 89 24.683 39.837 37.221 1.00 68.33 C ANISOU 721 CA GLY A 89 8523 7905 9537 -167 -76 738 C ATOM 722 C GLY A 89 24.429 41.071 38.056 1.00 71.96 C ANISOU 722 C GLY A 89 8958 8317 10069 -172 -164 785 C ATOM 723 O GLY A 89 25.111 42.087 37.901 1.00 80.14 O ANISOU 723 O GLY A 89 9980 9313 11159 -213 -117 836 O ATOM 724 N GLY A 90 23.464 40.978 38.969 1.00 68.59 N ANISOU 724 N GLY A 90 8522 7890 9648 -129 -289 765 N ATOM 725 CA GLY A 90 23.063 42.112 39.774 1.00 60.84 C ANISOU 725 CA GLY A 90 7531 6863 8723 -124 -376 800 C ATOM 726 C GLY A 90 23.537 42.083 41.215 1.00 63.23 C ANISOU 726 C GLY A 90 7719 7144 9160 -110 -430 753 C ATOM 727 O GLY A 90 24.220 43.014 41.651 1.00 65.47 O ANISOU 727 O GLY A 90 7959 7379 9537 -146 -420 768 O ATOM 728 N PHE A 91 23.202 41.027 41.966 1.00 43.27 N ANISOU 728 N PHE A 91 5139 4655 6646 -64 -487 696 N ATOM 729 CA PHE A 91 23.378 41.078 43.418 1.00 53.68 C ANISOU 729 CA PHE A 91 6356 5968 8071 -42 -563 660 C ATOM 730 C PHE A 91 24.845 41.277 43.807 1.00 56.46 C ANISOU 730 C PHE A 91 6604 6303 8544 -86 -497 646 C ATOM 731 O PHE A 91 25.155 42.117 44.659 1.00 56.12 O ANISOU 731 O PHE A 91 6511 6230 8583 -106 -541 643 O ATOM 732 CB PHE A 91 22.824 39.813 44.080 1.00 61.05 C ANISOU 732 CB PHE A 91 7247 6953 8997 17 -624 613 C ATOM 733 CG PHE A 91 21.351 39.608 43.886 1.00 67.46 C ANISOU 733 CG PHE A 91 8143 7788 9701 57 -705 628 C ATOM 734 CD1 PHE A 91 20.555 40.604 43.329 1.00 68.01 C ANISOU 734 CD1 PHE A 91 8310 7837 9695 51 -733 684 C ATOM 735 CD2 PHE A 91 20.753 38.407 44.266 1.00 55.44 C ANISOU 735 CD2 PHE A 91 6597 6311 8159 103 -752 593 C ATOM 736 CE1 PHE A 91 19.193 40.408 43.145 1.00 63.21 C ANISOU 736 CE1 PHE A 91 7769 7261 8987 88 -810 707 C ATOM 737 CE2 PHE A 91 19.384 38.207 44.087 1.00 56.28 C ANISOU 737 CE2 PHE A 91 6773 6445 8167 134 -831 612 C ATOM 738 CZ PHE A 91 18.604 39.207 43.524 1.00 54.31 C ANISOU 738 CZ PHE A 91 6615 6183 7837 127 -860 670 C ATOM 739 N THR A 92 25.765 40.499 43.218 1.00 52.66 N ANISOU 739 N THR A 92 6086 5844 8080 -101 -391 635 N ATOM 740 CA THR A 92 27.173 40.637 43.601 1.00 57.03 C ANISOU 740 CA THR A 92 6526 6392 8752 -142 -329 631 C ATOM 741 C THR A 92 27.735 41.984 43.168 1.00 56.61 C ANISOU 741 C THR A 92 6497 6286 8728 -211 -285 680 C ATOM 742 O THR A 92 28.491 42.615 43.917 1.00 55.18 O ANISOU 742 O THR A 92 6231 6084 8650 -252 -300 677 O ATOM 743 CB THR A 92 28.024 39.509 43.014 1.00 55.89 C ANISOU 743 CB THR A 92 6336 6280 8619 -134 -213 616 C ATOM 744 OG1 THR A 92 27.875 39.480 41.588 1.00 69.17 O ANISOU 744 OG1 THR A 92 8127 7957 10197 -150 -124 641 O ATOM 745 CG2 THR A 92 27.626 38.167 43.614 1.00 50.44 C ANISOU 745 CG2 THR A 92 5601 5631 7933 -68 -253 568 C ATOM 746 N THR A 93 27.385 42.432 41.959 1.00 60.91 N ANISOU 746 N THR A 93 7153 6809 9180 -230 -232 727 N ATOM 747 CA THR A 93 27.799 43.753 41.495 1.00 58.76 C ANISOU 747 CA THR A 93 6913 6479 8933 -293 -191 787 C ATOM 748 C THR A 93 27.336 44.838 42.461 1.00 63.13 C ANISOU 748 C THR A 93 7469 6977 9541 -302 -296 786 C ATOM 749 O THR A 93 28.109 45.730 42.838 1.00 54.74 O ANISOU 749 O THR A 93 6357 5866 8576 -361 -285 797 O ATOM 750 CB THR A 93 27.241 44.014 40.094 1.00 58.45 C ANISOU 750 CB THR A 93 7003 6438 8768 -297 -135 845 C ATOM 751 OG1 THR A 93 27.506 42.890 39.250 1.00 65.89 O ANISOU 751 OG1 THR A 93 7956 7437 9641 -281 -47 827 O ATOM 752 CG2 THR A 93 27.891 45.233 39.487 1.00 76.20 C ANISOU 752 CG2 THR A 93 9270 8631 11051 -365 -65 917 C ATOM 753 N THR A 94 26.073 44.765 42.883 1.00 48.98 N ANISOU 753 N THR A 94 5732 5190 7688 -244 -398 771 N ATOM 754 CA THR A 94 25.506 45.801 43.736 1.00 56.63 C ANISOU 754 CA THR A 94 6718 6103 8695 -240 -491 769 C ATOM 755 C THR A 94 26.055 45.719 45.150 1.00 62.07 C ANISOU 755 C THR A 94 7291 6801 9492 -247 -551 704 C ATOM 756 O THR A 94 26.123 46.737 45.850 1.00 72.55 O ANISOU 756 O THR A 94 8610 8070 10884 -277 -598 693 O ATOM 757 CB THR A 94 23.982 45.696 43.728 1.00 51.68 C ANISOU 757 CB THR A 94 6179 5491 7967 -170 -575 781 C ATOM 758 OG1 THR A 94 23.518 45.931 42.391 1.00 64.96 O ANISOU 758 OG1 THR A 94 7967 7168 9547 -174 -521 851 O ATOM 759 CG2 THR A 94 23.339 46.723 44.677 1.00 49.93 C ANISOU 759 CG2 THR A 94 5975 5211 7785 -152 -668 775 C ATOM 760 N LEU A 95 26.465 44.531 45.587 1.00 52.98 N ANISOU 760 N LEU A 95 6048 5722 8362 -222 -550 660 N ATOM 761 CA LEU A 95 27.209 44.446 46.835 1.00 65.96 C ANISOU 761 CA LEU A 95 7565 7388 10109 -239 -592 611 C ATOM 762 C LEU A 95 28.516 45.219 46.717 1.00 64.24 C ANISOU 762 C LEU A 95 7289 7133 9987 -331 -525 628 C ATOM 763 O LEU A 95 28.871 46.015 47.594 1.00 58.50 O ANISOU 763 O LEU A 95 6515 6376 9337 -376 -576 601 O ATOM 764 CB LEU A 95 27.465 42.981 47.194 1.00 56.25 C ANISOU 764 CB LEU A 95 6243 6242 8886 -192 -587 579 C ATOM 765 CG LEU A 95 28.400 42.711 48.375 1.00 55.10 C ANISOU 765 CG LEU A 95 5946 6143 8847 -210 -616 543 C ATOM 766 CD1 LEU A 95 27.864 43.343 49.650 1.00 60.92 C ANISOU 766 CD1 LEU A 95 6667 6877 9605 -200 -738 504 C ATOM 767 CD2 LEU A 95 28.595 41.218 48.564 1.00 47.60 C ANISOU 767 CD2 LEU A 95 4916 5267 7903 -153 -596 529 C ATOM 768 N TYR A 96 29.225 45.026 45.607 1.00 54.58 N ANISOU 768 N TYR A 96 6072 5910 8757 -363 -408 671 N ATOM 769 CA TYR A 96 30.502 45.694 45.420 1.00 59.89 C ANISOU 769 CA TYR A 96 6681 6553 9522 -452 -335 698 C ATOM 770 C TYR A 96 30.322 47.209 45.322 1.00 60.97 C ANISOU 770 C TYR A 96 6891 6592 9682 -511 -353 727 C ATOM 771 O TYR A 96 30.927 47.964 46.092 1.00 60.05 O ANISOU 771 O TYR A 96 6711 6441 9662 -575 -386 705 O ATOM 772 CB TYR A 96 31.193 45.118 44.184 1.00 56.57 C ANISOU 772 CB TYR A 96 6261 6160 9075 -461 -199 744 C ATOM 773 CG TYR A 96 32.629 45.555 44.012 1.00 58.93 C ANISOU 773 CG TYR A 96 6466 6451 9475 -546 -113 778 C ATOM 774 CD1 TYR A 96 33.635 45.041 44.823 1.00 59.14 C ANISOU 774 CD1 TYR A 96 6340 6533 9599 -563 -112 752 C ATOM 775 CD2 TYR A 96 32.984 46.473 43.030 1.00 58.04 C ANISOU 775 CD2 TYR A 96 6411 6282 9361 -608 -31 844 C ATOM 776 CE1 TYR A 96 34.956 45.437 44.668 1.00 57.21 C ANISOU 776 CE1 TYR A 96 5999 6290 9449 -644 -35 790 C ATOM 777 CE2 TYR A 96 34.304 46.871 42.862 1.00 57.84 C ANISOU 777 CE2 TYR A 96 6293 6252 9432 -689 49 882 C ATOM 778 CZ TYR A 96 35.286 46.351 43.685 1.00 60.61 C ANISOU 778 CZ TYR A 96 6489 6660 9879 -708 46 854 C ATOM 779 OH TYR A 96 36.599 46.743 43.528 1.00 71.67 O ANISOU 779 OH TYR A 96 7788 8064 11378 -791 123 899 O ATOM 780 N THR A 97 29.462 47.672 44.407 1.00 59.02 N ANISOU 780 N THR A 97 6777 6300 9350 -490 -335 776 N ATOM 781 CA THR A 97 29.315 49.111 44.175 1.00 54.01 C ANISOU 781 CA THR A 97 6215 5562 8743 -541 -334 819 C ATOM 782 C THR A 97 28.762 49.841 45.398 1.00 50.95 C ANISOU 782 C THR A 97 5834 5122 8402 -536 -448 765 C ATOM 783 O THR A 97 29.161 50.976 45.679 1.00 55.95 O ANISOU 783 O THR A 97 6470 5669 9118 -605 -451 767 O ATOM 784 CB THR A 97 28.404 49.362 42.976 1.00 52.13 C ANISOU 784 CB THR A 97 6114 5301 8394 -506 -298 892 C ATOM 785 OG1 THR A 97 27.086 48.886 43.288 1.00 58.78 O ANISOU 785 OG1 THR A 97 7014 6174 9147 -418 -387 866 O ATOM 786 CG2 THR A 97 28.931 48.644 41.742 1.00 48.59 C ANISOU 786 CG2 THR A 97 5668 4910 7885 -512 -182 937 C ATOM 787 N SER A 98 27.824 49.228 46.124 1.00 50.19 N ANISOU 787 N SER A 98 5744 5072 8253 -455 -540 715 N ATOM 788 CA SER A 98 27.263 49.909 47.287 1.00 60.84 C ANISOU 788 CA SER A 98 7102 6378 9635 -442 -643 661 C ATOM 789 C SER A 98 28.331 50.209 48.334 1.00 53.77 C ANISOU 789 C SER A 98 6093 5482 8855 -517 -669 598 C ATOM 790 O SER A 98 28.240 51.227 49.028 1.00 65.45 O ANISOU 790 O SER A 98 7593 6886 10387 -552 -719 562 O ATOM 791 CB SER A 98 26.118 49.088 47.892 1.00 57.28 C ANISOU 791 CB SER A 98 6664 5994 9106 -339 -732 624 C ATOM 792 OG SER A 98 26.575 47.836 48.366 1.00 72.10 O ANISOU 792 OG SER A 98 8432 7973 10989 -318 -742 584 O ATOM 793 N LEU A 99 29.359 49.357 48.444 1.00 61.60 N ANISOU 793 N LEU A 99 6964 6555 9885 -545 -633 586 N ATOM 794 CA LEU A 99 30.457 49.590 49.386 1.00 53.95 C ANISOU 794 CA LEU A 99 5871 5604 9022 -624 -657 538 C ATOM 795 C LEU A 99 31.393 50.715 48.942 1.00 59.16 C ANISOU 795 C LEU A 99 6531 6177 9771 -739 -593 571 C ATOM 796 O LEU A 99 32.177 51.215 49.762 1.00 63.75 O ANISOU 796 O LEU A 99 7030 6751 10442 -821 -627 526 O ATOM 797 CB LEU A 99 31.241 48.293 49.596 1.00 63.38 C ANISOU 797 CB LEU A 99 6930 6917 10233 -608 -633 531 C ATOM 798 CG LEU A 99 30.439 47.134 50.210 1.00 61.40 C ANISOU 798 CG LEU A 99 6659 6754 9917 -503 -701 496 C ATOM 799 CD1 LEU A 99 31.230 45.847 50.168 1.00 56.43 C ANISOU 799 CD1 LEU A 99 5908 6223 9308 -483 -652 507 C ATOM 800 CD2 LEU A 99 30.041 47.456 51.636 1.00 56.38 C ANISOU 800 CD2 LEU A 99 5990 6135 9297 -493 -823 423 C ATOM 801 N HIS A 100 31.341 51.115 47.667 1.00 55.37 N ANISOU 801 N HIS A 100 6136 5636 9265 -752 -502 651 N ATOM 802 CA HIS A 100 31.965 52.353 47.213 1.00 55.38 C ANISOU 802 CA HIS A 100 6164 5532 9344 -853 -446 694 C ATOM 803 C HIS A 100 31.031 53.556 47.300 1.00 59.78 C ANISOU 803 C HIS A 100 6851 5964 9898 -848 -488 693 C ATOM 804 O HIS A 100 31.506 54.697 47.247 1.00 62.81 O ANISOU 804 O HIS A 100 7253 6243 10368 -938 -464 709 O ATOM 805 CB HIS A 100 32.431 52.228 45.760 1.00 57.11 C ANISOU 805 CB HIS A 100 6407 5752 9539 -871 -318 792 C ATOM 806 CG HIS A 100 33.372 51.093 45.509 1.00 65.61 C ANISOU 806 CG HIS A 100 7368 6939 10622 -871 -252 802 C ATOM 807 ND1 HIS A 100 34.706 51.286 45.216 1.00 63.00 N ANISOU 807 ND1 HIS A 100 6941 6616 10379 -963 -171 841 N ATOM 808 CD2 HIS A 100 33.170 49.756 45.481 1.00 64.29 C ANISOU 808 CD2 HIS A 100 7165 6874 10387 -789 -249 784 C ATOM 809 CE1 HIS A 100 35.288 50.116 45.026 1.00 65.03 C ANISOU 809 CE1 HIS A 100 7107 6977 10622 -930 -118 847 C ATOM 810 NE2 HIS A 100 34.378 49.171 45.184 1.00 77.18 N ANISOU 810 NE2 HIS A 100 8684 8570 12070 -825 -163 809 N ATOM 811 N GLY A 101 29.721 53.334 47.402 1.00 64.70 N ANISOU 811 N GLY A 101 7562 6592 10430 -745 -545 683 N ATOM 812 CA GLY A 101 28.759 54.417 47.434 1.00 62.59 C ANISOU 812 CA GLY A 101 7418 6209 10155 -721 -577 694 C ATOM 813 C GLY A 101 28.330 54.949 46.084 1.00 65.56 C ANISOU 813 C GLY A 101 7905 6519 10487 -709 -497 806 C ATOM 814 O GLY A 101 27.647 55.984 46.035 1.00 58.65 O ANISOU 814 O GLY A 101 7129 5533 9624 -697 -509 833 O ATOM 815 N TYR A 102 28.706 54.285 44.992 1.00 54.10 N ANISOU 815 N TYR A 102 6440 5132 8982 -708 -413 876 N ATOM 816 CA TYR A 102 28.358 54.721 43.640 1.00 60.65 C ANISOU 816 CA TYR A 102 7368 5921 9755 -700 -332 990 C ATOM 817 C TYR A 102 28.736 53.603 42.675 1.00 56.71 C ANISOU 817 C TYR A 102 6837 5535 9175 -683 -257 1029 C ATOM 818 O TYR A 102 29.344 52.600 43.062 1.00 59.50 O ANISOU 818 O TYR A 102 7092 5978 9536 -683 -259 972 O ATOM 819 CB TYR A 102 29.050 56.034 43.259 1.00 55.83 C ANISOU 819 CB TYR A 102 6778 5185 9249 -798 -267 1049 C ATOM 820 CG TYR A 102 30.552 55.924 43.045 1.00 59.83 C ANISOU 820 CG TYR A 102 7178 5716 9840 -901 -190 1058 C ATOM 821 CD1 TYR A 102 31.434 55.903 44.125 1.00 64.71 C ANISOU 821 CD1 TYR A 102 7683 6341 10561 -970 -233 970 C ATOM 822 CD2 TYR A 102 31.092 55.869 41.761 1.00 60.76 C ANISOU 822 CD2 TYR A 102 7302 5854 9930 -930 -75 1159 C ATOM 823 CE1 TYR A 102 32.815 55.820 43.930 1.00 50.66 C ANISOU 823 CE1 TYR A 102 5795 4590 8863 -1066 -163 989 C ATOM 824 CE2 TYR A 102 32.471 55.785 41.558 1.00 50.73 C ANISOU 824 CE2 TYR A 102 5927 4609 8740 -1021 2 1176 C ATOM 825 CZ TYR A 102 33.326 55.762 42.646 1.00 54.40 C ANISOU 825 CZ TYR A 102 6276 5080 9314 -1089 -44 1093 C ATOM 826 OH TYR A 102 34.692 55.674 42.445 1.00 58.27 O ANISOU 826 OH TYR A 102 6652 5603 9885 -1179 31 1119 O ATOM 827 N PHE A 103 28.390 53.796 41.402 1.00 48.03 N ANISOU 827 N PHE A 103 5822 4429 7996 -668 -185 1129 N ATOM 828 CA PHE A 103 28.548 52.741 40.401 1.00 55.90 C ANISOU 828 CA PHE A 103 6815 5534 8890 -642 -114 1162 C ATOM 829 C PHE A 103 29.937 52.858 39.788 1.00 54.20 C ANISOU 829 C PHE A 103 6533 5321 8740 -729 2 1205 C ATOM 830 O PHE A 103 30.150 53.589 38.820 1.00 68.66 O ANISOU 830 O PHE A 103 8413 7107 10565 -768 83 1302 O ATOM 831 CB PHE A 103 27.452 52.819 39.343 1.00 56.53 C ANISOU 831 CB PHE A 103 7016 5627 8834 -583 -100 1245 C ATOM 832 CG PHE A 103 27.344 51.578 38.525 1.00 62.86 C ANISOU 832 CG PHE A 103 7825 6549 9510 -543 -56 1246 C ATOM 833 CD1 PHE A 103 26.590 50.504 38.975 1.00 58.32 C ANISOU 833 CD1 PHE A 103 7247 6050 8863 -471 -131 1176 C ATOM 834 CD2 PHE A 103 28.045 51.453 37.333 1.00 66.74 C ANISOU 834 CD2 PHE A 103 8322 7076 9960 -582 64 1312 C ATOM 835 CE1 PHE A 103 26.516 49.332 38.241 1.00 60.67 C ANISOU 835 CE1 PHE A 103 7554 6447 9049 -440 -89 1165 C ATOM 836 CE2 PHE A 103 27.971 50.283 36.593 1.00 76.52 C ANISOU 836 CE2 PHE A 103 9573 8422 11080 -547 109 1299 C ATOM 837 CZ PHE A 103 27.206 49.221 37.048 1.00 59.80 C ANISOU 837 CZ PHE A 103 7457 6369 8893 -478 32 1221 C ATOM 838 N VAL A 104 30.895 52.105 40.348 1.00 60.33 N ANISOU 838 N VAL A 104 7188 6158 9578 -755 12 1140 N ATOM 839 CA VAL A 104 32.307 52.275 39.990 1.00 60.55 C ANISOU 839 CA VAL A 104 7128 6187 9692 -842 113 1176 C ATOM 840 C VAL A 104 32.682 51.707 38.631 1.00 60.57 C ANISOU 840 C VAL A 104 7148 6257 9608 -833 239 1247 C ATOM 841 O VAL A 104 33.816 51.910 38.185 1.00 72.50 O ANISOU 841 O VAL A 104 8593 7771 11183 -901 336 1295 O ATOM 842 CB VAL A 104 33.246 51.627 41.025 1.00 66.76 C ANISOU 842 CB VAL A 104 7767 7027 10572 -869 86 1095 C ATOM 843 CG1 VAL A 104 33.245 52.420 42.302 1.00 71.65 C ANISOU 843 CG1 VAL A 104 8353 7576 11297 -914 -17 1034 C ATOM 844 CG2 VAL A 104 32.842 50.176 41.293 1.00 59.34 C ANISOU 844 CG2 VAL A 104 6799 6193 9553 -778 54 1031 C ATOM 845 N PHE A 105 31.776 51.012 37.953 1.00 64.43 N ANISOU 845 N PHE A 105 7723 6806 9953 -754 241 1254 N ATOM 846 CA PHE A 105 32.115 50.344 36.702 1.00 66.72 C ANISOU 846 CA PHE A 105 8032 7172 10146 -742 359 1301 C ATOM 847 C PHE A 105 31.817 51.184 35.468 1.00 65.06 C ANISOU 847 C PHE A 105 7925 6932 9863 -762 428 1417 C ATOM 848 O PHE A 105 32.145 50.759 34.355 1.00 74.37 O ANISOU 848 O PHE A 105 9126 8177 10956 -759 536 1464 O ATOM 849 CB PHE A 105 31.374 49.006 36.610 1.00 63.28 C ANISOU 849 CB PHE A 105 7629 6827 9589 -655 330 1236 C ATOM 850 CG PHE A 105 31.791 48.013 37.661 1.00 62.29 C ANISOU 850 CG PHE A 105 7393 6744 9530 -631 288 1137 C ATOM 851 CD1 PHE A 105 33.137 47.701 37.848 1.00 54.19 C ANISOU 851 CD1 PHE A 105 6243 5744 8605 -673 363 1129 C ATOM 852 CD2 PHE A 105 30.844 47.394 38.468 1.00 51.75 C ANISOU 852 CD2 PHE A 105 6071 5429 8161 -564 174 1063 C ATOM 853 CE1 PHE A 105 33.530 46.773 38.817 1.00 49.29 C ANISOU 853 CE1 PHE A 105 5512 5169 8046 -646 325 1051 C ATOM 854 CE2 PHE A 105 31.228 46.471 39.440 1.00 60.35 C ANISOU 854 CE2 PHE A 105 7055 6562 9313 -539 137 984 C ATOM 855 CZ PHE A 105 32.575 46.160 39.613 1.00 51.76 C ANISOU 855 CZ PHE A 105 5842 5500 8324 -579 213 979 C ATOM 856 N GLY A 106 31.194 52.345 35.626 1.00 69.07 N ANISOU 856 N GLY A 106 8498 7346 10400 -776 374 1466 N ATOM 857 CA GLY A 106 31.022 53.260 34.526 1.00 71.03 C ANISOU 857 CA GLY A 106 8830 7557 10602 -800 442 1592 C ATOM 858 C GLY A 106 29.849 52.918 33.633 1.00 80.30 C ANISOU 858 C GLY A 106 10119 8795 11597 -729 433 1634 C ATOM 859 O GLY A 106 29.113 51.949 33.861 1.00 70.65 O ANISOU 859 O GLY A 106 8917 7642 10285 -662 369 1560 O ATOM 860 N PRO A 107 29.658 53.727 32.586 1.00 78.94 N ANISOU 860 N PRO A 107 10021 8603 11371 -746 495 1761 N ATOM 861 CA PRO A 107 28.521 53.506 31.675 1.00 68.09 C ANISOU 861 CA PRO A 107 8756 7299 9818 -685 483 1817 C ATOM 862 C PRO A 107 28.537 52.150 30.992 1.00 66.55 C ANISOU 862 C PRO A 107 8568 7241 9476 -653 528 1766 C ATOM 863 O PRO A 107 27.465 51.584 30.748 1.00 81.02 O ANISOU 863 O PRO A 107 10471 9142 11173 -595 467 1748 O ATOM 864 CB PRO A 107 28.667 54.644 30.657 1.00 63.36 C ANISOU 864 CB PRO A 107 8207 6658 9209 -725 567 1974 C ATOM 865 CG PRO A 107 29.487 55.681 31.357 1.00 68.31 C ANISOU 865 CG PRO A 107 8772 7150 10033 -796 578 1989 C ATOM 866 CD PRO A 107 30.435 54.922 32.227 1.00 53.26 C ANISOU 866 CD PRO A 107 6753 5262 8222 -824 574 1865 C ATOM 867 N THR A 108 29.718 51.613 30.673 1.00 82.15 N ANISOU 867 N THR A 108 10475 9262 11478 -690 634 1744 N ATOM 868 CA THR A 108 29.787 50.287 30.065 1.00 84.95 C ANISOU 868 CA THR A 108 10839 9735 11702 -656 686 1682 C ATOM 869 C THR A 108 29.336 49.213 31.046 1.00 76.44 C ANISOU 869 C THR A 108 9731 8680 10631 -604 589 1547 C ATOM 870 O THR A 108 28.436 48.421 30.743 1.00 71.70 O ANISOU 870 O THR A 108 9197 8150 9895 -554 546 1506 O ATOM 871 CB THR A 108 31.205 49.999 29.568 1.00 80.33 C ANISOU 871 CB THR A 108 10179 9184 11160 -701 831 1692 C ATOM 872 OG1 THR A 108 31.535 50.900 28.502 1.00 82.88 O ANISOU 872 OG1 THR A 108 10539 9503 11448 -744 929 1828 O ATOM 873 CG2 THR A 108 31.303 48.566 29.063 1.00 74.47 C ANISOU 873 CG2 THR A 108 9445 8551 10298 -660 888 1610 C ATOM 874 N GLY A 109 29.946 49.177 32.235 1.00 68.77 N ANISOU 874 N GLY A 109 8657 7654 9817 -619 549 1479 N ATOM 875 CA GLY A 109 29.516 48.224 33.244 1.00 59.74 C ANISOU 875 CA GLY A 109 7477 6530 8690 -568 453 1362 C ATOM 876 C GLY A 109 28.062 48.403 33.624 1.00 70.20 C ANISOU 876 C GLY A 109 8880 7841 9951 -517 322 1355 C ATOM 877 O GLY A 109 27.407 47.452 34.061 1.00 71.99 O ANISOU 877 O GLY A 109 9112 8113 10128 -465 251 1275 O ATOM 878 N CYS A 110 27.538 49.620 33.458 1.00 70.99 N ANISOU 878 N CYS A 110 9040 7877 10056 -531 293 1445 N ATOM 879 CA CYS A 110 26.125 49.862 33.707 1.00 55.80 C ANISOU 879 CA CYS A 110 7192 5945 8066 -477 179 1457 C ATOM 880 C CYS A 110 25.259 49.091 32.721 1.00 69.33 C ANISOU 880 C CYS A 110 8991 7764 9590 -438 180 1471 C ATOM 881 O CYS A 110 24.245 48.499 33.115 1.00 57.96 O ANISOU 881 O CYS A 110 7576 6359 8086 -385 83 1422 O ATOM 882 CB CYS A 110 25.834 51.364 33.631 1.00 58.68 C ANISOU 882 CB CYS A 110 7603 6213 8482 -497 167 1564 C ATOM 883 SG CYS A 110 24.149 51.857 34.134 1.00 75.99 S ANISOU 883 SG CYS A 110 9872 8373 10628 -423 28 1589 S ATOM 884 N ASN A 111 25.647 49.078 31.437 1.00 64.42 N ANISOU 884 N ASN A 111 8410 7197 8871 -466 289 1536 N ATOM 885 CA ASN A 111 24.879 48.328 30.445 1.00 66.09 C ANISOU 885 CA ASN A 111 8704 7518 8889 -440 294 1542 C ATOM 886 C ASN A 111 24.997 46.823 30.670 1.00 65.72 C ANISOU 886 C ASN A 111 8629 7537 8805 -417 292 1411 C ATOM 887 O ASN A 111 24.003 46.097 30.560 1.00 70.43 O ANISOU 887 O ASN A 111 9277 8195 9287 -381 223 1371 O ATOM 888 CB ASN A 111 25.325 48.700 29.032 1.00 58.60 C ANISOU 888 CB ASN A 111 7805 6618 7841 -479 416 1641 C ATOM 889 CG ASN A 111 24.918 50.115 28.644 1.00 69.48 C ANISOU 889 CG ASN A 111 9231 7944 9223 -491 410 1789 C ATOM 890 OD1 ASN A 111 23.732 50.423 28.516 1.00 62.84 O ANISOU 890 OD1 ASN A 111 8456 7122 8300 -455 326 1842 O ATOM 891 ND2 ASN A 111 25.904 50.978 28.440 1.00 75.52 N ANISOU 891 ND2 ASN A 111 9960 8645 10088 -541 500 1861 N ATOM 892 N LEU A 112 26.199 46.338 30.992 1.00 66.65 N ANISOU 892 N LEU A 112 8662 7640 9024 -437 369 1349 N ATOM 893 CA LEU A 112 26.377 44.923 31.302 1.00 72.09 C ANISOU 893 CA LEU A 112 9314 8376 9703 -409 374 1229 C ATOM 894 C LEU A 112 25.502 44.505 32.475 1.00 72.70 C ANISOU 894 C LEU A 112 9369 8433 9819 -362 232 1159 C ATOM 895 O LEU A 112 24.731 43.540 32.383 1.00 70.18 O ANISOU 895 O LEU A 112 9091 8171 9405 -329 185 1100 O ATOM 896 CB LEU A 112 27.845 44.635 31.615 1.00 73.23 C ANISOU 896 CB LEU A 112 9351 8497 9976 -433 474 1191 C ATOM 897 CG LEU A 112 28.782 44.476 30.423 1.00 80.00 C ANISOU 897 CG LEU A 112 10220 9402 10775 -464 634 1225 C ATOM 898 CD1 LEU A 112 30.219 44.675 30.860 1.00 76.56 C ANISOU 898 CD1 LEU A 112 9663 8925 10501 -497 718 1230 C ATOM 899 CD2 LEU A 112 28.584 43.098 29.813 1.00 81.07 C ANISOU 899 CD2 LEU A 112 10402 9616 10784 -432 680 1140 C ATOM 900 N GLU A 113 25.624 45.216 33.597 1.00 57.79 N ANISOU 900 N GLU A 113 7416 6468 8073 -363 165 1162 N ATOM 901 CA GLU A 113 24.872 44.848 34.789 1.00 62.01 C ANISOU 901 CA GLU A 113 7921 6989 8653 -316 36 1098 C ATOM 902 C GLU A 113 23.372 44.970 34.546 1.00 71.96 C ANISOU 902 C GLU A 113 9274 8278 9790 -279 -61 1132 C ATOM 903 O GLU A 113 22.592 44.121 34.988 1.00 72.67 O ANISOU 903 O GLU A 113 9366 8405 9838 -237 -141 1072 O ATOM 904 CB GLU A 113 25.317 45.720 35.964 1.00 61.13 C ANISOU 904 CB GLU A 113 7730 6792 8705 -330 -11 1098 C ATOM 905 CG GLU A 113 24.991 45.153 37.328 1.00 82.52 C ANISOU 905 CG GLU A 113 10372 9497 11486 -288 -116 1013 C ATOM 906 CD GLU A 113 24.015 46.012 38.101 1.00 96.63 C ANISOU 906 CD GLU A 113 12186 11234 13295 -260 -233 1035 C ATOM 907 OE1 GLU A 113 22.960 46.354 37.535 1.00 82.57 O ANISOU 907 OE1 GLU A 113 10497 9466 11411 -236 -270 1093 O ATOM 908 OE2 GLU A 113 24.310 46.350 39.270 1.00114.23 O ANISOU 908 OE2 GLU A 113 14342 13416 15643 -261 -286 996 O ATOM 909 N GLY A 114 22.954 46.004 33.814 1.00 63.01 N ANISOU 909 N GLY A 114 8213 7133 8596 -294 -52 1237 N ATOM 910 CA GLY A 114 21.538 46.166 33.530 1.00 63.46 C ANISOU 910 CA GLY A 114 8351 7227 8535 -258 -140 1286 C ATOM 911 C GLY A 114 21.003 45.101 32.593 1.00 68.45 C ANISOU 911 C GLY A 114 9046 7966 8997 -254 -129 1261 C ATOM 912 O GLY A 114 19.886 44.609 32.774 1.00 74.22 O ANISOU 912 O GLY A 114 9807 8743 9652 -219 -226 1242 O ATOM 913 N PHE A 115 21.788 44.730 31.581 1.00 61.30 N ANISOU 913 N PHE A 115 8159 7103 8028 -293 -10 1257 N ATOM 914 CA PHE A 115 21.358 43.696 30.643 1.00 58.63 C ANISOU 914 CA PHE A 115 7888 6866 7523 -297 11 1218 C ATOM 915 C PHE A 115 21.189 42.345 31.336 1.00 66.02 C ANISOU 915 C PHE A 115 8787 7817 8480 -270 -35 1091 C ATOM 916 O PHE A 115 20.163 41.677 31.166 1.00 70.56 O ANISOU 916 O PHE A 115 9412 8452 8946 -255 -109 1063 O ATOM 917 CB PHE A 115 22.357 43.590 29.489 1.00 60.26 C ANISOU 917 CB PHE A 115 8118 7109 7667 -341 161 1232 C ATOM 918 CG PHE A 115 22.077 42.458 28.546 1.00 70.60 C ANISOU 918 CG PHE A 115 9498 8518 8811 -350 199 1170 C ATOM 919 CD1 PHE A 115 21.090 42.573 27.579 1.00 65.32 C ANISOU 919 CD1 PHE A 115 8925 7936 7957 -362 164 1227 C ATOM 920 CD2 PHE A 115 22.803 41.276 28.624 1.00 74.55 C ANISOU 920 CD2 PHE A 115 9965 9022 9337 -348 270 1053 C ATOM 921 CE1 PHE A 115 20.832 41.530 26.704 1.00 67.59 C ANISOU 921 CE1 PHE A 115 9282 8317 8083 -381 195 1158 C ATOM 922 CE2 PHE A 115 22.549 40.230 27.757 1.00 67.59 C ANISOU 922 CE2 PHE A 115 9156 8220 8304 -360 310 983 C ATOM 923 CZ PHE A 115 21.562 40.359 26.792 1.00 68.35 C ANISOU 923 CZ PHE A 115 9354 8405 8210 -381 270 1030 C ATOM 924 N PHE A 116 22.188 41.917 32.116 1.00 60.55 N ANISOU 924 N PHE A 116 8004 7074 7930 -265 7 1019 N ATOM 925 CA PHE A 116 22.138 40.563 32.670 1.00 67.62 C ANISOU 925 CA PHE A 116 8863 7984 8847 -238 -16 906 C ATOM 926 C PHE A 116 21.188 40.452 33.852 1.00 69.59 C ANISOU 926 C PHE A 116 9078 8214 9148 -194 -161 885 C ATOM 927 O PHE A 116 20.598 39.387 34.065 1.00 64.98 O ANISOU 927 O PHE A 116 8500 7662 8525 -173 -211 817 O ATOM 928 CB PHE A 116 23.537 40.084 33.075 1.00 53.36 C ANISOU 928 CB PHE A 116 6963 6140 7171 -241 83 847 C ATOM 929 CG PHE A 116 24.391 39.696 31.907 1.00 62.25 C ANISOU 929 CG PHE A 116 8122 7301 8229 -271 234 836 C ATOM 930 CD1 PHE A 116 24.127 38.531 31.196 1.00 69.83 C ANISOU 930 CD1 PHE A 116 9144 8315 9071 -268 273 763 C ATOM 931 CD2 PHE A 116 25.440 40.505 31.497 1.00 66.60 C ANISOU 931 CD2 PHE A 116 8645 7831 8830 -305 338 899 C ATOM 932 CE1 PHE A 116 24.901 38.175 30.102 1.00 75.39 C ANISOU 932 CE1 PHE A 116 9886 9055 9703 -292 419 747 C ATOM 933 CE2 PHE A 116 26.219 40.156 30.405 1.00 70.70 C ANISOU 933 CE2 PHE A 116 9194 8390 9279 -328 483 894 C ATOM 934 CZ PHE A 116 25.950 38.989 29.706 1.00 77.94 C ANISOU 934 CZ PHE A 116 10177 9364 10073 -318 525 815 C ATOM 935 N ALA A 117 21.027 41.525 34.624 1.00 68.81 N ANISOU 935 N ALA A 117 8944 8061 9138 -181 -226 941 N ATOM 936 CA ALA A 117 20.083 41.491 35.733 1.00 62.48 C ANISOU 936 CA ALA A 117 8115 7248 8378 -134 -360 927 C ATOM 937 C ALA A 117 18.647 41.597 35.236 1.00 64.90 C ANISOU 937 C ALA A 117 8506 7609 8543 -119 -445 979 C ATOM 938 O ALA A 117 17.743 40.957 35.787 1.00 59.49 O ANISOU 938 O ALA A 117 7813 6953 7837 -84 -541 945 O ATOM 939 CB ALA A 117 20.397 42.612 36.723 1.00 60.19 C ANISOU 939 CB ALA A 117 7765 6880 8224 -126 -395 960 C ATOM 940 N THR A 118 18.420 42.407 34.202 1.00 77.13 N ANISOU 940 N THR A 118 10131 9179 9997 -144 -413 1070 N ATOM 941 CA THR A 118 17.098 42.466 33.592 1.00 74.73 C ANISOU 941 CA THR A 118 9904 8945 9545 -134 -487 1130 C ATOM 942 C THR A 118 16.803 41.178 32.823 1.00 63.64 C ANISOU 942 C THR A 118 8547 7628 8007 -157 -474 1064 C ATOM 943 O THR A 118 15.682 40.658 32.883 1.00 73.75 O ANISOU 943 O THR A 118 9851 8963 9206 -142 -569 1057 O ATOM 944 CB THR A 118 16.987 43.717 32.697 1.00 59.93 C ANISOU 944 CB THR A 118 8091 7072 7609 -152 -451 1258 C ATOM 945 OG1 THR A 118 16.983 44.909 33.512 1.00 89.96 O ANISOU 945 OG1 THR A 118 11860 10785 11535 -124 -486 1317 O ATOM 946 CG2 THR A 118 15.722 43.676 31.841 1.00 49.64 C ANISOU 946 CG2 THR A 118 6866 5865 6128 -151 -513 1328 C ATOM 947 N LEU A 119 17.806 40.620 32.133 1.00 65.79 N ANISOU 947 N LEU A 119 8829 7909 8258 -195 -354 1009 N ATOM 948 CA LEU A 119 17.603 39.343 31.447 1.00 69.76 C ANISOU 948 CA LEU A 119 9380 8480 8644 -219 -332 927 C ATOM 949 C LEU A 119 17.274 38.231 32.436 1.00 69.90 C ANISOU 949 C LEU A 119 9346 8482 8731 -189 -401 830 C ATOM 950 O LEU A 119 16.372 37.424 32.194 1.00 71.93 O ANISOU 950 O LEU A 119 9646 8795 8888 -196 -464 794 O ATOM 951 CB LEU A 119 18.837 38.964 30.625 1.00 60.61 C ANISOU 951 CB LEU A 119 8236 7323 7469 -255 -177 881 C ATOM 952 CG LEU A 119 18.733 37.734 29.710 1.00 54.85 C ANISOU 952 CG LEU A 119 7577 6662 6602 -286 -127 792 C ATOM 953 CD1 LEU A 119 17.889 38.026 28.476 1.00 54.46 C ANISOU 953 CD1 LEU A 119 7633 6712 6346 -325 -147 854 C ATOM 954 CD2 LEU A 119 20.118 37.221 29.301 1.00 52.97 C ANISOU 954 CD2 LEU A 119 7322 6399 6405 -300 32 725 C ATOM 955 N GLY A 120 17.987 38.181 33.562 1.00 71.72 N ANISOU 955 N GLY A 120 9480 8639 9131 -157 -395 792 N ATOM 956 CA GLY A 120 17.715 37.150 34.551 1.00 66.47 C ANISOU 956 CA GLY A 120 8756 7960 8539 -124 -458 712 C ATOM 957 C GLY A 120 16.297 37.203 35.082 1.00 65.74 C ANISOU 957 C GLY A 120 8672 7899 8408 -95 -605 746 C ATOM 958 O GLY A 120 15.623 36.175 35.186 1.00 69.62 O ANISOU 958 O GLY A 120 9172 8423 8857 -92 -658 693 O ATOM 959 N GLY A 121 15.820 38.402 35.419 1.00 61.01 N ANISOU 959 N GLY A 121 8069 7288 7825 -73 -668 838 N ATOM 960 CA GLY A 121 14.485 38.524 35.977 1.00 51.61 C ANISOU 960 CA GLY A 121 6877 6127 6605 -36 -802 879 C ATOM 961 C GLY A 121 13.385 38.328 34.952 1.00 65.94 C ANISOU 961 C GLY A 121 8779 8032 8244 -63 -848 921 C ATOM 962 O GLY A 121 12.266 37.943 35.307 1.00 59.12 O ANISOU 962 O GLY A 121 7911 7211 7341 -43 -955 931 O ATOM 963 N GLU A 122 13.675 38.596 33.676 1.00 61.00 N ANISOU 963 N GLU A 122 8229 7443 7507 -112 -771 951 N ATOM 964 CA GLU A 122 12.664 38.393 32.645 1.00 60.99 C ANISOU 964 CA GLU A 122 8308 7541 7322 -146 -816 990 C ATOM 965 C GLU A 122 12.574 36.937 32.212 1.00 64.50 C ANISOU 965 C GLU A 122 8785 8030 7691 -188 -804 880 C ATOM 966 O GLU A 122 11.483 36.474 31.863 1.00 65.97 O ANISOU 966 O GLU A 122 9010 8295 7761 -210 -888 888 O ATOM 967 CB GLU A 122 12.948 39.287 31.437 1.00 65.03 C ANISOU 967 CB GLU A 122 8889 8088 7731 -181 -742 1075 C ATOM 968 CG GLU A 122 12.719 40.765 31.701 1.00 66.55 C ANISOU 968 CG GLU A 122 9069 8246 7973 -143 -770 1205 C ATOM 969 CD GLU A 122 11.278 41.094 32.051 1.00 73.57 C ANISOU 969 CD GLU A 122 9956 9180 8817 -104 -904 1287 C ATOM 970 OE1 GLU A 122 10.369 40.638 31.330 1.00 80.52 O ANISOU 970 OE1 GLU A 122 10884 10164 9545 -132 -959 1309 O ATOM 971 OE2 GLU A 122 11.053 41.812 33.049 1.00 85.35 O ANISOU 971 OE2 GLU A 122 11398 10608 10425 -45 -954 1329 O ATOM 972 N ILE A 123 13.700 36.213 32.204 1.00 65.96 N ANISOU 972 N ILE A 123 8954 8166 7941 -202 -698 779 N ATOM 973 CA ILE A 123 13.660 34.765 32.008 1.00 54.72 C ANISOU 973 CA ILE A 123 7552 6757 6482 -231 -682 661 C ATOM 974 C ILE A 123 12.889 34.109 33.143 1.00 59.78 C ANISOU 974 C ILE A 123 8130 7382 7201 -196 -796 634 C ATOM 975 O ILE A 123 12.080 33.200 32.920 1.00 53.75 O ANISOU 975 O ILE A 123 7400 6664 6359 -225 -855 589 O ATOM 976 CB ILE A 123 15.084 34.185 31.901 1.00 56.99 C ANISOU 976 CB ILE A 123 7821 6982 6849 -237 -537 569 C ATOM 977 CG1 ILE A 123 15.815 34.721 30.675 1.00 55.32 C ANISOU 977 CG1 ILE A 123 7676 6800 6543 -276 -417 595 C ATOM 978 CG2 ILE A 123 15.039 32.668 31.828 1.00 55.12 C ANISOU 978 CG2 ILE A 123 7602 6740 6600 -256 -518 446 C ATOM 979 CD1 ILE A 123 17.283 34.367 30.664 1.00 50.94 C ANISOU 979 CD1 ILE A 123 7086 6183 6087 -270 -270 528 C ATOM 980 N ALA A 124 13.125 34.564 34.377 1.00 57.21 N ANISOU 980 N ALA A 124 7713 6995 7031 -135 -829 660 N ATOM 981 CA ALA A 124 12.391 34.026 35.517 1.00 49.07 C ANISOU 981 CA ALA A 124 6614 5954 6075 -94 -937 646 C ATOM 982 C ALA A 124 10.901 34.321 35.398 1.00 64.30 C ANISOU 982 C ALA A 124 8573 7961 7898 -95 -1066 725 C ATOM 983 O ALA A 124 10.067 33.434 35.618 1.00 70.39 O ANISOU 983 O ALA A 124 9338 8766 8642 -103 -1143 695 O ATOM 984 CB ALA A 124 12.958 34.593 36.818 1.00 49.02 C ANISOU 984 CB ALA A 124 6507 5880 6239 -32 -945 664 C ATOM 985 N LEU A 125 10.550 35.558 35.037 1.00 66.46 N ANISOU 985 N LEU A 125 8875 8262 8114 -86 -1088 831 N ATOM 986 CA LEU A 125 9.145 35.929 34.887 1.00 56.05 C ANISOU 986 CA LEU A 125 7578 7023 6695 -80 -1205 923 C ATOM 987 C LEU A 125 8.453 35.059 33.843 1.00 62.75 C ANISOU 987 C LEU A 125 8500 7963 7380 -151 -1232 894 C ATOM 988 O LEU A 125 7.415 34.446 34.120 1.00 57.46 O ANISOU 988 O LEU A 125 7814 7342 6675 -156 -1334 896 O ATOM 989 CB LEU A 125 9.036 37.413 34.522 1.00 65.02 C ANISOU 989 CB LEU A 125 8739 8166 7798 -59 -1199 1046 C ATOM 990 CG LEU A 125 7.819 37.911 33.729 1.00 70.22 C ANISOU 990 CG LEU A 125 9451 8926 8301 -73 -1276 1159 C ATOM 991 CD1 LEU A 125 6.547 37.677 34.490 1.00 66.75 C ANISOU 991 CD1 LEU A 125 8965 8530 7867 -33 -1409 1199 C ATOM 992 CD2 LEU A 125 7.950 39.383 33.395 1.00 72.99 C ANISOU 992 CD2 LEU A 125 9823 9261 8649 -47 -1244 1279 C ATOM 993 N TRP A 126 9.014 34.990 32.633 1.00 61.60 N ANISOU 993 N TRP A 126 8433 7844 7128 -211 -1140 866 N ATOM 994 CA TRP A 126 8.368 34.224 31.574 1.00 62.80 C ANISOU 994 CA TRP A 126 8662 8090 7107 -288 -1165 832 C ATOM 995 C TRP A 126 8.442 32.721 31.817 1.00 75.47 C ANISOU 995 C TRP A 126 10263 9667 8744 -320 -1161 695 C ATOM 996 O TRP A 126 7.674 31.968 31.206 1.00 73.41 O ANISOU 996 O TRP A 126 10054 9478 8358 -383 -1213 660 O ATOM 997 CB TRP A 126 8.974 34.583 30.215 1.00 52.67 C ANISOU 997 CB TRP A 126 7468 6851 5695 -342 -1062 838 C ATOM 998 CG TRP A 126 8.491 35.918 29.722 1.00 71.85 C ANISOU 998 CG TRP A 126 9916 9341 8042 -328 -1094 991 C ATOM 999 CD1 TRP A 126 9.157 37.108 29.786 1.00 67.05 C ANISOU 999 CD1 TRP A 126 9292 8682 7501 -288 -1031 1071 C ATOM 1000 CD2 TRP A 126 7.219 36.202 29.121 1.00 75.01 C ANISOU 1000 CD2 TRP A 126 10351 9864 8287 -354 -1198 1089 C ATOM 1001 NE1 TRP A 126 8.386 38.110 29.248 1.00 69.75 N ANISOU 1001 NE1 TRP A 126 9660 9098 7743 -282 -1083 1215 N ATOM 1002 CE2 TRP A 126 7.191 37.581 28.834 1.00 76.16 C ANISOU 1002 CE2 TRP A 126 10500 10023 8415 -319 -1186 1232 C ATOM 1003 CE3 TRP A 126 6.102 35.423 28.796 1.00 68.31 C ANISOU 1003 CE3 TRP A 126 9526 9115 7315 -405 -1301 1074 C ATOM 1004 CZ2 TRP A 126 6.092 38.198 28.236 1.00 75.03 C ANISOU 1004 CZ2 TRP A 126 10380 9993 8136 -326 -1270 1368 C ATOM 1005 CZ3 TRP A 126 5.015 36.036 28.200 1.00 64.77 C ANISOU 1005 CZ3 TRP A 126 9098 8788 6726 -419 -1390 1206 C ATOM 1006 CH2 TRP A 126 5.018 37.411 27.926 1.00 68.98 C ANISOU 1006 CH2 TRP A 126 9630 9334 7244 -376 -1372 1354 C ATOM 1007 N SER A 127 9.341 32.268 32.693 1.00 64.57 N ANISOU 1007 N SER A 127 8821 8185 7528 -279 -1101 621 N ATOM 1008 CA SER A 127 9.320 30.865 33.085 1.00 57.12 C ANISOU 1008 CA SER A 127 7860 7204 6638 -295 -1105 508 C ATOM 1009 C SER A 127 8.060 30.546 33.881 1.00 61.51 C ANISOU 1009 C SER A 127 8365 7794 7213 -278 -1251 548 C ATOM 1010 O SER A 127 7.448 29.489 33.687 1.00 65.12 O ANISOU 1010 O SER A 127 8847 8276 7621 -329 -1296 487 O ATOM 1011 CB SER A 127 10.576 30.520 33.886 1.00 51.72 C ANISOU 1011 CB SER A 127 7109 6411 6132 -247 -1008 440 C ATOM 1012 OG SER A 127 11.701 30.385 33.030 1.00 53.25 O ANISOU 1012 OG SER A 127 7356 6579 6299 -276 -864 376 O ATOM 1013 N LEU A 128 7.652 31.456 34.771 1.00 58.35 N ANISOU 1013 N LEU A 128 7893 7393 6883 -209 -1325 650 N ATOM 1014 CA LEU A 128 6.411 31.278 35.519 1.00 56.87 C ANISOU 1014 CA LEU A 128 7652 7248 6707 -184 -1462 705 C ATOM 1015 C LEU A 128 5.193 31.289 34.602 1.00 68.73 C ANISOU 1015 C LEU A 128 9216 8867 8031 -246 -1550 761 C ATOM 1016 O LEU A 128 4.200 30.604 34.878 1.00 61.43 O ANISOU 1016 O LEU A 128 8269 7987 7086 -266 -1649 765 O ATOM 1017 CB LEU A 128 6.278 32.370 36.583 1.00 50.33 C ANISOU 1017 CB LEU A 128 6745 6397 5979 -93 -1508 802 C ATOM 1018 CG LEU A 128 7.433 32.455 37.582 1.00 53.45 C ANISOU 1018 CG LEU A 128 7070 6692 6548 -34 -1436 755 C ATOM 1019 CD1 LEU A 128 7.067 33.355 38.736 1.00 52.29 C ANISOU 1019 CD1 LEU A 128 6846 6533 6490 50 -1504 837 C ATOM 1020 CD2 LEU A 128 7.814 31.071 38.079 1.00 52.92 C ANISOU 1020 CD2 LEU A 128 6963 6576 6567 -43 -1412 650 C ATOM 1021 N VAL A 129 5.246 32.062 33.517 1.00 59.66 N ANISOU 1021 N VAL A 129 8140 7776 6753 -279 -1517 813 N ATOM 1022 CA VAL A 129 4.167 32.035 32.535 1.00 60.12 C ANISOU 1022 CA VAL A 129 8257 7958 6626 -347 -1595 865 C ATOM 1023 C VAL A 129 4.133 30.687 31.831 1.00 69.24 C ANISOU 1023 C VAL A 129 9477 9136 7697 -444 -1580 737 C ATOM 1024 O VAL A 129 3.085 30.031 31.754 1.00 66.94 O ANISOU 1024 O VAL A 129 9185 8912 7336 -494 -1683 737 O ATOM 1025 CB VAL A 129 4.327 33.188 31.525 1.00 59.49 C ANISOU 1025 CB VAL A 129 8238 7937 6429 -357 -1553 956 C ATOM 1026 CG1 VAL A 129 3.374 33.002 30.349 1.00 49.20 C ANISOU 1026 CG1 VAL A 129 7003 6775 4914 -443 -1619 992 C ATOM 1027 CG2 VAL A 129 4.104 34.534 32.199 1.00 54.21 C ANISOU 1027 CG2 VAL A 129 7511 7250 5836 -264 -1586 1093 C ATOM 1028 N VAL A 130 5.286 30.255 31.306 1.00 65.25 N ANISOU 1028 N VAL A 130 9026 8570 7197 -474 -1448 626 N ATOM 1029 CA VAL A 130 5.345 29.006 30.551 1.00 64.75 C ANISOU 1029 CA VAL A 130 9038 8515 7049 -566 -1414 492 C ATOM 1030 C VAL A 130 5.001 27.827 31.451 1.00 62.87 C ANISOU 1030 C VAL A 130 8746 8216 6924 -566 -1466 418 C ATOM 1031 O VAL A 130 4.304 26.893 31.033 1.00 49.54 O ANISOU 1031 O VAL A 130 7101 6569 5152 -647 -1520 356 O ATOM 1032 CB VAL A 130 6.725 28.850 29.884 1.00 58.66 C ANISOU 1032 CB VAL A 130 8329 7683 6276 -580 -1248 394 C ATOM 1033 CG1 VAL A 130 6.954 27.418 29.389 1.00 48.36 C ANISOU 1033 CG1 VAL A 130 7092 6346 4937 -655 -1192 231 C ATOM 1034 CG2 VAL A 130 6.847 29.827 28.725 1.00 49.99 C ANISOU 1034 CG2 VAL A 130 7301 6674 5018 -609 -1208 464 C ATOM 1035 N LEU A 131 5.449 27.867 32.710 1.00 52.63 N ANISOU 1035 N LEU A 131 7353 6825 5817 -478 -1454 427 N ATOM 1036 CA LEU A 131 5.094 26.809 33.651 1.00 47.88 C ANISOU 1036 CA LEU A 131 6689 6170 5333 -467 -1506 378 C ATOM 1037 C LEU A 131 3.585 26.669 33.776 1.00 62.68 C ANISOU 1037 C LEU A 131 8543 8139 7135 -501 -1663 450 C ATOM 1038 O LEU A 131 3.060 25.552 33.840 1.00 73.18 O ANISOU 1038 O LEU A 131 9876 9463 8467 -556 -1708 386 O ATOM 1039 CB LEU A 131 5.709 27.086 35.020 1.00 44.89 C ANISOU 1039 CB LEU A 131 6200 5703 5152 -361 -1485 407 C ATOM 1040 CG LEU A 131 5.453 26.047 36.110 1.00 52.65 C ANISOU 1040 CG LEU A 131 7104 6629 6272 -336 -1529 370 C ATOM 1041 CD1 LEU A 131 5.905 24.675 35.657 1.00 47.26 C ANISOU 1041 CD1 LEU A 131 6474 5880 5602 -398 -1452 230 C ATOM 1042 CD2 LEU A 131 6.172 26.443 37.385 1.00 59.11 C ANISOU 1042 CD2 LEU A 131 7816 7376 7267 -231 -1500 402 C ATOM 1043 N ALA A 132 2.873 27.796 33.798 1.00 67.82 N ANISOU 1043 N ALA A 132 9169 8876 7724 -467 -1743 588 N ATOM 1044 CA ALA A 132 1.425 27.759 33.947 1.00 52.78 C ANISOU 1044 CA ALA A 132 7230 7071 5753 -489 -1892 676 C ATOM 1045 C ALA A 132 0.748 27.304 32.660 1.00 60.62 C ANISOU 1045 C ALA A 132 8315 8169 6551 -612 -1935 648 C ATOM 1046 O ALA A 132 -0.234 26.554 32.708 1.00 64.55 O ANISOU 1046 O ALA A 132 8798 8717 7011 -671 -2036 644 O ATOM 1047 CB ALA A 132 0.905 29.133 34.376 1.00 49.91 C ANISOU 1047 CB ALA A 132 6811 6762 5392 -405 -1954 837 C ATOM 1048 N ILE A 133 1.242 27.761 31.502 1.00 60.77 N ANISOU 1048 N ILE A 133 8425 8228 6438 -655 -1862 631 N ATOM 1049 CA ILE A 133 0.675 27.316 30.227 1.00 63.31 C ANISOU 1049 CA ILE A 133 8840 8657 6557 -779 -1897 593 C ATOM 1050 C ILE A 133 0.771 25.802 30.114 1.00 74.48 C ANISOU 1050 C ILE A 133 10297 10014 7989 -863 -1877 430 C ATOM 1051 O ILE A 133 -0.162 25.131 29.654 1.00 77.72 O ANISOU 1051 O ILE A 133 10737 10502 8290 -962 -1968 406 O ATOM 1052 CB ILE A 133 1.383 28.006 29.043 1.00 58.17 C ANISOU 1052 CB ILE A 133 8281 8050 5773 -804 -1799 591 C ATOM 1053 CG1 ILE A 133 1.131 29.512 29.044 1.00 65.93 C ANISOU 1053 CG1 ILE A 133 9228 9097 6726 -732 -1829 766 C ATOM 1054 CG2 ILE A 133 0.939 27.407 27.711 1.00 47.21 C ANISOU 1054 CG2 ILE A 133 6997 6770 4168 -939 -1820 523 C ATOM 1055 CD1 ILE A 133 1.797 30.235 27.880 1.00 57.47 C ANISOU 1055 CD1 ILE A 133 8241 8072 5524 -755 -1734 783 C ATOM 1056 N GLU A 134 1.898 25.244 30.556 1.00 75.76 N ANISOU 1056 N GLU A 134 10457 10034 8292 -825 -1757 318 N ATOM 1057 CA GLU A 134 2.120 23.807 30.466 1.00 68.91 C ANISOU 1057 CA GLU A 134 9634 9087 7462 -893 -1715 159 C ATOM 1058 C GLU A 134 1.217 23.045 31.427 1.00 70.42 C ANISOU 1058 C GLU A 134 9744 9258 7755 -896 -1828 176 C ATOM 1059 O GLU A 134 0.539 22.090 31.027 1.00 65.91 O ANISOU 1059 O GLU A 134 9214 8711 7116 -1000 -1886 106 O ATOM 1060 CB GLU A 134 3.593 23.511 30.729 1.00 51.19 C ANISOU 1060 CB GLU A 134 7396 6700 5354 -835 -1551 59 C ATOM 1061 CG GLU A 134 4.478 24.001 29.597 1.00 63.40 C ANISOU 1061 CG GLU A 134 9039 8269 6782 -856 -1428 17 C ATOM 1062 CD GLU A 134 5.955 23.827 29.871 1.00 67.50 C ANISOU 1062 CD GLU A 134 9551 8657 7440 -790 -1264 -61 C ATOM 1063 OE1 GLU A 134 6.320 23.445 31.006 1.00 77.19 O ANISOU 1063 OE1 GLU A 134 10690 9781 8860 -719 -1250 -70 O ATOM 1064 OE2 GLU A 134 6.750 24.078 28.942 1.00 66.12 O ANISOU 1064 OE2 GLU A 134 9454 8491 7177 -810 -1150 -108 O ATOM 1065 N ARG A 135 1.192 23.455 32.699 1.00 61.16 N ANISOU 1065 N ARG A 135 8454 8043 6742 -787 -1861 267 N ATOM 1066 CA ARG A 135 0.291 22.838 33.670 1.00 59.30 C ANISOU 1066 CA ARG A 135 8128 7801 6601 -779 -1972 306 C ATOM 1067 C ARG A 135 -1.159 22.889 33.197 1.00 64.87 C ANISOU 1067 C ARG A 135 8839 8650 7158 -861 -2122 384 C ATOM 1068 O ARG A 135 -1.917 21.930 33.382 1.00 73.24 O ANISOU 1068 O ARG A 135 9882 9715 8232 -929 -2200 354 O ATOM 1069 CB ARG A 135 0.445 23.522 35.029 1.00 46.76 C ANISOU 1069 CB ARG A 135 6418 6175 5175 -643 -1988 411 C ATOM 1070 CG ARG A 135 1.825 23.315 35.633 1.00 52.55 C ANISOU 1070 CG ARG A 135 7127 6771 6070 -568 -1853 336 C ATOM 1071 CD ARG A 135 2.033 24.039 36.963 1.00 39.83 C ANISOU 1071 CD ARG A 135 5397 5130 4605 -440 -1869 431 C ATOM 1072 NE ARG A 135 3.184 23.472 37.659 1.00 60.52 N ANISOU 1072 NE ARG A 135 7979 7625 7392 -386 -1763 353 N ATOM 1073 CZ ARG A 135 3.733 23.970 38.761 1.00 58.21 C ANISOU 1073 CZ ARG A 135 7591 7289 7236 -281 -1742 402 C ATOM 1074 NH1 ARG A 135 3.252 25.073 39.317 1.00 67.90 N ANISOU 1074 NH1 ARG A 135 8762 8577 8459 -215 -1814 519 N ATOM 1075 NH2 ARG A 135 4.775 23.357 39.301 1.00 61.81 N ANISOU 1075 NH2 ARG A 135 8011 7641 7833 -242 -1647 331 N ATOM 1076 N TYR A 136 -1.558 23.997 32.574 1.00 68.27 N ANISOU 1076 N TYR A 136 9290 9201 7448 -860 -2164 489 N ATOM 1077 CA TYR A 136 -2.910 24.103 32.037 1.00 62.32 C ANISOU 1077 CA TYR A 136 8537 8600 6540 -938 -2304 575 C ATOM 1078 C TYR A 136 -3.117 23.122 30.890 1.00 63.65 C ANISOU 1078 C TYR A 136 8814 8807 6562 -1095 -2309 447 C ATOM 1079 O TYR A 136 -4.126 22.413 30.843 1.00 73.42 O ANISOU 1079 O TYR A 136 10037 10103 7756 -1183 -2420 447 O ATOM 1080 CB TYR A 136 -3.175 25.550 31.595 1.00 58.56 C ANISOU 1080 CB TYR A 136 8059 8238 5953 -891 -2331 723 C ATOM 1081 CG TYR A 136 -4.253 25.716 30.549 1.00 55.86 C ANISOU 1081 CG TYR A 136 7752 8064 5409 -986 -2422 784 C ATOM 1082 CD1 TYR A 136 -5.603 25.649 30.889 1.00 67.15 C ANISOU 1082 CD1 TYR A 136 9070 9546 6897 -945 -2439 844 C ATOM 1083 CD2 TYR A 136 -3.922 25.949 29.218 1.00 49.79 C ANISOU 1083 CD2 TYR A 136 7097 7370 4451 -1070 -2387 749 C ATOM 1084 CE1 TYR A 136 -6.596 25.800 29.923 1.00 62.57 C ANISOU 1084 CE1 TYR A 136 8496 9094 6183 -998 -2458 878 C ATOM 1085 CE2 TYR A 136 -4.901 26.099 28.248 1.00 57.06 C ANISOU 1085 CE2 TYR A 136 8026 8433 5219 -1131 -2423 791 C ATOM 1086 CZ TYR A 136 -6.234 26.026 28.607 1.00 62.34 C ANISOU 1086 CZ TYR A 136 8580 9147 5959 -1089 -2454 853 C ATOM 1087 OH TYR A 136 -7.199 26.180 27.644 1.00 66.56 O ANISOU 1087 OH TYR A 136 9113 9811 6364 -1138 -2476 890 O ATOM 1088 N VAL A 137 -2.148 23.047 29.973 1.00 69.64 N ANISOU 1088 N VAL A 137 9682 9532 7247 -1133 -2186 334 N ATOM 1089 CA VAL A 137 -2.247 22.143 28.828 1.00 66.20 C ANISOU 1089 CA VAL A 137 9364 9129 6661 -1280 -2174 195 C ATOM 1090 C VAL A 137 -2.279 20.684 29.283 1.00 73.34 C ANISOU 1090 C VAL A 137 10270 9916 7679 -1336 -2170 60 C ATOM 1091 O VAL A 137 -3.019 19.862 28.731 1.00 65.95 O ANISOU 1091 O VAL A 137 9384 9031 6645 -1468 -2243 -8 O ATOM 1092 CB VAL A 137 -1.086 22.413 27.849 1.00 66.50 C ANISOU 1092 CB VAL A 137 9513 9143 6610 -1288 -2024 103 C ATOM 1093 CG1 VAL A 137 -0.812 21.202 26.967 1.00 63.22 C ANISOU 1093 CG1 VAL A 137 9220 8691 6110 -1415 -1962 -93 C ATOM 1094 CG2 VAL A 137 -1.387 23.642 26.992 1.00 69.48 C ANISOU 1094 CG2 VAL A 137 9916 9679 6803 -1292 -2057 228 C ATOM 1095 N VAL A 138 -1.491 20.341 30.301 1.00 75.51 N ANISOU 1095 N VAL A 138 10489 10036 8166 -1240 -2087 22 N ATOM 1096 CA VAL A 138 -1.374 18.944 30.702 1.00 69.41 C ANISOU 1096 CA VAL A 138 9723 9135 7516 -1285 -2060 -107 C ATOM 1097 C VAL A 138 -2.568 18.511 31.551 1.00 72.41 C ANISOU 1097 C VAL A 138 10001 9543 7967 -1302 -2209 -24 C ATOM 1098 O VAL A 138 -3.095 17.409 31.374 1.00 75.37 O ANISOU 1098 O VAL A 138 10407 9893 8336 -1411 -2253 -110 O ATOM 1099 CB VAL A 138 -0.033 18.714 31.428 1.00 61.64 C ANISOU 1099 CB VAL A 138 8712 7981 6728 -1174 -1909 -170 C ATOM 1100 CG1 VAL A 138 -0.035 17.381 32.161 1.00 62.31 C ANISOU 1100 CG1 VAL A 138 8764 7931 6980 -1188 -1897 -254 C ATOM 1101 CG2 VAL A 138 1.120 18.760 30.433 1.00 55.67 C ANISOU 1101 CG2 VAL A 138 8073 7184 5895 -1190 -1752 -290 C ATOM 1102 N VAL A 139 -3.025 19.360 32.468 1.00 70.99 N ANISOU 1102 N VAL A 139 9701 9415 7856 -1198 -2286 142 N ATOM 1103 CA VAL A 139 -4.109 18.989 33.379 1.00 62.73 C ANISOU 1103 CA VAL A 139 8545 8397 6892 -1197 -2417 233 C ATOM 1104 C VAL A 139 -5.481 19.255 32.763 1.00 67.72 C ANISOU 1104 C VAL A 139 9176 9207 7350 -1293 -2571 325 C ATOM 1105 O VAL A 139 -6.350 18.379 32.754 1.00 77.68 O ANISOU 1105 O VAL A 139 10424 10492 8600 -1395 -2665 305 O ATOM 1106 CB VAL A 139 -3.949 19.722 34.729 1.00 58.95 C ANISOU 1106 CB VAL A 139 7935 7889 6574 -1034 -2421 362 C ATOM 1107 CG1 VAL A 139 -5.159 19.466 35.610 1.00 64.01 C ANISOU 1107 CG1 VAL A 139 8460 8585 7276 -1028 -2561 475 C ATOM 1108 CG2 VAL A 139 -2.676 19.276 35.438 1.00 56.63 C ANISOU 1108 CG2 VAL A 139 7626 7425 6464 -950 -2284 274 C ATOM 1109 N CYS A 140 -5.711 20.460 32.239 1.00 76.99 N ANISOU 1109 N CYS A 140 11166 7562 10525 -2129 -1969 -49 N ATOM 1110 CA CYS A 140 -7.022 20.790 31.688 1.00 72.96 C ANISOU 1110 CA CYS A 140 10599 7191 9933 -2207 -2127 -105 C ATOM 1111 C CYS A 140 -7.282 20.135 30.341 1.00 76.99 C ANISOU 1111 C CYS A 140 11221 7706 10325 -2357 -2131 -324 C ATOM 1112 O CYS A 140 -8.435 20.130 29.896 1.00 85.34 O ANISOU 1112 O CYS A 140 12222 8858 11345 -2425 -2229 -392 O ATOM 1113 CB CYS A 140 -7.177 22.305 31.556 1.00 65.64 C ANISOU 1113 CB CYS A 140 9625 6461 8853 -2166 -2301 26 C ATOM 1114 SG CYS A 140 -6.951 23.204 33.104 1.00 76.06 S ANISOU 1114 SG CYS A 140 10789 7810 10300 -1997 -2305 258 S ATOM 1115 N LYS A 141 -6.252 19.601 29.691 1.00 85.27 N ANISOU 1115 N LYS A 141 12420 8665 11312 -2404 -2020 -438 N ATOM 1116 CA LYS A 141 -6.378 18.872 28.433 1.00 80.04 C ANISOU 1116 CA LYS A 141 11863 8005 10542 -2547 -1992 -671 C ATOM 1117 C LYS A 141 -7.191 19.631 27.381 1.00 83.72 C ANISOU 1117 C LYS A 141 12322 8707 10782 -2630 -2184 -714 C ATOM 1118 O LYS A 141 -8.198 19.119 26.879 1.00 88.70 O ANISOU 1118 O LYS A 141 12908 9379 11417 -2721 -2218 -849 O ATOM 1119 CB LYS A 141 -6.973 17.493 28.673 1.00 69.33 C ANISOU 1119 CB LYS A 141 10458 6484 9401 -2596 -1860 -811 C ATOM 1120 CG LYS A 141 -6.051 16.496 29.352 1.00 78.80 C ANISOU 1120 CG LYS A 141 11691 7439 10811 -2535 -1629 -812 C ATOM 1121 CD LYS A 141 -6.877 15.543 30.199 1.00 81.64 C ANISOU 1121 CD LYS A 141 11918 7659 11441 -2518 -1538 -815 C ATOM 1122 CE LYS A 141 -6.458 14.099 30.036 1.00 85.93 C ANISOU 1122 CE LYS A 141 12509 7975 12165 -2562 -1310 -978 C ATOM 1123 NZ LYS A 141 -7.274 13.207 30.921 1.00 94.89 N ANISOU 1123 NZ LYS A 141 13505 8973 13576 -2539 -1216 -959 N ATOM 1124 N PRO A 142 -6.773 20.843 27.011 1.00 89.49 N ANISOU 1124 N PRO A 142 13086 9596 11319 -2598 -2302 -598 N ATOM 1125 CA PRO A 142 -7.550 21.616 26.031 1.00 82.99 C ANISOU 1125 CA PRO A 142 12238 9003 10291 -2658 -2472 -603 C ATOM 1126 C PRO A 142 -7.426 21.096 24.611 1.00 95.04 C ANISOU 1126 C PRO A 142 13878 10607 11626 -2794 -2457 -816 C ATOM 1127 O PRO A 142 -8.254 21.457 23.766 1.00 95.38 O ANISOU 1127 O PRO A 142 13880 10834 11525 -2856 -2579 -850 O ATOM 1128 CB PRO A 142 -6.966 23.032 26.150 1.00 75.42 C ANISOU 1128 CB PRO A 142 11276 8162 9217 -2566 -2568 -399 C ATOM 1129 CG PRO A 142 -5.836 22.943 27.161 1.00 81.43 C ANISOU 1129 CG PRO A 142 12071 8757 10111 -2471 -2449 -314 C ATOM 1130 CD PRO A 142 -5.503 21.505 27.339 1.00 92.15 C ANISOU 1130 CD PRO A 142 13495 9908 11611 -2513 -2268 -472 C ATOM 1131 N MET A 143 -6.424 20.274 24.317 1.00102.51 N ANISOU 1131 N MET A 143 14957 11426 12568 -2836 -2300 -961 N ATOM 1132 CA MET A 143 -6.185 19.772 22.975 1.00 99.59 C ANISOU 1132 CA MET A 143 14694 11136 12009 -2961 -2262 -1178 C ATOM 1133 C MET A 143 -6.518 18.289 22.893 1.00105.45 C ANISOU 1133 C MET A 143 15432 11719 12915 -3045 -2116 -1413 C ATOM 1134 O MET A 143 -6.439 17.558 23.884 1.00103.97 O ANISOU 1134 O MET A 143 15208 11310 12986 -2994 -1988 -1401 O ATOM 1135 CB MET A 143 -4.733 20.001 22.554 1.00 98.99 C ANISOU 1135 CB MET A 143 14777 11050 11784 -2947 -2175 -1186 C ATOM 1136 CG MET A 143 -4.544 21.188 21.636 1.00 97.46 C ANISOU 1136 CG MET A 143 14620 11110 11301 -2954 -2318 -1098 C ATOM 1137 SD MET A 143 -2.962 21.994 21.912 1.00 98.70 S ANISOU 1137 SD MET A 143 14866 11249 11388 -2814 -2233 -936 S ATOM 1138 CE MET A 143 -3.237 22.702 23.532 1.00102.75 C ANISOU 1138 CE MET A 143 15225 11675 12142 -2647 -2281 -670 C ATOM 1139 N SER A 144 -6.889 17.854 21.694 1.00118.48 N ANISOU 1139 N SER A 144 17107 13489 14419 -3169 -2130 -1624 N ATOM 1140 CA SER A 144 -7.296 16.474 21.476 1.00115.48 C ANISOU 1140 CA SER A 144 16705 12979 14192 -3260 -2002 -1872 C ATOM 1141 C SER A 144 -6.057 15.598 21.328 1.00122.84 C ANISOU 1141 C SER A 144 17763 13731 15181 -3272 -1773 -2015 C ATOM 1142 O SER A 144 -5.239 15.819 20.427 1.00131.00 O ANISOU 1142 O SER A 144 18913 14868 15995 -3308 -1744 -2089 O ATOM 1143 CB SER A 144 -8.187 16.379 20.239 1.00115.67 C ANISOU 1143 CB SER A 144 16693 13218 14040 -3383 -2111 -2048 C ATOM 1144 OG SER A 144 -8.870 15.140 20.191 1.00132.13 O ANISOU 1144 OG SER A 144 18711 15179 16313 -3459 -2024 -2267 O ATOM 1145 N ASN A 145 -5.910 14.624 22.231 1.00119.78 N ANISOU 1145 N ASN A 145 17343 13074 15093 -3229 -1600 -2040 N ATOM 1146 CA ASN A 145 -4.871 13.593 22.141 1.00123.39 C ANISOU 1146 CA ASN A 145 17887 13327 15670 -3232 -1349 -2187 C ATOM 1147 C ASN A 145 -3.466 14.190 22.057 1.00113.65 C ANISOU 1147 C ASN A 145 16794 12099 14289 -3166 -1281 -2092 C ATOM 1148 O ASN A 145 -2.603 13.690 21.333 1.00112.24 O ANISOU 1148 O ASN A 145 16715 11890 14042 -3204 -1129 -2255 O ATOM 1149 CB ASN A 145 -5.132 12.655 20.959 1.00129.37 C ANISOU 1149 CB ASN A 145 18653 14120 16380 -3366 -1283 -2496 C ATOM 1150 CG ASN A 145 -6.190 11.612 21.266 1.00134.38 C ANISOU 1150 CG ASN A 145 19159 14621 17280 -3408 -1250 -2618 C ATOM 1151 OD1 ASN A 145 -5.874 10.505 21.702 1.00135.40 O ANISOU 1151 OD1 ASN A 145 19268 14499 17677 -3382 -1050 -2695 O ATOM 1152 ND2 ASN A 145 -7.454 11.962 21.042 1.00132.00 N ANISOU 1152 ND2 ASN A 145 18760 14481 16912 -3463 -1444 -2625 N ATOM 1153 N PHE A 146 -3.230 15.260 22.812 1.00103.06 N ANISOU 1153 N PHE A 146 15453 10798 12909 -3060 -1388 -1832 N ATOM 1154 CA PHE A 146 -1.919 15.894 22.874 1.00 88.72 C ANISOU 1154 CA PHE A 146 13709 9010 10989 -2931 -1311 -1698 C ATOM 1155 C PHE A 146 -1.131 15.323 24.047 1.00 89.45 C ANISOU 1155 C PHE A 146 13760 8865 11360 -2769 -1094 -1581 C ATOM 1156 O PHE A 146 -1.650 15.238 25.165 1.00 98.76 O ANISOU 1156 O PHE A 146 14826 9946 12751 -2695 -1110 -1440 O ATOM 1157 CB PHE A 146 -2.067 17.410 23.016 1.00 82.66 C ANISOU 1157 CB PHE A 146 12908 8455 10045 -2856 -1524 -1463 C ATOM 1158 CG PHE A 146 -0.762 18.140 23.190 1.00 86.17 C ANISOU 1158 CG PHE A 146 13400 8934 10407 -2703 -1447 -1305 C ATOM 1159 CD1 PHE A 146 -0.029 18.550 22.087 1.00 89.00 C ANISOU 1159 CD1 PHE A 146 13872 9437 10505 -2740 -1443 -1374 C ATOM 1160 CD2 PHE A 146 -0.278 18.435 24.457 1.00 85.23 C ANISOU 1160 CD2 PHE A 146 13203 8716 10464 -2523 -1379 -1088 C ATOM 1161 CE1 PHE A 146 1.170 19.228 22.242 1.00 82.63 C ANISOU 1161 CE1 PHE A 146 13106 8657 9631 -2600 -1368 -1230 C ATOM 1162 CE2 PHE A 146 0.920 19.114 24.621 1.00 88.02 C ANISOU 1162 CE2 PHE A 146 13592 9106 10744 -2385 -1308 -952 C ATOM 1163 CZ PHE A 146 1.645 19.511 23.511 1.00 78.77 C ANISOU 1163 CZ PHE A 146 12539 8062 9328 -2423 -1301 -1023 C ATOM 1164 N ARG A 147 0.119 14.934 23.789 1.00 87.18 N ANISOU 1164 N ARG A 147 13559 8497 11070 -2715 -893 -1635 N ATOM 1165 CA ARG A 147 1.020 14.416 24.816 1.00 88.42 C ANISOU 1165 CA ARG A 147 13680 8446 11469 -2555 -677 -1515 C ATOM 1166 C ARG A 147 2.257 15.304 24.881 1.00 86.88 C ANISOU 1166 C ARG A 147 13535 8341 11134 -2412 -644 -1357 C ATOM 1167 O ARG A 147 2.970 15.456 23.882 1.00 87.87 O ANISOU 1167 O ARG A 147 13775 8547 11062 -2456 -604 -1469 O ATOM 1168 CB ARG A 147 1.410 12.963 24.532 1.00 92.26 C ANISOU 1168 CB ARG A 147 14206 8708 12141 -2615 -430 -1732 C ATOM 1169 CG ARG A 147 2.191 12.301 25.661 1.00108.96 C ANISOU 1169 CG ARG A 147 16259 10593 14547 -2454 -205 -1594 C ATOM 1170 CD ARG A 147 2.770 10.955 25.238 1.00122.63 C ANISOU 1170 CD ARG A 147 18040 12104 16450 -2507 56 -1807 C ATOM 1171 NE ARG A 147 1.746 9.934 25.018 1.00135.61 N ANISOU 1171 NE ARG A 147 19636 13630 18261 -2650 79 -2006 N ATOM 1172 CZ ARG A 147 1.373 9.039 25.928 1.00136.67 C ANISOU 1172 CZ ARG A 147 19631 13580 18718 -2578 184 -1934 C ATOM 1173 NH1 ARG A 147 1.936 9.037 27.129 1.00127.15 N ANISOU 1173 NH1 ARG A 147 18361 12256 17696 -2409 289 -1689 N ATOM 1174 NH2 ARG A 147 0.437 8.143 25.637 1.00140.77 N ANISOU 1174 NH2 ARG A 147 20071 14048 19368 -2670 179 -2096 N ATOM 1175 N PHE A 148 2.515 15.872 26.060 1.00 82.21 N ANISOU 1175 N PHE A 148 12852 7738 10646 -2246 -654 -1104 N ATOM 1176 CA PHE A 148 3.590 16.843 26.249 1.00 76.85 C ANISOU 1176 CA PHE A 148 12197 7158 9845 -2105 -644 -937 C ATOM 1177 C PHE A 148 4.941 16.134 26.313 1.00 76.55 C ANISOU 1177 C PHE A 148 12216 6967 9902 -2018 -385 -967 C ATOM 1178 O PHE A 148 5.194 15.346 27.231 1.00 75.98 O ANISOU 1178 O PHE A 148 12073 6712 10083 -1931 -226 -904 O ATOM 1179 CB PHE A 148 3.345 17.652 27.524 1.00 60.62 C ANISOU 1179 CB PHE A 148 10006 5149 7879 -1967 -741 -678 C ATOM 1180 CG PHE A 148 4.359 18.727 27.766 1.00 72.08 C ANISOU 1180 CG PHE A 148 11461 6710 9214 -1827 -744 -510 C ATOM 1181 CD1 PHE A 148 5.499 18.470 28.513 1.00 77.18 C ANISOU 1181 CD1 PHE A 148 12086 7256 9983 -1675 -555 -408 C ATOM 1182 CD2 PHE A 148 4.173 20.002 27.249 1.00 65.62 C ANISOU 1182 CD2 PHE A 148 10661 6099 8173 -1846 -932 -451 C ATOM 1183 CE1 PHE A 148 6.438 19.468 28.740 1.00 73.58 C ANISOU 1183 CE1 PHE A 148 11627 6905 9424 -1549 -556 -265 C ATOM 1184 CE2 PHE A 148 5.105 21.001 27.472 1.00 70.08 C ANISOU 1184 CE2 PHE A 148 11222 6757 8649 -1720 -927 -303 C ATOM 1185 CZ PHE A 148 6.238 20.736 28.216 1.00 66.85 C ANISOU 1185 CZ PHE A 148 10793 6248 8359 -1573 -740 -218 C ATOM 1186 N GLY A 149 5.818 16.433 25.356 1.00 71.78 N ANISOU 1186 N GLY A 149 11734 6443 9098 -2036 -341 -1051 N ATOM 1187 CA GLY A 149 7.101 15.760 25.275 1.00 67.72 C ANISOU 1187 CA GLY A 149 11282 5787 8660 -1969 -95 -1102 C ATOM 1188 C GLY A 149 8.315 16.660 25.417 1.00 83.17 C ANISOU 1188 C GLY A 149 13269 7831 10500 -1825 -61 -949 C ATOM 1189 O GLY A 149 8.208 17.820 25.829 1.00 84.10 O ANISOU 1189 O GLY A 149 13333 8098 10521 -1750 -213 -769 O ATOM 1190 N GLU A 150 9.486 16.128 25.058 1.00 82.85 N ANISOU 1190 N GLU A 150 13310 7692 10478 -1789 146 -1028 N ATOM 1191 CA GLU A 150 10.729 16.863 25.267 1.00 76.72 C ANISOU 1191 CA GLU A 150 12555 6971 9622 -1644 208 -886 C ATOM 1192 C GLU A 150 10.828 18.077 24.347 1.00 79.20 C ANISOU 1192 C GLU A 150 12949 7516 9627 -1687 48 -884 C ATOM 1193 O GLU A 150 11.339 19.126 24.755 1.00 81.66 O ANISOU 1193 O GLU A 150 13228 7934 9866 -1568 -9 -704 O ATOM 1194 CB GLU A 150 11.928 15.934 25.064 1.00 74.13 C ANISOU 1194 CB GLU A 150 12293 6472 9400 -1603 474 -980 C ATOM 1195 CG GLU A 150 13.241 16.518 25.564 1.00 89.92 C ANISOU 1195 CG GLU A 150 14286 8491 11387 -1427 568 -810 C ATOM 1196 CD GLU A 150 14.448 15.710 25.136 1.00102.89 C ANISOU 1196 CD GLU A 150 16013 9988 13094 -1403 817 -921 C ATOM 1197 OE1 GLU A 150 14.268 14.690 24.436 1.00104.27 O ANISOU 1197 OE1 GLU A 150 16250 10042 13326 -1527 924 -1141 O ATOM 1198 OE2 GLU A 150 15.577 16.101 25.502 1.00105.64 O ANISOU 1198 OE2 GLU A 150 16358 10342 13440 -1263 910 -796 O ATOM 1199 N ASN A 151 10.347 17.959 23.104 1.00 84.03 N ANISOU 1199 N ASN A 151 13657 8215 10056 -1856 -22 -1082 N ATOM 1200 CA ASN A 151 10.460 19.074 22.164 1.00 78.67 C ANISOU 1200 CA ASN A 151 13050 7763 9077 -1899 -166 -1071 C ATOM 1201 C ASN A 151 9.558 20.243 22.548 1.00 77.86 C ANISOU 1201 C ASN A 151 12858 7826 8901 -1882 -413 -893 C ATOM 1202 O ASN A 151 9.899 21.397 22.274 1.00 74.15 O ANISOU 1202 O ASN A 151 12401 7515 8258 -1835 -509 -776 O ATOM 1203 CB ASN A 151 10.145 18.615 20.739 1.00 77.44 C ANISOU 1203 CB ASN A 151 13009 7683 8734 -2091 -179 -1327 C ATOM 1204 CG ASN A 151 11.219 17.707 20.162 1.00 89.48 C ANISOU 1204 CG ASN A 151 14637 9082 10279 -2109 64 -1508 C ATOM 1205 OD1 ASN A 151 10.950 16.897 19.275 1.00 99.28 O ANISOU 1205 OD1 ASN A 151 15945 10305 11472 -2263 118 -1755 O ATOM 1206 ND2 ASN A 151 12.441 17.833 20.669 1.00 84.21 N ANISOU 1206 ND2 ASN A 151 13977 8330 9690 -1954 216 -1393 N ATOM 1207 N HIS A 152 8.408 19.980 23.168 1.00 79.05 N ANISOU 1207 N HIS A 152 12910 7936 9190 -1918 -514 -870 N ATOM 1208 CA HIS A 152 7.595 21.089 23.657 1.00 75.60 C ANISOU 1208 CA HIS A 152 12372 7637 8716 -1888 -733 -691 C ATOM 1209 C HIS A 152 8.287 21.792 24.814 1.00 76.47 C ANISOU 1209 C HIS A 152 12391 7729 8934 -1698 -696 -465 C ATOM 1210 O HIS A 152 8.253 23.025 24.907 1.00 77.31 O ANISOU 1210 O HIS A 152 12454 7982 8940 -1646 -832 -318 O ATOM 1211 CB HIS A 152 6.209 20.595 24.076 1.00 72.44 C ANISOU 1211 CB HIS A 152 11885 7190 8449 -1972 -839 -726 C ATOM 1212 CG HIS A 152 5.512 19.794 23.020 1.00 72.76 C ANISOU 1212 CG HIS A 152 12000 7237 8408 -2163 -862 -968 C ATOM 1213 ND1 HIS A 152 5.218 18.455 23.174 1.00 74.27 N ANISOU 1213 ND1 HIS A 152 12188 7243 8789 -2227 -731 -1127 N ATOM 1214 CD2 HIS A 152 5.069 20.137 21.788 1.00 63.93 C ANISOU 1214 CD2 HIS A 152 10954 6297 7040 -2305 -993 -1082 C ATOM 1215 CE1 HIS A 152 4.613 18.012 22.087 1.00 73.03 C ANISOU 1215 CE1 HIS A 152 12096 7148 8504 -2405 -782 -1346 C ATOM 1216 NE2 HIS A 152 4.512 19.012 21.230 1.00 77.65 N ANISOU 1216 NE2 HIS A 152 12728 7963 8811 -2456 -944 -1321 N ATOM 1217 N ALA A 153 8.944 21.023 25.688 1.00 78.40 N ANISOU 1217 N ALA A 153 12600 7801 9389 -1594 -508 -435 N ATOM 1218 CA ALA A 153 9.624 21.609 26.839 1.00 77.80 C ANISOU 1218 CA ALA A 153 12424 7719 9416 -1414 -463 -230 C ATOM 1219 C ALA A 153 10.780 22.506 26.407 1.00 73.41 C ANISOU 1219 C ALA A 153 11931 7263 8700 -1337 -429 -173 C ATOM 1220 O ALA A 153 11.007 23.566 27.004 1.00 69.55 O ANISOU 1220 O ALA A 153 11360 6869 8198 -1233 -499 -6 O ATOM 1221 CB ALA A 153 10.117 20.504 27.775 1.00 63.75 C ANISOU 1221 CB ALA A 153 10594 5744 7884 -1325 -258 -212 C ATOM 1222 N ILE A 154 11.519 22.095 25.372 1.00 76.71 N ANISOU 1222 N ILE A 154 12488 7659 8999 -1391 -316 -316 N ATOM 1223 CA ILE A 154 12.596 22.921 24.830 1.00 72.29 C ANISOU 1223 CA ILE A 154 11998 7195 8273 -1332 -282 -275 C ATOM 1224 C ILE A 154 12.028 24.166 24.157 1.00 74.71 C ANISOU 1224 C ILE A 154 12310 7708 8369 -1391 -497 -220 C ATOM 1225 O ILE A 154 12.578 25.267 24.289 1.00 72.68 O ANISOU 1225 O ILE A 154 12024 7549 8044 -1299 -535 -82 O ATOM 1226 CB ILE A 154 13.457 22.091 23.857 1.00 71.97 C ANISOU 1226 CB ILE A 154 12105 7079 8162 -1387 -104 -458 C ATOM 1227 CG1 ILE A 154 14.092 20.897 24.581 1.00 69.56 C ANISOU 1227 CG1 ILE A 154 11779 6557 8095 -1312 122 -488 C ATOM 1228 CG2 ILE A 154 14.518 22.960 23.198 1.00 60.21 C ANISOU 1228 CG2 ILE A 154 10694 5699 6484 -1338 -76 -421 C ATOM 1229 CD1 ILE A 154 14.626 19.830 23.645 1.00 70.48 C ANISOU 1229 CD1 ILE A 154 12024 6563 8193 -1400 298 -707 C ATOM 1230 N MET A 155 10.924 24.008 23.419 1.00 75.57 N ANISOU 1230 N MET A 155 12449 7887 8379 -1546 -636 -323 N ATOM 1231 CA MET A 155 10.236 25.157 22.838 1.00 76.35 C ANISOU 1231 CA MET A 155 12531 8183 8296 -1604 -853 -249 C ATOM 1232 C MET A 155 9.827 26.158 23.916 1.00 76.36 C ANISOU 1232 C MET A 155 12379 8227 8408 -1500 -974 -40 C ATOM 1233 O MET A 155 9.948 27.374 23.723 1.00 74.31 O ANISOU 1233 O MET A 155 12089 8101 8044 -1461 -1076 86 O ATOM 1234 CB MET A 155 9.018 24.676 22.047 1.00 96.06 C ANISOU 1234 CB MET A 155 15060 10737 10702 -1785 -980 -394 C ATOM 1235 CG MET A 155 8.229 25.761 21.332 1.00122.40 C ANISOU 1235 CG MET A 155 18378 14287 13843 -1862 -1208 -321 C ATOM 1236 SD MET A 155 6.619 25.160 20.760 1.00143.06 S ANISOU 1236 SD MET A 155 20985 16962 16410 -2059 -1373 -467 S ATOM 1237 CE MET A 155 5.690 25.145 22.294 1.00131.65 C ANISOU 1237 CE MET A 155 19372 15403 15247 -1988 -1446 -341 C ATOM 1238 N GLY A 156 9.365 25.664 25.069 1.00 67.96 N ANISOU 1238 N GLY A 156 11209 7051 7562 -1452 -956 0 N ATOM 1239 CA GLY A 156 8.984 26.560 26.149 1.00 57.19 C ANISOU 1239 CA GLY A 156 9690 5730 6310 -1356 -1058 182 C ATOM 1240 C GLY A 156 10.161 27.311 26.749 1.00 71.37 C ANISOU 1240 C GLY A 156 11440 7540 8136 -1196 -966 312 C ATOM 1241 O GLY A 156 10.036 28.483 27.114 1.00 74.37 O ANISOU 1241 O GLY A 156 11724 8021 8513 -1138 -1072 449 O ATOM 1242 N VAL A 157 11.315 26.647 26.872 1.00 74.31 N ANISOU 1242 N VAL A 157 11873 7810 8552 -1124 -762 269 N ATOM 1243 CA VAL A 157 12.501 27.320 27.396 1.00 73.71 C ANISOU 1243 CA VAL A 157 11757 7751 8497 -974 -666 380 C ATOM 1244 C VAL A 157 13.013 28.357 26.404 1.00 67.42 C ANISOU 1244 C VAL A 157 11034 7081 7503 -985 -715 401 C ATOM 1245 O VAL A 157 13.352 29.484 26.785 1.00 62.11 O ANISOU 1245 O VAL A 157 10278 6489 6832 -896 -758 530 O ATOM 1246 CB VAL A 157 13.594 26.296 27.752 1.00 66.26 C ANISOU 1246 CB VAL A 157 10856 6664 7654 -896 -434 332 C ATOM 1247 CG1 VAL A 157 14.865 27.019 28.185 1.00 60.86 C ANISOU 1247 CG1 VAL A 157 10136 6015 6972 -748 -337 436 C ATOM 1248 CG2 VAL A 157 13.112 25.374 28.852 1.00 53.56 C ANISOU 1248 CG2 VAL A 157 9150 4941 6261 -866 -383 351 C ATOM 1249 N ALA A 158 13.079 28.000 25.117 1.00 66.54 N ANISOU 1249 N ALA A 158 11071 6993 7220 -1097 -705 274 N ATOM 1250 CA ALA A 158 13.536 28.957 24.114 1.00 67.23 C ANISOU 1250 CA ALA A 158 11227 7211 7106 -1113 -752 303 C ATOM 1251 C ALA A 158 12.621 30.170 24.045 1.00 74.06 C ANISOU 1251 C ALA A 158 12000 8219 7922 -1139 -967 428 C ATOM 1252 O ALA A 158 13.091 31.288 23.795 1.00 73.53 O ANISOU 1252 O ALA A 158 11912 8246 7781 -1085 -1000 535 O ATOM 1253 CB ALA A 158 13.632 28.284 22.743 1.00 55.70 C ANISOU 1253 CB ALA A 158 9933 5771 5459 -1244 -713 132 C ATOM 1254 N PHE A 159 11.318 29.970 24.268 1.00 75.40 N ANISOU 1254 N PHE A 159 12105 8399 8143 -1221 -1110 419 N ATOM 1255 CA PHE A 159 10.372 31.081 24.231 1.00 69.83 C ANISOU 1255 CA PHE A 159 11301 7820 7412 -1249 -1315 541 C ATOM 1256 C PHE A 159 10.657 32.085 25.342 1.00 72.20 C ANISOU 1256 C PHE A 159 11448 8124 7863 -1109 -1322 702 C ATOM 1257 O PHE A 159 10.520 33.296 25.142 1.00 69.86 O ANISOU 1257 O PHE A 159 11086 7931 7525 -1091 -1428 821 O ATOM 1258 CB PHE A 159 8.941 30.550 24.331 1.00 66.33 C ANISOU 1258 CB PHE A 159 10816 7370 7016 -1362 -1452 488 C ATOM 1259 CG PHE A 159 7.896 31.624 24.426 1.00 66.10 C ANISOU 1259 CG PHE A 159 10668 7454 6995 -1387 -1661 617 C ATOM 1260 CD1 PHE A 159 7.507 32.333 23.297 1.00 64.04 C ANISOU 1260 CD1 PHE A 159 10443 7343 6545 -1471 -1797 653 C ATOM 1261 CD2 PHE A 159 7.291 31.919 25.644 1.00 63.28 C ANISOU 1261 CD2 PHE A 159 10152 7056 6835 -1327 -1719 707 C ATOM 1262 CE1 PHE A 159 6.536 33.325 23.379 1.00 64.97 C ANISOU 1262 CE1 PHE A 159 10440 7557 6687 -1491 -1986 784 C ATOM 1263 CE2 PHE A 159 6.322 32.909 25.738 1.00 65.00 C ANISOU 1263 CE2 PHE A 159 10252 7367 7078 -1351 -1905 822 C ATOM 1264 CZ PHE A 159 5.944 33.614 24.602 1.00 68.60 C ANISOU 1264 CZ PHE A 159 10744 7960 7360 -1431 -2038 864 C ATOM 1265 N THR A 160 11.059 31.604 26.523 1.00 62.20 N ANISOU 1265 N THR A 160 10111 6749 6774 -1011 -1206 709 N ATOM 1266 CA THR A 160 11.401 32.526 27.601 1.00 61.43 C ANISOU 1266 CA THR A 160 9859 6671 6811 -880 -1200 842 C ATOM 1267 C THR A 160 12.646 33.338 27.257 1.00 65.74 C ANISOU 1267 C THR A 160 10435 7260 7282 -794 -1111 895 C ATOM 1268 O THR A 160 12.704 34.539 27.542 1.00 69.72 O ANISOU 1268 O THR A 160 10829 7836 7825 -735 -1172 1008 O ATOM 1269 CB THR A 160 11.596 31.770 28.919 1.00 58.94 C ANISOU 1269 CB THR A 160 9459 6254 6681 -796 -1089 840 C ATOM 1270 OG1 THR A 160 12.700 30.868 28.805 1.00 68.56 O ANISOU 1270 OG1 THR A 160 10782 7381 7887 -751 -895 764 O ATOM 1271 CG2 THR A 160 10.343 30.982 29.281 1.00 55.24 C ANISOU 1271 CG2 THR A 160 8954 5738 6299 -879 -1172 796 C ATOM 1272 N ATRP A 161 13.650 32.694 26.651 0.51 64.44 N ANISOU 1272 N ATRP A 161 10412 7046 7025 -787 -961 809 N ATOM 1273 N BTRP A 161 13.646 32.714 26.630 0.49 64.51 N ANISOU 1273 N BTRP A 161 10422 7057 7030 -788 -964 810 N ATOM 1274 CA ATRP A 161 14.864 33.401 26.254 0.51 60.87 C ANISOU 1274 CA ATRP A 161 10000 6631 6497 -710 -868 851 C ATOM 1275 CA BTRP A 161 14.859 33.456 26.290 0.49 60.85 C ANISOU 1275 CA BTRP A 161 9990 6631 6499 -706 -872 857 C ATOM 1276 C ATRP A 161 14.558 34.489 25.229 0.51 67.80 C ANISOU 1276 C ATRP A 161 10898 7635 7228 -768 -999 918 C ATOM 1277 C BTRP A 161 14.596 34.490 25.197 0.49 67.66 C ANISOU 1277 C BTRP A 161 10886 7618 7205 -768 -996 917 C ATOM 1278 O ATRP A 161 15.067 35.612 25.331 0.51 65.11 O ANISOU 1278 O ATRP A 161 10486 7347 6905 -690 -1000 1024 O ATOM 1279 O BTRP A 161 15.170 35.585 25.225 0.49 66.28 O ANISOU 1279 O BTRP A 161 10651 7495 7036 -691 -988 1018 O ATOM 1280 CB ATRP A 161 15.891 32.415 25.690 0.51 57.70 C ANISOU 1280 CB ATRP A 161 9756 6150 6016 -710 -688 732 C ATOM 1281 CB BTRP A 161 15.973 32.492 25.880 0.49 57.00 C ANISOU 1281 CB BTRP A 161 9646 6058 5953 -688 -679 748 C ATOM 1282 CG ATRP A 161 16.351 31.343 26.653 0.51 53.64 C ANISOU 1282 CG ATRP A 161 9219 5505 5656 -639 -535 685 C ATOM 1283 CG BTRP A 161 16.692 31.872 27.055 0.49 56.10 C ANISOU 1283 CG BTRP A 161 9468 5840 6008 -571 -523 749 C ATOM 1284 CD1ATRP A 161 16.026 31.227 27.977 0.51 55.83 C ANISOU 1284 CD1ATRP A 161 9349 5747 6117 -568 -540 748 C ATOM 1285 CD1BTRP A 161 16.226 30.884 27.875 0.49 54.09 C ANISOU 1285 CD1BTRP A 161 9165 5495 5891 -571 -492 716 C ATOM 1286 CD2ATRP A 161 17.222 30.241 26.359 0.51 46.12 C ANISOU 1286 CD2ATRP A 161 8388 4445 4690 -632 -351 575 C ATOM 1287 CD2BTRP A 161 18.006 32.200 27.534 0.49 63.42 C ANISOU 1287 CD2BTRP A 161 10363 6751 6982 -436 -377 795 C ATOM 1288 NE1ATRP A 161 16.638 30.120 28.521 0.51 51.26 N ANISOU 1288 NE1ATRP A 161 8790 5051 5638 -514 -373 698 N ATOM 1289 NE1BTRP A 161 17.162 30.580 28.835 0.49 55.36 N ANISOU 1289 NE1BTRP A 161 9264 5595 6176 -442 -339 750 N ATOM 1290 CE2ATRP A 161 17.378 29.499 27.549 0.51 55.08 C ANISOU 1290 CE2ATRP A 161 9436 5479 6013 -551 -253 592 C ATOM 1291 CE2BTRP A 161 18.265 31.373 28.646 0.49 65.91 C ANISOU 1291 CE2BTRP A 161 10608 6978 7457 -359 -268 794 C ATOM 1292 CE3ATRP A 161 17.884 29.810 25.205 0.51 49.71 C ANISOU 1292 CE3ATRP A 161 9009 4883 4997 -688 -256 465 C ATOM 1293 CE3BTRP A 161 18.986 33.114 27.131 0.49 57.84 C ANISOU 1293 CE3BTRP A 161 9674 6099 6202 -373 -326 842 C ATOM 1294 CZ2ATRP A 161 18.172 28.348 27.616 0.51 55.11 C ANISOU 1294 CZ2ATRP A 161 9510 5353 6075 -519 -62 513 C ATOM 1295 CZ2BTRP A 161 19.464 31.431 29.357 0.49 60.97 C ANISOU 1295 CZ2BTRP A 161 9928 6330 6908 -223 -117 836 C ATOM 1296 CZ3ATRP A 161 18.672 28.664 25.274 0.51 48.52 C ANISOU 1296 CZ3ATRP A 161 8931 4598 4904 -662 -64 368 C ATOM 1297 CZ3BTRP A 161 20.171 33.170 27.839 0.49 53.63 C ANISOU 1297 CZ3BTRP A 161 9091 5533 5754 -240 -174 871 C ATOM 1298 CH2ATRP A 161 18.809 27.951 26.471 0.51 40.60 C ANISOU 1298 CH2ATRP A 161 7836 3485 4105 -576 32 398 C ATOM 1299 CH2BTRP A 161 20.400 32.334 28.938 0.49 55.26 C ANISOU 1299 CH2BTRP A 161 9226 5663 6108 -168 -74 867 C ATOM 1300 N VAL A 162 13.722 34.174 24.237 1.00 71.87 N ANISOU 1300 N VAL A 162 11501 8204 7601 -905 -1109 860 N ATOM 1301 CA VAL A 162 13.369 35.153 23.208 1.00 65.81 C ANISOU 1301 CA VAL A 162 10750 7575 6681 -967 -1240 939 C ATOM 1302 C VAL A 162 12.580 36.315 23.812 1.00 78.12 C ANISOU 1302 C VAL A 162 12131 9189 8361 -935 -1391 1091 C ATOM 1303 O VAL A 162 12.812 37.481 23.472 1.00 76.77 O ANISOU 1303 O VAL A 162 11911 9096 8164 -899 -1433 1213 O ATOM 1304 CB VAL A 162 12.588 34.467 22.068 1.00 68.30 C ANISOU 1304 CB VAL A 162 11185 7953 6813 -1128 -1327 834 C ATOM 1305 CG1 VAL A 162 11.932 35.493 21.158 1.00 55.64 C ANISOU 1305 CG1 VAL A 162 9558 6513 5070 -1196 -1500 945 C ATOM 1306 CG2 VAL A 162 13.499 33.558 21.260 1.00 67.68 C ANISOU 1306 CG2 VAL A 162 11280 7843 6591 -1163 -1171 686 C ATOM 1307 N MET A 163 11.639 36.022 24.718 1.00 77.95 N ANISOU 1307 N MET A 163 12005 9123 8488 -947 -1468 1088 N ATOM 1308 CA MET A 163 10.843 37.089 25.322 1.00 68.79 C ANISOU 1308 CA MET A 163 10669 8010 7458 -923 -1607 1219 C ATOM 1309 C MET A 163 11.691 37.975 26.227 1.00 71.50 C ANISOU 1309 C MET A 163 10885 8331 7949 -780 -1518 1305 C ATOM 1310 O MET A 163 11.496 39.196 26.267 1.00 72.19 O ANISOU 1310 O MET A 163 10833 8484 8111 -744 -1577 1402 O ATOM 1311 CB MET A 163 9.669 36.504 26.106 1.00 63.55 C ANISOU 1311 CB MET A 163 9924 7303 6919 -971 -1697 1184 C ATOM 1312 CG MET A 163 8.533 35.991 25.239 1.00 72.74 C ANISOU 1312 CG MET A 163 11160 8517 7962 -1122 -1838 1128 C ATOM 1313 SD MET A 163 7.703 37.308 24.334 1.00 74.00 S ANISOU 1313 SD MET A 163 11258 8830 8028 -1187 -2043 1273 S ATOM 1314 CE MET A 163 8.079 36.835 22.648 1.00 82.92 C ANISOU 1314 CE MET A 163 12594 10054 8858 -1293 -2028 1192 C ATOM 1315 N ALA A 164 12.630 37.380 26.966 1.00 65.68 N ANISOU 1315 N ALA A 164 10161 7513 7283 -691 -1353 1244 N ATOM 1316 CA ALA A 164 13.506 38.173 27.823 1.00 65.40 C ANISOU 1316 CA ALA A 164 10002 7470 7375 -558 -1260 1308 C ATOM 1317 C ALA A 164 14.480 39.013 27.001 1.00 73.33 C ANISOU 1317 C ALA A 164 11060 8519 8284 -518 -1201 1361 C ATOM 1318 O ALA A 164 14.792 40.150 27.371 1.00 70.97 O ANISOU 1318 O ALA A 164 10585 8271 8110 -432 -1165 1406 O ATOM 1319 CB ALA A 164 14.261 37.261 28.788 1.00 60.90 C ANISOU 1319 CB ALA A 164 9429 6817 6892 -475 -1100 1237 C ATOM 1320 N LEU A 165 14.979 38.474 25.886 1.00 81.98 N ANISOU 1320 N LEU A 165 12337 9618 9193 -569 -1145 1301 N ATOM 1321 CA LEU A 165 15.807 39.282 24.996 1.00 70.87 C ANISOU 1321 CA LEU A 165 10985 8264 7677 -543 -1100 1361 C ATOM 1322 C LEU A 165 15.011 40.439 24.409 1.00 71.23 C ANISOU 1322 C LEU A 165 10906 8422 7737 -578 -1231 1451 C ATOM 1323 O LEU A 165 15.548 41.535 24.216 1.00 77.28 O ANISOU 1323 O LEU A 165 11567 9236 8559 -504 -1179 1514 O ATOM 1324 CB LEU A 165 16.399 38.415 23.882 1.00 75.65 C ANISOU 1324 CB LEU A 165 11800 8867 8076 -603 -1014 1261 C ATOM 1325 CG LEU A 165 17.723 37.715 24.208 1.00 80.76 C ANISOU 1325 CG LEU A 165 12521 9424 8740 -518 -806 1173 C ATOM 1326 CD1 LEU A 165 17.842 36.380 23.478 1.00 60.17 C ANISOU 1326 CD1 LEU A 165 10096 6775 5992 -604 -736 1026 C ATOM 1327 CD2 LEU A 165 18.900 38.624 23.869 1.00 76.84 C ANISOU 1327 CD2 LEU A 165 12028 8954 8214 -433 -708 1240 C ATOM 1328 N ALA A 166 13.723 40.217 24.125 1.00 73.31 N ANISOU 1328 N ALA A 166 11165 8726 7965 -685 -1389 1455 N ATOM 1329 CA ALA A 166 12.884 41.288 23.596 1.00 71.99 C ANISOU 1329 CA ALA A 166 10857 8663 7834 -711 -1500 1536 C ATOM 1330 C ALA A 166 12.705 42.419 24.598 1.00 81.33 C ANISOU 1330 C ALA A 166 11790 9840 9271 -612 -1483 1587 C ATOM 1331 O ALA A 166 12.297 43.521 24.213 1.00 76.96 O ANISOU 1331 O ALA A 166 11112 9353 8775 -603 -1528 1665 O ATOM 1332 CB ALA A 166 11.517 40.740 23.183 1.00 59.92 C ANISOU 1332 CB ALA A 166 9365 7175 6227 -845 -1667 1517 C ATOM 1333 N CYS A 167 12.999 42.172 25.872 1.00 80.59 N ANISOU 1333 N CYS A 167 11620 9674 9325 -540 -1413 1542 N ATOM 1334 CA CYS A 167 12.906 43.185 26.912 1.00 74.58 C ANISOU 1334 CA CYS A 167 10630 8917 8791 -453 -1382 1563 C ATOM 1335 C CYS A 167 14.256 43.805 27.261 1.00 80.57 C ANISOU 1335 C CYS A 167 11343 9661 9611 -331 -1226 1571 C ATOM 1336 O CYS A 167 14.347 45.027 27.417 1.00 76.04 O ANISOU 1336 O CYS A 167 10620 9114 9158 -277 -1203 1617 O ATOM 1337 CB CYS A 167 12.268 42.580 28.166 1.00 63.32 C ANISOU 1337 CB CYS A 167 9120 7446 7490 -455 -1410 1506 C ATOM 1338 SG CYS A 167 12.435 43.596 29.644 1.00 97.47 S ANISOU 1338 SG CYS A 167 13188 11780 12065 -346 -1336 1495 S ATOM 1339 N ALA A 168 15.315 42.997 27.346 1.00 75.42 N ANISOU 1339 N ALA A 168 10822 8958 8877 -293 -1114 1527 N ATOM 1340 CA ALA A 168 16.605 43.455 27.848 1.00 70.20 C ANISOU 1340 CA ALA A 168 10109 8277 8286 -176 -961 1524 C ATOM 1341 C ALA A 168 17.534 44.004 26.768 1.00 80.61 C ANISOU 1341 C ALA A 168 11512 9617 9499 -152 -890 1572 C ATOM 1342 O ALA A 168 18.447 44.773 27.095 1.00 71.40 O ANISOU 1342 O ALA A 168 10262 8445 8420 -57 -784 1592 O ATOM 1343 CB ALA A 168 17.312 42.313 28.586 1.00 64.66 C ANISOU 1343 CB ALA A 168 9488 7508 7572 -136 -862 1455 C ATOM 1344 N ALA A 169 17.336 43.640 25.500 1.00 80.63 N ANISOU 1344 N ALA A 169 10186 10378 10072 -1613 -1127 1769 N ATOM 1345 CA ALA A 169 18.243 44.085 24.444 1.00 75.26 C ANISOU 1345 CA ALA A 169 9515 9684 9396 -1841 -1034 1793 C ATOM 1346 C ALA A 169 17.939 45.480 23.883 1.00 76.04 C ANISOU 1346 C ALA A 169 9839 9566 9487 -1946 -1014 1877 C ATOM 1347 O ALA A 169 18.888 46.224 23.605 1.00 83.42 O ANISOU 1347 O ALA A 169 10793 10445 10458 -2154 -957 1842 O ATOM 1348 CB ALA A 169 18.268 43.067 23.302 1.00 57.20 C ANISOU 1348 CB ALA A 169 7146 7531 7055 -1850 -958 1864 C ATOM 1349 N PRO A 170 16.679 45.878 23.677 1.00 67.48 N ANISOU 1349 N PRO A 170 8930 8355 8355 -1816 -1054 1981 N ATOM 1350 CA PRO A 170 16.402 47.220 23.095 1.00 65.53 C ANISOU 1350 CA PRO A 170 8918 7893 8088 -1906 -1034 2066 C ATOM 1351 C PRO A 170 17.086 48.361 23.839 1.00 70.45 C ANISOU 1351 C PRO A 170 9601 8383 8782 -2038 -1051 1980 C ATOM 1352 O PRO A 170 17.630 49.267 23.188 1.00 70.67 O ANISOU 1352 O PRO A 170 9747 8289 8816 -2228 -977 2012 O ATOM 1353 CB PRO A 170 14.869 47.329 23.173 1.00 78.50 C ANISOU 1353 CB PRO A 170 10701 9451 9674 -1686 -1110 2149 C ATOM 1354 CG PRO A 170 14.406 45.911 23.038 1.00 67.64 C ANISOU 1354 CG PRO A 170 9171 8263 8267 -1542 -1113 2158 C ATOM 1355 CD PRO A 170 15.437 45.074 23.766 1.00 66.36 C ANISOU 1355 CD PRO A 170 8783 8266 8163 -1587 -1105 2034 C ATOM 1356 N PRO A 171 17.105 48.385 25.181 1.00 75.15 N ANISOU 1356 N PRO A 171 10128 8993 9433 -1952 -1140 1868 N ATOM 1357 CA PRO A 171 17.818 49.484 25.863 1.00 62.51 C ANISOU 1357 CA PRO A 171 8576 7271 7905 -2089 -1154 1772 C ATOM 1358 C PRO A 171 19.308 49.556 25.545 1.00 71.34 C ANISOU 1358 C PRO A 171 9573 8458 9077 -2339 -1061 1684 C ATOM 1359 O PRO A 171 19.951 50.547 25.918 1.00 94.49 O ANISOU 1359 O PRO A 171 12554 11277 12070 -2490 -1052 1606 O ATOM 1360 CB PRO A 171 17.587 49.196 27.353 1.00 71.28 C ANISOU 1360 CB PRO A 171 9592 8438 9053 -1922 -1268 1659 C ATOM 1361 CG PRO A 171 16.366 48.360 27.393 1.00 71.99 C ANISOU 1361 CG PRO A 171 9684 8588 9081 -1685 -1317 1736 C ATOM 1362 CD PRO A 171 16.444 47.506 26.169 1.00 73.54 C ANISOU 1362 CD PRO A 171 9819 8898 9226 -1725 -1229 1821 C ATOM 1363 N LEU A 172 19.878 48.548 24.883 1.00 74.07 N ANISOU 1363 N LEU A 172 9756 8985 9402 -2390 -993 1686 N ATOM 1364 CA LEU A 172 21.272 48.606 24.460 1.00 76.41 C ANISOU 1364 CA LEU A 172 9934 9357 9743 -2632 -896 1605 C ATOM 1365 C LEU A 172 21.442 49.225 23.081 1.00 76.69 C ANISOU 1365 C LEU A 172 10116 9279 9742 -2817 -773 1721 C ATOM 1366 O LEU A 172 22.551 49.657 22.748 1.00 76.08 O ANISOU 1366 O LEU A 172 9997 9200 9709 -3053 -682 1657 O ATOM 1367 CB LEU A 172 21.898 47.204 24.455 1.00 67.06 C ANISOU 1367 CB LEU A 172 8493 8433 8552 -2596 -882 1535 C ATOM 1368 CG LEU A 172 22.038 46.447 25.779 1.00 64.73 C ANISOU 1368 CG LEU A 172 8022 8284 8288 -2436 -982 1399 C ATOM 1369 CD1 LEU A 172 22.444 45.018 25.506 1.00 67.34 C ANISOU 1369 CD1 LEU A 172 8149 8850 8588 -2379 -956 1375 C ATOM 1370 CD2 LEU A 172 23.050 47.107 26.696 1.00 62.62 C ANISOU 1370 CD2 LEU A 172 7675 8012 8105 -2555 -1008 1225 C ATOM 1371 N VAL A 173 20.376 49.292 22.284 1.00 72.63 N ANISOU 1371 N VAL A 173 9776 8673 9146 -2714 -767 1885 N ATOM 1372 CA VAL A 173 20.461 49.797 20.920 1.00 81.89 C ANISOU 1372 CA VAL A 173 11101 9749 10265 -2849 -650 2002 C ATOM 1373 C VAL A 173 19.522 50.985 20.685 1.00 83.13 C ANISOU 1373 C VAL A 173 11542 9665 10379 -2763 -662 2084 C ATOM 1374 O VAL A 173 19.185 51.289 19.549 1.00 85.25 O ANISOU 1374 O VAL A 173 11937 9878 10576 -2713 -580 2149 O ATOM 1375 CB VAL A 173 20.218 48.674 19.890 1.00 80.24 C ANISOU 1375 CB VAL A 173 10799 9711 9979 -2736 -600 2055 C ATOM 1376 CG1 VAL A 173 21.469 47.811 19.762 1.00 75.77 C ANISOU 1376 CG1 VAL A 173 9984 9357 9449 -2863 -535 1952 C ATOM 1377 CG2 VAL A 173 19.001 47.818 20.271 1.00 62.71 C ANISOU 1377 CG2 VAL A 173 8557 7554 7715 -2497 -710 2125 C ATOM 1378 N GLY A 174 19.103 51.672 21.744 1.00 78.32 N ANISOU 1378 N GLY A 174 11033 8912 9812 -2736 -765 2072 N ATOM 1379 CA GLY A 174 18.470 52.965 21.603 1.00 73.73 C ANISOU 1379 CA GLY A 174 10715 8095 9204 -2687 -764 2116 C ATOM 1380 C GLY A 174 16.975 53.045 21.835 1.00 85.51 C ANISOU 1380 C GLY A 174 12341 9516 10632 -2417 -872 2190 C ATOM 1381 O GLY A 174 16.389 54.104 21.583 1.00 97.88 O ANISOU 1381 O GLY A 174 14123 10904 12164 -2352 -863 2222 O ATOM 1382 N TRP A 175 16.332 51.977 22.292 1.00 87.43 N ANISOU 1382 N TRP A 175 12458 9901 10859 -2248 -965 2206 N ATOM 1383 CA TRP A 175 14.938 52.031 22.721 1.00 74.66 C ANISOU 1383 CA TRP A 175 10931 8238 9197 -1982 -1070 2233 C ATOM 1384 C TRP A 175 14.942 51.906 24.240 1.00 75.92 C ANISOU 1384 C TRP A 175 10995 8421 9429 -1918 -1185 2136 C ATOM 1385 O TRP A 175 15.236 50.834 24.780 1.00 77.17 O ANISOU 1385 O TRP A 175 10930 8774 9619 -1864 -1206 2056 O ATOM 1386 CB TRP A 175 14.106 50.938 22.056 1.00 74.03 C ANISOU 1386 CB TRP A 175 10755 8327 9047 -1781 -1059 2259 C ATOM 1387 CG TRP A 175 12.627 51.170 22.158 1.00 80.02 C ANISOU 1387 CG TRP A 175 11611 9040 9755 -1513 -1118 2255 C ATOM 1388 CD1 TRP A 175 12.000 52.354 22.412 1.00 69.81 C ANISOU 1388 CD1 TRP A 175 10508 7569 8449 -1440 -1153 2253 C ATOM 1389 CD2 TRP A 175 11.589 50.186 22.024 1.00 85.80 C ANISOU 1389 CD2 TRP A 175 12236 9916 10448 -1288 -1135 2231 C ATOM 1390 NE1 TRP A 175 10.637 52.171 22.440 1.00 79.70 N ANISOU 1390 NE1 TRP A 175 11768 8858 9655 -1182 -1191 2229 N ATOM 1391 CE2 TRP A 175 10.359 50.850 22.202 1.00 77.20 C ANISOU 1391 CE2 TRP A 175 11271 8736 9326 -1092 -1174 2209 C ATOM 1392 CE3 TRP A 175 11.581 48.810 21.768 1.00 82.54 C ANISOU 1392 CE3 TRP A 175 11632 9700 10030 -1238 -1111 2215 C ATOM 1393 CZ2 TRP A 175 9.135 50.188 22.130 1.00 73.94 C ANISOU 1393 CZ2 TRP A 175 10787 8427 8879 -861 -1179 2162 C ATOM 1394 CZ3 TRP A 175 10.361 48.152 21.698 1.00 72.97 C ANISOU 1394 CZ3 TRP A 175 10365 8575 8787 -1008 -1118 2168 C ATOM 1395 CH2 TRP A 175 9.158 48.842 21.880 1.00 69.94 C ANISOU 1395 CH2 TRP A 175 10099 8102 8375 -828 -1147 2139 C ATOM 1396 N SER A 176 14.622 53.010 24.920 1.00 79.39 N ANISOU 1396 N SER A 176 11595 8676 9893 -1895 -1248 2114 N ATOM 1397 CA SER A 176 14.924 53.206 26.335 1.00 71.67 C ANISOU 1397 CA SER A 176 10530 7703 8997 -1869 -1329 1973 C ATOM 1398 C SER A 176 16.435 53.146 26.567 1.00 71.11 C ANISOU 1398 C SER A 176 10296 7712 9012 -2094 -1265 1850 C ATOM 1399 O SER A 176 17.223 53.305 25.624 1.00 75.29 O ANISOU 1399 O SER A 176 10834 8230 9541 -2298 -1151 1880 O ATOM 1400 CB SER A 176 14.190 52.186 27.206 1.00 61.58 C ANISOU 1400 CB SER A 176 9107 6581 7711 -1632 -1424 1931 C ATOM 1401 OG SER A 176 14.358 52.478 28.584 1.00 69.60 O ANISOU 1401 OG SER A 176 10070 7582 8792 -1583 -1510 1806 O ATOM 1402 N ARG A 177 16.854 52.936 27.813 1.00 58.57 N ANISOU 1402 N ARG A 177 8556 6206 7492 -2057 -1334 1704 N ATOM 1403 CA ARG A 177 18.278 52.937 28.122 1.00 67.45 C ANISOU 1403 CA ARG A 177 9518 7412 8699 -2257 -1286 1563 C ATOM 1404 C ARG A 177 18.485 52.389 29.527 1.00 69.36 C ANISOU 1404 C ARG A 177 9576 7791 8988 -2131 -1386 1412 C ATOM 1405 O ARG A 177 17.540 52.283 30.315 1.00 69.55 O ANISOU 1405 O ARG A 177 9637 7798 8990 -1916 -1487 1419 O ATOM 1406 CB ARG A 177 18.865 54.346 28.008 1.00 54.04 C ANISOU 1406 CB ARG A 177 7974 5504 7053 -2473 -1237 1532 C ATOM 1407 CG ARG A 177 18.249 55.294 29.004 1.00 61.51 C ANISOU 1407 CG ARG A 177 9065 6281 8025 -2372 -1342 1494 C ATOM 1408 CD ARG A 177 18.803 56.681 28.861 1.00 67.46 C ANISOU 1408 CD ARG A 177 9985 6814 8832 -2589 -1286 1466 C ATOM 1409 NE ARG A 177 18.298 57.554 29.910 1.00 65.36 N ANISOU 1409 NE ARG A 177 9838 6399 8599 -2491 -1394 1409 N ATOM 1410 CZ ARG A 177 18.829 58.734 30.192 1.00 64.66 C ANISOU 1410 CZ ARG A 177 9860 6131 8578 -2658 -1373 1334 C ATOM 1411 NH1 ARG A 177 19.875 59.157 29.498 1.00 60.56 N ANISOU 1411 NH1 ARG A 177 9344 5564 8102 -2935 -1241 1307 N ATOM 1412 NH2 ARG A 177 18.326 59.481 31.164 1.00 61.18 N ANISOU 1412 NH2 ARG A 177 9523 5561 8163 -2552 -1478 1280 N ATOM 1413 N TYR A 178 19.737 52.046 29.832 1.00 62.77 N ANISOU 1413 N TYR A 178 8541 7096 8213 -2263 -1355 1272 N ATOM 1414 CA TYR A 178 20.130 51.615 31.168 1.00 55.22 C ANISOU 1414 CA TYR A 178 7410 6271 7300 -2162 -1445 1109 C ATOM 1415 C TYR A 178 20.829 52.767 31.870 1.00 54.34 C ANISOU 1415 C TYR A 178 7329 6043 7273 -2302 -1468 972 C ATOM 1416 O TYR A 178 21.769 53.354 31.322 1.00 66.51 O ANISOU 1416 O TYR A 178 8869 7539 8865 -2550 -1378 926 O ATOM 1417 CB TYR A 178 21.054 50.387 31.125 1.00 58.50 C ANISOU 1417 CB TYR A 178 7568 6941 7718 -2183 -1410 1025 C ATOM 1418 CG TYR A 178 20.362 49.112 30.708 1.00 59.94 C ANISOU 1418 CG TYR A 178 7695 7257 7823 -2011 -1404 1130 C ATOM 1419 CD1 TYR A 178 19.480 48.466 31.566 1.00 56.22 C ANISOU 1419 CD1 TYR A 178 7206 6838 7317 -1756 -1494 1137 C ATOM 1420 CD2 TYR A 178 20.582 48.558 29.454 1.00 69.78 C ANISOU 1420 CD2 TYR A 178 8908 8573 9032 -2107 -1302 1221 C ATOM 1421 CE1 TYR A 178 18.836 47.309 31.186 1.00 63.09 C ANISOU 1421 CE1 TYR A 178 8027 7820 8122 -1610 -1479 1226 C ATOM 1422 CE2 TYR A 178 19.946 47.395 29.067 1.00 76.23 C ANISOU 1422 CE2 TYR A 178 9673 9509 9783 -1954 -1296 1309 C ATOM 1423 CZ TYR A 178 19.072 46.774 29.937 1.00 75.60 C ANISOU 1423 CZ TYR A 178 9576 9473 9674 -1710 -1383 1310 C ATOM 1424 OH TYR A 178 18.430 45.616 29.560 1.00 67.68 O ANISOU 1424 OH TYR A 178 8523 8580 8611 -1568 -1367 1390 O ATOM 1425 N ILE A 179 20.364 53.095 33.071 1.00 46.14 N ANISOU 1425 N ILE A 179 6320 4957 6253 -2148 -1584 902 N ATOM 1426 CA ILE A 179 21.027 54.084 33.923 1.00 60.02 C ANISOU 1426 CA ILE A 179 8079 6631 8096 -2252 -1624 744 C ATOM 1427 C ILE A 179 21.007 53.573 35.356 1.00 54.39 C ANISOU 1427 C ILE A 179 7225 6050 7392 -2051 -1747 608 C ATOM 1428 O ILE A 179 20.246 52.655 35.692 1.00 63.75 O ANISOU 1428 O ILE A 179 8372 7335 8514 -1822 -1800 665 O ATOM 1429 CB ILE A 179 20.349 55.474 33.840 1.00 76.51 C ANISOU 1429 CB ILE A 179 10437 8437 10194 -2291 -1638 815 C ATOM 1430 CG1 ILE A 179 18.909 55.408 34.350 1.00 71.36 C ANISOU 1430 CG1 ILE A 179 9913 7721 9480 -2016 -1743 910 C ATOM 1431 CG2 ILE A 179 20.373 56.031 32.406 1.00 61.04 C ANISOU 1431 CG2 ILE A 179 8646 6332 8215 -2484 -1511 956 C ATOM 1432 CD1 ILE A 179 18.222 56.750 34.401 1.00 66.17 C ANISOU 1432 CD1 ILE A 179 9515 6798 8827 -2021 -1775 965 C ATOM 1433 N PRO A 180 21.863 54.122 36.218 1.00 48.38 N ANISOU 1433 N PRO A 180 6379 5298 6707 -2132 -1789 422 N ATOM 1434 CA PRO A 180 21.741 53.822 37.653 1.00 57.21 C ANISOU 1434 CA PRO A 180 7402 6510 7826 -1922 -1917 295 C ATOM 1435 C PRO A 180 20.389 54.271 38.194 1.00 63.54 C ANISOU 1435 C PRO A 180 8394 7159 8591 -1720 -2005 388 C ATOM 1436 O PRO A 180 19.917 55.372 37.897 1.00 78.37 O ANISOU 1436 O PRO A 180 10475 8815 10485 -1793 -1998 455 O ATOM 1437 CB PRO A 180 22.889 54.622 38.289 1.00 49.84 C ANISOU 1437 CB PRO A 180 6380 5569 6989 -2089 -1934 82 C ATOM 1438 CG PRO A 180 23.853 54.869 37.197 1.00 51.28 C ANISOU 1438 CG PRO A 180 6522 5746 7215 -2380 -1802 71 C ATOM 1439 CD PRO A 180 23.090 54.878 35.906 1.00 50.64 C ANISOU 1439 CD PRO A 180 6618 5546 7078 -2421 -1712 300 C ATOM 1440 N GLU A 181 19.770 53.413 39.001 1.00 63.10 N ANISOU 1440 N GLU A 181 8275 7220 8480 -1463 -2084 389 N ATOM 1441 CA GLU A 181 18.496 53.717 39.642 1.00 56.58 C ANISOU 1441 CA GLU A 181 7599 6282 7615 -1251 -2172 458 C ATOM 1442 C GLU A 181 18.702 53.973 41.134 1.00 60.45 C ANISOU 1442 C GLU A 181 8029 6806 8134 -1128 -2288 290 C ATOM 1443 O GLU A 181 19.780 53.743 41.690 1.00 56.44 O ANISOU 1443 O GLU A 181 7347 6433 7665 -1176 -2305 123 O ATOM 1444 CB GLU A 181 17.480 52.588 39.420 1.00 65.11 C ANISOU 1444 CB GLU A 181 8677 7453 8607 -1045 -2166 595 C ATOM 1445 CG GLU A 181 17.723 51.341 40.271 1.00 85.24 C ANISOU 1445 CG GLU A 181 11039 10226 11124 -870 -2203 513 C ATOM 1446 CD GLU A 181 16.787 50.187 39.925 1.00105.88 C ANISOU 1446 CD GLU A 181 13648 12923 13656 -701 -2173 648 C ATOM 1447 OE1 GLU A 181 15.661 50.436 39.429 1.00 88.57 O ANISOU 1447 OE1 GLU A 181 11609 10613 11431 -645 -2165 787 O ATOM 1448 OE2 GLU A 181 17.188 49.021 40.149 1.00119.57 O ANISOU 1448 OE2 GLU A 181 15226 14845 15361 -622 -2156 609 O ATOM 1449 N GLY A 182 17.652 54.490 41.768 1.00 61.31 N ANISOU 1449 N GLY A 182 8284 6791 8221 -965 -2369 330 N ATOM 1450 CA GLY A 182 17.618 54.728 43.199 1.00 44.70 C ANISOU 1450 CA GLY A 182 6148 4707 6129 -811 -2485 193 C ATOM 1451 C GLY A 182 18.869 55.320 43.817 1.00 55.05 C ANISOU 1451 C GLY A 182 7351 6044 7522 -948 -2517 -15 C ATOM 1452 O GLY A 182 19.233 56.467 43.538 1.00 59.68 O ANISOU 1452 O GLY A 182 8028 6469 8177 -1140 -2499 -54 O ATOM 1453 N MET A 183 19.532 54.543 44.672 1.00 52.40 N ANISOU 1453 N MET A 183 6822 5911 7176 -845 -2563 -156 N ATOM 1454 CA MET A 183 20.729 55.007 45.356 1.00 49.98 C ANISOU 1454 CA MET A 183 6385 5663 6941 -946 -2605 -379 C ATOM 1455 C MET A 183 21.953 54.980 44.459 1.00 53.44 C ANISOU 1455 C MET A 183 6700 6166 7437 -1216 -2505 -442 C ATOM 1456 O MET A 183 23.065 55.233 44.952 1.00 50.67 O ANISOU 1456 O MET A 183 6204 5901 7147 -1314 -2530 -646 O ATOM 1457 CB MET A 183 20.978 54.182 46.618 1.00 67.33 C ANISOU 1457 CB MET A 183 8427 8062 9094 -714 -2697 -514 C ATOM 1458 CG MET A 183 19.936 54.387 47.708 1.00 73.30 C ANISOU 1458 CG MET A 183 9293 8753 9805 -462 -2804 -498 C ATOM 1459 SD MET A 183 19.984 53.066 48.935 1.00 72.68 S ANISOU 1459 SD MET A 183 9063 8918 9634 -154 -2876 -581 S ATOM 1460 CE MET A 183 21.251 53.642 50.078 1.00 52.31 C ANISOU 1460 CE MET A 183 6334 6428 7114 -177 -2977 -874 C ATOM 1461 N GLN A 184 21.762 54.694 43.162 1.00 48.60 N ANISOU 1461 N GLN A 184 6141 5521 6805 -1335 -2394 -279 N ATOM 1462 CA GLN A 184 22.764 54.874 42.114 1.00 65.80 C ANISOU 1462 CA GLN A 184 8253 7708 9038 -1620 -2279 -303 C ATOM 1463 C GLN A 184 23.828 53.783 42.135 1.00 67.32 C ANISOU 1463 C GLN A 184 8193 8166 9221 -1630 -2255 -419 C ATOM 1464 O GLN A 184 24.892 53.936 41.530 1.00 71.70 O ANISOU 1464 O GLN A 184 8642 8770 9831 -1863 -2176 -504 O ATOM 1465 CB GLN A 184 23.418 56.269 42.199 1.00 70.19 C ANISOU 1465 CB GLN A 184 8865 8106 9698 -1851 -2271 -429 C ATOM 1466 CG GLN A 184 22.417 57.446 42.121 1.00 52.74 C ANISOU 1466 CG GLN A 184 6927 5614 7498 -1854 -2290 -317 C ATOM 1467 CD GLN A 184 21.646 57.459 40.798 1.00 63.75 C ANISOU 1467 CD GLN A 184 8500 6879 8844 -1911 -2194 -78 C ATOM 1468 OE1 GLN A 184 22.185 57.850 39.761 1.00 58.97 O ANISOU 1468 OE1 GLN A 184 7932 6199 8273 -2156 -2078 -41 O ATOM 1469 NE2 GLN A 184 20.391 57.005 40.825 1.00 50.17 N ANISOU 1469 NE2 GLN A 184 6884 5139 7040 -1683 -2237 78 N ATOM 1470 N CYS A 185 23.555 52.666 42.804 1.00 73.31 N ANISOU 1470 N CYS A 185 8855 9096 9904 -1378 -2316 -424 N ATOM 1471 CA CYS A 185 24.499 51.566 42.900 1.00 62.10 C ANISOU 1471 CA CYS A 185 7206 7930 8459 -1347 -2305 -532 C ATOM 1472 C CYS A 185 24.161 50.391 41.992 1.00 67.07 C ANISOU 1472 C CYS A 185 7814 8654 9016 -1298 -2224 -368 C ATOM 1473 O CYS A 185 25.016 49.522 41.800 1.00 71.06 O ANISOU 1473 O CYS A 185 8139 9356 9504 -1316 -2192 -443 O ATOM 1474 CB CYS A 185 24.586 51.085 44.345 1.00 50.89 C ANISOU 1474 CB CYS A 185 5687 6650 7000 -1092 -2428 -675 C ATOM 1475 SG CYS A 185 25.384 52.275 45.404 1.00 71.46 S ANISOU 1475 SG CYS A 185 8238 9218 9695 -1168 -2522 -931 S ATOM 1476 N SER A 186 22.946 50.326 41.447 1.00 52.62 N ANISOU 1476 N SER A 186 6156 6695 7141 -1229 -2194 -158 N ATOM 1477 CA SER A 186 22.593 49.297 40.480 1.00 61.28 C ANISOU 1477 CA SER A 186 7241 7866 8176 -1204 -2111 -3 C ATOM 1478 C SER A 186 21.904 49.951 39.294 1.00 59.00 C ANISOU 1478 C SER A 186 7135 7384 7896 -1346 -2033 177 C ATOM 1479 O SER A 186 21.313 51.026 39.419 1.00 67.47 O ANISOU 1479 O SER A 186 8378 8260 8996 -1372 -2063 216 O ATOM 1480 CB SER A 186 21.695 48.185 41.095 1.00 57.65 C ANISOU 1480 CB SER A 186 6783 7493 7626 -909 -2156 70 C ATOM 1481 OG SER A 186 20.681 48.694 41.941 1.00 76.59 O ANISOU 1481 OG SER A 186 9322 9767 10012 -745 -2238 100 O ATOM 1482 N CYS A 187 21.997 49.299 38.138 1.00 58.14 N ANISOU 1482 N CYS A 187 6995 7336 7759 -1432 -1934 284 N ATOM 1483 CA CYS A 187 21.488 49.845 36.888 1.00 53.32 C ANISOU 1483 CA CYS A 187 6546 6567 7148 -1575 -1850 449 C ATOM 1484 C CYS A 187 20.273 49.058 36.425 1.00 61.07 C ANISOU 1484 C CYS A 187 7606 7548 8048 -1404 -1835 629 C ATOM 1485 O CYS A 187 20.213 47.834 36.575 1.00 72.41 O ANISOU 1485 O CYS A 187 8926 9152 9436 -1264 -1835 635 O ATOM 1486 CB CYS A 187 22.562 49.837 35.791 1.00 44.12 C ANISOU 1486 CB CYS A 187 5292 5456 6014 -1833 -1736 432 C ATOM 1487 SG CYS A 187 23.887 51.076 36.024 1.00 69.35 S ANISOU 1487 SG CYS A 187 8440 8591 9320 -2106 -1719 238 S ATOM 1488 N GLY A 188 19.303 49.776 35.867 1.00 51.77 N ANISOU 1488 N GLY A 188 6632 6182 6856 -1414 -1823 769 N ATOM 1489 CA GLY A 188 18.126 49.168 35.295 1.00 39.24 C ANISOU 1489 CA GLY A 188 5127 4584 5197 -1276 -1804 934 C ATOM 1490 C GLY A 188 17.540 50.031 34.197 1.00 56.86 C ANISOU 1490 C GLY A 188 7558 6629 7417 -1384 -1753 1076 C ATOM 1491 O GLY A 188 18.079 51.081 33.834 1.00 55.41 O ANISOU 1491 O GLY A 188 7457 6315 7280 -1577 -1720 1057 O ATOM 1492 N ILE A 189 16.413 49.554 33.667 1.00 59.70 N ANISOU 1492 N ILE A 189 7996 6977 7711 -1251 -1744 1216 N ATOM 1493 CA ILE A 189 15.667 50.282 32.653 1.00 59.88 C ANISOU 1493 CA ILE A 189 8218 6831 7701 -1300 -1709 1359 C ATOM 1494 C ILE A 189 15.242 51.631 33.201 1.00 67.25 C ANISOU 1494 C ILE A 189 9335 7557 8660 -1291 -1778 1344 C ATOM 1495 O ILE A 189 14.830 51.751 34.362 1.00 74.24 O ANISOU 1495 O ILE A 189 10219 8432 9556 -1141 -1872 1275 O ATOM 1496 CB ILE A 189 14.446 49.455 32.211 1.00 71.06 C ANISOU 1496 CB ILE A 189 9661 8296 9040 -1118 -1708 1481 C ATOM 1497 CG1 ILE A 189 14.891 48.178 31.481 1.00 68.12 C ANISOU 1497 CG1 ILE A 189 9127 8112 8644 -1150 -1627 1506 C ATOM 1498 CG2 ILE A 189 13.478 50.294 31.377 1.00 56.17 C ANISOU 1498 CG2 ILE A 189 8000 6232 7111 -1110 -1703 1613 C ATOM 1499 CD1 ILE A 189 13.821 47.110 31.426 1.00 70.27 C ANISOU 1499 CD1 ILE A 189 9367 8476 8856 -949 -1634 1575 C ATOM 1500 N ASP A 190 15.364 52.661 32.363 1.00 69.95 N ANISOU 1500 N ASP A 190 9842 7728 9009 -1454 -1727 1408 N ATOM 1501 CA ASP A 190 14.897 54.012 32.668 1.00 70.32 C ANISOU 1501 CA ASP A 190 10101 7548 9070 -1455 -1779 1417 C ATOM 1502 C ASP A 190 13.402 54.051 32.374 1.00 77.26 C ANISOU 1502 C ASP A 190 11137 8350 9869 -1257 -1823 1548 C ATOM 1503 O ASP A 190 12.968 54.255 31.238 1.00 69.92 O ANISOU 1503 O ASP A 190 10338 7343 8884 -1289 -1769 1676 O ATOM 1504 CB ASP A 190 15.668 55.042 31.851 1.00 69.70 C ANISOU 1504 CB ASP A 190 10143 7315 9024 -1712 -1692 1434 C ATOM 1505 CG ASP A 190 15.216 56.465 32.118 1.00 70.21 C ANISOU 1505 CG ASP A 190 10447 7128 9103 -1721 -1739 1447 C ATOM 1506 OD1 ASP A 190 14.381 56.664 33.022 1.00 73.43 O ANISOU 1506 OD1 ASP A 190 10906 7495 9500 -1528 -1848 1425 O ATOM 1507 OD2 ASP A 190 15.712 57.392 31.438 1.00 70.55 O ANISOU 1507 OD2 ASP A 190 10630 7010 9165 -1922 -1662 1475 O ATOM 1508 N TYR A 191 12.600 53.828 33.412 1.00 82.63 N ANISOU 1508 N TYR A 191 11798 9061 10538 -1042 -1923 1510 N ATOM 1509 CA TYR A 191 11.150 53.832 33.290 1.00 82.92 C ANISOU 1509 CA TYR A 191 11959 9044 10502 -839 -1974 1607 C ATOM 1510 C TYR A 191 10.533 55.056 33.953 1.00 82.87 C ANISOU 1510 C TYR A 191 12139 8846 10502 -763 -2065 1589 C ATOM 1511 O TYR A 191 9.325 55.078 34.202 1.00 94.09 O ANISOU 1511 O TYR A 191 13640 10238 11872 -564 -2132 1631 O ATOM 1512 CB TYR A 191 10.557 52.547 33.880 1.00 62.54 C ANISOU 1512 CB TYR A 191 9218 6651 7894 -640 -2005 1587 C ATOM 1513 CG TYR A 191 10.714 52.429 35.379 1.00 63.11 C ANISOU 1513 CG TYR A 191 9195 6778 8006 -536 -2085 1458 C ATOM 1514 CD1 TYR A 191 9.742 52.922 36.247 1.00 72.61 C ANISOU 1514 CD1 TYR A 191 10496 7899 9194 -359 -2181 1441 C ATOM 1515 CD2 TYR A 191 11.833 51.825 35.930 1.00 63.84 C ANISOU 1515 CD2 TYR A 191 9102 7010 8146 -605 -2068 1348 C ATOM 1516 CE1 TYR A 191 9.890 52.819 37.627 1.00 75.58 C ANISOU 1516 CE1 TYR A 191 10790 8326 9600 -257 -2254 1323 C ATOM 1517 CE2 TYR A 191 11.988 51.716 37.303 1.00 69.74 C ANISOU 1517 CE2 TYR A 191 9767 7810 8919 -496 -2144 1228 C ATOM 1518 CZ TYR A 191 11.016 52.214 38.145 1.00 73.93 C ANISOU 1518 CZ TYR A 191 10402 8255 9434 -324 -2235 1219 C ATOM 1519 OH TYR A 191 11.177 52.100 39.508 1.00 85.74 O ANISOU 1519 OH TYR A 191 11822 9807 10950 -209 -2309 1100 O ATOM 1520 N TYR A 192 11.339 56.082 34.235 1.00 70.64 N ANISOU 1520 N TYR A 192 10659 7164 9015 -920 -2067 1519 N ATOM 1521 CA TYR A 192 10.873 57.201 35.049 1.00 67.91 C ANISOU 1521 CA TYR A 192 10470 6647 8687 -846 -2161 1476 C ATOM 1522 C TYR A 192 11.295 58.578 34.555 1.00 75.64 C ANISOU 1522 C TYR A 192 11655 7391 9692 -1028 -2128 1496 C ATOM 1523 O TYR A 192 10.703 59.566 35.004 1.00 99.46 O ANISOU 1523 O TYR A 192 14848 10237 12704 -951 -2202 1491 O ATOM 1524 CB TYR A 192 11.341 57.025 36.501 1.00 83.21 C ANISOU 1524 CB TYR A 192 12257 8671 10686 -792 -2235 1317 C ATOM 1525 CG TYR A 192 12.793 56.610 36.639 1.00 91.08 C ANISOU 1525 CG TYR A 192 13062 9792 11754 -975 -2178 1207 C ATOM 1526 CD1 TYR A 192 13.163 55.270 36.570 1.00 87.01 C ANISOU 1526 CD1 TYR A 192 12333 9501 11225 -949 -2137 1193 C ATOM 1527 CD2 TYR A 192 13.794 57.559 36.835 1.00 78.93 C ANISOU 1527 CD2 TYR A 192 11552 8144 10292 -1173 -2164 1109 C ATOM 1528 CE1 TYR A 192 14.484 54.886 36.696 1.00 86.13 C ANISOU 1528 CE1 TYR A 192 12042 9512 11170 -1101 -2092 1083 C ATOM 1529 CE2 TYR A 192 15.118 57.181 36.959 1.00 88.60 C ANISOU 1529 CE2 TYR A 192 12587 9496 11580 -1337 -2114 992 C ATOM 1530 CZ TYR A 192 15.457 55.844 36.889 1.00 91.81 C ANISOU 1530 CZ TYR A 192 12782 10134 11966 -1294 -2082 979 C ATOM 1531 OH TYR A 192 16.773 55.463 37.015 1.00105.12 O ANISOU 1531 OH TYR A 192 14276 11956 13709 -1444 -2039 854 O ATOM 1532 N THR A 193 12.298 58.706 33.670 1.00 71.80 N ANISOU 1532 N THR A 193 11163 6884 9234 -1268 -2015 1513 N ATOM 1533 CA THR A 193 12.516 60.016 33.067 1.00 74.17 C ANISOU 1533 CA THR A 193 11700 6939 9543 -1428 -1968 1559 C ATOM 1534 C THR A 193 12.061 59.982 31.609 1.00 79.24 C ANISOU 1534 C THR A 193 12485 7524 10096 -1449 -1885 1729 C ATOM 1535 O THR A 193 12.183 58.945 30.946 1.00 80.10 O ANISOU 1535 O THR A 193 12458 7804 10174 -1456 -1825 1778 O ATOM 1536 CB THR A 193 13.989 60.483 33.141 1.00 73.88 C ANISOU 1536 CB THR A 193 11598 6868 9605 -1709 -1890 1446 C ATOM 1537 OG1 THR A 193 14.772 59.897 32.089 1.00 63.97 O ANISOU 1537 OG1 THR A 193 10249 5711 8346 -1887 -1762 1490 O ATOM 1538 CG2 THR A 193 14.611 60.128 34.482 1.00 67.96 C ANISOU 1538 CG2 THR A 193 10629 6257 8935 -1686 -1962 1263 C ATOM 1539 N PRO A 194 11.486 61.097 31.088 1.00 91.00 N ANISOU 1539 N PRO A 194 14261 8777 11536 -1441 -1886 1821 N ATOM 1540 CA PRO A 194 10.944 61.108 29.717 1.00 88.41 C ANISOU 1540 CA PRO A 194 14003 8486 11104 -1385 -1773 1917 C ATOM 1541 C PRO A 194 12.013 61.385 28.664 1.00 90.41 C ANISOU 1541 C PRO A 194 14300 8680 11372 -1649 -1623 1958 C ATOM 1542 O PRO A 194 11.966 62.377 27.934 1.00106.79 O ANISOU 1542 O PRO A 194 16549 10619 13407 -1689 -1533 1989 O ATOM 1543 CB PRO A 194 9.901 62.227 29.798 1.00 89.67 C ANISOU 1543 CB PRO A 194 14346 8522 11205 -1207 -1800 1906 C ATOM 1544 CG PRO A 194 10.528 63.205 30.752 1.00 75.28 C ANISOU 1544 CG PRO A 194 12631 6502 9471 -1337 -1860 1834 C ATOM 1545 CD PRO A 194 11.248 62.376 31.784 1.00 87.69 C ANISOU 1545 CD PRO A 194 14031 8143 11145 -1419 -1953 1771 C ATOM 1546 N HIS A 195 12.998 60.495 28.583 1.00 86.77 N ANISOU 1546 N HIS A 195 13669 8331 10967 -1828 -1588 1952 N ATOM 1547 CA HIS A 195 14.142 60.670 27.689 1.00 75.69 C ANISOU 1547 CA HIS A 195 12260 6908 9591 -2098 -1435 1960 C ATOM 1548 C HIS A 195 13.687 60.385 26.263 1.00 76.62 C ANISOU 1548 C HIS A 195 12406 7108 9599 -2015 -1323 2060 C ATOM 1549 O HIS A 195 13.531 59.230 25.862 1.00 98.71 O ANISOU 1549 O HIS A 195 15049 10096 12361 -1948 -1316 2097 O ATOM 1550 CB HIS A 195 15.291 59.759 28.110 1.00 81.87 C ANISOU 1550 CB HIS A 195 12758 7885 10462 -2250 -1411 1850 C ATOM 1551 CG HIS A 195 16.620 60.166 27.553 1.00 88.55 C ANISOU 1551 CG HIS A 195 13590 8686 11369 -2562 -1270 1808 C ATOM 1552 ND1 HIS A 195 17.287 59.425 26.600 1.00 81.80 N ANISOU 1552 ND1 HIS A 195 12613 7970 10497 -2696 -1155 1846 N ATOM 1553 CD2 HIS A 195 17.404 61.241 27.813 1.00 80.57 C ANISOU 1553 CD2 HIS A 195 12670 7506 10438 -2773 -1221 1724 C ATOM 1554 CE1 HIS A 195 18.424 60.026 26.296 1.00 70.15 C ANISOU 1554 CE1 HIS A 195 11150 6417 9086 -2976 -1038 1787 C ATOM 1555 NE2 HIS A 195 18.519 61.130 27.018 1.00 86.13 N ANISOU 1555 NE2 HIS A 195 13302 8252 11172 -3033 -1072 1711 N ATOM 1556 N GLU A 196 13.477 61.446 25.485 1.00 84.25 N ANISOU 1556 N GLU A 196 13569 7927 10514 -2015 -1233 2099 N ATOM 1557 CA GLU A 196 12.850 61.318 24.175 1.00 85.58 C ANISOU 1557 CA GLU A 196 13790 8149 10576 -1893 -1147 2189 C ATOM 1558 C GLU A 196 13.806 60.844 23.085 1.00 90.97 C ANISOU 1558 C GLU A 196 14393 8914 11256 -2080 -1000 2225 C ATOM 1559 O GLU A 196 13.343 60.297 22.078 1.00101.83 O ANISOU 1559 O GLU A 196 15741 10397 12553 -1971 -950 2291 O ATOM 1560 CB GLU A 196 12.215 62.655 23.784 1.00 96.64 C ANISOU 1560 CB GLU A 196 15438 9359 11922 -1805 -1118 2221 C ATOM 1561 CG GLU A 196 10.964 62.969 24.588 1.00106.10 C ANISOU 1561 CG GLU A 196 16694 10529 13088 -1551 -1256 2194 C ATOM 1562 CD GLU A 196 10.734 64.451 24.768 1.00130.93 C ANISOU 1562 CD GLU A 196 20072 13448 16227 -1543 -1256 2185 C ATOM 1563 OE1 GLU A 196 11.286 65.247 23.976 1.00140.72 O ANISOU 1563 OE1 GLU A 196 21453 14554 17459 -1684 -1133 2226 O ATOM 1564 OE2 GLU A 196 10.002 64.818 25.713 1.00133.16 O ANISOU 1564 OE2 GLU A 196 20393 13688 16514 -1393 -1374 2135 O ATOM 1565 N GLU A 197 15.118 61.032 23.258 1.00 97.04 N ANISOU 1565 N GLU A 197 15111 9646 12114 -2355 -927 2169 N ATOM 1566 CA GLU A 197 16.072 60.541 22.266 1.00 97.29 C ANISOU 1566 CA GLU A 197 15039 9779 12148 -2532 -783 2185 C ATOM 1567 C GLU A 197 16.079 59.014 22.190 1.00 95.03 C ANISOU 1567 C GLU A 197 14518 9741 11848 -2480 -819 2194 C ATOM 1568 O GLU A 197 16.432 58.448 21.149 1.00 88.47 O ANISOU 1568 O GLU A 197 13613 9024 10979 -2526 -715 2234 O ATOM 1569 CB GLU A 197 17.472 61.071 22.585 1.00103.92 C ANISOU 1569 CB GLU A 197 15838 10550 13097 -2833 -696 2088 C ATOM 1570 CG GLU A 197 18.119 61.889 21.471 1.00123.04 C ANISOU 1570 CG GLU A 197 18378 12865 15507 -2985 -513 2116 C ATOM 1571 CD GLU A 197 17.613 63.322 21.408 1.00144.78 C ANISOU 1571 CD GLU A 197 21404 15370 18238 -2933 -496 2149 C ATOM 1572 OE1 GLU A 197 16.601 63.635 22.072 1.00153.81 O ANISOU 1572 OE1 GLU A 197 22649 16439 19351 -2742 -626 2162 O ATOM 1573 OE2 GLU A 197 18.235 64.141 20.695 1.00144.31 O ANISOU 1573 OE2 GLU A 197 21451 15191 18189 -3082 -350 2160 O ATOM 1574 N THR A 198 15.692 58.332 23.270 1.00 80.55 N ANISOU 1574 N THR A 198 12567 7993 10045 -2379 -964 2159 N ATOM 1575 CA THR A 198 15.566 56.879 23.275 1.00 85.76 C ANISOU 1575 CA THR A 198 13013 8883 10690 -2300 -1007 2173 C ATOM 1576 C THR A 198 14.116 56.418 23.389 1.00 89.88 C ANISOU 1576 C THR A 198 13547 9465 11136 -1992 -1107 2216 C ATOM 1577 O THR A 198 13.872 55.218 23.571 1.00 75.35 O ANISOU 1577 O THR A 198 11532 7808 9288 -1897 -1154 2217 O ATOM 1578 CB THR A 198 16.405 56.264 24.404 1.00 79.74 C ANISOU 1578 CB THR A 198 12057 8208 10032 -2441 -1079 2089 C ATOM 1579 OG1 THR A 198 16.103 56.906 25.651 1.00 85.92 O ANISOU 1579 OG1 THR A 198 12886 8890 10869 -2359 -1190 2003 O ATOM 1580 CG2 THR A 198 17.886 56.420 24.109 1.00 72.26 C ANISOU 1580 CG2 THR A 198 11013 7285 9156 -2739 -956 2013 C ATOM 1581 N ASN A 199 13.154 57.344 23.290 1.00 82.35 N ANISOU 1581 N ASN A 199 12784 8373 10131 -1833 -1129 2236 N ATOM 1582 CA ASN A 199 11.720 57.039 23.260 1.00 69.65 C ANISOU 1582 CA ASN A 199 11181 6832 8452 -1539 -1196 2249 C ATOM 1583 C ASN A 199 11.292 56.219 24.477 1.00 69.20 C ANISOU 1583 C ASN A 199 10973 6888 8432 -1412 -1326 2194 C ATOM 1584 O ASN A 199 10.695 55.146 24.360 1.00 67.24 O ANISOU 1584 O ASN A 199 10578 6816 8154 -1263 -1340 2188 O ATOM 1585 CB ASN A 199 11.340 56.325 21.959 1.00 68.96 C ANISOU 1585 CB ASN A 199 11034 6879 8288 -1453 -1109 2300 C ATOM 1586 CG ASN A 199 11.467 57.224 20.745 1.00 81.50 C ANISOU 1586 CG ASN A 199 12797 8346 9822 -1508 -992 2362 C ATOM 1587 OD1 ASN A 199 12.176 56.902 19.790 1.00 85.11 O ANISOU 1587 OD1 ASN A 199 13215 8855 10265 -1635 -884 2399 O ATOM 1588 ND2 ASN A 199 10.783 58.363 20.777 1.00 90.60 N ANISOU 1588 ND2 ASN A 199 14142 9339 10944 -1409 -1011 2373 N ATOM 1589 N ASN A 200 11.591 56.759 25.660 1.00 72.11 N ANISOU 1589 N ASN A 200 11382 7146 8869 -1468 -1417 2146 N ATOM 1590 CA ASN A 200 11.316 56.026 26.893 1.00 67.22 C ANISOU 1590 CA ASN A 200 10626 6623 8292 -1357 -1542 2095 C ATOM 1591 C ASN A 200 9.830 55.740 27.062 1.00 64.32 C ANISOU 1591 C ASN A 200 10231 6343 7864 -1055 -1585 2064 C ATOM 1592 O ASN A 200 9.454 54.660 27.531 1.00 78.08 O ANISOU 1592 O ASN A 200 11801 8255 9610 -932 -1622 2028 O ATOM 1593 CB ASN A 200 11.849 56.800 28.097 1.00 68.06 C ANISOU 1593 CB ASN A 200 10804 6572 8485 -1458 -1634 2041 C ATOM 1594 CG ASN A 200 13.350 56.701 28.226 1.00 81.59 C ANISOU 1594 CG ASN A 200 12365 8348 10288 -1703 -1554 1941 C ATOM 1595 OD1 ASN A 200 14.038 56.291 27.291 1.00 76.69 O ANISOU 1595 OD1 ASN A 200 11681 7798 9658 -1855 -1446 1980 O ATOM 1596 ND2 ASN A 200 13.869 57.072 29.391 1.00 88.94 N ANISOU 1596 ND2 ASN A 200 13227 9262 11303 -1739 -1609 1803 N ATOM 1597 N GLU A 201 8.968 56.686 26.677 1.00 73.21 N ANISOU 1597 N GLU A 201 11515 7365 8936 -939 -1566 2066 N ATOM 1598 CA GLU A 201 7.545 56.555 26.984 1.00 82.21 C ANISOU 1598 CA GLU A 201 12620 8582 10034 -672 -1602 2014 C ATOM 1599 C GLU A 201 6.937 55.334 26.301 1.00 84.88 C ANISOU 1599 C GLU A 201 12792 9128 10331 -552 -1538 2013 C ATOM 1600 O GLU A 201 6.224 54.547 26.934 1.00 82.28 O ANISOU 1600 O GLU A 201 12318 8936 10010 -398 -1564 1946 O ATOM 1601 CB GLU A 201 6.796 57.821 26.581 1.00 89.73 C ANISOU 1601 CB GLU A 201 13769 9389 10934 -587 -1588 2026 C ATOM 1602 CG GLU A 201 5.288 57.662 26.652 1.00103.10 C ANISOU 1602 CG GLU A 201 15410 11185 12580 -330 -1599 1977 C ATOM 1603 CD GLU A 201 4.546 58.861 26.115 1.00110.20 C ANISOU 1603 CD GLU A 201 16493 11958 13421 -246 -1587 2001 C ATOM 1604 OE1 GLU A 201 4.932 59.999 26.457 1.00120.71 O ANISOU 1604 OE1 GLU A 201 17998 13101 14766 -325 -1621 2007 O ATOM 1605 OE2 GLU A 201 3.584 58.663 25.342 1.00109.83 O ANISOU 1605 OE2 GLU A 201 16416 12000 13315 -103 -1543 2012 O ATOM 1606 N SER A 202 7.213 55.154 25.007 1.00 79.41 N ANISOU 1606 N SER A 202 12117 8459 9596 -623 -1444 2080 N ATOM 1607 CA SER A 202 6.646 54.014 24.296 1.00 67.18 C ANISOU 1607 CA SER A 202 10419 7096 8010 -512 -1383 2076 C ATOM 1608 C SER A 202 7.226 52.690 24.787 1.00 80.67 C ANISOU 1608 C SER A 202 11924 8961 9765 -563 -1394 2047 C ATOM 1609 O SER A 202 6.524 51.671 24.785 1.00 77.08 O ANISOU 1609 O SER A 202 11323 8665 9298 -423 -1370 1999 O ATOM 1610 CB SER A 202 6.857 54.173 22.788 1.00 60.06 C ANISOU 1610 CB SER A 202 9593 6178 7051 -574 -1284 2154 C ATOM 1611 OG SER A 202 8.213 53.986 22.423 1.00 73.88 O ANISOU 1611 OG SER A 202 11329 7913 8828 -806 -1240 2203 O ATOM 1612 N PHE A 203 8.489 52.675 25.226 1.00 79.77 N ANISOU 1612 N PHE A 203 11793 8808 9706 -764 -1425 2071 N ATOM 1613 CA PHE A 203 9.054 51.434 25.749 1.00 75.73 C ANISOU 1613 CA PHE A 203 11085 8453 9238 -803 -1445 2050 C ATOM 1614 C PHE A 203 8.415 51.048 27.078 1.00 68.82 C ANISOU 1614 C PHE A 203 10119 7637 8393 -639 -1524 1963 C ATOM 1615 O PHE A 203 8.209 49.859 27.349 1.00 66.05 O ANISOU 1615 O PHE A 203 9597 7450 8049 -553 -1506 1918 O ATOM 1616 CB PHE A 203 10.569 51.552 25.906 1.00 68.29 C ANISOU 1616 CB PHE A 203 10137 7463 8349 -1067 -1458 2099 C ATOM 1617 CG PHE A 203 11.230 50.273 26.365 1.00 72.66 C ANISOU 1617 CG PHE A 203 10481 8190 8938 -1113 -1478 2093 C ATOM 1618 CD1 PHE A 203 11.632 49.317 25.446 1.00 68.39 C ANISOU 1618 CD1 PHE A 203 9815 7796 8374 -1174 -1392 2123 C ATOM 1619 CD2 PHE A 203 11.448 50.028 27.714 1.00 72.69 C ANISOU 1619 CD2 PHE A 203 10386 8235 8998 -1065 -1560 2010 C ATOM 1620 CE1 PHE A 203 12.241 48.144 25.861 1.00 69.94 C ANISOU 1620 CE1 PHE A 203 9804 8169 8600 -1195 -1392 2088 C ATOM 1621 CE2 PHE A 203 12.063 48.860 28.137 1.00 67.36 C ANISOU 1621 CE2 PHE A 203 9485 7755 8355 -1064 -1539 1934 C ATOM 1622 CZ PHE A 203 12.456 47.915 27.210 1.00 69.66 C ANISOU 1622 CZ PHE A 203 9660 8185 8621 -1128 -1455 1973 C ATOM 1623 N VAL A 204 8.115 52.031 27.929 1.00 62.76 N ANISOU 1623 N VAL A 204 9466 6736 7642 -592 -1600 1930 N ATOM 1624 CA VAL A 204 7.471 51.724 29.202 1.00 69.36 C ANISOU 1624 CA VAL A 204 10219 7631 8503 -428 -1660 1837 C ATOM 1625 C VAL A 204 6.066 51.179 28.967 1.00 80.83 C ANISOU 1625 C VAL A 204 11597 9204 9911 -213 -1585 1777 C ATOM 1626 O VAL A 204 5.614 50.272 29.679 1.00 60.35 O ANISOU 1626 O VAL A 204 8861 6741 7330 -95 -1568 1703 O ATOM 1627 CB VAL A 204 7.458 52.965 30.113 1.00 67.10 C ANISOU 1627 CB VAL A 204 10080 7171 8244 -428 -1757 1813 C ATOM 1628 CG1 VAL A 204 6.846 52.625 31.457 1.00 73.18 C ANISOU 1628 CG1 VAL A 204 10754 8014 9037 -260 -1809 1710 C ATOM 1629 CG2 VAL A 204 8.868 53.477 30.311 1.00 79.10 C ANISOU 1629 CG2 VAL A 204 11676 8560 9818 -664 -1822 1871 C ATOM 1630 N ILE A 205 5.354 51.721 27.969 1.00 74.09 N ANISOU 1630 N ILE A 205 10841 8308 9003 -162 -1531 1809 N ATOM 1631 CA ILE A 205 4.056 51.167 27.587 1.00 80.35 C ANISOU 1631 CA ILE A 205 11554 9222 9752 21 -1458 1765 C ATOM 1632 C ILE A 205 4.216 49.722 27.127 1.00 76.96 C ANISOU 1632 C ILE A 205 10962 8959 9320 20 -1387 1755 C ATOM 1633 O ILE A 205 3.513 48.818 27.596 1.00 76.98 O ANISOU 1633 O ILE A 205 10836 9089 9324 144 -1347 1682 O ATOM 1634 CB ILE A 205 3.397 52.030 26.494 1.00 84.33 C ANISOU 1634 CB ILE A 205 12194 9653 10197 65 -1426 1815 C ATOM 1635 CG1 ILE A 205 3.002 53.407 27.034 1.00 89.33 C ANISOU 1635 CG1 ILE A 205 12981 10132 10827 103 -1492 1806 C ATOM 1636 CG2 ILE A 205 2.180 51.311 25.911 1.00 66.94 C ANISOU 1636 CG2 ILE A 205 9889 7596 7950 227 -1353 1785 C ATOM 1637 CD1 ILE A 205 1.934 53.362 28.102 1.00 89.10 C ANISOU 1637 CD1 ILE A 205 12879 10164 10811 265 -1517 1716 C ATOM 1638 N TYR A 206 5.148 49.487 26.199 1.00 63.68 N ANISOU 1638 N TYR A 206 9287 7276 7633 -128 -1361 1827 N ATOM 1639 CA TYR A 206 5.388 48.136 25.704 1.00 62.14 C ANISOU 1639 CA TYR A 206 8942 7233 7437 -143 -1298 1818 C ATOM 1640 C TYR A 206 5.786 47.192 26.835 1.00 65.41 C ANISOU 1640 C TYR A 206 9210 7742 7902 -138 -1321 1758 C ATOM 1641 O TYR A 206 5.370 46.029 26.852 1.00 74.38 O ANISOU 1641 O TYR A 206 10219 9010 9034 -53 -1261 1701 O ATOM 1642 CB TYR A 206 6.452 48.170 24.605 1.00 61.58 C ANISOU 1642 CB TYR A 206 8902 7140 7355 -326 -1270 1910 C ATOM 1643 CG TYR A 206 7.235 46.885 24.434 1.00 81.28 C ANISOU 1643 CG TYR A 206 11233 9777 9874 -411 -1236 1912 C ATOM 1644 CD1 TYR A 206 6.729 45.828 23.683 1.00 78.01 C ANISOU 1644 CD1 TYR A 206 10720 9489 9432 -332 -1162 1883 C ATOM 1645 CD2 TYR A 206 8.495 46.737 25.007 1.00 83.01 C ANISOU 1645 CD2 TYR A 206 11395 10004 10142 -574 -1283 1944 C ATOM 1646 CE1 TYR A 206 7.454 44.653 23.520 1.00 74.94 C ANISOU 1646 CE1 TYR A 206 10180 9228 9066 -408 -1130 1882 C ATOM 1647 CE2 TYR A 206 9.224 45.571 24.852 1.00 79.66 C ANISOU 1647 CE2 TYR A 206 10810 9723 9735 -645 -1252 1950 C ATOM 1648 CZ TYR A 206 8.703 44.531 24.108 1.00 80.12 C ANISOU 1648 CZ TYR A 206 10773 9902 9767 -560 -1173 1917 C ATOM 1649 OH TYR A 206 9.436 43.372 23.956 1.00 71.30 O ANISOU 1649 OH TYR A 206 9497 8925 8667 -628 -1139 1919 O ATOM 1650 N MET A 207 6.583 47.674 27.793 1.00 62.45 N ANISOU 1650 N MET A 207 8859 7296 7573 -225 -1406 1766 N ATOM 1651 CA MET A 207 6.914 46.860 28.963 1.00 66.40 C ANISOU 1651 CA MET A 207 9229 7885 8116 -192 -1433 1705 C ATOM 1652 C MET A 207 5.671 46.548 29.774 1.00 67.40 C ANISOU 1652 C MET A 207 9314 8066 8230 13 -1397 1602 C ATOM 1653 O MET A 207 5.460 45.406 30.204 1.00 71.94 O ANISOU 1653 O MET A 207 9764 8762 8807 93 -1341 1538 O ATOM 1654 CB MET A 207 7.926 47.583 29.849 1.00 60.03 C ANISOU 1654 CB MET A 207 8472 6981 7355 -309 -1550 1731 C ATOM 1655 CG MET A 207 9.341 47.405 29.423 1.00 73.79 C ANISOU 1655 CG MET A 207 10182 8737 9118 -522 -1580 1820 C ATOM 1656 SD MET A 207 9.863 45.725 29.717 1.00 94.23 S ANISOU 1656 SD MET A 207 12542 11542 11719 -498 -1542 1782 S ATOM 1657 CE MET A 207 10.125 45.779 31.490 1.00 81.72 C ANISOU 1657 CE MET A 207 10913 9960 10176 -416 -1651 1698 C ATOM 1658 N PHE A 208 4.848 47.570 30.011 1.00 69.74 N ANISOU 1658 N PHE A 208 9719 8270 8511 94 -1421 1587 N ATOM 1659 CA PHE A 208 3.665 47.417 30.845 1.00 67.12 C ANISOU 1659 CA PHE A 208 9345 7992 8167 270 -1385 1502 C ATOM 1660 C PHE A 208 2.696 46.416 30.238 1.00 73.25 C ANISOU 1660 C PHE A 208 10033 8898 8903 378 -1276 1469 C ATOM 1661 O PHE A 208 2.184 45.534 30.938 1.00 64.86 O ANISOU 1661 O PHE A 208 8870 7937 7837 476 -1220 1400 O ATOM 1662 CB PHE A 208 2.993 48.778 31.035 1.00 64.16 C ANISOU 1662 CB PHE A 208 9100 7496 7781 317 -1435 1506 C ATOM 1663 CG PHE A 208 1.886 48.775 32.047 1.00 61.65 C ANISOU 1663 CG PHE A 208 8734 7230 7462 467 -1413 1430 C ATOM 1664 CD1 PHE A 208 2.170 48.849 33.406 1.00 54.90 C ANISOU 1664 CD1 PHE A 208 7854 6363 6643 486 -1461 1376 C ATOM 1665 CD2 PHE A 208 0.563 48.703 31.643 1.00 53.38 C ANISOU 1665 CD2 PHE A 208 7656 6247 6379 580 -1347 1417 C ATOM 1666 CE1 PHE A 208 1.149 48.844 34.347 1.00 56.98 C ANISOU 1666 CE1 PHE A 208 8068 6677 6903 609 -1431 1313 C ATOM 1667 CE2 PHE A 208 -0.464 48.694 32.579 1.00 63.87 C ANISOU 1667 CE2 PHE A 208 8926 7629 7714 689 -1326 1360 C ATOM 1668 CZ PHE A 208 -0.171 48.764 33.932 1.00 59.10 C ANISOU 1668 CZ PHE A 208 8302 7010 7142 700 -1363 1310 C ATOM 1669 N VAL A 209 2.453 46.520 28.930 1.00 72.36 N ANISOU 1669 N VAL A 209 9962 8778 8752 359 -1243 1519 N ATOM 1670 CA VAL A 209 1.469 45.661 28.277 1.00 78.35 C ANISOU 1670 CA VAL A 209 10652 9649 9469 465 -1156 1485 C ATOM 1671 C VAL A 209 2.024 44.255 28.072 1.00 77.40 C ANISOU 1671 C VAL A 209 10428 9624 9357 425 -1109 1456 C ATOM 1672 O VAL A 209 1.451 43.269 28.550 1.00 79.37 O ANISOU 1672 O VAL A 209 10597 9962 9599 517 -1056 1379 O ATOM 1673 CB VAL A 209 1.011 46.284 26.945 1.00 70.79 C ANISOU 1673 CB VAL A 209 9778 8654 8463 473 -1145 1546 C ATOM 1674 CG1 VAL A 209 0.117 45.308 26.185 1.00 57.86 C ANISOU 1674 CG1 VAL A 209 8065 7137 6781 572 -1069 1511 C ATOM 1675 CG2 VAL A 209 0.288 47.624 27.184 1.00 56.74 C ANISOU 1675 CG2 VAL A 209 8096 6786 6676 531 -1191 1567 C ATOM 1676 N VAL A 210 3.157 44.145 27.373 1.00 68.60 N ANISOU 1676 N VAL A 210 9315 8489 8259 276 -1127 1519 N ATOM 1677 CA VAL A 210 3.649 42.845 26.924 1.00 64.23 C ANISOU 1677 CA VAL A 210 8656 8033 7717 224 -1080 1505 C ATOM 1678 C VAL A 210 4.320 42.063 28.055 1.00 71.86 C ANISOU 1678 C VAL A 210 9525 9052 8728 207 -1086 1460 C ATOM 1679 O VAL A 210 4.205 40.834 28.118 1.00 81.22 O ANISOU 1679 O VAL A 210 10620 10323 9916 241 -1030 1404 O ATOM 1680 CB VAL A 210 4.595 43.028 25.723 1.00 65.91 C ANISOU 1680 CB VAL A 210 8887 8228 7929 68 -1085 1601 C ATOM 1681 CG1 VAL A 210 5.278 41.717 25.371 1.00 62.97 C ANISOU 1681 CG1 VAL A 210 8381 7966 7578 -4 -1040 1596 C ATOM 1682 CG2 VAL A 210 3.825 43.552 24.528 1.00 58.40 C ANISOU 1682 CG2 VAL A 210 8027 7244 6920 118 -1060 1631 C ATOM 1683 N HIS A 211 5.038 42.730 28.959 1.00 67.59 N ANISOU 1683 N HIS A 211 9004 8456 8219 155 -1157 1481 N ATOM 1684 CA HIS A 211 5.780 42.006 29.988 1.00 65.00 C ANISOU 1684 CA HIS A 211 8584 8188 7925 145 -1169 1443 C ATOM 1685 C HIS A 211 5.180 42.136 31.379 1.00 58.81 C ANISOU 1685 C HIS A 211 7811 7396 7140 280 -1176 1362 C ATOM 1686 O HIS A 211 5.763 41.621 32.338 1.00 55.45 O ANISOU 1686 O HIS A 211 7322 7013 6732 294 -1188 1324 O ATOM 1687 CB HIS A 211 7.252 42.446 30.007 1.00 58.89 C ANISOU 1687 CB HIS A 211 7799 7388 7189 -26 -1254 1524 C ATOM 1688 CG HIS A 211 7.960 42.204 28.712 1.00 59.72 C ANISOU 1688 CG HIS A 211 7874 7527 7290 -172 -1232 1609 C ATOM 1689 ND1 HIS A 211 8.649 41.042 28.445 1.00 65.58 N ANISOU 1689 ND1 HIS A 211 8486 8391 8040 -222 -1188 1610 N ATOM 1690 CD2 HIS A 211 8.051 42.960 27.591 1.00 73.09 C ANISOU 1690 CD2 HIS A 211 9655 9153 8963 -269 -1237 1692 C ATOM 1691 CE1 HIS A 211 9.151 41.100 27.223 1.00 71.92 C ANISOU 1691 CE1 HIS A 211 9286 9209 8830 -351 -1170 1693 C ATOM 1692 NE2 HIS A 211 8.800 42.253 26.682 1.00 66.10 N ANISOU 1692 NE2 HIS A 211 8685 8355 8073 -382 -1195 1743 N ATOM 1693 N PHE A 212 4.027 42.782 31.521 1.00 63.46 N ANISOU 1693 N PHE A 212 8467 7945 7701 386 -1162 1338 N ATOM 1694 CA PHE A 212 3.319 42.696 32.793 1.00 72.10 C ANISOU 1694 CA PHE A 212 9543 9068 8785 519 -1138 1265 C ATOM 1695 C PHE A 212 1.870 42.248 32.617 1.00 71.33 C ANISOU 1695 C PHE A 212 9431 9030 8640 652 -1049 1219 C ATOM 1696 O PHE A 212 1.467 41.249 33.219 1.00 69.46 O ANISOU 1696 O PHE A 212 9142 8867 8383 738 -987 1151 O ATOM 1697 CB PHE A 212 3.363 44.026 33.545 1.00 59.77 C ANISOU 1697 CB PHE A 212 8053 7410 7247 513 -1222 1283 C ATOM 1698 CG PHE A 212 2.535 44.029 34.801 1.00 59.85 C ANISOU 1698 CG PHE A 212 8030 7459 7250 639 -1189 1225 C ATOM 1699 CD1 PHE A 212 2.877 43.217 35.870 1.00 59.72 C ANISOU 1699 CD1 PHE A 212 7938 7516 7236 686 -1159 1176 C ATOM 1700 CD2 PHE A 212 1.413 44.834 34.910 1.00 66.71 C ANISOU 1700 CD2 PHE A 212 8937 8298 8113 701 -1184 1229 C ATOM 1701 CE1 PHE A 212 2.122 43.210 37.025 1.00 67.56 C ANISOU 1701 CE1 PHE A 212 8889 8551 8228 779 -1119 1146 C ATOM 1702 CE2 PHE A 212 0.649 44.832 36.066 1.00 65.76 C ANISOU 1702 CE2 PHE A 212 8766 8217 8001 784 -1155 1194 C ATOM 1703 CZ PHE A 212 1.004 44.020 37.125 1.00 66.07 C ANISOU 1703 CZ PHE A 212 8727 8329 8048 814 -1120 1159 C ATOM 1704 N ILE A 213 1.084 42.972 31.806 1.00 60.57 N ANISOU 1704 N ILE A 213 8121 7637 7257 671 -1048 1256 N ATOM 1705 CA ILE A 213 -0.342 42.664 31.664 1.00 69.26 C ANISOU 1705 CA ILE A 213 9186 8811 8319 791 -977 1227 C ATOM 1706 C ILE A 213 -0.534 41.281 31.047 1.00 70.50 C ANISOU 1706 C ILE A 213 9314 9015 8458 794 -931 1156 C ATOM 1707 O ILE A 213 -1.245 40.431 31.595 1.00 72.77 O ANISOU 1707 O ILE A 213 9560 9339 8752 840 -895 1077 O ATOM 1708 CB ILE A 213 -1.056 43.752 30.836 1.00 75.21 C ANISOU 1708 CB ILE A 213 9993 9522 9061 797 -1001 1289 C ATOM 1709 CG1 ILE A 213 -1.090 45.081 31.591 1.00 74.24 C ANISOU 1709 CG1 ILE A 213 9928 9306 8974 780 -1075 1316 C ATOM 1710 CG2 ILE A 213 -2.488 43.327 30.505 1.00 60.75 C ANISOU 1710 CG2 ILE A 213 8095 7763 7224 857 -960 1267 C ATOM 1711 CD1 ILE A 213 -1.874 45.024 32.881 1.00 68.66 C ANISOU 1711 CD1 ILE A 213 9156 8635 8298 839 -1069 1281 C ATOM 1712 N ILE A 214 0.099 41.036 29.896 1.00 61.00 N ANISOU 1712 N ILE A 214 8139 7793 7245 722 -946 1187 N ATOM 1713 CA ILE A 214 -0.028 39.731 29.244 1.00 65.18 C ANISOU 1713 CA ILE A 214 8636 8353 7777 697 -925 1135 C ATOM 1714 C ILE A 214 0.428 38.586 30.143 1.00 67.22 C ANISOU 1714 C ILE A 214 8833 8633 8075 674 -914 1079 C ATOM 1715 O ILE A 214 -0.307 37.591 30.253 1.00 67.26 O ANISOU 1715 O ILE A 214 8809 8649 8099 691 -907 1023 O ATOM 1716 CB ILE A 214 0.691 39.748 27.882 1.00 64.38 C ANISOU 1716 CB ILE A 214 8528 8248 7685 579 -928 1208 C ATOM 1717 CG1 ILE A 214 -0.116 40.575 26.877 1.00 59.31 C ANISOU 1717 CG1 ILE A 214 7959 7585 6991 633 -936 1242 C ATOM 1718 CG2 ILE A 214 0.955 38.323 27.392 1.00 54.43 C ANISOU 1718 CG2 ILE A 214 7181 7043 6456 513 -891 1182 C ATOM 1719 CD1 ILE A 214 0.478 40.600 25.493 1.00 66.13 C ANISOU 1719 CD1 ILE A 214 8831 8445 7852 529 -936 1315 C ATOM 1720 N PRO A 215 1.596 38.639 30.802 1.00 76.38 N ANISOU 1720 N PRO A 215 9963 9798 9261 621 -922 1101 N ATOM 1721 CA PRO A 215 1.897 37.578 31.782 1.00 66.87 C ANISOU 1721 CA PRO A 215 8714 8616 8077 637 -906 1037 C ATOM 1722 C PRO A 215 0.838 37.447 32.860 1.00 58.45 C ANISOU 1722 C PRO A 215 7673 7527 7008 730 -908 966 C ATOM 1723 O PRO A 215 0.548 36.331 33.307 1.00 65.17 O ANISOU 1723 O PRO A 215 8492 8374 7895 718 -901 920 O ATOM 1724 CB PRO A 215 3.254 38.010 32.359 1.00 53.32 C ANISOU 1724 CB PRO A 215 6966 6910 6384 578 -939 1086 C ATOM 1725 CG PRO A 215 3.896 38.739 31.240 1.00 62.09 C ANISOU 1725 CG PRO A 215 8074 8007 7512 457 -970 1186 C ATOM 1726 CD PRO A 215 2.766 39.519 30.600 1.00 63.98 C ANISOU 1726 CD PRO A 215 8390 8204 7716 514 -968 1194 C ATOM 1727 N LEU A 216 0.236 38.559 33.282 1.00 65.11 N ANISOU 1727 N LEU A 216 8547 8365 7826 799 -901 970 N ATOM 1728 CA LEU A 216 -0.776 38.495 34.331 1.00 69.52 C ANISOU 1728 CA LEU A 216 9109 8925 8381 878 -875 904 C ATOM 1729 C LEU A 216 -2.021 37.774 33.835 1.00 77.53 C ANISOU 1729 C LEU A 216 10164 9858 9437 842 -938 829 C ATOM 1730 O LEU A 216 -2.563 36.900 34.525 1.00 68.52 O ANISOU 1730 O LEU A 216 8974 8651 8411 745 -1000 819 O ATOM 1731 CB LEU A 216 -1.123 39.903 34.814 1.00 69.73 C ANISOU 1731 CB LEU A 216 9054 9021 8418 902 -833 1028 C ATOM 1732 CG LEU A 216 -1.924 40.001 36.110 1.00 78.11 C ANISOU 1732 CG LEU A 216 9980 10127 9573 865 -809 1105 C ATOM 1733 CD1 LEU A 216 -1.150 39.356 37.239 1.00 84.99 C ANISOU 1733 CD1 LEU A 216 10801 11017 10473 845 -791 1098 C ATOM 1734 CD2 LEU A 216 -2.230 41.452 36.432 1.00 76.63 C ANISOU 1734 CD2 LEU A 216 9849 9858 9408 867 -907 1145 C ATOM 1735 N ILE A 217 -2.476 38.119 32.628 1.00 71.02 N ANISOU 1735 N ILE A 217 9345 9056 8584 849 -927 862 N ATOM 1736 CA ILE A 217 -3.678 37.506 32.068 1.00 70.48 C ANISOU 1736 CA ILE A 217 9257 8933 8588 780 -995 838 C ATOM 1737 C ILE A 217 -3.475 36.007 31.877 1.00 72.42 C ANISOU 1737 C ILE A 217 9396 9244 8875 727 -943 870 C ATOM 1738 O ILE A 217 -4.308 35.191 32.291 1.00 65.75 O ANISOU 1738 O ILE A 217 8478 8422 8083 721 -924 869 O ATOM 1739 CB ILE A 217 -4.057 38.193 30.745 1.00 64.96 C ANISOU 1739 CB ILE A 217 8601 8256 7825 823 -988 855 C ATOM 1740 CG1 ILE A 217 -4.547 39.618 31.001 1.00 64.86 C ANISOU 1740 CG1 ILE A 217 8513 8420 7711 990 -826 948 C ATOM 1741 CG2 ILE A 217 -5.106 37.382 30.003 1.00 69.37 C ANISOU 1741 CG2 ILE A 217 9083 8814 8462 747 -1030 868 C ATOM 1742 CD1 ILE A 217 -4.703 40.429 29.730 1.00 55.69 C ANISOU 1742 CD1 ILE A 217 7308 7306 6544 963 -815 1071 C ATOM 1743 N VAL A 218 -2.355 35.626 31.253 1.00 65.72 N ANISOU 1743 N VAL A 218 8529 8447 7997 704 -902 911 N ATOM 1744 CA VAL A 218 -2.087 34.222 30.946 1.00 64.77 C ANISOU 1744 CA VAL A 218 8299 8401 7908 650 -820 929 C ATOM 1745 C VAL A 218 -2.004 33.393 32.224 1.00 68.39 C ANISOU 1745 C VAL A 218 8717 8867 8401 657 -783 907 C ATOM 1746 O VAL A 218 -2.599 32.313 32.324 1.00 68.85 O ANISOU 1746 O VAL A 218 8701 8976 8483 657 -707 900 O ATOM 1747 CB VAL A 218 -0.802 34.099 30.108 1.00 64.54 C ANISOU 1747 CB VAL A 218 8240 8417 7865 583 -784 976 C ATOM 1748 CG1 VAL A 218 -0.359 32.647 30.024 1.00 57.27 C ANISOU 1748 CG1 VAL A 218 7212 7572 6976 533 -694 984 C ATOM 1749 CG2 VAL A 218 -1.023 34.687 28.718 1.00 52.98 C ANISOU 1749 CG2 VAL A 218 6800 6957 6372 567 -800 1009 C ATOM 1750 N ILE A 219 -1.275 33.887 33.224 1.00 64.70 N ANISOU 1750 N ILE A 219 8302 8355 7928 675 -827 897 N ATOM 1751 CA ILE A 219 -1.167 33.160 34.487 1.00 67.04 C ANISOU 1751 CA ILE A 219 8565 8653 8253 686 -798 882 C ATOM 1752 C ILE A 219 -2.535 33.011 35.152 1.00 58.97 C ANISOU 1752 C ILE A 219 7525 7619 7264 720 -787 867 C ATOM 1753 O ILE A 219 -2.851 31.959 35.717 1.00 77.62 O ANISOU 1753 O ILE A 219 9829 10027 9634 739 -697 861 O ATOM 1754 CB ILE A 219 -0.148 33.851 35.413 1.00 65.14 C ANISOU 1754 CB ILE A 219 8384 8364 8002 701 -866 870 C ATOM 1755 CG1 ILE A 219 1.278 33.538 34.946 1.00 66.91 C ANISOU 1755 CG1 ILE A 219 8580 8642 8203 669 -835 889 C ATOM 1756 CG2 ILE A 219 -0.357 33.441 36.876 1.00 52.62 C ANISOU 1756 CG2 ILE A 219 6775 6760 6456 718 -862 862 C ATOM 1757 CD1 ILE A 219 2.351 34.133 35.824 1.00 74.51 C ANISOU 1757 CD1 ILE A 219 9582 9580 9147 695 -891 870 C ATOM 1758 N PHE A 220 -3.367 34.054 35.094 1.00 63.73 N ANISOU 1758 N PHE A 220 8170 8166 7879 732 -868 865 N ATOM 1759 CA PHE A 220 -4.672 33.997 35.750 1.00 73.39 C ANISOU 1759 CA PHE A 220 9352 9397 9135 766 -846 861 C ATOM 1760 C PHE A 220 -5.630 33.080 35.001 1.00 75.96 C ANISOU 1760 C PHE A 220 9614 9795 9452 786 -760 842 C ATOM 1761 O PHE A 220 -6.367 32.301 35.619 1.00 60.99 O ANISOU 1761 O PHE A 220 7673 7942 7559 828 -677 821 O ATOM 1762 CB PHE A 220 -5.265 35.401 35.875 1.00 67.92 C ANISOU 1762 CB PHE A 220 8683 8653 8472 753 -926 882 C ATOM 1763 CG PHE A 220 -5.037 36.035 37.216 1.00 83.66 C ANISOU 1763 CG PHE A 220 10667 10626 10492 758 -939 910 C ATOM 1764 CD1 PHE A 220 -3.855 36.716 37.489 1.00 94.25 C ANISOU 1764 CD1 PHE A 220 12023 11938 11849 699 -976 942 C ATOM 1765 CD2 PHE A 220 -5.999 35.946 38.210 1.00 81.27 C ANISOU 1765 CD2 PHE A 220 10340 10347 10193 835 -907 904 C ATOM 1766 CE1 PHE A 220 -3.641 37.301 38.727 1.00 96.81 C ANISOU 1766 CE1 PHE A 220 12314 12284 12184 729 -961 985 C ATOM 1767 CE2 PHE A 220 -5.792 36.529 39.450 1.00 91.31 C ANISOU 1767 CE2 PHE A 220 11618 11609 11465 869 -908 915 C ATOM 1768 CZ PHE A 220 -4.610 37.208 39.708 1.00100.59 C ANISOU 1768 CZ PHE A 220 12797 12773 12652 822 -939 959 C ATOM 1769 N PHE A 221 -5.641 33.166 33.672 1.00 67.36 N ANISOU 1769 N PHE A 221 8524 8723 8346 762 -776 849 N ATOM 1770 CA PHE A 221 -6.456 32.254 32.880 1.00 64.25 C ANISOU 1770 CA PHE A 221 8055 8406 7950 773 -697 835 C ATOM 1771 C PHE A 221 -6.044 30.802 33.115 1.00 76.55 C ANISOU 1771 C PHE A 221 9550 10030 9504 764 -576 835 C ATOM 1772 O PHE A 221 -6.873 29.962 33.483 1.00 81.45 O ANISOU 1772 O PHE A 221 10120 10694 10132 800 -498 813 O ATOM 1773 CB PHE A 221 -6.346 32.618 31.401 1.00 58.18 C ANISOU 1773 CB PHE A 221 7296 7647 7161 744 -736 850 C ATOM 1774 CG PHE A 221 -7.090 31.685 30.491 1.00 75.61 C ANISOU 1774 CG PHE A 221 9419 9940 9370 749 -664 836 C ATOM 1775 CD1 PHE A 221 -8.456 31.839 30.288 1.00 71.97 C ANISOU 1775 CD1 PHE A 221 8926 9501 8920 795 -679 805 C ATOM 1776 CD2 PHE A 221 -6.426 30.658 29.832 1.00 79.43 C ANISOU 1776 CD2 PHE A 221 9845 10489 9847 706 -582 854 C ATOM 1777 CE1 PHE A 221 -9.145 30.984 29.448 1.00 65.46 C ANISOU 1777 CE1 PHE A 221 8011 8772 8090 811 -612 790 C ATOM 1778 CE2 PHE A 221 -7.111 29.798 28.986 1.00 76.74 C ANISOU 1778 CE2 PHE A 221 9415 10236 9505 713 -515 849 C ATOM 1779 CZ PHE A 221 -8.476 29.963 28.794 1.00 63.36 C ANISOU 1779 CZ PHE A 221 7685 8575 7812 771 -529 817 C ATOM 1780 N CYS A 222 -4.761 30.491 32.917 1.00 70.02 N ANISOU 1780 N CYS A 222 8726 9210 8666 719 -558 861 N ATOM 1781 CA CYS A 222 -4.312 29.103 32.987 1.00 61.24 C ANISOU 1781 CA CYS A 222 7553 8161 7553 705 -448 870 C ATOM 1782 C CYS A 222 -4.584 28.490 34.357 1.00 64.36 C ANISOU 1782 C CYS A 222 7951 8553 7951 755 -389 854 C ATOM 1783 O CYS A 222 -5.083 27.365 34.455 1.00 77.27 O ANISOU 1783 O CYS A 222 9533 10246 9581 782 -283 856 O ATOM 1784 CB CYS A 222 -2.828 29.014 32.641 1.00 52.12 C ANISOU 1784 CB CYS A 222 6400 7015 6389 651 -452 900 C ATOM 1785 SG CYS A 222 -2.522 29.216 30.887 1.00 69.48 S ANISOU 1785 SG CYS A 222 8568 9250 8580 589 -466 928 S ATOM 1786 N TYR A 223 -4.255 29.209 35.429 1.00 78.27 N ANISOU 1786 N TYR A 223 9582 9917 10241 -952 -1908 -233 N ATOM 1787 CA TYR A 223 -4.474 28.655 36.759 1.00 68.50 C ANISOU 1787 CA TYR A 223 8300 8627 9100 -957 -1754 -292 C ATOM 1788 C TYR A 223 -5.937 28.719 37.169 1.00 75.56 C ANISOU 1788 C TYR A 223 9004 9507 10197 -947 -1767 -278 C ATOM 1789 O TYR A 223 -6.398 27.852 37.921 1.00 77.49 O ANISOU 1789 O TYR A 223 9189 9732 10521 -986 -1681 -328 O ATOM 1790 CB TYR A 223 -3.594 29.368 37.786 1.00 59.46 C ANISOU 1790 CB TYR A 223 7223 7429 7939 -885 -1603 -294 C ATOM 1791 CG TYR A 223 -2.173 28.878 37.759 1.00 71.40 C ANISOU 1791 CG TYR A 223 8909 8957 9262 -910 -1541 -344 C ATOM 1792 CD1 TYR A 223 -1.896 27.533 37.540 1.00 66.30 C ANISOU 1792 CD1 TYR A 223 8331 8341 8519 -986 -1541 -411 C ATOM 1793 CD2 TYR A 223 -1.104 29.752 37.927 1.00 70.87 C ANISOU 1793 CD2 TYR A 223 8937 8875 9115 -858 -1487 -328 C ATOM 1794 CE1 TYR A 223 -0.602 27.066 37.499 1.00 66.08 C ANISOU 1794 CE1 TYR A 223 8462 8335 8310 -1000 -1489 -460 C ATOM 1795 CE2 TYR A 223 0.205 29.292 37.890 1.00 49.14 C ANISOU 1795 CE2 TYR A 223 6335 6150 6184 -880 -1432 -379 C ATOM 1796 CZ TYR A 223 0.447 27.947 37.670 1.00 56.61 C ANISOU 1796 CZ TYR A 223 7348 7134 7027 -947 -1434 -444 C ATOM 1797 OH TYR A 223 1.733 27.463 37.633 1.00 61.10 O ANISOU 1797 OH TYR A 223 8065 7737 7411 -960 -1382 -499 O ATOM 1798 N GLY A 224 -6.676 29.725 36.696 1.00 69.84 N ANISOU 1798 N GLY A 224 8183 8796 9557 -892 -1869 -207 N ATOM 1799 CA GLY A 224 -8.117 29.717 36.897 1.00 58.43 C ANISOU 1799 CA GLY A 224 6549 7360 8291 -887 -1907 -198 C ATOM 1800 C GLY A 224 -8.765 28.484 36.300 1.00 65.05 C ANISOU 1800 C GLY A 224 7328 8245 9141 -991 -1993 -251 C ATOM 1801 O GLY A 224 -9.580 27.817 36.944 1.00 69.72 O ANISOU 1801 O GLY A 224 7804 8824 9862 -1033 -1936 -288 O ATOM 1802 N GLN A 225 -8.394 28.153 35.060 1.00 62.66 N ANISOU 1802 N GLN A 225 7104 7998 8704 -1035 -2130 -258 N ATOM 1803 CA GLN A 225 -8.881 26.926 34.436 1.00 69.73 C ANISOU 1803 CA GLN A 225 7960 8935 9598 -1137 -2220 -327 C ATOM 1804 C GLN A 225 -8.445 25.691 35.219 1.00 70.35 C ANISOU 1804 C GLN A 225 8103 8963 9664 -1215 -2086 -406 C ATOM 1805 O GLN A 225 -9.226 24.746 35.393 1.00 73.59 O ANISOU 1805 O GLN A 225 8417 9364 10180 -1293 -2086 -459 O ATOM 1806 CB GLN A 225 -8.389 26.848 32.989 1.00 50.98 C ANISOU 1806 CB GLN A 225 5679 6638 7055 -1151 -2385 -324 C ATOM 1807 CG GLN A 225 -8.898 27.969 32.087 1.00 75.95 C ANISOU 1807 CG GLN A 225 8776 9859 10222 -1072 -2531 -240 C ATOM 1808 CD GLN A 225 -10.379 27.857 31.772 1.00 83.32 C ANISOU 1808 CD GLN A 225 9511 10838 11307 -1083 -2644 -253 C ATOM 1809 OE1 GLN A 225 -10.764 27.345 30.721 1.00 97.68 O ANISOU 1809 OE1 GLN A 225 11295 12736 13081 -1120 -2799 -290 O ATOM 1810 NE2 GLN A 225 -11.218 28.343 32.680 1.00 85.64 N ANISOU 1810 NE2 GLN A 225 9669 11093 11779 -1044 -2569 -228 N ATOM 1811 N LEU A 226 -7.202 25.683 35.706 1.00 76.23 N ANISOU 1811 N LEU A 226 9007 9673 10282 -1193 -1970 -415 N ATOM 1812 CA LEU A 226 -6.691 24.520 36.425 1.00 79.82 C ANISOU 1812 CA LEU A 226 9542 10084 10704 -1252 -1841 -487 C ATOM 1813 C LEU A 226 -7.443 24.300 37.734 1.00 73.35 C ANISOU 1813 C LEU A 226 8604 9207 10061 -1248 -1693 -489 C ATOM 1814 O LEU A 226 -7.817 23.167 38.058 1.00 73.20 O ANISOU 1814 O LEU A 226 8554 9157 10101 -1327 -1645 -539 O ATOM 1815 CB LEU A 226 -5.191 24.684 36.675 1.00 71.27 C ANISOU 1815 CB LEU A 226 8648 8991 9442 -1211 -1750 -495 C ATOM 1816 CG LEU A 226 -4.394 23.399 36.881 1.00 74.27 C ANISOU 1816 CG LEU A 226 9160 9353 9708 -1271 -1678 -575 C ATOM 1817 CD1 LEU A 226 -2.966 23.605 36.435 1.00 90.34 C ANISOU 1817 CD1 LEU A 226 11375 11424 11525 -1242 -1683 -584 C ATOM 1818 CD2 LEU A 226 -4.423 22.993 38.330 1.00 70.19 C ANISOU 1818 CD2 LEU A 226 8627 8768 9273 -1255 -1483 -595 C ATOM 1819 N VAL A 227 -7.672 25.367 38.500 1.00 70.75 N ANISOU 1819 N VAL A 227 8205 8860 9816 -1155 -1617 -435 N ATOM 1820 CA VAL A 227 -8.457 25.241 39.724 1.00 66.06 C ANISOU 1820 CA VAL A 227 7483 8230 9388 -1137 -1481 -430 C ATOM 1821 C VAL A 227 -9.885 24.818 39.401 1.00 79.98 C ANISOU 1821 C VAL A 227 9059 10013 11315 -1204 -1567 -431 C ATOM 1822 O VAL A 227 -10.508 24.050 40.145 1.00 78.96 O ANISOU 1822 O VAL A 227 8841 9856 11303 -1252 -1470 -450 O ATOM 1823 CB VAL A 227 -8.422 26.561 40.512 1.00 60.36 C ANISOU 1823 CB VAL A 227 6722 7495 8718 -1010 -1404 -380 C ATOM 1824 CG1 VAL A 227 -9.522 26.581 41.546 1.00 49.24 C ANISOU 1824 CG1 VAL A 227 5138 6074 7495 -982 -1307 -365 C ATOM 1825 CG2 VAL A 227 -7.056 26.751 41.174 1.00 69.56 C ANISOU 1825 CG2 VAL A 227 8050 8630 9747 -953 -1274 -401 C ATOM 1826 N PHE A 228 -10.425 25.299 38.282 1.00 75.36 N ANISOU 1826 N PHE A 228 8410 9484 10741 -1208 -1749 -410 N ATOM 1827 CA PHE A 228 -11.784 24.920 37.922 1.00 67.11 C ANISOU 1827 CA PHE A 228 7178 8472 9848 -1269 -1843 -422 C ATOM 1828 C PHE A 228 -11.859 23.449 37.528 1.00 74.03 C ANISOU 1828 C PHE A 228 8074 9335 10717 -1405 -1874 -499 C ATOM 1829 O PHE A 228 -12.792 22.742 37.927 1.00 71.82 O ANISOU 1829 O PHE A 228 7657 9039 10592 -1477 -1838 -523 O ATOM 1830 CB PHE A 228 -12.299 25.818 36.797 1.00 56.23 C ANISOU 1830 CB PHE A 228 5733 7166 8468 -1224 -2035 -383 C ATOM 1831 CG PHE A 228 -13.686 25.485 36.350 1.00 70.59 C ANISOU 1831 CG PHE A 228 7352 9036 10434 -1279 -2148 -405 C ATOM 1832 CD1 PHE A 228 -14.784 25.916 37.078 1.00 79.19 C ANISOU 1832 CD1 PHE A 228 8253 10132 11704 -1240 -2098 -375 C ATOM 1833 CD2 PHE A 228 -13.899 24.735 35.203 1.00 80.83 C ANISOU 1833 CD2 PHE A 228 8643 10381 11689 -1365 -2307 -463 C ATOM 1834 CE1 PHE A 228 -16.070 25.608 36.669 1.00 72.42 C ANISOU 1834 CE1 PHE A 228 7201 9331 10985 -1293 -2202 -400 C ATOM 1835 CE2 PHE A 228 -15.180 24.425 34.786 1.00 73.61 C ANISOU 1835 CE2 PHE A 228 7535 9520 10915 -1417 -2416 -496 C ATOM 1836 CZ PHE A 228 -16.267 24.864 35.520 1.00 69.29 C ANISOU 1836 CZ PHE A 228 6796 8980 10550 -1384 -2362 -464 C ATOM 1837 N THR A 229 -10.882 22.968 36.753 1.00 77.71 N ANISOU 1837 N THR A 229 8708 9808 11009 -1440 -1939 -540 N ATOM 1838 CA THR A 229 -10.870 21.561 36.360 1.00 78.11 C ANISOU 1838 CA THR A 229 8794 9838 11045 -1563 -1974 -623 C ATOM 1839 C THR A 229 -10.727 20.647 37.573 1.00 80.03 C ANISOU 1839 C THR A 229 9064 9994 11351 -1608 -1777 -645 C ATOM 1840 O THR A 229 -11.395 19.609 37.662 1.00 73.70 O ANISOU 1840 O THR A 229 8184 9155 10665 -1713 -1769 -691 O ATOM 1841 CB THR A 229 -9.743 21.305 35.357 1.00 74.16 C ANISOU 1841 CB THR A 229 8482 9369 10327 -1570 -2072 -661 C ATOM 1842 OG1 THR A 229 -10.088 21.887 34.095 1.00 81.18 O ANISOU 1842 OG1 THR A 229 9324 10348 11174 -1547 -2273 -648 O ATOM 1843 CG2 THR A 229 -9.499 19.808 35.173 1.00 63.78 C ANISOU 1843 CG2 THR A 229 7241 8013 8980 -1681 -2073 -754 C ATOM 1844 N VAL A 230 -9.876 21.027 38.527 1.00 70.45 N ANISOU 1844 N VAL A 230 7956 8747 10067 -1528 -1615 -612 N ATOM 1845 CA VAL A 230 -9.648 20.179 39.692 1.00 74.55 C ANISOU 1845 CA VAL A 230 8515 9192 10621 -1551 -1421 -626 C ATOM 1846 C VAL A 230 -10.867 20.177 40.612 1.00 75.19 C ANISOU 1846 C VAL A 230 8397 9251 10919 -1560 -1323 -589 C ATOM 1847 O VAL A 230 -11.245 19.134 41.160 1.00 71.88 O ANISOU 1847 O VAL A 230 7942 8776 10595 -1638 -1227 -607 O ATOM 1848 CB VAL A 230 -8.365 20.624 40.417 1.00 68.20 C ANISOU 1848 CB VAL A 230 7875 8374 9664 -1449 -1285 -612 C ATOM 1849 CG1 VAL A 230 -8.188 19.865 41.714 1.00 67.76 C ANISOU 1849 CG1 VAL A 230 7848 8253 9643 -1446 -1075 -616 C ATOM 1850 CG2 VAL A 230 -7.169 20.391 39.512 1.00 71.92 C ANISOU 1850 CG2 VAL A 230 8538 8867 9921 -1460 -1371 -656 C ATOM 1851 N LYS A 231 -11.515 21.331 40.789 1.00 78.09 N ANISOU 1851 N LYS A 231 8632 9666 11374 -1478 -1346 -533 N ATOM 1852 CA LYS A 231 -12.722 21.362 41.611 1.00 69.61 C ANISOU 1852 CA LYS A 231 7356 8590 10504 -1481 -1262 -497 C ATOM 1853 C LYS A 231 -13.853 20.582 40.954 1.00 74.14 C ANISOU 1853 C LYS A 231 7777 9172 11219 -1611 -1374 -532 C ATOM 1854 O LYS A 231 -14.644 19.922 41.641 1.00 73.81 O ANISOU 1854 O LYS A 231 7610 9099 11333 -1674 -1274 -525 O ATOM 1855 CB LYS A 231 -13.143 22.806 41.884 1.00 67.42 C ANISOU 1855 CB LYS A 231 6974 8364 10278 -1354 -1276 -437 C ATOM 1856 CG LYS A 231 -12.191 23.544 42.832 1.00 81.19 C ANISOU 1856 CG LYS A 231 8831 10089 11929 -1224 -1132 -410 C ATOM 1857 CD LYS A 231 -12.832 24.782 43.438 1.00 85.00 C ANISOU 1857 CD LYS A 231 9176 10605 12514 -1102 -1104 -357 C ATOM 1858 CE LYS A 231 -11.815 25.635 44.197 1.00 88.04 C ANISOU 1858 CE LYS A 231 9680 10973 12798 -970 -996 -346 C ATOM 1859 NZ LYS A 231 -11.186 24.950 45.370 1.00 82.84 N ANISOU 1859 NZ LYS A 231 9101 10278 12096 -951 -793 -365 N ATOM 1860 N GLU A 232 -13.936 20.645 39.624 1.00 66.80 N ANISOU 1860 N GLU A 232 6854 8289 10238 -1652 -1579 -570 N ATOM 1861 CA GLU A 232 -14.945 19.889 38.893 1.00 60.03 C ANISOU 1861 CA GLU A 232 5858 7449 9504 -1776 -1706 -623 C ATOM 1862 C GLU A 232 -14.706 18.389 39.025 1.00 86.73 C ANISOU 1862 C GLU A 232 9310 10745 12900 -1906 -1643 -686 C ATOM 1863 O GLU A 232 -15.651 17.614 39.216 1.00 82.88 O ANISOU 1863 O GLU A 232 8678 10227 12587 -2013 -1623 -709 O ATOM 1864 CB GLU A 232 -14.924 20.310 37.424 1.00 70.17 C ANISOU 1864 CB GLU A 232 7157 8811 10694 -1769 -1941 -655 C ATOM 1865 CG GLU A 232 -16.261 20.327 36.723 1.00 98.46 C ANISOU 1865 CG GLU A 232 10524 12463 14424 -1820 -2098 -683 C ATOM 1866 CD GLU A 232 -16.135 20.792 35.282 1.00125.11 C ANISOU 1866 CD GLU A 232 13932 15927 17678 -1788 -2324 -708 C ATOM 1867 OE1 GLU A 232 -14.985 20.933 34.809 1.00135.44 O ANISOU 1867 OE1 GLU A 232 15436 17235 18791 -1747 -2354 -708 O ATOM 1868 OE2 GLU A 232 -17.175 21.016 34.625 1.00129.64 O ANISOU 1868 OE2 GLU A 232 14333 16578 18346 -1798 -2471 -728 O ATOM 1869 N ALA A 233 -13.442 17.964 38.931 1.00 87.21 N ANISOU 1869 N ALA A 233 9593 10763 12781 -1899 -1608 -714 N ATOM 1870 CA ALA A 233 -13.123 16.546 39.048 1.00 74.42 C ANISOU 1870 CA ALA A 233 8064 9054 11160 -2009 -1548 -774 C ATOM 1871 C ALA A 233 -13.392 16.030 40.458 1.00 77.29 C ANISOU 1871 C ALA A 233 8382 9337 11647 -2024 -1318 -727 C ATOM 1872 O ALA A 233 -13.905 14.918 40.630 1.00 75.93 O ANISOU 1872 O ALA A 233 8157 9091 11601 -2145 -1275 -757 O ATOM 1873 CB ALA A 233 -11.666 16.304 38.653 1.00 64.47 C ANISOU 1873 CB ALA A 233 7053 7780 9662 -1976 -1562 -811 C ATOM 1874 N ALA A 234 -13.059 16.823 41.480 1.00 66.97 N ANISOU 1874 N ALA A 234 7094 8043 10308 -1900 -1166 -654 N ATOM 1875 CA ALA A 234 -13.301 16.376 42.848 1.00 67.79 C ANISOU 1875 CA ALA A 234 7155 8088 10515 -1894 -941 -603 C ATOM 1876 C ALA A 234 -14.797 16.320 43.164 1.00 73.55 C ANISOU 1876 C ALA A 234 7628 8830 11486 -1958 -925 -570 C ATOM 1877 O ALA A 234 -15.260 15.369 43.806 1.00 77.14 O ANISOU 1877 O ALA A 234 8026 9216 12069 -2042 -798 -556 O ATOM 1878 CB ALA A 234 -12.556 17.276 43.834 1.00 56.83 C ANISOU 1878 CB ALA A 234 5845 6725 9022 -1733 -795 -547 C ATOM 1879 N ALA A 235 -15.574 17.313 42.707 1.00 73.73 N ANISOU 1879 N ALA A 235 7495 8943 11577 -1919 -1050 -555 N ATOM 1880 CA ALA A 235 -17.016 17.309 42.961 1.00 71.94 C ANISOU 1880 CA ALA A 235 7012 8745 11575 -1973 -1045 -529 C ATOM 1881 C ALA A 235 -17.677 16.070 42.378 1.00 69.19 C ANISOU 1881 C ALA A 235 6586 8345 11357 -2156 -1117 -593 C ATOM 1882 O ALA A 235 -18.623 15.525 42.959 1.00 77.68 O ANISOU 1882 O ALA A 235 7497 9395 12625 -2238 -1023 -569 O ATOM 1883 CB ALA A 235 -17.669 18.562 42.380 1.00 60.08 C ANISOU 1883 CB ALA A 235 5373 7353 10102 -1896 -1199 -516 C ATOM 1884 N GLN A 236 -17.197 15.620 41.226 1.00 72.00 N ANISOU 1884 N GLN A 236 7055 8688 11614 -2221 -1283 -677 N ATOM 1885 CA GLN A 236 -17.716 14.451 40.543 1.00 69.39 C ANISOU 1885 CA GLN A 236 6669 8305 11391 -2391 -1377 -761 C ATOM 1886 C GLN A 236 -17.029 13.159 41.012 1.00 76.21 C ANISOU 1886 C GLN A 236 7693 9034 12231 -2472 -1241 -780 C ATOM 1887 O GLN A 236 -17.237 12.096 40.415 1.00 66.55 O ANISOU 1887 O GLN A 236 6469 7742 11073 -2612 -1320 -861 O ATOM 1888 CB GLN A 236 -17.574 14.671 39.030 1.00 63.17 C ANISOU 1888 CB GLN A 236 5915 7586 10500 -2403 -1637 -848 C ATOM 1889 CG GLN A 236 -18.473 13.837 38.135 1.00 92.11 C ANISOU 1889 CG GLN A 236 9442 11247 14307 -2557 -1796 -947 C ATOM 1890 CD GLN A 236 -19.955 14.076 38.345 1.00 88.97 C ANISOU 1890 CD GLN A 236 8758 10904 14143 -2605 -1809 -929 C ATOM 1891 OE1 GLN A 236 -20.373 15.053 38.966 1.00 93.23 O ANISOU 1891 OE1 GLN A 236 9191 11510 14722 -2503 -1739 -844 O ATOM 1892 NE2 GLN A 236 -20.760 13.173 37.819 1.00 99.12 N ANISOU 1892 NE2 GLN A 236 9912 12163 15586 -2759 -1902 -1017 N ATOM 1893 N GLN A 237 -16.259 13.226 42.096 1.00 70.52 N ANISOU 1893 N GLN A 237 7100 8270 11424 -2381 -1038 -710 N ATOM 1894 CA GLN A 237 -15.529 12.075 42.618 1.00 60.73 C ANISOU 1894 CA GLN A 237 6028 6907 10140 -2430 -896 -718 C ATOM 1895 C GLN A 237 -15.344 12.221 44.130 1.00 75.11 C ANISOU 1895 C GLN A 237 7864 8705 11972 -2335 -636 -613 C ATOM 1896 O GLN A 237 -14.251 12.042 44.670 1.00 75.20 O ANISOU 1896 O GLN A 237 8071 8678 11826 -2256 -516 -598 O ATOM 1897 CB GLN A 237 -14.188 11.929 41.900 1.00 68.05 C ANISOU 1897 CB GLN A 237 7205 7825 10825 -2389 -986 -784 C ATOM 1898 CG GLN A 237 -13.573 10.561 41.976 1.00 80.66 C ANISOU 1898 CG GLN A 237 8965 9294 12387 -2472 -919 -831 C ATOM 1899 CD GLN A 237 -12.554 10.354 40.885 1.00 93.71 C ANISOU 1899 CD GLN A 237 10811 10959 13834 -2465 -1080 -925 C ATOM 1900 OE1 GLN A 237 -12.224 11.286 40.147 1.00 87.15 O ANISOU 1900 OE1 GLN A 237 10003 10237 12875 -2388 -1222 -942 O ATOM 1901 NE2 GLN A 237 -12.056 9.127 40.765 1.00 99.20 N ANISOU 1901 NE2 GLN A 237 11648 11545 14497 -2541 -1059 -985 N ATOM 1902 N GLN A 238 -16.431 12.539 44.836 1.00 82.47 N ANISOU 1902 N GLN A 238 8580 9669 13087 -2337 -547 -543 N ATOM 1903 CA GLN A 238 -16.390 12.762 46.277 1.00 71.10 C ANISOU 1903 CA GLN A 238 7121 8229 11663 -2234 -305 -441 C ATOM 1904 C GLN A 238 -16.119 11.499 47.090 1.00 79.44 C ANISOU 1904 C GLN A 238 8269 9160 12754 -2293 -107 -407 C ATOM 1905 O GLN A 238 -15.846 11.615 48.289 1.00 77.54 O ANISOU 1905 O GLN A 238 8059 8921 12481 -2187 101 -325 O ATOM 1906 CB GLN A 238 -17.703 13.385 46.742 1.00 63.38 C ANISOU 1906 CB GLN A 238 5874 7329 10878 -2224 -273 -379 C ATOM 1907 CG GLN A 238 -17.670 14.897 46.792 1.00 71.35 C ANISOU 1907 CG GLN A 238 6837 8462 11811 -2061 -329 -356 C ATOM 1908 CD GLN A 238 -19.037 15.524 46.647 1.00 85.95 C ANISOU 1908 CD GLN A 238 8417 10401 13840 -2078 -405 -336 C ATOM 1909 OE1 GLN A 238 -19.174 16.570 46.022 1.00 98.84 O ANISOU 1909 OE1 GLN A 238 10002 12121 15430 -2006 -559 -356 O ATOM 1910 NE2 GLN A 238 -20.058 14.888 47.221 1.00 98.26 N ANISOU 1910 NE2 GLN A 238 9794 11940 15601 -2171 -296 -293 N ATOM 1911 N GLU A 239 -16.200 10.308 46.492 1.00 81.27 N ANISOU 1911 N GLU A 239 8543 9284 13052 -2453 -165 -466 N ATOM 1912 CA GLU A 239 -15.847 9.084 47.208 1.00 80.12 C ANISOU 1912 CA GLU A 239 8511 9004 12927 -2505 19 -432 C ATOM 1913 C GLU A 239 -14.341 8.906 47.358 1.00 72.12 C ANISOU 1913 C GLU A 239 7781 7958 11663 -2399 72 -454 C ATOM 1914 O GLU A 239 -13.906 7.949 48.007 1.00 77.94 O ANISOU 1914 O GLU A 239 8640 8589 12384 -2411 234 -422 O ATOM 1915 CB GLU A 239 -16.446 7.849 46.514 1.00 64.57 C ANISOU 1915 CB GLU A 239 6493 6914 11126 -2716 -63 -496 C ATOM 1916 CG GLU A 239 -15.830 7.480 45.154 1.00 64.19 C ANISOU 1916 CG GLU A 239 6588 6839 10964 -2780 -290 -631 C ATOM 1917 CD GLU A 239 -16.368 8.308 43.984 1.00 83.58 C ANISOU 1917 CD GLU A 239 8910 9413 13433 -2798 -542 -707 C ATOM 1918 OE1 GLU A 239 -17.034 9.340 44.220 1.00 75.11 O ANISOU 1918 OE1 GLU A 239 7667 8453 12419 -2732 -548 -654 O ATOM 1919 OE2 GLU A 239 -16.129 7.919 42.819 1.00 82.67 O ANISOU 1919 OE2 GLU A 239 8863 9281 13265 -2871 -738 -820 O ATOM 1920 N SER A 240 -13.540 9.800 46.788 1.00 68.41 N ANISOU 1920 N SER A 240 7416 7579 10998 -2292 -54 -504 N ATOM 1921 CA SER A 240 -12.085 9.730 46.861 1.00 59.13 C ANISOU 1921 CA SER A 240 6499 6394 9575 -2188 -19 -534 C ATOM 1922 C SER A 240 -11.586 10.827 47.796 1.00 64.88 C ANISOU 1922 C SER A 240 7246 7217 10186 -1997 105 -472 C ATOM 1923 O SER A 240 -11.609 12.010 47.438 1.00 79.05 O ANISOU 1923 O SER A 240 8984 9118 11935 -1923 -3 -481 O ATOM 1924 CB SER A 240 -11.479 9.870 45.466 1.00 58.63 C ANISOU 1924 CB SER A 240 6545 6361 9372 -2216 -256 -643 C ATOM 1925 OG SER A 240 -10.083 10.068 45.522 1.00 64.50 O ANISOU 1925 OG SER A 240 7512 7128 9866 -2097 -231 -669 O ATOM 1926 N ALA A 241 -11.141 10.438 48.995 1.00 75.62 N ANISOU 1926 N ALA A 241 8689 8542 11502 -1913 331 -410 N ATOM 1927 CA ALA A 241 -10.595 11.420 49.930 1.00 82.81 C ANISOU 1927 CA ALA A 241 9627 9544 12292 -1722 452 -366 C ATOM 1928 C ALA A 241 -9.295 12.024 49.411 1.00 80.56 C ANISOU 1928 C ALA A 241 9528 9315 11765 -1626 354 -439 C ATOM 1929 O ALA A 241 -9.001 13.195 49.691 1.00 60.89 O ANISOU 1929 O ALA A 241 7018 6919 9198 -1495 353 -432 O ATOM 1930 CB ALA A 241 -10.375 10.787 51.304 1.00 53.33 C ANISOU 1930 CB ALA A 241 5946 5767 8550 -1646 713 -289 C ATOM 1931 N THR A 242 -8.512 11.246 48.656 1.00 75.32 N ANISOU 1931 N THR A 242 9043 8593 10984 -1688 271 -512 N ATOM 1932 CA THR A 242 -7.284 11.767 48.065 1.00 75.14 C ANISOU 1932 CA THR A 242 9190 8629 10730 -1609 170 -582 C ATOM 1933 C THR A 242 -7.582 12.881 47.074 1.00 77.33 C ANISOU 1933 C THR A 242 9374 8992 11015 -1620 -34 -610 C ATOM 1934 O THR A 242 -6.880 13.902 47.048 1.00 64.66 O ANISOU 1934 O THR A 242 7824 7469 9276 -1507 -63 -621 O ATOM 1935 CB THR A 242 -6.508 10.644 47.377 1.00 72.88 C ANISOU 1935 CB THR A 242 9095 8267 10328 -1682 110 -657 C ATOM 1936 OG1 THR A 242 -6.001 9.744 48.366 1.00 80.33 O ANISOU 1936 OG1 THR A 242 10161 9141 11221 -1634 311 -629 O ATOM 1937 CG2 THR A 242 -5.342 11.206 46.579 1.00 71.09 C ANISOU 1937 CG2 THR A 242 9022 8117 9874 -1619 -21 -731 C ATOM 1938 N THR A 243 -8.624 12.702 46.249 1.00 70.25 N ANISOU 1938 N THR A 243 8335 8079 10280 -1753 -177 -621 N ATOM 1939 CA THR A 243 -8.975 13.730 45.277 1.00 66.30 C ANISOU 1939 CA THR A 243 7741 7662 9788 -1756 -375 -641 C ATOM 1940 C THR A 243 -9.463 15.002 45.961 1.00 64.30 C ANISOU 1940 C THR A 243 7344 7486 9601 -1646 -318 -573 C ATOM 1941 O THR A 243 -9.190 16.105 45.473 1.00 66.73 O ANISOU 1941 O THR A 243 7654 7869 9833 -1576 -427 -581 O ATOM 1942 CB THR A 243 -10.027 13.210 44.298 1.00 75.15 C ANISOU 1942 CB THR A 243 8730 8757 11068 -1914 -536 -675 C ATOM 1943 OG1 THR A 243 -9.613 11.942 43.772 1.00 72.68 O ANISOU 1943 OG1 THR A 243 8547 8358 10709 -2016 -575 -744 O ATOM 1944 CG2 THR A 243 -10.205 14.192 43.139 1.00 74.02 C ANISOU 1944 CG2 THR A 243 8528 8708 10890 -1905 -757 -704 C ATOM 1945 N GLN A 244 -10.160 14.879 47.095 1.00 59.90 N ANISOU 1945 N GLN A 244 6666 6912 9183 -1622 -147 -505 N ATOM 1946 CA GLN A 244 -10.515 16.074 47.858 1.00 61.47 C ANISOU 1946 CA GLN A 244 6745 7187 9426 -1494 -79 -449 C ATOM 1947 C GLN A 244 -9.270 16.751 48.420 1.00 67.83 C ANISOU 1947 C GLN A 244 7704 8030 10036 -1336 2 -460 C ATOM 1948 O GLN A 244 -9.197 17.984 48.471 1.00 72.69 O ANISOU 1948 O GLN A 244 8277 8715 10627 -1234 -38 -452 O ATOM 1949 CB GLN A 244 -11.481 15.725 48.991 1.00 55.26 C ANISOU 1949 CB GLN A 244 5798 6382 8814 -1494 99 -374 C ATOM 1950 CG GLN A 244 -12.699 14.947 48.566 1.00 56.53 C ANISOU 1950 CG GLN A 244 5800 6498 9181 -1660 46 -363 C ATOM 1951 CD GLN A 244 -13.348 15.506 47.318 1.00 69.48 C ANISOU 1951 CD GLN A 244 7328 8186 10886 -1731 -191 -404 C ATOM 1952 OE1 GLN A 244 -13.351 14.863 46.267 1.00 82.95 O ANISOU 1952 OE1 GLN A 244 9074 9852 12590 -1854 -337 -467 O ATOM 1953 NE2 GLN A 244 -13.916 16.699 47.429 1.00 71.78 N ANISOU 1953 NE2 GLN A 244 7477 8565 11232 -1645 -232 -372 N ATOM 1954 N LYS A 245 -8.288 15.957 48.857 1.00 70.70 N ANISOU 1954 N LYS A 245 8247 8351 10266 -1311 117 -482 N ATOM 1955 CA LYS A 245 -7.032 16.519 49.340 1.00 63.98 C ANISOU 1955 CA LYS A 245 7547 7542 9219 -1167 188 -509 C ATOM 1956 C LYS A 245 -6.277 17.214 48.215 1.00 75.29 C ANISOU 1956 C LYS A 245 9076 9016 10516 -1167 5 -567 C ATOM 1957 O LYS A 245 -5.727 18.307 48.412 1.00 74.42 O ANISOU 1957 O LYS A 245 8989 8965 10324 -1054 2 -574 O ATOM 1958 CB LYS A 245 -6.169 15.423 49.971 1.00 66.23 C ANISOU 1958 CB LYS A 245 8003 7776 9385 -1143 340 -525 C ATOM 1959 CG LYS A 245 -6.371 15.259 51.476 1.00 78.97 C ANISOU 1959 CG LYS A 245 9569 9393 11042 -1038 574 -463 C ATOM 1960 CD LYS A 245 -5.648 14.028 52.014 1.00 99.88 C ANISOU 1960 CD LYS A 245 12383 11980 13588 -1026 720 -469 C ATOM 1961 CE LYS A 245 -6.569 12.813 52.059 1.00109.82 C ANISOU 1961 CE LYS A 245 13575 13138 15013 -1163 774 -416 C ATOM 1962 NZ LYS A 245 -5.854 11.570 52.469 1.00110.58 N ANISOU 1962 NZ LYS A 245 13849 13157 15011 -1158 902 -420 N ATOM 1963 N ALA A 246 -6.244 16.599 47.028 1.00 70.96 N ANISOU 1963 N ALA A 246 8582 8438 9942 -1291 -149 -609 N ATOM 1964 CA ALA A 246 -5.578 17.231 45.893 1.00 73.40 C ANISOU 1964 CA ALA A 246 8974 8794 10119 -1293 -325 -653 C ATOM 1965 C ALA A 246 -6.199 18.584 45.574 1.00 77.53 C ANISOU 1965 C ALA A 246 9355 9377 10726 -1252 -428 -617 C ATOM 1966 O ALA A 246 -5.481 19.567 45.361 1.00 68.02 O ANISOU 1966 O ALA A 246 8213 8220 9411 -1172 -473 -624 O ATOM 1967 CB ALA A 246 -5.629 16.310 44.672 1.00 61.38 C ANISOU 1967 CB ALA A 246 7507 7240 8576 -1430 -479 -703 C ATOM 1968 N GLU A 247 -7.536 18.656 45.560 1.00 76.13 N ANISOU 1968 N GLU A 247 8984 9195 10747 -1306 -462 -576 N ATOM 1969 CA GLU A 247 -8.213 19.915 45.267 1.00 69.57 C ANISOU 1969 CA GLU A 247 8011 8419 10002 -1260 -562 -539 C ATOM 1970 C GLU A 247 -7.796 21.015 46.236 1.00 74.43 C ANISOU 1970 C GLU A 247 8627 9068 10585 -1105 -449 -513 C ATOM 1971 O GLU A 247 -7.554 22.154 45.821 1.00 70.03 O ANISOU 1971 O GLU A 247 8073 8548 9988 -1042 -540 -507 O ATOM 1972 CB GLU A 247 -9.726 19.721 45.304 1.00 74.24 C ANISOU 1972 CB GLU A 247 8385 9008 10815 -1331 -585 -503 C ATOM 1973 CG GLU A 247 -10.512 21.028 45.305 1.00 90.80 C ANISOU 1973 CG GLU A 247 10320 11164 13015 -1256 -649 -458 C ATOM 1974 CD GLU A 247 -11.608 21.055 46.357 1.00119.49 C ANISOU 1974 CD GLU A 247 13764 14804 16831 -1229 -522 -407 C ATOM 1975 OE1 GLU A 247 -11.752 20.064 47.107 1.00119.16 O ANISOU 1975 OE1 GLU A 247 13718 14720 16839 -1271 -375 -398 O ATOM 1976 OE2 GLU A 247 -12.328 22.073 46.433 1.00134.79 O ANISOU 1976 OE2 GLU A 247 15559 16792 18862 -1162 -566 -373 O ATOM 1977 N LYS A 248 -7.706 20.694 47.530 1.00 69.04 N ANISOU 1977 N LYS A 248 7943 8370 9920 -1038 -252 -499 N ATOM 1978 CA LYS A 248 -7.281 21.691 48.506 1.00 62.92 C ANISOU 1978 CA LYS A 248 7168 7630 9109 -881 -143 -491 C ATOM 1979 C LYS A 248 -5.825 22.098 48.292 1.00 69.88 C ANISOU 1979 C LYS A 248 8238 8525 9787 -820 -158 -543 C ATOM 1980 O LYS A 248 -5.481 23.281 48.426 1.00 63.40 O ANISOU 1980 O LYS A 248 7414 7735 8941 -723 -177 -547 O ATOM 1981 CB LYS A 248 -7.492 21.166 49.924 1.00 58.29 C ANISOU 1981 CB LYS A 248 6540 7037 8571 -816 73 -466 C ATOM 1982 CG LYS A 248 -8.955 20.966 50.282 1.00 87.96 C ANISOU 1982 CG LYS A 248 10087 10795 12538 -857 107 -405 C ATOM 1983 CD LYS A 248 -9.191 21.081 51.781 1.00103.33 C ANISOU 1983 CD LYS A 248 11959 12771 14532 -731 313 -368 C ATOM 1984 CE LYS A 248 -10.680 21.067 52.110 1.00103.30 C ANISOU 1984 CE LYS A 248 11726 12786 14740 -762 339 -303 C ATOM 1985 NZ LYS A 248 -10.964 21.700 53.431 1.00103.46 N ANISOU 1985 NZ LYS A 248 11644 12864 14801 -601 494 -270 N ATOM 1986 N GLU A 249 -4.958 21.138 47.954 1.00 65.63 N ANISOU 1986 N GLU A 249 7863 7964 9109 -876 -151 -587 N ATOM 1987 CA GLU A 249 -3.544 21.452 47.763 1.00 63.87 C ANISOU 1987 CA GLU A 249 7816 7765 8687 -821 -158 -641 C ATOM 1988 C GLU A 249 -3.333 22.317 46.529 1.00 67.11 C ANISOU 1988 C GLU A 249 8243 8201 9055 -853 -347 -641 C ATOM 1989 O GLU A 249 -2.564 23.286 46.566 1.00 67.53 O ANISOU 1989 O GLU A 249 8352 8282 9026 -773 -354 -656 O ATOM 1990 CB GLU A 249 -2.721 20.168 47.654 1.00 68.20 C ANISOU 1990 CB GLU A 249 8530 8289 9094 -871 -112 -688 C ATOM 1991 CG GLU A 249 -1.647 20.038 48.719 1.00 96.41 C ANISOU 1991 CG GLU A 249 12222 11881 12527 -753 58 -727 C ATOM 1992 CD GLU A 249 -0.694 21.223 48.747 1.00111.30 C ANISOU 1992 CD GLU A 249 14166 13821 14303 -654 39 -764 C ATOM 1993 OE1 GLU A 249 0.129 21.363 47.813 1.00117.15 O ANISOU 1993 OE1 GLU A 249 15017 14582 14912 -692 -70 -799 O ATOM 1994 OE2 GLU A 249 -0.773 22.019 49.706 1.00105.14 O ANISOU 1994 OE2 GLU A 249 13314 13064 13570 -539 135 -759 O ATOM 1995 N VAL A 250 -4.002 21.981 45.427 1.00 55.56 N ANISOU 1995 N VAL A 250 6732 6729 7648 -966 -500 -626 N ATOM 1996 CA VAL A 250 -3.870 22.773 44.210 1.00 59.72 C ANISOU 1996 CA VAL A 250 7271 7289 8133 -990 -681 -615 C ATOM 1997 C VAL A 250 -4.378 24.194 44.434 1.00 66.89 C ANISOU 1997 C VAL A 250 8059 8212 9145 -905 -705 -566 C ATOM 1998 O VAL A 250 -3.766 25.168 43.979 1.00 75.26 O ANISOU 1998 O VAL A 250 9173 9292 10132 -860 -772 -558 O ATOM 1999 CB VAL A 250 -4.607 22.083 43.050 1.00 55.64 C ANISOU 1999 CB VAL A 250 6707 6770 7664 -1117 -839 -614 C ATOM 2000 CG1 VAL A 250 -4.584 22.961 41.824 1.00 62.71 C ANISOU 2000 CG1 VAL A 250 7599 7710 8520 -1123 -1023 -591 C ATOM 2001 CG2 VAL A 250 -3.974 20.737 42.757 1.00 58.21 C ANISOU 2001 CG2 VAL A 250 7171 7073 7872 -1193 -829 -673 C ATOM 2002 N THR A 251 -5.498 24.338 45.144 1.00 63.73 N ANISOU 2002 N THR A 251 7493 7801 8919 -880 -647 -531 N ATOM 2003 CA THR A 251 -6.046 25.670 45.372 1.00 62.75 C ANISOU 2003 CA THR A 251 7251 7692 8902 -791 -674 -488 C ATOM 2004 C THR A 251 -5.122 26.496 46.258 1.00 64.48 C ANISOU 2004 C THR A 251 7540 7910 9050 -664 -562 -512 C ATOM 2005 O THR A 251 -4.969 27.704 46.048 1.00 76.04 O ANISOU 2005 O THR A 251 8993 9376 10525 -600 -622 -494 O ATOM 2006 CB THR A 251 -7.451 25.562 45.975 1.00 59.47 C ANISOU 2006 CB THR A 251 6637 7277 8681 -788 -631 -451 C ATOM 2007 OG1 THR A 251 -8.319 24.915 45.035 1.00 61.05 O ANISOU 2007 OG1 THR A 251 6760 7481 8955 -911 -758 -438 O ATOM 2008 CG2 THR A 251 -8.026 26.947 46.312 1.00 45.04 C ANISOU 2008 CG2 THR A 251 4685 5465 6962 -678 -650 -413 C ATOM 2009 N ARG A 252 -4.481 25.859 47.240 1.00 61.37 N ANISOU 2009 N ARG A 252 7222 7513 8584 -624 -400 -554 N ATOM 2010 CA ARG A 252 -3.556 26.583 48.107 1.00 63.79 C ANISOU 2010 CA ARG A 252 7593 7829 8815 -499 -293 -594 C ATOM 2011 C ARG A 252 -2.305 27.009 47.344 1.00 65.60 C ANISOU 2011 C ARG A 252 7977 8064 8884 -511 -369 -627 C ATOM 2012 O ARG A 252 -1.847 28.148 47.481 1.00 63.49 O ANISOU 2012 O ARG A 252 7718 7795 8610 -433 -377 -636 O ATOM 2013 CB ARG A 252 -3.184 25.722 49.315 1.00 62.74 C ANISOU 2013 CB ARG A 252 7504 7704 8631 -446 -103 -633 C ATOM 2014 CG ARG A 252 -2.583 26.496 50.479 1.00 72.70 C ANISOU 2014 CG ARG A 252 8774 8988 9861 -291 24 -677 C ATOM 2015 CD ARG A 252 -2.084 25.550 51.564 1.00 80.78 C ANISOU 2015 CD ARG A 252 9863 10032 10798 -234 206 -716 C ATOM 2016 NE ARG A 252 -1.001 24.703 51.069 1.00 92.37 N ANISOU 2016 NE ARG A 252 11508 11499 12088 -294 200 -760 N ATOM 2017 CZ ARG A 252 0.288 24.897 51.332 1.00 89.12 C ANISOU 2017 CZ ARG A 252 11226 11118 11516 -226 250 -833 C ATOM 2018 NH1 ARG A 252 0.669 25.905 52.104 1.00107.62 N ANISOU 2018 NH1 ARG A 252 13543 13489 13860 -99 309 -875 N ATOM 2019 NH2 ARG A 252 1.199 24.076 50.828 1.00 69.87 N ANISOU 2019 NH2 ARG A 252 8943 8687 8917 -284 237 -871 N ATOM 2020 N MET A 253 -1.749 26.112 46.524 1.00 58.23 N ANISOU 2020 N MET A 253 7162 7138 7826 -607 -425 -646 N ATOM 2021 CA MET A 253 -0.561 26.458 45.750 1.00 60.05 C ANISOU 2021 CA MET A 253 7534 7387 7895 -622 -496 -672 C ATOM 2022 C MET A 253 -0.853 27.552 44.728 1.00 64.65 C ANISOU 2022 C MET A 253 8072 7966 8526 -640 -655 -615 C ATOM 2023 O MET A 253 -0.026 28.445 44.517 1.00 74.44 O ANISOU 2023 O MET A 253 9378 9210 9697 -602 -676 -620 O ATOM 2024 CB MET A 253 0.004 25.213 45.060 1.00 50.43 C ANISOU 2024 CB MET A 253 6443 6184 6532 -715 -530 -705 C ATOM 2025 CG MET A 253 0.719 24.259 46.013 1.00 68.15 C ANISOU 2025 CG MET A 253 8784 8434 8675 -678 -369 -769 C ATOM 2026 SD MET A 253 2.105 25.044 46.874 1.00 76.37 S ANISOU 2026 SD MET A 253 9920 9510 9587 -550 -251 -835 S ATOM 2027 CE MET A 253 3.006 25.732 45.489 1.00 34.97 C ANISOU 2027 CE MET A 253 4774 4296 4218 -605 -408 -831 C ATOM 2028 N VAL A 254 -2.017 27.504 44.082 1.00 60.71 N ANISOU 2028 N VAL A 254 7460 7462 8146 -696 -766 -559 N ATOM 2029 CA VAL A 254 -2.334 28.519 43.083 1.00 62.89 C ANISOU 2029 CA VAL A 254 7695 7740 8462 -703 -919 -497 C ATOM 2030 C VAL A 254 -2.449 29.892 43.734 1.00 65.31 C ANISOU 2030 C VAL A 254 7933 8015 8866 -593 -881 -475 C ATOM 2031 O VAL A 254 -1.993 30.900 43.178 1.00 65.92 O ANISOU 2031 O VAL A 254 8050 8080 8915 -570 -952 -444 O ATOM 2032 CB VAL A 254 -3.612 28.133 42.319 1.00 61.22 C ANISOU 2032 CB VAL A 254 7365 7539 8358 -775 -1044 -453 C ATOM 2033 CG1 VAL A 254 -4.212 29.349 41.612 1.00 50.21 C ANISOU 2033 CG1 VAL A 254 5887 6145 7046 -742 -1177 -381 C ATOM 2034 CG2 VAL A 254 -3.304 27.024 41.316 1.00 48.02 C ANISOU 2034 CG2 VAL A 254 5784 5897 6566 -883 -1131 -479 C ATOM 2035 N ILE A 255 -3.041 29.955 44.929 1.00 50.39 N ANISOU 2035 N ILE A 255 5941 6111 7093 -521 -765 -491 N ATOM 2036 CA ILE A 255 -3.142 31.233 45.627 1.00 60.64 C ANISOU 2036 CA ILE A 255 7174 7381 8485 -405 -725 -484 C ATOM 2037 C ILE A 255 -1.753 31.759 45.974 1.00 68.58 C ANISOU 2037 C ILE A 255 8308 8375 9373 -353 -658 -540 C ATOM 2038 O ILE A 255 -1.454 32.942 45.772 1.00 74.06 O ANISOU 2038 O ILE A 255 9011 9035 10094 -306 -704 -522 O ATOM 2039 CB ILE A 255 -4.045 31.090 46.870 1.00 59.60 C ANISOU 2039 CB ILE A 255 6905 7252 8487 -331 -608 -496 C ATOM 2040 CG1 ILE A 255 -5.498 30.869 46.436 1.00 59.30 C ANISOU 2040 CG1 ILE A 255 6714 7226 8591 -378 -695 -435 C ATOM 2041 CG2 ILE A 255 -3.946 32.322 47.774 1.00 57.23 C ANISOU 2041 CG2 ILE A 255 6557 6928 8260 -192 -545 -517 C ATOM 2042 CD1 ILE A 255 -6.447 30.617 47.582 1.00 62.72 C ANISOU 2042 CD1 ILE A 255 7002 7675 9155 -319 -579 -436 C ATOM 2043 N ILE A 256 -0.871 30.880 46.463 1.00 63.09 N ANISOU 2043 N ILE A 256 7717 7707 8547 -362 -551 -608 N ATOM 2044 CA ILE A 256 0.495 31.287 46.794 1.00 55.57 C ANISOU 2044 CA ILE A 256 6884 6759 7473 -315 -485 -674 C ATOM 2045 C ILE A 256 1.236 31.768 45.551 1.00 57.64 C ANISOU 2045 C ILE A 256 7242 7016 7640 -382 -607 -642 C ATOM 2046 O ILE A 256 1.957 32.773 45.594 1.00 57.18 O ANISOU 2046 O ILE A 256 7223 6935 7570 -340 -605 -656 O ATOM 2047 CB ILE A 256 1.244 30.134 47.488 1.00 56.09 C ANISOU 2047 CB ILE A 256 7042 6866 7404 -310 -354 -751 C ATOM 2048 CG1 ILE A 256 0.612 29.831 48.849 1.00 48.51 C ANISOU 2048 CG1 ILE A 256 5986 5912 6533 -219 -212 -777 C ATOM 2049 CG2 ILE A 256 2.740 30.459 47.632 1.00 44.36 C ANISOU 2049 CG2 ILE A 256 5687 5402 5768 -277 -305 -825 C ATOM 2050 CD1 ILE A 256 0.993 28.468 49.399 1.00 51.55 C ANISOU 2050 CD1 ILE A 256 6446 6332 6810 -228 -94 -822 C ATOM 2051 N MET A 257 1.059 31.078 44.419 1.00 52.43 N ANISOU 2051 N MET A 257 6621 6382 6918 -486 -716 -598 N ATOM 2052 CA MET A 257 1.786 31.452 43.206 1.00 53.04 C ANISOU 2052 CA MET A 257 6793 6473 6886 -544 -827 -561 C ATOM 2053 C MET A 257 1.359 32.821 42.679 1.00 65.01 C ANISOU 2053 C MET A 257 8246 7942 8513 -517 -925 -479 C ATOM 2054 O MET A 257 2.213 33.656 42.356 1.00 75.30 O ANISOU 2054 O MET A 257 9617 9228 9765 -508 -941 -467 O ATOM 2055 CB MET A 257 1.618 30.383 42.127 1.00 40.45 C ANISOU 2055 CB MET A 257 5245 4926 5201 -648 -927 -539 C ATOM 2056 CG MET A 257 2.440 29.109 42.403 1.00 50.76 C ANISOU 2056 CG MET A 257 6664 6273 6349 -680 -845 -621 C ATOM 2057 SD MET A 257 2.306 27.856 41.107 1.00 68.29 S ANISOU 2057 SD MET A 257 8945 8543 8459 -796 -972 -611 S ATOM 2058 CE MET A 257 0.552 27.475 41.117 1.00 64.30 C ANISOU 2058 CE MET A 257 8271 8006 8154 -828 -1027 -568 C ATOM 2059 N VAL A 258 0.047 33.079 42.578 1.00 61.29 N ANISOU 2059 N VAL A 258 7642 7448 8195 -502 -990 -421 N ATOM 2060 CA VAL A 258 -0.366 34.356 41.995 1.00 67.35 C ANISOU 2060 CA VAL A 258 8360 8171 9060 -470 -1091 -337 C ATOM 2061 C VAL A 258 -0.136 35.500 42.977 1.00 67.25 C ANISOU 2061 C VAL A 258 8316 8092 9145 -367 -1008 -364 C ATOM 2062 O VAL A 258 0.216 36.611 42.566 1.00 68.26 O ANISOU 2062 O VAL A 258 8470 8168 9296 -344 -1057 -318 O ATOM 2063 CB VAL A 258 -1.827 34.323 41.487 1.00 68.30 C ANISOU 2063 CB VAL A 258 8348 8298 9304 -479 -1201 -268 C ATOM 2064 CG1 VAL A 258 -2.068 33.100 40.605 1.00 58.14 C ANISOU 2064 CG1 VAL A 258 7083 7078 7928 -581 -1281 -264 C ATOM 2065 CG2 VAL A 258 -2.835 34.404 42.626 1.00 72.65 C ANISOU 2065 CG2 VAL A 258 8756 8829 10019 -406 -1124 -292 C ATOM 2066 N ILE A 259 -0.294 35.258 44.281 1.00 55.32 N ANISOU 2066 N ILE A 259 6751 6579 7690 -299 -879 -440 N ATOM 2067 CA ILE A 259 0.066 36.286 45.254 1.00 56.48 C ANISOU 2067 CA ILE A 259 6878 6672 7910 -195 -797 -490 C ATOM 2068 C ILE A 259 1.560 36.585 45.185 1.00 66.24 C ANISOU 2068 C ILE A 259 8248 7901 9020 -211 -756 -540 C ATOM 2069 O ILE A 259 1.980 37.748 45.258 1.00 64.23 O ANISOU 2069 O ILE A 259 8003 7580 8821 -167 -763 -540 O ATOM 2070 CB ILE A 259 -0.360 35.862 46.669 1.00 55.16 C ANISOU 2070 CB ILE A 259 6628 6525 7804 -110 -662 -566 C ATOM 2071 CG1 ILE A 259 -1.888 35.929 46.799 1.00 59.58 C ANISOU 2071 CG1 ILE A 259 7031 7083 8525 -77 -703 -510 C ATOM 2072 CG2 ILE A 259 0.349 36.727 47.717 1.00 46.28 C ANISOU 2072 CG2 ILE A 259 5513 5365 6706 -2 -563 -651 C ATOM 2073 CD1 ILE A 259 -2.386 35.785 48.217 1.00 56.04 C ANISOU 2073 CD1 ILE A 259 6482 6653 8157 27 -572 -570 C ATOM 2074 N ALA A 260 2.384 35.543 45.032 1.00 59.82 N ANISOU 2074 N ALA A 260 7538 7152 8038 -275 -715 -586 N ATOM 2075 CA ALA A 260 3.826 35.746 44.933 1.00 53.57 C ANISOU 2075 CA ALA A 260 6869 6372 7113 -294 -676 -639 C ATOM 2076 C ALA A 260 4.189 36.513 43.667 1.00 60.61 C ANISOU 2076 C ALA A 260 7814 7234 7980 -357 -795 -547 C ATOM 2077 O ALA A 260 5.095 37.356 43.678 1.00 64.09 O ANISOU 2077 O ALA A 260 8307 7639 8407 -348 -775 -565 O ATOM 2078 CB ALA A 260 4.553 34.403 44.973 1.00 48.84 C ANISOU 2078 CB ALA A 260 6368 5857 6332 -343 -616 -703 C ATOM 2079 N PHE A 261 3.486 36.241 42.567 1.00 50.51 N ANISOU 2079 N PHE A 261 6521 5972 6698 -419 -917 -448 N ATOM 2080 CA PHE A 261 3.722 37.002 41.345 1.00 57.25 C ANISOU 2080 CA PHE A 261 7419 6804 7531 -464 -1031 -345 C ATOM 2081 C PHE A 261 3.331 38.466 41.522 1.00 73.56 C ANISOU 2081 C PHE A 261 9417 8763 9767 -396 -1055 -292 C ATOM 2082 O PHE A 261 4.047 39.365 41.061 1.00 65.03 O ANISOU 2082 O PHE A 261 8395 7635 8677 -409 -1076 -249 O ATOM 2083 CB PHE A 261 2.953 36.373 40.187 1.00 51.92 C ANISOU 2083 CB PHE A 261 6729 6181 6818 -527 -1161 -259 C ATOM 2084 CG PHE A 261 3.089 37.117 38.896 1.00 68.15 C ANISOU 2084 CG PHE A 261 8823 8227 8843 -558 -1281 -141 C ATOM 2085 CD1 PHE A 261 2.185 38.112 38.550 1.00 81.84 C ANISOU 2085 CD1 PHE A 261 10476 9896 10722 -512 -1365 -43 C ATOM 2086 CD2 PHE A 261 4.115 36.818 38.023 1.00 74.31 C ANISOU 2086 CD2 PHE A 261 9720 9069 9445 -626 -1310 -122 C ATOM 2087 CE1 PHE A 261 2.311 38.797 37.357 1.00 82.29 C ANISOU 2087 CE1 PHE A 261 10574 9947 10747 -532 -1471 77 C ATOM 2088 CE2 PHE A 261 4.241 37.494 36.832 1.00 76.51 C ANISOU 2088 CE2 PHE A 261 10034 9348 9689 -649 -1413 -2 C ATOM 2089 CZ PHE A 261 3.340 38.486 36.495 1.00 76.82 C ANISOU 2089 CZ PHE A 261 9997 9318 9873 -601 -1492 102 C ATOM 2090 N LEU A 262 2.199 38.726 42.185 1.00 59.94 N ANISOU 2090 N LEU A 262 7571 6999 8203 -321 -1050 -294 N ATOM 2091 CA LEU A 262 1.786 40.104 42.421 1.00 60.16 C ANISOU 2091 CA LEU A 262 7535 6923 8398 -242 -1073 -254 C ATOM 2092 C LEU A 262 2.778 40.833 43.319 1.00 66.04 C ANISOU 2092 C LEU A 262 8318 7608 9168 -194 -969 -345 C ATOM 2093 O LEU A 262 3.136 41.984 43.042 1.00 70.12 O ANISOU 2093 O LEU A 262 8857 8034 9750 -181 -999 -302 O ATOM 2094 CB LEU A 262 0.376 40.142 43.015 1.00 53.76 C ANISOU 2094 CB LEU A 262 6581 6101 7743 -165 -1083 -250 C ATOM 2095 CG LEU A 262 -0.720 39.667 42.050 1.00 59.16 C ANISOU 2095 CG LEU A 262 7207 6834 8437 -206 -1206 -155 C ATOM 2096 CD1 LEU A 262 -2.097 39.644 42.708 1.00 50.78 C ANISOU 2096 CD1 LEU A 262 5992 5775 7528 -133 -1205 -161 C ATOM 2097 CD2 LEU A 262 -0.734 40.510 40.783 1.00 54.95 C ANISOU 2097 CD2 LEU A 262 6712 6263 7905 -227 -1336 -29 C ATOM 2098 N ILE A 263 3.246 40.184 44.390 1.00 65.57 N ANISOU 2098 N ILE A 263 8264 7596 9055 -165 -847 -472 N ATOM 2099 CA ILE A 263 4.231 40.826 45.263 1.00 69.08 C ANISOU 2099 CA ILE A 263 8739 7998 9512 -114 -750 -578 C ATOM 2100 C ILE A 263 5.500 41.166 44.487 1.00 65.00 C ANISOU 2100 C ILE A 263 8338 7470 8888 -197 -768 -558 C ATOM 2101 O ILE A 263 6.195 42.139 44.800 1.00 68.81 O ANISOU 2101 O ILE A 263 8838 7879 9429 -174 -735 -599 O ATOM 2102 CB ILE A 263 4.538 39.928 46.481 1.00 75.90 C ANISOU 2102 CB ILE A 263 9595 8939 10306 -63 -617 -716 C ATOM 2103 CG1 ILE A 263 3.306 39.766 47.370 1.00 69.43 C ANISOU 2103 CG1 ILE A 263 8647 8122 9610 32 -584 -733 C ATOM 2104 CG2 ILE A 263 5.674 40.498 47.316 1.00 73.12 C ANISOU 2104 CG2 ILE A 263 9279 8564 9939 -13 -523 -840 C ATOM 2105 CD1 ILE A 263 3.548 38.842 48.551 1.00 67.35 C ANISOU 2105 CD1 ILE A 263 8377 7939 9273 89 -447 -850 C ATOM 2106 N CYS A 264 5.805 40.400 43.446 1.00 73.92 N ANISOU 2106 N CYS A 264 9545 8675 9866 -296 -822 -495 N ATOM 2107 CA CYS A 264 7.058 40.593 42.731 1.00 60.59 C ANISOU 2107 CA CYS A 264 7966 7001 8054 -374 -827 -479 C ATOM 2108 C CYS A 264 6.989 41.752 41.737 1.00 56.45 C ANISOU 2108 C CYS A 264 7453 6387 7608 -403 -923 -342 C ATOM 2109 O CYS A 264 7.944 42.527 41.622 1.00 66.15 O ANISOU 2109 O CYS A 264 8732 7564 8837 -429 -897 -345 O ATOM 2110 CB CYS A 264 7.441 39.298 42.015 1.00 50.19 C ANISOU 2110 CB CYS A 264 6730 5809 6533 -456 -848 -470 C ATOM 2111 SG CYS A 264 8.990 39.399 41.113 1.00 63.27 S ANISOU 2111 SG CYS A 264 8515 7514 8010 -549 -851 -451 S ATOM 2112 N TRP A 265 5.882 41.889 41.003 1.00 60.42 N ANISOU 2112 N TRP A 265 7907 6870 8178 -398 -1031 -220 N ATOM 2113 CA TRP A 265 5.823 42.824 39.889 1.00 66.98 C ANISOU 2113 CA TRP A 265 8765 7636 9049 -426 -1128 -71 C ATOM 2114 C TRP A 265 4.837 43.970 40.060 1.00 70.21 C ANISOU 2114 C TRP A 265 9088 7919 9669 -343 -1177 -6 C ATOM 2115 O TRP A 265 4.990 44.990 39.377 1.00 66.36 O ANISOU 2115 O TRP A 265 8630 7344 9238 -351 -1229 104 O ATOM 2116 CB TRP A 265 5.496 42.080 38.583 1.00 68.30 C ANISOU 2116 CB TRP A 265 8967 7902 9083 -490 -1235 38 C ATOM 2117 CG TRP A 265 6.637 41.225 38.121 1.00 87.13 C ANISOU 2117 CG TRP A 265 11456 10396 11253 -575 -1207 4 C ATOM 2118 CD1 TRP A 265 6.723 39.862 38.181 1.00 85.33 C ANISOU 2118 CD1 TRP A 265 11254 10286 10883 -608 -1190 -71 C ATOM 2119 CD2 TRP A 265 7.872 41.681 37.555 1.00 94.94 C ANISOU 2119 CD2 TRP A 265 12539 11388 12148 -635 -1188 40 C ATOM 2120 NE1 TRP A 265 7.931 39.442 37.672 1.00 82.35 N ANISOU 2120 NE1 TRP A 265 10981 9988 10320 -677 -1168 -86 N ATOM 2121 CE2 TRP A 265 8.654 40.539 37.284 1.00 90.79 C ANISOU 2121 CE2 TRP A 265 12089 10995 11412 -696 -1165 -19 C ATOM 2122 CE3 TRP A 265 8.388 42.942 37.242 1.00 94.26 C ANISOU 2122 CE3 TRP A 265 12477 11200 12136 -644 -1188 119 C ATOM 2123 CZ2 TRP A 265 9.925 40.623 36.718 1.00 99.38 C ANISOU 2123 CZ2 TRP A 265 13270 12133 12358 -761 -1141 -3 C ATOM 2124 CZ3 TRP A 265 9.648 43.022 36.681 1.00 98.06 C ANISOU 2124 CZ3 TRP A 265 13049 11724 12485 -719 -1159 141 C ATOM 2125 CH2 TRP A 265 10.402 41.871 36.424 1.00100.21 C ANISOU 2125 CH2 TRP A 265 13389 12144 12542 -775 -1137 79 C ATOM 2126 N LEU A 266 3.845 43.848 40.937 1.00 75.51 N ANISOU 2126 N LEU A 266 9657 8579 10455 -260 -1160 -65 N ATOM 2127 CA LEU A 266 2.882 44.935 41.090 1.00 77.41 C ANISOU 2127 CA LEU A 266 9814 8708 10891 -171 -1212 -6 C ATOM 2128 C LEU A 266 3.521 46.242 41.556 1.00 79.97 C ANISOU 2128 C LEU A 266 10158 8890 11337 -132 -1167 -32 C ATOM 2129 O LEU A 266 3.135 47.302 41.031 1.00 70.77 O ANISOU 2129 O LEU A 266 8986 7616 10288 -102 -1239 78 O ATOM 2130 CB LEU A 266 1.753 44.501 42.035 1.00 64.76 C ANISOU 2130 CB LEU A 266 8090 7136 9379 -86 -1188 -77 C ATOM 2131 CG LEU A 266 0.414 45.206 41.863 1.00 69.13 C ANISOU 2131 CG LEU A 266 8542 7631 10092 -3 -1279 8 C ATOM 2132 CD1 LEU A 266 -0.141 44.919 40.474 1.00 66.89 C ANISOU 2132 CD1 LEU A 266 8272 7402 9742 -56 -1408 150 C ATOM 2133 CD2 LEU A 266 -0.560 44.775 42.951 1.00 66.31 C ANISOU 2133 CD2 LEU A 266 8060 7314 9821 81 -1231 -78 C ATOM 2134 N PRO A 267 4.474 46.258 42.503 1.00 79.16 N ANISOU 2134 N PRO A 267 10079 8777 11222 -128 -1056 -173 N ATOM 2135 CA PRO A 267 5.114 47.542 42.848 1.00 73.71 C ANISOU 2135 CA PRO A 267 9406 7942 10657 -103 -1025 -200 C ATOM 2136 C PRO A 267 5.826 48.204 41.677 1.00 69.73 C ANISOU 2136 C PRO A 267 8995 7375 10124 -192 -1074 -67 C ATOM 2137 O PRO A 267 5.721 49.424 41.510 1.00 85.51 O ANISOU 2137 O PRO A 267 10991 9226 12274 -162 -1107 0 O ATOM 2138 CB PRO A 267 6.088 47.152 43.969 1.00 73.02 C ANISOU 2138 CB PRO A 267 9330 7901 10512 -96 -899 -386 C ATOM 2139 CG PRO A 267 5.478 45.942 44.585 1.00 68.45 C ANISOU 2139 CG PRO A 267 8698 7451 9860 -57 -862 -458 C ATOM 2140 CD PRO A 267 4.876 45.187 43.438 1.00 68.20 C ANISOU 2140 CD PRO A 267 8686 7498 9730 -125 -953 -323 C ATOM 2141 N TYR A 268 6.551 47.437 40.859 1.00 77.23 N ANISOU 2141 N TYR A 268 10027 8433 10883 -296 -1077 -24 N ATOM 2142 CA TYR A 268 7.188 48.010 39.675 1.00 72.13 C ANISOU 2142 CA TYR A 268 9465 7746 10194 -378 -1123 119 C ATOM 2143 C TYR A 268 6.152 48.554 38.705 1.00 77.84 C ANISOU 2143 C TYR A 268 10171 8416 10989 -346 -1242 302 C ATOM 2144 O TYR A 268 6.317 49.650 38.154 1.00 85.52 O ANISOU 2144 O TYR A 268 11176 9264 12052 -352 -1273 418 O ATOM 2145 CB TYR A 268 8.055 46.959 38.980 1.00 80.89 C ANISOU 2145 CB TYR A 268 10658 9009 11067 -482 -1110 127 C ATOM 2146 CG TYR A 268 9.533 47.170 39.173 1.00 92.45 C ANISOU 2146 CG TYR A 268 12187 10469 12468 -552 -1021 54 C ATOM 2147 CD1 TYR A 268 10.077 48.451 39.158 1.00 85.94 C ANISOU 2147 CD1 TYR A 268 11379 9496 11778 -568 -1000 91 C ATOM 2148 CD2 TYR A 268 10.389 46.092 39.385 1.00 87.01 C ANISOU 2148 CD2 TYR A 268 11543 9924 11593 -603 -956 -55 C ATOM 2149 CE1 TYR A 268 11.434 48.653 39.340 1.00 83.56 C ANISOU 2149 CE1 TYR A 268 11125 9194 11428 -639 -917 17 C ATOM 2150 CE2 TYR A 268 11.747 46.284 39.571 1.00 83.07 C ANISOU 2150 CE2 TYR A 268 11095 9434 11032 -664 -875 -130 C ATOM 2151 CZ TYR A 268 12.267 47.568 39.549 1.00 82.98 C ANISOU 2151 CZ TYR A 268 11090 9280 11161 -686 -855 -95 C ATOM 2152 OH TYR A 268 13.622 47.772 39.734 1.00 75.38 O ANISOU 2152 OH TYR A 268 10167 8329 10146 -754 -774 -175 O ATOM 2153 N ALA A 269 5.083 47.794 38.468 1.00 77.59 N ANISOU 2153 N ALA A 269 10086 8476 10917 -312 -1310 331 N ATOM 2154 CA ALA A 269 4.039 48.258 37.566 1.00 78.28 C ANISOU 2154 CA ALA A 269 10146 8532 11064 -269 -1430 492 C ATOM 2155 C ALA A 269 3.296 49.449 38.158 1.00 79.92 C ANISOU 2155 C ALA A 269 10285 8580 11501 -161 -1444 501 C ATOM 2156 O ALA A 269 2.929 50.382 37.433 1.00 75.27 O ANISOU 2156 O ALA A 269 9711 7896 10994 -129 -1517 646 O ATOM 2157 CB ALA A 269 3.077 47.112 37.249 1.00 60.02 C ANISOU 2157 CB ALA A 269 7779 6363 8661 -262 -1497 496 C ATOM 2158 N GLY A 270 3.084 49.446 39.475 1.00 69.11 N ANISOU 2158 N GLY A 270 8843 7181 10233 -94 -1373 347 N ATOM 2159 CA GLY A 270 2.369 50.549 40.096 1.00 67.91 C ANISOU 2159 CA GLY A 270 8622 6885 10295 20 -1387 339 C ATOM 2160 C GLY A 270 3.171 51.835 40.076 1.00 75.59 C ANISOU 2160 C GLY A 270 9656 7682 11382 11 -1362 368 C ATOM 2161 O GLY A 270 2.663 52.894 39.696 1.00 78.87 O ANISOU 2161 O GLY A 270 10068 7965 11934 70 -1426 479 O ATOM 2162 N VAL A 271 4.439 51.756 40.481 1.00 86.22 N ANISOU 2162 N VAL A 271 11059 9024 12676 -62 -1267 269 N ATOM 2163 CA VAL A 271 5.308 52.930 40.475 1.00 81.54 C ANISOU 2163 CA VAL A 271 10522 8265 12195 -90 -1234 284 C ATOM 2164 C VAL A 271 5.473 53.471 39.059 1.00 80.25 C ANISOU 2164 C VAL A 271 10440 8047 12004 -153 -1303 500 C ATOM 2165 O VAL A 271 5.420 54.685 38.835 1.00 85.93 O ANISOU 2165 O VAL A 271 11179 8590 12880 -125 -1328 589 O ATOM 2166 CB VAL A 271 6.663 52.582 41.119 1.00 75.40 C ANISOU 2166 CB VAL A 271 9780 7527 11339 -166 -1121 128 C ATOM 2167 CG1 VAL A 271 7.674 53.698 40.887 1.00 85.60 C ANISOU 2167 CG1 VAL A 271 11136 8662 12727 -229 -1090 161 C ATOM 2168 CG2 VAL A 271 6.478 52.311 42.608 1.00 62.92 C ANISOU 2168 CG2 VAL A 271 8117 5971 9817 -76 -1051 -83 C ATOM 2169 N ALA A 272 5.670 52.583 38.079 1.00 80.17 N ANISOU 2169 N ALA A 272 10480 8188 11794 -233 -1335 591 N ATOM 2170 CA ALA A 272 5.813 53.039 36.699 1.00 74.80 C ANISOU 2170 CA ALA A 272 9875 7480 11065 -281 -1400 803 C ATOM 2171 C ALA A 272 4.539 53.711 36.208 1.00 86.68 C ANISOU 2171 C ALA A 272 11342 8907 12686 -176 -1507 945 C ATOM 2172 O ALA A 272 4.596 54.751 35.537 1.00 93.69 O ANISOU 2172 O ALA A 272 12279 9660 13658 -168 -1540 1099 O ATOM 2173 CB ALA A 272 6.190 51.871 35.786 1.00 63.42 C ANISOU 2173 CB ALA A 272 8485 6237 9375 -368 -1421 855 C ATOM 2174 N PHE A 273 3.378 53.133 36.538 1.00 75.26 N ANISOU 2174 N PHE A 273 9807 7543 11245 -93 -1559 897 N ATOM 2175 CA PHE A 273 2.101 53.734 36.159 1.00 72.61 C ANISOU 2175 CA PHE A 273 9420 7150 11018 19 -1663 1012 C ATOM 2176 C PHE A 273 1.921 55.102 36.810 1.00 89.08 C ANISOU 2176 C PHE A 273 11488 9017 13341 106 -1648 1001 C ATOM 2177 O PHE A 273 1.462 56.053 36.164 1.00 81.57 O ANISOU 2177 O PHE A 273 10560 7950 12484 166 -1717 1155 O ATOM 2178 CB PHE A 273 0.955 52.793 36.548 1.00 68.09 C ANISOU 2178 CB PHE A 273 8740 6717 10415 82 -1706 933 C ATOM 2179 CG PHE A 273 -0.414 53.294 36.165 1.00 92.25 C ANISOU 2179 CG PHE A 273 11731 9748 13572 201 -1818 1037 C ATOM 2180 CD1 PHE A 273 -1.087 54.210 36.966 1.00 98.39 C ANISOU 2180 CD1 PHE A 273 12442 10390 14553 321 -1820 996 C ATOM 2181 CD2 PHE A 273 -1.042 52.829 35.018 1.00 97.09 C ANISOU 2181 CD2 PHE A 273 12342 10481 14068 202 -1924 1166 C ATOM 2182 CE1 PHE A 273 -2.342 54.672 36.617 1.00 95.62 C ANISOU 2182 CE1 PHE A 273 12026 10020 14284 438 -1924 1088 C ATOM 2183 CE2 PHE A 273 -2.303 53.284 34.666 1.00 96.80 C ANISOU 2183 CE2 PHE A 273 12235 10429 14113 318 -2029 1255 C ATOM 2184 CZ PHE A 273 -2.952 54.207 35.468 1.00 97.51 C ANISOU 2184 CZ PHE A 273 12262 10383 14405 437 -2028 1218 C ATOM 2185 N TYR A 274 2.263 55.212 38.096 1.00 87.79 N ANISOU 2185 N TYR A 274 11285 8798 13275 125 -1561 816 N ATOM 2186 CA TYR A 274 2.107 56.475 38.810 1.00 81.65 C ANISOU 2186 CA TYR A 274 10483 7813 12726 214 -1548 776 C ATOM 2187 C TYR A 274 3.018 57.548 38.225 1.00 96.55 C ANISOU 2187 C TYR A 274 12473 9525 14688 150 -1530 888 C ATOM 2188 O TYR A 274 2.592 58.685 37.996 1.00 95.52 O ANISOU 2188 O TYR A 274 12356 9219 14719 223 -1578 991 O ATOM 2189 CB TYR A 274 2.394 56.262 40.299 1.00 81.22 C ANISOU 2189 CB TYR A 274 10365 7762 12733 245 -1456 540 C ATOM 2190 CG TYR A 274 2.205 57.487 41.163 1.00101.78 C ANISOU 2190 CG TYR A 274 12933 10166 15571 350 -1445 464 C ATOM 2191 CD1 TYR A 274 0.960 57.799 41.702 1.00109.29 C ANISOU 2191 CD1 TYR A 274 13789 11093 16645 501 -1498 435 C ATOM 2192 CD2 TYR A 274 3.272 58.327 41.454 1.00112.17 C ANISOU 2192 CD2 TYR A 274 14305 11322 16990 299 -1383 412 C ATOM 2193 CE1 TYR A 274 0.785 58.920 42.498 1.00115.81 C ANISOU 2193 CE1 TYR A 274 14583 11738 17683 607 -1493 357 C ATOM 2194 CE2 TYR A 274 3.106 59.449 42.247 1.00121.49 C ANISOU 2194 CE2 TYR A 274 15454 12314 18393 397 -1379 330 C ATOM 2195 CZ TYR A 274 1.863 59.741 42.768 1.00126.81 C ANISOU 2195 CZ TYR A 274 16038 12965 19179 555 -1436 302 C ATOM 2196 OH TYR A 274 1.703 60.857 43.558 1.00135.56 O ANISOU 2196 OH TYR A 274 17116 13887 20506 662 -1437 212 O ATOM 2197 N ILE A 275 4.283 57.199 37.974 1.00 90.94 N ANISOU 2197 N ILE A 275 11835 8857 13861 14 -1459 874 N ATOM 2198 CA ILE A 275 5.208 58.136 37.341 1.00 91.33 C ANISOU 2198 CA ILE A 275 11978 8755 13968 -66 -1433 993 C ATOM 2199 C ILE A 275 4.708 58.527 35.954 1.00 84.27 C ANISOU 2199 C ILE A 275 11141 7840 13039 -52 -1524 1251 C ATOM 2200 O ILE A 275 4.818 59.687 35.541 1.00 85.06 O ANISOU 2200 O ILE A 275 11294 7749 13277 -39 -1535 1382 O ATOM 2201 CB ILE A 275 6.625 57.529 37.292 1.00 87.63 C ANISOU 2201 CB ILE A 275 11565 8379 13352 -216 -1340 926 C ATOM 2202 CG1 ILE A 275 7.216 57.469 38.701 1.00 80.43 C ANISOU 2202 CG1 ILE A 275 10604 7442 12514 -216 -1247 676 C ATOM 2203 CG2 ILE A 275 7.531 58.315 36.358 1.00 59.62 C ANISOU 2203 CG2 ILE A 275 8115 4718 9820 -315 -1319 1093 C ATOM 2204 CD1 ILE A 275 8.521 56.738 38.789 1.00 77.39 C ANISOU 2204 CD1 ILE A 275 10258 7178 11971 -343 -1157 580 C ATOM 2205 N PHE A 276 4.137 57.569 35.220 1.00 88.30 N ANISOU 2205 N PHE A 276 11640 8544 13367 -47 -1590 1325 N ATOM 2206 CA PHE A 276 3.641 57.850 33.876 1.00 84.74 C ANISOU 2206 CA PHE A 276 11236 8103 12856 -20 -1683 1562 C ATOM 2207 C PHE A 276 2.486 58.846 33.913 1.00 96.01 C ANISOU 2207 C PHE A 276 12627 9383 14469 129 -1761 1643 C ATOM 2208 O PHE A 276 2.483 59.837 33.176 1.00 94.85 O ANISOU 2208 O PHE A 276 12546 9095 14399 154 -1792 1826 O ATOM 2209 CB PHE A 276 3.212 56.545 33.197 1.00 74.63 C ANISOU 2209 CB PHE A 276 9935 7073 11346 -36 -1745 1587 C ATOM 2210 CG PHE A 276 2.978 56.670 31.715 1.00 83.24 C ANISOU 2210 CG PHE A 276 11086 8218 12325 -27 -1831 1821 C ATOM 2211 CD1 PHE A 276 1.800 57.222 31.223 1.00 90.75 C ANISOU 2211 CD1 PHE A 276 12007 9126 13346 102 -1936 1950 C ATOM 2212 CD2 PHE A 276 3.928 56.220 30.813 1.00 78.24 C ANISOU 2212 CD2 PHE A 276 10534 7691 11502 -138 -1807 1909 C ATOM 2213 CE1 PHE A 276 1.582 57.334 29.859 1.00 84.24 C ANISOU 2213 CE1 PHE A 276 11236 8363 12406 124 -2016 2164 C ATOM 2214 CE2 PHE A 276 3.715 56.327 29.449 1.00 91.58 C ANISOU 2214 CE2 PHE A 276 12276 9445 13076 -117 -1886 2125 C ATOM 2215 CZ PHE A 276 2.540 56.885 28.971 1.00 92.99 C ANISOU 2215 CZ PHE A 276 12426 9579 13325 16 -1990 2253 C ATOM 2216 N THR A 277 1.489 58.594 34.768 1.00105.98 N ANISOU 2216 N THR A 277 13785 10679 15805 234 -1793 1512 N ATOM 2217 CA THR A 277 0.312 59.454 34.843 1.00105.81 C ANISOU 2217 CA THR A 277 13715 10541 15946 388 -1874 1573 C ATOM 2218 C THR A 277 0.557 60.730 35.644 1.00117.96 C ANISOU 2218 C THR A 277 15266 11825 17728 438 -1828 1519 C ATOM 2219 O THR A 277 -0.170 61.711 35.456 1.00122.22 O ANISOU 2219 O THR A 277 15807 12220 18411 555 -1892 1619 O ATOM 2220 CB THR A 277 -0.866 58.683 35.444 1.00 97.17 C ANISOU 2220 CB THR A 277 12494 9593 14835 482 -1923 1454 C ATOM 2221 OG1 THR A 277 -0.500 58.170 36.732 1.00108.00 O ANISOU 2221 OG1 THR A 277 13807 10996 16231 454 -1832 1228 O ATOM 2222 CG2 THR A 277 -1.265 57.522 34.537 1.00 92.29 C ANISOU 2222 CG2 THR A 277 11859 9206 13999 445 -1989 1522 C ATOM 2223 N HIS A 278 1.552 60.739 36.532 1.00120.71 N ANISOU 2223 N HIS A 278 15622 12117 18125 359 -1724 1356 N ATOM 2224 CA HIS A 278 1.962 61.954 37.228 1.00105.74 C ANISOU 2224 CA HIS A 278 13746 9972 16459 386 -1679 1296 C ATOM 2225 C HIS A 278 3.366 62.349 36.784 1.00122.16 C ANISOU 2225 C HIS A 278 15930 11954 18532 235 -1601 1358 C ATOM 2226 O HIS A 278 4.286 62.422 37.609 1.00115.83 O ANISOU 2226 O HIS A 278 15124 11097 17788 166 -1512 1193 O ATOM 2227 CB HIS A 278 1.935 61.767 38.751 1.00 87.44 C ANISOU 2227 CB HIS A 278 11336 7658 14230 436 -1623 1032 C ATOM 2228 CG HIS A 278 0.590 61.403 39.306 1.00100.48 C ANISOU 2228 CG HIS A 278 12873 9407 15899 582 -1684 960 C ATOM 2229 ND1 HIS A 278 -0.114 60.290 38.893 1.00102.23 N ANISOU 2229 ND1 HIS A 278 13045 9852 15947 588 -1731 995 N ATOM 2230 CD2 HIS A 278 -0.165 61.989 40.265 1.00103.60 C ANISOU 2230 CD2 HIS A 278 13187 9710 16466 728 -1703 849 C ATOM 2231 CE1 HIS A 278 -1.250 60.216 39.562 1.00 98.68 C ANISOU 2231 CE1 HIS A 278 12486 9443 15566 724 -1773 916 C ATOM 2232 NE2 HIS A 278 -1.306 61.235 40.401 1.00111.94 N ANISOU 2232 NE2 HIS A 278 14144 10939 17447 815 -1757 828 N ATOM 2233 N GLN A 279 3.549 62.580 35.483 1.00135.04 N ANISOU 2233 N GLN A 279 17648 13573 20086 186 -1633 1592 N ATOM 2234 CA GLN A 279 4.850 62.995 34.970 1.00143.02 C ANISOU 2234 CA GLN A 279 18755 14494 21093 42 -1557 1677 C ATOM 2235 C GLN A 279 5.160 64.404 35.459 1.00144.72 C ANISOU 2235 C GLN A 279 18998 14408 21579 60 -1523 1665 C ATOM 2236 O GLN A 279 4.455 65.359 35.116 1.00139.79 O ANISOU 2236 O GLN A 279 18398 13617 21097 163 -1585 1803 O ATOM 2237 CB GLN A 279 4.874 62.932 33.445 1.00147.04 C ANISOU 2237 CB GLN A 279 19347 15070 21452 5 -1602 1945 C ATOM 2238 CG GLN A 279 5.304 61.582 32.878 1.00147.13 C ANISOU 2238 CG GLN A 279 19364 15356 21182 -92 -1592 1945 C ATOM 2239 CD GLN A 279 6.773 61.278 33.122 1.00147.71 C ANISOU 2239 CD GLN A 279 19474 15458 21193 -254 -1478 1850 C ATOM 2240 OE1 GLN A 279 7.566 62.174 33.413 1.00146.13 O ANISOU 2240 OE1 GLN A 279 19309 15065 21148 -316 -1407 1840 O ATOM 2241 NE2 GLN A 279 7.142 60.007 33.004 1.00149.56 N ANISOU 2241 NE2 GLN A 279 19696 15930 21199 -324 -1461 1776 N ATOM 2242 N GLY A 280 6.208 64.527 36.266 1.00145.27 N ANISOU 2242 N GLY A 280 19062 14411 21723 -35 -1427 1494 N ATOM 2243 CA GLY A 280 6.530 65.790 36.896 1.00140.10 C ANISOU 2243 CA GLY A 280 18418 13474 21338 -21 -1394 1433 C ATOM 2244 C GLY A 280 6.257 65.770 38.385 1.00131.38 C ANISOU 2244 C GLY A 280 17215 12349 20353 67 -1381 1153 C ATOM 2245 O GLY A 280 5.364 66.472 38.871 1.00106.81 O ANISOU 2245 O GLY A 280 14066 9102 17414 213 -1438 1121 O ATOM 2246 N SER A 281 7.011 64.953 39.118 1.00139.61 N ANISOU 2246 N SER A 281 18215 13536 21296 -9 -1306 948 N ATOM 2247 CA SER A 281 6.901 64.904 40.569 1.00136.57 C ANISOU 2247 CA SER A 281 17737 13147 21008 72 -1280 673 C ATOM 2248 C SER A 281 8.189 64.331 41.144 1.00132.07 C ANISOU 2248 C SER A 281 17156 12672 20353 -55 -1176 489 C ATOM 2249 O SER A 281 8.984 63.701 40.440 1.00123.75 O ANISOU 2249 O SER A 281 16153 11743 19122 -191 -1134 566 O ATOM 2250 CB SER A 281 5.684 64.088 41.020 1.00134.09 C ANISOU 2250 CB SER A 281 17335 13013 20601 212 -1337 604 C ATOM 2251 OG SER A 281 4.506 64.881 40.995 1.00123.71 O ANISOU 2251 OG SER A 281 15998 11566 19440 366 -1425 682 O ATOM 2252 N ASP A 282 8.379 64.566 42.438 1.00129.88 N ANISOU 2252 N ASP A 282 16808 12341 20198 3 -1139 240 N ATOM 2253 CA ASP A 282 9.607 64.210 43.137 1.00118.60 C ANISOU 2253 CA ASP A 282 15360 10977 18726 -95 -1043 36 C ATOM 2254 C ASP A 282 9.536 62.756 43.592 1.00108.84 C ANISOU 2254 C ASP A 282 14072 10031 17250 -78 -1014 -88 C ATOM 2255 O ASP A 282 8.637 62.387 44.357 1.00104.92 O ANISOU 2255 O ASP A 282 13499 9614 16751 61 -1041 -195 O ATOM 2256 CB ASP A 282 9.811 65.144 44.329 1.00120.38 C ANISOU 2256 CB ASP A 282 15530 11016 19192 -24 -1023 -184 C ATOM 2257 CG ASP A 282 11.084 64.858 45.092 1.00124.66 C ANISOU 2257 CG ASP A 282 16043 11620 19700 -113 -928 -411 C ATOM 2258 OD1 ASP A 282 11.128 63.857 45.839 1.00132.69 O ANISOU 2258 OD1 ASP A 282 17001 12852 20563 -70 -892 -581 O ATOM 2259 OD2 ASP A 282 12.035 65.652 44.963 1.00131.30 O ANISOU 2259 OD2 ASP A 282 16918 12293 20675 -223 -888 -422 O ATOM 2260 N PHE A 283 10.490 61.940 43.131 1.00100.57 N ANISOU 2260 N PHE A 283 13066 9140 16006 -217 -955 -72 N ATOM 2261 CA PHE A 283 10.594 60.527 43.492 1.00 90.69 C ANISOU 2261 CA PHE A 283 11782 8158 14519 -219 -919 -184 C ATOM 2262 C PHE A 283 12.004 60.257 43.997 1.00 90.41 C ANISOU 2262 C PHE A 283 11748 8183 14420 -323 -820 -358 C ATOM 2263 O PHE A 283 12.948 60.202 43.202 1.00 97.22 O ANISOU 2263 O PHE A 283 12676 9064 15199 -469 -785 -264 O ATOM 2264 CB PHE A 283 10.264 59.626 42.302 1.00102.54 C ANISOU 2264 CB PHE A 283 13335 9823 15801 -275 -959 20 C ATOM 2265 CG PHE A 283 8.862 59.786 41.796 1.00129.93 C ANISOU 2265 CG PHE A 283 16793 13264 19312 -168 -1060 180 C ATOM 2266 CD1 PHE A 283 7.804 59.170 42.445 1.00138.15 C ANISOU 2266 CD1 PHE A 283 17753 14414 20323 -41 -1092 96 C ATOM 2267 CD2 PHE A 283 8.598 60.559 40.676 1.00133.39 C ANISOU 2267 CD2 PHE A 283 17296 13570 19817 -191 -1120 417 C ATOM 2268 CE1 PHE A 283 6.510 59.321 41.987 1.00142.05 C ANISOU 2268 CE1 PHE A 283 18225 14891 20855 57 -1187 234 C ATOM 2269 CE2 PHE A 283 7.305 60.715 40.211 1.00137.13 C ANISOU 2269 CE2 PHE A 283 17755 14027 20322 -83 -1216 558 C ATOM 2270 CZ PHE A 283 6.259 60.095 40.867 1.00142.32 C ANISOU 2270 CZ PHE A 283 18325 14799 20952 39 -1252 461 C ATOM 2271 N GLY A 284 12.145 60.063 45.308 1.00 82.91 N ANISOU 2271 N GLY A 284 10722 7280 13499 -242 -775 -611 N ATOM 2272 CA GLY A 284 13.446 59.937 45.927 1.00 83.00 C ANISOU 2272 CA GLY A 284 10722 7337 13476 -316 -686 -805 C ATOM 2273 C GLY A 284 14.169 58.637 45.622 1.00 88.18 C ANISOU 2273 C GLY A 284 11409 8240 13853 -407 -632 -818 C ATOM 2274 O GLY A 284 13.603 57.694 45.059 1.00 82.97 O ANISOU 2274 O GLY A 284 10775 7734 13017 -401 -662 -700 O ATOM 2275 N PRO A 285 15.451 58.564 46.012 1.00 80.07 N ANISOU 2275 N PRO A 285 10380 7258 12785 -489 -552 -972 N ATOM 2276 CA PRO A 285 16.256 57.365 45.722 1.00 73.40 C ANISOU 2276 CA PRO A 285 9570 6648 11672 -575 -498 -992 C ATOM 2277 C PRO A 285 15.790 56.120 46.456 1.00 84.31 C ANISOU 2277 C PRO A 285 10914 8241 12878 -467 -480 -1114 C ATOM 2278 O PRO A 285 15.640 55.055 45.849 1.00105.80 O ANISOU 2278 O PRO A 285 13678 11131 15389 -499 -488 -1016 O ATOM 2279 CB PRO A 285 17.662 57.769 46.181 1.00 76.36 C ANISOU 2279 CB PRO A 285 9929 6997 12088 -662 -420 -1164 C ATOM 2280 CG PRO A 285 17.432 58.840 47.206 1.00 77.83 C ANISOU 2280 CG PRO A 285 10043 6994 12534 -566 -427 -1325 C ATOM 2281 CD PRO A 285 16.225 59.595 46.723 1.00 75.83 C ANISOU 2281 CD PRO A 285 9803 6558 12448 -506 -513 -1140 C ATOM 2282 N ILE A 286 15.576 56.242 47.767 1.00 90.49 N ANISOU 2282 N ILE A 286 11617 9018 13746 -337 -454 -1328 N ATOM 2283 CA ILE A 286 15.186 55.087 48.572 1.00103.32 C ANISOU 2283 CA ILE A 286 13203 10841 15212 -228 -421 -1451 C ATOM 2284 C ILE A 286 13.779 54.622 48.203 1.00 96.15 C ANISOU 2284 C ILE A 286 12291 9964 14276 -156 -489 -1296 C ATOM 2285 O ILE A 286 13.505 53.415 48.152 1.00 84.26 O ANISOU 2285 O ILE A 286 10796 8640 12578 -142 -475 -1280 O ATOM 2286 CB ILE A 286 15.326 55.424 50.070 1.00101.85 C ANISOU 2286 CB ILE A 286 12929 10641 15129 -95 -374 -1716 C ATOM 2287 CG1 ILE A 286 16.807 55.571 50.426 1.00 96.09 C ANISOU 2287 CG1 ILE A 286 12200 9941 14369 -172 -302 -1889 C ATOM 2288 CG2 ILE A 286 14.682 54.358 50.939 1.00106.22 C ANISOU 2288 CG2 ILE A 286 13434 11374 15549 44 -344 -1815 C ATOM 2289 CD1 ILE A 286 17.056 56.001 51.849 1.00102.73 C ANISOU 2289 CD1 ILE A 286 12952 10764 15317 -44 -261 -2162 C ATOM 2290 N PHE A 287 12.874 55.563 47.910 1.00 73.45 N ANISOU 2290 N PHE A 287 9400 6913 11593 -111 -563 -1179 N ATOM 2291 CA PHE A 287 11.552 55.188 47.412 1.00 80.74 C ANISOU 2291 CA PHE A 287 10318 7866 12494 -55 -636 -1017 C ATOM 2292 C PHE A 287 11.639 54.370 46.126 1.00 79.42 C ANISOU 2292 C PHE A 287 10230 7812 12134 -174 -664 -826 C ATOM 2293 O PHE A 287 10.811 53.477 45.906 1.00 76.44 O ANISOU 2293 O PHE A 287 9842 7556 11645 -138 -696 -759 O ATOM 2294 CB PHE A 287 10.705 56.444 47.188 1.00 80.81 C ANISOU 2294 CB PHE A 287 10308 7657 12741 4 -715 -913 C ATOM 2295 CG PHE A 287 9.500 56.228 46.304 1.00 94.60 C ANISOU 2295 CG PHE A 287 12064 9416 14463 28 -804 -701 C ATOM 2296 CD1 PHE A 287 8.291 55.817 46.844 1.00102.49 C ANISOU 2296 CD1 PHE A 287 12987 10483 15471 160 -833 -726 C ATOM 2297 CD2 PHE A 287 9.570 56.464 44.936 1.00104.55 C ANISOU 2297 CD2 PHE A 287 13403 10625 15695 -78 -857 -478 C ATOM 2298 CE1 PHE A 287 7.179 55.629 46.036 1.00103.30 C ANISOU 2298 CE1 PHE A 287 13088 10603 15557 181 -918 -543 C ATOM 2299 CE2 PHE A 287 8.463 56.275 44.124 1.00110.99 C ANISOU 2299 CE2 PHE A 287 14223 11463 16485 -47 -944 -294 C ATOM 2300 CZ PHE A 287 7.267 55.859 44.675 1.00104.72 C ANISOU 2300 CZ PHE A 287 13349 10737 15704 81 -977 -332 C ATOM 2301 N MET A 288 12.621 54.659 45.264 1.00 77.82 N ANISOU 2301 N MET A 288 11586 7583 10399 959 -2309 775 N ATOM 2302 CA MET A 288 12.754 53.940 43.999 1.00 75.53 C ANISOU 2302 CA MET A 288 11378 7301 10020 774 -2294 820 C ATOM 2303 C MET A 288 13.342 52.547 44.171 1.00 82.50 C ANISOU 2303 C MET A 288 12190 8281 10875 698 -2128 775 C ATOM 2304 O MET A 288 13.185 51.709 43.276 1.00 89.56 O ANISOU 2304 O MET A 288 13108 9211 11709 575 -2113 808 O ATOM 2305 CB MET A 288 13.618 54.738 43.022 1.00 72.31 C ANISOU 2305 CB MET A 288 11160 6779 9534 631 -2339 850 C ATOM 2306 CG MET A 288 12.976 56.033 42.532 1.00 81.87 C ANISOU 2306 CG MET A 288 12466 7885 10756 668 -2524 912 C ATOM 2307 SD MET A 288 11.808 55.797 41.179 1.00 87.57 S ANISOU 2307 SD MET A 288 13234 8607 11431 585 -2654 1007 S ATOM 2308 CE MET A 288 12.924 55.180 39.926 1.00102.89 C ANISOU 2308 CE MET A 288 15310 10539 13243 333 -2569 1023 C ATOM 2309 N THR A 289 14.012 52.282 45.290 1.00 75.62 N ANISOU 2309 N THR A 289 11235 7451 10046 768 -2006 701 N ATOM 2310 CA THR A 289 14.560 50.961 45.555 1.00 93.60 C ANISOU 2310 CA THR A 289 13438 9819 12305 708 -1850 653 C ATOM 2311 C THR A 289 13.541 50.011 46.187 1.00 90.88 C ANISOU 2311 C THR A 289 12921 9590 12020 805 -1831 652 C ATOM 2312 O THR A 289 13.846 48.821 46.347 1.00 72.62 O ANISOU 2312 O THR A 289 10541 7356 9694 754 -1716 621 O ATOM 2313 CB THR A 289 15.811 51.077 46.449 1.00 95.55 C ANISOU 2313 CB THR A 289 13678 10058 12567 730 -1724 573 C ATOM 2314 OG1 THR A 289 15.464 51.682 47.700 1.00100.27 O ANISOU 2314 OG1 THR A 289 14177 10664 13258 915 -1742 541 O ATOM 2315 CG2 THR A 289 16.886 51.933 45.769 1.00 77.89 C ANISOU 2315 CG2 THR A 289 11614 7716 10264 615 -1737 577 C ATOM 2316 N ILE A 290 12.345 50.495 46.525 1.00 77.98 N ANISOU 2316 N ILE A 290 11214 7968 10447 940 -1943 686 N ATOM 2317 CA ILE A 290 11.282 49.650 47.078 1.00 83.79 C ANISOU 2317 CA ILE A 290 11785 8819 11234 1030 -1938 695 C ATOM 2318 C ILE A 290 10.807 48.636 46.036 1.00 90.63 C ANISOU 2318 C ILE A 290 12665 9727 12044 901 -1949 747 C ATOM 2319 O ILE A 290 10.800 47.428 46.327 1.00 73.66 O ANISOU 2319 O ILE A 290 10419 7670 9898 878 -1855 727 O ATOM 2320 CB ILE A 290 10.110 50.494 47.614 1.00 84.95 C ANISOU 2320 CB ILE A 290 11856 8968 11452 1204 -2065 720 C ATOM 2321 CG1 ILE A 290 10.492 51.194 48.920 1.00 86.66 C ANISOU 2321 CG1 ILE A 290 12010 9181 11738 1356 -2030 655 C ATOM 2322 CG2 ILE A 290 8.866 49.634 47.819 1.00 70.11 C ANISOU 2322 CG2 ILE A 290 9828 7204 9605 1263 -2088 752 C ATOM 2323 CD1 ILE A 290 9.471 52.236 49.368 1.00 66.70 C ANISOU 2323 CD1 ILE A 290 9434 6636 9274 1526 -2168 672 C ATOM 2324 N PRO A 291 10.407 49.042 44.820 1.00 81.34 N ANISOU 2324 N PRO A 291 11605 8486 10815 814 -2061 813 N ATOM 2325 CA PRO A 291 10.034 48.019 43.830 1.00 66.70 C ANISOU 2325 CA PRO A 291 9766 6674 8904 686 -2062 857 C ATOM 2326 C PRO A 291 11.206 47.146 43.410 1.00 73.32 C ANISOU 2326 C PRO A 291 10663 7522 9674 532 -1933 817 C ATOM 2327 O PRO A 291 10.994 46.003 42.982 1.00 78.93 O ANISOU 2327 O PRO A 291 11338 8296 10355 453 -1894 828 O ATOM 2328 CB PRO A 291 9.480 48.843 42.659 1.00 64.19 C ANISOU 2328 CB PRO A 291 9575 6272 8544 630 -2214 932 C ATOM 2329 CG PRO A 291 10.142 50.161 42.784 1.00 71.22 C ANISOU 2329 CG PRO A 291 10568 7057 9436 658 -2252 917 C ATOM 2330 CD PRO A 291 10.273 50.404 44.262 1.00 72.30 C ANISOU 2330 CD PRO A 291 10585 7229 9658 822 -2195 853 C ATOM 2331 N ALA A 292 12.439 47.651 43.522 1.00 84.82 N ANISOU 2331 N ALA A 292 12206 8918 11104 490 -1867 770 N ATOM 2332 CA ALA A 292 13.615 46.816 43.288 1.00 67.85 C ANISOU 2332 CA ALA A 292 10096 6788 8895 362 -1732 719 C ATOM 2333 C ALA A 292 13.769 45.774 44.384 1.00 65.16 C ANISOU 2333 C ALA A 292 9606 6545 8608 427 -1608 658 C ATOM 2334 O ALA A 292 14.100 44.614 44.108 1.00 63.58 O ANISOU 2334 O ALA A 292 9387 6400 8372 335 -1525 637 O ATOM 2335 CB ALA A 292 14.868 47.683 43.201 1.00 69.16 C ANISOU 2335 CB ALA A 292 10385 6869 9022 309 -1697 685 C ATOM 2336 N PHE A 293 13.529 46.173 45.637 1.00 59.14 N ANISOU 2336 N PHE A 293 8736 5806 7930 588 -1597 629 N ATOM 2337 CA PHE A 293 13.580 45.230 46.750 1.00 53.15 C ANISOU 2337 CA PHE A 293 7824 5144 7227 660 -1488 577 C ATOM 2338 C PHE A 293 12.606 44.067 46.542 1.00 69.01 C ANISOU 2338 C PHE A 293 9735 7243 9243 644 -1503 615 C ATOM 2339 O PHE A 293 12.968 42.901 46.742 1.00 71.99 O ANISOU 2339 O PHE A 293 10055 7686 9614 593 -1403 581 O ATOM 2340 CB PHE A 293 13.303 45.991 48.054 1.00 70.89 C ANISOU 2340 CB PHE A 293 9973 7401 9563 844 -1499 550 C ATOM 2341 CG PHE A 293 12.760 45.145 49.178 1.00 98.05 C ANISOU 2341 CG PHE A 293 13227 10956 13072 951 -1440 527 C ATOM 2342 CD1 PHE A 293 13.615 44.510 50.064 1.00 97.65 C ANISOU 2342 CD1 PHE A 293 13109 10951 13043 962 -1301 456 C ATOM 2343 CD2 PHE A 293 11.390 45.023 49.375 1.00107.41 C ANISOU 2343 CD2 PHE A 293 14304 12206 14301 1043 -1528 578 C ATOM 2344 CE1 PHE A 293 13.111 43.745 51.109 1.00101.91 C ANISOU 2344 CE1 PHE A 293 13478 11599 13645 1057 -1252 439 C ATOM 2345 CE2 PHE A 293 10.885 44.254 50.414 1.00106.32 C ANISOU 2345 CE2 PHE A 293 13992 12181 14224 1137 -1477 561 C ATOM 2346 CZ PHE A 293 11.746 43.615 51.281 1.00 94.13 C ANISOU 2346 CZ PHE A 293 12385 10681 12700 1142 -1340 493 C ATOM 2347 N PHE A 294 11.376 44.359 46.104 1.00 83.26 N ANISOU 2347 N PHE A 294 11526 9051 11059 681 -1632 686 N ATOM 2348 CA PHE A 294 10.368 43.308 45.972 1.00 78.77 C ANISOU 2348 CA PHE A 294 10856 8571 10502 676 -1655 727 C ATOM 2349 C PHE A 294 10.692 42.362 44.823 1.00 78.09 C ANISOU 2349 C PHE A 294 10851 8484 10337 501 -1629 741 C ATOM 2350 O PHE A 294 10.609 41.136 44.976 1.00 76.08 O ANISOU 2350 O PHE A 294 10516 8305 10084 466 -1566 730 O ATOM 2351 CB PHE A 294 8.975 43.923 45.799 1.00 72.43 C ANISOU 2351 CB PHE A 294 10016 7772 9730 764 -1802 799 C ATOM 2352 CG PHE A 294 8.322 44.294 47.100 1.00 76.59 C ANISOU 2352 CG PHE A 294 10396 8360 10347 950 -1816 784 C ATOM 2353 CD1 PHE A 294 7.831 43.308 47.947 1.00 71.75 C ANISOU 2353 CD1 PHE A 294 9616 7864 9781 1010 -1761 775 C ATOM 2354 CD2 PHE A 294 8.224 45.620 47.493 1.00 70.86 C ANISOU 2354 CD2 PHE A 294 9693 7574 9655 1063 -1885 778 C ATOM 2355 CE1 PHE A 294 7.247 43.640 49.155 1.00 66.94 C ANISOU 2355 CE1 PHE A 294 8865 7321 9249 1179 -1771 760 C ATOM 2356 CE2 PHE A 294 7.638 45.960 48.700 1.00 62.93 C ANISOU 2356 CE2 PHE A 294 8549 6632 8731 1238 -1897 759 C ATOM 2357 CZ PHE A 294 7.149 44.970 49.532 1.00 68.13 C ANISOU 2357 CZ PHE A 294 9039 7415 9431 1296 -1838 750 C ATOM 2358 N ALA A 295 11.065 42.911 43.661 1.00 57.42 N ANISOU 2358 N ALA A 295 8392 5781 7645 389 -1679 767 N ATOM 2359 CA ALA A 295 11.337 42.067 42.498 1.00 55.75 C ANISOU 2359 CA ALA A 295 8262 5569 7351 224 -1663 781 C ATOM 2360 C ALA A 295 12.579 41.194 42.702 1.00 72.35 C ANISOU 2360 C ALA A 295 10369 7696 9423 145 -1516 703 C ATOM 2361 O ALA A 295 12.601 40.027 42.288 1.00 59.04 O ANISOU 2361 O ALA A 295 8667 6060 7707 58 -1475 697 O ATOM 2362 CB ALA A 295 11.491 42.938 41.255 1.00 47.85 C ANISOU 2362 CB ALA A 295 7429 4476 6277 125 -1751 825 C ATOM 2363 N LYS A 296 13.620 41.737 43.340 1.00 65.41 N ANISOU 2363 N LYS A 296 9514 6783 8553 174 -1437 641 N ATOM 2364 CA LYS A 296 14.878 41.010 43.454 1.00 63.61 C ANISOU 2364 CA LYS A 296 9307 6572 8290 93 -1300 565 C ATOM 2365 C LYS A 296 14.815 39.904 44.496 1.00 67.25 C ANISOU 2365 C LYS A 296 9617 7124 8812 156 -1209 521 C ATOM 2366 O LYS A 296 15.497 38.880 44.343 1.00 57.60 O ANISOU 2366 O LYS A 296 8395 5933 7556 70 -1119 474 O ATOM 2367 CB LYS A 296 16.021 41.976 43.787 1.00 72.54 C ANISOU 2367 CB LYS A 296 10515 7637 9409 100 -1248 516 C ATOM 2368 CG LYS A 296 16.652 42.639 42.575 1.00 55.04 C ANISOU 2368 CG LYS A 296 8472 5342 7099 -32 -1285 535 C ATOM 2369 CD LYS A 296 17.569 43.759 42.988 1.00 59.91 C ANISOU 2369 CD LYS A 296 9156 5890 7716 -4 -1259 501 C ATOM 2370 CE LYS A 296 17.963 44.603 41.785 1.00 69.26 C ANISOU 2370 CE LYS A 296 10509 6992 8812 -124 -1327 541 C ATOM 2371 NZ LYS A 296 18.522 45.910 42.230 1.00 80.60 N ANISOU 2371 NZ LYS A 296 12005 8352 10267 -72 -1344 530 N ATOM 2372 N THR A 297 14.023 40.088 45.558 1.00 57.63 N ANISOU 2372 N THR A 297 8267 5948 7681 305 -1233 534 N ATOM 2373 CA THR A 297 13.895 39.042 46.571 1.00 67.39 C ANISOU 2373 CA THR A 297 9353 7277 8976 365 -1154 500 C ATOM 2374 C THR A 297 13.218 37.791 46.017 1.00 69.51 C ANISOU 2374 C THR A 297 9577 7605 9227 292 -1176 536 C ATOM 2375 O THR A 297 13.295 36.726 46.641 1.00 52.54 O ANISOU 2375 O THR A 297 7327 5527 7109 301 -1104 505 O ATOM 2376 CB THR A 297 13.135 39.591 47.783 1.00 60.00 C ANISOU 2376 CB THR A 297 8286 6380 8132 540 -1185 511 C ATOM 2377 OG1 THR A 297 13.687 40.866 48.138 1.00 66.18 O ANISOU 2377 OG1 THR A 297 9128 7093 8926 603 -1187 485 O ATOM 2378 CG2 THR A 297 13.260 38.667 48.980 1.00 50.17 C ANISOU 2378 CG2 THR A 297 6892 5224 6946 604 -1085 465 C ATOM 2379 N SER A 298 12.587 37.888 44.845 1.00 62.75 N ANISOU 2379 N SER A 298 8800 6722 8321 217 -1276 600 N ATOM 2380 CA SER A 298 12.029 36.717 44.191 1.00 52.89 C ANISOU 2380 CA SER A 298 7529 5521 7047 134 -1300 633 C ATOM 2381 C SER A 298 13.088 35.704 43.778 1.00 65.04 C ANISOU 2381 C SER A 298 9119 7064 8529 8 -1201 571 C ATOM 2382 O SER A 298 12.723 34.578 43.431 1.00 66.18 O ANISOU 2382 O SER A 298 9227 7255 8662 -52 -1206 584 O ATOM 2383 CB SER A 298 11.228 37.135 42.961 1.00 55.10 C ANISOU 2383 CB SER A 298 7896 5760 7278 74 -1428 711 C ATOM 2384 OG SER A 298 12.091 37.454 41.886 1.00 45.82 O ANISOU 2384 OG SER A 298 6881 4513 6015 -53 -1420 696 O ATOM 2385 N ALA A 299 14.379 36.065 43.778 1.00 59.85 N ANISOU 2385 N ALA A 299 8545 6360 7834 -35 -1116 504 N ATOM 2386 CA ALA A 299 15.407 35.057 43.522 1.00 51.81 C ANISOU 2386 CA ALA A 299 7560 5357 6770 -140 -1015 435 C ATOM 2387 C ALA A 299 15.536 34.086 44.684 1.00 56.31 C ANISOU 2387 C ALA A 299 7991 5997 7406 -77 -928 387 C ATOM 2388 O ALA A 299 16.110 33.005 44.517 1.00 55.46 O ANISOU 2388 O ALA A 299 7884 5916 7272 -154 -861 339 O ATOM 2389 CB ALA A 299 16.764 35.708 43.242 1.00 49.93 C ANISOU 2389 CB ALA A 299 7442 5057 6471 -202 -946 376 C ATOM 2390 N VAL A 300 15.017 34.449 45.851 1.00 52.14 N ANISOU 2390 N VAL A 300 7346 5502 6962 62 -930 399 N ATOM 2391 CA VAL A 300 14.949 33.550 46.989 1.00 55.97 C ANISOU 2391 CA VAL A 300 7687 6063 7516 128 -863 368 C ATOM 2392 C VAL A 300 13.584 32.876 47.092 1.00 64.06 C ANISOU 2392 C VAL A 300 8599 7157 8582 163 -942 439 C ATOM 2393 O VAL A 300 13.501 31.653 47.225 1.00 55.62 O ANISOU 2393 O VAL A 300 7465 6142 7524 125 -913 429 O ATOM 2394 CB VAL A 300 15.299 34.307 48.286 1.00 55.10 C ANISOU 2394 CB VAL A 300 7508 5957 7472 258 -806 330 C ATOM 2395 CG1 VAL A 300 15.281 33.353 49.480 1.00 49.14 C ANISOU 2395 CG1 VAL A 300 6602 5283 6784 321 -732 297 C ATOM 2396 CG2 VAL A 300 16.647 34.994 48.144 1.00 52.12 C ANISOU 2396 CG2 VAL A 300 7245 5508 7050 218 -732 264 C ATOM 2397 N TYR A 301 12.491 33.652 47.023 1.00 53.36 N ANISOU 2397 N TYR A 301 7220 5803 7251 235 -1048 512 N ATOM 2398 CA TYR A 301 11.196 33.060 47.351 1.00 63.48 C ANISOU 2398 CA TYR A 301 8372 7164 8582 288 -1114 576 C ATOM 2399 C TYR A 301 10.545 32.324 46.182 1.00 66.74 C ANISOU 2399 C TYR A 301 8829 7581 8947 180 -1192 632 C ATOM 2400 O TYR A 301 9.702 31.458 46.427 1.00 66.22 O ANISOU 2400 O TYR A 301 8657 7589 8915 192 -1224 673 O ATOM 2401 CB TYR A 301 10.229 34.103 47.952 1.00 50.75 C ANISOU 2401 CB TYR A 301 6687 5570 7025 429 -1191 626 C ATOM 2402 CG TYR A 301 9.803 35.301 47.108 1.00 48.98 C ANISOU 2402 CG TYR A 301 6568 5275 6768 431 -1296 674 C ATOM 2403 CD1 TYR A 301 8.987 35.152 45.996 1.00 64.97 C ANISOU 2403 CD1 TYR A 301 8645 7289 8752 360 -1399 744 C ATOM 2404 CD2 TYR A 301 10.142 36.591 47.491 1.00 49.91 C ANISOU 2404 CD2 TYR A 301 6725 5339 6902 513 -1300 653 C ATOM 2405 CE1 TYR A 301 8.575 36.254 45.250 1.00 44.62 C ANISOU 2405 CE1 TYR A 301 6162 4645 6147 364 -1499 790 C ATOM 2406 CE2 TYR A 301 9.731 37.695 46.760 1.00 45.90 C ANISOU 2406 CE2 TYR A 301 6311 4762 6368 519 -1404 699 C ATOM 2407 CZ TYR A 301 8.952 37.518 45.637 1.00 53.00 C ANISOU 2407 CZ TYR A 301 7263 5649 7224 443 -1502 768 C ATOM 2408 OH TYR A 301 8.551 38.611 44.900 1.00 57.27 O ANISOU 2408 OH TYR A 301 7900 6119 7739 445 -1609 815 O ATOM 2409 N ASN A 302 10.927 32.603 44.927 1.00 60.38 N ANISOU 2409 N ASN A 302 8175 6705 8063 70 -1222 636 N ATOM 2410 CA ASN A 302 10.440 31.756 43.836 1.00 54.75 C ANISOU 2410 CA ASN A 302 7504 5999 7301 -41 -1282 678 C ATOM 2411 C ASN A 302 10.951 30.321 43.938 1.00 58.17 C ANISOU 2411 C ASN A 302 7902 6473 7729 -113 -1207 630 C ATOM 2412 O ASN A 302 10.130 29.393 43.828 1.00 61.84 O ANISOU 2412 O ASN A 302 8297 6990 8210 -133 -1255 674 O ATOM 2413 CB ASN A 302 10.770 32.380 42.477 1.00 43.56 C ANISOU 2413 CB ASN A 302 6255 4500 5797 -145 -1328 690 C ATOM 2414 CG ASN A 302 9.734 33.401 42.049 1.00 61.90 C ANISOU 2414 CG ASN A 302 8601 6795 8122 -98 -1452 773 C ATOM 2415 OD1 ASN A 302 8.610 33.399 42.549 1.00 59.94 O ANISOU 2415 OD1 ASN A 302 8243 6599 7933 -9 -1516 828 O ATOM 2416 ND2 ASN A 302 10.103 34.277 41.124 1.00 64.38 N ANISOU 2416 ND2 ASN A 302 9057 7032 8373 -160 -1489 781 N ATOM 2417 N PRO A 303 12.250 30.051 44.127 1.00 66.81 N ANISOU 2417 N PRO A 303 9039 7544 8800 -156 -1097 542 N ATOM 2418 CA PRO A 303 12.663 28.646 44.294 1.00 60.49 C ANISOU 2418 CA PRO A 303 8196 6786 8003 -213 -1035 495 C ATOM 2419 C PRO A 303 12.118 27.995 45.561 1.00 57.07 C ANISOU 2419 C PRO A 303 7593 6432 7658 -121 -1015 506 C ATOM 2420 O PRO A 303 11.985 26.768 45.594 1.00 59.69 O ANISOU 2420 O PRO A 303 7873 6805 8000 -167 -1009 502 O ATOM 2421 CB PRO A 303 14.199 28.719 44.307 1.00 70.94 C ANISOU 2421 CB PRO A 303 9601 8066 9285 -261 -921 395 C ATOM 2422 CG PRO A 303 14.527 30.145 44.632 1.00 65.55 C ANISOU 2422 CG PRO A 303 8959 7339 8609 -191 -908 390 C ATOM 2423 CD PRO A 303 13.416 30.959 44.055 1.00 62.54 C ANISOU 2423 CD PRO A 303 8602 6939 8222 -167 -1031 481 C ATOM 2424 N VAL A 304 11.794 28.759 46.605 1.00 53.47 N ANISOU 2424 N VAL A 304 7049 6002 7266 7 -1008 520 N ATOM 2425 CA VAL A 304 11.117 28.157 47.749 1.00 54.35 C ANISOU 2425 CA VAL A 304 6993 6201 7457 92 -1004 543 C ATOM 2426 C VAL A 304 9.739 27.647 47.333 1.00 69.99 C ANISOU 2426 C VAL A 304 8914 8231 9446 80 -1116 636 C ATOM 2427 O VAL A 304 9.348 26.522 47.663 1.00 63.08 O ANISOU 2427 O VAL A 304 7948 7419 8601 62 -1119 653 O ATOM 2428 CB VAL A 304 11.023 29.162 48.914 1.00 53.44 C ANISOU 2428 CB VAL A 304 6796 6106 7402 237 -979 538 C ATOM 2429 CG1 VAL A 304 10.060 28.654 49.984 1.00 47.24 C ANISOU 2429 CG1 VAL A 304 5832 5424 6692 328 -999 581 C ATOM 2430 CG2 VAL A 304 12.395 29.420 49.515 1.00 44.56 C ANISOU 2430 CG2 VAL A 304 5704 4946 6279 251 -858 443 C ATOM 2431 N ILE A 305 9.000 28.455 46.570 1.00 60.72 N ANISOU 2431 N ILE A 305 7797 7028 8246 83 -1213 699 N ATOM 2432 CA ILE A 305 7.632 28.121 46.199 1.00 57.49 C ANISOU 2432 CA ILE A 305 7330 6666 7847 82 -1324 791 C ATOM 2433 C ILE A 305 7.592 27.056 45.106 1.00 59.20 C ANISOU 2433 C ILE A 305 7614 6869 8011 -56 -1358 804 C ATOM 2434 O ILE A 305 6.808 26.103 45.184 1.00 68.59 O ANISOU 2434 O ILE A 305 8718 8120 9224 -73 -1403 852 O ATOM 2435 CB ILE A 305 6.894 29.405 45.776 1.00 52.96 C ANISOU 2435 CB ILE A 305 6797 6062 7265 138 -1417 849 C ATOM 2436 CG1 ILE A 305 6.701 30.308 46.997 1.00 49.97 C ANISOU 2436 CG1 ILE A 305 6319 5716 6950 291 -1399 842 C ATOM 2437 CG2 ILE A 305 5.565 29.065 45.080 1.00 51.16 C ANISOU 2437 CG2 ILE A 305 6543 5868 7029 110 -1539 943 C ATOM 2438 CD1 ILE A 305 6.196 31.684 46.682 1.00 44.27 C ANISOU 2438 CD1 ILE A 305 5646 4951 6222 356 -1480 880 C ATOM 2439 N TYR A 306 8.428 27.192 44.076 1.00 55.62 N ANISOU 2439 N TYR A 306 7313 6338 7483 -156 -1339 763 N ATOM 2440 CA TYR A 306 8.377 26.337 42.894 1.00 46.54 C ANISOU 2440 CA TYR A 306 6244 5168 6273 -286 -1381 775 C ATOM 2441 C TYR A 306 9.345 25.160 42.930 1.00 52.73 C ANISOU 2441 C TYR A 306 7040 5953 7040 -364 -1297 697 C ATOM 2442 O TYR A 306 9.247 24.284 42.065 1.00 62.08 O ANISOU 2442 O TYR A 306 8272 7132 8183 -465 -1334 704 O ATOM 2443 CB TYR A 306 8.671 27.152 41.638 1.00 45.89 C ANISOU 2443 CB TYR A 306 6322 5006 6110 -359 -1419 779 C ATOM 2444 CG TYR A 306 7.603 28.137 41.281 1.00 52.65 C ANISOU 2444 CG TYR A 306 7185 5851 6969 -310 -1527 864 C ATOM 2445 CD1 TYR A 306 6.538 27.759 40.490 1.00 51.02 C ANISOU 2445 CD1 TYR A 306 6980 5661 6746 -356 -1634 942 C ATOM 2446 CD2 TYR A 306 7.663 29.453 41.720 1.00 61.07 C ANISOU 2446 CD2 TYR A 306 8260 6889 8056 -218 -1527 866 C ATOM 2447 CE1 TYR A 306 5.561 28.650 40.144 1.00 66.17 C ANISOU 2447 CE1 TYR A 306 8906 7569 8667 -311 -1735 1019 C ATOM 2448 CE2 TYR A 306 6.682 30.353 41.380 1.00 51.64 C ANISOU 2448 CE2 TYR A 306 7074 5681 6865 -171 -1633 941 C ATOM 2449 CZ TYR A 306 5.631 29.941 40.589 1.00 48.75 C ANISOU 2449 CZ TYR A 306 6707 5333 6482 -218 -1736 1017 C ATOM 2450 OH TYR A 306 4.635 30.816 40.230 1.00 73.66 O ANISOU 2450 OH TYR A 306 9870 8476 9640 -171 -1845 1092 O ATOM 2451 N ILE A 307 10.290 25.126 43.869 1.00 53.05 N ANISOU 2451 N ILE A 307 7046 6000 7112 -321 -1189 622 N ATOM 2452 CA ILE A 307 11.248 24.028 43.940 1.00 57.30 C ANISOU 2452 CA ILE A 307 7597 6539 7637 -389 -1110 542 C ATOM 2453 C ILE A 307 11.122 23.349 45.296 1.00 63.04 C ANISOU 2453 C ILE A 307 8172 7334 8448 -315 -1064 533 C ATOM 2454 O ILE A 307 10.795 22.160 45.376 1.00 62.41 O ANISOU 2454 O ILE A 307 8031 7293 8387 -354 -1085 545 O ATOM 2455 CB ILE A 307 12.694 24.512 43.700 1.00 58.72 C ANISOU 2455 CB ILE A 307 7891 6658 7764 -427 -1014 447 C ATOM 2456 CG1 ILE A 307 12.838 25.195 42.330 1.00 47.06 C ANISOU 2456 CG1 ILE A 307 6565 5117 6197 -509 -1061 459 C ATOM 2457 CG2 ILE A 307 13.675 23.362 43.841 1.00 58.55 C ANISOU 2457 CG2 ILE A 307 7873 6642 7733 -488 -932 359 C ATOM 2458 CD1 ILE A 307 12.572 24.282 41.169 1.00 63.18 C ANISOU 2458 CD1 ILE A 307 8668 7155 8183 -625 -1121 475 C ATOM 2459 N MET A 308 11.368 24.099 46.375 1.00 57.75 N ANISOU 2459 N MET A 308 7437 6679 7827 -208 -1005 513 N ATOM 2460 CA MET A 308 11.429 23.481 47.696 1.00 54.75 C ANISOU 2460 CA MET A 308 6919 6363 7520 -142 -947 493 C ATOM 2461 C MET A 308 10.072 22.967 48.153 1.00 53.24 C ANISOU 2461 C MET A 308 6591 6254 7384 -99 -1029 583 C ATOM 2462 O MET A 308 10.007 21.999 48.920 1.00 62.09 O ANISOU 2462 O MET A 308 7607 7431 8552 -91 -1005 579 O ATOM 2463 CB MET A 308 12.004 24.458 48.721 1.00 59.65 C ANISOU 2463 CB MET A 308 7506 6982 8178 -36 -867 449 C ATOM 2464 CG MET A 308 13.537 24.469 48.751 1.00 83.48 C ANISOU 2464 CG MET A 308 10609 9946 11165 -74 -753 342 C ATOM 2465 SD MET A 308 14.250 25.773 49.776 1.00107.13 S ANISOU 2465 SD MET A 308 13590 12923 14192 41 -667 293 S ATOM 2466 CE MET A 308 13.363 25.537 51.316 1.00104.39 C ANISOU 2466 CE MET A 308 13039 12677 13946 171 -670 336 C ATOM 2467 N MET A 309 8.987 23.582 47.696 1.00 54.25 N ANISOU 2467 N MET A 309 6715 6392 7506 -73 -1127 667 N ATOM 2468 CA MET A 309 7.650 23.123 48.039 1.00 48.90 C ANISOU 2468 CA MET A 309 5910 5797 6873 -38 -1211 758 C ATOM 2469 C MET A 309 7.135 22.068 47.062 1.00 70.10 C ANISOU 2469 C MET A 309 8629 8482 9525 -151 -1289 801 C ATOM 2470 O MET A 309 5.970 21.654 47.156 1.00 66.29 O ANISOU 2470 O MET A 309 8054 8064 9071 -139 -1372 885 O ATOM 2471 CB MET A 309 6.695 24.314 48.116 1.00 50.30 C ANISOU 2471 CB MET A 309 6054 5993 7064 56 -1281 825 C ATOM 2472 CG MET A 309 6.942 25.219 49.330 1.00 57.79 C ANISOU 2472 CG MET A 309 6925 6968 8064 189 -1219 794 C ATOM 2473 SD MET A 309 5.780 26.603 49.410 1.00 71.08 S ANISOU 2473 SD MET A 309 8568 8674 9765 307 -1312 868 S ATOM 2474 CE MET A 309 4.262 25.733 49.803 1.00 73.01 C ANISOU 2474 CE MET A 309 8646 9042 10054 330 -1400 967 C ATOM 2475 N ASN A 310 7.988 21.627 46.139 1.00 55.65 N ANISOU 2475 N ASN A 310 6928 6583 7635 -258 -1264 744 N ATOM 2476 CA ASN A 310 7.687 20.545 45.211 1.00 52.10 C ANISOU 2476 CA ASN A 310 6520 6125 7151 -370 -1327 767 C ATOM 2477 C ASN A 310 8.208 19.234 45.804 1.00 60.04 C ANISOU 2477 C ASN A 310 7467 7157 8188 -405 -1275 718 C ATOM 2478 O ASN A 310 9.403 19.118 46.113 1.00 49.57 O ANISOU 2478 O ASN A 310 6178 5799 6855 -413 -1177 625 O ATOM 2479 CB ASN A 310 8.317 20.863 43.850 1.00 52.06 C ANISOU 2479 CB ASN A 310 6688 6035 7058 -464 -1332 728 C ATOM 2480 CG ASN A 310 8.236 19.717 42.861 1.00 58.26 C ANISOU 2480 CG ASN A 310 7532 6804 7801 -583 -1384 730 C ATOM 2481 OD1 ASN A 310 8.632 18.589 43.156 1.00 69.51 O ANISOU 2481 OD1 ASN A 310 8923 8244 9243 -622 -1354 689 O ATOM 2482 ND2 ASN A 310 7.743 20.011 41.663 1.00 49.91 N ANISOU 2482 ND2 ASN A 310 6565 5712 6685 -643 -1466 775 N ATOM 2483 N LYS A 311 7.310 18.251 45.946 1.00 60.14 N ANISOU 2483 N LYS A 311 7389 7226 8233 -427 -1346 784 N ATOM 2484 CA LYS A 311 7.618 16.999 46.642 1.00 47.61 C ANISOU 2484 CA LYS A 311 5727 5674 6689 -451 -1314 755 C ATOM 2485 C LYS A 311 8.886 16.343 46.102 1.00 60.22 C ANISOU 2485 C LYS A 311 7435 7203 8241 -538 -1253 651 C ATOM 2486 O LYS A 311 9.754 15.908 46.871 1.00 45.16 O ANISOU 2486 O LYS A 311 5497 5299 6363 -524 -1168 578 O ATOM 2487 CB LYS A 311 6.434 16.037 46.509 1.00 72.04 C ANISOU 2487 CB LYS A 311 8742 8823 9806 -490 -1422 848 C ATOM 2488 CG LYS A 311 6.055 15.284 47.773 1.00 95.48 C ANISOU 2488 CG LYS A 311 11550 11877 12851 -447 -1415 879 C ATOM 2489 CD LYS A 311 4.772 14.484 47.554 1.00109.95 C ANISOU 2489 CD LYS A 311 13308 13768 14701 -487 -1533 985 C ATOM 2490 CE LYS A 311 4.134 14.068 48.874 1.00122.48 C ANISOU 2490 CE LYS A 311 14715 15459 16361 -425 -1538 1041 C ATOM 2491 NZ LYS A 311 3.669 15.244 49.671 1.00128.38 N ANISOU 2491 NZ LYS A 311 15373 16267 17137 -301 -1515 1074 N ATOM 2492 N GLN A 312 9.007 16.258 44.773 1.00 61.59 N ANISOU 2492 N GLN A 312 7739 7319 8344 -629 -1296 640 N ATOM 2493 CA GLN A 312 10.139 15.554 44.174 1.00 55.08 C ANISOU 2493 CA GLN A 312 7018 6439 7472 -716 -1249 541 C ATOM 2494 C GLN A 312 11.458 16.262 44.464 1.00 70.69 C ANISOU 2494 C GLN A 312 9055 8377 9427 -687 -1128 440 C ATOM 2495 O GLN A 312 12.427 15.629 44.902 1.00 77.02 O ANISOU 2495 O GLN A 312 9855 9169 10239 -700 -1052 354 O ATOM 2496 CB GLN A 312 9.931 15.403 42.668 1.00 74.18 C ANISOU 2496 CB GLN A 312 9560 8811 9812 -815 -1325 554 C ATOM 2497 CG GLN A 312 9.596 13.986 42.241 1.00 96.14 C ANISOU 2497 CG GLN A 312 12334 11600 12595 -897 -1395 566 C ATOM 2498 CD GLN A 312 9.964 13.708 40.796 1.00110.99 C ANISOU 2498 CD GLN A 312 14359 13423 14388 -1003 -1429 526 C ATOM 2499 OE1 GLN A 312 10.247 12.567 40.428 1.00111.42 O ANISOU 2499 OE1 GLN A 312 14440 13465 14431 -1073 -1451 484 O ATOM 2500 NE2 GLN A 312 9.961 14.752 39.967 1.00111.81 N ANISOU 2500 NE2 GLN A 312 14557 13495 14431 -1014 -1438 538 N ATOM 2501 N PHE A 313 11.521 17.577 44.217 1.00 63.77 N ANISOU 2501 N PHE A 313 8234 7476 8521 -648 -1112 449 N ATOM 2502 CA PHE A 313 12.770 18.295 44.446 1.00 60.52 C ANISOU 2502 CA PHE A 313 7884 7025 8085 -626 -1003 358 C ATOM 2503 C PHE A 313 13.141 18.292 45.922 1.00 64.41 C ANISOU 2503 C PHE A 313 8263 7555 8653 -534 -919 326 C ATOM 2504 O PHE A 313 14.304 18.061 46.277 1.00 62.42 O ANISOU 2504 O PHE A 313 8036 7284 8397 -542 -823 231 O ATOM 2505 CB PHE A 313 12.677 19.724 43.911 1.00 55.55 C ANISOU 2505 CB PHE A 313 7333 6359 7412 -603 -1015 384 C ATOM 2506 CG PHE A 313 12.952 19.838 42.436 1.00 55.41 C ANISOU 2506 CG PHE A 313 7464 6288 7300 -707 -1051 369 C ATOM 2507 CD1 PHE A 313 14.243 20.042 41.971 1.00 57.84 C ANISOU 2507 CD1 PHE A 313 7883 6549 7544 -759 -971 274 C ATOM 2508 CD2 PHE A 313 11.920 19.733 41.512 1.00 53.32 C ANISOU 2508 CD2 PHE A 313 7226 6023 7008 -754 -1164 451 C ATOM 2509 CE1 PHE A 313 14.503 20.144 40.608 1.00 53.50 C ANISOU 2509 CE1 PHE A 313 7466 5959 6901 -858 -1003 260 C ATOM 2510 CE2 PHE A 313 12.170 19.835 40.149 1.00 49.38 C ANISOU 2510 CE2 PHE A 313 6864 5478 6420 -851 -1197 438 C ATOM 2511 CZ PHE A 313 13.467 20.042 39.697 1.00 53.44 C ANISOU 2511 CZ PHE A 313 7486 5951 6868 -904 -1116 342 C ATOM 2512 N ARG A 314 12.162 18.522 46.801 1.00 57.49 N ANISOU 2512 N ARG A 314 7260 6740 7845 -448 -954 404 N ATOM 2513 CA ARG A 314 12.465 18.561 48.228 1.00 61.59 C ANISOU 2513 CA ARG A 314 7666 7302 8435 -357 -877 378 C ATOM 2514 C ARG A 314 13.032 17.230 48.703 1.00 70.36 C ANISOU 2514 C ARG A 314 8733 8427 9574 -397 -836 323 C ATOM 2515 O ARG A 314 14.004 17.206 49.469 1.00 59.91 O ANISOU 2515 O ARG A 314 7394 7099 8272 -366 -737 245 O ATOM 2516 CB ARG A 314 11.214 18.936 49.024 1.00 61.64 C ANISOU 2516 CB ARG A 314 7534 7383 8504 -263 -934 476 C ATOM 2517 CG ARG A 314 11.464 19.175 50.509 1.00 47.09 C ANISOU 2517 CG ARG A 314 5572 5590 6730 -158 -856 454 C ATOM 2518 CD ARG A 314 10.201 19.695 51.202 1.00 55.09 C ANISOU 2518 CD ARG A 314 6454 6682 7794 -60 -915 549 C ATOM 2519 NE ARG A 314 9.090 18.733 51.212 1.00 51.29 N ANISOU 2519 NE ARG A 314 5880 6268 7339 -90 -1006 634 N ATOM 2520 CZ ARG A 314 8.014 18.810 50.433 1.00 64.77 C ANISOU 2520 CZ ARG A 314 7599 7987 9025 -116 -1113 718 C ATOM 2521 NH1 ARG A 314 7.887 19.803 49.562 1.00 78.32 N ANISOU 2521 NH1 ARG A 314 9415 9650 10692 -116 -1147 730 N ATOM 2522 NH2 ARG A 314 7.059 17.892 50.522 1.00 74.59 N ANISOU 2522 NH2 ARG A 314 8752 9295 10295 -145 -1191 794 N ATOM 2523 N ASN A 315 12.450 16.112 48.240 1.00 65.44 N ANISOU 2523 N ASN A 315 8096 7818 8949 -469 -915 362 N ATOM 2524 CA ASN A 315 12.948 14.792 48.625 1.00 59.72 C ANISOU 2524 CA ASN A 315 7338 7102 8253 -513 -892 312 C ATOM 2525 C ASN A 315 14.401 14.612 48.205 1.00 61.81 C ANISOU 2525 C ASN A 315 7716 7301 8467 -566 -806 188 C ATOM 2526 O ASN A 315 15.245 14.186 49.005 1.00 63.24 O ANISOU 2526 O ASN A 315 7863 7486 8682 -546 -725 115 O ATOM 2527 CB ASN A 315 12.082 13.688 48.013 1.00 68.24 C ANISOU 2527 CB ASN A 315 8403 8195 9330 -590 -1004 374 C ATOM 2528 CG ASN A 315 10.733 13.539 48.704 1.00 72.29 C ANISOU 2528 CG ASN A 315 8773 8790 9906 -541 -1079 490 C ATOM 2529 OD1 ASN A 315 10.550 13.969 49.843 1.00 74.79 O ANISOU 2529 OD1 ASN A 315 8979 9161 10277 -450 -1039 512 O ATOM 2530 ND2 ASN A 315 9.783 12.916 48.013 1.00 63.27 N ANISOU 2530 ND2 ASN A 315 7629 7659 8752 -602 -1190 565 N ATOM 2531 N CYS A 316 14.717 14.940 46.951 1.00 56.92 N ANISOU 2531 N CYS A 316 7233 6627 7767 -633 -822 161 N ATOM 2532 CA CYS A 316 16.090 14.782 46.485 1.00 55.47 C ANISOU 2532 CA CYS A 316 7157 6391 7527 -687 -743 42 C ATOM 2533 C CYS A 316 17.043 15.738 47.199 1.00 58.01 C ANISOU 2533 C CYS A 316 7484 6701 7855 -619 -627 -22 C ATOM 2534 O CYS A 316 18.187 15.373 47.488 1.00 71.32 O ANISOU 2534 O CYS A 316 9194 8369 9535 -631 -541 -122 O ATOM 2535 CB CYS A 316 16.154 14.977 44.973 1.00 60.72 C ANISOU 2535 CB CYS A 316 7962 7011 8100 -775 -790 34 C ATOM 2536 SG CYS A 316 15.233 13.733 44.054 1.00 64.75 S ANISOU 2536 SG CYS A 316 8481 7525 8595 -865 -920 89 S ATOM 2537 N MET A 317 16.598 16.963 47.492 1.00 68.47 N ANISOU 2537 N MET A 317 8787 8035 9192 -546 -626 33 N ATOM 2538 CA MET A 317 17.460 17.906 48.204 1.00 71.49 C ANISOU 2538 CA MET A 317 9174 8406 9585 -477 -522 -23 C ATOM 2539 C MET A 317 17.779 17.411 49.610 1.00 70.19 C ANISOU 2539 C MET A 317 8890 8281 9499 -411 -454 -55 C ATOM 2540 O MET A 317 18.934 17.456 50.049 1.00 67.08 O ANISOU 2540 O MET A 317 8517 7866 9102 -400 -353 -147 O ATOM 2541 CB MET A 317 16.805 19.284 48.267 1.00 64.95 C ANISOU 2541 CB MET A 317 8340 7580 8760 -406 -551 47 C ATOM 2542 CG MET A 317 16.949 20.091 47.002 1.00 76.43 C ANISOU 2542 CG MET A 317 9933 8978 10128 -464 -580 50 C ATOM 2543 SD MET A 317 16.068 21.651 47.130 1.00 79.46 S ANISOU 2543 SD MET A 317 10302 9362 10526 -375 -631 139 S ATOM 2544 CE MET A 317 16.709 22.503 45.692 1.00 91.99 C ANISOU 2544 CE MET A 317 12072 10874 12004 -461 -636 111 C ATOM 2545 N VAL A 318 16.757 16.954 50.337 1.00 63.19 N ANISOU 2545 N VAL A 318 7874 7454 8681 -366 -509 22 N ATOM 2546 CA VAL A 318 16.970 16.417 51.679 1.00 66.86 C ANISOU 2546 CA VAL A 318 8218 7964 9222 -309 -453 2 C ATOM 2547 C VAL A 318 17.924 15.230 51.633 1.00 73.11 C ANISOU 2547 C VAL A 318 9040 8731 10006 -377 -410 -88 C ATOM 2548 O VAL A 318 18.830 15.111 52.470 1.00 69.80 O ANISOU 2548 O VAL A 318 8592 8312 9616 -343 -317 -162 O ATOM 2549 CB VAL A 318 15.618 16.040 52.319 1.00 70.08 C ANISOU 2549 CB VAL A 318 8485 8449 9694 -266 -534 110 C ATOM 2550 CG1 VAL A 318 15.821 15.160 53.547 1.00 62.46 C ANISOU 2550 CG1 VAL A 318 7401 7532 8801 -236 -492 91 C ATOM 2551 CG2 VAL A 318 14.829 17.294 52.678 1.00 59.28 C ANISOU 2551 CG2 VAL A 318 7065 7113 8344 -171 -555 181 C ATOM 2552 N THR A 319 17.738 14.335 50.654 1.00 67.08 N ANISOU 2552 N THR A 319 8336 7946 9205 -472 -480 -86 N ATOM 2553 CA THR A 319 18.651 13.205 50.489 1.00 64.71 C ANISOU 2553 CA THR A 319 8077 7618 8893 -538 -450 -179 C ATOM 2554 C THR A 319 20.081 13.677 50.255 1.00 62.44 C ANISOU 2554 C THR A 319 7889 7281 8552 -549 -342 -297 C ATOM 2555 O THR A 319 21.023 13.128 50.833 1.00 69.89 O ANISOU 2555 O THR A 319 8819 8218 9516 -546 -268 -383 O ATOM 2556 CB THR A 319 18.202 12.317 49.326 1.00 66.62 C ANISOU 2556 CB THR A 319 8382 7840 9092 -637 -550 -159 C ATOM 2557 OG1 THR A 319 16.918 11.734 49.603 1.00 63.67 O ANISOU 2557 OG1 THR A 319 7908 7514 8770 -633 -650 -52 O ATOM 2558 CG2 THR A 319 19.211 11.221 49.097 1.00 59.86 C ANISOU 2558 CG2 THR A 319 7577 6951 8218 -701 -519 -266 C ATOM 2559 N THR A 320 20.261 14.705 49.421 1.00 62.16 N ANISOU 2559 N THR A 320 7955 7214 8448 -564 -334 -300 N ATOM 2560 CA THR A 320 21.600 15.188 49.097 1.00 58.06 C ANISOU 2560 CA THR A 320 7538 6653 7870 -584 -238 -406 C ATOM 2561 C THR A 320 22.239 15.907 50.278 1.00 61.98 C ANISOU 2561 C THR A 320 7980 7160 8412 -495 -133 -442 C ATOM 2562 O THR A 320 23.438 15.750 50.531 1.00 73.86 O ANISOU 2562 O THR A 320 9516 8645 9903 -502 -41 -544 O ATOM 2563 CB THR A 320 21.539 16.113 47.883 1.00 65.46 C ANISOU 2563 CB THR A 320 8594 7557 8721 -629 -267 -387 C ATOM 2564 OG1 THR A 320 21.206 15.347 46.720 1.00 64.21 O ANISOU 2564 OG1 THR A 320 8501 7386 8510 -723 -349 -379 O ATOM 2565 CG2 THR A 320 22.883 16.847 47.669 1.00 55.85 C ANISOU 2565 CG2 THR A 320 7472 6305 7444 -641 -163 -484 C ATOM 2566 N LEU A 321 21.462 16.709 51.003 1.00 73.45 N ANISOU 2566 N LEU A 321 9350 8642 9915 -409 -148 -363 N ATOM 2567 CA LEU A 321 22.025 17.489 52.099 1.00 82.17 C ANISOU 2567 CA LEU A 321 10406 9755 11060 -319 -53 -394 C ATOM 2568 C LEU A 321 22.265 16.640 53.337 1.00 83.23 C ANISOU 2568 C LEU A 321 10426 9926 11272 -277 -6 -424 C ATOM 2569 O LEU A 321 23.158 16.950 54.133 1.00 79.76 O ANISOU 2569 O LEU A 321 9970 9482 10854 -229 93 -491 O ATOM 2570 CB LEU A 321 21.105 18.668 52.433 1.00 78.83 C ANISOU 2570 CB LEU A 321 9936 9353 10664 -236 -90 -303 C ATOM 2571 CG LEU A 321 21.117 19.793 51.395 1.00 71.78 C ANISOU 2571 CG LEU A 321 9162 8413 9697 -261 -114 -287 C ATOM 2572 CD1 LEU A 321 20.099 20.862 51.743 1.00 62.41 C ANISOU 2572 CD1 LEU A 321 7921 7248 8544 -175 -166 -195 C ATOM 2573 CD2 LEU A 321 22.519 20.384 51.288 1.00 52.72 C ANISOU 2573 CD2 LEU A 321 6842 5954 7236 -276 -11 -386 C ATOM 2574 N CYS A 322 21.490 15.572 53.516 1.00 81.44 N ANISOU 2574 N CYS A 322 10121 9734 11086 -297 -77 -374 N ATOM 2575 CA CYS A 322 21.662 14.671 54.646 1.00 81.94 C ANISOU 2575 CA CYS A 322 10076 9833 11222 -268 -45 -395 C ATOM 2576 C CYS A 322 22.407 13.401 54.245 1.00102.08 C ANISOU 2576 C CYS A 322 12676 12354 13754 -351 -39 -476 C ATOM 2577 O CYS A 322 22.189 12.333 54.828 1.00114.90 O ANISOU 2577 O CYS A 322 14220 14005 15433 -359 -65 -467 O ATOM 2578 CB CYS A 322 20.305 14.364 55.274 1.00 80.70 C ANISOU 2578 CB CYS A 322 9786 9744 11131 -227 -127 -281 C ATOM 2579 SG CYS A 322 19.458 15.874 55.868 1.00 79.92 S ANISOU 2579 SG CYS A 322 9618 9689 11059 -112 -130 -196 S ATOM 2580 N CYS A 323 23.279 13.515 53.235 1.00104.66 N ANISOU 2580 N CYS A 323 13135 12628 14002 -415 -10 -556 N ATOM 2581 CA CYS A 323 24.298 12.537 52.856 1.00102.84 C ANISOU 2581 CA CYS A 323 12968 12365 13743 -483 22 -663 C ATOM 2582 C CYS A 323 23.735 11.238 52.280 1.00 98.18 C ANISOU 2582 C CYS A 323 12377 11774 13154 -557 -80 -641 C ATOM 2583 O CYS A 323 24.450 10.521 51.572 1.00103.02 O ANISOU 2583 O CYS A 323 13071 12353 13720 -626 -79 -726 O ATOM 2584 CB CYS A 323 25.212 12.226 54.047 1.00105.35 C ANISOU 2584 CB CYS A 323 13224 12691 14115 -435 120 -739 C ATOM 2585 SG CYS A 323 25.475 13.603 55.209 1.00 98.20 S ANISOU 2585 SG CYS A 323 12258 11806 13249 -321 220 -731 S ATOM 2586 N GLY A 324 22.472 10.919 52.564 1.00 94.53 N ANISOU 2586 N GLY A 324 11826 11350 12743 -543 -172 -531 N ATOM 2587 CA GLY A 324 21.857 9.737 51.983 1.00 73.19 C ANISOU 2587 CA GLY A 324 9124 8644 10040 -616 -278 -499 C ATOM 2588 C GLY A 324 20.573 9.279 52.647 1.00 83.17 C ANISOU 2588 C GLY A 324 10261 9963 11378 -591 -364 -381 C ATOM 2589 O GLY A 324 20.034 8.231 52.280 1.00 98.18 O ANISOU 2589 O GLY A 324 12152 11864 13288 -651 -457 -349 O ATOM 2590 N LYS A 325 20.069 10.043 53.615 1.00 86.75 N ANISOU 2590 N LYS A 325 10615 10466 11881 -506 -337 -316 N ATOM 2591 CA LYS A 325 18.844 9.688 54.320 1.00107.79 C ANISOU 2591 CA LYS A 325 13147 13196 14612 -477 -412 -202 C ATOM 2592 C LYS A 325 17.614 9.998 53.460 1.00125.62 C ANISOU 2592 C LYS A 325 15420 15469 16840 -502 -519 -97 C ATOM 2593 O LYS A 325 17.691 10.696 52.445 1.00139.38 O ANISOU 2593 O LYS A 325 17268 17173 18516 -525 -526 -108 O ATOM 2594 CB LYS A 325 18.768 10.427 55.661 1.00115.14 C ANISOU 2594 CB LYS A 325 13964 14182 15602 -372 -343 -176 C ATOM 2595 CG LYS A 325 17.811 9.809 56.680 1.00123.16 C ANISOU 2595 CG LYS A 325 14824 15276 16694 -343 -397 -84 C ATOM 2596 CD LYS A 325 17.558 10.742 57.853 1.00127.18 C ANISOU 2596 CD LYS A 325 15224 15850 17250 -232 -339 -48 C ATOM 2597 CE LYS A 325 16.356 10.285 58.669 1.00129.12 C ANISOU 2597 CE LYS A 325 15315 16187 17556 -207 -410 65 C ATOM 2598 NZ LYS A 325 16.069 11.204 59.805 1.00127.80 N ANISOU 2598 NZ LYS A 325 15035 16091 17430 -95 -357 99 N ATOM 2599 N ASN A 326 16.468 9.457 53.878 1.00123.79 N ANISOU 2599 N ASN A 326 15079 15296 16659 -499 -606 6 N ATOM 2600 CA ASN A 326 15.175 9.666 53.217 1.00126.14 C ANISOU 2600 CA ASN A 326 15368 15620 16940 -517 -714 117 C ATOM 2601 C ASN A 326 14.856 11.143 52.951 1.00122.79 C ANISOU 2601 C ASN A 326 14972 15201 16484 -456 -695 150 C ATOM 2602 O ASN A 326 14.102 11.481 52.030 1.00103.78 O ANISOU 2602 O ASN A 326 12611 12785 14036 -485 -772 211 O ATOM 2603 CB ASN A 326 14.061 9.036 54.063 1.00134.42 C ANISOU 2603 CB ASN A 326 16265 16750 18057 -499 -787 224 C ATOM 2604 CG ASN A 326 12.776 9.852 54.052 1.00138.94 C ANISOU 2604 CG ASN A 326 16773 17384 18634 -450 -848 340 C ATOM 2605 OD1 ASN A 326 12.605 10.778 54.848 1.00140.40 O ANISOU 2605 OD1 ASN A 326 16885 17616 18844 -357 -798 361 O ATOM 2606 ND2 ASN A 326 11.863 9.505 53.152 1.00134.56 N ANISOU 2606 ND2 ASN A 326 16245 16830 18054 -511 -959 412 N TER 2607 ASN A 326 ATOM 2608 N ILE B 340 -6.995 12.512 37.058 1.00 81.26 N ANISOU 2608 N ILE B 340 9676 8154 13046 -981 -1101 712 N ATOM 2609 CA ILE B 340 -6.434 13.847 37.207 1.00 80.84 C ANISOU 2609 CA ILE B 340 9601 8172 12941 -999 -1176 797 C ATOM 2610 C ILE B 340 -5.233 13.815 38.154 1.00 80.64 C ANISOU 2610 C ILE B 340 9462 8172 13003 -958 -1108 923 C ATOM 2611 O ILE B 340 -4.346 14.653 38.071 1.00 80.60 O ANISOU 2611 O ILE B 340 9441 8220 12964 -962 -1111 1003 O ATOM 2612 CB ILE B 340 -7.514 14.845 37.691 1.00 79.93 C ANISOU 2612 CB ILE B 340 9490 8091 12789 -1036 -1352 780 C ATOM 2613 CG1 ILE B 340 -7.112 16.278 37.342 1.00 79.70 C ANISOU 2613 CG1 ILE B 340 9485 8131 12667 -1069 -1435 833 C ATOM 2614 CG2 ILE B 340 -7.786 14.689 39.188 1.00 79.10 C ANISOU 2614 CG2 ILE B 340 9275 7987 12791 -1010 -1396 831 C ATOM 2615 CD1 ILE B 340 -8.196 17.283 37.608 1.00 78.91 C ANISOU 2615 CD1 ILE B 340 9406 8063 12514 -1109 -1607 804 C ATOM 2616 N LEU B 341 -5.208 12.814 39.034 1.00 89.55 N ANISOU 2616 N LEU B 341 10515 9264 14247 -917 -1043 938 N ATOM 2617 CA LEU B 341 -4.190 12.747 40.076 1.00 80.24 C ANISOU 2617 CA LEU B 341 9221 8107 13161 -876 -988 1055 C ATOM 2618 C LEU B 341 -2.794 12.562 39.494 1.00 84.10 C ANISOU 2618 C LEU B 341 9708 8604 13642 -854 -855 1113 C ATOM 2619 O LEU B 341 -1.835 13.193 39.956 1.00 80.75 O ANISOU 2619 O LEU B 341 9221 8229 13233 -842 -849 1219 O ATOM 2620 CB LEU B 341 -4.524 11.611 41.043 1.00 80.04 C ANISOU 2620 CB LEU B 341 9123 8033 13257 -837 -940 1047 C ATOM 2621 CG LEU B 341 -5.133 11.971 42.398 1.00 79.02 C ANISOU 2621 CG LEU B 341 8909 7922 13191 -832 -1049 1085 C ATOM 2622 CD1 LEU B 341 -5.949 13.249 42.312 1.00 78.39 C ANISOU 2622 CD1 LEU B 341 8871 7888 13024 -881 -1215 1065 C ATOM 2623 CD2 LEU B 341 -5.978 10.814 42.917 1.00 78.94 C ANISOU 2623 CD2 LEU B 341 8879 7850 13265 -812 -1026 1020 C ATOM 2624 N GLU B 342 -2.654 11.695 38.488 1.00 82.60 N ANISOU 2624 N GLU B 342 9587 8367 13430 -849 -746 1046 N ATOM 2625 CA GLU B 342 -1.338 11.445 37.909 1.00 82.64 C ANISOU 2625 CA GLU B 342 9593 8377 13431 -827 -614 1098 C ATOM 2626 C GLU B 342 -0.785 12.696 37.241 1.00 82.69 C ANISOU 2626 C GLU B 342 9642 8444 13334 -859 -662 1139 C ATOM 2627 O GLU B 342 0.407 12.998 37.365 1.00 82.83 O ANISOU 2627 O GLU B 342 9611 8495 13363 -840 -603 1234 O ATOM 2628 CB GLU B 342 -1.411 10.290 36.911 1.00 83.59 C ANISOU 2628 CB GLU B 342 9787 8433 13542 -818 -496 1008 C ATOM 2629 CG GLU B 342 -0.315 9.247 37.079 1.00117.81 C ANISOU 2629 CG GLU B 342 14065 12738 17961 -768 -331 1058 C ATOM 2630 CD GLU B 342 0.237 8.765 35.748 1.00130.04 C ANISOU 2630 CD GLU B 342 15697 14262 19452 -769 -216 1014 C ATOM 2631 OE1 GLU B 342 0.449 9.611 34.850 1.00136.31 O ANISOU 2631 OE1 GLU B 342 16560 15090 20142 -802 -250 1009 O ATOM 2632 OE2 GLU B 342 0.455 7.541 35.598 1.00121.51 O ANISOU 2632 OE2 GLU B 342 14613 13125 18429 -737 -93 984 O ATOM 2633 N ASN B 343 -1.638 13.438 36.528 1.00 82.59 N ANISOU 2633 N ASN B 343 9718 8445 13218 -907 -770 1069 N ATOM 2634 CA ASN B 343 -1.202 14.682 35.900 1.00 82.60 C ANISOU 2634 CA ASN B 343 9761 8505 13117 -940 -828 1105 C ATOM 2635 C ASN B 343 -0.776 15.707 36.942 1.00 86.69 C ANISOU 2635 C ASN B 343 10190 9086 13660 -938 -909 1216 C ATOM 2636 O ASN B 343 0.207 16.432 36.744 1.00 81.86 O ANISOU 2636 O ASN B 343 9567 8523 13014 -940 -893 1294 O ATOM 2637 CB ASN B 343 -2.315 15.251 35.020 1.00 85.02 C ANISOU 2637 CB ASN B 343 10177 8812 13313 -992 -936 1005 C ATOM 2638 CG ASN B 343 -2.507 14.467 33.735 1.00 83.53 C ANISOU 2638 CG ASN B 343 10090 8573 13073 -1000 -852 905 C ATOM 2639 OD1 ASN B 343 -1.583 13.812 33.246 1.00 84.27 O ANISOU 2639 OD1 ASN B 343 10189 8648 13184 -974 -716 922 O ATOM 2640 ND2 ASN B 343 -3.712 14.542 33.172 1.00 83.50 N ANISOU 2640 ND2 ASN B 343 10171 8548 13006 -1036 -934 799 N ATOM 2641 N LEU B 344 -1.501 15.780 38.061 1.00 80.93 N ANISOU 2641 N LEU B 344 9398 8359 12993 -933 -997 1225 N ATOM 2642 CA LEU B 344 -1.110 16.691 39.131 1.00 80.12 C ANISOU 2642 CA LEU B 344 9205 8314 12923 -928 -1072 1331 C ATOM 2643 C LEU B 344 0.262 16.330 39.694 1.00 80.30 C ANISOU 2643 C LEU B 344 9136 8347 13027 -882 -954 1440 C ATOM 2644 O LEU B 344 1.065 17.217 40.005 1.00 80.02 O ANISOU 2644 O LEU B 344 9055 8368 12980 -883 -978 1535 O ATOM 2645 CB LEU B 344 -2.173 16.697 40.230 1.00 79.24 C ANISOU 2645 CB LEU B 344 9043 8196 12869 -929 -1178 1315 C ATOM 2646 CG LEU B 344 -3.532 17.293 39.836 1.00 78.89 C ANISOU 2646 CG LEU B 344 9077 8153 12743 -977 -1319 1224 C ATOM 2647 CD1 LEU B 344 -4.481 17.342 41.025 1.00 77.98 C ANISOU 2647 CD1 LEU B 344 8900 8036 12691 -975 -1422 1221 C ATOM 2648 CD2 LEU B 344 -3.376 18.676 39.215 1.00 78.77 C ANISOU 2648 CD2 LEU B 344 9115 8198 12615 -1019 -1409 1245 C ATOM 2649 N LYS B 345 0.560 15.033 39.818 1.00 73.92 N ANISOU 2649 N LYS B 345 8491 8332 11262 -1597 -933 558 N ATOM 2650 CA LYS B 345 1.872 14.629 40.314 1.00 69.05 C ANISOU 2650 CA LYS B 345 7909 7705 10624 -1500 -932 458 C ATOM 2651 C LYS B 345 2.971 14.997 39.324 1.00 77.64 C ANISOU 2651 C LYS B 345 8991 8873 11634 -1460 -920 309 C ATOM 2652 O LYS B 345 4.039 15.480 39.725 1.00 70.95 O ANISOU 2652 O LYS B 345 8136 8081 10740 -1387 -867 247 O ATOM 2653 CB LYS B 345 1.896 13.129 40.608 1.00 77.71 C ANISOU 2653 CB LYS B 345 9071 8674 11782 -1481 -1022 437 C ATOM 2654 CG LYS B 345 3.178 12.678 41.308 1.00107.13 C ANISOU 2654 CG LYS B 345 12832 12379 15493 -1380 -1020 351 C ATOM 2655 CD LYS B 345 3.557 11.234 40.980 1.00115.14 C ANISOU 2655 CD LYS B 345 13913 13295 16539 -1355 -1117 263 C ATOM 2656 CE LYS B 345 4.777 10.797 41.789 1.00106.93 C ANISOU 2656 CE LYS B 345 12907 12231 15489 -1256 -1112 189 C ATOM 2657 NZ LYS B 345 5.393 9.531 41.301 1.00 97.51 N ANISOU 2657 NZ LYS B 345 11777 10964 14310 -1221 -1199 75 N ATOM 2658 N ASP B 346 2.714 14.799 38.025 1.00 68.77 N ANISOU 2658 N ASP B 346 7874 7759 10498 -1509 -967 251 N ATOM 2659 CA ASP B 346 3.707 15.119 37.000 1.00 70.04 C ANISOU 2659 CA ASP B 346 8030 7995 10586 -1476 -960 109 C ATOM 2660 C ASP B 346 4.124 16.586 37.045 1.00 69.34 C ANISOU 2660 C ASP B 346 7882 8034 10430 -1459 -859 109 C ATOM 2661 O ASP B 346 5.313 16.899 36.931 1.00 80.73 O ANISOU 2661 O ASP B 346 9324 9534 11815 -1391 -828 2 O ATOM 2662 CB ASP B 346 3.155 14.775 35.616 1.00 71.99 C ANISOU 2662 CB ASP B 346 8285 8234 10833 -1544 -1021 70 C ATOM 2663 CG ASP B 346 2.961 13.291 35.420 1.00 84.31 C ANISOU 2663 CG ASP B 346 9908 9674 12450 -1550 -1125 41 C ATOM 2664 OD1 ASP B 346 3.693 12.508 36.065 1.00 87.39 O ANISOU 2664 OD1 ASP B 346 10343 10005 12858 -1483 -1152 -7 O ATOM 2665 OD2 ASP B 346 2.079 12.911 34.621 1.00 99.92 O ANISOU 2665 OD2 ASP B 346 11893 11618 14455 -1623 -1179 65 O ATOM 2666 N VAL B 347 3.156 17.499 37.196 1.00 67.35 N ANISOU 2666 N VAL B 347 7580 7827 10184 -1522 -807 227 N ATOM 2667 CA VAL B 347 3.433 18.933 37.157 1.00 65.80 C ANISOU 2667 CA VAL B 347 7323 7753 9924 -1515 -713 234 C ATOM 2668 C VAL B 347 3.860 19.480 38.507 1.00 65.16 C ANISOU 2668 C VAL B 347 7225 7694 9840 -1458 -640 287 C ATOM 2669 O VAL B 347 4.142 20.681 38.620 1.00 69.34 O ANISOU 2669 O VAL B 347 7705 8324 10317 -1446 -557 297 O ATOM 2670 CB VAL B 347 2.214 19.728 36.639 1.00 74.30 C ANISOU 2670 CB VAL B 347 8351 8876 11005 -1610 -687 333 C ATOM 2671 CG1 VAL B 347 1.775 19.219 35.269 1.00 66.11 C ANISOU 2671 CG1 VAL B 347 7330 7820 9970 -1669 -758 281 C ATOM 2672 CG2 VAL B 347 1.062 19.683 37.635 1.00 65.45 C ANISOU 2672 CG2 VAL B 347 7219 7697 9950 -1655 -679 495 C ATOM 2673 N GLY B 348 3.922 18.643 39.537 1.00 65.50 N ANISOU 2673 N GLY B 348 7306 7646 9934 -1421 -669 321 N ATOM 2674 CA GLY B 348 4.490 19.078 40.798 1.00 64.94 C ANISOU 2674 CA GLY B 348 7225 7594 9857 -1356 -605 354 C ATOM 2675 C GLY B 348 3.535 19.798 41.715 1.00 71.40 C ANISOU 2675 C GLY B 348 8002 8423 10704 -1396 -547 511 C ATOM 2676 O GLY B 348 3.975 20.582 42.560 1.00 72.51 O ANISOU 2676 O GLY B 348 8115 8616 10819 -1352 -472 539 O ATOM 2677 N LEU B 349 2.231 19.550 41.578 1.00 74.56 N ANISOU 2677 N LEU B 349 8398 8774 11157 -1478 -580 615 N ATOM 2678 CA LEU B 349 1.230 20.245 42.373 1.00 75.66 C ANISOU 2678 CA LEU B 349 8497 8925 11326 -1523 -527 769 C ATOM 2679 C LEU B 349 0.618 19.393 43.472 1.00 72.91 C ANISOU 2679 C LEU B 349 8179 8466 11056 -1526 -562 868 C ATOM 2680 O LEU B 349 0.004 19.951 44.387 1.00 86.65 O ANISOU 2680 O LEU B 349 9890 10214 12819 -1543 -510 991 O ATOM 2681 CB LEU B 349 0.110 20.781 41.470 1.00 64.14 C ANISOU 2681 CB LEU B 349 7001 7503 9868 -1620 -526 830 C ATOM 2682 CG LEU B 349 0.491 21.989 40.608 1.00 68.86 C ANISOU 2682 CG LEU B 349 7549 8228 10388 -1627 -465 774 C ATOM 2683 CD1 LEU B 349 -0.669 22.404 39.713 1.00 63.51 C ANISOU 2683 CD1 LEU B 349 6838 7576 9717 -1725 -472 837 C ATOM 2684 CD2 LEU B 349 0.955 23.164 41.477 1.00 62.56 C ANISOU 2684 CD2 LEU B 349 6707 7514 9550 -1583 -364 810 C ATOM 2685 N PHE B 350 0.767 18.074 43.411 1.00 76.23 N ANISOU 2685 N PHE B 350 8659 8787 11519 -1510 -647 820 N ATOM 2686 CA PHE B 350 0.251 17.192 44.455 1.00 91.42 C ANISOU 2686 CA PHE B 350 10615 10601 13517 -1508 -684 907 C ATOM 2687 C PHE B 350 1.150 15.971 44.643 1.00 98.54 C ANISOU 2687 C PHE B 350 11581 11423 14435 -1440 -748 808 C ATOM 2688 O PHE B 350 1.059 15.259 45.645 1.00100.42 O ANISOU 2688 O PHE B 350 11850 11578 14725 -1414 -771 858 O ATOM 2689 CB PHE B 350 -1.175 16.747 44.130 1.00 87.23 C ANISOU 2689 CB PHE B 350 10088 10009 13049 -1602 -736 1008 C ATOM 2690 CG PHE B 350 -1.822 15.945 45.222 1.00 78.01 C ANISOU 2690 CG PHE B 350 8948 8734 11959 -1607 -768 1112 C ATOM 2691 CD1 PHE B 350 -2.133 16.533 46.440 1.00 78.83 C ANISOU 2691 CD1 PHE B 350 9025 8848 12080 -1597 -703 1226 C ATOM 2692 CD2 PHE B 350 -2.127 14.609 45.031 1.00 71.88 C ANISOU 2692 CD2 PHE B 350 8225 7848 11239 -1623 -862 1098 C ATOM 2693 CE1 PHE B 350 -2.732 15.801 47.451 1.00 69.19 C ANISOU 2693 CE1 PHE B 350 7830 7529 10931 -1603 -732 1323 C ATOM 2694 CE2 PHE B 350 -2.725 13.870 46.038 1.00 69.60 C ANISOU 2694 CE2 PHE B 350 7963 7461 11023 -1628 -892 1195 C ATOM 2695 CZ PHE B 350 -3.028 14.469 47.250 1.00 67.39 C ANISOU 2695 CZ PHE B 350 7655 7192 10759 -1618 -826 1307 C ATOM 2696 OXT PHE B 350 1.992 15.670 43.796 1.00 98.16 O ANISOU 2696 OXT PHE B 350 11555 11393 14348 -1408 -779 675 O TER 2697 PHE B 350 HETATM 2698 C1 NAG C 1 26.408 70.106 40.402 1.00 39.45 C HETATM 2699 C2 NAG C 1 27.082 69.514 39.160 1.00 48.77 C HETATM 2700 C3 NAG C 1 28.589 69.672 39.302 1.00 48.13 C HETATM 2701 C4 NAG C 1 28.946 71.127 39.542 1.00 52.05 C HETATM 2702 C5 NAG C 1 28.192 71.620 40.768 1.00 67.15 C HETATM 2703 C6 NAG C 1 28.478 73.105 41.010 1.00 59.00 C HETATM 2704 C7 NAG C 1 26.430 67.430 37.963 1.00 53.04 C HETATM 2705 C8 NAG C 1 26.189 65.925 38.148 1.00 60.52 C HETATM 2706 N2 NAG C 1 26.767 68.077 39.083 1.00 46.01 N HETATM 2707 O3 NAG C 1 29.263 69.185 38.106 1.00 56.55 O HETATM 2708 O4 NAG C 1 30.338 71.209 39.842 1.00 54.51 O HETATM 2709 O5 NAG C 1 26.792 71.482 40.567 1.00 54.79 O HETATM 2710 O6 NAG C 1 28.351 73.832 39.779 1.00 68.60 O HETATM 2711 O7 NAG C 1 26.324 67.956 36.858 1.00 66.67 O HETATM 2712 C1 NAG C 2 31.195 72.061 39.051 1.00 44.24 C HETATM 2713 C2 NAG C 2 32.459 72.269 39.863 1.00 40.19 C HETATM 2714 C3 NAG C 2 33.357 73.223 39.145 1.00 44.84 C HETATM 2715 C4 NAG C 2 33.670 72.665 37.755 1.00 50.89 C HETATM 2716 C5 NAG C 2 32.369 72.439 37.005 1.00 35.57 C HETATM 2717 C6 NAG C 2 32.725 71.949 35.588 1.00 43.12 C HETATM 2718 C7 NAG C 2 31.953 71.958 42.266 1.00 65.51 C HETATM 2719 C8 NAG C 2 31.562 72.645 43.567 1.00 38.53 C HETATM 2720 N2 NAG C 2 32.115 72.778 41.207 1.00 54.60 N HETATM 2721 O3 NAG C 2 34.562 73.349 39.918 1.00 51.56 O HETATM 2722 O4 NAG C 2 34.419 73.595 36.979 1.00 62.66 O HETATM 2723 O5 NAG C 2 31.546 71.506 37.741 1.00 44.75 O HETATM 2724 O6 NAG C 2 31.550 71.667 34.820 1.00 55.07 O HETATM 2725 O7 NAG C 2 32.099 70.736 42.228 1.00 89.79 O HETATM 2726 C1 BMA C 3 35.836 73.511 36.892 1.00 87.31 C HETATM 2727 C2 BMA C 3 36.254 74.456 35.769 1.00 98.15 C HETATM 2728 C3 BMA C 3 37.746 74.403 35.579 1.00108.12 C HETATM 2729 C4 BMA C 3 38.402 74.776 36.902 1.00121.49 C HETATM 2730 C5 BMA C 3 37.896 73.860 38.019 1.00121.76 C HETATM 2731 C6 BMA C 3 38.514 74.278 39.359 1.00115.00 C HETATM 2732 O2 BMA C 3 35.861 75.803 36.115 1.00100.27 O HETATM 2733 O3 BMA C 3 38.103 75.367 34.572 1.00124.33 O HETATM 2734 O4 BMA C 3 39.827 74.650 36.785 1.00136.20 O HETATM 2735 O5 BMA C 3 36.452 73.941 38.119 1.00110.03 O HETATM 2736 O6 BMA C 3 37.746 75.348 39.926 1.00110.75 O HETATM 2737 C1 BMA C 4 38.847 74.853 33.459 1.00138.49 C HETATM 2738 C2 BMA C 4 38.011 74.975 32.194 1.00137.67 C HETATM 2739 C3 BMA C 4 38.833 74.498 31.010 1.00141.91 C HETATM 2740 C4 BMA C 4 40.096 75.352 30.915 1.00156.90 C HETATM 2741 C5 BMA C 4 40.875 75.233 32.222 1.00156.83 C HETATM 2742 C6 BMA C 4 42.134 76.107 32.158 1.00145.75 C HETATM 2743 O2 BMA C 4 37.644 76.352 31.993 1.00140.49 O HETATM 2744 O3 BMA C 4 38.062 74.622 29.804 1.00132.10 O HETATM 2745 O4 BMA C 4 40.916 74.911 29.817 1.00160.56 O HETATM 2746 O5 BMA C 4 40.043 75.657 33.326 1.00156.17 O HETATM 2747 O6 BMA C 4 43.021 75.598 31.158 1.00137.38 O HETATM 2748 C1 BOG A 405 -11.779 28.837 47.983 1.00139.18 C HETATM 2749 O1 BOG A 405 -11.069 29.497 46.967 1.00130.95 O HETATM 2750 C2 BOG A 405 -13.258 28.718 47.598 1.00142.42 C HETATM 2751 O2 BOG A 405 -13.872 29.959 47.839 1.00142.28 O HETATM 2752 C3 BOG A 405 -14.039 27.688 48.307 1.00134.74 C HETATM 2753 O3 BOG A 405 -14.860 27.060 47.354 1.00127.78 O HETATM 2754 C4 BOG A 405 -13.317 26.624 49.031 1.00132.88 C HETATM 2755 O4 BOG A 405 -13.982 26.425 50.252 1.00125.59 O HETATM 2756 C5 BOG A 405 -11.834 26.871 49.331 1.00131.08 C HETATM 2757 O5 BOG A 405 -11.155 27.542 48.228 1.00134.98 O HETATM 2758 C6 BOG A 405 -11.137 25.535 49.624 1.00120.22 C HETATM 2759 O6 BOG A 405 -10.659 24.960 48.433 1.00105.11 O HETATM 2760 C1' BOG A 405 -11.257 28.986 45.675 1.00110.51 C HETATM 2761 C2' BOG A 405 -10.972 30.106 44.678 1.00 88.36 C HETATM 2762 C3' BOG A 405 -9.500 30.140 44.277 1.00 83.10 C HETATM 2763 C4' BOG A 405 -9.257 30.949 43.007 1.00 73.86 C HETATM 2764 C5' BOG A 405 -7.851 30.742 42.455 1.00 69.57 C HETATM 2765 C6' BOG A 405 -7.389 31.907 41.583 1.00 69.40 C HETATM 2766 C7' BOG A 405 -6.911 31.445 40.205 1.00 76.65 C HETATM 2767 C8' BOG A 405 -6.080 32.508 39.486 1.00 63.49 C HETATM 2768 C1 BOG A 406 5.890 16.874 17.219 1.00144.65 C HETATM 2769 O1 BOG A 406 4.553 16.479 17.427 1.00134.83 O HETATM 2770 C2 BOG A 406 6.525 17.340 18.549 1.00135.68 C HETATM 2771 O2 BOG A 406 7.201 18.545 18.295 1.00115.40 O HETATM 2772 C3 BOG A 406 7.461 16.412 19.212 1.00139.18 C HETATM 2773 O3 BOG A 406 7.226 16.390 20.597 1.00132.67 O HETATM 2774 C4 BOG A 406 7.357 15.050 18.698 1.00144.16 C HETATM 2775 O4 BOG A 406 8.282 14.221 19.344 1.00144.90 O HETATM 2776 C5 BOG A 406 7.643 15.099 17.205 1.00146.31 C HETATM 2777 O5 BOG A 406 6.550 15.768 16.503 1.00150.83 O HETATM 2778 C6 BOG A 406 7.798 13.679 16.667 1.00139.91 C HETATM 2779 O6 BOG A 406 8.722 13.006 17.476 1.00137.27 O HETATM 2780 C1' BOG A 406 3.789 17.269 18.298 1.00114.74 C HETATM 2781 C2' BOG A 406 3.109 18.354 17.470 1.00101.22 C HETATM 2782 C3' BOG A 406 2.024 19.081 18.256 1.00104.65 C HETATM 2783 C4' BOG A 406 0.731 18.275 18.380 1.00110.38 C HETATM 2784 C5' BOG A 406 -0.458 19.041 17.799 1.00113.65 C HETATM 2785 C6' BOG A 406 -1.802 18.590 18.365 1.00118.11 C HETATM 2786 C7' BOG A 406 -2.932 19.547 17.983 1.00121.84 C HETATM 2787 C8' BOG A 406 -4.313 18.899 18.085 1.00117.65 C HETATM 2788 C1 BOG A 407 37.667 53.587 48.605 1.00123.61 C HETATM 2789 O1 BOG A 407 37.583 52.191 48.630 1.00113.92 O HETATM 2790 C2 BOG A 407 37.238 54.116 49.965 1.00130.07 C HETATM 2791 O2 BOG A 407 35.929 53.700 50.237 1.00141.07 O HETATM 2792 C3 BOG A 407 37.266 55.576 49.999 1.00132.61 C HETATM 2793 O3 BOG A 407 37.138 55.985 51.336 1.00135.30 O HETATM 2794 C4 BOG A 407 38.471 56.202 49.436 1.00132.79 C HETATM 2795 O4 BOG A 407 38.031 57.248 48.615 1.00125.59 O HETATM 2796 C5 BOG A 407 39.439 55.335 48.606 1.00134.38 C HETATM 2797 O5 BOG A 407 39.061 53.936 48.357 1.00131.70 O HETATM 2798 C6 BOG A 407 40.820 55.332 49.282 1.00128.05 C HETATM 2799 O6 BOG A 407 40.837 56.227 50.363 1.00121.14 O HETATM 2800 C1' BOG A 407 36.440 51.625 48.054 1.00 90.47 C HETATM 2801 C2' BOG A 407 35.993 50.455 48.928 1.00 78.94 C HETATM 2802 C3' BOG A 407 35.838 49.179 48.101 1.00 86.17 C HETATM 2803 C4' BOG A 407 35.489 47.926 48.904 1.00 85.09 C HETATM 2804 C5' BOG A 407 35.612 46.643 48.079 1.00 79.68 C HETATM 2805 C6' BOG A 407 34.581 45.589 48.496 1.00 83.03 C HETATM 2806 C7' BOG A 407 35.046 44.148 48.263 1.00 75.21 C HETATM 2807 C8' BOG A 407 33.951 43.112 48.534 1.00 66.40 C HETATM 2808 C1 BOG A 408 -10.925 27.056 25.709 1.00153.39 C HETATM 2809 O1 BOG A 408 -11.196 28.357 25.249 1.00141.95 O HETATM 2810 C2 BOG A 408 -12.072 26.659 26.649 1.00154.37 C HETATM 2811 O2 BOG A 408 -11.687 27.050 27.942 1.00151.64 O HETATM 2812 C3 BOG A 408 -12.452 25.235 26.706 1.00152.78 C HETATM 2813 O3 BOG A 408 -13.844 25.169 26.859 1.00147.49 O HETATM 2814 C4 BOG A 408 -12.105 24.415 25.541 1.00151.53 C HETATM 2815 O4 BOG A 408 -12.122 23.067 25.926 1.00148.71 O HETATM 2816 C5 BOG A 408 -10.731 24.760 24.981 1.00152.44 C HETATM 2817 O5 BOG A 408 -10.714 26.160 24.569 1.00156.52 O HETATM 2818 C6 BOG A 408 -10.424 23.868 23.779 1.00148.74 C HETATM 2819 O6 BOG A 408 -11.150 22.675 23.901 1.00149.10 O HETATM 2820 C1' BOG A 408 -10.215 28.940 24.435 1.00133.73 C HETATM 2821 C2' BOG A 408 -8.842 28.743 25.077 1.00123.36 C HETATM 2822 C3' BOG A 408 -7.762 29.656 24.501 1.00105.83 C HETATM 2823 C4' BOG A 408 -6.373 29.200 24.938 1.00 98.81 C HETATM 2824 C5' BOG A 408 -5.440 30.355 25.283 1.00 92.45 C HETATM 2825 C6' BOG A 408 -4.524 30.019 26.460 1.00 89.32 C HETATM 2826 C7' BOG A 408 -3.050 30.054 26.065 1.00 79.88 C HETATM 2827 C8' BOG A 408 -2.276 31.115 26.839 1.00 75.00 C HETATM 2828 C1 PLM A 409 25.380 14.625 56.463 1.00 80.14 C1+ HETATM 2829 O2 PLM A 409 24.771 14.189 57.385 1.00 93.34 O HETATM 2830 C2 PLM A 409 25.456 16.146 56.423 1.00 73.25 C HETATM 2831 C3 PLM A 409 24.622 16.719 57.572 1.00 71.03 C HETATM 2832 C4 PLM A 409 24.661 18.243 57.639 1.00 64.97 C HETATM 2833 C5 PLM A 409 24.018 18.791 58.910 1.00 59.65 C HETATM 2834 C6 PLM A 409 24.556 20.190 59.205 1.00 71.00 C HETATM 2835 C7 PLM A 409 23.594 21.067 60.000 1.00 68.76 C HETATM 2836 C8 PLM A 409 24.108 22.500 60.070 1.00 72.62 C HETATM 2837 C9 PLM A 409 23.136 23.506 59.459 1.00 79.65 C HETATM 2838 CA PLM A 409 23.876 24.618 58.726 1.00 76.96 C HETATM 2839 CB PLM A 409 23.245 25.999 58.903 1.00 73.51 C HETATM 2840 CC PLM A 409 24.349 27.056 58.932 1.00 80.41 C HETATM 2841 CD PLM A 409 23.840 28.476 58.720 1.00 74.98 C HETATM 2842 CE PLM A 409 24.965 29.493 58.886 1.00 74.98 C HETATM 2843 CF PLM A 409 24.480 30.926 58.680 1.00 74.66 C HETATM 2844 CG PLM A 409 25.580 31.834 58.139 1.00 76.64 C HETATM 2845 S SO4 A 410 13.525 59.269 49.905 1.00127.56 S HETATM 2846 O1 SO4 A 410 14.860 58.781 49.571 1.00124.14 O HETATM 2847 O2 SO4 A 410 12.598 58.880 48.845 1.00118.62 O HETATM 2848 O3 SO4 A 410 13.094 58.692 51.177 1.00134.08 O HETATM 2849 O4 SO4 A 410 13.552 60.726 50.029 1.00138.42 O HETATM 2850 S SO4 A 411 -9.011 7.266 47.820 1.00136.36 S HETATM 2851 O1 SO4 A 411 -8.438 5.942 48.050 1.00143.93 O HETATM 2852 O2 SO4 A 411 -8.918 7.591 46.394 1.00101.23 O HETATM 2853 O3 SO4 A 411 -10.413 7.273 48.232 1.00147.58 O HETATM 2854 O4 SO4 A 411 -8.286 8.249 48.621 1.00132.08 O HETATM 2855 C1 BOG A 412 14.282 46.000 35.205 1.00116.44 C HETATM 2856 O1 BOG A 412 13.628 47.107 35.766 1.00103.20 O HETATM 2857 C2 BOG A 412 15.798 46.099 35.540 1.00113.29 C HETATM 2858 O2 BOG A 412 16.570 45.698 34.415 1.00 94.44 O HETATM 2859 C3 BOG A 412 16.239 45.356 36.748 1.00124.24 C HETATM 2860 O3 BOG A 412 16.941 46.208 37.615 1.00124.52 O HETATM 2861 C4 BOG A 412 15.119 44.720 37.456 1.00126.55 C HETATM 2862 O4 BOG A 412 15.543 43.911 38.519 1.00134.45 O HETATM 2863 C5 BOG A 412 14.404 43.889 36.402 1.00118.48 C HETATM 2864 O5 BOG A 412 13.548 44.787 35.633 1.00110.24 O HETATM 2865 C6 BOG A 412 13.642 42.711 37.001 1.00110.53 C HETATM 2866 O6 BOG A 412 13.723 41.667 36.066 1.00 89.31 O HETATM 2867 C1' BOG A 412 12.242 46.954 35.901 1.00 88.07 C HETATM 2868 C2' BOG A 412 11.585 48.254 35.445 1.00 76.45 C HETATM 2869 C3' BOG A 412 10.655 48.044 34.255 1.00 88.95 C HETATM 2870 C4' BOG A 412 9.316 48.764 34.420 1.00 96.93 C HETATM 2871 C5' BOG A 412 8.337 48.425 33.295 1.00 94.32 C HETATM 2872 C6' BOG A 412 6.868 48.546 33.697 1.00 82.72 C HETATM 2873 C7' BOG A 412 6.527 47.693 34.916 1.00 81.77 C HETATM 2874 C8' BOG A 412 6.144 46.261 34.543 1.00 66.86 C HETATM 2875 S SO4 B 401 -5.760 9.452 37.151 1.00128.68 S HETATM 2876 O1 SO4 B 401 -4.933 10.502 36.556 1.00137.39 O HETATM 2877 O2 SO4 B 401 -6.424 8.708 36.082 1.00133.81 O HETATM 2878 O3 SO4 B 401 -6.772 10.047 38.027 1.00125.09 O HETATM 2879 O4 SO4 B 401 -4.907 8.558 37.929 1.00 92.21 O HETATM 2880 O HOH A 501 9.221 24.047 28.987 1.00 71.13 O HETATM 2881 O HOH A 502 21.483 51.682 27.670 1.00 61.56 O HETATM 2882 O HOH A 503 21.416 57.559 37.252 1.00 50.40 O HETATM 2883 O HOH A 504 6.607 35.120 42.105 1.00 63.30 O HETATM 2884 O HOH A 505 26.305 56.637 57.973 1.00 62.11 O HETATM 2885 O HOH A 506 19.443 70.214 39.964 1.00 57.88 O HETATM 2886 O HOH A 507 19.860 61.739 30.866 1.00 66.62 O HETATM 2887 O HOH A 508 -12.347 18.273 35.408 1.00 62.10 O HETATM 2888 O HOH A 509 -2.407 15.598 29.240 1.00 94.47 O CONECT 117 2698 CONECT 883 1487 CONECT 1487 883 CONECT 2585 2828 CONECT 2698 117 2699 2709 CONECT 2699 2698 2700 2706 CONECT 2700 2699 2701 2707 CONECT 2701 2700 2702 2708 CONECT 2702 2701 2703 2709 CONECT 2703 2702 2710 CONECT 2704 2705 2706 2711 CONECT 2705 2704 CONECT 2706 2699 2704 CONECT 2707 2700 CONECT 2708 2701 2712 CONECT 2709 2698 2702 CONECT 2710 2703 CONECT 2711 2704 CONECT 2712 2708 2713 2723 CONECT 2713 2712 2714 2720 CONECT 2714 2713 2715 2721 CONECT 2715 2714 2716 2722 CONECT 2716 2715 2717 2723 CONECT 2717 2716 2724 CONECT 2718 2719 2720 2725 CONECT 2719 2718 CONECT 2720 2713 2718 CONECT 2721 2714 CONECT 2722 2715 2726 CONECT 2723 2712 2716 CONECT 2724 2717 CONECT 2725 2718 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 2737 CONECT 2734 2729 CONECT 2735 2726 2730 CONECT 2736 2731 CONECT 2737 2733 2738 2746 CONECT 2738 2737 2739 2743 CONECT 2739 2738 2740 2744 CONECT 2740 2739 2741 2745 CONECT 2741 2740 2742 2746 CONECT 2742 2741 2747 CONECT 2743 2738 CONECT 2744 2739 CONECT 2745 2740 CONECT 2746 2737 2741 CONECT 2747 2742 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 2769 2770 2777 CONECT 2769 2768 2780 CONECT 2770 2768 2771 2772 CONECT 2771 2770 CONECT 2772 2770 2773 2774 CONECT 2773 2772 CONECT 2774 2772 2775 2776 CONECT 2775 2774 CONECT 2776 2774 2777 2778 CONECT 2777 2768 2776 CONECT 2778 2776 2779 CONECT 2779 2778 CONECT 2780 2769 2781 CONECT 2781 2780 2782 CONECT 2782 2781 2783 CONECT 2783 2782 2784 CONECT 2784 2783 2785 CONECT 2785 2784 2786 CONECT 2786 2785 2787 CONECT 2787 2786 CONECT 2788 2789 2790 2797 CONECT 2789 2788 2800 CONECT 2790 2788 2791 2792 CONECT 2791 2790 CONECT 2792 2790 2793 2794 CONECT 2793 2792 CONECT 2794 2792 2795 2796 CONECT 2795 2794 CONECT 2796 2794 2797 2798 CONECT 2797 2788 2796 CONECT 2798 2796 2799 CONECT 2799 2798 CONECT 2800 2789 2801 CONECT 2801 2800 2802 CONECT 2802 2801 2803 CONECT 2803 2802 2804 CONECT 2804 2803 2805 CONECT 2805 2804 2806 CONECT 2806 2805 2807 CONECT 2807 2806 CONECT 2808 2809 2810 2817 CONECT 2809 2808 2820 CONECT 2810 2808 2811 2812 CONECT 2811 2810 CONECT 2812 2810 2813 2814 CONECT 2813 2812 CONECT 2814 2812 2815 2816 CONECT 2815 2814 CONECT 2816 2814 2817 2818 CONECT 2817 2808 2816 CONECT 2818 2816 2819 CONECT 2819 2818 CONECT 2820 2809 2821 CONECT 2821 2820 2822 CONECT 2822 2821 2823 CONECT 2823 2822 2824 CONECT 2824 2823 2825 CONECT 2825 2824 2826 CONECT 2826 2825 2827 CONECT 2827 2826 CONECT 2828 2585 2829 2830 CONECT 2829 2828 CONECT 2830 2828 2831 CONECT 2831 2830 2832 CONECT 2832 2831 2833 CONECT 2833 2832 2834 CONECT 2834 2833 2835 CONECT 2835 2834 2836 CONECT 2836 2835 2837 CONECT 2837 2836 2838 CONECT 2838 2837 2839 CONECT 2839 2838 2840 CONECT 2840 2839 2841 CONECT 2841 2840 2842 CONECT 2842 2841 2843 CONECT 2843 2842 2844 CONECT 2844 2843 CONECT 2845 2846 2847 2848 2849 CONECT 2846 2845 CONECT 2847 2845 CONECT 2848 2845 CONECT 2849 2845 CONECT 2850 2851 2852 2853 2854 CONECT 2851 2850 CONECT 2852 2850 CONECT 2853 2850 CONECT 2854 2850 CONECT 2855 2856 2857 2864 CONECT 2856 2855 2867 CONECT 2857 2855 2858 2859 CONECT 2858 2857 CONECT 2859 2857 2860 2861 CONECT 2860 2859 CONECT 2861 2859 2862 2863 CONECT 2862 2861 CONECT 2863 2861 2864 2865 CONECT 2864 2855 2863 CONECT 2865 2863 2866 CONECT 2866 2865 CONECT 2867 2856 2868 CONECT 2868 2867 2869 CONECT 2869 2868 2870 CONECT 2870 2869 2871 CONECT 2871 2870 2872 CONECT 2872 2871 2873 CONECT 2873 2872 2874 CONECT 2874 2873 CONECT 2875 2876 2877 2878 2879 CONECT 2876 2875 CONECT 2877 2875 CONECT 2878 2875 CONECT 2879 2875 MASTER 430 0 13 15 4 0 0 6 2872 2 186 28 END