HEADER SIGNALING PROTEIN 25-JUN-19 6PH7 TITLE CRYSTAL STRUCTURE OF BOVINE OPSIN WITH NEROL BOUND CAVEAT 6PH7 NAG C 1 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: G PROTEIN CT2 PEPTIDE; COMPND 6 CHAIN: B; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 8 ORGANISM_TAXID: 9913 KEYWDS OLFACTORY RECEPTOR, ODORANT, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.T.EGER,T.MORIZUMI,O.P.ERNST REVDAT 2 29-JUL-20 6PH7 1 CAVEAT COMPND REMARK HETNAM REVDAT 2 2 1 LINK SITE ATOM REVDAT 1 01-JUL-20 6PH7 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. 2.90 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 26877 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 1364 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.2592 - 6.2449 0.97 2575 153 0.2151 0.1986 REMARK 3 2 6.2449 - 4.9599 0.99 2561 137 0.2128 0.2179 REMARK 3 3 4.9599 - 4.3338 0.98 2541 145 0.1753 0.2053 REMARK 3 4 4.3338 - 3.9380 0.99 2559 117 0.1876 0.1885 REMARK 3 5 3.9380 - 3.6560 1.00 2556 128 0.1962 0.2283 REMARK 3 6 3.6560 - 3.4405 1.00 2577 128 0.2196 0.2501 REMARK 3 7 3.4405 - 3.2683 1.00 2570 123 0.2538 0.3067 REMARK 3 8 3.2683 - 3.1261 0.99 2492 164 0.2622 0.3077 REMARK 3 9 3.1261 - 3.0058 0.99 2519 140 0.2991 0.3242 REMARK 3 10 3.0058 - 2.9021 1.00 2563 129 0.3376 0.3620 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.210 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 : 0.003 2880 REMARK 3 ANGLE : 0.662 3918 REMARK 3 CHIRALITY : 0.043 445 REMARK 3 PLANARITY : 0.005 475 REMARK 3 DIHEDRAL : 12.767 1736 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): 19.9795 41.8092 39.3821 REMARK 3 T TENSOR REMARK 3 T11: 0.5517 T22: 0.4850 REMARK 3 T33: 0.6863 T12: 0.0334 REMARK 3 T13: -0.0479 T23: 0.0806 REMARK 3 L TENSOR REMARK 3 L11: 2.7591 L22: 2.1443 REMARK 3 L33: 1.6727 L12: 1.0065 REMARK 3 L13: -0.0511 L23: -0.3347 REMARK 3 S TENSOR REMARK 3 S11: -0.0733 S12: 0.0638 S13: 0.1430 REMARK 3 S21: 0.0002 S22: 0.1039 S23: -0.4555 REMARK 3 S31: -0.0733 S32: 0.0845 S33: 0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 140:168) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1591 26.0880 24.1722 REMARK 3 T TENSOR REMARK 3 T11: 1.1855 T22: 0.7390 REMARK 3 T33: 0.7998 T12: -0.1507 REMARK 3 T13: -0.0517 T23: -0.0439 REMARK 3 L TENSOR REMARK 3 L11: 1.4808 L22: 0.3833 REMARK 3 L33: 0.3606 L12: 0.0711 REMARK 3 L13: -0.0509 L23: 0.3564 REMARK 3 S TENSOR REMARK 3 S11: -0.1699 S12: 0.9023 S13: -0.3336 REMARK 3 S21: -0.4311 S22: 0.0706 S23: 0.9058 REMARK 3 S31: 0.4043 S32: -0.6326 S33: 0.0044 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 169:222) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5767 49.5387 29.8266 REMARK 3 T TENSOR REMARK 3 T11: 0.8265 T22: 0.5790 REMARK 3 T33: 0.8880 T12: -0.0365 REMARK 3 T13: -0.1530 T23: 0.2299 REMARK 3 L TENSOR REMARK 3 L11: 1.2197 L22: -0.1171 REMARK 3 L33: 0.8144 L12: 0.0216 REMARK 3 L13: -0.3674 L23: 0.0542 REMARK 3 S TENSOR REMARK 3 S11: -0.2825 S12: 0.1182 S13: 0.9843 REMARK 3 S21: -0.4818 S22: 0.1722 S23: -0.4687 REMARK 3 S31: -0.6836 S32: 0.2621 S33: 0.0227 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 223:287) REMARK 3 ORIGIN FOR THE GROUP (A): -1.6950 35.0001 41.3843 REMARK 3 T TENSOR REMARK 3 T11: 0.5706 T22: 0.6733 REMARK 3 T33: 0.7351 T12: 0.0432 REMARK 3 T13: -0.1264 T23: 0.0247 REMARK 3 L TENSOR REMARK 3 L11: 3.3349 L22: 1.9074 REMARK 3 L33: 3.4888 L12: -2.5283 REMARK 3 L13: -0.4690 L23: -0.1908 REMARK 3 S TENSOR REMARK 3 S11: -0.2127 S12: 0.3183 S13: 0.4819 REMARK 3 S21: -0.4240 S22: 0.1634 S23: 0.4588 REMARK 3 S31: -0.1335 S32: -0.3397 S33: 0.0002 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 288:326) REMARK 3 ORIGIN FOR THE GROUP (A): 13.2268 27.3972 46.1274 REMARK 3 T TENSOR REMARK 3 T11: 0.7703 T22: 0.6235 REMARK 3 T33: 0.8474 T12: -0.0142 REMARK 3 T13: -0.1205 T23: -0.0158 REMARK 3 L TENSOR REMARK 3 L11: 1.2274 L22: 0.1837 REMARK 3 L33: 0.6539 L12: 0.0802 REMARK 3 L13: 1.0923 L23: -0.3883 REMARK 3 S TENSOR REMARK 3 S11: -0.1607 S12: 0.1447 S13: -0.2646 REMARK 3 S21: 0.2806 S22: 0.3140 S23: 0.0731 REMARK 3 S31: 0.1200 S32: -0.1538 S33: 0.0002 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 340:344) REMARK 3 ORIGIN FOR THE GROUP (A): -2.8099 13.8031 36.8931 REMARK 3 T TENSOR REMARK 3 T11: 1.4007 T22: 1.0846 REMARK 3 T33: 1.9334 T12: -0.1124 REMARK 3 T13: 0.0569 T23: 0.1339 REMARK 3 L TENSOR REMARK 3 L11: 0.1521 L22: 0.0058 REMARK 3 L33: 0.0334 L12: -0.0346 REMARK 3 L13: 0.0424 L23: -0.0155 REMARK 3 S TENSOR REMARK 3 S11: -0.5951 S12: 0.3580 S13: -0.9648 REMARK 3 S21: -1.0167 S22: 0.1010 S23: -0.6787 REMARK 3 S31: 1.2664 S32: 1.2726 S33: -0.0013 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN B AND RESID 345:350) REMARK 3 ORIGIN FOR THE GROUP (A): 1.6271 16.7752 39.5409 REMARK 3 T TENSOR REMARK 3 T11: 1.0481 T22: 1.0534 REMARK 3 T33: 1.2838 T12: -0.2212 REMARK 3 T13: -0.0618 T23: 0.1260 REMARK 3 L TENSOR REMARK 3 L11: 0.0551 L22: 0.0460 REMARK 3 L33: 0.0303 L12: 0.0226 REMARK 3 L13: 0.0453 L23: -0.0147 REMARK 3 S TENSOR REMARK 3 S11: 0.5644 S12: -0.2453 S13: -0.4286 REMARK 3 S21: 0.5160 S22: 0.9573 S23: 0.2569 REMARK 3 S31: 0.6963 S32: -0.0567 S33: 0.0027 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 6PH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1000242515. 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 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26899 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 39.730 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : 0.05400 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : 6.60 REMARK 200 R MERGE FOR SHELL (I) : 0.58800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900 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: NULL 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: 3.1-3.3 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 121.56850 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.18761 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.14233 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.56850 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.18761 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.14233 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.56850 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.18761 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.14233 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.56850 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.18761 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.14233 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.56850 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.18761 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.14233 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.56850 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.18761 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.14233 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.37521 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 72.28467 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.37521 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 72.28467 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.37521 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 72.28467 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.37521 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 72.28467 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.37521 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 72.28467 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.37521 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 72.28467 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 108.42700 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 SG CYS A 323 C1 PLM A 406 1.62 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 GLU A 25 -31.70 -136.61 REMARK 500 GLN A 28 48.16 -107.20 REMARK 500 ARG A 69 59.45 -90.33 REMARK 500 ALA A 166 4.79 -68.47 REMARK 500 SER A 176 -162.35 60.80 REMARK 500 HIS A 195 93.37 -54.91 REMARK 500 PHE A 212 -46.48 -144.66 REMARK 500 GLN A 237 51.83 -154.08 REMARK 500 THR A 277 -70.31 -68.27 REMARK 500 ILE A 307 -61.12 -120.44 REMARK 500 CYS A 322 37.65 -92.63 REMARK 500 CYS A 323 -1.16 65.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PLM A 406 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6PEL RELATED DB: PDB REMARK 900 RELATED ID: 6NWE RELATED DB: PDB REMARK 900 RELATED ID: 6PGS RELATED DB: PDB DBREF 6PH7 A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 6PH7 B 340 350 PDB 6PH7 6PH7 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 401 20 HET PLM A 406 17 HET NZZ A 407 11 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 NZZ (2Z)-3,7-DIMETHYLOCTA-2,6-DIEN-1-OL HETSYN NZZ NEROL FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 3 BMA 2(C6 H12 O6) FORMUL 4 BOG C14 H28 O6 FORMUL 5 PLM C16 H32 O2 FORMUL 6 NZZ C10 H18 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 LEU A 72 5 3 HELIX 4 AA4 ASN A 73 GLY A 90 1 18 HELIX 5 AA5 GLY A 90 GLY A 101 1 12 HELIX 6 AA6 PHE A 105 LYS A 141 1 37 HELIX 7 AA7 GLY A 149 ALA A 169 1 21 HELIX 8 AA8 PRO A 170 VAL A 173 5 4 HELIX 9 AA9 HIS A 195 THR A 198 5 4 HELIX 10 AB1 ASN A 199 HIS A 211 1 13 HELIX 11 AB2 PHE A 212 GLN A 236 1 25 HELIX 12 AB3 SER A 240 HIS A 278 1 39 HELIX 13 AB4 GLY A 284 THR A 297 1 14 HELIX 14 AB5 THR A 297 ILE A 307 1 11 HELIX 15 AB6 ASN A 310 CYS A 322 1 13 HELIX 16 AB7 LEU B 341 VAL B 347 1 7 SHEET 1 AA1 2 THR A 4 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.03 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.43 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44 LINK O3 BMA C 3 C1 BMA C 4 1555 1555 1.46 CRYST1 243.137 243.137 108.427 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 0.004113 0.002375 0.000000 0.00000 SCALE2 0.000000 0.004749 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009223 0.00000 ATOM 1 N MET A 1 12.198 72.035 40.194 1.00119.28 N ANISOU 1 N MET A 1 15251 9167 20903 1212 -270 1178 N ATOM 2 CA MET A 1 13.148 71.131 39.555 1.00126.62 C ANISOU 2 CA MET A 1 16181 10406 21523 1015 -350 1321 C ATOM 3 C MET A 1 14.001 70.418 40.604 1.00110.87 C ANISOU 3 C MET A 1 14261 8600 19263 895 -332 982 C ATOM 4 O MET A 1 14.665 71.058 41.420 1.00120.22 O ANISOU 4 O MET A 1 15531 9583 20565 815 -314 725 O ATOM 5 CB MET A 1 14.031 71.900 38.572 1.00137.72 C ANISOU 5 CB MET A 1 17599 11625 23102 850 -421 1585 C ATOM 6 CG MET A 1 14.992 71.035 37.780 1.00144.48 C ANISOU 6 CG MET A 1 18439 12791 23665 651 -483 1755 C ATOM 7 SD MET A 1 16.065 72.028 36.725 1.00154.13 S ANISOU 7 SD MET A 1 19676 13786 25101 439 -544 2042 S ATOM 8 CE MET A 1 14.860 73.060 35.892 1.00160.78 C ANISOU 8 CE MET A 1 20466 14336 26287 608 -570 2385 C ATOM 9 N ASN A 2 13.984 69.085 40.570 1.00 89.49 N ANISOU 9 N ASN A 2 11521 6280 16202 876 -348 989 N ATOM 10 CA ASN A 2 14.562 68.268 41.631 1.00101.54 C ANISOU 10 CA ASN A 2 13102 8016 17464 801 -338 687 C ATOM 11 C ASN A 2 15.412 67.132 41.073 1.00100.09 C ANISOU 11 C ASN A 2 12888 8156 16986 653 -402 809 C ATOM 12 O ASN A 2 15.541 66.079 41.704 1.00 86.03 O ANISOU 12 O ASN A 2 11115 6637 14935 639 -403 654 O ATOM 13 CB ASN A 2 13.458 67.723 42.536 1.00105.88 C ANISOU 13 CB ASN A 2 13646 8694 17891 972 -261 489 C ATOM 14 CG ASN A 2 12.078 67.886 41.923 1.00117.54 C ANISOU 14 CG ASN A 2 15030 10131 19498 1169 -225 696 C ATOM 15 OD1 ASN A 2 11.884 67.636 40.733 1.00117.97 O ANISOU 15 OD1 ASN A 2 15011 10279 19533 1164 -283 1023 O ATOM 16 ND2 ASN A 2 11.119 68.330 42.727 1.00116.80 N ANISOU 16 ND2 ASN A 2 14933 9900 19544 1339 -128 506 N ATOM 17 N GLY A 3 15.997 67.330 39.886 1.00102.16 N ANISOU 17 N GLY A 3 13113 8401 17302 541 -452 1089 N ATOM 18 CA GLY A 3 16.888 66.349 39.306 1.00 82.22 C ANISOU 18 CA GLY A 3 10554 6155 14531 396 -492 1192 C ATOM 19 C GLY A 3 18.049 67.031 38.610 1.00 83.45 C ANISOU 19 C GLY A 3 10707 6175 14824 211 -526 1331 C ATOM 20 O GLY A 3 18.046 68.246 38.397 1.00 93.99 O ANISOU 20 O GLY A 3 12065 7201 16445 198 -529 1407 O ATOM 21 N THR A 4 19.050 66.225 38.262 1.00 82.64 N ANISOU 21 N THR A 4 10570 6302 14528 66 -547 1365 N ATOM 22 CA THR A 4 20.234 66.699 37.555 1.00 72.32 C ANISOU 22 CA THR A 4 9239 4927 13314 -128 -566 1503 C ATOM 23 C THR A 4 20.492 65.779 36.373 1.00 73.99 C ANISOU 23 C THR A 4 9382 5423 13310 -197 -553 1736 C ATOM 24 O THR A 4 20.666 64.569 36.552 1.00 79.86 O ANISOU 24 O THR A 4 10096 6440 13806 -190 -544 1648 O ATOM 25 CB THR A 4 21.454 66.741 38.478 1.00 72.55 C ANISOU 25 CB THR A 4 9281 4931 13355 -265 -594 1254 C ATOM 26 OG1 THR A 4 21.158 67.545 39.626 1.00 74.25 O ANISOU 26 OG1 THR A 4 9575 4900 13737 -209 -601 1004 O ATOM 27 CG2 THR A 4 22.640 67.336 37.748 1.00 73.98 C ANISOU 27 CG2 THR A 4 9422 5022 13667 -470 -607 1403 C ATOM 28 N GLU A 5 20.523 66.351 35.174 1.00 87.20 N ANISOU 28 N GLU A 5 11034 7025 15072 -269 -549 2031 N ATOM 29 CA GLU A 5 20.665 65.587 33.945 1.00 71.03 C ANISOU 29 CA GLU A 5 8934 5241 12814 -343 -525 2264 C ATOM 30 C GLU A 5 22.110 65.583 33.464 1.00 95.17 C ANISOU 30 C GLU A 5 11945 8358 15857 -557 -498 2309 C ATOM 31 O GLU A 5 22.865 66.535 33.678 1.00114.54 O ANISOU 31 O GLU A 5 14405 10589 18528 -668 -512 2288 O ATOM 32 CB GLU A 5 19.769 66.150 32.841 1.00 76.35 C ANISOU 32 CB GLU A 5 9610 5848 13554 -306 -540 2589 C ATOM 33 CG GLU A 5 18.288 66.152 33.167 1.00 90.75 C ANISOU 33 CG GLU A 5 11447 7626 15406 -91 -565 2585 C ATOM 34 CD GLU A 5 17.448 66.704 32.031 1.00108.78 C ANISOU 34 CD GLU A 5 13714 9856 17764 -63 -602 2938 C ATOM 35 OE1 GLU A 5 18.004 66.958 30.943 1.00114.84 O ANISOU 35 OE1 GLU A 5 14469 10659 18505 -222 -606 3190 O ATOM 36 OE2 GLU A 5 16.230 66.885 32.224 1.00118.57 O ANISOU 36 OE2 GLU A 5 14943 11022 19084 113 -629 2972 O ATOM 37 N GLY A 6 22.479 64.494 32.802 1.00101.32 N ANISOU 37 N GLY A 6 12673 9438 16387 -618 -453 2366 N ATOM 38 CA GLY A 6 23.756 64.384 32.145 1.00102.66 C ANISOU 38 CA GLY A 6 12778 9706 16523 -813 -402 2440 C ATOM 39 C GLY A 6 23.598 63.692 30.810 1.00106.93 C ANISOU 39 C GLY A 6 13292 10501 16834 -868 -340 2661 C ATOM 40 O GLY A 6 22.492 63.314 30.411 1.00112.49 O ANISOU 40 O GLY A 6 14030 11301 17408 -762 -354 2761 O ATOM 41 N PRO A 7 24.704 63.520 30.085 1.00106.61 N ANISOU 41 N PRO A 7 13187 10584 16737 -1045 -265 2738 N ATOM 42 CA PRO A 7 24.618 62.845 28.780 1.00111.68 C ANISOU 42 CA PRO A 7 13812 11486 17136 -1120 -186 2927 C ATOM 43 C PRO A 7 24.086 61.420 28.852 1.00109.78 C ANISOU 43 C PRO A 7 13572 11503 16636 -1007 -161 2799 C ATOM 44 O PRO A 7 23.406 60.983 27.915 1.00105.61 O ANISOU 44 O PRO A 7 13073 11143 15912 -1011 -138 2955 O ATOM 45 CB PRO A 7 26.065 62.891 28.273 1.00110.26 C ANISOU 45 CB PRO A 7 13545 11379 16971 -1325 -91 2954 C ATOM 46 CG PRO A 7 26.656 64.088 28.949 1.00103.61 C ANISOU 46 CG PRO A 7 12694 10243 16430 -1387 -148 2920 C ATOM 47 CD PRO A 7 26.028 64.122 30.314 1.00102.65 C ANISOU 47 CD PRO A 7 12625 9968 16411 -1205 -247 2688 C ATOM 48 N ASN A 8 24.349 60.684 29.939 1.00102.41 N ANISOU 48 N ASN A 8 12613 10604 15693 -916 -175 2528 N ATOM 49 CA ASN A 8 23.952 59.281 30.003 1.00 91.81 C ANISOU 49 CA ASN A 8 11269 9495 14120 -824 -146 2410 C ATOM 50 C ASN A 8 23.409 58.886 31.372 1.00 77.11 C ANISOU 50 C ASN A 8 9435 7577 12286 -655 -224 2184 C ATOM 51 O ASN A 8 23.556 57.730 31.786 1.00 82.03 O ANISOU 51 O ASN A 8 10033 8354 12779 -602 -206 2027 O ATOM 52 CB ASN A 8 25.123 58.364 29.645 1.00 88.05 C ANISOU 52 CB ASN A 8 10704 9213 13539 -925 -40 2328 C ATOM 53 CG ASN A 8 25.289 58.188 28.154 1.00 91.42 C ANISOU 53 CG ASN A 8 11121 9812 13801 -1063 70 2522 C ATOM 54 OD1 ASN A 8 24.314 58.206 27.403 1.00 97.14 O ANISOU 54 OD1 ASN A 8 11915 10603 14390 -1052 57 2686 O ATOM 55 ND2 ASN A 8 26.528 58.006 27.716 1.00 87.99 N ANISOU 55 ND2 ASN A 8 10594 9466 13371 -1200 180 2505 N ATOM 56 N PHE A 9 22.773 59.811 32.086 1.00 76.36 N ANISOU 56 N PHE A 9 9394 7262 12358 -571 -304 2165 N ATOM 57 CA PHE A 9 22.277 59.510 33.423 1.00 81.64 C ANISOU 57 CA PHE A 9 10094 7883 13042 -426 -364 1942 C ATOM 58 C PHE A 9 21.237 60.547 33.830 1.00 93.10 C ANISOU 58 C PHE A 9 11610 9112 14651 -321 -420 1975 C ATOM 59 O PHE A 9 20.976 61.518 33.113 1.00 78.59 O ANISOU 59 O PHE A 9 9787 7135 12938 -358 -425 2176 O ATOM 60 CB PHE A 9 23.422 59.454 34.441 1.00 84.16 C ANISOU 60 CB PHE A 9 10371 8158 13448 -476 -388 1729 C ATOM 61 CG PHE A 9 24.234 60.722 34.522 1.00 82.69 C ANISOU 61 CG PHE A 9 10171 7750 13496 -596 -407 1753 C ATOM 62 CD1 PHE A 9 23.847 61.764 35.352 1.00 79.73 C ANISOU 62 CD1 PHE A 9 9861 7125 13308 -549 -469 1670 C ATOM 63 CD2 PHE A 9 25.395 60.862 33.780 1.00 84.55 C ANISOU 63 CD2 PHE A 9 10328 8026 13773 -764 -354 1849 C ATOM 64 CE1 PHE A 9 24.599 62.923 35.430 1.00 87.94 C ANISOU 64 CE1 PHE A 9 10895 7944 14575 -672 -489 1683 C ATOM 65 CE2 PHE A 9 26.151 62.019 33.855 1.00 81.14 C ANISOU 65 CE2 PHE A 9 9879 7388 13563 -891 -374 1878 C ATOM 66 CZ PHE A 9 25.753 63.050 34.681 1.00 78.60 C ANISOU 66 CZ PHE A 9 9630 6804 13430 -848 -448 1795 C ATOM 67 N TYR A 10 20.649 60.325 35.007 1.00 89.19 N ANISOU 67 N TYR A 10 11150 8583 14156 -189 -458 1776 N ATOM 68 CA TYR A 10 19.692 61.251 35.609 1.00 72.70 C ANISOU 68 CA TYR A 10 9114 6277 12230 -70 -491 1744 C ATOM 69 C TYR A 10 19.737 61.016 37.117 1.00 73.30 C ANISOU 69 C TYR A 10 9221 6327 12302 -2 -517 1451 C ATOM 70 O TYR A 10 19.161 60.043 37.611 1.00 83.87 O ANISOU 70 O TYR A 10 10567 7832 13469 91 -516 1352 O ATOM 71 CB TYR A 10 18.289 61.044 35.053 1.00 73.87 C ANISOU 71 CB TYR A 10 9269 6494 12304 52 -491 1898 C ATOM 72 CG TYR A 10 17.225 61.864 35.757 1.00 77.24 C ANISOU 72 CG TYR A 10 9727 6713 12906 204 -509 1843 C ATOM 73 CD1 TYR A 10 16.991 63.187 35.403 1.00 70.76 C ANISOU 73 CD1 TYR A 10 8917 5628 12341 212 -524 1984 C ATOM 74 CD2 TYR A 10 16.455 61.313 36.774 1.00 66.76 C ANISOU 74 CD2 TYR A 10 8416 5450 11498 339 -504 1650 C ATOM 75 CE1 TYR A 10 16.023 63.938 36.047 1.00 81.85 C ANISOU 75 CE1 TYR A 10 10340 6825 13933 365 -526 1919 C ATOM 76 CE2 TYR A 10 15.488 62.055 37.422 1.00 75.69 C ANISOU 76 CE2 TYR A 10 9567 6399 12793 481 -497 1581 C ATOM 77 CZ TYR A 10 15.275 63.365 37.055 1.00 90.76 C ANISOU 77 CZ TYR A 10 11478 8034 14972 501 -504 1708 C ATOM 78 OH TYR A 10 14.309 64.100 37.704 1.00 95.78 O ANISOU 78 OH TYR A 10 12123 8473 15797 658 -482 1626 O ATOM 79 N VAL A 11 20.431 61.894 37.834 1.00 70.08 N ANISOU 79 N VAL A 11 8837 5718 12072 -64 -543 1316 N ATOM 80 CA VAL A 11 20.502 61.802 39.290 1.00 74.11 C ANISOU 80 CA VAL A 11 9390 6198 12570 -23 -575 1033 C ATOM 81 C VAL A 11 19.263 62.472 39.871 1.00 81.91 C ANISOU 81 C VAL A 11 10440 7020 13660 127 -557 958 C ATOM 82 O VAL A 11 19.018 63.658 39.604 1.00 93.01 O ANISOU 82 O VAL A 11 11869 8173 15299 137 -547 1029 O ATOM 83 CB VAL A 11 21.792 62.440 39.832 1.00 77.80 C ANISOU 83 CB VAL A 11 9855 6534 13172 -173 -617 904 C ATOM 84 CG1 VAL A 11 21.831 62.357 41.353 1.00 77.13 C ANISOU 84 CG1 VAL A 11 9825 6436 13044 -147 -662 611 C ATOM 85 CG2 VAL A 11 23.013 61.761 39.229 1.00 74.27 C ANISOU 85 CG2 VAL A 11 9317 6258 12644 -311 -622 985 C ATOM 86 N PRO A 12 18.440 61.749 40.666 1.00 81.78 N ANISOU 86 N PRO A 12 10448 7134 13491 249 -545 818 N ATOM 87 CA PRO A 12 17.221 62.344 41.244 1.00 70.54 C ANISOU 87 CA PRO A 12 9067 5570 12166 401 -506 733 C ATOM 88 C PRO A 12 17.523 63.236 42.445 1.00 70.37 C ANISOU 88 C PRO A 12 9119 5336 12282 381 -507 466 C ATOM 89 O PRO A 12 17.083 62.986 43.571 1.00 73.23 O ANISOU 89 O PRO A 12 9528 5747 12548 446 -486 241 O ATOM 90 CB PRO A 12 16.403 61.101 41.620 1.00 62.43 C ANISOU 90 CB PRO A 12 8027 4800 10892 502 -488 686 C ATOM 91 CG PRO A 12 17.437 60.086 41.974 1.00 61.32 C ANISOU 91 CG PRO A 12 7881 4859 10560 393 -534 600 C ATOM 92 CD PRO A 12 18.598 60.332 41.040 1.00 73.20 C ANISOU 92 CD PRO A 12 9341 6327 12143 249 -560 744 C ATOM 93 N PHE A 13 18.288 64.298 42.204 1.00 68.13 N ANISOU 93 N PHE A 13 8850 4818 12219 276 -528 487 N ATOM 94 CA PHE A 13 18.665 65.224 43.262 1.00 70.22 C ANISOU 94 CA PHE A 13 9193 4859 12630 227 -533 228 C ATOM 95 C PHE A 13 19.011 66.568 42.633 1.00 93.07 C ANISOU 95 C PHE A 13 12095 7430 15838 162 -535 342 C ATOM 96 O PHE A 13 19.711 66.620 41.619 1.00 91.58 O ANISOU 96 O PHE A 13 11851 7252 15691 51 -565 566 O ATOM 97 CB PHE A 13 19.846 64.676 44.074 1.00 69.62 C ANISOU 97 CB PHE A 13 9129 4927 12397 76 -605 44 C ATOM 98 CG PHE A 13 20.084 65.403 45.364 1.00 73.23 C ANISOU 98 CG PHE A 13 9680 5222 12922 25 -618 -267 C ATOM 99 CD1 PHE A 13 20.927 66.501 45.408 1.00 74.33 C ANISOU 99 CD1 PHE A 13 9848 5108 13285 -115 -652 -327 C ATOM 100 CD2 PHE A 13 19.470 64.987 46.534 1.00 76.43 C ANISOU 100 CD2 PHE A 13 10148 5734 13157 101 -593 -504 C ATOM 101 CE1 PHE A 13 21.150 67.175 46.593 1.00 76.00 C ANISOU 101 CE1 PHE A 13 10157 5171 13550 -180 -666 -633 C ATOM 102 CE2 PHE A 13 19.689 65.658 47.724 1.00 91.58 C ANISOU 102 CE2 PHE A 13 12166 7521 15111 38 -599 -808 C ATOM 103 CZ PHE A 13 20.531 66.753 47.752 1.00 75.86 C ANISOU 103 CZ PHE A 13 10209 5272 13343 -104 -638 -880 C ATOM 104 N SER A 14 18.514 67.646 43.237 1.00 86.57 N ANISOU 104 N SER A 14 11340 6316 15237 229 -493 186 N ATOM 105 CA SER A 14 18.720 68.979 42.684 1.00 86.82 C ANISOU 105 CA SER A 14 11387 5998 15603 183 -492 296 C ATOM 106 C SER A 14 20.175 69.410 42.826 1.00 93.65 C ANISOU 106 C SER A 14 12271 6774 16537 -48 -558 225 C ATOM 107 O SER A 14 20.817 69.166 43.851 1.00 97.89 O ANISOU 107 O SER A 14 12850 7388 16956 -143 -595 -39 O ATOM 108 CB SER A 14 17.808 69.992 43.375 1.00 86.02 C ANISOU 108 CB SER A 14 11354 5588 15742 324 -419 113 C ATOM 109 OG SER A 14 18.096 71.314 42.948 1.00 93.43 O ANISOU 109 OG SER A 14 12317 6151 17029 268 -424 197 O ATOM 110 N ASN A 15 20.692 70.068 41.789 1.00 92.01 N ANISOU 110 N ASN A 15 12027 6412 16521 -150 -580 475 N ATOM 111 CA ASN A 15 22.062 70.560 41.779 1.00 95.30 C ANISOU 111 CA ASN A 15 12442 6731 17038 -381 -638 449 C ATOM 112 C ASN A 15 22.152 72.040 42.136 1.00 84.58 C ANISOU 112 C ASN A 15 11166 4943 16027 -431 -632 336 C ATOM 113 O ASN A 15 23.126 72.703 41.766 1.00 95.90 O ANISOU 113 O ASN A 15 12588 6222 17627 -620 -673 416 O ATOM 114 CB ASN A 15 22.702 70.303 40.412 1.00 98.94 C ANISOU 114 CB ASN A 15 12807 7313 17472 -495 -654 791 C ATOM 115 CG ASN A 15 24.212 70.178 40.486 1.00109.80 C ANISOU 115 CG ASN A 15 14133 8772 18815 -729 -710 746 C ATOM 116 OD1 ASN A 15 24.788 70.092 41.571 1.00 80.69 O ANISOU 116 OD1 ASN A 15 10473 5105 15079 -805 -757 468 O ATOM 117 ND2 ASN A 15 24.860 70.155 39.327 1.00124.14 N ANISOU 117 ND2 ASN A 15 15867 10651 20649 -852 -705 1024 N ATOM 118 N LYS A 16 21.156 72.574 42.851 1.00 97.11 N ANISOU 118 N LYS A 16 12832 6327 17737 -269 -573 146 N ATOM 119 CA LYS A 16 21.181 73.988 43.208 1.00 89.57 C ANISOU 119 CA LYS A 16 11963 4932 17136 -303 -554 16 C ATOM 120 C LYS A 16 22.230 74.300 44.264 1.00 90.91 C ANISOU 120 C LYS A 16 12206 5037 17300 -504 -605 -312 C ATOM 121 O LYS A 16 22.522 75.476 44.498 1.00 95.01 O ANISOU 121 O LYS A 16 12797 5189 18113 -593 -604 -421 O ATOM 122 CB LYS A 16 19.809 74.448 43.704 1.00 90.93 C ANISOU 122 CB LYS A 16 12189 4906 17453 -62 -457 -121 C ATOM 123 CG LYS A 16 19.338 73.759 44.974 1.00109.82 C ANISOU 123 CG LYS A 16 14633 7500 19593 28 -411 -472 C ATOM 124 CD LYS A 16 18.219 74.538 45.650 1.00110.63 C ANISOU 124 CD LYS A 16 14804 7319 19911 220 -294 -690 C ATOM 125 CE LYS A 16 17.517 73.695 46.704 1.00111.10 C ANISOU 125 CE LYS A 16 14891 7642 19681 340 -227 -963 C ATOM 126 NZ LYS A 16 16.815 72.526 46.100 1.00103.79 N ANISOU 126 NZ LYS A 16 13857 7063 18516 476 -224 -719 N ATOM 127 N THR A 17 22.786 73.284 44.918 1.00 91.00 N ANISOU 127 N THR A 17 12199 5386 16990 -582 -657 -470 N ATOM 128 CA THR A 17 23.898 73.461 45.839 1.00101.13 C ANISOU 128 CA THR A 17 13527 6665 18233 -801 -737 -738 C ATOM 129 C THR A 17 25.236 73.096 45.208 1.00 97.69 C ANISOU 129 C THR A 17 12981 6394 17742 -1016 -832 -550 C ATOM 130 O THR A 17 26.281 73.300 45.834 1.00 98.43 O ANISOU 130 O THR A 17 13084 6480 17836 -1223 -917 -725 O ATOM 131 CB THR A 17 23.673 72.636 47.111 1.00104.10 C ANISOU 131 CB THR A 17 13955 7299 18298 -758 -747 -1049 C ATOM 132 OG1 THR A 17 23.400 71.273 46.764 1.00105.37 O ANISOU 132 OG1 THR A 17 14026 7844 18165 -656 -751 -885 O ATOM 133 CG2 THR A 17 22.504 73.198 47.908 1.00 90.57 C ANISOU 133 CG2 THR A 17 12361 5385 16668 -588 -638 -1306 C ATOM 134 N GLY A 18 25.227 72.571 43.983 1.00 89.80 N ANISOU 134 N GLY A 18 11873 5549 16697 -978 -815 -202 N ATOM 135 CA GLY A 18 26.448 72.264 43.268 1.00 93.11 C ANISOU 135 CA GLY A 18 12175 6116 17086 -1172 -873 -9 C ATOM 136 C GLY A 18 27.158 71.006 43.709 1.00 98.03 C ANISOU 136 C GLY A 18 12716 7124 17407 -1231 -937 -92 C ATOM 137 O GLY A 18 28.320 70.809 43.337 1.00110.03 O ANISOU 137 O GLY A 18 14129 8754 18925 -1410 -989 5 O ATOM 138 N VAL A 19 26.498 70.141 44.486 1.00 89.12 N ANISOU 138 N VAL A 19 11625 6203 16034 -1087 -933 -258 N ATOM 139 CA VAL A 19 27.148 68.943 45.011 1.00 81.66 C ANISOU 139 CA VAL A 19 10608 5605 14815 -1137 -1008 -338 C ATOM 140 C VAL A 19 26.910 67.707 44.157 1.00 84.00 C ANISOU 140 C VAL A 19 10802 6200 14912 -1026 -967 -104 C ATOM 141 O VAL A 19 27.591 66.689 44.360 1.00 82.21 O ANISOU 141 O VAL A 19 10488 6246 14501 -1075 -1025 -115 O ATOM 142 CB VAL A 19 26.682 68.643 46.451 1.00 83.82 C ANISOU 142 CB VAL A 19 10984 5953 14909 -1076 -1040 -660 C ATOM 143 CG1 VAL A 19 26.966 69.829 47.361 1.00 83.89 C ANISOU 143 CG1 VAL A 19 11106 5680 15089 -1206 -1078 -934 C ATOM 144 CG2 VAL A 19 25.201 68.284 46.469 1.00 82.07 C ANISOU 144 CG2 VAL A 19 10827 5770 14587 -829 -938 -656 C ATOM 145 N VAL A 20 25.971 67.756 43.210 1.00 88.63 N ANISOU 145 N VAL A 20 11397 6743 15538 -883 -876 107 N ATOM 146 CA VAL A 20 25.651 66.580 42.411 1.00 84.86 C ANISOU 146 CA VAL A 20 10839 6546 14857 -783 -835 306 C ATOM 147 C VAL A 20 26.824 66.233 41.503 1.00 82.64 C ANISOU 147 C VAL A 20 10426 6396 14575 -936 -843 495 C ATOM 148 O VAL A 20 27.424 67.108 40.863 1.00 83.51 O ANISOU 148 O VAL A 20 10508 6334 14889 -1072 -835 622 O ATOM 149 CB VAL A 20 24.368 66.815 41.597 1.00 84.73 C ANISOU 149 CB VAL A 20 10860 6445 14889 -615 -750 493 C ATOM 150 CG1 VAL A 20 24.032 65.583 40.768 1.00 71.29 C ANISOU 150 CG1 VAL A 20 9084 5040 12961 -533 -712 683 C ATOM 151 CG2 VAL A 20 23.217 67.166 42.523 1.00 90.04 C ANISOU 151 CG2 VAL A 20 11640 6987 15584 -455 -724 294 C ATOM 152 N ARG A 21 27.154 64.945 41.446 1.00 83.57 N ANISOU 152 N ARG A 21 10460 6818 14475 -916 -852 515 N ATOM 153 CA ARG A 21 28.245 64.433 40.634 1.00 86.70 C ANISOU 153 CA ARG A 21 10715 7375 14852 -1039 -839 667 C ATOM 154 C ARG A 21 27.715 63.350 39.704 1.00 88.02 C ANISOU 154 C ARG A 21 10841 7772 14831 -925 -758 841 C ATOM 155 O ARG A 21 26.610 62.831 39.881 1.00 89.92 O ANISOU 155 O ARG A 21 11149 8082 14933 -761 -738 817 O ATOM 156 CB ARG A 21 29.378 63.884 41.510 1.00 85.98 C ANISOU 156 CB ARG A 21 10538 7423 14708 -1145 -935 503 C ATOM 157 CG ARG A 21 29.973 64.909 42.455 1.00 73.78 C ANISOU 157 CG ARG A 21 9033 5674 13327 -1287 -1031 315 C ATOM 158 CD ARG A 21 30.674 66.017 41.688 1.00 76.00 C ANISOU 158 CD ARG A 21 9270 5749 13857 -1458 -1006 450 C ATOM 159 NE ARG A 21 31.202 67.046 42.578 1.00 78.52 N ANISOU 159 NE ARG A 21 9639 5849 14346 -1606 -1098 260 N ATOM 160 CZ ARG A 21 30.608 68.213 42.807 1.00 87.58 C ANISOU 160 CZ ARG A 21 10922 6690 15664 -1602 -1087 188 C ATOM 161 NH1 ARG A 21 29.463 68.507 42.206 1.00 91.77 N ANISOU 161 NH1 ARG A 21 11538 7102 16230 -1447 -994 311 N ATOM 162 NH2 ARG A 21 31.162 69.088 43.635 1.00 87.70 N ANISOU 162 NH2 ARG A 21 10984 6513 15826 -1756 -1171 -8 N ATOM 163 N SER A 22 28.520 63.015 38.703 1.00 89.67 N ANISOU 163 N SER A 22 10934 8101 15035 -1025 -704 1008 N ATOM 164 CA SER A 22 28.162 61.945 37.777 1.00 80.39 C ANISOU 164 CA SER A 22 9717 7155 13672 -946 -620 1152 C ATOM 165 C SER A 22 28.142 60.611 38.513 1.00 81.11 C ANISOU 165 C SER A 22 9780 7463 13574 -849 -656 1005 C ATOM 166 O SER A 22 29.089 60.299 39.242 1.00 87.40 O ANISOU 166 O SER A 22 10500 8318 14391 -916 -724 878 O ATOM 167 CB SER A 22 29.151 61.894 36.614 1.00 77.30 C ANISOU 167 CB SER A 22 9205 6850 13316 -1093 -539 1330 C ATOM 168 OG SER A 22 28.865 60.817 35.736 1.00 75.59 O ANISOU 168 OG SER A 22 8954 6862 12906 -1030 -448 1438 O ATOM 169 N PRO A 23 27.092 59.798 38.349 1.00 80.35 N ANISOU 169 N PRO A 23 9738 7490 13300 -699 -620 1031 N ATOM 170 CA PRO A 23 27.086 58.465 38.973 1.00 84.11 C ANISOU 170 CA PRO A 23 10186 8170 13603 -615 -650 916 C ATOM 171 C PRO A 23 28.142 57.529 38.412 1.00 80.22 C ANISOU 171 C PRO A 23 9553 7857 13070 -678 -607 966 C ATOM 172 O PRO A 23 28.317 56.427 38.950 1.00 73.99 O ANISOU 172 O PRO A 23 8723 7215 12176 -618 -641 878 O ATOM 173 CB PRO A 23 25.672 57.946 38.679 1.00 80.96 C ANISOU 173 CB PRO A 23 9874 7840 13048 -462 -605 972 C ATOM 174 CG PRO A 23 25.256 58.679 37.450 1.00 83.33 C ANISOU 174 CG PRO A 23 10194 8057 13410 -491 -531 1176 C ATOM 175 CD PRO A 23 25.882 60.042 37.546 1.00 79.99 C ANISOU 175 CD PRO A 23 9771 7408 13213 -609 -559 1183 C ATOM 176 N PHE A 24 28.846 57.927 37.356 1.00 78.55 N ANISOU 176 N PHE A 24 9263 7637 12948 -797 -527 1105 N ATOM 177 CA PHE A 24 29.947 57.153 36.807 1.00 75.01 C ANISOU 177 CA PHE A 24 8662 7346 12494 -867 -462 1138 C ATOM 178 C PHE A 24 31.306 57.602 37.330 1.00 77.49 C ANISOU 178 C PHE A 24 8849 7608 12986 -1003 -525 1071 C ATOM 179 O PHE A 24 32.326 57.056 36.902 1.00 79.46 O ANISOU 179 O PHE A 24 8943 7977 13271 -1066 -468 1098 O ATOM 180 CB PHE A 24 29.939 57.238 35.274 1.00 63.53 C ANISOU 180 CB PHE A 24 7185 5950 11003 -931 -315 1331 C ATOM 181 CG PHE A 24 28.662 56.750 34.637 1.00 72.62 C ANISOU 181 CG PHE A 24 8445 7179 11969 -821 -259 1413 C ATOM 182 CD1 PHE A 24 28.094 55.542 35.014 1.00 72.09 C ANISOU 182 CD1 PHE A 24 8404 7245 11744 -688 -271 1323 C ATOM 183 CD2 PHE A 24 28.028 57.506 33.659 1.00 78.47 C ANISOU 183 CD2 PHE A 24 9257 7859 12698 -860 -206 1595 C ATOM 184 CE1 PHE A 24 26.919 55.095 34.425 1.00 64.20 C ANISOU 184 CE1 PHE A 24 7496 6320 10576 -604 -228 1398 C ATOM 185 CE2 PHE A 24 26.854 57.067 33.068 1.00 75.05 C ANISOU 185 CE2 PHE A 24 8911 7510 12094 -771 -174 1681 C ATOM 186 CZ PHE A 24 26.298 55.860 33.452 1.00 74.91 C ANISOU 186 CZ PHE A 24 8914 7629 11918 -646 -183 1575 C ATOM 187 N GLU A 25 31.353 58.571 38.246 1.00 79.07 N ANISOU 187 N GLU A 25 9104 7635 13303 -1053 -639 977 N ATOM 188 CA GLU A 25 32.630 59.204 38.556 1.00 72.88 C ANISOU 188 CA GLU A 25 8202 6783 12705 -1220 -697 941 C ATOM 189 C GLU A 25 32.867 59.415 40.048 1.00 75.43 C ANISOU 189 C GLU A 25 8549 7044 13066 -1238 -867 745 C ATOM 190 O GLU A 25 34.016 59.374 40.502 1.00 90.68 O ANISOU 190 O GLU A 25 10343 9015 15096 -1349 -945 690 O ATOM 191 CB GLU A 25 32.745 60.540 37.823 1.00 69.01 C ANISOU 191 CB GLU A 25 7739 6106 12374 -1354 -644 1067 C ATOM 192 CG GLU A 25 33.959 60.635 36.913 1.00104.72 C ANISOU 192 CG GLU A 25 12089 10694 17007 -1516 -554 1192 C ATOM 193 CD GLU A 25 33.915 59.630 35.782 1.00115.82 C ANISOU 193 CD GLU A 25 13429 12309 18268 -1462 -399 1312 C ATOM 194 OE1 GLU A 25 32.908 59.608 35.042 1.00121.12 O ANISOU 194 OE1 GLU A 25 14218 12987 18817 -1389 -323 1421 O ATOM 195 OE2 GLU A 25 34.886 58.860 35.636 1.00115.44 O ANISOU 195 OE2 GLU A 25 13209 12420 18234 -1495 -354 1292 O ATOM 196 N ALA A 26 31.811 59.644 40.824 1.00 76.45 N ANISOU 196 N ALA A 26 8845 7089 13114 -1139 -925 637 N ATOM 197 CA ALA A 26 31.996 59.994 42.225 1.00 68.02 C ANISOU 197 CA ALA A 26 7825 5956 12064 -1181 -1077 439 C ATOM 198 C ALA A 26 30.858 59.421 43.051 1.00 79.13 C ANISOU 198 C ALA A 26 9369 7419 13278 -1019 -1112 325 C ATOM 199 O ALA A 26 29.743 59.260 42.538 1.00 74.80 O ANISOU 199 O ALA A 26 8911 6866 12642 -889 -1019 395 O ATOM 200 CB ALA A 26 32.072 61.517 42.418 1.00 70.23 C ANISOU 200 CB ALA A 26 8182 5973 12527 -1307 -1107 388 C ATOM 201 N PRO A 27 31.103 59.101 44.325 1.00 73.42 N ANISOU 201 N PRO A 27 8658 6762 12478 -1035 -1248 161 N ATOM 202 CA PRO A 27 30.034 58.559 45.174 1.00 79.99 C ANISOU 202 CA PRO A 27 9620 7661 13112 -898 -1276 52 C ATOM 203 C PRO A 27 28.863 59.519 45.307 1.00 85.30 C ANISOU 203 C PRO A 27 10464 8147 13799 -837 -1216 -18 C ATOM 204 O PRO A 27 29.012 60.741 45.223 1.00 95.23 O ANISOU 204 O PRO A 27 11763 9193 15228 -927 -1209 -52 O ATOM 205 CB PRO A 27 30.729 58.331 46.523 1.00 69.45 C ANISOU 205 CB PRO A 27 8263 6408 11716 -984 -1449 -107 C ATOM 206 CG PRO A 27 32.002 59.121 46.453 1.00 70.64 C ANISOU 206 CG PRO A 27 8303 6470 12065 -1176 -1516 -113 C ATOM 207 CD PRO A 27 32.403 59.111 45.017 1.00 68.34 C ANISOU 207 CD PRO A 27 7891 6166 11908 -1185 -1387 86 C ATOM 208 N GLN A 28 27.684 58.941 45.527 1.00 84.02 N ANISOU 208 N GLN A 28 10395 8058 13471 -680 -1171 -37 N ATOM 209 CA GLN A 28 26.438 59.694 45.562 1.00 76.57 C ANISOU 209 CA GLN A 28 9590 6960 12546 -585 -1094 -83 C ATOM 210 C GLN A 28 25.911 59.816 46.987 1.00 78.56 C ANISOU 210 C GLN A 28 9960 7209 12678 -561 -1151 -316 C ATOM 211 O GLN A 28 24.726 59.573 47.236 1.00 81.58 O ANISOU 211 O GLN A 28 10427 7621 12947 -424 -1089 -352 O ATOM 212 CB GLN A 28 25.392 59.023 44.668 1.00 68.18 C ANISOU 212 CB GLN A 28 8532 5982 11390 -429 -985 77 C ATOM 213 CG GLN A 28 25.840 58.796 43.233 1.00 73.62 C ANISOU 213 CG GLN A 28 9116 6708 12146 -458 -915 301 C ATOM 214 CD GLN A 28 25.918 60.081 42.434 1.00 87.33 C ANISOU 214 CD GLN A 28 10863 8224 14093 -525 -864 400 C ATOM 215 OE1 GLN A 28 24.913 60.764 42.233 1.00 89.06 O ANISOU 215 OE1 GLN A 28 11167 8300 14370 -444 -813 430 O ATOM 216 NE2 GLN A 28 27.116 60.419 41.975 1.00 94.20 N ANISOU 216 NE2 GLN A 28 11637 9062 15093 -675 -879 464 N ATOM 217 N TYR A 29 26.775 60.200 47.926 1.00 74.17 N ANISOU 217 N TYR A 29 9411 6630 12142 -704 -1268 -477 N ATOM 218 CA TYR A 29 26.374 60.272 49.327 1.00 78.59 C ANISOU 218 CA TYR A 29 10089 7219 12552 -711 -1327 -711 C ATOM 219 C TYR A 29 25.492 61.473 49.639 1.00 85.91 C ANISOU 219 C TYR A 29 11158 7910 13574 -673 -1242 -868 C ATOM 220 O TYR A 29 25.142 61.670 50.809 1.00 88.19 O ANISOU 220 O TYR A 29 11559 8207 13743 -690 -1268 -1094 O ATOM 221 CB TYR A 29 27.615 60.284 50.222 1.00 77.78 C ANISOU 221 CB TYR A 29 9945 7185 12424 -895 -1496 -830 C ATOM 222 CG TYR A 29 28.424 59.012 50.130 1.00 81.59 C ANISOU 222 CG TYR A 29 10281 7907 12811 -911 -1590 -694 C ATOM 223 CD1 TYR A 29 27.798 57.776 50.034 1.00 87.12 C ANISOU 223 CD1 TYR A 29 10971 8793 13337 -767 -1555 -597 C ATOM 224 CD2 TYR A 29 29.812 59.045 50.123 1.00 79.76 C ANISOU 224 CD2 TYR A 29 9914 7707 12686 -1067 -1711 -661 C ATOM 225 CE1 TYR A 29 28.529 56.609 49.944 1.00 78.88 C ANISOU 225 CE1 TYR A 29 9793 7939 12237 -770 -1635 -475 C ATOM 226 CE2 TYR A 29 30.553 57.882 50.032 1.00 70.64 C ANISOU 226 CE2 TYR A 29 8607 6756 11478 -1064 -1790 -535 C ATOM 227 CZ TYR A 29 29.906 56.667 49.943 1.00 78.58 C ANISOU 227 CZ TYR A 29 9614 7923 12321 -910 -1750 -445 C ATOM 228 OH TYR A 29 30.639 55.506 49.852 1.00 89.85 O ANISOU 228 OH TYR A 29 10890 9524 13723 -897 -1823 -323 O ATOM 229 N TYR A 30 25.122 62.274 48.639 1.00 92.11 N ANISOU 229 N TYR A 30 11941 8486 14570 -624 -1140 -753 N ATOM 230 CA TYR A 30 24.187 63.370 48.850 1.00 97.27 C ANISOU 230 CA TYR A 30 12714 8894 15349 -554 -1047 -878 C ATOM 231 C TYR A 30 22.736 62.969 48.619 1.00 94.54 C ANISOU 231 C TYR A 30 12404 8598 14921 -343 -928 -819 C ATOM 232 O TYR A 30 21.835 63.681 49.078 1.00103.80 O ANISOU 232 O TYR A 30 13671 9613 16154 -259 -847 -966 O ATOM 233 CB TYR A 30 24.539 64.556 47.945 1.00 82.56 C ANISOU 233 CB TYR A 30 10830 6747 13791 -618 -1012 -773 C ATOM 234 CG TYR A 30 24.807 64.179 46.507 1.00 83.84 C ANISOU 234 CG TYR A 30 10871 6965 14018 -603 -981 -463 C ATOM 235 CD1 TYR A 30 23.762 63.942 45.622 1.00 86.60 C ANISOU 235 CD1 TYR A 30 11213 7328 14364 -439 -880 -279 C ATOM 236 CD2 TYR A 30 26.105 64.067 46.032 1.00 71.53 C ANISOU 236 CD2 TYR A 30 9201 5458 12521 -762 -1048 -358 C ATOM 237 CE1 TYR A 30 24.005 63.597 44.307 1.00 89.23 C ANISOU 237 CE1 TYR A 30 11447 7729 14725 -445 -849 -7 C ATOM 238 CE2 TYR A 30 26.358 63.724 44.720 1.00 78.20 C ANISOU 238 CE2 TYR A 30 9940 6367 13406 -758 -998 -92 C ATOM 239 CZ TYR A 30 25.306 63.489 43.862 1.00 86.48 C ANISOU 239 CZ TYR A 30 11001 7433 14425 -605 -900 79 C ATOM 240 OH TYR A 30 25.561 63.149 42.554 1.00 93.00 O ANISOU 240 OH TYR A 30 11733 8339 15262 -620 -849 332 O ATOM 241 N LEU A 31 22.484 61.861 47.918 1.00 82.36 N ANISOU 241 N LEU A 31 10780 7261 13251 -257 -911 -617 N ATOM 242 CA LEU A 31 21.130 61.338 47.784 1.00 79.01 C ANISOU 242 CA LEU A 31 10378 6923 12719 -75 -816 -565 C ATOM 243 C LEU A 31 20.822 60.227 48.778 1.00 79.85 C ANISOU 243 C LEU A 31 10514 7282 12544 -42 -847 -675 C ATOM 244 O LEU A 31 19.677 59.766 48.833 1.00 93.82 O ANISOU 244 O LEU A 31 12303 9135 14209 96 -770 -657 O ATOM 245 CB LEU A 31 20.879 60.833 46.350 1.00 70.01 C ANISOU 245 CB LEU A 31 9145 5846 11608 -6 -770 -274 C ATOM 246 CG LEU A 31 21.844 59.892 45.618 1.00 85.11 C ANISOU 246 CG LEU A 31 10952 7937 13448 -84 -823 -106 C ATOM 247 CD1 LEU A 31 21.844 58.481 46.193 1.00102.30 C ANISOU 247 CD1 LEU A 31 13110 10381 15376 -56 -868 -139 C ATOM 248 CD2 LEU A 31 21.505 59.853 44.133 1.00 93.25 C ANISOU 248 CD2 LEU A 31 11923 8956 14552 -35 -753 152 C ATOM 249 N ALA A 32 21.808 59.789 49.557 1.00 77.30 N ANISOU 249 N ALA A 32 10187 7084 12101 -172 -966 -773 N ATOM 250 CA ALA A 32 21.617 58.759 50.566 1.00 71.36 C ANISOU 250 CA ALA A 32 9467 6569 11080 -164 -1017 -861 C ATOM 251 C ALA A 32 22.848 58.727 51.455 1.00 73.37 C ANISOU 251 C ALA A 32 9720 6887 11269 -340 -1170 -984 C ATOM 252 O ALA A 32 23.972 58.846 50.961 1.00 77.17 O ANISOU 252 O ALA A 32 10111 7333 11875 -446 -1248 -897 O ATOM 253 CB ALA A 32 21.386 57.381 49.931 1.00 62.77 C ANISOU 253 CB ALA A 32 8296 5690 9863 -81 -1012 -653 C ATOM 254 N GLU A 33 22.629 58.577 52.759 1.00 70.80 N ANISOU 254 N GLU A 33 9491 6667 10744 -379 -1213 -1179 N ATOM 255 CA GLU A 33 23.743 58.476 53.684 1.00 75.26 C ANISOU 255 CA GLU A 33 10057 7327 11212 -556 -1382 -1287 C ATOM 256 C GLU A 33 24.567 57.227 53.372 1.00 84.73 C ANISOU 256 C GLU A 33 11123 8727 12345 -579 -1499 -1085 C ATOM 257 O GLU A 33 24.052 56.264 52.796 1.00 84.70 O ANISOU 257 O GLU A 33 11069 8832 12282 -454 -1443 -918 O ATOM 258 CB GLU A 33 23.243 58.436 55.128 1.00 77.87 C ANISOU 258 CB GLU A 33 10525 7770 11292 -596 -1400 -1519 C ATOM 259 CG GLU A 33 22.614 59.732 55.615 1.00 96.07 C ANISOU 259 CG GLU A 33 12965 9867 13670 -599 -1289 -1776 C ATOM 260 CD GLU A 33 22.572 59.826 57.129 1.00117.17 C ANISOU 260 CD GLU A 33 15771 12657 16090 -716 -1342 -2044 C ATOM 261 OE1 GLU A 33 23.626 60.113 57.735 1.00124.85 O ANISOU 261 OE1 GLU A 33 16758 13649 17030 -908 -1498 -2149 O ATOM 262 OE2 GLU A 33 21.491 59.600 57.713 1.00119.04 O ANISOU 262 OE2 GLU A 33 16096 12981 16152 -627 -1228 -2146 O ATOM 263 N PRO A 34 25.857 57.223 53.723 1.00 91.92 N ANISOU 263 N PRO A 34 11964 9682 13281 -737 -1663 -1096 N ATOM 264 CA PRO A 34 26.694 56.053 53.407 1.00 87.76 C ANISOU 264 CA PRO A 34 11286 9326 12732 -746 -1769 -902 C ATOM 265 C PRO A 34 26.178 54.749 53.991 1.00 87.33 C ANISOU 265 C PRO A 34 11253 9497 12433 -669 -1805 -844 C ATOM 266 O PRO A 34 26.336 53.699 53.354 1.00 94.52 O ANISOU 266 O PRO A 34 12056 10501 13355 -590 -1805 -654 O ATOM 267 CB PRO A 34 28.058 56.432 53.999 1.00 68.74 C ANISOU 267 CB PRO A 34 8813 6928 10376 -943 -1954 -972 C ATOM 268 CG PRO A 34 28.066 57.912 53.994 1.00 70.57 C ANISOU 268 CG PRO A 34 9125 6928 10760 -1030 -1904 -1138 C ATOM 269 CD PRO A 34 26.651 58.323 54.294 1.00 70.48 C ANISOU 269 CD PRO A 34 9284 6841 10655 -917 -1753 -1275 C ATOM 270 N TRP A 35 25.561 54.775 55.176 1.00 84.08 N ANISOU 270 N TRP A 35 10979 9172 11796 -695 -1827 -1005 N ATOM 271 CA TRP A 35 25.063 53.533 55.758 1.00 77.27 C ANISOU 271 CA TRP A 35 10139 8525 10693 -638 -1863 -933 C ATOM 272 C TRP A 35 23.932 52.941 54.929 1.00 77.34 C ANISOU 272 C TRP A 35 10149 8534 10704 -455 -1695 -808 C ATOM 273 O TRP A 35 23.759 51.718 54.905 1.00 89.33 O ANISOU 273 O TRP A 35 11626 10199 12114 -394 -1722 -664 O ATOM 274 CB TRP A 35 24.606 53.757 57.201 1.00 70.75 C ANISOU 274 CB TRP A 35 9470 7805 9607 -723 -1905 -1137 C ATOM 275 CG TRP A 35 23.370 54.593 57.344 1.00 83.41 C ANISOU 275 CG TRP A 35 11212 9298 11182 -650 -1715 -1318 C ATOM 276 CD1 TRP A 35 23.315 55.942 57.529 1.00 84.56 C ANISOU 276 CD1 TRP A 35 11440 9257 11430 -707 -1653 -1534 C ATOM 277 CD2 TRP A 35 22.011 54.132 57.336 1.00 86.37 C ANISOU 277 CD2 TRP A 35 11647 9735 11434 -506 -1560 -1300 C ATOM 278 NE1 TRP A 35 22.008 56.353 57.628 1.00 82.64 N ANISOU 278 NE1 TRP A 35 11299 8949 11150 -592 -1463 -1652 N ATOM 279 CE2 TRP A 35 21.188 55.262 57.513 1.00 83.93 C ANISOU 279 CE2 TRP A 35 11443 9274 11172 -470 -1404 -1509 C ATOM 280 CE3 TRP A 35 21.410 52.877 57.191 1.00 84.94 C ANISOU 280 CE3 TRP A 35 11435 9716 11125 -406 -1537 -1127 C ATOM 281 CZ2 TRP A 35 19.796 55.176 57.549 1.00 72.46 C ANISOU 281 CZ2 TRP A 35 10048 7840 9645 -333 -1226 -1545 C ATOM 282 CZ3 TRP A 35 20.026 52.793 57.227 1.00 77.97 C ANISOU 282 CZ3 TRP A 35 10617 8855 10153 -287 -1366 -1163 C ATOM 283 CH2 TRP A 35 19.236 53.936 57.404 1.00 72.03 C ANISOU 283 CH2 TRP A 35 9952 7963 9453 -248 -1213 -1367 C ATOM 284 N GLN A 36 23.159 53.784 54.242 1.00 76.26 N ANISOU 284 N GLN A 36 10051 8227 10696 -371 -1529 -852 N ATOM 285 CA GLN A 36 22.117 53.267 53.363 1.00 73.16 C ANISOU 285 CA GLN A 36 9643 7838 10318 -209 -1385 -719 C ATOM 286 C GLN A 36 22.712 52.553 52.157 1.00 71.72 C ANISOU 286 C GLN A 36 9321 7662 10267 -171 -1394 -501 C ATOM 287 O GLN A 36 22.096 51.624 51.624 1.00 71.48 O ANISOU 287 O GLN A 36 9265 7712 10182 -70 -1333 -369 O ATOM 288 CB GLN A 36 21.195 54.400 52.921 1.00 68.22 C ANISOU 288 CB GLN A 36 9078 7023 9818 -132 -1225 -803 C ATOM 289 CG GLN A 36 20.593 55.165 54.086 1.00 72.97 C ANISOU 289 CG GLN A 36 9815 7597 10313 -160 -1185 -1050 C ATOM 290 CD GLN A 36 19.624 56.240 53.649 1.00 79.70 C ANISOU 290 CD GLN A 36 10711 8246 11323 -58 -1019 -1126 C ATOM 291 OE1 GLN A 36 20.019 57.257 53.079 1.00 84.67 O ANISOU 291 OE1 GLN A 36 11326 8664 12183 -82 -1001 -1141 O ATOM 292 NE2 GLN A 36 18.344 56.022 53.919 1.00 91.58 N ANISOU 292 NE2 GLN A 36 12264 9812 12722 58 -897 -1163 N ATOM 293 N PHE A 37 23.902 52.967 51.713 1.00 82.34 N ANISOU 293 N PHE A 37 10575 8926 11785 -259 -1462 -469 N ATOM 294 CA PHE A 37 24.598 52.215 50.674 1.00 76.67 C ANISOU 294 CA PHE A 37 9714 8238 11178 -236 -1467 -282 C ATOM 295 C PHE A 37 25.124 50.895 51.218 1.00 75.63 C ANISOU 295 C PHE A 37 9520 8285 10930 -246 -1591 -206 C ATOM 296 O PHE A 37 25.150 49.885 50.504 1.00 71.89 O ANISOU 296 O PHE A 37 8969 7870 10476 -172 -1556 -61 O ATOM 297 CB PHE A 37 25.738 53.046 50.088 1.00 59.47 C ANISOU 297 CB PHE A 37 7442 5933 9220 -337 -1494 -269 C ATOM 298 CG PHE A 37 25.286 54.096 49.119 1.00 75.86 C ANISOU 298 CG PHE A 37 9544 7826 11453 -308 -1359 -253 C ATOM 299 CD1 PHE A 37 25.082 53.781 47.786 1.00 67.63 C ANISOU 299 CD1 PHE A 37 8437 6770 10489 -235 -1248 -87 C ATOM 300 CD2 PHE A 37 25.068 55.399 49.539 1.00 80.31 C ANISOU 300 CD2 PHE A 37 10199 8227 12086 -360 -1344 -401 C ATOM 301 CE1 PHE A 37 24.664 54.746 46.889 1.00 79.91 C ANISOU 301 CE1 PHE A 37 10015 8166 12180 -217 -1140 -43 C ATOM 302 CE2 PHE A 37 24.652 56.369 48.647 1.00 79.52 C ANISOU 302 CE2 PHE A 37 10119 7942 12153 -329 -1230 -362 C ATOM 303 CZ PHE A 37 24.450 56.042 47.320 1.00 75.30 C ANISOU 303 CZ PHE A 37 9516 7408 11687 -259 -1135 -169 C ATOM 304 N SER A 38 25.552 50.887 52.483 1.00 60.48 N ANISOU 304 N SER A 38 7638 6451 8892 -343 -1740 -302 N ATOM 305 CA SER A 38 25.952 49.641 53.123 1.00 70.33 C ANISOU 305 CA SER A 38 8836 7867 10018 -351 -1874 -214 C ATOM 306 C SER A 38 24.767 48.696 53.281 1.00 74.78 C ANISOU 306 C SER A 38 9481 8531 10402 -242 -1803 -159 C ATOM 307 O SER A 38 24.894 47.488 53.048 1.00 65.99 O ANISOU 307 O SER A 38 8298 7497 9278 -185 -1832 -13 O ATOM 308 CB SER A 38 26.594 49.935 54.477 1.00 61.88 C ANISOU 308 CB SER A 38 7800 6878 8831 -497 -2061 -324 C ATOM 309 OG SER A 38 27.712 50.793 54.340 1.00 74.25 O ANISOU 309 OG SER A 38 9283 8355 10573 -613 -2137 -373 O ATOM 310 N MET A 39 23.604 49.224 53.674 1.00 76.80 N ANISOU 310 N MET A 39 9875 8776 10530 -212 -1703 -276 N ATOM 311 CA MET A 39 22.417 48.379 53.759 1.00 65.82 C ANISOU 311 CA MET A 39 8547 7479 8980 -115 -1620 -220 C ATOM 312 C MET A 39 21.992 47.894 52.382 1.00 68.75 C ANISOU 312 C MET A 39 8852 7794 9474 1 -1493 -80 C ATOM 313 O MET A 39 21.478 46.777 52.243 1.00 66.45 O ANISOU 313 O MET A 39 8557 7591 9101 65 -1472 29 O ATOM 314 CB MET A 39 21.271 49.127 54.441 1.00 64.88 C ANISOU 314 CB MET A 39 8569 7359 8722 -105 -1521 -385 C ATOM 315 CG MET A 39 21.453 49.302 55.937 1.00 71.24 C ANISOU 315 CG MET A 39 9470 8279 9321 -224 -1633 -525 C ATOM 316 SD MET A 39 21.987 47.778 56.740 1.00 83.26 S ANISOU 316 SD MET A 39 10960 10015 10660 -279 -1820 -369 S ATOM 317 CE MET A 39 20.628 46.677 56.348 1.00 84.81 C ANISOU 317 CE MET A 39 11180 10284 10759 -144 -1683 -239 C ATOM 318 N LEU A 40 22.191 48.719 51.352 1.00 66.66 N ANISOU 318 N LEU A 40 8542 7387 9399 17 -1410 -79 N ATOM 319 CA LEU A 40 21.973 48.248 49.989 1.00 69.29 C ANISOU 319 CA LEU A 40 8806 7684 9836 99 -1306 59 C ATOM 320 C LEU A 40 22.937 47.120 49.648 1.00 80.89 C ANISOU 320 C LEU A 40 10161 9213 11361 93 -1378 181 C ATOM 321 O LEU A 40 22.540 46.112 49.052 1.00 89.10 O ANISOU 321 O LEU A 40 11179 10299 12377 162 -1323 284 O ATOM 322 CB LEU A 40 22.122 49.403 48.999 1.00 67.72 C ANISOU 322 CB LEU A 40 8581 7329 9820 93 -1219 52 C ATOM 323 CG LEU A 40 22.159 49.003 47.521 1.00 64.28 C ANISOU 323 CG LEU A 40 8067 6869 9488 142 -1124 197 C ATOM 324 CD1 LEU A 40 20.867 48.310 47.114 1.00 51.93 C ANISOU 324 CD1 LEU A 40 6549 5370 7811 238 -1032 263 C ATOM 325 CD2 LEU A 40 22.435 50.207 46.631 1.00 68.17 C ANISOU 325 CD2 LEU A 40 8534 7214 10153 109 -1058 207 C ATOM 326 N ALA A 41 24.208 47.271 50.028 1.00 77.57 N ANISOU 326 N ALA A 41 9660 8788 11026 9 -1501 166 N ATOM 327 CA ALA A 41 25.172 46.191 49.844 1.00 76.93 C ANISOU 327 CA ALA A 41 9451 8760 11020 13 -1578 277 C ATOM 328 C ALA A 41 24.801 44.975 50.683 1.00 74.18 C ANISOU 328 C ALA A 41 9140 8533 10513 45 -1662 334 C ATOM 329 O ALA A 41 24.979 43.832 50.247 1.00 77.06 O ANISOU 329 O ALA A 41 9435 8921 10923 104 -1655 446 O ATOM 330 CB ALA A 41 26.578 46.676 50.198 1.00 55.55 C ANISOU 330 CB ALA A 41 6634 6031 8441 -91 -1709 251 C ATOM 331 N ALA A 42 24.286 45.204 51.894 1.00 70.02 N ANISOU 331 N ALA A 42 8726 8079 9799 0 -1734 255 N ATOM 332 CA ALA A 42 23.895 44.092 52.752 1.00 68.54 C ANISOU 332 CA ALA A 42 8584 8017 9440 12 -1816 324 C ATOM 333 C ALA A 42 22.760 43.289 52.130 1.00 77.36 C ANISOU 333 C ALA A 42 9746 9144 10502 113 -1681 397 C ATOM 334 O ALA A 42 22.744 42.055 52.213 1.00 84.16 O ANISOU 334 O ALA A 42 10582 10056 11337 147 -1724 514 O ATOM 335 CB ALA A 42 23.496 44.609 54.134 1.00 56.10 C ANISOU 335 CB ALA A 42 7135 6533 7648 -73 -1894 210 C ATOM 336 N TYR A 43 21.805 43.970 51.491 1.00 76.14 N ANISOU 336 N TYR A 43 9652 8935 10343 157 -1526 336 N ATOM 337 CA TYR A 43 20.691 43.254 50.881 1.00 79.97 C ANISOU 337 CA TYR A 43 10172 9441 10772 238 -1407 404 C ATOM 338 C TYR A 43 21.137 42.484 49.645 1.00 77.00 C ANISOU 338 C TYR A 43 9698 9010 10547 287 -1357 510 C ATOM 339 O TYR A 43 20.652 41.374 49.393 1.00 78.27 O ANISOU 339 O TYR A 43 9866 9206 10667 329 -1329 593 O ATOM 340 CB TYR A 43 19.559 44.217 50.529 1.00 74.24 C ANISOU 340 CB TYR A 43 9517 8676 10015 273 -1268 325 C ATOM 341 CG TYR A 43 18.275 43.494 50.196 1.00 82.39 C ANISOU 341 CG TYR A 43 10590 9765 10950 337 -1172 389 C ATOM 342 CD1 TYR A 43 17.531 42.877 51.194 1.00 88.76 C ANISOU 342 CD1 TYR A 43 11466 10688 11570 328 -1196 393 C ATOM 343 CD2 TYR A 43 17.816 43.411 48.889 1.00 82.84 C ANISOU 343 CD2 TYR A 43 10612 9771 11091 391 -1062 452 C ATOM 344 CE1 TYR A 43 16.362 42.205 50.902 1.00 98.59 C ANISOU 344 CE1 TYR A 43 12737 11989 12736 373 -1110 456 C ATOM 345 CE2 TYR A 43 16.645 42.741 48.586 1.00 92.81 C ANISOU 345 CE2 TYR A 43 11904 11093 12265 434 -988 511 C ATOM 346 CZ TYR A 43 15.922 42.140 49.597 1.00105.94 C ANISOU 346 CZ TYR A 43 13626 12863 13762 426 -1011 512 C ATOM 347 OH TYR A 43 14.757 41.469 49.303 1.00112.92 O ANISOU 347 OH TYR A 43 14529 13809 14567 455 -939 574 O ATOM 348 N MET A 44 22.050 43.055 48.856 1.00 70.15 N ANISOU 348 N MET A 44 8742 8058 9854 272 -1336 500 N ATOM 349 CA MET A 44 22.605 42.307 47.733 1.00 79.33 C ANISOU 349 CA MET A 44 9806 9181 11155 308 -1279 581 C ATOM 350 C MET A 44 23.334 41.062 48.217 1.00 83.87 C ANISOU 350 C MET A 44 10311 9789 11766 320 -1387 657 C ATOM 351 O MET A 44 23.267 40.006 47.578 1.00 82.62 O ANISOU 351 O MET A 44 10120 9616 11654 371 -1332 723 O ATOM 352 CB MET A 44 23.543 43.192 46.914 1.00 81.15 C ANISOU 352 CB MET A 44 9945 9328 11558 273 -1237 557 C ATOM 353 CG MET A 44 22.866 44.373 46.248 1.00 77.25 C ANISOU 353 CG MET A 44 9510 8778 11064 267 -1126 516 C ATOM 354 SD MET A 44 21.479 43.867 45.217 1.00 80.51 S ANISOU 354 SD MET A 44 9989 9216 11386 334 -981 576 S ATOM 355 CE MET A 44 20.103 44.439 46.210 1.00 76.04 C ANISOU 355 CE MET A 44 9550 8683 10659 357 -991 514 C ATOM 356 N PHE A 45 24.031 41.167 49.350 1.00 75.00 N ANISOU 356 N PHE A 45 9164 8704 10627 268 -1548 650 N ATOM 357 CA PHE A 45 24.701 40.002 49.918 1.00 76.79 C ANISOU 357 CA PHE A 45 9320 8963 10894 282 -1678 749 C ATOM 358 C PHE A 45 23.692 38.928 50.303 1.00 74.45 C ANISOU 358 C PHE A 45 9117 8718 10451 319 -1675 819 C ATOM 359 O PHE A 45 23.937 37.733 50.100 1.00 75.47 O ANISOU 359 O PHE A 45 9193 8820 10663 369 -1693 916 O ATOM 360 CB PHE A 45 25.539 40.423 51.127 1.00 73.51 C ANISOU 360 CB PHE A 45 8872 8602 10455 199 -1871 737 C ATOM 361 CG PHE A 45 26.436 39.338 51.659 1.00 70.53 C ANISOU 361 CG PHE A 45 8386 8249 10165 211 -2031 864 C ATOM 362 CD1 PHE A 45 27.473 38.837 50.887 1.00 64.27 C ANISOU 362 CD1 PHE A 45 7420 7379 9622 263 -2016 922 C ATOM 363 CD2 PHE A 45 26.256 38.833 52.937 1.00 73.83 C ANISOU 363 CD2 PHE A 45 8866 8766 10420 168 -2194 930 C ATOM 364 CE1 PHE A 45 28.305 37.843 51.375 1.00 63.55 C ANISOU 364 CE1 PHE A 45 7209 7292 9646 290 -2165 1049 C ATOM 365 CE2 PHE A 45 27.086 37.839 53.433 1.00 72.31 C ANISOU 365 CE2 PHE A 45 8565 8587 10322 182 -2359 1075 C ATOM 366 CZ PHE A 45 28.111 37.345 52.651 1.00 66.12 C ANISOU 366 CZ PHE A 45 7597 7707 9817 251 -2347 1136 C ATOM 367 N LEU A 46 22.543 39.339 50.843 1.00 73.40 N ANISOU 367 N LEU A 46 9121 8653 10116 296 -1643 768 N ATOM 368 CA LEU A 46 21.507 38.383 51.221 1.00 71.81 C ANISOU 368 CA LEU A 46 9007 8512 9765 316 -1630 836 C ATOM 369 C LEU A 46 20.958 37.653 50.000 1.00 75.70 C ANISOU 369 C LEU A 46 9489 8942 10331 383 -1489 876 C ATOM 370 O LEU A 46 20.793 36.427 50.016 1.00 79.35 O ANISOU 370 O LEU A 46 9952 9396 10801 408 -1508 971 O ATOM 371 CB LEU A 46 20.386 39.104 51.972 1.00 72.41 C ANISOU 371 CB LEU A 46 9213 8678 9623 278 -1596 755 C ATOM 372 CG LEU A 46 19.189 38.263 52.415 1.00 72.57 C ANISOU 372 CG LEU A 46 9323 8781 9469 282 -1564 817 C ATOM 373 CD1 LEU A 46 19.643 37.156 53.344 1.00 78.60 C ANISOU 373 CD1 LEU A 46 10082 9599 10182 248 -1721 945 C ATOM 374 CD2 LEU A 46 18.138 39.132 53.088 1.00 72.96 C ANISOU 374 CD2 LEU A 46 9477 8918 9328 251 -1500 711 C ATOM 375 N LEU A 47 20.673 38.393 48.925 1.00 73.92 N ANISOU 375 N LEU A 47 9259 8669 10159 402 -1351 809 N ATOM 376 CA LEU A 47 20.162 37.769 47.709 1.00 68.78 C ANISOU 376 CA LEU A 47 8604 7976 9555 444 -1221 837 C ATOM 377 C LEU A 47 21.176 36.816 47.089 1.00 70.93 C ANISOU 377 C LEU A 47 8774 8171 10007 476 -1223 884 C ATOM 378 O LEU A 47 20.791 35.805 46.494 1.00 83.27 O ANISOU 378 O LEU A 47 10349 9704 11587 503 -1158 921 O ATOM 379 CB LEU A 47 19.759 38.842 46.698 1.00 74.32 C ANISOU 379 CB LEU A 47 9314 8653 10272 444 -1094 773 C ATOM 380 CG LEU A 47 18.593 39.745 47.101 1.00 75.30 C ANISOU 380 CG LEU A 47 9527 8829 10254 437 -1059 726 C ATOM 381 CD1 LEU A 47 18.381 40.837 46.065 1.00 76.13 C ANISOU 381 CD1 LEU A 47 9620 8884 10420 443 -955 690 C ATOM 382 CD2 LEU A 47 17.322 38.928 47.291 1.00 68.41 C ANISOU 382 CD2 LEU A 47 8724 8027 9241 449 -1026 772 C ATOM 383 N ILE A 48 22.471 37.116 47.213 1.00 77.69 N ANISOU 383 N ILE A 48 9521 8988 11008 471 -1292 877 N ATOM 384 CA ILE A 48 23.490 36.219 46.677 1.00 82.35 C ANISOU 384 CA ILE A 48 9990 9502 11798 514 -1285 916 C ATOM 385 C ILE A 48 23.599 34.966 47.537 1.00 84.56 C ANISOU 385 C ILE A 48 10265 9774 12091 542 -1408 1018 C ATOM 386 O ILE A 48 23.632 33.840 47.024 1.00 77.36 O ANISOU 386 O ILE A 48 9327 8788 11278 591 -1357 1057 O ATOM 387 CB ILE A 48 24.845 36.943 46.566 1.00 73.72 C ANISOU 387 CB ILE A 48 8760 8379 10873 498 -1322 887 C ATOM 388 CG1 ILE A 48 24.754 38.126 45.597 1.00 71.53 C ANISOU 388 CG1 ILE A 48 8488 8093 10599 464 -1190 807 C ATOM 389 CG2 ILE A 48 25.938 35.967 46.129 1.00 56.67 C ANISOU 389 CG2 ILE A 48 6449 6142 8941 556 -1315 929 C ATOM 390 CD1 ILE A 48 25.924 39.099 45.695 1.00 65.23 C ANISOU 390 CD1 ILE A 48 7577 7278 9930 418 -1241 776 C ATOM 391 N MET A 49 23.650 35.144 48.860 1.00 84.32 N ANISOU 391 N MET A 49 10265 9816 11959 502 -1572 1064 N ATOM 392 CA MET A 49 23.844 34.014 49.763 1.00 78.56 C ANISOU 392 CA MET A 49 9524 9085 11239 515 -1717 1193 C ATOM 393 C MET A 49 22.659 33.056 49.753 1.00 79.35 C ANISOU 393 C MET A 49 9740 9186 11225 525 -1663 1246 C ATOM 394 O MET A 49 22.833 31.859 50.006 1.00 81.54 O ANISOU 394 O MET A 49 9994 9402 11584 557 -1728 1357 O ATOM 395 CB MET A 49 24.112 34.518 51.183 1.00 76.81 C ANISOU 395 CB MET A 49 9325 8971 10888 444 -1907 1228 C ATOM 396 CG MET A 49 25.444 35.241 51.367 1.00 81.69 C ANISOU 396 CG MET A 49 9809 9586 11643 420 -2009 1204 C ATOM 397 SD MET A 49 26.885 34.180 51.132 1.00 91.10 S ANISOU 397 SD MET A 49 10788 10671 13154 498 -2099 1325 S ATOM 398 CE MET A 49 27.347 34.588 49.449 1.00 91.11 C ANISOU 398 CE MET A 49 10685 10567 13365 554 -1871 1204 C ATOM 399 N LEU A 50 21.455 33.555 49.474 1.00 71.48 N ANISOU 399 N LEU A 50 8857 8248 10055 497 -1550 1178 N ATOM 400 CA LEU A 50 20.270 32.711 49.358 1.00 65.68 C ANISOU 400 CA LEU A 50 8218 7521 9214 493 -1486 1221 C ATOM 401 C LEU A 50 19.934 32.339 47.919 1.00 78.31 C ANISOU 401 C LEU A 50 9812 9039 10902 526 -1319 1167 C ATOM 402 O LEU A 50 19.532 31.203 47.660 1.00100.96 O ANISOU 402 O LEU A 50 12709 11850 13801 535 -1291 1218 O ATOM 403 CB LEU A 50 19.056 33.400 49.991 1.00 66.72 C ANISOU 403 CB LEU A 50 8467 7785 9099 437 -1466 1189 C ATOM 404 CG LEU A 50 19.149 33.784 51.467 1.00 69.17 C ANISOU 404 CG LEU A 50 8818 8206 9257 380 -1609 1219 C ATOM 405 CD1 LEU A 50 17.808 34.297 51.979 1.00 53.55 C ANISOU 405 CD1 LEU A 50 6952 6350 7043 335 -1544 1173 C ATOM 406 CD2 LEU A 50 19.640 32.614 52.309 1.00 52.50 C ANISOU 406 CD2 LEU A 50 6692 6086 7172 368 -1764 1374 C ATOM 407 N GLY A 51 20.094 33.267 46.974 1.00 67.78 N ANISOU 407 N GLY A 51 8446 7701 9605 531 -1211 1067 N ATOM 408 CA GLY A 51 19.680 32.999 45.609 1.00 61.92 C ANISOU 408 CA GLY A 51 7714 6914 8898 538 -1055 1015 C ATOM 409 C GLY A 51 20.593 32.048 44.864 1.00 75.09 C ANISOU 409 C GLY A 51 9299 8460 10772 583 -1008 1008 C ATOM 410 O GLY A 51 20.132 31.286 44.009 1.00 82.22 O ANISOU 410 O GLY A 51 10237 9316 11686 580 -904 982 O ATOM 411 N PHE A 52 21.897 32.078 45.159 1.00 81.13 N ANISOU 411 N PHE A 52 9946 9172 11708 622 -1077 1022 N ATOM 412 CA PHE A 52 22.813 31.212 44.418 1.00 87.08 C ANISOU 412 CA PHE A 52 10598 9803 12687 679 -1010 1001 C ATOM 413 C PHE A 52 22.683 29.749 44.823 1.00 94.16 C ANISOU 413 C PHE A 52 11512 10602 13663 716 -1064 1082 C ATOM 414 O PHE A 52 22.483 28.904 43.932 1.00103.67 O ANISOU 414 O PHE A 52 12735 11716 14939 732 -941 1030 O ATOM 415 CB PHE A 52 24.253 31.713 44.556 1.00 80.84 C ANISOU 415 CB PHE A 52 9648 8988 12081 712 -1060 996 C ATOM 416 CG PHE A 52 25.277 30.735 44.050 1.00 81.19 C ANISOU 416 CG PHE A 52 9560 8900 12390 789 -1009 990 C ATOM 417 CD1 PHE A 52 25.510 30.591 42.691 1.00 81.41 C ANISOU 417 CD1 PHE A 52 9551 8877 12503 801 -810 878 C ATOM 418 CD2 PHE A 52 25.995 29.949 44.935 1.00 81.42 C ANISOU 418 CD2 PHE A 52 9496 8856 12582 849 -1158 1098 C ATOM 419 CE1 PHE A 52 26.447 29.685 42.226 1.00 77.11 C ANISOU 419 CE1 PHE A 52 8879 8205 12216 879 -738 849 C ATOM 420 CE2 PHE A 52 26.931 29.043 44.477 1.00 80.23 C ANISOU 420 CE2 PHE A 52 9207 8566 12709 938 -1105 1092 C ATOM 421 CZ PHE A 52 27.158 28.910 43.121 1.00 75.75 C ANISOU 421 CZ PHE A 52 8602 7941 12237 957 -884 955 C ATOM 422 N PRO A 53 22.783 29.369 46.108 1.00 84.62 N ANISOU 422 N PRO A 53 10305 9401 12445 722 -1242 1209 N ATOM 423 CA PRO A 53 22.713 27.930 46.427 1.00 80.66 C ANISOU 423 CA PRO A 53 9815 8782 12052 758 -1293 1306 C ATOM 424 C PRO A 53 21.400 27.282 46.011 1.00 83.40 C ANISOU 424 C PRO A 53 10302 9117 12267 711 -1201 1289 C ATOM 425 O PRO A 53 21.416 26.205 45.404 1.00 92.82 O ANISOU 425 O PRO A 53 11496 10169 13602 741 -1126 1270 O ATOM 426 CB PRO A 53 22.926 27.896 47.951 1.00 72.97 C ANISOU 426 CB PRO A 53 8835 7866 11023 743 -1516 1463 C ATOM 427 CG PRO A 53 23.601 29.184 48.283 1.00 76.15 C ANISOU 427 CG PRO A 53 9169 8376 11388 724 -1577 1422 C ATOM 428 CD PRO A 53 23.017 30.176 47.321 1.00 78.94 C ANISOU 428 CD PRO A 53 9577 8792 11624 689 -1407 1272 C ATOM 429 N ILE A 54 20.261 27.923 46.291 1.00 83.58 N ANISOU 429 N ILE A 54 10438 9284 12037 635 -1198 1286 N ATOM 430 CA ILE A 54 18.967 27.318 45.974 1.00 85.92 C ANISOU 430 CA ILE A 54 10852 9588 12206 578 -1127 1285 C ATOM 431 C ILE A 54 18.807 27.139 44.468 1.00 80.30 C ANISOU 431 C ILE A 54 10147 8817 11548 573 -948 1151 C ATOM 432 O ILE A 54 18.240 26.142 44.003 1.00 80.03 O ANISOU 432 O ILE A 54 10172 8702 11533 545 -889 1140 O ATOM 433 CB ILE A 54 17.825 28.159 46.573 1.00 94.64 C ANISOU 433 CB ILE A 54 12045 10870 13045 508 -1150 1303 C ATOM 434 CG1 ILE A 54 18.074 28.387 48.065 1.00112.15 C ANISOU 434 CG1 ILE A 54 14262 13163 15186 498 -1317 1413 C ATOM 435 CG2 ILE A 54 16.477 27.478 46.350 1.00 86.04 C ANISOU 435 CG2 ILE A 54 11056 9800 11835 441 -1092 1324 C ATOM 436 CD1 ILE A 54 17.024 29.235 48.751 1.00114.66 C ANISOU 436 CD1 ILE A 54 14661 13654 15249 435 -1324 1410 C ATOM 437 N ASN A 55 19.306 28.094 43.681 1.00 77.13 N ANISOU 437 N ASN A 55 9689 8455 11162 586 -861 1048 N ATOM 438 CA ASN A 55 19.191 27.987 42.231 1.00 79.08 C ANISOU 438 CA ASN A 55 9947 8671 11427 564 -690 923 C ATOM 439 C ASN A 55 20.270 27.097 41.628 1.00 87.53 C ANISOU 439 C ASN A 55 10935 9578 12746 628 -616 860 C ATOM 440 O ASN A 55 20.012 26.412 40.632 1.00 93.26 O ANISOU 440 O ASN A 55 11702 10237 13495 600 -486 765 O ATOM 441 CB ASN A 55 19.236 29.375 41.591 1.00 78.84 C ANISOU 441 CB ASN A 55 9896 8756 11304 539 -621 855 C ATOM 442 CG ASN A 55 17.903 30.090 41.660 1.00 85.16 C ANISOU 442 CG ASN A 55 10789 9695 11873 473 -627 878 C ATOM 443 OD1 ASN A 55 16.978 29.769 40.913 1.00 93.19 O ANISOU 443 OD1 ASN A 55 11875 10742 12790 414 -552 849 O ATOM 444 ND2 ASN A 55 17.798 31.071 42.550 1.00 80.48 N ANISOU 444 ND2 ASN A 55 10191 9186 11201 480 -716 925 N ATOM 445 N PHE A 56 21.476 27.093 42.201 1.00 87.02 N ANISOU 445 N PHE A 56 10747 9446 12871 709 -693 904 N ATOM 446 CA PHE A 56 22.513 26.193 41.705 1.00 79.23 C ANISOU 446 CA PHE A 56 9658 8290 12157 788 -619 851 C ATOM 447 C PHE A 56 22.194 24.745 42.055 1.00 81.36 C ANISOU 447 C PHE A 56 9977 8402 12533 812 -659 910 C ATOM 448 O PHE A 56 22.400 23.843 41.234 1.00 86.01 O ANISOU 448 O PHE A 56 10561 8845 13273 837 -530 809 O ATOM 449 CB PHE A 56 23.877 26.595 42.266 1.00 75.18 C ANISOU 449 CB PHE A 56 8975 7755 11834 870 -707 901 C ATOM 450 CG PHE A 56 24.994 25.681 41.851 1.00 71.85 C ANISOU 450 CG PHE A 56 8416 7154 11729 971 -636 858 C ATOM 451 CD1 PHE A 56 25.629 25.851 40.631 1.00 72.37 C ANISOU 451 CD1 PHE A 56 8406 7197 11896 986 -436 700 C ATOM 452 CD2 PHE A 56 25.409 24.650 42.679 1.00 73.82 C ANISOU 452 CD2 PHE A 56 8608 7258 12182 1052 -763 980 C ATOM 453 CE1 PHE A 56 26.655 25.009 40.244 1.00 70.19 C ANISOU 453 CE1 PHE A 56 7990 6753 11926 1089 -347 643 C ATOM 454 CE2 PHE A 56 26.433 23.804 42.298 1.00 78.36 C ANISOU 454 CE2 PHE A 56 9041 7649 13083 1162 -692 941 C ATOM 455 CZ PHE A 56 27.058 23.984 41.080 1.00 79.08 C ANISOU 455 CZ PHE A 56 9049 7716 13281 1185 -475 761 C ATOM 456 N LEU A 57 21.693 24.505 43.270 1.00 82.35 N ANISOU 456 N LEU A 57 10155 8551 12582 796 -833 1070 N ATOM 457 CA LEU A 57 21.325 23.150 43.670 1.00 80.95 C ANISOU 457 CA LEU A 57 10034 8223 12500 803 -884 1156 C ATOM 458 C LEU A 57 20.249 22.570 42.761 1.00 81.52 C ANISOU 458 C LEU A 57 10238 8264 12473 719 -747 1051 C ATOM 459 O LEU A 57 20.222 21.356 42.530 1.00 88.85 O ANISOU 459 O LEU A 57 11193 9005 13561 734 -710 1039 O ATOM 460 CB LEU A 57 20.855 23.146 45.125 1.00 74.66 C ANISOU 460 CB LEU A 57 9286 7505 11577 769 -1088 1354 C ATOM 461 CG LEU A 57 20.401 21.818 45.731 1.00 88.46 C ANISOU 461 CG LEU A 57 11099 9114 13396 756 -1171 1492 C ATOM 462 CD1 LEU A 57 21.556 20.832 45.797 1.00 94.24 C ANISOU 462 CD1 LEU A 57 11715 9613 14481 875 -1210 1545 C ATOM 463 CD2 LEU A 57 19.798 22.041 47.109 1.00 86.82 C ANISOU 463 CD2 LEU A 57 10955 9048 12984 691 -1348 1676 C ATOM 464 N THR A 58 19.361 23.418 42.234 1.00 80.73 N ANISOU 464 N THR A 58 10215 8337 12121 628 -677 979 N ATOM 465 CA THR A 58 18.348 22.947 41.293 1.00 83.62 C ANISOU 465 CA THR A 58 10694 8700 12377 533 -557 878 C ATOM 466 C THR A 58 18.987 22.384 40.030 1.00 89.26 C ANISOU 466 C THR A 58 11382 9277 13257 556 -381 699 C ATOM 467 O THR A 58 18.568 21.336 39.526 1.00 96.35 O ANISOU 467 O THR A 58 12355 10048 14207 512 -310 629 O ATOM 468 CB THR A 58 17.384 24.084 40.948 1.00 73.11 C ANISOU 468 CB THR A 58 9422 7591 10766 444 -528 851 C ATOM 469 OG1 THR A 58 16.693 24.504 42.131 1.00 73.16 O ANISOU 469 OG1 THR A 58 9460 7715 10622 420 -667 996 O ATOM 470 CG2 THR A 58 16.367 23.634 39.906 1.00 69.17 C ANISOU 470 CG2 THR A 58 9025 7108 10148 332 -418 753 C ATOM 471 N LEU A 59 20.008 23.065 39.504 1.00 86.05 N ANISOU 471 N LEU A 59 10868 8893 12933 617 -301 613 N ATOM 472 CA LEU A 59 20.724 22.533 38.349 1.00 83.40 C ANISOU 472 CA LEU A 59 10492 8434 12761 644 -115 433 C ATOM 473 C LEU A 59 21.556 21.314 38.720 1.00 86.18 C ANISOU 473 C LEU A 59 10769 8533 13441 758 -127 448 C ATOM 474 O LEU A 59 21.766 20.429 37.882 1.00 89.76 O ANISOU 474 O LEU A 59 11239 8830 14036 766 25 295 O ATOM 475 CB LEU A 59 21.619 23.611 37.739 1.00 85.31 C ANISOU 475 CB LEU A 59 10627 8780 13008 672 -22 354 C ATOM 476 CG LEU A 59 20.939 24.893 37.257 1.00 95.09 C ANISOU 476 CG LEU A 59 11924 10247 13961 571 0 343 C ATOM 477 CD1 LEU A 59 21.964 25.839 36.651 1.00 93.99 C ANISOU 477 CD1 LEU A 59 11670 10175 13869 597 98 276 C ATOM 478 CD2 LEU A 59 19.839 24.575 36.257 1.00 94.74 C ANISOU 478 CD2 LEU A 59 12021 10256 13720 442 104 244 C ATOM 479 N TYR A 60 22.033 21.245 39.965 1.00 81.84 N ANISOU 479 N TYR A 60 10138 7937 13018 844 -308 630 N ATOM 480 CA TYR A 60 22.909 20.149 40.363 1.00 81.92 C ANISOU 480 CA TYR A 60 10052 7704 13372 967 -342 678 C ATOM 481 C TYR A 60 22.134 18.845 40.507 1.00 90.31 C ANISOU 481 C TYR A 60 11236 8588 14489 930 -360 709 C ATOM 482 O TYR A 60 22.553 17.803 39.989 1.00 96.13 O ANISOU 482 O TYR A 60 11954 9092 15481 988 -251 607 O ATOM 483 CB TYR A 60 23.627 20.501 41.667 1.00 81.91 C ANISOU 483 CB TYR A 60 9928 7729 13467 1051 -556 887 C ATOM 484 CG TYR A 60 24.636 19.465 42.115 1.00 88.08 C ANISOU 484 CG TYR A 60 10576 8266 14625 1192 -617 970 C ATOM 485 CD1 TYR A 60 25.918 19.438 41.581 1.00 84.43 C ANISOU 485 CD1 TYR A 60 9930 7704 14445 1312 -510 873 C ATOM 486 CD2 TYR A 60 24.308 18.518 43.078 1.00 93.00 C ANISOU 486 CD2 TYR A 60 11245 8756 15334 1205 -781 1160 C ATOM 487 CE1 TYR A 60 26.843 18.495 41.988 1.00 90.35 C ANISOU 487 CE1 TYR A 60 10535 8221 15571 1456 -568 959 C ATOM 488 CE2 TYR A 60 25.227 17.571 43.491 1.00100.61 C ANISOU 488 CE2 TYR A 60 12079 9484 16666 1341 -851 1262 C ATOM 489 CZ TYR A 60 26.492 17.564 42.944 1.00102.16 C ANISOU 489 CZ TYR A 60 12083 9577 17158 1474 -746 1159 C ATOM 490 OH TYR A 60 27.408 16.623 43.354 1.00106.66 O ANISOU 490 OH TYR A 60 12501 9901 18123 1624 -818 1269 O ATOM 491 N VAL A 61 20.997 18.881 41.209 1.00 87.12 N ANISOU 491 N VAL A 61 10956 8284 13859 829 -489 844 N ATOM 492 CA VAL A 61 20.233 17.657 41.436 1.00 84.53 C ANISOU 492 CA VAL A 61 10743 7792 13583 776 -521 900 C ATOM 493 C VAL A 61 19.654 17.124 40.133 1.00 92.05 C ANISOU 493 C VAL A 61 11802 8675 14497 686 -324 674 C ATOM 494 O VAL A 61 19.438 15.915 39.991 1.00105.29 O ANISOU 494 O VAL A 61 13543 10126 16337 672 -291 645 O ATOM 495 CB VAL A 61 19.131 17.893 42.487 1.00 74.58 C ANISOU 495 CB VAL A 61 9580 6688 12070 675 -690 1096 C ATOM 496 CG1 VAL A 61 19.750 18.272 43.822 1.00 75.16 C ANISOU 496 CG1 VAL A 61 9560 6817 12181 751 -890 1313 C ATOM 497 CG2 VAL A 61 18.157 18.964 42.014 1.00 69.49 C ANISOU 497 CG2 VAL A 61 9011 6308 11082 556 -633 1016 C ATOM 498 N THR A 62 19.394 18.004 39.165 1.00 86.02 N ANISOU 498 N THR A 62 11065 8098 13519 614 -196 515 N ATOM 499 CA THR A 62 18.926 17.542 37.863 1.00 87.94 C ANISOU 499 CA THR A 62 11408 8300 13705 514 -10 291 C ATOM 500 C THR A 62 19.998 16.717 37.162 1.00 90.05 C ANISOU 500 C THR A 62 11608 8321 14287 614 154 114 C ATOM 501 O THR A 62 19.692 15.720 36.497 1.00 95.50 O ANISOU 501 O THR A 62 12390 8841 15054 557 268 -37 O ATOM 502 CB THR A 62 18.508 18.738 37.007 1.00 86.17 C ANISOU 502 CB THR A 62 11213 8345 13182 417 75 190 C ATOM 503 OG1 THR A 62 17.441 19.437 37.660 1.00 85.31 O ANISOU 503 OG1 THR A 62 11161 8441 12811 334 -66 347 O ATOM 504 CG2 THR A 62 18.039 18.281 35.636 1.00 85.23 C ANISOU 504 CG2 THR A 62 11202 8211 12972 293 256 -38 C ATOM 505 N VAL A 63 21.265 17.109 37.316 1.00 87.79 N ANISOU 505 N VAL A 63 11154 8006 14196 761 170 122 N ATOM 506 CA VAL A 63 22.363 16.333 36.748 1.00 88.94 C ANISOU 506 CA VAL A 63 11201 7911 14681 882 329 -36 C ATOM 507 C VAL A 63 22.454 14.964 37.410 1.00 93.27 C ANISOU 507 C VAL A 63 11753 8147 15538 961 251 55 C ATOM 508 O VAL A 63 22.826 13.975 36.765 1.00 86.86 O ANISOU 508 O VAL A 63 10943 7087 14974 1006 409 -120 O ATOM 509 CB VAL A 63 23.681 17.126 36.878 1.00 80.00 C ANISOU 509 CB VAL A 63 9862 6840 13695 1019 341 -13 C ATOM 510 CG1 VAL A 63 24.876 16.285 36.451 1.00 69.50 C ANISOU 510 CG1 VAL A 63 8392 5250 12765 1171 495 -149 C ATOM 511 CG2 VAL A 63 23.608 18.402 36.055 1.00 71.89 C ANISOU 511 CG2 VAL A 63 8842 6089 12384 929 449 -121 C ATOM 512 N GLN A 64 22.090 14.872 38.690 1.00 93.54 N ANISOU 512 N GLN A 64 11796 8184 15560 970 14 326 N ATOM 513 CA GLN A 64 22.262 13.639 39.448 1.00 94.11 C ANISOU 513 CA GLN A 64 11857 7963 15938 1050 -92 469 C ATOM 514 C GLN A 64 21.052 12.714 39.399 1.00107.04 C ANISOU 514 C GLN A 64 13686 9489 17496 909 -102 467 C ATOM 515 O GLN A 64 21.220 11.491 39.468 1.00113.96 O ANISOU 515 O GLN A 64 14577 10050 18670 960 -88 467 O ATOM 516 CB GLN A 64 22.582 13.958 40.910 1.00 93.38 C ANISOU 516 CB GLN A 64 11670 7932 15878 1123 -355 785 C ATOM 517 CG GLN A 64 24.047 14.248 41.182 1.00105.84 C ANISOU 517 CG GLN A 64 13021 9462 17731 1306 -385 833 C ATOM 518 CD GLN A 64 24.364 14.235 42.663 1.00115.17 C ANISOU 518 CD GLN A 64 14121 10648 18990 1368 -665 1157 C ATOM 519 OE1 GLN A 64 23.462 14.173 43.498 1.00113.24 O ANISOU 519 OE1 GLN A 64 13998 10487 18542 1266 -826 1341 O ATOM 520 NE2 GLN A 64 25.648 14.285 42.997 1.00116.33 N ANISOU 520 NE2 GLN A 64 14057 10719 19426 1529 -724 1233 N ATOM 521 N HIS A 65 19.842 13.257 39.288 1.00101.43 N ANISOU 521 N HIS A 65 13114 9016 16411 733 -128 471 N ATOM 522 CA HIS A 65 18.615 12.469 39.367 1.00 91.58 C ANISOU 522 CA HIS A 65 12034 7700 15063 580 -165 504 C ATOM 523 C HIS A 65 17.993 12.373 37.979 1.00 93.38 C ANISOU 523 C HIS A 65 12381 7966 15132 437 35 216 C ATOM 524 O HIS A 65 17.521 13.376 37.432 1.00 89.74 O ANISOU 524 O HIS A 65 11949 7788 14360 343 81 140 O ATOM 525 CB HIS A 65 17.649 13.084 40.375 1.00 71.57 C ANISOU 525 CB HIS A 65 9550 5410 12233 481 -356 744 C ATOM 526 CG HIS A 65 18.200 13.146 41.765 1.00 78.06 C ANISOU 526 CG HIS A 65 10275 6214 13169 591 -561 1026 C ATOM 527 ND1 HIS A 65 17.867 12.231 42.739 1.00 82.23 N ANISOU 527 ND1 HIS A 65 10848 6587 13808 571 -711 1250 N ATOM 528 CD2 HIS A 65 19.077 14.004 42.338 1.00 81.35 C ANISOU 528 CD2 HIS A 65 10554 6754 13600 708 -647 1124 C ATOM 529 CE1 HIS A 65 18.508 12.527 43.856 1.00 83.60 C ANISOU 529 CE1 HIS A 65 10919 6802 14041 669 -886 1479 C ATOM 530 NE2 HIS A 65 19.248 13.599 43.640 1.00 86.10 N ANISOU 530 NE2 HIS A 65 11124 7288 14303 752 -853 1400 N ATOM 531 N LYS A 66 17.985 11.159 37.422 1.00 99.28 N ANISOU 531 N LYS A 66 13202 8423 16097 414 147 62 N ATOM 532 CA LYS A 66 17.492 10.958 36.062 1.00 98.75 C ANISOU 532 CA LYS A 66 13255 8374 15893 269 344 -237 C ATOM 533 C LYS A 66 16.015 11.311 35.944 1.00 97.42 C ANISOU 533 C LYS A 66 13223 8449 15344 46 275 -197 C ATOM 534 O LYS A 66 15.579 11.855 34.922 1.00 91.60 O ANISOU 534 O LYS A 66 12544 7911 14347 -79 385 -376 O ATOM 535 CB LYS A 66 17.734 9.510 35.631 1.00 94.69 C ANISOU 535 CB LYS A 66 12801 7470 15705 283 464 -406 C ATOM 536 CG LYS A 66 17.063 9.123 34.324 1.00 99.76 C ANISOU 536 CG LYS A 66 13602 8113 16191 92 646 -713 C ATOM 537 CD LYS A 66 17.203 7.635 34.051 1.00113.22 C ANISOU 537 CD LYS A 66 15384 9403 18233 94 746 -869 C ATOM 538 CE LYS A 66 16.208 7.178 32.998 1.00125.01 C ANISOU 538 CE LYS A 66 17068 10913 19516 -154 860 -1122 C ATOM 539 NZ LYS A 66 14.806 7.445 33.425 1.00126.27 N ANISOU 539 NZ LYS A 66 17326 11296 19356 -355 679 -933 N ATOM 540 N LYS A 67 15.228 11.019 36.981 1.00 95.83 N ANISOU 540 N LYS A 67 13063 8245 15104 -12 92 49 N ATOM 541 CA LYS A 67 13.792 11.259 36.923 1.00 92.25 C ANISOU 541 CA LYS A 67 12718 8008 14324 -221 27 98 C ATOM 542 C LYS A 67 13.432 12.738 36.837 1.00 86.23 C ANISOU 542 C LYS A 67 11910 7629 13224 -251 -5 143 C ATOM 543 O LYS A 67 12.265 13.054 36.585 1.00 93.66 O ANISOU 543 O LYS A 67 12922 8773 13891 -419 -34 153 O ATOM 544 CB LYS A 67 13.109 10.625 38.136 1.00 90.35 C ANISOU 544 CB LYS A 67 12514 7682 14132 -268 -152 366 C ATOM 545 CG LYS A 67 13.132 9.105 38.117 1.00 99.85 C ANISOU 545 CG LYS A 67 13797 8504 15636 -296 -127 326 C ATOM 546 CD LYS A 67 12.563 8.581 36.806 1.00104.14 C ANISOU 546 CD LYS A 67 14468 8989 16111 -470 31 32 C ATOM 547 CE LYS A 67 12.745 7.079 36.662 1.00110.84 C ANISOU 547 CE LYS A 67 15398 9416 17301 -483 88 -62 C ATOM 548 NZ LYS A 67 12.261 6.596 35.338 1.00115.44 N ANISOU 548 NZ LYS A 67 16114 9946 17804 -662 253 -386 N ATOM 549 N LEU A 68 14.390 13.645 37.031 1.00 77.04 N ANISOU 549 N LEU A 68 10623 6561 12088 -95 -2 174 N ATOM 550 CA LEU A 68 14.110 15.070 36.921 1.00 78.16 C ANISOU 550 CA LEU A 68 10722 7035 11939 -116 -26 210 C ATOM 551 C LEU A 68 14.276 15.603 35.505 1.00 80.82 C ANISOU 551 C LEU A 68 11076 7492 12140 -173 146 -31 C ATOM 552 O LEU A 68 13.807 16.710 35.217 1.00 88.99 O ANISOU 552 O LEU A 68 12102 8800 12912 -231 132 -9 O ATOM 553 CB LEU A 68 15.021 15.869 37.859 1.00 78.39 C ANISOU 553 CB LEU A 68 10616 7123 12045 56 -119 368 C ATOM 554 CG LEU A 68 14.814 15.688 39.362 1.00 83.40 C ANISOU 554 CG LEU A 68 11229 7737 12722 97 -313 639 C ATOM 555 CD1 LEU A 68 15.814 16.534 40.134 1.00 77.31 C ANISOU 555 CD1 LEU A 68 10325 7038 12010 251 -396 755 C ATOM 556 CD2 LEU A 68 13.390 16.043 39.758 1.00 74.68 C ANISOU 556 CD2 LEU A 68 10199 6846 11328 -52 -400 756 C ATOM 557 N ARG A 69 14.922 14.846 34.621 1.00 77.77 N ANISOU 557 N ARG A 69 10714 6908 11927 -160 311 -257 N ATOM 558 CA ARG A 69 15.233 15.317 33.272 1.00 82.39 C ANISOU 558 CA ARG A 69 11312 7607 12384 -214 492 -493 C ATOM 559 C ARG A 69 14.105 14.968 32.298 1.00 88.55 C ANISOU 559 C ARG A 69 12243 8472 12929 -443 546 -638 C ATOM 560 O ARG A 69 14.286 14.272 31.300 1.00 90.75 O ANISOU 560 O ARG A 69 12598 8633 13249 -518 708 -886 O ATOM 561 CB ARG A 69 16.568 14.742 32.813 1.00 82.93 C ANISOU 561 CB ARG A 69 11317 7441 12752 -80 663 -679 C ATOM 562 CG ARG A 69 17.753 15.232 33.632 1.00 80.33 C ANISOU 562 CG ARG A 69 10813 7070 12638 137 610 -543 C ATOM 563 CD ARG A 69 19.079 14.842 33.002 1.00 83.17 C ANISOU 563 CD ARG A 69 11081 7246 13274 265 807 -745 C ATOM 564 NE ARG A 69 19.320 13.405 33.062 1.00 97.73 N ANISOU 564 NE ARG A 69 12957 8740 15438 316 864 -835 N ATOM 565 CZ ARG A 69 19.894 12.787 34.088 1.00 95.17 C ANISOU 565 CZ ARG A 69 12540 8179 15442 476 754 -673 C ATOM 566 NH1 ARG A 69 20.286 13.482 35.148 1.00 92.39 N ANISOU 566 NH1 ARG A 69 12063 7924 15116 589 578 -421 N ATOM 567 NH2 ARG A 69 20.076 11.474 34.055 1.00 84.99 N ANISOU 567 NH2 ARG A 69 11285 6551 14457 519 815 -760 N ATOM 568 N THR A 70 12.915 15.484 32.610 1.00 93.61 N ANISOU 568 N THR A 70 12920 9330 13318 -562 408 -482 N ATOM 569 CA THR A 70 11.735 15.325 31.777 1.00 94.61 C ANISOU 569 CA THR A 70 13164 9591 13192 -790 417 -570 C ATOM 570 C THR A 70 11.411 16.639 31.068 1.00101.12 C ANISOU 570 C THR A 70 13964 10745 13711 -858 424 -564 C ATOM 571 O THR A 70 11.763 17.715 31.563 1.00 97.44 O ANISOU 571 O THR A 70 13395 10413 13213 -738 368 -422 O ATOM 572 CB THR A 70 10.524 14.882 32.608 1.00 88.44 C ANISOU 572 CB THR A 70 12426 8815 12364 -889 254 -388 C ATOM 573 OG1 THR A 70 10.228 15.877 33.596 1.00100.59 O ANISOU 573 OG1 THR A 70 13871 10541 13807 -810 112 -140 O ATOM 574 CG2 THR A 70 10.808 13.556 33.298 1.00 87.33 C ANISOU 574 CG2 THR A 70 12318 8336 12528 -838 238 -369 C ATOM 575 N PRO A 71 10.754 16.585 29.902 1.00 99.28 N ANISOU 575 N PRO A 71 13826 10644 13252 -1057 486 -713 N ATOM 576 CA PRO A 71 10.496 17.831 29.155 1.00 93.77 C ANISOU 576 CA PRO A 71 13104 10254 12272 -1124 489 -690 C ATOM 577 C PRO A 71 9.708 18.870 29.935 1.00 84.92 C ANISOU 577 C PRO A 71 11903 9343 11019 -1095 315 -425 C ATOM 578 O PRO A 71 9.988 20.068 29.810 1.00 93.52 O ANISOU 578 O PRO A 71 12918 10604 12009 -1031 309 -350 O ATOM 579 CB PRO A 71 9.724 17.339 27.923 1.00 86.47 C ANISOU 579 CB PRO A 71 12309 9417 11129 -1373 544 -868 C ATOM 580 CG PRO A 71 10.170 15.931 27.743 1.00 81.43 C ANISOU 580 CG PRO A 71 11759 8478 10705 -1391 662 -1084 C ATOM 581 CD PRO A 71 10.348 15.394 29.136 1.00 83.42 C ANISOU 581 CD PRO A 71 11953 8499 11242 -1231 567 -923 C ATOM 582 N LEU A 72 8.729 18.449 30.741 1.00 77.94 N ANISOU 582 N LEU A 72 11029 8444 10140 -1143 183 -284 N ATOM 583 CA LEU A 72 7.951 19.401 31.527 1.00 78.27 C ANISOU 583 CA LEU A 72 10989 8681 10069 -1111 38 -49 C ATOM 584 C LEU A 72 8.781 20.097 32.596 1.00 88.82 C ANISOU 584 C LEU A 72 12223 9979 11547 -893 3 82 C ATOM 585 O LEU A 72 8.304 21.069 33.194 1.00 92.74 O ANISOU 585 O LEU A 72 12647 10640 11950 -847 -91 248 O ATOM 586 CB LEU A 72 6.755 18.699 32.176 1.00 72.30 C ANISOU 586 CB LEU A 72 10260 7912 9298 -1218 -74 63 C ATOM 587 CG LEU A 72 5.589 18.354 31.247 1.00 83.46 C ANISOU 587 CG LEU A 72 11742 9456 10511 -1460 -96 0 C ATOM 588 CD1 LEU A 72 4.500 17.590 31.987 1.00 74.30 C ANISOU 588 CD1 LEU A 72 10594 8260 9375 -1562 -200 116 C ATOM 589 CD2 LEU A 72 5.023 19.618 30.620 1.00 83.74 C ANISOU 589 CD2 LEU A 72 11719 9793 10305 -1509 -139 73 C ATOM 590 N ASN A 73 10.002 19.630 32.849 1.00 82.82 N ANISOU 590 N ASN A 73 11447 9005 11014 -761 75 6 N ATOM 591 CA ASN A 73 10.898 20.256 33.808 1.00 76.87 C ANISOU 591 CA ASN A 73 10592 8216 10398 -567 35 118 C ATOM 592 C ASN A 73 11.909 21.196 33.165 1.00 75.97 C ANISOU 592 C ASN A 73 10417 8172 10276 -488 130 39 C ATOM 593 O ASN A 73 12.648 21.867 33.892 1.00 75.47 O ANISOU 593 O ASN A 73 10262 8105 10307 -343 91 129 O ATOM 594 CB ASN A 73 11.642 19.183 34.611 1.00 81.59 C ANISOU 594 CB ASN A 73 11185 8538 11278 -462 27 125 C ATOM 595 CG ASN A 73 10.825 18.656 35.770 1.00 83.83 C ANISOU 595 CG ASN A 73 11488 8784 11581 -486 -112 304 C ATOM 596 OD1 ASN A 73 9.685 19.070 35.976 1.00 92.58 O ANISOU 596 OD1 ASN A 73 12606 10073 12496 -581 -189 408 O ATOM 597 ND2 ASN A 73 11.403 17.737 36.534 1.00 92.01 N ANISOU 597 ND2 ASN A 73 12520 9585 12856 -402 -143 352 N ATOM 598 N TYR A 74 11.961 21.259 31.831 1.00 68.77 N ANISOU 598 N TYR A 74 9554 7331 9244 -594 252 -124 N ATOM 599 CA TYR A 74 12.923 22.134 31.166 1.00 70.30 C ANISOU 599 CA TYR A 74 9691 7600 9421 -538 356 -194 C ATOM 600 C TYR A 74 12.729 23.585 31.587 1.00 76.49 C ANISOU 600 C TYR A 74 10397 8574 10093 -485 260 -19 C ATOM 601 O TYR A 74 13.698 24.295 31.881 1.00 79.01 O ANISOU 601 O TYR A 74 10628 8881 10512 -361 278 9 O ATOM 602 CB TYR A 74 12.799 22.013 29.645 1.00 68.90 C ANISOU 602 CB TYR A 74 9596 7514 9069 -700 493 -378 C ATOM 603 CG TYR A 74 13.319 20.725 29.043 1.00 82.13 C ANISOU 603 CG TYR A 74 11343 8989 10875 -737 644 -612 C ATOM 604 CD1 TYR A 74 13.793 19.691 29.840 1.00 84.83 C ANISOU 604 CD1 TYR A 74 11670 9061 11500 -625 642 -632 C ATOM 605 CD2 TYR A 74 13.344 20.553 27.665 1.00 91.39 C ANISOU 605 CD2 TYR A 74 12599 10238 11887 -888 793 -814 C ATOM 606 CE1 TYR A 74 14.266 18.517 29.278 1.00 85.92 C ANISOU 606 CE1 TYR A 74 11871 8988 11788 -648 791 -855 C ATOM 607 CE2 TYR A 74 13.814 19.389 27.097 1.00 93.84 C ANISOU 607 CE2 TYR A 74 12981 10357 12318 -924 952 -1058 C ATOM 608 CZ TYR A 74 14.275 18.374 27.905 1.00 91.48 C ANISOU 608 CZ TYR A 74 12660 9767 12330 -796 954 -1082 C ATOM 609 OH TYR A 74 14.744 17.214 27.334 1.00 98.74 O ANISOU 609 OH TYR A 74 13646 10468 13401 -821 1121 -1333 O ATOM 610 N ILE A 75 11.474 24.041 31.628 1.00 79.02 N ANISOU 610 N ILE A 75 10741 9064 10220 -578 156 96 N ATOM 611 CA ILE A 75 11.203 25.446 31.911 1.00 81.91 C ANISOU 611 CA ILE A 75 11037 9601 10484 -532 79 246 C ATOM 612 C ILE A 75 11.524 25.781 33.362 1.00 83.07 C ANISOU 612 C ILE A 75 11109 9680 10774 -376 -16 373 C ATOM 613 O ILE A 75 11.807 26.940 33.690 1.00 83.92 O ANISOU 613 O ILE A 75 11149 9865 10872 -297 -50 455 O ATOM 614 CB ILE A 75 9.744 25.792 31.554 1.00 83.73 C ANISOU 614 CB ILE A 75 11296 10022 10497 -665 -3 337 C ATOM 615 CG1 ILE A 75 9.606 27.287 31.267 1.00 75.56 C ANISOU 615 CG1 ILE A 75 10198 9162 9349 -644 -35 445 C ATOM 616 CG2 ILE A 75 8.793 25.370 32.663 1.00 80.81 C ANISOU 616 CG2 ILE A 75 10918 9635 10150 -658 -120 455 C ATOM 617 CD1 ILE A 75 10.351 27.732 30.031 1.00 75.76 C ANISOU 617 CD1 ILE A 75 10240 9244 9303 -695 77 352 C ATOM 618 N LEU A 76 11.489 24.786 34.253 1.00 76.82 N ANISOU 618 N LEU A 76 10335 8744 10111 -340 -64 395 N ATOM 619 CA LEU A 76 11.933 25.016 35.624 1.00 77.21 C ANISOU 619 CA LEU A 76 10321 8730 10285 -204 -153 509 C ATOM 620 C LEU A 76 13.444 25.195 35.683 1.00 88.32 C ANISOU 620 C LEU A 76 11659 10026 11874 -81 -99 451 C ATOM 621 O LEU A 76 13.947 26.028 36.447 1.00 92.18 O ANISOU 621 O LEU A 76 12075 10543 12405 16 -160 533 O ATOM 622 CB LEU A 76 11.493 23.862 36.524 1.00 78.79 C ANISOU 622 CB LEU A 76 10561 8811 10565 -215 -224 570 C ATOM 623 CG LEU A 76 9.989 23.685 36.734 1.00 78.87 C ANISOU 623 CG LEU A 76 10615 8935 10417 -331 -293 656 C ATOM 624 CD1 LEU A 76 9.718 22.474 37.612 1.00 78.71 C ANISOU 624 CD1 LEU A 76 10636 8774 10498 -349 -352 721 C ATOM 625 CD2 LEU A 76 9.383 24.940 37.343 1.00 70.70 C ANISOU 625 CD2 LEU A 76 9521 8086 9254 -296 -365 782 C ATOM 626 N LEU A 77 14.184 24.418 34.889 1.00 87.50 N ANISOU 626 N LEU A 77 11570 9795 11883 -89 21 303 N ATOM 627 CA LEU A 77 15.624 24.628 34.795 1.00 83.99 C ANISOU 627 CA LEU A 77 11036 9260 11615 23 94 238 C ATOM 628 C LEU A 77 15.933 25.972 34.153 1.00 81.91 C ANISOU 628 C LEU A 77 10726 9156 11240 13 144 231 C ATOM 629 O LEU A 77 16.898 26.645 34.534 1.00 79.83 O ANISOU 629 O LEU A 77 10365 8879 11086 110 135 261 O ATOM 630 CB LEU A 77 16.271 23.494 34.003 1.00 87.98 C ANISOU 630 CB LEU A 77 11563 9596 12268 15 240 60 C ATOM 631 CG LEU A 77 16.210 22.115 34.657 1.00 86.39 C ANISOU 631 CG LEU A 77 11395 9180 12248 47 197 69 C ATOM 632 CD1 LEU A 77 16.734 21.056 33.704 1.00 92.75 C ANISOU 632 CD1 LEU A 77 12236 9816 13191 27 366 -141 C ATOM 633 CD2 LEU A 77 16.999 22.117 35.955 1.00 81.07 C ANISOU 633 CD2 LEU A 77 10621 8403 11781 201 81 207 C ATOM 634 N ASN A 78 15.122 26.379 33.174 1.00 83.11 N ANISOU 634 N ASN A 78 10942 9459 11176 -114 187 203 N ATOM 635 CA ASN A 78 15.275 27.705 32.591 1.00 78.51 C ANISOU 635 CA ASN A 78 10323 9030 10478 -135 214 234 C ATOM 636 C ASN A 78 15.027 28.792 33.626 1.00 74.89 C ANISOU 636 C ASN A 78 9809 8637 10007 -59 80 394 C ATOM 637 O ASN A 78 15.654 29.856 33.573 1.00 76.73 O ANISOU 637 O ASN A 78 9977 8916 10261 -17 90 424 O ATOM 638 CB ASN A 78 14.323 27.865 31.407 1.00 67.22 C ANISOU 638 CB ASN A 78 8975 7756 8810 -295 255 207 C ATOM 639 CG ASN A 78 14.659 29.065 30.551 1.00 71.37 C ANISOU 639 CG ASN A 78 9470 8418 9228 -333 312 226 C ATOM 640 OD1 ASN A 78 15.813 29.273 30.182 1.00 77.34 O ANISOU 640 OD1 ASN A 78 10174 9133 10078 -295 420 152 O ATOM 641 ND2 ASN A 78 13.650 29.870 30.239 1.00 75.46 N ANISOU 641 ND2 ASN A 78 10011 9097 9562 -409 238 339 N ATOM 642 N LEU A 79 14.125 28.537 34.579 1.00 79.18 N ANISOU 642 N LEU A 79 10379 9185 10521 -49 -38 489 N ATOM 643 CA LEU A 79 13.884 29.491 35.656 1.00 75.36 C ANISOU 643 CA LEU A 79 9849 8757 10027 23 -152 615 C ATOM 644 C LEU A 79 15.099 29.618 36.565 1.00 73.06 C ANISOU 644 C LEU A 79 9482 8360 9916 142 -186 624 C ATOM 645 O LEU A 79 15.434 30.722 37.010 1.00 84.76 O ANISOU 645 O LEU A 79 10911 9886 11407 193 -230 674 O ATOM 646 CB LEU A 79 12.655 29.068 36.460 1.00 65.43 C ANISOU 646 CB LEU A 79 8635 7536 8690 -4 -247 702 C ATOM 647 CG LEU A 79 12.245 29.979 37.617 1.00 67.81 C ANISOU 647 CG LEU A 79 8900 7907 8958 60 -347 813 C ATOM 648 CD1 LEU A 79 11.832 31.346 37.095 1.00 68.48 C ANISOU 648 CD1 LEU A 79 8958 8117 8944 49 -338 849 C ATOM 649 CD2 LEU A 79 11.124 29.348 38.431 1.00 60.98 C ANISOU 649 CD2 LEU A 79 8072 7073 8026 26 -418 888 C ATOM 650 N ALA A 80 15.769 28.500 36.858 1.00 73.30 N ANISOU 650 N ALA A 80 9503 8244 10104 185 -175 580 N ATOM 651 CA ALA A 80 16.941 28.553 37.724 1.00 70.93 C ANISOU 651 CA ALA A 80 9115 7848 9987 295 -228 605 C ATOM 652 C ALA A 80 18.099 29.272 37.044 1.00 79.88 C ANISOU 652 C ALA A 80 10162 8982 11207 325 -138 536 C ATOM 653 O ALA A 80 18.856 29.998 37.699 1.00 85.33 O ANISOU 653 O ALA A 80 10771 9672 11980 389 -201 581 O ATOM 654 CB ALA A 80 17.355 27.141 38.138 1.00 73.92 C ANISOU 654 CB ALA A 80 9492 8057 10538 338 -242 593 C ATOM 655 N VAL A 81 18.252 29.082 35.732 1.00 84.57 N ANISOU 655 N VAL A 81 10774 9586 11775 264 10 425 N ATOM 656 CA VAL A 81 19.307 29.776 34.999 1.00 83.22 C ANISOU 656 CA VAL A 81 10520 9433 11666 273 116 362 C ATOM 657 C VAL A 81 19.038 31.275 34.965 1.00 88.61 C ANISOU 657 C VAL A 81 11194 10250 12224 243 73 442 C ATOM 658 O VAL A 81 19.952 32.088 35.151 1.00 86.68 O ANISOU 658 O VAL A 81 10858 10002 12073 284 69 459 O ATOM 659 CB VAL A 81 19.444 29.188 33.582 1.00 78.08 C ANISOU 659 CB VAL A 81 9906 8781 10979 196 298 217 C ATOM 660 CG1 VAL A 81 20.277 30.103 32.703 1.00 82.69 C ANISOU 660 CG1 VAL A 81 10423 9440 11557 167 416 173 C ATOM 661 CG2 VAL A 81 20.068 27.804 33.649 1.00 74.11 C ANISOU 661 CG2 VAL A 81 9380 8100 10678 256 362 115 C ATOM 662 N ALA A 82 17.781 31.665 34.737 1.00 87.29 N ANISOU 662 N ALA A 82 11113 10192 11861 171 37 498 N ATOM 663 CA ALA A 82 17.433 33.083 34.739 1.00 78.89 C ANISOU 663 CA ALA A 82 10040 9231 10703 154 -9 584 C ATOM 664 C ALA A 82 17.734 33.724 36.086 1.00 81.13 C ANISOU 664 C ALA A 82 10270 9479 11076 243 -132 652 C ATOM 665 O ALA A 82 18.258 34.843 36.145 1.00 88.49 O ANISOU 665 O ALA A 82 11151 10427 12046 256 -142 679 O ATOM 666 CB ALA A 82 15.959 33.266 34.381 1.00 75.15 C ANISOU 666 CB ALA A 82 9649 8871 10034 78 -42 644 C ATOM 667 N ASP A 83 17.412 33.031 37.182 1.00 77.07 N ANISOU 667 N ASP A 83 9776 8920 10589 290 -228 682 N ATOM 668 CA ASP A 83 17.728 33.568 38.501 1.00 80.06 C ANISOU 668 CA ASP A 83 10114 9279 11026 357 -347 737 C ATOM 669 C ASP A 83 19.228 33.731 38.689 1.00 77.85 C ANISOU 669 C ASP A 83 9730 8923 10928 408 -346 705 C ATOM 670 O ASP A 83 19.670 34.657 39.377 1.00 83.32 O ANISOU 670 O ASP A 83 10377 9624 11656 432 -420 733 O ATOM 671 CB ASP A 83 17.156 32.668 39.595 1.00 81.42 C ANISOU 671 CB ASP A 83 10329 9427 11178 381 -443 784 C ATOM 672 CG ASP A 83 15.646 32.703 39.652 1.00 90.23 C ANISOU 672 CG ASP A 83 11526 10636 12121 332 -460 830 C ATOM 673 OD1 ASP A 83 15.046 33.582 38.999 1.00 99.66 O ANISOU 673 OD1 ASP A 83 12733 11914 13221 297 -421 838 O ATOM 674 OD2 ASP A 83 15.058 31.857 40.358 1.00 94.28 O ANISOU 674 OD2 ASP A 83 12080 11140 12600 328 -516 871 O ATOM 675 N LEU A 84 20.026 32.851 38.080 1.00 73.29 N ANISOU 675 N LEU A 84 9105 8268 10474 420 -260 640 N ATOM 676 CA LEU A 84 21.474 32.984 38.176 1.00 78.55 C ANISOU 676 CA LEU A 84 9642 8868 11333 471 -248 612 C ATOM 677 C LEU A 84 21.982 34.171 37.368 1.00 82.11 C ANISOU 677 C LEU A 84 10045 9376 11779 426 -164 589 C ATOM 678 O LEU A 84 22.961 34.813 37.765 1.00 80.16 O ANISOU 678 O LEU A 84 9696 9109 11654 451 -204 601 O ATOM 679 CB LEU A 84 22.150 31.692 37.723 1.00 74.85 C ANISOU 679 CB LEU A 84 9126 8291 11022 509 -159 540 C ATOM 680 CG LEU A 84 21.976 30.497 38.663 1.00 73.26 C ANISOU 680 CG LEU A 84 8943 7993 10899 567 -261 586 C ATOM 681 CD1 LEU A 84 22.761 29.307 38.144 1.00 73.62 C ANISOU 681 CD1 LEU A 84 8924 7900 11147 618 -158 505 C ATOM 682 CD2 LEU A 84 22.406 30.852 40.081 1.00 68.90 C ANISOU 682 CD2 LEU A 84 8332 7437 10409 620 -442 690 C ATOM 683 N PHE A 85 21.339 34.475 36.237 1.00 83.91 N ANISOU 683 N PHE A 85 10340 9677 11863 349 -58 568 N ATOM 684 CA PHE A 85 21.655 35.705 35.517 1.00 79.43 C ANISOU 684 CA PHE A 85 9744 9171 11266 292 4 582 C ATOM 685 C PHE A 85 21.380 36.930 36.380 1.00 84.08 C ANISOU 685 C PHE A 85 10337 9778 11832 304 -121 661 C ATOM 686 O PHE A 85 22.146 37.902 36.355 1.00 92.49 O ANISOU 686 O PHE A 85 11332 10834 12976 290 -120 674 O ATOM 687 CB PHE A 85 20.854 35.778 34.216 1.00 81.88 C ANISOU 687 CB PHE A 85 10140 9572 11398 197 112 573 C ATOM 688 CG PHE A 85 21.505 35.075 33.058 1.00 90.61 C ANISOU 688 CG PHE A 85 11222 10679 12527 151 285 470 C ATOM 689 CD1 PHE A 85 21.496 33.693 32.973 1.00 94.91 C ANISOU 689 CD1 PHE A 85 11789 11162 13113 175 336 378 C ATOM 690 CD2 PHE A 85 22.114 35.798 32.046 1.00 97.09 C ANISOU 690 CD2 PHE A 85 12001 11560 13327 78 405 460 C ATOM 691 CE1 PHE A 85 22.090 33.045 31.908 1.00 94.94 C ANISOU 691 CE1 PHE A 85 11773 11158 13140 134 515 254 C ATOM 692 CE2 PHE A 85 22.709 35.155 30.977 1.00 99.62 C ANISOU 692 CE2 PHE A 85 12302 11897 13652 28 585 348 C ATOM 693 CZ PHE A 85 22.696 33.776 30.908 1.00 97.85 C ANISOU 693 CZ PHE A 85 12100 11606 13471 60 645 233 C ATOM 694 N MET A 86 20.290 36.906 37.151 1.00 76.84 N ANISOU 694 N MET A 86 9501 8884 10812 325 -222 706 N ATOM 695 CA MET A 86 20.014 38.007 38.068 1.00 70.35 C ANISOU 695 CA MET A 86 8687 8068 9974 344 -329 754 C ATOM 696 C MET A 86 21.043 38.075 39.188 1.00 78.90 C ANISOU 696 C MET A 86 9693 9091 11194 390 -426 740 C ATOM 697 O MET A 86 21.352 39.167 39.680 1.00 94.92 O ANISOU 697 O MET A 86 11699 11109 13257 383 -484 748 O ATOM 698 CB MET A 86 18.610 37.864 38.658 1.00 66.32 C ANISOU 698 CB MET A 86 8270 7606 9323 357 -393 793 C ATOM 699 CG MET A 86 17.486 37.916 37.634 1.00 79.93 C ANISOU 699 CG MET A 86 10057 9403 10910 305 -326 826 C ATOM 700 SD MET A 86 15.886 37.435 38.318 1.00 85.41 S ANISOU 700 SD MET A 86 10829 10159 11464 318 -391 869 S ATOM 701 CE MET A 86 15.733 38.573 39.694 1.00 88.80 C ANISOU 701 CE MET A 86 11252 10576 11913 377 -487 883 C ATOM 702 N VAL A 87 21.588 36.930 39.598 1.00 74.08 N ANISOU 702 N VAL A 87 9041 8436 10669 432 -454 723 N ATOM 703 CA VAL A 87 22.506 36.909 40.732 1.00 78.70 C ANISOU 703 CA VAL A 87 9548 8979 11375 471 -576 733 C ATOM 704 C VAL A 87 23.869 37.460 40.331 1.00 87.36 C ANISOU 704 C VAL A 87 10512 10043 12639 458 -539 707 C ATOM 705 O VAL A 87 24.434 38.321 41.016 1.00 84.89 O ANISOU 705 O VAL A 87 10150 9725 12378 444 -631 715 O ATOM 706 CB VAL A 87 22.618 35.485 41.305 1.00 75.23 C ANISOU 706 CB VAL A 87 9099 8494 10992 523 -632 753 C ATOM 707 CG1 VAL A 87 23.859 35.355 42.175 1.00 91.83 C ANISOU 707 CG1 VAL A 87 11080 10550 13262 561 -747 778 C ATOM 708 CG2 VAL A 87 21.375 35.147 42.108 1.00 69.59 C ANISOU 708 CG2 VAL A 87 8504 7824 10114 522 -711 799 C ATOM 709 N PHE A 88 24.416 36.978 39.218 1.00 88.79 N ANISOU 709 N PHE A 88 10632 10203 12901 453 -398 667 N ATOM 710 CA PHE A 88 25.769 37.360 38.835 1.00 88.90 C ANISOU 710 CA PHE A 88 10497 10191 13090 442 -345 642 C ATOM 711 C PHE A 88 25.799 38.573 37.915 1.00 95.84 C ANISOU 711 C PHE A 88 11381 11113 13921 359 -248 642 C ATOM 712 O PHE A 88 26.694 39.416 38.034 1.00106.31 O ANISOU 712 O PHE A 88 12609 12426 15358 327 -268 649 O ATOM 713 CB PHE A 88 26.477 36.177 38.172 1.00 82.85 C ANISOU 713 CB PHE A 88 9639 9376 12463 486 -227 589 C ATOM 714 CG PHE A 88 26.727 35.030 39.106 1.00 89.58 C ANISOU 714 CG PHE A 88 10450 10156 13430 574 -335 611 C ATOM 715 CD1 PHE A 88 27.733 35.104 40.055 1.00 92.43 C ANISOU 715 CD1 PHE A 88 10677 10485 13959 613 -471 656 C ATOM 716 CD2 PHE A 88 25.958 33.880 39.039 1.00 95.01 C ANISOU 716 CD2 PHE A 88 11232 10808 14061 607 -313 601 C ATOM 717 CE1 PHE A 88 27.969 34.053 40.919 1.00 94.43 C ANISOU 717 CE1 PHE A 88 10888 10672 14320 692 -588 707 C ATOM 718 CE2 PHE A 88 26.190 32.823 39.902 1.00 92.66 C ANISOU 718 CE2 PHE A 88 10897 10428 13881 684 -420 645 C ATOM 719 CZ PHE A 88 27.197 32.911 40.842 1.00 92.85 C ANISOU 719 CZ PHE A 88 10786 10423 14072 730 -560 706 C ATOM 720 N GLY A 89 24.838 38.681 36.997 1.00 95.01 N ANISOU 720 N GLY A 89 11386 11058 13656 315 -151 645 N ATOM 721 CA GLY A 89 24.790 39.837 36.122 1.00 98.48 C ANISOU 721 CA GLY A 89 11839 11538 14042 232 -73 676 C ATOM 722 C GLY A 89 24.292 41.098 36.793 1.00 93.68 C ANISOU 722 C GLY A 89 11284 10918 13393 216 -187 731 C ATOM 723 O GLY A 89 24.469 42.190 36.243 1.00101.71 O ANISOU 723 O GLY A 89 12290 11935 14419 150 -146 771 O ATOM 724 N GLY A 90 23.684 40.977 37.971 1.00 84.45 N ANISOU 724 N GLY A 90 10172 9734 12182 270 -320 734 N ATOM 725 CA GLY A 90 23.095 42.127 38.628 1.00 77.11 C ANISOU 725 CA GLY A 90 9304 8788 11208 262 -408 760 C ATOM 726 C GLY A 90 23.419 42.258 40.102 1.00 82.54 C ANISOU 726 C GLY A 90 9975 9443 11943 294 -557 729 C ATOM 727 O GLY A 90 23.920 43.299 40.537 1.00 97.18 O ANISOU 727 O GLY A 90 11801 11255 13870 259 -612 716 O ATOM 728 N PHE A 91 23.142 41.211 40.883 1.00 75.13 N ANISOU 728 N PHE A 91 9060 8525 10959 347 -626 720 N ATOM 729 CA PHE A 91 23.276 41.313 42.334 1.00 78.71 C ANISOU 729 CA PHE A 91 9522 8976 11408 362 -777 703 C ATOM 730 C PHE A 91 24.731 41.514 42.745 1.00 79.37 C ANISOU 730 C PHE A 91 9477 9025 11655 338 -851 688 C ATOM 731 O PHE A 91 25.035 42.373 43.581 1.00 88.82 O ANISOU 731 O PHE A 91 10672 10210 12866 300 -952 660 O ATOM 732 CB PHE A 91 22.694 40.070 43.012 1.00 87.35 C ANISOU 732 CB PHE A 91 10667 10107 12416 412 -833 724 C ATOM 733 CG PHE A 91 21.214 39.890 42.802 1.00 84.94 C ANISOU 733 CG PHE A 91 10479 9847 11948 425 -782 741 C ATOM 734 CD1 PHE A 91 20.431 40.921 42.307 1.00 86.61 C ANISOU 734 CD1 PHE A 91 10744 10067 12096 407 -721 739 C ATOM 735 CD2 PHE A 91 20.605 38.684 43.112 1.00 81.01 C ANISOU 735 CD2 PHE A 91 10027 9378 11376 454 -800 769 C ATOM 736 CE1 PHE A 91 19.072 40.750 42.116 1.00 78.17 C ANISOU 736 CE1 PHE A 91 9758 9049 10894 421 -682 765 C ATOM 737 CE2 PHE A 91 19.246 38.507 42.924 1.00 75.99 C ANISOU 737 CE2 PHE A 91 9482 8793 10597 455 -756 789 C ATOM 738 CZ PHE A 91 18.479 39.540 42.427 1.00 72.05 C ANISOU 738 CZ PHE A 91 9022 8316 10038 441 -698 786 C ATOM 739 N THR A 92 25.645 40.725 42.174 1.00 73.08 N ANISOU 739 N THR A 92 8564 8213 10991 356 -800 699 N ATOM 740 CA THR A 92 27.056 40.857 42.527 1.00 75.75 C ANISOU 740 CA THR A 92 8747 8526 11508 337 -870 696 C ATOM 741 C THR A 92 27.615 42.198 42.072 1.00 77.73 C ANISOU 741 C THR A 92 8950 8753 11833 255 -830 677 C ATOM 742 O THR A 92 28.406 42.823 42.789 1.00 68.58 O ANISOU 742 O THR A 92 7718 7578 10760 208 -943 665 O ATOM 743 CB THR A 92 27.868 39.714 41.918 1.00 75.15 C ANISOU 743 CB THR A 92 8543 8429 11583 387 -795 706 C ATOM 744 OG1 THR A 92 27.747 39.746 40.491 1.00 84.91 O ANISOU 744 OG1 THR A 92 9781 9667 12815 369 -599 683 O ATOM 745 CG2 THR A 92 27.376 38.373 42.436 1.00 66.58 C ANISOU 745 CG2 THR A 92 7504 7340 10455 464 -849 735 C ATOM 746 N THR A 93 27.222 42.652 40.880 1.00 78.79 N ANISOU 746 N THR A 93 9122 8883 11930 226 -678 683 N ATOM 747 CA THR A 93 27.676 43.951 40.399 1.00 76.53 C ANISOU 747 CA THR A 93 8802 8563 11713 140 -637 688 C ATOM 748 C THR A 93 27.181 45.073 41.302 1.00 77.15 C ANISOU 748 C THR A 93 8974 8602 11737 107 -750 665 C ATOM 749 O THR A 93 27.921 46.020 41.592 1.00 78.80 O ANISOU 749 O THR A 93 9125 8763 12051 34 -804 646 O ATOM 750 CB THR A 93 27.199 44.175 38.965 1.00 73.16 C ANISOU 750 CB THR A 93 8419 8152 11225 110 -464 723 C ATOM 751 OG1 THR A 93 27.595 43.064 38.153 1.00 79.27 O ANISOU 751 OG1 THR A 93 9123 8967 12029 137 -344 714 O ATOM 752 CG2 THR A 93 27.801 45.450 38.396 1.00 74.57 C ANISOU 752 CG2 THR A 93 8547 8291 11495 10 -416 752 C ATOM 753 N THR A 94 25.934 44.978 41.764 1.00 66.77 N ANISOU 753 N THR A 94 7800 7304 10267 156 -780 656 N ATOM 754 CA THR A 94 25.387 46.034 42.607 1.00 72.08 C ANISOU 754 CA THR A 94 8565 7933 10888 134 -860 611 C ATOM 755 C THR A 94 26.014 46.013 43.995 1.00 79.75 C ANISOU 755 C THR A 94 9509 8914 11879 112 -1023 552 C ATOM 756 O THR A 94 26.263 47.071 44.584 1.00 90.36 O ANISOU 756 O THR A 94 10871 10204 13258 48 -1091 493 O ATOM 757 CB THR A 94 23.869 45.904 42.688 1.00 68.34 C ANISOU 757 CB THR A 94 8228 7486 10250 196 -829 617 C ATOM 758 OG1 THR A 94 23.324 45.999 41.365 1.00 77.53 O ANISOU 758 OG1 THR A 94 9412 8653 11394 199 -698 685 O ATOM 759 CG2 THR A 94 23.283 47.015 43.547 1.00 57.69 C ANISOU 759 CG2 THR A 94 6970 6085 8866 186 -886 551 C ATOM 760 N LEU A 95 26.287 44.820 44.530 1.00 81.29 N ANISOU 760 N LEU A 95 9661 9173 12052 155 -1094 570 N ATOM 761 CA LEU A 95 27.030 44.731 45.783 1.00 80.16 C ANISOU 761 CA LEU A 95 9471 9057 11930 119 -1267 542 C ATOM 762 C LEU A 95 28.382 45.422 45.661 1.00 83.62 C ANISOU 762 C LEU A 95 9768 9454 12552 35 -1310 531 C ATOM 763 O LEU A 95 28.823 46.113 46.586 1.00 81.38 O ANISOU 763 O LEU A 95 9483 9164 12276 -43 -1441 475 O ATOM 764 CB LEU A 95 27.205 43.268 46.186 1.00 61.70 C ANISOU 764 CB LEU A 95 7087 6781 9577 183 -1332 602 C ATOM 765 CG LEU A 95 28.268 42.982 47.248 1.00 61.20 C ANISOU 765 CG LEU A 95 6920 6752 9582 147 -1521 619 C ATOM 766 CD1 LEU A 95 27.907 43.623 48.583 1.00 63.88 C ANISOU 766 CD1 LEU A 95 7370 7136 9766 81 -1664 556 C ATOM 767 CD2 LEU A 95 28.480 41.486 47.403 1.00 61.32 C ANISOU 767 CD2 LEU A 95 6869 6797 9632 226 -1565 708 C ATOM 768 N TYR A 96 29.041 45.264 44.514 1.00 77.22 N ANISOU 768 N TYR A 96 8837 8620 11883 36 -1193 576 N ATOM 769 CA TYR A 96 30.340 45.893 44.312 1.00 72.57 C ANISOU 769 CA TYR A 96 8093 8000 11482 -51 -1214 576 C ATOM 770 C TYR A 96 30.204 47.407 44.187 1.00 75.65 C ANISOU 770 C TYR A 96 8548 8309 11886 -147 -1195 531 C ATOM 771 O TYR A 96 30.897 48.160 44.879 1.00 76.32 O ANISOU 771 O TYR A 96 8589 8365 12043 -242 -1313 485 O ATOM 772 CB TYR A 96 31.013 45.293 43.077 1.00 61.49 C ANISOU 772 CB TYR A 96 6546 6603 10215 -25 -1064 629 C ATOM 773 CG TYR A 96 32.449 45.716 42.885 1.00 70.86 C ANISOU 773 CG TYR A 96 7531 7778 11614 -107 -1078 639 C ATOM 774 CD1 TYR A 96 33.453 45.227 43.709 1.00 73.50 C ANISOU 774 CD1 TYR A 96 7710 8146 12071 -109 -1230 652 C ATOM 775 CD2 TYR A 96 32.803 46.595 41.871 1.00 69.39 C ANISOU 775 CD2 TYR A 96 7301 7553 11511 -190 -944 652 C ATOM 776 CE1 TYR A 96 34.768 45.609 43.534 1.00 75.19 C ANISOU 776 CE1 TYR A 96 7717 8357 12494 -187 -1246 668 C ATOM 777 CE2 TYR A 96 34.114 46.980 41.685 1.00 68.35 C ANISOU 777 CE2 TYR A 96 6973 7418 11579 -275 -948 666 C ATOM 778 CZ TYR A 96 35.093 46.486 42.521 1.00 79.59 C ANISOU 778 CZ TYR A 96 8232 8877 13131 -272 -1098 669 C ATOM 779 OH TYR A 96 36.403 46.867 42.344 1.00 90.83 O ANISOU 779 OH TYR A 96 9438 10306 14768 -361 -1106 688 O ATOM 780 N THR A 97 29.295 47.872 43.324 1.00 73.22 N ANISOU 780 N THR A 97 8347 7959 11513 -129 -1057 548 N ATOM 781 CA THR A 97 29.154 49.309 43.097 1.00 62.80 C ANISOU 781 CA THR A 97 7085 6537 10240 -211 -1029 527 C ATOM 782 C THR A 97 28.650 50.032 44.341 1.00 58.75 C ANISOU 782 C THR A 97 6694 5977 9652 -234 -1153 425 C ATOM 783 O THR A 97 29.105 51.140 44.646 1.00 80.98 O ANISOU 783 O THR A 97 9508 8701 12560 -333 -1204 371 O ATOM 784 CB THR A 97 28.218 49.569 41.918 1.00 65.66 C ANISOU 784 CB THR A 97 7532 6871 10545 -177 -871 594 C ATOM 785 OG1 THR A 97 26.933 48.994 42.190 1.00 68.72 O ANISOU 785 OG1 THR A 97 8047 7302 10761 -76 -865 585 O ATOM 786 CG2 THR A 97 28.786 48.960 40.645 1.00 66.30 C ANISOU 786 CG2 THR A 97 7502 7007 10683 -183 -735 675 C ATOM 787 N SER A 98 27.705 49.429 45.070 1.00 64.84 N ANISOU 787 N SER A 98 7574 6808 10255 -152 -1194 390 N ATOM 788 CA SER A 98 27.195 50.068 46.280 1.00 72.54 C ANISOU 788 CA SER A 98 8669 7756 11137 -176 -1290 274 C ATOM 789 C SER A 98 28.296 50.276 47.311 1.00 70.71 C ANISOU 789 C SER A 98 8370 7544 10954 -281 -1459 205 C ATOM 790 O SER A 98 28.245 51.237 48.088 1.00 81.29 O ANISOU 790 O SER A 98 9788 8821 12277 -357 -1526 88 O ATOM 791 CB SER A 98 26.056 49.242 46.878 1.00 76.25 C ANISOU 791 CB SER A 98 9248 8315 11407 -79 -1295 261 C ATOM 792 OG SER A 98 26.459 47.903 47.102 1.00 85.20 O ANISOU 792 OG SER A 98 10308 9560 12502 -42 -1356 324 O ATOM 793 N LEU A 99 29.298 49.395 47.334 1.00 75.61 N ANISOU 793 N LEU A 99 8842 8246 11642 -290 -1530 271 N ATOM 794 CA LEU A 99 30.434 49.581 48.227 1.00 80.70 C ANISOU 794 CA LEU A 99 9391 8921 12352 -400 -1707 231 C ATOM 795 C LEU A 99 31.312 50.752 47.804 1.00 84.47 C ANISOU 795 C LEU A 99 9787 9293 13017 -525 -1699 204 C ATOM 796 O LEU A 99 32.081 51.264 48.624 1.00 63.35 O ANISOU 796 O LEU A 99 7069 6619 10383 -647 -1850 137 O ATOM 797 CB LEU A 99 31.258 48.296 48.299 1.00 84.00 C ANISOU 797 CB LEU A 99 9646 9443 12826 -358 -1784 332 C ATOM 798 CG LEU A 99 30.564 47.139 49.021 1.00 82.75 C ANISOU 798 CG LEU A 99 9565 9386 12491 -266 -1848 363 C ATOM 799 CD1 LEU A 99 31.342 45.844 48.868 1.00 82.08 C ANISOU 799 CD1 LEU A 99 9311 9364 12512 -203 -1895 481 C ATOM 800 CD2 LEU A 99 30.374 47.476 50.485 1.00 72.43 C ANISOU 800 CD2 LEU A 99 8364 8137 11017 -345 -2020 274 C ATOM 801 N HIS A 100 31.216 51.180 46.545 1.00 93.76 N ANISOU 801 N HIS A 100 10940 10386 14298 -513 -1533 263 N ATOM 802 CA HIS A 100 31.892 52.385 46.085 1.00 94.29 C ANISOU 802 CA HIS A 100 10954 10336 14537 -639 -1507 251 C ATOM 803 C HIS A 100 31.061 53.643 46.288 1.00 96.88 C ANISOU 803 C HIS A 100 11456 10518 14835 -674 -1478 158 C ATOM 804 O HIS A 100 31.631 54.735 46.393 1.00103.99 O ANISOU 804 O HIS A 100 12342 11305 15865 -804 -1517 105 O ATOM 805 CB HIS A 100 32.244 52.266 44.599 1.00 88.71 C ANISOU 805 CB HIS A 100 10136 9616 13955 -626 -1337 376 C ATOM 806 CG HIS A 100 33.233 51.186 44.292 1.00 89.20 C ANISOU 806 CG HIS A 100 9997 9791 14104 -602 -1337 449 C ATOM 807 ND1 HIS A 100 34.595 51.392 44.331 1.00 94.62 N ANISOU 807 ND1 HIS A 100 10488 10489 14975 -711 -1400 465 N ATOM 808 CD2 HIS A 100 33.059 49.895 43.924 1.00 93.73 C ANISOU 808 CD2 HIS A 100 10528 10459 14626 -480 -1274 507 C ATOM 809 CE1 HIS A 100 35.217 50.272 44.010 1.00 97.49 C ANISOU 809 CE1 HIS A 100 10687 10951 15405 -643 -1372 531 C ATOM 810 NE2 HIS A 100 34.308 49.348 43.760 1.00101.71 N ANISOU 810 NE2 HIS A 100 11318 11528 15800 -503 -1294 552 N ATOM 811 N GLY A 101 29.737 53.517 46.344 1.00 88.65 N ANISOU 811 N GLY A 101 10570 9469 13645 -561 -1409 136 N ATOM 812 CA GLY A 101 28.859 54.662 46.413 1.00 91.04 C ANISOU 812 CA GLY A 101 11023 9620 13948 -562 -1356 60 C ATOM 813 C GLY A 101 28.333 55.141 45.077 1.00 86.06 C ANISOU 813 C GLY A 101 10408 8891 13401 -520 -1195 178 C ATOM 814 O GLY A 101 27.541 56.092 45.048 1.00 87.56 O ANISOU 814 O GLY A 101 10713 8938 13620 -503 -1146 139 O ATOM 815 N TYR A 102 28.742 54.517 43.976 1.00 76.86 N ANISOU 815 N TYR A 102 9131 7797 12275 -505 -1112 321 N ATOM 816 CA TYR A 102 28.313 54.909 42.637 1.00 72.14 C ANISOU 816 CA TYR A 102 8544 7137 11730 -488 -967 454 C ATOM 817 C TYR A 102 28.668 53.778 41.678 1.00 72.21 C ANISOU 817 C TYR A 102 8444 7291 11701 -453 -881 569 C ATOM 818 O TYR A 102 29.302 52.789 42.058 1.00 79.05 O ANISOU 818 O TYR A 102 9217 8275 12545 -438 -933 545 O ATOM 819 CB TYR A 102 28.951 56.230 42.204 1.00 63.19 C ANISOU 819 CB TYR A 102 7381 5837 10790 -622 -951 483 C ATOM 820 CG TYR A 102 30.446 56.156 41.975 1.00 77.49 C ANISOU 820 CG TYR A 102 9019 7691 12734 -750 -977 514 C ATOM 821 CD1 TYR A 102 31.331 56.100 43.045 1.00 73.13 C ANISOU 821 CD1 TYR A 102 8397 7166 12224 -827 -1122 401 C ATOM 822 CD2 TYR A 102 30.973 56.158 40.690 1.00 82.40 C ANISOU 822 CD2 TYR A 102 9537 8335 13435 -804 -856 660 C ATOM 823 CE1 TYR A 102 32.695 56.039 42.842 1.00 77.12 C ANISOU 823 CE1 TYR A 102 8719 7714 12871 -943 -1150 438 C ATOM 824 CE2 TYR A 102 32.338 56.096 40.477 1.00 72.19 C ANISOU 824 CE2 TYR A 102 8067 7088 12276 -920 -862 686 C ATOM 825 CZ TYR A 102 33.194 56.038 41.557 1.00 77.24 C ANISOU 825 CZ TYR A 102 8623 7747 12980 -984 -1012 577 C ATOM 826 OH TYR A 102 34.554 55.977 41.354 1.00 76.00 O ANISOU 826 OH TYR A 102 8263 7639 12974 -1098 -1023 610 O ATOM 827 N PHE A 103 28.257 53.939 40.422 1.00 69.51 N ANISOU 827 N PHE A 103 8115 6938 11359 -444 -750 696 N ATOM 828 CA PHE A 103 28.448 52.915 39.397 1.00 75.94 C ANISOU 828 CA PHE A 103 8852 7887 12114 -417 -640 788 C ATOM 829 C PHE A 103 29.820 53.122 38.766 1.00 75.90 C ANISOU 829 C PHE A 103 8689 7891 12260 -539 -590 838 C ATOM 830 O PHE A 103 30.009 54.009 37.930 1.00 92.21 O ANISOU 830 O PHE A 103 10745 9885 14405 -631 -516 931 O ATOM 831 CB PHE A 103 27.332 52.980 38.361 1.00 74.27 C ANISOU 831 CB PHE A 103 8734 7684 11800 -368 -532 899 C ATOM 832 CG PHE A 103 27.220 51.746 37.519 1.00 80.86 C ANISOU 832 CG PHE A 103 9534 8673 12517 -323 -432 950 C ATOM 833 CD1 PHE A 103 26.424 50.688 37.924 1.00 78.87 C ANISOU 833 CD1 PHE A 103 9340 8506 12121 -211 -454 904 C ATOM 834 CD2 PHE A 103 27.916 51.639 36.328 1.00 87.92 C ANISOU 834 CD2 PHE A 103 10340 9625 13441 -403 -308 1036 C ATOM 835 CE1 PHE A 103 26.321 49.547 37.156 1.00 81.91 C ANISOU 835 CE1 PHE A 103 9702 9014 12407 -178 -361 934 C ATOM 836 CE2 PHE A 103 27.818 50.500 35.555 1.00 88.13 C ANISOU 836 CE2 PHE A 103 10345 9787 13355 -369 -204 1054 C ATOM 837 CZ PHE A 103 27.018 49.452 35.969 1.00 82.81 C ANISOU 837 CZ PHE A 103 9735 9179 12551 -255 -234 999 C ATOM 838 N VAL A 104 30.783 52.288 39.160 1.00 73.35 N ANISOU 838 N VAL A 104 8229 7658 11984 -540 -630 788 N ATOM 839 CA VAL A 104 32.170 52.516 38.770 1.00 78.38 C ANISOU 839 CA VAL A 104 8685 8303 12791 -656 -597 818 C ATOM 840 C VAL A 104 32.485 52.036 37.360 1.00 83.04 C ANISOU 840 C VAL A 104 9192 8984 13375 -674 -408 913 C ATOM 841 O VAL A 104 33.484 52.474 36.777 1.00 93.61 O ANISOU 841 O VAL A 104 10398 10323 14848 -791 -337 962 O ATOM 842 CB VAL A 104 33.127 51.839 39.763 1.00 68.65 C ANISOU 842 CB VAL A 104 7313 7131 11638 -648 -724 739 C ATOM 843 CG1 VAL A 104 33.080 52.549 41.100 1.00 66.59 C ANISOU 843 CG1 VAL A 104 7120 6789 11394 -690 -912 642 C ATOM 844 CG2 VAL A 104 32.770 50.368 39.922 1.00 71.99 C ANISOU 844 CG2 VAL A 104 7734 7668 11951 -505 -718 720 C ATOM 845 N PHE A 105 31.670 51.151 36.793 1.00 82.12 N ANISOU 845 N PHE A 105 9151 8952 13101 -576 -318 933 N ATOM 846 CA PHE A 105 31.996 50.558 35.502 1.00 82.79 C ANISOU 846 CA PHE A 105 9162 9141 13154 -598 -131 992 C ATOM 847 C PHE A 105 31.606 51.439 34.322 1.00 93.54 C ANISOU 847 C PHE A 105 10596 10484 14461 -694 -14 1116 C ATOM 848 O PHE A 105 31.813 51.034 33.173 1.00 95.94 O ANISOU 848 O PHE A 105 10859 10890 14704 -736 151 1168 O ATOM 849 CB PHE A 105 31.335 49.184 35.377 1.00 79.26 C ANISOU 849 CB PHE A 105 8765 8790 12560 -469 -87 949 C ATOM 850 CG PHE A 105 31.707 48.233 36.482 1.00 82.23 C ANISOU 850 CG PHE A 105 9069 9182 12992 -372 -202 856 C ATOM 851 CD1 PHE A 105 33.020 47.813 36.643 1.00 77.22 C ANISOU 851 CD1 PHE A 105 8232 8577 12532 -389 -198 825 C ATOM 852 CD2 PHE A 105 30.744 47.757 37.358 1.00 77.23 C ANISOU 852 CD2 PHE A 105 8561 8541 12243 -269 -317 813 C ATOM 853 CE1 PHE A 105 33.365 46.937 37.660 1.00 71.74 C ANISOU 853 CE1 PHE A 105 7465 7896 11899 -300 -324 768 C ATOM 854 CE2 PHE A 105 31.083 46.880 38.375 1.00 78.86 C ANISOU 854 CE2 PHE A 105 8706 8766 12490 -192 -433 753 C ATOM 855 CZ PHE A 105 32.394 46.470 38.525 1.00 71.08 C ANISOU 855 CZ PHE A 105 7522 7803 11683 -206 -445 737 C ATOM 856 N GLY A 106 31.055 52.623 34.573 1.00 93.31 N ANISOU 856 N GLY A 106 10673 10326 14453 -734 -93 1167 N ATOM 857 CA GLY A 106 30.794 53.579 33.525 1.00 94.98 C ANISOU 857 CA GLY A 106 10940 10498 14651 -837 -8 1314 C ATOM 858 C GLY A 106 29.615 53.212 32.649 1.00 97.61 C ANISOU 858 C GLY A 106 11399 10908 14779 -786 67 1399 C ATOM 859 O GLY A 106 28.918 52.217 32.876 1.00 97.71 O ANISOU 859 O GLY A 106 11467 10998 14660 -669 54 1332 O ATOM 860 N PRO A 107 29.375 54.027 31.618 1.00 92.88 N ANISOU 860 N PRO A 107 10847 10291 14151 -887 138 1561 N ATOM 861 CA PRO A 107 28.213 53.783 30.744 1.00 90.53 C ANISOU 861 CA PRO A 107 10670 10076 13653 -857 187 1667 C ATOM 862 C PRO A 107 28.238 52.437 30.038 1.00 94.20 C ANISOU 862 C PRO A 107 11110 10738 13942 -838 312 1618 C ATOM 863 O PRO A 107 27.174 51.835 29.841 1.00111.66 O ANISOU 863 O PRO A 107 13422 13020 15985 -763 301 1622 O ATOM 864 CB PRO A 107 28.276 54.955 29.751 1.00 88.75 C ANISOU 864 CB PRO A 107 10465 9800 13456 -1003 238 1871 C ATOM 865 CG PRO A 107 29.671 55.511 29.873 1.00 81.47 C ANISOU 865 CG PRO A 107 9410 8820 12727 -1126 271 1856 C ATOM 866 CD PRO A 107 30.069 55.281 31.290 1.00 73.46 C ANISOU 866 CD PRO A 107 8342 7723 11847 -1037 152 1670 C ATOM 867 N THR A 108 29.415 51.941 29.647 1.00 94.67 N ANISOU 867 N THR A 108 11037 10888 14047 -906 435 1564 N ATOM 868 CA THR A 108 29.479 50.635 28.992 1.00100.90 C ANISOU 868 CA THR A 108 11803 11844 14690 -882 571 1488 C ATOM 869 C THR A 108 29.071 49.521 29.949 1.00 97.92 C ANISOU 869 C THR A 108 11443 11465 14297 -719 488 1336 C ATOM 870 O THR A 108 28.208 48.695 29.625 1.00 96.66 O ANISOU 870 O THR A 108 11374 11386 13964 -663 513 1312 O ATOM 871 CB THR A 108 30.881 50.384 28.435 1.00 99.56 C ANISOU 871 CB THR A 108 11464 11754 14608 -978 735 1449 C ATOM 872 OG1 THR A 108 31.859 50.940 29.323 1.00118.46 O ANISOU 872 OG1 THR A 108 13728 14037 17245 -990 653 1413 O ATOM 873 CG2 THR A 108 31.026 51.012 27.054 1.00 93.42 C ANISOU 873 CG2 THR A 108 10704 11068 13725 -1152 883 1602 C ATOM 874 N GLY A 109 29.677 49.486 31.138 1.00 90.97 N ANISOU 874 N GLY A 109 10478 10496 13592 -654 380 1241 N ATOM 875 CA GLY A 109 29.247 48.556 32.167 1.00 80.06 C ANISOU 875 CA GLY A 109 9123 9100 12195 -510 275 1126 C ATOM 876 C GLY A 109 27.809 48.744 32.595 1.00 88.98 C ANISOU 876 C GLY A 109 10418 10190 13200 -435 163 1156 C ATOM 877 O GLY A 109 27.185 47.791 33.073 1.00 97.20 O ANISOU 877 O GLY A 109 11510 11264 14158 -331 120 1085 O ATOM 878 N CYS A 110 27.266 49.954 32.434 1.00 90.99 N ANISOU 878 N CYS A 110 10750 10368 13456 -484 119 1265 N ATOM 879 CA CYS A 110 25.854 50.188 32.719 1.00 90.65 C ANISOU 879 CA CYS A 110 10844 10289 13309 -409 33 1305 C ATOM 880 C CYS A 110 24.967 49.454 31.724 1.00 94.28 C ANISOU 880 C CYS A 110 11378 10881 13562 -405 113 1360 C ATOM 881 O CYS A 110 23.944 48.873 32.105 1.00 89.27 O ANISOU 881 O CYS A 110 10821 10274 12825 -313 56 1329 O ATOM 882 CB CYS A 110 25.568 51.691 32.698 1.00 94.22 C ANISOU 882 CB CYS A 110 11344 10607 13851 -460 -21 1416 C ATOM 883 SG CYS A 110 23.891 52.209 33.153 1.00 98.83 S ANISOU 883 SG CYS A 110 12065 11111 14374 -353 -126 1465 S ATOM 884 N ASN A 111 25.341 49.470 30.443 1.00 96.52 N ANISOU 884 N ASN A 111 11640 11258 13774 -519 244 1440 N ATOM 885 CA ASN A 111 24.593 48.705 29.452 1.00 94.62 C ANISOU 885 CA ASN A 111 11471 11163 13316 -541 323 1474 C ATOM 886 C ASN A 111 24.752 47.209 29.681 1.00 93.82 C ANISOU 886 C ASN A 111 11347 11136 13163 -471 372 1314 C ATOM 887 O ASN A 111 23.802 46.443 29.485 1.00 92.19 O ANISOU 887 O ASN A 111 11224 11003 12803 -434 365 1297 O ATOM 888 CB ASN A 111 25.044 49.087 28.044 1.00 88.91 C ANISOU 888 CB ASN A 111 10735 10537 12509 -699 460 1589 C ATOM 889 CG ASN A 111 24.608 50.482 27.657 1.00 86.62 C ANISOU 889 CG ASN A 111 10494 10178 12240 -770 402 1791 C ATOM 890 OD1 ASN A 111 23.440 50.714 27.344 1.00 83.95 O ANISOU 890 OD1 ASN A 111 10250 9860 11787 -756 336 1905 O ATOM 891 ND2 ASN A 111 25.544 51.422 27.675 1.00 89.43 N ANISOU 891 ND2 ASN A 111 10777 10444 12758 -850 420 1844 N ATOM 892 N LEU A 112 25.943 46.776 30.098 1.00 94.93 N ANISOU 892 N LEU A 112 11368 11252 13447 -454 415 1203 N ATOM 893 CA LEU A 112 26.168 45.363 30.387 1.00 85.16 C ANISOU 893 CA LEU A 112 10097 10053 12208 -374 454 1059 C ATOM 894 C LEU A 112 25.327 44.906 31.572 1.00 80.61 C ANISOU 894 C LEU A 112 9584 9418 11624 -247 302 1012 C ATOM 895 O LEU A 112 24.502 43.992 31.453 1.00 76.72 O ANISOU 895 O LEU A 112 9170 8980 11002 -205 306 977 O ATOM 896 CB LEU A 112 27.654 45.116 30.652 1.00 89.33 C ANISOU 896 CB LEU A 112 10457 10552 12931 -373 515 974 C ATOM 897 CG LEU A 112 28.524 44.689 29.471 1.00 90.91 C ANISOU 897 CG LEU A 112 10572 10851 13118 -460 729 936 C ATOM 898 CD1 LEU A 112 29.976 44.586 29.903 1.00 88.66 C ANISOU 898 CD1 LEU A 112 10092 10523 13070 -444 764 867 C ATOM 899 CD2 LEU A 112 28.037 43.364 28.909 1.00 90.11 C ANISOU 899 CD2 LEU A 112 10534 10831 12872 -427 830 838 C ATOM 900 N GLU A 113 25.527 45.537 32.733 1.00 73.58 N ANISOU 900 N GLU A 113 8665 8424 10867 -197 167 1007 N ATOM 901 CA GLU A 113 24.762 45.167 33.919 1.00 69.96 C ANISOU 901 CA GLU A 113 8269 7925 10389 -89 30 963 C ATOM 902 C GLU A 113 23.268 45.377 33.708 1.00 79.41 C ANISOU 902 C GLU A 113 9597 9149 11425 -72 -5 1032 C ATOM 903 O GLU A 113 22.453 44.653 34.289 1.00 90.90 O ANISOU 903 O GLU A 113 11111 10623 12804 3 -64 995 O ATOM 904 CB GLU A 113 25.256 45.964 35.128 1.00 71.24 C ANISOU 904 CB GLU A 113 8388 7983 10697 -68 -100 940 C ATOM 905 CG GLU A 113 24.692 45.505 36.468 1.00 83.32 C ANISOU 905 CG GLU A 113 9967 9488 12203 30 -234 878 C ATOM 906 CD GLU A 113 23.383 46.185 36.819 1.00 95.79 C ANISOU 906 CD GLU A 113 11667 11041 13689 61 -298 916 C ATOM 907 OE1 GLU A 113 23.057 47.209 36.185 1.00102.64 O ANISOU 907 OE1 GLU A 113 12566 11875 14558 13 -266 996 O ATOM 908 OE2 GLU A 113 22.680 45.694 37.727 1.00105.37 O ANISOU 908 OE2 GLU A 113 12937 12264 14835 135 -376 874 O ATOM 909 N GLY A 114 22.889 46.351 32.878 1.00 79.98 N ANISOU 909 N GLY A 114 9707 9227 11454 -144 27 1148 N ATOM 910 CA GLY A 114 21.481 46.556 32.589 1.00 81.59 C ANISOU 910 CA GLY A 114 10012 9466 11523 -128 -11 1234 C ATOM 911 C GLY A 114 20.903 45.534 31.636 1.00 83.21 C ANISOU 911 C GLY A 114 10264 9805 11546 -162 66 1240 C ATOM 912 O GLY A 114 19.734 45.157 31.767 1.00 79.35 O ANISOU 912 O GLY A 114 9843 9359 10948 -119 13 1260 O ATOM 913 N PHE A 115 21.700 45.071 30.671 1.00 86.63 N ANISOU 913 N PHE A 115 10661 10313 11943 -247 196 1215 N ATOM 914 CA PHE A 115 21.215 44.072 29.724 1.00 84.00 C ANISOU 914 CA PHE A 115 10382 10107 11425 -298 280 1192 C ATOM 915 C PHE A 115 20.994 42.728 30.409 1.00 85.28 C ANISOU 915 C PHE A 115 10557 10263 11582 -211 261 1059 C ATOM 916 O PHE A 115 19.959 42.083 30.210 1.00 93.32 O ANISOU 916 O PHE A 115 11653 11346 12459 -211 239 1060 O ATOM 917 CB PHE A 115 22.199 43.933 28.561 1.00 84.69 C ANISOU 917 CB PHE A 115 10427 10274 11478 -415 447 1172 C ATOM 918 CG PHE A 115 21.881 42.803 27.625 1.00 90.30 C ANISOU 918 CG PHE A 115 11195 11111 12005 -477 556 1099 C ATOM 919 CD1 PHE A 115 20.927 42.955 26.633 1.00 95.11 C ANISOU 919 CD1 PHE A 115 11898 11843 12395 -578 559 1201 C ATOM 920 CD2 PHE A 115 22.544 41.590 27.731 1.00 94.43 C ANISOU 920 CD2 PHE A 115 11676 11624 12580 -439 652 928 C ATOM 921 CE1 PHE A 115 20.636 41.916 25.768 1.00 99.52 C ANISOU 921 CE1 PHE A 115 12520 12523 12769 -656 656 1117 C ATOM 922 CE2 PHE A 115 22.257 40.548 26.870 1.00 90.61 C ANISOU 922 CE2 PHE A 115 11255 11238 11935 -502 762 837 C ATOM 923 CZ PHE A 115 21.302 40.711 25.887 1.00 90.62 C ANISOU 923 CZ PHE A 115 11362 11372 11697 -619 765 923 C ATOM 924 N PHE A 116 21.956 42.290 31.223 1.00 85.48 N ANISOU 924 N PHE A 116 10502 10210 11768 -142 258 956 N ATOM 925 CA PHE A 116 21.844 40.979 31.852 1.00 89.52 C ANISOU 925 CA PHE A 116 11020 10701 12294 -63 238 849 C ATOM 926 C PHE A 116 20.868 40.976 33.022 1.00 85.68 C ANISOU 926 C PHE A 116 10588 10175 11793 23 86 874 C ATOM 927 O PHE A 116 20.254 39.941 33.304 1.00 85.90 O ANISOU 927 O PHE A 116 10663 10217 11759 59 65 830 O ATOM 928 CB PHE A 116 23.222 40.491 32.303 1.00 79.18 C ANISOU 928 CB PHE A 116 9589 9322 11173 -17 276 755 C ATOM 929 CG PHE A 116 24.112 40.070 31.168 1.00 81.42 C ANISOU 929 CG PHE A 116 9812 9654 11469 -85 460 689 C ATOM 930 CD1 PHE A 116 23.775 38.985 30.375 1.00 83.95 C ANISOU 930 CD1 PHE A 116 10190 10031 11675 -115 571 608 C ATOM 931 CD2 PHE A 116 25.284 40.754 30.894 1.00 84.82 C ANISOU 931 CD2 PHE A 116 10128 10075 12025 -129 531 698 C ATOM 932 CE1 PHE A 116 24.588 38.592 29.327 1.00 81.38 C ANISOU 932 CE1 PHE A 116 9813 9754 11352 -181 762 523 C ATOM 933 CE2 PHE A 116 26.102 40.365 29.848 1.00 82.79 C ANISOU 933 CE2 PHE A 116 9806 9875 11776 -194 722 629 C ATOM 934 CZ PHE A 116 25.753 39.282 29.064 1.00 76.06 C ANISOU 934 CZ PHE A 116 9017 9081 10800 -217 844 535 C ATOM 935 N ALA A 117 20.708 42.107 33.713 1.00 79.58 N ANISOU 935 N ALA A 117 9811 9349 11076 50 -9 936 N ATOM 936 CA ALA A 117 19.703 42.174 34.770 1.00 86.85 C ANISOU 936 CA ALA A 117 10787 10249 11964 124 -129 950 C ATOM 937 C ALA A 117 18.296 42.168 34.187 1.00 86.76 C ANISOU 937 C ALA A 117 10855 10317 11793 101 -131 1025 C ATOM 938 O ALA A 117 17.399 41.506 34.722 1.00 68.41 O ANISOU 938 O ALA A 117 8575 8019 9398 144 -182 1011 O ATOM 939 CB ALA A 117 19.922 43.414 35.636 1.00 88.56 C ANISOU 939 CB ALA A 117 10980 10380 12286 153 -213 970 C ATOM 940 N THR A 118 18.085 42.897 33.088 1.00 89.38 N ANISOU 940 N THR A 118 11199 10694 12066 26 -84 1118 N ATOM 941 CA THR A 118 16.792 42.863 32.414 1.00 88.67 C ANISOU 941 CA THR A 118 11170 10697 11824 -9 -97 1207 C ATOM 942 C THR A 118 16.543 41.502 31.775 1.00 91.96 C ANISOU 942 C THR A 118 11626 11208 12107 -63 -37 1146 C ATOM 943 O THR A 118 15.434 40.963 31.862 1.00 98.04 O ANISOU 943 O THR A 118 12440 12035 12775 -57 -83 1163 O ATOM 944 CB THR A 118 16.716 43.977 31.367 1.00 86.68 C ANISOU 944 CB THR A 118 10918 10473 11543 -89 -74 1345 C ATOM 945 OG1 THR A 118 16.902 45.246 32.005 1.00 87.54 O ANISOU 945 OG1 THR A 118 10997 10465 11800 -38 -132 1395 O ATOM 946 CG2 THR A 118 15.367 43.967 30.659 1.00 80.77 C ANISOU 946 CG2 THR A 118 10217 9832 10639 -129 -111 1461 C ATOM 947 N LEU A 119 17.567 40.924 31.142 1.00 89.69 N ANISOU 947 N LEU A 119 11319 10932 11829 -117 73 1064 N ATOM 948 CA LEU A 119 17.411 39.610 30.525 1.00 89.51 C ANISOU 948 CA LEU A 119 11339 10975 11697 -170 147 975 C ATOM 949 C LEU A 119 17.045 38.557 31.564 1.00 91.43 C ANISOU 949 C LEU A 119 11597 11161 11979 -86 87 898 C ATOM 950 O LEU A 119 16.141 37.743 31.347 1.00 94.27 O ANISOU 950 O LEU A 119 12018 11577 12222 -119 75 884 O ATOM 951 CB LEU A 119 18.696 39.220 29.795 1.00 85.22 C ANISOU 951 CB LEU A 119 10755 10430 11196 -223 296 877 C ATOM 952 CG LEU A 119 18.632 38.012 28.861 1.00 74.63 C ANISOU 952 CG LEU A 119 9467 9159 9731 -304 412 767 C ATOM 953 CD1 LEU A 119 17.936 38.369 27.556 1.00 70.26 C ANISOU 953 CD1 LEU A 119 8986 8759 8951 -450 448 847 C ATOM 954 CD2 LEU A 119 20.032 37.490 28.602 1.00 71.21 C ANISOU 954 CD2 LEU A 119 8961 8675 9420 -298 559 633 C ATOM 955 N GLY A 120 17.733 38.565 32.708 1.00 94.02 N ANISOU 955 N GLY A 120 11870 11386 12469 12 38 857 N ATOM 956 CA GLY A 120 17.458 37.569 33.732 1.00 88.33 C ANISOU 956 CA GLY A 120 11164 10614 11784 83 -26 806 C ATOM 957 C GLY A 120 16.047 37.667 34.280 1.00 84.99 C ANISOU 957 C GLY A 120 10796 10237 11261 101 -123 877 C ATOM 958 O GLY A 120 15.360 36.656 34.449 1.00 93.35 O ANISOU 958 O GLY A 120 11899 11313 12256 93 -140 855 O ATOM 959 N GLY A 121 15.594 38.889 34.563 1.00 83.70 N ANISOU 959 N GLY A 121 10623 10085 11096 124 -181 961 N ATOM 960 CA GLY A 121 14.245 39.068 35.067 1.00 75.86 C ANISOU 960 CA GLY A 121 9660 9138 10025 150 -256 1026 C ATOM 961 C GLY A 121 13.175 38.744 34.045 1.00 74.43 C ANISOU 961 C GLY A 121 9517 9067 9694 68 -239 1083 C ATOM 962 O GLY A 121 12.098 38.259 34.403 1.00 62.82 O ANISOU 962 O GLY A 121 8068 7646 8153 72 -285 1107 O ATOM 963 N GLU A 122 13.452 39.000 32.764 1.00 77.71 N ANISOU 963 N GLU A 122 9940 9536 10049 -20 -175 1110 N ATOM 964 CA GLU A 122 12.465 38.733 31.722 1.00 81.18 C ANISOU 964 CA GLU A 122 10420 10101 10324 -121 -173 1172 C ATOM 965 C GLU A 122 12.358 37.246 31.407 1.00 81.67 C ANISOU 965 C GLU A 122 10534 10192 10303 -188 -129 1068 C ATOM 966 O GLU A 122 11.255 36.745 31.159 1.00 83.10 O ANISOU 966 O GLU A 122 10747 10458 10368 -246 -170 1101 O ATOM 967 CB GLU A 122 12.805 39.525 30.460 1.00 83.51 C ANISOU 967 CB GLU A 122 10715 10458 10557 -212 -124 1247 C ATOM 968 CG GLU A 122 12.506 41.006 30.581 1.00 89.10 C ANISOU 968 CG GLU A 122 11381 11143 11329 -167 -187 1391 C ATOM 969 CD GLU A 122 11.053 41.276 30.925 1.00 94.87 C ANISOU 969 CD GLU A 122 12097 11923 12027 -127 -287 1495 C ATOM 970 OE1 GLU A 122 10.185 41.081 30.048 1.00 95.92 O ANISOU 970 OE1 GLU A 122 12246 12181 12019 -216 -315 1581 O ATOM 971 OE2 GLU A 122 10.779 41.671 32.077 1.00 97.11 O ANISOU 971 OE2 GLU A 122 12348 12127 12423 -11 -334 1487 O ATOM 972 N ILE A 123 13.484 36.527 31.404 1.00 80.91 N ANISOU 972 N ILE A 123 10441 10019 10282 -181 -45 941 N ATOM 973 CA ILE A 123 13.431 35.081 31.203 1.00 76.59 C ANISOU 973 CA ILE A 123 9945 9458 9697 -229 2 828 C ATOM 974 C ILE A 123 12.641 34.422 32.326 1.00 72.22 C ANISOU 974 C ILE A 123 9404 8867 9172 -171 -88 840 C ATOM 975 O ILE A 123 11.798 33.551 32.084 1.00 72.69 O ANISOU 975 O ILE A 123 9514 8970 9137 -243 -101 823 O ATOM 976 CB ILE A 123 14.851 34.494 31.089 1.00 74.42 C ANISOU 976 CB ILE A 123 9648 9082 9547 -204 113 694 C ATOM 977 CG1 ILE A 123 15.574 35.066 29.870 1.00 81.38 C ANISOU 977 CG1 ILE A 123 10519 10027 10375 -286 227 677 C ATOM 978 CG2 ILE A 123 14.794 32.978 30.985 1.00 72.27 C ANISOU 978 CG2 ILE A 123 9428 8756 9276 -235 163 570 C ATOM 979 CD1 ILE A 123 17.019 34.641 29.767 1.00 78.58 C ANISOU 979 CD1 ILE A 123 10111 9580 10165 -251 350 550 C ATOM 980 N ALA A 124 12.893 34.835 33.571 1.00 68.50 N ANISOU 980 N ALA A 124 8887 8321 8820 -56 -153 869 N ATOM 981 CA ALA A 124 12.115 34.318 34.692 1.00 67.59 C ANISOU 981 CA ALA A 124 8782 8190 8709 -11 -235 896 C ATOM 982 C ALA A 124 10.650 34.718 34.574 1.00 78.97 C ANISOU 982 C ALA A 124 10228 9750 10027 -50 -292 996 C ATOM 983 O ALA A 124 9.754 33.926 34.891 1.00 89.84 O ANISOU 983 O ALA A 124 11628 11158 11347 -83 -327 1008 O ATOM 984 CB ALA A 124 12.703 34.811 36.014 1.00 64.26 C ANISOU 984 CB ALA A 124 8317 7691 8409 103 -291 906 C ATOM 985 N LEU A 125 10.390 35.946 34.119 1.00 83.39 N ANISOU 985 N LEU A 125 10754 10370 10559 -47 -304 1078 N ATOM 986 CA LEU A 125 9.021 36.402 33.896 1.00 78.25 C ANISOU 986 CA LEU A 125 10084 9832 9817 -76 -360 1188 C ATOM 987 C LEU A 125 8.301 35.494 32.906 1.00 81.94 C ANISOU 987 C LEU A 125 10592 10398 10142 -212 -355 1188 C ATOM 988 O LEU A 125 7.235 34.944 33.205 1.00 89.12 O ANISOU 988 O LEU A 125 11499 11367 10996 -243 -403 1220 O ATOM 989 CB LEU A 125 9.037 37.854 33.402 1.00 92.15 C ANISOU 989 CB LEU A 125 11800 11615 11597 -53 -371 1286 C ATOM 990 CG LEU A 125 7.751 38.650 33.135 1.00 93.07 C ANISOU 990 CG LEU A 125 11866 11827 11669 -54 -435 1429 C ATOM 991 CD1 LEU A 125 7.122 38.331 31.777 1.00 97.23 C ANISOU 991 CD1 LEU A 125 12411 12490 12043 -194 -450 1498 C ATOM 992 CD2 LEU A 125 6.746 38.446 34.253 1.00 80.32 C ANISOU 992 CD2 LEU A 125 10215 10228 10077 15 -480 1442 C ATOM 993 N TRP A 126 8.880 35.324 31.717 1.00 82.26 N ANISOU 993 N TRP A 126 10673 10465 10115 -307 -291 1143 N ATOM 994 CA TRP A 126 8.239 34.537 30.672 1.00 92.71 C ANISOU 994 CA TRP A 126 12050 11896 11280 -460 -285 1127 C ATOM 995 C TRP A 126 8.312 33.037 30.926 1.00 95.13 C ANISOU 995 C TRP A 126 12417 12135 11593 -502 -251 996 C ATOM 996 O TRP A 126 7.500 32.291 30.368 1.00101.43 O ANISOU 996 O TRP A 126 13257 13011 12271 -627 -270 982 O ATOM 997 CB TRP A 126 8.855 34.875 29.313 1.00 92.66 C ANISOU 997 CB TRP A 126 12078 11953 11177 -562 -216 1112 C ATOM 998 CG TRP A 126 8.343 36.166 28.758 1.00 94.77 C ANISOU 998 CG TRP A 126 12297 12325 11384 -579 -278 1285 C ATOM 999 CD1 TRP A 126 9.000 37.360 28.709 1.00 90.28 C ANISOU 999 CD1 TRP A 126 11690 11718 10895 -515 -264 1356 C ATOM 1000 CD2 TRP A 126 7.047 36.397 28.194 1.00101.72 C ANISOU 1000 CD2 TRP A 126 13158 13357 12136 -664 -375 1423 C ATOM 1001 NE1 TRP A 126 8.198 38.318 28.137 1.00 86.72 N ANISOU 1001 NE1 TRP A 126 11201 11371 10378 -550 -344 1536 N ATOM 1002 CE2 TRP A 126 6.993 37.751 27.813 1.00 96.79 C ANISOU 1002 CE2 TRP A 126 12480 12770 11526 -637 -418 1585 C ATOM 1003 CE3 TRP A 126 5.930 35.587 27.969 1.00 99.64 C ANISOU 1003 CE3 TRP A 126 12906 13197 11754 -767 -438 1434 C ATOM 1004 CZ2 TRP A 126 5.865 38.314 27.220 1.00 96.00 C ANISOU 1004 CZ2 TRP A 126 12332 12807 11336 -697 -525 1767 C ATOM 1005 CZ3 TRP A 126 4.812 36.147 27.380 1.00 92.10 C ANISOU 1005 CZ3 TRP A 126 11900 12396 10700 -835 -546 1607 C ATOM 1006 CH2 TRP A 126 4.787 37.497 27.012 1.00 90.83 C ANISOU 1006 CH2 TRP A 126 11679 12269 10565 -793 -591 1777 C ATOM 1007 N SER A 127 9.251 32.576 31.754 1.00 83.70 N ANISOU 1007 N SER A 127 10973 10539 10292 -406 -210 907 N ATOM 1008 CA SER A 127 9.234 31.174 32.155 1.00 82.99 C ANISOU 1008 CA SER A 127 10932 10359 10241 -429 -196 813 C ATOM 1009 C SER A 127 7.986 30.857 32.967 1.00 86.58 C ANISOU 1009 C SER A 127 11374 10856 10665 -434 -290 898 C ATOM 1010 O SER A 127 7.405 29.774 32.832 1.00 90.54 O ANISOU 1010 O SER A 127 11925 11355 11122 -529 -297 859 O ATOM 1011 CB SER A 127 10.495 30.829 32.947 1.00 74.24 C ANISOU 1011 CB SER A 127 9809 9084 9314 -313 -155 736 C ATOM 1012 OG SER A 127 11.636 30.802 32.106 1.00 72.83 O ANISOU 1012 OG SER A 127 9638 8861 9173 -327 -44 631 O ATOM 1013 N LEU A 128 7.550 31.797 33.810 1.00 82.14 N ANISOU 1013 N LEU A 128 10745 10334 10132 -340 -354 1007 N ATOM 1014 CA LEU A 128 6.323 31.587 34.570 1.00 80.59 C ANISOU 1014 CA LEU A 128 10519 10200 9901 -346 -425 1090 C ATOM 1015 C LEU A 128 5.095 31.604 33.668 1.00 84.58 C ANISOU 1015 C LEU A 128 11009 10859 10268 -472 -464 1158 C ATOM 1016 O LEU A 128 4.089 30.958 33.981 1.00 78.96 O ANISOU 1016 O LEU A 128 10287 10199 9514 -534 -507 1195 O ATOM 1017 CB LEU A 128 6.194 32.643 35.667 1.00 68.80 C ANISOU 1017 CB LEU A 128 8955 8712 8472 -213 -461 1166 C ATOM 1018 CG LEU A 128 7.265 32.625 36.760 1.00 59.21 C ANISOU 1018 CG LEU A 128 7750 7370 7376 -103 -452 1114 C ATOM 1019 CD1 LEU A 128 6.775 33.380 37.985 1.00 64.06 C ANISOU 1019 CD1 LEU A 128 8314 8016 8010 -10 -492 1175 C ATOM 1020 CD2 LEU A 128 7.664 31.201 37.123 1.00 57.39 C ANISOU 1020 CD2 LEU A 128 7579 7039 7188 -135 -444 1052 C ATOM 1021 N VAL A 129 5.155 32.332 32.552 1.00 86.34 N ANISOU 1021 N VAL A 129 11223 11164 10417 -520 -457 1188 N ATOM 1022 CA VAL A 129 4.055 32.310 31.592 1.00 82.40 C ANISOU 1022 CA VAL A 129 10710 10825 9774 -658 -512 1262 C ATOM 1023 C VAL A 129 4.033 30.984 30.845 1.00 81.92 C ANISOU 1023 C VAL A 129 10744 10764 9618 -823 -483 1146 C ATOM 1024 O VAL A 129 2.989 30.329 30.737 1.00 77.81 O ANISOU 1024 O VAL A 129 10220 10322 9021 -935 -539 1173 O ATOM 1025 CB VAL A 129 4.165 33.501 30.624 1.00 79.80 C ANISOU 1025 CB VAL A 129 10349 10585 9386 -669 -525 1351 C ATOM 1026 CG1 VAL A 129 3.245 33.306 29.427 1.00 77.76 C ANISOU 1026 CG1 VAL A 129 10096 10499 8951 -846 -586 1416 C ATOM 1027 CG2 VAL A 129 3.833 34.788 31.346 1.00 81.14 C ANISOU 1027 CG2 VAL A 129 10416 10756 9659 -521 -570 1480 C ATOM 1028 N VAL A 130 5.188 30.568 30.322 1.00 80.71 N ANISOU 1028 N VAL A 130 10672 10518 9477 -843 -388 1007 N ATOM 1029 CA VAL A 130 5.264 29.323 29.563 1.00 81.00 C ANISOU 1029 CA VAL A 130 10808 10531 9435 -996 -336 863 C ATOM 1030 C VAL A 130 4.890 28.136 30.442 1.00 82.59 C ANISOU 1030 C VAL A 130 11037 10625 9721 -1001 -354 818 C ATOM 1031 O VAL A 130 4.200 27.210 29.998 1.00 84.80 O ANISOU 1031 O VAL A 130 11370 10935 9917 -1155 -373 769 O ATOM 1032 CB VAL A 130 6.668 29.167 28.948 1.00 76.53 C ANISOU 1032 CB VAL A 130 10306 9870 8903 -986 -205 710 C ATOM 1033 CG1 VAL A 130 6.871 27.760 28.412 1.00 70.67 C ANISOU 1033 CG1 VAL A 130 9669 9046 8136 -1108 -126 524 C ATOM 1034 CG2 VAL A 130 6.866 30.191 27.841 1.00 80.52 C ANISOU 1034 CG2 VAL A 130 10803 10517 9275 -1044 -187 762 C ATOM 1035 N LEU A 131 5.321 28.151 31.706 1.00 69.40 N ANISOU 1035 N LEU A 131 9331 8829 8209 -846 -355 842 N ATOM 1036 CA LEU A 131 4.966 27.068 32.618 1.00 61.97 C ANISOU 1036 CA LEU A 131 8412 7787 7345 -853 -381 832 C ATOM 1037 C LEU A 131 3.456 26.971 32.800 1.00 77.74 C ANISOU 1037 C LEU A 131 10365 9923 9249 -948 -472 946 C ATOM 1038 O LEU A 131 2.904 25.869 32.898 1.00 85.38 O ANISOU 1038 O LEU A 131 11376 10852 10211 -1058 -489 917 O ATOM 1039 CB LEU A 131 5.659 27.266 33.966 1.00 57.63 C ANISOU 1039 CB LEU A 131 7827 7116 6952 -678 -384 868 C ATOM 1040 CG LEU A 131 5.369 26.212 35.037 1.00 72.01 C ANISOU 1040 CG LEU A 131 9671 8834 8855 -678 -419 891 C ATOM 1041 CD1 LEU A 131 5.693 24.819 34.524 1.00 81.36 C ANISOU 1041 CD1 LEU A 131 10951 9873 10090 -776 -369 763 C ATOM 1042 CD2 LEU A 131 6.148 26.508 36.305 1.00 60.70 C ANISOU 1042 CD2 LEU A 131 8206 7308 7549 -517 -433 934 C ATOM 1043 N ALA A 132 2.769 28.115 32.837 1.00 83.58 N ANISOU 1043 N ALA A 132 11007 10816 9932 -907 -528 1079 N ATOM 1044 CA ALA A 132 1.316 28.096 32.961 1.00 74.22 C ANISOU 1044 CA ALA A 132 9749 9778 8673 -990 -611 1195 C ATOM 1045 C ALA A 132 0.659 27.584 31.685 1.00 79.73 C ANISOU 1045 C ALA A 132 10483 10587 9224 -1198 -645 1167 C ATOM 1046 O ALA A 132 -0.342 26.862 31.744 1.00 83.07 O ANISOU 1046 O ALA A 132 10891 11069 9603 -1325 -699 1198 O ATOM 1047 CB ALA A 132 0.799 29.490 33.311 1.00 74.69 C ANISOU 1047 CB ALA A 132 9682 9954 8742 -874 -653 1338 C ATOM 1048 N ILE A 133 1.209 27.947 30.524 1.00 80.10 N ANISOU 1048 N ILE A 133 10577 10674 9181 -1251 -616 1110 N ATOM 1049 CA ILE A 133 0.659 27.476 29.254 1.00 83.03 C ANISOU 1049 CA ILE A 133 11000 11168 9380 -1468 -650 1071 C ATOM 1050 C ILE A 133 0.779 25.961 29.155 1.00 96.49 C ANISOU 1050 C ILE A 133 12822 12748 11090 -1600 -604 904 C ATOM 1051 O ILE A 133 -0.171 25.267 28.770 1.00103.39 O ANISOU 1051 O ILE A 133 13710 13703 11870 -1782 -668 902 O ATOM 1052 CB ILE A 133 1.358 28.174 28.073 1.00 77.77 C ANISOU 1052 CB ILE A 133 10375 10571 8602 -1501 -611 1038 C ATOM 1053 CG1 ILE A 133 1.075 29.677 28.093 1.00 76.16 C ANISOU 1053 CG1 ILE A 133 10052 10487 8401 -1393 -676 1229 C ATOM 1054 CG2 ILE A 133 0.920 27.560 26.750 1.00 60.60 C ANISOU 1054 CG2 ILE A 133 8281 8522 6221 -1749 -634 964 C ATOM 1055 CD1 ILE A 133 1.786 30.442 26.996 1.00 72.48 C ANISOU 1055 CD1 ILE A 133 9622 10085 7832 -1425 -640 1229 C ATOM 1056 N GLU A 134 1.950 25.424 29.504 1.00 95.79 N ANISOU 1056 N GLU A 134 12814 12452 11128 -1511 -498 765 N ATOM 1057 CA GLU A 134 2.160 23.982 29.426 1.00 86.50 C ANISOU 1057 CA GLU A 134 11752 11116 10000 -1614 -444 601 C ATOM 1058 C GLU A 134 1.257 23.239 30.404 1.00 84.18 C ANISOU 1058 C GLU A 134 11428 10777 9778 -1646 -514 680 C ATOM 1059 O GLU A 134 0.636 22.231 30.046 1.00 87.54 O ANISOU 1059 O GLU A 134 11916 11188 10158 -1828 -536 615 O ATOM 1060 CB GLU A 134 3.629 23.652 29.689 1.00 84.45 C ANISOU 1060 CB GLU A 134 11553 10634 9902 -1479 -320 463 C ATOM 1061 CG GLU A 134 4.589 24.282 28.695 1.00 93.07 C ANISOU 1061 CG GLU A 134 12672 11763 10927 -1463 -226 369 C ATOM 1062 CD GLU A 134 6.040 24.018 29.040 1.00 97.68 C ANISOU 1062 CD GLU A 134 13279 12135 11698 -1313 -105 249 C ATOM 1063 OE1 GLU A 134 6.301 23.429 30.111 1.00103.59 O ANISOU 1063 OE1 GLU A 134 14018 12710 12632 -1207 -115 262 O ATOM 1064 OE2 GLU A 134 6.919 24.397 28.238 1.00 93.00 O ANISOU 1064 OE2 GLU A 134 12708 11557 11071 -1305 -4 151 O ATOM 1065 N ARG A 135 1.173 23.720 31.647 1.00 74.18 N ANISOU 1065 N ARG A 135 10073 9494 8619 -1485 -546 817 N ATOM 1066 CA ARG A 135 0.295 23.078 32.619 1.00 72.48 C ANISOU 1066 CA ARG A 135 9822 9261 8457 -1522 -604 910 C ATOM 1067 C ARG A 135 -1.163 23.149 32.186 1.00 84.36 C ANISOU 1067 C ARG A 135 11253 10975 9825 -1688 -698 1007 C ATOM 1068 O ARG A 135 -1.933 22.216 32.442 1.00 86.20 O ANISOU 1068 O ARG A 135 11496 11190 10064 -1823 -735 1022 O ATOM 1069 CB ARG A 135 0.478 23.715 33.997 1.00 67.15 C ANISOU 1069 CB ARG A 135 9065 8564 7886 -1325 -612 1033 C ATOM 1070 CG ARG A 135 1.828 23.422 34.633 1.00 75.14 C ANISOU 1070 CG ARG A 135 10139 9360 9050 -1181 -547 961 C ATOM 1071 CD ARG A 135 2.020 24.187 35.933 1.00 84.14 C ANISOU 1071 CD ARG A 135 11202 10513 10256 -1005 -566 1076 C ATOM 1072 NE ARG A 135 3.135 23.652 36.709 1.00 88.70 N ANISOU 1072 NE ARG A 135 11833 10888 10982 -899 -537 1038 N ATOM 1073 CZ ARG A 135 3.583 24.180 37.843 1.00 88.64 C ANISOU 1073 CZ ARG A 135 11783 10861 11034 -754 -553 1112 C ATOM 1074 NH1 ARG A 135 3.018 25.271 38.341 1.00 88.22 N ANISOU 1074 NH1 ARG A 135 11643 10967 10912 -691 -579 1205 N ATOM 1075 NH2 ARG A 135 4.602 23.618 38.478 1.00 95.40 N ANISOU 1075 NH2 ARG A 135 12682 11539 12026 -674 -546 1089 N ATOM 1076 N TYR A 136 -1.559 24.235 31.520 1.00 90.77 N ANISOU 1076 N TYR A 136 11982 11983 10522 -1687 -743 1085 N ATOM 1077 CA TYR A 136 -2.920 24.324 31.001 1.00 87.64 C ANISOU 1077 CA TYR A 136 11499 11798 10003 -1849 -847 1188 C ATOM 1078 C TYR A 136 -3.126 23.374 29.828 1.00 87.08 C ANISOU 1078 C TYR A 136 11538 11744 9806 -2097 -865 1056 C ATOM 1079 O TYR A 136 -4.152 22.689 29.750 1.00 93.31 O ANISOU 1079 O TYR A 136 12302 12603 10549 -2274 -937 1087 O ATOM 1080 CB TYR A 136 -3.228 25.767 30.598 1.00 78.61 C ANISOU 1080 CB TYR A 136 10232 10842 8794 -1768 -900 1324 C ATOM 1081 CG TYR A 136 -4.329 25.915 29.571 1.00 72.70 C ANISOU 1081 CG TYR A 136 9415 10317 7889 -1955 -1014 1408 C ATOM 1082 CD1 TYR A 136 -5.665 25.807 29.934 1.00 80.32 C ANISOU 1082 CD1 TYR A 136 10242 11420 8857 -2029 -1106 1545 C ATOM 1083 CD2 TYR A 136 -4.030 26.177 28.240 1.00 63.87 C ANISOU 1083 CD2 TYR A 136 8361 9289 6617 -2066 -1034 1360 C ATOM 1084 CE1 TYR A 136 -6.673 25.945 28.998 1.00 74.69 C ANISOU 1084 CE1 TYR A 136 9448 10922 8010 -2205 -1229 1637 C ATOM 1085 CE2 TYR A 136 -5.031 26.318 27.297 1.00 66.50 C ANISOU 1085 CE2 TYR A 136 8631 9844 6793 -2251 -1160 1453 C ATOM 1086 CZ TYR A 136 -6.351 26.201 27.682 1.00 75.53 C ANISOU 1086 CZ TYR A 136 9626 11115 7955 -2317 -1265 1595 C ATOM 1087 OH TYR A 136 -7.353 26.340 26.750 1.00 85.56 O ANISOU 1087 OH TYR A 136 10816 12616 9078 -2505 -1409 1703 O ATOM 1088 N VAL A 137 -2.157 23.310 28.911 1.00 85.95 N ANISOU 1088 N VAL A 137 11516 11539 9604 -2123 -793 900 N ATOM 1089 CA VAL A 137 -2.286 22.437 27.747 1.00 89.71 C ANISOU 1089 CA VAL A 137 12113 12034 9940 -2368 -792 742 C ATOM 1090 C VAL A 137 -2.296 20.973 28.170 1.00 99.29 C ANISOU 1090 C VAL A 137 13427 13040 11259 -2462 -753 613 C ATOM 1091 O VAL A 137 -3.069 20.163 27.642 1.00 99.04 O ANISOU 1091 O VAL A 137 13439 13052 11137 -2695 -808 557 O ATOM 1092 CB VAL A 137 -1.158 22.731 26.738 1.00 77.65 C ANISOU 1092 CB VAL A 137 10691 10485 8327 -2360 -692 591 C ATOM 1093 CG1 VAL A 137 -1.027 21.604 25.727 1.00 72.37 C ANISOU 1093 CG1 VAL A 137 10183 9764 7549 -2592 -640 360 C ATOM 1094 CG2 VAL A 137 -1.415 24.052 26.031 1.00 81.62 C ANISOU 1094 CG2 VAL A 137 11107 11228 8676 -2354 -762 735 C ATOM 1095 N VAL A 138 -1.453 20.613 29.138 1.00 97.70 N ANISOU 1095 N VAL A 138 13260 12606 11257 -2290 -668 575 N ATOM 1096 CA VAL A 138 -1.321 19.213 29.531 1.00 86.77 C ANISOU 1096 CA VAL A 138 11980 10987 10004 -2364 -627 461 C ATOM 1097 C VAL A 138 -2.536 18.752 30.330 1.00 86.89 C ANISOU 1097 C VAL A 138 11918 11045 10050 -2455 -725 611 C ATOM 1098 O VAL A 138 -3.052 17.649 30.118 1.00 91.04 O ANISOU 1098 O VAL A 138 12516 11494 10580 -2653 -746 536 O ATOM 1099 CB VAL A 138 -0.011 19.006 30.313 1.00 73.36 C ANISOU 1099 CB VAL A 138 10326 9031 8516 -2146 -522 402 C ATOM 1100 CG1 VAL A 138 -0.030 17.679 31.052 1.00 75.89 C ANISOU 1100 CG1 VAL A 138 10716 9107 9012 -2186 -511 370 C ATOM 1101 CG2 VAL A 138 1.181 19.073 29.371 1.00 66.20 C ANISOU 1101 CG2 VAL A 138 9512 8045 7596 -2112 -400 202 C ATOM 1102 N VAL A 139 -3.016 19.582 31.252 1.00 83.83 N ANISOU 1102 N VAL A 139 11384 10780 9688 -2321 -778 816 N ATOM 1103 CA VAL A 139 -4.078 19.165 32.167 1.00 83.30 C ANISOU 1103 CA VAL A 139 11232 10751 9666 -2385 -845 963 C ATOM 1104 C VAL A 139 -5.461 19.409 31.575 1.00 82.48 C ANISOU 1104 C VAL A 139 11017 10908 9412 -2572 -955 1059 C ATOM 1105 O VAL A 139 -6.317 18.521 31.589 1.00 98.37 O ANISOU 1105 O VAL A 139 13031 12927 11420 -2771 -1008 1072 O ATOM 1106 CB VAL A 139 -3.911 19.871 33.530 1.00 72.55 C ANISOU 1106 CB VAL A 139 9769 9392 8405 -2156 -829 1119 C ATOM 1107 CG1 VAL A 139 -5.154 19.684 34.382 1.00 59.99 C ANISOU 1107 CG1 VAL A 139 8060 7914 6818 -2228 -889 1288 C ATOM 1108 CG2 VAL A 139 -2.684 19.337 34.254 1.00 65.76 C ANISOU 1108 CG2 VAL A 139 9014 8263 7707 -2016 -750 1048 C ATOM 1109 N CYS A 140 -5.710 20.607 31.048 1.00100.67 N ANISOU 1109 N CYS A 140 13448 10117 14687 -2909 36 -1007 N ATOM 1110 CA CYS A 140 -7.026 20.925 30.506 1.00 96.47 C ANISOU 1110 CA CYS A 140 12634 9757 14264 -2993 -159 -1057 C ATOM 1111 C CYS A 140 -7.299 20.275 29.159 1.00103.43 C ANISOU 1111 C CYS A 140 13490 10767 15042 -3131 -369 -1262 C ATOM 1112 O CYS A 140 -8.452 20.291 28.712 1.00120.15 O ANISOU 1112 O CYS A 140 15373 13010 17270 -3234 -521 -1341 O ATOM 1113 CB CYS A 140 -7.198 22.443 30.385 1.00 95.67 C ANISOU 1113 CB CYS A 140 12407 9839 14103 -2820 -285 -873 C ATOM 1114 SG CYS A 140 -7.069 23.325 31.951 1.00105.21 S ANISOU 1114 SG CYS A 140 13587 10929 15459 -2662 -59 -646 S ATOM 1115 N LYS A 141 -6.280 19.712 28.515 1.00 96.64 N ANISOU 1115 N LYS A 141 12858 9884 13976 -3134 -380 -1355 N ATOM 1116 CA LYS A 141 -6.381 19.034 27.224 1.00100.77 C ANISOU 1116 CA LYS A 141 13383 10528 14377 -3261 -567 -1566 C ATOM 1117 C LYS A 141 -7.225 19.840 26.222 1.00107.99 C ANISOU 1117 C LYS A 141 14077 11730 15225 -3255 -846 -1563 C ATOM 1118 O LYS A 141 -8.206 19.327 25.679 1.00117.77 O ANISOU 1118 O LYS A 141 15138 13050 16560 -3412 -972 -1725 O ATOM 1119 CB LYS A 141 -6.929 17.620 27.384 1.00 98.80 C ANISOU 1119 CB LYS A 141 13098 10120 14323 -3479 -483 -1778 C ATOM 1120 CG LYS A 141 -6.007 16.675 28.143 1.00 99.31 C ANISOU 1120 CG LYS A 141 13401 9909 14423 -3499 -236 -1807 C ATOM 1121 CD LYS A 141 -6.624 15.280 28.237 1.00111.24 C ANISOU 1121 CD LYS A 141 14857 11264 16144 -3723 -168 -2017 C ATOM 1122 CE LYS A 141 -5.685 14.274 28.906 1.00114.39 C ANISOU 1122 CE LYS A 141 15498 11385 16578 -3747 66 -2052 C ATOM 1123 NZ LYS A 141 -6.309 12.917 29.012 1.00112.11 N ANISOU 1123 NZ LYS A 141 15150 10932 16516 -3969 136 -2250 N ATOM 1124 N PRO A 142 -6.860 21.102 25.965 1.00107.55 N ANISOU 1124 N PRO A 142 14026 11829 15008 -3074 -947 -1380 N ATOM 1125 CA PRO A 142 -7.673 21.929 25.060 1.00112.20 C ANISOU 1125 CA PRO A 142 14399 12689 15542 -3057 -1213 -1352 C ATOM 1126 C PRO A 142 -7.526 21.570 23.591 1.00124.86 C ANISOU 1126 C PRO A 142 16032 14491 16917 -3130 -1435 -1513 C ATOM 1127 O PRO A 142 -8.396 21.944 22.792 1.00131.95 O ANISOU 1127 O PRO A 142 16726 15609 17800 -3168 -1662 -1544 O ATOM 1128 CB PRO A 142 -7.152 23.348 25.327 1.00105.50 C ANISOU 1128 CB PRO A 142 13582 11909 14595 -2831 -1220 -1093 C ATOM 1129 CG PRO A 142 -5.711 23.126 25.681 1.00104.39 C ANISOU 1129 CG PRO A 142 13743 11617 14303 -2741 -1043 -1052 C ATOM 1130 CD PRO A 142 -5.627 21.795 26.383 1.00109.55 C ANISOU 1130 CD PRO A 142 14491 12025 15106 -2880 -834 -1200 C ATOM 1131 N MET A 143 -6.463 20.873 23.207 1.00125.21 N ANISOU 1131 N MET A 143 16318 14475 16782 -3149 -1382 -1617 N ATOM 1132 CA MET A 143 -6.253 20.468 21.826 1.00128.07 C ANISOU 1132 CA MET A 143 16718 15026 16917 -3224 -1580 -1788 C ATOM 1133 C MET A 143 -6.546 18.981 21.657 1.00137.54 C ANISOU 1133 C MET A 143 17921 16114 18224 -3437 -1534 -2066 C ATOM 1134 O MET A 143 -6.357 18.181 22.576 1.00136.98 O ANISOU 1134 O MET A 143 17940 15780 18325 -3497 -1311 -2112 O ATOM 1135 CB MET A 143 -4.824 20.779 21.376 1.00126.44 C ANISOU 1135 CB MET A 143 16772 14859 16411 -3093 -1573 -1724 C ATOM 1136 CG MET A 143 -4.532 22.268 21.267 1.00129.99 C ANISOU 1136 CG MET A 143 17209 15461 16721 -2891 -1663 -1467 C ATOM 1137 SD MET A 143 -2.843 22.632 20.755 1.00134.13 S ANISOU 1137 SD MET A 143 18039 16028 16898 -2742 -1645 -1392 S ATOM 1138 CE MET A 143 -1.925 22.073 22.187 1.00135.08 C ANISOU 1138 CE MET A 143 18383 15792 17148 -2697 -1303 -1360 C ATOM 1139 N SER A 144 -7.011 18.622 20.464 1.00144.58 N ANISOU 1139 N SER A 144 18710 17211 19013 -3553 -1750 -2250 N ATOM 1140 CA SER A 144 -7.466 17.265 20.192 1.00149.71 C ANISOU 1140 CA SER A 144 19315 17785 19782 -3767 -1740 -2532 C ATOM 1141 C SER A 144 -6.273 16.342 19.969 1.00152.73 C ANISOU 1141 C SER A 144 19964 18040 20027 -3799 -1634 -2675 C ATOM 1142 O SER A 144 -5.516 16.516 19.007 1.00151.54 O ANISOU 1142 O SER A 144 19932 18056 19592 -3750 -1757 -2713 O ATOM 1143 CB SER A 144 -8.391 17.252 18.978 1.00153.74 C ANISOU 1143 CB SER A 144 19610 18580 20226 -3873 -2016 -2685 C ATOM 1144 OG SER A 144 -8.926 15.959 18.751 1.00157.89 O ANISOU 1144 OG SER A 144 20066 19030 20895 -4086 -2005 -2966 O ATOM 1145 N ASN A 145 -6.112 15.359 20.859 1.00154.61 N ANISOU 1145 N ASN A 145 20293 17983 20469 -3883 -1406 -2752 N ATOM 1146 CA ASN A 145 -5.108 14.299 20.735 1.00156.20 C ANISOU 1146 CA ASN A 145 20725 18023 20600 -3940 -1291 -2917 C ATOM 1147 C ASN A 145 -3.702 14.888 20.576 1.00150.37 C ANISOU 1147 C ASN A 145 20237 17315 19581 -3761 -1261 -2787 C ATOM 1148 O ASN A 145 -3.043 14.750 19.543 1.00154.14 O ANISOU 1148 O ASN A 145 20818 17940 19809 -3761 -1382 -2903 O ATOM 1149 CB ASN A 145 -5.454 13.362 19.570 1.00161.94 C ANISOU 1149 CB ASN A 145 21381 18874 21276 -4122 -1451 -3224 C ATOM 1150 CG ASN A 145 -6.791 12.668 19.755 1.00167.83 C ANISOU 1150 CG ASN A 145 21889 19565 22313 -4310 -1462 -3374 C ATOM 1151 OD1 ASN A 145 -6.854 11.529 20.218 1.00172.33 O ANISOU 1151 OD1 ASN A 145 22495 19897 23085 -4445 -1310 -3525 O ATOM 1152 ND2 ASN A 145 -7.869 13.354 19.393 1.00169.48 N ANISOU 1152 ND2 ASN A 145 21851 19994 22551 -4320 -1642 -3332 N ATOM 1153 N PHE A 146 -3.259 15.545 21.644 1.00141.86 N ANISOU 1153 N PHE A 146 19249 16096 18554 -3609 -1093 -2549 N ATOM 1154 CA PHE A 146 -1.955 16.191 21.681 1.00134.32 C ANISOU 1154 CA PHE A 146 18522 15147 17365 -3426 -1039 -2399 C ATOM 1155 C PHE A 146 -1.191 15.725 22.909 1.00137.15 C ANISOU 1155 C PHE A 146 19073 15192 17846 -3379 -757 -2333 C ATOM 1156 O PHE A 146 -1.749 15.671 24.009 1.00138.06 O ANISOU 1156 O PHE A 146 19107 15138 18211 -3393 -607 -2242 O ATOM 1157 CB PHE A 146 -2.091 17.718 21.690 1.00130.96 C ANISOU 1157 CB PHE A 146 18012 14906 16842 -3252 -1139 -2142 C ATOM 1158 CG PHE A 146 -0.793 18.438 21.908 1.00124.53 C ANISOU 1158 CG PHE A 146 17421 14069 15826 -3058 -1056 -1968 C ATOM 1159 CD1 PHE A 146 0.111 18.593 20.871 1.00125.91 C ANISOU 1159 CD1 PHE A 146 17739 14405 15695 -3009 -1173 -2016 C ATOM 1160 CD2 PHE A 146 -0.475 18.959 23.151 1.00119.77 C ANISOU 1160 CD2 PHE A 146 16879 13291 15338 -2928 -858 -1763 C ATOM 1161 CE1 PHE A 146 1.307 19.254 21.069 1.00121.08 C ANISOU 1161 CE1 PHE A 146 17329 13772 14903 -2834 -1092 -1861 C ATOM 1162 CE2 PHE A 146 0.720 19.622 23.355 1.00115.80 C ANISOU 1162 CE2 PHE A 146 16575 12768 14654 -2750 -780 -1612 C ATOM 1163 CZ PHE A 146 1.612 19.770 22.313 1.00114.54 C ANISOU 1163 CZ PHE A 146 16559 12763 14198 -2703 -896 -1660 C ATOM 1164 N ARG A 147 0.084 15.395 22.716 1.00136.97 N ANISOU 1164 N ARG A 147 19300 15100 17643 -3322 -686 -2378 N ATOM 1165 CA ARG A 147 0.969 14.955 23.785 1.00141.43 C ANISOU 1165 CA ARG A 147 20071 15381 18284 -3262 -428 -2317 C ATOM 1166 C ARG A 147 2.184 15.871 23.817 1.00134.29 C ANISOU 1166 C ARG A 147 19358 14528 17138 -3055 -397 -2145 C ATOM 1167 O ARG A 147 2.840 16.073 22.789 1.00135.93 O ANISOU 1167 O ARG A 147 19657 14908 17083 -3019 -531 -2207 O ATOM 1168 CB ARG A 147 1.392 13.497 23.578 1.00153.08 C ANISOU 1168 CB ARG A 147 21675 16684 19804 -3406 -352 -2566 C ATOM 1169 CG ARG A 147 1.383 12.637 24.837 1.00161.09 C ANISOU 1169 CG ARG A 147 22749 17370 21088 -3459 -99 -2557 C ATOM 1170 CD ARG A 147 2.745 12.614 25.513 1.00165.34 C ANISOU 1170 CD ARG A 147 23555 17729 21537 -3319 92 -2455 C ATOM 1171 NE ARG A 147 3.823 12.847 24.556 1.00169.61 N ANISOU 1171 NE ARG A 147 24263 18410 21772 -3237 -9 -2515 N ATOM 1172 CZ ARG A 147 5.091 12.498 24.751 1.00163.72 C ANISOU 1172 CZ ARG A 147 23763 17526 20917 -3160 117 -2530 C ATOM 1173 NH1 ARG A 147 5.448 11.881 25.869 1.00160.22 N ANISOU 1173 NH1 ARG A 147 23432 16798 20646 -3151 346 -2485 N ATOM 1174 NH2 ARG A 147 6.000 12.758 23.822 1.00160.40 N ANISOU 1174 NH2 ARG A 147 23475 17258 20213 -3092 12 -2589 N ATOM 1175 N PHE A 148 2.473 16.429 24.990 1.00127.74 N ANISOU 1175 N PHE A 148 18581 13558 16396 -2922 -220 -1932 N ATOM 1176 CA PHE A 148 3.569 17.378 25.145 1.00118.85 C ANISOU 1176 CA PHE A 148 17618 12471 15068 -2718 -176 -1754 C ATOM 1177 C PHE A 148 4.898 16.631 25.145 1.00117.48 C ANISOU 1177 C PHE A 148 17720 12148 14770 -2694 -51 -1851 C ATOM 1178 O PHE A 148 5.129 15.762 25.992 1.00121.78 O ANISOU 1178 O PHE A 148 18357 12439 15475 -2738 143 -1893 O ATOM 1179 CB PHE A 148 3.393 18.175 26.435 1.00112.37 C ANISOU 1179 CB PHE A 148 16748 11547 14399 -2591 -22 -1514 C ATOM 1180 CG PHE A 148 4.352 19.321 26.578 1.00111.59 C ANISOU 1180 CG PHE A 148 16771 11515 14111 -2378 3 -1318 C ATOM 1181 CD1 PHE A 148 5.583 19.142 27.187 1.00110.52 C ANISOU 1181 CD1 PHE A 148 16875 11214 13905 -2274 188 -1276 C ATOM 1182 CD2 PHE A 148 4.019 20.581 26.109 1.00110.03 C ANISOU 1182 CD2 PHE A 148 16447 11544 13817 -2280 -160 -1176 C ATOM 1183 CE1 PHE A 148 6.464 20.195 27.322 1.00104.68 C ANISOU 1183 CE1 PHE A 148 16242 10535 12998 -2080 214 -1105 C ATOM 1184 CE2 PHE A 148 4.896 21.639 26.241 1.00108.45 C ANISOU 1184 CE2 PHE A 148 16353 11395 13456 -2086 -133 -997 C ATOM 1185 CZ PHE A 148 6.120 21.445 26.848 1.00107.68 C ANISOU 1185 CZ PHE A 148 16492 11134 13289 -1988 55 -966 C ATOM 1186 N GLY A 149 5.775 16.974 24.204 1.00113.99 N ANISOU 1186 N GLY A 149 17404 11863 14044 -2623 -161 -1882 N ATOM 1187 CA GLY A 149 7.035 16.271 24.065 1.00111.68 C ANISOU 1187 CA GLY A 149 17363 11453 13617 -2605 -65 -1997 C ATOM 1188 C GLY A 149 8.265 17.131 24.269 1.00109.14 C ANISOU 1188 C GLY A 149 17227 11149 13091 -2402 4 -1834 C ATOM 1189 O GLY A 149 8.172 18.266 24.747 1.00115.23 O ANISOU 1189 O GLY A 149 17942 11980 13861 -2265 17 -1612 O ATOM 1190 N GLU A 150 9.431 16.594 23.902 1.00108.43 N ANISOU 1190 N GLU A 150 17357 11007 12835 -2383 50 -1953 N ATOM 1191 CA GLU A 150 10.680 17.325 24.093 1.00106.97 C ANISOU 1191 CA GLU A 150 17362 10826 12454 -2195 127 -1818 C ATOM 1192 C GLU A 150 10.770 18.528 23.161 1.00107.69 C ANISOU 1192 C GLU A 150 17404 11211 12304 -2104 -64 -1716 C ATOM 1193 O GLU A 150 11.298 19.578 23.544 1.00106.30 O ANISOU 1193 O GLU A 150 17280 11067 12043 -1933 -17 -1513 O ATOM 1194 CB GLU A 150 11.873 16.392 23.879 1.00110.16 C ANISOU 1194 CB GLU A 150 18005 11106 12746 -2208 215 -1990 C ATOM 1195 CG GLU A 150 13.228 17.052 24.103 1.00116.95 C ANISOU 1195 CG GLU A 150 19072 11954 13409 -2019 307 -1870 C ATOM 1196 CD GLU A 150 14.377 16.228 23.552 1.00119.79 C ANISOU 1196 CD GLU A 150 19647 12261 13606 -2040 336 -2066 C ATOM 1197 OE1 GLU A 150 14.118 15.150 22.975 1.00117.16 O ANISOU 1197 OE1 GLU A 150 19299 11902 13315 -2201 280 -2298 O ATOM 1198 OE2 GLU A 150 15.540 16.661 23.691 1.00123.22 O ANISOU 1198 OE2 GLU A 150 20261 12682 13877 -1894 415 -1995 O ATOM 1199 N ASN A 151 10.268 18.396 21.931 1.00109.93 N ANISOU 1199 N ASN A 151 17585 11713 12472 -2216 -281 -1851 N ATOM 1200 CA ASN A 151 10.351 19.510 20.990 1.00105.36 C ANISOU 1200 CA ASN A 151 16957 11422 11652 -2135 -470 -1749 C ATOM 1201 C ASN A 151 9.449 20.666 21.401 1.00103.15 C ANISOU 1201 C ASN A 151 16480 11229 11483 -2057 -526 -1516 C ATOM 1202 O ASN A 151 9.785 21.829 21.149 1.00109.83 O ANISOU 1202 O ASN A 151 17331 12225 12175 -1919 -594 -1338 O ATOM 1203 CB ASN A 151 10.006 19.042 19.578 1.00112.25 C ANISOU 1203 CB ASN A 151 17761 12519 12371 -2278 -689 -1957 C ATOM 1204 CG ASN A 151 11.100 18.192 18.965 1.00119.35 C ANISOU 1204 CG ASN A 151 18866 13395 13086 -2319 -663 -2168 C ATOM 1205 OD1 ASN A 151 12.269 18.301 19.337 1.00120.06 O ANISOU 1205 OD1 ASN A 151 19161 13378 13077 -2203 -527 -2119 O ATOM 1206 ND2 ASN A 151 10.727 17.343 18.016 1.00123.99 N ANISOU 1206 ND2 ASN A 151 19394 14086 13628 -2485 -795 -2413 N ATOM 1207 N HIS A 152 8.307 20.377 22.027 1.00 99.98 N ANISOU 1207 N HIS A 152 15901 10735 11353 -2145 -498 -1514 N ATOM 1208 CA HIS A 152 7.468 21.454 22.540 1.00 94.05 C ANISOU 1208 CA HIS A 152 14961 10043 10732 -2066 -530 -1297 C ATOM 1209 C HIS A 152 8.098 22.116 23.756 1.00 97.71 C ANISOU 1209 C HIS A 152 15520 10342 11264 -1893 -326 -1092 C ATOM 1210 O HIS A 152 7.929 23.323 23.962 1.00101.99 O ANISOU 1210 O HIS A 152 15974 10976 11802 -1764 -363 -886 O ATOM 1211 CB HIS A 152 6.078 20.925 22.890 1.00 92.13 C ANISOU 1211 CB HIS A 152 14497 9744 10763 -2213 -548 -1364 C ATOM 1212 CG HIS A 152 5.374 20.272 21.743 1.00 97.88 C ANISOU 1212 CG HIS A 152 15109 10635 11445 -2387 -747 -1573 C ATOM 1213 ND1 HIS A 152 5.338 18.905 21.573 1.00104.86 N ANISOU 1213 ND1 HIS A 152 16042 11404 12398 -2551 -706 -1820 N ATOM 1214 CD2 HIS A 152 4.685 20.799 20.703 1.00 98.46 C ANISOU 1214 CD2 HIS A 152 15018 10981 11413 -2421 -990 -1576 C ATOM 1215 CE1 HIS A 152 4.653 18.617 20.480 1.00111.82 C ANISOU 1215 CE1 HIS A 152 16788 12482 13216 -2681 -914 -1975 C ATOM 1216 NE2 HIS A 152 4.248 19.748 19.933 1.00112.35 N ANISOU 1216 NE2 HIS A 152 16726 12793 13171 -2605 -1090 -1830 N ATOM 1217 N ALA A 153 8.828 21.347 24.567 1.00 97.65 N ANISOU 1217 N ALA A 153 15686 10093 11322 -1886 -112 -1148 N ATOM 1218 CA ALA A 153 9.477 21.916 25.743 1.00100.04 C ANISOU 1218 CA ALA A 153 16086 10243 11682 -1723 89 -967 C ATOM 1219 C ALA A 153 10.633 22.826 25.351 1.00 98.07 C ANISOU 1219 C ALA A 153 15988 10100 11174 -1555 68 -860 C ATOM 1220 O ALA A 153 10.851 23.867 25.981 1.00 92.21 O ANISOU 1220 O ALA A 153 15233 9355 10449 -1399 135 -659 O ATOM 1221 CB ALA A 153 9.959 20.798 26.665 1.00 88.58 C ANISOU 1221 CB ALA A 153 14783 8514 10359 -1764 314 -1058 C ATOM 1222 N ILE A 154 11.386 22.449 24.315 1.00 95.74 N ANISOU 1222 N ILE A 154 15833 9901 10642 -1586 -20 -997 N ATOM 1223 CA ILE A 154 12.506 23.273 23.871 1.00 95.06 C ANISOU 1223 CA ILE A 154 15895 9925 10300 -1438 -43 -906 C ATOM 1224 C ILE A 154 12.004 24.585 23.282 1.00 99.45 C ANISOU 1224 C ILE A 154 16294 10720 10773 -1365 -224 -735 C ATOM 1225 O ILE A 154 12.556 25.657 23.558 1.00 96.10 O ANISOU 1225 O ILE A 154 15909 10325 10278 -1200 -186 -549 O ATOM 1226 CB ILE A 154 13.376 22.491 22.870 1.00 88.46 C ANISOU 1226 CB ILE A 154 15234 9143 9233 -1505 -98 -1112 C ATOM 1227 CG1 ILE A 154 14.040 21.301 23.563 1.00 84.75 C ANISOU 1227 CG1 ILE A 154 14939 8412 8850 -1544 103 -1254 C ATOM 1228 CG2 ILE A 154 14.429 23.394 22.249 1.00 83.22 C ANISOU 1228 CG2 ILE A 154 14698 8632 8288 -1367 -150 -1020 C ATOM 1229 CD1 ILE A 154 14.832 20.420 22.629 1.00 83.97 C ANISOU 1229 CD1 ILE A 154 15000 8347 8558 -1623 57 -1482 C ATOM 1230 N MET A 155 10.946 24.525 22.468 1.00 97.37 N ANISOU 1230 N MET A 155 15844 10628 10524 -1485 -426 -793 N ATOM 1231 CA MET A 155 10.360 25.749 21.932 1.00 93.97 C ANISOU 1231 CA MET A 155 15246 10421 10039 -1420 -607 -623 C ATOM 1232 C MET A 155 9.832 26.649 23.041 1.00 92.25 C ANISOU 1232 C MET A 155 14896 10114 10042 -1309 -516 -409 C ATOM 1233 O MET A 155 9.850 27.878 22.905 1.00 95.75 O ANISOU 1233 O MET A 155 15274 10679 10429 -1181 -589 -216 O ATOM 1234 CB MET A 155 9.242 25.410 20.946 1.00102.34 C ANISOU 1234 CB MET A 155 16117 11668 11099 -1578 -831 -739 C ATOM 1235 CG MET A 155 9.715 24.695 19.692 1.00121.17 C ANISOU 1235 CG MET A 155 18605 14197 13236 -1682 -956 -944 C ATOM 1236 SD MET A 155 8.342 24.212 18.629 1.00140.41 S ANISOU 1236 SD MET A 155 20807 16848 15696 -1876 -1208 -1101 S ATOM 1237 CE MET A 155 9.209 23.353 17.319 1.00139.28 C ANISOU 1237 CE MET A 155 20831 16844 15245 -1974 -1302 -1350 C ATOM 1238 N GLY A 156 9.364 26.061 24.144 1.00 87.59 N ANISOU 1238 N GLY A 156 14260 9314 9706 -1355 -354 -439 N ATOM 1239 CA GLY A 156 8.913 26.870 25.264 1.00 87.66 C ANISOU 1239 CA GLY A 156 14147 9234 9924 -1250 -249 -251 C ATOM 1240 C GLY A 156 10.038 27.664 25.900 1.00 93.13 C ANISOU 1240 C GLY A 156 14991 9852 10541 -1058 -101 -97 C ATOM 1241 O GLY A 156 9.854 28.821 26.284 1.00 96.04 O ANISOU 1241 O GLY A 156 15257 10263 10970 -930 -105 94 O ATOM 1242 N VAL A 157 11.218 27.052 26.020 1.00 92.45 N ANISOU 1242 N VAL A 157 15147 9652 10328 -1033 32 -184 N ATOM 1243 CA VAL A 157 12.376 27.769 26.546 1.00 87.53 C ANISOU 1243 CA VAL A 157 14680 8967 9611 -851 168 -56 C ATOM 1244 C VAL A 157 12.872 28.795 25.535 1.00 85.11 C ANISOU 1244 C VAL A 157 14397 8872 9067 -757 11 42 C ATOM 1245 O VAL A 157 13.203 29.932 25.894 1.00 73.24 O ANISOU 1245 O VAL A 157 12880 7390 7559 -599 46 226 O ATOM 1246 CB VAL A 157 13.487 26.779 26.938 1.00 80.15 C ANISOU 1246 CB VAL A 157 13993 7851 8609 -855 349 -186 C ATOM 1247 CG1 VAL A 157 14.725 27.529 27.404 1.00 76.44 C ANISOU 1247 CG1 VAL A 157 13686 7334 8024 -666 480 -65 C ATOM 1248 CG2 VAL A 157 12.994 25.829 28.018 1.00 71.30 C ANISOU 1248 CG2 VAL A 157 12843 6512 7734 -939 514 -254 C ATOM 1249 N ALA A 158 12.931 28.411 24.256 1.00 83.49 N ANISOU 1249 N ALA A 158 14226 8831 8665 -854 -163 -78 N ATOM 1250 CA ALA A 158 13.362 29.344 23.221 1.00 80.40 C ANISOU 1250 CA ALA A 158 13853 8659 8036 -778 -324 17 C ATOM 1251 C ALA A 158 12.421 30.536 23.112 1.00 92.41 C ANISOU 1251 C ALA A 158 15143 10318 9650 -720 -463 213 C ATOM 1252 O ALA A 158 12.863 31.647 22.796 1.00 87.02 O ANISOU 1252 O ALA A 158 14470 9745 8850 -591 -520 378 O ATOM 1253 CB ALA A 158 13.468 28.620 21.878 1.00 77.91 C ANISOU 1253 CB ALA A 158 13594 8507 7502 -912 -490 -165 C ATOM 1254 N PHE A 159 11.128 30.328 23.372 1.00 99.08 N ANISOU 1254 N PHE A 159 15778 11157 10713 -813 -520 197 N ATOM 1255 CA PHE A 159 10.179 31.435 23.346 1.00 91.89 C ANISOU 1255 CA PHE A 159 14634 10362 9919 -758 -648 377 C ATOM 1256 C PHE A 159 10.463 32.449 24.446 1.00 90.49 C ANISOU 1256 C PHE A 159 14438 10067 9879 -582 -495 573 C ATOM 1257 O PHE A 159 10.264 33.651 24.241 1.00 89.07 O ANISOU 1257 O PHE A 159 14145 9998 9699 -475 -593 755 O ATOM 1258 CB PHE A 159 8.751 30.901 23.467 1.00 77.81 C ANISOU 1258 CB PHE A 159 12631 8580 8353 -902 -722 297 C ATOM 1259 CG PHE A 159 7.711 31.975 23.609 1.00 73.80 C ANISOU 1259 CG PHE A 159 11871 8162 8008 -845 -832 472 C ATOM 1260 CD1 PHE A 159 7.356 32.762 22.526 1.00 70.60 C ANISOU 1260 CD1 PHE A 159 11355 7994 7476 -826 -1070 566 C ATOM 1261 CD2 PHE A 159 7.084 32.194 24.826 1.00 75.30 C ANISOU 1261 CD2 PHE A 159 11928 8202 8479 -810 -700 542 C ATOM 1262 CE1 PHE A 159 6.399 33.753 22.656 1.00 74.88 C ANISOU 1262 CE1 PHE A 159 11661 8612 8180 -769 -1175 729 C ATOM 1263 CE2 PHE A 159 6.126 33.182 24.962 1.00 74.93 C ANISOU 1263 CE2 PHE A 159 11643 8236 8593 -757 -801 694 C ATOM 1264 CZ PHE A 159 5.783 33.962 23.876 1.00 73.34 C ANISOU 1264 CZ PHE A 159 11333 8260 8273 -734 -1040 787 C ATOM 1265 N THR A 160 10.927 31.991 25.611 1.00 88.47 N ANISOU 1265 N THR A 160 14286 9589 9741 -549 -258 537 N ATOM 1266 CA THR A 160 11.252 32.917 26.691 1.00 86.94 C ANISOU 1266 CA THR A 160 14078 9287 9670 -382 -102 706 C ATOM 1267 C THR A 160 12.466 33.770 26.342 1.00 92.43 C ANISOU 1267 C THR A 160 14927 10038 10154 -229 -92 814 C ATOM 1268 O THR A 160 12.488 34.973 26.627 1.00 95.12 O ANISOU 1268 O THR A 160 15183 10407 10551 -89 -92 996 O ATOM 1269 CB THR A 160 11.499 32.151 27.991 1.00 86.13 C ANISOU 1269 CB THR A 160 14058 8946 9722 -388 148 635 C ATOM 1270 OG1 THR A 160 12.517 31.165 27.779 1.00 95.33 O ANISOU 1270 OG1 THR A 160 15468 10035 10718 -431 233 484 O ATOM 1271 CG2 THR A 160 10.228 31.466 28.459 1.00 80.32 C ANISOU 1271 CG2 THR A 160 13144 8149 9225 -528 151 559 C ATOM 1272 N TRP A 161 13.490 33.163 25.734 1.00 86.89 N ANISOU 1272 N TRP A 161 14447 9349 9217 -254 -79 700 N ATOM 1273 CA ATRP A 161 14.683 33.913 25.349 0.57 81.41 C ANISOU 1273 CA ATRP A 161 13908 8714 8310 -119 -67 789 C ATOM 1274 CA BTRP A 161 14.675 33.929 25.368 0.43 81.26 C ANISOU 1274 CA BTRP A 161 13887 8694 8295 -117 -66 792 C ATOM 1275 C TRP A 161 14.358 34.960 24.291 1.00 84.52 C ANISOU 1275 C TRP A 161 14186 9336 8592 -84 -292 931 C ATOM 1276 O TRP A 161 14.866 36.086 24.339 1.00 90.87 O ANISOU 1276 O TRP A 161 14997 10173 9355 65 -282 1100 O ATOM 1277 CB ATRP A 161 15.762 32.963 24.826 0.57 77.17 C ANISOU 1277 CB ATRP A 161 13621 8160 7542 -173 -23 616 C ATOM 1278 CB BTRP A 161 15.789 32.987 24.914 0.43 77.24 C ANISOU 1278 CB BTRP A 161 13632 8156 7561 -164 -9 622 C ATOM 1279 CG ATRP A 161 16.195 31.903 25.792 0.57 74.29 C ANISOU 1279 CG ATRP A 161 13390 7569 7267 -203 193 480 C ATOM 1280 CG BTRP A 161 16.458 32.280 26.053 0.43 74.22 C ANISOU 1280 CG BTRP A 161 13398 7539 7264 -135 240 541 C ATOM 1281 CD1ATRP A 161 15.857 31.799 27.110 0.57 76.22 C ANISOU 1281 CD1ATRP A 161 13574 7631 7754 -170 367 515 C ATOM 1282 CD1BTRP A 161 15.960 31.234 26.774 0.43 76.06 C ANISOU 1282 CD1BTRP A 161 13611 7615 7672 -237 344 421 C ATOM 1283 CD2ATRP A 161 17.051 30.789 25.508 0.57 68.18 C ANISOU 1283 CD2ATRP A 161 12831 6732 6344 -272 258 290 C ATOM 1284 CD2BTRP A 161 17.748 32.569 26.604 0.43 74.50 C ANISOU 1284 CD2BTRP A 161 13622 7472 7214 7 414 579 C ATOM 1285 NE1ATRP A 161 16.450 30.690 27.664 0.57 78.57 N ANISOU 1285 NE1ATRP A 161 14040 7755 8059 -213 533 370 N ATOM 1286 NE1BTRP A 161 16.859 30.854 27.740 0.43 77.23 N ANISOU 1286 NE1BTRP A 161 13926 7573 7845 -165 570 390 N ATOM 1287 CE2ATRP A 161 17.188 30.053 26.701 0.57 74.93 C ANISOU 1287 CE2ATRP A 161 13749 7356 7366 -274 470 228 C ATOM 1288 CE2BTRP A 161 17.966 31.658 27.657 0.43 75.05 C ANISOU 1288 CE2BTRP A 161 13778 7327 7409 -14 616 480 C ATOM 1289 CE3ATRP A 161 17.714 30.344 24.361 0.57 57.36 C ANISOU 1289 CE3ATRP A 161 11601 5479 4713 -331 157 164 C ATOM 1290 CE3BTRP A 161 18.741 33.509 26.310 0.43 62.88 C ANISOU 1290 CE3BTRP A 161 12251 6068 5573 149 420 687 C ATOM 1291 CZ2ATRP A 161 17.963 28.896 26.780 0.57 67.98 C ANISOU 1291 CZ2ATRP A 161 13067 6350 6413 -330 579 51 C ATOM 1292 CZ2BTRP A 161 19.135 31.658 28.415 0.43 64.28 C ANISOU 1292 CZ2BTRP A 161 12597 5825 6003 106 816 484 C ATOM 1293 CZ3ATRP A 161 18.482 29.196 24.440 0.57 62.77 C ANISOU 1293 CZ3ATRP A 161 12480 6042 5329 -389 268 -25 C ATOM 1294 CZ3BTRP A 161 19.901 33.508 27.065 0.43 53.87 C ANISOU 1294 CZ3BTRP A 161 11289 4785 4394 264 623 682 C ATOM 1295 CH2ATRP A 161 18.599 28.485 25.641 0.57 64.82 C ANISOU 1295 CH2ATRP A 161 12798 6060 5769 -386 475 -77 C ATOM 1296 CH2BTRP A 161 20.088 32.589 28.105 0.43 55.82 C ANISOU 1296 CH2BTRP A 161 11617 4827 4764 244 816 580 C ATOM 1297 N VAL A 162 13.518 34.599 23.318 1.00 84.02 N ANISOU 1297 N VAL A 162 14012 9433 8479 -218 -499 863 N ATOM 1298 CA VAL A 162 13.137 35.546 22.274 1.00 83.66 C ANISOU 1298 CA VAL A 162 13846 9617 8325 -193 -727 1001 C ATOM 1299 C VAL A 162 12.364 36.715 22.872 1.00 90.83 C ANISOU 1299 C VAL A 162 14537 10514 9461 -87 -748 1208 C ATOM 1300 O VAL A 162 12.583 37.875 22.504 1.00101.46 O ANISOU 1300 O VAL A 162 15843 11961 10745 30 -829 1392 O ATOM 1301 CB VAL A 162 12.329 34.833 21.174 1.00 85.15 C ANISOU 1301 CB VAL A 162 13948 9981 8425 -367 -940 869 C ATOM 1302 CG1 VAL A 162 11.630 35.847 20.281 1.00 84.42 C ANISOU 1302 CG1 VAL A 162 13673 10117 8286 -341 -1180 1033 C ATOM 1303 CG2 VAL A 162 13.237 33.937 20.348 1.00 82.46 C ANISOU 1303 CG2 VAL A 162 13821 9700 7810 -448 -951 688 C ATOM 1304 N MET A 163 11.453 36.431 23.806 1.00 92.81 N ANISOU 1304 N MET A 163 14640 10640 9984 -127 -672 1180 N ATOM 1305 CA MET A 163 10.712 37.508 24.456 1.00 96.25 C ANISOU 1305 CA MET A 163 14861 11054 10654 -27 -678 1359 C ATOM 1306 C MET A 163 11.629 38.374 25.308 1.00 93.25 C ANISOU 1306 C MET A 163 14566 10552 10312 156 -498 1492 C ATOM 1307 O MET A 163 11.437 39.592 25.398 1.00 84.83 O ANISOU 1307 O MET A 163 13372 9527 9331 277 -547 1678 O ATOM 1308 CB MET A 163 9.580 36.935 25.307 1.00 92.53 C ANISOU 1308 CB MET A 163 14223 10476 10460 -119 -619 1282 C ATOM 1309 CG MET A 163 8.446 36.312 24.512 1.00 91.02 C ANISOU 1309 CG MET A 163 13885 10416 10284 -287 -816 1178 C ATOM 1310 SD MET A 163 7.586 37.501 23.467 1.00 94.30 S ANISOU 1310 SD MET A 163 14072 11079 10679 -251 -1108 1355 S ATOM 1311 CE MET A 163 8.249 37.082 21.856 1.00 91.71 C ANISOU 1311 CE MET A 163 13907 10963 9975 -326 -1288 1274 C ATOM 1312 N ALA A 164 12.633 37.763 25.941 1.00 98.92 N ANISOU 1312 N ALA A 164 15494 11118 10973 179 -290 1397 N ATOM 1313 CA ALA A 164 13.572 38.535 26.745 1.00 94.12 C ANISOU 1313 CA ALA A 164 14976 10399 10388 352 -114 1505 C ATOM 1314 C ALA A 164 14.491 39.378 25.867 1.00 90.74 C ANISOU 1314 C ALA A 164 14654 10093 9729 452 -198 1617 C ATOM 1315 O ALA A 164 14.772 40.538 26.192 1.00 80.97 O ANISOU 1315 O ALA A 164 13367 8843 8553 601 -164 1784 O ATOM 1316 CB ALA A 164 14.381 37.601 27.643 1.00 88.57 C ANISOU 1316 CB ALA A 164 14466 9506 9681 347 124 1368 C ATOM 1317 N LEU A 165 14.970 38.818 24.752 1.00 92.56 N ANISOU 1317 N LEU A 165 15026 10444 9697 369 -306 1525 N ATOM 1318 CA LEU A 165 15.779 39.605 23.826 1.00 87.03 C ANISOU 1318 CA LEU A 165 14418 9884 8766 449 -401 1635 C ATOM 1319 C LEU A 165 14.960 40.724 23.197 1.00 89.79 C ANISOU 1319 C LEU A 165 14556 10395 9166 487 -609 1827 C ATOM 1320 O LEU A 165 15.478 41.821 22.958 1.00 97.37 O ANISOU 1320 O LEU A 165 15525 11406 10067 614 -634 1998 O ATOM 1321 CB LEU A 165 16.377 38.707 22.745 1.00 87.01 C ANISOU 1321 CB LEU A 165 14596 9992 8471 337 -479 1480 C ATOM 1322 CG LEU A 165 17.509 37.788 23.207 1.00 96.41 C ANISOU 1322 CG LEU A 165 16035 11036 9562 333 -279 1313 C ATOM 1323 CD1 LEU A 165 18.011 36.929 22.057 1.00 98.37 C ANISOU 1323 CD1 LEU A 165 16437 11411 9530 216 -376 1152 C ATOM 1324 CD2 LEU A 165 18.641 38.607 23.809 1.00 99.84 C ANISOU 1324 CD2 LEU A 165 16588 11375 9970 509 -114 1423 C ATOM 1325 N ALA A 166 13.677 40.470 22.929 1.00 92.66 N ANISOU 1325 N ALA A 166 14724 10836 9647 380 -759 1805 N ATOM 1326 CA ALA A 166 12.773 41.516 22.463 1.00 95.35 C ANISOU 1326 CA ALA A 166 14837 11312 10078 419 -953 1989 C ATOM 1327 C ALA A 166 12.488 42.550 23.536 1.00110.61 C ANISOU 1327 C ALA A 166 16622 13118 12286 562 -851 2145 C ATOM 1328 O ALA A 166 11.669 43.450 23.311 1.00111.61 O ANISOU 1328 O ALA A 166 16539 13329 12539 604 -997 2300 O ATOM 1329 CB ALA A 166 11.459 40.901 21.970 1.00 80.33 C ANISOU 1329 CB ALA A 166 12760 9519 8243 264 -1130 1902 C ATOM 1330 N CYS A 167 13.148 42.437 24.686 1.00112.17 N ANISOU 1330 N CYS A 167 16920 13120 12578 637 -607 2104 N ATOM 1331 CA CYS A 167 12.916 43.313 25.821 1.00111.74 C ANISOU 1331 CA CYS A 167 16729 12936 12791 767 -484 2221 C ATOM 1332 C CYS A 167 14.178 43.956 26.377 1.00114.88 C ANISOU 1332 C CYS A 167 17276 13229 13144 926 -304 2291 C ATOM 1333 O CYS A 167 14.073 45.008 27.017 1.00116.80 O ANISOU 1333 O CYS A 167 17394 13413 13573 1057 -250 2430 O ATOM 1334 CB CYS A 167 12.217 42.536 26.946 1.00109.91 C ANISOU 1334 CB CYS A 167 16415 12558 12789 698 -345 2095 C ATOM 1335 SG CYS A 167 11.608 43.559 28.294 1.00117.32 S ANISOU 1335 SG CYS A 167 17126 13370 14080 829 -226 2220 S ATOM 1336 N ALA A 168 15.362 43.376 26.157 1.00108.44 N ANISOU 1336 N ALA A 168 16715 12390 12096 920 -210 2194 N ATOM 1337 CA ALA A 168 16.602 43.928 26.685 1.00100.44 C ANISOU 1337 CA ALA A 168 15718 11340 11106 1019 -37 2168 C ATOM 1338 C ALA A 168 17.528 44.499 25.621 1.00104.12 C ANISOU 1338 C ALA A 168 16158 11990 11412 1015 -126 2168 C ATOM 1339 O ALA A 168 18.366 45.344 25.947 1.00108.92 O ANISOU 1339 O ALA A 168 16603 12636 12144 1057 -41 2128 O ATOM 1340 CB ALA A 168 17.365 42.861 27.481 1.00 88.83 C ANISOU 1340 CB ALA A 168 14369 9754 9629 975 174 1944 C ATOM 1341 N ALA A 169 17.403 44.058 24.373 1.00103.19 N ANISOU 1341 N ALA A 169 13356 12210 13641 -1310 -119 2970 N ATOM 1342 CA ALA A 169 18.222 44.537 23.265 1.00 93.87 C ANISOU 1342 CA ALA A 169 12215 10957 12494 -1522 -2 3149 C ATOM 1343 C ALA A 169 17.843 45.935 22.769 1.00 99.01 C ANISOU 1343 C ALA A 169 13002 11351 13267 -1602 -102 3282 C ATOM 1344 O ALA A 169 18.744 46.696 22.392 1.00104.37 O ANISOU 1344 O ALA A 169 13663 11912 14082 -1779 -56 3362 O ATOM 1345 CB ALA A 169 18.164 43.541 22.104 1.00 77.63 C ANISOU 1345 CB ALA A 169 10217 9067 10211 -1561 165 3286 C ATOM 1346 N PRO A 170 16.561 46.316 22.720 1.00 90.85 N ANISOU 1346 N PRO A 170 12103 10223 12191 -1483 -230 3317 N ATOM 1347 CA PRO A 170 16.203 47.656 22.207 1.00 90.71 C ANISOU 1347 CA PRO A 170 12218 9955 12294 -1555 -317 3459 C ATOM 1348 C PRO A 170 16.930 48.788 22.919 1.00 91.56 C ANISOU 1348 C PRO A 170 12255 9860 12674 -1641 -395 3378 C ATOM 1349 O PRO A 170 17.375 49.735 22.252 1.00 92.17 O ANISOU 1349 O PRO A 170 12391 9762 12868 -1800 -371 3524 O ATOM 1350 CB PRO A 170 14.686 47.727 22.434 1.00 92.82 C ANISOU 1350 CB PRO A 170 12601 10189 12478 -1364 -463 3441 C ATOM 1351 CG PRO A 170 14.249 46.329 22.296 1.00 95.58 C ANISOU 1351 CG PRO A 170 12936 10792 12586 -1260 -384 3407 C ATOM 1352 CD PRO A 170 15.352 45.479 22.874 1.00 85.26 C ANISOU 1352 CD PRO A 170 11452 9647 11294 -1293 -277 3269 C ATOM 1353 N PRO A 171 17.073 48.765 24.254 1.00 87.19 N ANISOU 1353 N PRO A 171 11575 9322 12233 -1547 -488 3151 N ATOM 1354 CA PRO A 171 17.834 49.851 24.900 1.00 78.60 C ANISOU 1354 CA PRO A 171 10410 8048 11406 -1647 -551 3066 C ATOM 1355 C PRO A 171 19.283 49.941 24.447 1.00 96.50 C ANISOU 1355 C PRO A 171 12588 10330 13747 -1865 -402 3126 C ATOM 1356 O PRO A 171 19.880 51.020 24.551 1.00114.83 O ANISOU 1356 O PRO A 171 14895 12458 16278 -1996 -431 3132 O ATOM 1357 CB PRO A 171 17.733 49.518 26.394 1.00 83.62 C ANISOU 1357 CB PRO A 171 10904 8773 12096 -1494 -655 2801 C ATOM 1358 CG PRO A 171 16.498 48.716 26.514 1.00 87.86 C ANISOU 1358 CG PRO A 171 11507 9437 12441 -1291 -712 2776 C ATOM 1359 CD PRO A 171 16.454 47.888 25.269 1.00 86.68 C ANISOU 1359 CD PRO A 171 11437 9421 12075 -1342 -558 2960 C ATOM 1360 N LEU A 172 19.868 48.853 23.946 1.00 93.17 N ANISOU 1360 N LEU A 172 12106 10131 13164 -1909 -241 3169 N ATOM 1361 CA LEU A 172 21.240 48.892 23.455 1.00 92.18 C ANISOU 1361 CA LEU A 172 11895 10037 13092 -2114 -93 3234 C ATOM 1362 C LEU A 172 21.354 49.454 22.045 1.00100.50 C ANISOU 1362 C LEU A 172 13084 10975 14125 -2280 -12 3492 C ATOM 1363 O LEU A 172 22.476 49.684 21.581 1.00109.92 O ANISOU 1363 O LEU A 172 14220 12160 15383 -2469 100 3563 O ATOM 1364 CB LEU A 172 21.857 47.491 23.484 1.00 80.76 C ANISOU 1364 CB LEU A 172 10324 8878 11484 -2092 54 3177 C ATOM 1365 CG LEU A 172 21.913 46.767 24.829 1.00 76.77 C ANISOU 1365 CG LEU A 172 9660 8529 10980 -1936 6 2937 C ATOM 1366 CD1 LEU A 172 22.592 45.416 24.674 1.00 78.47 C ANISOU 1366 CD1 LEU A 172 9764 9011 11038 -1931 174 2918 C ATOM 1367 CD2 LEU A 172 22.630 47.613 25.864 1.00 68.65 C ANISOU 1367 CD2 LEU A 172 8502 7397 10184 -1989 -77 2780 C ATOM 1368 N VAL A 173 20.236 49.680 21.353 1.00100.30 N ANISOU 1368 N VAL A 173 13230 10870 14007 -2216 -64 3636 N ATOM 1369 CA VAL A 173 20.283 50.078 19.950 1.00 98.62 C ANISOU 1369 CA VAL A 173 13142 10587 13740 -2361 23 3894 C ATOM 1370 C VAL A 173 19.419 51.307 19.689 1.00 98.13 C ANISOU 1370 C VAL A 173 13238 10261 13785 -2345 -106 4012 C ATOM 1371 O VAL A 173 19.208 51.690 18.533 1.00101.39 O ANISOU 1371 O VAL A 173 13774 10609 14142 -2433 -56 4241 O ATOM 1372 CB VAL A 173 19.866 48.913 19.033 1.00100.01 C ANISOU 1372 CB VAL A 173 13371 10991 13639 -2318 141 4001 C ATOM 1373 CG1 VAL A 173 20.906 47.802 19.075 1.00 99.79 C ANISOU 1373 CG1 VAL A 173 13193 11199 13523 -2373 299 3925 C ATOM 1374 CG2 VAL A 173 18.501 48.382 19.436 1.00 99.81 C ANISOU 1374 CG2 VAL A 173 13413 11032 13479 -2093 37 3925 C ATOM 1375 N GLY A 174 18.906 51.932 20.745 1.00 89.33 N ANISOU 1375 N GLY A 174 12119 8999 12822 -2232 -270 3861 N ATOM 1376 CA GLY A 174 18.267 53.226 20.619 1.00 89.96 C ANISOU 1376 CA GLY A 174 12330 8799 13053 -2231 -391 3954 C ATOM 1377 C GLY A 174 16.775 53.300 20.882 1.00103.92 C ANISOU 1377 C GLY A 174 14213 10523 14750 -2021 -538 3935 C ATOM 1378 O GLY A 174 16.177 54.350 20.620 1.00114.83 O ANISOU 1378 O GLY A 174 15719 11675 16236 -2015 -627 4046 O ATOM 1379 N TRP A 175 16.147 52.237 21.375 1.00100.62 N ANISOU 1379 N TRP A 175 13759 10314 14160 -1848 -563 3806 N ATOM 1380 CA TRP A 175 14.767 52.300 21.848 1.00 95.30 C ANISOU 1380 CA TRP A 175 13169 9607 13434 -1638 -718 3745 C ATOM 1381 C TRP A 175 14.815 52.214 23.368 1.00 97.41 C ANISOU 1381 C TRP A 175 13305 9889 13818 -1521 -830 3465 C ATOM 1382 O TRP A 175 15.110 51.151 23.923 1.00 91.37 O ANISOU 1382 O TRP A 175 12417 9346 12954 -1462 -783 3320 O ATOM 1383 CB TRP A 175 13.906 51.190 21.250 1.00 98.63 C ANISOU 1383 CB TRP A 175 13655 10254 13566 -1525 -669 3813 C ATOM 1384 CG TRP A 175 12.436 51.482 21.350 1.00101.22 C ANISOU 1384 CG TRP A 175 14111 10518 13832 -1346 -816 3831 C ATOM 1385 CD1 TRP A 175 11.859 52.695 21.589 1.00101.26 C ANISOU 1385 CD1 TRP A 175 14204 10270 14001 -1303 -959 3857 C ATOM 1386 CD2 TRP A 175 11.359 50.544 21.224 1.00 99.60 C ANISOU 1386 CD2 TRP A 175 13956 10503 13382 -1185 -832 3820 C ATOM 1387 NE1 TRP A 175 10.491 52.573 21.615 1.00 99.70 N ANISOU 1387 NE1 TRP A 175 14106 10102 13672 -1121 -1065 3867 N ATOM 1388 CE2 TRP A 175 10.158 51.263 21.395 1.00 97.94 C ANISOU 1388 CE2 TRP A 175 13863 10153 13196 -1049 -991 3843 C ATOM 1389 CE3 TRP A 175 11.292 49.168 20.983 1.00 94.93 C ANISOU 1389 CE3 TRP A 175 13324 10186 12559 -1144 -723 3791 C ATOM 1390 CZ2 TRP A 175 8.907 50.653 21.331 1.00 94.04 C ANISOU 1390 CZ2 TRP A 175 13441 9795 12494 -878 -1047 3838 C ATOM 1391 CZ3 TRP A 175 10.048 48.565 20.921 1.00 93.21 C ANISOU 1391 CZ3 TRP A 175 13181 10094 12142 -979 -776 3782 C ATOM 1392 CH2 TRP A 175 8.873 49.307 21.094 1.00 92.37 C ANISOU 1392 CH2 TRP A 175 13186 9854 12056 -850 -938 3806 C ATOM 1393 N SER A 176 14.524 53.337 24.031 1.00105.87 N ANISOU 1393 N SER A 176 14400 10725 15099 -1488 -976 3392 N ATOM 1394 CA SER A 176 14.813 53.532 25.449 1.00107.07 C ANISOU 1394 CA SER A 176 14413 10853 15416 -1427 -1077 3130 C ATOM 1395 C SER A 176 16.318 53.420 25.676 1.00104.25 C ANISOU 1395 C SER A 176 13896 10549 15164 -1599 -963 3058 C ATOM 1396 O SER A 176 17.097 53.527 24.722 1.00104.32 O ANISOU 1396 O SER A 176 13927 10539 15172 -1779 -829 3225 O ATOM 1397 CB SER A 176 14.042 52.537 26.322 1.00101.41 C ANISOU 1397 CB SER A 176 13637 10345 14550 -1210 -1151 2950 C ATOM 1398 OG SER A 176 14.160 52.865 27.696 1.00103.96 O ANISOU 1398 OG SER A 176 13837 10629 15035 -1137 -1272 2706 O ATOM 1399 N ARG A 177 16.742 53.211 26.920 1.00 92.29 N ANISOU 1399 N ARG A 177 12217 9112 13737 -1547 -1014 2815 N ATOM 1400 CA ARG A 177 18.165 53.193 27.237 1.00 90.61 C ANISOU 1400 CA ARG A 177 11841 8949 13637 -1705 -919 2731 C ATOM 1401 C ARG A 177 18.346 52.677 28.660 1.00 91.78 C ANISOU 1401 C ARG A 177 11806 9254 13811 -1586 -985 2456 C ATOM 1402 O ARG A 177 17.396 52.611 29.445 1.00 96.24 O ANISOU 1402 O ARG A 177 12377 9831 14358 -1400 -1123 2328 O ATOM 1403 CB ARG A 177 18.788 54.581 27.086 1.00 84.67 C ANISOU 1403 CB ARG A 177 11113 7918 13139 -1884 -935 2778 C ATOM 1404 CG ARG A 177 18.119 55.631 27.949 1.00 82.64 C ANISOU 1404 CG ARG A 177 10887 7437 13076 -1796 -1117 2647 C ATOM 1405 CD ARG A 177 18.854 56.951 27.895 1.00 92.18 C ANISOU 1405 CD ARG A 177 12098 8375 14552 -1984 -1119 2667 C ATOM 1406 NE ARG A 177 18.325 57.884 28.882 1.00 95.35 N ANISOU 1406 NE ARG A 177 12498 8581 15151 -1899 -1288 2496 N ATOM 1407 CZ ARG A 177 18.824 59.093 29.110 1.00 93.16 C ANISOU 1407 CZ ARG A 177 12212 8049 15134 -2031 -1321 2456 C ATOM 1408 NH1 ARG A 177 19.870 59.522 28.418 1.00101.94 N ANISOU 1408 NH1 ARG A 177 13318 9073 16340 -2259 -1197 2580 N ATOM 1409 NH2 ARG A 177 18.275 59.872 30.032 1.00 94.28 N ANISOU 1409 NH2 ARG A 177 12351 8027 15445 -1939 -1475 2287 N ATOM 1410 N TYR A 178 19.588 52.322 28.984 1.00 85.90 N ANISOU 1410 N TYR A 178 10892 8638 13108 -1695 -885 2371 N ATOM 1411 CA TYR A 178 19.966 51.901 30.328 1.00 87.76 C ANISOU 1411 CA TYR A 178 10929 9030 13385 -1609 -932 2117 C ATOM 1412 C TYR A 178 20.693 53.038 31.031 1.00 85.13 C ANISOU 1412 C TYR A 178 10501 8527 13316 -1727 -994 1984 C ATOM 1413 O TYR A 178 21.685 53.560 30.513 1.00103.94 O ANISOU 1413 O TYR A 178 12866 10821 15807 -1932 -900 2064 O ATOM 1414 CB TYR A 178 20.861 50.660 30.293 1.00 91.60 C ANISOU 1414 CB TYR A 178 11273 9801 13729 -1634 -776 2099 C ATOM 1415 CG TYR A 178 20.169 49.395 29.841 1.00 87.03 C ANISOU 1415 CG TYR A 178 10754 9422 12893 -1498 -715 2176 C ATOM 1416 CD1 TYR A 178 19.128 48.848 30.580 1.00 76.77 C ANISOU 1416 CD1 TYR A 178 9454 8218 11497 -1277 -824 2060 C ATOM 1417 CD2 TYR A 178 20.569 48.737 28.686 1.00 89.63 C ANISOU 1417 CD2 TYR A 178 11134 9846 13074 -1594 -547 2359 C ATOM 1418 CE1 TYR A 178 18.496 47.690 30.172 1.00 84.06 C ANISOU 1418 CE1 TYR A 178 10432 9320 12190 -1160 -764 2125 C ATOM 1419 CE2 TYR A 178 19.945 47.577 28.272 1.00 91.78 C ANISOU 1419 CE2 TYR A 178 11459 10298 13116 -1476 -485 2418 C ATOM 1420 CZ TYR A 178 18.909 47.059 29.018 1.00 87.91 C ANISOU 1420 CZ TYR A 178 10970 9892 12539 -1262 -593 2301 C ATOM 1421 OH TYR A 178 18.284 45.904 28.608 1.00 81.35 O ANISOU 1421 OH TYR A 178 10191 9235 11482 -1152 -526 2355 O ATOM 1422 N ILE A 179 20.196 53.423 32.203 1.00 74.85 N ANISOU 1422 N ILE A 179 9137 7186 12118 -1601 -1150 1777 N ATOM 1423 CA ILE A 179 20.851 54.436 33.030 1.00 84.80 C ANISOU 1423 CA ILE A 179 10284 8310 13626 -1698 -1216 1609 C ATOM 1424 C ILE A 179 20.797 53.995 34.484 1.00 72.83 C ANISOU 1424 C ILE A 179 8580 6979 12113 -1548 -1309 1338 C ATOM 1425 O ILE A 179 19.952 53.175 34.870 1.00 79.28 O ANISOU 1425 O ILE A 179 9397 7953 12771 -1348 -1365 1289 O ATOM 1426 CB ILE A 179 20.201 55.830 32.874 1.00 84.12 C ANISOU 1426 CB ILE A 179 10350 7883 13730 -1726 -1336 1649 C ATOM 1427 CG1 ILE A 179 18.743 55.811 33.332 1.00 81.21 C ANISOU 1427 CG1 ILE A 179 10073 7482 13301 -1495 -1496 1590 C ATOM 1428 CG2 ILE A 179 20.310 56.331 31.435 1.00 88.90 C ANISOU 1428 CG2 ILE A 179 11133 8301 14342 -1883 -1240 1929 C ATOM 1429 CD1 ILE A 179 18.069 57.164 33.235 1.00 85.33 C ANISOU 1429 CD1 ILE A 179 10739 7671 14010 -1504 -1617 1622 C ATOM 1430 N PRO A 180 21.710 54.503 35.313 1.00 74.10 N ANISOU 1430 N PRO A 180 8568 7138 12447 -1644 -1323 1159 N ATOM 1431 CA PRO A 180 21.650 54.186 36.747 1.00 72.97 C ANISOU 1431 CA PRO A 180 8236 7171 12318 -1503 -1422 894 C ATOM 1432 C PRO A 180 20.354 54.690 37.367 1.00 87.36 C ANISOU 1432 C PRO A 180 10139 8867 14188 -1328 -1611 793 C ATOM 1433 O PRO A 180 19.923 55.818 37.117 1.00108.83 O ANISOU 1433 O PRO A 180 12990 11299 17062 -1378 -1690 830 O ATOM 1434 CB PRO A 180 22.873 54.909 37.324 1.00 75.01 C ANISOU 1434 CB PRO A 180 8324 7396 12781 -1680 -1399 747 C ATOM 1435 CG PRO A 180 23.803 55.062 36.177 1.00 76.48 C ANISOU 1435 CG PRO A 180 8565 7510 12982 -1901 -1238 944 C ATOM 1436 CD PRO A 180 22.939 55.239 34.963 1.00 79.67 C ANISOU 1436 CD PRO A 180 9224 7730 13319 -1892 -1229 1192 C ATOM 1437 N GLU A 181 19.735 53.841 38.181 1.00 71.28 N ANISOU 1437 N GLU A 181 8021 7048 12016 -1121 -1682 667 N ATOM 1438 CA GLU A 181 18.465 54.136 38.826 1.00 79.51 C ANISOU 1438 CA GLU A 181 9123 8019 13066 -932 -1861 563 C ATOM 1439 C GLU A 181 18.642 54.277 40.332 1.00 82.35 C ANISOU 1439 C GLU A 181 9270 8497 13523 -854 -1971 272 C ATOM 1440 O GLU A 181 19.639 53.834 40.909 1.00 91.30 O ANISOU 1440 O GLU A 181 10199 9833 14658 -904 -1903 159 O ATOM 1441 CB GLU A 181 17.427 53.047 38.525 1.00 80.96 C ANISOU 1441 CB GLU A 181 9403 8359 13001 -741 -1865 659 C ATOM 1442 CG GLU A 181 17.948 51.617 38.640 1.00112.57 C ANISOU 1442 CG GLU A 181 13273 12687 16812 -693 -1742 659 C ATOM 1443 CD GLU A 181 17.349 50.855 39.811 1.00125.94 C ANISOU 1443 CD GLU A 181 14840 14609 18404 -473 -1840 476 C ATOM 1444 OE1 GLU A 181 16.764 51.496 40.709 1.00136.22 O ANISOU 1444 OE1 GLU A 181 16109 15840 19810 -379 -2003 309 O ATOM 1445 OE2 GLU A 181 17.464 49.610 39.829 1.00115.50 O ANISOU 1445 OE2 GLU A 181 13449 13536 16899 -393 -1750 501 O ATOM 1446 N GLY A 182 17.648 54.905 40.960 1.00 79.32 N ANISOU 1446 N GLY A 182 8932 7990 13216 -726 -2144 153 N ATOM 1447 CA GLY A 182 17.614 55.084 42.400 1.00 71.13 C ANISOU 1447 CA GLY A 182 7705 7058 12263 -631 -2270 -127 C ATOM 1448 C GLY A 182 18.871 55.683 42.992 1.00 71.18 C ANISOU 1448 C GLY A 182 7522 7065 12457 -801 -2236 -287 C ATOM 1449 O GLY A 182 19.197 56.847 42.740 1.00 93.66 O ANISOU 1449 O GLY A 182 10427 9647 15512 -957 -2247 -288 O ATOM 1450 N MET A 183 19.586 54.888 43.787 1.00 72.41 N ANISOU 1450 N MET A 183 7448 7523 12540 -771 -2192 -423 N ATOM 1451 CA MET A 183 20.851 55.295 44.382 1.00 71.85 C ANISOU 1451 CA MET A 183 7170 7513 12616 -928 -2146 -579 C ATOM 1452 C MET A 183 22.020 55.183 43.409 1.00 72.92 C ANISOU 1452 C MET A 183 7315 7635 12754 -1143 -1959 -410 C ATOM 1453 O MET A 183 23.180 55.241 43.838 1.00 82.73 O ANISOU 1453 O MET A 183 8367 8997 14069 -1269 -1891 -518 O ATOM 1454 CB MET A 183 21.118 54.478 45.648 1.00 79.44 C ANISOU 1454 CB MET A 183 7871 8823 13488 -798 -2176 -787 C ATOM 1455 CG MET A 183 20.078 54.708 46.739 1.00 83.23 C ANISOU 1455 CG MET A 183 8308 9326 13989 -604 -2368 -986 C ATOM 1456 SD MET A 183 20.086 53.450 48.030 1.00 84.55 S ANISOU 1456 SD MET A 183 8214 9933 13979 -399 -2398 -1160 S ATOM 1457 CE MET A 183 21.665 53.761 48.814 1.00 78.14 C ANISOU 1457 CE MET A 183 7110 9278 13302 -569 -2333 -1352 C ATOM 1458 N GLN A 184 21.726 55.016 42.118 1.00 72.71 N ANISOU 1458 N GLN A 184 7503 7480 12645 -1184 -1877 -150 N ATOM 1459 CA GLN A 184 22.692 55.114 41.027 1.00 85.26 C ANISOU 1459 CA GLN A 184 9147 8994 14255 -1400 -1712 36 C ATOM 1460 C GLN A 184 23.734 54.005 41.052 1.00 92.06 C ANISOU 1460 C GLN A 184 9836 10164 14977 -1434 -1561 50 C ATOM 1461 O GLN A 184 24.811 54.158 40.467 1.00101.89 O ANISOU 1461 O GLN A 184 11051 11393 16271 -1630 -1429 133 O ATOM 1462 CB GLN A 184 23.397 56.477 41.025 1.00 94.64 C ANISOU 1462 CB GLN A 184 10323 9932 15706 -1615 -1719 -26 C ATOM 1463 CG GLN A 184 22.468 57.684 41.022 1.00 78.31 C ANISOU 1463 CG GLN A 184 8416 7531 13807 -1596 -1861 -46 C ATOM 1464 CD GLN A 184 21.494 57.675 39.860 1.00 82.45 C ANISOU 1464 CD GLN A 184 9209 7878 14241 -1543 -1858 210 C ATOM 1465 OE1 GLN A 184 21.867 57.945 38.718 1.00 82.16 O ANISOU 1465 OE1 GLN A 184 9301 7694 14223 -1698 -1749 425 O ATOM 1466 NE2 GLN A 184 20.237 57.360 40.147 1.00 83.35 N ANISOU 1466 NE2 GLN A 184 9402 8017 14250 -1324 -1977 190 N ATOM 1467 N CYS A 185 23.443 52.888 41.715 1.00 92.53 N ANISOU 1467 N CYS A 185 9782 10508 14865 -1245 -1574 -27 N ATOM 1468 CA CYS A 185 24.395 51.791 41.808 1.00 83.16 C ANISOU 1468 CA CYS A 185 8426 9624 13547 -1255 -1431 -18 C ATOM 1469 C CYS A 185 24.058 50.621 40.894 1.00 88.28 C ANISOU 1469 C CYS A 185 9192 10381 13969 -1177 -1319 194 C ATOM 1470 O CYS A 185 24.931 49.784 40.641 1.00 95.23 O ANISOU 1470 O CYS A 185 9972 11460 14749 -1224 -1169 254 O ATOM 1471 CB CYS A 185 24.496 51.297 43.256 1.00 74.53 C ANISOU 1471 CB CYS A 185 7088 8805 12427 -1108 -1503 -257 C ATOM 1472 SG CYS A 185 25.299 52.476 44.372 1.00 81.42 S ANISOU 1472 SG CYS A 185 7751 9640 13546 -1235 -1588 -527 S ATOM 1473 N SER A 186 22.826 50.547 40.396 1.00 81.00 N ANISOU 1473 N SER A 186 8473 9338 12965 -1062 -1384 302 N ATOM 1474 CA SER A 186 22.430 49.541 39.423 1.00 85.63 C ANISOU 1474 CA SER A 186 9193 9998 13344 -1005 -1278 507 C ATOM 1475 C SER A 186 21.699 50.218 38.272 1.00 84.20 C ANISOU 1475 C SER A 186 9274 9535 13183 -1067 -1297 698 C ATOM 1476 O SER A 186 21.077 51.270 38.444 1.00 85.92 O ANISOU 1476 O SER A 186 9582 9525 13539 -1064 -1431 653 O ATOM 1477 CB SER A 186 21.548 48.451 40.056 1.00 87.86 C ANISOU 1477 CB SER A 186 9439 10495 13449 -758 -1331 443 C ATOM 1478 OG SER A 186 20.685 48.990 41.041 1.00103.01 O ANISOU 1478 OG SER A 186 11338 12359 15442 -624 -1521 272 O ATOM 1479 N CYS A 187 21.788 49.610 37.094 1.00 80.96 N ANISOU 1479 N CYS A 187 8982 9147 12634 -1121 -1158 913 N ATOM 1480 CA CYS A 187 21.252 50.185 35.871 1.00 74.45 C ANISOU 1480 CA CYS A 187 8393 8084 11812 -1201 -1147 1122 C ATOM 1481 C CYS A 187 20.008 49.435 35.418 1.00 83.35 C ANISOU 1481 C CYS A 187 9671 9259 12737 -1032 -1169 1227 C ATOM 1482 O CYS A 187 19.861 48.234 35.655 1.00 92.70 O ANISOU 1482 O CYS A 187 10790 10682 13749 -905 -1118 1202 O ATOM 1483 CB CYS A 187 22.311 50.175 34.762 1.00 73.10 C ANISOU 1483 CB CYS A 187 8246 7890 11638 -1416 -969 1299 C ATOM 1484 SG CYS A 187 23.596 51.425 35.003 1.00 89.24 S ANISOU 1484 SG CYS A 187 10181 9779 13948 -1656 -956 1221 S ATOM 1485 N GLY A 188 19.111 50.161 34.763 1.00 78.31 N ANISOU 1485 N GLY A 188 9236 8394 12126 -1031 -1243 1345 N ATOM 1486 CA GLY A 188 17.882 49.581 34.276 1.00 63.54 C ANISOU 1486 CA GLY A 188 7520 6553 10070 -882 -1271 1449 C ATOM 1487 C GLY A 188 17.259 50.430 33.192 1.00 75.23 C ANISOU 1487 C GLY A 188 9223 7780 11580 -951 -1295 1644 C ATOM 1488 O GLY A 188 17.838 51.422 32.744 1.00 85.07 O ANISOU 1488 O GLY A 188 10509 8825 12989 -1123 -1274 1715 O ATOM 1489 N ILE A 189 16.059 50.022 32.775 1.00 79.16 N ANISOU 1489 N ILE A 189 9865 8297 11916 -813 -1337 1731 N ATOM 1490 CA ILE A 189 15.342 50.732 31.723 1.00 81.86 C ANISOU 1490 CA ILE A 189 10421 8426 12254 -853 -1361 1929 C ATOM 1491 C ILE A 189 14.946 52.118 32.211 1.00 88.80 C ANISOU 1491 C ILE A 189 11348 9039 13354 -848 -1521 1858 C ATOM 1492 O ILE A 189 14.514 52.296 33.358 1.00 93.14 O ANISOU 1492 O ILE A 189 11819 9599 13971 -717 -1661 1657 O ATOM 1493 CB ILE A 189 14.115 49.918 31.277 1.00 79.50 C ANISOU 1493 CB ILE A 189 10246 8240 11720 -692 -1375 2015 C ATOM 1494 CG1 ILE A 189 14.562 48.681 30.495 1.00 79.42 C ANISOU 1494 CG1 ILE A 189 10222 8446 11507 -738 -1190 2127 C ATOM 1495 CG2 ILE A 189 13.164 50.768 30.444 1.00 69.60 C ANISOU 1495 CG2 ILE A 189 9203 6768 10473 -689 -1445 2183 C ATOM 1496 CD1 ILE A 189 13.424 47.801 30.042 1.00 77.20 C ANISOU 1496 CD1 ILE A 189 10052 8294 10988 -595 -1187 2201 C ATOM 1497 N ASP A 190 15.098 53.111 31.336 1.00 91.32 N ANISOU 1497 N ASP A 190 11794 9118 13787 -993 -1499 2024 N ATOM 1498 CA ASP A 190 14.808 54.498 31.678 1.00 85.43 C ANISOU 1498 CA ASP A 190 11105 8087 13269 -1011 -1632 1978 C ATOM 1499 C ASP A 190 13.306 54.752 31.601 1.00 90.30 C ANISOU 1499 C ASP A 190 11878 8612 13818 -833 -1768 2021 C ATOM 1500 O ASP A 190 12.710 54.676 30.520 1.00 94.00 O ANISOU 1500 O ASP A 190 12511 9045 14161 -830 -1728 2237 O ATOM 1501 CB ASP A 190 15.567 55.437 30.742 1.00 86.52 C ANISOU 1501 CB ASP A 190 11318 7999 13554 -1236 -1544 2153 C ATOM 1502 CG ASP A 190 15.334 56.903 31.063 1.00 90.32 C ANISOU 1502 CG ASP A 190 11861 8165 14292 -1267 -1667 2111 C ATOM 1503 OD1 ASP A 190 14.852 57.209 32.173 1.00 91.67 O ANISOU 1503 OD1 ASP A 190 11971 8305 14555 -1140 -1813 1902 O ATOM 1504 OD2 ASP A 190 15.646 57.753 30.201 1.00 91.39 O ANISOU 1504 OD2 ASP A 190 12102 8081 14541 -1422 -1615 2287 O ATOM 1505 N TYR A 191 12.697 55.050 32.754 1.00 88.59 N ANISOU 1505 N TYR A 191 11607 8372 13682 -684 -1930 1814 N ATOM 1506 CA TYR A 191 11.303 55.475 32.804 1.00 97.09 C ANISOU 1506 CA TYR A 191 12823 9336 14732 -517 -2078 1832 C ATOM 1507 C TYR A 191 11.118 56.680 33.724 1.00103.17 C ANISOU 1507 C TYR A 191 13566 9881 15752 -488 -2233 1664 C ATOM 1508 O TYR A 191 9.984 56.993 34.106 1.00114.95 O ANISOU 1508 O TYR A 191 15131 11309 17237 -322 -2379 1611 O ATOM 1509 CB TYR A 191 10.389 54.326 33.250 1.00 95.72 C ANISOU 1509 CB TYR A 191 12624 9419 14324 -307 -2128 1752 C ATOM 1510 CG TYR A 191 10.834 53.629 34.517 1.00 95.78 C ANISOU 1510 CG TYR A 191 12419 9644 14328 -235 -2152 1503 C ATOM 1511 CD1 TYR A 191 10.474 54.121 35.765 1.00101.04 C ANISOU 1511 CD1 TYR A 191 12997 10272 15122 -122 -2314 1274 C ATOM 1512 CD2 TYR A 191 11.605 52.475 34.466 1.00 90.80 C ANISOU 1512 CD2 TYR A 191 11672 9263 13565 -277 -2012 1498 C ATOM 1513 CE1 TYR A 191 10.876 53.489 36.925 1.00 95.10 C ANISOU 1513 CE1 TYR A 191 12041 9732 14359 -55 -2336 1053 C ATOM 1514 CE2 TYR A 191 12.013 51.835 35.623 1.00 89.36 C ANISOU 1514 CE2 TYR A 191 11290 9286 13377 -205 -2031 1282 C ATOM 1515 CZ TYR A 191 11.645 52.348 36.850 1.00 90.76 C ANISOU 1515 CZ TYR A 191 11379 9430 13677 -95 -2194 1063 C ATOM 1516 OH TYR A 191 12.044 51.720 38.008 1.00 95.30 O ANISOU 1516 OH TYR A 191 11747 10222 14241 -20 -2215 854 O ATOM 1517 N TYR A 192 12.207 57.357 34.087 1.00109.15 N ANISOU 1517 N TYR A 192 14220 10525 16729 -648 -2203 1573 N ATOM 1518 CA TYR A 192 12.162 58.555 34.913 1.00108.73 C ANISOU 1518 CA TYR A 192 14136 10243 16934 -650 -2332 1408 C ATOM 1519 C TYR A 192 12.384 59.828 34.110 1.00102.83 C ANISOU 1519 C TYR A 192 13527 9158 16385 -806 -2307 1572 C ATOM 1520 O TYR A 192 12.062 60.917 34.596 1.00100.46 O ANISOU 1520 O TYR A 192 13258 8619 16294 -787 -2422 1478 O ATOM 1521 CB TYR A 192 13.213 58.456 36.028 1.00107.73 C ANISOU 1521 CB TYR A 192 13775 10232 16924 -715 -2325 1158 C ATOM 1522 CG TYR A 192 13.917 57.118 36.028 1.00123.13 C ANISOU 1522 CG TYR A 192 15592 12505 18685 -732 -2197 1151 C ATOM 1523 CD1 TYR A 192 15.049 56.912 35.253 1.00140.28 C ANISOU 1523 CD1 TYR A 192 17741 14707 20853 -929 -2026 1284 C ATOM 1524 CD2 TYR A 192 13.434 56.052 36.778 1.00126.77 C ANISOU 1524 CD2 TYR A 192 15956 13241 18970 -549 -2245 1020 C ATOM 1525 CE1 TYR A 192 15.686 55.691 35.231 1.00150.97 C ANISOU 1525 CE1 TYR A 192 18976 16349 22036 -939 -1905 1281 C ATOM 1526 CE2 TYR A 192 14.071 54.823 36.761 1.00137.07 C ANISOU 1526 CE2 TYR A 192 17143 14830 20107 -559 -2121 1022 C ATOM 1527 CZ TYR A 192 15.198 54.652 35.985 1.00149.90 C ANISOU 1527 CZ TYR A 192 18747 16473 21736 -753 -1951 1152 C ATOM 1528 OH TYR A 192 15.848 53.441 35.948 1.00151.84 O ANISOU 1528 OH TYR A 192 18878 16995 21821 -761 -1822 1157 O ATOM 1529 N THR A 193 12.925 59.708 32.897 1.00 96.03 N ANISOU 1529 N THR A 193 12748 8272 15466 -960 -2157 1813 N ATOM 1530 CA THR A 193 13.112 60.802 31.965 1.00 98.97 C ANISOU 1530 CA THR A 193 13265 8345 15996 -1110 -2114 2015 C ATOM 1531 C THR A 193 12.419 60.483 30.646 1.00102.17 C ANISOU 1531 C THR A 193 13854 8760 16204 -1080 -2054 2308 C ATOM 1532 O THR A 193 12.414 59.325 30.215 1.00103.99 O ANISOU 1532 O THR A 193 14069 9251 16193 -1049 -1968 2380 O ATOM 1533 CB THR A 193 14.600 61.063 31.697 1.00 96.05 C ANISOU 1533 CB THR A 193 12803 7932 15760 -1362 -1975 2038 C ATOM 1534 OG1 THR A 193 15.091 60.103 30.753 1.00 90.70 O ANISOU 1534 OG1 THR A 193 12130 7454 14876 -1442 -1816 2216 O ATOM 1535 CG2 THR A 193 15.395 60.939 32.980 1.00 94.51 C ANISOU 1535 CG2 THR A 193 12384 7851 15674 -1385 -2002 1743 C ATOM 1536 N PRO A 194 11.821 61.478 29.989 1.00100.55 N ANISOU 1536 N PRO A 194 13823 8285 16096 -1085 -2095 2480 N ATOM 1537 CA PRO A 194 11.178 61.264 28.688 1.00 97.50 C ANISOU 1537 CA PRO A 194 13611 7907 15528 -1066 -2037 2772 C ATOM 1538 C PRO A 194 12.142 61.454 27.519 1.00110.71 C ANISOU 1538 C PRO A 194 15325 9516 17223 -1296 -1868 3005 C ATOM 1539 O PRO A 194 11.868 62.205 26.579 1.00126.79 O ANISOU 1539 O PRO A 194 17515 11349 19310 -1352 -1846 3239 O ATOM 1540 CB PRO A 194 10.072 62.322 28.686 1.00102.05 C ANISOU 1540 CB PRO A 194 14338 8218 16218 -947 -2175 2826 C ATOM 1541 CG PRO A 194 10.684 63.460 29.447 1.00 97.93 C ANISOU 1541 CG PRO A 194 13753 7435 16020 -1042 -2228 2669 C ATOM 1542 CD PRO A 194 11.592 62.844 30.495 1.00101.37 C ANISOU 1542 CD PRO A 194 13970 8067 16479 -1085 -2211 2400 C ATOM 1543 N HIS A 195 13.287 60.769 27.575 1.00110.26 N ANISOU 1543 N HIS A 195 15127 9638 17128 -1429 -1746 2947 N ATOM 1544 CA HIS A 195 14.354 60.937 26.593 1.00111.98 C ANISOU 1544 CA HIS A 195 15355 9811 17382 -1662 -1584 3135 C ATOM 1545 C HIS A 195 13.840 60.720 25.174 1.00108.87 C ANISOU 1545 C HIS A 195 15124 9442 16800 -1671 -1505 3444 C ATOM 1546 O HIS A 195 13.799 59.586 24.687 1.00114.75 O ANISOU 1546 O HIS A 195 15853 10452 17294 -1644 -1419 3507 O ATOM 1547 CB HIS A 195 15.507 59.976 26.902 1.00113.89 C ANISOU 1547 CB HIS A 195 15413 10309 17549 -1759 -1469 3015 C ATOM 1548 CG HIS A 195 16.827 60.407 26.342 1.00112.82 C ANISOU 1548 CG HIS A 195 15235 10088 17542 -2015 -1332 3111 C ATOM 1549 ND1 HIS A 195 17.586 59.602 25.520 1.00110.05 N ANISOU 1549 ND1 HIS A 195 14849 9932 17033 -2136 -1167 3243 N ATOM 1550 CD2 HIS A 195 17.528 61.556 26.493 1.00111.79 C ANISOU 1550 CD2 HIS A 195 15089 9701 17683 -2175 -1332 3090 C ATOM 1551 CE1 HIS A 195 18.695 60.237 25.187 1.00109.12 C ANISOU 1551 CE1 HIS A 195 14695 9688 17078 -2359 -1076 3303 C ATOM 1552 NE2 HIS A 195 18.684 61.425 25.764 1.00115.45 N ANISOU 1552 NE2 HIS A 195 15510 10214 18143 -2390 -1172 3213 N ATOM 1553 N GLU A 196 13.442 61.808 24.506 1.00113.21 N ANISOU 1553 N GLU A 196 15827 9717 17470 -1709 -1531 3636 N ATOM 1554 CA GLU A 196 12.831 61.704 23.185 1.00118.20 C ANISOU 1554 CA GLU A 196 16617 10367 17927 -1700 -1472 3934 C ATOM 1555 C GLU A 196 13.793 61.181 22.126 1.00118.17 C ANISOU 1555 C GLU A 196 16591 10500 17809 -1893 -1285 4115 C ATOM 1556 O GLU A 196 13.336 60.662 21.102 1.00121.24 O ANISOU 1556 O GLU A 196 17069 11021 17976 -1872 -1219 4321 O ATOM 1557 CB GLU A 196 12.278 63.062 22.743 1.00127.34 C ANISOU 1557 CB GLU A 196 17934 11188 19263 -1704 -1537 4106 C ATOM 1558 CG GLU A 196 10.911 63.411 23.316 1.00133.25 C ANISOU 1558 CG GLU A 196 18766 11846 20019 -1469 -1711 4030 C ATOM 1559 CD GLU A 196 10.995 64.204 24.605 1.00144.20 C ANISOU 1559 CD GLU A 196 20083 13032 21676 -1432 -1837 3772 C ATOM 1560 OE1 GLU A 196 12.109 64.635 24.971 1.00152.03 O ANISOU 1560 OE1 GLU A 196 20976 13917 22870 -1602 -1788 3674 O ATOM 1561 OE2 GLU A 196 9.945 64.394 25.255 1.00143.89 O ANISOU 1561 OE2 GLU A 196 20083 12947 21643 -1233 -1986 3661 O ATOM 1562 N GLU A 197 15.106 61.310 22.338 1.00117.54 N ANISOU 1562 N GLU A 197 16390 10400 17869 -2081 -1198 4042 N ATOM 1563 CA GLU A 197 16.062 60.816 21.353 1.00116.25 C ANISOU 1563 CA GLU A 197 16196 10372 17599 -2266 -1019 4206 C ATOM 1564 C GLU A 197 15.987 59.305 21.183 1.00112.92 C ANISOU 1564 C GLU A 197 15711 10311 16881 -2192 -945 4174 C ATOM 1565 O GLU A 197 16.372 58.791 20.127 1.00116.96 O ANISOU 1565 O GLU A 197 16244 10959 17238 -2297 -805 4358 O ATOM 1566 CB GLU A 197 17.488 61.218 21.737 1.00116.72 C ANISOU 1566 CB GLU A 197 16123 10357 17867 -2474 -948 4104 C ATOM 1567 CG GLU A 197 17.772 62.713 21.684 1.00122.96 C ANISOU 1567 CG GLU A 197 16978 10786 18955 -2601 -980 4172 C ATOM 1568 CD GLU A 197 17.624 63.385 23.035 1.00131.69 C ANISOU 1568 CD GLU A 197 18021 11722 20292 -2526 -1124 3904 C ATOM 1569 OE1 GLU A 197 16.621 63.118 23.728 1.00126.54 O ANISOU 1569 OE1 GLU A 197 17383 11121 19575 -2310 -1253 3769 O ATOM 1570 OE2 GLU A 197 18.519 64.174 23.408 1.00140.03 O ANISOU 1570 OE2 GLU A 197 19011 12603 21592 -2686 -1106 3823 O ATOM 1571 N THR A 198 15.499 58.583 22.192 1.00105.86 N ANISOU 1571 N THR A 198 14738 9574 15908 -2015 -1031 3944 N ATOM 1572 CA THR A 198 15.392 57.131 22.131 1.00112.72 C ANISOU 1572 CA THR A 198 15544 10775 16510 -1933 -963 3896 C ATOM 1573 C THR A 198 13.960 56.638 22.302 1.00116.78 C ANISOU 1573 C THR A 198 16140 11385 16846 -1698 -1069 3870 C ATOM 1574 O THR A 198 13.747 55.427 22.438 1.00113.26 O ANISOU 1574 O THR A 198 15638 11205 16189 -1604 -1032 3793 O ATOM 1575 CB THR A 198 16.300 56.485 23.183 1.00107.86 C ANISOU 1575 CB THR A 198 14729 10317 15935 -1949 -938 3641 C ATOM 1576 OG1 THR A 198 16.012 57.039 24.473 1.00102.25 O ANISOU 1576 OG1 THR A 198 13962 9487 15403 -1844 -1093 3412 O ATOM 1577 CG2 THR A 198 17.763 56.734 22.844 1.00108.98 C ANISOU 1577 CG2 THR A 198 14782 10431 16193 -2189 -803 3686 C ATOM 1578 N ASN A 199 12.977 57.542 22.298 1.00113.76 N ANISOU 1578 N ASN A 199 15888 10793 16544 -1602 -1197 3932 N ATOM 1579 CA ASN A 199 11.557 57.192 22.370 1.00104.41 C ANISOU 1579 CA ASN A 199 14795 9685 15191 -1383 -1302 3931 C ATOM 1580 C ASN A 199 11.253 56.356 23.614 1.00 93.84 C ANISOU 1580 C ASN A 199 13337 8528 13790 -1217 -1384 3652 C ATOM 1581 O ASN A 199 10.819 55.204 23.538 1.00 97.54 O ANISOU 1581 O ASN A 199 13788 9251 14021 -1118 -1351 3625 O ATOM 1582 CB ASN A 199 11.108 56.468 21.096 1.00101.30 C ANISOU 1582 CB ASN A 199 14496 9470 14523 -1385 -1198 4157 C ATOM 1583 CG ASN A 199 11.337 57.293 19.849 1.00109.26 C ANISOU 1583 CG ASN A 199 15621 10314 15579 -1538 -1121 4445 C ATOM 1584 OD1 ASN A 199 12.421 57.270 19.266 1.00113.97 O ANISOU 1584 OD1 ASN A 199 16172 10924 16207 -1731 -985 4539 O ATOM 1585 ND2 ASN A 199 10.315 58.031 19.433 1.00115.27 N ANISOU 1585 ND2 ASN A 199 16531 10924 16345 -1449 -1209 4594 N ATOM 1586 N ASN A 200 11.489 56.967 24.777 1.00 90.75 N ANISOU 1586 N ASN A 200 12861 8002 13619 -1191 -1491 3442 N ATOM 1587 CA ASN A 200 11.237 56.276 26.036 1.00 92.64 C ANISOU 1587 CA ASN A 200 12975 8404 13819 -1036 -1578 3172 C ATOM 1588 C ASN A 200 9.754 56.006 26.252 1.00 94.69 C ANISOU 1588 C ASN A 200 13323 8724 13930 -807 -1705 3148 C ATOM 1589 O ASN A 200 9.395 54.989 26.856 1.00103.59 O ANISOU 1589 O ASN A 200 14374 10082 14903 -675 -1728 3002 O ATOM 1590 CB ASN A 200 11.795 57.090 27.204 1.00 93.74 C ANISOU 1590 CB ASN A 200 13003 8381 14233 -1065 -1668 2955 C ATOM 1591 CG ASN A 200 13.310 57.073 27.260 1.00 94.33 C ANISOU 1591 CG ASN A 200 12942 8476 14424 -1270 -1544 2913 C ATOM 1592 OD1 ASN A 200 13.976 56.664 26.308 1.00 89.60 O ANISOU 1592 OD1 ASN A 200 12353 7960 13731 -1410 -1390 3077 O ATOM 1593 ND2 ASN A 200 13.863 57.521 28.380 1.00 97.52 N ANISOU 1593 ND2 ASN A 200 13213 8813 15028 -1290 -1610 2688 N ATOM 1594 N GLU A 201 8.881 56.890 25.763 1.00100.57 N ANISOU 1594 N GLU A 201 14225 9271 14714 -757 -1786 3292 N ATOM 1595 CA GLU A 201 7.459 56.764 26.066 1.00100.13 C ANISOU 1595 CA GLU A 201 14249 9256 14539 -534 -1923 3253 C ATOM 1596 C GLU A 201 6.847 55.550 25.377 1.00102.09 C ANISOU 1596 C GLU A 201 14542 9780 14470 -461 -1851 3351 C ATOM 1597 O GLU A 201 6.170 54.738 26.019 1.00103.57 O ANISOU 1597 O GLU A 201 14686 10155 14513 -298 -1915 3206 O ATOM 1598 CB GLU A 201 6.719 58.041 25.671 1.00101.92 C ANISOU 1598 CB GLU A 201 14633 9201 14893 -501 -2019 3397 C ATOM 1599 CG GLU A 201 5.250 58.037 26.061 1.00108.87 C ANISOU 1599 CG GLU A 201 15590 10105 15672 -266 -2174 3345 C ATOM 1600 CD GLU A 201 4.596 59.391 25.889 1.00123.92 C ANISOU 1600 CD GLU A 201 17630 11707 17745 -222 -2282 3450 C ATOM 1601 OE1 GLU A 201 5.328 60.389 25.725 1.00136.52 O ANISOU 1601 OE1 GLU A 201 19239 13052 19579 -367 -2253 3511 O ATOM 1602 OE2 GLU A 201 3.349 59.456 25.916 1.00130.05 O ANISOU 1602 OE2 GLU A 201 18498 12497 18418 -41 -2392 3471 O ATOM 1603 N SER A 202 7.073 55.408 24.069 1.00 99.51 N ANISOU 1603 N SER A 202 14297 9484 14028 -582 -1716 3595 N ATOM 1604 CA SER A 202 6.508 54.276 23.343 1.00 87.53 C ANISOU 1604 CA SER A 202 12823 8227 12208 -527 -1638 3690 C ATOM 1605 C SER A 202 7.092 52.946 23.800 1.00 93.81 C ANISOU 1605 C SER A 202 13474 9291 12880 -530 -1547 3532 C ATOM 1606 O SER A 202 6.436 51.911 23.645 1.00 99.82 O ANISOU 1606 O SER A 202 14246 10278 13404 -427 -1523 3519 O ATOM 1607 CB SER A 202 6.723 54.446 21.838 1.00 88.44 C ANISOU 1607 CB SER A 202 13044 8324 12237 -672 -1505 3981 C ATOM 1608 OG SER A 202 8.046 54.100 21.468 1.00100.03 O ANISOU 1608 OG SER A 202 14423 9850 13734 -865 -1346 4012 O ATOM 1609 N PHE A 203 8.305 52.948 24.356 1.00 96.19 N ANISOU 1609 N PHE A 203 13637 9574 13336 -643 -1493 3412 N ATOM 1610 CA PHE A 203 8.877 51.705 24.861 1.00 96.67 C ANISOU 1610 CA PHE A 203 13553 9886 13293 -634 -1409 3260 C ATOM 1611 C PHE A 203 8.261 51.313 26.198 1.00 94.36 C ANISOU 1611 C PHE A 203 13177 9682 12994 -440 -1544 3013 C ATOM 1612 O PHE A 203 7.964 50.136 26.421 1.00 95.41 O ANISOU 1612 O PHE A 203 13259 10053 12938 -344 -1509 2934 O ATOM 1613 CB PHE A 203 10.395 51.831 24.993 1.00 93.31 C ANISOU 1613 CB PHE A 203 13001 9429 13025 -819 -1302 3221 C ATOM 1614 CG PHE A 203 11.074 50.552 25.397 1.00 89.50 C ANISOU 1614 CG PHE A 203 12368 9206 12432 -820 -1196 3092 C ATOM 1615 CD1 PHE A 203 11.462 49.628 24.442 1.00 84.33 C ANISOU 1615 CD1 PHE A 203 11719 8730 11593 -904 -1023 3218 C ATOM 1616 CD2 PHE A 203 11.324 50.274 26.732 1.00 89.93 C ANISOU 1616 CD2 PHE A 203 12272 9330 12569 -733 -1265 2846 C ATOM 1617 CE1 PHE A 203 12.086 48.451 24.809 1.00 84.05 C ANISOU 1617 CE1 PHE A 203 11548 8924 11463 -898 -920 3103 C ATOM 1618 CE2 PHE A 203 11.947 49.099 27.105 1.00 81.34 C ANISOU 1618 CE2 PHE A 203 11044 8480 11382 -725 -1164 2739 C ATOM 1619 CZ PHE A 203 12.329 48.187 26.143 1.00 82.63 C ANISOU 1619 CZ PHE A 203 11221 8807 11369 -806 -989 2869 C ATOM 1620 N VAL A 204 8.070 52.283 27.096 1.00 97.73 N ANISOU 1620 N VAL A 204 13586 9920 13628 -382 -1697 2887 N ATOM 1621 CA VAL A 204 7.439 51.994 28.381 1.00102.16 C ANISOU 1621 CA VAL A 204 14066 10562 14187 -194 -1837 2653 C ATOM 1622 C VAL A 204 6.025 51.467 28.172 1.00101.49 C ANISOU 1622 C VAL A 204 14087 10594 13879 -15 -1905 2691 C ATOM 1623 O VAL A 204 5.566 50.570 28.890 1.00 85.46 O ANISOU 1623 O VAL A 204 11986 8760 11724 126 -1944 2541 O ATOM 1624 CB VAL A 204 7.458 53.248 29.276 1.00 95.85 C ANISOU 1624 CB VAL A 204 13242 9521 13658 -175 -1988 2523 C ATOM 1625 CG1 VAL A 204 6.595 53.042 30.509 1.00 99.19 C ANISOU 1625 CG1 VAL A 204 13604 10020 14062 36 -2151 2301 C ATOM 1626 CG2 VAL A 204 8.884 53.586 29.679 1.00 88.13 C ANISOU 1626 CG2 VAL A 204 12126 8478 12883 -342 -1921 2436 C ATOM 1627 N ILE A 205 5.318 52.004 27.176 1.00103.25 N ANISOU 1627 N ILE A 205 14477 10707 14045 -19 -1916 2898 N ATOM 1628 CA ILE A 205 3.980 51.513 26.862 1.00 98.48 C ANISOU 1628 CA ILE A 205 13977 10227 13214 138 -1969 2951 C ATOM 1629 C ILE A 205 4.053 50.098 26.302 1.00 98.77 C ANISOU 1629 C ILE A 205 13991 10544 12994 123 -1821 2993 C ATOM 1630 O ILE A 205 3.347 49.193 26.762 1.00 99.40 O ANISOU 1630 O ILE A 205 14042 10817 12907 266 -1855 2883 O ATOM 1631 CB ILE A 205 3.274 52.474 25.890 1.00 89.22 C ANISOU 1631 CB ILE A 205 12983 8874 12045 130 -2008 3175 C ATOM 1632 CG1 ILE A 205 3.047 53.831 26.558 1.00 86.06 C ANISOU 1632 CG1 ILE A 205 12608 8194 11898 177 -2167 3111 C ATOM 1633 CG2 ILE A 205 1.957 51.881 25.419 1.00 79.27 C ANISOU 1633 CG2 ILE A 205 11824 7774 10520 274 -2040 3249 C ATOM 1634 CD1 ILE A 205 2.508 54.884 25.620 1.00 84.12 C ANISOU 1634 CD1 ILE A 205 12530 7738 11695 156 -2196 3343 C ATOM 1635 N TYR A 206 4.909 49.887 25.296 1.00 94.25 N ANISOU 1635 N TYR A 206 13429 9997 12387 -54 -1651 3151 N ATOM 1636 CA TYR A 206 5.155 48.538 24.796 1.00 83.37 C ANISOU 1636 CA TYR A 206 12012 8877 10789 -87 -1494 3174 C ATOM 1637 C TYR A 206 5.646 47.616 25.902 1.00 81.79 C ANISOU 1637 C TYR A 206 11645 8839 10594 -30 -1479 2946 C ATOM 1638 O TYR A 206 5.332 46.420 25.901 1.00 86.03 O ANISOU 1638 O TYR A 206 12153 9601 10932 40 -1415 2899 O ATOM 1639 CB TYR A 206 6.166 48.580 23.648 1.00 83.97 C ANISOU 1639 CB TYR A 206 12105 8935 10867 -300 -1318 3361 C ATOM 1640 CG TYR A 206 6.949 47.297 23.474 1.00 95.10 C ANISOU 1640 CG TYR A 206 13411 10573 12148 -368 -1146 3321 C ATOM 1641 CD1 TYR A 206 6.383 46.192 22.851 1.00 93.06 C ANISOU 1641 CD1 TYR A 206 13194 10536 11629 -324 -1056 3371 C ATOM 1642 CD2 TYR A 206 8.256 47.192 23.932 1.00105.00 C ANISOU 1642 CD2 TYR A 206 14526 11827 13545 -477 -1070 3231 C ATOM 1643 CE1 TYR A 206 7.097 45.016 22.693 1.00 93.31 C ANISOU 1643 CE1 TYR A 206 13134 10767 11553 -383 -893 3331 C ATOM 1644 CE2 TYR A 206 8.976 46.025 23.779 1.00100.12 C ANISOU 1644 CE2 TYR A 206 13813 11416 12814 -531 -910 3198 C ATOM 1645 CZ TYR A 206 8.394 44.941 23.160 1.00 93.67 C ANISOU 1645 CZ TYR A 206 13043 10803 11746 -483 -821 3249 C ATOM 1646 OH TYR A 206 9.121 43.782 23.011 1.00 93.95 O ANISOU 1646 OH TYR A 206 12985 11033 11680 -534 -656 3212 O ATOM 1647 N MET A 207 6.420 48.152 26.846 1.00 89.05 N ANISOU 1647 N MET A 207 12448 9649 11736 -59 -1533 2804 N ATOM 1648 CA MET A 207 6.841 47.370 28.003 1.00 90.90 C ANISOU 1648 CA MET A 207 12515 10037 11987 12 -1537 2583 C ATOM 1649 C MET A 207 5.642 46.956 28.845 1.00 85.58 C ANISOU 1649 C MET A 207 11840 9465 11210 231 -1677 2441 C ATOM 1650 O MET A 207 5.529 45.798 29.264 1.00 79.78 O ANISOU 1650 O MET A 207 11028 8949 10336 315 -1633 2340 O ATOM 1651 CB MET A 207 7.825 48.185 28.843 1.00 96.32 C ANISOU 1651 CB MET A 207 13082 10578 12939 -63 -1585 2460 C ATOM 1652 CG MET A 207 8.507 47.414 29.945 1.00 99.26 C ANISOU 1652 CG MET A 207 13261 11117 13337 -22 -1563 2253 C ATOM 1653 SD MET A 207 9.717 46.262 29.286 1.00109.57 S ANISOU 1653 SD MET A 207 14481 12618 14533 -164 -1321 2324 S ATOM 1654 CE MET A 207 10.515 45.737 30.799 1.00124.35 C ANISOU 1654 CE MET A 207 16115 14632 16501 -103 -1339 2068 C ATOM 1655 N PHE A 208 4.727 47.895 29.093 1.00 93.49 N ANISOU 1655 N PHE A 208 12931 10310 12283 326 -1843 2434 N ATOM 1656 CA PHE A 208 3.601 47.626 29.980 1.00 92.96 C ANISOU 1656 CA PHE A 208 12855 10327 12139 534 -1993 2287 C ATOM 1657 C PHE A 208 2.599 46.675 29.336 1.00 93.03 C ANISOU 1657 C PHE A 208 12958 10521 11869 622 -1950 2370 C ATOM 1658 O PHE A 208 2.095 45.758 29.994 1.00 92.76 O ANISOU 1658 O PHE A 208 12862 10674 11708 755 -1977 2239 O ATOM 1659 CB PHE A 208 2.927 48.943 30.368 1.00 97.59 C ANISOU 1659 CB PHE A 208 13513 10685 12883 607 -2177 2263 C ATOM 1660 CG PHE A 208 2.041 48.842 31.575 1.00113.40 C ANISOU 1660 CG PHE A 208 15461 12751 14874 808 -2347 2062 C ATOM 1661 CD1 PHE A 208 2.573 48.950 32.850 1.00121.92 C ANISOU 1661 CD1 PHE A 208 16378 13835 16110 843 -2418 1844 C ATOM 1662 CD2 PHE A 208 0.675 48.650 31.437 1.00118.83 C ANISOU 1662 CD2 PHE A 208 16253 13504 15391 962 -2437 2090 C ATOM 1663 CE1 PHE A 208 1.760 48.862 33.966 1.00128.21 C ANISOU 1663 CE1 PHE A 208 17118 14702 16893 1028 -2576 1658 C ATOM 1664 CE2 PHE A 208 -0.144 48.561 32.549 1.00120.48 C ANISOU 1664 CE2 PHE A 208 16410 13780 15587 1147 -2595 1905 C ATOM 1665 CZ PHE A 208 0.399 48.667 33.815 1.00125.28 C ANISOU 1665 CZ PHE A 208 16856 14391 16352 1180 -2665 1690 C ATOM 1666 N VAL A 209 2.306 46.869 28.050 1.00 85.92 N ANISOU 1666 N VAL A 209 12200 9579 10867 546 -1880 2586 N ATOM 1667 CA VAL A 209 1.280 46.067 27.387 1.00 84.80 C ANISOU 1667 CA VAL A 209 12153 9608 10457 624 -1847 2667 C ATOM 1668 C VAL A 209 1.801 44.664 27.096 1.00 91.77 C ANISOU 1668 C VAL A 209 12966 10725 11178 571 -1668 2654 C ATOM 1669 O VAL A 209 1.219 43.662 27.528 1.00 94.92 O ANISOU 1669 O VAL A 209 13330 11315 11421 690 -1670 2550 O ATOM 1670 CB VAL A 209 0.800 46.762 26.101 1.00 82.00 C ANISOU 1670 CB VAL A 209 11967 9147 10044 560 -1831 2906 C ATOM 1671 CG1 VAL A 209 -0.072 45.820 25.284 1.00 82.59 C ANISOU 1671 CG1 VAL A 209 12072 9473 9835 614 -1676 2901 C ATOM 1672 CG2 VAL A 209 0.042 48.036 26.437 1.00 80.19 C ANISOU 1672 CG2 VAL A 209 11797 8724 9946 652 -1986 2880 C ATOM 1673 N VAL A 210 2.909 44.574 26.360 1.00 89.07 N ANISOU 1673 N VAL A 210 12602 10368 10872 392 -1507 2761 N ATOM 1674 CA VAL A 210 3.364 43.285 25.849 1.00 75.87 C ANISOU 1674 CA VAL A 210 10887 8908 9034 331 -1320 2782 C ATOM 1675 C VAL A 210 4.012 42.448 26.947 1.00 77.39 C ANISOU 1675 C VAL A 210 10908 9224 9271 379 -1289 2585 C ATOM 1676 O VAL A 210 3.827 41.227 26.998 1.00 81.63 O ANISOU 1676 O VAL A 210 11409 9965 9644 434 -1202 2530 O ATOM 1677 CB VAL A 210 4.317 43.502 24.660 1.00 70.60 C ANISOU 1677 CB VAL A 210 10252 8187 8386 123 -1160 2968 C ATOM 1678 CG1 VAL A 210 4.909 42.182 24.196 1.00 56.10 C ANISOU 1678 CG1 VAL A 210 8355 6562 6399 55 -960 2972 C ATOM 1679 CG2 VAL A 210 3.583 44.188 23.518 1.00 74.58 C ANISOU 1679 CG2 VAL A 210 10922 8605 8808 88 -1179 3176 C ATOM 1680 N HIS A 211 4.773 43.075 27.844 1.00 81.47 N ANISOU 1680 N HIS A 211 11317 9628 10011 360 -1355 2475 N ATOM 1681 CA HIS A 211 5.575 42.336 28.812 1.00 74.82 C ANISOU 1681 CA HIS A 211 10299 8907 9222 384 -1308 2308 C ATOM 1682 C HIS A 211 5.033 42.433 30.235 1.00 73.85 C ANISOU 1682 C HIS A 211 10091 8802 9167 559 -1481 2104 C ATOM 1683 O HIS A 211 5.754 42.121 31.188 1.00 74.73 O ANISOU 1683 O HIS A 211 10043 8980 9372 580 -1474 1958 O ATOM 1684 CB HIS A 211 7.029 42.806 28.760 1.00 66.24 C ANISOU 1684 CB HIS A 211 9121 7727 8321 215 -1224 2327 C ATOM 1685 CG HIS A 211 7.695 42.559 27.442 1.00 78.60 C ANISOU 1685 CG HIS A 211 10741 9309 9813 42 -1038 2511 C ATOM 1686 ND1 HIS A 211 8.528 41.485 27.218 1.00 74.64 N ANISOU 1686 ND1 HIS A 211 10152 8976 9233 -23 -859 2507 N ATOM 1687 CD2 HIS A 211 7.647 43.248 26.277 1.00 91.46 C ANISOU 1687 CD2 HIS A 211 12501 10814 11435 -79 -1003 2707 C ATOM 1688 CE1 HIS A 211 8.967 41.523 25.972 1.00 82.39 C ANISOU 1688 CE1 HIS A 211 11206 9939 10160 -178 -723 2684 C ATOM 1689 NE2 HIS A 211 8.448 42.583 25.380 1.00 89.21 N ANISOU 1689 NE2 HIS A 211 12202 10631 11064 -216 -807 2811 N ATOM 1690 N PHE A 212 3.780 42.852 30.404 1.00 77.95 N ANISOU 1690 N PHE A 212 10707 9274 9636 689 -1635 2091 N ATOM 1691 CA PHE A 212 3.157 42.791 31.721 1.00 89.15 C ANISOU 1691 CA PHE A 212 12046 10745 11084 867 -1793 1896 C ATOM 1692 C PHE A 212 1.671 42.462 31.629 1.00 96.63 C ANISOU 1692 C PHE A 212 13100 11773 11841 1020 -1882 1903 C ATOM 1693 O PHE A 212 1.179 41.602 32.367 1.00 94.75 O ANISOU 1693 O PHE A 212 12796 11706 11499 1155 -1911 1776 O ATOM 1694 CB PHE A 212 3.358 44.100 32.485 1.00 88.22 C ANISOU 1694 CB PHE A 212 11887 10423 11207 872 -1950 1809 C ATOM 1695 CG PHE A 212 2.729 44.097 33.846 1.00 90.87 C ANISOU 1695 CG PHE A 212 12133 10816 11576 1052 -2119 1603 C ATOM 1696 CD1 PHE A 212 3.206 43.257 34.840 1.00 85.35 C ANISOU 1696 CD1 PHE A 212 11261 10293 10876 1113 -2093 1442 C ATOM 1697 CD2 PHE A 212 1.652 44.921 34.130 1.00 91.63 C ANISOU 1697 CD2 PHE A 212 12315 10799 11701 1165 -2301 1573 C ATOM 1698 CE1 PHE A 212 2.626 43.244 36.094 1.00 85.54 C ANISOU 1698 CE1 PHE A 212 11195 10383 10923 1279 -2248 1256 C ATOM 1699 CE2 PHE A 212 1.067 44.912 35.382 1.00 89.82 C ANISOU 1699 CE2 PHE A 212 11999 10633 11497 1332 -2457 1380 C ATOM 1700 CZ PHE A 212 1.555 44.072 36.366 1.00 85.93 C ANISOU 1700 CZ PHE A 212 11329 10321 10999 1386 -2431 1221 C ATOM 1701 N ILE A 213 0.946 43.134 30.731 1.00 96.33 N ANISOU 1701 N ILE A 213 13226 11623 11753 1001 -1922 2053 N ATOM 1702 CA ILE A 213 -0.483 42.865 30.582 1.00 93.85 C ANISOU 1702 CA ILE A 213 12959 11435 11264 1120 -1912 2009 C ATOM 1703 C ILE A 213 -0.702 41.505 29.930 1.00 93.39 C ANISOU 1703 C ILE A 213 12883 11616 10983 1103 -1712 2034 C ATOM 1704 O ILE A 213 -1.459 40.668 30.438 1.00 97.19 O ANISOU 1704 O ILE A 213 13239 12304 11386 1164 -1644 1898 O ATOM 1705 CB ILE A 213 -1.166 43.991 29.786 1.00 90.80 C ANISOU 1705 CB ILE A 213 12699 10901 10900 1095 -1940 2125 C ATOM 1706 CG1 ILE A 213 -1.099 45.311 30.558 1.00 93.08 C ANISOU 1706 CG1 ILE A 213 12991 10956 11418 1130 -2136 2070 C ATOM 1707 CG2 ILE A 213 -2.613 43.626 29.482 1.00 75.53 C ANISOU 1707 CG2 ILE A 213 10738 9161 8800 1171 -1836 2068 C ATOM 1708 CD1 ILE A 213 -1.867 45.291 31.862 1.00 88.29 C ANISOU 1708 CD1 ILE A 213 12259 10450 10838 1271 -2202 1823 C ATOM 1709 N ILE A 214 -0.041 41.267 28.793 1.00 85.68 N ANISOU 1709 N ILE A 214 12006 10613 9936 970 -1609 2220 N ATOM 1710 CA ILE A 214 -0.138 39.962 28.135 1.00 82.06 C ANISOU 1710 CA ILE A 214 11543 10366 9270 954 -1410 2227 C ATOM 1711 C ILE A 214 0.296 38.828 29.060 1.00 83.48 C ANISOU 1711 C ILE A 214 11594 10699 9428 1012 -1382 2097 C ATOM 1712 O ILE A 214 -0.428 37.824 29.148 1.00 87.07 O ANISOU 1712 O ILE A 214 11988 11267 9826 930 -1362 1973 O ATOM 1713 CB ILE A 214 0.634 39.976 26.808 1.00 70.35 C ANISOU 1713 CB ILE A 214 10160 8826 7743 766 -1288 2436 C ATOM 1714 CG1 ILE A 214 0.090 41.065 25.877 1.00 63.42 C ANISOU 1714 CG1 ILE A 214 9403 7817 6876 730 -1302 2554 C ATOM 1715 CG2 ILE A 214 0.583 38.610 26.137 1.00 61.29 C ANISOU 1715 CG2 ILE A 214 9037 7854 6397 729 -1095 2385 C ATOM 1716 CD1 ILE A 214 -1.391 40.931 25.569 1.00 77.20 C ANISOU 1716 CD1 ILE A 214 11168 9689 8477 873 -1252 2461 C ATOM 1717 N PRO A 215 1.432 38.911 29.772 1.00 89.01 N ANISOU 1717 N PRO A 215 12194 11340 10285 967 -1424 2064 N ATOM 1718 CA PRO A 215 1.751 37.827 30.718 1.00 89.28 C ANISOU 1718 CA PRO A 215 12082 11542 10298 1049 -1376 1910 C ATOM 1719 C PRO A 215 0.718 37.661 31.818 1.00 89.06 C ANISOU 1719 C PRO A 215 11967 11577 10294 1159 -1493 1717 C ATOM 1720 O PRO A 215 0.440 36.529 32.231 1.00 91.10 O ANISOU 1720 O PRO A 215 12148 11961 10506 1148 -1409 1575 O ATOM 1721 CB PRO A 215 3.116 38.245 31.282 1.00 82.42 C ANISOU 1721 CB PRO A 215 11073 10596 9649 965 -1351 1854 C ATOM 1722 CG PRO A 215 3.717 39.077 30.226 1.00 80.87 C ANISOU 1722 CG PRO A 215 10959 10241 9528 790 -1290 2017 C ATOM 1723 CD PRO A 215 2.564 39.847 29.641 1.00 83.90 C ANISOU 1723 CD PRO A 215 11510 10521 9849 826 -1406 2114 C ATOM 1724 N LEU A 216 0.133 38.758 32.302 1.00 86.35 N ANISOU 1724 N LEU A 216 11609 11139 10061 1216 -1619 1670 N ATOM 1725 CA LEU A 216 -0.820 38.659 33.402 1.00 88.21 C ANISOU 1725 CA LEU A 216 11711 11448 10357 1255 -1647 1473 C ATOM 1726 C LEU A 216 -2.119 38.003 32.952 1.00 92.62 C ANISOU 1726 C LEU A 216 12281 12093 10818 1170 -1558 1446 C ATOM 1727 O LEU A 216 -2.709 37.207 33.693 1.00 81.81 O ANISOU 1727 O LEU A 216 10828 10801 9453 1153 -1513 1291 O ATOM 1728 CB LEU A 216 -1.087 40.046 33.983 1.00 93.25 C ANISOU 1728 CB LEU A 216 12361 11944 11128 1330 -1793 1418 C ATOM 1729 CG LEU A 216 -1.774 40.113 35.345 1.00 96.33 C ANISOU 1729 CG LEU A 216 12617 12389 11596 1374 -1824 1211 C ATOM 1730 CD1 LEU A 216 -0.990 39.320 36.376 1.00 82.51 C ANISOU 1730 CD1 LEU A 216 10720 10737 9894 1389 -1798 1090 C ATOM 1731 CD2 LEU A 216 -1.920 41.559 35.780 1.00105.32 C ANISOU 1731 CD2 LEU A 216 13795 13356 12866 1434 -1981 1164 C ATOM 1732 N ILE A 217 -2.579 38.323 31.742 1.00 93.55 N ANISOU 1732 N ILE A 217 12508 12184 10854 1112 -1528 1591 N ATOM 1733 CA ILE A 217 -3.812 37.732 31.231 1.00 81.52 C ANISOU 1733 CA ILE A 217 10996 10732 9246 1022 -1464 1555 C ATOM 1734 C ILE A 217 -3.618 36.248 30.946 1.00 79.80 C ANISOU 1734 C ILE A 217 10802 10585 8933 942 -1355 1486 C ATOM 1735 O ILE A 217 -4.487 35.423 31.258 1.00 86.01 O ANISOU 1735 O ILE A 217 11549 11430 9700 913 -1297 1350 O ATOM 1736 CB ILE A 217 -4.287 38.498 29.982 1.00 72.27 C ANISOU 1736 CB ILE A 217 9918 9526 8015 984 -1460 1728 C ATOM 1737 CG1 ILE A 217 -4.810 39.883 30.369 1.00 68.43 C ANISOU 1737 CG1 ILE A 217 9436 8953 7614 1099 -1549 1729 C ATOM 1738 CG2 ILE A 217 -5.356 37.716 29.235 1.00 73.23 C ANISOU 1738 CG2 ILE A 217 10064 9724 8035 863 -1395 1699 C ATOM 1739 CD1 ILE A 217 -5.136 40.764 29.181 1.00 70.54 C ANISOU 1739 CD1 ILE A 217 9813 9157 7832 1099 -1538 1901 C ATOM 1740 N VAL A 218 -2.475 35.881 30.360 1.00 77.42 N ANISOU 1740 N VAL A 218 10577 10273 8567 924 -1298 1571 N ATOM 1741 CA VAL A 218 -2.220 34.483 30.021 1.00 76.77 C ANISOU 1741 CA VAL A 218 10515 10276 8377 887 -1141 1502 C ATOM 1742 C VAL A 218 -2.127 33.630 31.281 1.00 75.47 C ANISOU 1742 C VAL A 218 10215 10184 8274 959 -1106 1328 C ATOM 1743 O VAL A 218 -2.684 32.527 31.344 1.00 79.40 O ANISOU 1743 O VAL A 218 10686 10749 8732 936 -1001 1216 O ATOM 1744 CB VAL A 218 -0.950 34.367 29.158 1.00 66.61 C ANISOU 1744 CB VAL A 218 9311 8990 7008 864 -1035 1648 C ATOM 1745 CG1 VAL A 218 -0.511 32.916 29.039 1.00 62.94 C ANISOU 1745 CG1 VAL A 218 8795 8654 6466 850 -843 1581 C ATOM 1746 CG2 VAL A 218 -1.194 34.962 27.779 1.00 53.58 C ANISOU 1746 CG2 VAL A 218 7816 7267 5275 763 -1022 1798 C ATOM 1747 N ILE A 219 -1.431 34.128 32.306 1.00 79.00 N ANISOU 1747 N ILE A 219 10572 10614 8830 1046 -1190 1300 N ATOM 1748 CA ILE A 219 -1.308 33.371 33.549 1.00 81.79 C ANISOU 1748 CA ILE A 219 10793 11035 9249 1105 -1154 1136 C ATOM 1749 C ILE A 219 -2.668 33.207 34.218 1.00 82.81 C ANISOU 1749 C ILE A 219 10879 11159 9425 1080 -1164 1000 C ATOM 1750 O ILE A 219 -3.001 32.125 34.716 1.00 88.32 O ANISOU 1750 O ILE A 219 11529 11913 10115 1082 -1061 880 O ATOM 1751 CB ILE A 219 -0.289 34.045 34.486 1.00 77.08 C ANISOU 1751 CB ILE A 219 10096 10422 8769 1191 -1252 1129 C ATOM 1752 CG1 ILE A 219 1.126 33.876 33.933 1.00 76.96 C ANISOU 1752 CG1 ILE A 219 10088 10453 8700 1223 -1187 1257 C ATOM 1753 CG2 ILE A 219 -0.393 33.477 35.896 1.00 72.80 C ANISOU 1753 CG2 ILE A 219 9414 9934 8314 1230 -1231 948 C ATOM 1754 CD1 ILE A 219 2.202 34.439 34.828 1.00 77.03 C ANISOU 1754 CD1 ILE A 219 9969 10469 8832 1311 -1275 1245 C ATOM 1755 N PHE A 220 -3.477 34.269 34.234 1.00 87.83 N ANISOU 1755 N PHE A 220 11530 11733 10109 1065 -1266 1030 N ATOM 1756 CA PHE A 220 -4.786 34.185 34.875 1.00 91.98 C ANISOU 1756 CA PHE A 220 12031 12275 10641 1094 -1251 899 C ATOM 1757 C PHE A 220 -5.716 33.242 34.122 1.00 86.69 C ANISOU 1757 C PHE A 220 11437 11660 9840 1092 -1139 858 C ATOM 1758 O PHE A 220 -6.435 32.448 34.739 1.00 75.07 O ANISOU 1758 O PHE A 220 9941 10246 8334 1176 -1055 709 O ATOM 1759 CB PHE A 220 -5.408 35.578 34.987 1.00 87.49 C ANISOU 1759 CB PHE A 220 11470 11644 10128 1115 -1366 939 C ATOM 1760 CG PHE A 220 -5.232 36.216 36.337 1.00 98.10 C ANISOU 1760 CG PHE A 220 12728 12965 11580 1193 -1434 835 C ATOM 1761 CD1 PHE A 220 -4.111 36.982 36.620 1.00108.15 C ANISOU 1761 CD1 PHE A 220 13938 14199 12953 1207 -1513 904 C ATOM 1762 CD2 PHE A 220 -6.193 36.056 37.322 1.00 97.91 C ANISOU 1762 CD2 PHE A 220 12706 12957 11537 1285 -1421 648 C ATOM 1763 CE1 PHE A 220 -3.951 37.574 37.861 1.00109.28 C ANISOU 1763 CE1 PHE A 220 13999 14324 13199 1267 -1572 795 C ATOM 1764 CE2 PHE A 220 -6.039 36.644 38.565 1.00104.93 C ANISOU 1764 CE2 PHE A 220 13532 13821 12513 1348 -1484 538 C ATOM 1765 CZ PHE A 220 -4.917 37.405 38.834 1.00109.19 C ANISOU 1765 CZ PHE A 220 13993 14326 13169 1327 -1559 612 C ATOM 1766 N PHE A 221 -5.711 33.311 32.789 1.00 82.34 N ANISOU 1766 N PHE A 221 10973 11096 9218 1000 -1128 991 N ATOM 1767 CA PHE A 221 -6.571 32.436 31.999 1.00 77.28 C ANISOU 1767 CA PHE A 221 10391 10514 8459 994 -1018 955 C ATOM 1768 C PHE A 221 -6.165 30.974 32.153 1.00 85.94 C ANISOU 1768 C PHE A 221 11446 11690 9518 1024 -868 871 C ATOM 1769 O PHE A 221 -7.009 30.112 32.424 1.00 94.14 O ANISOU 1769 O PHE A 221 12455 12791 10524 1097 -775 755 O ATOM 1770 CB PHE A 221 -6.534 32.852 30.528 1.00 84.66 C ANISOU 1770 CB PHE A 221 11428 11420 9320 877 -1034 1115 C ATOM 1771 CG PHE A 221 -7.187 31.865 29.604 1.00 94.84 C ANISOU 1771 CG PHE A 221 12769 12777 10490 855 -909 1087 C ATOM 1772 CD1 PHE A 221 -8.559 31.875 29.417 1.00 89.43 C ANISOU 1772 CD1 PHE A 221 12099 12120 9760 898 -903 1033 C ATOM 1773 CD2 PHE A 221 -6.428 30.926 28.923 1.00 91.01 C ANISOU 1773 CD2 PHE A 221 12309 12328 9942 795 -792 1112 C ATOM 1774 CE1 PHE A 221 -9.162 30.966 28.570 1.00 80.15 C ANISOU 1774 CE1 PHE A 221 10953 11010 8491 879 -794 1009 C ATOM 1775 CE2 PHE A 221 -7.025 30.014 28.077 1.00 82.17 C ANISOU 1775 CE2 PHE A 221 11216 11274 8729 776 -675 1084 C ATOM 1776 CZ PHE A 221 -8.394 30.035 27.899 1.00 82.29 C ANISOU 1776 CZ PHE A 221 11238 11318 8711 817 -682 1035 C ATOM 1777 N CYS A 222 -4.875 30.677 31.981 1.00 84.63 N ANISOU 1777 N CYS A 222 11272 11523 9363 973 -838 934 N ATOM 1778 CA CYS A 222 -4.415 29.292 32.038 1.00 76.09 C ANISOU 1778 CA CYS A 222 10139 10524 8246 1002 -683 874 C ATOM 1779 C CYS A 222 -4.690 28.670 33.401 1.00 69.97 C ANISOU 1779 C CYS A 222 9253 9806 7528 1127 -637 720 C ATOM 1780 O CYS A 222 -5.296 27.597 33.496 1.00 88.42 O ANISOU 1780 O CYS A 222 11550 12212 9832 1189 -518 632 O ATOM 1781 CB CYS A 222 -2.925 29.222 31.707 1.00 75.27 C ANISOU 1781 CB CYS A 222 10044 10416 8139 950 -656 970 C ATOM 1782 SG CYS A 222 -2.549 29.546 29.974 1.00 85.28 S ANISOU 1782 SG CYS A 222 11451 11671 9280 849 -610 1141 S ATOM 1783 N TYR A 223 -4.247 29.330 34.472 1.00 84.64 N ANISOU 1783 N TYR A 223 10205 11484 10469 -151 -2114 13 N ATOM 1784 CA TYR A 223 -4.471 28.782 35.804 1.00 73.13 C ANISOU 1784 CA TYR A 223 8652 9902 9231 -241 -1944 -66 C ATOM 1785 C TYR A 223 -5.937 28.860 36.206 1.00 79.42 C ANISOU 1785 C TYR A 223 9171 10728 10278 -302 -2045 -93 C ATOM 1786 O TYR A 223 -6.392 28.065 37.035 1.00 89.29 O ANISOU 1786 O TYR A 223 10325 11901 11699 -411 -1944 -176 O ATOM 1787 CB TYR A 223 -3.589 29.501 36.822 1.00 69.33 C ANISOU 1787 CB TYR A 223 8193 9335 8815 -141 -1724 29 C ATOM 1788 CG TYR A 223 -2.150 29.045 36.781 1.00 82.45 C ANISOU 1788 CG TYR A 223 10087 10967 10272 -119 -1568 14 C ATOM 1789 CD1 TYR A 223 -1.835 27.706 36.589 1.00 83.87 C ANISOU 1789 CD1 TYR A 223 10426 11128 10314 -197 -1522 -114 C ATOM 1790 CD2 TYR A 223 -1.108 29.951 36.920 1.00 75.41 C ANISOU 1790 CD2 TYR A 223 9254 10067 9333 -20 -1467 126 C ATOM 1791 CE1 TYR A 223 -0.523 27.280 36.547 1.00 82.01 C ANISOU 1791 CE1 TYR A 223 10401 10894 9866 -145 -1376 -121 C ATOM 1792 CE2 TYR A 223 0.208 29.534 36.879 1.00 72.86 C ANISOU 1792 CE2 TYR A 223 9109 9755 8819 4 -1325 117 C ATOM 1793 CZ TYR A 223 0.495 28.198 36.691 1.00 79.26 C ANISOU 1793 CZ TYR A 223 10077 10577 9462 -43 -1278 -1 C ATOM 1794 OH TYR A 223 1.803 27.774 36.648 1.00 83.38 O ANISOU 1794 OH TYR A 223 10776 11136 9769 13 -1132 -3 O ATOM 1795 N GLY A 224 -6.690 29.801 35.634 1.00 76.14 N ANISOU 1795 N GLY A 224 8614 10432 9882 -219 -2230 -6 N ATOM 1796 CA GLY A 224 -8.124 29.818 35.869 1.00 71.76 C ANISOU 1796 CA GLY A 224 7775 9956 9535 -269 -2351 -36 C ATOM 1797 C GLY A 224 -8.810 28.612 35.256 1.00 77.48 C ANISOU 1797 C GLY A 224 8446 10735 10259 -459 -2512 -220 C ATOM 1798 O GLY A 224 -9.665 27.979 35.883 1.00 90.58 O ANISOU 1798 O GLY A 224 9905 12364 12146 -602 -2487 -295 O ATOM 1799 N GLN A 225 -8.435 28.274 34.018 1.00 72.92 N ANISOU 1799 N GLN A 225 8043 10233 9429 -457 -2677 -297 N ATOM 1800 CA GLN A 225 -8.969 27.078 33.374 1.00 83.55 C ANISOU 1800 CA GLN A 225 9378 11608 10759 -637 -2852 -520 C ATOM 1801 C GLN A 225 -8.540 25.816 34.111 1.00 99.45 C ANISOU 1801 C GLN A 225 11509 13404 12874 -816 -2653 -640 C ATOM 1802 O GLN A 225 -9.308 24.850 34.204 1.00109.37 O ANISOU 1802 O GLN A 225 12647 14601 14309 -1024 -2715 -799 O ATOM 1803 CB GLN A 225 -8.513 27.022 31.916 1.00 74.17 C ANISOU 1803 CB GLN A 225 8395 10557 9230 -537 -3059 -579 C ATOM 1804 CG GLN A 225 -9.108 28.100 31.029 1.00 83.68 C ANISOU 1804 CG GLN A 225 9476 12002 10316 -349 -3284 -476 C ATOM 1805 CD GLN A 225 -10.604 27.945 30.856 1.00 91.45 C ANISOU 1805 CD GLN A 225 10138 13139 11470 -445 -3526 -603 C ATOM 1806 OE1 GLN A 225 -11.121 26.830 30.792 1.00100.70 O ANISOU 1806 OE1 GLN A 225 11236 14278 12749 -665 -3632 -835 O ATOM 1807 NE2 GLN A 225 -11.309 29.067 30.784 1.00100.49 N ANISOU 1807 NE2 GLN A 225 11082 14449 12650 -282 -3612 -451 N ATOM 1808 N LEU A 226 -7.315 25.804 34.639 1.00 95.65 N ANISOU 1808 N LEU A 226 11256 12800 12289 -735 -2406 -562 N ATOM 1809 CA LEU A 226 -6.814 24.622 35.333 1.00 94.93 C ANISOU 1809 CA LEU A 226 11308 12511 12251 -852 -2193 -656 C ATOM 1810 C LEU A 226 -7.615 24.347 36.600 1.00100.71 C ANISOU 1810 C LEU A 226 11803 13139 13323 -960 -2030 -630 C ATOM 1811 O LEU A 226 -8.085 23.224 36.817 1.00113.65 O ANISOU 1811 O LEU A 226 13412 14649 15121 -1150 -1993 -751 O ATOM 1812 CB LEU A 226 -5.332 24.799 35.660 1.00 85.97 C ANISOU 1812 CB LEU A 226 10431 11322 10913 -702 -1968 -565 C ATOM 1813 CG LEU A 226 -4.582 23.546 36.111 1.00 80.16 C ANISOU 1813 CG LEU A 226 9921 10418 10120 -759 -1761 -662 C ATOM 1814 CD1 LEU A 226 -3.555 23.151 35.068 1.00 79.89 C ANISOU 1814 CD1 LEU A 226 10193 10425 9736 -683 -1822 -723 C ATOM 1815 CD2 LEU A 226 -3.920 23.777 37.454 1.00 80.21 C ANISOU 1815 CD2 LEU A 226 9928 10352 10197 -655 -1455 -550 C ATOM 1816 N VAL A 227 -7.783 25.366 37.448 1.00 93.52 N ANISOU 1816 N VAL A 227 10724 12276 12532 -828 -1922 -468 N ATOM 1817 CA VAL A 227 -8.565 25.203 38.670 1.00 85.32 C ANISOU 1817 CA VAL A 227 9446 11180 11791 -875 -1757 -415 C ATOM 1818 C VAL A 227 -9.997 24.801 38.346 1.00 89.00 C ANISOU 1818 C VAL A 227 9629 11707 12481 -1067 -1941 -489 C ATOM 1819 O VAL A 227 -10.617 24.025 39.084 1.00 94.15 O ANISOU 1819 O VAL A 227 10130 12260 13384 -1210 -1805 -500 O ATOM 1820 CB VAL A 227 -8.510 26.495 39.509 1.00 75.36 C ANISOU 1820 CB VAL A 227 8065 9986 10581 -656 -1657 -248 C ATOM 1821 CG1 VAL A 227 -9.493 26.434 40.665 1.00 72.43 C ANISOU 1821 CG1 VAL A 227 7411 9613 10495 -660 -1521 -179 C ATOM 1822 CG2 VAL A 227 -7.103 26.720 40.029 1.00 75.48 C ANISOU 1822 CG2 VAL A 227 8323 9925 10432 -504 -1451 -209 C ATOM 1823 N PHE A 228 -10.540 25.301 37.235 1.00 84.07 N ANISOU 1823 N PHE A 228 8917 11256 11771 -1068 -2246 -535 N ATOM 1824 CA PHE A 228 -11.886 24.905 36.835 1.00 86.85 C ANISOU 1824 CA PHE A 228 8975 11703 12319 -1255 -2458 -638 C ATOM 1825 C PHE A 228 -11.924 23.439 36.421 1.00 92.91 C ANISOU 1825 C PHE A 228 9843 12316 13144 -1520 -2504 -856 C ATOM 1826 O PHE A 228 -12.828 22.695 36.820 1.00104.17 O ANISOU 1826 O PHE A 228 11039 13670 14869 -1744 -2482 -917 O ATOM 1827 CB PHE A 228 -12.382 25.803 35.702 1.00 75.67 C ANISOU 1827 CB PHE A 228 7461 10542 10748 -1144 -2781 -646 C ATOM 1828 CG PHE A 228 -13.779 25.492 35.255 1.00 95.28 C ANISOU 1828 CG PHE A 228 9606 13182 13414 -1311 -3031 -767 C ATOM 1829 CD1 PHE A 228 -14.866 25.873 36.025 1.00 95.62 C ANISOU 1829 CD1 PHE A 228 9279 13323 13728 -1322 -2988 -658 C ATOM 1830 CD2 PHE A 228 -14.009 24.820 34.066 1.00100.28 C ANISOU 1830 CD2 PHE A 228 10277 13883 13940 -1444 -3318 -999 C ATOM 1831 CE1 PHE A 228 -16.154 25.588 35.619 1.00 96.95 C ANISOU 1831 CE1 PHE A 228 9097 13665 14074 -1484 -3220 -769 C ATOM 1832 CE2 PHE A 228 -15.296 24.533 33.654 1.00 96.65 C ANISOU 1832 CE2 PHE A 228 9477 13587 13659 -1609 -3571 -1141 C ATOM 1833 CZ PHE A 228 -16.370 24.918 34.431 1.00 97.35 C ANISOU 1833 CZ PHE A 228 9173 13782 14034 -1640 -3519 -1020 C ATOM 1834 N THR A 229 -10.947 23.006 35.621 1.00 87.48 N ANISOU 1834 N THR A 229 9497 11564 12179 -1496 -2563 -972 N ATOM 1835 CA THR A 229 -10.894 21.609 35.199 1.00 82.84 C ANISOU 1835 CA THR A 229 9058 10798 11620 -1720 -2611 -1200 C ATOM 1836 C THR A 229 -10.749 20.675 36.395 1.00 83.17 C ANISOU 1836 C THR A 229 9136 10565 11902 -1849 -2273 -1160 C ATOM 1837 O THR A 229 -11.410 19.631 36.462 1.00 93.61 O ANISOU 1837 O THR A 229 10365 11725 13478 -2113 -2284 -1294 O ATOM 1838 CB THR A 229 -9.745 21.406 34.207 1.00 83.11 C ANISOU 1838 CB THR A 229 9482 10833 11265 -1597 -2699 -1299 C ATOM 1839 OG1 THR A 229 -10.181 21.758 32.888 1.00 90.22 O ANISOU 1839 OG1 THR A 229 10333 11961 11987 -1555 -3067 -1422 O ATOM 1840 CG2 THR A 229 -9.260 19.961 34.210 1.00 82.25 C ANISOU 1840 CG2 THR A 229 9638 10456 11159 -1753 -2600 -1478 C ATOM 1841 N VAL A 230 -9.907 21.045 37.362 1.00 81.79 N ANISOU 1841 N VAL A 230 9083 10333 11659 -1661 -1968 -976 N ATOM 1842 CA VAL A 230 -9.651 20.165 38.497 1.00 87.14 C ANISOU 1842 CA VAL A 230 9831 10772 12505 -1717 -1623 -920 C ATOM 1843 C VAL A 230 -10.868 20.094 39.413 1.00 93.39 C ANISOU 1843 C VAL A 230 10246 11550 13690 -1844 -1512 -817 C ATOM 1844 O VAL A 230 -11.253 19.012 39.871 1.00101.48 O ANISOU 1844 O VAL A 230 11233 12360 14965 -2043 -1355 -846 O ATOM 1845 CB VAL A 230 -8.393 20.627 39.253 1.00 74.80 C ANISOU 1845 CB VAL A 230 8487 9205 10727 -1445 -1353 -771 C ATOM 1846 CG1 VAL A 230 -8.150 19.744 40.458 1.00 70.45 C ANISOU 1846 CG1 VAL A 230 8004 8447 10319 -1447 -986 -700 C ATOM 1847 CG2 VAL A 230 -7.187 20.598 38.329 1.00 81.05 C ANISOU 1847 CG2 VAL A 230 9631 10021 11144 -1336 -1442 -858 C ATOM 1848 N LYS A 231 -11.495 21.240 39.696 1.00 90.78 N ANISOU 1848 N LYS A 231 9629 11439 13424 -1721 -1578 -680 N ATOM 1849 CA LYS A 231 -12.687 21.235 40.539 1.00 87.29 C ANISOU 1849 CA LYS A 231 8802 11029 13336 -1809 -1476 -563 C ATOM 1850 C LYS A 231 -13.837 20.490 39.872 1.00 89.93 C ANISOU 1850 C LYS A 231 8894 11348 13929 -2142 -1697 -720 C ATOM 1851 O LYS A 231 -14.622 19.816 40.549 1.00 81.50 O ANISOU 1851 O LYS A 231 7591 10172 13204 -2327 -1538 -664 O ATOM 1852 CB LYS A 231 -13.100 22.665 40.885 1.00 86.34 C ANISOU 1852 CB LYS A 231 8450 11162 13192 -1572 -1529 -401 C ATOM 1853 CG LYS A 231 -12.171 23.368 41.864 1.00 93.58 C ANISOU 1853 CG LYS A 231 9523 12074 13960 -1265 -1274 -246 C ATOM 1854 CD LYS A 231 -12.786 24.667 42.361 1.00 92.90 C ANISOU 1854 CD LYS A 231 9178 12195 13924 -1048 -1307 -94 C ATOM 1855 CE LYS A 231 -11.816 25.449 43.236 1.00 88.79 C ANISOU 1855 CE LYS A 231 8825 11666 13246 -742 -1109 8 C ATOM 1856 NZ LYS A 231 -11.367 24.680 44.429 1.00 85.78 N ANISOU 1856 NZ LYS A 231 8521 11144 12926 -683 -757 68 N ATOM 1857 N GLU A 232 -13.955 20.598 38.546 1.00 91.54 N ANISOU 1857 N GLU A 232 9138 11665 13977 -2216 -2063 -918 N ATOM 1858 CA GLU A 232 -15.004 19.871 37.837 1.00 87.82 C ANISOU 1858 CA GLU A 232 8436 11193 13737 -2535 -2319 -1123 C ATOM 1859 C GLU A 232 -14.776 18.367 37.899 1.00102.32 C ANISOU 1859 C GLU A 232 10459 12678 15739 -2807 -2193 -1275 C ATOM 1860 O GLU A 232 -15.718 17.599 38.129 1.00114.87 O ANISOU 1860 O GLU A 232 11785 14148 17710 -3106 -2177 -1328 O ATOM 1861 CB GLU A 232 -15.079 20.332 36.382 1.00 88.95 C ANISOU 1861 CB GLU A 232 8618 11563 13616 -2492 -2745 -1318 C ATOM 1862 CG GLU A 232 -16.238 21.264 36.079 1.00111.76 C ANISOU 1862 CG GLU A 232 11093 14789 16581 -2447 -2993 -1277 C ATOM 1863 CD GLU A 232 -16.694 21.171 34.636 1.00133.62 C ANISOU 1863 CD GLU A 232 13808 17746 19214 -2528 -3436 -1548 C ATOM 1864 OE1 GLU A 232 -15.999 20.513 33.832 1.00137.34 O ANISOU 1864 OE1 GLU A 232 14603 18097 19484 -2572 -3556 -1758 O ATOM 1865 OE2 GLU A 232 -17.751 21.749 34.309 1.00143.82 O ANISOU 1865 OE2 GLU A 232 14733 19327 20585 -2520 -3668 -1556 O ATOM 1866 N ALA A 233 -13.533 17.929 37.692 1.00105.49 N ANISOU 1866 N ALA A 233 11310 12904 15868 -2705 -2096 -1339 N ATOM 1867 CA ALA A 233 -13.236 16.502 37.718 1.00 98.68 C ANISOU 1867 CA ALA A 233 10681 11683 15129 -2924 -1969 -1485 C ATOM 1868 C ALA A 233 -13.449 15.916 39.108 1.00100.17 C ANISOU 1868 C ALA A 233 10770 11642 15647 -2997 -1544 -1275 C ATOM 1869 O ALA A 233 -13.991 14.812 39.244 1.00106.97 O ANISOU 1869 O ALA A 233 11566 12233 16843 -3299 -1470 -1358 O ATOM 1870 CB ALA A 233 -11.806 16.257 37.242 1.00 84.33 C ANISOU 1870 CB ALA A 233 9369 9772 12900 -2733 -1936 -1567 C ATOM 1871 N ALA A 234 -13.035 16.638 40.152 1.00 94.32 N ANISOU 1871 N ALA A 234 10014 11000 14822 -2716 -1257 -1004 N ATOM 1872 CA ALA A 234 -13.222 16.136 41.510 1.00 92.02 C ANISOU 1872 CA ALA A 234 9628 10534 14801 -2717 -836 -780 C ATOM 1873 C ALA A 234 -14.697 16.106 41.891 1.00100.99 C ANISOU 1873 C ALA A 234 10264 11728 16378 -2944 -842 -691 C ATOM 1874 O ALA A 234 -15.140 15.195 42.601 1.00100.25 O ANISOU 1874 O ALA A 234 10067 11397 16625 -3124 -570 -592 O ATOM 1875 CB ALA A 234 -12.426 16.985 42.501 1.00 79.49 C ANISOU 1875 CB ALA A 234 8134 9084 12984 -2323 -569 -546 C ATOM 1876 N ALA A 235 -15.472 17.092 41.432 1.00101.48 N ANISOU 1876 N ALA A 235 10005 12111 16441 -2927 -1136 -706 N ATOM 1877 CA ALA A 235 -16.903 17.104 41.722 1.00 95.81 C ANISOU 1877 CA ALA A 235 8777 11501 16124 -3133 -1168 -626 C ATOM 1878 C ALA A 235 -17.600 15.899 41.104 1.00103.31 C ANISOU 1878 C ALA A 235 9615 12225 17415 -3587 -1312 -849 C ATOM 1879 O ALA A 235 -18.550 15.356 41.680 1.00115.35 O ANISOU 1879 O ALA A 235 10796 13659 19373 -3828 -1157 -744 O ATOM 1880 CB ALA A 235 -17.532 18.402 41.218 1.00 91.04 C ANISOU 1880 CB ALA A 235 7888 11303 15401 -2993 -1486 -623 C ATOM 1881 N GLN A 236 -17.141 15.467 39.933 1.00 97.13 N ANISOU 1881 N GLN A 236 9110 11347 16450 -3706 -1609 -1161 N ATOM 1882 CA GLN A 236 -17.676 14.288 39.267 1.00102.06 C ANISOU 1882 CA GLN A 236 9690 11719 17367 -4129 -1783 -1438 C ATOM 1883 C GLN A 236 -17.027 12.997 39.759 1.00116.13 C ANISOU 1883 C GLN A 236 11819 13024 19283 -4253 -1447 -1434 C ATOM 1884 O GLN A 236 -17.237 11.938 39.155 1.00106.67 O ANISOU 1884 O GLN A 236 10702 11540 18289 -4584 -1584 -1698 O ATOM 1885 CB GLN A 236 -17.502 14.430 37.750 1.00102.89 C ANISOU 1885 CB GLN A 236 9945 11965 17182 -4152 -2278 -1796 C ATOM 1886 CG GLN A 236 -18.498 13.643 36.905 1.00126.79 C ANISOU 1886 CG GLN A 236 12725 14919 20529 -4577 -2621 -2128 C ATOM 1887 CD GLN A 236 -19.908 14.203 36.964 1.00124.61 C ANISOU 1887 CD GLN A 236 11832 14962 20551 -4720 -2793 -2076 C ATOM 1888 OE1 GLN A 236 -20.152 15.253 37.559 1.00129.33 O ANISOU 1888 OE1 GLN A 236 12206 15854 21078 -4470 -2680 -1794 O ATOM 1889 NE2 GLN A 236 -20.847 13.500 36.342 1.00117.40 N ANISOU 1889 NE2 GLN A 236 10636 13996 19972 -5119 -3077 -2362 N ATOM 1890 N GLN A 237 -16.258 13.060 40.840 1.00106.21 N ANISOU 1890 N GLN A 237 10769 11673 17911 -3981 -1018 -1151 N ATOM 1891 CA GLN A 237 -15.547 11.895 41.352 1.00106.68 C ANISOU 1891 CA GLN A 237 11192 11304 18036 -4021 -667 -1114 C ATOM 1892 C GLN A 237 -15.305 12.065 42.851 1.00102.28 C ANISOU 1892 C GLN A 237 10603 10736 17521 -3756 -160 -722 C ATOM 1893 O GLN A 237 -14.185 11.932 43.346 1.00 97.13 O ANISOU 1893 O GLN A 237 10330 9987 16586 -3470 107 -623 O ATOM 1894 CB GLN A 237 -14.240 11.687 40.587 1.00104.13 C ANISOU 1894 CB GLN A 237 11416 10893 17257 -3846 -785 -1323 C ATOM 1895 CG GLN A 237 -13.665 10.289 40.693 1.00108.22 C ANISOU 1895 CG GLN A 237 12323 10935 17859 -3969 -554 -1406 C ATOM 1896 CD GLN A 237 -12.497 10.080 39.756 1.00111.54 C ANISOU 1896 CD GLN A 237 13247 11311 17822 -3810 -738 -1649 C ATOM 1897 OE1 GLN A 237 -12.008 11.025 39.135 1.00109.86 O ANISOU 1897 OE1 GLN A 237 13098 11430 17213 -3577 -984 -1708 O ATOM 1898 NE2 GLN A 237 -12.043 8.839 39.644 1.00112.77 N ANISOU 1898 NE2 GLN A 237 13766 11051 18031 -3922 -608 -1779 N ATOM 1899 N GLN A 238 -16.369 12.364 43.594 1.00104.31 N ANISOU 1899 N GLN A 238 10390 11124 18118 -3826 -25 -495 N ATOM 1900 CA GLN A 238 -16.272 12.595 45.029 1.00 99.05 C ANISOU 1900 CA GLN A 238 9645 10503 17488 -3539 439 -118 C ATOM 1901 C GLN A 238 -16.085 11.313 45.830 1.00109.52 C ANISOU 1901 C GLN A 238 11141 11405 19067 -3629 896 40 C ATOM 1902 O GLN A 238 -15.914 11.386 47.052 1.00111.47 O ANISOU 1902 O GLN A 238 11366 11677 19311 -3348 1318 360 O ATOM 1903 CB GLN A 238 -17.514 13.339 45.524 1.00103.48 C ANISOU 1903 CB GLN A 238 9638 11367 18312 -3556 430 82 C ATOM 1904 CG GLN A 238 -17.705 14.702 44.884 1.00113.80 C ANISOU 1904 CG GLN A 238 10781 13103 19354 -3394 32 -18 C ATOM 1905 CD GLN A 238 -18.903 15.450 45.433 1.00127.07 C ANISOU 1905 CD GLN A 238 11920 15098 21264 -3356 46 196 C ATOM 1906 OE1 GLN A 238 -19.658 14.926 46.252 1.00133.48 O ANISOU 1906 OE1 GLN A 238 12437 15822 22455 -3480 341 419 O ATOM 1907 NE2 GLN A 238 -19.083 16.687 44.984 1.00128.83 N ANISOU 1907 NE2 GLN A 238 12009 15687 21251 -3167 -260 146 N ATOM 1908 N GLU A 239 -16.123 10.147 45.183 1.00123.35 N ANISOU 1908 N GLU A 239 13066 12767 21033 -3990 828 -176 N ATOM 1909 CA GLU A 239 -15.821 8.895 45.861 1.00121.52 C ANISOU 1909 CA GLU A 239 13078 12082 21014 -4054 1270 -35 C ATOM 1910 C GLU A 239 -14.326 8.684 46.051 1.00113.93 C ANISOU 1910 C GLU A 239 12687 11015 19585 -3683 1463 -36 C ATOM 1911 O GLU A 239 -13.931 7.805 46.825 1.00113.13 O ANISOU 1911 O GLU A 239 12814 10602 19567 -3597 1899 150 O ATOM 1912 CB GLU A 239 -16.413 7.711 45.088 1.00111.18 C ANISOU 1912 CB GLU A 239 11763 10352 20130 -4587 1117 -288 C ATOM 1913 CG GLU A 239 -15.800 7.469 43.711 1.00110.88 C ANISOU 1913 CG GLU A 239 12091 10223 19817 -4694 678 -733 C ATOM 1914 CD GLU A 239 -16.427 8.323 42.623 1.00111.05 C ANISOU 1914 CD GLU A 239 11813 10612 19768 -4833 114 -1005 C ATOM 1915 OE1 GLU A 239 -17.151 9.282 42.960 1.00127.39 O ANISOU 1915 OE1 GLU A 239 13442 13057 21903 -4763 62 -836 O ATOM 1916 OE2 GLU A 239 -16.201 8.032 41.429 1.00112.19 O ANISOU 1916 OE2 GLU A 239 12170 10682 19775 -4982 -276 -1385 O ATOM 1917 N SER A 240 -13.495 9.471 45.372 1.00 97.48 N ANISOU 1917 N SER A 240 10826 9196 17017 -3452 1163 -224 N ATOM 1918 CA SER A 240 -12.043 9.364 45.456 1.00 93.81 C ANISOU 1918 CA SER A 240 10868 8694 16082 -3098 1302 -245 C ATOM 1919 C SER A 240 -11.525 10.453 46.387 1.00 89.24 C ANISOU 1919 C SER A 240 10228 8483 15196 -2634 1484 -4 C ATOM 1920 O SER A 240 -11.512 11.634 46.025 1.00 87.68 O ANISOU 1920 O SER A 240 9883 8645 14784 -2511 1196 -65 O ATOM 1921 CB SER A 240 -11.414 9.484 44.070 1.00 94.64 C ANISOU 1921 CB SER A 240 11258 8847 15856 -3146 864 -605 C ATOM 1922 OG SER A 240 -10.041 9.816 44.164 1.00 93.42 O ANISOU 1922 OG SER A 240 11480 8822 15193 -2745 950 -589 O ATOM 1923 N ALA A 241 -11.094 10.053 47.586 1.00 98.42 N ANISOU 1923 N ALA A 241 11511 9549 16336 -2362 1961 264 N ATOM 1924 CA ALA A 241 -10.534 11.014 48.529 1.00 96.58 C ANISOU 1924 CA ALA A 241 11243 9656 15797 -1894 2136 460 C ATOM 1925 C ALA A 241 -9.224 11.606 48.022 1.00 98.12 C ANISOU 1925 C ALA A 241 11770 10040 15470 -1626 1946 283 C ATOM 1926 O ALA A 241 -8.905 12.758 48.337 1.00 90.16 O ANISOU 1926 O ALA A 241 10659 9376 14223 -1345 1872 329 O ATOM 1927 CB ALA A 241 -10.327 10.353 49.891 1.00 90.79 C ANISOU 1927 CB ALA A 241 10586 8784 15125 -1632 2691 769 C ATOM 1928 N THR A 242 -8.459 10.839 47.240 1.00 96.78 N ANISOU 1928 N THR A 242 11995 9649 15127 -1707 1868 82 N ATOM 1929 CA THR A 242 -7.212 11.356 46.682 1.00 93.86 C ANISOU 1929 CA THR A 242 11924 9469 14269 -1468 1690 -73 C ATOM 1930 C THR A 242 -7.476 12.488 45.695 1.00 97.83 C ANISOU 1930 C THR A 242 12240 10253 14678 -1572 1224 -240 C ATOM 1931 O THR A 242 -6.774 13.506 45.708 1.00 98.71 O ANISOU 1931 O THR A 242 12374 10656 14474 -1311 1129 -237 O ATOM 1932 CB THR A 242 -6.426 10.227 46.012 1.00 90.12 C ANISOU 1932 CB THR A 242 11905 8698 13638 -1528 1708 -245 C ATOM 1933 OG1 THR A 242 -5.879 9.362 47.015 1.00 96.73 O ANISOU 1933 OG1 THR A 242 12976 9341 14437 -1297 2175 -63 O ATOM 1934 CG2 THR A 242 -5.295 10.784 45.157 1.00 79.50 C ANISOU 1934 CG2 THR A 242 10815 7572 11818 -1351 1449 -428 C ATOM 1935 N THR A 243 -8.486 12.330 44.835 1.00 97.76 N ANISOU 1935 N THR A 243 12039 10159 14946 -1947 930 -385 N ATOM 1936 CA THR A 243 -8.844 13.403 43.914 1.00 95.32 C ANISOU 1936 CA THR A 243 11532 10132 14554 -2019 500 -520 C ATOM 1937 C THR A 243 -9.324 14.641 44.664 1.00 89.81 C ANISOU 1937 C THR A 243 10476 9743 13904 -1840 527 -325 C ATOM 1938 O THR A 243 -9.147 15.767 44.183 1.00 85.49 O ANISOU 1938 O THR A 243 9862 9468 13151 -1726 269 -373 O ATOM 1939 CB THR A 243 -9.917 12.922 42.935 1.00 96.37 C ANISOU 1939 CB THR A 243 11494 10134 14988 -2439 190 -720 C ATOM 1940 OG1 THR A 243 -9.521 11.665 42.369 1.00 94.10 O ANISOU 1940 OG1 THR A 243 11553 9505 14695 -2601 196 -909 O ATOM 1941 CG2 THR A 243 -10.112 13.931 41.811 1.00 84.05 C ANISOU 1941 CG2 THR A 243 9812 8871 13251 -2462 -268 -885 C ATOM 1942 N GLN A 244 -9.919 14.458 45.845 1.00 89.88 N ANISOU 1942 N GLN A 244 10263 9709 14176 -1792 848 -94 N ATOM 1943 CA GLN A 244 -10.342 15.607 46.638 1.00 91.57 C ANISOU 1943 CA GLN A 244 10162 10218 14411 -1570 892 89 C ATOM 1944 C GLN A 244 -9.148 16.314 47.266 1.00 92.94 C ANISOU 1944 C GLN A 244 10538 10569 14206 -1148 1029 150 C ATOM 1945 O GLN A 244 -9.147 17.544 47.396 1.00 88.17 O ANISOU 1945 O GLN A 244 9784 10233 13486 -963 893 178 O ATOM 1946 CB GLN A 244 -11.338 15.169 47.711 1.00 87.53 C ANISOU 1946 CB GLN A 244 9348 9631 14278 -1613 1207 331 C ATOM 1947 CG GLN A 244 -12.555 14.453 47.158 1.00 95.72 C ANISOU 1947 CG GLN A 244 10134 10490 15744 -2063 1086 274 C ATOM 1948 CD GLN A 244 -13.207 15.210 46.019 1.00 97.01 C ANISOU 1948 CD GLN A 244 10078 10858 15925 -2263 604 82 C ATOM 1949 OE1 GLN A 244 -13.382 14.676 44.924 1.00 99.25 O ANISOU 1949 OE1 GLN A 244 10434 11006 16273 -2570 331 -157 O ATOM 1950 NE2 GLN A 244 -13.574 16.461 46.272 1.00 98.05 N ANISOU 1950 NE2 GLN A 244 9949 11320 15984 -2063 494 178 N ATOM 1951 N LYS A 245 -8.124 15.556 47.668 1.00 94.86 N ANISOU 1951 N LYS A 245 11117 10664 14259 -985 1296 164 N ATOM 1952 CA LYS A 245 -6.901 16.182 48.161 1.00 88.10 C ANISOU 1952 CA LYS A 245 10452 9995 13028 -603 1390 178 C ATOM 1953 C LYS A 245 -6.173 16.914 47.042 1.00 86.25 C ANISOU 1953 C LYS A 245 10365 9897 12510 -618 1040 -14 C ATOM 1954 O LYS A 245 -5.649 18.015 47.251 1.00 87.35 O ANISOU 1954 O LYS A 245 10466 10269 12454 -391 965 -7 O ATOM 1955 CB LYS A 245 -5.982 15.136 48.791 1.00 90.93 C ANISOU 1955 CB LYS A 245 11132 10187 13230 -414 1752 234 C ATOM 1956 CG LYS A 245 -6.533 14.468 50.036 1.00111.27 C ANISOU 1956 CG LYS A 245 13592 12650 16037 -306 2166 474 C ATOM 1957 CD LYS A 245 -5.594 13.369 50.507 1.00128.61 C ANISOU 1957 CD LYS A 245 16149 14662 18053 -114 2513 523 C ATOM 1958 CE LYS A 245 -6.223 12.530 51.605 1.00135.47 C ANISOU 1958 CE LYS A 245 16927 15356 19188 -46 2947 785 C ATOM 1959 NZ LYS A 245 -5.415 11.314 51.899 1.00135.78 N ANISOU 1959 NZ LYS A 245 17349 15152 19088 98 3281 834 N ATOM 1960 N ALA A 246 -6.128 16.316 45.849 1.00 81.57 N ANISOU 1960 N ALA A 246 9942 9157 11895 -876 828 -185 N ATOM 1961 CA ALA A 246 -5.439 16.948 44.729 1.00 83.07 C ANISOU 1961 CA ALA A 246 10279 9484 11800 -871 517 -341 C ATOM 1962 C ALA A 246 -6.091 18.272 44.356 1.00 90.85 C ANISOU 1962 C ALA A 246 10971 10699 12847 -898 230 -333 C ATOM 1963 O ALA A 246 -5.397 19.256 44.075 1.00 88.77 O ANISOU 1963 O ALA A 246 10758 10620 12349 -736 102 -348 O ATOM 1964 CB ALA A 246 -5.413 16.005 43.528 1.00 75.14 C ANISOU 1964 CB ALA A 246 9497 8286 10766 -1120 336 -532 C ATOM 1965 N GLU A 247 -7.425 18.318 44.359 1.00 94.99 N ANISOU 1965 N GLU A 247 11182 11215 13696 -1096 136 -298 N ATOM 1966 CA GLU A 247 -8.122 19.551 44.013 1.00 95.57 C ANISOU 1966 CA GLU A 247 10975 11512 13825 -1096 -128 -279 C ATOM 1967 C GLU A 247 -7.787 20.669 44.993 1.00 94.19 C ANISOU 1967 C GLU A 247 10703 11519 13565 -780 -2 -140 C ATOM 1968 O GLU A 247 -7.635 21.829 44.594 1.00 94.05 O ANISOU 1968 O GLU A 247 10637 11671 13425 -681 -205 -151 O ATOM 1969 CB GLU A 247 -9.630 19.299 43.963 1.00102.24 C ANISOU 1969 CB GLU A 247 11472 12334 15039 -1348 -216 -256 C ATOM 1970 CG GLU A 247 -10.470 20.541 43.709 1.00112.84 C ANISOU 1970 CG GLU A 247 12499 13928 16448 -1316 -464 -215 C ATOM 1971 CD GLU A 247 -10.914 21.215 44.992 1.00127.42 C ANISOU 1971 CD GLU A 247 14097 15896 18421 -1094 -253 -9 C ATOM 1972 OE1 GLU A 247 -11.177 20.497 45.980 1.00129.68 O ANISOU 1972 OE1 GLU A 247 14311 16072 18888 -1084 53 112 O ATOM 1973 OE2 GLU A 247 -10.991 22.460 45.015 1.00135.15 O ANISOU 1973 OE2 GLU A 247 14965 17074 19312 -910 -384 36 O ATOM 1974 N LYS A 248 -7.661 20.339 46.280 1.00 93.90 N ANISOU 1974 N LYS A 248 10647 11444 13588 -603 336 -11 N ATOM 1975 CA LYS A 248 -7.303 21.349 47.270 1.00 90.77 C ANISOU 1975 CA LYS A 248 10172 11221 13094 -274 449 85 C ATOM 1976 C LYS A 248 -5.861 21.808 47.090 1.00 93.54 C ANISOU 1976 C LYS A 248 10794 11636 13111 -91 423 -3 C ATOM 1977 O LYS A 248 -5.574 23.011 47.117 1.00 98.66 O ANISOU 1977 O LYS A 248 11385 12433 13667 57 293 -12 O ATOM 1978 CB LYS A 248 -7.523 20.806 48.682 1.00 79.79 C ANISOU 1978 CB LYS A 248 8699 9798 11820 -92 823 242 C ATOM 1979 CG LYS A 248 -8.983 20.665 49.076 1.00 90.38 C ANISOU 1979 CG LYS A 248 9692 11141 13506 -208 876 382 C ATOM 1980 CD LYS A 248 -9.114 20.196 50.515 1.00105.95 C ANISOU 1980 CD LYS A 248 11591 13107 15558 33 1279 575 C ATOM 1981 CE LYS A 248 -10.571 20.050 50.922 1.00110.38 C ANISOU 1981 CE LYS A 248 11778 13688 16473 -79 1359 748 C ATOM 1982 NZ LYS A 248 -11.302 21.346 50.850 1.00113.88 N ANISOU 1982 NZ LYS A 248 11938 14369 16962 1 1122 763 N ATOM 1983 N GLU A 249 -4.937 20.861 46.905 1.00 93.75 N ANISOU 1983 N GLU A 249 11113 11546 12963 -99 549 -67 N ATOM 1984 CA GLU A 249 -3.530 21.217 46.748 1.00 93.36 C ANISOU 1984 CA GLU A 249 11297 11582 12594 73 543 -141 C ATOM 1985 C GLU A 249 -3.301 22.029 45.479 1.00 83.27 C ANISOU 1985 C GLU A 249 10052 10380 11205 -44 214 -224 C ATOM 1986 O GLU A 249 -2.563 23.021 45.493 1.00 87.37 O ANISOU 1986 O GLU A 249 10587 11030 11579 103 148 -234 O ATOM 1987 CB GLU A 249 -2.667 19.954 46.746 1.00106.03 C ANISOU 1987 CB GLU A 249 13207 13056 14024 98 748 -181 C ATOM 1988 CG GLU A 249 -1.268 20.130 46.155 1.00126.71 C ANISOU 1988 CG GLU A 249 16078 15762 16303 196 684 -275 C ATOM 1989 CD GLU A 249 -0.327 20.928 47.046 1.00134.79 C ANISOU 1989 CD GLU A 249 17078 16977 17160 498 797 -260 C ATOM 1990 OE1 GLU A 249 -0.735 21.326 48.158 1.00142.89 O ANISOU 1990 OE1 GLU A 249 17918 18067 18306 665 925 -191 O ATOM 1991 OE2 GLU A 249 0.830 21.153 46.632 1.00122.81 O ANISOU 1991 OE2 GLU A 249 15718 15557 15385 576 753 -324 O ATOM 1992 N VAL A 250 -3.925 21.623 44.371 1.00 79.26 N ANISOU 1992 N VAL A 250 9551 9794 10769 -301 7 -286 N ATOM 1993 CA VAL A 250 -3.774 22.359 43.119 1.00 77.90 C ANISOU 1993 CA VAL A 250 9411 9714 10473 -378 -298 -344 C ATOM 1994 C VAL A 250 -4.331 23.770 43.260 1.00 86.32 C ANISOU 1994 C VAL A 250 10228 10920 11650 -304 -441 -268 C ATOM 1995 O VAL A 250 -3.725 24.743 42.793 1.00 92.20 O ANISOU 1995 O VAL A 250 11020 11760 12253 -221 -566 -259 O ATOM 1996 CB VAL A 250 -4.445 21.592 41.964 1.00 83.38 C ANISOU 1996 CB VAL A 250 10143 10318 11219 -639 -503 -449 C ATOM 1997 CG1 VAL A 250 -4.559 22.472 40.734 1.00 81.34 C ANISOU 1997 CG1 VAL A 250 9854 10198 10854 -678 -825 -481 C ATOM 1998 CG2 VAL A 250 -3.661 20.330 41.640 1.00 82.82 C ANISOU 1998 CG2 VAL A 250 10391 10101 10975 -676 -395 -547 C ATOM 1999 N THR A 251 -5.488 23.907 43.912 1.00 88.51 N ANISOU 1999 N THR A 251 10239 11204 12187 -324 -412 -199 N ATOM 2000 CA THR A 251 -6.061 25.232 44.129 1.00 86.15 C ANISOU 2000 CA THR A 251 9713 11032 11987 -216 -533 -125 C ATOM 2001 C THR A 251 -5.171 26.074 45.035 1.00 85.95 C ANISOU 2001 C THR A 251 9733 11064 11861 50 -400 -95 C ATOM 2002 O THR A 251 -4.971 27.269 44.787 1.00101.07 O ANISOU 2002 O THR A 251 11617 13046 13739 137 -542 -80 O ATOM 2003 CB THR A 251 -7.466 25.109 44.721 1.00 84.58 C ANISOU 2003 CB THR A 251 9211 10853 12073 -264 -499 -47 C ATOM 2004 OG1 THR A 251 -8.320 24.430 43.791 1.00 87.30 O ANISOU 2004 OG1 THR A 251 9477 11160 12532 -537 -670 -104 O ATOM 2005 CG2 THR A 251 -8.048 26.485 45.020 1.00 77.78 C ANISOU 2005 CG2 THR A 251 8132 10129 11291 -102 -608 33 C ATOM 2006 N ARG A 252 -4.619 25.465 46.087 1.00 84.18 N ANISOU 2006 N ARG A 252 9583 10808 11594 189 -129 -93 N ATOM 2007 CA ARG A 252 -3.758 26.209 47.000 1.00 87.94 C ANISOU 2007 CA ARG A 252 10086 11360 11966 454 -17 -105 C ATOM 2008 C ARG A 252 -2.490 26.685 46.299 1.00 88.03 C ANISOU 2008 C ARG A 252 10292 11395 11762 456 -116 -176 C ATOM 2009 O ARG A 252 -2.008 27.793 46.559 1.00 88.32 O ANISOU 2009 O ARG A 252 10293 11488 11777 588 -173 -194 O ATOM 2010 CB ARG A 252 -3.414 25.348 48.216 1.00 82.35 C ANISOU 2010 CB ARG A 252 9425 10645 11218 632 297 -91 C ATOM 2011 CG ARG A 252 -2.978 26.144 49.434 1.00 90.58 C ANISOU 2011 CG ARG A 252 10397 11805 12216 951 405 -108 C ATOM 2012 CD ARG A 252 -2.615 25.234 50.596 1.00104.51 C ANISOU 2012 CD ARG A 252 12218 13594 13897 1170 726 -85 C ATOM 2013 NE ARG A 252 -1.207 25.354 50.965 1.00124.20 N ANISOU 2013 NE ARG A 252 14871 16177 16143 1363 801 -195 N ATOM 2014 CZ ARG A 252 -0.246 24.545 50.529 1.00132.67 C ANISOU 2014 CZ ARG A 252 16170 17223 17018 1312 878 -240 C ATOM 2015 NH1 ARG A 252 -0.537 23.547 49.706 1.00139.61 N ANISOU 2015 NH1 ARG A 252 17169 17959 17919 1077 885 -199 N ATOM 2016 NH2 ARG A 252 1.008 24.733 50.918 1.00128.36 N ANISOU 2016 NH2 ARG A 252 15723 16800 16249 1505 940 -339 N ATOM 2017 N MET A 253 -1.943 25.867 45.396 1.00 80.26 N ANISOU 2017 N MET A 253 9510 10363 10623 312 -137 -216 N ATOM 2018 CA MET A 253 -0.735 26.266 44.679 1.00 81.72 C ANISOU 2018 CA MET A 253 9864 10594 10592 320 -212 -254 C ATOM 2019 C MET A 253 -1.023 27.370 43.669 1.00 88.51 C ANISOU 2019 C MET A 253 10659 11479 11493 232 -471 -210 C ATOM 2020 O MET A 253 -0.211 28.286 43.496 1.00101.79 O ANISOU 2020 O MET A 253 12370 13201 13103 296 -516 -198 O ATOM 2021 CB MET A 253 -0.108 25.059 43.983 1.00 77.61 C ANISOU 2021 CB MET A 253 9586 10032 9870 230 -158 -301 C ATOM 2022 CG MET A 253 0.893 24.303 44.836 1.00 88.19 C ANISOU 2022 CG MET A 253 11071 11392 11045 397 105 -340 C ATOM 2023 SD MET A 253 2.316 25.321 45.274 1.00 95.91 S ANISOU 2023 SD MET A 253 12052 12528 11862 593 143 -371 S ATOM 2024 CE MET A 253 2.855 25.860 43.653 1.00 92.61 C ANISOU 2024 CE MET A 253 11736 12141 11312 438 -84 -340 C ATOM 2025 N VAL A 254 -2.168 27.297 42.986 1.00 82.72 N ANISOU 2025 N VAL A 254 9828 10724 10879 90 -636 -180 N ATOM 2026 CA VAL A 254 -2.505 28.317 41.997 1.00 86.82 C ANISOU 2026 CA VAL A 254 10290 11284 11412 46 -874 -122 C ATOM 2027 C VAL A 254 -2.669 29.675 42.668 1.00 87.63 C ANISOU 2027 C VAL A 254 10241 11399 11655 191 -892 -65 C ATOM 2028 O VAL A 254 -2.254 30.707 42.127 1.00 86.24 O ANISOU 2028 O VAL A 254 10094 11227 11447 222 -997 -11 O ATOM 2029 CB VAL A 254 -3.766 27.905 41.216 1.00 86.42 C ANISOU 2029 CB VAL A 254 10137 11244 11453 -110 -1054 -125 C ATOM 2030 CG1 VAL A 254 -4.314 29.078 40.421 1.00 77.29 C ANISOU 2030 CG1 VAL A 254 8877 10160 10330 -89 -1281 -44 C ATOM 2031 CG2 VAL A 254 -3.448 26.742 40.288 1.00 91.25 C ANISOU 2031 CG2 VAL A 254 10944 11831 11896 -248 -1095 -210 C ATOM 2032 N ILE A 255 -3.260 29.695 43.864 1.00 86.31 N ANISOU 2032 N ILE A 255 9919 11228 11646 296 -779 -72 N ATOM 2033 CA ILE A 255 -3.386 30.944 44.609 1.00 82.36 C ANISOU 2033 CA ILE A 255 9295 10731 11265 471 -793 -49 C ATOM 2034 C ILE A 255 -2.012 31.466 45.005 1.00 83.37 C ANISOU 2034 C ILE A 255 9541 10841 11295 575 -713 -110 C ATOM 2035 O ILE A 255 -1.731 32.666 44.898 1.00 91.63 O ANISOU 2035 O ILE A 255 10572 11846 12396 631 -807 -93 O ATOM 2036 CB ILE A 255 -4.293 30.742 45.836 1.00 73.94 C ANISOU 2036 CB ILE A 255 8044 9696 10355 601 -672 -43 C ATOM 2037 CG1 ILE A 255 -5.727 30.461 45.390 1.00 68.80 C ANISOU 2037 CG1 ILE A 255 7217 9080 9844 484 -781 31 C ATOM 2038 CG2 ILE A 255 -4.244 31.956 46.749 1.00 71.72 C ANISOU 2038 CG2 ILE A 255 7675 9420 10157 833 -669 -59 C ATOM 2039 CD1 ILE A 255 -6.672 30.203 46.535 1.00 71.82 C ANISOU 2039 CD1 ILE A 255 7390 9511 10388 602 -642 75 C ATOM 2040 N ILE A 256 -1.131 30.572 45.457 1.00 80.84 N ANISOU 2040 N ILE A 256 9336 10547 10834 602 -538 -184 N ATOM 2041 CA ILE A 256 0.215 30.980 45.846 1.00 73.90 C ANISOU 2041 CA ILE A 256 8538 9690 9850 697 -465 -260 C ATOM 2042 C ILE A 256 0.990 31.506 44.643 1.00 79.52 C ANISOU 2042 C ILE A 256 9359 10382 10475 568 -584 -209 C ATOM 2043 O ILE A 256 1.692 32.518 44.739 1.00 86.62 O ANISOU 2043 O ILE A 256 10241 11253 11417 607 -619 -225 O ATOM 2044 CB ILE A 256 0.944 29.809 46.529 1.00 71.65 C ANISOU 2044 CB ILE A 256 8353 9471 9400 780 -246 -336 C ATOM 2045 CG1 ILE A 256 0.306 29.507 47.886 1.00 70.91 C ANISOU 2045 CG1 ILE A 256 8139 9409 9395 972 -95 -364 C ATOM 2046 CG2 ILE A 256 2.423 30.115 46.692 1.00 75.67 C ANISOU 2046 CG2 ILE A 256 8941 10045 9763 849 -192 -419 C ATOM 2047 CD1 ILE A 256 0.847 28.263 48.549 1.00 69.27 C ANISOU 2047 CD1 ILE A 256 8035 9257 9026 1079 147 -402 C ATOM 2048 N MET A 257 0.869 30.841 43.491 1.00 78.26 N ANISOU 2048 N MET A 257 9306 10231 10197 420 -648 -146 N ATOM 2049 CA MET A 257 1.626 31.270 42.317 1.00 76.83 C ANISOU 2049 CA MET A 257 9234 10061 9898 336 -737 -69 C ATOM 2050 C MET A 257 1.128 32.611 41.792 1.00 82.85 C ANISOU 2050 C MET A 257 9909 10757 10813 325 -900 39 C ATOM 2051 O MET A 257 1.932 33.475 41.422 1.00 92.81 O ANISOU 2051 O MET A 257 11201 11986 12077 318 -916 102 O ATOM 2052 CB MET A 257 1.553 30.209 41.220 1.00 74.53 C ANISOU 2052 CB MET A 257 9088 9813 9416 226 -778 -46 C ATOM 2053 CG MET A 257 2.308 28.930 41.537 1.00 81.75 C ANISOU 2053 CG MET A 257 10149 10771 10140 248 -607 -134 C ATOM 2054 SD MET A 257 2.248 27.741 40.183 1.00 99.00 S ANISOU 2054 SD MET A 257 12538 12979 12098 136 -684 -136 S ATOM 2055 CE MET A 257 0.486 27.444 40.068 1.00101.50 C ANISOU 2055 CE MET A 257 12718 13221 12626 22 -831 -158 C ATOM 2056 N VAL A 258 -0.191 32.802 41.750 1.00 81.78 N ANISOU 2056 N VAL A 258 9661 10601 10812 327 -1011 74 N ATOM 2057 CA VAL A 258 -0.742 34.053 41.239 1.00 80.38 C ANISOU 2057 CA VAL A 258 9413 10366 10761 353 -1160 189 C ATOM 2058 C VAL A 258 -0.440 35.203 42.193 1.00 84.45 C ANISOU 2058 C VAL A 258 9856 10776 11454 469 -1122 156 C ATOM 2059 O VAL A 258 -0.055 36.297 41.764 1.00 89.59 O ANISOU 2059 O VAL A 258 10533 11331 12176 473 -1177 243 O ATOM 2060 CB VAL A 258 -2.252 33.900 40.983 1.00 74.80 C ANISOU 2060 CB VAL A 258 8582 9703 10133 347 -1290 224 C ATOM 2061 CG1 VAL A 258 -2.917 35.260 40.858 1.00 84.45 C ANISOU 2061 CG1 VAL A 258 9710 10868 11507 446 -1410 328 C ATOM 2062 CG2 VAL A 258 -2.486 33.077 39.727 1.00 70.33 C ANISOU 2062 CG2 VAL A 258 8099 9227 9397 227 -1395 251 C ATOM 2063 N ILE A 259 -0.596 34.974 43.498 1.00 81.30 N ANISOU 2063 N ILE A 259 9372 10387 11132 577 -1025 29 N ATOM 2064 CA ILE A 259 -0.320 36.027 44.468 1.00 82.60 C ANISOU 2064 CA ILE A 259 9472 10460 11452 714 -1010 -49 C ATOM 2065 C ILE A 259 1.161 36.384 44.468 1.00 91.34 C ANISOU 2065 C ILE A 259 10660 11525 12520 669 -952 -105 C ATOM 2066 O ILE A 259 1.528 37.564 44.522 1.00 99.00 O ANISOU 2066 O ILE A 259 11616 12360 13640 685 -1007 -104 O ATOM 2067 CB ILE A 259 -0.807 35.605 45.865 1.00 75.70 C ANISOU 2067 CB ILE A 259 8490 9649 10623 884 -910 -173 C ATOM 2068 CG1 ILE A 259 -2.328 35.728 45.941 1.00 81.26 C ANISOU 2068 CG1 ILE A 259 9061 10374 11441 950 -987 -94 C ATOM 2069 CG2 ILE A 259 -0.134 36.436 46.950 1.00 61.36 C ANISOU 2069 CG2 ILE A 259 6643 7777 8895 1044 -878 -323 C ATOM 2070 CD1 ILE A 259 -2.892 35.412 47.296 1.00 90.90 C ANISOU 2070 CD1 ILE A 259 10157 11668 12715 1147 -875 -172 C ATOM 2071 N ALA A 260 2.034 35.377 44.396 1.00 85.99 N ANISOU 2071 N ALA A 260 10063 10957 11651 611 -838 -152 N ATOM 2072 CA ALA A 260 3.466 35.651 44.342 1.00 79.17 C ANISOU 2072 CA ALA A 260 9247 10099 10736 564 -779 -195 C ATOM 2073 C ALA A 260 3.833 36.422 43.081 1.00 85.13 C ANISOU 2073 C ALA A 260 10058 10766 11521 428 -858 -17 C ATOM 2074 O ALA A 260 4.713 37.291 43.110 1.00 97.27 O ANISOU 2074 O ALA A 260 11573 12218 13167 386 -852 -21 O ATOM 2075 CB ALA A 260 4.255 34.345 44.417 1.00 64.09 C ANISOU 2075 CB ALA A 260 7422 8352 8579 558 -637 -256 C ATOM 2076 N PHE A 261 3.170 36.117 41.963 1.00 77.10 N ANISOU 2076 N PHE A 261 9107 9773 10413 365 -931 141 N ATOM 2077 CA PHE A 261 3.435 36.845 40.727 1.00 74.47 C ANISOU 2077 CA PHE A 261 8834 9379 10081 285 -993 342 C ATOM 2078 C PHE A 261 3.035 38.308 40.857 1.00 85.99 C ANISOU 2078 C PHE A 261 10227 10637 11806 323 -1073 408 C ATOM 2079 O PHE A 261 3.741 39.200 40.372 1.00 94.60 O ANISOU 2079 O PHE A 261 11341 11610 12991 262 -1058 527 O ATOM 2080 CB PHE A 261 2.695 36.188 39.563 1.00 73.12 C ANISOU 2080 CB PHE A 261 8741 9309 9733 258 -1077 466 C ATOM 2081 CG PHE A 261 2.986 36.813 38.229 1.00 75.12 C ANISOU 2081 CG PHE A 261 9071 9547 9925 226 -1123 692 C ATOM 2082 CD1 PHE A 261 4.087 36.413 37.492 1.00 80.00 C ANISOU 2082 CD1 PHE A 261 9790 10263 10343 176 -1041 774 C ATOM 2083 CD2 PHE A 261 2.158 37.795 37.709 1.00 79.84 C ANISOU 2083 CD2 PHE A 261 9640 10049 10647 279 -1234 841 C ATOM 2084 CE1 PHE A 261 4.359 36.981 36.264 1.00 81.40 C ANISOU 2084 CE1 PHE A 261 10033 10446 10448 179 -1059 1013 C ATOM 2085 CE2 PHE A 261 2.427 38.369 36.481 1.00 84.19 C ANISOU 2085 CE2 PHE A 261 10269 10595 11125 286 -1252 1078 C ATOM 2086 CZ PHE A 261 3.529 37.960 35.757 1.00 82.12 C ANISOU 2086 CZ PHE A 261 10101 10433 10666 236 -1160 1170 C ATOM 2087 N LEU A 262 1.901 38.572 41.509 1.00 78.41 N ANISOU 2087 N LEU A 262 9188 9629 10977 430 -1146 344 N ATOM 2088 CA LEU A 262 1.472 39.948 41.726 1.00 76.92 C ANISOU 2088 CA LEU A 262 8956 9237 11032 505 -1221 388 C ATOM 2089 C LEU A 262 2.425 40.677 42.666 1.00 84.68 C ANISOU 2089 C LEU A 262 9903 10076 12195 507 -1170 234 C ATOM 2090 O LEU A 262 2.840 41.808 42.389 1.00 92.38 O ANISOU 2090 O LEU A 262 10899 10844 13355 463 -1190 313 O ATOM 2091 CB LEU A 262 0.043 39.969 42.271 1.00 73.45 C ANISOU 2091 CB LEU A 262 8427 8821 10659 651 -1304 346 C ATOM 2092 CG LEU A 262 -1.054 39.510 41.308 1.00 79.17 C ANISOU 2092 CG LEU A 262 9145 9672 11263 649 -1398 491 C ATOM 2093 CD1 LEU A 262 -2.420 39.622 41.965 1.00 81.34 C ANISOU 2093 CD1 LEU A 262 9288 9983 11634 795 -1468 450 C ATOM 2094 CD2 LEU A 262 -1.010 40.313 40.016 1.00 82.89 C ANISOU 2094 CD2 LEU A 262 9701 10068 11724 627 -1466 720 C ATOM 2095 N ILE A 263 2.795 40.038 43.780 1.00 78.60 N ANISOU 2095 N ILE A 263 9077 9412 11377 563 -1102 10 N ATOM 2096 CA ILE A 263 3.745 40.643 44.711 1.00 86.25 C ANISOU 2096 CA ILE A 263 9993 10289 12489 579 -1075 -185 C ATOM 2097 C ILE A 263 5.059 40.966 44.010 1.00 88.75 C ANISOU 2097 C ILE A 263 10340 10553 12828 392 -1022 -104 C ATOM 2098 O ILE A 263 5.746 41.930 44.370 1.00 88.65 O ANISOU 2098 O ILE A 263 10280 10368 13036 343 -1040 -191 O ATOM 2099 CB ILE A 263 3.958 39.714 45.925 1.00 89.87 C ANISOU 2099 CB ILE A 263 10391 10937 12818 707 -995 -421 C ATOM 2100 CG1 ILE A 263 2.652 39.540 46.700 1.00 89.39 C ANISOU 2100 CG1 ILE A 263 10275 10914 12776 908 -1026 -475 C ATOM 2101 CG2 ILE A 263 5.036 40.253 46.853 1.00 90.75 C ANISOU 2101 CG2 ILE A 263 10434 11010 13038 737 -984 -655 C ATOM 2102 CD1 ILE A 263 2.763 38.579 47.860 1.00 85.95 C ANISOU 2102 CD1 ILE A 263 9788 10671 12198 1068 -916 -657 C ATOM 2103 N CYS A 264 5.414 40.194 42.981 1.00 94.13 N ANISOU 2103 N CYS A 264 11094 11379 13294 287 -960 64 N ATOM 2104 CA CYS A 264 6.680 40.399 42.288 1.00 95.78 C ANISOU 2104 CA CYS A 264 11315 11586 13490 130 -884 172 C ATOM 2105 C CYS A 264 6.636 41.612 41.364 1.00 98.33 C ANISOU 2105 C CYS A 264 11671 11674 14015 43 -918 414 C ATOM 2106 O CYS A 264 7.527 42.467 41.410 1.00105.93 O ANISOU 2106 O CYS A 264 12581 12479 15190 -71 -884 423 O ATOM 2107 CB CYS A 264 7.050 39.146 41.492 1.00 92.13 C ANISOU 2107 CB CYS A 264 10937 11370 12697 94 -803 275 C ATOM 2108 SG CYS A 264 8.635 39.260 40.627 1.00 85.03 S ANISOU 2108 SG CYS A 264 10040 10541 11727 -60 -684 433 S ATOM 2109 N TRP A 265 5.614 41.704 40.511 1.00101.25 N ANISOU 2109 N TRP A 265 12122 12020 14330 99 -981 617 N ATOM 2110 CA TRP A 265 5.625 42.671 39.424 1.00100.87 C ANISOU 2110 CA TRP A 265 12134 11800 14394 50 -979 906 C ATOM 2111 C TRP A 265 4.619 43.803 39.562 1.00103.67 C ANISOU 2111 C TRP A 265 12500 11901 14986 151 -1076 958 C ATOM 2112 O TRP A 265 4.736 44.790 38.830 1.00112.08 O ANISOU 2112 O TRP A 265 13618 12764 16203 121 -1051 1192 O ATOM 2113 CB TRP A 265 5.382 41.964 38.082 1.00 99.16 C ANISOU 2113 CB TRP A 265 12017 11782 13878 69 -969 1143 C ATOM 2114 CG TRP A 265 6.418 40.934 37.767 1.00108.75 C ANISOU 2114 CG TRP A 265 13251 13229 14840 -6 -866 1133 C ATOM 2115 CD1 TRP A 265 6.264 39.578 37.798 1.00105.05 C ANISOU 2115 CD1 TRP A 265 12825 13006 14085 34 -870 1015 C ATOM 2116 CD2 TRP A 265 7.777 41.175 37.385 1.00117.08 C ANISOU 2116 CD2 TRP A 265 14283 14290 15911 -127 -734 1249 C ATOM 2117 NE1 TRP A 265 7.443 38.960 37.453 1.00109.91 N ANISOU 2117 NE1 TRP A 265 13466 13783 14511 -27 -753 1047 N ATOM 2118 CE2 TRP A 265 8.387 39.919 37.195 1.00115.98 C ANISOU 2118 CE2 TRP A 265 14181 14431 15455 -125 -668 1194 C ATOM 2119 CE3 TRP A 265 8.537 42.331 37.183 1.00117.42 C ANISOU 2119 CE3 TRP A 265 14272 14120 16221 -240 -658 1401 C ATOM 2120 CZ2 TRP A 265 9.721 39.787 36.812 1.00117.06 C ANISOU 2120 CZ2 TRP A 265 14291 14681 15506 -209 -531 1292 C ATOM 2121 CZ3 TRP A 265 9.861 42.198 36.803 1.00115.47 C ANISOU 2121 CZ3 TRP A 265 13978 13977 15920 -356 -517 1503 C ATOM 2122 CH2 TRP A 265 10.440 40.936 36.622 1.00114.29 C ANISOU 2122 CH2 TRP A 265 13854 14147 15423 -329 -456 1450 C ATOM 2123 N LEU A 266 3.644 43.695 40.461 1.00 98.20 N ANISOU 2123 N LEU A 266 11766 11219 14327 290 -1168 771 N ATOM 2124 CA LEU A 266 2.630 44.744 40.551 1.00100.83 C ANISOU 2124 CA LEU A 266 12119 11340 14852 425 -1261 833 C ATOM 2125 C LEU A 266 3.189 46.010 41.195 1.00110.41 C ANISOU 2125 C LEU A 266 13324 12216 16410 390 -1257 742 C ATOM 2126 O LEU A 266 2.892 47.114 40.715 1.00111.40 O ANISOU 2126 O LEU A 266 13521 12082 16723 425 -1274 923 O ATOM 2127 CB LEU A 266 1.394 44.257 41.320 1.00 86.62 C ANISOU 2127 CB LEU A 266 10256 9674 12980 601 -1352 677 C ATOM 2128 CG LEU A 266 0.090 44.987 40.996 1.00 88.15 C ANISOU 2128 CG LEU A 266 10471 9783 13237 774 -1453 820 C ATOM 2129 CD1 LEU A 266 -0.156 44.968 39.496 1.00 89.56 C ANISOU 2129 CD1 LEU A 266 10728 10037 13265 756 -1462 1122 C ATOM 2130 CD2 LEU A 266 -1.073 44.353 41.739 1.00 87.44 C ANISOU 2130 CD2 LEU A 266 10280 9882 13062 929 -1522 681 C ATOM 2131 N PRO A 267 3.983 45.919 42.274 1.00112.44 N ANISOU 2131 N PRO A 267 13499 12459 16766 335 -1241 458 N ATOM 2132 CA PRO A 267 4.652 47.139 42.759 1.00109.94 C ANISOU 2132 CA PRO A 267 13169 11804 16799 260 -1252 355 C ATOM 2133 C PRO A 267 5.543 47.777 41.712 1.00116.56 C ANISOU 2133 C PRO A 267 14048 12457 17783 53 -1152 622 C ATOM 2134 O PRO A 267 5.527 49.003 41.558 1.00119.06 O ANISOU 2134 O PRO A 267 14419 12415 18403 26 -1160 717 O ATOM 2135 CB PRO A 267 5.450 46.639 43.970 1.00109.43 C ANISOU 2135 CB PRO A 267 12985 11867 16725 239 -1254 -4 C ATOM 2136 CG PRO A 267 4.684 45.477 44.448 1.00110.37 C ANISOU 2136 CG PRO A 267 13080 12301 16554 410 -1268 -105 C ATOM 2137 CD PRO A 267 4.169 44.799 43.218 1.00112.54 C ANISOU 2137 CD PRO A 267 13426 12738 16595 380 -1228 193 C ATOM 2138 N TYR A 268 6.308 46.975 40.968 1.00118.94 N ANISOU 2138 N TYR A 268 14329 12987 17874 -80 -1045 764 N ATOM 2139 CA TYR A 268 7.099 47.523 39.874 1.00114.74 C ANISOU 2139 CA TYR A 268 13828 12322 17445 -248 -923 1076 C ATOM 2140 C TYR A 268 6.228 48.067 38.754 1.00110.88 C ANISOU 2140 C TYR A 268 13477 11721 16932 -137 -916 1434 C ATOM 2141 O TYR A 268 6.680 48.934 38.003 1.00104.90 O ANISOU 2141 O TYR A 268 12764 10729 16365 -228 -814 1709 O ATOM 2142 CB TYR A 268 8.055 46.461 39.323 1.00111.22 C ANISOU 2142 CB TYR A 268 13336 12199 16724 -361 -810 1153 C ATOM 2143 CG TYR A 268 9.330 47.032 38.737 1.00119.47 C ANISOU 2143 CG TYR A 268 14322 13120 17951 -579 -665 1348 C ATOM 2144 CD1 TYR A 268 9.371 47.502 37.429 1.00125.31 C ANISOU 2144 CD1 TYR A 268 15147 13774 18691 -598 -555 1766 C ATOM 2145 CD2 TYR A 268 10.492 47.104 39.494 1.00124.60 C ANISOU 2145 CD2 TYR A 268 14813 13758 18771 -753 -633 1121 C ATOM 2146 CE1 TYR A 268 10.534 48.028 36.894 1.00129.16 C ANISOU 2146 CE1 TYR A 268 15561 14150 19362 -798 -394 1981 C ATOM 2147 CE2 TYR A 268 11.659 47.627 38.967 1.00126.55 C ANISOU 2147 CE2 TYR A 268 14967 13902 19212 -974 -494 1307 C ATOM 2148 CZ TYR A 268 11.674 48.088 37.667 1.00124.64 C ANISOU 2148 CZ TYR A 268 14812 13560 18987 -1003 -364 1751 C ATOM 2149 OH TYR A 268 12.831 48.610 37.135 1.00115.34 O ANISOU 2149 OH TYR A 268 13525 12281 18017 -1222 -197 1974 O ATOM 2150 N ALA A 269 4.990 47.589 38.631 1.00101.98 N ANISOU 2150 N ALA A 269 12405 10762 15581 66 -1013 1444 N ATOM 2151 CA ALA A 269 4.096 48.115 37.607 1.00 95.67 C ANISOU 2151 CA ALA A 269 11720 9896 14733 212 -1027 1760 C ATOM 2152 C ALA A 269 3.588 49.499 37.986 1.00 98.67 C ANISOU 2152 C ALA A 269 12159 9877 15452 301 -1068 1778 C ATOM 2153 O ALA A 269 3.775 50.467 37.242 1.00101.31 O ANISOU 2153 O ALA A 269 12584 9949 15961 287 -980 2067 O ATOM 2154 CB ALA A 269 2.927 47.156 37.386 1.00 99.87 C ANISOU 2154 CB ALA A 269 12259 10754 14935 388 -1137 1734 C ATOM 2155 N GLY A 270 2.944 49.609 39.149 1.00 95.21 N ANISOU 2155 N GLY A 270 11681 9385 15108 414 -1190 1481 N ATOM 2156 CA GLY A 270 2.308 50.865 39.515 1.00 98.38 C ANISOU 2156 CA GLY A 270 12162 9430 15787 555 -1248 1483 C ATOM 2157 C GLY A 270 3.303 51.959 39.858 1.00106.45 C ANISOU 2157 C GLY A 270 13206 10021 17220 379 -1186 1433 C ATOM 2158 O GLY A 270 3.158 53.104 39.420 1.00105.01 O ANISOU 2158 O GLY A 270 13143 9477 17278 415 -1143 1644 O ATOM 2159 N VAL A 271 4.323 51.624 40.653 1.00104.37 N ANISOU 2159 N VAL A 271 12821 9785 17050 190 -1181 1147 N ATOM 2160 CA VAL A 271 5.289 52.634 41.079 1.00 98.92 C ANISOU 2160 CA VAL A 271 12113 8693 16780 -5 -1151 1036 C ATOM 2161 C VAL A 271 6.047 53.191 39.879 1.00102.62 C ANISOU 2161 C VAL A 271 12627 8961 17403 -202 -973 1431 C ATOM 2162 O VAL A 271 6.260 54.404 39.771 1.00114.22 O ANISOU 2162 O VAL A 271 14171 9973 19254 -277 -927 1535 O ATOM 2163 CB VAL A 271 6.242 52.053 42.140 1.00 93.96 C ANISOU 2163 CB VAL A 271 11314 8216 16170 -149 -1192 638 C ATOM 2164 CG1 VAL A 271 7.319 53.063 42.502 1.00 97.11 C ANISOU 2164 CG1 VAL A 271 11658 8222 17018 -390 -1175 508 C ATOM 2165 CG2 VAL A 271 5.461 51.643 43.380 1.00 89.86 C ANISOU 2165 CG2 VAL A 271 10762 7858 15521 92 -1347 273 C ATOM 2166 N ALA A 272 6.454 52.321 38.951 1.00102.02 N ANISOU 2166 N ALA A 272 12514 9213 17035 -274 -861 1669 N ATOM 2167 CA ALA A 272 7.096 52.810 37.735 1.00104.25 C ANISOU 2167 CA ALA A 272 12842 9354 17415 -407 -670 2096 C ATOM 2168 C ALA A 272 6.105 53.527 36.829 1.00116.77 C ANISOU 2168 C ALA A 272 14613 10769 18985 -185 -635 2464 C ATOM 2169 O ALA A 272 6.489 54.448 36.101 1.00132.38 O ANISOU 2169 O ALA A 272 16666 12430 21204 -258 -479 2797 O ATOM 2170 CB ALA A 272 7.767 51.661 36.984 1.00 89.08 C ANISOU 2170 CB ALA A 272 10844 7862 15140 -487 -566 2246 C ATOM 2171 N PHE A 273 4.833 53.120 36.854 1.00112.89 N ANISOU 2171 N PHE A 273 14187 10492 18212 92 -767 2422 N ATOM 2172 CA PHE A 273 3.813 53.850 36.109 1.00123.27 C ANISOU 2172 CA PHE A 273 15666 11667 19504 344 -758 2731 C ATOM 2173 C PHE A 273 3.612 55.244 36.689 1.00130.64 C ANISOU 2173 C PHE A 273 16702 12062 20873 378 -772 2681 C ATOM 2174 O PHE A 273 3.429 56.214 35.944 1.00136.71 O ANISOU 2174 O PHE A 273 17619 12528 21797 467 -659 3028 O ATOM 2175 CB PHE A 273 2.498 53.069 36.114 1.00120.99 C ANISOU 2175 CB PHE A 273 15378 11757 18835 617 -917 2650 C ATOM 2176 CG PHE A 273 1.446 53.638 35.204 1.00128.54 C ANISOU 2176 CG PHE A 273 16474 12690 19677 906 -916 2981 C ATOM 2177 CD1 PHE A 273 1.370 53.241 33.879 1.00128.84 C ANISOU 2177 CD1 PHE A 273 16554 12992 19408 998 -841 3324 C ATOM 2178 CD2 PHE A 273 0.528 54.563 35.675 1.00138.23 C ANISOU 2178 CD2 PHE A 273 17793 13654 21076 1121 -995 2942 C ATOM 2179 CE1 PHE A 273 0.402 53.760 33.040 1.00134.97 C ANISOU 2179 CE1 PHE A 273 17448 13785 20048 1299 -847 3620 C ATOM 2180 CE2 PHE A 273 -0.443 55.085 34.841 1.00138.98 C ANISOU 2180 CE2 PHE A 273 18009 13755 21040 1419 -991 3251 C ATOM 2181 CZ PHE A 273 -0.506 54.684 33.521 1.00136.47 C ANISOU 2181 CZ PHE A 273 17720 13718 20413 1509 -919 3589 C ATOM 2182 N TYR A 274 3.647 55.364 38.019 1.00126.50 N ANISOU 2182 N TYR A 274 16114 11408 20543 333 -907 2250 N ATOM 2183 CA TYR A 274 3.512 56.673 38.648 1.00124.60 C ANISOU 2183 CA TYR A 274 15982 10637 20725 367 -943 2144 C ATOM 2184 C TYR A 274 4.733 57.543 38.377 1.00131.26 C ANISOU 2184 C TYR A 274 16831 11036 22004 59 -783 2278 C ATOM 2185 O TYR A 274 4.598 58.736 38.083 1.00143.27 O ANISOU 2185 O TYR A 274 18513 12078 23844 96 -705 2483 O ATOM 2186 CB TYR A 274 3.289 56.510 40.152 1.00118.42 C ANISOU 2186 CB TYR A 274 15119 9874 20001 424 -1138 1624 C ATOM 2187 CG TYR A 274 3.048 57.814 40.880 1.00129.16 C ANISOU 2187 CG TYR A 274 16608 10707 21759 510 -1213 1456 C ATOM 2188 CD1 TYR A 274 1.775 58.362 40.957 1.00131.05 C ANISOU 2188 CD1 TYR A 274 17002 10849 21943 863 -1291 1515 C ATOM 2189 CD2 TYR A 274 4.094 58.496 41.490 1.00136.47 C ANISOU 2189 CD2 TYR A 274 17499 11236 23118 247 -1214 1223 C ATOM 2190 CE1 TYR A 274 1.549 59.553 41.620 1.00137.02 C ANISOU 2190 CE1 TYR A 274 17903 11110 23048 972 -1361 1354 C ATOM 2191 CE2 TYR A 274 3.878 59.688 42.154 1.00140.19 C ANISOU 2191 CE2 TYR A 274 18106 11195 23963 329 -1299 1038 C ATOM 2192 CZ TYR A 274 2.603 60.211 42.216 1.00140.54 C ANISOU 2192 CZ TYR A 274 18333 11136 23930 702 -1369 1107 C ATOM 2193 OH TYR A 274 2.381 61.398 42.877 1.00142.08 O ANISOU 2193 OH TYR A 274 18690 10810 24482 814 -1455 915 O ATOM 2194 N ILE A 275 5.934 56.964 38.476 1.00127.67 N ANISOU 2194 N ILE A 275 16199 10729 21581 -246 -723 2174 N ATOM 2195 CA ILE A 275 7.151 57.714 38.179 1.00123.13 C ANISOU 2195 CA ILE A 275 15579 9777 21429 -574 -558 2318 C ATOM 2196 C ILE A 275 7.181 58.126 36.714 1.00128.51 C ANISOU 2196 C ILE A 275 16379 10359 22092 -546 -320 2916 C ATOM 2197 O ILE A 275 7.702 59.195 36.368 1.00107.68 O ANISOU 2197 O ILE A 275 13802 7235 19878 -704 -163 3148 O ATOM 2198 CB ILE A 275 8.394 56.885 38.570 1.00123.40 C ANISOU 2198 CB ILE A 275 15365 10089 21434 -872 -547 2086 C ATOM 2199 CG1 ILE A 275 8.423 56.655 40.084 1.00112.98 C ANISOU 2199 CG1 ILE A 275 13938 8815 20177 -873 -773 1491 C ATOM 2200 CG2 ILE A 275 9.678 57.567 38.107 1.00102.54 C ANISOU 2200 CG2 ILE A 275 12631 7125 19204 -1228 -351 2296 C ATOM 2201 CD1 ILE A 275 9.590 55.819 40.565 1.00108.92 C ANISOU 2201 CD1 ILE A 275 13178 8610 19598 -1113 -778 1230 C ATOM 2202 N PHE A 276 6.604 57.307 35.834 1.00129.11 N ANISOU 2202 N PHE A 276 16492 10881 21683 -330 -289 3175 N ATOM 2203 CA PHE A 276 6.570 57.651 34.418 1.00144.64 C ANISOU 2203 CA PHE A 276 18577 12814 23564 -232 -71 3745 C ATOM 2204 C PHE A 276 5.553 58.754 34.144 1.00144.01 C ANISOU 2204 C PHE A 276 18731 12364 23621 46 -57 3967 C ATOM 2205 O PHE A 276 5.868 59.753 33.486 1.00147.23 O ANISOU 2205 O PHE A 276 19254 12364 24323 10 151 4347 O ATOM 2206 CB PHE A 276 6.263 56.407 33.585 1.00146.05 C ANISOU 2206 CB PHE A 276 18724 13606 23162 -64 -76 3901 C ATOM 2207 CG PHE A 276 6.453 56.608 32.115 1.00156.35 C ANISOU 2207 CG PHE A 276 20117 14963 24326 35 155 4468 C ATOM 2208 CD1 PHE A 276 7.664 57.063 31.621 1.00163.54 C ANISOU 2208 CD1 PHE A 276 20969 15659 25511 -219 404 4755 C ATOM 2209 CD2 PHE A 276 5.428 56.337 31.225 1.00156.49 C ANISOU 2209 CD2 PHE A 276 20260 15268 23930 395 127 4716 C ATOM 2210 CE1 PHE A 276 7.848 57.251 30.269 1.00165.95 C ANISOU 2210 CE1 PHE A 276 21354 16030 25670 -91 640 5306 C ATOM 2211 CE2 PHE A 276 5.607 56.521 29.870 1.00163.76 C ANISOU 2211 CE2 PHE A 276 21266 16268 24686 535 338 5236 C ATOM 2212 CZ PHE A 276 6.819 56.980 29.394 1.00168.12 C ANISOU 2212 CZ PHE A 276 21774 16600 25502 304 606 5545 C ATOM 2213 N THR A 277 4.328 58.594 34.646 1.00134.51 N ANISOU 2213 N THR A 277 17598 11298 22210 338 -263 3750 N ATOM 2214 CA THR A 277 3.279 59.586 34.435 1.00135.14 C ANISOU 2214 CA THR A 277 17897 11081 22369 654 -267 3939 C ATOM 2215 C THR A 277 3.589 60.879 35.178 1.00144.25 C ANISOU 2215 C THR A 277 19153 11557 24098 527 -248 3806 C ATOM 2216 O THR A 277 3.901 61.900 34.555 1.00147.66 O ANISOU 2216 O THR A 277 19727 11535 24841 492 -43 4168 O ATOM 2217 CB THR A 277 1.921 59.037 34.874 1.00134.73 C ANISOU 2217 CB THR A 277 17850 11385 21955 985 -499 3712 C ATOM 2218 OG1 THR A 277 2.016 58.533 36.213 1.00133.25 O ANISOU 2218 OG1 THR A 277 17522 11285 21821 864 -690 3182 O ATOM 2219 CG2 THR A 277 1.476 57.920 33.943 1.00137.13 C ANISOU 2219 CG2 THR A 277 18089 12293 21721 1139 -514 3899 C ATOM 2220 N HIS A 278 3.508 60.850 36.509 1.00141.56 N ANISOU 2220 N HIS A 278 18746 11135 23904 471 -456 3288 N ATOM 2221 CA HIS A 278 3.844 62.015 37.320 1.00141.36 C ANISOU 2221 CA HIS A 278 18810 10476 24425 344 -482 3072 C ATOM 2222 C HIS A 278 5.350 62.249 37.295 1.00137.30 C ANISOU 2222 C HIS A 278 18161 9689 24317 -121 -340 3072 C ATOM 2223 O HIS A 278 6.012 62.199 38.336 1.00131.27 O ANISOU 2223 O HIS A 278 17256 8827 23793 -360 -470 2619 O ATOM 2224 CB HIS A 278 3.343 61.833 38.756 1.00144.81 C ANISOU 2224 CB HIS A 278 19200 10974 24847 458 -758 2498 C ATOM 2225 CG HIS A 278 1.850 61.837 38.883 1.00151.17 C ANISOU 2225 CG HIS A 278 20134 11957 25348 914 -886 2499 C ATOM 2226 ND1 HIS A 278 1.030 61.080 38.074 1.00153.25 N ANISOU 2226 ND1 HIS A 278 20381 12720 25128 1155 -871 2769 N ATOM 2227 CD2 HIS A 278 1.030 62.503 39.730 1.00155.34 C ANISOU 2227 CD2 HIS A 278 20793 12246 25982 1182 -1038 2253 C ATOM 2228 CE1 HIS A 278 -0.230 61.282 38.415 1.00153.62 C ANISOU 2228 CE1 HIS A 278 20521 12838 25010 1534 -1003 2700 C ATOM 2229 NE2 HIS A 278 -0.258 62.141 39.417 1.00155.97 N ANISOU 2229 NE2 HIS A 278 20915 12699 25648 1571 -1098 2401 N ATOM 2230 N GLN A 279 5.892 62.522 36.111 1.00140.12 N ANISOU 2230 N GLN A 279 18551 9938 24751 -234 -71 3586 N ATOM 2231 CA GLN A 279 7.329 62.533 35.896 1.00147.99 C ANISOU 2231 CA GLN A 279 19367 10812 26049 -670 96 3667 C ATOM 2232 C GLN A 279 7.960 63.791 36.488 1.00153.91 C ANISOU 2232 C GLN A 279 20156 10830 27492 -948 126 3519 C ATOM 2233 O GLN A 279 7.280 64.752 36.855 1.00178.58 O ANISOU 2233 O GLN A 279 23502 13490 30862 -774 61 3449 O ATOM 2234 CB GLN A 279 7.637 62.438 34.402 1.00163.08 C ANISOU 2234 CB GLN A 279 21305 12862 27796 -652 394 4305 C ATOM 2235 CG GLN A 279 8.828 61.564 34.065 1.00173.50 C ANISOU 2235 CG GLN A 279 22364 14552 29005 -955 505 4362 C ATOM 2236 CD GLN A 279 8.865 61.183 32.600 1.00176.25 C ANISOU 2236 CD GLN A 279 22753 15220 28995 -800 747 4950 C ATOM 2237 OE1 GLN A 279 8.609 62.010 31.724 1.00176.88 O ANISOU 2237 OE1 GLN A 279 23015 15005 29188 -650 959 5436 O ATOM 2238 NE2 GLN A 279 9.170 59.921 32.325 1.00171.18 N ANISOU 2238 NE2 GLN A 279 21953 15189 27900 -805 716 4910 N ATOM 2239 N GLY A 280 9.289 63.772 36.579 1.00159.73 N ANISOU 2239 N GLY A 280 20669 11470 28551 -1386 220 3460 N ATOM 2240 CA GLY A 280 10.030 64.934 37.035 1.00132.58 C ANISOU 2240 CA GLY A 280 17228 7430 25717 -1705 260 3300 C ATOM 2241 C GLY A 280 9.749 65.354 38.456 1.00146.50 C ANISOU 2241 C GLY A 280 19025 8943 27694 -1686 -44 2655 C ATOM 2242 O GLY A 280 10.128 66.457 38.848 1.00137.99 O ANISOU 2242 O GLY A 280 18018 7433 26978 -1856 -40 2472 O ATOM 2243 N SER A 281 9.099 64.502 39.246 1.00149.79 N ANISOU 2243 N SER A 281 19399 9708 27808 -1457 -306 2281 N ATOM 2244 CA SER A 281 8.721 64.844 40.609 1.00155.22 C ANISOU 2244 CA SER A 281 20131 10197 28648 -1354 -602 1678 C ATOM 2245 C SER A 281 9.889 64.580 41.560 1.00153.22 C ANISOU 2245 C SER A 281 19585 9994 28640 -1723 -745 1164 C ATOM 2246 O SER A 281 11.003 64.256 41.142 1.00164.10 O ANISOU 2246 O SER A 281 20728 11494 30128 -2081 -601 1298 O ATOM 2247 CB SER A 281 7.466 64.073 41.012 1.00155.66 C ANISOU 2247 CB SER A 281 20265 10749 28129 -895 -788 1515 C ATOM 2248 OG SER A 281 6.340 64.515 40.275 1.00165.04 O ANISOU 2248 OG SER A 281 21723 11826 29157 -537 -696 1919 O ATOM 2249 N ASP A 282 9.638 64.724 42.862 1.00144.55 N ANISOU 2249 N ASP A 282 18489 8829 27604 -1608 -1034 565 N ATOM 2250 CA ASP A 282 10.677 64.569 43.882 1.00144.53 C ANISOU 2250 CA ASP A 282 18220 8921 27774 -1890 -1203 11 C ATOM 2251 C ASP A 282 10.681 63.127 44.393 1.00137.85 C ANISOU 2251 C ASP A 282 17163 8790 26423 -1764 -1333 -246 C ATOM 2252 O ASP A 282 10.357 62.830 45.545 1.00137.62 O ANISOU 2252 O ASP A 282 17104 8954 26231 -1552 -1582 -755 O ATOM 2253 CB ASP A 282 10.460 65.567 45.013 1.00152.00 C ANISOU 2253 CB ASP A 282 19295 9547 28913 -1784 -1422 -501 C ATOM 2254 CG ASP A 282 11.714 65.801 45.837 1.00170.57 C ANISOU 2254 CG ASP A 282 21388 11889 31532 -2137 -1543 -980 C ATOM 2255 OD1 ASP A 282 12.811 65.871 45.245 1.00181.64 O ANISOU 2255 OD1 ASP A 282 22597 13272 33146 -2542 -1363 -773 O ATOM 2256 OD2 ASP A 282 11.601 65.921 47.075 1.00175.27 O ANISOU 2256 OD2 ASP A 282 21965 12526 32103 -1987 -1816 -1557 O ATOM 2257 N PHE A 283 11.066 62.220 43.499 1.00129.18 N ANISOU 2257 N PHE A 283 15931 8140 25012 -1868 -1138 133 N ATOM 2258 CA PHE A 283 11.143 60.806 43.846 1.00116.45 C ANISOU 2258 CA PHE A 283 14134 7244 22866 -1759 -1210 -49 C ATOM 2259 C PHE A 283 12.325 60.566 44.774 1.00134.63 C ANISOU 2259 C PHE A 283 16143 9669 25343 -2029 -1341 -542 C ATOM 2260 O PHE A 283 13.469 60.876 44.426 1.00154.51 O ANISOU 2260 O PHE A 283 18477 12020 28211 -2426 -1226 -455 O ATOM 2261 CB PHE A 283 11.281 59.952 42.590 1.00110.59 C ANISOU 2261 CB PHE A 283 13350 6909 21760 -1794 -969 482 C ATOM 2262 CG PHE A 283 10.217 60.201 41.570 1.00119.73 C ANISOU 2262 CG PHE A 283 14770 7976 22745 -1538 -835 983 C ATOM 2263 CD1 PHE A 283 8.907 59.827 41.813 1.00117.70 C ANISOU 2263 CD1 PHE A 283 14671 7945 22106 -1129 -960 925 C ATOM 2264 CD2 PHE A 283 10.528 60.801 40.363 1.00130.69 C ANISOU 2264 CD2 PHE A 283 16231 9081 24344 -1689 -577 1522 C ATOM 2265 CE1 PHE A 283 7.925 60.054 40.874 1.00121.97 C ANISOU 2265 CE1 PHE A 283 15427 8442 22473 -879 -854 1367 C ATOM 2266 CE2 PHE A 283 9.551 61.030 39.419 1.00138.09 C ANISOU 2266 CE2 PHE A 283 17408 9972 25090 -1411 -458 1979 C ATOM 2267 CZ PHE A 283 8.248 60.656 39.676 1.00136.93 C ANISOU 2267 CZ PHE A 283 17406 10065 24555 -1007 -609 1887 C ATOM 2268 N GLY A 284 12.054 60.017 45.952 1.00127.14 N ANISOU 2268 N GLY A 284 15135 9029 24145 -1800 -1575 -1048 N ATOM 2269 CA GLY A 284 13.112 59.609 46.838 1.00134.47 C ANISOU 2269 CA GLY A 284 15773 10197 25121 -1979 -1705 -1519 C ATOM 2270 C GLY A 284 13.873 58.440 46.249 1.00142.53 C ANISOU 2270 C GLY A 284 16579 11771 25804 -2125 -1539 -1293 C ATOM 2271 O GLY A 284 13.282 57.452 45.804 1.00153.42 O ANISOU 2271 O GLY A 284 18030 13583 26679 -1900 -1452 -1044 O ATOM 2272 N PRO A 285 15.204 58.541 46.205 1.00138.69 N ANISOU 2272 N PRO A 285 15823 11274 25598 -2508 -1490 -1370 N ATOM 2273 CA PRO A 285 16.003 57.380 45.779 1.00131.93 C ANISOU 2273 CA PRO A 285 14746 10991 24389 -2612 -1349 -1214 C ATOM 2274 C PRO A 285 15.757 56.151 46.634 1.00134.14 C ANISOU 2274 C PRO A 285 14970 11870 24126 -2299 -1481 -1552 C ATOM 2275 O PRO A 285 15.953 55.024 46.163 1.00143.47 O ANISOU 2275 O PRO A 285 16091 13546 24873 -2244 -1350 -1340 O ATOM 2276 CB PRO A 285 17.449 57.884 45.897 1.00125.73 C ANISOU 2276 CB PRO A 285 13649 10051 24073 -3058 -1335 -1370 C ATOM 2277 CG PRO A 285 17.373 59.099 46.773 1.00125.52 C ANISOU 2277 CG PRO A 285 13657 9459 24575 -3135 -1557 -1803 C ATOM 2278 CD PRO A 285 16.042 59.714 46.495 1.00132.00 C ANISOU 2278 CD PRO A 285 14852 9890 25414 -2872 -1553 -1588 C ATOM 2279 N ILE A 286 15.334 56.341 47.885 1.00132.58 N ANISOU 2279 N ILE A 286 14801 11634 23939 -2072 -1730 -2066 N ATOM 2280 CA ILE A 286 14.871 55.224 48.702 1.00126.05 C ANISOU 2280 CA ILE A 286 13970 11337 22585 -1705 -1831 -2331 C ATOM 2281 C ILE A 286 13.522 54.725 48.195 1.00119.68 C ANISOU 2281 C ILE A 286 13425 10647 21401 -1391 -1749 -1991 C ATOM 2282 O ILE A 286 13.236 53.521 48.220 1.00123.79 O ANISOU 2282 O ILE A 286 13941 11658 21435 -1189 -1697 -1935 O ATOM 2283 CB ILE A 286 14.800 55.653 50.179 1.00132.43 C ANISOU 2283 CB ILE A 286 14734 12065 23519 -1519 -2113 -2966 C ATOM 2284 CG1 ILE A 286 16.137 56.257 50.618 1.00143.30 C ANISOU 2284 CG1 ILE A 286 15834 13287 25327 -1865 -2219 -3323 C ATOM 2285 CG2 ILE A 286 14.419 54.476 51.068 1.00135.54 C ANISOU 2285 CG2 ILE A 286 15102 13030 23369 -1127 -2186 -3222 C ATOM 2286 CD1 ILE A 286 16.042 57.112 51.868 1.00152.25 C ANISOU 2286 CD1 ILE A 286 16968 14135 26745 -1744 -2517 -3925 C ATOM 2287 N PHE A 287 12.672 55.643 47.724 1.00120.29 N ANISOU 2287 N PHE A 287 13729 10272 21704 -1345 -1737 -1761 N ATOM 2288 CA PHE A 287 11.371 55.274 47.178 1.00124.04 C ANISOU 2288 CA PHE A 287 14430 10848 21854 -1059 -1671 -1430 C ATOM 2289 C PHE A 287 11.491 54.621 45.806 1.00129.97 C ANISOU 2289 C PHE A 287 15196 11815 22371 -1179 -1438 -897 C ATOM 2290 O PHE A 287 10.606 53.850 45.417 1.00108.05 O ANISOU 2290 O PHE A 287 12532 9326 19198 -949 -1393 -688 O ATOM 2291 CB PHE A 287 10.478 56.519 47.121 1.00135.85 C ANISOU 2291 CB PHE A 287 16155 11800 23661 -947 -1734 -1363 C ATOM 2292 CG PHE A 287 9.345 56.426 46.140 1.00138.57 C ANISOU 2292 CG PHE A 287 16712 12153 23785 -759 -1617 -890 C ATOM 2293 CD1 PHE A 287 8.240 55.634 46.405 1.00133.62 C ANISOU 2293 CD1 PHE A 287 16157 11885 22728 -408 -1668 -899 C ATOM 2294 CD2 PHE A 287 9.376 57.152 44.961 1.00139.38 C ANISOU 2294 CD2 PHE A 287 16931 11909 24120 -922 -1452 -433 C ATOM 2295 CE1 PHE A 287 7.195 55.555 45.502 1.00130.50 C ANISOU 2295 CE1 PHE A 287 15926 11522 22136 -240 -1583 -492 C ATOM 2296 CE2 PHE A 287 8.334 57.079 44.055 1.00131.06 C ANISOU 2296 CE2 PHE A 287 16062 10896 22838 -716 -1359 -14 C ATOM 2297 CZ PHE A 287 7.243 56.281 44.325 1.00128.24 C ANISOU 2297 CZ PHE A 287 15757 10916 22052 -381 -1438 -60 C ATOM 2298 N MET A 288 12.575 54.899 45.075 1.00120.55 N ANISOU 2298 N MET A 288 15488 13925 16389 434 -3724 590 N ATOM 2299 CA MET A 288 12.796 54.254 43.784 1.00143.00 C ANISOU 2299 CA MET A 288 18172 16923 19239 187 -3650 644 C ATOM 2300 C MET A 288 12.945 52.744 43.934 1.00145.88 C ANISOU 2300 C MET A 288 18554 17352 19523 178 -3395 588 C ATOM 2301 O MET A 288 12.460 51.979 43.092 1.00135.60 O ANISOU 2301 O MET A 288 17133 16174 18217 35 -3245 603 O ATOM 2302 CB MET A 288 14.039 54.842 43.115 1.00150.57 C ANISOU 2302 CB MET A 288 19076 17903 20232 43 -3869 713 C ATOM 2303 CG MET A 288 13.819 56.151 42.370 1.00154.01 C ANISOU 2303 CG MET A 288 19410 18341 20767 -63 -4115 807 C ATOM 2304 SD MET A 288 13.104 55.892 40.737 1.00154.67 S ANISOU 2304 SD MET A 288 19256 18623 20888 -338 -4039 886 S ATOM 2305 CE MET A 288 13.980 54.418 40.222 1.00155.36 C ANISOU 2305 CE MET A 288 19292 18857 20882 -465 -3841 854 C ATOM 2306 N THR A 289 13.608 52.299 44.999 1.00154.32 N ANISOU 2306 N THR A 289 19771 18332 20531 329 -3351 524 N ATOM 2307 CA THR A 289 13.981 50.901 45.171 1.00148.13 C ANISOU 2307 CA THR A 289 19011 17591 19680 316 -3148 473 C ATOM 2308 C THR A 289 12.927 50.085 45.918 1.00137.64 C ANISOU 2308 C THR A 289 17738 16253 18306 441 -2927 425 C ATOM 2309 O THR A 289 13.189 48.929 46.266 1.00137.06 O ANISOU 2309 O THR A 289 17705 16190 18180 458 -2769 381 O ATOM 2310 CB THR A 289 15.327 50.809 45.900 1.00141.75 C ANISOU 2310 CB THR A 289 18328 16695 18835 396 -3223 440 C ATOM 2311 OG1 THR A 289 16.096 51.987 45.630 1.00124.10 O ANISOU 2311 OG1 THR A 289 16086 14419 16647 357 -3481 496 O ATOM 2312 CG2 THR A 289 16.117 49.594 45.425 1.00142.86 C ANISOU 2312 CG2 THR A 289 18422 16920 18939 279 -3101 415 C ATOM 2313 N ILE A 290 11.750 50.650 46.172 1.00137.19 N ANISOU 2313 N ILE A 290 17677 16181 18268 527 -2920 436 N ATOM 2314 CA ILE A 290 10.660 49.897 46.791 1.00149.03 C ANISOU 2314 CA ILE A 290 19204 17700 19721 630 -2711 410 C ATOM 2315 C ILE A 290 10.150 48.837 45.816 1.00154.77 C ANISOU 2315 C ILE A 290 19798 18553 20453 451 -2539 437 C ATOM 2316 O ILE A 290 9.977 47.678 46.221 1.00149.71 O ANISOU 2316 O ILE A 290 19190 17931 19763 480 -2360 410 O ATOM 2317 CB ILE A 290 9.526 50.823 47.263 1.00150.54 C ANISOU 2317 CB ILE A 290 19411 17858 19928 769 -2753 415 C ATOM 2318 CG1 ILE A 290 10.050 51.832 48.288 1.00148.58 C ANISOU 2318 CG1 ILE A 290 19305 17477 19672 964 -2931 373 C ATOM 2319 CG2 ILE A 290 8.375 50.007 47.842 1.00147.02 C ANISOU 2319 CG2 ILE A 290 18974 17461 19427 862 -2531 404 C ATOM 2320 CD1 ILE A 290 8.991 52.772 48.825 1.00141.28 C ANISOU 2320 CD1 ILE A 290 18404 16516 18760 1127 -2987 358 C ATOM 2321 N PRO A 291 9.890 49.160 44.541 1.00157.88 N ANISOU 2321 N PRO A 291 20044 19035 20907 264 -2591 492 N ATOM 2322 CA PRO A 291 9.516 48.083 43.610 1.00151.29 C ANISOU 2322 CA PRO A 291 19092 18320 20073 94 -2432 509 C ATOM 2323 C PRO A 291 10.648 47.109 43.330 1.00136.71 C ANISOU 2323 C PRO A 291 17245 16503 18194 9 -2389 468 C ATOM 2324 O PRO A 291 10.395 45.906 43.185 1.00139.78 O ANISOU 2324 O PRO A 291 17610 16941 18560 -37 -2223 445 O ATOM 2325 CB PRO A 291 9.088 48.847 42.349 1.00157.92 C ANISOU 2325 CB PRO A 291 19777 19242 20982 -81 -2532 578 C ATOM 2326 CG PRO A 291 9.776 50.150 42.441 1.00165.57 C ANISOU 2326 CG PRO A 291 20776 20144 21989 -50 -2769 597 C ATOM 2327 CD PRO A 291 9.759 50.482 43.897 1.00167.56 C ANISOU 2327 CD PRO A 291 21198 20263 22206 198 -2788 547 C ATOM 2328 N ALA A 292 11.893 47.591 43.255 1.00129.08 N ANISOU 2328 N ALA A 292 16304 15509 17231 -12 -2543 458 N ATOM 2329 CA ALA A 292 13.025 46.704 43.006 1.00119.58 C ANISOU 2329 CA ALA A 292 15098 14340 15996 -83 -2510 414 C ATOM 2330 C ALA A 292 13.229 45.690 44.122 1.00114.15 C ANISOU 2330 C ALA A 292 14543 13572 15256 60 -2376 348 C ATOM 2331 O ALA A 292 13.818 44.632 43.881 1.00116.55 O ANISOU 2331 O ALA A 292 14831 13912 15540 -2 -2293 304 O ATOM 2332 CB ALA A 292 14.301 47.527 42.815 1.00121.05 C ANISOU 2332 CB ALA A 292 15291 14511 16192 -117 -2713 431 C ATOM 2333 N PHE A 293 12.751 45.986 45.331 1.00110.57 N ANISOU 2333 N PHE A 293 14215 13017 14781 249 -2358 340 N ATOM 2334 CA PHE A 293 12.880 45.046 46.440 1.00104.88 C ANISOU 2334 CA PHE A 293 13616 12227 14008 381 -2234 289 C ATOM 2335 C PHE A 293 12.089 43.769 46.178 1.00112.53 C ANISOU 2335 C PHE A 293 14524 13263 14969 318 -2039 287 C ATOM 2336 O PHE A 293 12.618 42.660 46.313 1.00116.14 O ANISOU 2336 O PHE A 293 15006 13713 15409 298 -1955 245 O ATOM 2337 CB PHE A 293 12.421 45.715 47.737 1.00102.92 C ANISOU 2337 CB PHE A 293 13497 11880 13729 595 -2259 286 C ATOM 2338 CG PHE A 293 12.129 44.754 48.856 1.00 99.89 C ANISOU 2338 CG PHE A 293 13210 11457 13286 724 -2105 256 C ATOM 2339 CD1 PHE A 293 13.146 44.285 49.668 1.00100.25 C ANISOU 2339 CD1 PHE A 293 13372 11423 13297 802 -2110 210 C ATOM 2340 CD2 PHE A 293 10.831 44.336 49.107 1.00106.07 C ANISOU 2340 CD2 PHE A 293 13964 12288 14049 764 -1961 284 C ATOM 2341 CE1 PHE A 293 12.876 43.408 50.703 1.00105.67 C ANISOU 2341 CE1 PHE A 293 14141 12077 13931 911 -1977 193 C ATOM 2342 CE2 PHE A 293 10.557 43.457 50.138 1.00112.07 C ANISOU 2342 CE2 PHE A 293 14803 13026 14753 874 -1829 273 C ATOM 2343 CZ PHE A 293 11.582 42.993 50.936 1.00108.22 C ANISOU 2343 CZ PHE A 293 14428 12457 14232 945 -1839 228 C ATOM 2344 N PHE A 294 10.814 43.907 45.809 1.00114.49 N ANISOU 2344 N PHE A 294 14694 13571 15236 285 -1973 335 N ATOM 2345 CA PHE A 294 9.972 42.729 45.619 1.00104.04 C ANISOU 2345 CA PHE A 294 13318 12304 13908 231 -1797 347 C ATOM 2346 C PHE A 294 10.385 41.935 44.385 1.00 97.33 C ANISOU 2346 C PHE A 294 12354 11538 13087 36 -1770 328 C ATOM 2347 O PHE A 294 10.344 40.699 44.394 1.00102.98 O ANISOU 2347 O PHE A 294 13067 12263 13796 4 -1654 303 O ATOM 2348 CB PHE A 294 8.502 43.137 45.521 1.00110.09 C ANISOU 2348 CB PHE A 294 14026 13117 14687 244 -1741 412 C ATOM 2349 CG PHE A 294 7.892 43.532 46.834 1.00108.63 C ANISOU 2349 CG PHE A 294 13946 12873 14455 452 -1715 421 C ATOM 2350 CD1 PHE A 294 7.708 42.594 47.838 1.00100.82 C ANISOU 2350 CD1 PHE A 294 13037 11859 13413 556 -1590 412 C ATOM 2351 CD2 PHE A 294 7.489 44.837 47.061 1.00110.14 C ANISOU 2351 CD2 PHE A 294 14150 13042 14655 543 -1821 437 C ATOM 2352 CE1 PHE A 294 7.144 42.953 49.047 1.00 97.95 C ANISOU 2352 CE1 PHE A 294 12760 11466 12992 749 -1562 421 C ATOM 2353 CE2 PHE A 294 6.924 45.203 48.267 1.00107.32 C ANISOU 2353 CE2 PHE A 294 13884 12645 14246 746 -1797 432 C ATOM 2354 CZ PHE A 294 6.751 44.259 49.261 1.00103.75 C ANISOU 2354 CZ PHE A 294 13506 12186 13728 850 -1662 425 C ATOM 2355 N ALA A 295 10.786 42.624 43.314 1.00 90.62 N ANISOU 2355 N ALA A 295 11406 10756 12270 -96 -1882 341 N ATOM 2356 CA ALA A 295 11.105 41.928 42.071 1.00 86.05 C ANISOU 2356 CA ALA A 295 10703 10282 11709 -281 -1856 320 C ATOM 2357 C ALA A 295 12.433 41.187 42.168 1.00 91.82 C ANISOU 2357 C ALA A 295 11475 10996 12417 -284 -1869 241 C ATOM 2358 O ALA A 295 12.542 40.038 41.722 1.00 80.59 O ANISOU 2358 O ALA A 295 10009 9617 10996 -358 -1780 194 O ATOM 2359 CB ALA A 295 11.125 42.918 40.906 1.00 75.78 C ANISOU 2359 CB ALA A 295 9273 9078 10442 -426 -1977 367 C ATOM 2360 N LYS A 296 13.455 41.824 42.747 1.00 92.80 N ANISOU 2360 N LYS A 296 11685 11053 12524 -201 -1985 225 N ATOM 2361 CA LYS A 296 14.767 41.189 42.837 1.00 90.50 C ANISOU 2361 CA LYS A 296 11429 10745 12211 -202 -2006 155 C ATOM 2362 C LYS A 296 14.734 39.972 43.752 1.00 87.62 C ANISOU 2362 C LYS A 296 11164 10296 11831 -104 -1879 103 C ATOM 2363 O LYS A 296 15.429 38.981 43.500 1.00 86.69 O ANISOU 2363 O LYS A 296 11031 10195 11711 -150 -1842 36 O ATOM 2364 CB LYS A 296 15.808 42.196 43.326 1.00 95.71 C ANISOU 2364 CB LYS A 296 12164 11342 12859 -130 -2166 164 C ATOM 2365 CG LYS A 296 16.223 43.231 42.291 1.00101.48 C ANISOU 2365 CG LYS A 296 12781 12171 13608 -259 -2319 213 C ATOM 2366 CD LYS A 296 17.136 44.284 42.905 1.00104.22 C ANISOU 2366 CD LYS A 296 13217 12433 13950 -174 -2492 239 C ATOM 2367 CE LYS A 296 17.622 45.282 41.864 1.00100.99 C ANISOU 2367 CE LYS A 296 12684 12127 13560 -316 -2663 303 C ATOM 2368 NZ LYS A 296 18.494 44.640 40.841 1.00 99.58 N ANISOU 2368 NZ LYS A 296 12383 12093 13358 -465 -2655 273 N ATOM 2369 N THR A 297 13.937 40.028 44.820 1.00 81.71 N ANISOU 2369 N THR A 297 10514 9464 11070 31 -1817 135 N ATOM 2370 CA THR A 297 13.837 38.909 45.750 1.00 86.63 C ANISOU 2370 CA THR A 297 11227 10013 11677 120 -1704 105 C ATOM 2371 C THR A 297 13.181 37.685 45.122 1.00 87.51 C ANISOU 2371 C THR A 297 11253 10184 11813 16 -1582 96 C ATOM 2372 O THR A 297 13.307 36.584 45.671 1.00 75.63 O ANISOU 2372 O THR A 297 9802 8625 10309 53 -1509 64 O ATOM 2373 CB THR A 297 13.071 39.348 47.001 1.00 82.46 C ANISOU 2373 CB THR A 297 10804 9410 11116 286 -1672 152 C ATOM 2374 OG1 THR A 297 13.567 40.622 47.432 1.00 86.44 O ANISOU 2374 OG1 THR A 297 11376 9863 11605 376 -1805 159 O ATOM 2375 CG2 THR A 297 13.259 38.351 48.136 1.00 78.85 C ANISOU 2375 CG2 THR A 297 10457 8869 10632 391 -1589 128 C ATOM 2376 N SER A 298 12.510 37.839 43.977 1.00 82.00 N ANISOU 2376 N SER A 298 10423 9592 11141 -118 -1571 125 N ATOM 2377 CA SER A 298 11.939 36.684 43.295 1.00 68.33 C ANISOU 2377 CA SER A 298 8609 7915 9437 -224 -1471 112 C ATOM 2378 C SER A 298 13.006 35.683 42.871 1.00 83.08 C ANISOU 2378 C SER A 298 10460 9790 11316 -284 -1479 14 C ATOM 2379 O SER A 298 12.677 34.525 42.600 1.00 93.45 O ANISOU 2379 O SER A 298 11742 11111 12656 -336 -1403 -14 O ATOM 2380 CB SER A 298 11.127 37.129 42.079 1.00 66.58 C ANISOU 2380 CB SER A 298 8248 7810 9240 -365 -1471 159 C ATOM 2381 OG SER A 298 11.971 37.540 41.020 1.00 67.92 O ANISOU 2381 OG SER A 298 8326 8069 9412 -480 -1565 119 O ATOM 2382 N ALA A 299 14.274 36.097 42.814 1.00 76.78 N ANISOU 2382 N ALA A 299 9681 8990 10501 -274 -1577 -38 N ATOM 2383 CA ALA A 299 15.347 35.141 42.572 1.00 75.10 C ANISOU 2383 CA ALA A 299 9463 8778 10294 -303 -1585 -139 C ATOM 2384 C ALA A 299 15.476 34.134 43.706 1.00 82.65 C ANISOU 2384 C ALA A 299 10539 9605 11260 -194 -1524 -167 C ATOM 2385 O ALA A 299 16.117 33.093 43.528 1.00 82.10 O ANISOU 2385 O ALA A 299 10462 9522 11211 -219 -1513 -252 O ATOM 2386 CB ALA A 299 16.675 35.871 42.369 1.00 71.19 C ANISOU 2386 CB ALA A 299 8965 8312 9774 -306 -1706 -172 C ATOM 2387 N VAL A 300 14.878 34.418 44.859 1.00 78.63 N ANISOU 2387 N VAL A 300 10134 9007 10735 -75 -1489 -100 N ATOM 2388 CA VAL A 300 14.942 33.530 46.009 1.00 74.74 C ANISOU 2388 CA VAL A 300 9751 8400 10245 25 -1436 -107 C ATOM 2389 C VAL A 300 13.638 32.766 46.208 1.00 83.63 C ANISOU 2389 C VAL A 300 10860 9524 11390 14 -1329 -46 C ATOM 2390 O VAL A 300 13.660 31.557 46.443 1.00 79.97 O ANISOU 2390 O VAL A 300 10414 9012 10959 5 -1287 -72 O ATOM 2391 CB VAL A 300 15.324 34.329 47.273 1.00 73.18 C ANISOU 2391 CB VAL A 300 9689 8111 10004 177 -1478 -77 C ATOM 2392 CG1 VAL A 300 15.349 33.423 48.494 1.00 69.51 C ANISOU 2392 CG1 VAL A 300 9333 7539 9537 275 -1421 -74 C ATOM 2393 CG2 VAL A 300 16.672 35.005 47.078 1.00 85.68 C ANISOU 2393 CG2 VAL A 300 11291 9688 11575 181 -1595 -128 C ATOM 2394 N TYR A 301 12.490 33.438 46.108 1.00 83.72 N ANISOU 2394 N TYR A 301 10834 9590 11387 12 -1293 40 N ATOM 2395 CA TYR A 301 11.233 32.774 46.427 1.00 80.45 C ANISOU 2395 CA TYR A 301 10407 9178 10983 13 -1193 117 C ATOM 2396 C TYR A 301 10.573 32.097 45.231 1.00 87.19 C ANISOU 2396 C TYR A 301 11137 10108 11884 -138 -1153 119 C ATOM 2397 O TYR A 301 9.674 31.274 45.432 1.00 97.25 O ANISOU 2397 O TYR A 301 12399 11374 13179 -155 -1080 177 O ATOM 2398 CB TYR A 301 10.245 33.751 47.089 1.00 73.39 C ANISOU 2398 CB TYR A 301 9541 8301 10043 107 -1163 214 C ATOM 2399 CG TYR A 301 9.801 34.953 46.283 1.00 84.78 C ANISOU 2399 CG TYR A 301 10905 9825 11483 58 -1203 243 C ATOM 2400 CD1 TYR A 301 8.910 34.821 45.225 1.00 90.50 C ANISOU 2400 CD1 TYR A 301 11508 10637 12241 -71 -1163 281 C ATOM 2401 CD2 TYR A 301 10.226 36.231 46.623 1.00 82.22 C ANISOU 2401 CD2 TYR A 301 10630 9482 11127 142 -1289 238 C ATOM 2402 CE1 TYR A 301 8.488 35.919 44.505 1.00 83.61 C ANISOU 2402 CE1 TYR A 301 10561 9835 11372 -122 -1206 315 C ATOM 2403 CE2 TYR A 301 9.805 37.337 45.912 1.00 75.42 C ANISOU 2403 CE2 TYR A 301 9696 8687 10274 95 -1342 271 C ATOM 2404 CZ TYR A 301 8.938 37.174 44.854 1.00 76.27 C ANISOU 2404 CZ TYR A 301 9679 8884 10417 -40 -1298 310 C ATOM 2405 OH TYR A 301 8.521 38.273 44.141 1.00 74.87 O ANISOU 2405 OH TYR A 301 9424 8769 10253 -95 -1357 348 O ATOM 2406 N ASN A 302 10.983 32.407 44.003 1.00 79.26 N ANISOU 2406 N ASN A 302 10037 9182 10895 -250 -1204 63 N ATOM 2407 CA ASN A 302 10.504 31.612 42.877 1.00 80.58 C ANISOU 2407 CA ASN A 302 10093 9417 11107 -391 -1172 44 C ATOM 2408 C ASN A 302 11.053 30.188 42.946 1.00 83.88 C ANISOU 2408 C ASN A 302 10534 9773 11566 -404 -1167 -37 C ATOM 2409 O ASN A 302 10.307 29.240 42.671 1.00 78.82 O ANISOU 2409 O ASN A 302 9853 9128 10966 -465 -1120 -15 O ATOM 2410 CB ASN A 302 10.864 32.261 41.539 1.00 77.18 C ANISOU 2410 CB ASN A 302 9548 9103 10674 -511 -1230 0 C ATOM 2411 CG ASN A 302 9.937 33.400 41.181 1.00 86.22 C ANISOU 2411 CG ASN A 302 10634 10318 11806 -544 -1227 96 C ATOM 2412 OD1 ASN A 302 8.784 33.433 41.611 1.00 84.35 O ANISOU 2412 OD1 ASN A 302 10410 10067 11573 -513 -1160 189 O ATOM 2413 ND2 ASN A 302 10.432 34.341 40.387 1.00103.20 N ANISOU 2413 ND2 ASN A 302 12716 12553 13944 -611 -1306 78 N ATOM 2414 N PRO A 303 12.333 29.977 43.288 1.00 90.05 N ANISOU 2414 N PRO A 303 11375 10499 12343 -352 -1223 -130 N ATOM 2415 CA PRO A 303 12.777 28.591 43.519 1.00 82.08 C ANISOU 2415 CA PRO A 303 10397 9409 11381 -348 -1223 -201 C ATOM 2416 C PRO A 303 12.055 27.915 44.671 1.00 73.98 C ANISOU 2416 C PRO A 303 9452 8284 10372 -277 -1168 -114 C ATOM 2417 O PRO A 303 11.787 26.711 44.605 1.00 83.06 O ANISOU 2417 O PRO A 303 10590 9390 11579 -319 -1156 -126 O ATOM 2418 CB PRO A 303 14.278 28.746 43.798 1.00 87.36 C ANISOU 2418 CB PRO A 303 11122 10039 12033 -289 -1295 -300 C ATOM 2419 CG PRO A 303 14.657 29.995 43.110 1.00 90.73 C ANISOU 2419 CG PRO A 303 11490 10569 12414 -323 -1343 -305 C ATOM 2420 CD PRO A 303 13.480 30.906 43.255 1.00 86.10 C ANISOU 2420 CD PRO A 303 10894 10016 11803 -317 -1302 -182 C ATOM 2421 N VAL A 304 11.728 28.655 45.732 1.00 68.09 N ANISOU 2421 N VAL A 304 8786 7508 9576 -171 -1141 -24 N ATOM 2422 CA VAL A 304 11.024 28.051 46.861 1.00 77.94 C ANISOU 2422 CA VAL A 304 10100 8689 10825 -104 -1087 71 C ATOM 2423 C VAL A 304 9.643 27.570 46.434 1.00 83.09 C ANISOU 2423 C VAL A 304 10674 9393 11505 -185 -1024 165 C ATOM 2424 O VAL A 304 9.206 26.474 46.806 1.00 87.91 O ANISOU 2424 O VAL A 304 11293 9953 12157 -201 -1004 211 O ATOM 2425 CB VAL A 304 10.947 29.044 48.036 1.00 76.82 C ANISOU 2425 CB VAL A 304 10051 8528 10610 35 -1072 138 C ATOM 2426 CG1 VAL A 304 9.917 28.589 49.058 1.00 70.21 C ANISOU 2426 CG1 VAL A 304 9248 7675 9753 92 -1000 262 C ATOM 2427 CG2 VAL A 304 12.312 29.191 48.689 1.00 81.08 C ANISOU 2427 CG2 VAL A 304 10688 8985 11134 119 -1136 58 C ATOM 2428 N ILE A 305 8.944 28.366 45.626 1.00 80.03 N ANISOU 2428 N ILE A 305 10204 9103 11099 -243 -1002 203 N ATOM 2429 CA ILE A 305 7.577 28.029 45.244 1.00 72.45 C ANISOU 2429 CA ILE A 305 9170 8196 10161 -318 -940 307 C ATOM 2430 C ILE A 305 7.561 27.000 44.121 1.00 75.29 C ANISOU 2430 C ILE A 305 9448 8564 10593 -454 -962 247 C ATOM 2431 O ILE A 305 6.816 26.015 44.172 1.00 87.11 O ANISOU 2431 O ILE A 305 10926 10035 12136 -500 -937 311 O ATOM 2432 CB ILE A 305 6.811 29.305 44.851 1.00 77.52 C ANISOU 2432 CB ILE A 305 9758 8935 10762 -325 -912 374 C ATOM 2433 CG1 ILE A 305 6.663 30.218 46.068 1.00 78.89 C ANISOU 2433 CG1 ILE A 305 10015 9094 10865 -173 -892 436 C ATOM 2434 CG2 ILE A 305 5.454 28.959 44.253 1.00 73.96 C ANISOU 2434 CG2 ILE A 305 9216 8545 10339 -422 -853 474 C ATOM 2435 CD1 ILE A 305 5.934 31.492 45.780 1.00 59.61 C ANISOU 2435 CD1 ILE A 305 7528 6734 8389 -162 -879 494 C ATOM 2436 N TYR A 306 8.384 27.205 43.096 1.00 71.91 N ANISOU 2436 N TYR A 306 8969 8179 10176 -519 -1015 124 N ATOM 2437 CA TYR A 306 8.314 26.395 41.888 1.00 76.00 C ANISOU 2437 CA TYR A 306 9395 8733 10750 -648 -1037 56 C ATOM 2438 C TYR A 306 9.260 25.199 41.892 1.00 84.38 C ANISOU 2438 C TYR A 306 10485 9712 11864 -646 -1095 -69 C ATOM 2439 O TYR A 306 9.129 24.331 41.021 1.00 83.88 O ANISOU 2439 O TYR A 306 10357 9660 11855 -737 -1119 -129 O ATOM 2440 CB TYR A 306 8.598 27.265 40.659 1.00 75.76 C ANISOU 2440 CB TYR A 306 9268 8822 10693 -732 -1062 -6 C ATOM 2441 CG TYR A 306 7.514 28.278 40.366 1.00 86.26 C ANISOU 2441 CG TYR A 306 10543 10236 11995 -769 -1016 113 C ATOM 2442 CD1 TYR A 306 7.458 29.486 41.049 1.00 87.86 C ANISOU 2442 CD1 TYR A 306 10792 10445 12145 -680 -1009 177 C ATOM 2443 CD2 TYR A 306 6.547 28.026 39.403 1.00 89.64 C ANISOU 2443 CD2 TYR A 306 10874 10732 12455 -892 -987 158 C ATOM 2444 CE1 TYR A 306 6.468 30.412 40.782 1.00 86.68 C ANISOU 2444 CE1 TYR A 306 10590 10366 11978 -708 -976 278 C ATOM 2445 CE2 TYR A 306 5.555 28.946 39.128 1.00 95.63 C ANISOU 2445 CE2 TYR A 306 11579 11563 13194 -929 -947 267 C ATOM 2446 CZ TYR A 306 5.520 30.136 39.820 1.00 92.83 C ANISOU 2446 CZ TYR A 306 11268 11212 12791 -835 -943 325 C ATOM 2447 OH TYR A 306 4.532 31.054 39.548 1.00104.52 O ANISOU 2447 OH TYR A 306 12694 12760 14260 -866 -912 427 O ATOM 2448 N ILE A 307 10.200 25.123 42.834 1.00 84.52 N ANISOU 2448 N ILE A 307 10599 9645 11871 -543 -1125 -113 N ATOM 2449 CA ILE A 307 11.126 23.995 42.889 1.00 81.21 C ANISOU 2449 CA ILE A 307 10208 9138 11509 -534 -1187 -233 C ATOM 2450 C ILE A 307 10.993 23.274 44.224 1.00 77.32 C ANISOU 2450 C ILE A 307 9816 8518 11046 -455 -1182 -160 C ATOM 2451 O ILE A 307 10.653 22.087 44.267 1.00 80.55 O ANISOU 2451 O ILE A 307 10221 8857 11528 -494 -1206 -151 O ATOM 2452 CB ILE A 307 12.583 24.442 42.660 1.00 76.32 C ANISOU 2452 CB ILE A 307 9600 8539 10859 -497 -1244 -371 C ATOM 2453 CG1 ILE A 307 12.744 25.103 41.289 1.00 71.75 C ANISOU 2453 CG1 ILE A 307 8906 8109 10249 -588 -1257 -437 C ATOM 2454 CG2 ILE A 307 13.527 23.259 42.803 1.00 81.15 C ANISOU 2454 CG2 ILE A 307 10245 9056 11534 -476 -1308 -496 C ATOM 2455 CD1 ILE A 307 12.484 24.173 40.126 1.00 76.40 C ANISOU 2455 CD1 ILE A 307 9396 8743 10888 -696 -1276 -519 C ATOM 2456 N MET A 308 11.266 23.984 45.323 1.00 76.05 N ANISOU 2456 N MET A 308 9742 8325 10827 -348 -1161 -105 N ATOM 2457 CA MET A 308 11.264 23.349 46.638 1.00 75.35 C ANISOU 2457 CA MET A 308 9748 8127 10755 -271 -1161 -38 C ATOM 2458 C MET A 308 9.888 22.814 47.016 1.00 76.34 C ANISOU 2458 C MET A 308 9853 8253 10898 -302 -1111 118 C ATOM 2459 O MET A 308 9.790 21.810 47.730 1.00 84.28 O ANISOU 2459 O MET A 308 10898 9170 11953 -293 -1134 165 O ATOM 2460 CB MET A 308 11.760 24.332 47.698 1.00 84.44 C ANISOU 2460 CB MET A 308 10993 9262 11828 -148 -1145 -8 C ATOM 2461 CG MET A 308 13.273 24.372 47.842 1.00102.05 C ANISOU 2461 CG MET A 308 13280 11431 14062 -98 -1213 -140 C ATOM 2462 SD MET A 308 13.819 25.613 49.027 1.00125.61 S ANISOU 2462 SD MET A 308 16378 14395 16954 43 -1206 -101 S ATOM 2463 CE MET A 308 12.684 25.308 50.378 1.00126.98 C ANISOU 2463 CE MET A 308 16609 14537 17101 109 -1138 66 C ATOM 2464 N MET A 309 8.819 23.462 46.561 1.00 78.95 N ANISOU 2464 N MET A 309 10120 8684 11193 -342 -1050 209 N ATOM 2465 CA MET A 309 7.469 22.974 46.805 1.00 81.37 C ANISOU 2465 CA MET A 309 10393 9010 11515 -382 -1002 365 C ATOM 2466 C MET A 309 7.009 21.976 45.750 1.00 84.53 C ANISOU 2466 C MET A 309 10711 9404 12003 -512 -1036 346 C ATOM 2467 O MET A 309 5.819 21.645 45.700 1.00 84.44 O ANISOU 2467 O MET A 309 10653 9422 12007 -568 -1002 479 O ATOM 2468 CB MET A 309 6.489 24.146 46.897 1.00 85.59 C ANISOU 2468 CB MET A 309 10899 9653 11969 -353 -919 480 C ATOM 2469 CG MET A 309 6.550 24.880 48.229 1.00 95.72 C ANISOU 2469 CG MET A 309 12266 10935 13167 -211 -882 545 C ATOM 2470 SD MET A 309 5.326 26.193 48.394 1.00107.01 S ANISOU 2470 SD MET A 309 13659 12492 14507 -160 -794 672 S ATOM 2471 CE MET A 309 5.241 26.342 50.178 1.00110.63 C ANISOU 2471 CE MET A 309 14217 12934 14882 1 -757 765 C ATOM 2472 N ASN A 310 7.921 21.499 44.908 1.00 80.50 N ANISOU 2472 N ASN A 310 10179 8861 11546 -559 -1107 182 N ATOM 2473 CA ASN A 310 7.660 20.407 43.980 1.00 76.15 C ANISOU 2473 CA ASN A 310 9564 8284 11086 -667 -1162 133 C ATOM 2474 C ASN A 310 8.169 19.123 44.625 1.00 86.26 C ANISOU 2474 C ASN A 310 10902 9424 12450 -646 -1244 101 C ATOM 2475 O ASN A 310 9.347 19.036 44.991 1.00 81.43 O ANISOU 2475 O ASN A 310 10348 8750 11843 -581 -1290 -14 O ATOM 2476 CB ASN A 310 8.341 20.671 42.635 1.00 74.75 C ANISOU 2476 CB ASN A 310 9317 8175 10908 -725 -1195 -37 C ATOM 2477 CG ASN A 310 8.059 19.594 41.600 1.00 85.33 C ANISOU 2477 CG ASN A 310 10588 9500 12335 -830 -1254 -103 C ATOM 2478 OD1 ASN A 310 8.296 18.408 41.830 1.00102.04 O ANISOU 2478 OD1 ASN A 310 12732 11503 14534 -832 -1330 -144 O ATOM 2479 ND2 ASN A 310 7.560 20.010 40.441 1.00 79.85 N ANISOU 2479 ND2 ASN A 310 9802 8917 11623 -920 -1229 -117 N ATOM 2480 N LYS A 311 7.279 18.136 44.770 1.00 89.64 N ANISOU 2480 N LYS A 311 11312 9798 12947 -706 -1271 211 N ATOM 2481 CA LYS A 311 7.628 16.914 45.491 1.00 93.10 C ANISOU 2481 CA LYS A 311 11803 10096 13473 -693 -1361 213 C ATOM 2482 C LYS A 311 8.821 16.209 44.859 1.00 92.69 C ANISOU 2482 C LYS A 311 11755 9966 13498 -698 -1465 -5 C ATOM 2483 O LYS A 311 9.716 15.732 45.567 1.00 86.51 O ANISOU 2483 O LYS A 311 11039 9080 12752 -637 -1526 -65 O ATOM 2484 CB LYS A 311 6.426 15.970 45.543 1.00110.29 C ANISOU 2484 CB LYS A 311 13944 12240 15722 -777 -1391 370 C ATOM 2485 CG LYS A 311 5.254 16.480 46.362 1.00133.07 C ANISOU 2485 CG LYS A 311 16825 15200 18535 -763 -1296 601 C ATOM 2486 CD LYS A 311 4.107 15.482 46.342 1.00145.14 C ANISOU 2486 CD LYS A 311 18308 16700 20139 -858 -1340 764 C ATOM 2487 CE LYS A 311 2.899 16.004 47.101 1.00146.05 C ANISOU 2487 CE LYS A 311 18403 16918 20172 -843 -1240 998 C ATOM 2488 NZ LYS A 311 1.731 15.090 46.966 1.00142.49 N ANISOU 2488 NZ LYS A 311 17894 16455 19791 -949 -1284 1171 N ATOM 2489 N GLN A 312 8.853 16.134 43.527 1.00 94.54 N ANISOU 2489 N GLN A 312 11912 10255 13753 -767 -1489 -126 N ATOM 2490 CA GLN A 312 9.928 15.414 42.853 1.00 98.94 C ANISOU 2490 CA GLN A 312 12459 10757 14378 -768 -1591 -343 C ATOM 2491 C GLN A 312 11.272 16.104 43.054 1.00101.24 C ANISOU 2491 C GLN A 312 12789 11070 14607 -679 -1579 -476 C ATOM 2492 O GLN A 312 12.293 15.438 43.257 1.00102.28 O ANISOU 2492 O GLN A 312 12957 11108 14796 -634 -1662 -606 O ATOM 2493 CB GLN A 312 9.607 15.273 41.365 1.00107.65 C ANISOU 2493 CB GLN A 312 13463 11942 15498 -859 -1609 -439 C ATOM 2494 CG GLN A 312 10.353 14.145 40.673 1.00120.26 C ANISOU 2494 CG GLN A 312 15038 13464 17190 -871 -1737 -640 C ATOM 2495 CD GLN A 312 9.945 13.984 39.222 1.00131.59 C ANISOU 2495 CD GLN A 312 16374 14990 18635 -961 -1756 -730 C ATOM 2496 OE1 GLN A 312 9.667 14.964 38.530 1.00130.60 O ANISOU 2496 OE1 GLN A 312 16187 15015 18421 -1000 -1670 -717 O ATOM 2497 NE2 GLN A 312 9.900 12.742 38.754 1.00136.14 N ANISOU 2497 NE2 GLN A 312 16933 15472 19322 -996 -1877 -820 N ATOM 2498 N PHE A 313 11.294 17.439 43.006 1.00 97.63 N ANISOU 2498 N PHE A 313 12323 10732 14039 -653 -1486 -442 N ATOM 2499 CA PHE A 313 12.547 18.161 43.206 1.00 89.98 C ANISOU 2499 CA PHE A 313 11391 9787 13009 -574 -1483 -550 C ATOM 2500 C PHE A 313 12.971 18.148 44.668 1.00 90.52 C ANISOU 2500 C PHE A 313 11571 9748 13073 -477 -1483 -481 C ATOM 2501 O PHE A 313 14.160 18.000 44.974 1.00 89.60 O ANISOU 2501 O PHE A 313 11502 9573 12969 -416 -1533 -594 O ATOM 2502 CB PHE A 313 12.416 19.599 42.707 1.00 83.47 C ANISOU 2502 CB PHE A 313 10523 9115 12077 -582 -1403 -524 C ATOM 2503 CG PHE A 313 12.787 19.777 41.265 1.00 82.92 C ANISOU 2503 CG PHE A 313 10349 9165 11991 -650 -1425 -666 C ATOM 2504 CD1 PHE A 313 14.104 20.006 40.900 1.00 81.79 C ANISOU 2504 CD1 PHE A 313 10194 9064 11820 -615 -1467 -824 C ATOM 2505 CD2 PHE A 313 11.822 19.719 40.274 1.00 85.57 C ANISOU 2505 CD2 PHE A 313 10595 9583 12336 -753 -1403 -636 C ATOM 2506 CE1 PHE A 313 14.451 20.172 39.573 1.00 83.67 C ANISOU 2506 CE1 PHE A 313 10324 9437 12031 -679 -1486 -950 C ATOM 2507 CE2 PHE A 313 12.162 19.884 38.945 1.00 81.30 C ANISOU 2507 CE2 PHE A 313 9952 9167 11771 -819 -1423 -765 C ATOM 2508 CZ PHE A 313 13.478 20.111 38.594 1.00 80.43 C ANISOU 2508 CZ PHE A 313 9822 9111 11624 -782 -1464 -922 C ATOM 2509 N ARG A 314 12.016 18.309 45.586 1.00 89.49 N ANISOU 2509 N ARG A 314 11480 9600 12922 -463 -1428 -294 N ATOM 2510 CA ARG A 314 12.360 18.384 47.001 1.00 87.77 C ANISOU 2510 CA ARG A 314 11364 9301 12683 -371 -1421 -219 C ATOM 2511 C ARG A 314 12.944 17.068 47.502 1.00 91.18 C ANISOU 2511 C ARG A 314 11841 9581 13223 -365 -1522 -270 C ATOM 2512 O ARG A 314 13.889 17.066 48.299 1.00 93.63 O ANISOU 2512 O ARG A 314 12228 9816 13531 -290 -1549 -311 O ATOM 2513 CB ARG A 314 11.128 18.782 47.812 1.00 87.41 C ANISOU 2513 CB ARG A 314 11334 9295 12584 -359 -1339 -8 C ATOM 2514 CG ARG A 314 11.318 18.786 49.317 1.00 90.35 C ANISOU 2514 CG ARG A 314 11803 9600 12928 -268 -1329 88 C ATOM 2515 CD ARG A 314 10.012 19.154 49.997 1.00 99.28 C ANISOU 2515 CD ARG A 314 12926 10801 13994 -258 -1246 291 C ATOM 2516 NE ARG A 314 8.891 18.417 49.418 1.00103.82 N ANISOU 2516 NE ARG A 314 13421 11397 14630 -363 -1252 380 N ATOM 2517 CZ ARG A 314 7.616 18.761 49.561 1.00113.22 C ANISOU 2517 CZ ARG A 314 14568 12679 15769 -382 -1177 545 C ATOM 2518 NH1 ARG A 314 7.292 19.838 50.262 1.00121.04 N ANISOU 2518 NH1 ARG A 314 15587 13755 16648 -295 -1089 628 N ATOM 2519 NH2 ARG A 314 6.664 18.031 48.996 1.00117.24 N ANISOU 2519 NH2 ARG A 314 15006 13198 16343 -485 -1195 625 N ATOM 2520 N ASN A 315 12.406 15.936 47.035 1.00 90.38 N ANISOU 2520 N ASN A 315 11692 9425 13223 -444 -1588 -268 N ATOM 2521 CA ASN A 315 12.943 14.642 47.449 1.00 89.06 C ANISOU 2521 CA ASN A 315 11561 9102 13175 -444 -1707 -321 C ATOM 2522 C ASN A 315 14.370 14.450 46.950 1.00 90.49 C ANISOU 2522 C ASN A 315 11748 9244 13389 -405 -1777 -548 C ATOM 2523 O ASN A 315 15.240 13.985 47.695 1.00100.12 O ANISOU 2523 O ASN A 315 13035 10350 14656 -351 -1840 -594 O ATOM 2524 CB ASN A 315 12.046 13.509 46.949 1.00 96.07 C ANISOU 2524 CB ASN A 315 12393 9938 14171 -541 -1782 -276 C ATOM 2525 CG ASN A 315 10.673 13.516 47.598 1.00105.49 C ANISOU 2525 CG ASN A 315 13580 11158 15342 -581 -1729 -31 C ATOM 2526 OD1 ASN A 315 10.473 14.120 48.653 1.00116.32 O ANISOU 2526 OD1 ASN A 315 15001 12559 16635 -525 -1655 102 O ATOM 2527 ND2 ASN A 315 9.721 12.832 46.973 1.00 93.68 N ANISOU 2527 ND2 ASN A 315 12021 9658 13915 -676 -1771 29 N ATOM 2528 N CYS A 316 14.630 14.809 45.691 1.00 80.61 N ANISOU 2528 N CYS A 316 10422 8096 12109 -433 -1767 -688 N ATOM 2529 CA CYS A 316 15.979 14.688 45.150 1.00 81.43 C ANISOU 2529 CA CYS A 316 10516 8197 12227 -393 -1827 -903 C ATOM 2530 C CYS A 316 16.958 15.630 45.839 1.00 93.36 C ANISOU 2530 C CYS A 316 12093 9725 13654 -304 -1783 -915 C ATOM 2531 O CYS A 316 18.135 15.289 45.994 1.00106.36 O ANISOU 2531 O CYS A 316 13771 11308 15335 -251 -1848 -1046 O ATOM 2532 CB CYS A 316 15.962 14.948 43.646 1.00 84.42 C ANISOU 2532 CB CYS A 316 10787 8716 12574 -448 -1818 -1032 C ATOM 2533 SG CYS A 316 14.979 13.755 42.713 1.00 87.96 S ANISOU 2533 SG CYS A 316 11159 9134 13130 -548 -1893 -1055 S ATOM 2534 N MET A 317 16.501 16.813 46.257 1.00 96.39 N ANISOU 2534 N MET A 317 12500 10192 13931 -283 -1682 -784 N ATOM 2535 CA MET A 317 17.406 17.743 46.925 1.00100.33 C ANISOU 2535 CA MET A 317 13068 10700 14352 -197 -1653 -790 C ATOM 2536 C MET A 317 17.705 17.300 48.351 1.00101.99 C ANISOU 2536 C MET A 317 13388 10766 14599 -133 -1679 -716 C ATOM 2537 O MET A 317 18.829 17.472 48.835 1.00100.08 O ANISOU 2537 O MET A 317 13207 10472 14347 -65 -1709 -784 O ATOM 2538 CB MET A 317 16.826 19.156 46.910 1.00101.16 C ANISOU 2538 CB MET A 317 13165 10931 14339 -189 -1554 -682 C ATOM 2539 CG MET A 317 16.886 19.827 45.548 1.00108.09 C ANISOU 2539 CG MET A 317 13940 11962 15167 -244 -1537 -768 C ATOM 2540 SD MET A 317 16.459 21.578 45.591 1.00106.50 S ANISOU 2540 SD MET A 317 13737 11889 14838 -225 -1451 -656 S ATOM 2541 CE MET A 317 14.755 21.501 46.133 1.00113.51 C ANISOU 2541 CE MET A 317 14632 12769 15727 -250 -1377 -458 C ATOM 2542 N VAL A 318 16.714 16.735 49.043 1.00100.55 N ANISOU 2542 N VAL A 318 13227 10523 14454 -157 -1672 -568 N ATOM 2543 CA VAL A 318 16.965 16.206 50.381 1.00 97.94 C ANISOU 2543 CA VAL A 318 12989 10062 14162 -110 -1707 -490 C ATOM 2544 C VAL A 318 17.938 15.038 50.309 1.00100.75 C ANISOU 2544 C VAL A 318 13356 10283 14641 -112 -1829 -631 C ATOM 2545 O VAL A 318 18.824 14.892 51.160 1.00102.57 O ANISOU 2545 O VAL A 318 13664 10417 14890 -53 -1867 -652 O ATOM 2546 CB VAL A 318 15.643 15.806 51.061 1.00 88.02 C ANISOU 2546 CB VAL A 318 11733 8794 12917 -148 -1680 -290 C ATOM 2547 CG1 VAL A 318 15.917 15.047 52.350 1.00 83.63 C ANISOU 2547 CG1 VAL A 318 11255 8105 12418 -121 -1737 -213 C ATOM 2548 CG2 VAL A 318 14.806 17.040 51.345 1.00 89.10 C ANISOU 2548 CG2 VAL A 318 11871 9060 12923 -118 -1558 -155 C ATOM 2549 N THR A 319 17.796 14.194 49.286 1.00 96.97 N ANISOU 2549 N THR A 319 12800 9793 14250 -177 -1898 -735 N ATOM 2550 CA THR A 319 18.740 13.100 49.089 1.00 97.34 C ANISOU 2550 CA THR A 319 12849 9718 14418 -170 -2025 -896 C ATOM 2551 C THR A 319 20.146 13.629 48.835 1.00 96.22 C ANISOU 2551 C THR A 319 12720 9606 14233 -101 -2029 -1062 C ATOM 2552 O THR A 319 21.119 13.158 49.435 1.00 97.48 O ANISOU 2552 O THR A 319 12937 9650 14450 -51 -2099 -1127 O ATOM 2553 CB THR A 319 18.279 12.219 47.929 1.00 98.58 C ANISOU 2553 CB THR A 319 12914 9878 14663 -244 -2097 -991 C ATOM 2554 OG1 THR A 319 17.143 11.444 48.334 1.00 95.92 O ANISOU 2554 OG1 THR A 319 12577 9467 14401 -310 -2134 -835 O ATOM 2555 CG2 THR A 319 19.395 11.290 47.495 1.00108.55 C ANISOU 2555 CG2 THR A 319 14165 11048 16031 -218 -2224 -1206 C ATOM 2556 N THR A 320 20.269 14.624 47.954 1.00 95.39 N ANISOU 2556 N THR A 320 12558 9659 14025 -101 -1959 -1121 N ATOM 2557 CA THR A 320 21.585 15.151 47.611 1.00 90.40 C ANISOU 2557 CA THR A 320 11922 9080 13345 -45 -1969 -1268 C ATOM 2558 C THR A 320 22.213 15.892 48.786 1.00 93.70 C ANISOU 2558 C THR A 320 12446 9452 13704 32 -1935 -1187 C ATOM 2559 O THR A 320 23.406 15.724 49.066 1.00103.40 O ANISOU 2559 O THR A 320 13714 10618 14957 86 -1989 -1285 O ATOM 2560 CB THR A 320 21.479 16.066 46.392 1.00 84.78 C ANISOU 2560 CB THR A 320 11114 8561 12536 -78 -1909 -1324 C ATOM 2561 OG1 THR A 320 21.021 15.308 45.264 1.00 91.66 O ANISOU 2561 OG1 THR A 320 11888 9475 13465 -145 -1950 -1421 O ATOM 2562 CG2 THR A 320 22.830 16.683 46.065 1.00 77.73 C ANISOU 2562 CG2 THR A 320 10208 7742 11582 -26 -1922 -1451 C ATOM 2563 N LEU A 321 21.428 16.711 49.490 1.00 91.48 N ANISOU 2563 N LEU A 321 12213 9201 13343 41 -1850 -1013 N ATOM 2564 CA LEU A 321 21.974 17.468 50.611 1.00 93.35 C ANISOU 2564 CA LEU A 321 12554 9399 13516 120 -1821 -938 C ATOM 2565 C LEU A 321 22.303 16.568 51.797 1.00101.50 C ANISOU 2565 C LEU A 321 13675 10260 14632 150 -1881 -898 C ATOM 2566 O LEU A 321 23.251 16.849 52.539 1.00102.34 O ANISOU 2566 O LEU A 321 13861 10303 14720 215 -1898 -910 O ATOM 2567 CB LEU A 321 21.000 18.569 51.031 1.00 85.83 C ANISOU 2567 CB LEU A 321 11624 8531 12455 132 -1721 -774 C ATOM 2568 CG LEU A 321 20.788 19.709 50.030 1.00 87.00 C ANISOU 2568 CG LEU A 321 11701 8845 12511 111 -1667 -795 C ATOM 2569 CD1 LEU A 321 19.804 20.735 50.575 1.00 89.49 C ANISOU 2569 CD1 LEU A 321 12047 9222 12733 135 -1581 -634 C ATOM 2570 CD2 LEU A 321 22.112 20.367 49.673 1.00 82.34 C ANISOU 2570 CD2 LEU A 321 11113 8294 11878 150 -1700 -910 C ATOM 2571 N CYS A 322 21.546 15.490 51.993 1.00106.22 N ANISOU 2571 N CYS A 322 14258 10778 15324 97 -1921 -841 N ATOM 2572 CA CYS A 322 21.811 14.550 53.083 1.00112.93 C ANISOU 2572 CA CYS A 322 15179 11465 16266 109 -1994 -793 C ATOM 2573 C CYS A 322 22.706 13.398 52.650 1.00126.97 C ANISOU 2573 C CYS A 322 16934 13130 18180 98 -2120 -962 C ATOM 2574 O CYS A 322 22.504 12.253 53.066 1.00129.07 O ANISOU 2574 O CYS A 322 17208 13265 18566 63 -2210 -934 O ATOM 2575 CB CYS A 322 20.497 14.033 53.658 1.00110.61 C ANISOU 2575 CB CYS A 322 14881 11148 15999 55 -1982 -612 C ATOM 2576 SG CYS A 322 19.588 15.263 54.625 1.00117.97 S ANISOU 2576 SG CYS A 322 15864 12186 16774 98 -1846 -401 S ATOM 2577 N CYS A 323 23.693 13.679 51.799 1.00134.07 N ANISOU 2577 N CYS A 323 17796 14083 19063 128 -2136 -1139 N ATOM 2578 CA CYS A 323 24.792 12.792 51.428 1.00131.75 C ANISOU 2578 CA CYS A 323 17483 13701 18875 147 -2248 -1325 C ATOM 2579 C CYS A 323 24.353 11.553 50.653 1.00125.67 C ANISOU 2579 C CYS A 323 16636 12881 18232 89 -2344 -1417 C ATOM 2580 O CYS A 323 25.212 10.746 50.278 1.00127.72 O ANISOU 2580 O CYS A 323 16872 13068 18587 110 -2449 -1588 O ATOM 2581 CB CYS A 323 25.611 12.353 52.650 1.00138.17 C ANISOU 2581 CB CYS A 323 18397 14349 19753 193 -2310 -1299 C ATOM 2582 SG CYS A 323 26.231 13.739 53.641 1.00153.15 S ANISOU 2582 SG CYS A 323 20399 16282 21510 269 -2219 -1200 S ATOM 2583 N GLY A 324 23.058 11.365 50.403 1.00121.15 N ANISOU 2583 N GLY A 324 16023 12342 17666 19 -2320 -1311 N ATOM 2584 CA GLY A 324 22.628 10.298 49.519 1.00113.01 C ANISOU 2584 CA GLY A 324 14915 11277 16746 -36 -2415 -1406 C ATOM 2585 C GLY A 324 21.556 9.365 50.049 1.00117.02 C ANISOU 2585 C GLY A 324 15435 11671 17358 -105 -2479 -1257 C ATOM 2586 O GLY A 324 21.179 8.412 49.359 1.00116.26 O ANISOU 2586 O GLY A 324 15280 11525 17368 -154 -2579 -1329 O ATOM 2587 N LYS A 325 21.048 9.614 51.255 1.00120.69 N ANISOU 2587 N LYS A 325 15968 12098 17790 -111 -2432 -1048 N ATOM 2588 CA LYS A 325 20.071 8.720 51.873 1.00134.33 C ANISOU 2588 CA LYS A 325 17701 13726 19611 -181 -2500 -882 C ATOM 2589 C LYS A 325 18.984 9.541 52.552 1.00137.74 C ANISOU 2589 C LYS A 325 18152 14260 19922 -199 -2370 -647 C ATOM 2590 O LYS A 325 19.247 10.196 53.566 1.00134.65 O ANISOU 2590 O LYS A 325 17833 13879 19449 -147 -2301 -552 O ATOM 2591 CB LYS A 325 20.735 7.783 52.881 1.00139.81 C ANISOU 2591 CB LYS A 325 18459 14230 20431 -170 -2628 -870 C ATOM 2592 CG LYS A 325 21.665 6.750 52.273 1.00141.00 C ANISOU 2592 CG LYS A 325 18587 14256 20731 -156 -2785 -1092 C ATOM 2593 CD LYS A 325 22.261 5.860 53.352 1.00139.85 C ANISOU 2593 CD LYS A 325 18506 13916 20715 -153 -2915 -1059 C ATOM 2594 CE LYS A 325 23.259 4.879 52.766 1.00139.05 C ANISOU 2594 CE LYS A 325 18382 13687 20764 -123 -3076 -1296 C ATOM 2595 NZ LYS A 325 24.357 5.585 52.053 1.00134.57 N ANISOU 2595 NZ LYS A 325 17800 13219 20113 -37 -3011 -1505 N ATOM 2596 N ASN A 326 17.771 9.496 51.995 1.00140.88 N ANISOU 2596 N ASN A 326 18485 14735 20309 -269 -2340 -557 N ATOM 2597 CA ASN A 326 16.546 9.950 52.659 1.00143.44 C ANISOU 2597 CA ASN A 326 18811 15140 20550 -300 -2246 -316 C ATOM 2598 C ASN A 326 15.342 9.745 51.744 1.00139.47 C ANISOU 2598 C ASN A 326 18221 14710 20061 -384 -2238 -262 C ATOM 2599 O ASN A 326 14.363 10.488 51.814 1.00136.64 O ANISOU 2599 O ASN A 326 17841 14479 19598 -398 -2122 -116 O ATOM 2600 CB ASN A 326 16.628 11.420 53.080 1.00151.25 C ANISOU 2600 CB ASN A 326 19841 16262 21365 -225 -2088 -264 C ATOM 2601 CG ASN A 326 16.381 11.609 54.567 1.00154.67 C ANISOU 2601 CG ASN A 326 20343 16679 21744 -194 -2049 -74 C ATOM 2602 OD1 ASN A 326 17.249 12.089 55.297 1.00155.32 O ANISOU 2602 OD1 ASN A 326 20501 16734 21778 -118 -2027 -101 O ATOM 2603 ND2 ASN A 326 15.196 11.221 55.024 1.00153.94 N ANISOU 2603 ND2 ASN A 326 20221 16610 21658 -254 -2045 125 N TER 2604 ASN A 326 ATOM 2605 N ILE B 340 -7.015 13.002 35.938 1.00111.61 N ANISOU 2605 N ILE B 340 14700 9099 18610 -1992 88 840 N ATOM 2606 CA ILE B 340 -6.134 14.161 35.978 1.00114.03 C ANISOU 2606 CA ILE B 340 14587 9898 18840 -2050 19 979 C ATOM 2607 C ILE B 340 -4.963 13.925 36.921 1.00120.07 C ANISOU 2607 C ILE B 340 14946 10889 19786 -1624 160 1204 C ATOM 2608 O ILE B 340 -3.955 14.627 36.850 1.00132.50 O ANISOU 2608 O ILE B 340 16177 12862 21305 -1566 214 1304 O ATOM 2609 CB ILE B 340 -6.896 15.429 36.396 1.00111.03 C ANISOU 2609 CB ILE B 340 14068 9697 18422 -2449 -407 1076 C ATOM 2610 CG1 ILE B 340 -7.722 15.159 37.655 1.00106.79 C ANISOU 2610 CG1 ILE B 340 13521 8956 18098 -2418 -651 1215 C ATOM 2611 CG2 ILE B 340 -7.769 15.939 35.257 1.00109.88 C ANISOU 2611 CG2 ILE B 340 14249 9454 18046 -2893 -524 857 C ATOM 2612 CD1 ILE B 340 -8.304 16.407 38.275 1.00118.66 C ANISOU 2612 CD1 ILE B 340 14807 10680 19597 -2747 -1065 1356 C ATOM 2613 N LEU B 341 -5.107 12.930 37.803 1.00112.83 N ANISOU 2613 N LEU B 341 14070 9713 19085 -1328 219 1281 N ATOM 2614 CA LEU B 341 -4.099 12.693 38.834 1.00113.82 C ANISOU 2614 CA LEU B 341 13809 10033 19404 -927 321 1509 C ATOM 2615 C LEU B 341 -2.723 12.446 38.231 1.00121.36 C ANISOU 2615 C LEU B 341 14614 11200 20295 -641 684 1486 C ATOM 2616 O LEU B 341 -1.705 12.851 38.805 1.00126.58 O ANISOU 2616 O LEU B 341 14859 12209 21027 -436 719 1678 O ATOM 2617 CB LEU B 341 -4.515 11.515 39.714 1.00114.39 C ANISOU 2617 CB LEU B 341 14017 9741 19705 -650 367 1558 C ATOM 2618 CG LEU B 341 -5.655 11.784 40.696 1.00110.57 C ANISOU 2618 CG LEU B 341 13550 9117 19344 -842 -3 1664 C ATOM 2619 CD1 LEU B 341 -5.991 10.536 41.499 1.00111.53 C ANISOU 2619 CD1 LEU B 341 13817 8872 19688 -543 80 1702 C ATOM 2620 CD2 LEU B 341 -5.288 12.932 41.617 1.00107.71 C ANISOU 2620 CD2 LEU B 341 12716 9169 19042 -903 -265 1913 C ATOM 2621 N GLU B 342 -2.666 11.785 37.074 1.00120.93 N ANISOU 2621 N GLU B 342 14893 10945 20108 -623 956 1253 N ATOM 2622 CA GLU B 342 -1.371 11.517 36.459 1.00125.55 C ANISOU 2622 CA GLU B 342 15353 11721 20628 -351 1309 1221 C ATOM 2623 C GLU B 342 -0.783 12.781 35.842 1.00123.36 C ANISOU 2623 C GLU B 342 14832 11879 20159 -577 1247 1237 C ATOM 2624 O GLU B 342 0.424 13.025 35.946 1.00124.89 O ANISOU 2624 O GLU B 342 14687 12403 20363 -351 1403 1353 O ATOM 2625 CB GLU B 342 -1.503 10.413 35.412 1.00127.48 C ANISOU 2625 CB GLU B 342 16033 11613 20790 -261 1619 965 C ATOM 2626 CG GLU B 342 -0.198 9.694 35.122 1.00135.99 C ANISOU 2626 CG GLU B 342 17002 12778 21890 153 2021 959 C ATOM 2627 CD GLU B 342 0.374 9.015 36.353 1.00144.08 C ANISOU 2627 CD GLU B 342 17780 13792 23171 579 2105 1165 C ATOM 2628 OE1 GLU B 342 -0.417 8.508 37.177 1.00141.62 O ANISOU 2628 OE1 GLU B 342 17580 13205 23026 616 1963 1219 O ATOM 2629 OE2 GLU B 342 1.614 8.995 36.502 1.00148.61 O ANISOU 2629 OE2 GLU B 342 18048 14636 23782 876 2312 1273 O ATOM 2630 N ASN B 343 -1.623 13.600 35.205 1.00120.98 N ANISOU 2630 N ASN B 343 14696 11586 19684 -1022 1018 1123 N ATOM 2631 CA ASN B 343 -1.139 14.839 34.606 1.00120.07 C ANISOU 2631 CA ASN B 343 14361 11878 19382 -1263 939 1135 C ATOM 2632 C ASN B 343 -0.771 15.873 35.662 1.00122.93 C ANISOU 2632 C ASN B 343 14245 12623 19839 -1284 682 1403 C ATOM 2633 O ASN B 343 0.120 16.699 35.432 1.00117.48 O ANISOU 2633 O ASN B 343 13246 12333 19059 -1299 710 1479 O ATOM 2634 CB ASN B 343 -2.189 15.403 33.650 1.00120.97 C ANISOU 2634 CB ASN B 343 14796 11877 19289 -1736 759 938 C ATOM 2635 CG ASN B 343 -2.427 14.506 32.452 1.00121.18 C ANISOU 2635 CG ASN B 343 15272 11581 19189 -1734 1029 663 C ATOM 2636 OD1 ASN B 343 -1.550 13.738 32.056 1.00124.83 O ANISOU 2636 OD1 ASN B 343 15753 12023 19655 -1416 1378 607 O ATOM 2637 ND2 ASN B 343 -3.614 14.601 31.867 1.00119.60 N ANISOU 2637 ND2 ASN B 343 15438 11127 18875 -2088 870 488 N ATOM 2638 N LEU B 344 -1.442 15.851 36.817 1.00114.85 N ANISOU 2638 N LEU B 344 13154 11488 18996 -1287 430 1548 N ATOM 2639 CA LEU B 344 -1.082 16.772 37.890 1.00112.07 C ANISOU 2639 CA LEU B 344 12342 11489 18749 -1281 191 1810 C ATOM 2640 C LEU B 344 0.289 16.447 38.469 1.00123.44 C ANISOU 2640 C LEU B 344 13417 13164 20321 -836 427 1981 C ATOM 2641 O LEU B 344 0.987 17.349 38.947 1.00115.59 O ANISOU 2641 O LEU B 344 12006 12570 19342 -824 322 2165 O ATOM 2642 CB LEU B 344 -2.145 16.747 38.989 1.00108.83 C ANISOU 2642 CB LEU B 344 11964 10881 18505 -1376 -123 1919 C ATOM 2643 CG LEU B 344 -3.529 17.271 38.601 1.00105.76 C ANISOU 2643 CG LEU B 344 11870 10315 18001 -1845 -422 1791 C ATOM 2644 CD1 LEU B 344 -4.497 17.172 39.771 1.00102.76 C ANISOU 2644 CD1 LEU B 344 11499 9742 17804 -1893 -714 1914 C ATOM 2645 CD2 LEU B 344 -3.438 18.702 38.092 1.00103.65 C ANISOU 2645 CD2 LEU B 344 11419 10418 17546 -2204 -620 1801 C ATOM 2646 N LYS B 345 0.690 15.175 38.436 1.00100.85 N ANISOU 2646 N LYS B 345 12015 11800 14504 -2418 -1166 1651 N ATOM 2647 CA LYS B 345 2.017 14.800 38.913 1.00 93.56 C ANISOU 2647 CA LYS B 345 11225 10848 13475 -2227 -1401 1128 C ATOM 2648 C LYS B 345 3.094 15.149 37.894 1.00 91.26 C ANISOU 2648 C LYS B 345 10840 10624 13210 -2163 -1416 571 C ATOM 2649 O LYS B 345 4.207 15.534 38.271 1.00 88.76 O ANISOU 2649 O LYS B 345 10555 10376 12794 -1998 -1359 101 O ATOM 2650 CB LYS B 345 2.059 13.307 39.237 1.00 99.13 C ANISOU 2650 CB LYS B 345 12129 11357 14178 -2215 -1935 1198 C ATOM 2651 CG LYS B 345 1.127 12.887 40.358 1.00114.12 C ANISOU 2651 CG LYS B 345 14143 13182 16035 -2256 -1955 1705 C ATOM 2652 CD LYS B 345 1.202 11.390 40.594 1.00127.35 C ANISOU 2652 CD LYS B 345 16011 14661 17714 -2246 -2498 1755 C ATOM 2653 CE LYS B 345 0.260 10.959 41.704 1.00132.07 C ANISOU 2653 CE LYS B 345 16724 15184 18272 -2290 -2521 2265 C ATOM 2654 NZ LYS B 345 0.330 9.493 41.951 1.00135.62 N ANISOU 2654 NZ LYS B 345 17363 15441 18725 -2280 -3053 2317 N ATOM 2655 N ASP B 346 2.777 15.018 36.601 1.00 90.36 N ANISOU 2655 N ASP B 346 10612 10492 13229 -2291 -1493 616 N ATOM 2656 CA ASP B 346 3.736 15.363 35.555 1.00 87.19 C ANISOU 2656 CA ASP B 346 10110 10156 12861 -2243 -1500 108 C ATOM 2657 C ASP B 346 4.140 16.831 35.636 1.00 86.79 C ANISOU 2657 C ASP B 346 9917 10305 12755 -2175 -998 -122 C ATOM 2658 O ASP B 346 5.318 17.169 35.462 1.00 95.50 O ANISOU 2658 O ASP B 346 11008 11474 13804 -2040 -988 -659 O ATOM 2659 CB ASP B 346 3.150 15.047 34.177 1.00 91.27 C ANISOU 2659 CB ASP B 346 10516 10627 13536 -2412 -1624 272 C ATOM 2660 CG ASP B 346 2.763 13.590 34.025 1.00101.61 C ANISOU 2660 CG ASP B 346 11962 11739 14908 -2483 -2127 488 C ATOM 2661 OD1 ASP B 346 3.382 12.732 34.689 1.00102.73 O ANISOU 2661 OD1 ASP B 346 12282 11775 14974 -2370 -2465 306 O ATOM 2662 OD2 ASP B 346 1.841 13.304 33.232 1.00108.81 O ANISOU 2662 OD2 ASP B 346 12801 12599 15943 -2653 -2184 840 O ATOM 2663 N VAL B 347 3.173 17.718 35.901 1.00 85.15 N ANISOU 2663 N VAL B 347 9599 10195 12558 -2266 -577 279 N ATOM 2664 CA VAL B 347 3.442 19.148 35.987 1.00 83.65 C ANISOU 2664 CA VAL B 347 9266 10198 12321 -2214 -78 109 C ATOM 2665 C VAL B 347 3.873 19.569 37.382 1.00 93.89 C ANISOU 2665 C VAL B 347 10659 11551 13464 -2061 99 9 C ATOM 2666 O VAL B 347 4.066 20.768 37.630 1.00 90.15 O ANISOU 2666 O VAL B 347 10080 11236 12936 -2009 528 -107 O ATOM 2667 CB VAL B 347 2.206 19.962 35.555 1.00 88.58 C ANISOU 2667 CB VAL B 347 9715 10908 13034 -2387 309 577 C ATOM 2668 CG1 VAL B 347 1.846 19.647 34.117 1.00 82.30 C ANISOU 2668 CG1 VAL B 347 8810 10070 12390 -2533 162 639 C ATOM 2669 CG2 VAL B 347 1.028 19.690 36.485 1.00 84.13 C ANISOU 2669 CG2 VAL B 347 9224 10285 12457 -2468 358 1167 C ATOM 2670 N GLY B 348 4.021 18.622 38.306 1.00 85.64 N ANISOU 2670 N GLY B 348 9810 10382 12347 -1988 -217 54 N ATOM 2671 CA GLY B 348 4.535 18.942 39.623 1.00 86.08 C ANISOU 2671 CA GLY B 348 9970 10484 12254 -1832 -88 -83 C ATOM 2672 C GLY B 348 3.576 19.697 40.512 1.00 86.20 C ANISOU 2672 C GLY B 348 9947 10578 12227 -1880 312 365 C ATOM 2673 O GLY B 348 4.016 20.441 41.393 1.00 85.93 O ANISOU 2673 O GLY B 348 9926 10645 12077 -1759 582 209 O ATOM 2674 N LEU B 349 2.272 19.528 40.306 1.00 99.37 N ANISOU 2674 N LEU B 349 11567 12202 13985 -2054 359 920 N ATOM 2675 CA LEU B 349 1.276 20.193 41.132 1.00 92.51 C ANISOU 2675 CA LEU B 349 10664 11402 13084 -2111 728 1384 C ATOM 2676 C LEU B 349 0.672 19.286 42.194 1.00 93.98 C ANISOU 2676 C LEU B 349 11026 11456 13224 -2121 501 1763 C ATOM 2677 O LEU B 349 0.031 19.790 43.123 1.00 88.97 O ANISOU 2677 O LEU B 349 10397 10876 12532 -2130 784 2087 O ATOM 2678 CB LEU B 349 0.157 20.760 40.251 1.00 85.91 C ANISOU 2678 CB LEU B 349 9643 10624 12377 -2302 995 1777 C ATOM 2679 CG LEU B 349 0.540 21.955 39.376 1.00 85.94 C ANISOU 2679 CG LEU B 349 9446 10792 12417 -2304 1355 1496 C ATOM 2680 CD1 LEU B 349 -0.669 22.456 38.604 1.00 88.62 C ANISOU 2680 CD1 LEU B 349 9613 11177 12880 -2499 1610 1940 C ATOM 2681 CD2 LEU B 349 1.138 23.067 40.226 1.00 83.24 C ANISOU 2681 CD2 LEU B 349 9080 10602 11947 -2162 1742 1252 C ATOM 2682 N PHE B 350 0.859 17.975 42.086 1.00100.39 N ANISOU 2682 N PHE B 350 11982 12101 14060 -2119 2 1730 N ATOM 2683 CA PHE B 350 0.330 17.048 43.079 1.00107.90 C ANISOU 2683 CA PHE B 350 13109 12920 14968 -2125 -242 2074 C ATOM 2684 C PHE B 350 1.211 15.811 43.203 1.00111.39 C ANISOU 2684 C PHE B 350 13733 13214 15375 -2023 -768 1756 C ATOM 2685 O PHE B 350 1.230 15.137 44.235 1.00103.33 O ANISOU 2685 O PHE B 350 12883 12103 14274 -1957 -969 1854 O ATOM 2686 CB PHE B 350 -1.103 16.642 42.727 1.00102.85 C ANISOU 2686 CB PHE B 350 12429 12205 14443 -2327 -277 2685 C ATOM 2687 CG PHE B 350 -1.729 15.703 43.724 1.00 99.67 C ANISOU 2687 CG PHE B 350 12200 11668 14003 -2345 -517 3072 C ATOM 2688 CD1 PHE B 350 -1.995 16.122 45.018 1.00100.57 C ANISOU 2688 CD1 PHE B 350 12375 11830 14006 -2285 -282 3265 C ATOM 2689 CD2 PHE B 350 -2.056 14.404 43.367 1.00 97.19 C ANISOU 2689 CD2 PHE B 350 11987 11180 13762 -2423 -978 3244 C ATOM 2690 CE1 PHE B 350 -2.570 15.264 45.940 1.00 99.61 C ANISOU 2690 CE1 PHE B 350 12412 11587 13848 -2302 -501 3621 C ATOM 2691 CE2 PHE B 350 -2.633 13.542 44.285 1.00103.88 C ANISOU 2691 CE2 PHE B 350 12993 11904 14574 -2441 -1199 3600 C ATOM 2692 CZ PHE B 350 -2.890 13.974 45.572 1.00104.40 C ANISOU 2692 CZ PHE B 350 13117 12019 14529 -2380 -960 3789 C ATOM 2693 OXT PHE B 350 1.927 15.458 42.267 1.00117.67 O ANISOU 2693 OXT PHE B 350 14508 13977 16223 -2003 -1003 1391 O TER 2694 PHE B 350 HETATM 2695 C1 NAG C 1 26.189 70.678 39.248 1.00 71.54 C HETATM 2696 C2 NAG C 1 26.960 69.824 38.251 1.00 67.50 C HETATM 2697 C3 NAG C 1 28.446 69.919 38.519 1.00 69.17 C HETATM 2698 C4 NAG C 1 28.882 71.361 38.607 1.00 76.04 C HETATM 2699 C5 NAG C 1 28.158 72.025 39.787 1.00 85.11 C HETATM 2700 C6 NAG C 1 27.782 73.485 39.442 1.00 92.90 C HETATM 2701 C7 NAG C 1 26.409 67.615 37.315 1.00 61.43 C HETATM 2702 C8 NAG C 1 26.035 66.170 37.646 1.00 61.85 C HETATM 2703 N2 NAG C 1 26.583 68.410 38.380 1.00 59.20 N HETATM 2704 O3 NAG C 1 29.134 69.260 37.446 1.00 67.97 O HETATM 2705 O4 NAG C 1 30.284 71.355 38.893 1.00 74.09 O HETATM 2706 O5 NAG C 1 27.075 71.164 40.271 1.00 83.42 O HETATM 2707 O6 NAG C 1 26.734 73.549 38.466 1.00102.97 O HETATM 2708 O7 NAG C 1 26.526 67.987 36.149 1.00 62.65 O HETATM 2709 C1 NAG C 2 31.100 72.291 38.189 1.00 64.68 C HETATM 2710 C2 NAG C 2 32.361 72.498 39.009 1.00 43.23 C HETATM 2711 C3 NAG C 2 33.241 73.509 38.322 1.00 57.41 C HETATM 2712 C4 NAG C 2 33.588 72.983 36.926 1.00 57.11 C HETATM 2713 C5 NAG C 2 32.294 72.709 36.168 1.00 45.28 C HETATM 2714 C6 NAG C 2 32.641 72.138 34.790 1.00 56.93 C HETATM 2715 C7 NAG C 2 31.887 72.149 41.398 1.00 72.98 C HETATM 2716 C8 NAG C 2 31.517 72.824 42.720 1.00 52.05 C HETATM 2717 N2 NAG C 2 32.012 72.980 40.354 1.00 54.65 N HETATM 2718 O3 NAG C 2 34.423 73.693 39.121 1.00 65.00 O HETATM 2719 O4 NAG C 2 34.356 73.940 36.162 1.00 79.11 O HETATM 2720 O5 NAG C 2 31.470 71.772 36.895 1.00 63.84 O HETATM 2721 O6 NAG C 2 31.453 71.961 34.014 1.00 66.03 O HETATM 2722 O7 NAG C 2 32.056 70.932 41.336 1.00102.56 O HETATM 2723 C1 BMA C 3 35.781 73.925 36.365 1.00100.36 C HETATM 2724 C2 BMA C 3 36.423 74.679 35.220 1.00117.45 C HETATM 2725 C3 BMA C 3 37.931 74.732 35.415 1.00128.00 C HETATM 2726 C4 BMA C 3 38.204 75.424 36.743 1.00136.49 C HETATM 2727 C5 BMA C 3 37.506 74.655 37.858 1.00127.93 C HETATM 2728 C6 BMA C 3 37.711 75.373 39.194 1.00121.31 C HETATM 2729 O2 BMA C 3 35.901 76.017 35.197 1.00125.38 O HETATM 2730 O3 BMA C 3 38.567 75.464 34.330 1.00130.44 O HETATM 2731 O4 BMA C 3 39.617 75.467 36.994 1.00148.57 O HETATM 2732 O5 BMA C 3 36.091 74.593 37.603 1.00114.31 O HETATM 2733 O6 BMA C 3 36.617 76.268 39.421 1.00111.16 O HETATM 2734 C1 BMA C 4 38.017 75.100 33.030 1.00137.87 C HETATM 2735 C2 BMA C 4 37.581 76.378 32.293 1.00144.69 C HETATM 2736 C3 BMA C 4 37.496 76.029 30.835 1.00148.87 C HETATM 2737 C4 BMA C 4 38.909 75.770 30.289 1.00147.50 C HETATM 2738 C5 BMA C 4 39.711 74.819 31.201 1.00148.33 C HETATM 2739 C6 BMA C 4 40.920 75.544 31.825 1.00144.74 C HETATM 2740 O2 BMA C 4 38.529 77.444 32.469 1.00143.19 O HETATM 2741 O3 BMA C 4 36.900 77.109 30.104 1.00153.93 O HETATM 2742 O4 BMA C 4 38.786 75.207 28.975 1.00145.87 O HETATM 2743 O5 BMA C 4 38.809 74.211 32.160 1.00145.54 O HETATM 2744 O6 BMA C 4 42.015 74.633 31.961 1.00138.12 O HETATM 2745 C1 BOG A 401 37.309 53.184 47.187 1.00136.18 C HETATM 2746 O1 BOG A 401 37.279 51.818 47.488 1.00133.19 O HETATM 2747 C2 BOG A 401 36.422 53.930 48.189 1.00136.40 C HETATM 2748 O2 BOG A 401 35.439 54.629 47.474 1.00136.61 O HETATM 2749 C3 BOG A 401 37.125 54.883 49.065 1.00129.55 C HETATM 2750 O3 BOG A 401 37.703 54.168 50.124 1.00125.17 O HETATM 2751 C4 BOG A 401 38.177 55.697 48.439 1.00130.96 C HETATM 2752 O4 BOG A 401 37.637 56.950 48.118 1.00125.67 O HETATM 2753 C5 BOG A 401 38.777 55.080 47.179 1.00133.72 C HETATM 2754 O5 BOG A 401 38.698 53.626 47.227 1.00135.20 O HETATM 2755 C6 BOG A 401 40.242 55.497 47.056 1.00132.72 C HETATM 2756 O6 BOG A 401 40.988 54.790 48.007 1.00131.30 O HETATM 2757 C1' BOG A 401 36.043 51.204 47.262 1.00125.35 C HETATM 2758 C2' BOG A 401 36.027 49.863 47.991 1.00124.67 C HETATM 2759 C3' BOG A 401 35.863 48.687 47.030 1.00118.24 C HETATM 2760 C4' BOG A 401 35.151 47.498 47.672 1.00108.97 C HETATM 2761 C5' BOG A 401 35.533 46.163 47.036 1.00103.81 C HETATM 2762 C6' BOG A 401 34.406 45.139 47.150 1.00102.78 C HETATM 2763 C7' BOG A 401 34.903 43.714 47.392 1.00102.80 C HETATM 2764 C8' BOG A 401 33.761 42.742 47.686 1.00100.22 C HETATM 2765 C1 PLM A 406 25.278 14.430 54.756 1.00110.86 C HETATM 2766 O2 PLM A 406 24.362 13.827 55.205 1.00123.35 O HETATM 2767 C2 PLM A 406 25.405 15.923 55.051 1.00111.89 C HETATM 2768 C3 PLM A 406 25.320 16.240 56.544 1.00109.47 C HETATM 2769 C4 PLM A 406 24.252 17.286 56.858 1.00104.63 C HETATM 2770 C5 PLM A 406 24.825 18.476 57.624 1.00100.04 C HETATM 2771 C6 PLM A 406 23.753 19.471 58.058 1.00 95.93 C HETATM 2772 C7 PLM A 406 23.965 20.840 57.418 1.00 97.92 C HETATM 2773 C8 PLM A 406 23.604 21.986 58.358 1.00 97.78 C HETATM 2774 C9 PLM A 406 23.125 23.214 57.589 1.00101.16 C HETATM 2775 CA PLM A 406 23.780 24.497 58.087 1.00100.73 C HETATM 2776 CB PLM A 406 23.287 25.733 57.340 1.00101.85 C HETATM 2777 CC PLM A 406 23.725 27.030 58.016 1.00102.46 C HETATM 2778 CD PLM A 406 24.464 27.955 57.053 1.00 97.87 C HETATM 2779 CE PLM A 406 24.496 29.402 57.537 1.00 97.79 C HETATM 2780 CF PLM A 406 24.735 30.372 56.383 1.00 98.75 C HETATM 2781 CG PLM A 406 24.942 31.808 56.857 1.00 96.62 C HETATM 2782 CAA NZZ A 407 8.437 51.366 33.134 1.00162.98 C HETATM 2783 CAB NZZ A 407 7.522 50.161 33.335 1.00158.59 C HETATM 2784 CAE NZZ A 407 6.006 50.359 33.425 1.00161.35 C HETATM 2785 CAC NZZ A 407 8.063 48.927 33.429 1.00144.32 C HETATM 2786 CAF NZZ A 407 7.074 47.779 33.633 1.00135.29 C HETATM 2787 CAG NZZ A 407 7.811 46.608 34.281 1.00129.49 C HETATM 2788 CAH NZZ A 407 6.834 45.459 34.531 1.00113.19 C HETATM 2789 CAD NZZ A 407 5.631 45.675 35.443 1.00107.12 C HETATM 2790 CAI NZZ A 407 7.033 44.252 33.958 1.00101.57 C HETATM 2791 CAJ NZZ A 407 8.270 44.141 33.067 1.00 94.57 C HETATM 2792 OAK NZZ A 407 8.254 42.889 32.378 1.00106.52 O CONECT 117 2695 CONECT 883 1484 CONECT 1484 883 CONECT 2695 117 2696 2706 CONECT 2696 2695 2697 2703 CONECT 2697 2696 2698 2704 CONECT 2698 2697 2699 2705 CONECT 2699 2698 2700 2706 CONECT 2700 2699 2707 CONECT 2701 2702 2703 2708 CONECT 2702 2701 CONECT 2703 2696 2701 CONECT 2704 2697 CONECT 2705 2698 2709 CONECT 2706 2695 2699 CONECT 2707 2700 CONECT 2708 2701 CONECT 2709 2705 2710 2720 CONECT 2710 2709 2711 2717 CONECT 2711 2710 2712 2718 CONECT 2712 2711 2713 2719 CONECT 2713 2712 2714 2720 CONECT 2714 2713 2721 CONECT 2715 2716 2717 2722 CONECT 2716 2715 CONECT 2717 2710 2715 CONECT 2718 2711 CONECT 2719 2712 2723 CONECT 2720 2709 2713 CONECT 2721 2714 CONECT 2722 2715 CONECT 2723 2719 2724 2732 CONECT 2724 2723 2725 2729 CONECT 2725 2724 2726 2730 CONECT 2726 2725 2727 2731 CONECT 2727 2726 2728 2732 CONECT 2728 2727 2733 CONECT 2729 2724 CONECT 2730 2725 2734 CONECT 2731 2726 CONECT 2732 2723 2727 CONECT 2733 2728 CONECT 2734 2730 2735 2743 CONECT 2735 2734 2736 2740 CONECT 2736 2735 2737 2741 CONECT 2737 2736 2738 2742 CONECT 2738 2737 2739 2743 CONECT 2739 2738 2744 CONECT 2740 2735 CONECT 2741 2736 CONECT 2742 2737 CONECT 2743 2734 2738 CONECT 2744 2739 CONECT 2745 2746 2747 2754 CONECT 2746 2745 2757 CONECT 2747 2745 2748 2749 CONECT 2748 2747 CONECT 2749 2747 2750 2751 CONECT 2750 2749 CONECT 2751 2749 2752 2753 CONECT 2752 2751 CONECT 2753 2751 2754 2755 CONECT 2754 2745 2753 CONECT 2755 2753 2756 CONECT 2756 2755 CONECT 2757 2746 2758 CONECT 2758 2757 2759 CONECT 2759 2758 2760 CONECT 2760 2759 2761 CONECT 2761 2760 2762 CONECT 2762 2761 2763 CONECT 2763 2762 2764 CONECT 2764 2763 CONECT 2765 2766 2767 CONECT 2766 2765 CONECT 2767 2765 2768 CONECT 2768 2767 2769 CONECT 2769 2768 2770 CONECT 2770 2769 2771 CONECT 2771 2770 2772 CONECT 2772 2771 2773 CONECT 2773 2772 2774 CONECT 2774 2773 2775 CONECT 2775 2774 2776 CONECT 2776 2775 2777 CONECT 2777 2776 2778 CONECT 2778 2777 2779 CONECT 2779 2778 2780 CONECT 2780 2779 2781 CONECT 2781 2780 CONECT 2782 2783 CONECT 2783 2782 2784 2785 CONECT 2784 2783 CONECT 2785 2783 2786 CONECT 2786 2785 2787 CONECT 2787 2786 2788 CONECT 2788 2787 2789 2790 CONECT 2789 2788 CONECT 2790 2788 2791 CONECT 2791 2790 2792 CONECT 2792 2791 MASTER 457 0 7 16 4 0 0 6 2779 2 101 28 END