HEADER SIGNALING PROTEIN 24-JUN-19 6PGS TITLE CRYSTAL STRUCTURE OF BOVINE OPSIN WITH GERANIOL BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: G ALPHA 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_COMMON: BOVINE; SOURCE 9 ORGANISM_TAXID: 9913 KEYWDS OLFACTORY RECEPTOR, ODORANT, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.T.EGER,T.MORIZUMI,O.P.ERNST REVDAT 2 29-JUL-20 6PGS 1 COMPND REMARK HETNAM LINK REVDAT 2 2 1 SITE ATOM REVDAT 1 01-JUL-20 6PGS 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. 2.91 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.21 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 27336 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 1382 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 31.2060 - 6.2432 0.98 2652 143 0.2134 0.2263 REMARK 3 2 6.2432 - 4.9619 0.98 2583 138 0.2168 0.2408 REMARK 3 3 4.9619 - 4.3365 0.99 2626 138 0.1788 0.1931 REMARK 3 4 4.3365 - 3.9409 1.00 2598 123 0.1912 0.2292 REMARK 3 5 3.9409 - 3.6589 1.00 2600 143 0.2059 0.2490 REMARK 3 6 3.6589 - 3.4434 1.00 2593 139 0.2181 0.2443 REMARK 3 7 3.4434 - 3.2712 1.00 2605 136 0.2265 0.2136 REMARK 3 8 3.2712 - 3.1289 1.00 2590 137 0.2353 0.2647 REMARK 3 9 3.1289 - 3.0086 1.00 2561 157 0.2838 0.3182 REMARK 3 10 3.0086 - 2.9050 0.99 2546 128 0.2977 0.3279 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.600 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 : 0.002 2880 REMARK 3 ANGLE : 0.552 3918 REMARK 3 CHIRALITY : 0.037 445 REMARK 3 PLANARITY : 0.005 475 REMARK 3 DIHEDRAL : 11.384 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): 20.0057 41.9460 39.9464 REMARK 3 T TENSOR REMARK 3 T11: 0.3231 T22: 0.2896 REMARK 3 T33: 0.4763 T12: 0.0349 REMARK 3 T13: -0.0587 T23: 0.0671 REMARK 3 L TENSOR REMARK 3 L11: 1.6851 L22: 1.6807 REMARK 3 L33: 1.4471 L12: 0.3080 REMARK 3 L13: -0.2502 L23: -0.8208 REMARK 3 S TENSOR REMARK 3 S11: 0.0019 S12: 0.1176 S13: 0.1216 REMARK 3 S21: -0.1541 S22: -0.0123 S23: -0.2830 REMARK 3 S31: -0.0905 S32: -0.0275 S33: 0.0017 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 140:168) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1392 26.1284 24.6333 REMARK 3 T TENSOR REMARK 3 T11: 0.8814 T22: 0.5133 REMARK 3 T33: 0.6036 T12: -0.1375 REMARK 3 T13: -0.0784 T23: -0.0418 REMARK 3 L TENSOR REMARK 3 L11: 2.2155 L22: 0.7213 REMARK 3 L33: 0.0756 L12: 0.1630 REMARK 3 L13: -0.3283 L23: -0.0167 REMARK 3 S TENSOR REMARK 3 S11: -0.2197 S12: 0.7855 S13: -0.7377 REMARK 3 S21: -0.7180 S22: 0.0119 S23: 0.4322 REMARK 3 S31: 0.5499 S32: -0.4233 S33: -0.1577 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 169:222) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5181 49.6536 30.3163 REMARK 3 T TENSOR REMARK 3 T11: 0.6145 T22: 0.4397 REMARK 3 T33: 0.6576 T12: -0.0504 REMARK 3 T13: -0.1757 T23: 0.2086 REMARK 3 L TENSOR REMARK 3 L11: 0.9820 L22: 0.0090 REMARK 3 L33: 1.2185 L12: -0.0435 REMARK 3 L13: -0.2531 L23: 0.1424 REMARK 3 S TENSOR REMARK 3 S11: -0.3753 S12: 0.2761 S13: 0.9497 REMARK 3 S21: -0.4709 S22: 0.2567 S23: 0.2795 REMARK 3 S31: -0.5331 S32: 0.0761 S33: -0.1416 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 223:287) REMARK 3 ORIGIN FOR THE GROUP (A): -1.6994 35.0682 41.8995 REMARK 3 T TENSOR REMARK 3 T11: 0.4268 T22: 0.5028 REMARK 3 T33: 0.5166 T12: 0.0064 REMARK 3 T13: -0.1259 T23: -0.0106 REMARK 3 L TENSOR REMARK 3 L11: 2.1732 L22: 1.5307 REMARK 3 L33: 2.6547 L12: -1.8053 REMARK 3 L13: -0.3527 L23: -0.1304 REMARK 3 S TENSOR REMARK 3 S11: -0.0942 S12: 0.1054 S13: 0.2920 REMARK 3 S21: -0.2426 S22: -0.0154 S23: 0.4239 REMARK 3 S31: -0.1079 S32: -0.3563 S33: 0.0001 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 288:326) REMARK 3 ORIGIN FOR THE GROUP (A): 13.3600 27.3978 46.7527 REMARK 3 T TENSOR REMARK 3 T11: 0.6005 T22: 0.4162 REMARK 3 T33: 0.6620 T12: -0.0268 REMARK 3 T13: -0.0769 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.4593 L22: 0.2458 REMARK 3 L33: 0.4507 L12: 0.0977 REMARK 3 L13: 0.4521 L23: 0.2686 REMARK 3 S TENSOR REMARK 3 S11: -0.3195 S12: 0.0305 S13: -0.3565 REMARK 3 S21: 0.5708 S22: 0.2826 S23: -0.1787 REMARK 3 S31: 0.1437 S32: -0.1181 S33: -0.0168 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 340:344) REMARK 3 ORIGIN FOR THE GROUP (A): -2.8196 13.8654 37.4781 REMARK 3 T TENSOR REMARK 3 T11: 1.1497 T22: 0.9661 REMARK 3 T33: 1.8410 T12: -0.1058 REMARK 3 T13: -0.1022 T23: 0.1186 REMARK 3 L TENSOR REMARK 3 L11: 0.0041 L22: 0.0149 REMARK 3 L33: 0.0189 L12: 0.0062 REMARK 3 L13: -0.0029 L23: -0.0154 REMARK 3 S TENSOR REMARK 3 S11: -0.5730 S12: 0.2080 S13: -0.2480 REMARK 3 S21: -0.8088 S22: 0.0592 S23: -0.0484 REMARK 3 S31: 0.4173 S32: 0.5237 S33: -0.0007 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN B AND RESID 345:350) REMARK 3 ORIGIN FOR THE GROUP (A): 1.6151 16.8151 40.1431 REMARK 3 T TENSOR REMARK 3 T11: 0.9277 T22: 0.8998 REMARK 3 T33: 1.4181 T12: -0.2117 REMARK 3 T13: 0.0317 T23: -0.0351 REMARK 3 L TENSOR REMARK 3 L11: 0.0091 L22: 0.0250 REMARK 3 L33: 0.0132 L12: 0.0121 REMARK 3 L13: 0.0006 L23: -0.0141 REMARK 3 S TENSOR REMARK 3 S11: 0.1956 S12: -0.1699 S13: 0.1419 REMARK 3 S21: -0.2119 S22: 0.6898 S23: 0.1221 REMARK 3 S31: 0.2866 S32: 0.3768 S33: 0.0005 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 6PGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1000242502. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAR-15 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 : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27357 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890 REMARK 200 RESOLUTION RANGE LOW (A) : 97.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 9.70 REMARK 200 R MERGE FOR SHELL (I) : 1.01900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4J4Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 84.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.1-3.3M AMMONIUM SULFATE, 0.1M SODIUM REMARK 280 ACETATE BUFFER, PH 5.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 121.95950 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.41335 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.57733 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.95950 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.41335 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.57733 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.95950 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.41335 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.57733 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.95950 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.41335 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.57733 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.95950 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.41335 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.57733 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.95950 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.41335 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.57733 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.82670 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.15467 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.82670 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.15467 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.82670 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.15467 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.82670 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.15467 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.82670 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.15467 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.82670 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.15467 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 ND2 ASN A 15 O5 NAG C 1 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 15 31.22 -97.73 REMARK 500 GLN A 28 50.88 -109.48 REMARK 500 ARG A 69 59.30 -92.84 REMARK 500 LYS A 141 71.29 51.42 REMARK 500 CYS A 167 -32.18 -132.88 REMARK 500 SER A 176 -166.40 62.95 REMARK 500 HIS A 195 95.95 -34.79 REMARK 500 PHE A 212 -49.65 -146.67 REMARK 500 GLN A 237 53.49 -152.80 REMARK 500 THR A 277 -70.75 -74.61 REMARK 500 THR A 289 67.26 -105.20 REMARK 500 ILE A 290 -23.74 -142.09 REMARK 500 ILE A 307 -58.01 -120.89 REMARK 500 CYS A 322 43.60 -94.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6NWE RELATED DB: PDB REMARK 900 RELATED ID: 6PEL RELATED DB: PDB REMARK 900 RELATED ID: 6PH7 RELATED DB: PDB DBREF 6PGS A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 6PGS B 340 350 PDB 6PGS 6PGS 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 402 17 HET 64Z A 403 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 64Z GERANIOL 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 64Z 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 89 1 17 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 289 1 6 HELIX 14 AB5 ILE A 290 THR A 297 1 8 HELIX 15 AB6 THR A 297 ILE A 307 1 11 HELIX 16 AB7 ASN A 310 CYS A 322 1 13 HELIX 17 AB8 LEU B 341 VAL B 347 1 7 SHEET 1 AA1 2 THR A 4 GLU A 5 0 SHEET 2 AA1 2 TYR A 10 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 PRO A 180 0 SHEET 2 AA2 2 CYS A 187 ILE A 189 -1 O GLY A 188 N ILE A 179 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.03 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.43 LINK SG CYS A 323 C1 PLM A 402 1555 1555 1.63 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44 LINK O3 BMA C 3 C1 BMA C 4 1555 1555 1.43 CRYST1 243.919 243.919 109.732 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 0.004100 0.002367 0.000000 0.00000 SCALE2 0.000000 0.004734 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009113 0.00000 ATOM 1 N MET A 1 12.609 72.632 40.887 1.00101.82 N ANISOU 1 N MET A 1 13846 8773 16067 1534 417 1323 N ATOM 2 CA MET A 1 13.362 71.585 40.206 1.00104.87 C ANISOU 2 CA MET A 1 14123 9342 16383 1415 326 1405 C ATOM 3 C MET A 1 13.902 70.580 41.221 1.00 93.75 C ANISOU 3 C MET A 1 12734 7966 14921 1327 272 1222 C ATOM 4 O MET A 1 14.417 70.963 42.272 1.00105.64 O ANISOU 4 O MET A 1 14370 9293 16477 1256 278 1031 O ATOM 5 CB MET A 1 14.498 72.194 39.384 1.00107.00 C ANISOU 5 CB MET A 1 14404 9523 16728 1271 298 1498 C ATOM 6 CG MET A 1 15.181 71.221 38.440 1.00116.86 C ANISOU 6 CG MET A 1 15526 10970 17905 1171 224 1623 C ATOM 7 SD MET A 1 16.268 72.062 37.275 1.00127.19 S ANISOU 7 SD MET A 1 16827 12199 19299 1041 223 1782 S ATOM 8 CE MET A 1 15.105 73.160 36.467 1.00133.09 C ANISOU 8 CE MET A 1 17570 12912 20084 1206 297 1957 C ATOM 9 N ASN A 2 13.785 69.291 40.900 1.00 74.86 N ANISOU 9 N ASN A 2 10216 5823 12406 1320 208 1274 N ATOM 10 CA ASN A 2 14.052 68.230 41.861 1.00 75.81 C ANISOU 10 CA ASN A 2 10337 6094 12375 1241 143 1085 C ATOM 11 C ASN A 2 15.166 67.277 41.449 1.00 82.81 C ANISOU 11 C ASN A 2 11145 7148 13169 1071 40 1089 C ATOM 12 O ASN A 2 15.493 66.370 42.223 1.00 69.08 O ANISOU 12 O ASN A 2 9400 5532 11313 996 -22 946 O ATOM 13 CB ASN A 2 12.771 67.423 42.118 1.00 70.22 C ANISOU 13 CB ASN A 2 9553 5579 11548 1385 161 1091 C ATOM 14 CG ASN A 2 11.659 68.265 42.715 1.00 94.87 C ANISOU 14 CG ASN A 2 12745 8548 14755 1564 277 1065 C ATOM 15 OD1 ASN A 2 11.871 69.000 43.680 1.00103.29 O ANISOU 15 OD1 ASN A 2 13955 9405 15884 1554 328 901 O ATOM 16 ND2 ASN A 2 10.467 68.167 42.138 1.00100.11 N ANISOU 16 ND2 ASN A 2 13306 9312 15420 1727 320 1228 N ATOM 17 N GLY A 3 15.762 67.447 40.265 1.00 88.09 N ANISOU 17 N GLY A 3 11755 7829 13888 1012 26 1255 N ATOM 18 CA GLY A 3 16.770 66.521 39.796 1.00 73.37 C ANISOU 18 CA GLY A 3 9808 6129 11939 870 -50 1271 C ATOM 19 C GLY A 3 17.903 67.232 39.084 1.00 70.37 C ANISOU 19 C GLY A 3 9435 5623 11679 751 -48 1365 C ATOM 20 O GLY A 3 17.857 68.440 38.839 1.00 78.17 O ANISOU 20 O GLY A 3 10488 6398 12815 779 8 1437 O ATOM 21 N THR A 4 18.931 66.449 38.757 1.00 66.46 N ANISOU 21 N THR A 4 8867 5259 11125 620 -104 1368 N ATOM 22 CA THR A 4 20.104 66.930 38.037 1.00 61.41 C ANISOU 22 CA THR A 4 8207 4543 10585 494 -101 1467 C ATOM 23 C THR A 4 20.333 66.028 36.834 1.00 60.30 C ANISOU 23 C THR A 4 7947 4625 10337 483 -103 1610 C ATOM 24 O THR A 4 20.485 64.812 36.989 1.00 58.70 O ANISOU 24 O THR A 4 7683 4615 10005 457 -147 1542 O ATOM 25 CB THR A 4 21.344 66.945 38.937 1.00 49.36 C ANISOU 25 CB THR A 4 6709 2935 9111 324 -162 1318 C ATOM 26 OG1 THR A 4 21.121 67.818 40.051 1.00 58.69 O ANISOU 26 OG1 THR A 4 8022 3901 10375 326 -160 1171 O ATOM 27 CG2 THR A 4 22.560 67.422 38.160 1.00 50.28 C ANISOU 27 CG2 THR A 4 6782 2983 9341 191 -155 1437 C ATOM 28 N GLU A 5 20.360 66.619 35.644 1.00 71.11 N ANISOU 28 N GLU A 5 9294 5966 11759 501 -51 1807 N ATOM 29 CA GLU A 5 20.496 65.855 34.415 1.00 53.13 C ANISOU 29 CA GLU A 5 6924 3897 9365 497 -40 1949 C ATOM 30 C GLU A 5 21.959 65.726 34.006 1.00 76.58 C ANISOU 30 C GLU A 5 9845 6877 12377 346 -34 1981 C ATOM 31 O GLU A 5 22.830 66.476 34.453 1.00100.17 O ANISOU 31 O GLU A 5 12862 9687 15510 243 -37 1946 O ATOM 32 CB GLU A 5 19.705 66.504 33.280 1.00 76.83 C ANISOU 32 CB GLU A 5 9922 6893 12376 599 12 2163 C ATOM 33 CG GLU A 5 18.236 66.729 33.579 1.00 85.86 C ANISOU 33 CG GLU A 5 11095 8025 13504 759 15 2169 C ATOM 34 CD GLU A 5 17.492 67.299 32.389 1.00115.09 C ANISOU 34 CD GLU A 5 14773 11747 17210 855 54 2407 C ATOM 35 OE1 GLU A 5 17.096 66.514 31.501 1.00113.41 O ANISOU 35 OE1 GLU A 5 14495 11756 16840 879 34 2506 O ATOM 36 OE2 GLU A 5 17.320 68.534 32.332 1.00138.08 O ANISOU 36 OE2 GLU A 5 17736 14495 20232 888 97 2457 O ATOM 37 N GLY A 6 22.214 64.756 33.132 1.00 93.62 N ANISOU 37 N GLY A 6 11925 9243 14404 331 -23 2050 N ATOM 38 CA GLY A 6 23.530 64.530 32.588 1.00 74.21 C ANISOU 38 CA GLY A 6 9402 6824 11969 210 4 2103 C ATOM 39 C GLY A 6 23.454 63.819 31.254 1.00 87.18 C ANISOU 39 C GLY A 6 10990 8669 13463 237 54 2238 C ATOM 40 O GLY A 6 22.373 63.448 30.785 1.00 97.94 O ANISOU 40 O GLY A 6 12365 10151 14696 339 49 2282 O ATOM 41 N PRO A 7 24.606 63.624 30.607 1.00 91.05 N ANISOU 41 N PRO A 7 11421 9207 13969 144 105 2308 N ATOM 42 CA PRO A 7 24.599 62.930 29.308 1.00 98.84 C ANISOU 42 CA PRO A 7 12371 10388 14796 165 166 2424 C ATOM 43 C PRO A 7 24.048 61.514 29.372 1.00 98.75 C ANISOU 43 C PRO A 7 12348 10575 14598 216 134 2315 C ATOM 44 O PRO A 7 23.342 61.092 28.448 1.00103.26 O ANISOU 44 O PRO A 7 12932 11291 15011 275 152 2394 O ATOM 45 CB PRO A 7 26.078 62.952 28.898 1.00 97.20 C ANISOU 45 CB PRO A 7 12094 10173 14665 49 234 2483 C ATOM 46 CG PRO A 7 26.641 64.141 29.605 1.00 87.22 C ANISOU 46 CG PRO A 7 10842 8677 13622 -27 213 2483 C ATOM 47 CD PRO A 7 25.927 64.192 30.926 1.00 86.87 C ANISOU 47 CD PRO A 7 10857 8543 13608 14 118 2309 C ATOM 48 N ASN A 8 24.341 60.766 30.441 1.00 79.84 N ANISOU 48 N ASN A 8 9930 8192 12216 189 80 2140 N ATOM 49 CA ASN A 8 23.903 59.378 30.533 1.00 77.71 C ANISOU 49 CA ASN A 8 9646 8096 11784 228 53 2038 C ATOM 50 C ASN A 8 23.412 59.020 31.933 1.00 70.76 C ANISOU 50 C ASN A 8 8782 7182 10923 253 -37 1866 C ATOM 51 O ASN A 8 23.584 57.879 32.376 1.00 68.17 O ANISOU 51 O ASN A 8 8422 6952 10526 242 -64 1755 O ATOM 52 CB ASN A 8 25.026 58.416 30.132 1.00 72.57 C ANISOU 52 CB ASN A 8 8930 7550 11095 164 109 2020 C ATOM 53 CG ASN A 8 25.324 58.449 28.647 1.00 76.09 C ANISOU 53 CG ASN A 8 9370 8085 11456 158 211 2175 C ATOM 54 OD1 ASN A 8 24.419 58.567 27.822 1.00 82.98 O ANISOU 54 OD1 ASN A 8 10291 9030 12206 215 218 2264 O ATOM 55 ND2 ASN A 8 26.601 58.340 28.299 1.00 74.39 N ANISOU 55 ND2 ASN A 8 9091 7873 11302 86 290 2215 N ATOM 56 N PHE A 9 22.798 59.966 32.641 1.00 54.96 N ANISOU 56 N PHE A 9 6833 5039 9010 289 -75 1844 N ATOM 57 CA PHE A 9 22.333 59.692 33.994 1.00 70.70 C ANISOU 57 CA PHE A 9 8852 7001 11012 312 -148 1682 C ATOM 58 C PHE A 9 21.278 60.716 34.390 1.00 80.55 C ANISOU 58 C PHE A 9 10168 8122 12314 395 -159 1693 C ATOM 59 O PHE A 9 20.998 61.671 33.661 1.00 70.52 O ANISOU 59 O PHE A 9 8923 6775 11098 430 -116 1831 O ATOM 60 CB PHE A 9 23.493 59.693 34.997 1.00 73.06 C ANISOU 60 CB PHE A 9 9128 7213 11419 205 -184 1572 C ATOM 61 CG PHE A 9 24.241 60.998 35.068 1.00 72.87 C ANISOU 61 CG PHE A 9 9125 6997 11567 130 -167 1623 C ATOM 62 CD1 PHE A 9 23.810 62.018 35.905 1.00 64.78 C ANISOU 62 CD1 PHE A 9 8183 5795 10636 143 -196 1563 C ATOM 63 CD2 PHE A 9 25.382 61.200 34.310 1.00 73.42 C ANISOU 63 CD2 PHE A 9 9133 7056 11705 43 -115 1729 C ATOM 64 CE1 PHE A 9 24.498 63.214 35.975 1.00 69.58 C ANISOU 64 CE1 PHE A 9 8820 6209 11407 63 -184 1603 C ATOM 65 CE2 PHE A 9 26.075 62.395 34.377 1.00 54.06 C ANISOU 65 CE2 PHE A 9 6697 4424 9421 -40 -104 1783 C ATOM 66 CZ PHE A 9 25.632 63.403 35.211 1.00 61.20 C ANISOU 66 CZ PHE A 9 7692 5142 10421 -34 -143 1717 C ATOM 67 N TYR A 10 20.700 60.496 35.570 1.00 68.38 N ANISOU 67 N TYR A 10 8658 6561 10761 433 -210 1552 N ATOM 68 CA TYR A 10 19.744 61.432 36.158 1.00 55.75 C ANISOU 68 CA TYR A 10 7129 4829 9224 519 -208 1534 C ATOM 69 C TYR A 10 19.744 61.201 37.662 1.00 62.29 C ANISOU 69 C TYR A 10 7996 5612 10060 500 -259 1343 C ATOM 70 O TYR A 10 19.184 60.206 38.134 1.00 82.19 O ANISOU 70 O TYR A 10 10494 8267 12468 538 -294 1265 O ATOM 71 CB TYR A 10 18.351 61.240 35.569 1.00 60.92 C ANISOU 71 CB TYR A 10 7773 5592 9783 647 -197 1624 C ATOM 72 CG TYR A 10 17.290 62.092 36.232 1.00 64.29 C ANISOU 72 CG TYR A 10 8255 5895 10276 758 -182 1606 C ATOM 73 CD1 TYR A 10 17.119 63.424 35.876 1.00 55.63 C ANISOU 73 CD1 TYR A 10 7203 4623 9310 803 -131 1714 C ATOM 74 CD2 TYR A 10 16.458 61.564 37.212 1.00 52.25 C ANISOU 74 CD2 TYR A 10 6739 4425 8690 822 -209 1486 C ATOM 75 CE1 TYR A 10 16.152 64.206 36.479 1.00 61.80 C ANISOU 75 CE1 TYR A 10 8037 5279 10165 917 -101 1697 C ATOM 76 CE2 TYR A 10 15.489 62.339 37.821 1.00 61.42 C ANISOU 76 CE2 TYR A 10 7949 5474 9914 934 -176 1469 C ATOM 77 CZ TYR A 10 15.340 63.658 37.451 1.00 70.28 C ANISOU 77 CZ TYR A 10 9117 6415 11172 986 -119 1571 C ATOM 78 OH TYR A 10 14.376 64.433 38.055 1.00 67.04 O ANISOU 78 OH TYR A 10 8756 5880 10835 1111 -71 1554 O ATOM 79 N VAL A 11 20.366 62.109 38.406 1.00 55.83 N ANISOU 79 N VAL A 11 7238 4606 9367 435 -266 1272 N ATOM 80 CA VAL A 11 20.462 62.004 39.857 1.00 60.65 C ANISOU 80 CA VAL A 11 7903 5165 9978 399 -318 1089 C ATOM 81 C VAL A 11 19.230 62.669 40.462 1.00 71.94 C ANISOU 81 C VAL A 11 9418 6498 11417 523 -284 1040 C ATOM 82 O VAL A 11 19.016 63.871 40.233 1.00 85.33 O ANISOU 82 O VAL A 11 11177 8016 13228 560 -232 1097 O ATOM 83 CB VAL A 11 21.748 62.653 40.384 1.00 66.28 C ANISOU 83 CB VAL A 11 8647 5725 10812 252 -351 1027 C ATOM 84 CG1 VAL A 11 21.760 62.650 41.905 1.00 48.30 C ANISOU 84 CG1 VAL A 11 6445 3390 8516 212 -411 836 C ATOM 85 CG2 VAL A 11 22.969 61.928 39.834 1.00 50.34 C ANISOU 85 CG2 VAL A 11 6522 3814 8792 140 -375 1083 C ATOM 86 N PRO A 12 18.406 61.946 41.226 1.00 70.57 N ANISOU 86 N PRO A 12 9249 6430 11136 592 -303 945 N ATOM 87 CA PRO A 12 17.218 62.568 41.826 1.00 52.92 C ANISOU 87 CA PRO A 12 7086 4108 8912 721 -254 902 C ATOM 88 C PRO A 12 17.563 63.471 43.000 1.00 61.61 C ANISOU 88 C PRO A 12 8314 5004 10091 675 -251 748 C ATOM 89 O PRO A 12 17.176 63.196 44.141 1.00 69.13 O ANISOU 89 O PRO A 12 9319 5974 10974 695 -263 604 O ATOM 90 CB PRO A 12 16.384 61.361 42.272 1.00 52.09 C ANISOU 90 CB PRO A 12 6929 4203 8659 785 -279 852 C ATOM 91 CG PRO A 12 17.400 60.302 42.546 1.00 48.68 C ANISOU 91 CG PRO A 12 6449 3888 8159 657 -357 784 C ATOM 92 CD PRO A 12 18.496 60.508 41.533 1.00 60.45 C ANISOU 92 CD PRO A 12 7897 5351 9721 563 -361 885 C ATOM 93 N PHE A 13 18.288 64.552 42.728 1.00 50.43 N ANISOU 93 N PHE A 13 6953 3394 8815 605 -234 778 N ATOM 94 CA PHE A 13 18.689 65.495 43.769 1.00 51.44 C ANISOU 94 CA PHE A 13 7216 3304 9024 540 -236 629 C ATOM 95 C PHE A 13 19.071 66.800 43.092 1.00 66.72 C ANISOU 95 C PHE A 13 9202 5015 11135 516 -187 726 C ATOM 96 O PHE A 13 19.938 66.805 42.211 1.00 75.88 O ANISOU 96 O PHE A 13 10289 6192 12350 424 -209 844 O ATOM 97 CB PHE A 13 19.856 64.941 44.590 1.00 48.19 C ANISOU 97 CB PHE A 13 6805 2938 8567 365 -339 497 C ATOM 98 CG PHE A 13 20.107 65.685 45.871 1.00 53.44 C ANISOU 98 CG PHE A 13 7620 3423 9260 294 -360 309 C ATOM 99 CD1 PHE A 13 19.412 65.358 47.024 1.00 53.32 C ANISOU 99 CD1 PHE A 13 7679 3451 9128 352 -358 155 C ATOM 100 CD2 PHE A 13 21.042 66.706 45.924 1.00 63.19 C ANISOU 100 CD2 PHE A 13 8928 4448 10632 162 -381 285 C ATOM 101 CE1 PHE A 13 19.641 66.040 48.205 1.00 63.33 C ANISOU 101 CE1 PHE A 13 9104 4558 10399 280 -374 -29 C ATOM 102 CE2 PHE A 13 21.277 67.390 47.104 1.00 52.09 C ANISOU 102 CE2 PHE A 13 7677 2874 9240 81 -407 99 C ATOM 103 CZ PHE A 13 20.575 67.056 48.245 1.00 52.01 C ANISOU 103 CZ PHE A 13 7752 2912 9097 142 -403 -63 C ATOM 104 N SER A 14 18.429 67.895 43.491 1.00 57.89 N ANISOU 104 N SER A 14 8204 3683 10107 602 -112 682 N ATOM 105 CA SER A 14 18.676 69.178 42.849 1.00 83.49 C ANISOU 105 CA SER A 14 11501 6692 13530 594 -57 785 C ATOM 106 C SER A 14 20.100 69.646 43.118 1.00 89.66 C ANISOU 106 C SER A 14 12328 7336 14402 384 -123 719 C ATOM 107 O SER A 14 20.651 69.431 44.201 1.00 67.01 O ANISOU 107 O SER A 14 9521 4457 11484 269 -193 537 O ATOM 108 CB SER A 14 17.679 70.227 43.340 1.00 83.60 C ANISOU 108 CB SER A 14 11646 6489 13630 739 46 733 C ATOM 109 OG SER A 14 17.985 70.649 44.657 1.00 99.36 O ANISOU 109 OG SER A 14 13795 8328 15630 663 32 503 O ATOM 110 N ASN A 15 20.697 70.291 42.116 1.00 78.05 N ANISOU 110 N ASN A 15 10822 5767 13064 327 -104 881 N ATOM 111 CA ASN A 15 22.064 70.786 42.199 1.00 62.14 C ANISOU 111 CA ASN A 15 8827 3623 11159 122 -163 859 C ATOM 112 C ASN A 15 22.118 72.268 42.558 1.00 69.91 C ANISOU 112 C ASN A 15 9972 4270 12321 92 -117 807 C ATOM 113 O ASN A 15 23.036 72.978 42.135 1.00 73.17 O ANISOU 113 O ASN A 15 10387 4586 12829 -42 -128 871 O ATOM 114 CB ASN A 15 22.794 70.523 40.883 1.00 75.93 C ANISOU 114 CB ASN A 15 10428 5479 12941 61 -165 1072 C ATOM 115 CG ASN A 15 24.294 70.438 41.055 1.00 72.31 C ANISOU 115 CG ASN A 15 9923 5012 12537 -161 -250 1044 C ATOM 116 OD1 ASN A 15 24.801 70.404 42.177 1.00 68.92 O ANISOU 116 OD1 ASN A 15 9556 4534 12097 -277 -329 864 O ATOM 117 ND2 ASN A 15 25.013 70.393 39.941 1.00 89.92 N ANISOU 117 ND2 ASN A 15 12040 7301 14824 -221 -233 1229 N ATOM 118 N LYS A 16 21.144 72.750 43.334 1.00 84.00 N ANISOU 118 N LYS A 16 11892 5931 14094 216 -55 678 N ATOM 119 CA LYS A 16 21.119 74.160 43.705 1.00 71.48 C ANISOU 119 CA LYS A 16 10478 4091 12590 200 3 601 C ATOM 120 C LYS A 16 22.206 74.511 44.711 1.00 65.33 C ANISOU 120 C LYS A 16 9811 3167 11845 -23 -86 408 C ATOM 121 O LYS A 16 22.526 75.693 44.871 1.00 76.28 O ANISOU 121 O LYS A 16 11332 4341 13312 -94 -59 364 O ATOM 122 CB LYS A 16 19.745 74.537 44.266 1.00 69.05 C ANISOU 122 CB LYS A 16 10284 3706 12246 407 106 515 C ATOM 123 CG LYS A 16 19.661 74.529 45.786 1.00 85.74 C ANISOU 123 CG LYS A 16 12556 5710 14313 370 89 240 C ATOM 124 CD LYS A 16 18.291 74.977 46.269 1.00 94.17 C ANISOU 124 CD LYS A 16 13730 6702 15349 589 216 171 C ATOM 125 CE LYS A 16 17.291 73.833 46.249 1.00 93.66 C ANISOU 125 CE LYS A 16 13541 6860 15184 759 244 215 C ATOM 126 NZ LYS A 16 17.629 72.794 47.261 1.00 97.15 N ANISOU 126 NZ LYS A 16 13984 7466 15464 661 152 34 N ATOM 127 N THR A 17 22.776 73.517 45.393 1.00 72.78 N ANISOU 127 N THR A 17 10704 4224 12725 -139 -202 297 N ATOM 128 CA THR A 17 23.875 73.742 46.320 1.00 66.91 C ANISOU 128 CA THR A 17 10041 3387 11994 -372 -317 129 C ATOM 129 C THR A 17 25.233 73.396 45.725 1.00 76.05 C ANISOU 129 C THR A 17 11044 4646 13204 -566 -418 252 C ATOM 130 O THR A 17 26.257 73.645 46.372 1.00 83.36 O ANISOU 130 O THR A 17 12011 5512 14151 -778 -520 147 O ATOM 131 CB THR A 17 23.665 72.934 47.607 1.00 72.55 C ANISOU 131 CB THR A 17 10809 4239 12516 -385 -385 -87 C ATOM 132 OG1 THR A 17 23.593 71.537 47.294 1.00 77.35 O ANISOU 132 OG1 THR A 17 11237 5176 12978 -334 -426 -4 O ATOM 133 CG2 THR A 17 22.379 73.361 48.299 1.00 63.23 C ANISOU 133 CG2 THR A 17 9794 2943 11287 -202 -272 -224 C ATOM 134 N GLY A 18 25.268 72.832 44.520 1.00 63.69 N ANISOU 134 N GLY A 18 9303 3247 11652 -501 -387 471 N ATOM 135 CA GLY A 18 26.524 72.529 43.867 1.00 68.48 C ANISOU 135 CA GLY A 18 9756 3950 12314 -665 -454 603 C ATOM 136 C GLY A 18 27.216 71.276 44.346 1.00 73.38 C ANISOU 136 C GLY A 18 10255 4820 12804 -763 -568 544 C ATOM 137 O GLY A 18 28.405 71.095 44.066 1.00 83.54 O ANISOU 137 O GLY A 18 11426 6159 14156 -927 -637 620 O ATOM 138 N VAL A 19 26.509 70.395 45.057 1.00 66.67 N ANISOU 138 N VAL A 19 9422 4133 11776 -664 -586 421 N ATOM 139 CA VAL A 19 27.119 69.188 45.608 1.00 56.23 C ANISOU 139 CA VAL A 19 7994 3044 10328 -749 -696 362 C ATOM 140 C VAL A 19 26.874 67.953 44.752 1.00 65.43 C ANISOU 140 C VAL A 19 8988 4478 11393 -634 -661 500 C ATOM 141 O VAL A 19 27.546 66.930 44.960 1.00 65.40 O ANISOU 141 O VAL A 19 8867 4664 11320 -707 -740 498 O ATOM 142 CB VAL A 19 26.627 68.922 47.046 1.00 59.13 C ANISOU 142 CB VAL A 19 8489 3428 10551 -742 -752 134 C ATOM 143 CG1 VAL A 19 26.897 70.128 47.931 1.00 58.86 C ANISOU 143 CG1 VAL A 19 8645 3122 10597 -869 -788 -26 C ATOM 144 CG2 VAL A 19 25.145 68.572 47.045 1.00 69.03 C ANISOU 144 CG2 VAL A 19 9787 4754 11687 -508 -650 112 C ATOM 145 N VAL A 20 25.941 68.010 43.800 1.00 70.47 N ANISOU 145 N VAL A 20 9612 5139 12026 -459 -548 623 N ATOM 146 CA VAL A 20 25.621 66.840 42.991 1.00 69.10 C ANISOU 146 CA VAL A 20 9298 5215 11741 -353 -517 738 C ATOM 147 C VAL A 20 26.794 66.513 42.078 1.00 64.17 C ANISOU 147 C VAL A 20 8522 4675 11182 -461 -528 889 C ATOM 148 O VAL A 20 27.363 67.399 41.427 1.00 60.51 O ANISOU 148 O VAL A 20 8054 4073 10865 -532 -495 1000 O ATOM 149 CB VAL A 20 24.335 67.076 42.186 1.00 65.02 C ANISOU 149 CB VAL A 20 8806 4695 11202 -156 -406 840 C ATOM 150 CG1 VAL A 20 24.026 65.870 41.310 1.00 50.83 C ANISOU 150 CG1 VAL A 20 6875 3156 9283 -68 -383 953 C ATOM 151 CG2 VAL A 20 23.174 67.369 43.121 1.00 73.56 C ANISOU 151 CG2 VAL A 20 10022 5700 12228 -38 -381 696 C ATOM 152 N ARG A 21 27.165 65.238 42.031 1.00 66.41 N ANISOU 152 N ARG A 21 8683 5183 11365 -471 -566 898 N ATOM 153 CA ARG A 21 28.242 64.754 41.184 1.00 72.66 C ANISOU 153 CA ARG A 21 9321 6082 12204 -551 -559 1036 C ATOM 154 C ARG A 21 27.716 63.663 40.260 1.00 70.41 C ANISOU 154 C ARG A 21 8949 6010 11793 -419 -493 1128 C ATOM 155 O ARG A 21 26.600 63.162 40.420 1.00 72.78 O ANISOU 155 O ARG A 21 9293 6391 11967 -287 -478 1075 O ATOM 156 CB ARG A 21 29.410 64.224 42.025 1.00 66.36 C ANISOU 156 CB ARG A 21 8446 5343 11427 -710 -672 963 C ATOM 157 CG ARG A 21 30.006 65.244 42.980 1.00 62.85 C ANISOU 157 CG ARG A 21 8088 4700 11093 -870 -760 862 C ATOM 158 CD ARG A 21 30.711 66.362 42.231 1.00 57.64 C ANISOU 158 CD ARG A 21 7415 3870 10616 -970 -720 989 C ATOM 159 NE ARG A 21 31.258 67.366 43.140 1.00 67.74 N ANISOU 159 NE ARG A 21 8791 4943 12005 -1137 -810 884 N ATOM 160 CZ ARG A 21 30.633 68.490 43.474 1.00 80.05 C ANISOU 160 CZ ARG A 21 10526 6276 13614 -1121 -787 804 C ATOM 161 NH1 ARG A 21 29.436 68.761 42.972 1.00 83.32 N ANISOU 161 NH1 ARG A 21 11022 6648 13990 -935 -677 834 N ATOM 162 NH2 ARG A 21 31.206 69.347 44.308 1.00 83.29 N ANISOU 162 NH2 ARG A 21 11031 6498 14117 -1291 -875 696 N ATOM 163 N SER A 22 28.537 63.299 39.286 1.00 71.11 N ANISOU 163 N SER A 22 8916 6188 11917 -460 -449 1267 N ATOM 164 CA SER A 22 28.162 62.242 38.357 1.00 59.24 C ANISOU 164 CA SER A 22 7338 4882 10288 -354 -383 1346 C ATOM 165 C SER A 22 28.166 60.898 39.076 1.00 71.74 C ANISOU 165 C SER A 22 8871 6629 11758 -339 -445 1237 C ATOM 166 O SER A 22 29.117 60.595 39.806 1.00 77.10 O ANISOU 166 O SER A 22 9489 7319 12488 -449 -518 1182 O ATOM 167 CB SER A 22 29.121 62.210 37.169 1.00 71.01 C ANISOU 167 CB SER A 22 8720 6420 11842 -406 -307 1513 C ATOM 168 OG SER A 22 28.807 61.148 36.285 1.00 63.77 O ANISOU 168 OG SER A 22 7747 5693 10790 -312 -240 1572 O ATOM 169 N PRO A 23 27.132 60.068 38.901 1.00 74.85 N ANISOU 169 N PRO A 23 9283 7153 12005 -211 -423 1212 N ATOM 170 CA PRO A 23 27.129 58.741 39.534 1.00 69.97 C ANISOU 170 CA PRO A 23 8615 6686 11285 -197 -476 1120 C ATOM 171 C PRO A 23 28.173 57.790 38.975 1.00 65.87 C ANISOU 171 C PRO A 23 7963 6289 10775 -241 -449 1188 C ATOM 172 O PRO A 23 28.291 56.665 39.474 1.00 57.00 O ANISOU 172 O PRO A 23 6790 5280 9588 -233 -489 1126 O ATOM 173 CB PRO A 23 25.710 58.227 39.252 1.00 68.82 C ANISOU 173 CB PRO A 23 8521 6633 10995 -53 -444 1107 C ATOM 174 CG PRO A 23 25.297 58.941 38.015 1.00 71.84 C ANISOU 174 CG PRO A 23 8927 6977 11391 2 -358 1242 C ATOM 175 CD PRO A 23 25.917 60.306 38.104 1.00 69.75 C ANISOU 175 CD PRO A 23 8696 6521 11284 -80 -355 1278 C ATOM 176 N PHE A 24 28.925 58.200 37.957 1.00 66.19 N ANISOU 176 N PHE A 24 7945 6306 10897 -283 -374 1319 N ATOM 177 CA PHE A 24 30.001 57.400 37.393 1.00 66.99 C ANISOU 177 CA PHE A 24 7916 6510 11025 -322 -326 1392 C ATOM 178 C PHE A 24 31.377 57.833 37.880 1.00 57.62 C ANISOU 178 C PHE A 24 6638 5251 10003 -466 -373 1417 C ATOM 179 O PHE A 24 32.374 57.212 37.501 1.00 67.84 O ANISOU 179 O PHE A 24 7804 6624 11347 -501 -331 1486 O ATOM 180 CB PHE A 24 29.960 57.469 35.862 1.00 51.48 C ANISOU 180 CB PHE A 24 5938 4594 9026 -271 -195 1532 C ATOM 181 CG PHE A 24 28.711 56.893 35.259 1.00 57.30 C ANISOU 181 CG PHE A 24 6746 5433 9593 -144 -155 1523 C ATOM 182 CD1 PHE A 24 28.195 55.691 35.713 1.00 69.71 C ANISOU 182 CD1 PHE A 24 8319 7118 11050 -86 -193 1423 C ATOM 183 CD2 PHE A 24 28.052 57.556 34.236 1.00 63.66 C ANISOU 183 CD2 PHE A 24 7613 6222 10354 -91 -88 1624 C ATOM 184 CE1 PHE A 24 27.047 55.158 35.156 1.00 60.60 C ANISOU 184 CE1 PHE A 24 7225 6058 9744 14 -167 1417 C ATOM 185 CE2 PHE A 24 26.902 57.030 33.677 1.00 67.66 C ANISOU 185 CE2 PHE A 24 8175 6831 10700 13 -68 1625 C ATOM 186 CZ PHE A 24 26.399 55.829 34.138 1.00 65.99 C ANISOU 186 CZ PHE A 24 7963 6731 10378 60 -109 1518 C ATOM 187 N GLU A 25 31.459 58.874 38.705 1.00 65.65 N ANISOU 187 N GLU A 25 7716 6118 11110 -552 -456 1364 N ATOM 188 CA GLU A 25 32.756 59.441 39.064 1.00 68.02 C ANISOU 188 CA GLU A 25 7932 6337 11575 -711 -508 1404 C ATOM 189 C GLU A 25 32.958 59.615 40.563 1.00 69.76 C ANISOU 189 C GLU A 25 8186 6497 11823 -810 -660 1268 C ATOM 190 O GLU A 25 34.056 59.352 41.059 1.00 93.78 O ANISOU 190 O GLU A 25 11113 9568 14950 -925 -732 1282 O ATOM 191 CB GLU A 25 32.945 60.799 38.361 1.00 49.36 C ANISOU 191 CB GLU A 25 5605 3819 9329 -765 -451 1509 C ATOM 192 CG GLU A 25 32.709 60.781 36.853 1.00 89.59 C ANISOU 192 CG GLU A 25 10684 8971 14386 -675 -302 1656 C ATOM 193 CD GLU A 25 33.791 60.038 36.085 1.00104.99 C ANISOU 193 CD GLU A 25 12473 11047 16371 -700 -220 1772 C ATOM 194 OE1 GLU A 25 34.812 59.655 36.694 1.00102.73 O ANISOU 194 OE1 GLU A 25 12069 10789 16173 -793 -279 1760 O ATOM 195 OE2 GLU A 25 33.619 59.843 34.863 1.00105.12 O ANISOU 195 OE2 GLU A 25 12480 11138 16325 -624 -92 1879 O ATOM 196 N ALA A 26 31.942 60.053 41.292 1.00 64.90 N ANISOU 196 N ALA A 26 7723 5803 11134 -769 -709 1142 N ATOM 197 CA ALA A 26 32.065 60.385 42.702 1.00 61.37 C ANISOU 197 CA ALA A 26 7342 5282 10695 -869 -845 1002 C ATOM 198 C ALA A 26 30.946 59.734 43.497 1.00 60.37 C ANISOU 198 C ALA A 26 7308 5227 10402 -762 -880 866 C ATOM 199 O ALA A 26 29.881 59.428 42.950 1.00 56.40 O ANISOU 199 O ALA A 26 6853 4774 9801 -614 -797 875 O ATOM 200 CB ALA A 26 32.035 61.907 42.909 1.00 53.21 C ANISOU 200 CB ALA A 26 6429 4025 9764 -954 -863 973 C ATOM 201 N PRO A 27 31.159 59.500 44.794 1.00 61.02 N ANISOU 201 N PRO A 27 7414 5325 10446 -840 -1004 748 N ATOM 202 CA PRO A 27 30.099 58.915 45.623 1.00 72.62 C ANISOU 202 CA PRO A 27 8973 6863 11755 -745 -1033 621 C ATOM 203 C PRO A 27 28.875 59.817 45.700 1.00 78.10 C ANISOU 203 C PRO A 27 9839 7430 12404 -656 -977 546 C ATOM 204 O PRO A 27 28.947 61.034 45.517 1.00 86.69 O ANISOU 204 O PRO A 27 11005 8343 13590 -702 -954 550 O ATOM 205 CB PRO A 27 30.764 58.761 46.996 1.00 60.48 C ANISOU 205 CB PRO A 27 7435 5342 10203 -882 -1185 522 C ATOM 206 CG PRO A 27 32.225 58.701 46.703 1.00 55.93 C ANISOU 206 CG PRO A 27 6700 4784 9769 -1019 -1231 633 C ATOM 207 CD PRO A 27 32.433 59.608 45.526 1.00 46.68 C ANISOU 207 CD PRO A 27 5518 3495 8722 -1022 -1128 741 C ATOM 208 N GLN A 28 27.733 59.191 45.983 1.00 76.56 N ANISOU 208 N GLN A 28 9697 7322 12069 -523 -951 484 N ATOM 209 CA GLN A 28 26.461 59.899 46.047 1.00 67.80 C ANISOU 209 CA GLN A 28 8729 6117 10913 -410 -884 425 C ATOM 210 C GLN A 28 25.960 59.991 47.483 1.00 69.60 C ANISOU 210 C GLN A 28 9079 6322 11046 -420 -949 255 C ATOM 211 O GLN A 28 24.807 59.652 47.766 1.00 72.35 O ANISOU 211 O GLN A 28 9481 6725 11281 -293 -906 204 O ATOM 212 CB GLN A 28 25.421 59.199 45.169 1.00 49.76 C ANISOU 212 CB GLN A 28 6409 3953 8545 -244 -792 501 C ATOM 213 CG GLN A 28 25.856 59.004 43.725 1.00 55.98 C ANISOU 213 CG GLN A 28 7091 4788 9393 -229 -722 663 C ATOM 214 CD GLN A 28 25.922 60.307 42.954 1.00 71.50 C ANISOU 214 CD GLN A 28 9102 6587 11477 -238 -658 745 C ATOM 215 OE1 GLN A 28 24.943 61.050 42.885 1.00 71.66 O ANISOU 215 OE1 GLN A 28 9221 6512 11494 -148 -607 734 O ATOM 216 NE2 GLN A 28 27.080 60.593 42.373 1.00 76.88 N ANISOU 216 NE2 GLN A 28 9706 7232 12274 -344 -655 838 N ATOM 217 N TYR A 29 26.815 60.452 48.394 1.00 63.24 N ANISOU 217 N TYR A 29 8314 5437 10276 -576 -1051 169 N ATOM 218 CA TYR A 29 26.472 60.530 49.809 1.00 70.62 C ANISOU 218 CA TYR A 29 9373 6358 11101 -609 -1120 0 C ATOM 219 C TYR A 29 25.593 61.729 50.149 1.00 72.67 C ANISOU 219 C TYR A 29 9821 6428 11363 -551 -1051 -107 C ATOM 220 O TYR A 29 25.311 61.953 51.332 1.00 73.76 O ANISOU 220 O TYR A 29 10089 6530 11408 -581 -1092 -263 O ATOM 221 CB TYR A 29 27.747 60.561 50.656 1.00 71.97 C ANISOU 221 CB TYR A 29 9520 6526 11298 -813 -1269 -50 C ATOM 222 CG TYR A 29 28.539 59.275 50.609 1.00 65.48 C ANISOU 222 CG TYR A 29 8517 5902 10461 -856 -1343 40 C ATOM 223 CD1 TYR A 29 27.898 58.045 50.521 1.00 72.99 C ANISOU 223 CD1 TYR A 29 9403 7028 11303 -728 -1309 71 C ATOM 224 CD2 TYR A 29 29.927 59.289 50.644 1.00 55.85 C ANISOU 224 CD2 TYR A 29 7186 4687 9347 -1024 -1445 100 C ATOM 225 CE1 TYR A 29 28.617 56.866 50.476 1.00 61.70 C ANISOU 225 CE1 TYR A 29 7814 5758 9872 -759 -1366 153 C ATOM 226 CE2 TYR A 29 30.655 58.116 50.599 1.00 57.05 C ANISOU 226 CE2 TYR A 29 7164 5011 9501 -1049 -1501 193 C ATOM 227 CZ TYR A 29 29.995 56.908 50.515 1.00 64.01 C ANISOU 227 CZ TYR A 29 7995 6050 10275 -912 -1458 215 C ATOM 228 OH TYR A 29 30.717 55.738 50.469 1.00 73.97 O ANISOU 228 OH TYR A 29 9090 7465 11552 -928 -1505 307 O ATOM 229 N TYR A 30 25.154 62.502 49.156 1.00 72.98 N ANISOU 229 N TYR A 30 9881 6345 11504 -466 -942 -25 N ATOM 230 CA TYR A 30 24.239 63.607 49.406 1.00 84.97 C ANISOU 230 CA TYR A 30 11568 7676 13040 -382 -857 -109 C ATOM 231 C TYR A 30 22.777 63.216 49.236 1.00 80.83 C ANISOU 231 C TYR A 30 11058 7234 12421 -172 -752 -95 C ATOM 232 O TYR A 30 21.900 63.912 49.761 1.00 85.88 O ANISOU 232 O TYR A 30 11836 7754 13041 -85 -683 -192 O ATOM 233 CB TYR A 30 24.564 64.792 48.489 1.00 58.78 C ANISOU 233 CB TYR A 30 8274 4157 9904 -408 -799 -17 C ATOM 234 CG TYR A 30 24.791 64.414 47.044 1.00 67.00 C ANISOU 234 CG TYR A 30 9157 5287 11014 -364 -751 188 C ATOM 235 CD1 TYR A 30 23.722 64.217 46.179 1.00 58.00 C ANISOU 235 CD1 TYR A 30 7986 4207 9845 -183 -645 290 C ATOM 236 CD2 TYR A 30 26.077 64.260 46.542 1.00 48.82 C ANISOU 236 CD2 TYR A 30 6735 3014 8801 -507 -809 283 C ATOM 237 CE1 TYR A 30 23.927 63.872 44.857 1.00 64.57 C ANISOU 237 CE1 TYR A 30 8690 5127 10716 -152 -603 470 C ATOM 238 CE2 TYR A 30 26.292 63.916 45.222 1.00 50.71 C ANISOU 238 CE2 TYR A 30 6842 3337 9089 -464 -750 464 C ATOM 239 CZ TYR A 30 25.214 63.723 44.384 1.00 70.17 C ANISOU 239 CZ TYR A 30 9297 5861 11505 -290 -648 551 C ATOM 240 OH TYR A 30 25.424 63.381 43.069 1.00 84.88 O ANISOU 240 OH TYR A 30 11043 7813 13392 -256 -591 723 O ATOM 241 N LEU A 31 22.493 62.129 48.518 1.00 66.59 N ANISOU 241 N LEU A 31 9113 5625 10562 -90 -735 22 N ATOM 242 CA LEU A 31 21.136 61.613 48.400 1.00 72.36 C ANISOU 242 CA LEU A 31 9836 6461 11196 89 -657 41 C ATOM 243 C LEU A 31 20.839 60.496 49.392 1.00 61.47 C ANISOU 243 C LEU A 31 8442 5256 9657 96 -711 -48 C ATOM 244 O LEU A 31 19.670 60.131 49.558 1.00 85.68 O ANISOU 244 O LEU A 31 11519 8399 12637 233 -650 -57 O ATOM 245 CB LEU A 31 20.871 61.121 46.968 1.00 62.63 C ANISOU 245 CB LEU A 31 8474 5333 9991 173 -605 222 C ATOM 246 CG LEU A 31 21.865 60.180 46.278 1.00 73.28 C ANISOU 246 CG LEU A 31 9678 6820 11345 87 -660 319 C ATOM 247 CD1 LEU A 31 21.687 58.733 46.719 1.00 89.65 C ANISOU 247 CD1 LEU A 31 11677 9101 13284 103 -709 290 C ATOM 248 CD2 LEU A 31 21.733 60.294 44.767 1.00 86.23 C ANISOU 248 CD2 LEU A 31 11244 8474 13044 148 -588 489 C ATOM 249 N ALA A 32 21.860 59.951 50.048 1.00 66.07 N ANISOU 249 N ALA A 32 8992 5905 10204 -47 -825 -100 N ATOM 250 CA ALA A 32 21.679 58.911 51.049 1.00 59.47 C ANISOU 250 CA ALA A 32 8144 5230 9220 -55 -886 -175 C ATOM 251 C ALA A 32 22.934 58.847 51.906 1.00 56.40 C ANISOU 251 C ALA A 32 7762 4840 8826 -240 -1020 -246 C ATOM 252 O ALA A 32 24.047 58.980 51.392 1.00 61.11 O ANISOU 252 O ALA A 32 8281 5405 9532 -352 -1074 -176 O ATOM 253 CB ALA A 32 21.401 57.547 50.405 1.00 50.81 C ANISOU 253 CB ALA A 32 6899 4334 8071 16 -880 -61 C ATOM 254 N GLU A 33 22.746 58.651 53.209 1.00 49.72 N ANISOU 254 N GLU A 33 7006 4038 7850 -274 -1073 -377 N ATOM 255 CA GLU A 33 23.871 58.573 54.123 1.00 57.50 C ANISOU 255 CA GLU A 33 8001 5039 8807 -456 -1217 -444 C ATOM 256 C GLU A 33 24.707 57.329 53.829 1.00 66.24 C ANISOU 256 C GLU A 33 8921 6320 9926 -512 -1304 -325 C ATOM 257 O GLU A 33 24.219 56.369 53.226 1.00 64.09 O ANISOU 257 O GLU A 33 8545 6174 9631 -401 -1251 -231 O ATOM 258 CB GLU A 33 23.381 58.558 55.569 1.00 55.40 C ANISOU 258 CB GLU A 33 7878 4804 8370 -469 -1249 -604 C ATOM 259 CG GLU A 33 22.580 59.786 55.967 1.00 84.36 C ANISOU 259 CG GLU A 33 11744 8288 12022 -410 -1151 -740 C ATOM 260 CD GLU A 33 22.774 60.158 57.423 1.00112.57 C ANISOU 260 CD GLU A 33 15485 11828 15458 -523 -1225 -924 C ATOM 261 OE1 GLU A 33 23.938 60.344 57.838 1.00119.60 O ANISOU 261 OE1 GLU A 33 16381 12696 16368 -715 -1367 -956 O ATOM 262 OE2 GLU A 33 21.767 60.257 58.155 1.00124.67 O ANISOU 262 OE2 GLU A 33 17143 13366 16861 -424 -1143 -1032 O ATOM 263 N PRO A 34 25.983 57.331 54.230 1.00 67.43 N ANISOU 263 N PRO A 34 9024 6475 10120 -685 -1435 -322 N ATOM 264 CA PRO A 34 26.832 56.158 53.957 1.00 64.23 C ANISOU 264 CA PRO A 34 8431 6227 9748 -728 -1508 -198 C ATOM 265 C PRO A 34 26.304 54.864 54.551 1.00 60.93 C ANISOU 265 C PRO A 34 7971 5991 9187 -657 -1529 -195 C ATOM 266 O PRO A 34 26.471 53.805 53.934 1.00 78.77 O ANISOU 266 O PRO A 34 10085 8366 11478 -605 -1514 -78 O ATOM 267 CB PRO A 34 28.179 56.555 54.576 1.00 49.94 C ANISOU 267 CB PRO A 34 6600 4381 7993 -935 -1659 -217 C ATOM 268 CG PRO A 34 28.181 58.039 54.535 1.00 46.92 C ANISOU 268 CG PRO A 34 6361 3788 7679 -996 -1634 -303 C ATOM 269 CD PRO A 34 26.759 58.450 54.790 1.00 59.42 C ANISOU 269 CD PRO A 34 8111 5310 9157 -851 -1518 -414 C ATOM 270 N TRP A 35 25.671 54.909 55.727 1.00 59.53 N ANISOU 270 N TRP A 35 7923 5842 8854 -654 -1555 -318 N ATOM 271 CA TRP A 35 25.134 53.683 56.310 1.00 57.26 C ANISOU 271 CA TRP A 35 7596 5728 8432 -589 -1570 -303 C ATOM 272 C TRP A 35 23.978 53.131 55.486 1.00 61.74 C ANISOU 272 C TRP A 35 8125 6343 8990 -408 -1433 -243 C ATOM 273 O TRP A 35 23.745 51.917 55.484 1.00 87.22 O ANISOU 273 O TRP A 35 11260 9712 12169 -355 -1439 -174 O ATOM 274 CB TRP A 35 24.692 53.924 57.754 1.00 45.77 C ANISOU 274 CB TRP A 35 6296 4293 6800 -628 -1617 -448 C ATOM 275 CG TRP A 35 23.470 54.782 57.895 1.00 68.80 C ANISOU 275 CG TRP A 35 9379 7107 9655 -518 -1488 -562 C ATOM 276 CD1 TRP A 35 23.432 56.140 58.019 1.00 70.67 C ANISOU 276 CD1 TRP A 35 9768 7161 9924 -553 -1453 -675 C ATOM 277 CD2 TRP A 35 22.109 54.336 57.943 1.00 79.98 C ANISOU 277 CD2 TRP A 35 10821 8593 10976 -353 -1371 -567 C ATOM 278 NE1 TRP A 35 22.132 56.568 58.134 1.00 71.63 N ANISOU 278 NE1 TRP A 35 10005 7230 9981 -406 -1313 -748 N ATOM 279 CE2 TRP A 35 21.300 55.480 58.090 1.00 77.11 C ANISOU 279 CE2 TRP A 35 10618 8086 10596 -284 -1263 -679 C ATOM 280 CE3 TRP A 35 21.496 53.081 57.872 1.00 86.72 C ANISOU 280 CE3 TRP A 35 11574 9611 11765 -259 -1346 -482 C ATOM 281 CZ2 TRP A 35 19.910 55.408 58.167 1.00 75.89 C ANISOU 281 CZ2 TRP A 35 10509 7958 10366 -119 -1129 -700 C ATOM 282 CZ3 TRP A 35 20.116 53.011 57.949 1.00 68.51 C ANISOU 282 CZ3 TRP A 35 9318 7333 9381 -111 -1223 -506 C ATOM 283 CH2 TRP A 35 19.339 54.167 58.095 1.00 73.35 C ANISOU 283 CH2 TRP A 35 10076 7813 9982 -39 -1116 -609 C ATOM 284 N GLN A 36 23.247 53.999 54.784 1.00 65.05 N ANISOU 284 N GLN A 36 8614 6643 9459 -317 -1316 -261 N ATOM 285 CA GLN A 36 22.192 53.522 53.897 1.00 53.06 C ANISOU 285 CA GLN A 36 7046 5173 7940 -158 -1201 -187 C ATOM 286 C GLN A 36 22.768 52.784 52.696 1.00 56.14 C ANISOU 286 C GLN A 36 7280 5618 8433 -152 -1195 -47 C ATOM 287 O GLN A 36 22.129 51.866 52.170 1.00 61.72 O ANISOU 287 O GLN A 36 7917 6425 9108 -58 -1145 20 O ATOM 288 CB GLN A 36 21.319 54.691 53.445 1.00 56.78 C ANISOU 288 CB GLN A 36 7621 5503 8449 -64 -1085 -224 C ATOM 289 CG GLN A 36 20.591 55.381 54.587 1.00 67.05 C ANISOU 289 CG GLN A 36 9086 6745 9646 -39 -1056 -369 C ATOM 290 CD GLN A 36 19.797 56.587 54.131 1.00 70.64 C ANISOU 290 CD GLN A 36 9638 7038 10164 61 -934 -397 C ATOM 291 OE1 GLN A 36 20.363 57.625 53.791 1.00 73.75 O ANISOU 291 OE1 GLN A 36 10085 7268 10668 2 -933 -414 O ATOM 292 NE2 GLN A 36 18.477 56.455 54.122 1.00 71.05 N ANISOU 292 NE2 GLN A 36 9707 7132 10157 214 -830 -392 N ATOM 293 N PHE A 37 23.967 53.168 52.248 1.00 63.65 N ANISOU 293 N PHE A 37 8175 6503 9505 -255 -1240 -2 N ATOM 294 CA PHE A 37 24.649 52.389 51.221 1.00 63.56 C ANISOU 294 CA PHE A 37 8013 6554 9583 -256 -1230 125 C ATOM 295 C PHE A 37 25.171 51.073 51.779 1.00 65.80 C ANISOU 295 C PHE A 37 8196 6979 9825 -293 -1312 161 C ATOM 296 O PHE A 37 25.187 50.061 51.068 1.00 53.61 O ANISOU 296 O PHE A 37 6550 5517 8302 -236 -1275 247 O ATOM 297 CB PHE A 37 25.793 53.199 50.611 1.00 38.15 C ANISOU 297 CB PHE A 37 4754 3228 6512 -355 -1245 174 C ATOM 298 CG PHE A 37 25.337 54.283 49.678 1.00 72.61 C ANISOU 298 CG PHE A 37 9181 7463 10945 -300 -1144 191 C ATOM 299 CD1 PHE A 37 25.158 54.023 48.329 1.00 65.33 C ANISOU 299 CD1 PHE A 37 8188 6563 10070 -221 -1051 301 C ATOM 300 CD2 PHE A 37 25.086 55.562 50.148 1.00 64.61 C ANISOU 300 CD2 PHE A 37 8303 6301 9943 -329 -1141 101 C ATOM 301 CE1 PHE A 37 24.737 55.017 47.466 1.00 63.94 C ANISOU 301 CE1 PHE A 37 8066 6277 9953 -171 -965 335 C ATOM 302 CE2 PHE A 37 24.665 56.561 49.289 1.00 69.50 C ANISOU 302 CE2 PHE A 37 8976 6791 10638 -273 -1047 133 C ATOM 303 CZ PHE A 37 24.490 56.288 47.947 1.00 67.89 C ANISOU 303 CZ PHE A 37 8690 6623 10481 -194 -963 259 C ATOM 304 N SER A 38 25.599 51.066 53.044 1.00 54.81 N ANISOU 304 N SER A 38 6837 5614 8374 -388 -1425 97 N ATOM 305 CA SER A 38 26.016 49.819 53.675 1.00 55.77 C ANISOU 305 CA SER A 38 6866 5873 8452 -417 -1508 141 C ATOM 306 C SER A 38 24.835 48.876 53.860 1.00 61.01 C ANISOU 306 C SER A 38 7547 6637 8998 -299 -1456 137 C ATOM 307 O SER A 38 24.978 47.656 53.714 1.00 52.21 O ANISOU 307 O SER A 38 6330 5621 7889 -271 -1465 216 O ATOM 308 CB SER A 38 26.690 50.109 55.015 1.00 40.53 C ANISOU 308 CB SER A 38 4977 3956 6466 -554 -1650 78 C ATOM 309 OG SER A 38 27.852 50.900 54.841 1.00 60.58 O ANISOU 309 OG SER A 38 7482 6410 9126 -681 -1713 94 O ATOM 310 N MET A 39 23.659 49.421 54.182 1.00 69.05 N ANISOU 310 N MET A 39 8690 7627 9918 -230 -1395 51 N ATOM 311 CA MET A 39 22.464 48.590 54.278 1.00 60.47 C ANISOU 311 CA MET A 39 7609 6635 8731 -119 -1337 59 C ATOM 312 C MET A 39 22.049 48.065 52.910 1.00 62.08 C ANISOU 312 C MET A 39 7735 6851 9000 -26 -1246 148 C ATOM 313 O MET A 39 21.563 46.934 52.795 1.00 53.54 O ANISOU 313 O MET A 39 6597 5866 7879 28 -1230 196 O ATOM 314 CB MET A 39 21.324 49.375 54.925 1.00 55.91 C ANISOU 314 CB MET A 39 7173 6022 8047 -61 -1282 -46 C ATOM 315 CG MET A 39 21.439 49.486 56.433 1.00 65.36 C ANISOU 315 CG MET A 39 8458 7257 9118 -135 -1362 -138 C ATOM 316 SD MET A 39 21.693 47.872 57.196 1.00 75.53 S ANISOU 316 SD MET A 39 9648 8724 10325 -166 -1454 -65 S ATOM 317 CE MET A 39 21.460 48.273 58.925 1.00103.30 C ANISOU 317 CE MET A 39 13311 12283 13655 -230 -1516 -189 C ATOM 318 N LEU A 40 22.225 48.876 51.864 1.00 56.19 N ANISOU 318 N LEU A 40 6992 6008 8351 -13 -1186 170 N ATOM 319 CA LEU A 40 22.029 48.375 50.508 1.00 58.89 C ANISOU 319 CA LEU A 40 7261 6368 8746 54 -1111 258 C ATOM 320 C LEU A 40 22.998 47.240 50.205 1.00 70.16 C ANISOU 320 C LEU A 40 8568 7859 10231 15 -1146 334 C ATOM 321 O LEU A 40 22.612 46.221 49.620 1.00 69.70 O ANISOU 321 O LEU A 40 8459 7869 10156 73 -1106 383 O ATOM 322 CB LEU A 40 22.198 49.509 49.497 1.00 59.03 C ANISOU 322 CB LEU A 40 7304 6271 8855 61 -1049 280 C ATOM 323 CG LEU A 40 22.244 49.090 48.025 1.00 57.39 C ANISOU 323 CG LEU A 40 7025 6082 8700 107 -976 376 C ATOM 324 CD1 LEU A 40 20.925 48.461 47.600 1.00 37.45 C ANISOU 324 CD1 LEU A 40 4508 3634 6088 210 -922 394 C ATOM 325 CD2 LEU A 40 22.596 50.271 47.133 1.00 62.46 C ANISOU 325 CD2 LEU A 40 7688 6610 9433 94 -925 410 C ATOM 326 N ALA A 41 24.263 47.398 50.603 1.00 64.68 N ANISOU 326 N ALA A 41 7825 7142 9609 -85 -1221 345 N ATOM 327 CA ALA A 41 25.234 46.325 50.431 1.00 53.50 C ANISOU 327 CA ALA A 41 6283 5784 8262 -115 -1251 425 C ATOM 328 C ALA A 41 24.902 45.123 51.302 1.00 64.69 C ANISOU 328 C ALA A 41 7676 7305 9597 -98 -1303 429 C ATOM 329 O ALA A 41 25.170 43.981 50.910 1.00 69.18 O ANISOU 329 O ALA A 41 8157 7923 10204 -68 -1285 497 O ATOM 330 CB ALA A 41 26.640 46.835 50.746 1.00 36.52 C ANISOU 330 CB ALA A 41 4072 3591 6214 -231 -1330 449 C ATOM 331 N ALA A 42 24.320 45.355 52.481 1.00 63.97 N ANISOU 331 N ALA A 42 7667 7243 9394 -114 -1360 358 N ATOM 332 CA ALA A 42 23.966 44.247 53.361 1.00 62.86 C ANISOU 332 CA ALA A 42 7507 7207 9169 -101 -1409 372 C ATOM 333 C ALA A 42 22.834 43.414 52.774 1.00 63.95 C ANISOU 333 C ALA A 42 7646 7390 9262 2 -1324 394 C ATOM 334 O ALA A 42 22.853 42.181 52.864 1.00 73.32 O ANISOU 334 O ALA A 42 8768 8641 10450 19 -1336 451 O ATOM 335 CB ALA A 42 23.586 44.775 54.743 1.00 33.51 C ANISOU 335 CB ALA A 42 3891 3515 5325 -145 -1477 288 C ATOM 336 N TYR A 43 21.840 44.066 52.166 1.00 55.73 N ANISOU 336 N TYR A 43 6674 6312 8187 67 -1242 355 N ATOM 337 CA TYR A 43 20.727 43.320 51.590 1.00 58.05 C ANISOU 337 CA TYR A 43 6964 6655 8436 150 -1174 381 C ATOM 338 C TYR A 43 21.156 42.570 50.335 1.00 54.27 C ANISOU 338 C TYR A 43 6410 6168 8042 169 -1127 448 C ATOM 339 O TYR A 43 20.682 41.457 50.080 1.00 57.12 O ANISOU 339 O TYR A 43 6741 6581 8381 202 -1108 481 O ATOM 340 CB TYR A 43 19.558 44.255 51.282 1.00 40.68 C ANISOU 340 CB TYR A 43 4845 4426 6186 216 -1106 338 C ATOM 341 CG TYR A 43 18.293 43.512 50.919 1.00 66.12 C ANISOU 341 CG TYR A 43 8058 7718 9347 289 -1057 367 C ATOM 342 CD1 TYR A 43 17.504 42.927 51.902 1.00 73.24 C ANISOU 342 CD1 TYR A 43 8971 8702 10156 306 -1076 356 C ATOM 343 CD2 TYR A 43 17.893 43.383 49.595 1.00 63.85 C ANISOU 343 CD2 TYR A 43 7748 7422 9090 332 -996 410 C ATOM 344 CE1 TYR A 43 16.351 42.241 51.578 1.00 71.34 C ANISOU 344 CE1 TYR A 43 8709 8526 9870 361 -1037 392 C ATOM 345 CE2 TYR A 43 16.740 42.698 49.262 1.00 78.49 C ANISOU 345 CE2 TYR A 43 9589 9344 10888 381 -968 439 C ATOM 346 CZ TYR A 43 15.973 42.129 50.257 1.00 89.54 C ANISOU 346 CZ TYR A 43 10991 10820 12212 394 -989 432 C ATOM 347 OH TYR A 43 14.825 41.445 49.930 1.00102.14 O ANISOU 347 OH TYR A 43 12562 12484 13761 432 -965 470 O ATOM 348 N MET A 44 22.045 43.166 49.536 1.00 58.03 N ANISOU 348 N MET A 44 6861 6574 8612 144 -1102 467 N ATOM 349 CA MET A 44 22.595 42.447 48.391 1.00 57.46 C ANISOU 349 CA MET A 44 6721 6494 8615 159 -1047 526 C ATOM 350 C MET A 44 23.372 41.219 48.844 1.00 63.92 C ANISOU 350 C MET A 44 7455 7351 9481 137 -1088 572 C ATOM 351 O MET A 44 23.313 40.165 48.201 1.00 66.66 O ANISOU 351 O MET A 44 7769 7713 9846 172 -1040 605 O ATOM 352 CB MET A 44 23.486 43.372 47.562 1.00 56.16 C ANISOU 352 CB MET A 44 6540 6254 8544 131 -1008 548 C ATOM 353 CG MET A 44 22.752 44.517 46.879 1.00 59.06 C ANISOU 353 CG MET A 44 6983 6573 8882 163 -953 527 C ATOM 354 SD MET A 44 21.516 43.967 45.687 1.00 66.69 S ANISOU 354 SD MET A 44 7979 7586 9773 245 -871 548 S ATOM 355 CE MET A 44 20.004 44.267 46.599 1.00 73.58 C ANISOU 355 CE MET A 44 8923 8498 10538 290 -901 498 C ATOM 356 N PHE A 45 24.102 41.336 49.957 1.00 57.98 N ANISOU 356 N PHE A 45 6671 6610 8748 75 -1180 575 N ATOM 357 CA PHE A 45 24.790 40.178 50.517 1.00 60.68 C ANISOU 357 CA PHE A 45 6926 6994 9136 59 -1231 636 C ATOM 358 C PHE A 45 23.802 39.113 50.970 1.00 58.77 C ANISOU 358 C PHE A 45 6707 6814 8810 100 -1236 637 C ATOM 359 O PHE A 45 24.092 37.915 50.874 1.00 61.35 O ANISOU 359 O PHE A 45 6970 7154 9187 120 -1228 694 O ATOM 360 CB PHE A 45 25.682 40.616 51.680 1.00 49.90 C ANISOU 360 CB PHE A 45 5526 5643 7789 -27 -1348 645 C ATOM 361 CG PHE A 45 26.499 39.505 52.274 1.00 52.58 C ANISOU 361 CG PHE A 45 5758 6029 8191 -46 -1412 731 C ATOM 362 CD1 PHE A 45 27.564 38.961 51.576 1.00 52.16 C ANISOU 362 CD1 PHE A 45 5589 5946 8284 -35 -1374 813 C ATOM 363 CD2 PHE A 45 26.212 39.015 53.538 1.00 64.94 C ANISOU 363 CD2 PHE A 45 7335 7668 9670 -71 -1505 740 C ATOM 364 CE1 PHE A 45 28.321 37.941 52.121 1.00 47.72 C ANISOU 364 CE1 PHE A 45 4917 5418 7795 -40 -1428 906 C ATOM 365 CE2 PHE A 45 26.966 37.996 54.090 1.00 67.93 C ANISOU 365 CE2 PHE A 45 7609 8088 10112 -85 -1569 838 C ATOM 366 CZ PHE A 45 28.022 37.458 53.381 1.00 54.64 C ANISOU 366 CZ PHE A 45 5803 6366 8590 -67 -1532 924 C ATOM 367 N LEU A 46 22.629 39.527 51.456 1.00 59.62 N ANISOU 367 N LEU A 46 6901 6954 8797 117 -1242 580 N ATOM 368 CA LEU A 46 21.606 38.565 51.852 1.00 59.80 C ANISOU 368 CA LEU A 46 6940 7041 8741 152 -1241 590 C ATOM 369 C LEU A 46 21.060 37.809 50.646 1.00 65.97 C ANISOU 369 C LEU A 46 7715 7806 9544 203 -1157 607 C ATOM 370 O LEU A 46 20.862 36.590 50.708 1.00 69.11 O ANISOU 370 O LEU A 46 8084 8227 9949 215 -1156 645 O ATOM 371 CB LEU A 46 20.478 39.282 52.594 1.00 67.91 C ANISOU 371 CB LEU A 46 8054 8109 9642 163 -1249 529 C ATOM 372 CG LEU A 46 19.294 38.441 53.072 1.00 61.31 C ANISOU 372 CG LEU A 46 7231 7347 8716 196 -1242 544 C ATOM 373 CD1 LEU A 46 19.755 37.387 54.058 1.00 70.90 C ANISOU 373 CD1 LEU A 46 8396 8614 9928 162 -1314 603 C ATOM 374 CD2 LEU A 46 18.229 39.326 53.698 1.00 70.85 C ANISOU 374 CD2 LEU A 46 8519 8588 9812 221 -1226 484 C ATOM 375 N LEU A 47 20.814 38.515 49.539 1.00 65.16 N ANISOU 375 N LEU A 47 7647 7663 9448 227 -1089 580 N ATOM 376 CA LEU A 47 20.283 37.862 48.346 1.00 57.87 C ANISOU 376 CA LEU A 47 6732 6732 8523 263 -1018 589 C ATOM 377 C LEU A 47 21.301 36.925 47.711 1.00 66.03 C ANISOU 377 C LEU A 47 7707 7724 9656 262 -981 627 C ATOM 378 O LEU A 47 20.917 35.959 47.042 1.00 70.36 O ANISOU 378 O LEU A 47 8265 8269 10199 281 -937 631 O ATOM 379 CB LEU A 47 19.824 38.909 47.332 1.00 64.49 C ANISOU 379 CB LEU A 47 7620 7547 9337 286 -961 564 C ATOM 380 CG LEU A 47 18.660 39.807 47.752 1.00 64.95 C ANISOU 380 CG LEU A 47 7734 7635 9309 310 -972 534 C ATOM 381 CD1 LEU A 47 18.343 40.817 46.659 1.00 58.73 C ANISOU 381 CD1 LEU A 47 6984 6813 8519 336 -916 532 C ATOM 382 CD2 LEU A 47 17.434 38.972 48.088 1.00 57.79 C ANISOU 382 CD2 LEU A 47 6833 6801 8325 330 -982 542 C ATOM 383 N ILE A 48 22.594 37.189 47.898 1.00 70.50 N ANISOU 383 N ILE A 48 8214 8256 10317 238 -997 654 N ATOM 384 CA ILE A 48 23.615 36.305 47.346 1.00 71.10 C ANISOU 384 CA ILE A 48 8221 8291 10503 250 -948 699 C ATOM 385 C ILE A 48 23.764 35.052 48.200 1.00 72.78 C ANISOU 385 C ILE A 48 8384 8521 10748 252 -995 745 C ATOM 386 O ILE A 48 23.872 33.939 47.674 1.00 69.85 O ANISOU 386 O ILE A 48 7998 8116 10426 283 -938 764 O ATOM 387 CB ILE A 48 24.952 37.057 47.205 1.00 64.60 C ANISOU 387 CB ILE A 48 7330 7430 9784 224 -944 731 C ATOM 388 CG1 ILE A 48 24.805 38.236 46.241 1.00 64.56 C ANISOU 388 CG1 ILE A 48 7377 7397 9757 223 -886 699 C ATOM 389 CG2 ILE A 48 26.047 36.117 46.722 1.00 37.89 C ANISOU 389 CG2 ILE A 48 3859 4008 6529 248 -884 790 C ATOM 390 CD1 ILE A 48 26.013 39.152 46.211 1.00 43.01 C ANISOU 390 CD1 ILE A 48 4586 4631 7127 181 -892 732 C ATOM 391 N MET A 49 23.762 35.209 49.527 1.00 77.07 N ANISOU 391 N MET A 49 8910 9114 11261 218 -1097 763 N ATOM 392 CA MET A 49 23.938 34.060 50.409 1.00 68.33 C ANISOU 392 CA MET A 49 7750 8030 10182 217 -1150 827 C ATOM 393 C MET A 49 22.727 33.136 50.389 1.00 66.28 C ANISOU 393 C MET A 49 7544 7789 9851 240 -1130 815 C ATOM 394 O MET A 49 22.861 31.940 50.669 1.00 70.83 O ANISOU 394 O MET A 49 8082 8351 10480 252 -1135 871 O ATOM 395 CB MET A 49 24.220 34.530 51.837 1.00 63.48 C ANISOU 395 CB MET A 49 7114 7479 9528 164 -1270 851 C ATOM 396 CG MET A 49 25.521 35.305 52.009 1.00 65.86 C ANISOU 396 CG MET A 49 7347 7766 9913 120 -1316 878 C ATOM 397 SD MET A 49 27.009 34.309 51.775 1.00 78.47 S ANISOU 397 SD MET A 49 8793 9321 11700 138 -1303 995 S ATOM 398 CE MET A 49 27.445 34.716 50.086 1.00 80.49 C ANISOU 398 CE MET A 49 9046 9493 12042 179 -1158 963 C ATOM 399 N LEU A 50 21.546 33.662 50.069 1.00 62.62 N ANISOU 399 N LEU A 50 7160 7353 9279 245 -1108 753 N ATOM 400 CA LEU A 50 20.337 32.852 50.001 1.00 54.98 C ANISOU 400 CA LEU A 50 6233 6409 8246 255 -1094 747 C ATOM 401 C LEU A 50 19.939 32.483 48.580 1.00 77.12 C ANISOU 401 C LEU A 50 9079 9167 11056 274 -1009 711 C ATOM 402 O LEU A 50 19.293 31.450 48.380 1.00 89.22 O ANISOU 402 O LEU A 50 10631 10692 12579 272 -995 718 O ATOM 403 CB LEU A 50 19.164 33.581 50.667 1.00 56.72 C ANISOU 403 CB LEU A 50 6504 6708 8339 247 -1130 716 C ATOM 404 CG LEU A 50 19.277 33.905 52.158 1.00 65.77 C ANISOU 404 CG LEU A 50 7638 7916 9434 223 -1210 736 C ATOM 405 CD1 LEU A 50 17.977 34.516 52.665 1.00 37.17 C ANISOU 405 CD1 LEU A 50 4073 4364 5685 232 -1212 700 C ATOM 406 CD2 LEU A 50 19.640 32.664 52.959 1.00 50.23 C ANISOU 406 CD2 LEU A 50 5617 5964 7506 208 -1258 816 C ATOM 407 N GLY A 51 20.305 33.295 47.592 1.00 73.75 N ANISOU 407 N GLY A 51 8671 8709 10641 285 -955 676 N ATOM 408 CA GLY A 51 19.886 33.055 46.226 1.00 46.73 C ANISOU 408 CA GLY A 51 5301 5258 7195 295 -879 640 C ATOM 409 C GLY A 51 20.778 32.103 45.457 1.00 61.48 C ANISOU 409 C GLY A 51 7156 7048 9157 311 -804 644 C ATOM 410 O GLY A 51 20.293 31.321 44.634 1.00 70.35 O ANISOU 410 O GLY A 51 8332 8144 10254 309 -756 614 O ATOM 411 N PHE A 52 22.094 32.159 45.712 1.00 69.14 N ANISOU 411 N PHE A 52 8054 7979 10238 326 -792 683 N ATOM 412 CA PHE A 52 23.014 31.301 44.964 1.00 83.51 C ANISOU 412 CA PHE A 52 9851 9717 12161 358 -700 693 C ATOM 413 C PHE A 52 22.874 29.831 45.345 1.00 83.72 C ANISOU 413 C PHE A 52 9872 9701 12238 369 -701 716 C ATOM 414 O PHE A 52 22.636 29.000 44.451 1.00 84.65 O ANISOU 414 O PHE A 52 10052 9759 12354 380 -623 673 O ATOM 415 CB PHE A 52 24.451 31.802 45.124 1.00 77.05 C ANISOU 415 CB PHE A 52 8937 8877 11462 373 -685 745 C ATOM 416 CG PHE A 52 25.486 30.825 44.642 1.00 76.11 C ANISOU 416 CG PHE A 52 8766 8676 11477 421 -590 778 C ATOM 417 CD1 PHE A 52 25.707 30.642 43.287 1.00 77.66 C ANISOU 417 CD1 PHE A 52 9012 8820 11676 451 -457 732 C ATOM 418 CD2 PHE A 52 26.234 30.086 45.544 1.00 80.10 C ANISOU 418 CD2 PHE A 52 9173 9160 12103 439 -628 860 C ATOM 419 CE1 PHE A 52 26.657 29.743 42.840 1.00 74.65 C ANISOU 419 CE1 PHE A 52 8588 8356 11421 507 -349 757 C ATOM 420 CE2 PHE A 52 27.186 29.184 45.102 1.00 70.79 C ANISOU 420 CE2 PHE A 52 7937 7896 11064 498 -528 899 C ATOM 421 CZ PHE A 52 27.397 29.013 43.749 1.00 67.63 C ANISOU 421 CZ PHE A 52 7591 7434 10670 535 -381 842 C ATOM 422 N PRO A 53 23.009 29.432 46.618 1.00 80.23 N ANISOU 422 N PRO A 53 9366 9280 11837 362 -786 783 N ATOM 423 CA PRO A 53 22.979 27.988 46.909 1.00 74.38 C ANISOU 423 CA PRO A 53 8616 8480 11166 377 -776 820 C ATOM 424 C PRO A 53 21.637 27.341 46.619 1.00 61.97 C ANISOU 424 C PRO A 53 7136 6907 9501 347 -777 771 C ATOM 425 O PRO A 53 21.600 26.186 46.181 1.00 83.53 O ANISOU 425 O PRO A 53 9900 9550 12287 357 -720 760 O ATOM 426 CB PRO A 53 23.336 27.924 48.400 1.00 61.77 C ANISOU 426 CB PRO A 53 6931 6933 9608 367 -884 915 C ATOM 427 CG PRO A 53 22.897 29.226 48.940 1.00 73.05 C ANISOU 427 CG PRO A 53 8372 8461 10922 328 -961 891 C ATOM 428 CD PRO A 53 23.169 30.225 47.853 1.00 75.31 C ANISOU 428 CD PRO A 53 8688 8734 11194 336 -893 827 C ATOM 429 N ILE A 54 20.531 28.052 46.844 1.00 69.29 N ANISOU 429 N ILE A 54 8103 7925 10298 308 -837 743 N ATOM 430 CA ILE A 54 19.217 27.470 46.586 1.00 68.47 C ANISOU 430 CA ILE A 54 8069 7836 10112 270 -848 711 C ATOM 431 C ILE A 54 19.012 27.249 45.092 1.00 64.56 C ANISOU 431 C ILE A 54 7659 7286 9587 262 -763 631 C ATOM 432 O ILE A 54 18.469 26.220 44.672 1.00 79.43 O ANISOU 432 O ILE A 54 9598 9116 11465 233 -744 604 O ATOM 433 CB ILE A 54 18.112 28.355 47.191 1.00 80.42 C ANISOU 433 CB ILE A 54 9588 9466 11503 242 -922 712 C ATOM 434 CG1 ILE A 54 18.260 28.421 48.713 1.00102.68 C ANISOU 434 CG1 ILE A 54 12342 12340 14330 242 -1000 784 C ATOM 435 CG2 ILE A 54 16.737 27.825 46.819 1.00 74.68 C ANISOU 435 CG2 ILE A 54 8915 8764 10696 198 -934 691 C ATOM 436 CD1 ILE A 54 17.156 29.196 49.403 1.00103.38 C ANISOU 436 CD1 ILE A 54 12442 12540 14299 224 -1055 783 C ATOM 437 N ASN A 55 19.451 28.200 44.265 1.00 64.24 N ANISOU 437 N ASN A 55 7634 7255 9520 281 -714 592 N ATOM 438 CA ASN A 55 19.305 28.046 42.822 1.00 60.59 C ANISOU 438 CA ASN A 55 7260 6754 9008 271 -632 519 C ATOM 439 C ASN A 55 20.366 27.128 42.229 1.00 71.35 C ANISOU 439 C ASN A 55 8636 7997 10478 309 -524 498 C ATOM 440 O ASN A 55 20.097 26.444 41.236 1.00 88.15 O ANISOU 440 O ASN A 55 10857 10068 12568 289 -459 429 O ATOM 441 CB ASN A 55 19.350 29.412 42.137 1.00 57.26 C ANISOU 441 CB ASN A 55 6852 6391 8514 277 -614 499 C ATOM 442 CG ASN A 55 18.052 30.178 42.282 1.00 73.88 C ANISOU 442 CG ASN A 55 8975 8597 10498 243 -693 501 C ATOM 443 OD1 ASN A 55 17.105 29.963 41.525 1.00 80.81 O ANISOU 443 OD1 ASN A 55 9919 9502 11283 203 -698 467 O ATOM 444 ND2 ASN A 55 17.999 31.079 43.257 1.00 65.53 N ANISOU 444 ND2 ASN A 55 7859 7596 9442 258 -753 541 N ATOM 445 N PHE A 56 21.567 27.100 42.811 1.00 69.39 N ANISOU 445 N PHE A 56 8295 7708 10360 361 -502 558 N ATOM 446 CA PHE A 56 22.597 26.193 42.314 1.00 63.47 C ANISOU 446 CA PHE A 56 7541 6841 9734 414 -387 552 C ATOM 447 C PHE A 56 22.280 24.749 42.682 1.00 72.75 C ANISOU 447 C PHE A 56 8742 7927 10971 409 -389 559 C ATOM 448 O PHE A 56 22.531 23.832 41.891 1.00 74.43 O ANISOU 448 O PHE A 56 9025 8028 11228 430 -283 504 O ATOM 449 CB PHE A 56 23.967 26.598 42.857 1.00 57.59 C ANISOU 449 CB PHE A 56 6668 6088 9126 471 -372 635 C ATOM 450 CG PHE A 56 25.086 25.702 42.405 1.00 65.70 C ANISOU 450 CG PHE A 56 7666 6996 10303 542 -242 649 C ATOM 451 CD1 PHE A 56 25.683 25.888 41.169 1.00 64.10 C ANISOU 451 CD1 PHE A 56 7504 6751 10102 577 -101 595 C ATOM 452 CD2 PHE A 56 25.542 24.675 43.216 1.00 60.91 C ANISOU 452 CD2 PHE A 56 6989 6318 9837 579 -254 725 C ATOM 453 CE1 PHE A 56 26.712 25.066 40.749 1.00 63.12 C ANISOU 453 CE1 PHE A 56 7351 6513 10119 655 38 607 C ATOM 454 CE2 PHE A 56 26.569 23.849 42.802 1.00 70.48 C ANISOU 454 CE2 PHE A 56 8167 7410 11202 660 -123 746 C ATOM 455 CZ PHE A 56 27.155 24.046 41.567 1.00 76.98 C ANISOU 455 CZ PHE A 56 9032 8189 12028 701 29 682 C ATOM 456 N LEU A 57 21.731 24.527 43.879 1.00 62.67 N ANISOU 456 N LEU A 57 7419 6696 9699 381 -502 625 N ATOM 457 CA LEU A 57 21.348 23.177 44.276 1.00 65.97 C ANISOU 457 CA LEU A 57 7860 7030 10176 368 -512 645 C ATOM 458 C LEU A 57 20.249 22.625 43.380 1.00 75.81 C ANISOU 458 C LEU A 57 9240 8244 11322 302 -492 547 C ATOM 459 O LEU A 57 20.180 21.411 43.159 1.00 85.72 O ANISOU 459 O LEU A 57 10552 9377 12641 294 -446 524 O ATOM 460 CB LEU A 57 20.902 23.165 45.739 1.00 55.54 C ANISOU 460 CB LEU A 57 6462 5786 8854 343 -640 744 C ATOM 461 CG LEU A 57 20.591 21.808 46.371 1.00 79.17 C ANISOU 461 CG LEU A 57 9456 8700 11926 329 -662 801 C ATOM 462 CD1 LEU A 57 21.823 20.917 46.359 1.00 82.64 C ANISOU 462 CD1 LEU A 57 9849 9000 12550 407 -578 851 C ATOM 463 CD2 LEU A 57 20.067 21.987 47.787 1.00 84.03 C ANISOU 463 CD2 LEU A 57 10000 9423 12502 298 -786 900 C ATOM 464 N THR A 58 19.385 23.497 42.853 1.00 75.68 N ANISOU 464 N THR A 58 9273 8331 11152 250 -531 494 N ATOM 465 CA THR A 58 18.353 23.051 41.923 1.00 70.24 C ANISOU 465 CA THR A 58 8705 7627 10355 175 -526 406 C ATOM 466 C THR A 58 18.969 22.461 40.661 1.00 81.31 C ANISOU 466 C THR A 58 10210 8909 11777 193 -393 310 C ATOM 467 O THR A 58 18.528 21.411 40.177 1.00 82.13 O ANISOU 467 O THR A 58 10414 8918 11873 144 -366 245 O ATOM 468 CB THR A 58 17.425 24.215 41.571 1.00 61.20 C ANISOU 468 CB THR A 58 7574 6626 9053 129 -591 388 C ATOM 469 OG1 THR A 58 16.823 24.727 42.767 1.00 67.66 O ANISOU 469 OG1 THR A 58 8305 7547 9854 120 -698 469 O ATOM 470 CG2 THR A 58 16.334 23.761 40.613 1.00 57.71 C ANISOU 470 CG2 THR A 58 7246 6187 8496 38 -606 312 C ATOM 471 N LEU A 59 19.994 23.119 40.116 1.00 82.07 N ANISOU 471 N LEU A 59 10287 9002 11895 260 -302 297 N ATOM 472 CA LEU A 59 20.667 22.589 38.936 1.00 75.30 C ANISOU 472 CA LEU A 59 9525 8033 11053 290 -152 207 C ATOM 473 C LEU A 59 21.535 21.386 39.279 1.00 73.42 C ANISOU 473 C LEU A 59 9266 7634 10997 358 -64 227 C ATOM 474 O LEU A 59 21.793 20.544 38.412 1.00 73.67 O ANISOU 474 O LEU A 59 9408 7538 11045 370 57 137 O ATOM 475 CB LEU A 59 21.511 23.680 38.278 1.00 66.01 C ANISOU 475 CB LEU A 59 8321 6910 9852 343 -73 205 C ATOM 476 CG LEU A 59 20.778 24.960 37.873 1.00 85.91 C ANISOU 476 CG LEU A 59 10857 9576 12208 291 -145 198 C ATOM 477 CD1 LEU A 59 21.736 25.942 37.216 1.00 83.31 C ANISOU 477 CD1 LEU A 59 10500 9277 11878 345 -53 207 C ATOM 478 CD2 LEU A 59 19.611 24.644 36.951 1.00 94.05 C ANISOU 478 CD2 LEU A 59 12030 10631 13074 198 -171 108 C ATOM 479 N TYR A 60 21.989 21.284 40.529 1.00 72.18 N ANISOU 479 N TYR A 60 8974 7477 10974 403 -122 346 N ATOM 480 CA TYR A 60 22.871 20.188 40.912 1.00 70.03 C ANISOU 480 CA TYR A 60 8660 7055 10893 480 -43 393 C ATOM 481 C TYR A 60 22.101 18.891 41.128 1.00 76.28 C ANISOU 481 C TYR A 60 9533 7737 11713 428 -68 371 C ATOM 482 O TYR A 60 22.548 17.823 40.696 1.00 90.41 O ANISOU 482 O TYR A 60 11388 9356 13607 470 49 327 O ATOM 483 CB TYR A 60 23.656 20.561 42.170 1.00 69.70 C ANISOU 483 CB TYR A 60 8439 7066 10978 538 -110 544 C ATOM 484 CG TYR A 60 24.688 19.532 42.575 1.00 75.60 C ANISOU 484 CG TYR A 60 9114 7671 11940 631 -32 622 C ATOM 485 CD1 TYR A 60 25.929 19.485 41.955 1.00 82.88 C ANISOU 485 CD1 TYR A 60 9998 8515 12979 730 119 622 C ATOM 486 CD2 TYR A 60 24.421 18.611 43.579 1.00 83.46 C ANISOU 486 CD2 TYR A 60 10072 8611 13026 624 -103 710 C ATOM 487 CE1 TYR A 60 26.876 18.548 42.321 1.00 85.60 C ANISOU 487 CE1 TYR A 60 10261 8727 13535 827 198 708 C ATOM 488 CE2 TYR A 60 25.362 17.670 43.953 1.00 88.31 C ANISOU 488 CE2 TYR A 60 10614 9092 13849 716 -33 799 C ATOM 489 CZ TYR A 60 26.587 17.643 43.320 1.00 93.09 C ANISOU 489 CZ TYR A 60 11175 9619 14577 821 118 798 C ATOM 490 OH TYR A 60 27.527 16.707 43.689 1.00100.87 O ANISOU 490 OH TYR A 60 12074 10468 15784 925 194 900 O ATOM 491 N VAL A 61 20.945 18.959 41.795 1.00 69.37 N ANISOU 491 N VAL A 61 8655 6950 10753 339 -212 402 N ATOM 492 CA VAL A 61 20.159 17.754 42.033 1.00 57.15 C ANISOU 492 CA VAL A 61 7176 5303 9234 275 -245 393 C ATOM 493 C VAL A 61 19.564 17.206 40.743 1.00 65.82 C ANISOU 493 C VAL A 61 8455 6317 10238 202 -180 237 C ATOM 494 O VAL A 61 19.261 16.011 40.666 1.00 81.79 O ANISOU 494 O VAL A 61 10562 8192 12323 164 -155 202 O ATOM 495 CB VAL A 61 19.050 18.017 43.069 1.00 52.81 C ANISOU 495 CB VAL A 61 6566 4885 8613 196 -408 475 C ATOM 496 CG1 VAL A 61 19.656 18.437 44.400 1.00 64.14 C ANISOU 496 CG1 VAL A 61 7843 6396 10132 259 -472 622 C ATOM 497 CG2 VAL A 61 18.075 19.070 42.559 1.00 53.77 C ANISOU 497 CG2 VAL A 61 6725 5165 8538 120 -477 416 C ATOM 498 N THR A 62 19.389 18.048 39.722 1.00 71.00 N ANISOU 498 N THR A 62 9178 7058 10739 175 -155 145 N ATOM 499 CA THR A 62 18.902 17.550 38.441 1.00 74.71 C ANISOU 499 CA THR A 62 9829 7457 11099 100 -95 -7 C ATOM 500 C THR A 62 19.956 16.702 37.741 1.00 76.22 C ANISOU 500 C THR A 62 10108 7455 11399 181 91 -87 C ATOM 501 O THR A 62 19.614 15.780 36.991 1.00 74.06 O ANISOU 501 O THR A 62 9996 7051 11093 121 149 -208 O ATOM 502 CB THR A 62 18.476 18.718 37.550 1.00 72.83 C ANISOU 502 CB THR A 62 9634 7376 10663 54 -120 -65 C ATOM 503 OG1 THR A 62 17.663 19.624 38.306 1.00 72.83 O ANISOU 503 OG1 THR A 62 9528 7550 10593 12 -273 28 O ATOM 504 CG2 THR A 62 17.675 18.214 36.362 1.00 70.79 C ANISOU 504 CG2 THR A 62 9562 7082 10255 -61 -110 -207 C ATOM 505 N VAL A 63 21.237 16.990 37.981 1.00 80.08 N ANISOU 505 N VAL A 63 10490 7918 12019 315 189 -22 N ATOM 506 CA VAL A 63 22.305 16.193 37.387 1.00 82.46 C ANISOU 506 CA VAL A 63 10849 8034 12447 414 384 -80 C ATOM 507 C VAL A 63 22.412 14.835 38.071 1.00 81.39 C ANISOU 507 C VAL A 63 10713 7711 12500 442 404 -37 C ATOM 508 O VAL A 63 22.775 13.838 37.435 1.00 83.80 O ANISOU 508 O VAL A 63 11140 7821 12878 477 551 -132 O ATOM 509 CB VAL A 63 23.636 16.969 37.448 1.00 71.35 C ANISOU 509 CB VAL A 63 9303 6673 11134 547 477 -1 C ATOM 510 CG1 VAL A 63 24.761 16.170 36.808 1.00 60.86 C ANISOU 510 CG1 VAL A 63 8021 5158 9947 664 698 -52 C ATOM 511 CG2 VAL A 63 23.492 18.323 36.770 1.00 66.02 C ANISOU 511 CG2 VAL A 63 8634 6172 10277 512 456 -35 C ATOM 512 N GLN A 64 22.086 14.763 39.362 1.00 73.52 N ANISOU 512 N GLN A 64 9588 6765 11582 427 263 105 N ATOM 513 CA GLN A 64 22.247 13.540 40.135 1.00 84.92 C ANISOU 513 CA GLN A 64 11006 8042 13219 460 272 182 C ATOM 514 C GLN A 64 20.983 12.695 40.223 1.00 93.55 C ANISOU 514 C GLN A 64 12215 9071 14260 324 183 134 C ATOM 515 O GLN A 64 21.046 11.574 40.739 1.00100.84 O ANISOU 515 O GLN A 64 13143 9828 15342 339 201 186 O ATOM 516 CB GLN A 64 22.724 13.868 41.556 1.00 78.64 C ANISOU 516 CB GLN A 64 9998 7334 12546 525 174 384 C ATOM 517 CG GLN A 64 24.164 14.339 41.638 1.00 87.69 C ANISOU 517 CG GLN A 64 11009 8488 13819 668 269 462 C ATOM 518 CD GLN A 64 24.659 14.433 43.068 1.00103.61 C ANISOU 518 CD GLN A 64 12829 10568 15969 720 166 664 C ATOM 519 OE1 GLN A 64 25.856 14.583 43.314 1.00124.25 O ANISOU 519 OE1 GLN A 64 15312 13169 18727 833 227 760 O ATOM 520 NE2 GLN A 64 23.737 14.344 44.020 1.00 84.96 N ANISOU 520 NE2 GLN A 64 10442 8283 13556 633 7 737 N ATOM 521 N HIS A 65 19.845 13.190 39.741 1.00 81.67 N ANISOU 521 N HIS A 65 10794 7691 12548 189 85 51 N ATOM 522 CA HIS A 65 18.578 12.472 39.844 1.00 71.55 C ANISOU 522 CA HIS A 65 9601 6374 11213 42 -19 20 C ATOM 523 C HIS A 65 17.948 12.379 38.461 1.00 77.64 C ANISOU 523 C HIS A 65 10571 7121 11809 -68 14 -171 C ATOM 524 O HIS A 65 17.530 13.393 37.893 1.00 81.77 O ANISOU 524 O HIS A 65 11105 7817 12147 -117 -37 -216 O ATOM 525 CB HIS A 65 17.641 13.155 40.839 1.00 46.08 C ANISOU 525 CB HIS A 65 6248 3352 7908 -30 -205 144 C ATOM 526 CG HIS A 65 18.161 13.159 42.244 1.00 61.29 C ANISOU 526 CG HIS A 65 7999 5306 9982 56 -250 327 C ATOM 527 ND1 HIS A 65 17.747 12.250 43.194 1.00 66.00 N ANISOU 527 ND1 HIS A 65 8559 5831 10688 20 -314 433 N ATOM 528 CD2 HIS A 65 19.070 13.954 42.856 1.00 70.23 C ANISOU 528 CD2 HIS A 65 8985 6533 11165 167 -246 429 C ATOM 529 CE1 HIS A 65 18.374 12.489 44.332 1.00 63.02 C ANISOU 529 CE1 HIS A 65 8022 5511 10409 109 -348 593 C ATOM 530 NE2 HIS A 65 19.182 13.518 44.154 1.00 72.97 N ANISOU 530 NE2 HIS A 65 9216 6874 11637 195 -313 589 N ATOM 531 N LYS A 66 17.877 11.156 37.929 1.00 83.39 N ANISOU 531 N LYS A 66 11460 7629 12595 -111 95 -280 N ATOM 532 CA LYS A 66 17.358 10.947 36.582 1.00 86.90 C ANISOU 532 CA LYS A 66 12118 8031 12870 -224 132 -477 C ATOM 533 C LYS A 66 15.869 11.263 36.489 1.00 89.48 C ANISOU 533 C LYS A 66 12469 8515 13014 -412 -56 -487 C ATOM 534 O LYS A 66 15.400 11.721 35.440 1.00 88.77 O ANISOU 534 O LYS A 66 12491 8514 12722 -501 -75 -605 O ATOM 535 CB LYS A 66 17.644 9.506 36.146 1.00 75.67 C ANISOU 535 CB LYS A 66 10869 6316 11568 -228 265 -593 C ATOM 536 CG LYS A 66 16.505 8.794 35.433 1.00 88.90 C ANISOU 536 CG LYS A 66 12744 7917 13116 -428 197 -739 C ATOM 537 CD LYS A 66 16.888 7.357 35.112 1.00111.78 C ANISOU 537 CD LYS A 66 15814 10496 16162 -419 340 -851 C ATOM 538 CE LYS A 66 15.737 6.597 34.473 1.00129.13 C ANISOU 538 CE LYS A 66 18214 12608 18242 -639 257 -996 C ATOM 539 NZ LYS A 66 16.116 5.192 34.153 1.00135.92 N ANISOU 539 NZ LYS A 66 19261 13132 19250 -632 405 -1119 N ATOM 540 N LYS A 67 15.118 11.049 37.570 1.00 86.39 N ANISOU 540 N LYS A 67 11967 8172 12688 -473 -197 -354 N ATOM 541 CA LYS A 67 13.680 11.291 37.546 1.00 76.94 C ANISOU 541 CA LYS A 67 10770 7122 11340 -647 -371 -344 C ATOM 542 C LYS A 67 13.324 12.772 37.506 1.00 68.98 C ANISOU 542 C LYS A 67 9653 6386 10170 -640 -459 -290 C ATOM 543 O LYS A 67 12.151 13.100 37.298 1.00 81.50 O ANISOU 543 O LYS A 67 11240 8111 11616 -775 -593 -287 O ATOM 544 CB LYS A 67 13.018 10.629 38.756 1.00 76.96 C ANISOU 544 CB LYS A 67 10674 7098 11469 -703 -478 -202 C ATOM 545 CG LYS A 67 13.133 9.115 38.760 1.00 91.87 C ANISOU 545 CG LYS A 67 12683 8710 13514 -744 -413 -251 C ATOM 546 CD LYS A 67 12.624 8.530 37.452 1.00 99.23 C ANISOU 546 CD LYS A 67 13844 9533 14327 -892 -395 -454 C ATOM 547 CE LYS A 67 12.888 7.037 37.368 1.00107.29 C ANISOU 547 CE LYS A 67 15009 10241 15513 -916 -302 -526 C ATOM 548 NZ LYS A 67 12.478 6.478 36.050 1.00117.39 N ANISOU 548 NZ LYS A 67 16537 11403 16663 -1063 -275 -748 N ATOM 549 N LEU A 68 14.292 13.666 37.697 1.00 67.45 N ANISOU 549 N LEU A 68 9362 6266 10001 -489 -389 -240 N ATOM 550 CA LEU A 68 14.041 15.099 37.619 1.00 60.81 C ANISOU 550 CA LEU A 68 8429 5658 9019 -474 -457 -195 C ATOM 551 C LEU A 68 14.214 15.661 36.214 1.00 68.42 C ANISOU 551 C LEU A 68 9516 6664 9815 -490 -393 -328 C ATOM 552 O LEU A 68 13.810 16.802 35.968 1.00 72.75 O ANISOU 552 O LEU A 68 10014 7401 10228 -504 -461 -298 O ATOM 553 CB LEU A 68 14.967 15.855 38.579 1.00 64.20 C ANISOU 553 CB LEU A 68 8688 6151 9554 -319 -429 -69 C ATOM 554 CG LEU A 68 14.709 15.692 40.077 1.00 72.69 C ANISOU 554 CG LEU A 68 9613 7261 10744 -303 -520 89 C ATOM 555 CD1 LEU A 68 15.724 16.491 40.881 1.00 63.79 C ANISOU 555 CD1 LEU A 68 8340 6199 9697 -161 -492 193 C ATOM 556 CD2 LEU A 68 13.293 16.118 40.426 1.00 66.28 C ANISOU 556 CD2 LEU A 68 8750 6617 9814 -417 -674 145 C ATOM 557 N ARG A 69 14.797 14.896 35.292 1.00 74.23 N ANISOU 557 N ARG A 69 10418 7230 10557 -485 -259 -469 N ATOM 558 CA ARG A 69 15.073 15.385 33.941 1.00 71.30 C ANISOU 558 CA ARG A 69 10176 6896 10018 -493 -176 -596 C ATOM 559 C ARG A 69 13.921 15.043 32.994 1.00 75.35 C ANISOU 559 C ARG A 69 10851 7438 10340 -682 -267 -710 C ATOM 560 O ARG A 69 14.078 14.359 31.983 1.00 71.92 O ANISOU 560 O ARG A 69 10613 6879 9834 -736 -177 -870 O ATOM 561 CB ARG A 69 16.398 14.823 33.438 1.00 76.51 C ANISOU 561 CB ARG A 69 10928 7369 10776 -373 38 -688 C ATOM 562 CG ARG A 69 17.600 15.264 34.259 1.00 72.17 C ANISOU 562 CG ARG A 69 10204 6812 10404 -191 122 -566 C ATOM 563 CD ARG A 69 18.912 14.892 33.589 1.00 66.92 C ANISOU 563 CD ARG A 69 9615 5994 9818 -65 347 -650 C ATOM 564 NE ARG A 69 19.113 13.448 33.525 1.00 86.17 N ANISOU 564 NE ARG A 69 12175 8184 12383 -63 445 -733 N ATOM 565 CZ ARG A 69 19.703 12.733 34.477 1.00 77.04 C ANISOU 565 CZ ARG A 69 10922 6886 11464 34 487 -639 C ATOM 566 NH1 ARG A 69 20.151 13.328 35.574 1.00 70.31 N ANISOU 566 NH1 ARG A 69 9854 6129 10732 126 430 -463 N ATOM 567 NH2 ARG A 69 19.845 11.423 34.334 1.00 80.23 N ANISOU 567 NH2 ARG A 69 11451 7048 11982 35 584 -719 N ATOM 568 N THR A 70 12.729 15.552 33.348 1.00 86.75 N ANISOU 568 N THR A 70 12206 9055 11700 -787 -450 -623 N ATOM 569 CA THR A 70 11.519 15.432 32.553 1.00 78.02 C ANISOU 569 CA THR A 70 11205 8029 10409 -976 -576 -689 C ATOM 570 C THR A 70 11.254 16.727 31.792 1.00 83.88 C ANISOU 570 C THR A 70 11930 8987 10955 -984 -622 -674 C ATOM 571 O THR A 70 11.662 17.806 32.234 1.00 87.31 O ANISOU 571 O THR A 70 12221 9536 11418 -863 -610 -569 O ATOM 572 CB THR A 70 10.313 15.106 33.441 1.00 75.80 C ANISOU 572 CB THR A 70 10819 7804 10178 -1088 -748 -581 C ATOM 573 OG1 THR A 70 10.144 16.139 34.421 1.00 99.92 O ANISOU 573 OG1 THR A 70 13661 11028 13275 -1001 -816 -412 O ATOM 574 CG2 THR A 70 10.516 13.773 34.146 1.00 66.76 C ANISOU 574 CG2 THR A 70 9702 6439 9224 -1095 -707 -587 C ATOM 575 N PRO A 71 10.587 16.651 30.636 1.00 77.91 N ANISOU 575 N PRO A 71 11321 8285 9997 -1131 -680 -774 N ATOM 576 CA PRO A 71 10.336 17.877 29.857 1.00 74.77 C ANISOU 576 CA PRO A 71 10909 8092 9408 -1140 -726 -746 C ATOM 577 C PRO A 71 9.552 18.935 30.612 1.00 68.42 C ANISOU 577 C PRO A 71 9893 7490 8613 -1123 -870 -566 C ATOM 578 O PRO A 71 9.807 20.131 30.422 1.00 82.06 O ANISOU 578 O PRO A 71 11549 9350 10281 -1038 -855 -500 O ATOM 579 CB PRO A 71 9.559 17.360 28.639 1.00 71.91 C ANISOU 579 CB PRO A 71 10741 7746 8836 -1336 -799 -874 C ATOM 580 CG PRO A 71 9.983 15.938 28.504 1.00 64.32 C ANISOU 580 CG PRO A 71 9951 6537 7952 -1375 -698 -1027 C ATOM 581 CD PRO A 71 10.169 15.441 29.909 1.00 49.09 C ANISOU 581 CD PRO A 71 7877 4496 6279 -1292 -689 -929 C ATOM 582 N LEU A 72 8.608 18.538 31.469 1.00 61.46 N ANISOU 582 N LEU A 72 8912 6631 7809 -1199 -999 -481 N ATOM 583 CA LEU A 72 7.857 19.509 32.256 1.00 55.41 C ANISOU 583 CA LEU A 72 7943 6047 7062 -1170 -1116 -311 C ATOM 584 C LEU A 72 8.717 20.229 33.286 1.00 71.18 C ANISOU 584 C LEU A 72 9797 8045 9203 -981 -1033 -218 C ATOM 585 O LEU A 72 8.259 21.223 33.861 1.00 69.12 O ANISOU 585 O LEU A 72 9385 7934 8945 -933 -1101 -93 O ATOM 586 CB LEU A 72 6.680 18.824 32.954 1.00 48.62 C ANISOU 586 CB LEU A 72 7011 5205 6259 -1295 -1255 -241 C ATOM 587 CG LEU A 72 5.424 18.614 32.106 1.00 72.64 C ANISOU 587 CG LEU A 72 10110 8350 9142 -1496 -1407 -259 C ATOM 588 CD1 LEU A 72 4.430 17.720 32.825 1.00 59.05 C ANISOU 588 CD1 LEU A 72 8324 6602 7509 -1624 -1521 -199 C ATOM 589 CD2 LEU A 72 4.787 19.953 31.767 1.00 90.20 C ANISOU 589 CD2 LEU A 72 12224 10806 11241 -1483 -1497 -150 C ATOM 590 N ASN A 73 9.939 19.760 33.532 1.00 64.59 N ANISOU 590 N ASN A 73 9004 7049 8490 -876 -889 -275 N ATOM 591 CA ASN A 73 10.854 20.403 34.464 1.00 59.97 C ANISOU 591 CA ASN A 73 8287 6460 8037 -709 -816 -191 C ATOM 592 C ASN A 73 11.900 21.266 33.771 1.00 61.61 C ANISOU 592 C ASN A 73 8526 6686 8199 -604 -700 -227 C ATOM 593 O ASN A 73 12.733 21.869 34.455 1.00 58.72 O ANISOU 593 O ASN A 73 8054 6319 7937 -475 -641 -161 O ATOM 594 CB ASN A 73 11.549 19.351 35.334 1.00 59.61 C ANISOU 594 CB ASN A 73 8231 6235 8182 -654 -744 -194 C ATOM 595 CG ASN A 73 10.622 18.745 36.367 1.00 64.68 C ANISOU 595 CG ASN A 73 8790 6883 8902 -725 -857 -107 C ATOM 596 OD1 ASN A 73 9.407 18.934 36.316 1.00 90.99 O ANISOU 596 OD1 ASN A 73 12089 10338 12145 -833 -984 -64 O ATOM 597 ND2 ASN A 73 11.192 18.009 37.314 1.00 79.95 N ANISOU 597 ND2 ASN A 73 10681 8689 11007 -663 -810 -68 N ATOM 598 N TYR A 74 11.881 21.338 32.437 1.00 60.52 N ANISOU 598 N TYR A 74 8529 6566 7900 -665 -667 -325 N ATOM 599 CA TYR A 74 12.836 22.188 31.731 1.00 56.81 C ANISOU 599 CA TYR A 74 8085 6123 7376 -571 -551 -346 C ATOM 600 C TYR A 74 12.653 23.653 32.108 1.00 65.40 C ANISOU 600 C TYR A 74 9027 7375 8448 -508 -613 -217 C ATOM 601 O TYR A 74 13.634 24.380 32.300 1.00 69.43 O ANISOU 601 O TYR A 74 9475 7880 9026 -388 -523 -180 O ATOM 602 CB TYR A 74 12.693 22.015 30.218 1.00 49.66 C ANISOU 602 CB TYR A 74 7366 5232 6271 -664 -518 -467 C ATOM 603 CG TYR A 74 13.248 20.721 29.661 1.00 68.96 C ANISOU 603 CG TYR A 74 9987 7487 8726 -693 -396 -624 C ATOM 604 CD1 TYR A 74 13.776 19.744 30.496 1.00 69.17 C ANISOU 604 CD1 TYR A 74 9993 7338 8950 -637 -330 -639 C ATOM 605 CD2 TYR A 74 13.254 20.485 28.292 1.00 75.29 C ANISOU 605 CD2 TYR A 74 10984 8285 9339 -772 -341 -756 C ATOM 606 CE1 TYR A 74 14.283 18.564 29.982 1.00 65.92 C ANISOU 606 CE1 TYR A 74 9747 6735 8563 -652 -206 -783 C ATOM 607 CE2 TYR A 74 13.760 19.310 27.770 1.00 75.92 C ANISOU 607 CE2 TYR A 74 11241 8179 9424 -794 -214 -914 C ATOM 608 CZ TYR A 74 14.273 18.353 28.618 1.00 79.51 C ANISOU 608 CZ TYR A 74 11669 8446 10095 -729 -143 -927 C ATOM 609 OH TYR A 74 14.778 17.183 28.100 1.00 88.30 O ANISOU 609 OH TYR A 74 12963 9356 11229 -739 -5 -1085 O ATOM 610 N ILE A 75 11.400 24.103 32.219 1.00 67.08 N ANISOU 610 N ILE A 75 9180 7728 8579 -586 -763 -143 N ATOM 611 CA ILE A 75 11.138 25.503 32.527 1.00 67.60 C ANISOU 611 CA ILE A 75 9117 7938 8629 -524 -816 -23 C ATOM 612 C ILE A 75 11.476 25.832 33.975 1.00 75.10 C ANISOU 612 C ILE A 75 9916 8869 9748 -419 -814 64 C ATOM 613 O ILE A 75 11.722 27.000 34.299 1.00 71.50 O ANISOU 613 O ILE A 75 9371 8483 9314 -335 -809 139 O ATOM 614 CB ILE A 75 9.672 25.856 32.206 1.00 69.36 C ANISOU 614 CB ILE A 75 9312 8315 8725 -630 -970 40 C ATOM 615 CG1 ILE A 75 9.520 27.360 31.975 1.00 58.99 C ANISOU 615 CG1 ILE A 75 7921 7139 7353 -567 -993 139 C ATOM 616 CG2 ILE A 75 8.744 25.388 33.317 1.00 57.75 C ANISOU 616 CG2 ILE A 75 7736 6864 7344 -670 -1075 109 C ATOM 617 CD1 ILE A 75 10.244 27.860 30.743 1.00 64.40 C ANISOU 617 CD1 ILE A 75 8713 7834 7924 -551 -906 91 C ATOM 618 N LEU A 76 11.504 24.831 34.858 1.00 67.54 N ANISOU 618 N LEU A 76 8935 7816 8910 -427 -820 57 N ATOM 619 CA LEU A 76 11.909 25.080 36.238 1.00 62.97 C ANISOU 619 CA LEU A 76 8226 7222 8478 -333 -817 138 C ATOM 620 C LEU A 76 13.416 25.278 36.345 1.00 73.01 C ANISOU 620 C LEU A 76 9491 8402 9848 -220 -690 118 C ATOM 621 O LEU A 76 13.881 26.078 37.164 1.00 74.28 O ANISOU 621 O LEU A 76 9545 8595 10082 -136 -688 189 O ATOM 622 CB LEU A 76 11.449 23.934 37.140 1.00 64.49 C ANISOU 622 CB LEU A 76 8393 7349 8761 -381 -866 155 C ATOM 623 CG LEU A 76 9.939 23.813 37.352 1.00 61.18 C ANISOU 623 CG LEU A 76 7932 7035 8278 -485 -999 211 C ATOM 624 CD1 LEU A 76 9.620 22.677 38.310 1.00 66.05 C ANISOU 624 CD1 LEU A 76 8518 7577 9001 -527 -1032 240 C ATOM 625 CD2 LEU A 76 9.364 25.126 37.862 1.00 57.03 C ANISOU 625 CD2 LEU A 76 7283 6665 7720 -434 -1059 315 C ATOM 626 N LEU A 77 14.193 24.558 35.531 1.00 72.94 N ANISOU 626 N LEU A 77 9592 8278 9843 -218 -582 22 N ATOM 627 CA LEU A 77 15.630 24.803 35.483 1.00 70.17 C ANISOU 627 CA LEU A 77 9224 7852 9584 -110 -451 13 C ATOM 628 C LEU A 77 15.932 26.142 34.825 1.00 68.65 C ANISOU 628 C LEU A 77 9019 7757 9308 -72 -422 36 C ATOM 629 O LEU A 77 16.885 26.831 35.211 1.00 65.11 O ANISOU 629 O LEU A 77 8489 7302 8949 17 -368 84 O ATOM 630 CB LEU A 77 16.336 23.671 34.738 1.00 72.55 C ANISOU 630 CB LEU A 77 9651 8003 9913 -110 -324 -96 C ATOM 631 CG LEU A 77 16.275 22.277 35.363 1.00 68.15 C ANISOU 631 CG LEU A 77 9114 7309 9473 -130 -324 -118 C ATOM 632 CD1 LEU A 77 17.330 21.388 34.729 1.00 76.68 C ANISOU 632 CD1 LEU A 77 10293 8220 10621 -79 -158 -212 C ATOM 633 CD2 LEU A 77 16.455 22.348 36.872 1.00 78.24 C ANISOU 633 CD2 LEU A 77 10235 8592 10901 -70 -383 -1 C ATOM 634 N ASN A 78 15.131 26.526 33.829 1.00 65.28 N ANISOU 634 N ASN A 78 8669 7420 8713 -146 -465 11 N ATOM 635 CA ASN A 78 15.283 27.844 33.227 1.00 67.31 C ANISOU 635 CA ASN A 78 8909 7776 8889 -115 -450 54 C ATOM 636 C ASN A 78 15.028 28.944 34.246 1.00 66.54 C ANISOU 636 C ASN A 78 8670 7757 8854 -64 -529 164 C ATOM 637 O ASN A 78 15.642 30.015 34.172 1.00 63.00 O ANISOU 637 O ASN A 78 8175 7336 8424 -2 -488 209 O ATOM 638 CB ASN A 78 14.335 27.989 32.036 1.00 56.24 C ANISOU 638 CB ASN A 78 7610 6469 7290 -213 -504 25 C ATOM 639 CG ASN A 78 14.658 29.196 31.177 1.00 60.56 C ANISOU 639 CG ASN A 78 8168 7098 7745 -181 -461 64 C ATOM 640 OD1 ASN A 78 15.824 29.490 30.914 1.00 72.32 O ANISOU 640 OD1 ASN A 78 9661 8534 9283 -109 -335 52 O ATOM 641 ND2 ASN A 78 13.624 29.905 30.738 1.00 63.88 N ANISOU 641 ND2 ASN A 78 8583 7649 8040 -235 -565 123 N ATOM 642 N LEU A 79 14.132 28.697 35.204 1.00 63.20 N ANISOU 642 N LEU A 79 8182 7368 8463 -92 -636 207 N ATOM 643 CA LEU A 79 13.899 29.661 36.274 1.00 56.34 C ANISOU 643 CA LEU A 79 7190 6562 7653 -39 -697 298 C ATOM 644 C LEU A 79 15.115 29.778 37.184 1.00 53.28 C ANISOU 644 C LEU A 79 6733 6099 7412 46 -638 315 C ATOM 645 O LEU A 79 15.458 30.878 37.633 1.00 70.02 O ANISOU 645 O LEU A 79 8784 8252 9567 100 -642 366 O ATOM 646 CB LEU A 79 12.663 29.256 37.078 1.00 53.31 C ANISOU 646 CB LEU A 79 6757 6234 7265 -88 -809 339 C ATOM 647 CG LEU A 79 12.304 30.119 38.288 1.00 58.09 C ANISOU 647 CG LEU A 79 7246 6903 7921 -33 -863 423 C ATOM 648 CD1 LEU A 79 11.895 31.516 37.851 1.00 58.47 C ANISOU 648 CD1 LEU A 79 7272 7044 7902 -4 -882 473 C ATOM 649 CD2 LEU A 79 11.204 29.463 39.108 1.00 53.18 C ANISOU 649 CD2 LEU A 79 6577 6323 7306 -81 -948 461 C ATOM 650 N ALA A 80 15.781 28.655 37.464 1.00 58.80 N ANISOU 650 N ALA A 80 7447 6692 8202 53 -587 276 N ATOM 651 CA ALA A 80 16.960 28.689 38.323 1.00 50.93 C ANISOU 651 CA ALA A 80 6372 5630 7350 128 -542 308 C ATOM 652 C ALA A 80 18.124 29.391 37.636 1.00 60.69 C ANISOU 652 C ALA A 80 7609 6841 8610 182 -439 301 C ATOM 653 O ALA A 80 18.870 30.141 38.277 1.00 69.74 O ANISOU 653 O ALA A 80 8668 7991 9840 233 -437 353 O ATOM 654 CB ALA A 80 17.353 27.270 38.732 1.00 48.95 C ANISOU 654 CB ALA A 80 6132 5267 7199 129 -510 284 C ATOM 655 N VAL A 81 18.298 29.160 36.332 1.00 68.27 N ANISOU 655 N VAL A 81 8668 7778 9493 164 -354 238 N ATOM 656 CA VAL A 81 19.355 29.843 35.592 1.00 69.20 C ANISOU 656 CA VAL A 81 8788 7883 9623 212 -245 239 C ATOM 657 C VAL A 81 19.067 31.338 35.512 1.00 74.23 C ANISOU 657 C VAL A 81 9386 8617 10203 215 -294 300 C ATOM 658 O VAL A 81 19.984 32.165 35.586 1.00 69.43 O ANISOU 658 O VAL A 81 8716 8000 9664 261 -246 343 O ATOM 659 CB VAL A 81 19.516 29.215 34.195 1.00 64.61 C ANISOU 659 CB VAL A 81 8339 7263 8947 188 -136 152 C ATOM 660 CG1 VAL A 81 20.523 29.997 33.365 1.00 69.60 C ANISOU 660 CG1 VAL A 81 8972 7900 9574 235 -15 166 C ATOM 661 CG2 VAL A 81 19.942 27.761 34.317 1.00 63.29 C ANISOU 661 CG2 VAL A 81 8214 6970 8865 200 -66 89 C ATOM 662 N ALA A 82 17.792 31.707 35.371 1.00 71.02 N ANISOU 662 N ALA A 82 9006 8298 9680 165 -391 313 N ATOM 663 CA ALA A 82 17.430 33.121 35.336 1.00 63.24 C ANISOU 663 CA ALA A 82 7983 7393 8653 178 -436 379 C ATOM 664 C ALA A 82 17.757 33.805 36.657 1.00 62.51 C ANISOU 664 C ALA A 82 7782 7292 8677 224 -482 433 C ATOM 665 O ALA A 82 18.256 34.936 36.671 1.00 59.00 O ANISOU 665 O ALA A 82 7300 6852 8265 255 -463 475 O ATOM 666 CB ALA A 82 15.947 33.276 35.004 1.00 51.22 C ANISOU 666 CB ALA A 82 6495 5967 7000 123 -533 395 C ATOM 667 N ASP A 83 17.482 33.135 37.779 1.00 60.63 N ANISOU 667 N ASP A 83 7500 7039 8499 221 -542 432 N ATOM 668 CA ASP A 83 17.809 33.712 39.078 1.00 64.71 C ANISOU 668 CA ASP A 83 7928 7552 9107 255 -588 475 C ATOM 669 C ASP A 83 19.314 33.837 39.274 1.00 68.97 C ANISOU 669 C ASP A 83 8417 8021 9766 292 -522 485 C ATOM 670 O ASP A 83 19.771 34.732 39.993 1.00 76.59 O ANISOU 670 O ASP A 83 9321 8989 10790 311 -550 521 O ATOM 671 CB ASP A 83 17.198 32.874 40.200 1.00 64.47 C ANISOU 671 CB ASP A 83 7866 7529 9099 240 -662 479 C ATOM 672 CG ASP A 83 15.683 32.850 40.152 1.00 82.49 C ANISOU 672 CG ASP A 83 10170 9892 11279 203 -733 488 C ATOM 673 OD1 ASP A 83 15.092 33.754 39.526 1.00 87.94 O ANISOU 673 OD1 ASP A 83 10879 10641 11893 203 -744 506 O ATOM 674 OD2 ASP A 83 15.084 31.928 40.745 1.00 97.16 O ANISOU 674 OD2 ASP A 83 12019 11756 13140 174 -779 489 O ATOM 675 N LEU A 84 20.098 32.955 38.648 1.00 59.81 N ANISOU 675 N LEU A 84 7281 6797 8648 301 -432 455 N ATOM 676 CA LEU A 84 21.549 33.074 38.733 1.00 54.69 C ANISOU 676 CA LEU A 84 6567 6088 8123 340 -359 480 C ATOM 677 C LEU A 84 22.059 34.270 37.939 1.00 67.00 C ANISOU 677 C LEU A 84 8127 7664 9667 349 -302 503 C ATOM 678 O LEU A 84 23.067 34.878 38.318 1.00 69.20 O ANISOU 678 O LEU A 84 8325 7919 10049 367 -286 548 O ATOM 679 CB LEU A 84 22.214 31.785 38.253 1.00 51.50 C ANISOU 679 CB LEU A 84 6186 5604 7776 362 -259 444 C ATOM 680 CG LEU A 84 22.020 30.563 39.155 1.00 59.55 C ANISOU 680 CG LEU A 84 7186 6580 8860 362 -305 442 C ATOM 681 CD1 LEU A 84 22.740 29.350 38.586 1.00 54.48 C ANISOU 681 CD1 LEU A 84 6574 5835 8289 395 -186 405 C ATOM 682 CD2 LEU A 84 22.497 30.859 40.570 1.00 50.58 C ANISOU 682 CD2 LEU A 84 5933 5454 7830 377 -387 513 C ATOM 683 N PHE A 85 21.386 34.621 36.840 1.00 71.55 N ANISOU 683 N PHE A 85 8788 8283 10114 328 -277 483 N ATOM 684 CA PHE A 85 21.739 35.845 36.129 1.00 67.61 C ANISOU 684 CA PHE A 85 8290 7805 9593 333 -233 523 C ATOM 685 C PHE A 85 21.430 37.079 36.967 1.00 78.40 C ANISOU 685 C PHE A 85 9605 9197 10988 332 -324 572 C ATOM 686 O PHE A 85 22.128 38.093 36.857 1.00 86.70 O ANISOU 686 O PHE A 85 10618 10230 12093 339 -296 616 O ATOM 687 CB PHE A 85 21.003 35.921 34.788 1.00 70.38 C ANISOU 687 CB PHE A 85 8747 8208 9786 308 -199 503 C ATOM 688 CG PHE A 85 21.584 35.036 33.717 1.00 93.24 C ANISOU 688 CG PHE A 85 11712 11071 12644 309 -73 452 C ATOM 689 CD1 PHE A 85 22.541 34.080 34.020 1.00105.22 C ANISOU 689 CD1 PHE A 85 13195 12508 14275 343 3 423 C ATOM 690 CD2 PHE A 85 21.179 35.173 32.399 1.00 93.92 C ANISOU 690 CD2 PHE A 85 11901 11208 12578 281 -25 435 C ATOM 691 CE1 PHE A 85 23.072 33.272 33.033 1.00108.87 C ANISOU 691 CE1 PHE A 85 13730 12929 14707 355 138 368 C ATOM 692 CE2 PHE A 85 21.708 34.370 31.407 1.00 91.10 C ANISOU 692 CE2 PHE A 85 11626 10819 12168 282 102 374 C ATOM 693 CZ PHE A 85 22.656 33.418 31.725 1.00104.32 C ANISOU 693 CZ PHE A 85 13271 12402 13964 324 192 335 C ATOM 694 N MET A 86 20.394 37.011 37.806 1.00 73.09 N ANISOU 694 N MET A 86 8931 8560 10279 322 -427 563 N ATOM 695 CA MET A 86 20.085 38.123 38.697 1.00 67.17 C ANISOU 695 CA MET A 86 8144 7824 9555 329 -501 595 C ATOM 696 C MET A 86 21.108 38.240 39.819 1.00 78.38 C ANISOU 696 C MET A 86 9485 9196 11100 332 -524 605 C ATOM 697 O MET A 86 21.297 39.330 40.372 1.00 98.25 O ANISOU 697 O MET A 86 11976 11700 13655 329 -560 626 O ATOM 698 CB MET A 86 18.680 37.952 39.277 1.00 52.86 C ANISOU 698 CB MET A 86 6349 6069 7665 324 -587 585 C ATOM 699 CG MET A 86 17.563 37.970 38.243 1.00 70.95 C ANISOU 699 CG MET A 86 8702 8423 9833 311 -590 592 C ATOM 700 SD MET A 86 15.966 37.495 38.938 1.00 76.95 S ANISOU 700 SD MET A 86 9457 9256 10524 300 -686 593 S ATOM 701 CE MET A 86 15.811 38.671 40.280 1.00 85.26 C ANISOU 701 CE MET A 86 10457 10303 11634 342 -732 618 C ATOM 702 N VAL A 87 21.776 37.140 40.162 1.00 58.87 N ANISOU 702 N VAL A 87 6976 6696 8696 334 -507 594 N ATOM 703 CA VAL A 87 22.723 37.159 41.270 1.00 69.44 C ANISOU 703 CA VAL A 87 8229 8004 10150 331 -547 619 C ATOM 704 C VAL A 87 24.078 37.687 40.817 1.00 74.51 C ANISOU 704 C VAL A 87 8814 8602 10894 332 -479 658 C ATOM 705 O VAL A 87 24.617 38.634 41.401 1.00 69.77 O ANISOU 705 O VAL A 87 8166 7989 10355 309 -523 686 O ATOM 706 CB VAL A 87 22.845 35.756 41.895 1.00 65.89 C ANISOU 706 CB VAL A 87 7750 7543 9743 339 -565 614 C ATOM 707 CG1 VAL A 87 24.043 35.694 42.836 1.00 76.30 C ANISOU 707 CG1 VAL A 87 8965 8833 11191 336 -596 661 C ATOM 708 CG2 VAL A 87 21.569 35.393 42.638 1.00 54.48 C ANISOU 708 CG2 VAL A 87 6340 6147 8214 327 -649 594 C ATOM 709 N PHE A 88 24.651 37.085 39.776 1.00 65.16 N ANISOU 709 N PHE A 88 7636 7392 9730 353 -368 659 N ATOM 710 CA PHE A 88 25.986 37.461 39.330 1.00 65.68 C ANISOU 710 CA PHE A 88 7631 7421 9904 359 -286 707 C ATOM 711 C PHE A 88 25.980 38.618 38.342 1.00 74.98 C ANISOU 711 C PHE A 88 8847 8606 11035 347 -230 728 C ATOM 712 O PHE A 88 26.970 39.354 38.259 1.00 88.42 O ANISOU 712 O PHE A 88 10481 10283 12833 333 -198 782 O ATOM 713 CB PHE A 88 26.690 36.253 38.708 1.00 51.73 C ANISOU 713 CB PHE A 88 5847 5618 8192 401 -169 703 C ATOM 714 CG PHE A 88 26.902 35.121 39.670 1.00 68.98 C ANISOU 714 CG PHE A 88 7975 7777 10455 418 -214 707 C ATOM 715 CD1 PHE A 88 27.987 35.121 40.530 1.00 70.71 C ANISOU 715 CD1 PHE A 88 8065 7979 10824 420 -248 775 C ATOM 716 CD2 PHE A 88 26.011 34.061 39.723 1.00 70.47 C ANISOU 716 CD2 PHE A 88 8237 7964 10574 427 -229 653 C ATOM 717 CE1 PHE A 88 28.185 34.084 41.421 1.00 69.93 C ANISOU 717 CE1 PHE A 88 7909 7861 10798 438 -294 797 C ATOM 718 CE2 PHE A 88 26.203 33.021 40.611 1.00 79.53 C ANISOU 718 CE2 PHE A 88 9333 9082 11802 444 -268 670 C ATOM 719 CZ PHE A 88 27.292 33.033 41.461 1.00 79.62 C ANISOU 719 CZ PHE A 88 9215 9078 11958 454 -300 746 C ATOM 720 N GLY A 89 24.897 38.798 37.596 1.00 71.68 N ANISOU 720 N GLY A 89 8530 8225 10478 348 -223 698 N ATOM 721 CA GLY A 89 24.787 39.907 36.677 1.00 72.37 C ANISOU 721 CA GLY A 89 8658 8325 10515 338 -181 733 C ATOM 722 C GLY A 89 24.226 41.179 37.267 1.00 83.73 C ANISOU 722 C GLY A 89 10101 9763 11948 319 -272 754 C ATOM 723 O GLY A 89 24.119 42.184 36.558 1.00 96.76 O ANISOU 723 O GLY A 89 11781 11412 13570 314 -242 796 O ATOM 724 N GLY A 90 23.867 41.173 38.549 1.00 81.55 N ANISOU 724 N GLY A 90 9801 9485 11698 311 -377 729 N ATOM 725 CA GLY A 90 23.287 42.346 39.171 1.00 72.47 C ANISOU 725 CA GLY A 90 8670 8325 10540 301 -452 733 C ATOM 726 C GLY A 90 23.542 42.457 40.660 1.00 68.13 C ANISOU 726 C GLY A 90 8075 7755 10057 279 -545 710 C ATOM 727 O GLY A 90 23.989 43.504 41.138 1.00 84.22 O ANISOU 727 O GLY A 90 10096 9746 12158 248 -578 723 O ATOM 728 N PHE A 91 23.262 41.386 41.407 1.00 52.03 N ANISOU 728 N PHE A 91 6021 5747 7999 286 -592 677 N ATOM 729 CA PHE A 91 23.396 41.446 42.861 1.00 59.34 C ANISOU 729 CA PHE A 91 6915 6672 8959 261 -687 659 C ATOM 730 C PHE A 91 24.852 41.607 43.282 1.00 64.17 C ANISOU 730 C PHE A 91 7440 7245 9699 220 -701 693 C ATOM 731 O PHE A 91 25.161 42.414 44.166 1.00 72.16 O ANISOU 731 O PHE A 91 8439 8233 10743 176 -773 686 O ATOM 732 CB PHE A 91 22.788 40.198 43.504 1.00 68.10 C ANISOU 732 CB PHE A 91 8024 7829 10021 277 -728 634 C ATOM 733 CG PHE A 91 21.296 40.086 43.338 1.00 63.88 C ANISOU 733 CG PHE A 91 7559 7344 9370 305 -737 608 C ATOM 734 CD1 PHE A 91 20.541 41.179 42.945 1.00 68.45 C ANISOU 734 CD1 PHE A 91 8189 7923 9895 320 -729 608 C ATOM 735 CD2 PHE A 91 20.649 38.886 43.583 1.00 62.31 C ANISOU 735 CD2 PHE A 91 7366 7187 9124 314 -756 595 C ATOM 736 CE1 PHE A 91 19.169 41.074 42.793 1.00 60.53 C ANISOU 736 CE1 PHE A 91 7230 6974 8796 348 -741 601 C ATOM 737 CE2 PHE A 91 19.278 38.775 43.433 1.00 53.62 C ANISOU 737 CE2 PHE A 91 6312 6137 7924 330 -770 583 C ATOM 738 CZ PHE A 91 18.538 39.870 43.038 1.00 41.26 C ANISOU 738 CZ PHE A 91 4785 4585 6308 348 -764 588 C ATOM 739 N THR A 92 25.761 40.846 42.666 1.00 53.71 N ANISOU 739 N THR A 92 6052 5910 8446 230 -632 731 N ATOM 740 CA THR A 92 27.176 40.971 43.005 1.00 58.51 C ANISOU 740 CA THR A 92 6552 6488 9191 193 -641 784 C ATOM 741 C THR A 92 27.726 42.327 42.584 1.00 68.74 C ANISOU 741 C THR A 92 7840 7740 10540 151 -621 814 C ATOM 742 O THR A 92 28.546 42.919 43.296 1.00 72.13 O ANISOU 742 O THR A 92 8205 8144 11056 89 -688 839 O ATOM 743 CB THR A 92 27.981 39.846 42.353 1.00 61.12 C ANISOU 743 CB THR A 92 6813 6813 9595 231 -547 824 C ATOM 744 OG1 THR A 92 27.785 39.875 40.934 1.00 74.86 O ANISOU 744 OG1 THR A 92 8608 8546 11288 266 -422 819 O ATOM 745 CG2 THR A 92 27.549 38.492 42.896 1.00 47.08 C ANISOU 745 CG2 THR A 92 5037 5059 7791 265 -575 802 C ATOM 746 N THR A 93 27.288 42.835 41.430 1.00 73.43 N ANISOU 746 N THR A 93 8497 8323 11080 176 -536 817 N ATOM 747 CA THR A 93 27.749 44.142 40.974 1.00 58.52 C ANISOU 747 CA THR A 93 6606 6383 9244 137 -511 857 C ATOM 748 C THR A 93 27.234 45.254 41.880 1.00 64.01 C ANISOU 748 C THR A 93 7356 7043 9922 97 -610 819 C ATOM 749 O THR A 93 27.971 46.197 42.195 1.00 64.31 O ANISOU 749 O THR A 93 7362 7024 10049 32 -644 842 O ATOM 750 CB THR A 93 27.307 44.380 39.530 1.00 61.41 C ANISOU 750 CB THR A 93 7035 6757 9541 176 -399 880 C ATOM 751 OG1 THR A 93 27.709 43.271 38.716 1.00 74.66 O ANISOU 751 OG1 THR A 93 8687 8467 11215 215 -299 894 O ATOM 752 CG2 THR A 93 27.934 45.653 38.984 1.00 59.98 C ANISOU 752 CG2 THR A 93 6839 6520 9432 135 -359 944 C ATOM 753 N THR A 94 25.974 45.159 42.312 1.00 54.45 N ANISOU 753 N THR A 94 6229 5860 8600 133 -654 759 N ATOM 754 CA THR A 94 25.411 46.186 43.183 1.00 61.37 C ANISOU 754 CA THR A 94 7169 6696 9452 111 -728 712 C ATOM 755 C THR A 94 26.074 46.171 44.555 1.00 56.30 C ANISOU 755 C THR A 94 6487 6047 8859 44 -834 682 C ATOM 756 O THR A 94 26.283 47.228 45.161 1.00 77.82 O ANISOU 756 O THR A 94 9242 8709 11615 -12 -887 656 O ATOM 757 CB THR A 94 23.899 45.994 43.310 1.00 50.80 C ANISOU 757 CB THR A 94 5913 5401 7988 175 -736 666 C ATOM 758 OG1 THR A 94 23.304 46.036 42.007 1.00 59.80 O ANISOU 758 OG1 THR A 94 7086 6558 9077 224 -654 704 O ATOM 759 CG2 THR A 94 23.288 47.090 44.170 1.00 38.06 C ANISOU 759 CG2 THR A 94 4371 3739 6353 169 -788 615 C ATOM 760 N LEU A 95 26.414 44.982 45.061 1.00 58.26 N ANISOU 760 N LEU A 95 6669 6354 9111 45 -867 688 N ATOM 761 CA LEU A 95 27.160 44.899 46.313 1.00 67.06 C ANISOU 761 CA LEU A 95 7731 7477 10271 -25 -976 682 C ATOM 762 C LEU A 95 28.501 45.611 46.200 1.00 69.87 C ANISOU 762 C LEU A 95 8007 7779 10760 -108 -991 735 C ATOM 763 O LEU A 95 28.940 46.283 47.140 1.00 70.74 O ANISOU 763 O LEU A 95 8118 7863 10896 -193 -1091 712 O ATOM 764 CB LEU A 95 27.363 43.435 46.708 1.00 57.88 C ANISOU 764 CB LEU A 95 6497 6384 9109 0 -997 709 C ATOM 765 CG LEU A 95 28.372 43.149 47.824 1.00 54.27 C ANISOU 765 CG LEU A 95 5949 5951 8719 -72 -1106 741 C ATOM 766 CD1 LEU A 95 27.937 43.794 49.130 1.00 58.92 C ANISOU 766 CD1 LEU A 95 6613 6550 9223 -129 -1222 672 C ATOM 767 CD2 LEU A 95 28.573 41.650 48.004 1.00 47.26 C ANISOU 767 CD2 LEU A 95 4985 5120 7854 -28 -1104 790 C ATOM 768 N TYR A 96 29.160 45.486 45.047 1.00 56.76 N ANISOU 768 N TYR A 96 6280 6105 9183 -89 -892 807 N ATOM 769 CA TYR A 96 30.465 46.111 44.865 1.00 63.39 C ANISOU 769 CA TYR A 96 7023 6900 10163 -168 -895 876 C ATOM 770 C TYR A 96 30.336 47.624 44.727 1.00 65.72 C ANISOU 770 C TYR A 96 7392 7107 10470 -223 -904 855 C ATOM 771 O TYR A 96 31.052 48.380 45.393 1.00 66.89 O ANISOU 771 O TYR A 96 7513 7209 10693 -327 -990 858 O ATOM 772 CB TYR A 96 31.160 45.508 43.643 1.00 49.38 C ANISOU 772 CB TYR A 96 5158 5139 8465 -121 -764 961 C ATOM 773 CG TYR A 96 32.588 45.961 43.451 1.00 59.64 C ANISOU 773 CG TYR A 96 6325 6410 9927 -195 -755 1055 C ATOM 774 CD1 TYR A 96 33.608 45.463 44.252 1.00 52.87 C ANISOU 774 CD1 TYR A 96 5331 5583 9172 -246 -835 1108 C ATOM 775 CD2 TYR A 96 32.920 46.876 42.460 1.00 57.84 C ANISOU 775 CD2 TYR A 96 6097 6129 9751 -215 -667 1105 C ATOM 776 CE1 TYR A 96 34.917 45.870 44.076 1.00 57.36 C ANISOU 776 CE1 TYR A 96 5759 6134 9901 -318 -831 1208 C ATOM 777 CE2 TYR A 96 34.227 47.288 42.276 1.00 57.72 C ANISOU 777 CE2 TYR A 96 5948 6091 9892 -288 -654 1202 C ATOM 778 CZ TYR A 96 35.221 46.783 43.088 1.00 64.49 C ANISOU 778 CZ TYR A 96 6663 6983 10857 -341 -737 1253 C ATOM 779 OH TYR A 96 36.523 47.191 42.909 1.00 72.83 O ANISOU 779 OH TYR A 96 7569 8025 12080 -419 -729 1363 O ATOM 780 N THR A 97 29.418 48.084 43.872 1.00 56.85 N ANISOU 780 N THR A 97 6365 5956 9278 -160 -820 839 N ATOM 781 CA THR A 97 29.282 49.518 43.633 1.00 55.44 C ANISOU 781 CA THR A 97 6257 5679 9127 -200 -812 835 C ATOM 782 C THR A 97 28.753 50.256 44.857 1.00 52.60 C ANISOU 782 C THR A 97 5994 5269 8723 -243 -918 738 C ATOM 783 O THR A 97 29.147 51.402 45.102 1.00 65.29 O ANISOU 783 O THR A 97 7632 6778 10398 -324 -954 728 O ATOM 784 CB THR A 97 28.369 49.772 42.435 1.00 50.19 C ANISOU 784 CB THR A 97 5667 5008 8395 -113 -702 856 C ATOM 785 OG1 THR A 97 27.078 49.200 42.684 1.00 58.60 O ANISOU 785 OG1 THR A 97 6809 6130 9326 -32 -712 791 O ATOM 786 CG2 THR A 97 28.961 49.157 41.178 1.00 46.78 C ANISOU 786 CG2 THR A 97 5159 4622 7995 -82 -588 944 C ATOM 787 N SER A 98 27.860 49.629 45.631 1.00 43.15 N ANISOU 787 N SER A 98 4852 4133 7411 -194 -962 664 N ATOM 788 CA SER A 98 27.325 50.285 46.821 1.00 52.58 C ANISOU 788 CA SER A 98 6148 5287 8545 -227 -1046 565 C ATOM 789 C SER A 98 28.412 50.551 47.855 1.00 50.02 C ANISOU 789 C SER A 98 5782 4941 8282 -358 -1166 547 C ATOM 790 O SER A 98 28.344 51.546 48.586 1.00 71.97 O ANISOU 790 O SER A 98 8652 7639 11053 -424 -1225 472 O ATOM 791 CB SER A 98 26.206 49.440 47.431 1.00 57.74 C ANISOU 791 CB SER A 98 6851 6027 9062 -148 -1060 506 C ATOM 792 OG SER A 98 26.662 48.132 47.731 1.00 67.44 O ANISOU 792 OG SER A 98 7984 7354 10285 -151 -1096 539 O ATOM 793 N LEU A 99 29.422 49.681 47.930 1.00 60.60 N ANISOU 793 N LEU A 99 6986 6351 9687 -399 -1203 617 N ATOM 794 CA LEU A 99 30.526 49.904 48.856 1.00 57.55 C ANISOU 794 CA LEU A 99 6537 5961 9369 -533 -1331 623 C ATOM 795 C LEU A 99 31.425 51.051 48.416 1.00 60.38 C ANISOU 795 C LEU A 99 6867 6214 9861 -635 -1332 664 C ATOM 796 O LEU A 99 32.164 51.596 49.243 1.00 48.13 O ANISOU 796 O LEU A 99 5303 4631 8355 -769 -1451 645 O ATOM 797 CB LEU A 99 31.342 48.622 49.018 1.00 70.59 C ANISOU 797 CB LEU A 99 8033 7719 11070 -535 -1365 709 C ATOM 798 CG LEU A 99 30.600 47.482 49.718 1.00 62.27 C ANISOU 798 CG LEU A 99 7002 6763 9894 -464 -1396 674 C ATOM 799 CD1 LEU A 99 31.464 46.239 49.802 1.00 63.01 C ANISOU 799 CD1 LEU A 99 6937 6941 10063 -459 -1420 774 C ATOM 800 CD2 LEU A 99 30.153 47.917 51.102 1.00 56.65 C ANISOU 800 CD2 LEU A 99 6400 6058 9068 -528 -1516 572 C ATOM 801 N HIS A 100 31.382 51.426 47.137 1.00 74.53 N ANISOU 801 N HIS A 100 8649 7955 11714 -584 -1207 725 N ATOM 802 CA HIS A 100 32.071 52.621 46.666 1.00 71.41 C ANISOU 802 CA HIS A 100 8245 7447 11443 -675 -1194 768 C ATOM 803 C HIS A 100 31.227 53.877 46.823 1.00 74.61 C ANISOU 803 C HIS A 100 8820 7723 11805 -678 -1187 678 C ATOM 804 O HIS A 100 31.781 54.974 46.958 1.00 90.97 O ANISOU 804 O HIS A 100 10918 9679 13968 -790 -1227 674 O ATOM 805 CB HIS A 100 32.464 52.468 45.194 1.00 59.91 C ANISOU 805 CB HIS A 100 6697 5997 10069 -620 -1053 890 C ATOM 806 CG HIS A 100 33.499 51.416 44.945 1.00 69.74 C ANISOU 806 CG HIS A 100 7765 7338 11395 -623 -1037 990 C ATOM 807 ND1 HIS A 100 34.845 51.701 44.862 1.00 86.88 N ANISOU 807 ND1 HIS A 100 9793 9492 13723 -731 -1063 1087 N ATOM 808 CD2 HIS A 100 33.385 50.082 44.746 1.00 77.72 C ANISOU 808 CD2 HIS A 100 8714 8454 12361 -527 -991 1013 C ATOM 809 CE1 HIS A 100 35.516 50.587 44.630 1.00 87.45 C ANISOU 809 CE1 HIS A 100 9719 9661 13848 -690 -1026 1169 C ATOM 810 NE2 HIS A 100 34.654 49.590 44.556 1.00 95.71 N ANISOU 810 NE2 HIS A 100 10818 10774 14774 -567 -981 1121 N ATOM 811 N GLY A 101 29.903 53.740 46.809 1.00 67.24 N ANISOU 811 N GLY A 101 8001 6803 10745 -558 -1135 610 N ATOM 812 CA GLY A 101 29.004 54.870 46.873 1.00 71.96 C ANISOU 812 CA GLY A 101 8752 7279 11310 -530 -1105 537 C ATOM 813 C GLY A 101 28.433 55.307 45.542 1.00 62.04 C ANISOU 813 C GLY A 101 7519 5977 10078 -435 -974 611 C ATOM 814 O GLY A 101 27.601 56.222 45.517 1.00 55.76 O ANISOU 814 O GLY A 101 6844 5078 9264 -390 -937 568 O ATOM 815 N TYR A 102 28.848 54.684 44.442 1.00 62.01 N ANISOU 815 N TYR A 102 7407 6045 10110 -399 -898 724 N ATOM 816 CA TYR A 102 28.380 55.057 43.114 1.00 54.86 C ANISOU 816 CA TYR A 102 6519 5114 9210 -320 -778 809 C ATOM 817 C TYR A 102 28.730 53.939 42.144 1.00 59.66 C ANISOU 817 C TYR A 102 7018 5847 9802 -271 -704 898 C ATOM 818 O TYR A 102 29.458 53.001 42.480 1.00 75.02 O ANISOU 818 O TYR A 102 8865 7873 11765 -302 -739 903 O ATOM 819 CB TYR A 102 28.988 56.388 42.658 1.00 49.48 C ANISOU 819 CB TYR A 102 5852 4286 8661 -400 -754 869 C ATOM 820 CG TYR A 102 30.486 56.345 42.439 1.00 68.04 C ANISOU 820 CG TYR A 102 8068 6639 11144 -518 -769 954 C ATOM 821 CD1 TYR A 102 31.367 56.354 43.514 1.00 62.80 C ANISOU 821 CD1 TYR A 102 7357 5961 10542 -644 -890 907 C ATOM 822 CD2 TYR A 102 31.018 56.308 41.157 1.00 72.24 C ANISOU 822 CD2 TYR A 102 8517 7196 11737 -504 -662 1089 C ATOM 823 CE1 TYR A 102 32.735 56.319 43.317 1.00 61.98 C ANISOU 823 CE1 TYR A 102 7110 5868 10573 -753 -907 1001 C ATOM 824 CE2 TYR A 102 32.385 56.274 40.951 1.00 55.87 C ANISOU 824 CE2 TYR A 102 6306 5129 9794 -605 -662 1178 C ATOM 825 CZ TYR A 102 33.238 56.280 42.034 1.00 59.06 C ANISOU 825 CZ TYR A 102 6648 5518 10273 -729 -787 1138 C ATOM 826 OH TYR A 102 34.599 56.246 41.834 1.00 52.23 O ANISOU 826 OH TYR A 102 5626 4667 9551 -830 -791 1242 O ATOM 827 N PHE A 103 28.202 54.052 40.927 1.00 60.08 N ANISOU 827 N PHE A 103 7094 5913 9820 -192 -600 969 N ATOM 828 CA PHE A 103 28.450 53.060 39.886 1.00 62.51 C ANISOU 828 CA PHE A 103 7327 6330 10092 -143 -512 1043 C ATOM 829 C PHE A 103 29.826 53.320 39.282 1.00 57.73 C ANISOU 829 C PHE A 103 6615 5700 9619 -221 -462 1145 C ATOM 830 O PHE A 103 30.007 54.271 38.515 1.00 77.71 O ANISOU 830 O PHE A 103 9161 8159 12207 -243 -401 1227 O ATOM 831 CB PHE A 103 27.356 53.114 38.824 1.00 49.05 C ANISOU 831 CB PHE A 103 5694 4659 8283 -44 -430 1082 C ATOM 832 CG PHE A 103 27.292 51.889 37.962 1.00 63.71 C ANISOU 832 CG PHE A 103 7513 6643 10052 14 -358 1111 C ATOM 833 CD1 PHE A 103 26.567 50.780 38.366 1.00 62.82 C ANISOU 833 CD1 PHE A 103 7417 6619 9834 70 -391 1037 C ATOM 834 CD2 PHE A 103 27.963 51.841 36.752 1.00 76.73 C ANISOU 834 CD2 PHE A 103 9115 8317 11723 9 -252 1209 C ATOM 835 CE1 PHE A 103 26.509 49.648 37.577 1.00 70.80 C ANISOU 835 CE1 PHE A 103 8406 7728 10765 115 -325 1051 C ATOM 836 CE2 PHE A 103 27.910 50.711 35.960 1.00 79.32 C ANISOU 836 CE2 PHE A 103 9426 8751 11959 61 -177 1219 C ATOM 837 CZ PHE A 103 27.181 49.613 36.373 1.00 72.60 C ANISOU 837 CZ PHE A 103 8602 7975 11008 112 -216 1135 C ATOM 838 N VAL A 104 30.799 52.468 39.624 1.00 59.79 N ANISOU 838 N VAL A 104 6760 6021 9935 -260 -482 1155 N ATOM 839 CA VAL A 104 32.194 52.715 39.272 1.00 65.59 C ANISOU 839 CA VAL A 104 7368 6734 10818 -343 -447 1255 C ATOM 840 C VAL A 104 32.583 52.148 37.915 1.00 70.26 C ANISOU 840 C VAL A 104 7898 7396 11401 -286 -294 1353 C ATOM 841 O VAL A 104 33.732 52.327 37.489 1.00 78.74 O ANISOU 841 O VAL A 104 8857 8462 12598 -342 -238 1452 O ATOM 842 CB VAL A 104 33.139 52.135 40.344 1.00 57.27 C ANISOU 842 CB VAL A 104 6201 5712 9849 -417 -547 1236 C ATOM 843 CG1 VAL A 104 32.930 52.841 41.669 1.00 59.23 C ANISOU 843 CG1 VAL A 104 6515 5886 10103 -501 -699 1143 C ATOM 844 CG2 VAL A 104 32.913 50.638 40.492 1.00 55.79 C ANISOU 844 CG2 VAL A 104 5977 5638 9580 -331 -535 1201 C ATOM 845 N PHE A 105 31.672 51.471 37.220 1.00 72.43 N ANISOU 845 N PHE A 105 8245 7743 11532 -181 -223 1329 N ATOM 846 CA PHE A 105 31.995 50.838 35.949 1.00 66.27 C ANISOU 846 CA PHE A 105 7428 7035 10715 -126 -75 1401 C ATOM 847 C PHE A 105 31.624 51.691 34.743 1.00 74.08 C ANISOU 847 C PHE A 105 8488 8005 11656 -110 19 1482 C ATOM 848 O PHE A 105 31.846 51.261 33.607 1.00 73.39 O ANISOU 848 O PHE A 105 8389 7982 11515 -69 150 1542 O ATOM 849 CB PHE A 105 31.313 49.470 35.855 1.00 64.68 C ANISOU 849 CB PHE A 105 7265 6929 10380 -35 -54 1326 C ATOM 850 CG PHE A 105 31.706 48.525 36.956 1.00 70.19 C ANISOU 850 CG PHE A 105 7889 7652 11128 -42 -133 1267 C ATOM 851 CD1 PHE A 105 33.007 48.059 37.053 1.00 63.80 C ANISOU 851 CD1 PHE A 105 6935 6856 10452 -71 -98 1326 C ATOM 852 CD2 PHE A 105 30.777 48.104 37.893 1.00 56.62 C ANISOU 852 CD2 PHE A 105 6236 5951 9328 -18 -241 1167 C ATOM 853 CE1 PHE A 105 33.375 47.191 38.065 1.00 58.31 C ANISOU 853 CE1 PHE A 105 6162 6186 9806 -75 -177 1291 C ATOM 854 CE2 PHE A 105 31.138 47.236 38.906 1.00 67.91 C ANISOU 854 CE2 PHE A 105 7597 7407 10797 -27 -316 1127 C ATOM 855 CZ PHE A 105 32.439 46.779 38.992 1.00 60.90 C ANISOU 855 CZ PHE A 105 6567 6531 10043 -55 -289 1192 C ATOM 856 N GLY A 106 31.072 52.882 34.958 1.00 78.95 N ANISOU 856 N GLY A 106 9180 8531 12288 -138 -39 1487 N ATOM 857 CA GLY A 106 30.804 53.804 33.880 1.00 76.70 C ANISOU 857 CA GLY A 106 8950 8213 11981 -130 40 1587 C ATOM 858 C GLY A 106 29.615 53.407 33.029 1.00 86.91 C ANISOU 858 C GLY A 106 10344 9589 13091 -35 87 1582 C ATOM 859 O GLY A 106 28.888 52.456 33.332 1.00 92.44 O ANISOU 859 O GLY A 106 11080 10362 13681 23 49 1489 O ATOM 860 N PRO A 107 29.396 54.144 31.936 1.00 79.53 N ANISOU 860 N PRO A 107 9453 8647 12119 -24 163 1692 N ATOM 861 CA PRO A 107 28.243 53.846 31.070 1.00 70.47 C ANISOU 861 CA PRO A 107 8400 7589 10789 55 193 1704 C ATOM 862 C PRO A 107 28.313 52.480 30.410 1.00 71.60 C ANISOU 862 C PRO A 107 8539 7867 10800 95 269 1669 C ATOM 863 O PRO A 107 27.265 51.862 30.182 1.00 96.89 O ANISOU 863 O PRO A 107 11815 11149 13850 150 243 1617 O ATOM 864 CB PRO A 107 28.286 54.975 30.029 1.00 69.31 C ANISOU 864 CB PRO A 107 8279 7403 10652 41 265 1856 C ATOM 865 CG PRO A 107 29.090 56.063 30.671 1.00 66.70 C ANISOU 865 CG PRO A 107 7897 6923 10522 -40 234 1895 C ATOM 866 CD PRO A 107 30.108 55.361 31.513 1.00 49.05 C ANISOU 866 CD PRO A 107 5562 4692 8385 -90 210 1817 C ATOM 867 N THR A 108 29.513 51.990 30.090 1.00 82.42 N ANISOU 867 N THR A 108 9825 9262 12230 69 365 1697 N ATOM 868 CA THR A 108 29.633 50.669 29.479 1.00 86.03 C ANISOU 868 CA THR A 108 10288 9829 12571 113 454 1652 C ATOM 869 C THR A 108 29.173 49.580 30.441 1.00 80.56 C ANISOU 869 C THR A 108 9599 9158 11851 144 365 1513 C ATOM 870 O THR A 108 28.364 48.718 30.081 1.00 78.57 O ANISOU 870 O THR A 108 9424 8984 11446 190 368 1449 O ATOM 871 CB THR A 108 31.074 50.422 29.032 1.00 81.38 C ANISOU 871 CB THR A 108 9593 9248 12080 89 589 1716 C ATOM 872 OG1 THR A 108 31.959 50.596 30.145 1.00103.83 O ANISOU 872 OG1 THR A 108 12316 12014 15120 37 524 1707 O ATOM 873 CG2 THR A 108 31.461 51.389 27.923 1.00 91.16 C ANISOU 873 CG2 THR A 108 10836 10484 13317 61 697 1864 C ATOM 874 N GLY A 109 29.681 49.606 31.675 1.00 72.41 N ANISOU 874 N GLY A 109 8488 8061 10963 111 280 1469 N ATOM 875 CA GLY A 109 29.210 48.677 32.686 1.00 58.92 C ANISOU 875 CA GLY A 109 6784 6371 9233 135 185 1352 C ATOM 876 C GLY A 109 27.760 48.881 33.066 1.00 73.96 C ANISOU 876 C GLY A 109 8789 8283 11031 165 81 1294 C ATOM 877 O GLY A 109 27.115 47.945 33.550 1.00 84.44 O ANISOU 877 O GLY A 109 10143 9655 12286 198 29 1206 O ATOM 878 N CYS A 110 27.230 50.089 32.858 1.00 70.64 N ANISOU 878 N CYS A 110 8418 7815 10608 157 57 1351 N ATOM 879 CA CYS A 110 25.819 50.341 33.129 1.00 68.68 C ANISOU 879 CA CYS A 110 8254 7576 10266 198 -26 1314 C ATOM 880 C CYS A 110 24.931 49.609 32.132 1.00 79.33 C ANISOU 880 C CYS A 110 9671 9036 11436 245 11 1316 C ATOM 881 O CYS A 110 23.866 49.097 32.498 1.00 81.84 O ANISOU 881 O CYS A 110 10031 9401 11665 279 -59 1253 O ATOM 882 CB CYS A 110 25.548 51.844 33.096 1.00 72.09 C ANISOU 882 CB CYS A 110 8717 7913 10760 186 -46 1388 C ATOM 883 SG CYS A 110 23.877 52.358 33.559 1.00 78.91 S ANISOU 883 SG CYS A 110 9665 8766 11553 250 -137 1360 S ATOM 884 N ASN A 111 25.354 49.547 30.868 1.00 79.23 N ANISOU 884 N ASN A 111 9671 9072 11361 241 120 1390 N ATOM 885 CA ASN A 111 24.594 48.799 29.872 1.00 79.08 C ANISOU 885 CA ASN A 111 9728 9165 11155 269 153 1383 C ATOM 886 C ASN A 111 24.741 47.297 30.082 1.00 84.49 C ANISOU 886 C ASN A 111 10410 9901 11791 278 167 1272 C ATOM 887 O ASN A 111 23.792 46.539 29.857 1.00 98.54 O ANISOU 887 O ASN A 111 12254 11754 13434 295 131 1219 O ATOM 888 CB ASN A 111 25.041 49.194 28.465 1.00 83.06 C ANISOU 888 CB ASN A 111 10259 9709 11590 256 271 1491 C ATOM 889 CG ASN A 111 24.694 50.630 28.126 1.00 78.99 C ANISOU 889 CG ASN A 111 9760 9150 11103 252 253 1617 C ATOM 890 OD1 ASN A 111 23.593 50.921 27.659 1.00 71.09 O ANISOU 890 OD1 ASN A 111 8822 8200 9988 276 206 1662 O ATOM 891 ND2 ASN A 111 25.635 51.538 28.358 1.00 92.77 N ANISOU 891 ND2 ASN A 111 11444 10796 13009 218 287 1683 N ATOM 892 N LEU A 112 25.922 46.849 30.514 1.00 78.36 N ANISOU 892 N LEU A 112 9555 9083 11136 266 219 1245 N ATOM 893 CA LEU A 112 26.122 45.429 30.785 1.00 70.27 C ANISOU 893 CA LEU A 112 8520 8086 10092 283 237 1149 C ATOM 894 C LEU A 112 25.326 44.988 32.007 1.00 69.66 C ANISOU 894 C LEU A 112 8443 8000 10026 293 104 1065 C ATOM 895 O LEU A 112 24.572 44.010 31.950 1.00 73.55 O ANISOU 895 O LEU A 112 8989 8544 10412 309 78 996 O ATOM 896 CB LEU A 112 27.610 45.134 30.977 1.00 85.63 C ANISOU 896 CB LEU A 112 10361 9988 12186 276 325 1165 C ATOM 897 CG LEU A 112 28.514 45.320 29.759 1.00104.09 C ANISOU 897 CG LEU A 112 12689 12346 14516 275 488 1244 C ATOM 898 CD1 LEU A 112 29.968 45.072 30.131 1.00109.69 C ANISOU 898 CD1 LEU A 112 13264 13009 15404 271 562 1273 C ATOM 899 CD2 LEU A 112 28.083 44.400 28.629 1.00104.76 C ANISOU 899 CD2 LEU A 112 12881 12509 14414 303 582 1198 C ATOM 900 N GLU A 113 25.484 45.701 33.126 1.00 62.85 N ANISOU 900 N GLU A 113 7523 7071 9285 276 18 1070 N ATOM 901 CA GLU A 113 24.750 45.350 34.337 1.00 62.56 C ANISOU 901 CA GLU A 113 7487 7031 9251 284 -101 995 C ATOM 902 C GLU A 113 23.251 45.549 34.161 1.00 74.73 C ANISOU 902 C GLU A 113 9109 8620 10664 309 -162 987 C ATOM 903 O GLU A 113 22.456 44.872 34.821 1.00 87.04 O ANISOU 903 O GLU A 113 10683 10211 12178 323 -234 924 O ATOM 904 CB GLU A 113 25.268 46.174 35.518 1.00 59.32 C ANISOU 904 CB GLU A 113 7015 6541 8981 253 -174 999 C ATOM 905 CG GLU A 113 24.822 45.676 36.886 1.00 79.69 C ANISOU 905 CG GLU A 113 9585 9122 11573 256 -282 920 C ATOM 906 CD GLU A 113 23.616 46.422 37.424 1.00 93.36 C ANISOU 906 CD GLU A 113 11377 10845 13253 274 -361 900 C ATOM 907 OE1 GLU A 113 23.008 47.205 36.665 1.00 96.13 O ANISOU 907 OE1 GLU A 113 11777 11194 13554 293 -336 950 O ATOM 908 OE2 GLU A 113 23.281 46.230 38.612 1.00113.29 O ANISOU 908 OE2 GLU A 113 13895 13364 15787 273 -444 841 O ATOM 909 N GLY A 114 22.847 46.461 33.280 1.00 74.18 N ANISOU 909 N GLY A 114 9083 8561 10542 314 -136 1063 N ATOM 910 CA GLY A 114 21.440 46.689 33.020 1.00 62.77 C ANISOU 910 CA GLY A 114 7698 7170 8983 341 -193 1080 C ATOM 911 C GLY A 114 20.842 45.655 32.090 1.00 71.16 C ANISOU 911 C GLY A 114 8817 8335 9887 340 -173 1060 C ATOM 912 O GLY A 114 19.680 45.268 32.246 1.00 77.59 O ANISOU 912 O GLY A 114 9658 9207 10615 351 -246 1036 O ATOM 913 N PHE A 115 21.630 45.200 31.113 1.00 81.14 N ANISOU 913 N PHE A 115 10100 9622 11109 322 -71 1068 N ATOM 914 CA PHE A 115 21.144 44.181 30.188 1.00 75.04 C ANISOU 914 CA PHE A 115 9402 8937 10173 310 -44 1031 C ATOM 915 C PHE A 115 20.960 42.841 30.888 1.00 73.53 C ANISOU 915 C PHE A 115 9208 8749 9981 307 -81 920 C ATOM 916 O PHE A 115 19.948 42.162 30.682 1.00 88.48 O ANISOU 916 O PHE A 115 11154 10706 11756 293 -136 882 O ATOM 917 CB PHE A 115 22.106 44.044 29.007 1.00 66.55 C ANISOU 917 CB PHE A 115 8357 7877 9051 296 95 1058 C ATOM 918 CG PHE A 115 21.761 42.925 28.064 1.00 74.41 C ANISOU 918 CG PHE A 115 9448 8951 9873 276 138 996 C ATOM 919 CD1 PHE A 115 20.787 43.094 27.094 1.00 82.05 C ANISOU 919 CD1 PHE A 115 10500 10015 10661 251 103 1037 C ATOM 920 CD2 PHE A 115 22.420 41.708 28.140 1.00 75.25 C ANISOU 920 CD2 PHE A 115 9563 9031 9999 280 211 900 C ATOM 921 CE1 PHE A 115 20.471 42.068 26.222 1.00 90.34 C ANISOU 921 CE1 PHE A 115 11651 11135 11538 216 134 969 C ATOM 922 CE2 PHE A 115 22.107 40.678 27.272 1.00 73.40 C ANISOU 922 CE2 PHE A 115 9434 8850 9604 256 256 828 C ATOM 923 CZ PHE A 115 21.132 40.859 26.312 1.00 83.29 C ANISOU 923 CZ PHE A 115 10781 10201 10663 218 214 856 C ATOM 924 N PHE A 116 21.921 42.448 31.726 1.00 66.77 N ANISOU 924 N PHE A 116 8285 7823 9262 316 -56 878 N ATOM 925 CA PHE A 116 21.855 41.143 32.377 1.00 66.93 C ANISOU 925 CA PHE A 116 8299 7836 9295 318 -81 787 C ATOM 926 C PHE A 116 20.845 41.126 33.518 1.00 66.71 C ANISOU 926 C PHE A 116 8251 7818 9279 321 -211 764 C ATOM 927 O PHE A 116 20.184 40.106 33.746 1.00 71.02 O ANISOU 927 O PHE A 116 8823 8392 9769 312 -254 706 O ATOM 928 CB PHE A 116 23.242 40.739 32.877 1.00 54.53 C ANISOU 928 CB PHE A 116 6651 6196 7873 330 -13 773 C ATOM 929 CG PHE A 116 24.174 40.301 31.783 1.00 74.34 C ANISOU 929 CG PHE A 116 9181 8700 10363 338 136 774 C ATOM 930 CD1 PHE A 116 23.736 39.441 30.788 1.00 80.58 C ANISOU 930 CD1 PHE A 116 10076 9535 11006 331 193 720 C ATOM 931 CD2 PHE A 116 25.481 40.756 31.740 1.00 78.08 C ANISOU 931 CD2 PHE A 116 9573 9128 10965 347 224 830 C ATOM 932 CE1 PHE A 116 24.586 39.035 29.777 1.00 79.26 C ANISOU 932 CE1 PHE A 116 9942 9363 10810 343 348 712 C ATOM 933 CE2 PHE A 116 26.336 40.355 30.729 1.00 86.73 C ANISOU 933 CE2 PHE A 116 10683 10224 12046 363 380 836 C ATOM 934 CZ PHE A 116 25.887 39.494 29.747 1.00 80.76 C ANISOU 934 CZ PHE A 116 10044 9510 11133 366 449 773 C ATOM 935 N ALA A 117 20.710 42.236 34.248 1.00 65.70 N ANISOU 935 N ALA A 117 8080 7661 9223 333 -269 806 N ATOM 936 CA ALA A 117 19.717 42.289 35.317 1.00 68.93 C ANISOU 936 CA ALA A 117 8475 8082 9632 345 -375 784 C ATOM 937 C ALA A 117 18.302 42.293 34.754 1.00 76.99 C ANISOU 937 C ALA A 117 9546 9185 10521 347 -423 806 C ATOM 938 O ALA A 117 17.396 41.678 35.329 1.00 65.42 O ANISOU 938 O ALA A 117 8078 7759 9020 346 -491 774 O ATOM 939 CB ALA A 117 19.950 43.516 36.197 1.00 70.50 C ANISOU 939 CB ALA A 117 8633 8219 9934 358 -411 813 C ATOM 940 N THR A 118 18.091 42.982 33.630 1.00 74.32 N ANISOU 940 N THR A 118 9247 8880 10113 346 -391 874 N ATOM 941 CA THR A 118 16.780 42.962 32.990 1.00 70.14 C ANISOU 941 CA THR A 118 8756 8442 9454 340 -445 912 C ATOM 942 C THR A 118 16.519 41.619 32.320 1.00 76.28 C ANISOU 942 C THR A 118 9588 9281 10112 293 -441 854 C ATOM 943 O THR A 118 15.393 41.108 32.359 1.00 85.23 O ANISOU 943 O THR A 118 10732 10484 11167 273 -518 847 O ATOM 944 CB THR A 118 16.672 44.102 31.976 1.00 72.59 C ANISOU 944 CB THR A 118 9089 8772 9721 350 -417 1017 C ATOM 945 OG1 THR A 118 16.922 45.352 32.632 1.00 65.37 O ANISOU 945 OG1 THR A 118 8132 7776 8930 391 -418 1064 O ATOM 946 CG2 THR A 118 15.284 44.138 31.350 1.00 64.66 C ANISOU 946 CG2 THR A 118 8107 7873 8587 344 -489 1078 C ATOM 947 N LEU A 119 17.548 41.028 31.708 1.00 72.51 N ANISOU 947 N LEU A 119 9147 8776 9626 274 -347 810 N ATOM 948 CA LEU A 119 17.385 39.730 31.061 1.00 76.83 C ANISOU 948 CA LEU A 119 9767 9360 10064 229 -327 737 C ATOM 949 C LEU A 119 17.012 38.655 32.075 1.00 78.47 C ANISOU 949 C LEU A 119 9951 9547 10317 220 -387 662 C ATOM 950 O LEU A 119 16.065 37.889 31.865 1.00 84.21 O ANISOU 950 O LEU A 119 10719 10328 10947 175 -448 632 O ATOM 951 CB LEU A 119 18.668 39.348 30.321 1.00 76.23 C ANISOU 951 CB LEU A 119 9730 9241 9992 228 -190 702 C ATOM 952 CG LEU A 119 18.629 38.104 29.431 1.00 68.17 C ANISOU 952 CG LEU A 119 8813 8243 8845 184 -138 617 C ATOM 953 CD1 LEU A 119 17.816 38.370 28.176 1.00 60.32 C ANISOU 953 CD1 LEU A 119 7910 7354 7654 134 -162 653 C ATOM 954 CD2 LEU A 119 20.037 37.653 29.077 1.00 65.69 C ANISOU 954 CD2 LEU A 119 8511 7859 8590 210 17 574 C ATOM 955 N GLY A 120 17.747 38.588 33.187 1.00 76.70 N ANISOU 955 N GLY A 120 9657 9246 10238 253 -377 641 N ATOM 956 CA GLY A 120 17.467 37.569 34.186 1.00 71.32 C ANISOU 956 CA GLY A 120 8950 8544 9604 246 -429 585 C ATOM 957 C GLY A 120 16.096 37.721 34.815 1.00 75.38 C ANISOU 957 C GLY A 120 9440 9121 10081 239 -543 611 C ATOM 958 O GLY A 120 15.423 36.729 35.108 1.00 86.53 O ANISOU 958 O GLY A 120 10862 10554 11461 206 -593 574 O ATOM 959 N GLY A 121 15.660 38.963 35.029 1.00 74.49 N ANISOU 959 N GLY A 121 9291 9032 9979 271 -578 679 N ATOM 960 CA GLY A 121 14.344 39.186 35.602 1.00 56.83 C ANISOU 960 CA GLY A 121 7022 6858 7715 278 -669 714 C ATOM 961 C GLY A 121 13.214 38.890 34.638 1.00 63.85 C ANISOU 961 C GLY A 121 7948 7843 8469 234 -717 744 C ATOM 962 O GLY A 121 12.118 38.510 35.060 1.00 56.33 O ANISOU 962 O GLY A 121 6965 6949 7488 218 -793 758 O ATOM 963 N GLU A 122 13.459 39.053 33.336 1.00 67.18 N ANISOU 963 N GLU A 122 8432 8290 8801 207 -677 761 N ATOM 964 CA GLU A 122 12.417 38.805 32.346 1.00 62.67 C ANISOU 964 CA GLU A 122 7903 7823 8085 151 -736 795 C ATOM 965 C GLU A 122 12.332 37.337 31.955 1.00 63.57 C ANISOU 965 C GLU A 122 8088 7946 8121 70 -744 704 C ATOM 966 O GLU A 122 11.238 36.847 31.653 1.00 69.92 O ANISOU 966 O GLU A 122 8903 8832 8833 8 -831 717 O ATOM 967 CB GLU A 122 12.654 39.669 31.109 1.00 62.32 C ANISOU 967 CB GLU A 122 7906 7815 7960 151 -697 863 C ATOM 968 CG GLU A 122 12.386 41.138 31.347 1.00 63.10 C ANISOU 968 CG GLU A 122 7941 7913 8122 221 -710 973 C ATOM 969 CD GLU A 122 10.917 41.433 31.577 1.00 73.46 C ANISOU 969 CD GLU A 122 9193 9313 9406 231 -814 1054 C ATOM 970 OE1 GLU A 122 10.070 40.761 30.952 1.00 77.93 O ANISOU 970 OE1 GLU A 122 9781 9977 9852 163 -884 1065 O ATOM 971 OE2 GLU A 122 10.610 42.333 32.385 1.00 83.75 O ANISOU 971 OE2 GLU A 122 10427 10586 10810 305 -824 1107 O ATOM 972 N ILE A 123 13.461 36.625 31.944 1.00 68.92 N ANISOU 972 N ILE A 123 8810 8535 8841 69 -654 617 N ATOM 973 CA ILE A 123 13.417 35.183 31.724 1.00 59.97 C ANISOU 973 CA ILE A 123 7747 7379 7660 3 -650 520 C ATOM 974 C ILE A 123 12.630 34.508 32.838 1.00 58.51 C ANISOU 974 C ILE A 123 7502 7194 7535 -13 -738 512 C ATOM 975 O ILE A 123 11.804 33.621 32.587 1.00 54.74 O ANISOU 975 O ILE A 123 7064 6754 6982 -93 -802 482 O ATOM 976 CB ILE A 123 14.842 34.609 31.608 1.00 56.51 C ANISOU 976 CB ILE A 123 7352 6832 7288 29 -520 441 C ATOM 977 CG1 ILE A 123 15.548 35.165 30.371 1.00 62.21 C ANISOU 977 CG1 ILE A 123 8141 7567 7929 35 -423 451 C ATOM 978 CG2 ILE A 123 14.802 33.089 31.548 1.00 53.86 C ANISOU 978 CG2 ILE A 123 7088 6444 6934 -26 -509 338 C ATOM 979 CD1 ILE A 123 16.991 34.727 30.243 1.00 48.71 C ANISOU 979 CD1 ILE A 123 6452 5756 6298 75 -277 391 C ATOM 980 N ALA A 124 12.859 34.929 34.084 1.00 57.24 N ANISOU 980 N ALA A 124 7249 6996 7505 53 -743 541 N ATOM 981 CA ALA A 124 12.119 34.366 35.208 1.00 47.79 C ANISOU 981 CA ALA A 124 5991 5809 6360 43 -818 545 C ATOM 982 C ALA A 124 10.637 34.709 35.125 1.00 59.87 C ANISOU 982 C ALA A 124 7480 7452 7815 14 -919 619 C ATOM 983 O ALA A 124 9.785 33.896 35.504 1.00 75.22 O ANISOU 983 O ALA A 124 9404 9430 9748 -39 -986 617 O ATOM 984 CB ALA A 124 12.711 34.861 36.527 1.00 49.08 C ANISOU 984 CB ALA A 124 6074 5919 6656 119 -800 562 C ATOM 985 N LEU A 125 10.310 35.906 34.633 1.00 59.07 N ANISOU 985 N LEU A 125 7359 7412 7675 48 -929 695 N ATOM 986 CA LEU A 125 8.909 36.294 34.502 1.00 57.63 C ANISOU 986 CA LEU A 125 7122 7343 7434 32 -1021 785 C ATOM 987 C LEU A 125 8.198 35.437 33.462 1.00 71.64 C ANISOU 987 C LEU A 125 8954 9189 9074 -82 -1087 773 C ATOM 988 O LEU A 125 7.137 34.864 33.734 1.00 64.23 O ANISOU 988 O LEU A 125 7972 8316 8117 -138 -1174 800 O ATOM 989 CB LEU A 125 8.804 37.778 34.146 1.00 63.84 C ANISOU 989 CB LEU A 125 7876 8161 8219 102 -1009 879 C ATOM 990 CG LEU A 125 7.403 38.319 33.841 1.00 67.51 C ANISOU 990 CG LEU A 125 8275 8747 8630 100 -1097 997 C ATOM 991 CD1 LEU A 125 7.179 39.650 34.535 1.00 66.27 C ANISOU 991 CD1 LEU A 125 8038 8576 8566 214 -1075 1078 C ATOM 992 CD2 LEU A 125 7.189 38.465 32.340 1.00 73.97 C ANISOU 992 CD2 LEU A 125 9154 9642 9310 38 -1128 1042 C ATOM 993 N TRP A 126 8.769 35.339 32.259 1.00 66.31 N ANISOU 993 N TRP A 126 8384 8510 8303 -124 -1047 733 N ATOM 994 CA TRP A 126 8.144 34.543 31.210 1.00 79.28 C ANISOU 994 CA TRP A 126 10105 10220 9796 -245 -1112 707 C ATOM 995 C TRP A 126 8.247 33.046 31.475 1.00 85.21 C ANISOU 995 C TRP A 126 10915 10902 10558 -322 -1113 594 C ATOM 996 O TRP A 126 7.459 32.278 30.913 1.00 76.44 O ANISOU 996 O TRP A 126 9852 9847 9346 -438 -1195 574 O ATOM 997 CB TRP A 126 8.758 34.885 29.852 1.00 71.61 C ANISOU 997 CB TRP A 126 9243 9266 8701 -266 -1056 692 C ATOM 998 CG TRP A 126 8.304 36.212 29.323 1.00 79.95 C ANISOU 998 CG TRP A 126 10250 10418 9709 -226 -1091 827 C ATOM 999 CD1 TRP A 126 9.018 37.375 29.300 1.00 81.63 C ANISOU 999 CD1 TRP A 126 10441 10596 9981 -131 -1013 883 C ATOM 1000 CD2 TRP A 126 7.026 36.515 28.751 1.00 81.33 C ANISOU 1000 CD2 TRP A 126 10385 10735 9780 -283 -1216 937 C ATOM 1001 NE1 TRP A 126 8.265 38.381 28.743 1.00 69.48 N ANISOU 1001 NE1 TRP A 126 8858 9159 8383 -117 -1075 1020 N ATOM 1002 CE2 TRP A 126 7.038 37.879 28.398 1.00 78.82 C ANISOU 1002 CE2 TRP A 126 10024 10458 9466 -205 -1202 1061 C ATOM 1003 CE3 TRP A 126 5.873 35.764 28.501 1.00 76.26 C ANISOU 1003 CE3 TRP A 126 9735 10191 9050 -396 -1344 952 C ATOM 1004 CZ2 TRP A 126 5.943 38.507 27.809 1.00 87.28 C ANISOU 1004 CZ2 TRP A 126 11038 11665 10458 -225 -1308 1206 C ATOM 1005 CZ3 TRP A 126 4.787 36.389 27.916 1.00 66.86 C ANISOU 1005 CZ3 TRP A 126 8482 9146 7777 -425 -1457 1095 C ATOM 1006 CH2 TRP A 126 4.830 37.747 27.576 1.00 82.10 C ANISOU 1006 CH2 TRP A 126 10364 11115 9715 -334 -1437 1224 C ATOM 1007 N SER A 127 9.195 32.613 32.312 1.00 67.07 N ANISOU 1007 N SER A 127 8615 8483 8385 -267 -1029 526 N ATOM 1008 CA SER A 127 9.233 31.207 32.701 1.00 59.41 C ANISOU 1008 CA SER A 127 7687 7436 7451 -328 -1031 437 C ATOM 1009 C SER A 127 8.014 30.839 33.537 1.00 69.10 C ANISOU 1009 C SER A 127 8821 8722 8713 -371 -1143 496 C ATOM 1010 O SER A 127 7.488 29.727 33.421 1.00 69.76 O ANISOU 1010 O SER A 127 8947 8793 8765 -475 -1196 452 O ATOM 1011 CB SER A 127 10.521 30.899 33.463 1.00 55.72 C ANISOU 1011 CB SER A 127 7217 6833 7122 -248 -923 379 C ATOM 1012 OG SER A 127 11.649 30.966 32.608 1.00 64.57 O ANISOU 1012 OG SER A 127 8426 7892 8213 -224 -809 317 O ATOM 1013 N LEU A 128 7.551 31.761 34.385 1.00 63.30 N ANISOU 1013 N LEU A 128 7962 8046 8044 -294 -1172 596 N ATOM 1014 CA LEU A 128 6.322 31.528 35.133 1.00 63.51 C ANISOU 1014 CA LEU A 128 7887 8148 8096 -326 -1266 669 C ATOM 1015 C LEU A 128 5.089 31.593 34.243 1.00 71.60 C ANISOU 1015 C LEU A 128 8898 9304 9003 -420 -1376 736 C ATOM 1016 O LEU A 128 4.062 30.995 34.582 1.00 72.08 O ANISOU 1016 O LEU A 128 8898 9422 9067 -494 -1463 778 O ATOM 1017 CB LEU A 128 6.196 32.539 36.274 1.00 54.54 C ANISOU 1017 CB LEU A 128 6633 7035 7056 -208 -1248 749 C ATOM 1018 CG LEU A 128 7.311 32.523 37.322 1.00 48.47 C ANISOU 1018 CG LEU A 128 5860 6157 6400 -125 -1164 699 C ATOM 1019 CD1 LEU A 128 6.937 33.393 38.512 1.00 56.33 C ANISOU 1019 CD1 LEU A 128 6749 7189 7466 -33 -1164 770 C ATOM 1020 CD2 LEU A 128 7.618 31.100 37.764 1.00 48.06 C ANISOU 1020 CD2 LEU A 128 5844 6023 6393 -185 -1159 631 C ATOM 1021 N VAL A 129 5.166 32.305 33.119 1.00 70.15 N ANISOU 1021 N VAL A 129 8764 9175 8716 -424 -1379 758 N ATOM 1022 CA VAL A 129 4.054 32.338 32.176 1.00 72.57 C ANISOU 1022 CA VAL A 129 9062 9615 8895 -525 -1496 828 C ATOM 1023 C VAL A 129 4.011 31.056 31.356 1.00 74.84 C ANISOU 1023 C VAL A 129 9480 9880 9075 -682 -1538 722 C ATOM 1024 O VAL A 129 2.946 30.457 31.167 1.00 65.83 O ANISOU 1024 O VAL A 129 8312 8818 7881 -803 -1657 755 O ATOM 1025 CB VAL A 129 4.157 33.583 31.276 1.00 67.70 C ANISOU 1025 CB VAL A 129 8452 9069 8202 -473 -1487 904 C ATOM 1026 CG1 VAL A 129 3.038 33.591 30.246 1.00 60.16 C ANISOU 1026 CG1 VAL A 129 7490 8266 7105 -586 -1620 988 C ATOM 1027 CG2 VAL A 129 4.121 34.844 32.118 1.00 70.93 C ANISOU 1027 CG2 VAL A 129 8738 9482 8728 -323 -1445 1005 C ATOM 1028 N VAL A 130 5.169 30.616 30.859 1.00 72.31 N ANISOU 1028 N VAL A 130 9303 9448 8724 -683 -1437 593 N ATOM 1029 CA VAL A 130 5.230 29.373 30.094 1.00 70.20 C ANISOU 1029 CA VAL A 130 9184 9131 8357 -822 -1453 469 C ATOM 1030 C VAL A 130 4.865 28.187 30.977 1.00 72.65 C ANISOU 1030 C VAL A 130 9471 9368 8766 -883 -1487 427 C ATOM 1031 O VAL A 130 4.188 27.250 30.535 1.00 70.73 O ANISOU 1031 O VAL A 130 9288 9136 8448 -1034 -1575 385 O ATOM 1032 CB VAL A 130 6.623 29.208 29.457 1.00 62.71 C ANISOU 1032 CB VAL A 130 8384 8067 7375 -783 -1306 343 C ATOM 1033 CG1 VAL A 130 6.784 27.817 28.862 1.00 55.38 C ANISOU 1033 CG1 VAL A 130 7620 7049 6373 -907 -1293 192 C ATOM 1034 CG2 VAL A 130 6.841 30.269 28.390 1.00 58.57 C ANISOU 1034 CG2 VAL A 130 7900 7634 6722 -757 -1286 391 C ATOM 1035 N LEU A 131 5.296 28.213 32.241 1.00 61.81 N ANISOU 1035 N LEU A 131 8010 7918 7558 -776 -1425 445 N ATOM 1036 CA LEU A 131 4.941 27.141 33.167 1.00 49.33 C ANISOU 1036 CA LEU A 131 6394 6273 6077 -826 -1455 429 C ATOM 1037 C LEU A 131 3.431 27.044 33.343 1.00 63.74 C ANISOU 1037 C LEU A 131 8111 8229 7877 -923 -1601 536 C ATOM 1038 O LEU A 131 2.877 25.941 33.421 1.00 67.97 O ANISOU 1038 O LEU A 131 8672 8736 8420 -1049 -1667 506 O ATOM 1039 CB LEU A 131 5.628 27.362 34.515 1.00 45.75 C ANISOU 1039 CB LEU A 131 5853 5744 5786 -688 -1372 454 C ATOM 1040 CG LEU A 131 5.313 26.361 35.629 1.00 64.12 C ANISOU 1040 CG LEU A 131 8126 8011 8225 -720 -1395 464 C ATOM 1041 CD1 LEU A 131 5.628 24.942 35.187 1.00 73.93 C ANISOU 1041 CD1 LEU A 131 9504 9120 9464 -826 -1379 345 C ATOM 1042 CD2 LEU A 131 6.080 26.712 36.895 1.00 51.88 C ANISOU 1042 CD2 LEU A 131 6499 6404 6808 -582 -1316 492 C ATOM 1043 N ALA A 132 2.747 28.188 33.402 1.00 67.98 N ANISOU 1043 N ALA A 132 8525 8908 8398 -866 -1651 667 N ATOM 1044 CA ALA A 132 1.293 28.171 33.519 1.00 52.62 C ANISOU 1044 CA ALA A 132 6456 7102 6437 -949 -1785 788 C ATOM 1045 C ALA A 132 0.642 27.663 32.239 1.00 70.36 C ANISOU 1045 C ALA A 132 8785 9420 8528 -1127 -1903 766 C ATOM 1046 O ALA A 132 -0.385 26.975 32.288 1.00 69.62 O ANISOU 1046 O ALA A 132 8639 9385 8427 -1261 -2020 810 O ATOM 1047 CB ALA A 132 0.776 29.565 33.871 1.00 57.28 C ANISOU 1047 CB ALA A 132 6893 7813 7057 -825 -1792 936 C ATOM 1048 N ILE A 133 1.223 27.992 31.082 1.00 71.50 N ANISOU 1048 N ILE A 133 9059 9565 8542 -1139 -1877 702 N ATOM 1049 CA ILE A 133 0.683 27.504 29.817 1.00 74.43 C ANISOU 1049 CA ILE A 133 9534 10007 8738 -1317 -1989 667 C ATOM 1050 C ILE A 133 0.855 25.995 29.710 1.00 82.25 C ANISOU 1050 C ILE A 133 10667 10867 9719 -1459 -1994 515 C ATOM 1051 O ILE A 133 -0.063 25.280 29.291 1.00 80.31 O ANISOU 1051 O ILE A 133 10438 10677 9400 -1639 -2129 517 O ATOM 1052 CB ILE A 133 1.345 28.235 28.634 1.00 69.48 C ANISOU 1052 CB ILE A 133 9024 9411 7964 -1288 -1942 633 C ATOM 1053 CG1 ILE A 133 1.033 29.731 28.685 1.00 67.91 C ANISOU 1053 CG1 ILE A 133 8682 9340 7781 -1162 -1954 802 C ATOM 1054 CG2 ILE A 133 0.884 27.642 27.312 1.00 45.15 C ANISOU 1054 CG2 ILE A 133 6082 6397 4676 -1484 -2052 575 C ATOM 1055 CD1 ILE A 133 1.678 30.527 27.570 1.00 54.25 C ANISOU 1055 CD1 ILE A 133 7053 7644 5916 -1127 -1905 794 C ATOM 1056 N GLU A 134 2.030 25.485 30.089 1.00 76.05 N ANISOU 1056 N GLU A 134 9980 9901 9014 -1384 -1848 387 N ATOM 1057 CA GLU A 134 2.271 24.047 30.018 1.00 62.41 C ANISOU 1057 CA GLU A 134 8393 8022 7298 -1500 -1832 241 C ATOM 1058 C GLU A 134 1.345 23.282 30.955 1.00 72.64 C ANISOU 1058 C GLU A 134 9577 9313 8708 -1582 -1925 306 C ATOM 1059 O GLU A 134 0.788 22.244 30.578 1.00 71.28 O ANISOU 1059 O GLU A 134 9485 9107 8490 -1761 -2012 246 O ATOM 1060 CB GLU A 134 3.734 23.743 30.344 1.00 59.12 C ANISOU 1060 CB GLU A 134 8071 7416 6975 -1374 -1648 122 C ATOM 1061 CG GLU A 134 4.726 24.303 29.338 1.00 64.69 C ANISOU 1061 CG GLU A 134 8905 8108 7568 -1310 -1539 43 C ATOM 1062 CD GLU A 134 6.165 24.039 29.733 1.00 79.44 C ANISOU 1062 CD GLU A 134 10832 9799 9553 -1176 -1356 -51 C ATOM 1063 OE1 GLU A 134 6.390 23.493 30.834 1.00 85.94 O ANISOU 1063 OE1 GLU A 134 11590 10518 10545 -1126 -1322 -43 O ATOM 1064 OE2 GLU A 134 7.072 24.377 28.942 1.00 81.87 O ANISOU 1064 OE2 GLU A 134 11245 10077 9784 -1123 -1246 -121 O ATOM 1065 N ARG A 135 1.164 23.781 32.180 1.00 66.02 N ANISOU 1065 N ARG A 135 8559 8509 8015 -1460 -1905 428 N ATOM 1066 CA ARG A 135 0.274 23.111 33.123 1.00 61.73 C ANISOU 1066 CA ARG A 135 7898 7976 7581 -1530 -1981 508 C ATOM 1067 C ARG A 135 -1.181 23.198 32.682 1.00 70.73 C ANISOU 1067 C ARG A 135 8940 9292 8642 -1678 -2156 621 C ATOM 1068 O ARG A 135 -1.974 22.301 32.988 1.00 74.30 O ANISOU 1068 O ARG A 135 9353 9739 9138 -1817 -2246 649 O ATOM 1069 CB ARG A 135 0.450 23.704 34.520 1.00 52.42 C ANISOU 1069 CB ARG A 135 6559 6805 6553 -1357 -1907 610 C ATOM 1070 CG ARG A 135 1.805 23.403 35.141 1.00 45.75 C ANISOU 1070 CG ARG A 135 5788 5785 5810 -1237 -1758 516 C ATOM 1071 CD ARG A 135 1.975 24.093 36.484 1.00 62.71 C ANISOU 1071 CD ARG A 135 7788 7960 8080 -1077 -1699 615 C ATOM 1072 NE ARG A 135 3.190 23.653 37.164 1.00 71.93 N ANISOU 1072 NE ARG A 135 9011 8968 9353 -986 -1581 543 N ATOM 1073 CZ ARG A 135 3.624 24.152 38.317 1.00 72.14 C ANISOU 1073 CZ ARG A 135 8945 8991 9475 -850 -1518 600 C ATOM 1074 NH1 ARG A 135 2.945 25.115 38.924 1.00 79.86 N ANISOU 1074 NH1 ARG A 135 9783 10105 10457 -784 -1546 717 N ATOM 1075 NH2 ARG A 135 4.740 23.688 38.862 1.00 81.48 N ANISOU 1075 NH2 ARG A 135 10175 10034 10750 -781 -1427 543 N ATOM 1076 N TYR A 136 -1.550 24.261 31.965 1.00 76.89 N ANISOU 1076 N TYR A 136 9673 10228 9312 -1654 -2210 700 N ATOM 1077 CA TYR A 136 -2.908 24.361 31.439 1.00 68.60 C ANISOU 1077 CA TYR A 136 8525 9358 8182 -1798 -2387 821 C ATOM 1078 C TYR A 136 -3.125 23.392 30.284 1.00 74.82 C ANISOU 1078 C TYR A 136 9486 10122 8820 -2026 -2492 704 C ATOM 1079 O TYR A 136 -4.205 22.805 30.153 1.00 82.14 O ANISOU 1079 O TYR A 136 10355 11126 9729 -2205 -2644 763 O ATOM 1080 CB TYR A 136 -3.193 25.799 31.002 1.00 60.82 C ANISOU 1080 CB TYR A 136 7437 8539 7131 -1695 -2410 951 C ATOM 1081 CG TYR A 136 -4.349 25.939 30.037 1.00 55.05 C ANISOU 1081 CG TYR A 136 6654 7994 6269 -1854 -2596 1055 C ATOM 1082 CD1 TYR A 136 -5.664 25.856 30.478 1.00 66.02 C ANISOU 1082 CD1 TYR A 136 7845 9517 7722 -1928 -2723 1219 C ATOM 1083 CD2 TYR A 136 -4.125 26.165 28.684 1.00 49.67 C ANISOU 1083 CD2 TYR A 136 6114 7362 5395 -1931 -2644 999 C ATOM 1084 CE1 TYR A 136 -6.723 25.985 29.598 1.00 60.21 C ANISOU 1084 CE1 TYR A 136 7043 8960 6872 -2079 -2905 1330 C ATOM 1085 CE2 TYR A 136 -5.178 26.296 27.797 1.00 55.44 C ANISOU 1085 CE2 TYR A 136 6795 8275 5994 -2084 -2828 1104 C ATOM 1086 CZ TYR A 136 -6.474 26.206 28.259 1.00 64.34 C ANISOU 1086 CZ TYR A 136 7713 9533 7198 -2159 -2964 1273 C ATOM 1087 OH TYR A 136 -7.524 26.336 27.380 1.00 77.28 O ANISOU 1087 OH TYR A 136 9299 11328 8736 -2277 -3093 1373 O ATOM 1088 N VAL A 137 -2.110 23.208 29.439 1.00 76.68 N ANISOU 1088 N VAL A 137 9937 10252 8947 -2027 -2409 536 N ATOM 1089 CA VAL A 137 -2.246 22.307 28.300 1.00 81.66 C ANISOU 1089 CA VAL A 137 10764 10850 9415 -2241 -2492 401 C ATOM 1090 C VAL A 137 -2.278 20.855 28.764 1.00 97.88 C ANISOU 1090 C VAL A 137 12898 12730 11561 -2365 -2494 294 C ATOM 1091 O VAL A 137 -3.046 20.038 28.241 1.00 97.42 O ANISOU 1091 O VAL A 137 12901 12688 11426 -2588 -2635 259 O ATOM 1092 CB VAL A 137 -1.113 22.560 27.287 1.00 61.94 C ANISOU 1092 CB VAL A 137 8476 8286 6770 -2190 -2377 252 C ATOM 1093 CG1 VAL A 137 -1.085 21.474 26.226 1.00 69.35 C ANISOU 1093 CG1 VAL A 137 9656 9148 7547 -2400 -2425 71 C ATOM 1094 CG2 VAL A 137 -1.278 23.928 26.640 1.00 63.71 C ANISOU 1094 CG2 VAL A 137 8630 8700 6878 -2116 -2412 375 C ATOM 1095 N VAL A 138 -1.464 20.515 29.764 1.00 93.19 N ANISOU 1095 N VAL A 138 12300 11969 11139 -2228 -2345 249 N ATOM 1096 CA VAL A 138 -1.345 19.121 30.185 1.00 78.40 C ANISOU 1096 CA VAL A 138 10520 9904 9365 -2328 -2325 145 C ATOM 1097 C VAL A 138 -2.561 18.699 31.002 1.00 78.73 C ANISOU 1097 C VAL A 138 10382 10016 9517 -2435 -2456 290 C ATOM 1098 O VAL A 138 -3.129 17.623 30.784 1.00 80.35 O ANISOU 1098 O VAL A 138 10656 10156 9715 -2639 -2553 239 O ATOM 1099 CB VAL A 138 -0.035 18.910 30.968 1.00 58.82 C ANISOU 1099 CB VAL A 138 8087 7230 7034 -2141 -2126 69 C ATOM 1100 CG1 VAL A 138 -0.027 17.547 31.642 1.00 74.19 C ANISOU 1100 CG1 VAL A 138 10079 8987 9123 -2221 -2110 14 C ATOM 1101 CG2 VAL A 138 1.164 19.047 30.042 1.00 53.98 C ANISOU 1101 CG2 VAL A 138 7674 6522 6315 -2073 -1993 -94 C ATOM 1102 N VAL A 139 -2.987 19.541 31.942 1.00 73.11 N ANISOU 1102 N VAL A 139 9439 9433 8905 -2304 -2457 471 N ATOM 1103 CA VAL A 139 -4.051 19.152 32.864 1.00 64.76 C ANISOU 1103 CA VAL A 139 8198 8437 7972 -2376 -2547 619 C ATOM 1104 C VAL A 139 -5.423 19.360 32.234 1.00 60.59 C ANISOU 1104 C VAL A 139 7560 8115 7347 -2550 -2745 739 C ATOM 1105 O VAL A 139 -6.221 18.421 32.125 1.00 85.55 O ANISOU 1105 O VAL A 139 10721 11267 10518 -2761 -2870 748 O ATOM 1106 CB VAL A 139 -3.922 19.916 34.194 1.00 51.81 C ANISOU 1106 CB VAL A 139 6365 6844 6476 -2160 -2448 755 C ATOM 1107 CG1 VAL A 139 -5.147 19.668 35.067 1.00 59.31 C ANISOU 1107 CG1 VAL A 139 7106 7899 7531 -2231 -2539 930 C ATOM 1108 CG2 VAL A 139 -2.658 19.495 34.924 1.00 46.32 C ANISOU 1108 CG2 VAL A 139 5764 5944 5890 -2026 -2281 652 C ATOM 1109 N CYS A 140 -5.723 20.594 31.820 1.00 73.43 N ANISOU 1109 N CYS A 140 9706 6778 11415 -2725 -1231 -531 N ATOM 1110 CA CYS A 140 -7.048 20.889 31.280 1.00 74.47 C ANISOU 1110 CA CYS A 140 9721 7029 11546 -2854 -1456 -641 C ATOM 1111 C CYS A 140 -7.298 20.170 29.961 1.00 87.59 C ANISOU 1111 C CYS A 140 11469 8670 13140 -2984 -1563 -942 C ATOM 1112 O CYS A 140 -8.453 19.876 29.629 1.00113.65 O ANISOU 1112 O CYS A 140 14665 11977 16542 -3131 -1705 -1078 O ATOM 1113 CB CYS A 140 -7.219 22.397 31.098 1.00 73.21 C ANISOU 1113 CB CYS A 140 9513 7136 11168 -2772 -1614 -514 C ATOM 1114 SG CYS A 140 -7.041 23.360 32.615 1.00 84.52 S ANISOU 1114 SG CYS A 140 10817 8622 12676 -2631 -1509 -191 S ATOM 1115 N LYS A 141 -6.238 19.877 29.207 1.00 90.93 N ANISOU 1115 N LYS A 141 12078 9074 13397 -2934 -1494 -1055 N ATOM 1116 CA LYS A 141 -6.305 19.215 27.908 1.00102.51 C ANISOU 1116 CA LYS A 141 13645 10539 14764 -3046 -1578 -1357 C ATOM 1117 C LYS A 141 -7.293 19.905 26.973 1.00108.14 C ANISOU 1117 C LYS A 141 14295 11494 15299 -3132 -1851 -1461 C ATOM 1118 O LYS A 141 -8.368 19.358 26.694 1.00122.77 O ANISOU 1118 O LYS A 141 16049 13312 17286 -3291 -1963 -1625 O ATOM 1119 CB LYS A 141 -6.675 17.738 28.072 1.00 90.72 C ANISOU 1119 CB LYS A 141 12117 8775 13575 -3183 -1475 -1533 C ATOM 1120 CG LYS A 141 -5.472 16.822 28.245 1.00 87.16 C ANISOU 1120 CG LYS A 141 11802 8101 13214 -3124 -1234 -1565 C ATOM 1121 CD LYS A 141 -5.868 15.354 28.270 1.00100.49 C ANISOU 1121 CD LYS A 141 13449 9518 15216 -3270 -1143 -1762 C ATOM 1122 CE LYS A 141 -6.528 14.973 29.584 1.00111.33 C ANISOU 1122 CE LYS A 141 14649 10725 16927 -3299 -1053 -1581 C ATOM 1123 NZ LYS A 141 -6.756 13.503 29.680 1.00114.01 N ANISOU 1123 NZ LYS A 141 14950 10769 17600 -3423 -930 -1745 N ATOM 1124 N PRO A 142 -6.975 21.099 26.473 1.00102.28 N ANISOU 1124 N PRO A 142 13598 10997 14265 -3034 -1965 -1364 N ATOM 1125 CA PRO A 142 -7.830 21.749 25.474 1.00103.13 C ANISOU 1125 CA PRO A 142 13654 11349 14183 -3112 -2228 -1457 C ATOM 1126 C PRO A 142 -7.488 21.398 24.034 1.00111.45 C ANISOU 1126 C PRO A 142 14854 12503 14989 -3172 -2309 -1717 C ATOM 1127 O PRO A 142 -8.114 21.945 23.119 1.00110.22 O ANISOU 1127 O PRO A 142 14664 12575 14638 -3233 -2531 -1791 O ATOM 1128 CB PRO A 142 -7.561 23.234 25.742 1.00 96.12 C ANISOU 1128 CB PRO A 142 12733 10663 13125 -2961 -2287 -1193 C ATOM 1129 CG PRO A 142 -6.119 23.258 26.128 1.00 83.00 C ANISOU 1129 CG PRO A 142 11217 8918 11400 -2804 -2071 -1082 C ATOM 1130 CD PRO A 142 -5.847 21.963 26.867 1.00 92.73 C ANISOU 1130 CD PRO A 142 12471 9857 12905 -2843 -1859 -1142 C ATOM 1131 N MET A 143 -6.520 20.512 23.816 1.00126.49 N ANISOU 1131 N MET A 143 16913 14252 16896 -3157 -2133 -1853 N ATOM 1132 CA MET A 143 -6.051 20.153 22.484 1.00139.08 C ANISOU 1132 CA MET A 143 18658 15938 18249 -3204 -2178 -2107 C ATOM 1133 C MET A 143 -6.278 18.662 22.280 1.00141.70 C ANISOU 1133 C MET A 143 19003 16042 18794 -3354 -2096 -2397 C ATOM 1134 O MET A 143 -5.681 17.839 22.982 1.00142.18 O ANISOU 1134 O MET A 143 19102 15838 19084 -3325 -1873 -2385 O ATOM 1135 CB MET A 143 -4.574 20.518 22.316 1.00149.80 C ANISOU 1135 CB MET A 143 20194 17323 19399 -3040 -2034 -2019 C ATOM 1136 CG MET A 143 -4.086 20.546 20.879 1.00156.81 C ANISOU 1136 CG MET A 143 21231 18393 19956 -3061 -2112 -2227 C ATOM 1137 SD MET A 143 -2.934 21.903 20.578 1.00147.34 S ANISOU 1137 SD MET A 143 20152 17418 18414 -2855 -2103 -1996 S ATOM 1138 CE MET A 143 -4.067 23.281 20.409 1.00141.84 C ANISOU 1138 CE MET A 143 19289 17019 17587 -2862 -2386 -1819 C ATOM 1139 N SER A 144 -7.142 18.322 21.326 1.00150.00 N ANISOU 1139 N SER A 144 20015 17198 19783 -3515 -2277 -2654 N ATOM 1140 CA SER A 144 -7.534 16.934 21.111 1.00162.67 C ANISOU 1140 CA SER A 144 21600 18591 21615 -3677 -2223 -2951 C ATOM 1141 C SER A 144 -6.341 16.111 20.641 1.00162.76 C ANISOU 1141 C SER A 144 21791 18468 21583 -3652 -2032 -3135 C ATOM 1142 O SER A 144 -5.716 16.434 19.625 1.00160.82 O ANISOU 1142 O SER A 144 21680 18410 21014 -3620 -2079 -3243 O ATOM 1143 CB SER A 144 -8.671 16.861 20.094 1.00171.29 C ANISOU 1143 CB SER A 144 22613 19867 22604 -3850 -2475 -3195 C ATOM 1144 OG SER A 144 -8.296 17.460 18.866 1.00177.80 O ANISOU 1144 OG SER A 144 23549 20982 23025 -3832 -2609 -3292 O ATOM 1145 N ASN A 145 -6.030 15.047 21.384 1.00161.42 N ANISOU 1145 N ASN A 145 21616 17971 21747 -3666 -1814 -3165 N ATOM 1146 CA ASN A 145 -4.941 14.121 21.071 1.00158.52 C ANISOU 1146 CA ASN A 145 21395 17417 21418 -3650 -1608 -3341 C ATOM 1147 C ASN A 145 -3.605 14.866 20.976 1.00145.30 C ANISOU 1147 C ASN A 145 19884 15848 19476 -3464 -1512 -3174 C ATOM 1148 O ASN A 145 -2.986 14.981 19.916 1.00147.96 O ANISOU 1148 O ASN A 145 20360 16333 19527 -3453 -1538 -3339 O ATOM 1149 CB ASN A 145 -5.238 13.346 19.781 1.00165.30 C ANISOU 1149 CB ASN A 145 22294 18321 22192 -3817 -1694 -3758 C ATOM 1150 CG ASN A 145 -6.657 12.813 19.735 1.00164.64 C ANISOU 1150 CG ASN A 145 22039 18196 22320 -4004 -1837 -3926 C ATOM 1151 OD1 ASN A 145 -7.344 12.752 20.755 1.00165.59 O ANISOU 1151 OD1 ASN A 145 22014 18179 22723 -4017 -1822 -3751 O ATOM 1152 ND2 ASN A 145 -7.103 12.419 18.548 1.00164.63 N ANISOU 1152 ND2 ASN A 145 22050 18322 22181 -4152 -1976 -4273 N ATOM 1153 N PHE A 146 -3.178 15.373 22.130 1.00135.04 N ANISOU 1153 N PHE A 146 18560 14473 18278 -3318 -1397 -2842 N ATOM 1154 CA PHE A 146 -1.936 16.125 22.245 1.00124.08 C ANISOU 1154 CA PHE A 146 17303 13161 16680 -3130 -1296 -2644 C ATOM 1155 C PHE A 146 -1.084 15.522 23.351 1.00120.62 C ANISOU 1155 C PHE A 146 16886 12431 16512 -3035 -1029 -2489 C ATOM 1156 O PHE A 146 -1.590 15.225 24.437 1.00121.98 O ANISOU 1156 O PHE A 146 16927 12441 16980 -3050 -968 -2341 O ATOM 1157 CB PHE A 146 -2.206 17.607 22.534 1.00115.29 C ANISOU 1157 CB PHE A 146 16131 12305 15370 -3026 -1444 -2362 C ATOM 1158 CG PHE A 146 -0.959 18.440 22.645 1.00107.39 C ANISOU 1158 CG PHE A 146 15253 11390 14160 -2833 -1347 -2159 C ATOM 1159 CD1 PHE A 146 -0.371 18.984 21.516 1.00107.98 C ANISOU 1159 CD1 PHE A 146 15461 11682 13883 -2790 -1420 -2245 C ATOM 1160 CD2 PHE A 146 -0.378 18.683 23.880 1.00100.51 C ANISOU 1160 CD2 PHE A 146 14358 10390 13441 -2696 -1185 -1881 C ATOM 1161 CE1 PHE A 146 0.776 19.751 21.614 1.00102.35 C ANISOU 1161 CE1 PHE A 146 14856 11040 12992 -2613 -1328 -2058 C ATOM 1162 CE2 PHE A 146 0.769 19.448 23.984 1.00 95.60 C ANISOU 1162 CE2 PHE A 146 13842 9844 12637 -2521 -1098 -1703 C ATOM 1163 CZ PHE A 146 1.345 19.983 22.850 1.00 94.56 C ANISOU 1163 CZ PHE A 146 13843 9913 12172 -2478 -1168 -1791 C ATOM 1164 N ARG A 147 0.206 15.348 23.071 1.00120.53 N ANISOU 1164 N ARG A 147 17034 12360 16400 -2936 -870 -2515 N ATOM 1165 CA ARG A 147 1.172 14.859 24.047 1.00127.88 C ANISOU 1165 CA ARG A 147 17999 13037 17551 -2826 -616 -2351 C ATOM 1166 C ARG A 147 2.283 15.889 24.187 1.00118.66 C ANISOU 1166 C ARG A 147 16939 12006 16138 -2632 -563 -2124 C ATOM 1167 O ARG A 147 2.970 16.201 23.208 1.00122.35 O ANISOU 1167 O ARG A 147 17548 12612 16327 -2591 -583 -2238 O ATOM 1168 CB ARG A 147 1.744 13.502 23.632 1.00145.48 C ANISOU 1168 CB ARG A 147 20310 15010 19955 -2895 -444 -2612 C ATOM 1169 CG ARG A 147 2.937 13.062 24.466 1.00157.41 C ANISOU 1169 CG ARG A 147 21879 16281 21647 -2765 -181 -2443 C ATOM 1170 CD ARG A 147 4.184 12.911 23.610 1.00164.47 C ANISOU 1170 CD ARG A 147 22961 17174 22354 -2700 -73 -2591 C ATOM 1171 NE ARG A 147 4.250 13.924 22.560 1.00166.57 N ANISOU 1171 NE ARG A 147 23319 17768 22200 -2673 -246 -2659 N ATOM 1172 CZ ARG A 147 5.302 14.116 21.770 1.00165.01 C ANISOU 1172 CZ ARG A 147 23286 17650 21760 -2598 -186 -2748 C ATOM 1173 NH1 ARG A 147 6.387 13.368 21.914 1.00164.42 N ANISOU 1173 NH1 ARG A 147 23302 17343 21826 -2540 43 -2786 N ATOM 1174 NH2 ARG A 147 5.270 15.059 20.839 1.00164.97 N ANISOU 1174 NH2 ARG A 147 23348 17956 21377 -2580 -352 -2788 N ATOM 1175 N PHE A 148 2.455 16.414 25.397 1.00108.24 N ANISOU 1175 N PHE A 148 15548 10656 14922 -2514 -493 -1808 N ATOM 1176 CA PHE A 148 3.501 17.396 25.674 1.00107.69 C ANISOU 1176 CA PHE A 148 15560 10699 14657 -2326 -432 -1577 C ATOM 1177 C PHE A 148 4.831 16.660 25.781 1.00108.65 C ANISOU 1177 C PHE A 148 15810 10608 14862 -2244 -192 -1597 C ATOM 1178 O PHE A 148 5.125 16.025 26.797 1.00100.41 O ANISOU 1178 O PHE A 148 14719 9337 14096 -2212 -20 -1468 O ATOM 1179 CB PHE A 148 3.187 18.172 26.948 1.00 91.33 C ANISOU 1179 CB PHE A 148 13353 8671 12679 -2240 -439 -1257 C ATOM 1180 CG PHE A 148 4.193 19.238 27.270 1.00 83.76 C ANISOU 1180 CG PHE A 148 12458 7836 11532 -2050 -386 -1025 C ATOM 1181 CD1 PHE A 148 5.191 19.009 28.202 1.00 93.82 C ANISOU 1181 CD1 PHE A 148 13759 8951 12936 -1927 -175 -847 C ATOM 1182 CD2 PHE A 148 4.143 20.469 26.637 1.00 84.67 C ANISOU 1182 CD2 PHE A 148 12596 8226 11347 -1994 -548 -981 C ATOM 1183 CE1 PHE A 148 6.120 19.988 28.498 1.00 91.13 C ANISOU 1183 CE1 PHE A 148 13471 8725 12429 -1755 -128 -645 C ATOM 1184 CE2 PHE A 148 5.069 21.452 26.929 1.00 82.52 C ANISOU 1184 CE2 PHE A 148 12374 8058 10922 -1820 -495 -774 C ATOM 1185 CZ PHE A 148 6.059 21.211 27.860 1.00 84.75 C ANISOU 1185 CZ PHE A 148 12685 8180 11335 -1702 -286 -613 C ATOM 1186 N GLY A 149 5.640 16.744 24.730 1.00108.11 N ANISOU 1186 N GLY A 149 15902 10619 14555 -2211 -178 -1751 N ATOM 1187 CA GLY A 149 6.898 16.038 24.651 1.00105.89 C ANISOU 1187 CA GLY A 149 15751 10145 14337 -2143 41 -1808 C ATOM 1188 C GLY A 149 8.093 16.928 24.924 1.00103.01 C ANISOU 1188 C GLY A 149 15478 9865 13795 -1947 127 -1582 C ATOM 1189 O GLY A 149 7.987 17.997 25.536 1.00104.51 O ANISOU 1189 O GLY A 149 15605 10207 13897 -1849 58 -1331 O ATOM 1190 N GLU A 150 9.257 16.473 24.456 1.00106.25 N ANISOU 1190 N GLU A 150 16036 10171 14164 -1889 284 -1683 N ATOM 1191 CA GLU A 150 10.496 17.208 24.685 1.00 94.34 C ANISOU 1191 CA GLU A 150 14622 8715 12508 -1702 386 -1486 C ATOM 1192 C GLU A 150 10.623 18.405 23.751 1.00104.03 C ANISOU 1192 C GLU A 150 15926 10254 13347 -1648 233 -1491 C ATOM 1193 O GLU A 150 11.149 19.451 24.148 1.00103.71 O ANISOU 1193 O GLU A 150 15891 10337 13176 -1500 231 -1254 O ATOM 1194 CB GLU A 150 11.697 16.276 24.516 1.00 97.60 C ANISOU 1194 CB GLU A 150 15157 8896 13031 -1661 614 -1590 C ATOM 1195 CG GLU A 150 13.031 16.905 24.880 1.00106.85 C ANISOU 1195 CG GLU A 150 16417 10080 14101 -1466 744 -1377 C ATOM 1196 CD GLU A 150 14.211 16.116 24.349 1.00122.04 C ANISOU 1196 CD GLU A 150 18484 11828 16058 -1434 937 -1533 C ATOM 1197 OE1 GLU A 150 14.101 15.557 23.237 1.00129.61 O ANISOU 1197 OE1 GLU A 150 19521 12788 16938 -1542 915 -1838 O ATOM 1198 OE2 GLU A 150 15.247 16.051 25.043 1.00129.73 O ANISOU 1198 OE2 GLU A 150 19489 12665 17138 -1302 1111 -1355 O ATOM 1199 N ASN A 151 10.153 18.271 22.508 1.00111.14 N ANISOU 1199 N ASN A 151 16878 11287 14062 -1765 105 -1758 N ATOM 1200 CA ASN A 151 10.275 19.366 21.552 1.00 99.22 C ANISOU 1200 CA ASN A 151 15439 10083 12177 -1718 -41 -1758 C ATOM 1201 C ASN A 151 9.422 20.564 21.950 1.00 90.92 C ANISOU 1201 C ASN A 151 14259 9249 11038 -1691 -233 -1539 C ATOM 1202 O ASN A 151 9.782 21.706 21.643 1.00 97.54 O ANISOU 1202 O ASN A 151 15131 10302 11629 -1583 -305 -1400 O ATOM 1203 CB ASN A 151 9.897 18.889 20.149 1.00109.84 C ANISOU 1203 CB ASN A 151 16855 11535 13342 -1864 -140 -2098 C ATOM 1204 CG ASN A 151 10.916 17.929 19.567 1.00119.86 C ANISOU 1204 CG ASN A 151 18271 12639 14631 -1869 50 -2323 C ATOM 1205 OD1 ASN A 151 12.085 17.937 19.953 1.00117.61 O ANISOU 1205 OD1 ASN A 151 18067 12233 14386 -1733 233 -2203 O ATOM 1206 ND2 ASN A 151 10.478 17.098 18.628 1.00124.30 N ANISOU 1206 ND2 ASN A 151 18862 13198 15169 -2029 9 -2660 N ATOM 1207 N HIS A 152 8.297 20.330 22.630 1.00 82.95 N ANISOU 1207 N HIS A 152 13096 8183 10240 -1785 -313 -1504 N ATOM 1208 CA HIS A 152 7.470 21.445 23.080 1.00 77.09 C ANISOU 1208 CA HIS A 152 12217 7629 9446 -1760 -484 -1297 C ATOM 1209 C HIS A 152 8.099 22.165 24.265 1.00 85.01 C ANISOU 1209 C HIS A 152 13176 8597 10529 -1591 -379 -982 C ATOM 1210 O HIS A 152 7.962 23.387 24.390 1.00 89.06 O ANISOU 1210 O HIS A 152 13632 9307 10901 -1508 -487 -799 O ATOM 1211 CB HIS A 152 6.069 20.952 23.443 1.00 68.76 C ANISOU 1211 CB HIS A 152 11006 6520 8598 -1916 -595 -1364 C ATOM 1212 CG HIS A 152 5.399 20.179 22.350 1.00 87.49 C ANISOU 1212 CG HIS A 152 13404 8915 10921 -2093 -698 -1687 C ATOM 1213 ND1 HIS A 152 5.644 18.841 22.127 1.00 89.17 N ANISOU 1213 ND1 HIS A 152 13679 8902 11301 -2182 -564 -1923 N ATOM 1214 CD2 HIS A 152 4.492 20.556 21.418 1.00 91.37 C ANISOU 1214 CD2 HIS A 152 13862 9635 11221 -2198 -922 -1818 C ATOM 1215 CE1 HIS A 152 4.916 18.427 21.106 1.00 92.19 C ANISOU 1215 CE1 HIS A 152 14063 9372 11592 -2338 -700 -2200 C ATOM 1216 NE2 HIS A 152 4.209 19.448 20.657 1.00 96.62 N ANISOU 1216 NE2 HIS A 152 14569 10216 11927 -2350 -922 -2139 N ATOM 1217 N ALA A 153 8.789 21.430 25.141 1.00 89.36 N ANISOU 1217 N ALA A 153 13743 8903 11309 -1539 -169 -916 N ATOM 1218 CA ALA A 153 9.423 22.055 26.295 1.00 88.76 C ANISOU 1218 CA ALA A 153 13620 8799 11305 -1382 -64 -627 C ATOM 1219 C ALA A 153 10.616 22.911 25.889 1.00 78.85 C ANISOU 1219 C ALA A 153 12486 7661 9812 -1223 -15 -537 C ATOM 1220 O ALA A 153 10.901 23.922 26.541 1.00 71.30 O ANISOU 1220 O ALA A 153 11474 6802 8815 -1096 -17 -305 O ATOM 1221 CB ALA A 153 9.852 20.988 27.301 1.00 74.89 C ANISOU 1221 CB ALA A 153 11845 6758 9852 -1373 145 -576 C ATOM 1222 N ILE A 154 11.323 22.525 24.825 1.00 77.24 N ANISOU 1222 N ILE A 154 12443 7450 9456 -1228 35 -723 N ATOM 1223 CA ILE A 154 12.446 23.328 24.352 1.00 78.15 C ANISOU 1223 CA ILE A 154 12675 7681 9337 -1081 81 -646 C ATOM 1224 C ILE A 154 11.948 24.631 23.741 1.00 81.35 C ANISOU 1224 C ILE A 154 13042 8384 9484 -1060 -125 -576 C ATOM 1225 O ILE A 154 12.557 25.693 23.926 1.00 79.60 O ANISOU 1225 O ILE A 154 12823 8276 9146 -916 -118 -384 O ATOM 1226 CB ILE A 154 13.299 22.519 23.358 1.00 77.43 C ANISOU 1226 CB ILE A 154 12761 7504 9157 -1102 194 -877 C ATOM 1227 CG1 ILE A 154 13.905 21.298 24.052 1.00 78.07 C ANISOU 1227 CG1 ILE A 154 12867 7271 9523 -1101 415 -910 C ATOM 1228 CG2 ILE A 154 14.393 23.387 22.755 1.00 76.40 C ANISOU 1228 CG2 ILE A 154 12750 7514 8763 -959 228 -807 C ATOM 1229 CD1 ILE A 154 14.781 20.455 23.152 1.00 80.50 C ANISOU 1229 CD1 ILE A 154 13338 7466 9783 -1119 548 -1141 C ATOM 1230 N MET A 155 10.833 24.575 23.008 1.00 80.15 N ANISOU 1230 N MET A 155 12844 8360 9249 -1203 -311 -727 N ATOM 1231 CA MET A 155 10.238 25.799 22.480 1.00 74.94 C ANISOU 1231 CA MET A 155 12122 7980 8371 -1191 -519 -641 C ATOM 1232 C MET A 155 9.772 26.720 23.599 1.00 73.77 C ANISOU 1232 C MET A 155 11806 7875 8347 -1121 -571 -378 C ATOM 1233 O MET A 155 9.853 27.946 23.465 1.00 86.44 O ANISOU 1233 O MET A 155 13373 9668 9804 -1027 -659 -218 O ATOM 1234 CB MET A 155 9.071 25.463 21.551 1.00 79.31 C ANISOU 1234 CB MET A 155 12644 8654 8837 -1369 -711 -855 C ATOM 1235 CG MET A 155 9.459 24.641 20.335 1.00102.27 C ANISOU 1235 CG MET A 155 15707 11563 11588 -1450 -679 -1140 C ATOM 1236 SD MET A 155 8.036 24.178 19.329 1.00126.98 S ANISOU 1236 SD MET A 155 18780 14834 14631 -1671 -907 -1408 S ATOM 1237 CE MET A 155 8.819 23.181 18.062 1.00126.12 C ANISOU 1237 CE MET A 155 18868 14699 14354 -1736 -807 -1742 C ATOM 1238 N GLY A 156 9.282 26.153 24.705 1.00 65.19 N ANISOU 1238 N GLY A 156 10613 6619 7538 -1165 -513 -332 N ATOM 1239 CA GLY A 156 8.869 26.973 25.831 1.00 65.83 C ANISOU 1239 CA GLY A 156 10531 6739 7743 -1100 -544 -96 C ATOM 1240 C GLY A 156 10.020 27.699 26.496 1.00 76.49 C ANISOU 1240 C GLY A 156 11904 8082 9077 -913 -408 115 C ATOM 1241 O GLY A 156 9.855 28.826 26.973 1.00 88.71 O ANISOU 1241 O GLY A 156 13342 9759 10607 -832 -473 300 O ATOM 1242 N VAL A 157 11.197 27.072 26.541 1.00 73.50 N ANISOU 1242 N VAL A 157 11660 7551 8716 -844 -218 84 N ATOM 1243 CA VAL A 157 12.372 27.744 27.086 1.00 73.17 C ANISOU 1243 CA VAL A 157 11649 7506 8646 -664 -88 271 C ATOM 1244 C VAL A 157 12.883 28.794 26.108 1.00 77.63 C ANISOU 1244 C VAL A 157 12289 8269 8938 -576 -163 298 C ATOM 1245 O VAL A 157 13.245 29.909 26.504 1.00 68.29 O ANISOU 1245 O VAL A 157 11046 7188 7712 -449 -169 487 O ATOM 1246 CB VAL A 157 13.463 26.717 27.437 1.00 61.84 C ANISOU 1246 CB VAL A 157 10328 5840 7330 -618 138 236 C ATOM 1247 CG1 VAL A 157 14.700 27.420 27.979 1.00 68.00 C ANISOU 1247 CG1 VAL A 157 11138 6623 8075 -432 267 425 C ATOM 1248 CG2 VAL A 157 12.936 25.706 28.443 1.00 54.81 C ANISOU 1248 CG2 VAL A 157 9347 4757 6723 -702 212 239 C ATOM 1249 N ALA A 158 12.916 28.459 24.815 1.00 71.19 N ANISOU 1249 N ALA A 158 11598 7515 7937 -645 -218 108 N ATOM 1250 CA ALA A 158 13.362 29.419 23.812 1.00 68.99 C ANISOU 1250 CA ALA A 158 11390 7440 7385 -570 -292 137 C ATOM 1251 C ALA A 158 12.410 30.602 23.703 1.00 78.88 C ANISOU 1251 C ALA A 158 12495 8913 8562 -578 -500 259 C ATOM 1252 O ALA A 158 12.839 31.710 23.360 1.00 66.81 O ANISOU 1252 O ALA A 158 10965 7537 6882 -468 -541 392 O ATOM 1253 CB ALA A 158 13.511 28.730 22.455 1.00 59.78 C ANISOU 1253 CB ALA A 158 10377 6308 6029 -659 -311 -107 C ATOM 1254 N PHE A 159 11.122 30.391 23.987 1.00 84.01 N ANISOU 1254 N PHE A 159 13015 9576 9331 -705 -630 220 N ATOM 1255 CA PHE A 159 10.168 31.493 23.948 1.00 80.49 C ANISOU 1255 CA PHE A 159 12412 9323 8845 -716 -826 341 C ATOM 1256 C PHE A 159 10.448 32.516 25.041 1.00 76.84 C ANISOU 1256 C PHE A 159 11826 8869 8501 -577 -778 586 C ATOM 1257 O PHE A 159 10.235 33.716 24.833 1.00 66.31 O ANISOU 1257 O PHE A 159 10403 7707 7084 -516 -892 721 O ATOM 1258 CB PHE A 159 8.741 30.958 24.071 1.00 62.59 C ANISOU 1258 CB PHE A 159 10030 7048 6703 -886 -963 237 C ATOM 1259 CG PHE A 159 7.691 32.032 24.111 1.00 60.73 C ANISOU 1259 CG PHE A 159 9617 6993 6462 -905 -1161 360 C ATOM 1260 CD1 PHE A 159 7.317 32.697 22.954 1.00 64.25 C ANISOU 1260 CD1 PHE A 159 10065 7662 6684 -931 -1341 346 C ATOM 1261 CD2 PHE A 159 7.073 32.372 25.303 1.00 57.78 C ANISOU 1261 CD2 PHE A 159 9069 6573 6313 -897 -1167 494 C ATOM 1262 CE1 PHE A 159 6.350 33.685 22.987 1.00 64.10 C ANISOU 1262 CE1 PHE A 159 9873 7801 6681 -947 -1523 470 C ATOM 1263 CE2 PHE A 159 6.106 33.359 25.343 1.00 67.33 C ANISOU 1263 CE2 PHE A 159 10106 7938 7537 -915 -1343 602 C ATOM 1264 CZ PHE A 159 5.744 34.016 24.183 1.00 66.42 C ANISOU 1264 CZ PHE A 159 9992 8030 7215 -938 -1522 593 C ATOM 1265 N THR A 160 10.926 32.067 26.204 1.00 67.46 N ANISOU 1265 N THR A 160 10622 7501 7510 -525 -609 646 N ATOM 1266 CA THR A 160 11.272 33.004 27.268 1.00 63.23 C ANISOU 1266 CA THR A 160 9968 6979 7077 -392 -550 861 C ATOM 1267 C THR A 160 12.499 33.828 26.898 1.00 76.90 C ANISOU 1267 C THR A 160 11786 8776 8658 -230 -477 961 C ATOM 1268 O THR A 160 12.569 35.022 27.211 1.00 89.28 O ANISOU 1268 O THR A 160 13244 10452 10225 -131 -516 1124 O ATOM 1269 CB THR A 160 11.511 32.252 28.578 1.00 70.49 C ANISOU 1269 CB THR A 160 10852 7706 8225 -382 -386 899 C ATOM 1270 OG1 THR A 160 12.564 31.296 28.398 1.00 78.63 O ANISOU 1270 OG1 THR A 160 12055 8579 9241 -354 -216 813 O ATOM 1271 CG2 THR A 160 10.248 31.529 29.017 1.00 51.47 C ANISOU 1271 CG2 THR A 160 8336 5237 5984 -538 -457 824 C ATOM 1272 N TRP A 161 13.475 33.208 26.230 1.00 78.01 N ANISOU 1272 N TRP A 161 12114 8846 8680 -203 -367 861 N ATOM 1273 CA ATRP A 161 14.674 33.936 25.828 0.61 69.89 C ANISOU 1273 CA ATRP A 161 11174 7873 7507 -51 -290 949 C ATOM 1274 CA BTRP A 161 14.673 33.940 25.830 0.39 69.74 C ANISOU 1274 CA BTRP A 161 11155 7854 7488 -51 -290 950 C ATOM 1275 C TRP A 161 14.355 34.986 24.770 1.00 77.22 C ANISOU 1275 C TRP A 161 12082 9027 8231 -39 -457 992 C ATOM 1276 O TRP A 161 14.933 36.079 24.777 1.00 78.88 O ANISOU 1276 O TRP A 161 12257 9324 8388 95 -446 1148 O ATOM 1277 CB ATRP A 161 15.733 32.960 25.314 0.61 64.27 C ANISOU 1277 CB ATRP A 161 10666 7030 6721 -37 -133 817 C ATOM 1278 CB BTRP A 161 15.740 32.969 25.324 0.39 64.71 C ANISOU 1278 CB BTRP A 161 10722 7087 6779 -35 -132 819 C ATOM 1279 CG ATRP A 161 16.201 31.970 26.342 0.61 62.74 C ANISOU 1279 CG ATRP A 161 10493 6609 6736 -29 47 804 C ATOM 1280 CG BTRP A 161 16.500 32.284 26.419 0.39 62.67 C ANISOU 1280 CG BTRP A 161 10483 6617 6711 24 68 857 C ATOM 1281 CD1ATRP A 161 15.902 31.965 27.674 0.61 59.36 C ANISOU 1281 CD1ATRP A 161 9926 6103 6524 -15 89 919 C ATOM 1282 CD1BTRP A 161 16.183 31.103 27.024 0.39 63.53 C ANISOU 1282 CD1BTRP A 161 10588 6550 7001 -69 139 771 C ATOM 1283 CD2ATRP A 161 17.052 30.838 26.118 0.61 59.66 C ANISOU 1283 CD2ATRP A 161 10263 6042 6361 -35 209 676 C ATOM 1284 CD2BTRP A 161 17.708 32.741 27.039 0.39 57.56 C ANISOU 1284 CD2BTRP A 161 9855 5917 6099 189 220 1001 C ATOM 1285 NE1ATRP A 161 16.514 30.901 28.293 0.61 62.61 N ANISOU 1285 NE1ATRP A 161 10401 6307 7079 -11 264 887 N ATOM 1286 NE1BTRP A 161 17.119 30.796 27.982 0.39 64.76 N ANISOU 1286 NE1BTRP A 161 10757 6553 7296 30 324 864 N ATOM 1287 CE2ATRP A 161 17.226 30.194 27.359 0.61 66.63 C ANISOU 1287 CE2ATRP A 161 11091 6744 7482 -22 341 738 C ATOM 1288 CE2BTRP A 161 18.066 31.786 28.011 0.39 67.01 C ANISOU 1288 CE2BTRP A 161 11058 6913 7490 187 375 1000 C ATOM 1289 CE3ATRP A 161 17.684 30.308 24.989 0.61 43.15 C ANISOU 1289 CE3ATRP A 161 8350 3935 4110 -52 260 515 C ATOM 1290 CE3BTRP A 161 18.522 33.865 26.867 0.39 33.63 C ANISOU 1290 CE3BTRP A 161 6830 2988 2962 338 241 1134 C ATOM 1291 CZ2ATRP A 161 18.004 29.047 27.503 0.61 58.84 C ANISOU 1291 CZ2ATRP A 161 10218 5548 6593 -22 518 656 C ATOM 1292 CZ2BTRP A 161 19.201 31.921 28.808 0.39 57.60 C ANISOU 1292 CZ2BTRP A 161 9827 5666 6392 322 531 1099 C ATOM 1293 CZ3ATRP A 161 18.456 29.169 25.133 0.61 52.94 C ANISOU 1293 CZ3ATRP A 161 9702 4961 5450 -54 440 415 C ATOM 1294 CZ3BTRP A 161 19.649 33.997 27.658 0.39 35.27 C ANISOU 1294 CZ3BTRP A 161 6881 3187 3333 447 385 1153 C ATOM 1295 CH2ATRP A 161 18.610 28.551 26.381 0.61 53.30 C ANISOU 1295 CH2ATRP A 161 9686 4816 5749 -37 567 492 C ATOM 1296 CH2BTRP A 161 19.978 33.030 28.617 0.39 43.11 C ANISOU 1296 CH2BTRP A 161 7830 4039 4513 433 511 1117 C ATOM 1297 N VAL A 162 13.437 34.674 23.852 1.00 79.68 N ANISOU 1297 N VAL A 162 12406 9439 8431 -177 -614 859 N ATOM 1298 CA VAL A 162 13.074 35.630 22.811 1.00 77.24 C ANISOU 1298 CA VAL A 162 12069 9360 7920 -174 -784 910 C ATOM 1299 C VAL A 162 12.316 36.810 23.407 1.00 85.06 C ANISOU 1299 C VAL A 162 12843 10452 9022 -139 -906 1097 C ATOM 1300 O VAL A 162 12.578 37.969 23.066 1.00 88.95 O ANISOU 1300 O VAL A 162 13285 11081 9429 -39 -958 1248 O ATOM 1301 CB VAL A 162 12.264 34.933 21.704 1.00 75.72 C ANISOU 1301 CB VAL A 162 11936 9257 7576 -339 -925 710 C ATOM 1302 CG1 VAL A 162 11.688 35.958 20.738 1.00 74.33 C ANISOU 1302 CG1 VAL A 162 11693 9339 7210 -348 -1127 790 C ATOM 1303 CG2 VAL A 162 13.136 33.935 20.961 1.00 66.58 C ANISOU 1303 CG2 VAL A 162 10993 8025 6281 -359 -800 522 C ATOM 1304 N MET A 163 11.367 36.537 24.308 1.00 85.96 N ANISOU 1304 N MET A 163 12821 10498 9343 -220 -948 1091 N ATOM 1305 CA MET A 163 10.626 37.620 24.947 1.00 87.78 C ANISOU 1305 CA MET A 163 12836 10813 9704 -192 -1052 1254 C ATOM 1306 C MET A 163 11.529 38.486 25.814 1.00 92.85 C ANISOU 1306 C MET A 163 13418 11418 10443 -21 -922 1429 C ATOM 1307 O MET A 163 11.317 39.701 25.905 1.00 79.99 O ANISOU 1307 O MET A 163 11646 9901 8844 49 -999 1580 O ATOM 1308 CB MET A 163 9.476 37.055 25.781 1.00 69.10 C ANISOU 1308 CB MET A 163 10342 8370 7543 -316 -1102 1199 C ATOM 1309 CG MET A 163 8.365 36.407 24.971 1.00 73.71 C ANISOU 1309 CG MET A 163 10933 9013 8060 -491 -1266 1041 C ATOM 1310 SD MET A 163 7.511 37.561 23.879 1.00 82.78 S ANISOU 1310 SD MET A 163 11976 10425 9051 -518 -1521 1119 S ATOM 1311 CE MET A 163 8.221 37.130 22.292 1.00 86.65 C ANISOU 1311 CE MET A 163 12693 11015 9214 -533 -1533 987 C ATOM 1312 N ALA A 164 12.535 37.887 26.456 1.00 89.63 N ANISOU 1312 N ALA A 164 13108 10852 10095 47 -724 1412 N ATOM 1313 CA ALA A 164 13.452 38.669 27.278 1.00 77.81 C ANISOU 1313 CA ALA A 164 11557 9323 8683 209 -596 1565 C ATOM 1314 C ALA A 164 14.390 39.506 26.418 1.00 80.54 C ANISOU 1314 C ALA A 164 11894 9797 8911 323 -556 1602 C ATOM 1315 O ALA A 164 14.657 40.671 26.734 1.00 76.35 O ANISOU 1315 O ALA A 164 11080 9394 8536 395 -514 1675 O ATOM 1316 CB ALA A 164 14.244 37.745 28.202 1.00 69.54 C ANISOU 1316 CB ALA A 164 10587 8087 7747 241 -396 1530 C ATOM 1317 N LEU A 165 14.904 38.930 25.327 1.00 79.37 N ANISOU 1317 N LEU A 165 11996 9634 8528 308 -556 1525 N ATOM 1318 CA LEU A 165 15.744 39.700 24.415 1.00 68.08 C ANISOU 1318 CA LEU A 165 10497 8351 7019 388 -516 1535 C ATOM 1319 C LEU A 165 14.951 40.795 23.714 1.00 75.40 C ANISOU 1319 C LEU A 165 11267 9488 7893 378 -684 1625 C ATOM 1320 O LEU A 165 15.507 41.851 23.392 1.00 82.29 O ANISOU 1320 O LEU A 165 11944 10489 8832 437 -644 1697 O ATOM 1321 CB LEU A 165 16.402 38.777 23.391 1.00 63.13 C ANISOU 1321 CB LEU A 165 10182 7670 6134 372 -473 1421 C ATOM 1322 CG LEU A 165 17.519 37.881 23.929 1.00 84.52 C ANISOU 1322 CG LEU A 165 13006 10187 8921 421 -259 1342 C ATOM 1323 CD1 LEU A 165 18.058 36.974 22.835 1.00 83.00 C ANISOU 1323 CD1 LEU A 165 13137 9945 8456 393 -216 1220 C ATOM 1324 CD2 LEU A 165 18.634 38.724 24.530 1.00 87.77 C ANISOU 1324 CD2 LEU A 165 13139 10639 9571 521 -129 1376 C ATOM 1325 N ALA A 166 13.658 40.576 23.483 1.00 66.69 N ANISOU 1325 N ALA A 166 10227 8416 6696 265 -891 1623 N ATOM 1326 CA ALA A 166 12.776 41.614 22.946 1.00 76.56 C ANISOU 1326 CA ALA A 166 11287 9859 7942 258 -1051 1705 C ATOM 1327 C ALA A 166 12.387 42.643 23.990 1.00 94.97 C ANISOU 1327 C ALA A 166 13337 12199 10550 351 -998 1788 C ATOM 1328 O ALA A 166 11.460 43.445 23.777 1.00 95.89 O ANISOU 1328 O ALA A 166 13315 12412 10708 341 -1127 1823 O ATOM 1329 CB ALA A 166 11.518 40.982 22.352 1.00 59.70 C ANISOU 1329 CB ALA A 166 9241 7779 5665 67 -1294 1634 C ATOM 1330 N CYS A 167 13.084 42.617 25.123 1.00 94.91 N ANISOU 1330 N CYS A 167 13250 12083 10728 435 -802 1791 N ATOM 1331 CA CYS A 167 12.811 43.527 26.233 1.00 92.60 C ANISOU 1331 CA CYS A 167 12813 11731 10641 546 -727 1765 C ATOM 1332 C CYS A 167 14.054 44.190 26.813 1.00 93.58 C ANISOU 1332 C CYS A 167 13029 11639 10890 506 -675 1576 C ATOM 1333 O CYS A 167 13.956 45.329 27.278 1.00 85.38 O ANISOU 1333 O CYS A 167 11855 10606 9979 537 -683 1554 O ATOM 1334 CB CYS A 167 12.072 42.773 27.351 1.00 87.02 C ANISOU 1334 CB CYS A 167 12066 10922 10075 426 -766 1769 C ATOM 1335 SG CYS A 167 12.078 43.568 28.967 1.00117.04 S ANISOU 1335 SG CYS A 167 15729 14624 14117 488 -659 1683 S ATOM 1336 N ALA A 168 15.209 43.524 26.809 1.00 86.06 N ANISOU 1336 N ALA A 168 11904 10757 10036 340 -622 1692 N ATOM 1337 CA ALA A 168 16.443 44.065 27.365 1.00 81.43 C ANISOU 1337 CA ALA A 168 11300 10083 9556 364 -535 1591 C ATOM 1338 C ALA A 168 17.410 44.582 26.305 1.00 88.67 C ANISOU 1338 C ALA A 168 12237 11061 10391 388 -515 1608 C ATOM 1339 O ALA A 168 18.350 45.312 26.645 1.00 91.50 O ANISOU 1339 O ALA A 168 12550 11390 10827 467 -420 1542 O ATOM 1340 CB ALA A 168 17.143 42.993 28.212 1.00 68.99 C ANISOU 1340 CB ALA A 168 9735 8441 8038 385 -391 1562 C ATOM 1341 N ALA A 169 17.202 44.226 25.038 1.00 90.26 N ANISOU 1341 N ALA A 169 12329 11519 10445 -1535 -994 2465 N ATOM 1342 CA ALA A 169 18.087 44.644 23.953 1.00 80.15 C ANISOU 1342 CA ALA A 169 11095 10275 9084 -1698 -991 2550 C ATOM 1343 C ALA A 169 17.720 45.999 23.341 1.00 83.18 C ANISOU 1343 C ALA A 169 11512 10445 9647 -1778 -1163 2718 C ATOM 1344 O ALA A 169 18.631 46.744 22.956 1.00 88.06 O ANISOU 1344 O ALA A 169 12155 11034 10269 -1906 -1167 2771 O ATOM 1345 CB ALA A 169 18.127 43.578 22.854 1.00 54.98 C ANISOU 1345 CB ALA A 169 7903 7265 5722 -1692 -902 2477 C ATOM 1346 N PRO A 170 16.440 46.356 23.201 1.00 73.08 N ANISOU 1346 N PRO A 170 10231 9022 8515 -1704 -1301 2796 N ATOM 1347 CA PRO A 170 16.095 47.685 22.656 1.00 82.13 C ANISOU 1347 CA PRO A 170 11406 9959 9841 -1759 -1457 2944 C ATOM 1348 C PRO A 170 16.773 48.830 23.396 1.00 79.42 C ANISOU 1348 C PRO A 170 11081 9428 9666 -1819 -1499 2983 C ATOM 1349 O PRO A 170 17.182 49.808 22.752 1.00 74.33 O ANISOU 1349 O PRO A 170 10472 8684 9085 -1928 -1556 3078 O ATOM 1350 CB PRO A 170 14.568 47.740 22.805 1.00 81.40 C ANISOU 1350 CB PRO A 170 11288 9752 9890 -1621 -1579 2978 C ATOM 1351 CG PRO A 170 14.156 46.336 22.635 1.00 79.36 C ANISOU 1351 CG PRO A 170 11003 9701 9450 -1557 -1482 2879 C ATOM 1352 CD PRO A 170 15.238 45.498 23.274 1.00 60.85 C ANISOU 1352 CD PRO A 170 8652 7520 6947 -1573 -1313 2751 C ATOM 1353 N PRO A 171 16.914 48.780 24.729 1.00 70.73 N ANISOU 1353 N PRO A 171 9906 8300 8669 -1698 -1430 2792 N ATOM 1354 CA PRO A 171 17.668 49.853 25.406 1.00 54.00 C ANISOU 1354 CA PRO A 171 7762 6038 6716 -1730 -1425 2721 C ATOM 1355 C PRO A 171 19.131 49.940 24.997 1.00 79.32 C ANISOU 1355 C PRO A 171 11009 9361 9767 -1920 -1331 2750 C ATOM 1356 O PRO A 171 19.774 50.954 25.298 1.00109.54 O ANISOU 1356 O PRO A 171 14836 13059 13725 -1992 -1345 2736 O ATOM 1357 CB PRO A 171 17.526 49.504 26.892 1.00 69.08 C ANISOU 1357 CB PRO A 171 9558 7971 8721 -1537 -1335 2458 C ATOM 1358 CG PRO A 171 16.262 48.755 26.971 1.00 72.80 C ANISOU 1358 CG PRO A 171 10000 8469 9191 -1385 -1372 2442 C ATOM 1359 CD PRO A 171 16.229 47.928 25.723 1.00 67.79 C ANISOU 1359 CD PRO A 171 9445 7996 8315 -1497 -1366 2599 C ATOM 1360 N LEU A 172 19.676 48.926 24.328 1.00 82.61 N ANISOU 1360 N LEU A 172 11460 10018 9910 -2005 -1236 2785 N ATOM 1361 CA LEU A 172 21.056 48.967 23.863 1.00 72.40 C ANISOU 1361 CA LEU A 172 10204 8857 8449 -2188 -1148 2821 C ATOM 1362 C LEU A 172 21.194 49.495 22.441 1.00 85.20 C ANISOU 1362 C LEU A 172 11868 10464 10039 -2295 -1215 2942 C ATOM 1363 O LEU A 172 22.322 49.724 21.992 1.00103.77 O ANISOU 1363 O LEU A 172 14230 12905 12293 -2422 -1155 2939 O ATOM 1364 CB LEU A 172 21.687 47.572 23.939 1.00 58.71 C ANISOU 1364 CB LEU A 172 8439 7420 6448 -2156 -974 2688 C ATOM 1365 CG LEU A 172 21.781 46.905 25.312 1.00 59.79 C ANISOU 1365 CG LEU A 172 8481 7645 6592 -1984 -847 2446 C ATOM 1366 CD1 LEU A 172 22.494 45.568 25.200 1.00 63.74 C ANISOU 1366 CD1 LEU A 172 8981 8434 6804 -1986 -680 2369 C ATOM 1367 CD2 LEU A 172 22.489 47.808 26.306 1.00 54.22 C ANISOU 1367 CD2 LEU A 172 7709 6848 6045 -1978 -817 2312 C ATOM 1368 N VAL A 173 20.086 49.695 21.723 1.00 86.11 N ANISOU 1368 N VAL A 173 11999 10485 10234 -2237 -1333 3034 N ATOM 1369 CA VAL A 173 20.132 50.104 20.326 1.00 81.60 C ANISOU 1369 CA VAL A 173 11457 9927 9620 -2321 -1389 3137 C ATOM 1370 C VAL A 173 19.332 51.367 20.046 1.00 84.57 C ANISOU 1370 C VAL A 173 11868 10050 10217 -2320 -1552 3282 C ATOM 1371 O VAL A 173 19.247 51.784 18.890 1.00 91.38 O ANISOU 1371 O VAL A 173 12754 10909 11055 -2381 -1609 3385 O ATOM 1372 CB VAL A 173 19.668 48.967 19.392 1.00 88.93 C ANISOU 1372 CB VAL A 173 12364 11048 10377 -2267 -1347 3098 C ATOM 1373 CG1 VAL A 173 20.660 47.814 19.428 1.00 90.01 C ANISOU 1373 CG1 VAL A 173 12472 11429 10299 -2275 -1179 2949 C ATOM 1374 CG2 VAL A 173 18.278 48.494 19.781 1.00 84.98 C ANISOU 1374 CG2 VAL A 173 11842 10499 9949 -2119 -1401 3083 C ATOM 1375 N GLY A 174 18.734 51.992 21.058 1.00 73.83 N ANISOU 1375 N GLY A 174 10505 8470 9078 -2242 -1630 3290 N ATOM 1376 CA GLY A 174 18.107 53.281 20.838 1.00 74.69 C ANISOU 1376 CA GLY A 174 10646 8324 9411 -2234 -1776 3410 C ATOM 1377 C GLY A 174 16.683 53.437 21.329 1.00 92.12 C ANISOU 1377 C GLY A 174 12828 10369 11803 -2064 -1889 3421 C ATOM 1378 O GLY A 174 16.136 54.542 21.281 1.00103.12 O ANISOU 1378 O GLY A 174 14243 11536 13402 -2033 -2006 3503 O ATOM 1379 N TRP A 175 16.061 52.356 21.792 1.00 88.26 N ANISOU 1379 N TRP A 175 12294 9997 11245 -1946 -1853 3334 N ATOM 1380 CA TRP A 175 14.709 52.410 22.340 1.00 72.59 C ANISOU 1380 CA TRP A 175 10273 7881 9426 -1773 -1954 3326 C ATOM 1381 C TRP A 175 14.816 52.358 23.860 1.00 81.78 C ANISOU 1381 C TRP A 175 11403 8939 10730 -1686 -1936 3216 C ATOM 1382 O TRP A 175 15.090 51.297 24.430 1.00 83.85 O ANISOU 1382 O TRP A 175 11608 9395 10855 -1628 -1803 3048 O ATOM 1383 CB TRP A 175 13.848 51.268 21.805 1.00 73.49 C ANISOU 1383 CB TRP A 175 10354 8188 9380 -1698 -1934 3302 C ATOM 1384 CG TRP A 175 12.380 51.529 21.941 1.00 86.54 C ANISOU 1384 CG TRP A 175 11974 9717 11191 -1546 -2059 3331 C ATOM 1385 CD1 TRP A 175 11.788 52.708 22.289 1.00 88.62 C ANISOU 1385 CD1 TRP A 175 12236 9727 11707 -1471 -2186 3382 C ATOM 1386 CD2 TRP A 175 11.315 50.592 21.733 1.00 91.43 C ANISOU 1386 CD2 TRP A 175 12551 10465 11725 -1446 -2062 3296 C ATOM 1387 NE1 TRP A 175 10.422 52.565 22.310 1.00 94.17 N ANISOU 1387 NE1 TRP A 175 12893 10407 12481 -1325 -2270 3382 N ATOM 1388 CE2 TRP A 175 10.106 51.275 21.973 1.00 95.90 C ANISOU 1388 CE2 TRP A 175 13085 10857 12493 -1315 -2198 3334 C ATOM 1389 CE3 TRP A 175 11.268 49.243 21.369 1.00 80.34 C ANISOU 1389 CE3 TRP A 175 11128 9303 10094 -1456 -1958 3227 C ATOM 1390 CZ2 TRP A 175 8.864 50.655 21.859 1.00 89.11 C ANISOU 1390 CZ2 TRP A 175 12176 10072 11609 -1202 -2234 3312 C ATOM 1391 CZ3 TRP A 175 10.033 48.629 21.256 1.00 77.71 C ANISOU 1391 CZ3 TRP A 175 10753 9029 9745 -1350 -1994 3205 C ATOM 1392 CH2 TRP A 175 8.848 49.335 21.501 1.00 81.99 C ANISOU 1392 CH2 TRP A 175 11262 9406 10483 -1229 -2133 3251 C ATOM 1393 N SER A 176 14.592 53.506 24.507 1.00 90.78 N ANISOU 1393 N SER A 176 12528 9826 12140 -1622 -2016 3187 N ATOM 1394 CA SER A 176 14.875 53.709 25.926 1.00 89.66 C ANISOU 1394 CA SER A 176 12294 9630 12145 -1505 -1940 2938 C ATOM 1395 C SER A 176 16.372 53.561 26.179 1.00 86.19 C ANISOU 1395 C SER A 176 11851 9319 11580 -1638 -1790 2838 C ATOM 1396 O SER A 176 17.166 53.564 25.232 1.00 88.73 O ANISOU 1396 O SER A 176 12250 9719 11744 -1828 -1770 2981 O ATOM 1397 CB SER A 176 14.069 52.744 26.803 1.00 82.11 C ANISOU 1397 CB SER A 176 11235 8785 11177 -1299 -1889 2751 C ATOM 1398 OG SER A 176 14.267 53.018 28.179 1.00 81.87 O ANISOU 1398 OG SER A 176 11110 8694 11301 -1177 -1828 2518 O ATOM 1399 N ARG A 177 16.774 53.439 27.441 1.00 72.14 N ANISOU 1399 N ARG A 177 9976 7573 9861 -1540 -1687 2593 N ATOM 1400 CA ARG A 177 18.192 53.395 27.773 1.00 64.97 C ANISOU 1400 CA ARG A 177 9051 6784 8849 -1655 -1548 2486 C ATOM 1401 C ARG A 177 18.363 52.844 29.181 1.00 71.57 C ANISOU 1401 C ARG A 177 9763 7729 9703 -1495 -1424 2204 C ATOM 1402 O ARG A 177 17.402 52.715 29.944 1.00 74.80 O ANISOU 1402 O ARG A 177 10101 8077 10242 -1305 -1457 2096 O ATOM 1403 CB ARG A 177 18.830 54.783 27.654 1.00 55.92 C ANISOU 1403 CB ARG A 177 7955 5426 7865 -1795 -1605 2555 C ATOM 1404 CG ARG A 177 18.200 55.822 28.564 1.00 63.64 C ANISOU 1404 CG ARG A 177 8890 6135 9157 -1667 -1692 2460 C ATOM 1405 CD ARG A 177 18.933 57.150 28.492 1.00 81.67 C ANISOU 1405 CD ARG A 177 11227 8212 11593 -1817 -1728 2510 C ATOM 1406 NE ARG A 177 18.375 58.124 29.425 1.00 87.76 N ANISOU 1406 NE ARG A 177 11955 8726 12665 -1690 -1800 2398 N ATOM 1407 CZ ARG A 177 18.870 59.340 29.622 1.00 77.61 C ANISOU 1407 CZ ARG A 177 10702 7223 11562 -1784 -1831 2394 C ATOM 1408 NH1 ARG A 177 19.942 59.738 28.950 1.00 94.34 N ANISOU 1408 NH1 ARG A 177 12897 9355 13593 -2013 -1797 2502 N ATOM 1409 NH2 ARG A 177 18.296 60.158 30.492 1.00 82.21 N ANISOU 1409 NH2 ARG A 177 11243 7577 12417 -1652 -1895 2280 N ATOM 1410 N TYR A 178 19.612 52.523 29.516 1.00 58.05 N ANISOU 1410 N TYR A 178 8019 6188 7849 -1575 -1278 2089 N ATOM 1411 CA TYR A 178 19.992 52.069 30.848 1.00 68.35 C ANISOU 1411 CA TYR A 178 9203 7614 9153 -1443 -1147 1824 C ATOM 1412 C TYR A 178 20.747 53.188 31.552 1.00 71.07 C ANISOU 1412 C TYR A 178 9510 7829 9666 -1498 -1137 1717 C ATOM 1413 O TYR A 178 21.773 53.659 31.050 1.00 90.69 O ANISOU 1413 O TYR A 178 12045 10327 12086 -1689 -1110 1786 O ATOM 1414 CB TYR A 178 20.859 50.810 30.783 1.00 74.80 C ANISOU 1414 CB TYR A 178 10002 8745 9674 -1473 -978 1757 C ATOM 1415 CG TYR A 178 20.128 49.561 30.346 1.00 66.54 C ANISOU 1415 CG TYR A 178 8976 7845 8463 -1390 -958 1805 C ATOM 1416 CD1 TYR A 178 19.089 49.040 31.106 1.00 67.78 C ANISOU 1416 CD1 TYR A 178 9063 7993 8697 -1183 -964 1691 C ATOM 1417 CD2 TYR A 178 20.491 48.892 29.185 1.00 63.22 C ANISOU 1417 CD2 TYR A 178 8641 7576 7802 -1524 -930 1958 C ATOM 1418 CE1 TYR A 178 18.423 47.895 30.714 1.00 72.52 C ANISOU 1418 CE1 TYR A 178 9683 8724 9147 -1119 -940 1730 C ATOM 1419 CE2 TYR A 178 19.833 47.745 28.787 1.00 76.92 C ANISOU 1419 CE2 TYR A 178 10396 9442 9386 -1456 -907 1992 C ATOM 1420 CZ TYR A 178 18.799 47.253 29.553 1.00 76.11 C ANISOU 1420 CZ TYR A 178 10227 9320 9369 -1257 -911 1878 C ATOM 1421 OH TYR A 178 18.140 46.112 29.160 1.00 62.19 O ANISOU 1421 OH TYR A 178 8487 7684 7457 -1200 -884 1907 O ATOM 1422 N ILE A 179 20.237 53.614 32.703 1.00 57.05 N ANISOU 1422 N ILE A 179 7643 5931 8103 -1337 -1157 1545 N ATOM 1423 CA ILE A 179 20.909 54.614 33.533 1.00 63.96 C ANISOU 1423 CA ILE A 179 8465 6693 9144 -1370 -1136 1402 C ATOM 1424 C ILE A 179 20.846 54.170 34.985 1.00 57.07 C ANISOU 1424 C ILE A 179 7446 5927 8312 -1175 -1038 1129 C ATOM 1425 O ILE A 179 19.986 53.365 35.370 1.00 56.54 O ANISOU 1425 O ILE A 179 7328 5932 8223 -997 -1031 1070 O ATOM 1426 CB ILE A 179 20.280 56.017 33.380 1.00 64.29 C ANISOU 1426 CB ILE A 179 8561 6391 9475 -1390 -1299 1498 C ATOM 1427 CG1 ILE A 179 18.848 56.035 33.916 1.00 53.80 C ANISOU 1427 CG1 ILE A 179 7186 4927 8330 -1167 -1397 1452 C ATOM 1428 CG2 ILE A 179 20.315 56.480 31.929 1.00 64.51 C ANISOU 1428 CG2 ILE A 179 8735 6311 9463 -1578 -1399 1783 C ATOM 1429 CD1 ILE A 179 18.211 57.406 33.868 1.00 67.64 C ANISOU 1429 CD1 ILE A 179 8986 6340 10374 -1160 -1552 1527 C ATOM 1430 N PRO A 180 21.768 54.662 35.815 1.00 51.46 N ANISOU 1430 N PRO A 180 6662 5240 7651 -1210 -958 955 N ATOM 1431 CA PRO A 180 21.688 54.370 37.252 1.00 54.32 C ANISOU 1431 CA PRO A 180 6877 5690 8072 -1022 -874 691 C ATOM 1432 C PRO A 180 20.383 54.877 37.847 1.00 62.41 C ANISOU 1432 C PRO A 180 7863 6493 9357 -842 -993 642 C ATOM 1433 O PRO A 180 19.841 55.904 37.433 1.00 92.53 O ANISOU 1433 O PRO A 180 11748 10036 13374 -884 -1135 758 O ATOM 1434 CB PRO A 180 22.896 55.112 37.834 1.00 57.55 C ANISOU 1434 CB PRO A 180 7233 6113 8520 -1133 -799 551 C ATOM 1435 CG PRO A 180 23.856 55.208 36.700 1.00 48.68 C ANISOU 1435 CG PRO A 180 6214 5049 7232 -1374 -780 722 C ATOM 1436 CD PRO A 180 23.015 55.366 35.466 1.00 60.99 C ANISOU 1436 CD PRO A 180 7910 6442 8822 -1431 -921 987 C ATOM 1437 N GLU A 181 19.878 54.138 38.832 1.00 55.98 N ANISOU 1437 N GLU A 181 6934 5801 8534 -636 -933 469 N ATOM 1438 CA GLU A 181 18.588 54.422 39.441 1.00 60.36 C ANISOU 1438 CA GLU A 181 7438 6192 9305 -445 -1033 411 C ATOM 1439 C GLU A 181 18.735 54.531 40.952 1.00 55.85 C ANISOU 1439 C GLU A 181 6712 5674 8835 -296 -957 133 C ATOM 1440 O GLU A 181 19.696 54.031 41.543 1.00 77.61 O ANISOU 1440 O GLU A 181 9390 8651 11446 -303 -810 -14 O ATOM 1441 CB GLU A 181 17.558 53.338 39.099 1.00 50.16 C ANISOU 1441 CB GLU A 181 6159 4994 7906 -323 -1052 491 C ATOM 1442 CG GLU A 181 17.942 51.949 39.583 1.00 88.44 C ANISOU 1442 CG GLU A 181 10936 10151 12517 -241 -886 372 C ATOM 1443 CD GLU A 181 17.007 50.871 39.071 1.00120.86 C ANISOU 1443 CD GLU A 181 15077 14344 16500 -161 -900 473 C ATOM 1444 OE1 GLU A 181 15.977 51.218 38.456 1.00139.68 O ANISOU 1444 OE1 GLU A 181 17520 16556 18994 -148 -1044 617 O ATOM 1445 OE2 GLU A 181 17.305 49.677 39.282 1.00117.24 O ANISOU 1445 OE2 GLU A 181 14587 14127 15831 -110 -766 408 O ATOM 1446 N GLY A 182 17.756 55.192 41.569 1.00 57.75 N ANISOU 1446 N GLY A 182 6902 5716 9322 -154 -1060 62 N ATOM 1447 CA GLY A 182 17.695 55.333 43.011 1.00 54.66 C ANISOU 1447 CA GLY A 182 6360 5360 9050 7 -1007 -199 C ATOM 1448 C GLY A 182 18.951 55.910 43.626 1.00 57.71 C ANISOU 1448 C GLY A 182 6687 5792 9447 -91 -915 -358 C ATOM 1449 O GLY A 182 19.264 57.089 43.434 1.00 72.11 O ANISOU 1449 O GLY A 182 8561 7404 11435 -213 -985 -332 O ATOM 1450 N MET A 183 19.681 55.082 44.370 1.00 64.50 N ANISOU 1450 N MET A 183 7442 6934 10133 -40 -756 -523 N ATOM 1451 CA MET A 183 20.950 55.481 44.963 1.00 52.89 C ANISOU 1451 CA MET A 183 5900 5564 8631 -133 -651 -682 C ATOM 1452 C MET A 183 22.113 55.392 43.981 1.00 52.31 C ANISOU 1452 C MET A 183 5924 5587 8364 -365 -593 -547 C ATOM 1453 O MET A 183 23.271 55.425 44.411 1.00 62.61 O ANISOU 1453 O MET A 183 7163 7055 9571 -444 -477 -674 O ATOM 1454 CB MET A 183 21.234 54.633 46.205 1.00 78.05 C ANISOU 1454 CB MET A 183 8923 9027 11705 34 -504 -917 C ATOM 1455 CG MET A 183 20.332 54.966 47.385 1.00 69.16 C ANISOU 1455 CG MET A 183 7675 7812 10793 243 -548 -1100 C ATOM 1456 SD MET A 183 20.490 53.809 48.758 1.00 81.02 S ANISOU 1456 SD MET A 183 8990 9651 12142 459 -380 -1340 S ATOM 1457 CE MET A 183 19.721 52.352 48.057 1.00 92.59 C ANISOU 1457 CE MET A 183 10530 11243 13408 545 -363 -1167 C ATOM 1458 N GLN A 184 21.821 55.269 42.684 1.00 59.31 N ANISOU 1458 N GLN A 184 6956 6390 9187 -474 -670 -297 N ATOM 1459 CA GLN A 184 22.818 55.361 41.616 1.00 54.15 C ANISOU 1459 CA GLN A 184 6410 5784 8380 -711 -644 -140 C ATOM 1460 C GLN A 184 23.872 54.261 41.713 1.00 55.15 C ANISOU 1460 C GLN A 184 6488 6260 8207 -736 -469 -205 C ATOM 1461 O GLN A 184 25.019 54.449 41.300 1.00 83.48 O ANISOU 1461 O GLN A 184 10105 9940 11673 -919 -406 -177 O ATOM 1462 CB GLN A 184 23.486 56.740 41.603 1.00 64.51 C ANISOU 1462 CB GLN A 184 7749 6904 9859 -882 -688 -159 C ATOM 1463 CG GLN A 184 22.507 57.907 41.606 1.00 54.43 C ANISOU 1463 CG GLN A 184 6519 5269 8894 -847 -853 -112 C ATOM 1464 CD GLN A 184 21.547 57.870 40.431 1.00 64.45 C ANISOU 1464 CD GLN A 184 7926 6377 10186 -862 -988 153 C ATOM 1465 OE1 GLN A 184 21.959 57.956 39.274 1.00 71.51 O ANISOU 1465 OE1 GLN A 184 8942 7252 10978 -1045 -1014 359 O ATOM 1466 NE2 GLN A 184 20.259 57.739 40.725 1.00 70.23 N ANISOU 1466 NE2 GLN A 184 8632 7006 11046 -668 -1075 148 N ATOM 1467 N CYS A 185 23.495 53.100 42.252 1.00 65.68 N ANISOU 1467 N CYS A 185 7748 7792 9415 -552 -387 -291 N ATOM 1468 CA CYS A 185 24.406 51.969 42.351 1.00 63.07 C ANISOU 1468 CA CYS A 185 7376 7791 8796 -548 -218 -346 C ATOM 1469 C CYS A 185 24.043 50.809 41.436 1.00 68.39 C ANISOU 1469 C CYS A 185 8143 8578 9265 -537 -201 -178 C ATOM 1470 O CYS A 185 24.898 49.954 41.185 1.00 85.07 O ANISOU 1470 O CYS A 185 10260 10938 11124 -582 -74 -172 O ATOM 1471 CB CYS A 185 24.471 51.459 43.798 1.00 58.81 C ANISOU 1471 CB CYS A 185 6670 7433 8243 -345 -103 -600 C ATOM 1472 SG CYS A 185 25.249 52.614 44.950 1.00 69.56 S ANISOU 1472 SG CYS A 185 7897 8762 9770 -373 -74 -838 S ATOM 1473 N SER A 186 22.811 50.759 40.936 1.00 69.41 N ANISOU 1473 N SER A 186 8341 8538 9493 -479 -322 -46 N ATOM 1474 CA SER A 186 22.384 49.739 39.992 1.00 60.28 C ANISOU 1474 CA SER A 186 7280 7467 8158 -484 -320 120 C ATOM 1475 C SER A 186 21.709 50.407 38.804 1.00 68.91 C ANISOU 1475 C SER A 186 8506 8319 9358 -604 -488 353 C ATOM 1476 O SER A 186 21.058 51.446 38.943 1.00 64.70 O ANISOU 1476 O SER A 186 7975 7534 9073 -589 -619 367 O ATOM 1477 CB SER A 186 21.433 48.726 40.646 1.00 63.19 C ANISOU 1477 CB SER A 186 7585 7922 8503 -260 -282 35 C ATOM 1478 OG SER A 186 20.356 49.382 41.292 1.00 98.85 O ANISOU 1478 OG SER A 186 12047 12236 13278 -130 -394 -29 O ATOM 1479 N CYS A 187 21.872 49.803 37.631 1.00 63.54 N ANISOU 1479 N CYS A 187 7934 7723 8484 -719 -482 535 N ATOM 1480 CA CYS A 187 21.356 50.357 36.390 1.00 62.48 C ANISOU 1480 CA CYS A 187 7930 7400 8411 -850 -630 773 C ATOM 1481 C CYS A 187 20.117 49.598 35.928 1.00 70.82 C ANISOU 1481 C CYS A 187 9027 8443 9436 -747 -691 876 C ATOM 1482 O CYS A 187 20.002 48.384 36.115 1.00 82.11 O ANISOU 1482 O CYS A 187 10431 10071 10696 -651 -590 820 O ATOM 1483 CB CYS A 187 22.429 50.330 35.298 1.00 53.57 C ANISOU 1483 CB CYS A 187 6896 6369 7089 -1075 -592 920 C ATOM 1484 SG CYS A 187 23.638 51.665 35.455 1.00 82.84 S ANISOU 1484 SG CYS A 187 10594 9984 10899 -1258 -590 880 S ATOM 1485 N GLY A 188 19.190 50.331 35.323 1.00 66.52 N ANISOU 1485 N GLY A 188 8548 7666 9059 -770 -857 1026 N ATOM 1486 CA GLY A 188 17.959 49.745 34.847 1.00 46.72 C ANISOU 1486 CA GLY A 188 6076 5135 6540 -683 -933 1129 C ATOM 1487 C GLY A 188 17.316 50.597 33.775 1.00 61.34 C ANISOU 1487 C GLY A 188 8031 6765 8509 -782 -1109 1356 C ATOM 1488 O GLY A 188 17.895 51.576 33.300 1.00 66.21 O ANISOU 1488 O GLY A 188 8707 7253 9195 -933 -1164 1451 O ATOM 1489 N ILE A 189 16.096 50.207 33.402 1.00 70.59 N ANISOU 1489 N ILE A 189 9223 7900 9700 -694 -1195 1443 N ATOM 1490 CA ILE A 189 15.363 50.904 32.352 1.00 72.02 C ANISOU 1490 CA ILE A 189 9496 7893 9974 -766 -1364 1668 C ATOM 1491 C ILE A 189 14.976 52.298 32.828 1.00 78.20 C ANISOU 1491 C ILE A 189 10259 8397 11056 -720 -1487 1650 C ATOM 1492 O ILE A 189 14.605 52.499 33.993 1.00 80.45 O ANISOU 1492 O ILE A 189 10442 8627 11499 -559 -1478 1465 O ATOM 1493 CB ILE A 189 14.129 50.083 31.936 1.00 73.49 C ANISOU 1493 CB ILE A 189 9691 8134 10099 -670 -1418 1741 C ATOM 1494 CG1 ILE A 189 14.564 48.798 31.229 1.00 70.81 C ANISOU 1494 CG1 ILE A 189 9399 8045 9459 -753 -1308 1793 C ATOM 1495 CG2 ILE A 189 13.199 50.895 31.043 1.00 65.81 C ANISOU 1495 CG2 ILE A 189 8789 6956 9258 -702 -1606 1952 C ATOM 1496 CD1 ILE A 189 13.413 47.937 30.763 1.00 73.30 C ANISOU 1496 CD1 ILE A 189 9728 8428 9696 -682 -1350 1861 C ATOM 1497 N ASP A 190 15.072 53.274 31.926 1.00 74.91 N ANISOU 1497 N ASP A 190 9941 7801 10719 -860 -1600 1843 N ATOM 1498 CA ASP A 190 14.756 54.660 32.249 1.00 70.06 C ANISOU 1498 CA ASP A 190 9330 6900 10389 -834 -1719 1850 C ATOM 1499 C ASP A 190 13.248 54.879 32.173 1.00 77.33 C ANISOU 1499 C ASP A 190 10243 7674 11465 -680 -1867 1920 C ATOM 1500 O ASP A 190 12.641 54.708 31.110 1.00 83.28 O ANISOU 1500 O ASP A 190 11071 8422 12148 -723 -1956 2124 O ATOM 1501 CB ASP A 190 15.486 55.603 31.294 1.00 74.08 C ANISOU 1501 CB ASP A 190 9956 7275 10916 -1049 -1775 2039 C ATOM 1502 CG ASP A 190 15.407 57.058 31.727 1.00 73.43 C ANISOU 1502 CG ASP A 190 9882 6893 11124 -1041 -1869 2020 C ATOM 1503 OD1 ASP A 190 14.692 57.362 32.705 1.00 74.03 O ANISOU 1503 OD1 ASP A 190 9875 6858 11394 -860 -1905 1872 O ATOM 1504 OD2 ASP A 190 16.060 57.904 31.081 1.00 77.39 O ANISOU 1504 OD2 ASP A 190 10477 7267 11661 -1217 -1904 2155 O ATOM 1505 N TYR A 191 12.647 55.261 33.304 1.00 69.50 N ANISOU 1505 N TYR A 191 9154 6573 10678 -500 -1893 1747 N ATOM 1506 CA TYR A 191 11.243 55.654 33.333 1.00 70.94 C ANISOU 1506 CA TYR A 191 9321 6594 11039 -346 -2041 1799 C ATOM 1507 C TYR A 191 11.018 56.854 34.246 1.00 77.60 C ANISOU 1507 C TYR A 191 10116 7190 12178 -245 -2108 1681 C ATOM 1508 O TYR A 191 9.890 57.075 34.703 1.00109.10 O ANISOU 1508 O TYR A 191 14048 11078 16327 -67 -2199 1638 O ATOM 1509 CB TYR A 191 10.347 54.489 33.769 1.00 75.90 C ANISOU 1509 CB TYR A 191 9860 7404 11575 -180 -2004 1701 C ATOM 1510 CG TYR A 191 10.803 53.792 35.029 1.00 79.58 C ANISOU 1510 CG TYR A 191 10208 8039 11991 -81 -1850 1438 C ATOM 1511 CD1 TYR A 191 10.337 54.188 36.276 1.00 90.66 C ANISOU 1511 CD1 TYR A 191 11498 9356 13592 97 -1860 1241 C ATOM 1512 CD2 TYR A 191 11.697 52.734 34.971 1.00 68.69 C ANISOU 1512 CD2 TYR A 191 8828 6909 10362 -160 -1692 1387 C ATOM 1513 CE1 TYR A 191 10.753 53.548 37.429 1.00 85.46 C ANISOU 1513 CE1 TYR A 191 10726 8863 12881 190 -1718 1005 C ATOM 1514 CE2 TYR A 191 12.115 52.086 36.116 1.00 73.61 C ANISOU 1514 CE2 TYR A 191 9343 7692 10933 -62 -1549 1156 C ATOM 1515 CZ TYR A 191 11.642 52.497 37.342 1.00 83.87 C ANISOU 1515 CZ TYR A 191 10528 8909 12428 111 -1563 967 C ATOM 1516 OH TYR A 191 12.061 51.854 38.484 1.00 99.99 O ANISOU 1516 OH TYR A 191 12459 11121 14413 212 -1419 742 O ATOM 1517 N TYR A 192 12.066 57.627 34.524 1.00 96.74 N ANISOU 1517 N TYR A 192 12561 9520 14677 -356 -2062 1623 N ATOM 1518 CA TYR A 192 11.976 58.828 35.339 1.00105.64 C ANISOU 1518 CA TYR A 192 13655 10401 16085 -286 -2119 1510 C ATOM 1519 C TYR A 192 12.269 60.095 34.552 1.00100.56 C ANISOU 1519 C TYR A 192 13138 9491 15577 -435 -2221 1696 C ATOM 1520 O TYR A 192 11.978 61.192 35.042 1.00103.98 O ANISOU 1520 O TYR A 192 13569 9671 16267 -370 -2299 1645 O ATOM 1521 CB TYR A 192 12.940 58.726 36.531 1.00112.67 C ANISOU 1521 CB TYR A 192 14442 11395 16972 -278 -1972 1244 C ATOM 1522 CG TYR A 192 13.734 57.440 36.531 1.00129.17 C ANISOU 1522 CG TYR A 192 16498 13809 18773 -337 -1810 1182 C ATOM 1523 CD1 TYR A 192 14.979 57.371 35.922 1.00146.48 C ANISOU 1523 CD1 TYR A 192 18759 16096 20801 -549 -1728 1253 C ATOM 1524 CD2 TYR A 192 13.230 56.289 37.123 1.00138.62 C ANISOU 1524 CD2 TYR A 192 17596 15216 19857 -181 -1739 1057 C ATOM 1525 CE1 TYR A 192 15.703 56.196 35.911 1.00157.66 C ANISOU 1525 CE1 TYR A 192 20145 17807 21950 -593 -1580 1197 C ATOM 1526 CE2 TYR A 192 13.947 55.108 37.114 1.00145.16 C ANISOU 1526 CE2 TYR A 192 18401 16329 20423 -227 -1589 1006 C ATOM 1527 CZ TYR A 192 15.184 55.069 36.508 1.00155.26 C ANISOU 1527 CZ TYR A 192 19750 17698 21544 -429 -1510 1075 C ATOM 1528 OH TYR A 192 15.905 53.898 36.495 1.00154.34 O ANISOU 1528 OH TYR A 192 19612 17865 21165 -466 -1360 1023 O ATOM 1529 N THR A 193 12.837 59.972 33.352 1.00 82.31 N ANISOU 1529 N THR A 193 10941 7230 13101 -631 -2220 1908 N ATOM 1530 CA THR A 193 13.072 61.075 32.442 1.00 92.43 C ANISOU 1530 CA THR A 193 12357 8279 14484 -783 -2318 2124 C ATOM 1531 C THR A 193 12.335 60.828 31.132 1.00 93.66 C ANISOU 1531 C THR A 193 12605 8442 14541 -813 -2428 2401 C ATOM 1532 O THR A 193 12.281 59.688 30.658 1.00 86.00 O ANISOU 1532 O THR A 193 11624 7720 13333 -832 -2376 2445 O ATOM 1533 CB THR A 193 14.570 61.258 32.153 1.00 90.11 C ANISOU 1533 CB THR A 193 12117 8043 14076 -1020 -2214 2135 C ATOM 1534 OG1 THR A 193 15.046 60.157 31.368 1.00 73.40 O ANISOU 1534 OG1 THR A 193 10028 6203 11660 -1132 -2135 2229 O ATOM 1535 CG2 THR A 193 15.357 61.321 33.451 1.00 83.51 C ANISOU 1535 CG2 THR A 193 11174 7262 13293 -993 -2088 1847 C ATOM 1536 N PRO A 194 11.756 61.865 30.527 1.00 90.86 N ANISOU 1536 N PRO A 194 12341 7822 14360 -816 -2577 2589 N ATOM 1537 CA PRO A 194 11.010 61.664 29.278 1.00 80.75 C ANISOU 1537 CA PRO A 194 11138 6564 12980 -835 -2683 2852 C ATOM 1538 C PRO A 194 11.907 61.659 28.050 1.00 96.06 C ANISOU 1538 C PRO A 194 13180 8604 14713 -1074 -2640 3036 C ATOM 1539 O PRO A 194 11.454 62.012 26.958 1.00114.77 O ANISOU 1539 O PRO A 194 15605 10990 17013 -1102 -2695 3202 O ATOM 1540 CB PRO A 194 10.049 62.855 29.261 1.00 87.54 C ANISOU 1540 CB PRO A 194 12001 7217 14044 -704 -2786 2869 C ATOM 1541 CG PRO A 194 10.818 63.935 29.952 1.00 80.43 C ANISOU 1541 CG PRO A 194 11124 6084 13351 -760 -2765 2768 C ATOM 1542 CD PRO A 194 11.655 63.252 31.013 1.00 82.85 C ANISOU 1542 CD PRO A 194 11353 6481 13644 -778 -2654 2557 C ATOM 1543 N HIS A 195 13.168 61.250 28.229 1.00104.14 N ANISOU 1543 N HIS A 195 14210 9742 15615 -1232 -2521 2973 N ATOM 1544 CA HIS A 195 14.220 61.279 27.213 1.00 97.56 C ANISOU 1544 CA HIS A 195 13475 8987 14606 -1479 -2475 3136 C ATOM 1545 C HIS A 195 13.703 61.002 25.805 1.00 93.73 C ANISOU 1545 C HIS A 195 13035 8656 13923 -1508 -2512 3325 C ATOM 1546 O HIS A 195 13.555 59.842 25.406 1.00 91.03 O ANISOU 1546 O HIS A 195 12670 8555 13363 -1509 -2473 3349 O ATOM 1547 CB HIS A 195 15.310 60.269 27.581 1.00 85.39 C ANISOU 1547 CB HIS A 195 11872 7734 12837 -1564 -2299 2974 C ATOM 1548 CG HIS A 195 16.612 60.494 26.877 1.00 94.62 C ANISOU 1548 CG HIS A 195 13123 8957 13871 -1818 -2234 3078 C ATOM 1549 ND1 HIS A 195 17.052 59.686 25.851 1.00 98.35 N ANISOU 1549 ND1 HIS A 195 13643 9658 14067 -1956 -2190 3221 N ATOM 1550 CD2 HIS A 195 17.574 61.430 27.059 1.00 93.11 C ANISOU 1550 CD2 HIS A 195 12970 8629 13779 -1964 -2203 3055 C ATOM 1551 CE1 HIS A 195 18.228 60.116 25.428 1.00 85.94 C ANISOU 1551 CE1 HIS A 195 12133 8092 12428 -2173 -2137 3284 C ATOM 1552 NE2 HIS A 195 18.566 61.174 26.144 1.00 95.83 N ANISOU 1552 NE2 HIS A 195 13381 9125 13905 -2185 -2143 3187 N ATOM 1553 N GLU A 196 13.428 62.068 25.047 1.00102.42 N ANISOU 1553 N GLU A 196 14197 9618 15099 -1531 -2583 3452 N ATOM 1554 CA GLU A 196 12.811 61.925 23.732 1.00100.78 C ANISOU 1554 CA GLU A 196 14021 9529 14739 -1540 -2631 3623 C ATOM 1555 C GLU A 196 13.765 61.363 22.686 1.00 89.45 C ANISOU 1555 C GLU A 196 12632 8321 13033 -1738 -2549 3720 C ATOM 1556 O GLU A 196 13.300 60.845 21.665 1.00 96.72 O ANISOU 1556 O GLU A 196 13557 9411 13783 -1743 -2565 3822 O ATOM 1557 CB GLU A 196 12.265 63.272 23.249 1.00111.61 C ANISOU 1557 CB GLU A 196 15449 10678 16279 -1503 -2726 3734 C ATOM 1558 CG GLU A 196 10.985 63.728 23.937 1.00114.69 C ANISOU 1558 CG GLU A 196 15788 10900 16889 -1276 -2822 3669 C ATOM 1559 CD GLU A 196 11.237 64.378 25.283 1.00128.21 C ANISOU 1559 CD GLU A 196 17474 12391 18850 -1210 -2815 3497 C ATOM 1560 OE1 GLU A 196 12.417 64.604 25.627 1.00140.51 O ANISOU 1560 OE1 GLU A 196 19062 13902 20424 -1354 -2741 3444 O ATOM 1561 OE2 GLU A 196 10.254 64.657 26.002 1.00118.98 O ANISOU 1561 OE2 GLU A 196 16246 11105 17856 -1014 -2879 3405 O ATOM 1562 N GLU A 197 15.079 61.458 22.904 1.00 96.89 N ANISOU 1562 N GLU A 197 13603 9280 13931 -1902 -2458 3679 N ATOM 1563 CA GLU A 197 16.026 60.944 21.921 1.00103.42 C ANISOU 1563 CA GLU A 197 14465 10335 14495 -2084 -2375 3756 C ATOM 1564 C GLU A 197 15.926 59.434 21.755 1.00108.24 C ANISOU 1564 C GLU A 197 15024 11238 14864 -2062 -2309 3712 C ATOM 1565 O GLU A 197 16.322 58.909 20.708 1.00111.09 O ANISOU 1565 O GLU A 197 15404 11810 14997 -2164 -2262 3784 O ATOM 1566 CB GLU A 197 17.458 61.324 22.305 1.00103.16 C ANISOU 1566 CB GLU A 197 14460 10275 14462 -2258 -2283 3699 C ATOM 1567 CG GLU A 197 17.765 62.814 22.251 1.00109.76 C ANISOU 1567 CG GLU A 197 15361 10849 15495 -2325 -2325 3753 C ATOM 1568 CD GLU A 197 17.436 63.534 23.545 1.00121.33 C ANISOU 1568 CD GLU A 197 16802 12044 17255 -2216 -2365 3623 C ATOM 1569 OE1 GLU A 197 16.365 63.265 24.128 1.00115.91 O ANISOU 1569 OE1 GLU A 197 16061 11301 16678 -2023 -2429 3562 O ATOM 1570 OE2 GLU A 197 18.257 64.366 23.984 1.00133.18 O ANISOU 1570 OE2 GLU A 197 18332 13394 18877 -2322 -2329 3570 O ATOM 1571 N THR A 198 15.406 58.725 22.757 1.00102.78 N ANISOU 1571 N THR A 198 14268 10562 14221 -1926 -2302 3589 N ATOM 1572 CA THR A 198 15.293 57.273 22.707 1.00101.67 C ANISOU 1572 CA THR A 198 14083 10688 13859 -1896 -2230 3535 C ATOM 1573 C THR A 198 13.852 56.788 22.809 1.00104.78 C ANISOU 1573 C THR A 198 14425 11093 14293 -1706 -2305 3524 C ATOM 1574 O THR A 198 13.625 55.573 22.879 1.00 94.10 O ANISOU 1574 O THR A 198 13033 9944 12777 -1662 -2247 3465 O ATOM 1575 CB THR A 198 16.138 56.636 23.816 1.00 90.22 C ANISOU 1575 CB THR A 198 12600 9303 12377 -1924 -2122 3392 C ATOM 1576 OG1 THR A 198 15.819 57.244 25.073 1.00 93.79 O ANISOU 1576 OG1 THR A 198 13009 9527 13099 -1803 -2164 3272 O ATOM 1577 CG2 THR A 198 17.619 56.821 23.527 1.00 77.52 C ANISOU 1577 CG2 THR A 198 11031 7778 10646 -2133 -2021 3400 C ATOM 1578 N ASN A 199 12.877 57.700 22.818 1.00100.12 N ANISOU 1578 N ASN A 199 13835 10299 13909 -1593 -2426 3572 N ATOM 1579 CA ASN A 199 11.454 57.361 22.875 1.00 88.22 C ANISOU 1579 CA ASN A 199 12272 8801 12446 -1413 -2503 3562 C ATOM 1580 C ASN A 199 11.144 56.488 24.093 1.00 81.15 C ANISOU 1580 C ASN A 199 11301 7949 11584 -1278 -2469 3402 C ATOM 1581 O ASN A 199 10.734 55.331 23.981 1.00 87.49 O ANISOU 1581 O ASN A 199 12066 8955 12222 -1235 -2428 3368 O ATOM 1582 CB ASN A 199 11.001 56.682 21.578 1.00 80.41 C ANISOU 1582 CB ASN A 199 11289 8029 11234 -1454 -2501 3662 C ATOM 1583 CG ASN A 199 11.284 57.523 20.350 1.00 92.22 C ANISOU 1583 CG ASN A 199 12853 9489 12698 -1575 -2537 3821 C ATOM 1584 OD1 ASN A 199 10.485 58.379 19.971 1.00106.29 O ANISOU 1584 OD1 ASN A 199 14648 11129 14607 -1509 -2640 3913 O ATOM 1585 ND2 ASN A 199 12.427 57.281 19.718 1.00 93.40 N ANISOU 1585 ND2 ASN A 199 13043 9773 12672 -1748 -2451 3853 N ATOM 1586 N ASN A 200 11.349 57.073 25.275 1.00 78.50 N ANISOU 1586 N ASN A 200 10942 7413 11471 -1210 -2483 3296 N ATOM 1587 CA ASN A 200 11.112 56.336 26.512 1.00 83.92 C ANISOU 1587 CA ASN A 200 11534 8151 12199 -1062 -2431 3097 C ATOM 1588 C ASN A 200 9.626 56.108 26.761 1.00 84.30 C ANISOU 1588 C ASN A 200 11518 8173 12337 -857 -2528 3080 C ATOM 1589 O ASN A 200 9.258 55.148 27.447 1.00101.16 O ANISOU 1589 O ASN A 200 13560 10471 14403 -736 -2452 2908 O ATOM 1590 CB ASN A 200 11.740 57.075 27.694 1.00 84.65 C ANISOU 1590 CB ASN A 200 11578 8102 12484 -1025 -2376 2900 C ATOM 1591 CG ASN A 200 13.254 57.088 27.634 1.00 89.24 C ANISOU 1591 CG ASN A 200 12194 8768 12946 -1215 -2250 2864 C ATOM 1592 OD1 ASN A 200 13.847 56.833 26.586 1.00 84.49 O ANISOU 1592 OD1 ASN A 200 11674 8273 12156 -1392 -2231 3028 O ATOM 1593 ND2 ASN A 200 13.889 57.383 28.763 1.00 92.39 N ANISOU 1593 ND2 ASN A 200 12525 9131 13449 -1181 -2163 2646 N ATOM 1594 N GLU A 201 8.762 56.965 26.214 1.00 82.16 N ANISOU 1594 N GLU A 201 11261 7779 12176 -803 -2637 3173 N ATOM 1595 CA GLU A 201 7.331 56.827 26.462 1.00 80.83 C ANISOU 1595 CA GLU A 201 11016 7613 12084 -606 -2711 3125 C ATOM 1596 C GLU A 201 6.759 55.614 25.738 1.00 89.50 C ANISOU 1596 C GLU A 201 12095 8971 12941 -615 -2682 3168 C ATOM 1597 O GLU A 201 5.996 54.834 26.320 1.00 89.63 O ANISOU 1597 O GLU A 201 12030 9080 12944 -477 -2676 3063 O ATOM 1598 CB GLU A 201 6.598 58.103 26.048 1.00 82.80 C ANISOU 1598 CB GLU A 201 11286 7675 12499 -551 -2820 3209 C ATOM 1599 CG GLU A 201 5.086 58.017 26.186 1.00 96.48 C ANISOU 1599 CG GLU A 201 12940 9426 14290 -361 -2894 3172 C ATOM 1600 CD GLU A 201 4.408 59.362 26.018 1.00108.72 C ANISOU 1600 CD GLU A 201 14509 10768 16032 -283 -2995 3231 C ATOM 1601 OE1 GLU A 201 4.952 60.369 26.515 1.00117.50 O ANISOU 1601 OE1 GLU A 201 15653 11667 17326 -292 -3006 3198 O ATOM 1602 OE2 GLU A 201 3.332 59.411 25.386 1.00117.46 O ANISOU 1602 OE2 GLU A 201 15601 11925 17105 -214 -3058 3309 O ATOM 1603 N SER A 202 7.118 55.437 24.465 1.00 88.94 N ANISOU 1603 N SER A 202 12092 9025 12676 -775 -2659 3310 N ATOM 1604 CA SER A 202 6.621 54.293 23.709 1.00 72.29 C ANISOU 1604 CA SER A 202 9966 7163 10336 -796 -2622 3339 C ATOM 1605 C SER A 202 7.184 52.973 24.218 1.00 82.55 C ANISOU 1605 C SER A 202 11244 8652 11470 -820 -2503 3232 C ATOM 1606 O SER A 202 6.588 51.922 23.961 1.00 81.33 O ANISOU 1606 O SER A 202 11056 8685 11162 -789 -2469 3204 O ATOM 1607 CB SER A 202 6.949 54.459 22.224 1.00 62.90 C ANISOU 1607 CB SER A 202 8848 6061 8988 -959 -2619 3498 C ATOM 1608 OG SER A 202 8.349 54.484 22.010 1.00100.57 O ANISOU 1608 OG SER A 202 13681 10865 13666 -1127 -2535 3520 O ATOM 1609 N PHE A 203 8.310 53.001 24.933 1.00 87.78 N ANISOU 1609 N PHE A 203 11927 9270 12157 -875 -2434 3171 N ATOM 1610 CA PHE A 203 8.881 51.766 25.460 1.00 80.19 C ANISOU 1610 CA PHE A 203 10943 8495 11029 -888 -2308 3063 C ATOM 1611 C PHE A 203 8.233 51.368 26.780 1.00 75.94 C ANISOU 1611 C PHE A 203 10286 7970 10599 -680 -2264 2827 C ATOM 1612 O PHE A 203 7.974 50.182 27.012 1.00 81.26 O ANISOU 1612 O PHE A 203 10913 8840 11123 -627 -2174 2723 O ATOM 1613 CB PHE A 203 10.393 51.914 25.630 1.00 76.40 C ANISOU 1613 CB PHE A 203 10499 8045 10486 -1027 -2186 3006 C ATOM 1614 CG PHE A 203 11.086 50.640 26.020 1.00 72.14 C ANISOU 1614 CG PHE A 203 9922 7757 9729 -1041 -2004 2844 C ATOM 1615 CD1 PHE A 203 11.419 49.697 25.061 1.00 64.53 C ANISOU 1615 CD1 PHE A 203 9015 7003 8499 -1166 -1943 2938 C ATOM 1616 CD2 PHE A 203 11.406 50.384 27.343 1.00 68.08 C ANISOU 1616 CD2 PHE A 203 9317 7275 9276 -925 -1891 2598 C ATOM 1617 CE1 PHE A 203 12.056 48.523 25.415 1.00 71.65 C ANISOU 1617 CE1 PHE A 203 9891 8129 9204 -1171 -1773 2791 C ATOM 1618 CE2 PHE A 203 12.044 49.213 27.702 1.00 63.67 C ANISOU 1618 CE2 PHE A 203 8729 6948 8517 -928 -1722 2457 C ATOM 1619 CZ PHE A 203 12.369 48.280 26.737 1.00 68.59 C ANISOU 1619 CZ PHE A 203 9416 7766 8879 -1048 -1662 2555 C ATOM 1620 N VAL A 204 7.969 52.341 27.657 1.00 83.69 N ANISOU 1620 N VAL A 204 11218 8744 11838 -561 -2325 2740 N ATOM 1621 CA VAL A 204 7.310 52.039 28.925 1.00 85.61 C ANISOU 1621 CA VAL A 204 11340 8995 12193 -357 -2293 2519 C ATOM 1622 C VAL A 204 5.902 51.509 28.680 1.00 80.50 C ANISOU 1622 C VAL A 204 10652 8408 11527 -242 -2377 2563 C ATOM 1623 O VAL A 204 5.441 50.587 29.365 1.00 68.76 O ANISOU 1623 O VAL A 204 9082 7061 9985 -128 -2303 2405 O ATOM 1624 CB VAL A 204 7.301 53.285 29.832 1.00 88.71 C ANISOU 1624 CB VAL A 204 11693 9142 12872 -261 -2353 2428 C ATOM 1625 CG1 VAL A 204 6.456 53.041 31.073 1.00 95.25 C ANISOU 1625 CG1 VAL A 204 12391 9973 13825 -40 -2344 2218 C ATOM 1626 CG2 VAL A 204 8.721 53.660 30.227 1.00 93.80 C ANISOU 1626 CG2 VAL A 204 12358 9763 13518 -373 -2246 2342 C ATOM 1627 N ILE A 205 5.202 52.073 27.694 1.00 80.40 N ANISOU 1627 N ILE A 205 10696 8298 11554 -271 -2531 2780 N ATOM 1628 CA ILE A 205 3.868 51.586 27.357 1.00 81.91 C ANISOU 1628 CA ILE A 205 10836 8591 11694 -179 -2580 2789 C ATOM 1629 C ILE A 205 3.948 50.188 26.756 1.00 84.74 C ANISOU 1629 C ILE A 205 11214 9210 11775 -267 -2489 2809 C ATOM 1630 O ILE A 205 3.186 49.289 27.129 1.00 82.25 O ANISOU 1630 O ILE A 205 10830 9021 11400 -169 -2464 2717 O ATOM 1631 CB ILE A 205 3.161 52.570 26.408 1.00 78.41 C ANISOU 1631 CB ILE A 205 10424 8052 11314 -196 -2685 2925 C ATOM 1632 CG1 ILE A 205 2.953 53.919 27.099 1.00 78.54 C ANISOU 1632 CG1 ILE A 205 10418 7814 11609 -86 -2767 2883 C ATOM 1633 CG2 ILE A 205 1.832 51.998 25.937 1.00 55.36 C ANISOU 1633 CG2 ILE A 205 7454 5272 8309 -124 -2718 2935 C ATOM 1634 CD1 ILE A 205 2.296 54.960 26.220 1.00 62.34 C ANISOU 1634 CD1 ILE A 205 8404 5656 9627 -91 -2867 3021 C ATOM 1635 N TYR A 206 4.874 49.985 25.813 1.00 84.46 N ANISOU 1635 N TYR A 206 11269 9261 11560 -457 -2429 2916 N ATOM 1636 CA TYR A 206 5.085 48.655 25.251 1.00 73.88 C ANISOU 1636 CA TYR A 206 9952 8171 9949 -549 -2320 2912 C ATOM 1637 C TYR A 206 5.459 47.647 26.328 1.00 79.63 C ANISOU 1637 C TYR A 206 10629 9013 10612 -480 -2189 2726 C ATOM 1638 O TYR A 206 5.081 46.473 26.241 1.00 84.64 O ANISOU 1638 O TYR A 206 11244 9832 11081 -468 -2116 2671 O ATOM 1639 CB TYR A 206 6.169 48.705 24.172 1.00 63.38 C ANISOU 1639 CB TYR A 206 8716 6913 8455 -754 -2258 3017 C ATOM 1640 CG TYR A 206 6.907 47.398 23.977 1.00 78.51 C ANISOU 1640 CG TYR A 206 10658 9060 10113 -848 -2104 2960 C ATOM 1641 CD1 TYR A 206 6.329 46.350 23.273 1.00 78.00 C ANISOU 1641 CD1 TYR A 206 10586 9188 9863 -869 -2052 2944 C ATOM 1642 CD2 TYR A 206 8.185 47.216 24.492 1.00 87.16 C ANISOU 1642 CD2 TYR A 206 11786 10181 11150 -914 -2004 2914 C ATOM 1643 CE1 TYR A 206 7.000 45.154 23.093 1.00 83.57 C ANISOU 1643 CE1 TYR A 206 11316 10095 10341 -945 -1899 2871 C ATOM 1644 CE2 TYR A 206 8.863 46.024 24.316 1.00 79.93 C ANISOU 1644 CE2 TYR A 206 10893 9485 9993 -988 -1849 2847 C ATOM 1645 CZ TYR A 206 8.267 44.998 23.616 1.00 85.46 C ANISOU 1645 CZ TYR A 206 11586 10363 10522 -998 -1795 2819 C ATOM 1646 OH TYR A 206 8.938 43.810 23.438 1.00 90.27 O ANISOU 1646 OH TYR A 206 12216 11176 10905 -1058 -1630 2730 O ATOM 1647 N MET A 207 6.194 48.085 27.349 1.00 74.55 N ANISOU 1647 N MET A 207 9950 8286 10090 -430 -2118 2577 N ATOM 1648 CA MET A 207 6.580 47.191 28.432 1.00 74.79 C ANISOU 1648 CA MET A 207 9909 8447 10059 -349 -1953 2345 C ATOM 1649 C MET A 207 5.417 46.908 29.374 1.00 79.89 C ANISOU 1649 C MET A 207 10446 9089 10821 -149 -1975 2202 C ATOM 1650 O MET A 207 5.258 45.776 29.844 1.00 82.04 O ANISOU 1650 O MET A 207 10672 9526 10971 -91 -1858 2070 O ATOM 1651 CB MET A 207 7.749 47.794 29.203 1.00 73.48 C ANISOU 1651 CB MET A 207 9732 8206 9980 -364 -1874 2233 C ATOM 1652 CG MET A 207 9.097 47.571 28.566 1.00 91.09 C ANISOU 1652 CG MET A 207 12047 10536 12026 -549 -1776 2295 C ATOM 1653 SD MET A 207 9.723 45.934 28.952 1.00105.43 S ANISOU 1653 SD MET A 207 13843 12635 13581 -545 -1557 2134 S ATOM 1654 CE MET A 207 10.092 46.112 30.697 1.00 97.11 C ANISOU 1654 CE MET A 207 12669 11548 12679 -380 -1458 1865 C ATOM 1655 N PHE A 208 4.602 47.924 29.667 1.00 86.39 N ANISOU 1655 N PHE A 208 11224 9723 11876 -39 -2120 2226 N ATOM 1656 CA PHE A 208 3.472 47.726 30.567 1.00 78.54 C ANISOU 1656 CA PHE A 208 10118 8726 10999 154 -2149 2091 C ATOM 1657 C PHE A 208 2.438 46.790 29.955 1.00 80.49 C ANISOU 1657 C PHE A 208 10357 9120 11103 161 -2176 2153 C ATOM 1658 O PHE A 208 1.827 45.982 30.665 1.00 78.78 O ANISOU 1658 O PHE A 208 10059 9011 10861 273 -2114 2007 O ATOM 1659 CB PHE A 208 2.840 49.073 30.918 1.00 69.71 C ANISOU 1659 CB PHE A 208 8961 7368 10157 266 -2307 2116 C ATOM 1660 CG PHE A 208 1.742 48.984 31.943 1.00 78.59 C ANISOU 1660 CG PHE A 208 9960 8483 11419 474 -2338 1963 C ATOM 1661 CD1 PHE A 208 2.041 48.950 33.295 1.00 81.83 C ANISOU 1661 CD1 PHE A 208 10279 8889 11925 592 -2244 1736 C ATOM 1662 CD2 PHE A 208 0.413 48.941 31.554 1.00 77.40 C ANISOU 1662 CD2 PHE A 208 9776 8337 11296 551 -2462 2044 C ATOM 1663 CE1 PHE A 208 1.035 48.870 34.241 1.00 87.86 C ANISOU 1663 CE1 PHE A 208 10922 9651 12810 782 -2273 1595 C ATOM 1664 CE2 PHE A 208 -0.598 48.861 32.495 1.00 76.91 C ANISOU 1664 CE2 PHE A 208 9594 8294 11335 729 -2460 1878 C ATOM 1665 CZ PHE A 208 -0.286 48.826 33.840 1.00 80.73 C ANISOU 1665 CZ PHE A 208 9988 8756 11928 853 -2390 1674 C ATOM 1666 N VAL A 209 2.238 46.872 28.641 1.00 73.34 N ANISOU 1666 N VAL A 209 9536 8230 10100 36 -2265 2366 N ATOM 1667 CA VAL A 209 1.212 46.067 27.986 1.00 75.69 C ANISOU 1667 CA VAL A 209 9825 8668 10267 32 -2304 2432 C ATOM 1668 C VAL A 209 1.742 44.677 27.654 1.00 87.31 C ANISOU 1668 C VAL A 209 11339 10364 11471 -76 -2144 2389 C ATOM 1669 O VAL A 209 1.185 43.661 28.086 1.00 79.18 O ANISOU 1669 O VAL A 209 10255 9470 10361 -10 -2067 2268 O ATOM 1670 CB VAL A 209 0.691 46.782 26.726 1.00 60.18 C ANISOU 1670 CB VAL A 209 7910 6656 8301 -48 -2413 2609 C ATOM 1671 CG1 VAL A 209 -0.287 45.891 25.977 1.00 65.50 C ANISOU 1671 CG1 VAL A 209 8568 7509 8809 -73 -2405 2631 C ATOM 1672 CG2 VAL A 209 0.040 48.106 27.096 1.00 64.55 C ANISOU 1672 CG2 VAL A 209 8415 7005 9105 75 -2532 2607 C ATOM 1673 N VAL A 210 2.830 44.613 26.885 1.00 81.74 N ANISOU 1673 N VAL A 210 10732 9700 10624 -244 -2089 2486 N ATOM 1674 CA VAL A 210 3.297 43.331 26.363 1.00 66.64 C ANISOU 1674 CA VAL A 210 8874 7998 8446 -358 -1952 2474 C ATOM 1675 C VAL A 210 3.940 42.494 27.463 1.00 64.77 C ANISOU 1675 C VAL A 210 8599 7855 8155 -293 -1763 2253 C ATOM 1676 O VAL A 210 3.724 41.278 27.538 1.00 76.47 O ANISOU 1676 O VAL A 210 10076 9499 9480 -287 -1654 2170 O ATOM 1677 CB VAL A 210 4.262 43.557 25.185 1.00 67.93 C ANISOU 1677 CB VAL A 210 9149 8188 8476 -553 -1945 2633 C ATOM 1678 CG1 VAL A 210 4.894 42.244 24.750 1.00 47.30 C ANISOU 1678 CG1 VAL A 210 6586 5790 5597 -659 -1775 2577 C ATOM 1679 CG2 VAL A 210 3.531 44.211 24.022 1.00 62.92 C ANISOU 1679 CG2 VAL A 210 8524 7511 7871 -604 -2051 2755 C ATOM 1680 N HIS A 211 4.732 43.120 28.334 1.00 70.42 N ANISOU 1680 N HIS A 211 9287 8472 8997 -242 -1719 2155 N ATOM 1681 CA HIS A 211 5.529 42.391 29.313 1.00 64.87 C ANISOU 1681 CA HIS A 211 8553 7868 8227 -192 -1535 1961 C ATOM 1682 C HIS A 211 4.979 42.503 30.732 1.00 63.62 C ANISOU 1682 C HIS A 211 8274 7655 8245 7 -1519 1771 C ATOM 1683 O HIS A 211 5.705 42.232 31.694 1.00 62.51 O ANISOU 1683 O HIS A 211 8092 7558 8101 67 -1386 1610 O ATOM 1684 CB HIS A 211 6.981 42.866 29.265 1.00 63.17 C ANISOU 1684 CB HIS A 211 8389 7629 7985 -293 -1469 1972 C ATOM 1685 CG HIS A 211 7.658 42.601 27.957 1.00 75.16 C ANISOU 1685 CG HIS A 211 10021 9235 9301 -488 -1455 2136 C ATOM 1686 ND1 HIS A 211 8.367 41.446 27.706 1.00 61.31 N ANISOU 1686 ND1 HIS A 211 8315 7674 7307 -561 -1297 2094 N ATOM 1687 CD2 HIS A 211 7.727 43.337 26.823 1.00 89.21 C ANISOU 1687 CD2 HIS A 211 11875 10941 11080 -622 -1578 2343 C ATOM 1688 CE1 HIS A 211 8.847 41.484 26.476 1.00 75.00 C ANISOU 1688 CE1 HIS A 211 10144 9453 8900 -734 -1325 2262 C ATOM 1689 NE2 HIS A 211 8.472 42.621 25.918 1.00 80.23 N ANISOU 1689 NE2 HIS A 211 10823 9959 9702 -776 -1494 2418 N ATOM 1690 N PHE A 212 3.714 42.892 30.887 1.00 63.73 N ANISOU 1690 N PHE A 212 8224 7586 8406 112 -1650 1786 N ATOM 1691 CA PHE A 212 3.092 42.873 32.206 1.00 71.49 C ANISOU 1691 CA PHE A 212 9086 8542 9536 303 -1632 1602 C ATOM 1692 C PHE A 212 1.606 42.545 32.118 1.00 75.89 C ANISOU 1692 C PHE A 212 9587 9128 10121 387 -1721 1616 C ATOM 1693 O PHE A 212 1.120 41.670 32.841 1.00 79.08 O ANISOU 1693 O PHE A 212 9923 9638 10483 483 -1633 1476 O ATOM 1694 CB PHE A 212 3.292 44.206 32.929 1.00 71.36 C ANISOU 1694 CB PHE A 212 9017 8330 9768 386 -1712 1556 C ATOM 1695 CG PHE A 212 2.631 44.261 34.276 1.00 74.92 C ANISOU 1695 CG PHE A 212 9337 8754 10377 585 -1703 1368 C ATOM 1696 CD1 PHE A 212 3.122 43.512 35.333 1.00 73.47 C ANISOU 1696 CD1 PHE A 212 9093 8686 10136 662 -1537 1175 C ATOM 1697 CD2 PHE A 212 1.514 45.053 34.485 1.00 75.44 C ANISOU 1697 CD2 PHE A 212 9336 8686 10642 702 -1860 1385 C ATOM 1698 CE1 PHE A 212 2.513 43.553 36.574 1.00 68.60 C ANISOU 1698 CE1 PHE A 212 8351 8055 9657 844 -1528 1003 C ATOM 1699 CE2 PHE A 212 0.901 45.100 35.724 1.00 69.32 C ANISOU 1699 CE2 PHE A 212 8435 7897 10007 886 -1852 1208 C ATOM 1700 CZ PHE A 212 1.401 44.347 36.769 1.00 66.69 C ANISOU 1700 CZ PHE A 212 8041 7684 9614 953 -1686 1017 C ATOM 1701 N ILE A 213 0.876 43.238 31.243 1.00 74.29 N ANISOU 1701 N ILE A 213 9408 8836 9983 352 -1892 1786 N ATOM 1702 CA ILE A 213 -0.553 42.970 31.100 1.00 65.90 C ANISOU 1702 CA ILE A 213 8286 7813 8939 427 -1986 1807 C ATOM 1703 C ILE A 213 -0.777 41.617 30.435 1.00 74.03 C ANISOU 1703 C ILE A 213 9359 9045 9723 330 -1898 1829 C ATOM 1704 O ILE A 213 -1.572 40.798 30.911 1.00 73.69 O ANISOU 1704 O ILE A 213 9251 9106 9642 408 -1851 1722 O ATOM 1705 CB ILE A 213 -1.242 44.105 30.320 1.00 69.60 C ANISOU 1705 CB ILE A 213 8768 8139 9539 422 -2193 1991 C ATOM 1706 CG1 ILE A 213 -1.241 45.395 31.143 1.00 74.53 C ANISOU 1706 CG1 ILE A 213 9335 8552 10430 551 -2280 1940 C ATOM 1707 CG2 ILE A 213 -2.665 43.715 29.952 1.00 60.50 C ANISOU 1707 CG2 ILE A 213 7563 7068 8358 471 -2286 2035 C ATOM 1708 CD1 ILE A 213 -1.929 45.266 32.483 1.00 70.81 C ANISOU 1708 CD1 ILE A 213 8731 8083 10091 745 -2256 1738 C ATOM 1709 N ILE A 214 -0.078 41.361 29.326 1.00 74.97 N ANISOU 1709 N ILE A 214 9591 9225 9671 155 -1872 1963 N ATOM 1710 CA ILE A 214 -0.204 40.067 28.653 1.00 76.18 C ANISOU 1710 CA ILE A 214 9795 9567 9582 52 -1781 1979 C ATOM 1711 C ILE A 214 0.212 38.910 29.556 1.00 76.45 C ANISOU 1711 C ILE A 214 9810 9722 9515 100 -1580 1785 C ATOM 1712 O ILE A 214 -0.532 37.919 29.633 1.00 71.70 O ANISOU 1712 O ILE A 214 9183 9240 8818 121 -1526 1722 O ATOM 1713 CB ILE A 214 0.561 40.087 27.317 1.00 67.30 C ANISOU 1713 CB ILE A 214 8793 8482 8297 -143 -1790 2155 C ATOM 1714 CG1 ILE A 214 -0.009 41.160 26.387 1.00 52.48 C ANISOU 1714 CG1 ILE A 214 6931 6498 6511 -183 -1993 2359 C ATOM 1715 CG2 ILE A 214 0.515 38.718 26.653 1.00 52.08 C ANISOU 1715 CG2 ILE A 214 6922 6751 6115 -251 -1682 2155 C ATOM 1716 CD1 ILE A 214 -1.474 40.974 26.065 1.00 70.92 C ANISOU 1716 CD1 ILE A 214 9204 8885 8856 -131 -2081 2374 C ATOM 1717 N PRO A 215 1.357 38.954 30.253 1.00 81.18 N ANISOU 1717 N PRO A 215 10419 10302 10123 119 -1460 1687 N ATOM 1718 CA PRO A 215 1.666 37.858 31.187 1.00 77.47 C ANISOU 1718 CA PRO A 215 9922 9948 9564 189 -1272 1504 C ATOM 1719 C PRO A 215 0.649 37.707 32.303 1.00 77.58 C ANISOU 1719 C PRO A 215 9814 9954 9707 365 -1277 1359 C ATOM 1720 O PRO A 215 0.389 36.580 32.743 1.00 76.36 O ANISOU 1720 O PRO A 215 9644 9922 9447 403 -1151 1249 O ATOM 1721 CB PRO A 215 3.047 38.245 31.735 1.00 69.79 C ANISOU 1721 CB PRO A 215 8965 8937 8615 191 -1179 1441 C ATOM 1722 CG PRO A 215 3.638 39.105 30.687 1.00 74.37 C ANISOU 1722 CG PRO A 215 9626 9438 9192 50 -1278 1617 C ATOM 1723 CD PRO A 215 2.491 39.889 30.135 1.00 74.72 C ANISOU 1723 CD PRO A 215 9647 9379 9366 61 -1477 1745 C ATOM 1724 N LEU A 216 0.063 38.809 32.777 1.00 80.24 N ANISOU 1724 N LEU A 216 10067 10150 10270 474 -1418 1356 N ATOM 1725 CA LEU A 216 -0.894 38.719 33.873 1.00 69.30 C ANISOU 1725 CA LEU A 216 8556 8762 9011 646 -1427 1213 C ATOM 1726 C LEU A 216 -2.206 38.090 33.424 1.00 81.38 C ANISOU 1726 C LEU A 216 10062 10379 10479 642 -1482 1249 C ATOM 1727 O LEU A 216 -2.845 37.372 34.201 1.00 79.88 O ANISOU 1727 O LEU A 216 9798 10270 10283 738 -1412 1118 O ATOM 1728 CB LEU A 216 -1.141 40.106 34.466 1.00 73.70 C ANISOU 1728 CB LEU A 216 9033 9142 9827 764 -1565 1199 C ATOM 1729 CG LEU A 216 -1.722 40.160 35.879 1.00 74.28 C ANISOU 1729 CG LEU A 216 8969 9203 10051 959 -1545 1014 C ATOM 1730 CD1 LEU A 216 -0.835 39.391 36.844 1.00 55.01 C ANISOU 1730 CD1 LEU A 216 6513 6857 7531 1001 -1345 847 C ATOM 1731 CD2 LEU A 216 -1.884 41.602 36.332 1.00 74.61 C ANISOU 1731 CD2 LEU A 216 8946 9056 10346 1060 -1687 1010 C ATOM 1732 N ILE A 217 -2.621 38.341 32.181 1.00 83.24 N ANISOU 1732 N ILE A 217 10355 10609 10662 529 -1605 1425 N ATOM 1733 CA ILE A 217 -3.858 37.752 31.679 1.00 69.14 C ANISOU 1733 CA ILE A 217 8544 8923 8805 511 -1660 1462 C ATOM 1734 C ILE A 217 -3.672 36.263 31.412 1.00 68.42 C ANISOU 1734 C ILE A 217 8515 9004 8477 414 -1493 1413 C ATOM 1735 O ILE A 217 -4.564 35.451 31.690 1.00 73.61 O ANISOU 1735 O ILE A 217 9122 9761 9085 451 -1454 1334 O ATOM 1736 CB ILE A 217 -4.331 38.503 30.420 1.00 56.31 C ANISOU 1736 CB ILE A 217 6957 7249 7191 423 -1844 1669 C ATOM 1737 CG1 ILE A 217 -4.680 39.952 30.764 1.00 61.75 C ANISOU 1737 CG1 ILE A 217 7578 7756 8128 542 -2011 1710 C ATOM 1738 CG2 ILE A 217 -5.527 37.804 29.790 1.00 55.29 C ANISOU 1738 CG2 ILE A 217 6804 7252 6952 381 -1891 1711 C ATOM 1739 CD1 ILE A 217 -5.068 40.789 29.564 1.00 58.96 C ANISOU 1739 CD1 ILE A 217 7267 7338 7797 468 -2192 1925 C ATOM 1740 N VAL A 218 -2.510 35.878 30.880 1.00 64.13 N ANISOU 1740 N VAL A 218 8084 8499 7784 290 -1388 1455 N ATOM 1741 CA VAL A 218 -2.258 34.473 30.573 1.00 68.08 C ANISOU 1741 CA VAL A 218 8658 9154 8056 196 -1224 1411 C ATOM 1742 C VAL A 218 -2.199 33.643 31.851 1.00 65.17 C ANISOU 1742 C VAL A 218 8238 8839 7685 316 -1058 1215 C ATOM 1743 O VAL A 218 -2.742 32.533 31.911 1.00 65.27 O ANISOU 1743 O VAL A 218 8255 8964 7581 303 -965 1149 O ATOM 1744 CB VAL A 218 -0.968 34.333 29.744 1.00 58.04 C ANISOU 1744 CB VAL A 218 7513 7908 6631 48 -1153 1499 C ATOM 1745 CG1 VAL A 218 -0.588 32.871 29.591 1.00 49.80 C ANISOU 1745 CG1 VAL A 218 6546 7013 5361 -25 -963 1430 C ATOM 1746 CG2 VAL A 218 -1.144 34.983 28.380 1.00 47.03 C ANISOU 1746 CG2 VAL A 218 6173 6489 5208 -84 -1310 1702 C ATOM 1747 N ILE A 219 -1.549 34.166 32.893 1.00 69.40 N ANISOU 1747 N ILE A 219 8723 9298 8348 433 -1016 1119 N ATOM 1748 CA ILE A 219 -1.424 33.417 34.140 1.00 72.15 C ANISOU 1748 CA ILE A 219 9018 9703 8692 555 -856 938 C ATOM 1749 C ILE A 219 -2.785 33.249 34.807 1.00 61.84 C ANISOU 1749 C ILE A 219 7598 8416 7483 671 -904 855 C ATOM 1750 O ILE A 219 -3.122 32.161 35.291 1.00 74.98 O ANISOU 1750 O ILE A 219 9251 10181 9058 702 -775 752 O ATOM 1751 CB ILE A 219 -0.410 34.101 35.075 1.00 62.97 C ANISOU 1751 CB ILE A 219 7818 8464 7644 651 -811 856 C ATOM 1752 CG1 ILE A 219 1.009 33.941 34.527 1.00 71.12 C ANISOU 1752 CG1 ILE A 219 8964 9525 8535 535 -714 908 C ATOM 1753 CG2 ILE A 219 -0.507 33.534 36.484 1.00 57.34 C ANISOU 1753 CG2 ILE A 219 7016 7802 6968 809 -681 669 C ATOM 1754 CD1 ILE A 219 2.081 34.509 35.431 1.00 75.33 C ANISOU 1754 CD1 ILE A 219 9459 10009 9153 617 -652 819 C ATOM 1755 N PHE A 220 -3.590 34.313 34.839 1.00 72.77 N ANISOU 1755 N PHE A 220 8898 9703 9050 737 -1088 900 N ATOM 1756 CA PHE A 220 -4.907 34.220 35.462 1.00 81.86 C ANISOU 1756 CA PHE A 220 9929 10879 10295 851 -1144 822 C ATOM 1757 C PHE A 220 -5.826 33.282 34.689 1.00 76.34 C ANISOU 1757 C PHE A 220 9260 10301 9445 750 -1142 867 C ATOM 1758 O PHE A 220 -6.613 32.542 35.289 1.00 58.08 O ANISOU 1758 O PHE A 220 6883 8072 7114 810 -1081 762 O ATOM 1759 CB PHE A 220 -5.536 35.608 35.582 1.00 61.69 C ANISOU 1759 CB PHE A 220 7283 8192 7963 944 -1347 870 C ATOM 1760 CG PHE A 220 -5.251 36.293 36.889 1.00 76.20 C ANISOU 1760 CG PHE A 220 9024 9942 9988 1112 -1338 739 C ATOM 1761 CD1 PHE A 220 -4.175 37.156 37.017 1.00 89.51 C ANISOU 1761 CD1 PHE A 220 10740 11512 11756 1115 -1347 755 C ATOM 1762 CD2 PHE A 220 -6.061 36.072 37.990 1.00 74.87 C ANISOU 1762 CD2 PHE A 220 8730 9813 9906 1263 -1318 595 C ATOM 1763 CE1 PHE A 220 -3.913 37.786 38.220 1.00 95.02 C ANISOU 1763 CE1 PHE A 220 11345 12136 12623 1264 -1337 625 C ATOM 1764 CE2 PHE A 220 -5.805 36.699 39.195 1.00 78.89 C ANISOU 1764 CE2 PHE A 220 9142 10250 10581 1418 -1309 468 C ATOM 1765 CZ PHE A 220 -4.729 37.557 39.310 1.00 95.14 C ANISOU 1765 CZ PHE A 220 11231 12194 12722 1418 -1318 480 C ATOM 1766 N PHE A 221 -5.739 33.294 33.357 1.00 65.97 N ANISOU 1766 N PHE A 221 8040 9006 8019 592 -1205 1021 N ATOM 1767 CA PHE A 221 -6.595 32.425 32.555 1.00 62.80 C ANISOU 1767 CA PHE A 221 7666 8729 7468 483 -1207 1063 C ATOM 1768 C PHE A 221 -6.181 30.965 32.689 1.00 80.27 C ANISOU 1768 C PHE A 221 9954 11057 9486 419 -992 971 C ATOM 1769 O PHE A 221 -7.016 30.096 32.963 1.00 86.47 O ANISOU 1769 O PHE A 221 10704 11935 10215 427 -932 890 O ATOM 1770 CB PHE A 221 -6.562 32.861 31.090 1.00 66.39 C ANISOU 1770 CB PHE A 221 8198 9179 7849 333 -1332 1253 C ATOM 1771 CG PHE A 221 -7.250 31.902 30.159 1.00 79.69 C ANISOU 1771 CG PHE A 221 9925 11006 9349 196 -1316 1296 C ATOM 1772 CD1 PHE A 221 -8.630 31.907 30.034 1.00 71.42 C ANISOU 1772 CD1 PHE A 221 8785 10016 8334 219 -1426 1302 C ATOM 1773 CD2 PHE A 221 -6.517 30.997 29.407 1.00 79.07 C ANISOU 1773 CD2 PHE A 221 9974 11009 9060 43 -1190 1324 C ATOM 1774 CE1 PHE A 221 -9.265 31.027 29.179 1.00 63.38 C ANISOU 1774 CE1 PHE A 221 7801 9137 7142 84 -1409 1333 C ATOM 1775 CE2 PHE A 221 -7.147 30.114 28.551 1.00 64.91 C ANISOU 1775 CE2 PHE A 221 8220 9346 7097 -89 -1172 1354 C ATOM 1776 CZ PHE A 221 -8.523 30.129 28.437 1.00 71.24 C ANISOU 1776 CZ PHE A 221 8927 10206 7933 -73 -1282 1357 C ATOM 1777 N CYS A 222 -4.892 30.675 32.494 1.00 75.74 N ANISOU 1777 N CYS A 222 9488 10481 8809 354 -871 981 N ATOM 1778 CA CYS A 222 -4.424 29.293 32.532 1.00 61.15 C ANISOU 1778 CA CYS A 222 7729 8737 6769 293 -664 905 C ATOM 1779 C CYS A 222 -4.647 28.671 33.905 1.00 63.13 C ANISOU 1779 C CYS A 222 7908 9013 7065 437 -531 733 C ATOM 1780 O CYS A 222 -5.155 27.549 34.017 1.00 87.13 O ANISOU 1780 O CYS A 222 10966 12144 9995 410 -420 664 O ATOM 1781 CB CYS A 222 -2.946 29.229 32.144 1.00 50.39 C ANISOU 1781 CB CYS A 222 6482 7364 5301 220 -568 947 C ATOM 1782 SG CYS A 222 -2.619 29.580 30.403 1.00 76.87 S ANISOU 1782 SG CYS A 222 9944 10729 8533 17 -677 1148 S ATOM 1783 N TYR A 223 -4.272 29.387 34.967 1.00 62.96 N ANISOU 1783 N TYR A 223 7617 8472 7832 -239 -1950 -285 N ATOM 1784 CA TYR A 223 -4.468 28.855 36.311 1.00 62.23 C ANISOU 1784 CA TYR A 223 7442 8329 7873 -358 -1798 -326 C ATOM 1785 C TYR A 223 -5.933 28.892 36.723 1.00 65.59 C ANISOU 1785 C TYR A 223 7628 8810 8482 -418 -1849 -401 C ATOM 1786 O TYR A 223 -6.370 28.052 37.517 1.00 76.51 O ANISOU 1786 O TYR A 223 8932 10163 9976 -545 -1756 -456 O ATOM 1787 CB TYR A 223 -3.603 29.620 37.311 1.00 49.77 C ANISOU 1787 CB TYR A 223 5896 6708 6307 -300 -1636 -237 C ATOM 1788 CG TYR A 223 -2.159 29.176 37.309 1.00 67.06 C ANISOU 1788 CG TYR A 223 8286 8850 8345 -292 -1531 -184 C ATOM 1789 CD1 TYR A 223 -1.825 27.848 37.079 1.00 67.75 C ANISOU 1789 CD1 TYR A 223 8495 8909 8338 -366 -1503 -230 C ATOM 1790 CD2 TYR A 223 -1.130 30.082 37.528 1.00 62.30 C ANISOU 1790 CD2 TYR A 223 7746 8230 7697 -211 -1462 -90 C ATOM 1791 CE1 TYR A 223 -0.509 27.432 37.073 1.00 66.64 C ANISOU 1791 CE1 TYR A 223 8533 8746 8040 -335 -1404 -176 C ATOM 1792 CE2 TYR A 223 0.191 29.675 37.523 1.00 60.30 C ANISOU 1792 CE2 TYR A 223 7647 7960 7303 -201 -1367 -39 C ATOM 1793 CZ TYR A 223 0.495 28.349 37.294 1.00 54.30 C ANISOU 1793 CZ TYR A 223 7007 7196 6430 -252 -1337 -78 C ATOM 1794 OH TYR A 223 1.807 27.937 37.289 1.00 77.34 O ANISOU 1794 OH TYR A 223 10077 10117 9190 -218 -1239 -22 O ATOM 1795 N GLY A 224 -6.703 29.847 36.200 1.00 66.42 N ANISOU 1795 N GLY A 224 7612 9001 8622 -320 -1985 -392 N ATOM 1796 CA GLY A 224 -8.132 29.848 36.461 1.00 55.56 C ANISOU 1796 CA GLY A 224 5991 7712 7407 -367 -2052 -465 C ATOM 1797 C GLY A 224 -8.826 28.642 35.858 1.00 67.13 C ANISOU 1797 C GLY A 224 7397 9206 8905 -513 -2168 -594 C ATOM 1798 O GLY A 224 -9.673 28.015 36.501 1.00 71.43 O ANISOU 1798 O GLY A 224 7769 9758 9612 -651 -2124 -658 O ATOM 1799 N GLN A 225 -8.474 28.298 34.616 1.00 58.94 N ANISOU 1799 N GLN A 225 6500 8180 7714 -481 -2314 -636 N ATOM 1800 CA GLN A 225 -9.022 27.098 33.994 1.00 66.59 C ANISOU 1800 CA GLN A 225 7445 9154 8703 -621 -2442 -786 C ATOM 1801 C GLN A 225 -8.549 25.834 34.698 1.00 86.05 C ANISOU 1801 C GLN A 225 10011 11470 11214 -797 -2283 -819 C ATOM 1802 O GLN A 225 -9.277 24.835 34.732 1.00 96.16 O ANISOU 1802 O GLN A 225 11197 12718 12621 -973 -2321 -939 O ATOM 1803 CB GLN A 225 -8.637 27.049 32.515 1.00 64.03 C ANISOU 1803 CB GLN A 225 7282 8879 8169 -505 -2633 -823 C ATOM 1804 CG GLN A 225 -9.236 28.157 31.661 1.00 74.82 C ANISOU 1804 CG GLN A 225 8549 10404 9475 -316 -2808 -802 C ATOM 1805 CD GLN A 225 -10.666 27.873 31.244 1.00 83.66 C ANISOU 1805 CD GLN A 225 9424 11658 10703 -378 -3009 -961 C ATOM 1806 OE1 GLN A 225 -11.511 27.524 32.067 1.00100.82 O ANISOU 1806 OE1 GLN A 225 11384 13834 13087 -540 -2960 -1020 O ATOM 1807 NE2 GLN A 225 -10.943 28.017 29.953 1.00 86.06 N ANISOU 1807 NE2 GLN A 225 9749 12090 10860 -241 -3234 -1029 N ATOM 1808 N LEU A 226 -7.340 25.857 35.264 1.00 90.06 N ANISOU 1808 N LEU A 226 10707 11886 11627 -752 -2102 -714 N ATOM 1809 CA LEU A 226 -6.817 24.672 35.935 1.00 89.42 C ANISOU 1809 CA LEU A 226 10744 11670 11561 -881 -1936 -730 C ATOM 1810 C LEU A 226 -7.560 24.402 37.237 1.00 93.43 C ANISOU 1810 C LEU A 226 11063 12150 12288 -1003 -1777 -725 C ATOM 1811 O LEU A 226 -7.878 23.249 37.548 1.00 98.86 O ANISOU 1811 O LEU A 226 11744 12742 13076 -1167 -1710 -788 O ATOM 1812 CB LEU A 226 -5.318 24.833 36.185 1.00 70.94 C ANISOU 1812 CB LEU A 226 8634 9276 9042 -774 -1792 -617 C ATOM 1813 CG LEU A 226 -4.564 23.590 36.656 1.00 68.69 C ANISOU 1813 CG LEU A 226 8530 8867 8702 -853 -1633 -625 C ATOM 1814 CD1 LEU A 226 -3.339 23.351 35.790 1.00 86.86 C ANISOU 1814 CD1 LEU A 226 11093 11155 10755 -748 -1665 -594 C ATOM 1815 CD2 LEU A 226 -4.165 23.736 38.110 1.00 70.23 C ANISOU 1815 CD2 LEU A 226 8696 9032 8956 -843 -1394 -538 C ATOM 1816 N VAL A 227 -7.849 25.452 38.010 1.00 85.03 N ANISOU 1816 N VAL A 227 9849 11159 11301 -916 -1707 -646 N ATOM 1817 CA VAL A 227 -8.624 25.274 39.233 1.00 75.02 C ANISOU 1817 CA VAL A 227 8385 9892 10228 -996 -1555 -629 C ATOM 1818 C VAL A 227 -10.047 24.838 38.908 1.00 84.35 C ANISOU 1818 C VAL A 227 9325 11129 11593 -1140 -1677 -728 C ATOM 1819 O VAL A 227 -10.647 24.048 39.647 1.00 94.92 O ANISOU 1819 O VAL A 227 10542 12421 13102 -1288 -1552 -738 O ATOM 1820 CB VAL A 227 -8.602 26.568 40.070 1.00 58.95 C ANISOU 1820 CB VAL A 227 6258 7931 8210 -837 -1475 -536 C ATOM 1821 CG1 VAL A 227 -9.441 26.409 41.327 1.00 60.73 C ANISOU 1821 CG1 VAL A 227 6277 8183 8617 -884 -1316 -510 C ATOM 1822 CG2 VAL A 227 -7.175 26.936 40.433 1.00 60.77 C ANISOU 1822 CG2 VAL A 227 6706 8102 8281 -723 -1360 -459 C ATOM 1823 N PHE A 228 -10.607 25.326 37.798 1.00 77.66 N ANISOU 1823 N PHE A 228 8399 10391 10717 -1097 -1916 -797 N ATOM 1824 CA PHE A 228 -11.955 24.922 37.414 1.00 71.25 C ANISOU 1824 CA PHE A 228 7337 9660 10075 -1233 -2060 -912 C ATOM 1825 C PHE A 228 -11.994 23.458 36.992 1.00 76.18 C ANISOU 1825 C PHE A 228 8037 10157 10751 -1447 -2097 -1035 C ATOM 1826 O PHE A 228 -12.937 22.734 37.331 1.00 84.95 O ANISOU 1826 O PHE A 228 8949 11250 12079 -1641 -2075 -1099 O ATOM 1827 CB PHE A 228 -12.473 25.821 36.292 1.00 62.21 C ANISOU 1827 CB PHE A 228 6105 8682 8852 -1097 -2316 -961 C ATOM 1828 CG PHE A 228 -13.872 25.496 35.852 1.00 75.91 C ANISOU 1828 CG PHE A 228 7554 10540 10748 -1217 -2491 -1093 C ATOM 1829 CD1 PHE A 228 -14.961 25.925 36.592 1.00 75.86 C ANISOU 1829 CD1 PHE A 228 7241 10655 10926 -1233 -2442 -1061 C ATOM 1830 CD2 PHE A 228 -14.099 24.767 34.696 1.00 81.92 C ANISOU 1830 CD2 PHE A 228 8345 11309 11471 -1305 -2712 -1257 C ATOM 1831 CE1 PHE A 228 -16.250 25.629 36.191 1.00 79.63 C ANISOU 1831 CE1 PHE A 228 7426 11269 11560 -1350 -2605 -1183 C ATOM 1832 CE2 PHE A 228 -15.385 24.467 34.289 1.00 82.06 C ANISOU 1832 CE2 PHE A 228 8079 11454 11647 -1425 -2891 -1400 C ATOM 1833 CZ PHE A 228 -16.462 24.899 35.038 1.00 78.13 C ANISOU 1833 CZ PHE A 228 7255 11086 11344 -1455 -2835 -1359 C ATOM 1834 N THR A 229 -10.980 23.005 36.251 1.00 78.70 N ANISOU 1834 N THR A 229 8642 10381 10877 -1413 -2148 -1068 N ATOM 1835 CA THR A 229 -10.935 21.608 35.830 1.00 75.68 C ANISOU 1835 CA THR A 229 8377 9854 10525 -1595 -2186 -1194 C ATOM 1836 C THR A 229 -10.755 20.676 37.022 1.00 70.05 C ANISOU 1836 C THR A 229 7700 8969 9946 -1743 -1913 -1134 C ATOM 1837 O THR A 229 -11.409 19.629 37.103 1.00 81.75 O ANISOU 1837 O THR A 229 9104 10344 11613 -1963 -1904 -1227 O ATOM 1838 CB THR A 229 -9.812 21.403 34.811 1.00 72.01 C ANISOU 1838 CB THR A 229 8229 9340 9791 -1477 -2286 -1223 C ATOM 1839 OG1 THR A 229 -10.141 22.079 33.590 1.00 84.14 O ANISOU 1839 OG1 THR A 229 9721 11034 11213 -1350 -2552 -1295 O ATOM 1840 CG2 THR A 229 -9.602 19.923 34.524 1.00 79.41 C ANISOU 1840 CG2 THR A 229 9340 10093 10739 -1642 -2288 -1345 C ATOM 1841 N VAL A 230 -9.884 21.044 37.963 1.00 76.40 N ANISOU 1841 N VAL A 230 8620 9744 10665 -1623 -1687 -981 N ATOM 1842 CA VAL A 230 -9.621 20.181 39.110 1.00 81.08 C ANISOU 1842 CA VAL A 230 9273 10190 11346 -1715 -1412 -908 C ATOM 1843 C VAL A 230 -10.827 20.139 40.043 1.00 79.90 C ANISOU 1843 C VAL A 230 8814 10075 11468 -1837 -1298 -875 C ATOM 1844 O VAL A 230 -11.174 19.080 40.581 1.00 86.95 O ANISOU 1844 O VAL A 230 9680 10829 12526 -2013 -1149 -875 O ATOM 1845 CB VAL A 230 -8.347 20.644 39.840 1.00 63.91 C ANISOU 1845 CB VAL A 230 7290 8010 8983 -1525 -1222 -768 C ATOM 1846 CG1 VAL A 230 -8.155 19.865 41.128 1.00 59.78 C ANISOU 1846 CG1 VAL A 230 6804 7373 8538 -1575 -928 -681 C ATOM 1847 CG2 VAL A 230 -7.134 20.477 38.939 1.00 69.49 C ANISOU 1847 CG2 VAL A 230 8296 8674 9433 -1427 -1305 -790 C ATOM 1848 N LYS A 231 -11.490 21.280 40.245 1.00 71.70 N ANISOU 1848 N LYS A 231 7540 9218 10483 -1739 -1356 -836 N ATOM 1849 CA LYS A 231 -12.627 21.314 41.160 1.00 74.41 C ANISOU 1849 CA LYS A 231 7578 9626 11069 -1822 -1238 -785 C ATOM 1850 C LYS A 231 -13.823 20.553 40.598 1.00 78.78 C ANISOU 1850 C LYS A 231 7912 10171 11850 -2068 -1374 -913 C ATOM 1851 O LYS A 231 -14.565 19.913 41.352 1.00 67.74 O ANISOU 1851 O LYS A 231 6330 8724 10683 -2230 -1215 -875 O ATOM 1852 CB LYS A 231 -13.011 22.759 41.479 1.00 63.54 C ANISOU 1852 CB LYS A 231 6024 8450 9670 -1626 -1275 -717 C ATOM 1853 CG LYS A 231 -12.091 23.439 42.482 1.00 75.12 C ANISOU 1853 CG LYS A 231 7625 9916 11002 -1421 -1080 -585 C ATOM 1854 CD LYS A 231 -12.648 24.784 42.923 1.00 77.95 C ANISOU 1854 CD LYS A 231 7789 10448 11379 -1244 -1103 -528 C ATOM 1855 CE LYS A 231 -11.747 25.449 43.953 1.00 81.25 C ANISOU 1855 CE LYS A 231 8340 10858 11675 -1045 -925 -426 C ATOM 1856 NZ LYS A 231 -11.560 24.609 45.168 1.00 83.63 N ANISOU 1856 NZ LYS A 231 8663 11080 12030 -1081 -648 -348 N ATOM 1857 N GLU A 232 -14.029 20.607 39.280 1.00 69.17 N ANISOU 1857 N GLU A 232 6702 9006 10575 -2097 -1666 -1067 N ATOM 1858 CA GLU A 232 -15.153 19.886 38.693 1.00 77.09 C ANISOU 1858 CA GLU A 232 7486 10011 11794 -2335 -1829 -1222 C ATOM 1859 C GLU A 232 -14.853 18.402 38.525 1.00 93.99 C ANISOU 1859 C GLU A 232 9808 11896 14008 -2559 -1778 -1310 C ATOM 1860 O GLU A 232 -15.781 17.586 38.513 1.00114.31 O ANISOU 1860 O GLU A 232 12187 14404 16842 -2815 -1802 -1402 O ATOM 1861 CB GLU A 232 -15.544 20.501 37.347 1.00 92.62 C ANISOU 1861 CB GLU A 232 9382 12152 13659 -2257 -2175 -1370 C ATOM 1862 CG GLU A 232 -14.590 20.194 36.205 1.00113.26 C ANISOU 1862 CG GLU A 232 12322 14681 16030 -2189 -2344 -1475 C ATOM 1863 CD GLU A 232 -15.148 20.610 34.858 1.00133.09 C ANISOU 1863 CD GLU A 232 14736 17368 18463 -2125 -2690 -1638 C ATOM 1864 OE1 GLU A 232 -16.277 21.143 34.821 1.00123.28 O ANISOU 1864 OE1 GLU A 232 13168 16318 17356 -2137 -2801 -1673 O ATOM 1865 OE2 GLU A 232 -14.460 20.400 33.837 1.00152.24 O ANISOU 1865 OE2 GLU A 232 17411 19755 20677 -2042 -2848 -1728 O ATOM 1866 N ALA A 233 -13.577 18.033 38.393 1.00 95.91 N ANISOU 1866 N ALA A 233 10418 11989 14035 -2469 -1707 -1285 N ATOM 1867 CA ALA A 233 -13.226 16.618 38.329 1.00 88.36 C ANISOU 1867 CA ALA A 233 9669 10769 13133 -2652 -1628 -1353 C ATOM 1868 C ALA A 233 -13.394 15.954 39.689 1.00 85.88 C ANISOU 1868 C ALA A 233 9300 10311 13017 -2771 -1288 -1207 C ATOM 1869 O ALA A 233 -13.821 14.796 39.773 1.00 92.96 O ANISOU 1869 O ALA A 233 10186 11010 14126 -3016 -1222 -1267 O ATOM 1870 CB ALA A 233 -11.796 16.450 37.818 1.00 62.93 C ANISOU 1870 CB ALA A 233 6853 7457 9600 -2486 -1639 -1352 C ATOM 1871 N ALA A 234 -13.064 16.671 40.765 1.00 71.31 N ANISOU 1871 N ALA A 234 7425 8558 11110 -2592 -1065 -1017 N ATOM 1872 CA ALA A 234 -13.292 16.141 42.104 1.00 77.94 C ANISOU 1872 CA ALA A 234 8190 9302 12122 -2661 -732 -861 C ATOM 1873 C ALA A 234 -14.776 16.100 42.442 1.00 82.68 C ANISOU 1873 C ALA A 234 8386 9979 13051 -2852 -721 -859 C ATOM 1874 O ALA A 234 -15.206 15.258 43.238 1.00 83.81 O ANISOU 1874 O ALA A 234 8447 9984 13415 -3013 -482 -773 O ATOM 1875 CB ALA A 234 -12.532 16.973 43.137 1.00 60.99 C ANISOU 1875 CB ALA A 234 6119 7260 9796 -2387 -523 -680 C ATOM 1876 N ALA A 235 -15.571 16.996 41.851 1.00 83.89 N ANISOU 1876 N ALA A 235 8278 10357 13239 -2827 -964 -941 N ATOM 1877 CA ALA A 235 -17.008 16.990 42.101 1.00 83.02 C ANISOU 1877 CA ALA A 235 7754 10357 13433 -3001 -974 -945 C ATOM 1878 C ALA A 235 -17.678 15.760 41.503 1.00 84.05 C ANISOU 1878 C ALA A 235 7801 10314 13819 -3346 -1072 -1105 C ATOM 1879 O ALA A 235 -18.676 15.273 42.046 1.00 95.79 O ANISOU 1879 O ALA A 235 8998 11781 15616 -3558 -948 -1061 O ATOM 1880 CB ALA A 235 -17.643 18.265 41.548 1.00 70.69 C ANISOU 1880 CB ALA A 235 5953 9092 11814 -2860 -1225 -1001 C ATOM 1881 N GLN A 236 -17.152 15.248 40.393 1.00 74.68 N ANISOU 1881 N GLN A 236 6860 9001 12515 -3403 -1293 -1291 N ATOM 1882 CA GLN A 236 -17.657 14.034 39.767 1.00 78.26 C ANISOU 1882 CA GLN A 236 7291 9253 13192 -3724 -1408 -1475 C ATOM 1883 C GLN A 236 -16.980 12.776 40.295 1.00 87.86 C ANISOU 1883 C GLN A 236 8801 10123 14459 -3845 -1145 -1412 C ATOM 1884 O GLN A 236 -17.182 11.694 39.733 1.00 91.08 O ANISOU 1884 O GLN A 236 9282 10305 15021 -4096 -1236 -1576 O ATOM 1885 CB GLN A 236 -17.489 14.115 38.248 1.00 78.67 C ANISOU 1885 CB GLN A 236 7461 9354 13075 -3699 -1802 -1729 C ATOM 1886 CG GLN A 236 -18.557 14.935 37.547 1.00 87.20 C ANISOU 1886 CG GLN A 236 8181 10733 14218 -3694 -2103 -1857 C ATOM 1887 CD GLN A 236 -19.898 14.227 37.507 1.00 97.56 C ANISOU 1887 CD GLN A 236 9124 12024 15920 -4040 -2174 -1984 C ATOM 1888 OE1 GLN A 236 -19.965 13.008 37.344 1.00 98.91 O ANISOU 1888 OE1 GLN A 236 9396 11934 16251 -4299 -2155 -2088 O ATOM 1889 NE2 GLN A 236 -20.974 14.989 37.661 1.00105.35 N ANISOU 1889 NE2 GLN A 236 9707 13296 17025 -4026 -2238 -1952 N ATOM 1890 N GLN A 237 -16.189 12.891 41.356 1.00 83.50 N ANISOU 1890 N GLN A 237 8425 9524 13777 -3662 -827 -1187 N ATOM 1891 CA GLN A 237 -15.466 11.752 41.907 1.00 82.95 C ANISOU 1891 CA GLN A 237 8659 9145 13713 -3722 -554 -1103 C ATOM 1892 C GLN A 237 -15.226 11.987 43.398 1.00 86.85 C ANISOU 1892 C GLN A 237 9129 9672 14196 -3563 -167 -824 C ATOM 1893 O GLN A 237 -14.100 11.920 43.892 1.00 76.99 O ANISOU 1893 O GLN A 237 8187 8357 12708 -3354 17 -710 O ATOM 1894 CB GLN A 237 -14.157 11.528 41.149 1.00 80.74 C ANISOU 1894 CB GLN A 237 8817 8758 13103 -3566 -667 -1194 C ATOM 1895 CG GLN A 237 -13.555 10.143 41.320 1.00 96.37 C ANISOU 1895 CG GLN A 237 11123 10385 15106 -3676 -479 -1188 C ATOM 1896 CD GLN A 237 -12.322 9.941 40.461 1.00103.35 C ANISOU 1896 CD GLN A 237 12421 11194 15652 -3510 -620 -1292 C ATOM 1897 OE1 GLN A 237 -11.859 10.866 39.793 1.00101.57 O ANISOU 1897 OE1 GLN A 237 12238 11184 15172 -3306 -833 -1344 O ATOM 1898 NE2 GLN A 237 -11.785 8.727 40.473 1.00 99.43 N ANISOU 1898 NE2 GLN A 237 12236 10390 15153 -3587 -489 -1310 N ATOM 1899 N GLN A 238 -16.300 12.272 44.133 1.00 93.87 N ANISOU 1899 N GLN A 238 9643 10686 15336 -3644 -44 -714 N ATOM 1900 CA GLN A 238 -16.203 12.570 45.556 1.00 83.97 C ANISOU 1900 CA GLN A 238 8331 9503 14070 -3467 311 -453 C ATOM 1901 C GLN A 238 -16.014 11.327 46.414 1.00 97.14 C ANISOU 1901 C GLN A 238 10148 10883 15878 -3576 674 -303 C ATOM 1902 O GLN A 238 -15.840 11.456 47.631 1.00 96.17 O ANISOU 1902 O GLN A 238 10017 10805 15717 -3401 994 -78 O ATOM 1903 CB GLN A 238 -17.448 13.335 46.014 1.00 84.71 C ANISOU 1903 CB GLN A 238 7967 9852 14368 -3487 317 -379 C ATOM 1904 CG GLN A 238 -17.719 14.598 45.213 1.00106.98 C ANISOU 1904 CG GLN A 238 10631 12961 17057 -3359 -24 -510 C ATOM 1905 CD GLN A 238 -18.910 15.378 45.732 1.00122.15 C ANISOU 1905 CD GLN A 238 12115 15147 19151 -3336 0 -423 C ATOM 1906 OE1 GLN A 238 -19.322 15.212 46.879 1.00125.80 O ANISOU 1906 OE1 GLN A 238 12421 15621 19755 -3322 306 -225 O ATOM 1907 NE2 GLN A 238 -19.471 16.234 44.886 1.00128.56 N ANISOU 1907 NE2 GLN A 238 12728 16183 19935 -3307 -316 -562 N ATOM 1908 N GLU A 239 -16.046 10.133 45.821 1.00111.00 N ANISOU 1908 N GLU A 239 12047 12341 17786 -3843 636 -423 N ATOM 1909 CA GLU A 239 -15.751 8.913 46.559 1.00105.49 C ANISOU 1909 CA GLU A 239 11552 11331 17199 -3929 985 -280 C ATOM 1910 C GLU A 239 -14.259 8.701 46.769 1.00 96.69 C ANISOU 1910 C GLU A 239 10899 10117 15723 -3657 1114 -220 C ATOM 1911 O GLU A 239 -13.878 7.856 47.587 1.00104.21 O ANISOU 1911 O GLU A 239 12040 10860 16696 -3628 1451 -53 O ATOM 1912 CB GLU A 239 -16.346 7.697 45.839 1.00 84.95 C ANISOU 1912 CB GLU A 239 8948 8418 14913 -4325 893 -444 C ATOM 1913 CG GLU A 239 -15.736 7.403 44.472 1.00 90.35 C ANISOU 1913 CG GLU A 239 9918 8984 15426 -4370 548 -721 C ATOM 1914 CD GLU A 239 -16.351 8.227 43.354 1.00 99.39 C ANISOU 1914 CD GLU A 239 10815 10377 16571 -4427 114 -955 C ATOM 1915 OE1 GLU A 239 -17.066 9.207 43.653 1.00114.97 O ANISOU 1915 OE1 GLU A 239 12432 12646 18604 -4368 75 -891 O ATOM 1916 OE2 GLU A 239 -16.124 7.892 42.172 1.00 85.92 O ANISOU 1916 OE2 GLU A 239 9278 8576 14791 -4510 -187 -1202 O ATOM 1917 N SER A 240 -13.413 9.442 46.059 1.00 89.45 N ANISOU 1917 N SER A 240 10158 9352 14478 -3450 863 -339 N ATOM 1918 CA SER A 240 -11.966 9.339 46.187 1.00 79.64 C ANISOU 1918 CA SER A 240 9322 8062 12877 -3182 956 -291 C ATOM 1919 C SER A 240 -11.474 10.418 47.144 1.00 79.52 C ANISOU 1919 C SER A 240 9257 8318 12641 -2850 1098 -123 C ATOM 1920 O SER A 240 -11.595 11.613 46.852 1.00 85.64 O ANISOU 1920 O SER A 240 9865 9354 13320 -2738 888 -177 O ATOM 1921 CB SER A 240 -11.289 9.479 44.824 1.00 70.07 C ANISOU 1921 CB SER A 240 8332 6853 11439 -3152 609 -512 C ATOM 1922 OG SER A 240 -9.878 9.445 44.949 1.00 89.37 O ANISOU 1922 OG SER A 240 11139 9286 13532 -2883 699 -455 O ATOM 1923 N ALA A 241 -10.922 9.996 48.283 1.00 90.66 N ANISOU 1923 N ALA A 241 10819 9660 13966 -2684 1452 75 N ATOM 1924 CA ALA A 241 -10.419 10.957 49.258 1.00 88.20 C ANISOU 1924 CA ALA A 241 10473 9601 13439 -2356 1589 217 C ATOM 1925 C ALA A 241 -9.153 11.648 48.768 1.00 96.74 C ANISOU 1925 C ALA A 241 11791 10813 14152 -2116 1409 132 C ATOM 1926 O ALA A 241 -8.937 12.827 49.073 1.00 91.94 O ANISOU 1926 O ALA A 241 11076 10457 13400 -1910 1343 151 O ATOM 1927 CB ALA A 241 -10.165 10.266 50.597 1.00 73.56 C ANISOU 1927 CB ALA A 241 8722 7652 11576 -2220 2015 446 C ATOM 1928 N THR A 242 -8.308 10.939 48.015 1.00 88.51 N ANISOU 1928 N THR A 242 11069 9601 12959 -2137 1333 40 N ATOM 1929 CA THR A 242 -7.091 11.556 47.498 1.00 85.32 C ANISOU 1929 CA THR A 242 10877 9327 12214 -1919 1171 -28 C ATOM 1930 C THR A 242 -7.400 12.597 46.432 1.00 87.44 C ANISOU 1930 C THR A 242 10986 9764 12473 -1967 806 -183 C ATOM 1931 O THR A 242 -6.675 13.591 46.310 1.00 87.91 O ANISOU 1931 O THR A 242 11080 10016 12307 -1763 696 -191 O ATOM 1932 CB THR A 242 -6.151 10.490 46.935 1.00 82.16 C ANISOU 1932 CB THR A 242 10856 8711 11650 -1914 1189 -79 C ATOM 1933 OG1 THR A 242 -6.674 9.995 45.696 1.00 96.95 O ANISOU 1933 OG1 THR A 242 12744 10428 13663 -2169 940 -259 O ATOM 1934 CG2 THR A 242 -6.010 9.334 47.915 1.00 85.16 C ANISOU 1934 CG2 THR A 242 11396 8883 12078 -1893 1558 76 C ATOM 1935 N THR A 243 -8.463 12.389 45.651 1.00 93.87 N ANISOU 1935 N THR A 243 11624 10510 13532 -2229 616 -306 N ATOM 1936 CA THR A 243 -8.864 13.392 44.670 1.00 89.33 C ANISOU 1936 CA THR A 243 10879 10114 12949 -2252 279 -442 C ATOM 1937 C THR A 243 -9.369 14.656 45.357 1.00 78.29 C ANISOU 1937 C THR A 243 9190 8967 11590 -2127 295 -356 C ATOM 1938 O THR A 243 -9.128 15.770 44.877 1.00 70.09 O ANISOU 1938 O THR A 243 8108 8111 10410 -1995 95 -405 O ATOM 1939 CB THR A 243 -9.930 12.818 43.735 1.00 88.84 C ANISOU 1939 CB THR A 243 10678 9938 13141 -2551 73 -604 C ATOM 1940 OG1 THR A 243 -9.431 11.626 43.115 1.00 86.30 O ANISOU 1940 OG1 THR A 243 10654 9361 12775 -2654 56 -698 O ATOM 1941 CG2 THR A 243 -10.294 13.826 42.653 1.00 74.23 C ANISOU 1941 CG2 THR A 243 8673 8286 11243 -2538 -282 -748 C ATOM 1942 N GLN A 244 -10.063 14.504 46.488 1.00 75.24 N ANISOU 1942 N GLN A 244 8612 8586 11390 -2152 541 -222 N ATOM 1943 CA GLN A 244 -10.492 15.670 47.251 1.00 73.88 C ANISOU 1943 CA GLN A 244 8190 8650 11230 -1994 581 -134 C ATOM 1944 C GLN A 244 -9.305 16.361 47.909 1.00 77.94 C ANISOU 1944 C GLN A 244 8881 9279 11454 -1686 679 -56 C ATOM 1945 O GLN A 244 -9.283 17.591 48.031 1.00 81.70 O ANISOU 1945 O GLN A 244 9243 9952 11848 -1527 576 -59 O ATOM 1946 CB GLN A 244 -11.526 15.261 48.299 1.00 60.44 C ANISOU 1946 CB GLN A 244 6243 6931 9790 -2082 837 4 C ATOM 1947 CG GLN A 244 -12.735 14.541 47.726 1.00 72.08 C ANISOU 1947 CG GLN A 244 7506 8291 11589 -2415 755 -71 C ATOM 1948 CD GLN A 244 -13.380 15.307 46.591 1.00 79.37 C ANISOU 1948 CD GLN A 244 8234 9360 12562 -2504 389 -242 C ATOM 1949 OE1 GLN A 244 -13.480 14.807 45.471 1.00 93.95 O ANISOU 1949 OE1 GLN A 244 10144 11098 14454 -2690 167 -408 O ATOM 1950 NE2 GLN A 244 -13.825 16.526 46.874 1.00 81.91 N ANISOU 1950 NE2 GLN A 244 8328 9933 12862 -2351 323 -206 N ATOM 1951 N LYS A 245 -8.306 15.585 48.337 1.00 81.70 N ANISOU 1951 N LYS A 245 9636 9632 11774 -1596 875 7 N ATOM 1952 CA LYS A 245 -7.102 16.182 48.902 1.00 73.63 C ANISOU 1952 CA LYS A 245 8780 8729 10469 -1310 948 58 C ATOM 1953 C LYS A 245 -6.300 16.910 47.832 1.00 75.47 C ANISOU 1953 C LYS A 245 9135 9036 10506 -1252 671 -61 C ATOM 1954 O LYS A 245 -5.769 17.999 48.080 1.00 67.37 O ANISOU 1954 O LYS A 245 8088 8175 9335 -1064 615 -55 O ATOM 1955 CB LYS A 245 -6.247 15.108 49.575 1.00 76.16 C ANISOU 1955 CB LYS A 245 9362 8915 10659 -1217 1223 154 C ATOM 1956 CG LYS A 245 -4.964 15.638 50.201 1.00102.76 C ANISOU 1956 CG LYS A 245 12891 12424 13728 -918 1301 196 C ATOM 1957 CD LYS A 245 -4.092 14.507 50.725 1.00124.46 C ANISOU 1957 CD LYS A 245 15917 15050 16324 -814 1555 281 C ATOM 1958 CE LYS A 245 -2.840 15.042 51.403 1.00127.99 C ANISOU 1958 CE LYS A 245 16488 15671 16472 -508 1626 312 C ATOM 1959 NZ LYS A 245 -2.029 15.893 50.488 1.00121.26 N ANISOU 1959 NZ LYS A 245 15694 14925 15454 -471 1355 196 N ATOM 1960 N ALA A 246 -6.204 16.325 46.636 1.00 71.72 N ANISOU 1960 N ALA A 246 8790 8435 10026 -1407 498 -168 N ATOM 1961 CA ALA A 246 -5.464 16.967 45.555 1.00 69.47 C ANISOU 1961 CA ALA A 246 8623 8222 9550 -1341 248 -261 C ATOM 1962 C ALA A 246 -6.141 18.255 45.108 1.00 80.25 C ANISOU 1962 C ALA A 246 9749 9754 10989 -1337 25 -312 C ATOM 1963 O ALA A 246 -5.464 19.222 44.740 1.00 84.01 O ANISOU 1963 O ALA A 246 10272 10346 11302 -1197 -102 -326 O ATOM 1964 CB ALA A 246 -5.314 16.004 44.379 1.00 55.85 C ANISOU 1964 CB ALA A 246 7089 6332 7802 -1488 114 -368 C ATOM 1965 N GLU A 247 -7.475 18.288 45.134 1.00 83.91 N ANISOU 1965 N GLU A 247 9949 10230 11701 -1486 -18 -334 N ATOM 1966 CA GLU A 247 -8.193 19.493 44.734 1.00 73.67 C ANISOU 1966 CA GLU A 247 8421 9101 10470 -1462 -222 -377 C ATOM 1967 C GLU A 247 -7.877 20.658 45.664 1.00 74.07 C ANISOU 1967 C GLU A 247 8402 9304 10437 -1238 -136 -291 C ATOM 1968 O GLU A 247 -7.746 21.803 45.214 1.00 84.87 O ANISOU 1968 O GLU A 247 9730 10786 11729 -1134 -306 -321 O ATOM 1969 CB GLU A 247 -9.698 19.215 44.696 1.00 77.04 C ANISOU 1969 CB GLU A 247 8558 9531 11181 -1658 -260 -409 C ATOM 1970 CG GLU A 247 -10.565 20.447 44.484 1.00 97.63 C ANISOU 1970 CG GLU A 247 10897 12334 13864 -1604 -431 -432 C ATOM 1971 CD GLU A 247 -11.064 21.039 45.789 1.00121.80 C ANISOU 1971 CD GLU A 247 13759 15510 17009 -1484 -240 -311 C ATOM 1972 OE1 GLU A 247 -11.375 20.261 46.715 1.00131.65 O ANISOU 1972 OE1 GLU A 247 14953 16690 18379 -1544 2 -223 O ATOM 1973 OE2 GLU A 247 -11.138 22.282 45.890 1.00128.30 O ANISOU 1973 OE2 GLU A 247 14491 16486 17771 -1317 -325 -299 O ATOM 1974 N LYS A 248 -7.740 20.386 46.963 1.00 69.75 N ANISOU 1974 N LYS A 248 7851 8753 9898 -1150 129 -186 N ATOM 1975 CA LYS A 248 -7.420 21.451 47.907 1.00 73.62 C ANISOU 1975 CA LYS A 248 8286 9385 10299 -922 206 -127 C ATOM 1976 C LYS A 248 -5.957 21.867 47.801 1.00 71.16 C ANISOU 1976 C LYS A 248 8209 9091 9736 -765 177 -141 C ATOM 1977 O LYS A 248 -5.638 23.058 47.900 1.00 78.07 O ANISOU 1977 O LYS A 248 9050 10075 10538 -624 88 -156 O ATOM 1978 CB LYS A 248 -7.753 21.006 49.331 1.00 56.06 C ANISOU 1978 CB LYS A 248 5983 7173 8145 -848 497 -13 C ATOM 1979 CG LYS A 248 -9.237 20.797 49.579 1.00 80.82 C ANISOU 1979 CG LYS A 248 8836 10329 11544 -980 546 27 C ATOM 1980 CD LYS A 248 -9.511 20.425 51.027 1.00101.53 C ANISOU 1980 CD LYS A 248 11383 12978 14215 -869 858 168 C ATOM 1981 CE LYS A 248 -11.004 20.315 51.292 1.00118.44 C ANISOU 1981 CE LYS A 248 13209 15166 16625 -990 915 226 C ATOM 1982 NZ LYS A 248 -11.710 21.595 51.009 1.00129.50 N ANISOU 1982 NZ LYS A 248 14389 16744 18070 -926 711 173 N ATOM 1983 N GLU A 249 -5.056 20.903 47.601 1.00 64.27 N ANISOU 1983 N GLU A 249 7574 8113 8735 -786 254 -137 N ATOM 1984 CA GLU A 249 -3.638 21.228 47.472 1.00 67.17 C ANISOU 1984 CA GLU A 249 8145 8514 8861 -642 233 -144 C ATOM 1985 C GLU A 249 -3.364 22.017 46.197 1.00 62.09 C ANISOU 1985 C GLU A 249 7529 7903 8159 -668 -32 -213 C ATOM 1986 O GLU A 249 -2.602 22.991 46.216 1.00 64.95 O ANISOU 1986 O GLU A 249 7920 8351 8406 -538 -92 -212 O ATOM 1987 CB GLU A 249 -2.802 19.947 47.507 1.00 79.36 C ANISOU 1987 CB GLU A 249 9934 9946 10274 -646 381 -116 C ATOM 1988 CG GLU A 249 -1.458 20.038 46.791 1.00111.15 C ANISOU 1988 CG GLU A 249 14178 13989 14065 -568 290 -142 C ATOM 1989 CD GLU A 249 -0.459 20.941 47.495 1.00136.24 C ANISOU 1989 CD GLU A 249 17368 17311 17088 -365 333 -119 C ATOM 1990 OE1 GLU A 249 -0.707 21.328 48.656 1.00146.41 O ANISOU 1990 OE1 GLU A 249 18538 18674 18418 -257 459 -88 O ATOM 1991 OE2 GLU A 249 0.581 21.262 46.882 1.00133.47 O ANISOU 1991 OE2 GLU A 249 17139 17002 16572 -308 239 -135 O ATOM 1992 N VAL A 250 -3.974 21.612 45.081 1.00 65.90 N ANISOU 1992 N VAL A 250 7999 8317 8721 -829 -190 -273 N ATOM 1993 CA VAL A 250 -3.774 22.326 43.823 1.00 66.83 C ANISOU 1993 CA VAL A 250 8145 8475 8770 -828 -434 -326 C ATOM 1994 C VAL A 250 -4.336 23.740 43.916 1.00 76.32 C ANISOU 1994 C VAL A 250 9150 9794 10053 -755 -542 -323 C ATOM 1995 O VAL A 250 -3.716 24.702 43.448 1.00 79.44 O ANISOU 1995 O VAL A 250 9593 10243 10348 -658 -652 -317 O ATOM 1996 CB VAL A 250 -4.401 21.538 42.658 1.00 69.68 C ANISOU 1996 CB VAL A 250 8528 8754 9195 -996 -588 -409 C ATOM 1997 CG1 VAL A 250 -4.500 22.405 41.418 1.00 52.79 C ANISOU 1997 CG1 VAL A 250 6363 6690 7007 -970 -845 -458 C ATOM 1998 CG2 VAL A 250 -3.585 20.288 42.366 1.00 74.22 C ANISOU 1998 CG2 VAL A 250 9362 9201 9636 -1029 -513 -421 C ATOM 1999 N THR A 251 -5.512 23.890 44.532 1.00 80.10 N ANISOU 1999 N THR A 251 9406 10310 10718 -794 -503 -319 N ATOM 2000 CA THR A 251 -6.105 25.215 44.679 1.00 76.04 C ANISOU 2000 CA THR A 251 8711 9905 10275 -701 -595 -315 C ATOM 2001 C THR A 251 -5.244 26.110 45.563 1.00 66.93 C ANISOU 2001 C THR A 251 7609 8800 9021 -518 -505 -275 C ATOM 2002 O THR A 251 -5.093 27.306 45.290 1.00 76.21 O ANISOU 2002 O THR A 251 8762 10023 10173 -425 -624 -281 O ATOM 2003 CB THR A 251 -7.520 25.098 45.247 1.00 70.47 C ANISOU 2003 CB THR A 251 7751 9247 9778 -764 -545 -307 C ATOM 2004 OG1 THR A 251 -8.318 24.279 44.383 1.00 77.41 O ANISOU 2004 OG1 THR A 251 8562 10081 10768 -956 -652 -367 O ATOM 2005 CG2 THR A 251 -8.167 26.470 45.368 1.00 62.23 C ANISOU 2005 CG2 THR A 251 6529 8323 8792 -643 -645 -304 C ATOM 2006 N ARG A 252 -4.663 25.545 46.625 1.00 68.82 N ANISOU 2006 N ARG A 252 7924 9024 9199 -459 -298 -238 N ATOM 2007 CA ARG A 252 -3.821 26.340 47.513 1.00 68.93 C ANISOU 2007 CA ARG A 252 7980 9097 9112 -280 -224 -227 C ATOM 2008 C ARG A 252 -2.536 26.783 46.824 1.00 74.75 C ANISOU 2008 C ARG A 252 8888 9821 9693 -245 -321 -242 C ATOM 2009 O ARG A 252 -2.043 27.885 47.089 1.00 77.26 O ANISOU 2009 O ARG A 252 9196 10180 9979 -136 -367 -256 O ATOM 2010 CB ARG A 252 -3.497 25.550 48.780 1.00 61.90 C ANISOU 2010 CB ARG A 252 7133 8216 8170 -202 20 -186 C ATOM 2011 CG ARG A 252 -2.917 26.395 49.905 1.00 88.89 C ANISOU 2011 CG ARG A 252 10541 11725 11509 4 94 -197 C ATOM 2012 CD ARG A 252 -2.282 25.530 50.981 1.00114.19 C ANISOU 2012 CD ARG A 252 13840 14952 14594 111 324 -160 C ATOM 2013 NE ARG A 252 -1.051 24.900 50.514 1.00134.43 N ANISOU 2013 NE ARG A 252 16609 17478 16989 92 336 -161 N ATOM 2014 CZ ARG A 252 -0.296 24.093 51.252 1.00143.57 C ANISOU 2014 CZ ARG A 252 17888 18658 18003 195 521 -129 C ATOM 2015 NH1 ARG A 252 -0.646 23.811 52.500 1.00156.58 N ANISOU 2015 NH1 ARG A 252 19477 20361 19654 328 715 -88 N ATOM 2016 NH2 ARG A 252 0.809 23.566 50.743 1.00135.47 N ANISOU 2016 NH2 ARG A 252 17045 17612 16816 187 520 -128 N ATOM 2017 N MET A 253 -1.981 25.946 45.944 1.00 61.84 N ANISOU 2017 N MET A 253 7407 8125 7963 -333 -351 -238 N ATOM 2018 CA MET A 253 -0.754 26.319 45.246 1.00 67.55 C ANISOU 2018 CA MET A 253 8280 8852 8532 -293 -429 -231 C ATOM 2019 C MET A 253 -1.011 27.401 44.205 1.00 78.37 C ANISOU 2019 C MET A 253 9600 10230 9946 -303 -632 -235 C ATOM 2020 O MET A 253 -0.162 28.274 43.988 1.00 84.98 O ANISOU 2020 O MET A 253 10486 11083 10717 -236 -681 -215 O ATOM 2021 CB MET A 253 -0.121 25.089 44.596 1.00 56.37 C ANISOU 2021 CB MET A 253 7052 7380 6984 -354 -397 -220 C ATOM 2022 CG MET A 253 0.877 24.362 45.483 1.00 65.87 C ANISOU 2022 CG MET A 253 8382 8599 8045 -269 -202 -194 C ATOM 2023 SD MET A 253 2.286 25.400 45.925 1.00 83.79 S ANISOU 2023 SD MET A 253 10683 10974 10180 -120 -194 -185 S ATOM 2024 CE MET A 253 2.902 25.848 44.302 1.00 60.02 C ANISOU 2024 CE MET A 253 7764 7950 7091 -168 -380 -158 C ATOM 2025 N VAL A 254 -2.171 27.359 43.547 1.00 72.74 N ANISOU 2025 N VAL A 254 8784 9507 9348 -384 -747 -257 N ATOM 2026 CA VAL A 254 -2.499 28.386 42.562 1.00 75.05 C ANISOU 2026 CA VAL A 254 9028 9818 9669 -363 -934 -253 C ATOM 2027 C VAL A 254 -2.636 29.746 43.236 1.00 77.61 C ANISOU 2027 C VAL A 254 9247 10172 10070 -253 -938 -243 C ATOM 2028 O VAL A 254 -2.197 30.769 42.696 1.00 78.79 O ANISOU 2028 O VAL A 254 9433 10311 10194 -193 -1029 -214 O ATOM 2029 CB VAL A 254 -3.774 27.999 41.791 1.00 70.52 C ANISOU 2029 CB VAL A 254 8346 9255 9195 -457 -1061 -296 C ATOM 2030 CG1 VAL A 254 -4.237 29.149 40.910 1.00 65.80 C ANISOU 2030 CG1 VAL A 254 7679 8701 8623 -393 -1242 -286 C ATOM 2031 CG2 VAL A 254 -3.524 26.755 40.954 1.00 68.50 C ANISOU 2031 CG2 VAL A 254 8226 8948 8851 -558 -1094 -327 C ATOM 2032 N ILE A 255 -3.238 29.780 44.426 1.00 73.71 N ANISOU 2032 N ILE A 255 8629 9708 9670 -216 -831 -263 N ATOM 2033 CA ILE A 255 -3.359 31.035 45.163 1.00 65.37 C ANISOU 2033 CA ILE A 255 7489 8674 8674 -90 -832 -272 C ATOM 2034 C ILE A 255 -1.983 31.557 45.557 1.00 67.19 C ANISOU 2034 C ILE A 255 7842 8879 8808 -19 -788 -273 C ATOM 2035 O ILE A 255 -1.720 32.765 45.501 1.00 72.96 O ANISOU 2035 O ILE A 255 8572 9582 9569 51 -860 -277 O ATOM 2036 CB ILE A 255 -4.273 30.844 46.388 1.00 61.28 C ANISOU 2036 CB ILE A 255 6819 8212 8252 -40 -713 -288 C ATOM 2037 CG1 ILE A 255 -5.697 30.510 45.940 1.00 54.53 C ANISOU 2037 CG1 ILE A 255 5800 7396 7523 -120 -776 -285 C ATOM 2038 CG2 ILE A 255 -4.262 32.083 47.271 1.00 57.69 C ANISOU 2038 CG2 ILE A 255 6310 7779 7831 120 -706 -314 C ATOM 2039 CD1 ILE A 255 -6.664 30.296 47.084 1.00 59.28 C ANISOU 2039 CD1 ILE A 255 6228 8066 8230 -75 -645 -276 C ATOM 2040 N ILE A 256 -1.079 30.657 45.947 1.00 65.64 N ANISOU 2040 N ILE A 256 7750 8690 8497 -36 -668 -272 N ATOM 2041 CA ILE A 256 0.268 31.074 46.325 1.00 57.16 C ANISOU 2041 CA ILE A 256 6770 7621 7326 27 -630 -283 C ATOM 2042 C ILE A 256 1.031 31.592 45.111 1.00 60.97 C ANISOU 2042 C ILE A 256 7345 8060 7761 -17 -745 -235 C ATOM 2043 O ILE A 256 1.720 32.616 45.187 1.00 64.90 O ANISOU 2043 O ILE A 256 7851 8533 8274 24 -782 -238 O ATOM 2044 CB ILE A 256 1.011 29.915 47.014 1.00 66.51 C ANISOU 2044 CB ILE A 256 8041 8849 8381 43 -469 -286 C ATOM 2045 CG1 ILE A 256 0.383 29.615 48.376 1.00 60.86 C ANISOU 2045 CG1 ILE A 256 7234 8184 7707 130 -330 -317 C ATOM 2046 CG2 ILE A 256 2.491 30.238 47.165 1.00 72.38 C ANISOU 2046 CG2 ILE A 256 8874 9622 9004 92 -451 -296 C ATOM 2047 CD1 ILE A 256 1.033 28.461 49.109 1.00 56.07 C ANISOU 2047 CD1 ILE A 256 6718 7622 6966 176 -151 -306 C ATOM 2048 N MET A 257 0.914 30.906 43.972 1.00 61.78 N ANISOU 2048 N MET A 257 7516 8148 7809 -96 -802 -189 N ATOM 2049 CA MET A 257 1.649 31.325 42.781 1.00 61.91 C ANISOU 2049 CA MET A 257 7626 8140 7756 -111 -895 -123 C ATOM 2050 C MET A 257 1.110 32.636 42.223 1.00 71.01 C ANISOU 2050 C MET A 257 8713 9249 9020 -79 -1021 -95 C ATOM 2051 O MET A 257 1.879 33.466 41.723 1.00 85.78 O ANISOU 2051 O MET A 257 10634 11082 10877 -59 -1058 -35 O ATOM 2052 CB MET A 257 1.597 30.228 41.717 1.00 55.17 C ANISOU 2052 CB MET A 257 6873 7293 6797 -173 -932 -95 C ATOM 2053 CG MET A 257 2.368 28.971 42.083 1.00 62.18 C ANISOU 2053 CG MET A 257 7876 8204 7547 -187 -804 -102 C ATOM 2054 SD MET A 257 2.315 27.721 40.785 1.00 83.48 S ANISOU 2054 SD MET A 257 10720 10884 10117 -245 -865 -88 S ATOM 2055 CE MET A 257 0.554 27.412 40.684 1.00 85.28 C ANISOU 2055 CE MET A 257 10811 11078 10515 -332 -950 -161 C ATOM 2056 N VAL A 258 -0.206 32.842 42.295 1.00 69.61 N ANISOU 2056 N VAL A 258 8419 9076 8953 -68 -1079 -127 N ATOM 2057 CA VAL A 258 -0.791 34.078 41.780 1.00 67.44 C ANISOU 2057 CA VAL A 258 8088 8765 8771 -9 -1193 -97 C ATOM 2058 C VAL A 258 -0.457 35.252 42.693 1.00 72.56 C ANISOU 2058 C VAL A 258 8706 9358 9507 64 -1160 -122 C ATOM 2059 O VAL A 258 -0.075 36.331 42.224 1.00 65.29 O ANISOU 2059 O VAL A 258 7824 8359 8622 100 -1215 -70 O ATOM 2060 CB VAL A 258 -2.310 33.913 41.595 1.00 52.13 C ANISOU 2060 CB VAL A 258 6018 6876 6914 -6 -1268 -129 C ATOM 2061 CG1 VAL A 258 -2.976 35.267 41.422 1.00 63.72 C ANISOU 2061 CG1 VAL A 258 7415 8318 8478 97 -1358 -107 C ATOM 2062 CG2 VAL A 258 -2.600 33.023 40.397 1.00 56.41 C ANISOU 2062 CG2 VAL A 258 6600 7455 7378 -73 -1355 -116 C ATOM 2063 N ILE A 259 -0.594 35.064 44.008 1.00 68.96 N ANISOU 2063 N ILE A 259 8186 8933 9084 96 -1067 -201 N ATOM 2064 CA ILE A 259 -0.300 36.144 44.946 1.00 66.04 C ANISOU 2064 CA ILE A 259 7792 8514 8788 180 -1050 -257 C ATOM 2065 C ILE A 259 1.185 36.491 44.919 1.00 70.38 C ANISOU 2065 C ILE A 259 8437 9013 9291 149 -1028 -248 C ATOM 2066 O ILE A 259 1.559 37.670 44.932 1.00 80.24 O ANISOU 2066 O ILE A 259 9699 10165 10623 176 -1075 -253 O ATOM 2067 CB ILE A 259 -0.775 35.763 46.360 1.00 61.46 C ANISOU 2067 CB ILE A 259 7124 8005 8223 251 -951 -344 C ATOM 2068 CG1 ILE A 259 -2.303 35.808 46.435 1.00 67.76 C ANISOU 2068 CG1 ILE A 259 7791 8846 9108 298 -981 -343 C ATOM 2069 CG2 ILE A 259 -0.158 36.679 47.405 1.00 49.84 C ANISOU 2069 CG2 ILE A 259 5657 6497 6783 345 -931 -430 C ATOM 2070 CD1 ILE A 259 -2.857 35.504 47.809 1.00 77.33 C ANISOU 2070 CD1 ILE A 259 8906 10137 10340 391 -869 -402 C ATOM 2071 N ALA A 260 2.053 35.477 44.868 1.00 63.00 N ANISOU 2071 N ALA A 260 7568 8140 8229 90 -954 -233 N ATOM 2072 CA ALA A 260 3.488 35.741 44.815 1.00 59.34 C ANISOU 2072 CA ALA A 260 7171 7661 7714 59 -930 -218 C ATOM 2073 C ALA A 260 3.878 36.467 43.535 1.00 66.79 C ANISOU 2073 C ALA A 260 8170 8521 8686 14 -1008 -103 C ATOM 2074 O ALA A 260 4.806 37.284 43.545 1.00 77.18 O ANISOU 2074 O ALA A 260 9501 9775 10051 -8 -1011 -89 O ATOM 2075 CB ALA A 260 4.274 34.437 44.943 1.00 45.66 C ANISOU 2075 CB ALA A 260 5502 6032 5816 31 -831 -211 C ATOM 2076 N PHE A 261 3.190 36.184 42.427 1.00 57.41 N ANISOU 2076 N PHE A 261 7010 7334 7469 5 -1069 -20 N ATOM 2077 CA PHE A 261 3.469 36.899 41.187 1.00 56.63 C ANISOU 2077 CA PHE A 261 6969 7166 7383 0 -1134 106 C ATOM 2078 C PHE A 261 3.057 38.362 41.294 1.00 79.40 C ANISOU 2078 C PHE A 261 9815 9922 10432 50 -1190 111 C ATOM 2079 O PHE A 261 3.739 39.246 40.763 1.00 77.87 O ANISOU 2079 O PHE A 261 9667 9629 10293 37 -1197 201 O ATOM 2080 CB PHE A 261 2.756 36.222 40.016 1.00 55.35 C ANISOU 2080 CB PHE A 261 6844 7056 7130 10 -1201 172 C ATOM 2081 CG PHE A 261 3.155 36.758 38.670 1.00 58.67 C ANISOU 2081 CG PHE A 261 7342 7439 7509 37 -1250 319 C ATOM 2082 CD1 PHE A 261 4.239 36.225 37.993 1.00 68.03 C ANISOU 2082 CD1 PHE A 261 8622 8671 8556 13 -1206 408 C ATOM 2083 CD2 PHE A 261 2.446 37.792 38.080 1.00 61.35 C ANISOU 2083 CD2 PHE A 261 7666 7707 7936 110 -1329 380 C ATOM 2084 CE1 PHE A 261 4.611 36.713 36.754 1.00 70.39 C ANISOU 2084 CE1 PHE A 261 8992 8948 8806 61 -1235 564 C ATOM 2085 CE2 PHE A 261 2.813 38.285 36.842 1.00 63.17 C ANISOU 2085 CE2 PHE A 261 7976 7907 8119 160 -1356 535 C ATOM 2086 CZ PHE A 261 3.896 37.745 36.178 1.00 61.21 C ANISOU 2086 CZ PHE A 261 7816 7708 7733 135 -1306 631 C ATOM 2087 N LEU A 262 1.944 38.636 41.979 1.00 70.57 N ANISOU 2087 N LEU A 262 8617 8798 9398 113 -1221 23 N ATOM 2088 CA LEU A 262 1.511 40.016 42.166 1.00 61.66 C ANISOU 2088 CA LEU A 262 7469 7542 8418 185 -1271 15 C ATOM 2089 C LEU A 262 2.458 40.766 43.095 1.00 73.47 C ANISOU 2089 C LEU A 262 8971 8942 10003 164 -1233 -62 C ATOM 2090 O LEU A 262 2.874 41.890 42.796 1.00 72.49 O ANISOU 2090 O LEU A 262 8889 8664 9989 159 -1257 -14 O ATOM 2091 CB LEU A 262 0.081 40.050 42.707 1.00 62.77 C ANISOU 2091 CB LEU A 262 7514 7729 8607 279 -1307 -59 C ATOM 2092 CG LEU A 262 -1.013 39.540 41.767 1.00 65.88 C ANISOU 2092 CG LEU A 262 7869 8211 8949 304 -1375 0 C ATOM 2093 CD1 LEU A 262 -2.377 39.631 42.430 1.00 59.58 C ANISOU 2093 CD1 LEU A 262 6945 7476 8216 392 -1399 -74 C ATOM 2094 CD2 LEU A 262 -0.998 40.314 40.457 1.00 61.44 C ANISOU 2094 CD2 LEU A 262 7380 7575 8388 348 -1449 132 C ATOM 2095 N ILE A 263 2.819 40.153 44.226 1.00 64.79 N ANISOU 2095 N ILE A 263 7830 7928 8859 155 -1172 -185 N ATOM 2096 CA ILE A 263 3.757 40.784 45.150 1.00 72.19 C ANISOU 2096 CA ILE A 263 8761 8803 9864 141 -1153 -289 C ATOM 2097 C ILE A 263 5.084 41.075 44.459 1.00 74.05 C ANISOU 2097 C ILE A 263 9047 8978 10112 28 -1139 -200 C ATOM 2098 O ILE A 263 5.785 42.030 44.815 1.00 72.68 O ANISOU 2098 O ILE A 263 8869 8684 10062 -9 -1156 -251 O ATOM 2099 CB ILE A 263 3.945 39.898 46.400 1.00 73.83 C ANISOU 2099 CB ILE A 263 8918 9156 9976 178 -1083 -423 C ATOM 2100 CG1 ILE A 263 2.611 39.706 47.124 1.00 77.53 C ANISOU 2100 CG1 ILE A 263 9323 9682 10453 297 -1078 -491 C ATOM 2101 CG2 ILE A 263 4.967 40.499 47.353 1.00 71.15 C ANISOU 2101 CG2 ILE A 263 8563 8784 9686 176 -1082 -555 C ATOM 2102 CD1 ILE A 263 2.708 38.837 48.360 1.00 71.19 C ANISOU 2102 CD1 ILE A 263 8477 9021 9551 362 -987 -597 C ATOM 2103 N CYS A 264 5.433 40.286 43.442 1.00 80.34 N ANISOU 2103 N CYS A 264 9888 9852 10787 -25 -1110 -66 N ATOM 2104 CA CYS A 264 6.715 40.457 42.767 1.00 75.29 C ANISOU 2104 CA CYS A 264 9283 9186 10135 -118 -1077 41 C ATOM 2105 C CYS A 264 6.704 41.648 41.814 1.00 73.82 C ANISOU 2105 C CYS A 264 9140 8823 10085 -132 -1113 179 C ATOM 2106 O CYS A 264 7.608 42.489 41.853 1.00 83.59 O ANISOU 2106 O CYS A 264 10370 9945 11447 -208 -1097 201 O ATOM 2107 CB CYS A 264 7.081 39.177 42.014 1.00 65.32 C ANISOU 2107 CB CYS A 264 8069 8077 8673 -136 -1029 139 C ATOM 2108 SG CYS A 264 8.677 39.239 41.169 1.00 66.20 S ANISOU 2108 SG CYS A 264 8212 8206 8734 -222 -969 293 S ATOM 2109 N TRP A 265 5.688 41.742 40.950 1.00 78.89 N ANISOU 2109 N TRP A 265 9824 9441 10710 -57 -1158 276 N ATOM 2110 CA TRP A 265 5.716 42.696 39.849 1.00 74.32 C ANISOU 2110 CA TRP A 265 9307 8721 10211 -41 -1171 449 C ATOM 2111 C TRP A 265 4.700 43.824 39.953 1.00 76.07 C ANISOU 2111 C TRP A 265 9539 8786 10579 53 -1232 432 C ATOM 2112 O TRP A 265 4.855 44.828 39.251 1.00 78.31 O ANISOU 2112 O TRP A 265 9882 8906 10965 67 -1225 567 O ATOM 2113 CB TRP A 265 5.506 41.969 38.512 1.00 78.80 C ANISOU 2113 CB TRP A 265 9934 9399 10607 7 -1177 607 C ATOM 2114 CG TRP A 265 6.561 40.946 38.223 1.00 88.69 C ANISOU 2114 CG TRP A 265 11205 10791 11703 -59 -1112 655 C ATOM 2115 CD1 TRP A 265 6.424 39.590 38.275 1.00 67.61 C ANISOU 2115 CD1 TRP A 265 8542 8291 8855 -53 -1110 597 C ATOM 2116 CD2 TRP A 265 7.921 41.198 37.848 1.00 95.21 C ANISOU 2116 CD2 TRP A 265 12044 11595 12538 -136 -1035 776 C ATOM 2117 NE1 TRP A 265 7.613 38.982 37.949 1.00 83.44 N ANISOU 2117 NE1 TRP A 265 10579 10386 10739 -100 -1038 671 N ATOM 2118 CE2 TRP A 265 8.548 39.947 37.685 1.00 87.98 C ANISOU 2118 CE2 TRP A 265 11146 10860 11423 -151 -991 784 C ATOM 2119 CE3 TRP A 265 8.669 42.361 37.633 1.00 89.13 C ANISOU 2119 CE3 TRP A 265 11268 10664 11934 -196 -991 883 C ATOM 2120 CZ2 TRP A 265 9.886 39.825 37.314 1.00 86.00 C ANISOU 2120 CZ2 TRP A 265 10897 10664 11116 -207 -907 899 C ATOM 2121 CZ3 TRP A 265 9.997 42.237 37.266 1.00 80.90 C ANISOU 2121 CZ3 TRP A 265 10211 9667 10859 -277 -905 1000 C ATOM 2122 CH2 TRP A 265 10.592 40.979 37.111 1.00 88.57 C ANISOU 2122 CH2 TRP A 265 11191 10850 11612 -273 -865 1008 C ATOM 2123 N LEU A 266 3.673 43.696 40.791 1.00 78.44 N ANISOU 2123 N LEU A 266 9787 9130 10888 129 -1279 285 N ATOM 2124 CA LEU A 266 2.688 44.769 40.894 1.00 82.54 C ANISOU 2124 CA LEU A 266 10319 9514 11529 245 -1335 271 C ATOM 2125 C LEU A 266 3.281 46.008 41.566 1.00 92.42 C ANISOU 2125 C LEU A 266 11598 10543 12976 211 -1328 206 C ATOM 2126 O LEU A 266 3.027 47.126 41.100 1.00 99.01 O ANISOU 2126 O LEU A 266 12502 11187 13930 269 -1343 292 O ATOM 2127 CB LEU A 266 1.434 44.301 41.639 1.00 64.83 C ANISOU 2127 CB LEU A 266 7995 7395 9242 345 -1377 139 C ATOM 2128 CG LEU A 266 0.228 45.240 41.596 1.00 65.21 C ANISOU 2128 CG LEU A 266 8045 7363 9370 502 -1439 143 C ATOM 2129 CD1 LEU A 266 -0.241 45.437 40.163 1.00 65.91 C ANISOU 2129 CD1 LEU A 266 8185 7452 9406 572 -1475 323 C ATOM 2130 CD2 LEU A 266 -0.901 44.709 42.466 1.00 57.23 C ANISOU 2130 CD2 LEU A 266 6925 6501 8319 590 -1462 14 C ATOM 2131 N PRO A 267 4.058 45.878 42.655 1.00 88.33 N ANISOU 2131 N PRO A 267 11032 10032 12496 128 -1309 49 N ATOM 2132 CA PRO A 267 4.743 47.074 43.175 1.00 73.35 C ANISOU 2132 CA PRO A 267 9161 7907 10799 71 -1318 -22 C ATOM 2133 C PRO A 267 5.686 47.708 42.168 1.00 82.71 C ANISOU 2133 C PRO A 267 10404 8933 12088 -44 -1270 162 C ATOM 2134 O PRO A 267 5.808 48.938 42.131 1.00 80.97 O ANISOU 2134 O PRO A 267 10242 8459 12064 -57 -1278 181 O ATOM 2135 CB PRO A 267 5.491 46.541 44.404 1.00 78.98 C ANISOU 2135 CB PRO A 267 9796 8731 11483 6 -1311 -223 C ATOM 2136 CG PRO A 267 4.687 45.384 44.847 1.00 81.85 C ANISOU 2136 CG PRO A 267 10106 9327 11666 101 -1305 -286 C ATOM 2137 CD PRO A 267 4.204 44.739 43.582 1.00 90.66 C ANISOU 2137 CD PRO A 267 11249 10531 12665 110 -1287 -94 C ATOM 2138 N TYR A 268 6.360 46.902 41.343 1.00 93.38 N ANISOU 2138 N TYR A 268 11746 10420 13315 -120 -1211 308 N ATOM 2139 CA TYR A 268 7.203 47.477 40.301 1.00 82.52 C ANISOU 2139 CA TYR A 268 10418 8913 12024 -206 -1145 521 C ATOM 2140 C TYR A 268 6.366 48.123 39.207 1.00 82.21 C ANISOU 2140 C TYR A 268 10479 8758 12000 -78 -1146 713 C ATOM 2141 O TYR A 268 6.815 49.079 38.566 1.00 83.96 O ANISOU 2141 O TYR A 268 10761 8772 12366 -113 -1091 874 O ATOM 2142 CB TYR A 268 8.123 46.409 39.709 1.00 87.45 C ANISOU 2142 CB TYR A 268 11009 9738 12481 -285 -1078 630 C ATOM 2143 CG TYR A 268 9.392 46.971 39.103 1.00106.09 C ANISOU 2143 CG TYR A 268 13364 11987 14957 -419 -993 796 C ATOM 2144 CD1 TYR A 268 9.407 47.469 37.806 1.00112.16 C ANISOU 2144 CD1 TYR A 268 14213 12658 15745 -379 -931 1061 C ATOM 2145 CD2 TYR A 268 10.574 47.005 39.831 1.00121.84 C ANISOU 2145 CD2 TYR A 268 15264 13988 17043 -578 -968 693 C ATOM 2146 CE1 TYR A 268 10.565 47.986 37.252 1.00124.26 C ANISOU 2146 CE1 TYR A 268 15728 14088 17395 -503 -831 1237 C ATOM 2147 CE2 TYR A 268 11.737 47.519 39.286 1.00131.82 C ANISOU 2147 CE2 TYR A 268 16494 15159 18431 -717 -884 850 C ATOM 2148 CZ TYR A 268 11.726 48.008 37.996 1.00130.96 C ANISOU 2148 CZ TYR A 268 16465 14942 18353 -683 -807 1132 C ATOM 2149 OH TYR A 268 12.881 48.520 37.450 1.00122.78 O ANISOU 2149 OH TYR A 268 15385 13815 17452 -822 -702 1313 O ATOM 2150 N ALA A 269 5.148 47.626 38.987 1.00 82.31 N ANISOU 2150 N ALA A 269 10501 8904 11869 75 -1202 701 N ATOM 2151 CA ALA A 269 4.282 48.209 37.972 1.00 77.37 C ANISOU 2151 CA ALA A 269 9960 8206 11232 229 -1216 867 C ATOM 2152 C ALA A 269 3.619 49.488 38.466 1.00 84.56 C ANISOU 2152 C ALA A 269 10922 8884 12325 319 -1251 808 C ATOM 2153 O ALA A 269 3.543 50.473 37.725 1.00 79.92 O ANISOU 2153 O ALA A 269 10433 8102 11830 387 -1216 975 O ATOM 2154 CB ALA A 269 3.222 47.197 37.540 1.00 77.43 C ANISOU 2154 CB ALA A 269 9937 8459 11024 353 -1280 861 C ATOM 2155 N GLY A 270 3.140 49.492 39.711 1.00 81.61 N ANISOU 2155 N GLY A 270 10494 8523 11992 340 -1311 578 N ATOM 2156 CA GLY A 270 2.435 50.659 40.215 1.00 64.71 C ANISOU 2156 CA GLY A 270 8413 6175 9999 458 -1351 507 C ATOM 2157 C GLY A 270 3.353 51.846 40.443 1.00 85.66 C ANISOU 2157 C GLY A 270 11142 8510 12895 348 -1313 509 C ATOM 2158 O GLY A 270 3.029 52.977 40.070 1.00 80.23 O ANISOU 2158 O GLY A 270 10568 7579 12338 436 -1300 603 O ATOM 2159 N VAL A 271 4.511 51.605 41.062 1.00 97.07 N ANISOU 2159 N VAL A 271 12523 9949 14410 155 -1293 402 N ATOM 2160 CA VAL A 271 5.434 52.698 41.353 1.00 85.67 C ANISOU 2160 CA VAL A 271 11123 8204 13224 15 -1270 372 C ATOM 2161 C VAL A 271 6.007 53.276 40.065 1.00 90.21 C ANISOU 2161 C VAL A 271 11776 8606 13894 -48 -1166 663 C ATOM 2162 O VAL A 271 6.075 54.499 39.896 1.00 99.12 O ANISOU 2162 O VAL A 271 13009 9415 15238 -53 -1137 729 O ATOM 2163 CB VAL A 271 6.543 52.221 42.308 1.00 81.43 C ANISOU 2163 CB VAL A 271 10470 7751 12720 -170 -1285 179 C ATOM 2164 CG1 VAL A 271 7.563 53.323 42.530 1.00 93.03 C ANISOU 2164 CG1 VAL A 271 11959 8913 14474 -346 -1270 144 C ATOM 2165 CG2 VAL A 271 5.942 51.777 43.632 1.00 74.88 C ANISOU 2165 CG2 VAL A 271 9581 7070 11799 -69 -1374 -98 C ATOM 2166 N ALA A 272 6.425 52.413 39.135 1.00 93.18 N ANISOU 2166 N ALA A 272 12113 9183 14109 -85 -1101 847 N ATOM 2167 CA ALA A 272 6.938 52.902 37.859 1.00 90.54 C ANISOU 2167 CA ALA A 272 11852 8718 13833 -110 -987 1150 C ATOM 2168 C ALA A 272 5.848 53.571 37.031 1.00 90.93 C ANISOU 2168 C ALA A 272 12036 8658 13855 118 -979 1319 C ATOM 2169 O ALA A 272 6.150 54.430 36.195 1.00112.48 O ANISOU 2169 O ALA A 272 14864 11167 16707 129 -879 1551 O ATOM 2170 CB ALA A 272 7.578 51.761 37.070 1.00 72.52 C ANISOU 2170 CB ALA A 272 9504 6706 11345 -158 -927 1298 C ATOM 2171 N PHE A 273 4.585 53.192 37.240 1.00 87.09 N ANISOU 2171 N PHE A 273 11549 8332 13209 310 -1074 1216 N ATOM 2172 CA PHE A 273 3.491 53.884 36.568 1.00106.83 C ANISOU 2172 CA PHE A 273 14164 10746 15680 549 -1081 1347 C ATOM 2173 C PHE A 273 3.237 55.251 37.187 1.00119.72 C ANISOU 2173 C PHE A 273 15903 12035 17552 590 -1087 1274 C ATOM 2174 O PHE A 273 2.795 56.172 36.491 1.00129.29 O ANISOU 2174 O PHE A 273 17249 13054 18819 744 -1038 1452 O ATOM 2175 CB PHE A 273 2.220 53.034 36.614 1.00108.89 C ANISOU 2175 CB PHE A 273 14363 11305 15706 729 -1186 1253 C ATOM 2176 CG PHE A 273 1.075 53.609 35.831 1.00117.29 C ANISOU 2176 CG PHE A 273 15517 12351 16698 996 -1204 1391 C ATOM 2177 CD1 PHE A 273 1.018 53.464 34.455 1.00119.29 C ANISOU 2177 CD1 PHE A 273 15824 12693 16810 1110 -1158 1639 C ATOM 2178 CD2 PHE A 273 0.050 54.284 36.472 1.00126.88 C ANISOU 2178 CD2 PHE A 273 16763 13480 17966 1158 -1269 1270 C ATOM 2179 CE1 PHE A 273 -0.036 53.989 33.731 1.00126.71 C ANISOU 2179 CE1 PHE A 273 16840 13641 17662 1381 -1181 1760 C ATOM 2180 CE2 PHE A 273 -1.007 54.811 35.755 1.00125.11 C ANISOU 2180 CE2 PHE A 273 16614 13263 17659 1424 -1287 1398 C ATOM 2181 CZ PHE A 273 -1.051 54.663 34.383 1.00122.18 C ANISOU 2181 CZ PHE A 273 16290 12987 17147 1535 -1245 1641 C ATOM 2182 N TYR A 274 3.508 55.403 38.485 1.00116.04 N ANISOU 2182 N TYR A 274 15387 11485 17218 473 -1148 1011 N ATOM 2183 CA TYR A 274 3.370 56.702 39.133 1.00 99.75 C ANISOU 2183 CA TYR A 274 13436 9073 15391 501 -1165 910 C ATOM 2184 C TYR A 274 4.576 57.590 38.855 1.00105.89 C ANISOU 2184 C TYR A 274 14279 9512 16444 294 -1065 1024 C ATOM 2185 O TYR A 274 4.428 58.802 38.662 1.00127.97 O ANISOU 2185 O TYR A 274 17228 11964 19431 352 -1021 1106 O ATOM 2186 CB TYR A 274 3.178 56.515 40.640 1.00 85.79 C ANISOU 2186 CB TYR A 274 11592 7362 13641 483 -1279 569 C ATOM 2187 CG TYR A 274 2.830 57.783 41.388 1.00 97.90 C ANISOU 2187 CG TYR A 274 13253 8568 15376 567 -1325 424 C ATOM 2188 CD1 TYR A 274 3.823 58.613 41.892 1.00115.80 C ANISOU 2188 CD1 TYR A 274 15565 10514 17918 373 -1319 322 C ATOM 2189 CD2 TYR A 274 1.505 58.144 41.599 1.00 97.53 C ANISOU 2189 CD2 TYR A 274 13277 8535 15244 845 -1381 380 C ATOM 2190 CE1 TYR A 274 3.507 59.771 42.579 1.00118.53 C ANISOU 2190 CE1 TYR A 274 16046 10540 18449 455 -1372 170 C ATOM 2191 CE2 TYR A 274 1.180 59.299 42.286 1.00109.13 C ANISOU 2191 CE2 TYR A 274 14882 9704 16881 948 -1424 244 C ATOM 2192 CZ TYR A 274 2.185 60.109 42.773 1.00117.13 C ANISOU 2192 CZ TYR A 274 15960 10379 18166 753 -1422 133 C ATOM 2193 OH TYR A 274 1.865 61.260 43.456 1.00123.21 O ANISOU 2193 OH TYR A 274 16882 10826 19104 860 -1475 -21 O ATOM 2194 N ILE A 275 5.775 57.004 38.834 1.00104.53 N ANISOU 2194 N ILE A 275 13988 9429 16299 53 -1021 1035 N ATOM 2195 CA ILE A 275 6.981 57.774 38.542 1.00 96.65 C ANISOU 2195 CA ILE A 275 13013 8138 15573 -172 -917 1156 C ATOM 2196 C ILE A 275 6.944 58.304 37.114 1.00 94.27 C ANISOU 2196 C ILE A 275 12833 7696 15288 -82 -769 1532 C ATOM 2197 O ILE A 275 7.357 59.439 36.847 1.00 93.40 O ANISOU 2197 O ILE A 275 12830 7213 15444 -154 -676 1660 O ATOM 2198 CB ILE A 275 8.232 56.914 38.799 1.00 84.27 C ANISOU 2198 CB ILE A 275 11265 6763 13990 -423 -903 1095 C ATOM 2199 CG1 ILE A 275 8.396 56.651 40.296 1.00 83.01 C ANISOU 2199 CG1 ILE A 275 11003 6673 13863 -510 -1039 718 C ATOM 2200 CG2 ILE A 275 9.478 57.579 38.229 1.00 80.81 C ANISOU 2200 CG2 ILE A 275 10818 6080 13807 -652 -768 1291 C ATOM 2201 CD1 ILE A 275 9.550 55.735 40.627 1.00 83.74 C ANISOU 2201 CD1 ILE A 275 10915 6999 13903 -717 -1034 638 C ATOM 2202 N PHE A 276 6.443 57.499 36.176 1.00 99.46 N ANISOU 2202 N PHE A 276 13483 8644 15662 87 -745 1713 N ATOM 2203 CA PHE A 276 6.384 57.933 34.787 1.00119.10 C ANISOU 2203 CA PHE A 276 16087 11045 18120 217 -606 2074 C ATOM 2204 C PHE A 276 5.222 58.887 34.533 1.00118.07 C ANISOU 2204 C PHE A 276 16135 10720 18007 488 -612 2143 C ATOM 2205 O PHE A 276 5.326 59.762 33.667 1.00118.53 O ANISOU 2205 O PHE A 276 16333 10533 18171 566 -475 2419 O ATOM 2206 CB PHE A 276 6.286 56.721 33.862 1.00121.80 C ANISOU 2206 CB PHE A 276 16362 11779 18138 319 -595 2221 C ATOM 2207 CG PHE A 276 6.702 57.004 32.451 1.00132.38 C ANISOU 2207 CG PHE A 276 17783 13068 19447 395 -429 2601 C ATOM 2208 CD1 PHE A 276 5.775 56.998 31.423 1.00138.91 C ANISOU 2208 CD1 PHE A 276 18713 14008 20056 699 -418 2792 C ATOM 2209 CD2 PHE A 276 8.024 57.288 32.154 1.00129.58 C ANISOU 2209 CD2 PHE A 276 17392 12565 19276 174 -282 2772 C ATOM 2210 CE1 PHE A 276 6.162 57.262 30.124 1.00140.34 C ANISOU 2210 CE1 PHE A 276 18978 14157 20188 804 -258 3150 C ATOM 2211 CE2 PHE A 276 8.416 57.554 30.860 1.00123.89 C ANISOU 2211 CE2 PHE A 276 16745 11806 18523 262 -109 3145 C ATOM 2212 CZ PHE A 276 7.485 57.541 29.844 1.00130.90 C ANISOU 2212 CZ PHE A 276 17752 12806 19175 588 -95 3337 C ATOM 2213 N THR A 277 4.120 58.743 35.268 1.00105.22 N ANISOU 2213 N THR A 277 14504 9200 16272 647 -755 1912 N ATOM 2214 CA THR A 277 2.995 59.665 35.122 1.00106.52 C ANISOU 2214 CA THR A 277 14832 9197 16446 923 -768 1958 C ATOM 2215 C THR A 277 3.310 61.011 35.772 1.00128.09 C ANISOU 2215 C THR A 277 17698 11458 19513 838 -735 1885 C ATOM 2216 O THR A 277 3.501 62.019 35.084 1.00129.62 O ANISOU 2216 O THR A 277 18053 11330 19868 882 -602 2122 O ATOM 2217 CB THR A 277 1.727 59.052 35.724 1.00107.53 C ANISOU 2217 CB THR A 277 14889 9614 16353 1119 -926 1738 C ATOM 2218 OG1 THR A 277 1.474 57.770 35.132 1.00116.28 O ANISOU 2218 OG1 THR A 277 15870 11136 17177 1166 -963 1788 O ATOM 2219 CG2 THR A 277 0.530 59.960 35.488 1.00117.25 C ANISOU 2219 CG2 THR A 277 16273 10717 17558 1437 -937 1805 C ATOM 2220 N HIS A 278 3.360 61.041 37.104 1.00125.43 N ANISOU 2220 N HIS A 278 17304 11070 19284 726 -853 1554 N ATOM 2221 CA HIS A 278 3.698 62.256 37.846 1.00118.89 C ANISOU 2221 CA HIS A 278 16597 9798 18777 628 -854 1423 C ATOM 2222 C HIS A 278 5.212 62.478 37.820 1.00115.40 C ANISOU 2222 C HIS A 278 16098 9142 18605 273 -765 1468 C ATOM 2223 O HIS A 278 5.897 62.493 38.842 1.00 98.75 O ANISOU 2223 O HIS A 278 13902 6957 16660 51 -845 1203 O ATOM 2224 CB HIS A 278 3.169 62.163 39.272 1.00115.90 C ANISOU 2224 CB HIS A 278 16175 9480 18380 674 -1024 1042 C ATOM 2225 CG HIS A 278 1.676 62.081 39.362 1.00126.89 C ANISOU 2225 CG HIS A 278 17613 11054 19543 1021 -1100 1002 C ATOM 2226 ND1 HIS A 278 0.863 61.991 38.252 1.00132.48 N ANISOU 2226 ND1 HIS A 278 18375 11903 20057 1265 -1043 1262 N ATOM 2227 CD2 HIS A 278 0.848 62.081 40.433 1.00130.82 C ANISOU 2227 CD2 HIS A 278 18099 11634 19971 1175 -1229 733 C ATOM 2228 CE1 HIS A 278 -0.400 61.935 38.636 1.00131.60 C ANISOU 2228 CE1 HIS A 278 18268 11956 19778 1538 -1138 1150 C ATOM 2229 NE2 HIS A 278 -0.436 61.988 39.955 1.00129.51 N ANISOU 2229 NE2 HIS A 278 17965 11658 19585 1491 -1243 841 N ATOM 2230 N GLN A 279 5.726 62.658 36.606 1.00123.33 N ANISOU 2230 N GLN A 279 17145 10066 19649 237 -595 1819 N ATOM 2231 CA GLN A 279 7.160 62.733 36.382 1.00121.67 C ANISOU 2231 CA GLN A 279 16846 9720 19663 -89 -484 1925 C ATOM 2232 C GLN A 279 7.732 64.037 36.932 1.00133.31 C ANISOU 2232 C GLN A 279 18422 10675 21554 -281 -455 1838 C ATOM 2233 O GLN A 279 7.024 65.030 37.127 1.00165.63 O ANISOU 2233 O GLN A 279 22713 14456 25762 -121 -468 1804 O ATOM 2234 CB GLN A 279 7.464 62.612 34.888 1.00134.78 C ANISOU 2234 CB GLN A 279 18536 11439 21234 -29 -293 2352 C ATOM 2235 CG GLN A 279 8.803 61.978 34.565 1.00150.41 C ANISOU 2235 CG GLN A 279 20336 13558 23255 -308 -204 2463 C ATOM 2236 CD GLN A 279 8.980 61.734 33.080 1.00153.05 C ANISOU 2236 CD GLN A 279 20702 14016 23432 -185 -25 2882 C ATOM 2237 OE1 GLN A 279 8.551 62.537 32.252 1.00145.55 O ANISOU 2237 OE1 GLN A 279 19934 12850 22520 6 101 3153 O ATOM 2238 NE2 GLN A 279 9.606 60.615 32.735 1.00153.05 N ANISOU 2238 NE2 GLN A 279 20538 14374 23239 -267 -10 2938 N ATOM 2239 N GLY A 280 9.039 64.021 37.187 1.00109.13 N ANISOU 2239 N GLY A 280 15219 7524 18722 -628 -420 1795 N ATOM 2240 CA GLY A 280 9.747 65.189 37.664 1.00111.37 C ANISOU 2240 CA GLY A 280 15564 7318 19436 -870 -394 1707 C ATOM 2241 C GLY A 280 9.536 65.530 39.123 1.00120.26 C ANISOU 2241 C GLY A 280 16699 8314 20681 -913 -601 1256 C ATOM 2242 O GLY A 280 10.117 66.514 39.599 1.00112.48 O ANISOU 2242 O GLY A 280 15767 6908 20062 -1121 -608 1132 O ATOM 2243 N SER A 281 8.731 64.757 39.848 1.00126.31 N ANISOU 2243 N SER A 281 17415 9424 21153 -721 -767 1004 N ATOM 2244 CA SER A 281 8.472 65.049 41.248 1.00124.21 C ANISOU 2244 CA SER A 281 17165 9069 20961 -712 -960 580 C ATOM 2245 C SER A 281 9.691 64.703 42.102 1.00111.46 C ANISOU 2245 C SER A 281 15336 7520 19495 -1041 -1051 314 C ATOM 2246 O SER A 281 10.647 64.064 41.650 1.00124.10 O ANISOU 2246 O SER A 281 16755 9309 21090 -1254 -971 451 O ATOM 2247 CB SER A 281 7.244 64.282 41.736 1.00130.51 C ANISOU 2247 CB SER A 281 17955 10241 21392 -397 -1086 426 C ATOM 2248 OG SER A 281 6.086 64.661 41.012 1.00143.01 O ANISOU 2248 OG SER A 281 19721 11771 22843 -82 -1022 642 O ATOM 2249 N ASP A 282 9.647 65.136 43.362 1.00 90.12 N ANISOU 2249 N ASP A 282 12654 4675 16911 -1060 -1224 -77 N ATOM 2250 CA ASP A 282 10.738 64.902 44.307 1.00 94.53 C ANISOU 2250 CA ASP A 282 13016 5293 17608 -1339 -1342 -385 C ATOM 2251 C ASP A 282 10.706 63.438 44.739 1.00111.85 C ANISOU 2251 C ASP A 282 15006 8054 19439 -1268 -1416 -502 C ATOM 2252 O ASP A 282 10.262 63.081 45.833 1.00103.17 O ANISOU 2252 O ASP A 282 13879 7140 18183 -1126 -1574 -821 O ATOM 2253 CB ASP A 282 10.627 65.843 45.502 1.00102.48 C ANISOU 2253 CB ASP A 282 14130 6007 18801 -1332 -1506 -776 C ATOM 2254 CG ASP A 282 11.854 65.801 46.392 1.00137.51 C ANISOU 2254 CG ASP A 282 18367 10539 23343 -1622 -1602 -1077 C ATOM 2255 OD1 ASP A 282 11.725 66.095 47.599 1.00149.25 O ANISOU 2255 OD1 ASP A 282 19875 12033 24801 -1553 -1771 -1458 O ATOM 2256 OD2 ASP A 282 12.947 65.475 45.885 1.00150.86 O ANISOU 2256 OD2 ASP A 282 19874 12318 25127 -1899 -1508 -927 O ATOM 2257 N PHE A 283 11.188 62.573 43.850 1.00119.50 N ANISOU 2257 N PHE A 283 15840 9299 20267 -1354 -1288 -226 N ATOM 2258 CA PHE A 283 11.257 61.144 44.125 1.00 98.67 C ANISOU 2258 CA PHE A 283 13018 7176 17296 -1306 -1331 -295 C ATOM 2259 C PHE A 283 12.493 60.847 44.964 1.00118.68 C ANISOU 2259 C PHE A 283 15341 9816 19937 -1567 -1417 -553 C ATOM 2260 O PHE A 283 13.623 61.061 44.513 1.00149.46 O ANISOU 2260 O PHE A 283 19129 13610 24051 -1844 -1334 -431 O ATOM 2261 CB PHE A 283 11.295 60.350 42.822 1.00 84.35 C ANISOU 2261 CB PHE A 283 11163 5604 15282 -1277 -1168 90 C ATOM 2262 CG PHE A 283 10.038 60.455 42.011 1.00105.94 C ANISOU 2262 CG PHE A 283 14075 8327 17850 -990 -1105 321 C ATOM 2263 CD1 PHE A 283 8.798 60.449 42.627 1.00119.44 C ANISOU 2263 CD1 PHE A 283 15881 10099 19401 -720 -1215 147 C ATOM 2264 CD2 PHE A 283 10.096 60.567 40.633 1.00116.29 C ANISOU 2264 CD2 PHE A 283 15447 9583 19153 -972 -934 714 C ATOM 2265 CE1 PHE A 283 7.640 60.546 41.883 1.00125.94 C ANISOU 2265 CE1 PHE A 283 16844 10938 20069 -451 -1166 350 C ATOM 2266 CE2 PHE A 283 8.941 60.667 39.884 1.00122.59 C ANISOU 2266 CE2 PHE A 283 16400 10395 19783 -688 -889 912 C ATOM 2267 CZ PHE A 283 7.712 60.655 40.510 1.00127.87 C ANISOU 2267 CZ PHE A 283 17149 11134 20302 -434 -1010 725 C ATOM 2268 N GLY A 284 12.281 60.356 46.180 1.00106.71 N ANISOU 2268 N GLY A 284 13759 8520 18267 -1466 -1578 -901 N ATOM 2269 CA GLY A 284 13.376 59.981 47.039 1.00122.13 C ANISOU 2269 CA GLY A 284 15506 10634 20265 -1660 -1675 -1167 C ATOM 2270 C GLY A 284 14.046 58.711 46.559 1.00130.71 C ANISOU 2270 C GLY A 284 16403 12134 21128 -1736 -1584 -999 C ATOM 2271 O GLY A 284 13.390 57.778 46.086 1.00146.82 O ANISOU 2271 O GLY A 284 18465 14459 22862 -1552 -1518 -826 O ATOM 2272 N PRO A 285 15.377 58.658 46.656 1.00123.86 N ANISOU 2272 N PRO A 285 15343 11306 20413 -2011 -1581 -1048 N ATOM 2273 CA PRO A 285 16.084 57.413 46.312 1.00115.13 C ANISOU 2273 CA PRO A 285 14053 10619 19073 -2064 -1504 -917 C ATOM 2274 C PRO A 285 15.661 56.231 47.166 1.00112.96 C ANISOU 2274 C PRO A 285 13727 10761 18434 -1849 -1591 -1121 C ATOM 2275 O PRO A 285 15.819 55.083 46.731 1.00128.85 O ANISOU 2275 O PRO A 285 15664 13115 20180 -1799 -1507 -962 O ATOM 2276 CB PRO A 285 17.561 57.771 46.531 1.00110.40 C ANISOU 2276 CB PRO A 285 13245 9958 18744 -2389 -1523 -1013 C ATOM 2277 CG PRO A 285 17.542 58.978 47.420 1.00102.93 C ANISOU 2277 CG PRO A 285 12355 8640 18112 -2472 -1676 -1332 C ATOM 2278 CD PRO A 285 16.301 59.730 47.060 1.00112.75 C ANISOU 2278 CD PRO A 285 13872 9564 19404 -2287 -1649 -1224 C ATOM 2279 N ILE A 286 15.132 56.474 48.366 1.00104.83 N ANISOU 2279 N ILE A 286 12744 9706 17382 -1708 -1749 -1464 N ATOM 2280 CA ILE A 286 14.528 55.399 49.147 1.00 97.97 C ANISOU 2280 CA ILE A 286 11856 9205 16162 -1461 -1805 -1619 C ATOM 2281 C ILE A 286 13.192 54.992 48.539 1.00 89.49 C ANISOU 2281 C ILE A 286 10936 8188 14878 -1224 -1726 -1402 C ATOM 2282 O ILE A 286 12.866 53.801 48.458 1.00 91.64 O ANISOU 2282 O ILE A 286 11171 8798 14851 -1095 -1676 -1325 O ATOM 2283 CB ILE A 286 14.370 55.833 50.615 1.00 97.90 C ANISOU 2283 CB ILE A 286 11852 9156 16189 -1358 -1990 -2041 C ATOM 2284 CG1 ILE A 286 15.715 56.280 51.189 1.00 96.57 C ANISOU 2284 CG1 ILE A 286 11517 8931 16246 -1605 -2091 -2279 C ATOM 2285 CG2 ILE A 286 13.778 54.704 51.446 1.00116.58 C ANISOU 2285 CG2 ILE A 286 14193 11912 18192 -1091 -2023 -2178 C ATOM 2286 CD1 ILE A 286 15.608 56.884 52.571 1.00112.75 C ANISOU 2286 CD1 ILE A 286 13585 10891 18364 -1509 -2293 -2714 C ATOM 2287 N PHE A 287 12.397 55.975 48.106 1.00100.41 N ANISOU 2287 N PHE A 287 12492 9241 16418 -1161 -1716 -1308 N ATOM 2288 CA PHE A 287 11.128 55.686 47.444 1.00101.28 C ANISOU 2288 CA PHE A 287 12734 9402 16347 -940 -1648 -1096 C ATOM 2289 C PHE A 287 11.333 54.870 46.175 1.00108.30 C ANISOU 2289 C PHE A 287 13585 10473 17092 -990 -1502 -752 C ATOM 2290 O PHE A 287 10.479 54.050 45.818 1.00 83.07 O ANISOU 2290 O PHE A 287 10421 7498 13644 -814 -1465 -635 O ATOM 2291 CB PHE A 287 10.401 57.000 47.140 1.00119.50 C ANISOU 2291 CB PHE A 287 15231 11304 18869 -871 -1656 -1042 C ATOM 2292 CG PHE A 287 9.321 56.880 46.101 1.00114.50 C ANISOU 2292 CG PHE A 287 14719 10684 18102 -693 -1562 -749 C ATOM 2293 CD1 PHE A 287 9.565 57.241 44.785 1.00109.34 C ANISOU 2293 CD1 PHE A 287 14123 9871 17552 -785 -1432 -419 C ATOM 2294 CD2 PHE A 287 8.059 56.424 46.442 1.00118.17 C ANISOU 2294 CD2 PHE A 287 15232 11332 18337 -423 -1603 -803 C ATOM 2295 CE1 PHE A 287 8.575 57.138 43.828 1.00107.17 C ANISOU 2295 CE1 PHE A 287 13955 9629 17136 -597 -1360 -166 C ATOM 2296 CE2 PHE A 287 7.064 56.319 45.487 1.00115.80 C ANISOU 2296 CE2 PHE A 287 15021 11063 17915 -259 -1533 -553 C ATOM 2297 CZ PHE A 287 7.323 56.677 44.179 1.00107.11 C ANISOU 2297 CZ PHE A 287 13982 9812 16903 -340 -1420 -244 C ATOM 2298 N MET A 288 12.458 55.075 45.488 1.00106.07 N ANISOU 2298 N MET A 288 14166 13018 13119 106 -2848 108 N ATOM 2299 CA MET A 288 12.762 54.283 44.301 1.00133.84 C ANISOU 2299 CA MET A 288 17564 16586 16704 -49 -2826 87 C ATOM 2300 C MET A 288 13.031 52.824 44.647 1.00141.24 C ANISOU 2300 C MET A 288 18519 17479 17668 -34 -2858 88 C ATOM 2301 O MET A 288 12.768 51.938 43.826 1.00128.51 O ANISOU 2301 O MET A 288 16812 15918 16096 -155 -2832 68 O ATOM 2302 CB MET A 288 13.969 54.876 43.573 1.00138.66 C ANISOU 2302 CB MET A 288 18104 17200 17383 -138 -2815 71 C ATOM 2303 CG MET A 288 13.696 56.178 42.840 1.00138.26 C ANISOU 2303 CG MET A 288 18005 17209 17317 -194 -2773 69 C ATOM 2304 SD MET A 288 13.037 55.897 41.187 1.00133.37 S ANISOU 2304 SD MET A 288 17235 16719 16722 -373 -2684 43 S ATOM 2305 CE MET A 288 14.204 54.686 40.573 1.00137.33 C ANISOU 2305 CE MET A 288 17644 17223 17310 -479 -2664 14 C ATOM 2306 N THR A 289 13.547 52.555 45.842 1.00156.89 N ANISOU 2306 N THR A 289 20615 19364 19630 108 -2906 108 N ATOM 2307 CA THR A 289 13.992 51.218 46.222 1.00148.99 C ANISOU 2307 CA THR A 289 19643 18305 18662 138 -2943 113 C ATOM 2308 C THR A 289 12.982 50.590 47.179 1.00134.38 C ANISOU 2308 C THR A 289 17904 16429 16724 271 -2932 156 C ATOM 2309 O THR A 289 13.251 50.367 48.361 1.00139.23 O ANISOU 2309 O THR A 289 18644 16958 17299 426 -2955 188 O ATOM 2310 CB THR A 289 15.396 51.280 46.840 1.00134.03 C ANISOU 2310 CB THR A 289 17798 16316 16813 203 -2987 107 C ATOM 2311 OG1 THR A 289 16.228 52.139 46.050 1.00104.67 O ANISOU 2311 OG1 THR A 289 13993 12625 13150 100 -2974 79 O ATOM 2312 CG2 THR A 289 16.022 49.892 46.878 1.00140.71 C ANISOU 2312 CG2 THR A 289 18632 17110 17722 193 -3026 98 C ATOM 2313 N ILE A 290 11.796 50.313 46.647 1.00118.00 N ANISOU 2313 N ILE A 290 15765 14436 14634 201 -2789 150 N ATOM 2314 CA ILE A 290 10.791 49.500 47.329 1.00132.80 C ANISOU 2314 CA ILE A 290 17690 16305 16461 278 -2620 178 C ATOM 2315 C ILE A 290 10.067 48.608 46.319 1.00135.34 C ANISOU 2315 C ILE A 290 17876 16702 16843 126 -2427 151 C ATOM 2316 O ILE A 290 9.526 47.568 46.720 1.00124.20 O ANISOU 2316 O ILE A 290 16481 15275 15432 154 -2265 168 O ATOM 2317 CB ILE A 290 9.810 50.364 48.142 1.00131.56 C ANISOU 2317 CB ILE A 290 17643 16167 16176 414 -2667 208 C ATOM 2318 CG1 ILE A 290 9.467 49.661 49.459 1.00129.62 C ANISOU 2318 CG1 ILE A 290 17521 15859 15869 569 -2578 251 C ATOM 2319 CG2 ILE A 290 8.522 50.635 47.380 1.00113.43 C ANISOU 2319 CG2 ILE A 290 15267 13980 13851 328 -2581 191 C ATOM 2320 CD1 ILE A 290 8.445 50.392 50.301 1.00125.66 C ANISOU 2320 CD1 ILE A 290 17121 15386 15238 706 -2604 275 C ATOM 2321 N PRO A 291 10.015 48.945 45.001 1.00141.16 N ANISOU 2321 N PRO A 291 18478 17523 17633 -41 -2436 111 N ATOM 2322 CA PRO A 291 9.626 47.913 44.031 1.00133.80 C ANISOU 2322 CA PRO A 291 17409 16647 16780 -190 -2255 80 C ATOM 2323 C PRO A 291 10.751 46.922 43.783 1.00114.45 C ANISOU 2323 C PRO A 291 14901 14144 14439 -249 -2221 55 C ATOM 2324 O PRO A 291 10.505 45.744 43.502 1.00122.70 O ANISOU 2324 O PRO A 291 15883 15193 15546 -308 -2056 41 O ATOM 2325 CB PRO A 291 9.297 48.720 42.770 1.00140.39 C ANISOU 2325 CB PRO A 291 18130 17586 17627 -338 -2301 47 C ATOM 2326 CG PRO A 291 10.078 49.956 42.903 1.00141.78 C ANISOU 2326 CG PRO A 291 18359 17739 17773 -301 -2522 52 C ATOM 2327 CD PRO A 291 10.024 50.276 44.360 1.00149.31 C ANISOU 2327 CD PRO A 291 19480 18613 18638 -97 -2591 97 C ATOM 2328 N ALA A 292 11.995 47.395 43.887 1.00111.43 N ANISOU 2328 N ALA A 292 14540 13713 14084 -231 -2381 45 N ATOM 2329 CA ALA A 292 13.141 46.513 43.699 1.00 95.72 C ANISOU 2329 CA ALA A 292 12499 11672 12199 -277 -2366 13 C ATOM 2330 C ALA A 292 13.286 45.526 44.849 1.00 89.33 C ANISOU 2330 C ALA A 292 11795 10758 11388 -142 -2294 44 C ATOM 2331 O ALA A 292 13.840 44.438 44.663 1.00 98.53 O ANISOU 2331 O ALA A 292 12907 11887 12645 -186 -2215 17 O ATOM 2332 CB ALA A 292 14.420 47.336 43.541 1.00 82.76 C ANISOU 2332 CB ALA A 292 10855 10010 10582 -291 -2561 -7 C ATOM 2333 N PHE A 293 12.798 45.884 46.039 1.00 79.11 N ANISOU 2333 N PHE A 293 10649 9415 9992 21 -2324 98 N ATOM 2334 CA PHE A 293 12.864 44.968 47.173 1.00 67.60 C ANISOU 2334 CA PHE A 293 9301 7861 8522 148 -2256 134 C ATOM 2335 C PHE A 293 12.030 43.717 46.921 1.00 84.55 C ANISOU 2335 C PHE A 293 11392 10029 10704 87 -2041 135 C ATOM 2336 O PHE A 293 12.431 42.610 47.295 1.00 99.58 O ANISOU 2336 O PHE A 293 13315 11859 12663 110 -1967 139 O ATOM 2337 CB PHE A 293 12.401 45.678 48.447 1.00 76.65 C ANISOU 2337 CB PHE A 293 10613 8970 9541 328 -2328 191 C ATOM 2338 CG PHE A 293 12.183 44.755 49.615 1.00 70.06 C ANISOU 2338 CG PHE A 293 9894 8054 8673 453 -2235 237 C ATOM 2339 CD1 PHE A 293 10.910 44.308 49.935 1.00 83.51 C ANISOU 2339 CD1 PHE A 293 11623 9793 10312 476 -2082 269 C ATOM 2340 CD2 PHE A 293 13.248 44.340 50.396 1.00 76.97 C ANISOU 2340 CD2 PHE A 293 10853 8816 9577 545 -2304 248 C ATOM 2341 CE1 PHE A 293 10.706 43.461 51.008 1.00 98.43 C ANISOU 2341 CE1 PHE A 293 13622 11612 12167 582 -1998 316 C ATOM 2342 CE2 PHE A 293 13.049 43.494 51.472 1.00 89.84 C ANISOU 2342 CE2 PHE A 293 12595 10368 11172 656 -2224 295 C ATOM 2343 CZ PHE A 293 11.776 43.053 51.777 1.00 83.93 C ANISOU 2343 CZ PHE A 293 11873 9659 10358 672 -2070 331 C ATOM 2344 N PHE A 294 10.867 43.873 46.286 1.00 91.13 N ANISOU 2344 N PHE A 294 12156 10961 11509 7 -1942 131 N ATOM 2345 CA PHE A 294 9.996 42.727 46.047 1.00 75.98 C ANISOU 2345 CA PHE A 294 10185 9066 9619 -52 -1736 133 C ATOM 2346 C PHE A 294 10.404 41.955 44.798 1.00 68.67 C ANISOU 2346 C PHE A 294 9094 8175 8821 -224 -1659 74 C ATOM 2347 O PHE A 294 10.291 40.725 44.763 1.00 66.66 O ANISOU 2347 O PHE A 294 8809 7890 8629 -255 -1521 70 O ATOM 2348 CB PHE A 294 8.542 43.186 45.935 1.00 83.75 C ANISOU 2348 CB PHE A 294 11163 10141 10516 -59 -1658 151 C ATOM 2349 CG PHE A 294 7.957 43.673 47.231 1.00 85.23 C ANISOU 2349 CG PHE A 294 11508 10301 10576 112 -1691 207 C ATOM 2350 CD1 PHE A 294 7.582 42.774 48.216 1.00 72.31 C ANISOU 2350 CD1 PHE A 294 9964 8606 8905 204 -1581 253 C ATOM 2351 CD2 PHE A 294 7.773 45.026 47.460 1.00 87.31 C ANISOU 2351 CD2 PHE A 294 11825 10596 10752 179 -1833 214 C ATOM 2352 CE1 PHE A 294 7.041 43.216 49.409 1.00 78.86 C ANISOU 2352 CE1 PHE A 294 10935 9419 9611 358 -1608 302 C ATOM 2353 CE2 PHE A 294 7.232 45.475 48.650 1.00 80.72 C ANISOU 2353 CE2 PHE A 294 11130 9741 9798 340 -1864 258 C ATOM 2354 CZ PHE A 294 6.865 44.569 49.626 1.00 79.37 C ANISOU 2354 CZ PHE A 294 11047 9520 9589 429 -1748 302 C ATOM 2355 N ALA A 295 10.878 42.654 43.765 1.00 65.61 N ANISOU 2355 N ALA A 295 8601 7852 8475 -337 -1748 26 N ATOM 2356 CA ALA A 295 11.226 41.985 42.516 1.00 63.73 C ANISOU 2356 CA ALA A 295 8198 7663 8353 -506 -1676 -36 C ATOM 2357 C ALA A 295 12.563 41.258 42.613 1.00 77.44 C ANISOU 2357 C ALA A 295 9919 9319 10186 -503 -1716 -68 C ATOM 2358 O ALA A 295 12.690 40.126 42.134 1.00 60.65 O ANISOU 2358 O ALA A 295 7707 7186 8152 -580 -1600 -104 O ATOM 2359 CB ALA A 295 11.250 42.993 41.368 1.00 57.41 C ANISOU 2359 CB ALA A 295 7289 6968 7557 -635 -1757 -74 C ATOM 2360 N LYS A 296 13.571 41.889 43.223 1.00 72.34 N ANISOU 2360 N LYS A 296 9356 8610 9522 -413 -1883 -60 N ATOM 2361 CA LYS A 296 14.879 41.249 43.331 1.00 72.92 C ANISOU 2361 CA LYS A 296 9414 8606 9685 -405 -1933 -97 C ATOM 2362 C LYS A 296 14.852 40.063 44.285 1.00 76.11 C ANISOU 2362 C LYS A 296 9908 8903 10107 -302 -1841 -67 C ATOM 2363 O LYS A 296 15.568 39.079 44.066 1.00 71.07 O ANISOU 2363 O LYS A 296 9214 8219 9569 -339 -1804 -110 O ATOM 2364 CB LYS A 296 15.931 42.264 43.780 1.00 77.11 C ANISOU 2364 CB LYS A 296 10014 9095 10187 -331 -2138 -94 C ATOM 2365 CG LYS A 296 16.293 43.298 42.727 1.00 76.45 C ANISOU 2365 CG LYS A 296 9826 9108 10114 -456 -2245 -133 C ATOM 2366 CD LYS A 296 17.274 44.321 43.279 1.00 91.23 C ANISOU 2366 CD LYS A 296 11781 10932 11950 -372 -2451 -121 C ATOM 2367 CE LYS A 296 17.763 45.267 42.194 1.00 96.11 C ANISOU 2367 CE LYS A 296 12289 11641 12587 -511 -2562 -161 C ATOM 2368 NZ LYS A 296 18.551 44.554 41.150 1.00 92.50 N ANISOU 2368 NZ LYS A 296 11671 11227 12246 -660 -2518 -238 N ATOM 2369 N THR A 297 14.040 40.132 45.342 1.00 67.95 N ANISOU 2369 N THR A 297 9014 7830 8975 -174 -1806 3 N ATOM 2370 CA THR A 297 13.928 39.022 46.280 1.00 69.31 C ANISOU 2370 CA THR A 297 9280 7902 9152 -80 -1716 40 C ATOM 2371 C THR A 297 13.285 37.790 45.652 1.00 66.95 C ANISOU 2371 C THR A 297 8883 7629 8925 -186 -1527 21 C ATOM 2372 O THR A 297 13.372 36.702 46.232 1.00 54.94 O ANISOU 2372 O THR A 297 7415 6021 7438 -137 -1454 39 O ATOM 2373 CB THR A 297 13.136 39.461 47.516 1.00 59.31 C ANISOU 2373 CB THR A 297 8178 6605 7751 72 -1721 120 C ATOM 2374 OG1 THR A 297 13.549 40.778 47.899 1.00 74.78 O ANISOU 2374 OG1 THR A 297 10207 8566 9639 151 -1896 132 O ATOM 2375 CG2 THR A 297 13.383 38.519 48.687 1.00 51.58 C ANISOU 2375 CG2 THR A 297 7327 5503 6768 194 -1687 165 C ATOM 2376 N SER A 298 12.663 37.928 44.477 1.00 64.55 N ANISOU 2376 N SER A 298 8440 7440 8647 -330 -1451 -16 N ATOM 2377 CA SER A 298 12.093 36.770 43.797 1.00 59.28 C ANISOU 2377 CA SER A 298 7668 6799 8056 -438 -1276 -42 C ATOM 2378 C SER A 298 13.154 35.746 43.419 1.00 72.22 C ANISOU 2378 C SER A 298 9232 8380 9827 -490 -1270 -102 C ATOM 2379 O SER A 298 12.812 34.597 43.128 1.00 82.04 O ANISOU 2379 O SER A 298 10420 9612 11140 -547 -1133 -117 O ATOM 2380 CB SER A 298 11.323 37.210 42.551 1.00 40.44 C ANISOU 2380 CB SER A 298 5141 4550 5674 -586 -1213 -77 C ATOM 2381 OG SER A 298 12.196 37.725 41.562 1.00 64.74 O ANISOU 2381 OG SER A 298 8102 7683 8815 -690 -1311 -143 O ATOM 2382 N ALA A 299 14.431 36.132 43.418 1.00 56.01 N ANISOU 2382 N ALA A 299 7175 6292 7814 -470 -1419 -140 N ATOM 2383 CA ALA A 299 15.500 35.161 43.229 1.00 56.38 C ANISOU 2383 CA ALA A 299 7167 6273 7983 -495 -1427 -199 C ATOM 2384 C ALA A 299 15.604 34.177 44.385 1.00 67.86 C ANISOU 2384 C ALA A 299 8753 7590 9442 -369 -1392 -154 C ATOM 2385 O ALA A 299 16.308 33.170 44.257 1.00 66.23 O ANISOU 2385 O ALA A 299 8504 7320 9341 -388 -1375 -201 O ATOM 2386 CB ALA A 299 16.837 35.880 43.040 1.00 47.93 C ANISOU 2386 CB ALA A 299 6069 5198 6942 -494 -1602 -248 C ATOM 2387 N VAL A 300 14.921 34.437 45.497 1.00 62.23 N ANISOU 2387 N VAL A 300 8196 6832 8617 -245 -1384 -67 N ATOM 2388 CA VAL A 300 14.970 33.587 46.679 1.00 53.88 C ANISOU 2388 CA VAL A 300 7279 5646 7546 -122 -1357 -13 C ATOM 2389 C VAL A 300 13.665 32.821 46.872 1.00 67.66 C ANISOU 2389 C VAL A 300 9049 7401 9258 -137 -1180 40 C ATOM 2390 O VAL A 300 13.676 31.606 47.070 1.00 72.16 O ANISOU 2390 O VAL A 300 9629 7896 9891 -139 -1095 44 O ATOM 2391 CB VAL A 300 15.321 34.412 47.938 1.00 60.95 C ANISOU 2391 CB VAL A 300 8349 6474 8337 45 -1494 48 C ATOM 2392 CG1 VAL A 300 15.252 33.539 49.181 1.00 63.19 C ANISOU 2392 CG1 VAL A 300 8784 6630 8594 168 -1457 112 C ATOM 2393 CG2 VAL A 300 16.701 35.032 47.795 1.00 77.94 C ANISOU 2393 CG2 VAL A 300 10478 8601 10534 62 -1669 -6 C ATOM 2394 N TYR A 301 12.526 33.515 46.815 1.00 65.85 N ANISOU 2394 N TYR A 301 8828 7263 8930 -148 -1124 80 N ATOM 2395 CA TYR A 301 11.258 32.867 47.127 1.00 70.61 C ANISOU 2395 CA TYR A 301 9466 7877 9484 -150 -961 136 C ATOM 2396 C TYR A 301 10.604 32.189 45.927 1.00 80.21 C ANISOU 2396 C TYR A 301 10522 9173 10782 -310 -812 90 C ATOM 2397 O TYR A 301 9.667 31.407 46.121 1.00 92.82 O ANISOU 2397 O TYR A 301 12137 10767 12365 -325 -668 129 O ATOM 2398 CB TYR A 301 10.274 33.863 47.767 1.00 54.41 C ANISOU 2398 CB TYR A 301 7511 5882 7281 -72 -965 200 C ATOM 2399 CG TYR A 301 9.863 35.056 46.927 1.00 71.95 C ANISOU 2399 CG TYR A 301 9641 8230 9464 -141 -1005 168 C ATOM 2400 CD1 TYR A 301 8.947 34.924 45.889 1.00 77.81 C ANISOU 2400 CD1 TYR A 301 10253 9079 10231 -274 -881 140 C ATOM 2401 CD2 TYR A 301 10.352 36.326 47.207 1.00 73.94 C ANISOU 2401 CD2 TYR A 301 9947 8494 9653 -70 -1169 170 C ATOM 2402 CE1 TYR A 301 8.558 36.014 45.134 1.00 68.50 C ANISOU 2402 CE1 TYR A 301 8999 8013 9016 -337 -922 113 C ATOM 2403 CE2 TYR A 301 9.965 37.423 46.460 1.00 59.43 C ANISOU 2403 CE2 TYR A 301 8036 6767 7779 -133 -1213 145 C ATOM 2404 CZ TYR A 301 9.069 37.260 45.424 1.00 59.67 C ANISOU 2404 CZ TYR A 301 7937 6900 7836 -267 -1091 116 C ATOM 2405 OH TYR A 301 8.683 38.347 44.675 1.00 64.15 O ANISOU 2405 OH TYR A 301 8433 7573 8367 -332 -1141 92 O ATOM 2406 N ASN A 302 11.061 32.459 44.698 1.00 70.34 N ANISOU 2406 N ASN A 302 9116 7998 9613 -433 -842 9 N ATOM 2407 CA ASN A 302 10.573 31.667 43.569 1.00 64.20 C ANISOU 2407 CA ASN A 302 8183 7283 8925 -582 -703 -41 C ATOM 2408 C ASN A 302 11.073 30.228 43.629 1.00 68.15 C ANISOU 2408 C ASN A 302 8668 7686 9539 -595 -644 -64 C ATOM 2409 O ASN A 302 10.266 29.309 43.404 1.00 69.51 O ANISOU 2409 O ASN A 302 8804 7863 9743 -653 -495 -54 O ATOM 2410 CB ASN A 302 10.940 32.342 42.243 1.00 55.49 C ANISOU 2410 CB ASN A 302 6918 6291 7874 -712 -753 -121 C ATOM 2411 CG ASN A 302 9.997 33.470 41.882 1.00 66.89 C ANISOU 2411 CG ASN A 302 8341 7851 9222 -745 -749 -102 C ATOM 2412 OD1 ASN A 302 8.858 33.517 42.347 1.00 65.87 O ANISOU 2412 OD1 ASN A 302 8277 7742 9009 -706 -661 -44 O ATOM 2413 ND2 ASN A 302 10.463 34.383 41.037 1.00 81.08 N ANISOU 2413 ND2 ASN A 302 10047 9729 11032 -820 -845 -152 N ATOM 2414 N PRO A 303 12.353 29.949 43.908 1.00 71.72 N ANISOU 2414 N PRO A 303 9145 8047 10060 -546 -754 -98 N ATOM 2415 CA PRO A 303 12.746 28.543 44.107 1.00 57.51 C ANISOU 2415 CA PRO A 303 7350 6140 8360 -541 -701 -113 C ATOM 2416 C PRO A 303 12.086 27.905 45.315 1.00 60.93 C ANISOU 2416 C PRO A 303 7944 6478 8727 -439 -632 -17 C ATOM 2417 O PRO A 303 11.875 26.686 45.323 1.00 78.18 O ANISOU 2417 O PRO A 303 10120 8602 10981 -469 -534 -14 O ATOM 2418 CB PRO A 303 14.270 28.622 44.271 1.00 64.43 C ANISOU 2418 CB PRO A 303 8236 6942 9302 -490 -859 -167 C ATOM 2419 CG PRO A 303 14.658 29.900 43.621 1.00 74.78 C ANISOU 2419 CG PRO A 303 9471 8356 10585 -534 -962 -209 C ATOM 2420 CD PRO A 303 13.529 30.838 43.897 1.00 56.91 C ANISOU 2420 CD PRO A 303 7270 6167 8188 -510 -930 -136 C ATOM 2421 N VAL A 304 11.752 28.689 46.341 1.00 63.93 N ANISOU 2421 N VAL A 304 8471 6844 8974 -322 -681 62 N ATOM 2422 CA VAL A 304 11.058 28.133 47.498 1.00 72.54 C ANISOU 2422 CA VAL A 304 9715 7860 9989 -230 -610 157 C ATOM 2423 C VAL A 304 9.660 27.667 47.109 1.00 72.58 C ANISOU 2423 C VAL A 304 9667 7938 9971 -317 -429 185 C ATOM 2424 O VAL A 304 9.192 26.614 47.561 1.00 75.69 O ANISOU 2424 O VAL A 304 10115 8267 10377 -312 -326 231 O ATOM 2425 CB VAL A 304 11.018 29.166 48.640 1.00 63.46 C ANISOU 2425 CB VAL A 304 8723 6693 8695 -86 -708 227 C ATOM 2426 CG1 VAL A 304 10.111 28.690 49.765 1.00 53.44 C ANISOU 2426 CG1 VAL A 304 7601 5376 7328 -5 -617 327 C ATOM 2427 CG2 VAL A 304 12.421 29.429 49.162 1.00 64.38 C ANISOU 2427 CG2 VAL A 304 8909 6714 8840 10 -881 206 C ATOM 2428 N ILE A 305 8.980 28.428 46.252 1.00 65.54 N ANISOU 2428 N ILE A 305 8669 7182 9051 -402 -388 157 N ATOM 2429 CA ILE A 305 7.606 28.097 45.887 1.00 59.12 C ANISOU 2429 CA ILE A 305 7806 6448 8208 -480 -221 182 C ATOM 2430 C ILE A 305 7.569 27.069 44.762 1.00 57.83 C ANISOU 2430 C ILE A 305 7487 6302 8185 -622 -117 116 C ATOM 2431 O ILE A 305 6.787 26.113 44.808 1.00 73.97 O ANISOU 2431 O ILE A 305 9530 8330 10247 -662 22 146 O ATOM 2432 CB ILE A 305 6.841 29.379 45.510 1.00 68.11 C ANISOU 2432 CB ILE A 305 8907 7721 9251 -500 -227 182 C ATOM 2433 CG1 ILE A 305 6.703 30.293 46.729 1.00 61.79 C ANISOU 2433 CG1 ILE A 305 8270 6901 8305 -351 -313 253 C ATOM 2434 CG2 ILE A 305 5.475 29.042 44.931 1.00 71.35 C ANISOU 2434 CG2 ILE A 305 9237 8224 9648 -598 -55 189 C ATOM 2435 CD1 ILE A 305 6.027 31.606 46.430 1.00 43.54 C ANISOU 2435 CD1 ILE A 305 5933 4712 5899 -356 -342 249 C ATOM 2436 N TYR A 306 8.409 27.239 43.742 1.00 53.80 N ANISOU 2436 N TYR A 306 6842 5827 7772 -702 -183 25 N ATOM 2437 CA TYR A 306 8.335 26.422 42.538 1.00 62.59 C ANISOU 2437 CA TYR A 306 7788 6981 9011 -846 -89 -49 C ATOM 2438 C TYR A 306 9.272 25.220 42.547 1.00 72.17 C ANISOU 2438 C TYR A 306 8986 8081 10355 -848 -105 -91 C ATOM 2439 O TYR A 306 9.112 24.331 41.705 1.00 80.37 O ANISOU 2439 O TYR A 306 9903 9136 11499 -954 -12 -145 O ATOM 2440 CB TYR A 306 8.624 27.283 41.301 1.00 56.90 C ANISOU 2440 CB TYR A 306 6912 6383 8322 -949 -139 -132 C ATOM 2441 CG TYR A 306 7.567 28.330 41.032 1.00 74.95 C ANISOU 2441 CG TYR A 306 9182 8792 10502 -977 -104 -104 C ATOM 2442 CD1 TYR A 306 7.637 29.585 41.625 1.00 78.43 C ANISOU 2442 CD1 TYR A 306 9717 9252 10829 -887 -217 -66 C ATOM 2443 CD2 TYR A 306 6.497 28.063 40.189 1.00 73.69 C ANISOU 2443 CD2 TYR A 306 8915 8727 10359 -1091 38 -120 C ATOM 2444 CE1 TYR A 306 6.671 30.543 41.384 1.00 69.39 C ANISOU 2444 CE1 TYR A 306 8559 8216 9590 -908 -194 -46 C ATOM 2445 CE2 TYR A 306 5.527 29.016 39.942 1.00 71.86 C ANISOU 2445 CE2 TYR A 306 8668 8604 10032 -1114 66 -100 C ATOM 2446 CZ TYR A 306 5.618 30.254 40.543 1.00 69.71 C ANISOU 2446 CZ TYR A 306 8490 8348 9648 -1022 -53 -64 C ATOM 2447 OH TYR A 306 4.655 31.205 40.299 1.00100.07 O ANISOU 2447 OH TYR A 306 12321 12299 13402 -1040 -34 -49 O ATOM 2448 N ILE A 307 10.237 25.163 43.464 1.00 65.21 N ANISOU 2448 N ILE A 307 8223 7084 9472 -732 -223 -72 N ATOM 2449 CA ILE A 307 11.173 24.043 43.502 1.00 69.57 C ANISOU 2449 CA ILE A 307 8764 7522 10149 -726 -253 -117 C ATOM 2450 C ILE A 307 11.091 23.339 44.851 1.00 66.84 C ANISOU 2450 C ILE A 307 8600 7034 9763 -608 -248 -28 C ATOM 2451 O ILE A 307 10.812 22.137 44.917 1.00 56.11 O ANISOU 2451 O ILE A 307 7245 5604 8469 -635 -159 -16 O ATOM 2452 CB ILE A 307 12.614 24.503 43.213 1.00 64.57 C ANISOU 2452 CB ILE A 307 8082 6874 9578 -708 -413 -199 C ATOM 2453 CG1 ILE A 307 12.709 25.136 41.824 1.00 59.53 C ANISOU 2453 CG1 ILE A 307 7257 6381 8982 -840 -415 -288 C ATOM 2454 CG2 ILE A 307 13.578 23.335 43.334 1.00 65.83 C ANISOU 2454 CG2 ILE A 307 8238 6909 9864 -689 -451 -249 C ATOM 2455 CD1 ILE A 307 12.354 24.192 40.698 1.00 62.94 C ANISOU 2455 CD1 ILE A 307 7526 6861 9526 -979 -291 -357 C ATOM 2456 N MET A 308 11.333 24.081 45.935 1.00 64.56 N ANISOU 2456 N MET A 308 8464 6701 9366 -477 -346 37 N ATOM 2457 CA MET A 308 11.364 23.465 47.258 1.00 57.74 C ANISOU 2457 CA MET A 308 7781 5700 8458 -360 -356 122 C ATOM 2458 C MET A 308 9.996 22.939 47.678 1.00 59.90 C ANISOU 2458 C MET A 308 8116 5984 8660 -376 -200 210 C ATOM 2459 O MET A 308 9.918 21.993 48.470 1.00 76.43 O ANISOU 2459 O MET A 308 10318 7964 10758 -329 -167 269 O ATOM 2460 CB MET A 308 11.894 24.458 48.291 1.00 64.43 C ANISOU 2460 CB MET A 308 8772 6511 9198 -218 -497 169 C ATOM 2461 CG MET A 308 13.406 24.624 48.264 1.00 96.31 C ANISOU 2461 CG MET A 308 12798 10481 13313 -171 -661 99 C ATOM 2462 SD MET A 308 14.001 25.838 49.456 1.00125.56 S ANISOU 2462 SD MET A 308 16671 14146 16892 -5 -827 153 S ATOM 2463 CE MET A 308 13.292 25.201 50.973 1.00122.12 C ANISOU 2463 CE MET A 308 16448 13602 16352 110 -767 283 C ATOM 2464 N MET A 309 8.917 23.528 47.171 1.00 64.50 N ANISOU 2464 N MET A 309 8631 6699 9176 -442 -105 221 N ATOM 2465 CA MET A 309 7.578 23.024 47.439 1.00 59.02 C ANISOU 2465 CA MET A 309 7973 6031 8421 -473 54 294 C ATOM 2466 C MET A 309 7.140 21.958 46.443 1.00 66.40 C ANISOU 2466 C MET A 309 8769 6985 9475 -611 184 248 C ATOM 2467 O MET A 309 6.014 21.460 46.545 1.00 62.28 O ANISOU 2467 O MET A 309 8259 6489 8916 -653 325 301 O ATOM 2468 CB MET A 309 6.567 24.174 47.454 1.00 61.88 C ANISOU 2468 CB MET A 309 8339 6526 8648 -468 92 328 C ATOM 2469 CG MET A 309 6.516 24.920 48.779 1.00 74.28 C ANISOU 2469 CG MET A 309 10088 8066 10070 -320 18 410 C ATOM 2470 SD MET A 309 5.241 26.192 48.840 1.00 98.83 S ANISOU 2470 SD MET A 309 13202 11329 13021 -309 67 446 S ATOM 2471 CE MET A 309 5.274 26.613 50.580 1.00103.89 C ANISOU 2471 CE MET A 309 14070 11896 13506 -127 -8 547 C ATOM 2472 N ASN A 310 7.996 21.602 45.488 1.00 68.33 N ANISOU 2472 N ASN A 310 8881 7221 9859 -682 141 147 N ATOM 2473 CA ASN A 310 7.739 20.465 44.616 1.00 66.46 C ANISOU 2473 CA ASN A 310 8522 6983 9749 -801 250 98 C ATOM 2474 C ASN A 310 8.192 19.191 45.319 1.00 73.98 C ANISOU 2474 C ASN A 310 9568 7771 10770 -754 240 127 C ATOM 2475 O ASN A 310 9.296 19.136 45.869 1.00 82.02 O ANISOU 2475 O ASN A 310 10660 8687 11817 -666 110 115 O ATOM 2476 CB ASN A 310 8.468 20.640 43.283 1.00 66.84 C ANISOU 2476 CB ASN A 310 8383 7100 9915 -897 205 -28 C ATOM 2477 CG ASN A 310 8.005 19.655 42.225 1.00 71.72 C ANISOU 2477 CG ASN A 310 8850 7751 10649 -1032 331 -86 C ATOM 2478 OD1 ASN A 310 7.848 18.463 42.488 1.00101.55 O ANISOU 2478 OD1 ASN A 310 12661 11434 14490 -1040 393 -64 O ATOM 2479 ND2 ASN A 310 7.783 20.155 41.014 1.00 62.52 N ANISOU 2479 ND2 ASN A 310 7520 6720 9513 -1142 365 -159 N ATOM 2480 N LYS A 311 7.334 18.168 45.303 1.00 74.16 N ANISOU 2480 N LYS A 311 9589 7768 10819 -813 376 166 N ATOM 2481 CA LYS A 311 7.610 16.962 46.077 1.00 76.28 C ANISOU 2481 CA LYS A 311 9968 7878 11138 -767 372 212 C ATOM 2482 C LYS A 311 8.828 16.217 45.542 1.00 83.96 C ANISOU 2482 C LYS A 311 10862 8764 12276 -786 284 111 C ATOM 2483 O LYS A 311 9.607 15.654 46.320 1.00 72.34 O ANISOU 2483 O LYS A 311 9501 7148 10836 -701 195 130 O ATOM 2484 CB LYS A 311 6.381 16.054 46.085 1.00 80.76 C ANISOU 2484 CB LYS A 311 10539 8445 11699 -841 539 273 C ATOM 2485 CG LYS A 311 6.421 14.959 47.139 1.00 91.43 C ANISOU 2485 CG LYS A 311 12046 9638 13056 -785 542 357 C ATOM 2486 CD LYS A 311 5.131 14.155 47.145 1.00112.99 C ANISOU 2486 CD LYS A 311 14780 12383 15769 -865 710 424 C ATOM 2487 CE LYS A 311 5.146 13.091 48.231 1.00118.74 C ANISOU 2487 CE LYS A 311 15672 12952 16493 -814 710 516 C ATOM 2488 NZ LYS A 311 3.914 12.255 48.205 1.00115.86 N ANISOU 2488 NZ LYS A 311 15306 12599 16118 -903 873 581 N ATOM 2489 N GLN A 312 9.014 16.206 44.220 1.00 91.60 N ANISOU 2489 N GLN A 312 11638 9819 13348 -894 306 0 N ATOM 2490 CA GLN A 312 10.155 15.501 43.642 1.00 98.37 C ANISOU 2490 CA GLN A 312 12404 10608 14365 -916 227 -108 C ATOM 2491 C GLN A 312 11.465 16.211 43.962 1.00107.55 C ANISOU 2491 C GLN A 312 13602 11737 15525 -823 52 -152 C ATOM 2492 O GLN A 312 12.444 15.574 44.367 1.00114.47 O ANISOU 2492 O GLN A 312 14529 12484 16480 -761 -45 -181 O ATOM 2493 CB GLN A 312 9.977 15.359 42.130 1.00110.28 C ANISOU 2493 CB GLN A 312 13693 12234 15975 -1059 299 -217 C ATOM 2494 CG GLN A 312 9.077 14.209 41.711 1.00126.07 C ANISOU 2494 CG GLN A 312 15637 14220 18044 -1153 445 -208 C ATOM 2495 CD GLN A 312 9.768 13.253 40.758 1.00144.69 C ANISOU 2495 CD GLN A 312 17848 16548 20581 -1225 430 -331 C ATOM 2496 OE1 GLN A 312 9.505 13.258 39.555 1.00150.71 O ANISOU 2496 OE1 GLN A 312 18435 17423 21406 -1340 497 -413 O ATOM 2497 NE2 GLN A 312 10.658 12.424 41.293 1.00150.36 N ANISOU 2497 NE2 GLN A 312 18635 17113 21381 -1158 339 -348 N ATOM 2498 N PHE A 313 11.504 17.534 43.781 1.00 98.84 N ANISOU 2498 N PHE A 313 12474 10747 14334 -813 7 -159 N ATOM 2499 CA PHE A 313 12.733 18.277 44.042 1.00 85.43 C ANISOU 2499 CA PHE A 313 10803 9024 12631 -731 -159 -201 C ATOM 2500 C PHE A 313 13.096 18.256 45.522 1.00 84.59 C ANISOU 2500 C PHE A 313 10909 8781 12450 -580 -246 -111 C ATOM 2501 O PHE A 313 14.274 18.127 45.875 1.00 84.37 O ANISOU 2501 O PHE A 313 10921 8659 12478 -506 -379 -151 O ATOM 2502 CB PHE A 313 12.595 19.717 43.549 1.00 72.19 C ANISOU 2502 CB PHE A 313 9062 7498 10869 -757 -187 -218 C ATOM 2503 CG PHE A 313 12.878 19.889 42.084 1.00 81.38 C ANISOU 2503 CG PHE A 313 10013 8781 12126 -886 -175 -338 C ATOM 2504 CD1 PHE A 313 14.171 20.105 41.637 1.00 84.23 C ANISOU 2504 CD1 PHE A 313 10293 9142 12567 -887 -301 -438 C ATOM 2505 CD2 PHE A 313 11.852 19.842 41.154 1.00 82.83 C ANISOU 2505 CD2 PHE A 313 10075 9082 12315 -1009 -38 -351 C ATOM 2506 CE1 PHE A 313 14.438 20.267 40.291 1.00 77.46 C ANISOU 2506 CE1 PHE A 313 9239 8403 11789 -1011 -289 -549 C ATOM 2507 CE2 PHE A 313 12.113 20.003 39.805 1.00 69.59 C ANISOU 2507 CE2 PHE A 313 8204 7518 10720 -1131 -28 -460 C ATOM 2508 CZ PHE A 313 13.408 20.216 39.374 1.00 69.79 C ANISOU 2508 CZ PHE A 313 8150 7546 10819 -1133 -153 -558 C ATOM 2509 N ARG A 314 12.099 18.380 46.401 1.00 80.72 N ANISOU 2509 N ARG A 314 10555 8281 11834 -533 -174 10 N ATOM 2510 CA ARG A 314 12.380 18.419 47.833 1.00 75.00 C ANISOU 2510 CA ARG A 314 10038 7436 11024 -390 -253 102 C ATOM 2511 C ARG A 314 12.966 17.098 48.318 1.00 82.61 C ANISOU 2511 C ARG A 314 11071 8230 12087 -354 -286 103 C ATOM 2512 O ARG A 314 13.861 17.086 49.170 1.00 96.74 O ANISOU 2512 O ARG A 314 12980 9905 13871 -241 -412 118 O ATOM 2513 CB ARG A 314 11.108 18.765 48.607 1.00 71.81 C ANISOU 2513 CB ARG A 314 9751 7071 10463 -360 -154 226 C ATOM 2514 CG ARG A 314 11.306 18.886 50.110 1.00 70.82 C ANISOU 2514 CG ARG A 314 9841 6837 10231 -214 -229 326 C ATOM 2515 CD ARG A 314 10.035 19.345 50.813 1.00 86.83 C ANISOU 2515 CD ARG A 314 11969 8928 12094 -188 -131 438 C ATOM 2516 NE ARG A 314 8.924 18.415 50.627 1.00 98.61 N ANISOU 2516 NE ARG A 314 13439 10431 13597 -278 34 482 N ATOM 2517 CZ ARG A 314 7.922 18.605 49.774 1.00100.35 C ANISOU 2517 CZ ARG A 314 13536 10784 13808 -386 162 464 C ATOM 2518 NH1 ARG A 314 7.885 19.699 49.025 1.00100.93 N ANISOU 2518 NH1 ARG A 314 13500 10988 13859 -419 141 405 N ATOM 2519 NH2 ARG A 314 6.955 17.704 49.672 1.00107.18 N ANISOU 2519 NH2 ARG A 314 14388 11649 14686 -463 308 506 N ATOM 2520 N ASN A 315 12.479 15.976 47.783 1.00 86.01 N ANISOU 2520 N ASN A 315 11430 8640 12611 -448 -178 86 N ATOM 2521 CA ASN A 315 13.031 14.680 48.168 1.00 74.61 C ANISOU 2521 CA ASN A 315 10044 7031 11272 -421 -214 81 C ATOM 2522 C ASN A 315 14.460 14.518 47.667 1.00 77.87 C ANISOU 2522 C ASN A 315 10370 7396 11822 -406 -351 -47 C ATOM 2523 O ASN A 315 15.330 14.033 48.401 1.00 84.36 O ANISOU 2523 O ASN A 315 11297 8073 12684 -313 -462 -45 O ATOM 2524 CB ASN A 315 12.147 13.551 47.639 1.00 78.39 C ANISOU 2524 CB ASN A 315 10456 7505 11823 -531 -68 88 C ATOM 2525 CG ASN A 315 10.783 13.520 48.300 1.00 95.92 C ANISOU 2525 CG ASN A 315 12784 9748 13913 -538 63 221 C ATOM 2526 OD1 ASN A 315 10.616 13.985 49.427 1.00103.27 O ANISOU 2526 OD1 ASN A 315 13881 10646 14712 -440 32 321 O ATOM 2527 ND2 ASN A 315 9.799 12.965 47.601 1.00 94.92 N ANISOU 2527 ND2 ASN A 315 12561 9683 13821 -655 210 221 N ATOM 2528 N CYS A 316 14.723 14.918 46.420 1.00 74.37 N ANISOU 2528 N CYS A 316 9733 7075 11449 -497 -346 -161 N ATOM 2529 CA CYS A 316 16.072 14.804 45.876 1.00 72.55 C ANISOU 2529 CA CYS A 316 9402 6817 11344 -491 -470 -291 C ATOM 2530 C CYS A 316 17.038 15.766 46.555 1.00 87.41 C ANISOU 2530 C CYS A 316 11373 8675 13164 -375 -626 -290 C ATOM 2531 O CYS A 316 18.229 15.457 46.682 1.00104.80 O ANISOU 2531 O CYS A 316 13577 10788 15454 -318 -753 -362 O ATOM 2532 CB CYS A 316 16.050 15.048 44.368 1.00 75.37 C ANISOU 2532 CB CYS A 316 9530 7328 11779 -626 -419 -409 C ATOM 2533 SG CYS A 316 15.062 13.852 43.439 1.00 75.27 S ANISOU 2533 SG CYS A 316 9391 7343 11865 -767 -247 -434 S ATOM 2534 N MET A 317 16.553 16.929 46.996 1.00 91.45 N ANISOU 2534 N MET A 317 11957 9264 13527 -335 -624 -212 N ATOM 2535 CA MET A 317 17.424 17.874 47.687 1.00 86.34 C ANISOU 2535 CA MET A 317 11401 8590 12814 -220 -773 -204 C ATOM 2536 C MET A 317 17.792 17.374 49.078 1.00 92.16 C ANISOU 2536 C MET A 317 12344 9153 13518 -83 -849 -125 C ATOM 2537 O MET A 317 18.943 17.510 49.506 1.00 86.09 O ANISOU 2537 O MET A 317 11624 8303 12782 7 -996 -164 O ATOM 2538 CB MET A 317 16.757 19.246 47.771 1.00 85.45 C ANISOU 2538 CB MET A 317 11309 8606 12551 -214 -752 -145 C ATOM 2539 CG MET A 317 16.854 20.061 46.494 1.00 95.67 C ANISOU 2539 CG MET A 317 12415 10063 13874 -321 -747 -238 C ATOM 2540 SD MET A 317 16.152 21.710 46.681 1.00109.57 S ANISOU 2540 SD MET A 317 14217 11956 15459 -300 -749 -168 S ATOM 2541 CE MET A 317 16.659 22.466 45.141 1.00 99.63 C ANISOU 2541 CE MET A 317 12731 10854 14269 -428 -782 -296 C ATOM 2542 N VAL A 318 16.827 16.800 49.801 1.00 93.45 N ANISOU 2542 N VAL A 318 12631 9260 13616 -67 -753 -12 N ATOM 2543 CA VAL A 318 17.122 16.241 51.117 1.00 86.92 C ANISOU 2543 CA VAL A 318 12003 8265 12757 54 -819 70 C ATOM 2544 C VAL A 318 18.102 15.082 50.991 1.00 90.51 C ANISOU 2544 C VAL A 318 12434 8582 13372 62 -895 -9 C ATOM 2545 O VAL A 318 19.008 14.921 51.818 1.00 89.53 O ANISOU 2545 O VAL A 318 12429 8329 13261 175 -1026 -4 O ATOM 2546 CB VAL A 318 15.821 15.816 51.824 1.00 74.64 C ANISOU 2546 CB VAL A 318 10571 6691 11099 49 -687 206 C ATOM 2547 CG1 VAL A 318 16.129 15.020 53.084 1.00 67.22 C ANISOU 2547 CG1 VAL A 318 9826 5569 10144 154 -748 286 C ATOM 2548 CG2 VAL A 318 14.985 17.038 52.166 1.00 83.65 C ANISOU 2548 CG2 VAL A 318 11761 7954 12069 73 -641 283 C ATOM 2549 N THR A 319 17.948 14.266 49.946 1.00 88.93 N ANISOU 2549 N THR A 319 12080 8409 13300 -54 -820 -90 N ATOM 2550 CA THR A 319 18.887 13.172 49.716 1.00 85.48 C ANISOU 2550 CA THR A 319 11602 7851 13027 -50 -896 -182 C ATOM 2551 C THR A 319 20.288 13.704 49.438 1.00 87.05 C ANISOU 2551 C THR A 319 11730 8052 13291 -1 -1052 -300 C ATOM 2552 O THR A 319 21.267 13.253 50.043 1.00 93.44 O ANISOU 2552 O THR A 319 12621 8723 14159 92 -1180 -326 O ATOM 2553 CB THR A 319 18.402 12.299 48.557 1.00 78.88 C ANISOU 2553 CB THR A 319 10596 7063 12311 -189 -780 -254 C ATOM 2554 OG1 THR A 319 17.167 11.668 48.915 1.00 80.40 O ANISOU 2554 OG1 THR A 319 10867 7229 12451 -228 -644 -141 O ATOM 2555 CG2 THR A 319 19.434 11.233 48.227 1.00 87.70 C ANISOU 2555 CG2 THR A 319 11651 8067 13604 -185 -869 -369 C ATOM 2556 N THR A 320 20.400 14.676 48.530 1.00 85.53 N ANISOU 2556 N THR A 320 11388 8020 13088 -65 -1047 -372 N ATOM 2557 CA THR A 320 21.710 15.219 48.181 1.00 80.47 C ANISOU 2557 CA THR A 320 10666 7400 12508 -34 -1190 -488 C ATOM 2558 C THR A 320 22.360 15.914 49.372 1.00 85.33 C ANISOU 2558 C THR A 320 11454 7935 13033 114 -1326 -428 C ATOM 2559 O THR A 320 23.556 15.732 49.630 1.00 97.62 O ANISOU 2559 O THR A 320 13027 9400 14663 189 -1466 -498 O ATOM 2560 CB THR A 320 21.579 16.183 47.001 1.00 72.29 C ANISOU 2560 CB THR A 320 9446 6560 11462 -142 -1150 -559 C ATOM 2561 OG1 THR A 320 21.159 15.460 45.836 1.00 78.54 O ANISOU 2561 OG1 THR A 320 10065 7420 12357 -278 -1039 -635 O ATOM 2562 CG2 THR A 320 22.908 16.869 46.714 1.00 69.78 C ANISOU 2562 CG2 THR A 320 9055 6272 11187 -111 -1299 -666 C ATOM 2563 N LEU A 321 21.586 16.707 50.118 1.00 85.91 N ANISOU 2563 N LEU A 321 11656 8040 12947 163 -1290 -303 N ATOM 2564 CA LEU A 321 22.155 17.436 51.247 1.00 79.82 C ANISOU 2564 CA LEU A 321 11048 7200 12081 305 -1418 -245 C ATOM 2565 C LEU A 321 22.506 16.510 52.405 1.00 89.85 C ANISOU 2565 C LEU A 321 12498 8275 13367 416 -1482 -187 C ATOM 2566 O LEU A 321 23.445 16.794 53.158 1.00 92.90 O ANISOU 2566 O LEU A 321 12985 8572 13741 534 -1625 -191 O ATOM 2567 CB LEU A 321 21.190 18.526 51.712 1.00 67.87 C ANISOU 2567 CB LEU A 321 9617 5779 10391 326 -1360 -132 C ATOM 2568 CG LEU A 321 20.996 19.702 50.752 1.00 81.47 C ANISOU 2568 CG LEU A 321 11193 7685 12077 244 -1338 -181 C ATOM 2569 CD1 LEU A 321 20.015 20.713 51.326 1.00 89.01 C ANISOU 2569 CD1 LEU A 321 12248 8714 12858 280 -1289 -66 C ATOM 2570 CD2 LEU A 321 22.331 20.362 50.439 1.00 73.00 C ANISOU 2570 CD2 LEU A 321 10049 6627 11059 274 -1493 -284 C ATOM 2571 N CYS A 322 21.776 15.408 52.569 1.00 95.73 N ANISOU 2571 N CYS A 322 13288 8948 14137 380 -1382 -132 N ATOM 2572 CA CYS A 322 22.051 14.456 53.645 1.00101.13 C ANISOU 2572 CA CYS A 322 14146 9442 14837 474 -1439 -71 C ATOM 2573 C CYS A 322 22.940 13.307 53.193 1.00117.30 C ANISOU 2573 C CYS A 322 16118 11383 17068 458 -1506 -185 C ATOM 2574 O CYS A 322 22.680 12.145 53.519 1.00122.45 O ANISOU 2574 O CYS A 322 16839 11914 17773 454 -1475 -148 O ATOM 2575 CB CYS A 322 20.741 13.929 54.223 1.00101.40 C ANISOU 2575 CB CYS A 322 14295 9450 14781 451 -1303 68 C ATOM 2576 SG CYS A 322 19.786 15.169 55.125 1.00118.52 S ANISOU 2576 SG CYS A 322 16604 11707 16722 511 -1251 213 S ATOM 2577 N CYS A 323 23.991 13.614 52.434 1.00125.98 N ANISOU 2577 N CYS A 323 17072 12527 18267 445 -1599 -327 N ATOM 2578 CA CYS A 323 25.055 12.682 52.067 1.00122.74 C ANISOU 2578 CA CYS A 323 16588 12019 18028 452 -1694 -455 C ATOM 2579 C CYS A 323 24.567 11.509 51.224 1.00111.40 C ANISOU 2579 C CYS A 323 15035 10579 16714 338 -1589 -505 C ATOM 2580 O CYS A 323 25.283 10.512 51.087 1.00118.39 O ANISOU 2580 O CYS A 323 15890 11352 17739 351 -1660 -592 O ATOM 2581 CB CYS A 323 25.787 12.162 53.312 1.00136.25 C ANISOU 2581 CB CYS A 323 18492 13529 19746 596 -1830 -413 C ATOM 2582 SG CYS A 323 25.959 13.407 54.619 1.00151.17 S ANISOU 2582 SG CYS A 323 20580 15401 21456 740 -1921 -299 S ATOM 2583 N GLY A 324 23.364 11.596 50.657 1.00106.40 N ANISOU 2583 N GLY A 324 14334 10062 16032 227 -1426 -456 N ATOM 2584 CA GLY A 324 22.889 10.608 49.710 1.00 98.36 C ANISOU 2584 CA GLY A 324 13179 9064 15129 108 -1322 -515 C ATOM 2585 C GLY A 324 21.933 9.565 50.251 1.00107.21 C ANISOU 2585 C GLY A 324 14417 10079 16238 92 -1228 -404 C ATOM 2586 O GLY A 324 21.419 8.763 49.462 1.00109.91 O ANISOU 2586 O GLY A 324 14648 10444 16670 -13 -1130 -444 O ATOM 2587 N LYS A 325 21.671 9.546 51.558 1.00112.35 N ANISOU 2587 N LYS A 325 15288 10620 16781 189 -1253 -266 N ATOM 2588 CA LYS A 325 20.825 8.520 52.174 1.00132.65 C ANISOU 2588 CA LYS A 325 17988 13079 19336 177 -1175 -152 C ATOM 2589 C LYS A 325 19.782 9.179 53.073 1.00141.70 C ANISOU 2589 C LYS A 325 19287 14265 20287 206 -1091 15 C ATOM 2590 O LYS A 325 20.043 9.428 54.253 1.00145.13 O ANISOU 2590 O LYS A 325 19907 14608 20630 321 -1172 101 O ATOM 2591 CB LYS A 325 21.670 7.514 52.954 1.00146.45 C ANISOU 2591 CB LYS A 325 19864 14612 21168 270 -1309 -157 C ATOM 2592 CG LYS A 325 21.895 6.194 52.233 1.00151.65 C ANISOU 2592 CG LYS A 325 20419 15193 22010 203 -1309 -255 C ATOM 2593 CD LYS A 325 22.921 6.328 51.122 1.00149.07 C ANISOU 2593 CD LYS A 325 19882 14934 21823 175 -1383 -446 C ATOM 2594 CE LYS A 325 24.293 6.664 51.682 1.00146.10 C ANISOU 2594 CE LYS A 325 19567 14472 21472 305 -1571 -508 C ATOM 2595 NZ LYS A 325 25.327 6.738 50.615 1.00144.26 N ANISOU 2595 NZ LYS A 325 19128 14307 21378 275 -1646 -700 N ATOM 2596 N ASN A 326 18.607 9.451 52.509 1.00142.18 N ANISOU 2596 N ASN A 326 19269 14466 20288 101 -929 54 N ATOM 2597 CA ASN A 326 17.437 9.863 53.283 1.00138.71 C ANISOU 2597 CA ASN A 326 18961 14067 19675 109 -825 210 C ATOM 2598 C ASN A 326 16.194 9.875 52.397 1.00126.61 C ANISOU 2598 C ASN A 326 17300 12680 18126 -29 -643 220 C ATOM 2599 O ASN A 326 15.159 10.430 52.767 1.00112.80 O ANISOU 2599 O ASN A 326 15610 11015 16234 -41 -541 324 O ATOM 2600 CB ASN A 326 17.641 11.240 53.918 1.00139.15 C ANISOU 2600 CB ASN A 326 19096 14188 19585 205 -888 253 C ATOM 2601 CG ASN A 326 16.852 11.407 55.204 1.00136.36 C ANISOU 2601 CG ASN A 326 18951 13798 19062 272 -846 418 C ATOM 2602 OD1 ASN A 326 16.391 10.429 55.793 1.00137.59 O ANISOU 2602 OD1 ASN A 326 19218 13845 19214 266 -803 502 O ATOM 2603 ND2 ASN A 326 16.697 12.648 55.648 1.00125.96 N ANISOU 2603 ND2 ASN A 326 17686 12570 17602 335 -863 463 N TER 2604 ASN A 326 ATOM 2605 N ILE B 340 -7.116 12.933 36.665 1.00103.22 N ANISOU 2605 N ILE B 340 11862 8936 18419 -1376 -1445 777 N ATOM 2606 CA ILE B 340 -6.141 13.993 36.444 1.00103.29 C ANISOU 2606 CA ILE B 340 11770 9130 18344 -1426 -1506 883 C ATOM 2607 C ILE B 340 -5.023 13.919 37.476 1.00102.95 C ANISOU 2607 C ILE B 340 11489 9259 18369 -1224 -1343 1013 C ATOM 2608 O ILE B 340 -4.087 14.717 37.440 1.00116.09 O ANISOU 2608 O ILE B 340 13042 11091 19974 -1233 -1362 1115 O ATOM 2609 CB ILE B 340 -6.807 15.379 36.475 1.00105.34 C ANISOU 2609 CB ILE B 340 11975 9422 18629 -1598 -1863 882 C ATOM 2610 CG1 ILE B 340 -7.542 15.586 37.801 1.00100.31 C ANISOU 2610 CG1 ILE B 340 11155 8776 18183 -1523 -2017 889 C ATOM 2611 CG2 ILE B 340 -7.753 15.547 35.296 1.00116.12 C ANISOU 2611 CG2 ILE B 340 13584 10636 19899 -1812 -2019 763 C ATOM 2612 CD1 ILE B 340 -8.140 16.964 37.957 1.00100.64 C ANISOU 2612 CD1 ILE B 340 11117 8862 18261 -1675 -2364 898 C ATOM 2613 N LEU B 341 -5.127 12.957 38.397 1.00102.62 N ANISOU 2613 N LEU B 341 11369 9173 18450 -1042 -1183 1010 N ATOM 2614 CA LEU B 341 -4.126 12.833 39.452 1.00102.24 C ANISOU 2614 CA LEU B 341 11090 9279 18478 -841 -1027 1130 C ATOM 2615 C LEU B 341 -2.742 12.547 38.886 1.00106.45 C ANISOU 2615 C LEU B 341 11643 9925 18878 -777 -773 1205 C ATOM 2616 O LEU B 341 -1.736 12.968 39.469 1.00103.40 O ANISOU 2616 O LEU B 341 11065 9715 18507 -678 -716 1326 O ATOM 2617 CB LEU B 341 -4.527 11.738 40.440 1.00101.78 C ANISOU 2617 CB LEU B 341 10970 9134 18566 -661 -884 1102 C ATOM 2618 CG LEU B 341 -5.759 12.013 41.302 1.00101.09 C ANISOU 2618 CG LEU B 341 10805 8964 18639 -681 -1118 1051 C ATOM 2619 CD1 LEU B 341 -5.875 10.986 42.418 1.00 99.68 C ANISOU 2619 CD1 LEU B 341 10522 8745 18608 -473 -949 1053 C ATOM 2620 CD2 LEU B 341 -5.712 13.423 41.865 1.00 98.80 C ANISOU 2620 CD2 LEU B 341 10323 8815 18400 -744 -1383 1130 C ATOM 2621 N GLU B 342 -2.666 11.839 37.759 1.00111.25 N ANISOU 2621 N GLU B 342 12479 10436 19355 -831 -618 1137 N ATOM 2622 CA GLU B 342 -1.369 11.558 37.159 1.00106.61 C ANISOU 2622 CA GLU B 342 11923 9950 18635 -777 -376 1204 C ATOM 2623 C GLU B 342 -0.797 12.776 36.446 1.00106.83 C ANISOU 2623 C GLU B 342 11947 10106 18539 -925 -521 1262 C ATOM 2624 O GLU B 342 0.422 12.977 36.455 1.00109.02 O ANISOU 2624 O GLU B 342 12127 10540 18754 -854 -387 1367 O ATOM 2625 CB GLU B 342 -1.479 10.380 36.190 1.00108.18 C ANISOU 2625 CB GLU B 342 12369 10000 18735 -784 -160 1110 C ATOM 2626 CG GLU B 342 -0.171 9.636 35.984 1.00118.97 C ANISOU 2626 CG GLU B 342 13732 11451 20018 -643 168 1178 C ATOM 2627 CD GLU B 342 0.357 9.025 37.269 1.00128.15 C ANISOU 2627 CD GLU B 342 14692 12687 21314 -407 347 1254 C ATOM 2628 OE1 GLU B 342 -0.463 8.611 38.116 1.00125.56 O ANISOU 2628 OE1 GLU B 342 14307 12269 21129 -335 303 1210 O ATOM 2629 OE2 GLU B 342 1.593 8.965 37.436 1.00138.54 O ANISOU 2629 OE2 GLU B 342 15901 14150 22589 -292 532 1358 O ATOM 2630 N ASN B 343 -1.653 13.596 35.830 1.00109.67 N ANISOU 2630 N ASN B 343 12408 10401 18860 -1131 -792 1197 N ATOM 2631 CA ASN B 343 -1.175 14.825 35.206 1.00106.54 C ANISOU 2631 CA ASN B 343 11998 10127 18355 -1277 -952 1253 C ATOM 2632 C ASN B 343 -0.757 15.855 36.247 1.00114.05 C ANISOU 2632 C ASN B 343 12680 11253 19399 -1226 -1098 1369 C ATOM 2633 O ASN B 343 0.165 16.641 36.003 1.00105.39 O ANISOU 2633 O ASN B 343 11509 10314 18221 -1258 -1115 1460 O ATOM 2634 CB ASN B 343 -2.250 15.405 34.288 1.00106.48 C ANISOU 2634 CB ASN B 343 12173 9997 18287 -1510 -1207 1149 C ATOM 2635 CG ASN B 343 -2.501 14.543 33.067 1.00108.02 C ANISOU 2635 CG ASN B 343 12644 10040 18357 -1584 -1068 1045 C ATOM 2636 OD1 ASN B 343 -1.589 13.899 32.549 1.00109.37 O ANISOU 2636 OD1 ASN B 343 12884 10244 18428 -1516 -813 1072 O ATOM 2637 ND2 ASN B 343 -3.745 14.526 32.600 1.00109.63 N ANISOU 2637 ND2 ASN B 343 13009 10078 18569 -1725 -1237 926 N ATOM 2638 N LEU B 344 -1.420 15.870 37.407 1.00117.75 N ANISOU 2638 N LEU B 344 13002 11699 20037 -1148 -1204 1367 N ATOM 2639 CA LEU B 344 -1.037 16.799 38.464 1.00102.37 C ANISOU 2639 CA LEU B 344 10792 9916 18187 -1088 -1335 1477 C ATOM 2640 C LEU B 344 0.323 16.449 39.054 1.00102.74 C ANISOU 2640 C LEU B 344 10676 10122 18240 -892 -1082 1598 C ATOM 2641 O LEU B 344 1.043 17.340 39.517 1.00102.15 O ANISOU 2641 O LEU B 344 10416 10220 18175 -871 -1154 1708 O ATOM 2642 CB LEU B 344 -2.103 16.820 39.559 1.00100.77 C ANISOU 2642 CB LEU B 344 10480 9641 18167 -1047 -1499 1440 C ATOM 2643 CG LEU B 344 -3.470 17.384 39.164 1.00100.08 C ANISOU 2643 CG LEU B 344 10510 9420 18095 -1241 -1795 1335 C ATOM 2644 CD1 LEU B 344 -4.456 17.266 40.315 1.00 98.56 C ANISOU 2644 CD1 LEU B 344 10202 9156 18089 -1175 -1921 1302 C ATOM 2645 CD2 LEU B 344 -3.342 18.830 38.708 1.00100.50 C ANISOU 2645 CD2 LEU B 344 10531 9580 18075 -1414 -2047 1378 C ATOM 2646 N LYS B 345 0.691 15.166 39.049 1.00 95.24 N ANISOU 2646 N LYS B 345 10761 10050 15376 -2149 -52 -21 N ATOM 2647 CA LYS B 345 2.009 14.772 39.535 1.00 87.16 C ANISOU 2647 CA LYS B 345 9698 9186 14235 -2015 -67 -383 C ATOM 2648 C LYS B 345 3.096 15.091 38.517 1.00 86.06 C ANISOU 2648 C LYS B 345 9570 9097 14033 -2069 12 -667 C ATOM 2649 O LYS B 345 4.216 15.454 38.896 1.00 86.26 O ANISOU 2649 O LYS B 345 9506 9267 14004 -2005 130 -994 O ATOM 2650 CB LYS B 345 2.024 13.282 39.879 1.00 86.00 C ANISOU 2650 CB LYS B 345 9650 9036 13989 -1887 -340 -352 C ATOM 2651 CG LYS B 345 1.129 12.900 41.046 1.00100.79 C ANISOU 2651 CG LYS B 345 11502 10887 15908 -1806 -420 -123 C ATOM 2652 CD LYS B 345 1.337 11.447 41.445 1.00112.27 C ANISOU 2652 CD LYS B 345 13042 12363 17252 -1666 -678 -147 C ATOM 2653 CE LYS B 345 0.462 11.065 42.627 1.00118.77 C ANISOU 2653 CE LYS B 345 13842 13168 18119 -1582 -758 76 C ATOM 2654 NZ LYS B 345 -0.987 11.168 42.304 1.00122.32 N ANISOU 2654 NZ LYS B 345 14348 13450 18678 -1690 -799 479 N ATOM 2655 N ASP B 346 2.787 14.958 37.224 1.00 92.02 N ANISOU 2655 N ASP B 346 10435 9735 14794 -2188 -52 -546 N ATOM 2656 CA ASP B 346 3.765 15.287 36.192 1.00 86.29 C ANISOU 2656 CA ASP B 346 9724 9047 14014 -2250 25 -799 C ATOM 2657 C ASP B 346 4.127 16.766 36.228 1.00 86.17 C ANISOU 2657 C ASP B 346 9573 9097 14072 -2326 318 -943 C ATOM 2658 O ASP B 346 5.295 17.132 36.057 1.00 88.22 O ANISOU 2658 O ASP B 346 9779 9471 14271 -2306 427 -1271 O ATOM 2659 CB ASP B 346 3.224 14.904 34.813 1.00 89.36 C ANISOU 2659 CB ASP B 346 10257 9287 14410 -2371 -96 -605 C ATOM 2660 CG ASP B 346 2.908 13.427 34.700 1.00104.67 C ANISOU 2660 CG ASP B 346 12337 11161 16273 -2299 -389 -472 C ATOM 2661 OD1 ASP B 346 3.566 12.620 35.390 1.00102.15 O ANISOU 2661 OD1 ASP B 346 12017 10938 15856 -2153 -502 -646 O ATOM 2662 OD2 ASP B 346 2.000 13.073 33.918 1.00121.26 O ANISOU 2662 OD2 ASP B 346 14549 13113 18412 -2390 -506 -192 O ATOM 2663 N VAL B 347 3.134 17.633 36.453 1.00 93.01 N ANISOU 2663 N VAL B 347 10380 9891 15068 -2413 449 -701 N ATOM 2664 CA VAL B 347 3.382 19.072 36.525 1.00 85.68 C ANISOU 2664 CA VAL B 347 9319 9017 14218 -2489 731 -814 C ATOM 2665 C VAL B 347 3.862 19.517 37.895 1.00 89.36 C ANISOU 2665 C VAL B 347 9640 9628 14686 -2376 862 -993 C ATOM 2666 O VAL B 347 4.113 20.713 38.093 1.00 87.69 O ANISOU 2666 O VAL B 347 9308 9475 14537 -2425 1101 -1102 O ATOM 2667 CB VAL B 347 2.114 19.863 36.141 1.00 85.29 C ANISOU 2667 CB VAL B 347 9269 8827 14311 -2638 825 -479 C ATOM 2668 CG1 VAL B 347 1.661 19.490 34.737 1.00 85.29 C ANISOU 2668 CG1 VAL B 347 9410 8685 14312 -2758 708 -308 C ATOM 2669 CG2 VAL B 347 1.007 19.611 37.147 1.00 85.03 C ANISOU 2669 CG2 VAL B 347 9219 8741 14346 -2590 758 -192 C ATOM 2670 N GLY B 348 3.999 18.596 38.846 1.00 85.79 N ANISOU 2670 N GLY B 348 9195 9235 14168 -2227 714 -1027 N ATOM 2671 CA GLY B 348 4.518 18.937 40.155 1.00 85.82 C ANISOU 2671 CA GLY B 348 9064 9381 14163 -2110 825 -1212 C ATOM 2672 C GLY B 348 3.564 19.683 41.057 1.00 85.46 C ANISOU 2672 C GLY B 348 8923 9309 14240 -2129 949 -994 C ATOM 2673 O GLY B 348 4.013 20.360 41.986 1.00 85.44 O ANISOU 2673 O GLY B 348 8787 9423 14254 -2072 1113 -1160 O ATOM 2674 N LEU B 349 2.257 19.580 40.818 1.00 92.15 N ANISOU 2674 N LEU B 349 9834 10005 15173 -2208 877 -626 N ATOM 2675 CA LEU B 349 1.263 20.264 41.633 1.00 93.25 C ANISOU 2675 CA LEU B 349 9890 10108 15434 -2233 987 -393 C ATOM 2676 C LEU B 349 0.684 19.390 42.738 1.00 84.77 C ANISOU 2676 C LEU B 349 8829 9030 14349 -2109 824 -236 C ATOM 2677 O LEU B 349 0.029 19.919 43.642 1.00 84.51 O ANISOU 2677 O LEU B 349 8710 8998 14403 -2098 920 -94 O ATOM 2678 CB LEU B 349 0.123 20.789 40.751 1.00 87.62 C ANISOU 2678 CB LEU B 349 9227 9230 14834 -2400 1025 -74 C ATOM 2679 CG LEU B 349 0.457 21.997 39.874 1.00 84.48 C ANISOU 2679 CG LEU B 349 8779 8830 14488 -2538 1246 -179 C ATOM 2680 CD1 LEU B 349 -0.724 22.360 38.987 1.00 91.65 C ANISOU 2680 CD1 LEU B 349 9754 9568 15503 -2698 1252 157 C ATOM 2681 CD2 LEU B 349 0.866 23.180 40.736 1.00 84.39 C ANISOU 2681 CD2 LEU B 349 8598 8935 14530 -2521 1503 -348 C ATOM 2682 N PHE B 350 0.905 18.081 42.691 1.00 93.15 N ANISOU 2682 N PHE B 350 9996 10090 15307 -2016 584 -256 N ATOM 2683 CA PHE B 350 0.390 17.183 43.718 1.00109.69 C ANISOU 2683 CA PHE B 350 12109 12182 17384 -1894 418 -114 C ATOM 2684 C PHE B 350 1.235 15.917 43.812 1.00118.37 C ANISOU 2684 C PHE B 350 13283 13353 18339 -1761 212 -311 C ATOM 2685 O PHE B 350 1.312 15.280 44.863 1.00105.33 O ANISOU 2685 O PHE B 350 11609 11766 16644 -1625 117 -339 O ATOM 2686 CB PHE B 350 -1.071 16.827 43.433 1.00103.79 C ANISOU 2686 CB PHE B 350 11455 11263 16719 -1968 291 306 C ATOM 2687 CG PHE B 350 -1.661 15.854 44.413 1.00103.08 C ANISOU 2687 CG PHE B 350 11396 11160 16612 -1849 106 473 C ATOM 2688 CD1 PHE B 350 -1.930 16.241 45.716 1.00 99.54 C ANISOU 2688 CD1 PHE B 350 10834 10774 16214 -1776 198 503 C ATOM 2689 CD2 PHE B 350 -1.952 14.555 44.031 1.00 97.66 C ANISOU 2689 CD2 PHE B 350 10852 10397 15858 -1811 -158 601 C ATOM 2690 CE1 PHE B 350 -2.474 15.348 46.621 1.00 86.99 C ANISOU 2690 CE1 PHE B 350 9272 9171 14608 -1667 29 657 C ATOM 2691 CE2 PHE B 350 -2.496 13.658 44.931 1.00 88.50 C ANISOU 2691 CE2 PHE B 350 9721 9224 14682 -1702 -328 755 C ATOM 2692 CZ PHE B 350 -2.758 14.056 46.227 1.00 84.54 C ANISOU 2692 CZ PHE B 350 9105 8786 14231 -1630 -235 783 C ATOM 2693 OXT PHE B 350 1.867 15.504 42.840 1.00131.03 O ANISOU 2693 OXT PHE B 350 14969 14951 19865 -1786 136 -448 O TER 2694 PHE B 350 HETATM 2695 C1 NAG C 1 26.392 70.207 40.268 1.00 62.20 C HETATM 2696 C2 NAG C 1 27.069 69.593 39.061 1.00 36.24 C HETATM 2697 C3 NAG C 1 28.571 69.730 39.230 1.00 65.15 C HETATM 2698 C4 NAG C 1 28.963 71.182 39.463 1.00 61.24 C HETATM 2699 C5 NAG C 1 28.169 71.707 40.663 1.00 74.43 C HETATM 2700 C6 NAG C 1 28.482 73.181 40.935 1.00 78.67 C HETATM 2701 C7 NAG C 1 26.388 67.516 37.892 1.00 61.71 C HETATM 2702 C8 NAG C 1 26.074 66.029 38.079 1.00 63.62 C HETATM 2703 N2 NAG C 1 26.726 68.163 39.016 1.00 53.05 N HETATM 2704 O3 NAG C 1 29.239 69.227 38.060 1.00 82.74 O HETATM 2705 O4 NAG C 1 30.370 71.213 39.759 1.00 77.35 O HETATM 2706 O5 NAG C 1 26.761 71.589 40.405 1.00 70.61 O HETATM 2707 O6 NAG C 1 28.221 73.947 39.756 1.00 79.03 O HETATM 2708 O7 NAG C 1 26.318 68.042 36.782 1.00 36.87 O HETATM 2709 C1 NAG C 2 31.165 72.179 39.041 1.00 45.11 C HETATM 2710 C2 NAG C 2 32.438 72.411 39.843 1.00 51.22 C HETATM 2711 C3 NAG C 2 33.300 73.432 39.134 1.00 44.30 C HETATM 2712 C4 NAG C 2 33.616 72.919 37.742 1.00 63.08 C HETATM 2713 C5 NAG C 2 32.314 72.670 37.000 1.00 29.53 C HETATM 2714 C6 NAG C 2 32.658 72.153 35.600 1.00 51.69 C HETATM 2715 C7 NAG C 2 31.957 72.068 42.231 1.00 77.43 C HETATM 2716 C8 NAG C 2 31.593 72.745 43.554 1.00 53.43 C HETATM 2717 N2 NAG C 2 32.094 72.900 41.188 1.00 37.84 N HETATM 2718 O3 NAG C 2 34.516 73.625 39.873 1.00 66.80 O HETATM 2719 O4 NAG C 2 34.351 73.909 37.015 1.00 53.51 O HETATM 2720 O5 NAG C 2 31.503 71.709 37.717 1.00 63.78 O HETATM 2721 O6 NAG C 2 31.490 72.135 34.781 1.00 56.12 O HETATM 2722 O7 NAG C 2 32.112 70.849 42.164 1.00104.57 O HETATM 2723 C1 BMA C 3 35.755 73.657 36.858 1.00 91.91 C HETATM 2724 C2 BMA C 3 36.236 74.574 35.748 1.00108.84 C HETATM 2725 C3 BMA C 3 37.733 74.464 35.580 1.00128.82 C HETATM 2726 C4 BMA C 3 38.385 74.796 36.910 1.00144.23 C HETATM 2727 C5 BMA C 3 37.865 73.843 37.977 1.00144.10 C HETATM 2728 C6 BMA C 3 38.486 74.200 39.328 1.00147.94 C HETATM 2729 O2 BMA C 3 35.910 75.923 36.099 1.00103.98 O HETATM 2730 O3 BMA C 3 38.143 75.432 34.601 1.00118.47 O HETATM 2731 O4 BMA C 3 39.812 74.678 36.797 1.00155.08 O HETATM 2732 O5 BMA C 3 36.433 73.975 38.088 1.00123.81 O HETATM 2733 O6 BMA C 3 37.831 75.357 39.858 1.00142.81 O HETATM 2734 C1 BMA C 4 38.870 74.879 33.497 1.00140.84 C HETATM 2735 C2 BMA C 4 38.025 74.982 32.234 1.00134.79 C HETATM 2736 C3 BMA C 4 38.839 74.495 31.050 1.00142.94 C HETATM 2737 C4 BMA C 4 40.094 75.341 30.944 1.00157.91 C HETATM 2738 C5 BMA C 4 40.880 75.213 32.241 1.00163.30 C HETATM 2739 C6 BMA C 4 42.140 76.078 32.166 1.00158.22 C HETATM 2740 O2 BMA C 4 37.659 76.352 32.020 1.00130.29 O HETATM 2741 O3 BMA C 4 38.069 74.621 29.845 1.00134.22 O HETATM 2742 O4 BMA C 4 40.895 74.891 29.842 1.00162.38 O HETATM 2743 O5 BMA C 4 40.069 75.662 33.344 1.00163.89 O HETATM 2744 O6 BMA C 4 43.001 75.584 31.138 1.00155.68 O HETATM 2745 C1 BOG A 401 37.419 53.336 47.950 1.00126.42 C HETATM 2746 O1 BOG A 401 37.306 52.009 48.379 1.00113.33 O HETATM 2747 C2 BOG A 401 36.485 54.206 48.794 1.00134.72 C HETATM 2748 O2 BOG A 401 35.556 54.819 47.940 1.00135.32 O HETATM 2749 C3 BOG A 401 37.157 55.256 49.578 1.00129.27 C HETATM 2750 O3 BOG A 401 37.689 54.668 50.734 1.00121.44 O HETATM 2751 C4 BOG A 401 38.235 55.985 48.892 1.00123.59 C HETATM 2752 O4 BOG A 401 37.686 57.117 48.273 1.00106.22 O HETATM 2753 C5 BOG A 401 38.973 55.162 47.839 1.00126.64 C HETATM 2754 O5 BOG A 401 38.816 53.733 48.079 1.00128.21 O HETATM 2755 C6 BOG A 401 40.460 55.507 47.877 1.00123.40 C HETATM 2756 O6 BOG A 401 40.988 55.054 49.093 1.00119.40 O HETATM 2757 C1' BOG A 401 36.152 51.355 47.936 1.00101.29 C HETATM 2758 C2' BOG A 401 36.058 50.010 48.652 1.00103.91 C HETATM 2759 C3' BOG A 401 35.781 48.857 47.690 1.00100.73 C HETATM 2760 C4' BOG A 401 35.262 47.614 48.408 1.00 94.41 C HETATM 2761 C5' BOG A 401 35.406 46.343 47.574 1.00 84.64 C HETATM 2762 C6' BOG A 401 34.395 45.278 47.990 1.00 83.95 C HETATM 2763 C7' BOG A 401 34.888 43.851 47.762 1.00 86.10 C HETATM 2764 C8' BOG A 401 33.915 42.816 48.322 1.00 77.08 C HETATM 2765 C1 PLM A 402 25.702 14.433 55.856 1.00117.70 C HETATM 2766 O2 PLM A 402 25.584 13.893 56.904 1.00142.70 O HETATM 2767 C2 PLM A 402 25.300 15.903 55.766 1.00116.64 C HETATM 2768 C3 PLM A 402 25.283 16.572 57.139 1.00111.18 C HETATM 2769 C4 PLM A 402 24.164 17.602 57.270 1.00106.17 C HETATM 2770 C5 PLM A 402 24.364 18.519 58.474 1.00 94.85 C HETATM 2771 C6 PLM A 402 23.472 19.755 58.406 1.00 90.43 C HETATM 2772 C7 PLM A 402 24.185 21.004 58.915 1.00 79.25 C HETATM 2773 C8 PLM A 402 23.373 22.273 58.673 1.00 85.71 C HETATM 2774 C9 PLM A 402 24.274 23.488 58.470 1.00 86.28 C HETATM 2775 CA PLM A 402 23.488 24.779 58.256 1.00 93.24 C HETATM 2776 CB PLM A 402 24.375 25.880 57.684 1.00 98.96 C HETATM 2777 CC PLM A 402 23.937 27.276 58.119 1.00 94.89 C HETATM 2778 CD PLM A 402 24.940 28.340 57.682 1.00 91.28 C HETATM 2779 CE PLM A 402 24.518 29.744 58.106 1.00 92.37 C HETATM 2780 CF PLM A 402 25.315 30.826 57.382 1.00 91.48 C HETATM 2781 CG PLM A 402 24.897 32.230 57.810 1.00 96.40 C HETATM 2782 C1 64Z A 403 8.515 49.434 33.695 1.00119.89 C HETATM 2783 C2 64Z A 403 7.266 49.138 34.519 1.00108.80 C HETATM 2784 C3 64Z A 403 6.150 48.433 33.749 1.00105.48 C HETATM 2785 C4 64Z A 403 5.412 47.486 34.693 1.00103.73 C HETATM 2786 C5 64Z A 403 6.195 46.182 34.866 1.00 89.40 C HETATM 2787 C6 64Z A 403 6.771 45.467 33.645 1.00 70.62 C HETATM 2788 C7 64Z A 403 7.519 44.168 33.953 1.00 72.65 C HETATM 2789 C8 64Z A 403 6.383 45.578 36.261 1.00 80.08 C HETATM 2790 C9 64Z A 403 8.575 49.034 32.232 1.00121.79 C HETATM 2791 O 64Z A 403 8.178 43.706 32.773 1.00 76.46 O HETATM 2792 C 64Z A 403 9.711 50.124 34.330 1.00125.17 C CONECT 117 2695 CONECT 883 1484 CONECT 1484 883 CONECT 2582 2765 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 2582 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 2790 2792 CONECT 2783 2782 2784 CONECT 2784 2783 2785 CONECT 2785 2784 2786 CONECT 2786 2785 2787 2789 CONECT 2787 2786 2788 CONECT 2788 2787 2791 CONECT 2789 2786 CONECT 2790 2782 CONECT 2791 2788 CONECT 2792 2782 MASTER 438 0 7 17 4 0 0 6 2779 2 102 28 END