HEADER HYDROLASE 16-OCT-08 3EXD TITLE SULFUR-SAD PHASED HEWL CRYSTAL COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOZYME C; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV; COMPND 5 EC: 3.2.1.17 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS; SOURCE 4 ORGANISM_TAXID: 9031 KEYWDS HEWL, SULFUR, SAD PHASING, ALLERGEN, ANTIMICROBIAL, KEYWDS 2 BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR A.S.NASCIMENTO,M.V.LIBERATO,I.POLIKARPOV REVDAT 3 14-APR-09 3EXD 1 JRNL REVDAT 2 24-FEB-09 3EXD 1 VERSN REVDAT 1 28-OCT-08 3EXD 0 JRNL AUTH B.G.GUIMARAES,L.SANFELICI,R.T.NEUENSCHWANDER, JRNL AUTH 2 F.RODRIGUES,W.C.GRIZOLLI,M.A.RAULIK,J.R.PITON, JRNL AUTH 3 B.C.MEYER,A.S.NASCIMENTO,I.POLIKARPOV JRNL TITL THE MX2 MACROMOLECULAR CRYSTALLOGRAPHY BEAMLINE: A JRNL TITL 2 WIGGLER X-RAY SOURCE AT THE LNLS. JRNL REF J.SYNCHROTRON RADIAT. V. 16 69 2009 JRNL REFN ISSN 0909-0495 JRNL PMID 19096177 JRNL DOI 10.1107/S0909049508034870 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.190 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 19252 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.165 REMARK 3 R VALUE (WORKING SET) : 0.163 REMARK 3 FREE R VALUE : 0.184 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1926 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 7.9890 - 3.4957 1.00 1345 150 0.1646 0.1739 REMARK 3 2 3.4957 - 2.8144 1.00 1276 142 0.1568 0.1641 REMARK 3 3 2.8144 - 2.4707 1.00 1252 139 0.1689 0.1826 REMARK 3 4 2.4707 - 2.2503 1.00 1258 140 0.1566 0.1822 REMARK 3 5 2.2503 - 2.0921 1.00 1242 138 0.1553 0.1835 REMARK 3 6 2.0921 - 1.9707 1.00 1241 137 0.1534 0.1973 REMARK 3 7 1.9707 - 1.8734 1.00 1235 138 0.1498 0.1764 REMARK 3 8 1.8734 - 1.7928 1.00 1223 136 0.1525 0.1934 REMARK 3 9 1.7928 - 1.7245 1.00 1224 136 0.1530 0.1920 REMARK 3 10 1.7245 - 1.6655 0.99 1208 135 0.1525 0.1987 REMARK 3 11 1.6655 - 1.6139 0.99 1205 134 0.1455 0.1628 REMARK 3 12 1.6139 - 1.5681 0.99 1220 135 0.1534 0.1911 REMARK 3 13 1.5681 - 1.5271 0.99 1194 133 0.1615 0.1725 REMARK 3 14 1.5271 - 1.4900 0.98 1203 133 0.1609 0.2023 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 : 0.53 REMARK 3 B_SOL : 99.11 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.20 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 : 0.006 NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : 16.308 NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 1:13) REMARK 3 ORIGIN FOR THE GROUP (A): 45.3675 22.3753 8.6845 REMARK 3 T TENSOR REMARK 3 T11: 0.1330 T22: 0.1954 REMARK 3 T33: 0.1824 T12: -0.0075 REMARK 3 T13: 0.0302 T23: 0.0133 REMARK 3 L TENSOR REMARK 3 L11: 0.2536 L22: 0.3002 REMARK 3 L33: 0.6670 L12: 0.3988 REMARK 3 L13: -0.2940 L23: -0.2643 REMARK 3 S TENSOR REMARK 3 S11: 0.0063 S12: 0.1562 S13: 0.0032 REMARK 3 S21: -0.0578 S22: -0.0450 S23: -0.2666 REMARK 3 S31: -0.0455 S32: 0.0979 S33: 0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 14:21) REMARK 3 ORIGIN FOR THE GROUP (A): 51.6242 19.2364 19.8682 REMARK 3 T TENSOR REMARK 3 T11: 0.1286 T22: 0.2091 REMARK 3 T33: 0.2068 T12: -0.0095 REMARK 3 T13: -0.0173 T23: 0.0237 REMARK 3 L TENSOR REMARK 3 L11: 0.5738 L22: 0.4370 REMARK 3 L33: 0.4039 L12: -0.1014 REMARK 3 L13: -0.1098 L23: 0.5222 REMARK 3 S TENSOR REMARK 3 S11: -0.1812 S12: 0.3213 S13: 0.1430 REMARK 3 S21: 0.2607 S22: 0.2129 S23: -0.6516 REMARK 3 S31: -0.4128 S32: 0.3969 S33: 0.0018 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 22:40) REMARK 3 ORIGIN FOR THE GROUP (A): 41.2366 15.6269 13.6212 REMARK 3 T TENSOR REMARK 3 T11: 0.0948 T22: 0.1088 REMARK 3 T33: 0.1267 T12: 0.0063 REMARK 3 T13: 0.0142 T23: -0.0051 REMARK 3 L TENSOR REMARK 3 L11: 0.5846 L22: 0.6247 REMARK 3 L33: 0.6294 L12: 0.2004 REMARK 3 L13: -0.3861 L23: 0.1767 REMARK 3 S TENSOR REMARK 3 S11: 0.0532 S12: 0.0279 S13: -0.0284 REMARK 3 S21: -0.0194 S22: -0.0463 S23: -0.0413 REMARK 3 S31: 0.0266 S32: 0.0621 S33: -0.0002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 41:58) REMARK 3 ORIGIN FOR THE GROUP (A): 29.5860 21.2967 20.7247 REMARK 3 T TENSOR REMARK 3 T11: 0.1272 T22: 0.1246 REMARK 3 T33: 0.1183 T12: 0.0037 REMARK 3 T13: 0.0319 T23: 0.0223 REMARK 3 L TENSOR REMARK 3 L11: 0.5753 L22: 1.1435 REMARK 3 L33: 0.7359 L12: -0.2909 REMARK 3 L13: 0.3162 L23: 0.6731 REMARK 3 S TENSOR REMARK 3 S11: -0.0037 S12: -0.0243 S13: 0.0128 REMARK 3 S21: 0.2039 S22: 0.0515 S23: 0.0980 REMARK 3 S31: 0.2855 S32: -0.0206 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 59:68) REMARK 3 ORIGIN FOR THE GROUP (A): 31.3830 23.4237 29.4998 REMARK 3 T TENSOR REMARK 3 T11: 0.2151 T22: 0.2052 REMARK 3 T33: 0.1684 T12: 0.0389 REMARK 3 T13: 0.0248 T23: 0.0174 REMARK 3 L TENSOR REMARK 3 L11: 0.4158 L22: 0.4602 REMARK 3 L33: 0.3588 L12: -0.0938 REMARK 3 L13: -0.0195 L23: 0.3060 REMARK 3 S TENSOR REMARK 3 S11: -0.3096 S12: -0.5729 S13: -0.0341 REMARK 3 S21: 0.3995 S22: 0.2848 S23: 0.2840 REMARK 3 S31: 0.3196 S32: -0.0911 S33: 0.0013 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 69:96) REMARK 3 ORIGIN FOR THE GROUP (A): 38.4804 26.5628 25.2082 REMARK 3 T TENSOR REMARK 3 T11: 0.1384 T22: 0.1376 REMARK 3 T33: 0.1578 T12: 0.0071 REMARK 3 T13: -0.0062 T23: -0.0011 REMARK 3 L TENSOR REMARK 3 L11: 1.5680 L22: 1.4607 REMARK 3 L33: 0.5817 L12: -0.7346 REMARK 3 L13: 0.8019 L23: 0.6106 REMARK 3 S TENSOR REMARK 3 S11: -0.1105 S12: -0.2092 S13: 0.1970 REMARK 3 S21: 0.1578 S22: 0.1008 S23: -0.1616 REMARK 3 S31: -0.0730 S32: -0.0195 S33: 0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 97:108) REMARK 3 ORIGIN FOR THE GROUP (A): 42.0888 13.3561 26.5502 REMARK 3 T TENSOR REMARK 3 T11: 0.1659 T22: 0.1530 REMARK 3 T33: 0.1665 T12: 0.0130 REMARK 3 T13: 0.0002 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 0.6570 L22: 0.3325 REMARK 3 L33: 0.2960 L12: -0.2768 REMARK 3 L13: -0.0318 L23: -0.0317 REMARK 3 S TENSOR REMARK 3 S11: -0.0638 S12: -0.2758 S13: 0.1060 REMARK 3 S21: 0.2849 S22: 0.0510 S23: -0.0244 REMARK 3 S31: -0.0222 S32: -0.0740 S33: -0.0002 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 109:119) REMARK 3 ORIGIN FOR THE GROUP (A): 39.1203 6.2798 16.2047 REMARK 3 T TENSOR REMARK 3 T11: 0.1166 T22: 0.1454 REMARK 3 T33: 0.1423 T12: -0.0101 REMARK 3 T13: 0.0006 T23: -0.0148 REMARK 3 L TENSOR REMARK 3 L11: 0.5822 L22: 0.9200 REMARK 3 L33: 0.4242 L12: 0.2479 REMARK 3 L13: 1.2306 L23: -0.0648 REMARK 3 S TENSOR REMARK 3 S11: 0.0391 S12: -0.1403 S13: 0.1109 REMARK 3 S21: -0.1582 S22: -0.0632 S23: -0.0150 REMARK 3 S31: 0.2710 S32: -0.0804 S33: 0.0001 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND RESID 120:124) REMARK 3 ORIGIN FOR THE GROUP (A): 46.9589 10.1871 7.9697 REMARK 3 T TENSOR REMARK 3 T11: 0.1390 T22: 0.1739 REMARK 3 T33: 0.1736 T12: 0.0334 REMARK 3 T13: 0.0163 T23: -0.0348 REMARK 3 L TENSOR REMARK 3 L11: 0.0267 L22: 0.0920 REMARK 3 L33: 0.1317 L12: 0.2074 REMARK 3 L13: -0.0533 L23: -0.0540 REMARK 3 S TENSOR REMARK 3 S11: -0.0553 S12: 0.3915 S13: -0.1357 REMARK 3 S21: -0.0458 S22: -0.0234 S23: -0.5491 REMARK 3 S31: 0.6537 S32: 0.4658 S33: -0.0001 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN A AND RESID 125:129) REMARK 3 ORIGIN FOR THE GROUP (A): 52.8793 16.3339 3.1387 REMARK 3 T TENSOR REMARK 3 T11: 0.1955 T22: 0.4152 REMARK 3 T33: 0.3444 T12: -0.0306 REMARK 3 T13: 0.1073 T23: -0.0809 REMARK 3 L TENSOR REMARK 3 L11: 0.1236 L22: 0.1215 REMARK 3 L33: -0.0813 L12: -0.2219 REMARK 3 L13: -0.0933 L23: -0.3061 REMARK 3 S TENSOR REMARK 3 S11: -0.0816 S12: 0.7942 S13: -0.4653 REMARK 3 S21: -0.1339 S22: 0.1691 S23: -1.1432 REMARK 3 S31: 0.3798 S32: 0.3783 S33: 0.0070 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 3EXD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-08. REMARK 100 THE RCSB ID CODE IS RCSB049885. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-AUG-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LNLS REMARK 200 BEAMLINE : W01B-MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.46 REMARK 200 MONOCHROMATOR : SI REMARK 200 OPTICS : SI MONOCHROMATOR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25761 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350 REMARK 200 RESOLUTION RANGE LOW (A) : 30.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 24.500 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : 0.07800 REMARK 200 FOR THE DATA SET : 31.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3 REMARK 200 DATA REDUNDANCY IN SHELL : 10.50 REMARK 200 R MERGE FOR SHELL (I) : 0.71900 REMARK 200 R SYM FOR SHELL (I) : 0.71900 REMARK 200 FOR SHELL : 2.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELXS REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, PH 5.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.46000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.34100 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.34100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.69000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.34100 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.34100 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.23000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.34100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.34100 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.69000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.34100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.34100 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.23000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.46000 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 152 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 230 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 251 LIES ON A SPECIAL POSITION. DBREF 3EXD A 1 129 UNP P00698 LYSC_CHICK 19 147 SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU FORMUL 2 HOH *233(H2 O) HELIX 1 1 GLY A 4 HIS A 15 1 12 HELIX 2 2 ASN A 19 TYR A 23 5 5 HELIX 3 3 SER A 24 ASN A 37 1 14 HELIX 4 4 PRO A 79 SER A 85 5 7 HELIX 5 5 ILE A 88 SER A 100 1 13 HELIX 6 6 ASN A 103 ALA A 107 5 5 HELIX 7 7 TRP A 108 CYS A 115 1 8 HELIX 8 8 ASP A 119 ARG A 125 5 7 SHEET 1 A 3 THR A 43 ARG A 45 0 SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44 SHEET 3 A 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53 SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.11 SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04 SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.04 SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03 CRYST1 78.682 78.682 36.920 90.00 90.00 90.00 P 43 21 2 8 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 0.012709 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012709 0.000000 0.00000 SCALE3 0.000000 0.000000 0.027086 0.00000 ATOM 1 N LYS A 1 36.342 29.290 9.890 1.00 14.29 N ANISOU 1 N LYS A 1 1833 2033 1561 -6 229 291 N ATOM 2 CA LYS A 1 37.270 28.908 8.833 1.00 13.73 C ANISOU 2 CA LYS A 1 1718 2000 1498 -16 260 291 C ATOM 3 C LYS A 1 37.197 27.410 8.618 1.00 12.52 C ANISOU 3 C LYS A 1 1539 1892 1327 -12 249 242 C ATOM 4 O LYS A 1 37.230 26.646 9.584 1.00 13.37 O ANISOU 4 O LYS A 1 1650 1975 1457 -19 210 202 O ATOM 5 CB LYS A 1 38.694 29.304 9.216 1.00 15.40 C ANISOU 5 CB LYS A 1 1911 2160 1779 -52 259 294 C ATOM 6 CG LYS A 1 39.761 28.842 8.244 1.00 15.00 C ANISOU 6 CG LYS A 1 1810 2144 1747 -63 291 290 C ATOM 7 CD LYS A 1 41.120 29.399 8.641 1.00 17.66 C ANISOU 7 CD LYS A 1 2128 2434 2149 -100 289 304 C ATOM 8 CE LYS A 1 42.229 28.747 7.830 1.00 20.15 C ANISOU 8 CE LYS A 1 2385 2781 2490 -109 318 295 C ATOM 9 NZ LYS A 1 42.197 29.137 6.395 1.00 28.05 N ANISOU 9 NZ LYS A 1 3376 3828 3453 -100 371 320 N ATOM 10 N VAL A 2 37.079 26.997 7.361 1.00 13.98 N ANISOU 10 N VAL A 2 1703 2141 1468 -4 287 246 N ATOM 11 CA VAL A 2 37.199 25.591 7.007 1.00 13.64 C ANISOU 11 CA VAL A 2 1637 2137 1408 -6 291 200 C ATOM 12 C VAL A 2 38.608 25.346 6.488 1.00 13.30 C ANISOU 12 C VAL A 2 1552 2085 1415 -24 322 194 C ATOM 13 O VAL A 2 38.996 25.858 5.424 1.00 14.69 O ANISOU 13 O VAL A 2 1713 2289 1582 -29 366 223 O ATOM 14 CB VAL A 2 36.159 25.154 5.954 1.00 13.83 C ANISOU 14 CB VAL A 2 1668 2241 1345 4 316 203 C ATOM 15 CG1 VAL A 2 36.345 23.689 5.613 1.00 15.60 C ANISOU 15 CG1 VAL A 2 1879 2497 1551 -5 328 151 C ATOM 16 CG2 VAL A 2 34.738 25.383 6.485 1.00 12.53 C ANISOU 16 CG2 VAL A 2 1539 2091 1131 24 285 214 C ATOM 17 N PHE A 3 39.391 24.598 7.268 1.00 13.62 N ANISOU 17 N PHE A 3 1573 2089 1512 -32 299 160 N ATOM 18 CA PHE A 3 40.774 24.283 6.899 1.00 13.55 C ANISOU 18 CA PHE A 3 1518 2072 1560 -45 327 156 C ATOM 19 C PHE A 3 40.828 23.201 5.852 1.00 15.37 C ANISOU 19 C PHE A 3 1731 2351 1757 -38 373 128 C ATOM 20 O PHE A 3 39.976 22.304 5.810 1.00 14.37 O ANISOU 20 O PHE A 3 1627 2253 1581 -29 368 95 O ATOM 21 CB PHE A 3 41.564 23.755 8.114 1.00 13.85 C ANISOU 21 CB PHE A 3 1536 2059 1669 -54 286 135 C ATOM 22 CG PHE A 3 42.138 24.828 9.001 1.00 14.00 C ANISOU 22 CG PHE A 3 1555 2025 1738 -78 255 166 C ATOM 23 CD1 PHE A 3 43.483 25.174 8.914 1.00 15.40 C ANISOU 23 CD1 PHE A 3 1689 2186 1976 -100 269 188 C ATOM 24 CD2 PHE A 3 41.339 25.479 9.939 1.00 13.31 C ANISOU 24 CD2 PHE A 3 1513 1906 1638 -83 214 173 C ATOM 25 CE1 PHE A 3 44.020 26.154 9.741 1.00 13.12 C ANISOU 25 CE1 PHE A 3 1405 1852 1728 -132 241 217 C ATOM 26 CE2 PHE A 3 41.869 26.463 10.760 1.00 14.26 C ANISOU 26 CE2 PHE A 3 1643 1975 1800 -114 191 199 C ATOM 27 CZ PHE A 3 43.218 26.798 10.661 1.00 14.48 C ANISOU 27 CZ PHE A 3 1629 1990 1883 -141 203 221 C ATOM 28 N GLY A 4 41.865 23.267 5.027 1.00 16.77 N ANISOU 28 N GLY A 4 1871 2537 1963 -47 420 139 N ATOM 29 CA GLY A 4 42.239 22.127 4.218 1.00 16.26 C ANISOU 29 CA GLY A 4 1786 2501 1890 -44 468 106 C ATOM 30 C GLY A 4 42.950 21.106 5.083 1.00 16.11 C ANISOU 30 C GLY A 4 1743 2443 1935 -35 449 74 C ATOM 31 O GLY A 4 43.444 21.418 6.166 1.00 15.97 O ANISOU 31 O GLY A 4 1710 2381 1977 -39 404 85 O ATOM 32 N ARG A 5 42.997 19.871 4.617 1.00 15.99 N ANISOU 32 N ARG A 5 1725 2445 1905 -26 486 35 N ATOM 33 CA ARG A 5 43.606 18.800 5.385 1.00 13.83 C ANISOU 33 CA ARG A 5 1430 2135 1689 -12 474 6 C ATOM 34 C ARG A 5 45.068 19.091 5.762 1.00 16.11 C ANISOU 34 C ARG A 5 1658 2388 2075 -12 474 33 C ATOM 35 O ARG A 5 45.449 19.067 6.942 1.00 16.33 O ANISOU 35 O ARG A 5 1669 2377 2160 -12 420 40 O ATOM 36 CB ARG A 5 43.514 17.514 4.571 1.00 16.29 C ANISOU 36 CB ARG A 5 1753 2471 1967 -4 534 -36 C ATOM 37 CG ARG A 5 44.149 16.315 5.219 1.00 18.47 C ANISOU 37 CG ARG A 5 2009 2707 2302 17 534 -65 C ATOM 38 CD ARG A 5 43.908 15.063 4.370 1.00 18.81 C ANISOU 38 CD ARG A 5 2078 2771 2299 22 602 -110 C ATOM 39 NE ARG A 5 44.495 15.165 3.035 1.00 21.52 N ANISOU 39 NE ARG A 5 2403 3141 2634 13 684 -104 N ATOM 40 CZ ARG A 5 45.762 14.879 2.744 1.00 21.01 C ANISOU 40 CZ ARG A 5 2287 3054 2642 28 734 -97 C ATOM 41 NH1 ARG A 5 46.601 14.479 3.693 1.00 20.39 N ANISOU 41 NH1 ARG A 5 2167 2929 2652 54 709 -90 N ATOM 42 NH2 ARG A 5 46.206 14.997 1.499 1.00 23.55 N ANISOU 42 NH2 ARG A 5 2597 3402 2948 16 811 -94 N ATOM 43 N CYS A 6 45.897 19.350 4.757 1.00 15.79 N ANISOU 43 N CYS A 6 1582 2365 2051 -17 534 50 N ATOM 44 CA CYS A 6 47.308 19.643 5.023 1.00 15.90 C ANISOU 44 CA CYS A 6 1533 2355 2154 -20 537 80 C ATOM 45 C CYS A 6 47.503 20.989 5.707 1.00 15.34 C ANISOU 45 C CYS A 6 1458 2266 2105 -45 485 123 C ATOM 46 O CYS A 6 48.425 21.160 6.502 1.00 15.62 O ANISOU 46 O CYS A 6 1451 2273 2211 -54 455 146 O ATOM 47 CB CYS A 6 48.125 19.596 3.736 1.00 19.16 C ANISOU 47 CB CYS A 6 1912 2794 2575 -21 619 86 C ATOM 48 SG CYS A 6 48.272 17.943 3.025 1.00 19.36 S ANISOU 48 SG CYS A 6 1935 2826 2595 6 694 37 S ATOM 49 N GLU A 7 46.633 21.941 5.393 1.00 14.91 N ANISOU 49 N GLU A 7 1448 2227 1990 -58 477 137 N ATOM 50 CA GLU A 7 46.671 23.235 6.058 1.00 15.47 C ANISOU 50 CA GLU A 7 1529 2273 2074 -83 433 175 C ATOM 51 C GLU A 7 46.496 23.072 7.570 1.00 14.26 C ANISOU 51 C GLU A 7 1387 2078 1952 -88 362 168 C ATOM 52 O GLU A 7 47.239 23.675 8.367 1.00 15.28 O ANISOU 52 O GLU A 7 1495 2177 2133 -114 328 196 O ATOM 53 CB GLU A 7 45.590 24.154 5.501 1.00 17.28 C ANISOU 53 CB GLU A 7 1812 2525 2231 -86 439 190 C ATOM 54 CG GLU A 7 45.697 25.570 6.008 1.00 17.38 C ANISOU 54 CG GLU A 7 1840 2508 2256 -111 411 231 C ATOM 55 CD GLU A 7 44.493 26.404 5.650 1.00 20.01 C ANISOU 55 CD GLU A 7 2228 2854 2520 -105 412 248 C ATOM 56 OE1 GLU A 7 43.470 25.832 5.192 1.00 20.18 O ANISOU 56 OE1 GLU A 7 2274 2912 2483 -84 421 228 O ATOM 57 OE2 GLU A 7 44.565 27.633 5.837 1.00 20.69 O ANISOU 57 OE2 GLU A 7 2334 2918 2611 -123 405 285 O ATOM 58 N LEU A 8 45.527 22.256 7.973 1.00 13.71 N ANISOU 58 N LEU A 8 1352 2008 1848 -69 338 132 N ATOM 59 CA LEU A 8 45.313 22.007 9.396 1.00 13.27 C ANISOU 59 CA LEU A 8 1310 1914 1818 -75 271 122 C ATOM 60 C LEU A 8 46.453 21.213 10.012 1.00 13.53 C ANISOU 60 C LEU A 8 1286 1925 1929 -75 257 121 C ATOM 61 O LEU A 8 46.873 21.488 11.137 1.00 13.66 O ANISOU 61 O LEU A 8 1291 1909 1991 -100 204 139 O ATOM 62 CB LEU A 8 43.984 21.282 9.632 1.00 12.75 C ANISOU 62 CB LEU A 8 1295 1857 1693 -56 250 82 C ATOM 63 CG LEU A 8 43.619 21.051 11.100 1.00 12.44 C ANISOU 63 CG LEU A 8 1276 1778 1671 -66 180 68 C ATOM 64 CD1 LEU A 8 43.519 22.367 11.850 1.00 14.15 C ANISOU 64 CD1 LEU A 8 1516 1964 1897 -96 142 100 C ATOM 65 CD2 LEU A 8 42.310 20.278 11.183 1.00 14.47 C ANISOU 65 CD2 LEU A 8 1582 2053 1863 -47 167 26 C ATOM 66 N ALA A 9 46.967 20.226 9.284 1.00 14.20 N ANISOU 66 N ALA A 9 1336 2028 2030 -50 307 105 N ATOM 67 CA ALA A 9 48.107 19.470 9.785 1.00 15.22 C ANISOU 67 CA ALA A 9 1405 2140 2239 -42 303 112 C ATOM 68 C ALA A 9 49.239 20.428 10.131 1.00 16.17 C ANISOU 68 C ALA A 9 1476 2251 2418 -75 286 163 C ATOM 69 O ALA A 9 49.833 20.342 11.198 1.00 16.74 O ANISOU 69 O ALA A 9 1517 2300 2545 -92 237 183 O ATOM 70 CB ALA A 9 48.566 18.448 8.752 1.00 15.08 C ANISOU 70 CB ALA A 9 1358 2142 2230 -9 377 93 C ATOM 71 N ALA A 10 49.534 21.354 9.224 1.00 16.33 N ANISOU 71 N ALA A 10 1490 2292 2423 -89 327 187 N ATOM 72 CA ALA A 10 50.616 22.304 9.455 1.00 15.28 C ANISOU 72 CA ALA A 10 1313 2155 2338 -126 316 235 C ATOM 73 C ALA A 10 50.353 23.225 10.650 1.00 16.85 C ANISOU 73 C ALA A 10 1545 2322 2536 -170 247 255 C ATOM 74 O ALA A 10 51.250 23.486 11.444 1.00 18.65 O ANISOU 74 O ALA A 10 1732 2536 2816 -204 212 287 O ATOM 75 CB ALA A 10 50.891 23.124 8.195 1.00 17.07 C ANISOU 75 CB ALA A 10 1535 2410 2540 -134 376 252 C ATOM 76 N ALA A 11 49.136 23.740 10.766 1.00 15.16 N ANISOU 76 N ALA A 11 1403 2097 2259 -172 230 238 N ATOM 77 CA ALA A 11 48.805 24.597 11.903 1.00 15.38 C ANISOU 77 CA ALA A 11 1472 2089 2284 -213 172 253 C ATOM 78 C ALA A 11 48.908 23.838 13.219 1.00 15.29 C ANISOU 78 C ALA A 11 1448 2051 2309 -223 110 242 C ATOM 79 O ALA A 11 49.417 24.367 14.209 1.00 16.86 O ANISOU 79 O ALA A 11 1641 2225 2539 -272 65 268 O ATOM 80 CB ALA A 11 47.413 25.194 11.741 1.00 16.65 C ANISOU 80 CB ALA A 11 1710 2243 2372 -203 172 237 C ATOM 81 N MET A 12 48.426 22.599 13.237 1.00 14.66 N ANISOU 81 N MET A 12 1369 1977 2223 -183 108 204 N ATOM 82 CA MET A 12 48.557 21.785 14.437 1.00 13.67 C ANISOU 82 CA MET A 12 1230 1828 2134 -190 51 195 C ATOM 83 C MET A 12 50.010 21.550 14.812 1.00 16.75 C ANISOU 83 C MET A 12 1540 2222 2604 -209 40 234 C ATOM 84 O MET A 12 50.366 21.610 15.990 1.00 17.23 O ANISOU 84 O MET A 12 1588 2261 2698 -249 -19 253 O ATOM 85 CB MET A 12 47.824 20.461 14.269 1.00 13.63 C ANISOU 85 CB MET A 12 1242 1831 2107 -142 60 148 C ATOM 86 CG MET A 12 46.315 20.618 14.328 1.00 12.98 C ANISOU 86 CG MET A 12 1238 1746 1949 -134 47 112 C ATOM 87 SD MET A 12 45.514 19.053 13.971 1.00 13.73 S ANISOU 87 SD MET A 12 1353 1857 2007 -85 65 57 S ATOM 88 CE MET A 12 43.921 19.323 14.740 1.00 16.44 C ANISOU 88 CE MET A 12 1778 2188 2281 -96 14 27 C ATOM 89 N LYS A 13 50.853 21.297 13.812 1.00 15.52 N ANISOU 89 N LYS A 13 1327 2094 2476 -184 99 249 N ATOM 90 CA LYS A 13 52.266 21.081 14.075 1.00 17.12 C ANISOU 90 CA LYS A 13 1443 2306 2755 -197 95 292 C ATOM 91 C LYS A 13 52.901 22.363 14.594 1.00 18.05 C ANISOU 91 C LYS A 13 1551 2420 2886 -266 63 339 C ATOM 92 O LYS A 13 53.684 22.340 15.547 1.00 20.05 O ANISOU 92 O LYS A 13 1759 2669 3188 -304 15 375 O ATOM 93 CB LYS A 13 52.983 20.614 12.811 1.00 18.16 C ANISOU 93 CB LYS A 13 1520 2468 2910 -155 173 296 C ATOM 94 CG LYS A 13 54.451 20.278 13.039 1.00 23.44 C ANISOU 94 CG LYS A 13 2091 3151 3663 -159 175 345 C ATOM 95 CD LYS A 13 55.126 19.806 11.768 1.00 25.37 C ANISOU 95 CD LYS A 13 2286 3424 3932 -114 261 346 C ATOM 96 CE LYS A 13 56.592 19.489 12.046 1.00 29.86 C ANISOU 96 CE LYS A 13 2750 4009 4588 -115 263 400 C ATOM 97 NZ LYS A 13 57.358 19.213 10.798 1.00 32.84 N ANISOU 97 NZ LYS A 13 3074 4413 4992 -78 351 407 N ATOM 98 N ARG A 14 52.558 23.489 13.982 1.00 20.22 N ANISOU 98 N ARG A 14 1747 3174 2764 -857 370 626 N ATOM 99 CA ARG A 14 53.138 24.756 14.412 1.00 22.06 C ANISOU 99 CA ARG A 14 2062 3266 3054 -966 278 667 C ATOM 100 C ARG A 14 52.810 25.031 15.880 1.00 19.47 C ANISOU 100 C ARG A 14 1922 2756 2720 -860 111 649 C ATOM 101 O ARG A 14 53.596 25.667 16.590 1.00 24.23 O ANISOU 101 O ARG A 14 2542 3246 3418 -924 -9 624 O ATOM 102 CB ARG A 14 52.661 25.913 13.531 1.00 30.80 C ANISOU 102 CB ARG A 14 3267 4364 4073 -1061 374 798 C ATOM 103 CG ARG A 14 53.381 27.217 13.826 1.00 41.61 C ANISOU 103 CG ARG A 14 4693 5599 5517 -1197 298 839 C ATOM 104 CD ARG A 14 52.612 28.414 13.307 1.00 45.81 C ANISOU 104 CD ARG A 14 5398 6069 5939 -1242 358 976 C ATOM 105 NE ARG A 14 53.071 29.655 13.924 1.00 49.74 N ANISOU 105 NE ARG A 14 6005 6396 6499 -1331 256 1011 N ATOM 106 CZ ARG A 14 52.608 30.133 15.075 1.00 49.31 C ANISOU 106 CZ ARG A 14 6135 6175 6424 -1247 122 1014 C ATOM 107 NH1 ARG A 14 51.673 29.472 15.744 1.00 52.91 N ANISOU 107 NH1 ARG A 14 6694 6612 6796 -1073 75 986 N ATOM 108 NH2 ARG A 14 53.085 31.269 15.562 1.00 49.46 N ANISOU 108 NH2 ARG A 14 6237 6048 6509 -1339 37 1041 N ATOM 109 N HIS A 15 51.651 24.549 16.326 1.00 17.79 N ANISOU 109 N HIS A 15 1846 2519 2394 -699 105 655 N ATOM 110 CA HIS A 15 51.185 24.778 17.694 1.00 19.44 C ANISOU 110 CA HIS A 15 2248 2561 2576 -587 -42 642 C ATOM 111 C HIS A 15 51.562 23.640 18.652 1.00 19.11 C ANISOU 111 C HIS A 15 2147 2514 2601 -477 -139 527 C ATOM 112 O HIS A 15 51.055 23.565 19.774 1.00 20.81 O ANISOU 112 O HIS A 15 2517 2614 2777 -357 -247 508 O ATOM 113 CB HIS A 15 49.673 25.038 17.711 1.00 18.91 C ANISOU 113 CB HIS A 15 2387 2451 2345 -479 1 718 C ATOM 114 CG HIS A 15 49.284 26.381 17.168 1.00 19.89 C ANISOU 114 CG HIS A 15 2631 2519 2405 -568 42 834 C ATOM 115 ND1 HIS A 15 49.057 26.609 15.827 1.00 20.54 N ANISOU 115 ND1 HIS A 15 2652 2720 2432 -644 194 906 N ATOM 116 CD2 HIS A 15 49.092 27.569 17.787 1.00 25.50 C ANISOU 116 CD2 HIS A 15 3520 3068 3101 -592 -51 890 C ATOM 117 CE1 HIS A 15 48.739 27.879 15.645 1.00 23.89 C ANISOU 117 CE1 HIS A 15 3217 3052 2808 -709 193 1006 C ATOM 118 NE2 HIS A 15 48.750 28.483 16.819 1.00 26.49 N ANISOU 118 NE2 HIS A 15 3692 3210 3164 -680 46 997 N ATOM 119 N GLY A 16 52.440 22.752 18.198 1.00 20.44 N ANISOU 119 N GLY A 16 2091 2808 2866 -515 -100 450 N ATOM 120 CA GLY A 16 53.031 21.739 19.058 1.00 19.11 C ANISOU 120 CA GLY A 16 1843 2633 2783 -431 -201 337 C ATOM 121 C GLY A 16 52.176 20.526 19.358 1.00 16.45 C ANISOU 121 C GLY A 16 1541 2336 2373 -261 -172 299 C ATOM 122 O GLY A 16 52.392 19.837 20.355 1.00 20.37 O ANISOU 122 O GLY A 16 2052 2778 2909 -159 -279 224 O ATOM 123 N LEU A 17 51.210 20.240 18.498 1.00 18.43 N ANISOU 123 N LEU A 17 1805 2681 2516 -227 -26 348 N ATOM 124 CA LEU A 17 50.326 19.109 18.741 1.00 16.83 C ANISOU 124 CA LEU A 17 1638 2514 2241 -68 16 310 C ATOM 125 C LEU A 17 50.910 17.796 18.223 1.00 18.85 C ANISOU 125 C LEU A 17 1666 2921 2577 -57 84 222 C ATOM 126 O LEU A 17 50.513 16.721 18.659 1.00 18.65 O ANISOU 126 O LEU A 17 1645 2908 2535 74 84 165 O ATOM 127 CB LEU A 17 48.968 19.374 18.100 1.00 19.17 C ANISOU 127 CB LEU A 17 2055 2843 2385 -26 138 390 C ATOM 128 CG LEU A 17 47.728 18.827 18.785 1.00 22.05 C ANISOU 128 CG LEU A 17 2585 3152 2639 144 135 381 C ATOM 129 CD1 LEU A 17 47.695 19.164 20.267 1.00 15.98 C ANISOU 129 CD1 LEU A 17 1996 2203 1875 217 -35 367 C ATOM 130 CD2 LEU A 17 46.526 19.390 18.053 1.00 15.15 C ANISOU 130 CD2 LEU A 17 1824 2307 1626 153 248 465 C ATOM 131 N ASP A 18 51.855 17.876 17.295 1.00 20.85 N ANISOU 131 N ASP A 18 1719 3285 2919 -194 144 209 N ATOM 132 CA ASP A 18 52.419 16.665 16.713 1.00 22.02 C ANISOU 132 CA ASP A 18 1638 3585 3145 -193 216 124 C ATOM 133 C ASP A 18 53.207 15.848 17.745 1.00 21.09 C ANISOU 133 C ASP A 18 1460 3415 3137 -120 82 19 C ATOM 134 O ASP A 18 54.183 16.312 18.312 1.00 21.59 O ANISOU 134 O ASP A 18 1498 3405 3299 -182 -42 -12 O ATOM 135 CB ASP A 18 53.260 16.986 15.474 1.00 25.56 C ANISOU 135 CB ASP A 18 1885 4165 3660 -364 313 133 C ATOM 136 CG ASP A 18 54.296 18.052 15.725 1.00 28.39 C ANISOU 136 CG ASP A 18 2233 4443 4112 -501 216 145 C ATOM 137 OD1 ASP A 18 54.014 19.049 16.437 1.00 26.25 O ANISOU 137 OD1 ASP A 18 2153 4021 3802 -500 123 203 O ATOM 138 OD2 ASP A 18 55.412 17.890 15.188 1.00 34.26 O ANISOU 138 OD2 ASP A 18 2769 5276 4973 -614 236 90 O ATOM 139 N ASN A 19 52.745 14.626 17.981 1.00 20.28 N ANISOU 139 N ASN A 19 1341 3351 3015 15 110 -37 N ATOM 140 CA ASN A 19 53.293 13.737 19.007 1.00 18.09 C ANISOU 140 CA ASN A 19 1035 3019 2821 114 -12 -130 C ATOM 141 C ASN A 19 53.059 14.198 20.455 1.00 16.12 C ANISOU 141 C ASN A 19 1007 2579 2538 202 -177 -117 C ATOM 142 O ASN A 19 53.683 13.677 21.387 1.00 18.09 O ANISOU 142 O ASN A 19 1243 2769 2863 268 -304 -189 O ATOM 143 CB ASN A 19 54.768 13.419 18.763 1.00 22.86 C ANISOU 143 CB ASN A 19 1403 3695 3587 20 -54 -215 C ATOM 144 CG ASN A 19 55.114 11.999 19.142 1.00 29.88 C ANISOU 144 CG ASN A 19 2180 4624 4547 130 -81 -319 C ATOM 145 OD1 ASN A 19 56.265 11.685 19.447 1.00 37.68 O ANISOU 145 OD1 ASN A 19 3032 5619 5666 103 -175 -401 O ATOM 146 ND2 ASN A 19 54.111 11.123 19.121 1.00 30.34 N ANISOU 146 ND2 ASN A 19 2295 4710 4523 256 1 -318 N ATOM 147 N TYR A 20 52.154 15.154 20.644 1.00 16.36 N ANISOU 147 N TYR A 20 1242 2520 2454 207 -177 -28 N ATOM 148 CA TYR A 20 51.803 15.593 21.993 1.00 14.80 C ANISOU 148 CA TYR A 20 1265 2148 2213 296 -323 -14 C ATOM 149 C TYR A 20 51.146 14.436 22.749 1.00 13.87 C ANISOU 149 C TYR A 20 1224 1999 2046 472 -336 -60 C ATOM 150 O TYR A 20 50.205 13.820 22.243 1.00 15.03 O ANISOU 150 O TYR A 20 1384 2215 2111 537 -207 -47 O ATOM 151 CB TYR A 20 50.866 16.804 21.953 1.00 16.35 C ANISOU 151 CB TYR A 20 1659 2263 2291 269 -304 89 C ATOM 152 CG TYR A 20 50.712 17.442 23.313 1.00 15.60 C ANISOU 152 CG TYR A 20 1771 1988 2169 330 -467 99 C ATOM 153 CD1 TYR A 20 51.587 18.434 23.737 1.00 14.22 C ANISOU 153 CD1 TYR A 20 1604 1728 2072 234 -589 103 C ATOM 154 CD2 TYR A 20 49.712 17.038 24.186 1.00 15.01 C ANISOU 154 CD2 TYR A 20 1880 1829 1995 482 -498 100 C ATOM 155 CE1 TYR A 20 51.467 19.007 24.995 1.00 17.34 C ANISOU 155 CE1 TYR A 20 2182 1962 2444 292 -742 105 C ATOM 156 CE2 TYR A 20 49.587 17.599 25.450 1.00 15.94 C ANISOU 156 CE2 TYR A 20 2184 1786 2087 539 -649 105 C ATOM 157 CZ TYR A 20 50.466 18.583 25.848 1.00 17.65 C ANISOU 157 CZ TYR A 20 2402 1924 2380 445 -772 107 C ATOM 158 OH TYR A 20 50.336 19.161 27.090 1.00 20.28 O ANISOU 158 OH TYR A 20 2917 2102 2686 501 -921 109 O ATOM 159 N ARG A 21 51.657 14.140 23.948 1.00 14.91 N ANISOU 159 N ARG A 21 1406 2030 2229 548 -491 -115 N ATOM 160 CA ARG A 21 51.208 12.984 24.736 1.00 15.72 C ANISOU 160 CA ARG A 21 1575 2097 2301 714 -515 -164 C ATOM 161 C ARG A 21 51.290 11.696 23.922 1.00 17.09 C ANISOU 161 C ARG A 21 1558 2418 2517 740 -388 -220 C ATOM 162 O ARG A 21 50.561 10.741 24.183 1.00 17.44 O ANISOU 162 O ARG A 21 1657 2462 2507 866 -338 -241 O ATOM 163 CB ARG A 21 49.799 13.183 25.291 1.00 17.81 C ANISOU 163 CB ARG A 21 2085 2267 2415 819 -496 -108 C ATOM 164 CG ARG A 21 49.715 14.167 26.451 1.00 22.76 C ANISOU 164 CG ARG A 21 2918 2727 3004 839 -652 -77 C ATOM 165 CD ARG A 21 50.132 13.519 27.758 1.00 24.23 C ANISOU 165 CD ARG A 21 3163 2818 3224 956 -799 -141 C ATOM 166 NE ARG A 21 50.249 14.502 28.833 1.00 30.28 N ANISOU 166 NE ARG A 21 4096 3436 3971 960 -959 -121 N ATOM 167 CZ ARG A 21 50.389 14.194 30.118 1.00 34.31 C ANISOU 167 CZ ARG A 21 4720 3838 4477 1070 -1100 -159 C ATOM 168 NH1 ARG A 21 50.425 12.923 30.497 1.00 38.90 N ANISOU 168 NH1 ARG A 21 5279 4449 5052 1149 -1080 -235 N ATOM 169 NH2 ARG A 21 50.483 15.160 31.023 1.00 36.25 N ANISOU 169 NH2 ARG A 21 5111 3958 4704 1064 -1240 -141 N ATOM 170 N GLY A 22 52.176 11.693 22.932 1.00 13.89 N ANISOU 170 N GLY A 22 1319 2022 1935 122 -150 165 N ATOM 171 CA GLY A 22 52.453 10.503 22.145 1.00 14.82 C ANISOU 171 CA GLY A 22 1432 2102 2095 191 -144 180 C ATOM 172 C GLY A 22 51.516 10.297 20.970 1.00 14.30 C ANISOU 172 C GLY A 22 1409 1978 2048 200 -96 154 C ATOM 173 O GLY A 22 51.561 9.256 20.315 1.00 15.80 O ANISOU 173 O GLY A 22 1606 2129 2270 250 -83 161 O ATOM 174 N TYR A 23 50.651 11.271 20.709 1.00 11.89 N ANISOU 174 N TYR A 23 1130 1664 1723 151 -68 124 N ATOM 175 CA TYR A 23 49.691 11.157 19.619 1.00 12.12 C ANISOU 175 CA TYR A 23 1197 1645 1763 156 -29 100 C ATOM 176 C TYR A 23 50.206 11.844 18.371 1.00 12.21 C ANISOU 176 C TYR A 23 1179 1669 1792 158 5 71 C ATOM 177 O TYR A 23 50.377 13.061 18.351 1.00 13.57 O ANISOU 177 O TYR A 23 1335 1869 1951 120 18 54 O ATOM 178 CB TYR A 23 48.341 11.725 20.044 1.00 12.71 C ANISOU 178 CB TYR A 23 1319 1701 1809 109 -20 89 C ATOM 179 CG TYR A 23 47.657 10.839 21.042 1.00 12.63 C ANISOU 179 CG TYR A 23 1349 1664 1784 108 -42 113 C ATOM 180 CD1 TYR A 23 46.897 9.756 20.619 1.00 11.58 C ANISOU 180 CD1 TYR A 23 1254 1480 1666 135 -29 113 C ATOM 181 CD2 TYR A 23 47.778 11.069 22.416 1.00 11.44 C ANISOU 181 CD2 TYR A 23 1203 1541 1603 78 -72 134 C ATOM 182 CE1 TYR A 23 46.268 8.922 21.535 1.00 12.27 C ANISOU 182 CE1 TYR A 23 1383 1538 1740 132 -42 135 C ATOM 183 CE2 TYR A 23 47.157 10.235 23.336 1.00 12.70 C ANISOU 183 CE2 TYR A 23 1406 1674 1745 76 -89 159 C ATOM 184 CZ TYR A 23 46.405 9.163 22.891 1.00 13.27 C ANISOU 184 CZ TYR A 23 1517 1690 1835 104 -72 160 C ATOM 185 OH TYR A 23 45.767 8.332 23.800 1.00 13.23 O ANISOU 185 OH TYR A 23 1560 1654 1813 99 -81 184 O ATOM 186 N SER A 24 50.505 11.044 17.353 1.00 12.52 N ANISOU 186 N SER A 24 1212 1685 1861 202 24 64 N ATOM 187 CA SER A 24 51.028 11.586 16.106 1.00 14.12 C ANISOU 187 CA SER A 24 1391 1897 2077 206 60 37 C ATOM 188 C SER A 24 50.043 12.555 15.457 1.00 14.90 C ANISOU 188 C SER A 24 1525 1984 2152 170 89 14 C ATOM 189 O SER A 24 48.829 12.516 15.697 1.00 14.86 O ANISOU 189 O SER A 24 1563 1954 2130 155 85 14 O ATOM 190 CB SER A 24 51.357 10.457 15.138 1.00 15.79 C ANISOU 190 CB SER A 24 1600 2079 2320 256 80 31 C ATOM 191 OG SER A 24 50.157 9.845 14.692 1.00 17.30 O ANISOU 191 OG SER A 24 1844 2225 2504 259 94 22 O ATOM 192 N LEU A 25 50.581 13.432 14.625 1.00 15.48 N ANISOU 192 N LEU A 25 1579 2076 2227 159 119 -5 N ATOM 193 CA LEU A 25 49.792 14.435 13.934 1.00 12.53 C ANISOU 193 CA LEU A 25 1235 1692 1832 131 147 -21 C ATOM 194 C LEU A 25 48.557 13.865 13.212 1.00 13.35 C ANISOU 194 C LEU A 25 1386 1760 1927 145 154 -28 C ATOM 195 O LEU A 25 47.482 14.479 13.215 1.00 13.55 O ANISOU 195 O LEU A 25 1441 1774 1931 123 157 -30 O ATOM 196 CB LEU A 25 50.691 15.171 12.955 1.00 16.52 C ANISOU 196 CB LEU A 25 1718 2217 2343 128 184 -39 C ATOM 197 CG LEU A 25 50.114 16.410 12.303 1.00 14.61 C ANISOU 197 CG LEU A 25 1503 1968 2078 99 216 -48 C ATOM 198 CD1 LEU A 25 49.617 17.389 13.361 1.00 19.28 C ANISOU 198 CD1 LEU A 25 2105 2566 2656 58 206 -42 C ATOM 199 CD2 LEU A 25 51.177 17.056 11.416 1.00 16.77 C ANISOU 199 CD2 LEU A 25 1754 2259 2358 94 257 -64 C ATOM 200 N GLY A 26 48.701 12.699 12.590 1.00 13.73 N ANISOU 200 N GLY A 26 1437 1790 1991 181 159 -33 N ATOM 201 CA GLY A 26 47.583 12.083 11.890 1.00 12.38 C ANISOU 201 CA GLY A 26 1306 1589 1810 189 166 -46 C ATOM 202 C GLY A 26 46.395 11.785 12.791 1.00 11.91 C ANISOU 202 C GLY A 26 1275 1510 1741 174 142 -37 C ATOM 203 O GLY A 26 45.231 11.865 12.375 1.00 12.03 O ANISOU 203 O GLY A 26 1320 1512 1739 164 146 -50 O ATOM 204 N ASN A 27 46.676 11.417 14.039 1.00 11.49 N ANISOU 204 N ASN A 27 1213 1456 1695 174 116 -16 N ATOM 205 CA ASN A 27 45.594 11.215 15.015 1.00 10.97 C ANISOU 205 CA ASN A 27 1177 1373 1618 153 98 -8 C ATOM 206 C ASN A 27 44.782 12.479 15.239 1.00 10.54 C ANISOU 206 C ASN A 27 1133 1329 1542 114 101 -15 C ATOM 207 O ASN A 27 43.558 12.441 15.303 1.00 11.52 O ANISOU 207 O ASN A 27 1284 1434 1657 100 102 -24 O ATOM 208 CB ASN A 27 46.153 10.738 16.356 1.00 13.41 C ANISOU 208 CB ASN A 27 1477 1687 1932 156 69 20 C ATOM 209 CG ASN A 27 46.468 9.262 16.349 1.00 12.01 C ANISOU 209 CG ASN A 27 1306 1480 1777 196 65 32 C ATOM 210 OD1 ASN A 27 45.552 8.428 16.419 1.00 12.29 O ANISOU 210 OD1 ASN A 27 1379 1479 1813 197 70 28 O ATOM 211 ND2 ASN A 27 47.763 8.923 16.238 1.00 13.28 N ANISOU 211 ND2 ASN A 27 1429 1656 1960 230 61 45 N ATOM 212 N TRP A 28 45.484 13.591 15.388 1.00 11.01 N ANISOU 212 N TRP A 28 1169 1417 1597 97 106 -11 N ATOM 213 CA TRP A 28 44.839 14.883 15.579 1.00 11.27 C ANISOU 213 CA TRP A 28 1211 1455 1615 62 117 -17 C ATOM 214 C TRP A 28 44.047 15.342 14.362 1.00 10.82 C ANISOU 214 C TRP A 28 1172 1387 1551 69 139 -31 C ATOM 215 O TRP A 28 42.957 15.896 14.509 1.00 11.35 O ANISOU 215 O TRP A 28 1257 1443 1611 52 142 -35 O ATOM 216 CB TRP A 28 45.880 15.930 15.976 1.00 12.35 C ANISOU 216 CB TRP A 28 1320 1623 1751 39 125 -14 C ATOM 217 CG TRP A 28 46.515 15.637 17.320 1.00 12.06 C ANISOU 217 CG TRP A 28 1265 1606 1712 25 96 1 C ATOM 218 CD1 TRP A 28 47.767 15.135 17.549 1.00 13.78 C ANISOU 218 CD1 TRP A 28 1446 1849 1940 43 79 11 C ATOM 219 CD2 TRP A 28 45.905 15.801 18.603 1.00 10.45 C ANISOU 219 CD2 TRP A 28 1079 1401 1493 -9 81 7 C ATOM 220 NE1 TRP A 28 47.979 14.994 18.902 1.00 13.25 N ANISOU 220 NE1 TRP A 28 1373 1801 1861 24 49 27 N ATOM 221 CE2 TRP A 28 46.847 15.396 19.570 1.00 11.22 C ANISOU 221 CE2 TRP A 28 1152 1526 1585 -11 51 24 C ATOM 222 CE3 TRP A 28 44.650 16.256 19.029 1.00 13.44 C ANISOU 222 CE3 TRP A 28 1489 1758 1861 -38 90 -1 C ATOM 223 CZ2 TRP A 28 46.575 15.441 20.938 1.00 11.85 C ANISOU 223 CZ2 TRP A 28 1244 1615 1642 -46 30 33 C ATOM 224 CZ3 TRP A 28 44.382 16.295 20.386 1.00 12.28 C ANISOU 224 CZ3 TRP A 28 1354 1616 1698 -73 75 5 C ATOM 225 CH2 TRP A 28 45.334 15.885 21.322 1.00 11.58 C ANISOU 225 CH2 TRP A 28 1247 1556 1597 -78 45 22 C ATOM 226 N VAL A 29 44.601 15.120 13.172 1.00 10.59 N ANISOU 226 N VAL A 29 1135 1363 1524 94 154 -38 N ATOM 227 CA VAL A 29 43.911 15.511 11.938 1.00 10.51 C ANISOU 227 CA VAL A 29 1144 1349 1499 102 171 -48 C ATOM 228 C VAL A 29 42.659 14.647 11.747 1.00 12.00 C ANISOU 228 C VAL A 29 1356 1520 1684 110 157 -59 C ATOM 229 O VAL A 29 41.580 15.157 11.422 1.00 11.85 O ANISOU 229 O VAL A 29 1350 1498 1652 103 156 -64 O ATOM 230 CB VAL A 29 44.854 15.454 10.726 1.00 11.21 C ANISOU 230 CB VAL A 29 1225 1450 1587 122 193 -55 C ATOM 231 CG1 VAL A 29 44.095 15.739 9.433 1.00 11.81 C ANISOU 231 CG1 VAL A 29 1325 1525 1638 130 206 -63 C ATOM 232 CG2 VAL A 29 45.977 16.468 10.884 1.00 12.82 C ANISOU 232 CG2 VAL A 29 1405 1672 1795 107 213 -48 C ATOM 233 N CYS A 30 42.804 13.348 11.988 1.00 11.28 N ANISOU 233 N CYS A 30 1266 1416 1605 123 147 -64 N ATOM 234 CA CYS A 30 41.679 12.421 11.906 1.00 10.26 C ANISOU 234 CA CYS A 30 1157 1266 1474 124 138 -80 C ATOM 235 C CYS A 30 40.567 12.831 12.868 1.00 12.61 C ANISOU 235 C CYS A 30 1465 1556 1770 97 126 -79 C ATOM 236 O CYS A 30 39.395 12.843 12.494 1.00 11.70 O ANISOU 236 O CYS A 30 1361 1438 1648 91 125 -95 O ATOM 237 CB CYS A 30 42.148 10.986 12.205 1.00 10.19 C ANISOU 237 CB CYS A 30 1152 1237 1484 140 136 -82 C ATOM 238 SG CYS A 30 40.878 9.734 11.970 1.00 12.05 S ANISOU 238 SG CYS A 30 1415 1443 1720 137 138 -110 S ATOM 239 N ALA A 31 40.930 13.160 14.106 1.00 10.91 N ANISOU 239 N ALA A 31 1245 1341 1561 80 119 -61 N ATOM 240 CA ALA A 31 39.931 13.548 15.084 1.00 11.00 C ANISOU 240 CA ALA A 31 1267 1342 1571 50 114 -62 C ATOM 241 C ALA A 31 39.220 14.808 14.614 1.00 11.04 C ANISOU 241 C ALA A 31 1270 1356 1570 41 125 -68 C ATOM 242 O ALA A 31 37.994 14.900 14.690 1.00 11.94 O ANISOU 242 O ALA A 31 1391 1460 1685 31 124 -80 O ATOM 243 CB ALA A 31 40.582 13.782 16.444 1.00 12.92 C ANISOU 243 CB ALA A 31 1506 1589 1814 29 105 -44 C ATOM 244 N ALA A 32 39.983 15.778 14.113 1.00 9.68 N ANISOU 244 N ALA A 32 1085 1199 1392 47 137 -57 N ATOM 245 CA ALA A 32 39.362 17.020 13.664 1.00 8.54 C ANISOU 245 CA ALA A 32 944 1058 1245 43 151 -56 C ATOM 246 C ALA A 32 38.428 16.766 12.486 1.00 8.87 C ANISOU 246 C ALA A 32 991 1103 1276 66 146 -66 C ATOM 247 O ALA A 32 37.366 17.370 12.384 1.00 10.18 O ANISOU 247 O ALA A 32 1159 1266 1444 65 146 -68 O ATOM 248 CB ALA A 32 40.409 18.044 13.293 1.00 10.14 C ANISOU 248 CB ALA A 32 1138 1273 1443 43 172 -43 C ATOM 249 N LYS A 33 38.831 15.865 11.593 1.00 10.14 N ANISOU 249 N LYS A 33 1154 1272 1428 86 141 -75 N ATOM 250 CA LYS A 33 37.989 15.535 10.441 1.00 11.50 C ANISOU 250 CA LYS A 33 1332 1454 1584 102 134 -90 C ATOM 251 C LYS A 33 36.605 15.075 10.868 1.00 10.07 C ANISOU 251 C LYS A 33 1151 1265 1410 91 119 -108 C ATOM 252 O LYS A 33 35.594 15.572 10.372 1.00 11.79 O ANISOU 252 O LYS A 33 1365 1495 1621 96 111 -113 O ATOM 253 CB LYS A 33 38.633 14.451 9.575 1.00 11.61 C ANISOU 253 CB LYS A 33 1351 1473 1589 118 136 -104 C ATOM 254 CG LYS A 33 37.706 13.918 8.477 1.00 12.72 C ANISOU 254 CG LYS A 33 1498 1628 1708 126 127 -127 C ATOM 255 CD LYS A 33 37.551 14.932 7.358 1.00 14.09 C ANISOU 255 CD LYS A 33 1676 1827 1852 141 128 -114 C ATOM 256 CE LYS A 33 36.683 14.363 6.249 1.00 19.20 C ANISOU 256 CE LYS A 33 2327 2497 2470 146 113 -139 C ATOM 257 NZ LYS A 33 36.378 15.385 5.204 1.00 22.84 N ANISOU 257 NZ LYS A 33 2794 2986 2898 163 108 -120 N ATOM 258 N PHE A 34 36.559 14.131 11.795 1.00 10.98 N ANISOU 258 N PHE A 34 1271 1361 1540 75 116 -119 N ATOM 259 CA PHE A 34 35.277 13.564 12.172 1.00 12.32 C ANISOU 259 CA PHE A 34 1443 1522 1719 59 108 -143 C ATOM 260 C PHE A 34 34.534 14.347 13.245 1.00 12.63 C ANISOU 260 C PHE A 34 1477 1550 1773 36 111 -138 C ATOM 261 O PHE A 34 33.323 14.211 13.366 1.00 14.34 O ANISOU 261 O PHE A 34 1688 1765 1997 25 107 -160 O ATOM 262 CB PHE A 34 35.440 12.095 12.522 1.00 11.99 C ANISOU 262 CB PHE A 34 1414 1458 1683 52 109 -158 C ATOM 263 CG PHE A 34 35.922 11.271 11.365 1.00 11.46 C ANISOU 263 CG PHE A 34 1352 1398 1606 72 113 -172 C ATOM 264 CD1 PHE A 34 35.226 11.289 10.165 1.00 13.18 C ANISOU 264 CD1 PHE A 34 1564 1640 1803 78 107 -194 C ATOM 265 CD2 PHE A 34 37.078 10.521 11.448 1.00 13.48 C ANISOU 265 CD2 PHE A 34 1615 1639 1869 85 122 -163 C ATOM 266 CE1 PHE A 34 35.653 10.548 9.086 1.00 13.82 C ANISOU 266 CE1 PHE A 34 1652 1729 1870 90 114 -212 C ATOM 267 CE2 PHE A 34 37.511 9.773 10.368 1.00 15.51 C ANISOU 267 CE2 PHE A 34 1876 1899 2119 101 132 -181 C ATOM 268 CZ PHE A 34 36.799 9.788 9.189 1.00 13.91 C ANISOU 268 CZ PHE A 34 1672 1719 1893 101 130 -207 C ATOM 269 N GLU A 35 35.241 15.185 13.995 1.00 9.84 N ANISOU 269 N GLU A 35 1124 1191 1424 27 120 -116 N ATOM 270 CA GLU A 35 34.560 16.033 14.956 1.00 10.58 C ANISOU 270 CA GLU A 35 1214 1274 1531 3 130 -115 C ATOM 271 C GLU A 35 33.884 17.208 14.262 1.00 10.74 C ANISOU 271 C GLU A 35 1222 1304 1556 19 135 -111 C ATOM 272 O GLU A 35 32.741 17.544 14.570 1.00 11.93 O ANISOU 272 O GLU A 35 1363 1448 1722 10 139 -123 O ATOM 273 CB GLU A 35 35.537 16.558 16.013 1.00 11.15 C ANISOU 273 CB GLU A 35 1292 1340 1604 -19 141 -97 C ATOM 274 CG GLU A 35 36.050 15.492 16.953 1.00 10.86 C ANISOU 274 CG GLU A 35 1269 1294 1564 -35 132 -96 C ATOM 275 CD GLU A 35 34.979 14.905 17.858 1.00 12.18 C ANISOU 275 CD GLU A 35 1449 1440 1738 -62 134 -113 C ATOM 276 OE1 GLU A 35 33.817 15.378 17.859 1.00 12.58 O ANISOU 276 OE1 GLU A 35 1493 1486 1802 -73 144 -131 O ATOM 277 OE2 GLU A 35 35.306 13.941 18.587 1.00 12.19 O ANISOU 277 OE2 GLU A 35 1468 1429 1735 -73 128 -109 O ATOM 278 N SER A 36 34.593 17.845 13.325 1.00 11.05 N ANISOU 278 N SER A 36 1261 1357 1581 43 139 -91 N ATOM 279 CA SER A 36 34.147 19.135 12.792 1.00 10.80 C ANISOU 279 CA SER A 36 1223 1327 1552 60 149 -76 C ATOM 280 C SER A 36 34.212 19.272 11.270 1.00 10.54 C ANISOU 280 C SER A 36 1192 1319 1496 96 139 -64 C ATOM 281 O SER A 36 33.814 20.311 10.732 1.00 11.64 O ANISOU 281 O SER A 36 1331 1460 1634 117 145 -45 O ATOM 282 CB SER A 36 35.014 20.245 13.382 1.00 12.11 C ANISOU 282 CB SER A 36 1396 1480 1725 45 177 -56 C ATOM 283 OG SER A 36 36.334 20.160 12.852 1.00 11.15 O ANISOU 283 OG SER A 36 1281 1370 1586 53 182 -44 O ATOM 284 N ASN A 37 34.714 18.251 10.578 1.00 12.07 N ANISOU 284 N ASN A 37 1391 1528 1668 104 126 -74 N ATOM 285 CA ASN A 37 35.013 18.373 9.144 1.00 12.00 C ANISOU 285 CA ASN A 37 1389 1542 1628 132 121 -64 C ATOM 286 C ASN A 37 35.923 19.581 8.879 1.00 11.21 C ANISOU 286 C ASN A 37 1300 1436 1522 140 147 -33 C ATOM 287 O ASN A 37 35.833 20.236 7.834 1.00 12.34 O ANISOU 287 O ASN A 37 1453 1592 1643 164 150 -14 O ATOM 288 CB ASN A 37 33.732 18.455 8.303 1.00 12.61 C ANISOU 288 CB ASN A 37 1456 1642 1692 152 98 -69 C ATOM 289 CG ASN A 37 33.942 18.011 6.865 1.00 17.68 C ANISOU 289 CG ASN A 37 2108 2316 2293 171 85 -72 C ATOM 290 OD1 ASN A 37 33.111 18.288 5.998 1.00 22.85 O ANISOU 290 OD1 ASN A 37 2759 2999 2926 192 64 -68 O ATOM 291 ND2 ASN A 37 35.043 17.333 6.605 1.00 15.95 N ANISOU 291 ND2 ASN A 37 1902 2096 2063 165 97 -80 N ATOM 292 N PHE A 38 36.800 19.862 9.839 1.00 10.36 N ANISOU 292 N PHE A 38 1192 1310 1432 117 168 -29 N ATOM 293 CA PHE A 38 37.849 20.885 9.699 1.00 9.81 C ANISOU 293 CA PHE A 38 1132 1235 1361 114 199 -8 C ATOM 294 C PHE A 38 37.307 22.320 9.771 1.00 10.51 C ANISOU 294 C PHE A 38 1228 1306 1459 119 221 13 C ATOM 295 O PHE A 38 38.001 23.287 9.408 1.00 11.93 O ANISOU 295 O PHE A 38 1422 1478 1635 120 252 33 O ATOM 296 CB PHE A 38 38.651 20.716 8.392 1.00 11.78 C ANISOU 296 CB PHE A 38 1393 1502 1580 134 206 -2 C ATOM 297 CG PHE A 38 39.386 19.395 8.246 1.00 10.69 C ANISOU 297 CG PHE A 38 1247 1375 1437 132 196 -23 C ATOM 298 CD1 PHE A 38 39.908 18.702 9.340 1.00 10.49 C ANISOU 298 CD1 PHE A 38 1208 1343 1435 113 191 -35 C ATOM 299 CD2 PHE A 38 39.596 18.878 6.972 1.00 12.74 C ANISOU 299 CD2 PHE A 38 1518 1654 1669 150 194 -29 C ATOM 300 CE1 PHE A 38 40.602 17.496 9.154 1.00 11.58 C ANISOU 300 CE1 PHE A 38 1341 1487 1574 119 185 -50 C ATOM 301 CE2 PHE A 38 40.291 17.684 6.777 1.00 11.99 C ANISOU 301 CE2 PHE A 38 1418 1564 1575 150 193 -50 C ATOM 302 CZ PHE A 38 40.796 16.989 7.863 1.00 13.25 C ANISOU 302 CZ PHE A 38 1560 1710 1762 138 189 -60 C ATOM 303 N ASN A 39 36.082 22.451 10.260 1.00 10.11 N ANISOU 303 N ASN A 39 1168 1246 1427 120 209 9 N ATOM 304 CA ASN A 39 35.418 23.744 10.386 1.00 9.30 C ANISOU 304 CA ASN A 39 1069 1121 1342 129 231 28 C ATOM 305 C ASN A 39 35.544 24.301 11.799 1.00 10.73 C ANISOU 305 C ASN A 39 1247 1274 1554 91 259 18 C ATOM 306 O ASN A 39 34.975 23.744 12.732 1.00 11.74 O ANISOU 306 O ASN A 39 1362 1398 1699 70 248 -4 O ATOM 307 CB ASN A 39 33.944 23.575 10.006 1.00 13.51 C ANISOU 307 CB ASN A 39 1589 1665 1881 157 202 27 C ATOM 308 CG ASN A 39 33.198 24.897 9.899 1.00 12.64 C ANISOU 308 CG ASN A 39 1480 1533 1790 181 222 53 C ATOM 309 OD1 ASN A 39 33.714 25.952 10.256 1.00 11.16 O ANISOU 309 OD1 ASN A 39 1308 1315 1618 171 263 69 O ATOM 310 ND2 ASN A 39 31.971 24.837 9.390 1.00 16.04 N ANISOU 310 ND2 ASN A 39 1892 1979 2223 213 193 57 N ATOM 311 N THR A 40 36.274 25.401 11.954 1.00 12.16 N ANISOU 311 N THR A 40 1442 1435 1742 78 300 32 N ATOM 312 CA THR A 40 36.434 26.010 13.273 1.00 11.24 C ANISOU 312 CA THR A 40 1325 1295 1652 35 332 19 C ATOM 313 C THR A 40 35.118 26.468 13.887 1.00 10.96 C ANISOU 313 C THR A 40 1282 1235 1647 35 341 13 C ATOM 314 O THR A 40 35.024 26.564 15.108 1.00 12.14 O ANISOU 314 O THR A 40 1428 1371 1814 -6 357 -8 O ATOM 315 CB THR A 40 37.408 27.212 13.265 1.00 9.68 C ANISOU 315 CB THR A 40 1143 1078 1457 16 382 30 C ATOM 316 OG1 THR A 40 36.801 28.331 12.605 1.00 12.38 O ANISOU 316 OG1 THR A 40 1502 1391 1810 47 411 57 O ATOM 317 CG2 THR A 40 38.708 26.847 12.578 1.00 11.86 C ANISOU 317 CG2 THR A 40 1422 1379 1706 16 379 34 C ATOM 318 N GLN A 41 34.106 26.749 13.073 1.00 11.24 N ANISOU 318 N GLN A 41 980 1718 1574 94 249 224 N ATOM 319 CA GLN A 41 32.856 27.289 13.607 1.00 10.69 C ANISOU 319 CA GLN A 41 904 1623 1537 65 251 249 C ATOM 320 C GLN A 41 31.824 26.221 13.972 1.00 12.55 C ANISOU 320 C GLN A 41 1189 1831 1747 54 243 250 C ATOM 321 O GLN A 41 30.700 26.557 14.349 1.00 13.99 O ANISOU 321 O GLN A 41 1360 1997 1957 26 251 264 O ATOM 322 CB GLN A 41 32.244 28.300 12.633 1.00 11.74 C ANISOU 322 CB GLN A 41 1000 1762 1699 35 256 287 C ATOM 323 CG GLN A 41 33.152 29.469 12.330 1.00 11.47 C ANISOU 323 CG GLN A 41 920 1742 1694 33 272 294 C ATOM 324 CD GLN A 41 32.430 30.582 11.615 1.00 12.42 C ANISOU 324 CD GLN A 41 1020 1854 1846 4 270 335 C ATOM 325 OE1 GLN A 41 32.562 30.752 10.399 1.00 16.17 O ANISOU 325 OE1 GLN A 41 1505 2341 2299 -6 274 362 O ATOM 326 NE2 GLN A 41 31.665 31.352 12.360 1.00 11.44 N ANISOU 326 NE2 GLN A 41 872 1708 1769 -5 260 337 N ATOM 327 N ALA A 42 32.198 24.944 13.865 1.00 10.52 N ANISOU 327 N ALA A 42 985 1570 1443 74 228 232 N ATOM 328 CA ALA A 42 31.291 23.857 14.199 1.00 13.04 C ANISOU 328 CA ALA A 42 1359 1856 1741 58 223 235 C ATOM 329 C ALA A 42 30.813 23.931 15.648 1.00 12.57 C ANISOU 329 C ALA A 42 1320 1767 1688 49 242 231 C ATOM 330 O ALA A 42 31.608 24.130 16.563 1.00 11.78 O ANISOU 330 O ALA A 42 1234 1665 1579 82 241 210 O ATOM 331 CB ALA A 42 31.968 22.509 13.949 1.00 14.44 C ANISOU 331 CB ALA A 42 1596 2026 1865 88 196 212 C ATOM 332 N THR A 43 29.514 23.752 15.851 1.00 12.42 N ANISOU 332 N THR A 43 1305 1726 1687 6 260 245 N ATOM 333 CA THR A 43 28.958 23.602 17.192 1.00 12.84 C ANISOU 333 CA THR A 43 1392 1752 1736 -9 290 242 C ATOM 334 C THR A 43 27.959 22.459 17.188 1.00 15.15 C ANISOU 334 C THR A 43 1732 2008 2016 -51 304 249 C ATOM 335 O THR A 43 27.313 22.187 16.176 1.00 15.84 O ANISOU 335 O THR A 43 1795 2097 2126 -76 292 254 O ATOM 336 CB THR A 43 28.216 24.868 17.676 1.00 13.80 C ANISOU 336 CB THR A 43 1448 1886 1910 -30 316 245 C ATOM 337 OG1 THR A 43 27.126 25.151 16.784 1.00 15.71 O ANISOU 337 OG1 THR A 43 1638 2133 2196 -69 315 255 O ATOM 338 CG2 THR A 43 29.142 26.064 17.738 1.00 13.88 C ANISOU 338 CG2 THR A 43 1410 1923 1942 5 302 238 C ATOM 339 N ASN A 44 27.808 21.793 18.321 1.00 13.82 N ANISOU 339 N ASN A 44 1634 1804 1813 -58 329 248 N ATOM 340 CA AASN A 44 26.809 20.747 18.424 0.50 14.36 C ANISOU 340 CA AASN A 44 1748 1832 1877 -110 354 256 C ATOM 341 CA BASN A 44 26.848 20.697 18.435 0.50 15.12 C ANISOU 341 CA BASN A 44 1849 1927 1971 -108 353 256 C ATOM 342 C ASN A 44 26.297 20.660 19.846 1.00 14.30 C ANISOU 342 C ASN A 44 1788 1796 1850 -135 409 261 C ATOM 343 O ASN A 44 27.065 20.616 20.794 1.00 13.34 O ANISOU 343 O ASN A 44 1729 1663 1676 -94 408 258 O ATOM 344 CB AASN A 44 27.369 19.413 17.926 0.50 18.32 C ANISOU 344 CB AASN A 44 2325 2302 2333 -92 314 255 C ATOM 345 CB BASN A 44 27.523 19.359 18.105 0.50 18.72 C ANISOU 345 CB BASN A 44 2390 2349 2374 -85 314 254 C ATOM 346 CG AASN A 44 27.595 19.405 16.418 0.50 19.11 C ANISOU 346 CG AASN A 44 2376 2432 2453 -77 269 249 C ATOM 347 CG BASN A 44 26.524 18.234 17.870 0.50 24.22 C ANISOU 347 CG BASN A 44 3125 3000 3078 -141 328 262 C ATOM 348 OD1AASN A 44 28.733 19.453 15.949 0.50 22.14 O ANISOU 348 OD1AASN A 44 2762 2840 2811 -24 231 237 O ATOM 349 OD1BASN A 44 25.317 18.427 17.967 0.50 25.44 O ANISOU 349 OD1BASN A 44 3237 3148 3280 -201 371 265 O ATOM 350 ND2AASN A 44 26.505 19.366 15.653 0.50 19.04 N ANISOU 350 ND2AASN A 44 2322 2422 2491 -121 273 251 N ATOM 351 ND2BASN A 44 27.034 17.052 17.544 0.50 30.37 N ANISOU 351 ND2BASN A 44 3979 3744 3816 -121 287 259 N ATOM 352 N ARG A 45 24.978 20.671 19.977 1.00 13.55 N ANISOU 352 N ARG A 45 1660 1692 1796 -200 459 263 N ATOM 353 CA ARG A 45 24.322 20.640 21.269 1.00 14.22 C ANISOU 353 CA ARG A 45 1780 1757 1865 -236 528 266 C ATOM 354 C ARG A 45 24.183 19.193 21.703 1.00 16.68 C ANISOU 354 C ARG A 45 2208 2005 2123 -268 551 283 C ATOM 355 O ARG A 45 23.711 18.350 20.933 1.00 19.20 O ANISOU 355 O ARG A 45 2531 2298 2466 -306 541 285 O ATOM 356 CB ARG A 45 22.937 21.271 21.110 1.00 15.79 C ANISOU 356 CB ARG A 45 1879 1978 2142 -296 571 249 C ATOM 357 CG ARG A 45 22.029 21.227 22.309 1.00 21.42 C ANISOU 357 CG ARG A 45 2610 2678 2851 -348 657 245 C ATOM 358 CD ARG A 45 22.583 21.993 23.489 1.00 21.28 C ANISOU 358 CD ARG A 45 2619 2680 2789 -303 676 244 C ATOM 359 NE ARG A 45 23.291 23.231 23.164 1.00 23.14 N ANISOU 359 NE ARG A 45 2783 2961 3050 -240 620 231 N ATOM 360 CZ ARG A 45 22.724 24.386 22.816 1.00 21.65 C ANISOU 360 CZ ARG A 45 2481 2812 2934 -245 614 209 C ATOM 361 NH1 ARG A 45 21.401 24.478 22.690 1.00 26.40 N ANISOU 361 NH1 ARG A 45 3016 3420 3593 -305 656 188 N ATOM 362 NH2 ARG A 45 23.500 25.452 22.572 1.00 22.45 N ANISOU 362 NH2 ARG A 45 2536 2943 3052 -189 563 203 N ATOM 363 N ASN A 46 24.586 18.906 22.935 1.00 16.27 N ANISOU 363 N ASN A 46 2257 1925 2000 -249 579 294 N ATOM 364 CA ASN A 46 24.448 17.572 23.515 1.00 17.99 C ANISOU 364 CA ASN A 46 2607 2071 2157 -281 606 317 C ATOM 365 C ASN A 46 23.131 17.427 24.262 1.00 19.85 C ANISOU 365 C ASN A 46 2848 2287 2408 -369 708 326 C ATOM 366 O ASN A 46 22.531 18.420 24.671 1.00 19.65 O ANISOU 366 O ASN A 46 2742 2306 2419 -386 756 311 O ATOM 367 CB ASN A 46 25.631 17.291 24.440 1.00 20.67 C ANISOU 367 CB ASN A 46 3071 2383 2402 -206 574 323 C ATOM 368 CG ASN A 46 26.952 17.369 23.706 1.00 22.78 C ANISOU 368 CG ASN A 46 3324 2671 2661 -122 478 302 C ATOM 369 OD1 ASN A 46 27.109 16.760 22.652 1.00 31.58 O ANISOU 369 OD1 ASN A 46 4425 3778 3794 -124 433 299 O ATOM 370 ND2 ASN A 46 27.902 18.116 24.250 1.00 25.11 N ANISOU 370 ND2 ASN A 46 3618 2994 2930 -48 447 282 N ATOM 371 N THR A 47 22.682 16.189 24.440 1.00 25.23 N ANISOU 371 N THR A 47 3622 2900 3064 -427 742 348 N ATOM 372 CA THR A 47 21.405 15.938 25.093 1.00 28.04 C ANISOU 372 CA THR A 47 3983 3233 3440 -525 851 356 C ATOM 373 C THR A 47 21.361 16.505 26.513 1.00 25.15 C ANISOU 373 C THR A 47 3665 2878 3011 -517 923 363 C ATOM 374 O THR A 47 20.306 16.930 26.987 1.00 28.02 O ANISOU 374 O THR A 47 3969 3264 3412 -582 1014 350 O ATOM 375 CB THR A 47 21.071 14.429 25.130 1.00 31.80 C ANISOU 375 CB THR A 47 4574 3620 3889 -589 877 384 C ATOM 376 OG1 THR A 47 22.180 13.703 25.674 1.00 37.34 O ANISOU 376 OG1 THR A 47 5439 4266 4484 -527 830 413 O ATOM 377 CG2 THR A 47 20.787 13.916 23.730 1.00 29.17 C ANISOU 377 CG2 THR A 47 4169 3278 3635 -612 819 366 C ATOM 378 N ASP A 48 22.511 16.516 27.182 1.00 22.40 N ANISOU 378 N ASP A 48 3423 2517 2571 -433 878 376 N ATOM 379 CA ASP A 48 22.582 16.980 28.565 1.00 22.28 C ANISOU 379 CA ASP A 48 3476 2507 2482 -410 935 382 C ATOM 380 C ASP A 48 22.572 18.500 28.688 1.00 23.20 C ANISOU 380 C ASP A 48 3461 2707 2645 -369 930 345 C ATOM 381 O ASP A 48 22.589 19.035 29.798 1.00 24.91 O ANISOU 381 O ASP A 48 3715 2939 2810 -345 973 341 O ATOM 382 CB ASP A 48 23.802 16.396 29.291 1.00 22.83 C ANISOU 382 CB ASP A 48 3716 2524 2433 -327 878 401 C ATOM 383 CG ASP A 48 25.124 16.995 28.818 1.00 25.16 C ANISOU 383 CG ASP A 48 3970 2856 2733 -215 761 371 C ATOM 384 OD1 ASP A 48 25.145 17.759 27.831 1.00 20.61 O ANISOU 384 OD1 ASP A 48 3245 2340 2246 -208 724 346 O ATOM 385 OD2 ASP A 48 26.160 16.702 29.445 1.00 31.07 O ANISOU 385 OD2 ASP A 48 4837 3571 3396 -134 706 370 O ATOM 386 N GLY A 49 22.535 19.187 27.550 1.00 18.93 N ANISOU 386 N GLY A 49 2776 2217 2200 -361 877 319 N ATOM 387 CA GLY A 49 22.462 20.636 27.534 1.00 18.75 C ANISOU 387 CA GLY A 49 2626 2266 2233 -328 866 285 C ATOM 388 C GLY A 49 23.792 21.326 27.301 1.00 17.45 C ANISOU 388 C GLY A 49 2446 2127 2057 -227 770 273 C ATOM 389 O GLY A 49 23.818 22.526 27.021 1.00 18.79 O ANISOU 389 O GLY A 49 2503 2350 2288 -201 745 247 O ATOM 390 N SER A 50 24.895 20.586 27.424 1.00 14.91 N ANISOU 390 N SER A 50 2236 1765 1664 -171 715 287 N ATOM 391 CA SER A 50 26.206 21.141 27.104 1.00 14.10 C ANISOU 391 CA SER A 50 2110 1686 1562 -81 624 266 C ATOM 392 C SER A 50 26.346 21.277 25.594 1.00 13.60 C ANISOU 392 C SER A 50 1945 1648 1573 -89 573 261 C ATOM 393 O SER A 50 25.507 20.767 24.845 1.00 13.54 O ANISOU 393 O SER A 50 1908 1631 1604 -155 595 273 O ATOM 394 CB SER A 50 27.332 20.260 27.654 1.00 15.95 C ANISOU 394 CB SER A 50 2490 1869 1702 -14 574 269 C ATOM 395 OG SER A 50 27.366 19.016 26.978 1.00 17.47 O ANISOU 395 OG SER A 50 2745 2015 1878 -40 554 289 O ATOM 396 N THR A 51 27.392 21.970 25.155 1.00 12.01 N ANISOU 396 N THR A 51 1692 1478 1391 -23 506 240 N ATOM 397 CA THR A 51 27.629 22.196 23.735 1.00 10.54 C ANISOU 397 CA THR A 51 1418 1321 1266 -26 461 237 C ATOM 398 C THR A 51 29.092 21.936 23.422 1.00 11.24 C ANISOU 398 C THR A 51 1539 1408 1324 47 390 220 C ATOM 399 O THR A 51 29.952 22.210 24.260 1.00 10.49 O ANISOU 399 O THR A 51 1482 1310 1195 109 366 198 O ATOM 400 CB THR A 51 27.248 23.635 23.331 1.00 10.13 C ANISOU 400 CB THR A 51 1235 1320 1292 -34 464 226 C ATOM 401 OG1 THR A 51 25.871 23.854 23.669 1.00 11.51 O ANISOU 401 OG1 THR A 51 1375 1499 1499 -97 527 229 O ATOM 402 CG2 THR A 51 27.453 23.888 21.843 1.00 12.69 C ANISOU 402 CG2 THR A 51 1483 1670 1668 -38 422 229 C ATOM 403 N ASP A 52 29.354 21.379 22.237 1.00 10.09 N ANISOU 403 N ASP A 52 1378 1265 1192 42 355 223 N ATOM 404 CA ASP A 52 30.715 21.130 21.754 1.00 10.22 C ANISOU 404 CA ASP A 52 1406 1289 1188 106 291 198 C ATOM 405 C ASP A 52 31.099 22.223 20.753 1.00 9.89 C ANISOU 405 C ASP A 52 1246 1303 1210 113 275 189 C ATOM 406 O ASP A 52 30.284 22.626 19.902 1.00 10.65 O ANISOU 406 O ASP A 52 1273 1419 1354 65 294 209 O ATOM 407 CB ASP A 52 30.793 19.785 21.025 1.00 12.78 C ANISOU 407 CB ASP A 52 1792 1583 1482 99 263 204 C ATOM 408 CG ASP A 52 30.413 18.614 21.902 1.00 19.12 C ANISOU 408 CG ASP A 52 2724 2319 2222 85 277 219 C ATOM 409 OD1 ASP A 52 30.664 18.656 23.123 1.00 16.12 O ANISOU 409 OD1 ASP A 52 2416 1915 1795 115 285 214 O ATOM 410 OD2 ASP A 52 29.874 17.632 21.350 1.00 26.43 O ANISOU 410 OD2 ASP A 52 3686 3214 3143 45 278 235 O ATOM 411 N TYR A 53 32.337 22.702 20.835 1.00 10.01 N ANISOU 411 N TYR A 53 1239 1339 1227 173 239 157 N ATOM 412 CA TYR A 53 32.756 23.859 20.048 1.00 9.72 C ANISOU 412 CA TYR A 53 1095 1348 1251 174 234 151 C ATOM 413 C TYR A 53 34.050 23.642 19.295 1.00 10.15 C ANISOU 413 C TYR A 53 1131 1424 1300 216 195 120 C ATOM 414 O TYR A 53 35.020 23.153 19.857 1.00 11.07 O ANISOU 414 O TYR A 53 1294 1528 1384 273 160 79 O ATOM 415 CB TYR A 53 32.973 25.062 20.967 1.00 10.48 C ANISOU 415 CB TYR A 53 1149 1454 1378 196 240 134 C ATOM 416 CG TYR A 53 31.745 25.536 21.675 1.00 9.48 C ANISOU 416 CG TYR A 53 1017 1320 1266 158 282 156 C ATOM 417 CD1 TYR A 53 31.001 26.590 21.165 1.00 10.78 C ANISOU 417 CD1 TYR A 53 1094 1508 1493 118 301 174 C ATOM 418 CD2 TYR A 53 31.334 24.957 22.879 1.00 10.04 C ANISOU 418 CD2 TYR A 53 1172 1357 1283 163 302 155 C ATOM 419 CE1 TYR A 53 29.868 27.046 21.828 1.00 9.53 C ANISOU 419 CE1 TYR A 53 922 1347 1353 87 337 181 C ATOM 420 CE2 TYR A 53 30.208 25.399 23.554 1.00 9.41 C ANISOU 420 CE2 TYR A 53 1082 1277 1215 126 350 168 C ATOM 421 CZ TYR A 53 29.465 26.442 23.023 1.00 9.17 C ANISOU 421 CZ TYR A 53 952 1276 1255 89 366 177 C ATOM 422 OH TYR A 53 28.347 26.891 23.686 1.00 11.38 O ANISOU 422 OH TYR A 53 1212 1560 1553 56 411 179 O ATOM 423 N GLY A 54 34.068 24.043 18.029 1.00 10.26 N ANISOU 423 N GLY A 54 1078 1471 1347 191 201 134 N ATOM 424 CA GLY A 54 35.316 24.186 17.304 1.00 10.18 C ANISOU 424 CA GLY A 54 1027 1494 1345 224 182 102 C ATOM 425 C GLY A 54 35.817 22.935 16.610 1.00 11.71 C ANISOU 425 C GLY A 54 1266 1690 1493 247 153 82 C ATOM 426 O GLY A 54 35.110 21.925 16.506 1.00 11.53 O ANISOU 426 O GLY A 54 1307 1640 1435 232 145 100 O ATOM 427 N ILE A 55 37.047 23.015 16.113 1.00 10.14 N ANISOU 427 N ILE A 55 1028 1524 1300 283 138 39 N ATOM 428 CA ILE A 55 37.601 21.957 15.270 1.00 13.68 C ANISOU 428 CA ILE A 55 1501 1986 1710 308 111 12 C ATOM 429 C ILE A 55 37.708 20.610 15.961 1.00 12.36 C ANISOU 429 C ILE A 55 1433 1774 1488 350 63 -16 C ATOM 430 O ILE A 55 37.658 19.563 15.303 1.00 13.89 O ANISOU 430 O ILE A 55 1669 1964 1647 358 38 -22 O ATOM 431 CB ILE A 55 39.003 22.306 14.716 1.00 17.51 C ANISOU 431 CB ILE A 55 1918 2520 2215 341 110 -43 C ATOM 432 CG1 ILE A 55 39.986 22.644 15.849 1.00 16.71 C ANISOU 432 CG1 ILE A 55 1803 2410 2137 393 85 -104 C ATOM 433 CG2 ILE A 55 38.905 23.403 13.683 1.00 21.79 C ANISOU 433 CG2 ILE A 55 2381 3104 2795 293 161 -7 C ATOM 434 CD1 ILE A 55 41.457 22.606 15.421 1.00 21.25 C ANISOU 434 CD1 ILE A 55 2318 3026 2729 437 72 -182 C ATOM 435 N LEU A 56 37.884 20.635 17.278 1.00 11.53 N ANISOU 435 N LEU A 56 1372 1634 1374 382 46 -35 N ATOM 436 CA LEU A 56 37.949 19.408 18.058 1.00 10.51 C ANISOU 436 CA LEU A 56 1358 1451 1186 422 -1 -56 C ATOM 437 C LEU A 56 36.727 19.231 18.976 1.00 11.36 C ANISOU 437 C LEU A 56 1540 1505 1270 383 25 -2 C ATOM 438 O LEU A 56 36.730 18.388 19.871 1.00 12.57 O ANISOU 438 O LEU A 56 1802 1604 1371 412 -4 -10 O ATOM 439 CB LEU A 56 39.262 19.326 18.850 1.00 12.86 C ANISOU 439 CB LEU A 56 1671 1742 1473 507 -55 -133 C ATOM 440 CG LEU A 56 40.483 19.064 17.957 1.00 12.03 C ANISOU 440 CG LEU A 56 1509 1681 1379 551 -88 -201 C ATOM 441 CD1 LEU A 56 41.770 19.335 18.715 1.00 15.60 C ANISOU 441 CD1 LEU A 56 1941 2138 1849 629 -135 -288 C ATOM 442 CD2 LEU A 56 40.475 17.624 17.445 1.00 14.92 C ANISOU 442 CD2 LEU A 56 1954 2024 1691 573 -134 -214 C ATOM 443 N GLN A 57 35.680 20.028 18.745 1.00 11.15 N ANISOU 443 N GLN A 57 1460 1495 1284 316 81 50 N ATOM 444 CA GLN A 57 34.400 19.826 19.438 1.00 10.78 C ANISOU 444 CA GLN A 57 1468 1406 1223 266 118 97 C ATOM 445 C GLN A 57 34.554 19.665 20.958 1.00 12.17 C ANISOU 445 C GLN A 57 1731 1538 1355 301 111 85 C ATOM 446 O GLN A 57 34.089 18.694 21.570 1.00 13.54 O ANISOU 446 O GLN A 57 2013 1655 1475 293 111 102 O ATOM 447 CB GLN A 57 33.645 18.645 18.821 1.00 11.69 C ANISOU 447 CB GLN A 57 1639 1490 1314 228 115 122 C ATOM 448 CG GLN A 57 33.140 18.965 17.424 1.00 10.94 C ANISOU 448 CG GLN A 57 1460 1434 1262 186 130 142 C ATOM 449 CD GLN A 57 32.046 20.024 17.437 1.00 11.06 C ANISOU 449 CD GLN A 57 1406 1466 1329 128 182 177 C ATOM 450 OE1 GLN A 57 32.295 21.223 17.211 1.00 15.02 O ANISOU 450 OE1 GLN A 57 1827 2009 1872 130 194 177 O ATOM 451 NE2 GLN A 57 30.834 19.591 17.698 1.00 11.45 N ANISOU 451 NE2 GLN A 57 1486 1481 1382 74 211 204 N ATOM 452 N ILE A 58 35.211 20.651 21.551 1.00 10.41 N ANISOU 452 N ILE A 58 1463 1338 1155 341 104 55 N ATOM 453 CA ILE A 58 35.462 20.685 22.983 1.00 11.80 C ANISOU 453 CA ILE A 58 1713 1479 1290 388 91 35 C ATOM 454 C ILE A 58 34.199 21.108 23.736 1.00 10.67 C ANISOU 454 C ILE A 58 1587 1323 1145 333 155 81 C ATOM 455 O ILE A 58 33.494 22.048 23.344 1.00 11.89 O ANISOU 455 O ILE A 58 1647 1513 1359 282 199 105 O ATOM 456 CB ILE A 58 36.674 21.586 23.262 1.00 13.52 C ANISOU 456 CB ILE A 58 1866 1728 1543 455 53 -25 C ATOM 457 CG1 ILE A 58 37.920 20.909 22.673 1.00 14.90 C ANISOU 457 CG1 ILE A 58 2042 1910 1709 513 -10 -83 C ATOM 458 CG2 ILE A 58 36.783 21.936 24.739 1.00 15.38 C ANISOU 458 CG2 ILE A 58 2159 1936 1748 503 43 -45 C ATOM 459 CD1 ILE A 58 39.179 21.756 22.712 1.00 18.49 C ANISOU 459 CD1 ILE A 58 2408 2401 2216 570 -43 -153 C ATOM 460 N ASN A 59 33.901 20.370 24.800 1.00 12.17 N ANISOU 460 N ASN A 59 1925 1139 1561 -4 23 317 N ATOM 461 CA ASN A 59 32.604 20.436 25.461 1.00 14.63 C ANISOU 461 CA ASN A 59 2195 1490 1873 -6 138 378 C ATOM 462 C ASN A 59 32.572 21.424 26.622 1.00 16.99 C ANISOU 462 C ASN A 59 2455 1927 2072 126 140 295 C ATOM 463 O ASN A 59 33.524 21.512 27.405 1.00 18.53 O ANISOU 463 O ASN A 59 2705 2205 2133 262 108 248 O ATOM 464 CB ASN A 59 32.234 19.038 25.952 1.00 18.19 C ANISOU 464 CB ASN A 59 2738 1914 2257 2 266 533 C ATOM 465 CG ASN A 59 30.845 18.967 26.519 1.00 26.90 C ANISOU 465 CG ASN A 59 3802 3044 3377 -21 395 608 C ATOM 466 OD1 ASN A 59 30.668 18.861 27.728 1.00 32.70 O ANISOU 466 OD1 ASN A 59 4571 3871 3984 90 476 641 O ATOM 467 ND2 ASN A 59 29.845 19.025 25.650 1.00 30.83 N ANISOU 467 ND2 ASN A 59 4224 3462 4029 -165 415 635 N ATOM 468 N SER A 60 31.456 22.140 26.744 1.00 13.47 N ANISOU 468 N SER A 60 1916 1508 1694 88 180 278 N ATOM 469 CA SER A 60 31.268 23.140 27.779 1.00 14.11 C ANISOU 469 CA SER A 60 1946 1715 1699 200 187 197 C ATOM 470 C SER A 60 31.025 22.575 29.173 1.00 15.61 C ANISOU 470 C SER A 60 2201 1998 1731 321 306 273 C ATOM 471 O SER A 60 30.995 23.341 30.118 1.00 18.76 O ANISOU 471 O SER A 60 2571 2512 2047 430 311 203 O ATOM 472 CB SER A 60 30.098 24.057 27.407 1.00 13.91 C ANISOU 472 CB SER A 60 1798 1682 1806 115 193 156 C ATOM 473 OG SER A 60 28.881 23.312 27.356 1.00 14.55 O ANISOU 473 OG SER A 60 1871 1716 1942 31 315 278 O ATOM 474 N ARG A 61 30.838 21.267 29.307 1.00 16.24 N ANISOU 474 N ARG A 61 2369 2031 1771 303 403 412 N ATOM 475 CA ARG A 61 30.567 20.709 30.630 1.00 18.86 C ANISOU 475 CA ARG A 61 2769 2448 1950 414 524 493 C ATOM 476 C ARG A 61 31.806 20.830 31.503 1.00 20.37 C ANISOU 476 C ARG A 61 3034 2735 1972 582 469 432 C ATOM 477 O ARG A 61 31.703 21.070 32.704 1.00 19.15 O ANISOU 477 O ARG A 61 2895 2696 1687 707 522 423 O ATOM 478 CB ARG A 61 30.101 19.257 30.551 1.00 26.11 C ANISOU 478 CB ARG A 61 3770 3285 2867 353 642 659 C ATOM 479 CG ARG A 61 30.174 18.568 31.895 1.00 35.50 C ANISOU 479 CG ARG A 61 5059 4555 3874 486 749 742 C ATOM 480 CD ARG A 61 29.064 17.566 32.114 1.00 43.92 C ANISOU 480 CD ARG A 61 6158 5575 4955 420 909 896 C ATOM 481 NE ARG A 61 28.690 17.534 33.526 1.00 49.04 N ANISOU 481 NE ARG A 61 6843 6338 5452 541 1018 934 N ATOM 482 CZ ARG A 61 29.466 17.064 34.498 1.00 54.33 C ANISOU 482 CZ ARG A 61 7626 7076 5942 686 1037 965 C ATOM 483 NH1 ARG A 61 30.668 16.580 34.216 1.00 59.06 N ANISOU 483 NH1 ARG A 61 8309 7640 6493 729 952 960 N ATOM 484 NH2 ARG A 61 29.045 17.084 35.754 1.00 52.79 N ANISOU 484 NH2 ARG A 61 7458 6986 5613 790 1139 1000 N ATOM 485 N TRP A 62 32.978 20.694 30.892 1.00 17.17 N ANISOU 485 N TRP A 62 2668 2285 1569 586 359 385 N ATOM 486 CA TRP A 62 34.228 20.729 31.641 1.00 17.45 C ANISOU 486 CA TRP A 62 2776 2405 1450 742 299 325 C ATOM 487 C TRP A 62 35.199 21.825 31.240 1.00 16.39 C ANISOU 487 C TRP A 62 2585 2299 1345 770 147 159 C ATOM 488 O TRP A 62 35.934 22.336 32.081 1.00 16.79 O ANISOU 488 O TRP A 62 2649 2456 1273 911 102 73 O ATOM 489 CB TRP A 62 34.963 19.393 31.503 1.00 18.16 C ANISOU 489 CB TRP A 62 2990 2430 1479 756 313 423 C ATOM 490 CG TRP A 62 34.345 18.314 32.285 1.00 21.41 C ANISOU 490 CG TRP A 62 3488 2847 1800 789 458 575 C ATOM 491 CD1 TRP A 62 33.601 17.282 31.805 1.00 28.19 C ANISOU 491 CD1 TRP A 62 4379 3601 2730 676 552 714 C ATOM 492 CD2 TRP A 62 34.399 18.151 33.707 1.00 25.01 C ANISOU 492 CD2 TRP A 62 4011 3419 2074 945 529 606 C ATOM 493 NE1 TRP A 62 33.192 16.479 32.840 1.00 29.72 N ANISOU 493 NE1 TRP A 62 4658 3835 2800 749 682 831 N ATOM 494 CE2 TRP A 62 33.673 16.988 34.018 1.00 29.19 C ANISOU 494 CE2 TRP A 62 4615 3903 2572 916 670 770 C ATOM 495 CE3 TRP A 62 34.997 18.873 34.745 1.00 25.94 C ANISOU 495 CE3 TRP A 62 4132 3673 2051 1107 488 510 C ATOM 496 CZ2 TRP A 62 33.523 16.529 35.326 1.00 32.49 C ANISOU 496 CZ2 TRP A 62 5116 4407 2821 1043 773 845 C ATOM 497 CZ3 TRP A 62 34.852 18.413 36.046 1.00 32.02 C ANISOU 497 CZ3 TRP A 62 4984 4533 2651 1236 586 581 C ATOM 498 CH2 TRP A 62 34.120 17.254 36.322 1.00 32.11 C ANISOU 498 CH2 TRP A 62 5073 4495 2632 1203 728 749 C ATOM 499 N TRP A 63 35.224 22.179 29.960 1.00 15.09 N ANISOU 499 N TRP A 63 2358 2039 1338 638 69 114 N ATOM 500 CA TRP A 63 36.434 22.794 29.418 1.00 14.05 C ANISOU 500 CA TRP A 63 2210 1903 1225 655 -74 -16 C ATOM 501 C TRP A 63 36.364 24.278 29.133 1.00 13.81 C ANISOU 501 C TRP A 63 2064 1905 1276 636 -161 -162 C ATOM 502 O TRP A 63 37.381 24.960 29.192 1.00 16.51 O ANISOU 502 O TRP A 63 2395 2294 1585 704 -264 -287 O ATOM 503 CB TRP A 63 36.919 22.017 28.182 1.00 13.07 C ANISOU 503 CB TRP A 63 2126 1647 1193 540 -119 27 C ATOM 504 CG TRP A 63 37.098 20.557 28.500 1.00 13.80 C ANISOU 504 CG TRP A 63 2337 1706 1198 571 -40 164 C ATOM 505 CD1 TRP A 63 36.311 19.519 28.077 1.00 15.83 C ANISOU 505 CD1 TRP A 63 2629 1870 1515 469 53 306 C ATOM 506 CD2 TRP A 63 38.097 19.980 29.349 1.00 14.50 C ANISOU 506 CD2 TRP A 63 2527 1858 1124 717 -46 172 C ATOM 507 NE1 TRP A 63 36.766 18.336 28.604 1.00 16.07 N ANISOU 507 NE1 TRP A 63 2778 1897 1432 540 107 403 N ATOM 508 CE2 TRP A 63 37.851 18.589 29.404 1.00 15.12 C ANISOU 508 CE2 TRP A 63 2702 1873 1171 696 47 326 C ATOM 509 CE3 TRP A 63 39.162 20.508 30.094 1.00 15.26 C ANISOU 509 CE3 TRP A 63 2641 2059 1099 867 -122 62 C ATOM 510 CZ2 TRP A 63 38.654 17.715 30.134 1.00 17.71 C ANISOU 510 CZ2 TRP A 63 3147 2233 1350 819 63 375 C ATOM 511 CZ3 TRP A 63 39.953 19.643 30.820 1.00 18.00 C ANISOU 511 CZ3 TRP A 63 3100 2443 1297 990 -107 107 C ATOM 512 CH2 TRP A 63 39.695 18.257 30.844 1.00 18.64 C ANISOU 512 CH2 TRP A 63 3279 2455 1347 968 -16 265 C ATOM 513 N CYS A 64 35.175 24.786 28.827 1.00 13.26 N ANISOU 513 N CYS A 64 1910 1813 1317 544 -121 -150 N ATOM 514 CA CYS A 64 35.045 26.192 28.465 1.00 13.92 C ANISOU 514 CA CYS A 64 1883 1914 1492 515 -204 -284 C ATOM 515 C CYS A 64 33.753 26.743 29.013 1.00 13.60 C ANISOU 515 C CYS A 64 1768 1925 1475 514 -125 -272 C ATOM 516 O CYS A 64 32.834 25.979 29.354 1.00 14.10 O ANISOU 516 O CYS A 64 1854 1979 1523 491 -5 -150 O ATOM 517 CB CYS A 64 35.104 26.379 26.944 1.00 13.19 C ANISOU 517 CB CYS A 64 1748 1695 1567 359 -284 -307 C ATOM 518 SG CYS A 64 33.767 25.573 26.005 1.00 12.46 S ANISOU 518 SG CYS A 64 1640 1478 1618 184 -198 -164 S ATOM 519 N ASN A 65 33.677 28.068 29.121 1.00 13.05 N ANISOU 519 N ASN A 65 1607 1909 1442 539 -189 -400 N ATOM 520 CA ASN A 65 32.461 28.688 29.604 1.00 13.69 C ANISOU 520 CA ASN A 65 1608 2040 1554 537 -123 -403 C ATOM 521 C ASN A 65 31.592 29.238 28.489 1.00 13.50 C ANISOU 521 C ASN A 65 1490 1923 1716 387 -151 -416 C ATOM 522 O ASN A 65 32.061 30.054 27.689 1.00 12.21 O ANISOU 522 O ASN A 65 1279 1718 1642 340 -264 -516 O ATOM 523 CB ASN A 65 32.752 29.835 30.564 1.00 14.15 C ANISOU 523 CB ASN A 65 1618 2225 1532 669 -162 -534 C ATOM 524 CG ASN A 65 31.475 30.510 31.002 1.00 17.93 C ANISOU 524 CG ASN A 65 2007 2751 2053 662 -97 -543 C ATOM 525 OD1 ASN A 65 30.572 29.850 31.511 1.00 16.53 O ANISOU 525 OD1 ASN A 65 1846 2590 1843 659 25 -436 O ATOM 526 ND2 ASN A 65 31.349 31.805 30.721 1.00 20.05 N ANISOU 526 ND2 ASN A 65 2178 3031 2409 647 -177 -668 N ATOM 527 N ASP A 66 30.332 28.807 28.453 1.00 13.39 N ANISOU 527 N ASP A 66 1448 1879 1759 315 -48 -317 N ATOM 528 CA ASP A 66 29.353 29.382 27.531 1.00 12.81 C ANISOU 528 CA ASP A 66 1278 1733 1858 185 -67 -331 C ATOM 529 C ASP A 66 28.151 30.020 28.238 1.00 13.80 C ANISOU 529 C ASP A 66 1318 1929 1996 210 5 -346 C ATOM 530 O ASP A 66 27.235 30.520 27.581 1.00 13.93 O ANISOU 530 O ASP A 66 1247 1894 2151 112 -4 -358 O ATOM 531 CB ASP A 66 28.907 28.368 26.455 1.00 12.34 C ANISOU 531 CB ASP A 66 1243 1541 1903 37 -35 -214 C ATOM 532 CG ASP A 66 28.098 27.189 27.005 1.00 13.41 C ANISOU 532 CG ASP A 66 1425 1678 1991 30 114 -68 C ATOM 533 OD1 ASP A 66 27.736 27.165 28.207 1.00 14.57 O ANISOU 533 OD1 ASP A 66 1580 1927 2029 131 203 -49 O ATOM 534 OD2 ASP A 66 27.808 26.262 26.204 1.00 13.10 O ANISOU 534 OD2 ASP A 66 1417 1536 2027 -82 145 30 O ATOM 535 N GLY A 67 28.151 30.002 29.569 1.00 14.83 N ANISOU 535 N GLY A 67 1473 2180 1983 343 76 -346 N ATOM 536 CA GLY A 67 27.106 30.650 30.350 1.00 15.75 C ANISOU 536 CA GLY A 67 1510 2379 2096 383 144 -371 C ATOM 537 C GLY A 67 25.765 29.947 30.361 1.00 16.47 C ANISOU 537 C GLY A 67 1581 2438 2240 304 275 -251 C ATOM 538 O GLY A 67 24.805 30.441 30.958 1.00 18.90 O ANISOU 538 O GLY A 67 1816 2809 2556 326 340 -268 O ATOM 539 N ARG A 68 25.676 28.796 29.698 1.00 16.23 N ANISOU 539 N ARG A 68 1609 2309 2250 209 317 -133 N ATOM 540 CA ARG A 68 24.393 28.097 29.611 1.00 16.89 C ANISOU 540 CA ARG A 68 1668 2350 2399 119 440 -19 C ATOM 541 C ARG A 68 24.537 26.595 29.844 1.00 19.95 C ANISOU 541 C ARG A 68 2169 2704 2706 114 541 126 C ATOM 542 O ARG A 68 23.747 25.802 29.325 1.00 19.19 O ANISOU 542 O ARG A 68 2072 2527 2694 3 615 228 O ATOM 543 CB ARG A 68 23.691 28.381 28.270 1.00 15.96 C ANISOU 543 CB ARG A 68 1467 2119 2480 -38 388 -28 C ATOM 544 CG ARG A 68 24.427 27.853 27.027 1.00 21.48 C ANISOU 544 CG ARG A 68 2217 2696 3250 -133 303 -2 C ATOM 545 CD ARG A 68 23.838 26.513 26.539 1.00 37.50 C ANISOU 545 CD ARG A 68 4289 4631 5329 -241 397 143 C ATOM 546 NE ARG A 68 22.526 26.690 25.922 1.00 43.54 N ANISOU 546 NE ARG A 68 4956 5341 6247 -359 430 162 N ATOM 547 CZ ARG A 68 21.608 25.735 25.766 1.00 36.23 C ANISOU 547 CZ ARG A 68 4032 4361 5371 -444 540 277 C ATOM 548 NH1 ARG A 68 21.820 24.489 26.186 1.00 19.13 N ANISOU 548 NH1 ARG A 68 1967 2185 3117 -428 635 392 N ATOM 549 NH2 ARG A 68 20.452 26.037 25.187 1.00 41.36 N ANISOU 549 NH2 ARG A 68 4582 4967 6166 -546 555 274 N ATOM 550 N THR A 69 25.540 26.202 30.628 1.00 15.90 N ANISOU 550 N THR A 69 1811 2639 1590 357 474 -112 N ATOM 551 CA THR A 69 25.715 24.784 30.954 1.00 16.08 C ANISOU 551 CA THR A 69 1846 2687 1578 312 549 25 C ATOM 552 C THR A 69 25.748 24.598 32.471 1.00 17.34 C ANISOU 552 C THR A 69 2029 2984 1577 361 606 48 C ATOM 553 O THR A 69 26.814 24.601 33.078 1.00 19.41 O ANISOU 553 O THR A 69 2354 3262 1758 393 555 58 O ATOM 554 CB THR A 69 26.979 24.194 30.292 1.00 15.12 C ANISOU 554 CB THR A 69 1773 2469 1504 268 486 93 C ATOM 555 OG1 THR A 69 26.999 24.543 28.898 1.00 14.11 O ANISOU 555 OG1 THR A 69 1631 2229 1502 239 431 60 O ATOM 556 CG2 THR A 69 27.005 22.668 30.413 1.00 15.43 C ANISOU 556 CG2 THR A 69 1814 2508 1541 217 547 230 C ATOM 557 N PRO A 70 24.574 24.429 33.085 1.00 18.40 N ANISOU 557 N PRO A 70 2110 3220 1662 373 713 56 N ATOM 558 CA PRO A 70 24.507 24.357 34.547 1.00 19.84 C ANISOU 558 CA PRO A 70 2316 3553 1668 433 778 73 C ATOM 559 C PRO A 70 25.471 23.361 35.181 1.00 23.14 C ANISOU 559 C PRO A 70 2814 3984 1995 423 784 200 C ATOM 560 O PRO A 70 25.622 22.224 34.719 1.00 28.47 O ANISOU 560 O PRO A 70 3494 4587 2737 346 810 325 O ATOM 561 CB PRO A 70 23.063 23.931 34.796 1.00 26.98 C ANISOU 561 CB PRO A 70 3136 4539 2576 409 921 109 C ATOM 562 CG PRO A 70 22.313 24.585 33.680 1.00 22.64 C ANISOU 562 CG PRO A 70 2515 3906 2182 391 883 6 C ATOM 563 CD PRO A 70 23.229 24.468 32.480 1.00 18.93 C ANISOU 563 CD PRO A 70 2089 3275 1831 344 774 24 C ATOM 564 N GLY A 71 26.139 23.810 36.236 1.00 20.87 N ANISOU 564 N GLY A 71 2589 3781 1559 510 743 156 N ATOM 565 CA GLY A 71 26.954 22.929 37.045 1.00 23.50 C ANISOU 565 CA GLY A 71 3006 4146 1776 522 747 264 C ATOM 566 C GLY A 71 28.273 22.578 36.396 1.00 20.84 C ANISOU 566 C GLY A 71 2722 3675 1523 487 632 286 C ATOM 567 O GLY A 71 29.031 21.771 36.933 1.00 27.79 O ANISOU 567 O GLY A 71 3673 4556 2329 491 615 372 O ATOM 568 N SER A 72 28.553 23.180 35.243 1.00 20.53 N ANISOU 568 N SER A 72 2648 3521 1632 454 553 209 N ATOM 569 CA SER A 72 29.756 22.878 34.481 1.00 19.16 C ANISOU 569 CA SER A 72 2505 3224 1551 413 458 225 C ATOM 570 C SER A 72 30.981 23.573 35.059 1.00 23.89 C ANISOU 570 C SER A 72 3160 3823 2096 488 344 135 C ATOM 571 O SER A 72 30.878 24.370 35.996 1.00 25.80 O ANISOU 571 O SER A 72 3416 4154 2233 579 327 49 O ATOM 572 CB SER A 72 29.573 23.291 33.014 1.00 21.49 C ANISOU 572 CB SER A 72 2744 3406 2014 354 427 183 C ATOM 573 OG SER A 72 29.604 24.706 32.859 1.00 20.61 O ANISOU 573 OG SER A 72 2617 3285 1930 401 362 49 O ATOM 574 N ARG A 73 32.138 23.239 34.499 1.00 20.91 N ANISOU 574 N ARG A 73 2805 3344 1794 454 264 148 N ATOM 575 CA ARG A 73 33.389 23.907 34.808 1.00 17.15 C ANISOU 575 CA ARG A 73 2363 2836 1318 510 146 53 C ATOM 576 C ARG A 73 33.944 24.559 33.547 1.00 17.25 C ANISOU 576 C ARG A 73 2330 2728 1495 458 83 -4 C ATOM 577 O ARG A 73 33.371 24.429 32.459 1.00 19.69 O ANISOU 577 O ARG A 73 2597 2987 1899 388 128 34 O ATOM 578 CB ARG A 73 34.405 22.901 35.356 1.00 17.73 C ANISOU 578 CB ARG A 73 2503 2900 1334 521 103 114 C ATOM 579 CG ARG A 73 33.902 22.160 36.569 1.00 19.92 C ANISOU 579 CG ARG A 73 2839 3290 1440 567 170 198 C ATOM 580 CD ARG A 73 33.942 23.034 37.817 1.00 22.88 C ANISOU 580 CD ARG A 73 3251 3770 1670 694 135 98 C ATOM 581 NE ARG A 73 35.313 23.313 38.227 1.00 23.54 N ANISOU 581 NE ARG A 73 3383 3811 1752 761 -2 11 N ATOM 582 CZ ARG A 73 36.044 22.501 38.983 1.00 27.49 C ANISOU 582 CZ ARG A 73 3966 4324 2156 804 -45 58 C ATOM 583 NH1 ARG A 73 35.525 21.367 39.433 1.00 30.03 N ANISOU 583 NH1 ARG A 73 4338 4701 2370 782 43 205 N ATOM 584 NH2 ARG A 73 37.287 22.827 39.301 1.00 30.56 N ANISOU 584 NH2 ARG A 73 4386 4663 2564 870 -181 -43 N ATOM 585 N ASN A 74 35.063 25.256 33.712 1.00 17.29 N ANISOU 585 N ASN A 74 2345 2688 1536 496 -22 -94 N ATOM 586 CA ASN A 74 35.749 25.968 32.643 1.00 16.05 C ANISOU 586 CA ASN A 74 2147 2419 1531 450 -81 -145 C ATOM 587 C ASN A 74 37.250 25.751 32.837 1.00 15.69 C ANISOU 587 C ASN A 74 2119 2320 1520 461 -170 -174 C ATOM 588 O ASN A 74 37.997 26.682 33.148 1.00 17.31 O ANISOU 588 O ASN A 74 2314 2492 1773 507 -260 -277 O ATOM 589 CB ASN A 74 35.394 27.465 32.700 1.00 15.52 C ANISOU 589 CB ASN A 74 2049 2345 1503 494 -126 -257 C ATOM 590 CG ASN A 74 36.143 28.304 31.662 1.00 14.91 C ANISOU 590 CG ASN A 74 1933 2145 1587 444 -189 -299 C ATOM 591 OD1 ASN A 74 36.722 27.780 30.716 1.00 14.40 O ANISOU 591 OD1 ASN A 74 1857 2014 1600 371 -173 -238 O ATOM 592 ND2 ASN A 74 36.105 29.626 31.833 1.00 16.68 N ANISOU 592 ND2 ASN A 74 2134 2343 1863 487 -259 -403 N ATOM 593 N LEU A 75 37.696 24.511 32.658 1.00 14.99 N ANISOU 593 N LEU A 75 2053 2220 1423 422 -154 -91 N ATOM 594 CA LEU A 75 39.068 24.148 33.055 1.00 16.72 C ANISOU 594 CA LEU A 75 2296 2403 1655 447 -243 -126 C ATOM 595 C LEU A 75 40.139 24.728 32.129 1.00 16.70 C ANISOU 595 C LEU A 75 2236 2299 1812 402 -301 -186 C ATOM 596 O LEU A 75 41.306 24.861 32.520 1.00 18.69 O ANISOU 596 O LEU A 75 2486 2512 2102 435 -390 -259 O ATOM 597 CB LEU A 75 39.221 22.631 33.165 1.00 17.04 C ANISOU 597 CB LEU A 75 2377 2456 1642 423 -223 -25 C ATOM 598 CG LEU A 75 38.391 21.985 34.276 1.00 18.48 C ANISOU 598 CG LEU A 75 2625 2735 1661 471 -173 47 C ATOM 599 CD1 LEU A 75 38.515 20.474 34.232 1.00 22.37 C ANISOU 599 CD1 LEU A 75 3152 3215 2131 431 -159 162 C ATOM 600 CD2 LEU A 75 38.792 22.529 35.644 1.00 21.68 C ANISOU 600 CD2 LEU A 75 3086 3200 1951 587 -242 -37 C ATOM 601 N CYS A 76 39.743 25.088 30.911 1.00 14.59 N ANISOU 601 N CYS A 76 1920 1986 1637 329 -248 -157 N ATOM 602 CA CYS A 76 40.669 25.734 29.984 1.00 14.96 C ANISOU 602 CA CYS A 76 1911 1944 1829 280 -282 -198 C ATOM 603 C CYS A 76 40.682 27.246 30.157 1.00 15.89 C ANISOU 603 C CYS A 76 2002 2025 2011 308 -331 -287 C ATOM 604 O CYS A 76 41.446 27.948 29.495 1.00 17.11 O ANISOU 604 O CYS A 76 2107 2098 2296 268 -360 -319 O ATOM 605 CB CYS A 76 40.337 25.347 28.544 1.00 14.36 C ANISOU 605 CB CYS A 76 1806 1838 1814 197 -208 -117 C ATOM 606 SG CYS A 76 40.715 23.609 28.214 1.00 14.42 S ANISOU 606 SG CYS A 76 1824 1860 1796 166 -190 -40 S ATOM 607 N ASN A 77 39.827 27.748 31.046 1.00 15.79 N ANISOU 607 N ASN A 77 2016 2072 1910 378 -339 -326 N ATOM 608 CA ASN A 77 39.793 29.184 31.357 1.00 17.27 C ANISOU 608 CA ASN A 77 2178 2228 2157 423 -408 -429 C ATOM 609 C ASN A 77 39.598 30.044 30.112 1.00 16.26 C ANISOU 609 C ASN A 77 2005 2014 2159 348 -389 -411 C ATOM 610 O ASN A 77 40.335 31.006 29.880 1.00 17.98 O ANISOU 610 O ASN A 77 2181 2143 2506 336 -456 -468 O ATOM 611 CB ASN A 77 41.076 29.599 32.085 1.00 20.27 C ANISOU 611 CB ASN A 77 2543 2564 2596 478 -525 -532 C ATOM 612 CG ASN A 77 41.314 28.793 33.345 1.00 33.15 C ANISOU 612 CG ASN A 77 4233 4276 4087 567 -559 -555 C ATOM 613 OD1 ASN A 77 40.533 28.856 34.290 1.00 40.78 O ANISOU 613 OD1 ASN A 77 5242 5336 4917 649 -556 -577 O ATOM 614 ND2 ASN A 77 42.401 28.030 33.365 1.00 36.73 N ANISOU 614 ND2 ASN A 77 4689 4697 4568 554 -594 -551 N ATOM 615 N ILE A 78 38.602 29.683 29.307 1.00 14.68 N ANISOU 615 N ILE A 78 1815 1834 1930 300 -300 -329 N ATOM 616 CA ILE A 78 38.281 30.409 28.085 1.00 14.15 C ANISOU 616 CA ILE A 78 1724 1691 1961 239 -278 -301 C ATOM 617 C ILE A 78 36.779 30.444 27.842 1.00 14.79 C ANISOU 617 C ILE A 78 1823 1816 1980 247 -222 -276 C ATOM 618 O ILE A 78 36.052 29.518 28.223 1.00 14.66 O ANISOU 618 O ILE A 78 1828 1882 1860 264 -164 -238 O ATOM 619 CB ILE A 78 38.915 29.755 26.822 1.00 14.80 C ANISOU 619 CB ILE A 78 1792 1727 2105 153 -223 -213 C ATOM 620 CG1 ILE A 78 38.640 28.245 26.779 1.00 16.41 C ANISOU 620 CG1 ILE A 78 2019 1999 2217 145 -159 -141 C ATOM 621 CG2 ILE A 78 40.400 30.083 26.722 1.00 18.24 C ANISOU 621 CG2 ILE A 78 2186 2093 2652 126 -274 -244 C ATOM 622 CD1 ILE A 78 39.021 27.598 25.454 1.00 18.01 C ANISOU 622 CD1 ILE A 78 2205 2170 2469 77 -108 -66 C ATOM 623 N PRO A 79 36.303 31.503 27.185 1.00 13.65 N ANISOU 623 N PRO A 79 1668 1608 1910 232 -243 -297 N ATOM 624 CA PRO A 79 34.941 31.452 26.648 1.00 13.43 C ANISOU 624 CA PRO A 79 1653 1602 1847 229 -191 -270 C ATOM 625 C PRO A 79 34.906 30.417 25.532 1.00 12.32 C ANISOU 625 C PRO A 79 1522 1452 1708 167 -113 -167 C ATOM 626 O PRO A 79 35.865 30.306 24.761 1.00 12.34 O ANISOU 626 O PRO A 79 1517 1399 1772 116 -109 -122 O ATOM 627 CB PRO A 79 34.730 32.850 26.065 1.00 14.54 C ANISOU 627 CB PRO A 79 1787 1651 2088 222 -252 -313 C ATOM 628 CG PRO A 79 36.109 33.382 25.808 1.00 15.97 C ANISOU 628 CG PRO A 79 1948 1743 2377 183 -303 -309 C ATOM 629 CD PRO A 79 37.052 32.703 26.762 1.00 14.23 C ANISOU 629 CD PRO A 79 1716 1572 2117 207 -315 -332 C ATOM 630 N CYS A 80 33.823 29.652 25.443 1.00 12.01 N ANISOU 630 N CYS A 80 1490 1469 1606 175 -52 -134 N ATOM 631 CA CYS A 80 33.709 28.651 24.390 1.00 11.35 C ANISOU 631 CA CYS A 80 1409 1373 1530 131 6 -50 C ATOM 632 C CYS A 80 33.825 29.292 23.002 1.00 11.12 C ANISOU 632 C CYS A 80 1389 1258 1578 96 -2 -26 C ATOM 633 O CYS A 80 34.301 28.665 22.052 1.00 11.66 O ANISOU 633 O CYS A 80 1459 1307 1666 61 27 36 O ATOM 634 CB CYS A 80 32.388 27.875 24.520 1.00 11.22 C ANISOU 634 CB CYS A 80 1388 1414 1462 148 62 -32 C ATOM 635 SG CYS A 80 32.234 26.923 26.077 1.00 11.68 S ANISOU 635 SG CYS A 80 1443 1581 1415 180 97 -22 S ATOM 636 N SER A 81 33.401 30.543 22.877 1.00 11.80 N ANISOU 636 N SER A 81 1484 1294 1705 111 -48 -75 N ATOM 637 CA SER A 81 33.509 31.234 21.590 1.00 11.85 C ANISOU 637 CA SER A 81 1512 1213 1778 79 -59 -40 C ATOM 638 C SER A 81 34.946 31.303 21.069 1.00 11.56 C ANISOU 638 C SER A 81 1466 1131 1793 27 -54 11 C ATOM 639 O SER A 81 35.167 31.343 19.853 1.00 14.51 O ANISOU 639 O SER A 81 1859 1462 2192 -5 -26 75 O ATOM 640 CB SER A 81 32.905 32.630 21.691 1.00 13.83 C ANISOU 640 CB SER A 81 1775 1406 2074 105 -128 -105 C ATOM 641 OG SER A 81 33.641 33.417 22.612 1.00 15.01 O ANISOU 641 OG SER A 81 1901 1538 2263 114 -191 -163 O ATOM 642 N ALA A 82 35.920 31.307 21.971 1.00 13.31 N ANISOU 642 N ALA A 82 1659 1367 2031 23 -79 -19 N ATOM 643 CA ALA A 82 37.318 31.339 21.553 1.00 14.48 C ANISOU 643 CA ALA A 82 1782 1476 2245 -28 -73 17 C ATOM 644 C ALA A 82 37.679 30.101 20.754 1.00 13.66 C ANISOU 644 C ALA A 82 1675 1412 2104 -53 -5 85 C ATOM 645 O ALA A 82 38.649 30.116 19.992 1.00 15.47 O ANISOU 645 O ALA A 82 1884 1613 2380 -99 22 128 O ATOM 646 CB ALA A 82 38.243 31.460 22.753 1.00 16.13 C ANISOU 646 CB ALA A 82 1957 1693 2480 -13 -125 -48 C ATOM 647 N LEU A 83 36.913 29.029 20.942 1.00 13.44 N ANISOU 647 N LEU A 83 1658 1449 1998 -24 22 92 N ATOM 648 CA LEU A 83 37.154 27.764 20.250 1.00 13.42 C ANISOU 648 CA LEU A 83 1648 1484 1966 -35 67 143 C ATOM 649 C LEU A 83 36.622 27.779 18.825 1.00 13.20 C ANISOU 649 C LEU A 83 1645 1433 1938 -38 101 192 C ATOM 650 O LEU A 83 36.779 26.797 18.100 1.00 14.40 O ANISOU 650 O LEU A 83 1788 1614 2068 -36 130 227 O ATOM 651 CB LEU A 83 36.527 26.604 21.022 1.00 14.34 C ANISOU 651 CB LEU A 83 1765 1666 2019 -4 73 138 C ATOM 652 CG LEU A 83 37.116 26.350 22.406 1.00 14.82 C ANISOU 652 CG LEU A 83 1815 1760 2054 10 42 101 C ATOM 653 CD1 LEU A 83 36.257 25.354 23.179 1.00 14.50 C ANISOU 653 CD1 LEU A 83 1786 1782 1943 39 58 114 C ATOM 654 CD2 LEU A 83 38.554 25.858 22.278 1.00 14.97 C ANISOU 654 CD2 LEU A 83 1806 1774 2106 -16 29 105 C ATOM 655 N LEU A 84 35.978 28.874 18.429 1.00 12.64 N ANISOU 655 N LEU A 84 1605 1309 1887 -33 86 189 N ATOM 656 CA LEU A 84 35.425 28.983 17.077 1.00 12.83 C ANISOU 656 CA LEU A 84 1668 1306 1901 -23 107 232 C ATOM 657 C LEU A 84 36.286 29.850 16.163 1.00 13.13 C ANISOU 657 C LEU A 84 1720 1290 1978 -63 123 286 C ATOM 658 O LEU A 84 35.982 30.002 14.973 1.00 15.47 O ANISOU 658 O LEU A 84 2059 1565 2253 -52 144 333 O ATOM 659 CB LEU A 84 33.994 29.547 17.119 1.00 13.27 C ANISOU 659 CB LEU A 84 1758 1334 1950 19 73 194 C ATOM 660 CG LEU A 84 33.012 28.753 17.989 1.00 14.31 C ANISOU 660 CG LEU A 84 1868 1521 2049 55 72 147 C ATOM 661 CD1 LEU A 84 31.637 29.390 17.878 1.00 16.55 C ANISOU 661 CD1 LEU A 84 2175 1775 2340 95 42 99 C ATOM 662 CD2 LEU A 84 32.934 27.286 17.610 1.00 12.77 C ANISOU 662 CD2 LEU A 84 1652 1373 1827 65 106 177 C ATOM 663 N SER A 85 37.344 30.435 16.715 1.00 13.86 N ANISOU 663 N SER A 85 1778 1356 2131 -108 114 280 N ATOM 664 CA SER A 85 38.202 31.343 15.972 1.00 14.76 C ANISOU 664 CA SER A 85 1892 1409 2306 -160 135 338 C ATOM 665 C SER A 85 38.893 30.696 14.771 1.00 15.31 C ANISOU 665 C SER A 85 1957 1519 2343 -178 212 410 C ATOM 666 O SER A 85 39.143 29.490 14.769 1.00 15.44 O ANISOU 666 O SER A 85 1943 1610 2314 -160 235 396 O ATOM 667 CB SER A 85 39.271 31.909 16.906 1.00 15.43 C ANISOU 667 CB SER A 85 1920 1461 2483 -201 105 303 C ATOM 668 OG SER A 85 40.143 32.772 16.204 1.00 19.42 O ANISOU 668 OG SER A 85 2411 1900 3069 -262 133 366 O ATOM 669 N SER A 86 39.205 31.504 13.760 1.00 17.30 N ANISOU 669 N SER A 86 2237 1723 2615 -210 248 487 N ATOM 670 CA SER A 86 40.039 31.028 12.658 1.00 15.57 C ANISOU 670 CA SER A 86 2002 1552 2361 -230 332 557 C ATOM 671 C SER A 86 41.448 30.677 13.151 1.00 19.31 C ANISOU 671 C SER A 86 2382 2056 2899 -281 362 537 C ATOM 672 O SER A 86 42.148 29.880 12.531 1.00 20.79 O ANISOU 672 O SER A 86 2533 2315 3051 -283 422 555 O ATOM 673 CB SER A 86 40.088 32.051 11.526 1.00 17.98 C ANISOU 673 CB SER A 86 2363 1799 2668 -256 374 658 C ATOM 674 OG SER A 86 40.536 33.307 11.993 1.00 22.81 O ANISOU 674 OG SER A 86 2958 2313 3397 -322 348 677 O ATOM 675 N ASP A 87 41.852 31.273 14.271 1.00 15.14 N ANISOU 675 N ASP A 87 1812 1473 2467 -314 310 486 N ATOM 676 CA ASP A 87 43.144 31.006 14.905 1.00 16.32 C ANISOU 676 CA ASP A 87 1871 1636 2695 -354 314 443 C ATOM 677 C ASP A 87 42.938 29.832 15.867 1.00 14.10 C ANISOU 677 C ASP A 87 1575 1421 2361 -302 265 358 C ATOM 678 O ASP A 87 42.118 29.921 16.795 1.00 15.71 O ANISOU 678 O ASP A 87 1811 1612 2547 -263 200 307 O ATOM 679 CB ASP A 87 43.597 32.265 15.658 1.00 17.15 C ANISOU 679 CB ASP A 87 1944 1639 2936 -398 261 420 C ATOM 680 CG ASP A 87 44.936 32.101 16.373 1.00 23.83 C ANISOU 680 CG ASP A 87 2690 2480 3883 -432 249 359 C ATOM 681 OD1 ASP A 87 45.312 30.979 16.741 1.00 20.25 O ANISOU 681 OD1 ASP A 87 2206 2102 3386 -405 246 305 O ATOM 682 OD2 ASP A 87 45.619 33.126 16.588 1.00 29.48 O ANISOU 682 OD2 ASP A 87 3356 3106 4737 -485 230 360 O ATOM 683 N ILE A 88 43.624 28.714 15.620 1.00 14.72 N ANISOU 683 N ILE A 88 1610 1573 2411 -297 297 345 N ATOM 684 CA ILE A 88 43.370 27.491 16.385 1.00 14.15 C ANISOU 684 CA ILE A 88 1535 1558 2284 -248 250 283 C ATOM 685 C ILE A 88 44.074 27.420 17.733 1.00 14.55 C ANISOU 685 C ILE A 88 1543 1593 2392 -250 185 203 C ATOM 686 O ILE A 88 43.936 26.417 18.430 1.00 13.93 O ANISOU 686 O ILE A 88 1469 1558 2266 -211 143 161 O ATOM 687 CB ILE A 88 43.684 26.192 15.590 1.00 13.19 C ANISOU 687 CB ILE A 88 1389 1518 2104 -225 285 290 C ATOM 688 CG1 ILE A 88 45.189 26.012 15.349 1.00 15.61 C ANISOU 688 CG1 ILE A 88 1610 1848 2474 -266 318 271 C ATOM 689 CG2 ILE A 88 42.889 26.161 14.281 1.00 16.93 C ANISOU 689 CG2 ILE A 88 1914 2015 2505 -198 334 356 C ATOM 690 CD1 ILE A 88 45.544 24.619 14.855 1.00 18.73 C ANISOU 690 CD1 ILE A 88 1971 2327 2819 -230 322 245 C ATOM 691 N THR A 89 44.785 28.482 18.109 1.00 14.48 N ANISOU 691 N THR A 89 1497 1517 2488 -290 168 184 N ATOM 692 CA THR A 89 45.545 28.467 19.360 1.00 15.85 C ANISOU 692 CA THR A 89 1628 1671 2724 -280 94 94 C ATOM 693 C THR A 89 44.714 28.025 20.571 1.00 15.76 C ANISOU 693 C THR A 89 1670 1687 2633 -213 22 43 C ATOM 694 O THR A 89 45.127 27.136 21.308 1.00 15.23 O ANISOU 694 O THR A 89 1592 1655 2539 -182 -20 -8 O ATOM 695 CB THR A 89 46.171 29.837 19.662 1.00 16.68 C ANISOU 695 CB THR A 89 1689 1682 2968 -320 65 72 C ATOM 696 OG1 THR A 89 47.012 30.222 18.570 1.00 18.38 O ANISOU 696 OG1 THR A 89 1846 1873 3263 -391 146 132 O ATOM 697 CG2 THR A 89 47.005 29.767 20.946 1.00 20.67 C ANISOU 697 CG2 THR A 89 2147 2166 3540 -293 -25 -39 C ATOM 698 N ALA A 90 43.550 28.634 20.782 1.00 13.27 N ANISOU 698 N ALA A 90 1411 1355 2277 -189 10 57 N ATOM 699 CA ALA A 90 42.728 28.266 21.935 1.00 13.63 C ANISOU 699 CA ALA A 90 1499 1438 2240 -126 -41 14 C ATOM 700 C ALA A 90 42.315 26.797 21.915 1.00 14.09 C ANISOU 700 C ALA A 90 1582 1571 2203 -101 -20 40 C ATOM 701 O ALA A 90 42.394 26.105 22.935 1.00 13.82 O ANISOU 701 O ALA A 90 1559 1570 2121 -64 -62 4 O ATOM 702 CB ALA A 90 41.511 29.164 22.057 1.00 14.91 C ANISOU 702 CB ALA A 90 1707 1579 2380 -105 -52 17 C ATOM 703 N SER A 91 41.882 26.304 20.762 1.00 12.79 N ANISOU 703 N SER A 91 1425 1426 2009 -117 38 102 N ATOM 704 CA SER A 91 41.497 24.898 20.667 1.00 12.75 C ANISOU 704 CA SER A 91 1431 1476 1936 -93 46 123 C ATOM 705 C SER A 91 42.671 23.963 20.947 1.00 11.25 C ANISOU 705 C SER A 91 1202 1309 1765 -95 16 92 C ATOM 706 O SER A 91 42.526 22.957 21.637 1.00 12.75 O ANISOU 706 O SER A 91 1408 1528 1909 -66 -20 84 O ATOM 707 CB SER A 91 40.916 24.591 19.295 1.00 13.66 C ANISOU 707 CB SER A 91 1555 1603 2031 -96 99 179 C ATOM 708 OG SER A 91 39.581 25.069 19.238 1.00 12.03 O ANISOU 708 OG SER A 91 1394 1384 1794 -76 109 197 O ATOM 709 N VAL A 92 43.831 24.295 20.399 1.00 12.55 N ANISOU 709 N VAL A 92 1313 1455 2002 -130 29 75 N ATOM 710 CA VAL A 92 45.009 23.463 20.612 1.00 12.96 C ANISOU 710 CA VAL A 92 1315 1524 2084 -130 -6 27 C ATOM 711 C VAL A 92 45.425 23.458 22.085 1.00 12.43 C ANISOU 711 C VAL A 92 1260 1441 2023 -100 -89 -41 C ATOM 712 O VAL A 92 45.644 22.390 22.666 1.00 13.99 O ANISOU 712 O VAL A 92 1468 1662 2183 -69 -141 -64 O ATOM 713 CB VAL A 92 46.183 23.906 19.716 1.00 11.90 C ANISOU 713 CB VAL A 92 1106 1378 2036 -178 37 17 C ATOM 714 CG1 VAL A 92 47.444 23.163 20.104 1.00 14.48 C ANISOU 714 CG1 VAL A 92 1373 1717 2411 -173 -13 -58 C ATOM 715 CG2 VAL A 92 45.845 23.658 18.252 1.00 14.42 C ANISOU 715 CG2 VAL A 92 1422 1736 2320 -189 115 82 C ATOM 716 N ASN A 93 45.525 24.632 22.701 1.00 13.17 N ANISOU 716 N ASN A 93 1353 1489 2160 -101 -111 -75 N ATOM 717 CA ASN A 93 45.908 24.680 24.105 1.00 14.33 C ANISOU 717 CA ASN A 93 1516 1625 2305 -53 -198 -151 C ATOM 718 C ASN A 93 44.939 23.920 24.986 1.00 13.70 C ANISOU 718 C ASN A 93 1512 1594 2101 1 -222 -128 C ATOM 719 O ASN A 93 45.351 23.252 25.938 1.00 15.43 O ANISOU 719 O ASN A 93 1754 1827 2282 44 -288 -168 O ATOM 720 CB ASN A 93 46.007 26.118 24.597 1.00 17.03 C ANISOU 720 CB ASN A 93 1845 1910 2716 -50 -229 -198 C ATOM 721 CG ASN A 93 47.140 26.874 23.949 1.00 22.62 C ANISOU 721 CG ASN A 93 2468 2555 3571 -107 -217 -223 C ATOM 722 OD1 ASN A 93 48.012 26.280 23.311 1.00 24.38 O ANISOU 722 OD1 ASN A 93 2636 2788 3839 -141 -191 -225 O ATOM 723 ND2 ASN A 93 47.127 28.193 24.098 1.00 25.22 N ANISOU 723 ND2 ASN A 93 2779 2819 3984 -119 -236 -244 N ATOM 724 N CYS A 94 43.652 24.028 24.677 1.00 12.00 N ANISOU 724 N CYS A 94 1335 1401 1824 -1 -167 -64 N ATOM 725 CA CYS A 94 42.651 23.320 25.468 1.00 14.17 C ANISOU 725 CA CYS A 94 1669 1724 1989 40 -170 -32 C ATOM 726 C CYS A 94 42.731 21.811 25.216 1.00 14.02 C ANISOU 726 C CYS A 94 1655 1731 1941 37 -172 12 C ATOM 727 O CYS A 94 42.675 21.009 26.158 1.00 12.85 O ANISOU 727 O CYS A 94 1547 1606 1728 71 -212 19 O ATOM 728 CB CYS A 94 41.250 23.864 25.184 1.00 13.28 C ANISOU 728 CB CYS A 94 1582 1624 1839 39 -112 12 C ATOM 729 SG CYS A 94 40.000 23.270 26.345 1.00 13.85 S ANISOU 729 SG CYS A 94 1713 1761 1788 88 -102 44 S ATOM 730 N ALA A 95 42.890 21.421 23.952 1.00 13.17 N ANISOU 730 N ALA A 95 1508 1617 1879 0 -136 40 N ATOM 731 CA ALA A 95 43.081 20.005 23.624 1.00 11.82 C ANISOU 731 CA ALA A 95 1328 1463 1701 2 -158 63 C ATOM 732 C ALA A 95 44.278 19.389 24.359 1.00 11.18 C ANISOU 732 C ALA A 95 1239 1374 1634 22 -242 6 C ATOM 733 O ALA A 95 44.238 18.232 24.772 1.00 12.86 O ANISOU 733 O ALA A 95 1477 1595 1813 43 -289 26 O ATOM 734 CB ALA A 95 43.215 19.823 22.128 1.00 12.39 C ANISOU 734 CB ALA A 95 1351 1538 1819 -25 -116 80 C ATOM 735 N LYS A 96 45.353 20.149 24.528 1.00 12.63 N ANISOU 735 N LYS A 96 1387 1533 1880 18 -269 -69 N ATOM 736 CA LYS A 96 46.503 19.635 25.277 1.00 12.79 C ANISOU 736 CA LYS A 96 1399 1538 1922 46 -361 -142 C ATOM 737 C LYS A 96 46.126 19.309 26.725 1.00 13.02 C ANISOU 737 C LYS A 96 1511 1576 1858 103 -422 -138 C ATOM 738 O LYS A 96 46.575 18.300 27.281 1.00 14.80 O ANISOU 738 O LYS A 96 1765 1800 2058 134 -497 -150 O ATOM 739 CB LYS A 96 47.684 20.617 25.235 1.00 13.39 C ANISOU 739 CB LYS A 96 1410 1576 2102 31 -380 -232 C ATOM 740 CG LYS A 96 48.285 20.787 23.842 1.00 15.19 C ANISOU 740 CG LYS A 96 1550 1804 2418 -25 -317 -234 C ATOM 741 CD LYS A 96 49.391 21.832 23.849 1.00 15.35 C ANISOU 741 CD LYS A 96 1496 1778 2558 -51 -324 -310 C ATOM 742 CE LYS A 96 50.110 21.872 22.506 1.00 16.46 C ANISOU 742 CE LYS A 96 1544 1931 2779 -107 -251 -307 C ATOM 743 NZ LYS A 96 51.119 22.973 22.449 1.00 22.65 N ANISOU 743 NZ LYS A 96 2245 2662 3698 -147 -240 -363 N ATOM 744 N LYS A 97 45.312 20.167 27.341 1.00 14.35 N ANISOU 744 N LYS A 97 1833 1534 2085 201 -257 -408 N ATOM 745 CA LYS A 97 44.810 19.876 28.678 1.00 15.00 C ANISOU 745 CA LYS A 97 1966 1681 2052 232 -245 -435 C ATOM 746 C LYS A 97 43.936 18.618 28.674 1.00 15.72 C ANISOU 746 C LYS A 97 2069 1827 2078 226 -181 -362 C ATOM 747 O LYS A 97 44.097 17.732 29.520 1.00 15.08 O ANISOU 747 O LYS A 97 2025 1795 1910 235 -185 -341 O ATOM 748 CB LYS A 97 44.019 21.064 29.229 1.00 16.15 C ANISOU 748 CB LYS A 97 2121 1828 2186 265 -227 -511 C ATOM 749 CG LYS A 97 44.839 22.224 29.690 1.00 27.28 C ANISOU 749 CG LYS A 97 3535 3198 3631 279 -294 -598 C ATOM 750 CD LYS A 97 44.021 23.058 30.680 1.00 37.07 C ANISOU 750 CD LYS A 97 4804 4466 4813 323 -276 -675 C ATOM 751 CE LYS A 97 44.911 23.958 31.524 1.00 43.90 C ANISOU 751 CE LYS A 97 5688 5312 5681 343 -352 -771 C ATOM 752 NZ LYS A 97 45.652 24.938 30.671 1.00 48.61 N ANISOU 752 NZ LYS A 97 6241 5819 6410 319 -394 -799 N ATOM 753 N ILE A 98 43.027 18.535 27.709 1.00 14.18 N ANISOU 753 N ILE A 98 1841 1621 1927 212 -123 -321 N ATOM 754 CA ILE A 98 42.084 17.417 27.653 1.00 13.96 C ANISOU 754 CA ILE A 98 1817 1639 1848 205 -59 -255 C ATOM 755 C ILE A 98 42.808 16.083 27.502 1.00 13.92 C ANISOU 755 C ILE A 98 1819 1642 1827 180 -76 -190 C ATOM 756 O ILE A 98 42.531 15.122 28.218 1.00 14.41 O ANISOU 756 O ILE A 98 1913 1753 1810 185 -54 -156 O ATOM 757 CB ILE A 98 41.077 17.598 26.509 1.00 13.42 C ANISOU 757 CB ILE A 98 1704 1553 1843 191 -2 -226 C ATOM 758 CG1 ILE A 98 40.188 18.805 26.788 1.00 13.92 C ANISOU 758 CG1 ILE A 98 1764 1618 1908 221 26 -285 C ATOM 759 CG2 ILE A 98 40.242 16.332 26.322 1.00 15.21 C ANISOU 759 CG2 ILE A 98 1928 1820 2032 176 57 -155 C ATOM 760 CD1 ILE A 98 39.326 19.211 25.604 1.00 16.26 C ANISOU 760 CD1 ILE A 98 2011 1890 2278 212 72 -265 C ATOM 761 N VAL A 99 43.744 16.022 26.562 1.00 13.11 N ANISOU 761 N VAL A 99 1687 1491 1802 154 -116 -170 N ATOM 762 CA VAL A 99 44.462 14.779 26.280 1.00 13.17 C ANISOU 762 CA VAL A 99 1698 1501 1806 130 -133 -108 C ATOM 763 C VAL A 99 45.416 14.371 27.411 1.00 14.63 C ANISOU 763 C VAL A 99 1926 1711 1922 144 -184 -121 C ATOM 764 O VAL A 99 45.903 13.230 27.441 1.00 15.05 O ANISOU 764 O VAL A 99 1991 1777 1951 132 -193 -67 O ATOM 765 CB VAL A 99 45.201 14.870 24.925 1.00 12.08 C ANISOU 765 CB VAL A 99 1513 1306 1770 103 -159 -84 C ATOM 766 CG1 VAL A 99 46.454 15.712 25.054 1.00 14.78 C ANISOU 766 CG1 VAL A 99 1852 1611 2154 107 -231 -132 C ATOM 767 CG2 VAL A 99 45.523 13.489 24.375 1.00 13.05 C ANISOU 767 CG2 VAL A 99 1631 1434 1895 79 -153 -12 C ATOM 768 N SER A 100 45.671 15.295 28.336 1.00 14.72 N ANISOU 768 N SER A 100 1961 1731 1902 172 -219 -192 N ATOM 769 CA SER A 100 46.501 15.008 29.504 1.00 15.97 C ANISOU 769 CA SER A 100 2161 1921 1984 192 -270 -214 C ATOM 770 C SER A 100 45.665 14.548 30.703 1.00 17.52 C ANISOU 770 C SER A 100 2403 2189 2065 223 -229 -210 C ATOM 771 O SER A 100 46.211 14.281 31.773 1.00 22.98 O ANISOU 771 O SER A 100 3133 2919 2678 247 -264 -226 O ATOM 772 CB SER A 100 47.307 16.253 29.893 1.00 17.08 C ANISOU 772 CB SER A 100 2302 2035 2154 207 -337 -299 C ATOM 773 OG SER A 100 48.136 16.695 28.829 1.00 20.09 O ANISOU 773 OG SER A 100 2639 2350 2644 179 -374 -299 O ATOM 774 N ASP A 101 44.346 14.487 30.524 1.00 17.78 N ANISOU 774 N ASP A 101 2429 2240 2086 225 -155 -190 N ATOM 775 CA ASP A 101 43.403 14.330 31.641 1.00 21.16 C ANISOU 775 CA ASP A 101 2894 2735 2412 259 -109 -196 C ATOM 776 C ASP A 101 43.375 12.921 32.236 1.00 24.00 C ANISOU 776 C ASP A 101 3284 3143 2692 260 -85 -124 C ATOM 777 O ASP A 101 42.920 12.726 33.367 1.00 24.19 O ANISOU 777 O ASP A 101 3346 3227 2617 294 -62 -128 O ATOM 778 CB ASP A 101 41.990 14.747 31.198 1.00 22.99 C ANISOU 778 CB ASP A 101 3102 2969 2665 259 -36 -195 C ATOM 779 CG ASP A 101 40.992 14.787 32.345 1.00 31.52 C ANISOU 779 CG ASP A 101 4216 4116 3644 298 13 -210 C ATOM 780 OD1 ASP A 101 41.217 15.536 33.320 1.00 33.66 O ANISOU 780 OD1 ASP A 101 4518 4411 3861 336 -18 -279 O ATOM 781 OD2 ASP A 101 39.968 14.076 32.260 1.00 35.64 O ANISOU 781 OD2 ASP A 101 4732 4667 4142 291 83 -154 O ATOM 782 N GLY A 102 43.854 11.943 31.477 1.00 20.82 N ANISOU 782 N GLY A 102 2864 2714 2333 226 -90 -58 N ATOM 783 CA GLY A 102 43.916 10.578 31.973 1.00 21.95 C ANISOU 783 CA GLY A 102 3034 2893 2412 225 -71 13 C ATOM 784 C GLY A 102 43.623 9.518 30.919 1.00 19.99 C ANISOU 784 C GLY A 102 2756 2616 2222 184 -32 92 C ATOM 785 O GLY A 102 44.266 8.471 30.902 1.00 18.87 O ANISOU 785 O GLY A 102 2625 2472 2073 172 -48 146 O ATOM 786 N ASN A 103 42.668 9.788 30.031 1.00 20.09 N ANISOU 786 N ASN A 103 2732 2609 2294 164 16 96 N ATOM 787 CA ASN A 103 42.239 8.781 29.064 1.00 16.75 C ANISOU 787 CA ASN A 103 2279 2164 1921 127 57 165 C ATOM 788 C ASN A 103 42.752 9.055 27.664 1.00 14.92 C ANISOU 788 C ASN A 103 2003 1873 1794 98 27 161 C ATOM 789 O ASN A 103 42.305 8.438 26.695 1.00 13.68 O ANISOU 789 O ASN A 103 1813 1695 1689 69 60 204 O ATOM 790 CB ASN A 103 40.718 8.638 29.057 1.00 18.80 C ANISOU 790 CB ASN A 103 2526 2451 2166 125 138 186 C ATOM 791 CG ASN A 103 40.180 8.169 30.390 1.00 23.88 C ANISOU 791 CG ASN A 103 3211 3156 2706 153 176 206 C ATOM 792 OD1 ASN A 103 39.158 8.663 30.868 1.00 32.68 O ANISOU 792 OD1 ASN A 103 4327 4305 3784 173 223 186 O ATOM 793 ND2 ASN A 103 40.891 7.239 31.025 1.00 26.33 N ANISOU 793 ND2 ASN A 103 3555 3483 2968 158 156 248 N ATOM 794 N GLY A 104 43.708 9.965 27.557 1.00 14.23 N ANISOU 794 N GLY A 104 1912 1758 1738 106 -34 110 N ATOM 795 CA GLY A 104 44.290 10.242 26.262 1.00 12.83 C ANISOU 795 CA GLY A 104 1691 1526 1657 81 -63 110 C ATOM 796 C GLY A 104 43.236 10.714 25.277 1.00 13.23 C ANISOU 796 C GLY A 104 1699 1561 1767 69 -14 108 C ATOM 797 O GLY A 104 42.318 11.461 25.626 1.00 12.54 O ANISOU 797 O GLY A 104 1612 1493 1659 87 19 73 O ATOM 798 N MET A 105 43.355 10.267 24.037 1.00 12.53 N ANISOU 798 N MET A 105 1573 1440 1747 43 -11 144 N ATOM 799 CA MET A 105 42.463 10.761 23.001 1.00 10.77 C ANISOU 799 CA MET A 105 1306 1204 1584 34 28 140 C ATOM 800 C MET A 105 41.101 10.081 23.031 1.00 12.17 C ANISOU 800 C MET A 105 1478 1414 1734 27 98 173 C ATOM 801 O MET A 105 40.200 10.479 22.289 1.00 11.53 O ANISOU 801 O MET A 105 1360 1329 1691 23 135 168 O ATOM 802 CB MET A 105 43.099 10.690 21.609 1.00 11.39 C ANISOU 802 CB MET A 105 1342 1239 1748 14 4 161 C ATOM 803 CG MET A 105 44.145 11.773 21.395 1.00 10.59 C ANISOU 803 CG MET A 105 1230 1101 1693 23 -53 121 C ATOM 804 SD MET A 105 44.595 12.000 19.649 1.00 11.88 S ANISOU 804 SD MET A 105 1334 1219 1961 8 -65 143 S ATOM 805 CE MET A 105 43.114 12.819 19.025 1.00 12.75 C ANISOU 805 CE MET A 105 1409 1336 2099 16 -5 126 C ATOM 806 N ASN A 106 40.935 9.090 23.907 1.00 11.97 N ANISOU 806 N ASN A 106 1486 1419 1641 26 117 206 N ATOM 807 CA ASN A 106 39.616 8.478 24.102 1.00 11.37 C ANISOU 807 CA ASN A 106 1407 1377 1538 19 186 237 C ATOM 808 C ASN A 106 38.591 9.518 24.568 1.00 12.44 C ANISOU 808 C ASN A 106 1540 1539 1647 44 223 193 C ATOM 809 O ASN A 106 37.390 9.281 24.464 1.00 14.74 O ANISOU 809 O ASN A 106 1812 1853 1934 38 282 211 O ATOM 810 CB ASN A 106 39.677 7.311 25.091 1.00 13.46 C ANISOU 810 CB ASN A 106 1711 1670 1732 19 200 282 C ATOM 811 CG ASN A 106 40.583 6.202 24.617 1.00 15.49 C ANISOU 811 CG ASN A 106 1970 1899 2017 -4 170 329 C ATOM 812 OD1 ASN A 106 41.658 5.980 25.181 1.00 19.28 O ANISOU 812 OD1 ASN A 106 2482 2378 2467 6 124 332 O ATOM 813 ND2 ASN A 106 40.163 5.500 23.572 1.00 12.06 N ANISOU 813 ND2 ASN A 106 1499 1444 1639 -33 195 363 N ATOM 814 N ALA A 107 39.061 10.648 25.104 1.00 12.01 N ANISOU 814 N ALA A 107 1503 1482 1577 71 187 135 N ATOM 815 CA ALA A 107 38.155 11.735 25.472 1.00 13.28 C ANISOU 815 CA ALA A 107 1660 1663 1721 97 218 88 C ATOM 816 C ALA A 107 37.289 12.148 24.285 1.00 12.55 C ANISOU 816 C ALA A 107 1516 1554 1700 85 253 89 C ATOM 817 O ALA A 107 36.143 12.580 24.467 1.00 17.55 O ANISOU 817 O ALA A 107 2138 2214 2318 99 303 74 O ATOM 818 CB ALA A 107 38.941 12.926 26.013 1.00 14.56 C ANISOU 818 CB ALA A 107 1844 1811 1877 124 165 20 C ATOM 819 N TRP A 108 37.834 12.032 23.078 1.00 12.06 N ANISOU 819 N TRP A 108 1419 1450 1712 63 227 105 N ATOM 820 CA TRP A 108 37.075 12.300 21.866 1.00 12.65 C ANISOU 820 CA TRP A 108 1441 1512 1852 52 257 113 C ATOM 821 C TRP A 108 36.444 11.003 21.391 1.00 13.80 C ANISOU 821 C TRP A 108 1568 1673 2002 24 296 169 C ATOM 822 O TRP A 108 37.122 10.160 20.809 1.00 13.80 O ANISOU 822 O TRP A 108 1562 1653 2030 1 271 203 O ATOM 823 CB TRP A 108 37.978 12.901 20.791 1.00 12.65 C ANISOU 823 CB TRP A 108 1413 1464 1930 48 211 102 C ATOM 824 CG TRP A 108 38.389 14.309 21.079 1.00 11.91 C ANISOU 824 CG TRP A 108 1326 1349 1852 73 181 45 C ATOM 825 CD1 TRP A 108 37.692 15.448 20.758 1.00 12.51 C ANISOU 825 CD1 TRP A 108 1377 1418 1960 93 203 11 C ATOM 826 CD2 TRP A 108 39.579 14.746 21.754 1.00 12.44 C ANISOU 826 CD2 TRP A 108 1424 1395 1908 83 123 12 C ATOM 827 NE1 TRP A 108 38.378 16.558 21.190 1.00 11.66 N ANISOU 827 NE1 TRP A 108 1283 1281 1864 112 163 -41 N ATOM 828 CE2 TRP A 108 39.532 16.155 21.810 1.00 11.82 C ANISOU 828 CE2 TRP A 108 1338 1295 1859 106 112 -43 C ATOM 829 CE3 TRP A 108 40.672 14.083 22.327 1.00 12.05 C ANISOU 829 CE3 TRP A 108 1408 1344 1827 75 78 23 C ATOM 830 CZ2 TRP A 108 40.536 16.912 22.404 1.00 11.65 C ANISOU 830 CZ2 TRP A 108 1338 1247 1840 119 57 -90 C ATOM 831 CZ3 TRP A 108 41.670 14.836 22.917 1.00 11.58 C ANISOU 831 CZ3 TRP A 108 1370 1265 1766 89 22 -22 C ATOM 832 CH2 TRP A 108 41.596 16.239 22.947 1.00 12.19 C ANISOU 832 CH2 TRP A 108 1437 1318 1878 109 11 -80 C ATOM 833 N VAL A 109 35.155 10.828 21.659 1.00 16.43 N ANISOU 833 N VAL A 109 1199 2713 2332 -224 -100 -550 N ATOM 834 CA VAL A 109 34.487 9.586 21.268 1.00 17.81 C ANISOU 834 CA VAL A 109 1462 2877 2426 -296 -86 -498 C ATOM 835 C VAL A 109 34.667 9.282 19.769 1.00 18.82 C ANISOU 835 C VAL A 109 1698 2883 2570 -282 -97 -435 C ATOM 836 O VAL A 109 34.918 8.134 19.402 1.00 16.86 O ANISOU 836 O VAL A 109 1564 2585 2256 -303 -83 -366 O ATOM 837 CB VAL A 109 33.003 9.554 21.716 1.00 20.05 C ANISOU 837 CB VAL A 109 1670 3263 2685 -365 -97 -553 C ATOM 838 CG1 VAL A 109 32.323 8.278 21.246 1.00 21.70 C ANISOU 838 CG1 VAL A 109 1975 3450 2819 -441 -98 -483 C ATOM 839 CG2 VAL A 109 32.918 9.659 23.238 1.00 22.88 C ANISOU 839 CG2 VAL A 109 1938 3755 2999 -385 -73 -607 C ATOM 840 N ALA A 110 34.581 10.297 18.910 1.00 16.39 N ANISOU 840 N ALA A 110 1359 2523 2346 -246 -130 -461 N ATOM 841 CA ALA A 110 34.783 10.084 17.472 1.00 16.96 C ANISOU 841 CA ALA A 110 1536 2481 2427 -236 -139 -402 C ATOM 842 C ALA A 110 36.195 9.603 17.151 1.00 14.60 C ANISOU 842 C ALA A 110 1323 2122 2101 -185 -98 -334 C ATOM 843 O ALA A 110 36.373 8.811 16.225 1.00 13.88 O ANISOU 843 O ALA A 110 1349 1958 1966 -186 -86 -277 O ATOM 844 CB ALA A 110 34.448 11.331 16.667 1.00 17.93 C ANISOU 844 CB ALA A 110 1605 2561 2645 -220 -194 -442 C ATOM 845 N TRP A 111 37.202 10.083 17.885 1.00 13.38 N ANISOU 845 N TRP A 111 1112 1994 1977 -136 -80 -343 N ATOM 846 CA TRP A 111 38.548 9.529 17.712 1.00 11.58 C ANISOU 846 CA TRP A 111 957 1714 1728 -90 -38 -281 C ATOM 847 C TRP A 111 38.558 8.041 18.058 1.00 11.96 C ANISOU 847 C TRP A 111 1099 1762 1684 -125 -16 -246 C ATOM 848 O TRP A 111 39.076 7.224 17.297 1.00 13.20 O ANISOU 848 O TRP A 111 1362 1852 1803 -106 2 -195 O ATOM 849 CB TRP A 111 39.606 10.274 18.540 1.00 13.49 C ANISOU 849 CB TRP A 111 1120 1977 2028 -35 -32 -292 C ATOM 850 CG TRP A 111 40.972 9.628 18.411 1.00 11.10 C ANISOU 850 CG TRP A 111 887 1621 1712 10 11 -230 C ATOM 851 CD1 TRP A 111 41.896 9.852 17.432 1.00 11.57 C ANISOU 851 CD1 TRP A 111 978 1619 1801 60 33 -183 C ATOM 852 CD2 TRP A 111 41.550 8.626 19.278 1.00 11.89 C ANISOU 852 CD2 TRP A 111 1030 1724 1765 3 34 -212 C ATOM 853 NE1 TRP A 111 43.006 9.064 17.635 1.00 11.91 N ANISOU 853 NE1 TRP A 111 1073 1628 1823 95 73 -144 N ATOM 854 CE2 TRP A 111 42.809 8.294 18.750 1.00 10.24 C ANISOU 854 CE2 TRP A 111 875 1448 1569 59 67 -162 C ATOM 855 CE3 TRP A 111 41.107 7.969 20.431 1.00 12.85 C ANISOU 855 CE3 TRP A 111 1151 1901 1832 -51 25 -234 C ATOM 856 CZ2 TRP A 111 43.645 7.363 19.352 1.00 12.63 C ANISOU 856 CZ2 TRP A 111 1226 1725 1848 68 83 -139 C ATOM 857 CZ3 TRP A 111 41.939 7.035 21.023 1.00 12.07 C ANISOU 857 CZ3 TRP A 111 1110 1775 1702 -52 35 -203 C ATOM 858 CH2 TRP A 111 43.194 6.745 20.486 1.00 12.50 C ANISOU 858 CH2 TRP A 111 1216 1750 1785 10 60 -160 C ATOM 859 N ARG A 112 38.000 7.683 19.212 1.00 13.59 N ANISOU 859 N ARG A 112 1267 2046 1852 -176 -24 -273 N ATOM 860 CA ARG A 112 37.978 6.276 19.605 1.00 13.89 C ANISOU 860 CA ARG A 112 1391 2084 1802 -224 -24 -234 C ATOM 861 C ARG A 112 37.246 5.425 18.564 1.00 13.16 C ANISOU 861 C ARG A 112 1402 1940 1660 -257 -46 -194 C ATOM 862 O ARG A 112 37.719 4.350 18.178 1.00 14.34 O ANISOU 862 O ARG A 112 1662 2028 1758 -250 -53 -145 O ATOM 863 CB ARG A 112 37.356 6.078 20.996 1.00 15.33 C ANISOU 863 CB ARG A 112 1510 2372 1941 -292 -33 -265 C ATOM 864 CG ARG A 112 37.281 4.617 21.404 1.00 19.67 C ANISOU 864 CG ARG A 112 2151 2923 2398 -359 -53 -215 C ATOM 865 CD ARG A 112 36.790 4.421 22.835 1.00 24.15 C ANISOU 865 CD ARG A 112 2657 3604 2913 -438 -60 -239 C ATOM 866 NE ARG A 112 35.545 5.139 23.094 1.00 27.66 N ANISOU 866 NE ARG A 112 2996 4149 3364 -475 -56 -294 N ATOM 867 CZ ARG A 112 34.335 4.689 22.777 1.00 31.96 C ANISOU 867 CZ ARG A 112 3548 4726 3868 -542 -78 -281 C ATOM 868 NH1 ARG A 112 34.191 3.507 22.187 1.00 28.47 N ANISOU 868 NH1 ARG A 112 3222 4222 3373 -581 -114 -208 N ATOM 869 NH2 ARG A 112 33.265 5.424 23.050 1.00 33.73 N ANISOU 869 NH2 ARG A 112 3660 5043 4111 -568 -72 -343 N ATOM 870 N ASN A 113 36.105 5.917 18.090 1.00 11.97 N ANISOU 870 N ASN A 113 1217 1803 1529 -288 -68 -219 N ATOM 871 CA ASN A 113 35.272 5.136 17.174 1.00 12.86 C ANISOU 871 CA ASN A 113 1427 1860 1598 -326 -102 -179 C ATOM 872 C ASN A 113 35.718 5.120 15.705 1.00 14.13 C ANISOU 872 C ASN A 113 1688 1910 1772 -273 -100 -144 C ATOM 873 O ASN A 113 35.394 4.177 14.976 1.00 14.56 O ANISOU 873 O ASN A 113 1858 1900 1773 -287 -128 -98 O ATOM 874 CB ASN A 113 33.802 5.544 17.302 1.00 13.83 C ANISOU 874 CB ASN A 113 1477 2038 1740 -390 -133 -215 C ATOM 875 CG ASN A 113 33.203 5.124 18.628 1.00 15.21 C ANISOU 875 CG ASN A 113 1586 2329 1866 -461 -135 -230 C ATOM 876 OD1 ASN A 113 33.622 4.129 19.227 1.00 17.42 O ANISOU 876 OD1 ASN A 113 1920 2624 2075 -488 -137 -188 O ATOM 877 ND2 ASN A 113 32.210 5.872 19.090 1.00 15.85 N ANISOU 877 ND2 ASN A 113 1547 2494 1980 -495 -140 -292 N ATOM 878 N ARG A 114 36.464 6.133 15.264 1.00 13.13 N ANISOU 878 N ARG A 114 1520 1760 1709 -213 -72 -162 N ATOM 879 CA ARG A 114 36.735 6.271 13.834 1.00 12.92 C ANISOU 879 CA ARG A 114 1576 1642 1689 -177 -69 -133 C ATOM 880 C ARG A 114 38.205 6.416 13.472 1.00 15.56 C ANISOU 880 C ARG A 114 1932 1948 2034 -101 -19 -110 C ATOM 881 O ARG A 114 38.561 6.270 12.306 1.00 16.75 O ANISOU 881 O ARG A 114 2167 2032 2164 -70 -5 -79 O ATOM 882 CB ARG A 114 35.932 7.448 13.275 1.00 13.36 C ANISOU 882 CB ARG A 114 1571 1687 1818 -199 -104 -167 C ATOM 883 CG ARG A 114 34.449 7.336 13.612 1.00 14.35 C ANISOU 883 CG ARG A 114 1663 1842 1946 -272 -153 -195 C ATOM 884 CD ARG A 114 33.647 8.487 13.092 1.00 15.75 C ANISOU 884 CD ARG A 114 1776 2000 2208 -294 -200 -239 C ATOM 885 NE ARG A 114 33.477 8.432 11.641 1.00 13.12 N ANISOU 885 NE ARG A 114 1556 1555 1874 -298 -227 -201 N ATOM 886 CZ ARG A 114 32.687 9.259 10.968 1.00 15.51 C ANISOU 886 CZ ARG A 114 1837 1809 2248 -331 -286 -228 C ATOM 887 NH1 ARG A 114 32.018 10.207 11.624 1.00 13.51 N ANISOU 887 NH1 ARG A 114 1445 1613 2075 -353 -325 -302 N ATOM 888 NH2 ARG A 114 32.576 9.149 9.649 1.00 15.85 N ANISOU 888 NH2 ARG A 114 1998 1744 2281 -340 -312 -187 N ATOM 889 N CYS A 115 39.054 6.700 14.456 1.00 12.78 N ANISOU 889 N CYS A 115 1502 1645 1710 -72 8 -124 N ATOM 890 CA CYS A 115 40.478 6.941 14.191 1.00 12.34 C ANISOU 890 CA CYS A 115 1444 1566 1679 0 55 -100 C ATOM 891 C CYS A 115 41.385 5.930 14.871 1.00 11.75 C ANISOU 891 C CYS A 115 1409 1488 1568 27 80 -84 C ATOM 892 O CYS A 115 42.365 5.449 14.279 1.00 12.88 O ANISOU 892 O CYS A 115 1613 1586 1694 83 115 -56 O ATOM 893 CB CYS A 115 40.889 8.348 14.646 1.00 11.23 C ANISOU 893 CB CYS A 115 1173 1463 1629 22 53 -123 C ATOM 894 SG CYS A 115 39.981 9.656 13.799 1.00 12.36 S ANISOU 894 SG CYS A 115 1265 1596 1834 -8 1 -147 S ATOM 895 N LYS A 116 41.072 5.628 16.123 1.00 12.31 N ANISOU 895 N LYS A 116 1440 1609 1629 -14 58 -105 N ATOM 896 CA LYS A 116 41.901 4.759 16.938 1.00 13.46 C ANISOU 896 CA LYS A 116 1614 1748 1752 -3 63 -93 C ATOM 897 C LYS A 116 42.169 3.440 16.227 1.00 14.69 C ANISOU 897 C LYS A 116 1902 1839 1842 14 54 -63 C ATOM 898 O LYS A 116 41.237 2.766 15.786 1.00 15.10 O ANISOU 898 O LYS A 116 2028 1876 1834 -27 15 -52 O ATOM 899 CB LYS A 116 41.203 4.519 18.272 1.00 12.63 C ANISOU 899 CB LYS A 116 1466 1711 1623 -77 28 -116 C ATOM 900 CG LYS A 116 41.985 3.674 19.272 1.00 12.32 C ANISOU 900 CG LYS A 116 1454 1665 1564 -86 16 -105 C ATOM 901 CD LYS A 116 41.184 3.560 20.550 1.00 12.21 C ANISOU 901 CD LYS A 116 1393 1732 1514 -172 -16 -126 C ATOM 902 CE LYS A 116 41.946 2.791 21.615 1.00 14.59 C ANISOU 902 CE LYS A 116 1723 2023 1798 -196 -40 -114 C ATOM 903 NZ LYS A 116 41.176 2.793 22.887 1.00 14.55 N ANISOU 903 NZ LYS A 116 1666 2113 1751 -286 -64 -135 N ATOM 904 N GLY A 117 43.446 3.092 16.103 1.00 15.07 N ANISOU 904 N GLY A 117 1976 1845 1904 80 84 -51 N ATOM 905 CA GLY A 117 43.830 1.818 15.521 1.00 16.36 C ANISOU 905 CA GLY A 117 2259 1947 2010 110 67 -36 C ATOM 906 C GLY A 117 43.927 1.796 14.007 1.00 17.93 C ANISOU 906 C GLY A 117 2529 2103 2182 166 99 -24 C ATOM 907 O GLY A 117 44.421 0.822 13.433 1.00 21.39 O ANISOU 907 O GLY A 117 3061 2490 2575 214 92 -21 O ATOM 908 N THR A 118 43.463 2.859 13.358 1.00 15.45 N ANISOU 908 N THR A 118 2170 1806 1892 159 126 -21 N ATOM 909 CA THR A 118 43.474 2.932 11.902 1.00 14.66 C ANISOU 909 CA THR A 118 2142 1668 1761 198 153 -7 C ATOM 910 C THR A 118 44.777 3.526 11.375 1.00 15.89 C ANISOU 910 C THR A 118 2255 1828 1955 272 229 3 C ATOM 911 O THR A 118 45.629 3.987 12.141 1.00 15.76 O ANISOU 911 O THR A 118 2148 1838 2003 294 255 2 O ATOM 912 CB THR A 118 42.290 3.768 11.366 1.00 15.24 C ANISOU 912 CB THR A 118 2200 1748 1845 142 130 -5 C ATOM 913 OG1 THR A 118 42.517 5.155 11.636 1.00 14.05 O ANISOU 913 OG1 THR A 118 1923 1640 1775 137 152 -13 O ATOM 914 CG2 THR A 118 40.990 3.325 12.018 1.00 13.73 C ANISOU 914 CG2 THR A 118 2020 1568 1630 63 61 -14 C ATOM 915 N ASP A 119 44.932 3.508 10.056 1.00 14.60 N ANISOU 915 N ASP A 119 2160 1638 1749 308 263 17 N ATOM 916 CA ASP A 119 46.124 4.060 9.434 1.00 16.84 C ANISOU 916 CA ASP A 119 2403 1938 2056 371 340 33 C ATOM 917 C ASP A 119 46.033 5.586 9.411 1.00 17.62 C ANISOU 917 C ASP A 119 2392 2076 2228 336 347 54 C ATOM 918 O ASP A 119 45.828 6.201 8.363 1.00 19.48 O ANISOU 918 O ASP A 119 2645 2309 2448 322 360 74 O ATOM 919 CB ASP A 119 46.293 3.491 8.019 1.00 19.47 C ANISOU 919 CB ASP A 119 2852 2240 2304 418 375 39 C ATOM 920 CG ASP A 119 47.539 4.009 7.325 1.00 28.59 C ANISOU 920 CG ASP A 119 3962 3430 3471 480 465 58 C ATOM 921 OD1 ASP A 119 48.480 4.451 8.023 1.00 27.83 O ANISOU 921 OD1 ASP A 119 3758 3366 3448 505 498 67 O ATOM 922 OD2 ASP A 119 47.585 3.952 6.077 1.00 33.27 O ANISOU 922 OD2 ASP A 119 4627 4016 3996 501 502 68 O ATOM 923 N VAL A 120 46.202 6.200 10.579 1.00 16.16 N ANISOU 923 N VAL A 120 2543 1539 2057 583 -4 -573 N ATOM 924 CA VAL A 120 46.045 7.645 10.704 1.00 14.45 C ANISOU 924 CA VAL A 120 2150 1438 1900 447 -50 -475 C ATOM 925 C VAL A 120 47.110 8.461 9.952 1.00 13.57 C ANISOU 925 C VAL A 120 1774 1514 1868 501 12 -416 C ATOM 926 O VAL A 120 46.896 9.640 9.674 1.00 13.55 O ANISOU 926 O VAL A 120 1626 1634 1888 379 11 -347 O ATOM 927 CB VAL A 120 45.994 8.103 12.189 1.00 16.81 C ANISOU 927 CB VAL A 120 2446 1650 2292 407 -205 -410 C ATOM 928 CG1 VAL A 120 44.783 7.508 12.901 1.00 16.71 C ANISOU 928 CG1 VAL A 120 2684 1469 2197 317 -270 -459 C ATOM 929 CG2 VAL A 120 47.281 7.708 12.900 1.00 16.51 C ANISOU 929 CG2 VAL A 120 2333 1571 2368 586 -257 -393 C ATOM 930 N GLN A 121 48.240 7.848 9.609 1.00 16.98 N ANISOU 930 N GLN A 121 2143 1969 2341 679 69 -444 N ATOM 931 CA GLN A 121 49.264 8.577 8.863 1.00 19.80 C ANISOU 931 CA GLN A 121 2252 2503 2769 734 132 -393 C ATOM 932 C GLN A 121 48.703 9.029 7.510 1.00 19.13 C ANISOU 932 C GLN A 121 2126 2551 2593 625 249 -407 C ATOM 933 O GLN A 121 49.166 10.010 6.918 1.00 17.61 O ANISOU 933 O GLN A 121 1725 2520 2446 594 286 -347 O ATOM 934 CB GLN A 121 50.536 7.731 8.685 1.00 24.83 C ANISOU 934 CB GLN A 121 2844 3133 3457 949 181 -430 C ATOM 935 CG GLN A 121 50.414 6.642 7.635 1.00 34.61 C ANISOU 935 CG GLN A 121 4211 4352 4587 1019 310 -534 C ATOM 936 CD GLN A 121 51.608 5.696 7.615 1.00 44.23 C ANISOU 936 CD GLN A 121 5412 5535 5857 1236 347 -575 C ATOM 937 OE1 GLN A 121 52.638 5.956 8.242 1.00 50.42 O ANISOU 937 OE1 GLN A 121 6056 6337 6764 1337 286 -520 O ATOM 938 NE2 GLN A 121 51.471 4.589 6.888 1.00 43.94 N ANISOU 938 NE2 GLN A 121 5521 5449 5727 1307 448 -672 N ATOM 939 N ALA A 122 47.689 8.324 7.020 1.00 15.23 N ANISOU 939 N ALA A 122 1832 1988 1966 563 305 -486 N ATOM 940 CA ALA A 122 47.090 8.698 5.744 1.00 15.90 C ANISOU 940 CA ALA A 122 1894 2190 1957 454 414 -501 C ATOM 941 C ALA A 122 46.570 10.136 5.783 1.00 14.75 C ANISOU 941 C ALA A 122 1614 2152 1840 278 370 -410 C ATOM 942 O ALA A 122 46.486 10.794 4.746 1.00 17.53 O ANISOU 942 O ALA A 122 1850 2649 2161 206 452 -391 O ATOM 943 CB ALA A 122 45.967 7.733 5.366 1.00 18.64 C ANISOU 943 CB ALA A 122 2495 2432 2156 399 465 -595 C ATOM 944 N TRP A 123 46.226 10.626 6.976 1.00 14.04 N ANISOU 944 N TRP A 123 1538 1989 1808 208 241 -354 N ATOM 945 CA TRP A 123 45.673 11.976 7.107 1.00 13.81 C ANISOU 945 CA TRP A 123 1395 2047 1807 37 193 -268 C ATOM 946 C TRP A 123 46.689 13.088 6.867 1.00 16.74 C ANISOU 946 C TRP A 123 1487 2585 2288 61 198 -181 C ATOM 947 O TRP A 123 46.310 14.233 6.618 1.00 16.00 O ANISOU 947 O TRP A 123 1274 2600 2206 -76 192 -114 O ATOM 948 CB TRP A 123 44.959 12.155 8.459 1.00 12.65 C ANISOU 948 CB TRP A 123 1354 1768 1685 -50 56 -237 C ATOM 949 CG TRP A 123 43.697 11.371 8.493 1.00 13.80 C ANISOU 949 CG TRP A 123 1755 1784 1705 -130 60 -312 C ATOM 950 CD1 TRP A 123 43.495 10.163 9.085 1.00 16.27 C ANISOU 950 CD1 TRP A 123 2278 1927 1976 -53 30 -386 C ATOM 951 CD2 TRP A 123 42.470 11.714 7.844 1.00 15.15 C ANISOU 951 CD2 TRP A 123 1998 1988 1771 -301 104 -322 C ATOM 952 NE1 TRP A 123 42.208 9.733 8.862 1.00 16.58 N ANISOU 952 NE1 TRP A 123 2518 1891 1889 -167 50 -442 N ATOM 953 CE2 TRP A 123 41.558 10.665 8.093 1.00 15.19 C ANISOU 953 CE2 TRP A 123 2262 1838 1672 -319 97 -404 C ATOM 954 CE3 TRP A 123 42.058 12.804 7.069 1.00 15.75 C ANISOU 954 CE3 TRP A 123 1944 2211 1830 -439 149 -269 C ATOM 955 CZ2 TRP A 123 40.250 10.685 7.613 1.00 18.11 C ANISOU 955 CZ2 TRP A 123 2762 2196 1923 -473 131 -433 C ATOM 956 CZ3 TRP A 123 40.765 12.819 6.581 1.00 17.63 C ANISOU 956 CZ3 TRP A 123 2310 2437 1952 -590 184 -297 C ATOM 957 CH2 TRP A 123 39.876 11.758 6.852 1.00 17.66 C ANISOU 957 CH2 TRP A 123 2572 2285 1854 -606 175 -378 C ATOM 958 N ILE A 124 47.974 12.751 6.933 1.00 15.62 N ANISOU 958 N ILE A 124 1243 2465 2226 234 209 -180 N ATOM 959 CA ILE A 124 49.020 13.735 6.662 1.00 16.05 C ANISOU 959 CA ILE A 124 1033 2681 2383 270 220 -102 C ATOM 960 C ILE A 124 49.850 13.366 5.419 1.00 17.72 C ANISOU 960 C ILE A 124 1153 3004 2575 386 353 -144 C ATOM 961 O ILE A 124 50.813 14.054 5.072 1.00 21.75 O ANISOU 961 O ILE A 124 1446 3653 3166 435 377 -90 O ATOM 962 CB ILE A 124 49.930 13.960 7.896 1.00 19.41 C ANISOU 962 CB ILE A 124 1365 3065 2945 361 106 -40 C ATOM 963 CG1 ILE A 124 50.685 12.679 8.269 1.00 23.06 C ANISOU 963 CG1 ILE A 124 1922 3412 3427 554 105 -103 C ATOM 964 CG2 ILE A 124 49.091 14.484 9.059 1.00 19.73 C ANISOU 964 CG2 ILE A 124 1476 3014 3007 228 -21 9 C ATOM 965 CD1 ILE A 124 51.761 12.883 9.342 1.00 28.96 C ANISOU 965 CD1 ILE A 124 2551 4138 4313 662 6 -41 C ATOM 966 N ARG A 125 49.461 12.285 4.751 1.00 22.15 N ANISOU 966 N ARG A 125 2401 3249 2767 -183 665 -1073 N ATOM 967 CA ARG A 125 50.145 11.843 3.536 1.00 25.07 C ANISOU 967 CA ARG A 125 2595 3750 3181 -169 921 -1272 C ATOM 968 C ARG A 125 50.129 12.949 2.484 1.00 24.53 C ANISOU 968 C ARG A 125 2436 3970 2916 -293 1128 -1206 C ATOM 969 O ARG A 125 49.091 13.567 2.237 1.00 25.83 O ANISOU 969 O ARG A 125 2747 4281 2785 -415 1151 -1089 O ATOM 970 CB ARG A 125 49.479 10.578 2.981 1.00 31.75 C ANISOU 970 CB ARG A 125 3564 4590 3911 -154 1009 -1463 C ATOM 971 CG ARG A 125 50.202 9.945 1.796 1.00 38.10 C ANISOU 971 CG ARG A 125 4197 5498 4781 -121 1260 -1687 C ATOM 972 CD ARG A 125 49.325 8.896 1.110 1.00 42.22 C ANISOU 972 CD ARG A 125 4868 6064 5111 -141 1365 -1852 C ATOM 973 NE ARG A 125 50.064 8.112 0.121 1.00 51.47 N ANISOU 973 NE ARG A 125 5885 7290 6382 -85 1578 -2082 N ATOM 974 CZ ARG A 125 49.544 7.099 -0.568 1.00 56.88 C ANISOU 974 CZ ARG A 125 6657 8006 6948 -84 1693 -2260 C ATOM 975 NH1 ARG A 125 48.277 6.744 -0.380 1.00 57.33 N ANISOU 975 NH1 ARG A 125 6953 8046 6785 -137 1613 -2234 N ATOM 976 NH2 ARG A 125 50.288 6.437 -1.445 1.00 57.62 N ANISOU 976 NH2 ARG A 125 6602 8146 7144 -29 1885 -2463 N ATOM 977 N GLY A 126 51.283 13.202 1.877 1.00 28.82 N ANISOU 977 N GLY A 126 2733 4591 3626 -261 1279 -1276 N ATOM 978 CA GLY A 126 51.377 14.203 0.832 1.00 31.01 C ANISOU 978 CA GLY A 126 2899 5141 3742 -366 1489 -1227 C ATOM 979 C GLY A 126 51.688 15.590 1.355 1.00 29.28 C ANISOU 979 C GLY A 126 2608 4959 3559 -414 1398 -1004 C ATOM 980 O GLY A 126 52.205 16.436 0.628 1.00 33.42 O ANISOU 980 O GLY A 126 2966 5669 4065 -465 1557 -969 O ATOM 981 N CYS A 127 51.370 15.823 2.624 1.00 24.12 N ANISOU 981 N CYS A 127 2077 4127 2960 -395 1139 -853 N ATOM 982 CA CYS A 127 51.461 17.158 3.204 1.00 23.76 C ANISOU 982 CA CYS A 127 1984 4097 2945 -439 1027 -633 C ATOM 983 C CYS A 127 52.909 17.635 3.266 1.00 25.16 C ANISOU 983 C CYS A 127 1897 4210 3452 -353 1028 -647 C ATOM 984 O CYS A 127 53.806 16.879 3.639 1.00 26.41 O ANISOU 984 O CYS A 127 1984 4158 3894 -227 922 -733 O ATOM 985 CB CYS A 127 50.841 17.178 4.602 1.00 20.46 C ANISOU 985 CB CYS A 127 1774 3490 2508 -430 742 -475 C ATOM 986 SG CYS A 127 49.066 16.838 4.637 1.00 20.03 S ANISOU 986 SG CYS A 127 2042 3487 2081 -523 716 -443 S ATOM 987 N ARG A 128 53.128 18.893 2.897 1.00 34.03 N ANISOU 987 N ARG A 128 2888 5648 4396 -514 1166 -412 N ATOM 988 CA ARG A 128 54.368 19.584 3.230 1.00 33.26 C ANISOU 988 CA ARG A 128 2570 5443 4626 -428 1101 -386 C ATOM 989 C ARG A 128 54.385 20.009 4.695 1.00 28.72 C ANISOU 989 C ARG A 128 2099 4634 4179 -383 794 -234 C ATOM 990 O ARG A 128 53.630 20.891 5.104 1.00 32.12 O ANISOU 990 O ARG A 128 2677 5100 4426 -469 687 -52 O ATOM 991 CB ARG A 128 54.563 20.802 2.326 1.00 36.32 C ANISOU 991 CB ARG A 128 2782 6055 4963 -510 1258 -285 C ATOM 992 CG ARG A 128 55.927 21.460 2.456 1.00 35.93 C ANISOU 992 CG ARG A 128 2453 5971 5229 -427 1308 -325 C ATOM 993 CD ARG A 128 56.416 21.985 1.116 1.00 37.16 C ANISOU 993 CD ARG A 128 2439 6397 5281 -509 1546 -290 C ATOM 994 NE ARG A 128 57.813 22.407 1.172 1.00 39.41 N ANISOU 994 NE ARG A 128 2449 6657 5870 -433 1594 -310 N ATOM 995 CZ ARG A 128 58.775 21.907 0.403 1.00 44.07 C ANISOU 995 CZ ARG A 128 2862 7278 6605 -359 1774 -488 C ATOM 996 NH1 ARG A 128 58.494 20.963 -0.485 1.00 48.85 N ANISOU 996 NH1 ARG A 128 3539 7941 7082 -352 1922 -668 N ATOM 997 NH2 ARG A 128 60.019 22.351 0.522 1.00 44.01 N ANISOU 997 NH2 ARG A 128 2606 7241 6873 -292 1805 -484 N ATOM 998 N LEU A 129 55.252 19.377 5.479 1.00 30.08 N ANISOU 998 N LEU A 129 2202 4568 4660 -249 653 -306 N ATOM 999 CA LEU A 129 55.260 19.571 6.932 1.00 30.61 C ANISOU 999 CA LEU A 129 2356 4407 4867 -196 359 -166 C ATOM 1000 C LEU A 129 56.663 19.821 7.470 1.00 34.33 C ANISOU 1000 C LEU A 129 2603 4745 5697 -100 275 -150 C ATOM 1001 O LEU A 129 57.624 19.198 7.014 1.00 38.96 O ANISOU 1001 O LEU A 129 3007 5304 6491 -18 389 -309 O ATOM 1002 CB LEU A 129 54.625 18.379 7.650 1.00 30.26 C ANISOU 1002 CB LEU A 129 2511 4158 4831 -123 204 -244 C ATOM 1003 CG LEU A 129 53.113 18.241 7.477 1.00 28.43 C ANISOU 1003 CG LEU A 129 2541 4009 4251 -217 209 -207 C ATOM 1004 CD1 LEU A 129 52.646 16.884 7.971 1.00 31.26 C ANISOU 1004 CD1 LEU A 129 3055 4176 4647 -131 102 -330 C ATOM 1005 CD2 LEU A 129 52.379 19.358 8.207 1.00 28.82 C ANISOU 1005 CD2 LEU A 129 2738 4074 4140 -302 47 41 C TER 1006 LEU A 129 HETATM 1007 O HOH A 130 47.630 7.769 26.048 1.00 6.89 O HETATM 1008 O HOH A 131 27.611 27.757 32.381 1.00 8.04 O HETATM 1009 O HOH A 132 33.944 33.396 29.670 1.00 13.12 O HETATM 1010 O HOH A 133 27.995 26.082 14.390 1.00 13.60 O HETATM 1011 O HOH A 134 50.518 10.303 11.754 1.00 11.68 O HETATM 1012 O HOH A 135 37.816 22.705 19.314 1.00 11.45 O HETATM 1013 O HOH A 136 28.941 33.725 30.742 1.00 14.95 O HETATM 1014 O HOH A 137 40.683 28.320 18.757 1.00 15.12 O HETATM 1015 O HOH A 138 29.730 26.691 30.252 1.00 13.87 O HETATM 1016 O HOH A 139 31.412 25.244 31.278 1.00 10.42 O HETATM 1017 O HOH A 140 34.782 6.493 9.944 1.00 14.81 O HETATM 1018 O HOH A 141 42.774 31.024 19.355 1.00 19.38 O HETATM 1019 O HOH A 142 41.810 12.467 28.250 1.00 18.64 O HETATM 1020 O HOH A 143 38.450 25.381 16.624 1.00 15.14 O HETATM 1021 O HOH A 144 39.975 27.371 16.164 1.00 16.02 O HETATM 1022 O HOH A 145 45.356 21.954 2.648 1.00 19.71 O HETATM 1023 O HOH A 146 38.455 3.323 15.419 1.00 17.69 O HETATM 1024 O HOH A 147 38.658 20.919 4.063 1.00 18.86 O HETATM 1025 O HOH A 148 33.405 12.867 22.641 1.00 21.13 O HETATM 1026 O HOH A 149 43.258 1.955 8.400 1.00 21.20 O HETATM 1027 O HOH A 150 49.947 8.069 23.753 1.00 16.74 O HETATM 1028 O HOH A 151 46.621 4.044 14.743 1.00 19.75 O HETATM 1029 O HOH A 152 26.541 26.541 36.920 0.50 12.18 O HETATM 1030 O HOH A 153 53.687 7.596 20.375 1.00 20.15 O HETATM 1031 O HOH A 154 45.090 19.315 1.715 1.00 22.56 O HETATM 1032 O HOH A 155 36.383 19.735 5.016 1.00 19.12 O HETATM 1033 O HOH A 156 45.441 5.604 16.730 1.00 16.53 O HETATM 1034 O HOH A 157 36.438 25.891 36.391 1.00 21.07 O HETATM 1035 O HOH A 158 37.619 5.842 9.847 1.00 17.44 O HETATM 1036 O HOH A 159 41.952 6.881 9.536 1.00 16.31 O HETATM 1037 O HOH A 160 31.204 11.367 8.337 1.00 16.01 O HETATM 1038 O HOH A 161 31.593 27.303 32.598 1.00 17.79 O HETATM 1039 O HOH A 162 35.351 17.781 25.257 1.00 22.01 O HETATM 1040 O HOH A 163 30.201 17.031 18.458 1.00 17.90 O HETATM 1041 O HOH A 164 45.637 11.260 29.288 1.00 19.49 O HETATM 1042 O HOH A 165 36.685 32.383 30.493 1.00 21.78 O HETATM 1043 O HOH A 166 53.978 15.566 25.115 1.00 27.70 O HETATM 1044 O HOH A 167 48.529 6.108 15.802 1.00 18.30 O HETATM 1045 O HOH A 168 35.491 32.222 13.363 1.00 16.29 O HETATM 1046 O HOH A 169 39.328 0.790 21.902 1.00 20.28 O HETATM 1047 O HOH A 170 49.213 5.314 10.717 1.00 24.88 O HETATM 1048 O HOH A 171 42.500 27.468 25.373 1.00 22.65 O HETATM 1049 O HOH A 172 36.496 31.929 10.783 1.00 18.88 O HETATM 1050 O HOH A 173 31.783 13.159 15.325 1.00 17.99 O HETATM 1051 O HOH A 174 42.764 0.313 18.235 1.00 19.75 O HETATM 1052 O HOH A 175 33.423 12.667 19.838 1.00 18.22 O HETATM 1053 O HOH A 176 40.534 32.407 20.197 1.00 24.14 O HETATM 1054 O HOH A 177 43.347 26.670 27.805 1.00 25.03 O HETATM 1055 O HOH A 178 39.144 0.796 10.034 1.00 21.33 O HETATM 1056 O HOH A 179 33.496 14.741 8.731 1.00 24.86 O HETATM 1057 O HOH A 180 27.817 24.865 39.866 1.00 28.82 O HETATM 1058 O HOH A 181 20.938 29.472 24.459 1.00 23.81 O HETATM 1059 O HOH A 182 40.678 0.325 14.764 1.00 26.72 O HETATM 1060 O HOH A 183 35.069 33.275 17.847 1.00 21.37 O HETATM 1061 O HOH A 184 48.390 26.202 8.141 1.00 22.53 O HETATM 1062 O HOH A 185 39.431 7.349 8.301 1.00 21.58 O HETATM 1063 O HOH A 186 37.786 8.461 5.899 1.00 23.28 O HETATM 1064 O HOH A 187 47.411 23.818 27.552 1.00 25.72 O HETATM 1065 O HOH A 188 43.270 6.076 7.332 1.00 22.76 O HETATM 1066 O HOH A 189 37.887 34.202 13.809 1.00 23.22 O HETATM 1067 O HOH A 190 51.116 6.787 15.008 1.00 25.91 O HETATM 1068 O HOH A 191 31.206 21.301 10.492 1.00 25.50 O HETATM 1069 O HOH A 192 44.191 29.768 24.992 1.00 27.40 O HETATM 1070 O HOH A 193 44.050 30.278 10.754 1.00 29.29 O HETATM 1071 O HOH A 194 34.331 30.678 33.997 1.00 25.55 O HETATM 1072 O HOH A 195 24.513 31.973 33.110 1.00 27.02 O HETATM 1073 O HOH A 196 44.680 17.815 32.125 1.00 26.41 O HETATM 1074 O HOH A 197 31.301 22.190 7.921 1.00 21.93 O HETATM 1075 O HOH A 198 36.048 34.626 21.726 1.00 22.51 O HETATM 1076 O HOH A 199 51.691 21.503 27.577 1.00 35.39 O HETATM 1077 O HOH A 200 41.989 0.109 9.874 1.00 32.92 O HETATM 1078 O HOH A 201 24.409 23.153 17.454 1.00 27.56 O HETATM 1079 O HOH A 202 27.340 33.172 33.045 1.00 29.66 O HETATM 1080 O HOH A 203 39.778 2.828 25.611 1.00 28.65 O HETATM 1081 O HOH A 204 24.554 14.652 26.457 1.00 25.75 O HETATM 1082 O HOH A 205 33.605 21.659 6.916 1.00 22.52 O HETATM 1083 O HOH A 206 37.086 34.761 16.649 1.00 23.66 O HETATM 1084 O HOH A 207 23.264 20.829 17.615 1.00 25.15 O HETATM 1085 O HOH A 208 31.420 12.978 17.997 1.00 25.00 O HETATM 1086 O HOH A 209 21.800 23.557 29.567 1.00 27.30 O HETATM 1087 O HOH A 210 42.215 7.801 5.161 1.00 29.75 O HETATM 1088 O HOH A 211 28.875 30.839 33.716 1.00 35.41 O HETATM 1089 O HOH A 212 30.530 18.696 13.469 1.00 28.34 O HETATM 1090 O HOH A 213 28.227 16.008 28.132 1.00 40.69 O HETATM 1091 O HOH A 214 46.632 28.451 7.786 1.00 32.41 O HETATM 1092 O HOH A 215 37.991 35.491 23.422 1.00 36.06 O HETATM 1093 O HOH A 216 22.746 27.675 23.415 1.00 23.57 O HETATM 1094 O HOH A 217 53.337 21.957 24.041 1.00 33.87 O HETATM 1095 O HOH A 218 41.249 27.300 4.591 1.00 26.41 O HETATM 1096 O HOH A 219 31.728 15.268 19.186 1.00 27.14 O HETATM 1097 O HOH A 220 36.573 1.086 21.208 1.00 29.82 O HETATM 1098 O HOH A 221 34.524 1.471 19.199 1.00 31.82 O HETATM 1099 O HOH A 222 49.120 28.167 12.288 1.00 33.11 O HETATM 1100 O HOH A 223 31.129 20.281 37.432 1.00 33.64 O HETATM 1101 O HOH A 224 48.732 26.687 20.791 1.00 36.25 O HETATM 1102 O HOH A 225 54.696 19.871 21.702 1.00 30.93 O HETATM 1103 O HOH A 226 51.339 7.945 12.474 1.00 40.05 O HETATM 1104 O HOH A 227 50.522 25.229 24.033 1.00 32.95 O HETATM 1105 O HOH A 228 53.517 14.366 5.088 1.00 37.33 O HETATM 1106 O HOH A 229 55.462 29.219 15.228 1.00 43.38 O HETATM 1107 O HOH A 230 20.495 20.495 18.460 0.50 19.70 O HETATM 1108 O HOH A 231 46.563 -0.504 14.754 1.00 29.65 O HETATM 1109 O HOH A 232 31.132 19.308 35.129 1.00 35.27 O HETATM 1110 O HOH A 233 53.765 24.136 10.593 1.00 33.93 O HETATM 1111 O HOH A 234 46.130 9.995 2.095 1.00 39.73 O HETATM 1112 O HOH A 235 42.397 10.120 4.149 1.00 40.67 O HETATM 1113 O HOH A 236 32.789 19.723 39.151 1.00 32.64 O HETATM 1114 O HOH A 237 40.226 18.876 3.113 1.00 33.42 O HETATM 1115 O HOH A 238 43.206 -2.010 16.542 1.00 32.64 O HETATM 1116 O HOH A 239 27.225 14.925 26.007 1.00 49.98 O HETATM 1117 O HOH A 240 50.425 26.804 9.977 1.00 34.75 O HETATM 1118 O HOH A 241 26.929 14.622 30.988 1.00 36.19 O HETATM 1119 O HOH A 242 53.476 9.005 17.659 1.00 32.28 O HETATM 1120 O HOH A 243 37.914 1.680 18.712 1.00 31.90 O HETATM 1121 O HOH A 244 36.548 15.489 25.646 1.00 36.81 O HETATM 1122 O HOH A 245 30.235 24.988 38.557 1.00 32.95 O HETATM 1123 O HOH A 246 32.728 21.923 41.252 1.00 29.84 O HETATM 1124 O HOH A 247 39.657 33.762 24.860 1.00 35.34 O HETATM 1125 O HOH A 248 35.374 16.042 23.360 1.00 43.55 O HETATM 1126 O HOH A 249 23.502 21.285 30.790 1.00 36.96 O HETATM 1127 O HOH A 250 33.217 17.096 39.889 1.00 28.05 O HETATM 1128 O HOH A 251 25.129 25.129 18.460 0.50 22.47 O HETATM 1129 O HOH A 252 50.165 7.432 3.450 1.00 36.83 O HETATM 1130 O HOH A 253 29.706 15.314 15.831 1.00 37.60 O HETATM 1131 O HOH A 254 19.650 19.534 24.479 1.00 36.59 O HETATM 1132 O HOH A 255 56.125 13.168 22.448 1.00 34.58 O HETATM 1133 O HOH A 256 35.520 7.366 24.524 1.00 32.62 O HETATM 1134 O HOH A 257 55.169 9.810 15.660 1.00 35.81 O HETATM 1135 O HOH A 258 55.553 24.547 12.426 1.00 32.04 O HETATM 1136 O HOH A 259 37.302 10.958 4.600 1.00 35.28 O HETATM 1137 O HOH A 260 54.451 8.031 13.976 1.00 42.10 O HETATM 1138 O HOH A 261 42.538 -1.767 13.897 1.00 35.82 O HETATM 1139 O HOH A 262 49.390 31.402 19.115 1.00 35.65 O HETATM 1140 O HOH A 263 39.067 12.453 3.059 1.00 33.99 O HETATM 1141 O HOH A 264 49.001 5.763 4.902 1.00 37.66 O HETATM 1142 O HOH A 265 42.068 19.609 1.491 1.00 38.55 O HETATM 1143 O HOH A 266 51.350 27.284 20.724 1.00 43.66 O HETATM 1144 O HOH A 267 40.280 34.750 19.524 1.00 47.72 O HETATM 1145 O HOH A 268 36.774 15.241 28.641 1.00 41.94 O HETATM 1146 O HOH A 269 35.934 17.632 3.183 1.00 35.37 O HETATM 1147 O HOH A 270 32.392 15.103 25.297 1.00 37.64 O HETATM 1148 O HOH A 271 54.923 19.866 24.324 1.00 42.22 O HETATM 1149 O HOH A 272 48.423 31.484 15.894 1.00 40.61 O HETATM 1150 O HOH A 273 44.814 33.188 20.214 1.00 45.70 O HETATM 1151 O HOH A 274 34.631 16.306 27.558 1.00 36.38 O HETATM 1152 O HOH A 275 41.985 15.219 1.307 1.00 40.01 O HETATM 1153 O HOH A 276 43.298 33.339 11.808 1.00 41.84 O HETATM 1154 O HOH A 277 33.245 14.260 6.218 1.00 33.35 O HETATM 1155 O HOH A 278 31.321 35.025 29.304 1.00 41.29 O HETATM 1156 O HOH A 279 34.904 14.153 3.114 1.00 42.65 O HETATM 1157 O HOH A 280 20.496 19.590 31.272 1.00 43.56 O HETATM 1158 O HOH A 281 19.113 22.199 25.751 1.00 32.15 O HETATM 1159 O HOH A 282 50.256 30.219 13.540 1.00 48.02 O HETATM 1160 O HOH A 283 38.209 28.989 34.894 1.00 35.56 O HETATM 1161 O HOH A 284 43.770 35.530 17.194 1.00 46.92 O HETATM 1162 O HOH A 285 42.624 24.690 34.827 1.00 48.91 O HETATM 1163 O HOH A 286 50.113 24.016 26.774 1.00 37.94 O HETATM 1164 O HOH A 287 28.607 14.562 22.026 1.00 42.38 O HETATM 1165 O HOH A 288 33.973 33.474 32.862 1.00 46.83 O HETATM 1166 O HOH A 289 28.710 26.797 35.402 1.00 32.34 O HETATM 1167 O HOH A 290 30.736 15.762 23.392 1.00 35.09 O HETATM 1168 O HOH A 291 42.885 31.746 6.235 1.00 33.05 O HETATM 1169 O HOH A 292 43.136 22.071 35.097 1.00 49.79 O HETATM 1170 O HOH A 293 23.705 20.222 33.361 1.00 49.69 O HETATM 1171 O HOH A 294 57.427 8.842 16.489 1.00 40.01 O HETATM 1172 O HOH A 295 53.079 25.340 21.823 1.00 36.60 O HETATM 1173 O HOH A 296 44.479 15.126 -1.112 1.00 41.51 O HETATM 1174 O HOH A 297 57.208 27.545 13.677 1.00 43.97 O HETATM 1175 O HOH A 298 46.431 0.315 11.395 1.00 48.88 O HETATM 1176 O HOH A 299 54.435 17.445 21.090 1.00 37.98 O HETATM 1177 O HOH A 300 41.669 33.036 23.010 1.00 41.15 O HETATM 1178 O HOH A 301 33.748 28.405 9.065 1.00 12.86 O HETATM 1179 O HOH A 302 36.984 29.078 5.154 1.00 20.52 O HETATM 1180 O HOH A 303 53.527 13.448 14.451 1.00 19.63 O HETATM 1181 O HOH A 304 51.041 20.430 1.441 1.00 26.63 O HETATM 1182 O HOH A 305 49.747 29.804 23.059 1.00 40.79 O HETATM 1183 O HOH A 306 27.744 16.534 20.066 1.00 41.97 O HETATM 1184 O HOH A 307 48.574 10.692 29.635 1.00 40.15 O HETATM 1185 O HOH A 308 19.006 22.719 23.318 1.00 40.08 O HETATM 1186 O HOH A 309 26.012 19.332 31.449 1.00 43.81 O HETATM 1187 O HOH A 310 57.094 17.041 4.710 1.00 31.57 O HETATM 1188 O HOH A 311 42.642 17.529 33.549 1.00 41.87 O HETATM 1189 O HOH A 312 56.322 8.381 20.179 1.00 48.76 O HETATM 1190 O HOH A 313 39.997 29.695 4.632 1.00 42.68 O HETATM 1191 O HOH A 314 48.634 20.262 29.115 1.00 45.47 O HETATM 1192 O HOH A 315 47.724 22.530 29.958 1.00 42.34 O HETATM 1193 O HOH A 316 31.850 26.979 35.248 1.00 42.88 O HETATM 1194 O HOH A 317 48.054 31.485 24.287 1.00 43.96 O HETATM 1195 O HOH A 318 40.659 34.663 27.146 1.00 50.93 O HETATM 1196 O HOH A 319 41.592 8.146 33.772 1.00 41.51 O HETATM 1197 O HOH A 320 43.137 30.766 29.513 1.00 38.23 O HETATM 1198 O HOH A 321 27.264 20.311 33.587 1.00 38.81 O HETATM 1199 O HOH A 322 29.856 10.878 17.899 1.00 42.81 O HETATM 1200 O HOH A 323 30.885 12.497 23.925 1.00 50.13 O HETATM 1201 O HOH A 324 24.711 14.070 23.249 1.00 35.51 O HETATM 1202 O HOH A 325 47.956 10.099 32.679 1.00 38.18 O HETATM 1203 O HOH A 326 37.277 9.303 2.042 1.00 50.07 O HETATM 1204 O HOH A 327 43.857 1.188 5.838 1.00 44.79 O HETATM 1205 O HOH A 328 58.075 9.798 18.851 1.00 44.36 O HETATM 1206 O HOH A 329 39.330 33.902 29.927 1.00 38.04 O HETATM 1207 O HOH A 330 43.600 17.278 0.049 1.00 49.92 O HETATM 1208 O HOH A 331 33.697 27.668 36.940 1.00 52.32 O HETATM 1209 O HOH A 332 52.003 9.440 5.851 1.00 44.45 O HETATM 1210 O HOH A 333 57.840 18.419 15.608 1.00 50.08 O HETATM 1211 O HOH A 334 46.375 16.101 -2.653 1.00 48.45 O HETATM 1212 O HOH A 335 44.510 28.921 30.958 1.00 45.53 O HETATM 1213 O HOH A 336 35.652 14.445 0.607 1.00 45.84 O HETATM 1214 O HOH A 337 53.083 16.426 27.831 1.00 48.50 O HETATM 1215 O HOH A 338 55.157 15.419 14.076 1.00 49.48 O HETATM 1216 O HOH A 339 38.835 14.530 34.644 1.00 44.51 O HETATM 1217 O HOH A 340 38.417 17.098 34.750 1.00 45.25 O HETATM 1218 O HOH A 341 55.765 16.479 10.969 1.00 50.13 O HETATM 1219 O HOH A 342 28.196 21.911 40.859 1.00 44.05 O HETATM 1220 O HOH A 343 39.269 9.140 35.755 1.00 44.09 O HETATM 1221 O HOH A 344 31.011 33.869 33.838 1.00 41.14 O HETATM 1222 O HOH A 345 46.658 18.449 -0.436 1.00 45.93 O HETATM 1223 O HOH A 346 28.611 16.742 14.031 1.00 47.03 O HETATM 1224 O HOH A 347 19.017 19.588 21.672 1.00 52.39 O HETATM 1225 O HOH A 348 36.987 1.925 25.162 1.00 45.64 O HETATM 1226 O HOH A 349 38.536 7.952 33.622 1.00 49.68 O HETATM 1227 O HOH A 350 39.577 12.038 29.821 1.00 40.57 O HETATM 1228 O HOH A 351 37.009 15.672 32.959 1.00 48.60 O HETATM 1229 O HOH A 352 47.332 19.977 31.818 1.00 48.38 O HETATM 1230 O HOH A 353 20.812 26.234 29.645 1.00 49.40 O HETATM 1231 O HOH A 354 30.567 16.162 26.986 1.00 49.93 O HETATM 1232 O HOH A 355 36.342 27.533 2.731 1.00 46.54 O HETATM 1233 O HOH A 356 32.232 29.420 34.305 1.00 48.72 O HETATM 1234 O HOH A 357 50.144 4.099 12.468 1.00 51.48 O HETATM 1235 O HOH A 358 55.108 24.674 19.583 1.00 49.28 O HETATM 1236 O HOH A 359 29.865 20.406 7.774 1.00 47.78 O HETATM 1237 O HOH A 360 46.456 28.825 26.992 1.00 50.87 O HETATM 1238 O HOH A 361 45.996 26.415 28.487 1.00 46.68 O HETATM 1239 O HOH A 362 57.267 13.161 14.352 1.00 49.07 O CONECT 48 986 CONECT 238 894 CONECT 518 635 CONECT 606 729 CONECT 635 518 CONECT 729 606 CONECT 894 238 CONECT 986 48 MASTER 380 0 0 8 3 0 0 6 1238 1 8 10 END