HEADER MEMBRANE PROTEIN 28-JUL-17 5OLV TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-LUAA47070 COMPLEX AT 2.0A OBTAINED TITLE 2 FROM IN MESO SOAKING EXPERIMENTS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS KEYWDS G-PROTEIN COUPLED RECEPTOR, ADENOSINE 2A RECEPTOR, 7 TM INTEGRAL KEYWDS 2 MEMBRANE PROTEIN, THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN,R.COOKE, AUTHOR 2 F.H.MARSHALL,A.S.DORE REVDAT 1 17-JAN-18 5OLV 0 JRNL AUTH P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN, JRNL AUTH 2 R.M.COOKE,F.H.MARSHALL,A.S.DORE JRNL TITL TOWARDS HIGH THROUGHPUT GPCR CRYSTALLOGRAPHY: IN MESO JRNL TITL 2 SOAKING OF ADENOSINE A2A RECEPTOR CRYSTALS. JRNL REF SCI REP V. 8 41 2018 JRNL REFN ESSN 2045-2322 JRNL PMID 29311713 JRNL DOI 10.1038/S41598-017-18570-W REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12RC2_2821: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 34171 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.181 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 3254 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 76.1343 - 5.6804 0.93 2551 101 0.1700 0.1678 REMARK 3 2 5.6804 - 4.5088 0.95 2609 122 0.1723 0.1913 REMARK 3 3 4.5088 - 3.9389 0.97 2652 130 0.1532 0.2024 REMARK 3 4 3.9389 - 3.5788 0.98 2680 131 0.1472 0.1687 REMARK 3 5 3.5788 - 3.3223 0.99 2735 142 0.1541 0.1670 REMARK 3 6 3.3223 - 3.1264 1.00 2755 120 0.1625 0.1879 REMARK 3 7 3.1264 - 2.9698 0.99 2703 131 0.1613 0.1840 REMARK 3 8 2.9698 - 2.8405 0.99 2683 158 0.1586 0.2211 REMARK 3 9 2.8405 - 2.7312 1.00 2690 183 0.1655 0.1999 REMARK 3 10 2.7312 - 2.6369 0.99 2662 131 0.1593 0.2046 REMARK 3 11 2.6369 - 2.5545 1.00 2741 149 0.1692 0.2012 REMARK 3 12 2.5545 - 2.4814 0.99 2715 141 0.1731 0.2115 REMARK 3 13 2.4814 - 2.4161 0.99 2709 161 0.1801 0.2268 REMARK 3 14 2.4161 - 2.3572 0.99 2696 145 0.1969 0.2344 REMARK 3 15 2.3572 - 2.3036 0.99 2664 131 0.2053 0.2346 REMARK 3 16 2.3036 - 2.2546 0.99 2772 124 0.2254 0.2421 REMARK 3 17 2.2546 - 2.2094 1.00 2701 159 0.2278 0.2567 REMARK 3 18 2.2094 - 2.1678 1.00 2711 148 0.2460 0.2378 REMARK 3 19 2.1678 - 2.1290 0.99 2753 137 0.2588 0.2727 REMARK 3 20 2.1290 - 2.0929 1.00 2652 163 0.2639 0.3007 REMARK 3 21 2.0929 - 2.0592 1.00 2695 147 0.2759 0.3076 REMARK 3 22 2.0592 - 2.0275 1.00 2758 151 0.2958 0.2812 REMARK 3 23 2.0275 - 1.9977 0.90 2420 149 0.3095 0.3509 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.190 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.60 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 : 0.009 3668 REMARK 3 ANGLE : 1.186 4909 REMARK 3 CHIRALITY : 0.052 544 REMARK 3 PLANARITY : 0.006 592 REMARK 3 DIHEDRAL : 13.416 1921 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ -1:208 OR RESSEQ 219:305 OR REMARK 3 RESSEQ 1201)) REMARK 3 ORIGIN FOR THE GROUP (A): -22.0262 -6.8298 17.9139 REMARK 3 T TENSOR REMARK 3 T11: 0.1546 T22: 0.1885 REMARK 3 T33: 0.1225 T12: -0.0061 REMARK 3 T13: 0.0019 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 1.1457 L22: 1.7163 REMARK 3 L33: 1.5380 L12: 0.2469 REMARK 3 L13: 0.2009 L23: 0.1413 REMARK 3 S TENSOR REMARK 3 S11: -0.0126 S12: 0.0109 S13: -0.1076 REMARK 3 S21: -0.1188 S22: -0.0149 S23: -0.0502 REMARK 3 S31: 0.1797 S32: -0.0684 S33: 0.0344 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ 1001:1106)) REMARK 3 ORIGIN FOR THE GROUP (A): 0.5976 -54.9833 20.1385 REMARK 3 T TENSOR REMARK 3 T11: 0.4223 T22: 0.3671 REMARK 3 T33: 0.8546 T12: 0.0597 REMARK 3 T13: -0.0041 T23: -0.0845 REMARK 3 L TENSOR REMARK 3 L11: 1.4719 L22: 7.3501 REMARK 3 L33: 5.6253 L12: -1.7882 REMARK 3 L13: 1.2922 L23: -1.9988 REMARK 3 S TENSOR REMARK 3 S11: 0.0917 S12: -0.2537 S13: 0.5615 REMARK 3 S21: -0.3813 S22: 0.0637 S23: -0.2192 REMARK 3 S31: 0.0754 S32: 0.0632 S33: -0.1574 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 5OLV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1200006023. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-SEP-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.3-5.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96857 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34210 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.998 REMARK 200 RESOLUTION RANGE LOW (A) : 76.080 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 1.08200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5MZJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH: 0.L M TRI-SODIUM REMARK 280 CITRATE PH 5.3-5.4, 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2% REMARK 280 (V/V) 2,5-HEXANEDIOL AND 0.5 MM THEOPHYLLINE LUAA47070 WAS ADDED REMARK 280 TO THE MOTHER LIQUOR TO A CONCENTRATION OF 0.005 MM FOR THE REMARK 280 SOAKING EXPERIMENTS., LIPIDIC CUBIC PHASE, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 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 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z 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 70.45150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.45150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.71450 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.38700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.71450 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.38700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.45150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.71450 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.38700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.45150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.71450 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.38700 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 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 TOTAL BURIED SURFACE AREA: 8230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21450 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 40.0 KCAL/MOL 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O23 OLC A 1220 C24 OLC A 1222 1.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -55.64 -122.42 REMARK 500 TYR A1101 -57.53 -126.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 LEU A 208 -10.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 1207 REMARK 610 OLA A 1208 REMARK 610 OLA A 1209 REMARK 610 OLA A 1210 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1217 REMARK 610 OLC A 1218 REMARK 610 OLC A 1219 REMARK 610 OLC A 1220 REMARK 610 OLC A 1221 REMARK 610 OLC A 1223 REMARK 610 OLC A 1224 REMARK 610 OLC A 1225 REMARK 610 OLC A 1226 REMARK 610 OLA A 1228 REMARK 610 OLC A 1229 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1202 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 122.9 REMARK 620 3 HOH A1311 O 98.4 119.2 REMARK 620 4 HOH A1378 O 87.1 125.9 95.4 REMARK 620 5 HOH A1360 O 77.6 62.3 90.1 164.4 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 9Y2 A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1228 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1229 DBREF 5OLV A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5OLV A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5OLV A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5OLV ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5OLV ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5OLV TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5OLV LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5OLV ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5OLV ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5OLV ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5OLV ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5OLV GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5OLV ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5OLV PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5OLV LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5OLV ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5OLV ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5OLV ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5OLV ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5OLV ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5OLV TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5OLV ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5OLV LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5OLV ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5OLV ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5OLV ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5OLV ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5OLV HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 434 ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE SEQRES 2 A 434 MET GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE SEQRES 3 A 434 ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP SEQRES 4 A 434 ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN SEQRES 5 A 434 TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL SEQRES 6 A 434 GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR SEQRES 7 A 434 GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA SEQRES 8 A 434 CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER SEQRES 9 A 434 LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA SEQRES 10 A 434 ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG SEQRES 11 A 434 ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE SEQRES 12 A 434 ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS SEQRES 13 A 434 GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS SEQRES 14 A 434 GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL SEQRES 15 A 434 PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS SEQRES 16 A 434 VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU SEQRES 17 A 434 ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU SEQRES 18 A 434 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL SEQRES 19 A 434 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA SEQRES 20 A 434 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS SEQRES 21 A 434 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER SEQRES 22 A 434 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU SEQRES 23 A 434 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU SEQRES 24 A 434 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU SEQRES 25 A 434 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU SEQRES 26 A 434 ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA SEQRES 27 A 434 LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS SEQRES 28 A 434 TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE SEQRES 29 A 434 CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR SEQRES 30 A 434 LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN SEQRES 31 A 434 PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN SEQRES 32 A 434 THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN SEQRES 33 A 434 GLN GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 34 A 434 HIS HIS HIS HIS HIS HET 9Y2 A1201 24 HET NA A1202 1 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET CLR A1206 28 HET OLA A1207 15 HET OLA A1208 9 HET OLA A1209 9 HET OLA A1210 18 HET OLA A1211 20 HET OLA A1212 12 HET OLA A1213 8 HET OLA A1214 15 HET OLA A1215 19 HET OLA A1216 20 HET OLA A1217 9 HET OLC A1218 17 HET OLC A1219 18 HET OLC A1220 22 HET OLC A1221 20 HET OLC A1222 25 HET OLC A1223 24 HET OLC A1224 18 HET OLC A1225 19 HET OLC A1226 20 HET OLA A1227 20 HET OLA A1228 9 HET OLC A1229 13 HETNAM 9Y2 4-(3,3-DIMETHYLBUTANOYLAMINO)-3,5-BIS(FLUORANYL)-~{N}- HETNAM 2 9Y2 (1,3-THIAZOL-2-YL)BENZAMIDE HETNAM NA SODIUM ION HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 9Y2 C16 H17 F2 N3 O2 S FORMUL 3 NA NA 1+ FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 13(C18 H34 O2) FORMUL 19 OLC 10(C21 H40 O4) FORMUL 31 HOH *115(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ILE A 108 VAL A 116 1 9 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 LYS A 1059 GLU A 1081 1 23 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 SER A 305 1 14 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.06 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.07 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.07 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.06 LINK OD1 ASP A 52 NA NA A1202 1555 1555 2.45 LINK OG SER A 91 NA NA A1202 1555 1555 2.60 LINK NA NA A1202 O HOH A1311 1555 1555 2.60 LINK NA NA A1202 O HOH A1378 1555 1555 2.32 LINK NA NA A1202 O HOH A1360 1555 1555 2.86 SITE 1 AC1 13 ALA A 63 ILE A 66 VAL A 84 PHE A 168 SITE 2 AC1 13 MET A 177 LEU A 249 HIS A 250 ASN A 253 SITE 3 AC1 13 ILE A 274 HOH A1325 HOH A1335 HOH A1370 SITE 4 AC1 13 HOH A1383 SITE 1 AC2 5 ASP A 52 SER A 91 HOH A1311 HOH A1360 SITE 2 AC2 5 HOH A1378 SITE 1 AC3 5 HIS A 75 GLY A 76 OLC A1218 HOH A1318 SITE 2 AC3 5 HOH A1343 SITE 1 AC4 7 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC4 7 CLR A1206 OLC A1222 OLC A1225 SITE 1 AC5 6 PRO A 248 CYS A 262 SER A 263 LEU A 269 SITE 2 AC5 6 OLA A1207 OLA A1214 SITE 1 AC6 5 PHE A 255 PHE A 258 CLR A1204 OLC A1222 SITE 2 AC6 5 HOH A1346 SITE 1 AC7 2 LEU A 272 CLR A1205 SITE 1 AC8 3 PHE A 44 ALA A 97 VAL A 116 SITE 1 AC9 2 THR A 279 VAL A 282 SITE 1 AD1 3 GLY A 5 TRP A 268 VAL A 275 SITE 1 AD2 3 SER A 7 LEU A 26 PHE A 286 SITE 1 AD3 3 CLR A1205 OLA A1216 OLC A1220 SITE 1 AD4 4 CYS A 28 TRP A 29 TRP A 32 LYS A 233 SITE 1 AD5 2 THR A 65 OLA A1214 SITE 1 AD6 2 TYR A 197 OLC A1229 SITE 1 AD7 4 TYR A 179 PHE A 258 CLR A1203 OLC A1225 SITE 1 AD8 6 PRO A 2 SER A 6 SER A 67 THR A 68 SITE 2 AD8 6 HOH A1301 HOH A1345 SITE 1 AD9 5 PHE A 255 ASP A 261 LYS A1085 OLA A1214 SITE 2 AD9 5 OLC A1222 SITE 1 AE1 3 LEU A 141 OLC A1226 OLA A1228 SITE 1 AE2 7 THR A 65 CYS A 71 CYS A 259 ASP A 261 SITE 2 AE2 7 CLR A1204 CLR A1206 OLC A1220 SITE 1 AE3 4 TYR A 43 PHE A 83 ILE A 125 TRP A 129 SITE 1 AE4 8 CYS A 28 VAL A 31 TRP A 32 GLN A 38 SITE 2 AE4 8 TYR A 43 ALA A 50 LEU A 54 ARG A 205 SITE 1 AE5 9 ALA A 73 GLN A 163 PHE A 183 LEU A 187 SITE 2 AE5 9 PHE A 258 CLR A1204 OLC A1218 HOH A1318 SITE 3 AE5 9 HOH A1346 SITE 1 AE6 9 HIS A 75 MET A 140 LEU A 141 GLY A 142 SITE 2 AE6 9 ASN A 144 TYR A 179 ALA A 184 OLC A1221 SITE 3 AE6 9 OLA A1228 SITE 1 AE7 2 SER A 7 THR A 11 SITE 1 AE8 3 HIS A 75 OLC A1221 OLC A1226 SITE 1 AE9 6 ALA A 236 ILE A 237 GLY A 240 LEU A 244 SITE 2 AE9 6 OLA A1217 HOH A1302 CRYST1 39.429 180.774 140.903 90.00 90.00 90.00 C 2 2 21 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 0.025362 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005532 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007097 0.00000 ATOM 1 N GLY A -1 -20.731 24.840 1.361 1.00 89.01 N ANISOU 1 N GLY A -1 13497 9884 10437 -333 -836 1512 N ATOM 2 CA GLY A -1 -21.177 23.618 2.011 1.00 86.79 C ANISOU 2 CA GLY A -1 13086 9722 10167 -262 -840 1424 C ATOM 3 C GLY A -1 -22.443 23.032 1.405 1.00 85.38 C ANISOU 3 C GLY A -1 12888 9624 9930 -145 -948 1409 C ATOM 4 O GLY A -1 -23.510 23.645 1.474 1.00 87.14 O ANISOU 4 O GLY A -1 13117 9779 10213 -21 -1086 1407 O ATOM 5 N ALA A 0 -22.319 21.843 0.813 1.00 81.22 N ANISOU 5 N ALA A 0 12328 9242 9291 -185 -882 1394 N ATOM 6 CA ALA A 0 -23.438 21.221 0.120 1.00 79.41 C ANISOU 6 CA ALA A 0 12081 9095 8994 -99 -977 1379 C ATOM 7 C ALA A 0 -24.593 20.940 1.085 1.00 76.64 C ANISOU 7 C ALA A 0 11606 8761 8753 50 -1093 1298 C ATOM 8 O ALA A 0 -24.367 20.682 2.275 1.00 75.36 O ANISOU 8 O ALA A 0 11354 8600 8681 70 -1062 1235 O ATOM 9 CB ALA A 0 -22.989 19.922 -0.544 1.00 78.17 C ANISOU 9 CB ALA A 0 11906 9087 8708 -177 -870 1357 C ATOM 10 N PRO A 1 -25.837 20.976 0.596 1.00 73.33 N ANISOU 10 N PRO A 1 11172 8360 8332 154 -1226 1295 N ATOM 11 CA PRO A 1 -27.000 20.707 1.467 1.00 69.97 C ANISOU 11 CA PRO A 1 10605 7964 8018 297 -1329 1212 C ATOM 12 C PRO A 1 -26.819 19.411 2.237 1.00 66.94 C ANISOU 12 C PRO A 1 10097 7701 7638 285 -1260 1126 C ATOM 13 O PRO A 1 -26.509 18.359 1.654 1.00 65.60 O ANISOU 13 O PRO A 1 9928 7641 7357 211 -1193 1119 O ATOM 14 CB PRO A 1 -28.175 20.613 0.478 1.00 68.86 C ANISOU 14 CB PRO A 1 10466 7869 7828 363 -1451 1230 C ATOM 15 CG PRO A 1 -27.735 21.393 -0.711 1.00 70.58 C ANISOU 15 CG PRO A 1 10854 8014 7948 290 -1450 1337 C ATOM 16 CD PRO A 1 -26.239 21.233 -0.802 1.00 71.93 C ANISOU 16 CD PRO A 1 11099 8184 8046 141 -1286 1367 C ATOM 17 N PRO A 2 -26.973 19.453 3.561 1.00 64.64 N ANISOU 17 N PRO A 2 9701 7388 7469 356 -1269 1056 N ATOM 18 CA PRO A 2 -26.719 18.245 4.364 1.00 57.55 C ANISOU 18 CA PRO A 2 8644 6625 6599 330 -1159 949 C ATOM 19 C PRO A 2 -27.649 17.091 4.037 1.00 51.06 C ANISOU 19 C PRO A 2 7734 5936 5732 370 -1210 903 C ATOM 20 O PRO A 2 -27.278 15.934 4.269 1.00 49.20 O ANISOU 20 O PRO A 2 7412 5813 5470 313 -1107 839 O ATOM 21 CB PRO A 2 -26.911 18.736 5.808 1.00 59.09 C ANISOU 21 CB PRO A 2 8719 6778 6953 407 -1151 861 C ATOM 22 CG PRO A 2 -26.668 20.231 5.739 1.00 63.41 C ANISOU 22 CG PRO A 2 9401 7149 7543 421 -1206 933 C ATOM 23 CD PRO A 2 -27.244 20.636 4.398 1.00 65.87 C ANISOU 23 CD PRO A 2 9851 7412 7763 444 -1327 1042 C ATOM 24 N ILE A 3 -28.835 17.356 3.484 1.00 52.86 N ANISOU 24 N ILE A 3 7974 6154 5957 462 -1363 930 N ATOM 25 CA ILE A 3 -29.744 16.266 3.159 1.00 55.36 C ANISOU 25 CA ILE A 3 8191 6600 6242 485 -1409 878 C ATOM 26 C ILE A 3 -29.180 15.362 2.057 1.00 57.27 C ANISOU 26 C ILE A 3 8518 6917 6324 368 -1343 906 C ATOM 27 O ILE A 3 -29.572 14.192 1.952 1.00 55.93 O ANISOU 27 O ILE A 3 8274 6859 6117 353 -1340 849 O ATOM 28 CB ILE A 3 -31.127 16.814 2.757 1.00 54.79 C ANISOU 28 CB ILE A 3 8072 6518 6229 591 -1551 881 C ATOM 29 CG1 ILE A 3 -32.200 15.749 2.999 1.00 56.08 C ANISOU 29 CG1 ILE A 3 8068 6813 6427 636 -1598 798 C ATOM 30 CG2 ILE A 3 -31.121 17.224 1.299 1.00 55.83 C ANISOU 30 CG2 ILE A 3 8347 6618 6247 545 -1595 972 C ATOM 31 CD1 ILE A 3 -33.508 16.004 2.287 1.00 59.55 C ANISOU 31 CD1 ILE A 3 8465 7274 6887 707 -1730 810 C ATOM 32 N MET A 4 -28.258 15.868 1.235 1.00 54.52 N ANISOU 32 N MET A 4 8323 6510 5882 280 -1280 986 N ATOM 33 CA MET A 4 -27.684 15.037 0.181 1.00 49.20 C ANISOU 33 CA MET A 4 7727 5910 5057 174 -1199 1001 C ATOM 34 C MET A 4 -26.737 13.985 0.755 1.00 46.66 C ANISOU 34 C MET A 4 7364 5656 4708 101 -1058 947 C ATOM 35 O MET A 4 -26.894 12.782 0.491 1.00 43.77 O ANISOU 35 O MET A 4 6958 5392 4282 74 -1031 891 O ATOM 36 CB MET A 4 -26.975 15.921 -0.839 1.00 44.02 C ANISOU 36 CB MET A 4 7234 5177 4315 102 -1161 1098 C ATOM 37 CG MET A 4 -27.898 16.934 -1.447 1.00 45.27 C ANISOU 37 CG MET A 4 7445 5264 4492 174 -1304 1156 C ATOM 38 SD MET A 4 -27.104 17.812 -2.788 1.00 53.57 S ANISOU 38 SD MET A 4 8697 6241 5416 78 -1261 1271 S ATOM 39 CE MET A 4 -26.705 16.466 -3.920 1.00 55.75 C ANISOU 39 CE MET A 4 9017 6651 5514 -22 -1169 1246 C ATOM 40 N GLY A 5 -25.754 14.415 1.553 1.00 42.81 N ANISOU 40 N GLY A 5 6862 5118 4286 66 -955 948 N ATOM 41 CA GLY A 5 -24.854 13.457 2.169 1.00 38.81 C ANISOU 41 CA GLY A 5 6253 4687 3805 5 -794 870 C ATOM 42 C GLY A 5 -25.572 12.545 3.144 1.00 40.86 C ANISOU 42 C GLY A 5 6336 5029 4161 71 -809 762 C ATOM 43 O GLY A 5 -25.268 11.347 3.235 1.00 42.41 O ANISOU 43 O GLY A 5 6469 5311 4333 32 -724 700 O ATOM 44 N ASER A 6 -26.536 13.083 3.890 0.71 38.42 N ANISOU 44 N ASER A 6 5945 4690 3963 170 -913 738 N ATOM 45 N BSER A 6 -26.528 13.100 3.895 0.29 38.66 N ANISOU 45 N BSER A 6 5976 4719 3995 170 -913 739 N ATOM 46 CA ASER A 6 -27.258 12.202 4.797 0.71 37.02 C ANISOU 46 CA ASER A 6 5601 4598 3869 222 -919 640 C ATOM 47 CA BSER A 6 -27.336 12.285 4.795 0.29 36.61 C ANISOU 47 CA BSER A 6 5550 4540 3821 229 -930 642 C ATOM 48 C ASER A 6 -28.158 11.236 4.032 0.71 33.54 C ANISOU 48 C ASER A 6 5151 4239 3352 226 -994 622 C ATOM 49 C BSER A 6 -28.133 11.245 4.022 0.29 33.71 C ANISOU 49 C BSER A 6 5176 4260 3372 224 -993 623 C ATOM 50 O ASER A 6 -28.419 10.135 4.520 0.71 32.40 O ANISOU 50 O ASER A 6 4897 4179 3235 218 -957 545 O ATOM 51 O BSER A 6 -28.316 10.117 4.492 0.29 31.97 O ANISOU 51 O BSER A 6 4849 4123 3174 211 -947 547 O ATOM 52 CB ASER A 6 -28.050 13.014 5.824 0.71 37.44 C ANISOU 52 CB ASER A 6 5560 4607 4060 327 -993 608 C ATOM 53 CB BSER A 6 -28.273 13.176 5.613 0.29 37.49 C ANISOU 53 CB BSER A 6 5584 4602 4058 341 -1029 622 C ATOM 54 OG ASER A 6 -28.991 13.857 5.210 0.71 38.69 O ANISOU 54 OG ASER A 6 5776 4707 4216 404 -1143 662 O ATOM 55 OG BSER A 6 -27.545 14.151 6.336 0.29 37.56 O ANISOU 55 OG BSER A 6 5610 4521 4138 342 -977 632 O ATOM 56 N SER A 7 -28.609 11.607 2.828 1.00 31.46 N ANISOU 56 N SER A 7 5014 3952 2989 229 -1103 694 N ATOM 57 CA SER A 7 -29.393 10.674 2.021 1.00 33.74 C ANISOU 57 CA SER A 7 5308 4319 3191 218 -1182 675 C ATOM 58 C SER A 7 -28.598 9.418 1.690 1.00 31.15 C ANISOU 58 C SER A 7 5004 4058 2772 121 -1053 632 C ATOM 59 O SER A 7 -29.125 8.303 1.808 1.00 28.49 O ANISOU 59 O SER A 7 4586 3800 2439 112 -1061 561 O ATOM 60 CB SER A 7 -29.864 11.330 0.727 1.00 37.84 C ANISOU 60 CB SER A 7 5946 4803 3627 225 -1285 751 C ATOM 61 OG SER A 7 -30.913 12.238 0.996 1.00 44.25 O ANISOU 61 OG SER A 7 6692 5574 4547 330 -1413 765 O ATOM 62 N VAL A 8 -27.330 9.580 1.282 1.00 25.85 N ANISOU 62 N VAL A 8 4441 3356 2026 46 -929 671 N ATOM 63 CA VAL A 8 -26.493 8.419 0.988 1.00 28.04 C ANISOU 63 CA VAL A 8 4736 3692 2228 -34 -794 624 C ATOM 64 C VAL A 8 -26.298 7.570 2.245 1.00 27.30 C ANISOU 64 C VAL A 8 4477 3641 2256 -22 -707 532 C ATOM 65 O VAL A 8 -26.514 6.352 2.228 1.00 22.79 O ANISOU 65 O VAL A 8 3862 3132 1666 -42 -685 465 O ATOM 66 CB VAL A 8 -25.141 8.849 0.400 1.00 29.09 C ANISOU 66 CB VAL A 8 4991 3786 2275 -111 -666 681 C ATOM 67 CG1 VAL A 8 -24.282 7.597 0.158 1.00 28.55 C ANISOU 67 CG1 VAL A 8 4921 3781 2146 -176 -517 618 C ATOM 68 CG2 VAL A 8 -25.339 9.619 -0.884 1.00 32.37 C ANISOU 68 CG2 VAL A 8 5569 4161 2568 -130 -737 771 C ATOM 69 N TYR A 9 -25.875 8.208 3.351 1.00 24.21 N ANISOU 69 N TYR A 9 4003 3212 1986 6 -660 530 N ATOM 70 CA TYR A 9 -25.671 7.498 4.608 1.00 22.55 C ANISOU 70 CA TYR A 9 3647 3039 1884 17 -586 453 C ATOM 71 C TYR A 9 -26.939 6.753 5.041 1.00 21.65 C ANISOU 71 C TYR A 9 3426 2982 1816 61 -669 393 C ATOM 72 O TYR A 9 -26.875 5.570 5.405 1.00 20.34 O ANISOU 72 O TYR A 9 3197 2868 1663 36 -613 331 O ATOM 73 CB TYR A 9 -25.194 8.488 5.687 1.00 25.46 C ANISOU 73 CB TYR A 9 3958 3352 2363 45 -555 463 C ATOM 74 CG TYR A 9 -25.378 7.986 7.106 1.00 23.92 C ANISOU 74 CG TYR A 9 3614 3194 2281 78 -526 390 C ATOM 75 CD1 TYR A 9 -24.529 6.997 7.624 1.00 20.46 C ANISOU 75 CD1 TYR A 9 3122 2795 1858 37 -413 345 C ATOM 76 CD2 TYR A 9 -26.382 8.500 7.929 1.00 17.78 C ANISOU 76 CD2 TYR A 9 2753 2410 1593 153 -607 366 C ATOM 77 CE1 TYR A 9 -24.690 6.508 8.885 1.00 21.30 C ANISOU 77 CE1 TYR A 9 3109 2932 2050 60 -391 288 C ATOM 78 CE2 TYR A 9 -26.552 8.012 9.235 1.00 21.72 C ANISOU 78 CE2 TYR A 9 3124 2950 2178 174 -569 299 C ATOM 79 CZ TYR A 9 -25.701 7.020 9.701 1.00 23.87 C ANISOU 79 CZ TYR A 9 3360 3258 2450 124 -465 266 C ATOM 80 OH TYR A 9 -25.841 6.507 10.961 1.00 22.92 O ANISOU 80 OH TYR A 9 3133 3176 2400 138 -432 211 O ATOM 81 N ILE A 10 -28.102 7.417 4.987 1.00 19.81 N ANISOU 81 N ILE A 10 3172 2739 1615 125 -804 411 N ATOM 82 CA ILE A 10 -29.349 6.797 5.446 1.00 27.78 C ANISOU 82 CA ILE A 10 4059 3811 2685 163 -881 353 C ATOM 83 C ILE A 10 -29.764 5.636 4.538 1.00 27.71 C ANISOU 83 C ILE A 10 4087 3859 2583 111 -915 329 C ATOM 84 O ILE A 10 -30.237 4.596 5.020 1.00 22.86 O ANISOU 84 O ILE A 10 3377 3302 2007 93 -903 264 O ATOM 85 CB ILE A 10 -30.485 7.842 5.539 1.00 29.39 C ANISOU 85 CB ILE A 10 4220 3991 2954 254 -1020 377 C ATOM 86 CG1 ILE A 10 -30.232 8.876 6.662 1.00 29.33 C ANISOU 86 CG1 ILE A 10 4158 3928 3059 314 -985 374 C ATOM 87 CG2 ILE A 10 -31.873 7.142 5.724 1.00 23.19 C ANISOU 87 CG2 ILE A 10 3308 3287 2218 282 -1111 322 C ATOM 88 CD1 ILE A 10 -31.323 9.976 6.669 1.00 27.29 C ANISOU 88 CD1 ILE A 10 3870 3632 2868 419 -1122 396 C ATOM 89 N THR A 11 -29.629 5.803 3.216 1.00 24.12 N ANISOU 89 N THR A 11 3778 3388 1999 80 -962 378 N ATOM 90 CA THR A 11 -29.950 4.706 2.300 1.00 25.68 C ANISOU 90 CA THR A 11 4032 3635 2092 23 -993 347 C ATOM 91 C THR A 11 -29.081 3.475 2.565 1.00 23.09 C ANISOU 91 C THR A 11 3696 3329 1749 -39 -847 285 C ATOM 92 O THR A 11 -29.580 2.348 2.603 1.00 25.11 O ANISOU 92 O THR A 11 3907 3627 2005 -70 -860 223 O ATOM 93 CB THR A 11 -29.790 5.161 0.854 1.00 25.19 C ANISOU 93 CB THR A 11 4150 3548 1873 -5 -1051 414 C ATOM 94 OG1 THR A 11 -30.658 6.274 0.612 1.00 26.10 O ANISOU 94 OG1 THR A 11 4267 3635 2014 63 -1199 474 O ATOM 95 CG2 THR A 11 -30.173 4.007 -0.116 1.00 23.71 C ANISOU 95 CG2 THR A 11 4023 3413 1574 -65 -1085 367 C ATOM 96 N VAL A 12 -27.787 3.675 2.788 1.00 22.48 N ANISOU 96 N VAL A 12 3655 3217 1670 -58 -711 300 N ATOM 97 CA VAL A 12 -26.899 2.560 3.103 1.00 22.25 C ANISOU 97 CA VAL A 12 3607 3202 1644 -100 -574 243 C ATOM 98 C VAL A 12 -27.295 1.897 4.425 1.00 22.76 C ANISOU 98 C VAL A 12 3519 3291 1836 -79 -560 187 C ATOM 99 O VAL A 12 -27.317 0.664 4.526 1.00 23.63 O ANISOU 99 O VAL A 12 3610 3424 1945 -112 -523 129 O ATOM 100 CB VAL A 12 -25.441 3.041 3.110 1.00 23.26 C ANISOU 100 CB VAL A 12 3783 3294 1760 -119 -440 276 C ATOM 101 CG1 VAL A 12 -24.516 1.942 3.645 1.00 24.44 C ANISOU 101 CG1 VAL A 12 3882 3456 1947 -140 -306 216 C ATOM 102 CG2 VAL A 12 -25.020 3.525 1.665 1.00 22.35 C ANISOU 102 CG2 VAL A 12 3839 3163 1492 -160 -433 332 C ATOM 103 N GLU A 13 -27.581 2.701 5.471 1.00 18.24 N ANISOU 103 N GLU A 13 2847 2710 1373 -27 -583 202 N ATOM 104 CA GLU A 13 -28.033 2.135 6.746 1.00 17.08 C ANISOU 104 CA GLU A 13 2562 2593 1333 -11 -569 153 C ATOM 105 C GLU A 13 -29.269 1.277 6.556 1.00 18.62 C ANISOU 105 C GLU A 13 2711 2837 1526 -29 -654 112 C ATOM 106 O GLU A 13 -29.364 0.187 7.131 1.00 20.15 O ANISOU 106 O GLU A 13 2848 3053 1755 -61 -611 64 O ATOM 107 CB GLU A 13 -28.350 3.240 7.777 1.00 20.94 C ANISOU 107 CB GLU A 13 2964 3071 1923 51 -596 169 C ATOM 108 CG GLU A 13 -27.165 4.051 8.339 1.00 20.98 C ANISOU 108 CG GLU A 13 2984 3027 1962 62 -512 196 C ATOM 109 CD GLU A 13 -26.474 3.337 9.527 1.00 25.88 C ANISOU 109 CD GLU A 13 3528 3662 2644 47 -413 157 C ATOM 110 OE1 GLU A 13 -26.267 3.962 10.609 1.00 23.91 O ANISOU 110 OE1 GLU A 13 3218 3399 2468 77 -393 153 O ATOM 111 OE2 GLU A 13 -26.133 2.147 9.363 1.00 24.61 O ANISOU 111 OE2 GLU A 13 3377 3520 2455 7 -361 129 O ATOM 112 N LEU A 14 -30.248 1.758 5.776 1.00 18.50 N ANISOU 112 N LEU A 14 2716 2836 1476 -12 -781 132 N ATOM 113 CA LEU A 14 -31.457 0.966 5.579 1.00 23.47 C ANISOU 113 CA LEU A 14 3287 3518 2111 -37 -873 92 C ATOM 114 C LEU A 14 -31.167 -0.329 4.812 1.00 24.60 C ANISOU 114 C LEU A 14 3519 3665 2163 -116 -843 52 C ATOM 115 O LEU A 14 -31.731 -1.383 5.132 1.00 21.81 O ANISOU 115 O LEU A 14 3103 3340 1842 -159 -851 0 O ATOM 116 CB LEU A 14 -32.521 1.796 4.857 1.00 27.15 C ANISOU 116 CB LEU A 14 3755 4000 2561 4 -1031 125 C ATOM 117 CG LEU A 14 -33.013 3.021 5.641 1.00 25.57 C ANISOU 117 CG LEU A 14 3456 3793 2468 95 -1073 150 C ATOM 118 CD1 LEU A 14 -33.873 3.911 4.752 1.00 26.37 C ANISOU 118 CD1 LEU A 14 3586 3889 2542 148 -1234 196 C ATOM 119 CD2 LEU A 14 -33.772 2.564 6.881 1.00 29.27 C ANISOU 119 CD2 LEU A 14 3749 4315 3057 105 -1051 94 C ATOM 120 N ALA A 15 -30.291 -0.269 3.800 1.00 20.62 N ANISOU 120 N ALA A 15 3163 3128 1543 -138 -804 73 N ATOM 121 CA ALA A 15 -29.883 -1.482 3.094 1.00 21.61 C ANISOU 121 CA ALA A 15 3383 3249 1580 -204 -756 24 C ATOM 122 C ALA A 15 -29.267 -2.499 4.056 1.00 22.28 C ANISOU 122 C ALA A 15 3409 3320 1738 -221 -635 -24 C ATOM 123 O ALA A 15 -29.580 -3.691 4.004 1.00 21.76 O ANISOU 123 O ALA A 15 3346 3256 1667 -270 -637 -80 O ATOM 124 CB ALA A 15 -28.885 -1.122 1.991 1.00 21.25 C ANISOU 124 CB ALA A 15 3498 3174 1402 -217 -700 55 C ATOM 125 N ILE A 16 -28.400 -2.038 4.959 1.00 19.90 N ANISOU 125 N ILE A 16 3057 2997 1508 -184 -539 0 N ATOM 126 CA ILE A 16 -27.784 -2.937 5.933 1.00 17.21 C ANISOU 126 CA ILE A 16 2660 2640 1238 -192 -438 -35 C ATOM 127 C ILE A 16 -28.829 -3.512 6.888 1.00 19.31 C ANISOU 127 C ILE A 16 2810 2935 1592 -206 -485 -62 C ATOM 128 O ILE A 16 -28.778 -4.700 7.237 1.00 19.72 O ANISOU 128 O ILE A 16 2855 2973 1666 -244 -446 -103 O ATOM 129 CB ILE A 16 -26.675 -2.198 6.704 1.00 16.39 C ANISOU 129 CB ILE A 16 2523 2514 1190 -150 -346 0 C ATOM 130 CG1 ILE A 16 -25.565 -1.814 5.745 1.00 19.77 C ANISOU 130 CG1 ILE A 16 3060 2918 1534 -154 -277 22 C ATOM 131 CG2 ILE A 16 -26.150 -3.063 7.876 1.00 16.27 C ANISOU 131 CG2 ILE A 16 2436 2486 1257 -149 -266 -27 C ATOM 132 CD1 ILE A 16 -24.637 -0.765 6.372 1.00 20.57 C ANISOU 132 CD1 ILE A 16 3124 3001 1690 -121 -216 68 C ATOM 133 N ALA A 17 -29.773 -2.677 7.342 1.00 20.49 N ANISOU 133 N ALA A 17 2868 3122 1797 -175 -564 -40 N ATOM 134 CA ALA A 17 -30.802 -3.138 8.274 1.00 22.41 C ANISOU 134 CA ALA A 17 2987 3405 2124 -191 -596 -66 C ATOM 135 C ALA A 17 -31.628 -4.281 7.669 1.00 22.96 C ANISOU 135 C ALA A 17 3071 3489 2161 -265 -657 -110 C ATOM 136 O ALA A 17 -31.872 -5.294 8.330 1.00 26.59 O ANISOU 136 O ALA A 17 3486 3950 2667 -314 -625 -140 O ATOM 137 CB ALA A 17 -31.703 -1.965 8.683 1.00 17.91 C ANISOU 137 CB ALA A 17 2316 2875 1613 -135 -671 -43 C ATOM 138 N AVAL A 18 -32.066 -4.122 6.416 1.00 21.85 N ANISOU 138 N AVAL A 18 3004 3359 1940 -280 -751 -111 N ATOM 139 CA AVAL A 18 -32.834 -5.157 5.725 1.00 23.22 C ANISOU 139 CA AVAL A 18 3205 3545 2072 -358 -824 -158 C ATOM 140 C AVAL A 18 -32.047 -6.464 5.673 1.00 23.68 C ANISOU 140 C AVAL A 18 3352 3547 2100 -411 -731 -203 C ATOM 141 O AVAL A 18 -32.566 -7.546 5.996 1.00 23.79 O ANISOU 141 O AVAL A 18 3334 3555 2150 -478 -738 -243 O ATOM 142 CB AVAL A 18 -33.218 -4.666 4.314 1.00 26.27 C ANISOU 142 CB AVAL A 18 3685 3946 2351 -358 -941 -147 C ATOM 143 CG1AVAL A 18 -33.747 -5.796 3.458 1.00 26.02 C ANISOU 143 CG1AVAL A 18 3721 3915 2251 -447 -1008 -205 C ATOM 144 CG2AVAL A 18 -34.243 -3.506 4.376 1.00 25.14 C ANISOU 144 CG2AVAL A 18 3439 3855 2257 -303 -1062 -108 C ATOM 145 N LEU A 19 -30.776 -6.383 5.271 1.00 21.78 N ANISOU 145 N LEU A 19 3220 3259 1798 -382 -640 -195 N ATOM 146 CA LEU A 19 -29.979 -7.595 5.117 1.00 24.30 C ANISOU 146 CA LEU A 19 3627 3518 2089 -416 -551 -243 C ATOM 147 C LEU A 19 -29.637 -8.206 6.469 1.00 21.73 C ANISOU 147 C LEU A 19 3220 3165 1870 -412 -469 -243 C ATOM 148 O LEU A 19 -29.545 -9.429 6.581 1.00 22.08 O ANISOU 148 O LEU A 19 3302 3161 1925 -456 -439 -286 O ATOM 149 CB LEU A 19 -28.697 -7.304 4.332 1.00 23.17 C ANISOU 149 CB LEU A 19 3604 3342 1859 -381 -465 -238 C ATOM 150 CG LEU A 19 -28.823 -6.907 2.855 1.00 23.12 C ANISOU 150 CG LEU A 19 3723 3350 1712 -397 -524 -241 C ATOM 151 CD1 LEU A 19 -27.476 -6.291 2.376 1.00 23.45 C ANISOU 151 CD1 LEU A 19 3848 3372 1690 -355 -413 -214 C ATOM 152 CD2 LEU A 19 -29.220 -8.086 1.962 1.00 24.93 C ANISOU 152 CD2 LEU A 19 4057 3557 1859 -467 -564 -317 C ATOM 153 N ALA A 20 -29.463 -7.371 7.502 1.00 21.52 N ANISOU 153 N ALA A 20 3095 3164 1919 -360 -440 -196 N ATOM 154 CA ALA A 20 -29.204 -7.899 8.843 1.00 22.92 C ANISOU 154 CA ALA A 20 3200 3323 2185 -359 -374 -189 C ATOM 155 C ALA A 20 -30.410 -8.681 9.359 1.00 24.49 C ANISOU 155 C ALA A 20 3330 3542 2432 -429 -426 -210 C ATOM 156 O ALA A 20 -30.257 -9.735 9.986 1.00 24.90 O ANISOU 156 O ALA A 20 3388 3551 2520 -467 -381 -223 O ATOM 157 CB ALA A 20 -28.858 -6.754 9.803 1.00 20.75 C ANISOU 157 CB ALA A 20 2840 3077 1965 -294 -343 -141 C ATOM 158 N ILE A 21 -31.617 -8.185 9.085 1.00 21.00 N ANISOU 158 N ILE A 21 2821 3165 1994 -450 -523 -211 N ATOM 159 CA ILE A 21 -32.820 -8.855 9.559 1.00 23.69 C ANISOU 159 CA ILE A 21 3075 3539 2388 -526 -570 -230 C ATOM 160 C ILE A 21 -33.043 -10.153 8.789 1.00 26.56 C ANISOU 160 C ILE A 21 3529 3854 2710 -615 -600 -281 C ATOM 161 O ILE A 21 -33.228 -11.225 9.384 1.00 29.21 O ANISOU 161 O ILE A 21 3858 4153 3087 -682 -570 -296 O ATOM 162 CB ILE A 21 -34.032 -7.908 9.456 1.00 24.28 C ANISOU 162 CB ILE A 21 3033 3701 2490 -512 -668 -221 C ATOM 163 CG1 ILE A 21 -33.891 -6.743 10.470 1.00 20.62 C ANISOU 163 CG1 ILE A 21 2474 3276 2086 -428 -625 -182 C ATOM 164 CG2 ILE A 21 -35.312 -8.687 9.682 1.00 26.41 C ANISOU 164 CG2 ILE A 21 3212 4013 2810 -606 -724 -250 C ATOM 165 CD1 ILE A 21 -34.706 -5.457 10.109 1.00 22.60 C ANISOU 165 CD1 ILE A 21 2647 3588 2351 -367 -720 -168 C ATOM 166 N LEU A 22 -32.976 -10.088 7.455 1.00 24.55 N ANISOU 166 N LEU A 22 3376 3588 2365 -618 -658 -308 N ATOM 167 CA LEU A 22 -33.248 -11.272 6.640 1.00 23.77 C ANISOU 167 CA LEU A 22 3375 3443 2216 -705 -699 -368 C ATOM 168 C LEU A 22 -32.255 -12.399 6.925 1.00 25.74 C ANISOU 168 C LEU A 22 3720 3590 2469 -715 -594 -393 C ATOM 169 O LEU A 22 -32.648 -13.560 7.074 1.00 26.65 O ANISOU 169 O LEU A 22 3860 3655 2610 -799 -604 -429 O ATOM 170 CB LEU A 22 -33.227 -10.911 5.155 1.00 28.01 C ANISOU 170 CB LEU A 22 4021 3987 2633 -699 -772 -392 C ATOM 171 CG LEU A 22 -34.381 -10.081 4.573 1.00 34.55 C ANISOU 171 CG LEU A 22 4784 4902 3443 -706 -916 -378 C ATOM 172 CD1 LEU A 22 -34.160 -9.864 3.074 1.00 34.26 C ANISOU 172 CD1 LEU A 22 4897 4859 3263 -705 -979 -398 C ATOM 173 CD2 LEU A 22 -35.701 -10.764 4.808 1.00 40.48 C ANISOU 173 CD2 LEU A 22 5435 5689 4256 -804 -1007 -409 C ATOM 174 N GLY A 23 -30.961 -12.091 6.980 1.00 22.26 N ANISOU 174 N GLY A 23 3336 3112 2010 -632 -498 -376 N ATOM 175 CA GLY A 23 -29.988 -13.155 7.142 1.00 21.44 C ANISOU 175 CA GLY A 23 3322 2910 1916 -626 -408 -405 C ATOM 176 C GLY A 23 -30.078 -13.808 8.507 1.00 22.99 C ANISOU 176 C GLY A 23 3449 3074 2211 -650 -369 -377 C ATOM 177 O GLY A 23 -29.990 -15.037 8.630 1.00 25.59 O ANISOU 177 O GLY A 23 3845 3316 2560 -697 -350 -408 O ATOM 178 N ASN A 24 -30.269 -13.005 9.552 1.00 19.86 N ANISOU 178 N ASN A 24 2930 2742 1874 -619 -359 -318 N ATOM 179 CA ASN A 24 -30.275 -13.575 10.892 1.00 23.58 C ANISOU 179 CA ASN A 24 3349 3187 2423 -641 -315 -284 C ATOM 180 C ASN A 24 -31.614 -14.212 11.257 1.00 25.73 C ANISOU 180 C ASN A 24 3563 3480 2732 -754 -370 -291 C ATOM 181 O ASN A 24 -31.640 -15.179 12.030 1.00 27.95 O ANISOU 181 O ASN A 24 3860 3703 3057 -807 -338 -279 O ATOM 182 CB ASN A 24 -29.834 -12.502 11.877 1.00 20.08 C ANISOU 182 CB ASN A 24 2814 2799 2015 -564 -272 -227 C ATOM 183 CG ASN A 24 -28.372 -12.232 11.739 1.00 19.78 C ANISOU 183 CG ASN A 24 2834 2719 1963 -474 -204 -218 C ATOM 184 OD1 ASN A 24 -27.552 -13.062 12.155 1.00 23.14 O ANISOU 184 OD1 ASN A 24 3310 3068 2415 -457 -150 -216 O ATOM 185 ND2 ASN A 24 -28.015 -11.125 11.074 1.00 18.88 N ANISOU 185 ND2 ASN A 24 2718 2648 1808 -417 -208 -214 N ATOM 186 N VAL A 25 -32.718 -13.739 10.679 1.00 24.45 N ANISOU 186 N VAL A 25 3338 3396 2555 -797 -456 -310 N ATOM 187 CA VAL A 25 -33.968 -14.488 10.790 1.00 27.74 C ANISOU 187 CA VAL A 25 3706 3829 3006 -920 -513 -330 C ATOM 188 C VAL A 25 -33.799 -15.878 10.187 1.00 28.31 C ANISOU 188 C VAL A 25 3915 3787 3054 -997 -522 -381 C ATOM 189 O VAL A 25 -34.285 -16.871 10.740 1.00 30.27 O ANISOU 189 O VAL A 25 4162 3990 3349 -1096 -517 -381 O ATOM 190 CB VAL A 25 -35.123 -13.694 10.144 1.00 28.68 C ANISOU 190 CB VAL A 25 3727 4054 3116 -940 -619 -346 C ATOM 191 CG1 VAL A 25 -36.303 -14.609 9.766 1.00 29.92 C ANISOU 191 CG1 VAL A 25 3863 4216 3291 -1079 -701 -389 C ATOM 192 CG2 VAL A 25 -35.565 -12.591 11.106 1.00 26.71 C ANISOU 192 CG2 VAL A 25 3318 3905 2925 -888 -601 -299 C ATOM 193 N LEU A 26 -33.050 -15.984 9.081 1.00 24.91 N ANISOU 193 N LEU A 26 3615 3302 2549 -952 -525 -426 N ATOM 194 CA LEU A 26 -32.799 -17.298 8.482 1.00 28.39 C ANISOU 194 CA LEU A 26 4202 3622 2963 -1011 -524 -487 C ATOM 195 C LEU A 26 -31.974 -18.199 9.412 1.00 29.41 C ANISOU 195 C LEU A 26 4386 3640 3149 -994 -433 -464 C ATOM 196 O LEU A 26 -32.230 -19.408 9.509 1.00 28.54 O ANISOU 196 O LEU A 26 4346 3433 3065 -1080 -442 -490 O ATOM 197 CB LEU A 26 -32.103 -17.116 7.132 1.00 32.14 C ANISOU 197 CB LEU A 26 4803 4072 3336 -954 -529 -544 C ATOM 198 CG LEU A 26 -31.865 -18.365 6.291 1.00 41.41 C ANISOU 198 CG LEU A 26 6144 5127 4463 -1004 -532 -629 C ATOM 199 CD1 LEU A 26 -33.195 -18.978 5.836 1.00 41.18 C ANISOU 199 CD1 LEU A 26 6115 5104 4427 -1149 -649 -675 C ATOM 200 CD2 LEU A 26 -30.977 -18.017 5.095 1.00 47.43 C ANISOU 200 CD2 LEU A 26 7025 5879 5117 -925 -502 -677 C ATOM 201 N VAL A 27 -30.965 -17.635 10.090 1.00 25.99 N ANISOU 201 N VAL A 27 3926 3213 2737 -884 -354 -413 N ATOM 202 CA VAL A 27 -30.199 -18.410 11.066 1.00 26.83 C ANISOU 202 CA VAL A 27 4071 3223 2901 -859 -284 -378 C ATOM 203 C VAL A 27 -31.130 -18.990 12.137 1.00 29.66 C ANISOU 203 C VAL A 27 4370 3580 3320 -967 -299 -334 C ATOM 204 O VAL A 27 -31.051 -20.176 12.477 1.00 30.63 O ANISOU 204 O VAL A 27 4577 3587 3476 -1022 -286 -334 O ATOM 205 CB VAL A 27 -29.092 -17.542 11.708 1.00 22.81 C ANISOU 205 CB VAL A 27 3513 2747 2407 -732 -215 -325 C ATOM 206 CG1 VAL A 27 -28.546 -18.222 12.951 1.00 21.02 C ANISOU 206 CG1 VAL A 27 3297 2447 2244 -717 -167 -270 C ATOM 207 CG2 VAL A 27 -27.943 -17.229 10.699 1.00 22.10 C ANISOU 207 CG2 VAL A 27 3498 2633 2265 -631 -174 -368 C ATOM 208 N CYS A 28 -31.990 -18.141 12.715 1.00 26.57 N ANISOU 208 N CYS A 28 3837 3314 2946 -996 -320 -295 N ATOM 209 CA CYS A 28 -32.872 -18.571 13.793 1.00 28.31 C ANISOU 209 CA CYS A 28 3985 3553 3218 -1100 -315 -250 C ATOM 210 C CYS A 28 -33.865 -19.609 13.297 1.00 31.78 C ANISOU 210 C CYS A 28 4461 3945 3668 -1248 -373 -293 C ATOM 211 O CYS A 28 -34.123 -20.606 13.982 1.00 35.79 O ANISOU 211 O CYS A 28 5005 4378 4215 -1342 -354 -265 O ATOM 212 CB CYS A 28 -33.597 -17.365 14.396 1.00 26.80 C ANISOU 212 CB CYS A 28 3626 3515 3042 -1088 -317 -215 C ATOM 213 SG CYS A 28 -32.495 -16.166 15.253 1.00 29.78 S ANISOU 213 SG CYS A 28 3959 3941 3415 -935 -248 -160 S ATOM 214 N ATRP A 29 -34.424 -19.403 12.101 0.51 32.52 N ANISOU 214 N ATRP A 29 4554 4076 3724 -1277 -451 -358 N ATOM 215 N BTRP A 29 -34.419 -19.395 12.100 0.49 32.52 N ANISOU 215 N BTRP A 29 4554 4077 3724 -1276 -451 -358 N ATOM 216 CA ATRP A 29 -35.324 -20.396 11.523 0.51 35.19 C ANISOU 216 CA ATRP A 29 4935 4365 4069 -1423 -520 -410 C ATOM 217 CA BTRP A 29 -35.316 -20.368 11.483 0.49 35.17 C ANISOU 217 CA BTRP A 29 4933 4365 4064 -1420 -522 -412 C ATOM 218 C ATRP A 29 -34.626 -21.738 11.326 0.51 36.06 C ANISOU 218 C ATRP A 29 5229 4295 4178 -1448 -496 -441 C ATOM 219 C BTRP A 29 -34.634 -21.723 11.307 0.49 36.05 C ANISOU 219 C BTRP A 29 5226 4295 4175 -1448 -497 -442 C ATOM 220 O ATRP A 29 -35.200 -22.790 11.633 0.51 38.16 O ANISOU 220 O ATRP A 29 5531 4483 4483 -1580 -510 -441 O ATOM 221 O BTRP A 29 -35.224 -22.766 11.613 0.49 38.14 O ANISOU 221 O BTRP A 29 5526 4484 4480 -1580 -512 -442 O ATOM 222 CB ATRP A 29 -35.897 -19.888 10.199 0.51 37.77 C ANISOU 222 CB ATRP A 29 5248 4762 4340 -1434 -620 -477 C ATOM 223 CB BTRP A 29 -35.802 -19.823 10.138 0.49 37.69 C ANISOU 223 CB BTRP A 29 5244 4753 4324 -1421 -618 -478 C ATOM 224 CG ATRP A 29 -37.198 -19.173 10.357 0.51 41.32 C ANISOU 224 CG ATRP A 29 5514 5361 4825 -1495 -685 -463 C ATOM 225 CG BTRP A 29 -37.080 -20.407 9.623 0.49 41.90 C ANISOU 225 CG BTRP A 29 5747 5304 4871 -1578 -719 -526 C ATOM 226 CD1ATRP A 29 -37.421 -17.836 10.227 0.51 42.67 C ANISOU 226 CD1ATRP A 29 5567 5662 4984 -1407 -712 -445 C ATOM 227 CD1BTRP A 29 -37.275 -21.004 8.412 0.49 44.11 C ANISOU 227 CD1BTRP A 29 6140 5525 5095 -1640 -801 -609 C ATOM 228 CD2ATRP A 29 -38.458 -19.758 10.701 0.51 44.29 C ANISOU 228 CD2ATRP A 29 5795 5770 5262 -1654 -729 -466 C ATOM 229 CD2BTRP A 29 -38.345 -20.442 10.294 0.49 44.56 C ANISOU 229 CD2BTRP A 29 5923 5726 5280 -1699 -748 -499 C ATOM 230 NE1ATRP A 29 -38.746 -17.552 10.453 0.51 43.37 N ANISOU 230 NE1ATRP A 29 5489 5863 5127 -1489 -773 -442 N ATOM 231 NE1BTRP A 29 -38.580 -21.403 8.283 0.49 43.71 N ANISOU 231 NE1BTRP A 29 6008 5518 5083 -1795 -892 -633 N ATOM 232 CE2ATRP A 29 -39.403 -18.714 10.754 0.51 44.96 C ANISOU 232 CE2ATRP A 29 5692 6015 5375 -1645 -780 -454 C ATOM 233 CE2BTRP A 29 -39.259 -21.073 9.426 0.49 46.11 C ANISOU 233 CE2BTRP A 29 6136 5914 5471 -1835 -857 -565 C ATOM 234 CE3ATRP A 29 -38.881 -21.066 10.965 0.51 45.80 C ANISOU 234 CE3ATRP A 29 6041 5867 5493 -1806 -729 -477 C ATOM 235 CE3BTRP A 29 -38.796 -19.996 11.542 0.49 44.78 C ANISOU 235 CE3BTRP A 29 5795 5845 5376 -1709 -688 -429 C ATOM 236 CZ2ATRP A 29 -40.747 -18.936 11.051 0.51 46.94 C ANISOU 236 CZ2ATRP A 29 5793 6348 5696 -1781 -826 -458 C ATOM 237 CZ2BTRP A 29 -40.596 -21.272 9.766 0.49 48.90 C ANISOU 237 CZ2BTRP A 29 6338 6346 5894 -1982 -909 -561 C ATOM 238 CZ3ATRP A 29 -40.209 -21.283 11.267 0.51 47.53 C ANISOU 238 CZ3ATRP A 29 6120 6164 5776 -1955 -773 -474 C ATOM 239 CZ3BTRP A 29 -40.121 -20.200 11.880 0.49 46.62 C ANISOU 239 CZ3BTRP A 29 5884 6158 5672 -1850 -725 -427 C ATOM 240 CH2ATRP A 29 -41.130 -20.223 11.303 0.51 48.12 C ANISOU 240 CH2ATRP A 29 5991 6412 5880 -1940 -819 -467 C ATOM 241 CH2BTRP A 29 -41.007 -20.829 10.994 0.49 48.52 C ANISOU 241 CH2BTRP A 29 6128 6390 5917 -1985 -836 -491 C ATOM 242 N ALA A 30 -33.386 -21.725 10.825 1.00 34.15 N ANISOU 242 N ALA A 30 5101 3980 3895 -1323 -455 -467 N ATOM 243 CA ALA A 30 -32.653 -22.978 10.610 1.00 34.76 C ANISOU 243 CA ALA A 30 5352 3877 3978 -1322 -427 -505 C ATOM 244 C ALA A 30 -32.461 -23.762 11.914 1.00 34.78 C ANISOU 244 C ALA A 30 5373 3788 4054 -1353 -377 -430 C ATOM 245 O ALA A 30 -32.679 -24.978 11.951 1.00 35.38 O ANISOU 245 O ALA A 30 5556 3728 4160 -1448 -392 -447 O ATOM 246 CB ALA A 30 -31.296 -22.696 9.953 1.00 31.21 C ANISOU 246 CB ALA A 30 4990 3386 3481 -1165 -374 -542 C ATOM 247 N VAL A 31 -32.041 -23.088 12.994 1.00 32.20 N ANISOU 247 N VAL A 31 4957 3527 3752 -1278 -321 -345 N ATOM 248 CA VAL A 31 -31.863 -23.804 14.259 1.00 33.36 C ANISOU 248 CA VAL A 31 5131 3591 3952 -1309 -280 -264 C ATOM 249 C VAL A 31 -33.207 -24.309 14.779 1.00 35.68 C ANISOU 249 C VAL A 31 5374 3907 4277 -1493 -308 -236 C ATOM 250 O VAL A 31 -33.309 -25.435 15.285 1.00 33.47 O ANISOU 250 O VAL A 31 5187 3497 4033 -1582 -302 -205 O ATOM 251 CB VAL A 31 -31.144 -22.924 15.308 1.00 33.43 C ANISOU 251 CB VAL A 31 5058 3677 3968 -1194 -223 -183 C ATOM 252 CG1 VAL A 31 -31.041 -23.679 16.638 1.00 33.34 C ANISOU 252 CG1 VAL A 31 5086 3587 3997 -1239 -191 -93 C ATOM 253 CG2 VAL A 31 -29.742 -22.515 14.830 1.00 27.84 C ANISOU 253 CG2 VAL A 31 4395 2940 3243 -1023 -191 -209 C ATOM 254 N TRP A 32 -34.262 -23.500 14.642 1.00 36.76 N ANISOU 254 N TRP A 32 5361 4201 4404 -1555 -340 -245 N ATOM 255 CA TRP A 32 -35.576 -23.934 15.108 1.00 41.69 C ANISOU 255 CA TRP A 32 5911 4865 5067 -1735 -360 -223 C ATOM 256 C TRP A 32 -36.043 -25.210 14.405 1.00 43.21 C ANISOU 256 C TRP A 32 6222 4922 5274 -1874 -417 -281 C ATOM 257 O TRP A 32 -36.737 -26.030 15.014 1.00 44.77 O ANISOU 257 O TRP A 32 6427 5071 5514 -2027 -412 -244 O ATOM 258 CB TRP A 32 -36.612 -22.825 14.906 1.00 44.45 C ANISOU 258 CB TRP A 32 6067 5407 5413 -1759 -395 -240 C ATOM 259 CG TRP A 32 -38.013 -23.241 15.324 1.00 53.87 C ANISOU 259 CG TRP A 32 7155 6658 6654 -1947 -412 -226 C ATOM 260 CD1 TRP A 32 -38.894 -24.030 14.617 1.00 53.98 C ANISOU 260 CD1 TRP A 32 7187 6634 6690 -2102 -486 -282 C ATOM 261 CD2 TRP A 32 -38.686 -22.889 16.546 1.00 59.44 C ANISOU 261 CD2 TRP A 32 7718 7475 7393 -2006 -348 -156 C ATOM 262 NE1 TRP A 32 -40.056 -24.189 15.330 1.00 57.88 N ANISOU 262 NE1 TRP A 32 7546 7210 7237 -2256 -470 -247 N ATOM 263 CE2 TRP A 32 -39.957 -23.500 16.514 1.00 61.59 C ANISOU 263 CE2 TRP A 32 7916 7774 7712 -2198 -379 -170 C ATOM 264 CE3 TRP A 32 -38.334 -22.119 17.664 1.00 59.65 C ANISOU 264 CE3 TRP A 32 7673 7581 7409 -1919 -264 -88 C ATOM 265 CZ2 TRP A 32 -40.880 -23.360 17.559 1.00 65.15 C ANISOU 265 CZ2 TRP A 32 8216 8336 8201 -2303 -317 -117 C ATOM 266 CZ3 TRP A 32 -39.254 -21.978 18.698 1.00 60.47 C ANISOU 266 CZ3 TRP A 32 7641 7791 7541 -2018 -206 -40 C ATOM 267 CH2 TRP A 32 -40.509 -22.595 18.638 1.00 63.96 C ANISOU 267 CH2 TRP A 32 8005 8265 8032 -2207 -226 -54 C ATOM 268 N LEU A 33 -35.675 -25.396 13.138 1.00 45.87 N ANISOU 268 N LEU A 33 6660 5195 5572 -1831 -468 -373 N ATOM 269 CA LEU A 33 -36.220 -26.461 12.304 1.00 51.18 C ANISOU 269 CA LEU A 33 7442 5757 6249 -1965 -538 -450 C ATOM 270 C LEU A 33 -35.364 -27.721 12.240 1.00 50.09 C ANISOU 270 C LEU A 33 7516 5391 6123 -1951 -516 -469 C ATOM 271 O LEU A 33 -35.905 -28.798 11.992 1.00 54.39 O ANISOU 271 O LEU A 33 8156 5816 6693 -2096 -559 -506 O ATOM 272 CB LEU A 33 -36.427 -25.951 10.876 1.00 57.32 C ANISOU 272 CB LEU A 33 8218 6600 6961 -1939 -618 -551 C ATOM 273 CG LEU A 33 -37.600 -25.003 10.645 1.00 62.66 C ANISOU 273 CG LEU A 33 8703 7471 7635 -1999 -686 -555 C ATOM 274 CD1 LEU A 33 -37.610 -24.561 9.191 1.00 65.33 C ANISOU 274 CD1 LEU A 33 9081 7850 7892 -1956 -772 -647 C ATOM 275 CD2 LEU A 33 -38.910 -25.687 11.009 1.00 65.61 C ANISOU 275 CD2 LEU A 33 8997 7859 8074 -2197 -727 -544 C ATOM 276 N ASN A 34 -34.056 -27.631 12.433 1.00 44.43 N ANISOU 276 N ASN A 34 6876 4607 5397 -1781 -453 -451 N ATOM 277 CA ASN A 34 -33.157 -28.760 12.223 1.00 44.45 C ANISOU 277 CA ASN A 34 7078 4393 5417 -1734 -435 -484 C ATOM 278 C ASN A 34 -32.596 -29.214 13.574 1.00 43.31 C ANISOU 278 C ASN A 34 6966 4160 5331 -1701 -377 -372 C ATOM 279 O ASN A 34 -31.761 -28.526 14.171 1.00 38.25 O ANISOU 279 O ASN A 34 6269 3578 4688 -1558 -325 -313 O ATOM 280 CB ASN A 34 -32.053 -28.364 11.245 1.00 45.73 C ANISOU 280 CB ASN A 34 7305 4544 5527 -1558 -412 -564 C ATOM 281 CG ASN A 34 -31.133 -29.517 10.881 1.00 48.52 C ANISOU 281 CG ASN A 34 7858 4676 5901 -1494 -391 -622 C ATOM 282 OD1 ASN A 34 -31.159 -30.579 11.507 1.00 49.28 O ANISOU 282 OD1 ASN A 34 8052 4614 6059 -1557 -391 -585 O ATOM 283 ND2 ASN A 34 -30.284 -29.295 9.880 1.00 46.83 N ANISOU 283 ND2 ASN A 34 7708 4449 5635 -1363 -365 -712 N ATOM 284 N ASER A 35 -33.048 -30.384 14.046 0.70 43.71 N ANISOU 284 N ASER A 35 7115 4064 5429 -1839 -393 -340 N ATOM 285 N BSER A 35 -33.050 -30.384 14.043 0.30 43.91 N ANISOU 285 N BSER A 35 7141 4089 5454 -1840 -393 -340 N ATOM 286 CA ASER A 35 -32.574 -30.888 15.333 0.70 44.09 C ANISOU 286 CA ASER A 35 7214 4016 5522 -1822 -349 -223 C ATOM 287 CA BSER A 35 -32.581 -30.903 15.326 0.30 44.23 C ANISOU 287 CA BSER A 35 7234 4032 5540 -1824 -350 -223 C ATOM 288 C ASER A 35 -31.065 -31.103 15.328 0.70 44.74 C ANISOU 288 C ASER A 35 7404 3975 5618 -1617 -317 -225 C ATOM 289 C BSER A 35 -31.073 -31.121 15.330 0.30 44.65 C ANISOU 289 C BSER A 35 7395 3962 5608 -1619 -318 -225 C ATOM 290 O ASER A 35 -30.414 -30.944 16.368 0.70 44.68 O ANISOU 290 O ASER A 35 7381 3966 5629 -1532 -281 -125 O ATOM 291 O BSER A 35 -30.432 -30.987 16.379 0.30 44.89 O ANISOU 291 O BSER A 35 7412 3987 5658 -1537 -282 -124 O ATOM 292 CB ASER A 35 -33.295 -32.190 15.701 0.70 46.04 C ANISOU 292 CB ASER A 35 7570 4106 5815 -2007 -375 -191 C ATOM 293 CB BSER A 35 -33.307 -32.207 15.671 0.30 45.94 C ANISOU 293 CB BSER A 35 7559 4093 5803 -2008 -377 -194 C ATOM 294 OG ASER A 35 -32.881 -33.268 14.873 0.70 46.52 O ANISOU 294 OG ASER A 35 7790 3987 5898 -1961 -402 -274 O ATOM 295 OG BSER A 35 -34.680 -31.983 15.945 0.30 45.74 O ANISOU 295 OG BSER A 35 7382 4219 5777 -2171 -386 -165 O ATOM 296 N ASN A 36 -30.485 -31.451 14.175 1.00 44.30 N ANISOU 296 N ASN A 36 7455 3822 5553 -1535 -329 -342 N ATOM 297 CA ASN A 36 -29.028 -31.532 14.091 1.00 47.33 C ANISOU 297 CA ASN A 36 7910 4116 5957 -1326 -288 -357 C ATOM 298 C ASN A 36 -28.355 -30.179 14.353 1.00 46.59 C ANISOU 298 C ASN A 36 7660 4207 5833 -1178 -243 -320 C ATOM 299 O ASN A 36 -27.141 -30.132 14.590 1.00 47.85 O ANISOU 299 O ASN A 36 7841 4320 6022 -1010 -207 -302 O ATOM 300 CB ASN A 36 -28.594 -32.058 12.727 1.00 50.19 C ANISOU 300 CB ASN A 36 8403 4365 6304 -1267 -293 -504 C ATOM 301 CG ASN A 36 -29.090 -33.452 12.457 1.00 55.90 C ANISOU 301 CG ASN A 36 9303 4875 7062 -1396 -339 -551 C ATOM 302 OD1 ASN A 36 -29.280 -34.246 13.385 1.00 60.11 O ANISOU 302 OD1 ASN A 36 9882 5301 7655 -1457 -350 -458 O ATOM 303 ND2 ASN A 36 -29.315 -33.763 11.182 1.00 54.49 N ANISOU 303 ND2 ASN A 36 9184 4676 6843 -1413 -360 -684 N ATOM 304 N LEU A 37 -29.103 -29.078 14.313 1.00 42.86 N ANISOU 304 N LEU A 37 7033 3940 5313 -1234 -249 -309 N ATOM 305 CA LEU A 37 -28.553 -27.777 14.668 1.00 39.54 C ANISOU 305 CA LEU A 37 6470 3686 4868 -1112 -211 -267 C ATOM 306 C LEU A 37 -28.901 -27.362 16.095 1.00 36.72 C ANISOU 306 C LEU A 37 6012 3416 4524 -1156 -199 -140 C ATOM 307 O LEU A 37 -28.490 -26.289 16.530 1.00 33.39 O ANISOU 307 O LEU A 37 5476 3126 4083 -1065 -171 -101 O ATOM 308 CB LEU A 37 -29.022 -26.707 13.668 1.00 37.99 C ANISOU 308 CB LEU A 37 6173 3655 4605 -1116 -224 -339 C ATOM 309 CG LEU A 37 -28.427 -26.742 12.238 1.00 38.49 C ANISOU 309 CG LEU A 37 6319 3679 4626 -1033 -218 -460 C ATOM 310 CD1 LEU A 37 -29.054 -25.658 11.343 1.00 37.02 C ANISOU 310 CD1 LEU A 37 6039 3662 4364 -1060 -246 -510 C ATOM 311 CD2 LEU A 37 -26.898 -26.640 12.208 1.00 32.62 C ANISOU 311 CD2 LEU A 37 5608 2884 3903 -843 -153 -467 C ATOM 312 N GLN A 38 -29.619 -28.187 16.851 1.00 40.77 N ANISOU 312 N GLN A 38 6574 3855 5064 -1297 -214 -77 N ATOM 313 CA GLN A 38 -30.062 -27.798 18.194 1.00 42.18 C ANISOU 313 CA GLN A 38 6662 4128 5237 -1357 -193 39 C ATOM 314 C GLN A 38 -29.071 -28.335 19.228 1.00 44.83 C ANISOU 314 C GLN A 38 7087 4344 5601 -1271 -179 133 C ATOM 315 O GLN A 38 -29.246 -29.403 19.790 1.00 45.67 O ANISOU 315 O GLN A 38 7311 4308 5736 -1355 -192 192 O ATOM 316 CB GLN A 38 -31.484 -28.277 18.451 1.00 39.47 C ANISOU 316 CB GLN A 38 6300 3799 4897 -1573 -208 60 C ATOM 317 CG GLN A 38 -32.510 -27.452 17.698 1.00 42.33 C ANISOU 317 CG GLN A 38 6521 4331 5232 -1645 -228 -11 C ATOM 318 CD GLN A 38 -33.858 -28.134 17.596 1.00 48.94 C ANISOU 318 CD GLN A 38 7351 5155 6089 -1861 -258 -22 C ATOM 319 OE1 GLN A 38 -34.108 -29.145 18.254 1.00 50.96 O ANISOU 319 OE1 GLN A 38 7699 5288 6374 -1976 -251 38 O ATOM 320 NE2 GLN A 38 -34.735 -27.589 16.757 1.00 49.72 N ANISOU 320 NE2 GLN A 38 7342 5377 6174 -1923 -298 -98 N ATOM 321 N ASN A 39 -28.034 -27.560 19.496 1.00 45.12 N ANISOU 321 N ASN A 39 7068 4444 5632 -1107 -159 152 N ATOM 322 CA ASN A 39 -27.023 -27.900 20.481 1.00 43.08 C ANISOU 322 CA ASN A 39 6871 4099 5399 -1007 -160 242 C ATOM 323 C ASN A 39 -26.636 -26.612 21.187 1.00 40.50 C ANISOU 323 C ASN A 39 6405 3947 5036 -924 -137 290 C ATOM 324 O ASN A 39 -27.014 -25.516 20.758 1.00 36.24 O ANISOU 324 O ASN A 39 5738 3569 4462 -923 -118 241 O ATOM 325 CB ASN A 39 -25.809 -28.555 19.817 1.00 45.34 C ANISOU 325 CB ASN A 39 7263 4224 5740 -856 -171 188 C ATOM 326 CG ASN A 39 -25.319 -27.762 18.621 1.00 43.60 C ANISOU 326 CG ASN A 39 6970 4089 5508 -747 -147 75 C ATOM 327 OD1 ASN A 39 -24.867 -26.632 18.769 1.00 42.69 O ANISOU 327 OD1 ASN A 39 6733 4118 5369 -662 -125 84 O ATOM 328 ND2 ASN A 39 -25.447 -28.332 17.424 1.00 43.67 N ANISOU 328 ND2 ASN A 39 7060 4008 5523 -762 -149 -32 N ATOM 329 N VAL A 40 -25.848 -26.739 22.265 1.00 40.44 N ANISOU 329 N VAL A 40 6431 3900 5036 -851 -147 384 N ATOM 330 CA VAL A 40 -25.561 -25.582 23.120 1.00 34.50 C ANISOU 330 CA VAL A 40 5561 3306 4241 -796 -133 436 C ATOM 331 C VAL A 40 -24.790 -24.512 22.356 1.00 35.49 C ANISOU 331 C VAL A 40 5582 3529 4373 -657 -119 359 C ATOM 332 O VAL A 40 -25.052 -23.311 22.507 1.00 38.47 O ANISOU 332 O VAL A 40 5836 4071 4709 -656 -98 351 O ATOM 333 CB VAL A 40 -24.810 -26.025 24.392 1.00 36.29 C ANISOU 333 CB VAL A 40 5861 3458 4469 -746 -163 553 C ATOM 334 CG1 VAL A 40 -24.128 -24.842 25.032 1.00 35.48 C ANISOU 334 CG1 VAL A 40 5648 3496 4335 -645 -161 580 C ATOM 335 CG2 VAL A 40 -25.772 -26.656 25.374 1.00 35.98 C ANISOU 335 CG2 VAL A 40 5892 3392 4389 -910 -159 648 C ATOM 336 N THR A 41 -23.816 -24.920 21.539 1.00 34.08 N ANISOU 336 N THR A 41 5454 3247 4248 -539 -125 301 N ATOM 337 CA THR A 41 -23.091 -23.953 20.726 1.00 35.42 C ANISOU 337 CA THR A 41 5530 3506 4421 -422 -100 227 C ATOM 338 C THR A 41 -24.056 -23.086 19.928 1.00 33.90 C ANISOU 338 C THR A 41 5254 3448 4177 -499 -78 160 C ATOM 339 O THR A 41 -23.911 -21.859 19.874 1.00 29.94 O ANISOU 339 O THR A 41 4640 3086 3649 -455 -61 149 O ATOM 340 CB THR A 41 -22.135 -24.664 19.760 1.00 38.15 C ANISOU 340 CB THR A 41 5950 3718 4825 -310 -92 154 C ATOM 341 OG1 THR A 41 -21.630 -25.860 20.360 1.00 38.62 O ANISOU 341 OG1 THR A 41 6126 3606 4942 -274 -126 210 O ATOM 342 CG2 THR A 41 -20.984 -23.755 19.416 1.00 35.12 C ANISOU 342 CG2 THR A 41 5470 3414 4459 -165 -64 121 C ATOM 343 N ASN A 42 -25.067 -23.709 19.315 1.00 31.13 N ANISOU 343 N ASN A 42 4958 3053 3817 -616 -86 117 N ATOM 344 CA ASN A 42 -25.953 -22.949 18.455 1.00 27.32 C ANISOU 344 CA ASN A 42 4399 2690 3291 -679 -82 50 C ATOM 345 C ASN A 42 -27.007 -22.160 19.225 1.00 26.76 C ANISOU 345 C ASN A 42 4217 2765 3185 -775 -81 98 C ATOM 346 O ASN A 42 -27.638 -21.274 18.636 1.00 28.43 O ANISOU 346 O ASN A 42 4338 3098 3367 -798 -82 52 O ATOM 347 CB ASN A 42 -26.599 -23.876 17.416 1.00 27.67 C ANISOU 347 CB ASN A 42 4537 2638 3337 -767 -102 -26 C ATOM 348 CG ASN A 42 -25.620 -24.277 16.315 1.00 32.90 C ANISOU 348 CG ASN A 42 5284 3201 4014 -657 -88 -111 C ATOM 349 OD1 ASN A 42 -24.542 -23.682 16.185 1.00 36.30 O ANISOU 349 OD1 ASN A 42 5675 3665 4453 -521 -57 -120 O ATOM 350 ND2 ASN A 42 -25.980 -25.287 15.529 1.00 32.99 N ANISOU 350 ND2 ASN A 42 5412 3091 4030 -719 -106 -179 N ATOM 351 N TYR A 43 -27.205 -22.414 20.518 1.00 26.42 N ANISOU 351 N TYR A 43 4178 2719 3140 -824 -76 189 N ATOM 352 CA TYR A 43 -28.033 -21.478 21.289 1.00 27.52 C ANISOU 352 CA TYR A 43 4198 3015 3241 -885 -57 225 C ATOM 353 C TYR A 43 -27.326 -20.134 21.449 1.00 22.83 C ANISOU 353 C TYR A 43 3509 2536 2630 -764 -44 221 C ATOM 354 O TYR A 43 -27.973 -19.078 21.402 1.00 22.37 O ANISOU 354 O TYR A 43 3340 2614 2546 -780 -33 199 O ATOM 355 CB TYR A 43 -28.425 -22.073 22.651 1.00 25.03 C ANISOU 355 CB TYR A 43 3923 2676 2912 -976 -45 322 C ATOM 356 CG TYR A 43 -29.070 -23.434 22.468 1.00 32.80 C ANISOU 356 CG TYR A 43 5013 3529 3919 -1105 -58 330 C ATOM 357 CD1 TYR A 43 -29.825 -23.716 21.318 1.00 38.04 C ANISOU 357 CD1 TYR A 43 5674 4180 4601 -1181 -77 248 C ATOM 358 CD2 TYR A 43 -28.882 -24.450 23.393 1.00 37.45 C ANISOU 358 CD2 TYR A 43 5718 3998 4513 -1152 -62 419 C ATOM 359 CE1 TYR A 43 -30.386 -24.966 21.105 1.00 41.26 C ANISOU 359 CE1 TYR A 43 6185 4457 5034 -1306 -96 247 C ATOM 360 CE2 TYR A 43 -29.441 -25.700 23.199 1.00 42.53 C ANISOU 360 CE2 TYR A 43 6471 4505 5183 -1275 -77 427 C ATOM 361 CZ TYR A 43 -30.193 -25.956 22.056 1.00 45.53 C ANISOU 361 CZ TYR A 43 6841 4873 5586 -1354 -92 337 C ATOM 362 OH TYR A 43 -30.741 -27.210 21.874 1.00 50.06 O ANISOU 362 OH TYR A 43 7529 5302 6188 -1487 -112 341 O ATOM 363 N PHE A 44 -25.999 -20.143 21.593 1.00 21.81 N ANISOU 363 N PHE A 44 3416 2349 2521 -640 -49 238 N ATOM 364 CA PHE A 44 -25.274 -18.867 21.598 1.00 21.70 C ANISOU 364 CA PHE A 44 3313 2436 2498 -533 -39 226 C ATOM 365 C PHE A 44 -25.236 -18.248 20.206 1.00 21.47 C ANISOU 365 C PHE A 44 3245 2445 2468 -493 -33 140 C ATOM 366 O PHE A 44 -25.298 -17.021 20.064 1.00 22.75 O ANISOU 366 O PHE A 44 3315 2719 2608 -462 -26 122 O ATOM 367 CB PHE A 44 -23.861 -19.052 22.154 1.00 23.26 C ANISOU 367 CB PHE A 44 3544 2569 2725 -419 -51 269 C ATOM 368 CG PHE A 44 -23.829 -19.477 23.612 1.00 27.99 C ANISOU 368 CG PHE A 44 4182 3145 3307 -450 -69 364 C ATOM 369 CD1 PHE A 44 -24.102 -18.562 24.631 1.00 31.99 C ANISOU 369 CD1 PHE A 44 4620 3771 3763 -471 -61 404 C ATOM 370 CD2 PHE A 44 -23.516 -20.773 23.955 1.00 25.48 C ANISOU 370 CD2 PHE A 44 3981 2683 3018 -456 -94 413 C ATOM 371 CE1 PHE A 44 -24.074 -18.961 25.964 1.00 33.05 C ANISOU 371 CE1 PHE A 44 4806 3890 3863 -505 -76 493 C ATOM 372 CE2 PHE A 44 -23.491 -21.176 25.275 1.00 30.67 C ANISOU 372 CE2 PHE A 44 4690 3315 3647 -489 -116 511 C ATOM 373 CZ PHE A 44 -23.773 -20.281 26.280 1.00 34.04 C ANISOU 373 CZ PHE A 44 5053 3871 4011 -517 -105 552 C ATOM 374 N VAL A 45 -25.143 -19.075 19.162 1.00 23.08 N ANISOU 374 N VAL A 45 3529 2553 2689 -496 -38 85 N ATOM 375 CA VAL A 45 -25.297 -18.564 17.793 1.00 25.62 C ANISOU 375 CA VAL A 45 3833 2915 2989 -482 -35 4 C ATOM 376 C VAL A 45 -26.634 -17.836 17.618 1.00 22.99 C ANISOU 376 C VAL A 45 3418 2698 2619 -572 -54 -11 C ATOM 377 O VAL A 45 -26.712 -16.792 16.960 1.00 22.01 O ANISOU 377 O VAL A 45 3233 2661 2468 -538 -57 -44 O ATOM 378 CB VAL A 45 -25.156 -19.722 16.784 1.00 28.41 C ANISOU 378 CB VAL A 45 4303 3138 3353 -492 -38 -58 C ATOM 379 CG1 VAL A 45 -25.637 -19.297 15.401 1.00 26.01 C ANISOU 379 CG1 VAL A 45 3997 2883 3003 -514 -46 -140 C ATOM 380 CG2 VAL A 45 -23.714 -20.212 16.738 1.00 28.45 C ANISOU 380 CG2 VAL A 45 4365 3044 3402 -369 -11 -62 C ATOM 381 N VAL A 46 -27.718 -18.401 18.158 1.00 24.13 N ANISOU 381 N VAL A 46 3561 2842 2766 -688 -69 14 N ATOM 382 CA VAL A 46 -29.026 -17.760 18.044 1.00 20.94 C ANISOU 382 CA VAL A 46 3059 2554 2342 -770 -88 -2 C ATOM 383 C VAL A 46 -29.077 -16.464 18.860 1.00 21.68 C ANISOU 383 C VAL A 46 3039 2774 2425 -725 -68 33 C ATOM 384 O VAL A 46 -29.637 -15.458 18.412 1.00 23.14 O ANISOU 384 O VAL A 46 3137 3058 2596 -715 -84 2 O ATOM 385 CB VAL A 46 -30.129 -18.747 18.465 1.00 24.87 C ANISOU 385 CB VAL A 46 3574 3021 2855 -916 -98 16 C ATOM 386 CG1 VAL A 46 -31.473 -18.027 18.716 1.00 26.69 C ANISOU 386 CG1 VAL A 46 3669 3392 3080 -996 -104 14 C ATOM 387 CG2 VAL A 46 -30.287 -19.816 17.414 1.00 24.72 C ANISOU 387 CG2 VAL A 46 3658 2890 2843 -972 -131 -40 C ATOM 388 N SER A 47 -28.509 -16.459 20.068 1.00 18.67 N ANISOU 388 N SER A 47 2662 2386 2047 -694 -40 95 N ATOM 389 CA SER A 47 -28.457 -15.211 20.838 1.00 21.84 C ANISOU 389 CA SER A 47 2970 2898 2431 -646 -21 116 C ATOM 390 C SER A 47 -27.725 -14.110 20.065 1.00 21.28 C ANISOU 390 C SER A 47 2866 2862 2357 -540 -30 80 C ATOM 391 O SER A 47 -28.130 -12.942 20.079 1.00 19.09 O ANISOU 391 O SER A 47 2502 2681 2068 -518 -32 65 O ATOM 392 CB SER A 47 -27.779 -15.454 22.189 1.00 21.35 C ANISOU 392 CB SER A 47 2941 2811 2362 -625 -1 186 C ATOM 393 OG SER A 47 -27.812 -14.276 22.993 1.00 24.44 O ANISOU 393 OG SER A 47 3250 3307 2727 -590 16 199 O ATOM 394 N LEU A 48 -26.640 -14.465 19.384 1.00 21.32 N ANISOU 394 N LEU A 48 2940 2787 2374 -474 -30 64 N ATOM 395 CA LEU A 48 -25.904 -13.485 18.589 1.00 21.61 C ANISOU 395 CA LEU A 48 2953 2853 2404 -387 -27 33 C ATOM 396 C LEU A 48 -26.723 -13.027 17.376 1.00 20.80 C ANISOU 396 C LEU A 48 2832 2796 2277 -415 -52 -20 C ATOM 397 O LEU A 48 -26.730 -11.836 17.029 1.00 21.54 O ANISOU 397 O LEU A 48 2871 2958 2354 -374 -60 -30 O ATOM 398 CB LEU A 48 -24.574 -14.112 18.174 1.00 22.42 C ANISOU 398 CB LEU A 48 3128 2861 2530 -316 -8 25 C ATOM 399 CG LEU A 48 -23.587 -13.399 17.285 1.00 27.64 C ANISOU 399 CG LEU A 48 3782 3533 3189 -233 14 -6 C ATOM 400 CD1 LEU A 48 -23.063 -12.136 18.004 1.00 22.21 C ANISOU 400 CD1 LEU A 48 3013 2920 2507 -183 19 27 C ATOM 401 CD2 LEU A 48 -22.435 -14.378 16.980 1.00 30.67 C ANISOU 401 CD2 LEU A 48 4235 3813 3607 -174 41 -19 C ATOM 402 N ALA A 49 -27.456 -13.949 16.738 1.00 20.80 N ANISOU 402 N ALA A 49 2879 2754 2270 -490 -75 -51 N ATOM 403 CA ALA A 49 -28.341 -13.563 15.638 1.00 19.73 C ANISOU 403 CA ALA A 49 2725 2667 2106 -526 -118 -98 C ATOM 404 C ALA A 49 -29.468 -12.636 16.109 1.00 21.71 C ANISOU 404 C ALA A 49 2857 3030 2361 -555 -144 -86 C ATOM 405 O ALA A 49 -29.902 -11.746 15.364 1.00 20.10 O ANISOU 405 O ALA A 49 2613 2888 2138 -535 -182 -109 O ATOM 406 CB ALA A 49 -28.932 -14.810 14.986 1.00 20.51 C ANISOU 406 CB ALA A 49 2898 2696 2199 -613 -146 -136 C ATOM 407 N ALA A 50 -29.997 -12.866 17.314 1.00 19.46 N ANISOU 407 N ALA A 50 2521 2772 2101 -604 -123 -50 N ATOM 408 CA ALA A 50 -31.032 -11.978 17.849 1.00 21.14 C ANISOU 408 CA ALA A 50 2613 3097 2324 -621 -131 -47 C ATOM 409 C ALA A 50 -30.493 -10.572 18.057 1.00 20.81 C ANISOU 409 C ALA A 50 2524 3107 2276 -520 -121 -39 C ATOM 410 O ALA A 50 -31.175 -9.580 17.771 1.00 22.14 O ANISOU 410 O ALA A 50 2615 3349 2449 -498 -151 -58 O ATOM 411 CB ALA A 50 -31.574 -12.518 19.176 1.00 20.09 C ANISOU 411 CB ALA A 50 2444 2983 2207 -694 -89 -9 C ATOM 412 N ALA A 51 -29.288 -10.467 18.603 1.00 18.30 N ANISOU 412 N ALA A 51 2250 2748 1954 -460 -85 -11 N ATOM 413 CA ALA A 51 -28.660 -9.160 18.730 1.00 20.03 C ANISOU 413 CA ALA A 51 2437 3003 2170 -373 -79 -7 C ATOM 414 C ALA A 51 -28.528 -8.484 17.372 1.00 21.53 C ANISOU 414 C ALA A 51 2642 3193 2344 -333 -115 -35 C ATOM 415 O ALA A 51 -28.747 -7.275 17.251 1.00 21.55 O ANISOU 415 O ALA A 51 2594 3246 2346 -289 -134 -40 O ATOM 416 CB ALA A 51 -27.286 -9.298 19.400 1.00 15.18 C ANISOU 416 CB ALA A 51 1870 2339 1560 -324 -46 26 C ATOM 417 N ASP A 52 -28.169 -9.246 16.332 1.00 20.37 N ANISOU 417 N ASP A 52 2576 2986 2179 -346 -123 -55 N ATOM 418 CA ASP A 52 -28.006 -8.627 15.017 1.00 21.63 C ANISOU 418 CA ASP A 52 2767 3147 2303 -315 -151 -78 C ATOM 419 C ASP A 52 -29.354 -8.252 14.399 1.00 22.36 C ANISOU 419 C ASP A 52 2813 3298 2384 -350 -220 -99 C ATOM 420 O ASP A 52 -29.446 -7.236 13.688 1.00 20.06 O ANISOU 420 O ASP A 52 2516 3036 2070 -310 -257 -101 O ATOM 421 CB ASP A 52 -27.178 -9.543 14.103 1.00 20.63 C ANISOU 421 CB ASP A 52 2746 2944 2150 -315 -129 -101 C ATOM 422 CG ASP A 52 -25.688 -9.597 14.513 1.00 28.91 C ANISOU 422 CG ASP A 52 3821 3946 3219 -252 -66 -81 C ATOM 423 OD1 ASP A 52 -25.162 -8.577 15.056 1.00 26.95 O ANISOU 423 OD1 ASP A 52 3524 3731 2986 -204 -52 -53 O ATOM 424 OD2 ASP A 52 -25.033 -10.666 14.292 1.00 33.53 O ANISOU 424 OD2 ASP A 52 4474 4456 3809 -250 -36 -96 O ATOM 425 N ILE A 53 -30.408 -9.032 14.668 1.00 18.96 N ANISOU 425 N ILE A 53 2346 2886 1973 -427 -243 -112 N ATOM 426 CA ILE A 53 -31.755 -8.634 14.249 1.00 20.81 C ANISOU 426 CA ILE A 53 2503 3190 2214 -459 -314 -132 C ATOM 427 C ILE A 53 -32.144 -7.299 14.877 1.00 23.11 C ANISOU 427 C ILE A 53 2691 3554 2536 -397 -319 -117 C ATOM 428 O ILE A 53 -32.691 -6.415 14.197 1.00 20.00 O ANISOU 428 O ILE A 53 2261 3199 2137 -362 -383 -126 O ATOM 429 CB ILE A 53 -32.789 -9.725 14.592 1.00 23.23 C ANISOU 429 CB ILE A 53 2769 3507 2548 -565 -327 -147 C ATOM 430 CG1 ILE A 53 -32.599 -10.971 13.720 1.00 24.79 C ANISOU 430 CG1 ILE A 53 3079 3626 2715 -629 -345 -175 C ATOM 431 CG2 ILE A 53 -34.204 -9.179 14.411 1.00 23.70 C ANISOU 431 CG2 ILE A 53 2707 3660 2637 -589 -395 -165 C ATOM 432 CD1 ILE A 53 -33.376 -12.196 14.228 1.00 24.08 C ANISOU 432 CD1 ILE A 53 2973 3518 2659 -745 -342 -181 C ATOM 433 N LEU A 54 -31.874 -7.129 16.185 1.00 20.20 N ANISOU 433 N LEU A 54 2281 3200 2196 -381 -256 -97 N ATOM 434 CA LEU A 54 -32.171 -5.861 16.850 1.00 21.16 C ANISOU 434 CA LEU A 54 2316 3380 2343 -318 -251 -94 C ATOM 435 C LEU A 54 -31.283 -4.716 16.356 1.00 20.88 C ANISOU 435 C LEU A 54 2328 3317 2290 -231 -263 -82 C ATOM 436 O LEU A 54 -31.651 -3.550 16.527 1.00 19.33 O ANISOU 436 O LEU A 54 2075 3157 2115 -173 -285 -86 O ATOM 437 CB LEU A 54 -32.034 -6.003 18.362 1.00 21.04 C ANISOU 437 CB LEU A 54 2266 3384 2344 -328 -179 -79 C ATOM 438 CG LEU A 54 -33.007 -6.991 19.035 1.00 22.77 C ANISOU 438 CG LEU A 54 2430 3641 2580 -422 -153 -82 C ATOM 439 CD1 LEU A 54 -32.693 -7.159 20.542 1.00 21.82 C ANISOU 439 CD1 LEU A 54 2307 3533 2452 -435 -76 -57 C ATOM 440 CD2 LEU A 54 -34.462 -6.544 18.832 1.00 22.87 C ANISOU 440 CD2 LEU A 54 2316 3741 2632 -436 -191 -114 C ATOM 441 N VAL A 55 -30.119 -5.005 15.769 1.00 17.73 N ANISOU 441 N VAL A 55 2028 2852 1855 -221 -245 -69 N ATOM 442 CA VAL A 55 -29.359 -3.908 15.173 1.00 15.64 C ANISOU 442 CA VAL A 55 1805 2567 1573 -156 -255 -55 C ATOM 443 C VAL A 55 -30.137 -3.351 13.988 1.00 16.51 C ANISOU 443 C VAL A 55 1919 2695 1660 -146 -336 -63 C ATOM 444 O VAL A 55 -30.245 -2.135 13.818 1.00 19.44 O ANISOU 444 O VAL A 55 2273 3075 2037 -90 -369 -51 O ATOM 445 CB VAL A 55 -27.923 -4.356 14.792 1.00 19.93 C ANISOU 445 CB VAL A 55 2440 3045 2087 -151 -206 -42 C ATOM 446 CG1 VAL A 55 -27.257 -3.371 13.773 1.00 13.32 C ANISOU 446 CG1 VAL A 55 1659 2187 1216 -109 -217 -28 C ATOM 447 CG2 VAL A 55 -27.034 -4.482 16.064 1.00 17.38 C ANISOU 447 CG2 VAL A 55 2102 2708 1796 -135 -146 -25 C ATOM 448 N GLY A 56 -30.764 -4.228 13.202 1.00 17.15 N ANISOU 448 N GLY A 56 2021 2781 1716 -202 -378 -83 N ATOM 449 CA GLY A 56 -31.565 -3.754 12.079 1.00 21.14 C ANISOU 449 CA GLY A 56 2530 3309 2192 -196 -473 -89 C ATOM 450 C GLY A 56 -32.873 -3.110 12.505 1.00 21.51 C ANISOU 450 C GLY A 56 2451 3424 2298 -174 -533 -97 C ATOM 451 O GLY A 56 -33.317 -2.127 11.906 1.00 23.11 O ANISOU 451 O GLY A 56 2641 3642 2499 -123 -608 -87 O ATOM 452 N VAL A 57 -33.536 -3.682 13.508 1.00 19.82 N ANISOU 452 N VAL A 57 2141 3252 2137 -214 -501 -116 N ATOM 453 CA VAL A 57 -34.862 -3.197 13.868 1.00 21.47 C ANISOU 453 CA VAL A 57 2212 3538 2407 -199 -548 -135 C ATOM 454 C VAL A 57 -34.792 -1.922 14.723 1.00 22.32 C ANISOU 454 C VAL A 57 2261 3662 2559 -107 -519 -130 C ATOM 455 O VAL A 57 -35.654 -1.039 14.593 1.00 24.43 O ANISOU 455 O VAL A 57 2444 3968 2868 -49 -581 -141 O ATOM 456 CB VAL A 57 -35.633 -4.335 14.574 1.00 24.72 C ANISOU 456 CB VAL A 57 2544 3994 2855 -291 -514 -158 C ATOM 457 CG1 VAL A 57 -36.939 -3.819 15.178 1.00 27.59 C ANISOU 457 CG1 VAL A 57 2740 4450 3293 -274 -532 -182 C ATOM 458 CG2 VAL A 57 -35.898 -5.485 13.569 1.00 24.10 C ANISOU 458 CG2 VAL A 57 2523 3895 2740 -382 -569 -172 C ATOM 459 N LEU A 58 -33.774 -1.785 15.582 1.00 18.44 N ANISOU 459 N LEU A 58 1813 3136 2059 -90 -433 -117 N ATOM 460 CA LEU A 58 -33.708 -0.683 16.556 1.00 20.79 C ANISOU 460 CA LEU A 58 2061 3446 2393 -16 -398 -124 C ATOM 461 C LEU A 58 -32.452 0.174 16.429 1.00 19.85 C ANISOU 461 C LEU A 58 2037 3256 2247 37 -384 -97 C ATOM 462 O LEU A 58 -32.557 1.405 16.281 1.00 17.83 O ANISOU 462 O LEU A 58 1775 2985 2013 111 -422 -96 O ATOM 463 CB LEU A 58 -33.805 -1.244 17.990 1.00 22.06 C ANISOU 463 CB LEU A 58 2166 3645 2570 -55 -308 -139 C ATOM 464 CG LEU A 58 -35.142 -1.907 18.384 1.00 24.69 C ANISOU 464 CG LEU A 58 2380 4060 2941 -112 -301 -167 C ATOM 465 CD1 LEU A 58 -35.117 -2.458 19.823 1.00 23.35 C ANISOU 465 CD1 LEU A 58 2181 3923 2767 -160 -200 -171 C ATOM 466 CD2 LEU A 58 -36.313 -0.975 18.222 1.00 26.76 C ANISOU 466 CD2 LEU A 58 2521 4382 3263 -48 -354 -199 C ATOM 467 N ALA A 59 -31.254 -0.424 16.498 1.00 18.62 N ANISOU 467 N ALA A 59 1967 3054 2053 2 -331 -76 N ATOM 468 CA ALA A 59 -30.045 0.399 16.574 1.00 18.42 C ANISOU 468 CA ALA A 59 2009 2974 2017 44 -307 -54 C ATOM 469 C ALA A 59 -29.844 1.233 15.306 1.00 18.39 C ANISOU 469 C ALA A 59 2069 2929 1989 78 -366 -29 C ATOM 470 O ALA A 59 -29.407 2.393 15.384 1.00 18.40 O ANISOU 470 O ALA A 59 2094 2895 2003 127 -373 -16 O ATOM 471 CB ALA A 59 -28.805 -0.461 16.838 1.00 15.59 C ANISOU 471 CB ALA A 59 1711 2579 1632 4 -244 -37 C ATOM 472 N ILE A 60 -30.171 0.684 14.135 1.00 17.85 N ANISOU 472 N ILE A 60 2040 2862 1881 47 -413 -22 N ATOM 473 CA ILE A 60 -29.977 1.447 12.897 1.00 18.13 C ANISOU 473 CA ILE A 60 2154 2860 1874 72 -470 8 C ATOM 474 C ILE A 60 -31.036 2.545 12.765 1.00 18.92 C ANISOU 474 C ILE A 60 2202 2974 2012 137 -558 9 C ATOM 475 O ILE A 60 -30.669 3.686 12.459 1.00 21.64 O ANISOU 475 O ILE A 60 2598 3271 2354 185 -583 40 O ATOM 476 CB ILE A 60 -29.914 0.518 11.665 1.00 20.84 C ANISOU 476 CB ILE A 60 2574 3198 2145 17 -492 12 C ATOM 477 CG1 ILE A 60 -28.549 -0.198 11.647 1.00 18.87 C ANISOU 477 CG1 ILE A 60 2397 2910 1862 -18 -399 16 C ATOM 478 CG2 ILE A 60 -30.116 1.311 10.323 1.00 20.28 C ANISOU 478 CG2 ILE A 60 2582 3106 2017 40 -576 45 C ATOM 479 CD1 ILE A 60 -28.397 -1.307 10.506 1.00 14.84 C ANISOU 479 CD1 ILE A 60 1972 2389 1278 -73 -399 2 C ATOM 480 N PRO A 61 -32.330 2.298 12.993 1.00 20.49 N ANISOU 480 N PRO A 61 2298 3234 2254 144 -606 -21 N ATOM 481 CA PRO A 61 -33.259 3.444 13.062 1.00 19.98 C ANISOU 481 CA PRO A 61 2165 3180 2246 227 -680 -26 C ATOM 482 C PRO A 61 -32.851 4.488 14.097 1.00 18.43 C ANISOU 482 C PRO A 61 1953 2952 2099 291 -631 -36 C ATOM 483 O PRO A 61 -33.035 5.686 13.847 1.00 20.52 O ANISOU 483 O PRO A 61 2234 3174 2390 366 -689 -21 O ATOM 484 CB PRO A 61 -34.605 2.782 13.406 1.00 19.75 C ANISOU 484 CB PRO A 61 1999 3238 2268 210 -708 -69 C ATOM 485 CG PRO A 61 -34.513 1.455 12.716 1.00 19.02 C ANISOU 485 CG PRO A 61 1952 3158 2116 115 -711 -67 C ATOM 486 CD PRO A 61 -33.075 1.016 12.990 1.00 19.13 C ANISOU 486 CD PRO A 61 2068 3119 2082 76 -611 -51 C ATOM 487 N PHE A 62 -32.270 4.072 15.227 1.00 16.12 N ANISOU 487 N PHE A 62 1640 2670 1814 261 -533 -58 N ATOM 488 CA PHE A 62 -31.784 5.026 16.224 1.00 16.55 C ANISOU 488 CA PHE A 62 1695 2692 1903 310 -489 -73 C ATOM 489 C PHE A 62 -30.636 5.869 15.665 1.00 20.30 C ANISOU 489 C PHE A 62 2287 3078 2350 321 -498 -28 C ATOM 490 O PHE A 62 -30.638 7.101 15.802 1.00 20.89 O ANISOU 490 O PHE A 62 2379 3100 2457 385 -527 -28 O ATOM 491 CB PHE A 62 -31.343 4.294 17.519 1.00 17.31 C ANISOU 491 CB PHE A 62 1760 2822 1996 264 -392 -100 C ATOM 492 CG PHE A 62 -32.508 3.705 18.350 1.00 18.21 C ANISOU 492 CG PHE A 62 1753 3023 2142 254 -364 -145 C ATOM 493 CD1 PHE A 62 -33.840 3.921 17.988 1.00 22.86 C ANISOU 493 CD1 PHE A 62 2249 3661 2778 292 -422 -169 C ATOM 494 CD2 PHE A 62 -32.244 2.942 19.497 1.00 18.56 C ANISOU 494 CD2 PHE A 62 1778 3104 2172 203 -281 -161 C ATOM 495 CE1 PHE A 62 -34.901 3.378 18.756 1.00 22.46 C ANISOU 495 CE1 PHE A 62 2072 3699 2761 273 -384 -212 C ATOM 496 CE2 PHE A 62 -33.276 2.384 20.270 1.00 18.20 C ANISOU 496 CE2 PHE A 62 1629 3140 2147 179 -241 -197 C ATOM 497 CZ PHE A 62 -34.607 2.600 19.901 1.00 22.64 C ANISOU 497 CZ PHE A 62 2086 3757 2760 210 -286 -225 C ATOM 498 N ALA A 63 -29.641 5.222 15.023 1.00 18.53 N ANISOU 498 N ALA A 63 2144 2831 2067 257 -468 8 N ATOM 499 CA ALA A 63 -28.523 5.969 14.436 1.00 19.17 C ANISOU 499 CA ALA A 63 2327 2836 2119 253 -463 52 C ATOM 500 C ALA A 63 -28.994 6.917 13.321 1.00 17.09 C ANISOU 500 C ALA A 63 2122 2528 1842 295 -554 91 C ATOM 501 O ALA A 63 -28.463 8.020 13.167 1.00 20.28 O ANISOU 501 O ALA A 63 2592 2861 2253 318 -566 122 O ATOM 502 CB ALA A 63 -27.450 5.000 13.906 1.00 16.86 C ANISOU 502 CB ALA A 63 2095 2541 1769 181 -404 75 C ATOM 503 N ILE A 64 -29.980 6.501 12.527 1.00 18.73 N ANISOU 503 N ILE A 64 2314 2775 2030 301 -625 94 N ATOM 504 CA ILE A 64 -30.519 7.393 11.503 1.00 20.52 C ANISOU 504 CA ILE A 64 2595 2961 2242 348 -730 136 C ATOM 505 C ILE A 64 -31.163 8.612 12.163 1.00 23.11 C ANISOU 505 C ILE A 64 2871 3256 2655 444 -777 119 C ATOM 506 O ILE A 64 -30.961 9.754 11.732 1.00 19.24 O ANISOU 506 O ILE A 64 2460 2683 2167 486 -827 162 O ATOM 507 CB ILE A 64 -31.517 6.621 10.617 1.00 20.21 C ANISOU 507 CB ILE A 64 2533 2980 2166 333 -810 134 C ATOM 508 CG1 ILE A 64 -30.783 5.654 9.675 1.00 21.07 C ANISOU 508 CG1 ILE A 64 2738 3093 2172 246 -775 156 C ATOM 509 CG2 ILE A 64 -32.495 7.578 9.869 1.00 20.87 C ANISOU 509 CG2 ILE A 64 2626 3041 2264 409 -948 165 C ATOM 510 CD1 ILE A 64 -31.739 4.597 9.075 1.00 17.91 C ANISOU 510 CD1 ILE A 64 2303 2760 1742 211 -838 131 C ATOM 511 N THR A 65 -31.917 8.380 13.247 1.00 20.28 N ANISOU 511 N THR A 65 2384 2956 2365 477 -753 55 N ATOM 512 CA THR A 65 -32.575 9.466 13.964 1.00 23.82 C ANISOU 512 CA THR A 65 2772 3380 2899 577 -782 20 C ATOM 513 C THR A 65 -31.551 10.446 14.521 1.00 21.74 C ANISOU 513 C THR A 65 2586 3025 2647 588 -737 26 C ATOM 514 O THR A 65 -31.686 11.662 14.368 1.00 21.21 O ANISOU 514 O THR A 65 2565 2876 2619 661 -795 40 O ATOM 515 CB THR A 65 -33.425 8.866 15.091 1.00 28.00 C ANISOU 515 CB THR A 65 3152 4004 3484 589 -732 -56 C ATOM 516 OG1 THR A 65 -34.397 7.994 14.513 1.00 30.63 O ANISOU 516 OG1 THR A 65 3409 4417 3813 567 -783 -60 O ATOM 517 CG2 THR A 65 -34.137 9.950 15.887 1.00 30.41 C ANISOU 517 CG2 THR A 65 3386 4291 3876 699 -746 -108 C ATOM 518 N ILE A 66 -30.490 9.918 15.141 1.00 19.55 N ANISOU 518 N ILE A 66 2331 2757 2341 515 -640 18 N ATOM 519 CA ILE A 66 -29.446 10.754 15.718 1.00 20.01 C ANISOU 519 CA ILE A 66 2454 2738 2410 508 -599 19 C ATOM 520 C ILE A 66 -28.724 11.574 14.644 1.00 22.40 C ANISOU 520 C ILE A 66 2886 2942 2683 492 -641 94 C ATOM 521 O ILE A 66 -28.295 12.705 14.907 1.00 22.09 O ANISOU 521 O ILE A 66 2904 2811 2676 516 -651 100 O ATOM 522 CB ILE A 66 -28.461 9.865 16.507 1.00 20.01 C ANISOU 522 CB ILE A 66 2440 2781 2383 429 -501 1 C ATOM 523 CG1 ILE A 66 -29.151 9.269 17.755 1.00 18.29 C ANISOU 523 CG1 ILE A 66 2113 2645 2191 444 -456 -69 C ATOM 524 CG2 ILE A 66 -27.183 10.640 16.860 1.00 17.18 C ANISOU 524 CG2 ILE A 66 2156 2344 2029 399 -469 15 C ATOM 525 CD1 ILE A 66 -28.395 8.046 18.334 1.00 18.86 C ANISOU 525 CD1 ILE A 66 2171 2772 2225 363 -379 -72 C ATOM 526 N SER A 67 -28.574 11.034 13.422 1.00 21.48 N ANISOU 526 N SER A 67 2826 2838 2498 445 -663 152 N ATOM 527 CA SER A 67 -27.898 11.804 12.373 1.00 21.11 C ANISOU 527 CA SER A 67 2910 2702 2406 420 -692 229 C ATOM 528 C SER A 67 -28.637 13.101 12.049 1.00 24.23 C ANISOU 528 C SER A 67 3350 3012 2844 509 -797 255 C ATOM 529 O SER A 67 -28.030 14.024 11.490 1.00 24.88 O ANISOU 529 O SER A 67 3550 2995 2908 493 -818 317 O ATOM 530 CB SER A 67 -27.709 10.970 11.089 1.00 20.82 C ANISOU 530 CB SER A 67 2935 2703 2274 358 -696 279 C ATOM 531 OG SER A 67 -28.934 10.776 10.358 1.00 20.82 O ANISOU 531 OG SER A 67 2918 2736 2255 404 -797 287 O ATOM 532 N THR A 68 -29.923 13.203 12.392 1.00 23.53 N ANISOU 532 N THR A 68 3169 2955 2815 602 -862 209 N ATOM 533 CA THR A 68 -30.628 14.463 12.162 1.00 24.44 C ANISOU 533 CA THR A 68 3318 2981 2986 706 -966 228 C ATOM 534 C THR A 68 -30.306 15.516 13.219 1.00 25.00 C ANISOU 534 C THR A 68 3399 2966 3135 751 -936 184 C ATOM 535 O THR A 68 -30.554 16.692 12.977 1.00 27.59 O ANISOU 535 O THR A 68 3795 3181 3505 823 -1012 210 O ATOM 536 CB THR A 68 -32.149 14.260 12.125 1.00 27.39 C ANISOU 536 CB THR A 68 3575 3421 3412 801 -1051 190 C ATOM 537 OG1 THR A 68 -32.636 13.913 13.442 1.00 26.40 O ANISOU 537 OG1 THR A 68 3305 3369 3356 836 -983 91 O ATOM 538 CG2 THR A 68 -32.537 13.166 11.110 1.00 24.71 C ANISOU 538 CG2 THR A 68 3223 3170 2996 748 -1091 223 C ATOM 539 N GLY A 69 -29.754 15.142 14.372 1.00 23.94 N ANISOU 539 N GLY A 69 3209 2873 3017 711 -835 119 N ATOM 540 CA GLY A 69 -29.527 16.148 15.415 1.00 22.13 C ANISOU 540 CA GLY A 69 2991 2563 2854 755 -814 64 C ATOM 541 C GLY A 69 -30.796 16.768 15.963 1.00 25.60 C ANISOU 541 C GLY A 69 3353 2992 3380 893 -865 -5 C ATOM 542 O GLY A 69 -30.761 17.896 16.476 1.00 26.83 O ANISOU 542 O GLY A 69 3555 3043 3596 955 -883 -38 O ATOM 543 N PHE A 70 -31.924 16.053 15.871 1.00 23.34 N ANISOU 543 N PHE A 70 2947 2814 3109 941 -888 -32 N ATOM 544 CA PHE A 70 -33.226 16.565 16.282 1.00 25.59 C ANISOU 544 CA PHE A 70 3132 3108 3485 1078 -935 -98 C ATOM 545 C PHE A 70 -33.251 16.906 17.781 1.00 24.80 C ANISOU 545 C PHE A 70 2975 3012 3433 1117 -849 -207 C ATOM 546 O PHE A 70 -32.493 16.358 18.590 1.00 25.42 O ANISOU 546 O PHE A 70 3054 3138 3467 1031 -751 -238 O ATOM 547 CB PHE A 70 -34.317 15.526 15.941 1.00 25.90 C ANISOU 547 CB PHE A 70 3032 3285 3525 1089 -960 -108 C ATOM 548 CG PHE A 70 -34.365 14.367 16.904 1.00 25.10 C ANISOU 548 CG PHE A 70 2819 3317 3402 1023 -846 -173 C ATOM 549 CD1 PHE A 70 -33.307 13.487 17.005 1.00 24.30 C ANISOU 549 CD1 PHE A 70 2767 3248 3219 895 -768 -147 C ATOM 550 CD2 PHE A 70 -35.474 14.167 17.716 1.00 29.19 C ANISOU 550 CD2 PHE A 70 3181 3926 3985 1090 -814 -259 C ATOM 551 CE1 PHE A 70 -33.340 12.434 17.908 1.00 26.77 C ANISOU 551 CE1 PHE A 70 2992 3670 3511 835 -672 -197 C ATOM 552 CE2 PHE A 70 -35.523 13.108 18.618 1.00 26.96 C ANISOU 552 CE2 PHE A 70 2808 3761 3674 1019 -706 -310 C ATOM 553 CZ PHE A 70 -34.468 12.244 18.716 1.00 25.45 C ANISOU 553 CZ PHE A 70 2682 3590 3398 893 -641 -275 C ATOM 554 N CYS A 71 -34.123 17.843 18.137 1.00 24.98 N ANISOU 554 N CYS A 71 2958 2984 3547 1255 -890 -267 N ATOM 555 CA CYS A 71 -34.300 18.260 19.523 1.00 26.15 C ANISOU 555 CA CYS A 71 3059 3137 3741 1310 -810 -384 C ATOM 556 C CYS A 71 -34.939 17.128 20.326 1.00 27.83 C ANISOU 556 C CYS A 71 3112 3523 3938 1286 -716 -453 C ATOM 557 O CYS A 71 -35.955 16.563 19.915 1.00 26.71 O ANISOU 557 O CYS A 71 2849 3476 3826 1321 -746 -450 O ATOM 558 CB CYS A 71 -35.177 19.512 19.583 1.00 30.88 C ANISOU 558 CB CYS A 71 3648 3636 4448 1479 -879 -434 C ATOM 559 SG CYS A 71 -34.428 21.021 18.833 1.00 35.51 S ANISOU 559 SG CYS A 71 4446 3984 5062 1511 -986 -359 S ATOM 560 N ALA A 72 -34.367 16.817 21.486 1.00 23.20 N ANISOU 560 N ALA A 72 2528 2978 3308 1223 -608 -513 N ATOM 561 CA ALA A 72 -34.816 15.678 22.270 1.00 24.60 C ANISOU 561 CA ALA A 72 2581 3314 3452 1175 -511 -563 C ATOM 562 C ALA A 72 -34.498 15.922 23.730 1.00 25.18 C ANISOU 562 C ALA A 72 2667 3398 3501 1171 -410 -659 C ATOM 563 O ALA A 72 -33.434 16.456 24.036 1.00 29.10 O ANISOU 563 O ALA A 72 3288 3803 3966 1130 -408 -656 O ATOM 564 CB ALA A 72 -34.101 14.382 21.828 1.00 22.39 C ANISOU 564 CB ALA A 72 2320 3103 3085 1031 -491 -482 C ATOM 565 N ALA A 73 -35.385 15.485 24.627 1.00 25.08 N ANISOU 565 N ALA A 73 2530 3504 3495 1200 -325 -742 N ATOM 566 CA ALA A 73 -35.028 15.400 26.044 1.00 25.43 C ANISOU 566 CA ALA A 73 2594 3591 3480 1163 -216 -823 C ATOM 567 C ALA A 73 -33.717 14.641 26.200 1.00 24.63 C ANISOU 567 C ALA A 73 2584 3494 3278 1017 -197 -758 C ATOM 568 O ALA A 73 -33.516 13.583 25.585 1.00 22.17 O ANISOU 568 O ALA A 73 2251 3240 2933 932 -207 -677 O ATOM 569 CB ALA A 73 -36.143 14.714 26.839 1.00 25.95 C ANISOU 569 CB ALA A 73 2506 3810 3544 1178 -115 -895 C ATOM 570 N CYS A 74 -32.808 15.196 27.004 1.00 23.66 N ANISOU 570 N CYS A 74 2567 3308 3114 991 -175 -797 N ATOM 571 CA CYS A 74 -31.426 14.724 26.963 1.00 23.70 C ANISOU 571 CA CYS A 74 2666 3289 3050 868 -187 -727 C ATOM 572 C CYS A 74 -31.316 13.241 27.307 1.00 22.93 C ANISOU 572 C CYS A 74 2515 3321 2877 769 -126 -691 C ATOM 573 O CYS A 74 -30.541 12.504 26.673 1.00 21.07 O ANISOU 573 O CYS A 74 2308 3086 2613 685 -152 -603 O ATOM 574 CB CYS A 74 -30.542 15.558 27.893 1.00 29.24 C ANISOU 574 CB CYS A 74 3475 3913 3721 854 -179 -786 C ATOM 575 SG CYS A 74 -28.787 15.112 27.673 1.00 34.13 S ANISOU 575 SG CYS A 74 4191 4494 4282 711 -213 -694 S ATOM 576 N HIS A 75 -32.099 12.772 28.283 1.00 20.20 N ANISOU 576 N HIS A 75 2092 3083 2499 777 -39 -757 N ATOM 577 CA HIS A 75 -32.013 11.355 28.645 1.00 23.36 C ANISOU 577 CA HIS A 75 2454 3594 2826 676 17 -715 C ATOM 578 C HIS A 75 -32.679 10.452 27.608 1.00 24.12 C ANISOU 578 C HIS A 75 2462 3745 2958 657 -4 -650 C ATOM 579 O HIS A 75 -32.340 9.264 27.512 1.00 23.77 O ANISOU 579 O HIS A 75 2416 3751 2865 564 12 -588 O ATOM 580 CB HIS A 75 -32.619 11.124 30.029 1.00 23.41 C ANISOU 580 CB HIS A 75 2421 3700 2776 675 123 -799 C ATOM 581 CG HIS A 75 -31.784 11.694 31.126 1.00 28.73 C ANISOU 581 CG HIS A 75 3200 4335 3380 659 141 -853 C ATOM 582 ND1 HIS A 75 -31.901 13.002 31.537 1.00 31.56 N ANISOU 582 ND1 HIS A 75 3602 4623 3769 746 137 -947 N ATOM 583 CD2 HIS A 75 -30.775 11.158 31.855 1.00 28.98 C ANISOU 583 CD2 HIS A 75 3310 4382 3317 566 150 -827 C ATOM 584 CE1 HIS A 75 -31.023 13.241 32.497 1.00 32.33 C ANISOU 584 CE1 HIS A 75 3801 4698 3786 699 146 -982 C ATOM 585 NE2 HIS A 75 -30.319 12.141 32.697 1.00 30.27 N ANISOU 585 NE2 HIS A 75 3560 4492 3450 591 148 -906 N ATOM 586 N GLY A 76 -33.642 10.977 26.849 1.00 23.97 N ANISOU 586 N GLY A 76 2372 3713 3023 746 -46 -664 N ATOM 587 CA GLY A 76 -34.177 10.209 25.736 1.00 23.96 C ANISOU 587 CA GLY A 76 2301 3750 3052 723 -91 -599 C ATOM 588 C GLY A 76 -33.144 10.035 24.643 1.00 22.42 C ANISOU 588 C GLY A 76 2203 3476 2840 671 -167 -506 C ATOM 589 O GLY A 76 -32.942 8.930 24.136 1.00 23.09 O ANISOU 589 O GLY A 76 2281 3599 2891 590 -170 -446 O ATOM 590 N CYS A 77 -32.473 11.129 24.268 1.00 23.16 N ANISOU 590 N CYS A 77 2390 3453 2956 713 -225 -496 N ATOM 591 CA CYS A 77 -31.326 11.047 23.367 1.00 20.70 C ANISOU 591 CA CYS A 77 2178 3068 2619 653 -276 -412 C ATOM 592 C CYS A 77 -30.293 10.050 23.892 1.00 22.89 C ANISOU 592 C CYS A 77 2491 3382 2825 546 -223 -383 C ATOM 593 O CYS A 77 -29.777 9.201 23.150 1.00 19.16 O ANISOU 593 O CYS A 77 2038 2917 2325 481 -236 -316 O ATOM 594 CB CYS A 77 -30.700 12.438 23.209 1.00 21.98 C ANISOU 594 CB CYS A 77 2439 3101 2813 700 -325 -415 C ATOM 595 SG CYS A 77 -29.252 12.489 22.095 1.00 25.41 S ANISOU 595 SG CYS A 77 2992 3445 3219 619 -373 -313 S ATOM 596 N LEU A 78 -29.978 10.149 25.185 1.00 18.39 N ANISOU 596 N LEU A 78 1934 2832 2221 533 -168 -436 N ATOM 597 CA LEU A 78 -29.013 9.237 25.772 1.00 19.70 C ANISOU 597 CA LEU A 78 2133 3030 2321 442 -132 -407 C ATOM 598 C LEU A 78 -29.437 7.784 25.566 1.00 19.60 C ANISOU 598 C LEU A 78 2062 3104 2282 386 -101 -368 C ATOM 599 O LEU A 78 -28.607 6.937 25.210 1.00 21.69 O ANISOU 599 O LEU A 78 2361 3363 2518 319 -107 -308 O ATOM 600 CB LEU A 78 -28.847 9.568 27.267 1.00 17.35 C ANISOU 600 CB LEU A 78 1856 2755 1981 442 -83 -477 C ATOM 601 CG LEU A 78 -27.721 8.886 28.038 1.00 20.74 C ANISOU 601 CG LEU A 78 2336 3202 2341 359 -67 -451 C ATOM 602 CD1 LEU A 78 -26.344 9.159 27.369 1.00 15.36 C ANISOU 602 CD1 LEU A 78 1721 2437 1678 322 -125 -394 C ATOM 603 CD2 LEU A 78 -27.777 9.389 29.505 1.00 18.83 C ANISOU 603 CD2 LEU A 78 2121 2984 2047 370 -27 -533 C ATOM 604 N PHE A 79 -30.725 7.475 25.761 1.00 19.08 N ANISOU 604 N PHE A 79 1905 3113 2230 410 -68 -403 N ATOM 605 CA PHE A 79 -31.161 6.085 25.599 1.00 19.83 C ANISOU 605 CA PHE A 79 1948 3283 2302 343 -40 -368 C ATOM 606 C PHE A 79 -30.946 5.583 24.166 1.00 17.86 C ANISOU 606 C PHE A 79 1716 3000 2071 318 -100 -302 C ATOM 607 O PHE A 79 -30.366 4.514 23.956 1.00 15.95 O ANISOU 607 O PHE A 79 1504 2762 1794 247 -91 -253 O ATOM 608 CB PHE A 79 -32.620 5.908 26.023 1.00 18.97 C ANISOU 608 CB PHE A 79 1725 3267 2217 365 8 -420 C ATOM 609 CG PHE A 79 -33.106 4.474 25.864 1.00 25.31 C ANISOU 609 CG PHE A 79 2477 4140 3000 280 36 -382 C ATOM 610 CD1 PHE A 79 -32.756 3.493 26.799 1.00 28.95 C ANISOU 610 CD1 PHE A 79 2965 4641 3392 197 101 -364 C ATOM 611 CD2 PHE A 79 -33.852 4.094 24.754 1.00 24.19 C ANISOU 611 CD2 PHE A 79 2272 4014 2905 277 -12 -361 C ATOM 612 CE1 PHE A 79 -33.164 2.170 26.637 1.00 29.70 C ANISOU 612 CE1 PHE A 79 3029 4783 3473 112 123 -325 C ATOM 613 CE2 PHE A 79 -34.255 2.773 24.583 1.00 25.69 C ANISOU 613 CE2 PHE A 79 2425 4256 3079 188 7 -330 C ATOM 614 CZ PHE A 79 -33.916 1.816 25.519 1.00 29.41 C ANISOU 614 CZ PHE A 79 2927 4757 3489 106 77 -312 C ATOM 615 N ILE A 80 -31.393 6.342 23.160 1.00 18.47 N ANISOU 615 N ILE A 80 1782 3039 2199 379 -164 -299 N ATOM 616 CA ILE A 80 -31.261 5.844 21.792 1.00 18.59 C ANISOU 616 CA ILE A 80 1821 3029 2212 351 -220 -240 C ATOM 617 C ILE A 80 -29.806 5.803 21.367 1.00 17.73 C ANISOU 617 C ILE A 80 1817 2850 2070 311 -228 -189 C ATOM 618 O ILE A 80 -29.439 5.017 20.484 1.00 17.47 O ANISOU 618 O ILE A 80 1815 2809 2013 264 -242 -144 O ATOM 619 CB ILE A 80 -32.101 6.661 20.787 1.00 21.09 C ANISOU 619 CB ILE A 80 2110 3322 2580 425 -299 -241 C ATOM 620 CG1 ILE A 80 -31.712 8.136 20.763 1.00 16.15 C ANISOU 620 CG1 ILE A 80 1544 2607 1984 500 -335 -250 C ATOM 621 CG2 ILE A 80 -33.560 6.531 21.120 1.00 26.16 C ANISOU 621 CG2 ILE A 80 2625 4049 3268 460 -292 -290 C ATOM 622 CD1 ILE A 80 -32.340 8.893 19.578 1.00 21.84 C ANISOU 622 CD1 ILE A 80 2269 3282 2745 569 -432 -226 C ATOM 623 N ALA A 81 -28.961 6.638 21.973 1.00 15.47 N ANISOU 623 N ALA A 81 1582 2512 1783 327 -218 -201 N ATOM 624 CA ALA A 81 -27.536 6.595 21.675 1.00 17.21 C ANISOU 624 CA ALA A 81 1881 2677 1981 283 -218 -157 C ATOM 625 C ALA A 81 -26.874 5.359 22.301 1.00 20.46 C ANISOU 625 C ALA A 81 2291 3129 2354 217 -171 -141 C ATOM 626 O ALA A 81 -25.988 4.749 21.696 1.00 19.39 O ANISOU 626 O ALA A 81 2192 2971 2204 176 -168 -97 O ATOM 627 CB ALA A 81 -26.873 7.890 22.177 1.00 18.75 C ANISOU 627 CB ALA A 81 2124 2805 2196 311 -230 -178 C ATOM 628 N CYS A 82 -27.271 4.985 23.520 1.00 17.70 N ANISOU 628 N CYS A 82 1905 2835 1985 208 -130 -176 N ATOM 629 CA CYS A 82 -26.604 3.881 24.215 1.00 18.77 C ANISOU 629 CA CYS A 82 2054 2997 2080 150 -96 -153 C ATOM 630 C CYS A 82 -27.108 2.506 23.793 1.00 19.40 C ANISOU 630 C CYS A 82 2110 3114 2148 106 -80 -125 C ATOM 631 O CYS A 82 -26.463 1.500 24.106 1.00 20.04 O ANISOU 631 O CYS A 82 2216 3195 2203 61 -62 -94 O ATOM 632 CB CYS A 82 -26.804 4.011 25.734 1.00 18.34 C ANISOU 632 CB CYS A 82 1990 2986 1993 148 -60 -195 C ATOM 633 SG CYS A 82 -25.845 5.372 26.458 1.00 21.33 S ANISOU 633 SG CYS A 82 2421 3312 2371 175 -83 -230 S ATOM 634 N PHE A 83 -28.263 2.424 23.140 1.00 17.47 N ANISOU 634 N PHE A 83 1817 2897 1923 117 -92 -138 N ATOM 635 CA PHE A 83 -28.851 1.106 22.971 1.00 19.85 C ANISOU 635 CA PHE A 83 2093 3238 2212 62 -74 -121 C ATOM 636 C PHE A 83 -27.944 0.195 22.137 1.00 18.05 C ANISOU 636 C PHE A 83 1924 2962 1970 25 -85 -76 C ATOM 637 O PHE A 83 -27.815 -0.997 22.440 1.00 19.79 O ANISOU 637 O PHE A 83 2158 3189 2171 -27 -60 -55 O ATOM 638 CB PHE A 83 -30.267 1.204 22.380 1.00 19.13 C ANISOU 638 CB PHE A 83 1926 3191 2152 76 -96 -146 C ATOM 639 CG PHE A 83 -30.963 -0.124 22.339 1.00 19.11 C ANISOU 639 CG PHE A 83 1889 3231 2140 4 -77 -136 C ATOM 640 CD1 PHE A 83 -31.448 -0.707 23.510 1.00 21.54 C ANISOU 640 CD1 PHE A 83 2158 3597 2430 -40 -15 -148 C ATOM 641 CD2 PHE A 83 -31.066 -0.825 21.147 1.00 19.36 C ANISOU 641 CD2 PHE A 83 1940 3241 2174 -28 -117 -115 C ATOM 642 CE1 PHE A 83 -32.053 -1.960 23.498 1.00 25.35 C ANISOU 642 CE1 PHE A 83 2617 4109 2906 -121 5 -132 C ATOM 643 CE2 PHE A 83 -31.687 -2.086 21.114 1.00 20.39 C ANISOU 643 CE2 PHE A 83 2048 3401 2300 -105 -103 -109 C ATOM 644 CZ PHE A 83 -32.179 -2.654 22.282 1.00 22.66 C ANISOU 644 CZ PHE A 83 2293 3739 2578 -155 -43 -114 C ATOM 645 N VAL A 84 -27.250 0.745 21.133 1.00 14.96 N ANISOU 645 N VAL A 84 1577 2519 1589 50 -117 -59 N ATOM 646 CA VAL A 84 -26.386 -0.108 20.310 1.00 13.06 C ANISOU 646 CA VAL A 84 1390 2239 1334 20 -113 -26 C ATOM 647 C VAL A 84 -25.287 -0.757 21.164 1.00 13.35 C ANISOU 647 C VAL A 84 1450 2259 1362 1 -81 -7 C ATOM 648 O VAL A 84 -24.814 -1.864 20.857 1.00 11.77 O ANISOU 648 O VAL A 84 1280 2037 1157 -26 -67 13 O ATOM 649 CB VAL A 84 -25.773 0.688 19.138 1.00 13.67 C ANISOU 649 CB VAL A 84 1512 2270 1414 46 -138 -11 C ATOM 650 CG1 VAL A 84 -24.716 1.728 19.640 1.00 14.34 C ANISOU 650 CG1 VAL A 84 1613 2322 1514 69 -132 -5 C ATOM 651 CG2 VAL A 84 -25.103 -0.286 18.117 1.00 13.33 C ANISOU 651 CG2 VAL A 84 1521 2197 1348 16 -123 10 C ATOM 652 N LEU A 85 -24.867 -0.086 22.244 1.00 11.67 N ANISOU 652 N LEU A 85 1229 2055 1152 17 -75 -15 N ATOM 653 CA LEU A 85 -23.851 -0.647 23.142 1.00 14.50 C ANISOU 653 CA LEU A 85 1607 2402 1500 2 -62 6 C ATOM 654 C LEU A 85 -24.347 -1.910 23.846 1.00 16.93 C ANISOU 654 C LEU A 85 1916 2735 1782 -38 -42 20 C ATOM 655 O LEU A 85 -23.556 -2.812 24.139 1.00 18.44 O ANISOU 655 O LEU A 85 2137 2900 1969 -52 -40 52 O ATOM 656 CB LEU A 85 -23.452 0.403 24.182 1.00 17.30 C ANISOU 656 CB LEU A 85 1957 2766 1850 21 -72 -13 C ATOM 657 CG LEU A 85 -23.046 1.788 23.629 1.00 17.81 C ANISOU 657 CG LEU A 85 2028 2796 1944 52 -95 -28 C ATOM 658 CD1 LEU A 85 -22.671 2.731 24.794 1.00 12.99 C ANISOU 658 CD1 LEU A 85 1422 2189 1327 62 -108 -56 C ATOM 659 CD2 LEU A 85 -21.852 1.608 22.666 1.00 16.60 C ANISOU 659 CD2 LEU A 85 1894 2598 1815 45 -96 6 C ATOM 660 N VAL A 86 -25.641 -1.959 24.192 1.00 17.69 N ANISOU 660 N VAL A 86 1978 2880 1863 -57 -26 -1 N ATOM 661 CA VAL A 86 -26.236 -3.176 24.746 1.00 17.13 C ANISOU 661 CA VAL A 86 1910 2832 1768 -112 0 17 C ATOM 662 C VAL A 86 -26.065 -4.338 23.767 1.00 18.50 C ANISOU 662 C VAL A 86 2116 2957 1956 -140 -7 41 C ATOM 663 O VAL A 86 -25.709 -5.464 24.149 1.00 18.12 O ANISOU 663 O VAL A 86 2109 2879 1896 -173 1 75 O ATOM 664 CB VAL A 86 -27.732 -2.943 25.061 1.00 17.83 C ANISOU 664 CB VAL A 86 1934 2989 1850 -131 26 -18 C ATOM 665 CG1 VAL A 86 -28.351 -4.217 25.685 1.00 17.44 C ANISOU 665 CG1 VAL A 86 1889 2963 1773 -208 62 7 C ATOM 666 CG2 VAL A 86 -27.932 -1.742 25.979 1.00 13.57 C ANISOU 666 CG2 VAL A 86 1367 2493 1297 -92 41 -57 C ATOM 667 N LEU A 87 -26.352 -4.087 22.492 1.00 15.21 N ANISOU 667 N LEU A 87 1690 2528 1560 -126 -27 23 N ATOM 668 CA LEU A 87 -26.329 -5.155 21.505 1.00 18.41 C ANISOU 668 CA LEU A 87 2134 2891 1971 -156 -33 32 C ATOM 669 C LEU A 87 -24.901 -5.582 21.193 1.00 17.18 C ANISOU 669 C LEU A 87 2034 2671 1823 -130 -29 54 C ATOM 670 O LEU A 87 -24.637 -6.772 20.978 1.00 17.81 O ANISOU 670 O LEU A 87 2158 2703 1906 -153 -21 67 O ATOM 671 CB LEU A 87 -27.035 -4.701 20.222 1.00 18.03 C ANISOU 671 CB LEU A 87 2070 2854 1928 -149 -64 5 C ATOM 672 CG LEU A 87 -28.481 -4.215 20.390 1.00 19.46 C ANISOU 672 CG LEU A 87 2174 3102 2117 -161 -78 -21 C ATOM 673 CD1 LEU A 87 -29.048 -3.771 19.041 1.00 16.70 C ANISOU 673 CD1 LEU A 87 1818 2756 1773 -146 -129 -39 C ATOM 674 CD2 LEU A 87 -29.387 -5.292 21.059 1.00 15.50 C ANISOU 674 CD2 LEU A 87 1644 2632 1613 -236 -54 -19 C ATOM 675 N ALA A 88 -23.976 -4.618 21.116 1.00 15.59 N ANISOU 675 N ALA A 88 1827 2462 1633 -83 -32 55 N ATOM 676 CA ALA A 88 -22.577 -4.964 20.931 1.00 17.71 C ANISOU 676 CA ALA A 88 2124 2683 1922 -56 -22 73 C ATOM 677 C ALA A 88 -22.068 -5.783 22.113 1.00 18.58 C ANISOU 677 C ALA A 88 2247 2779 2036 -62 -23 103 C ATOM 678 O ALA A 88 -21.301 -6.733 21.925 1.00 17.98 O ANISOU 678 O ALA A 88 2200 2650 1979 -49 -17 120 O ATOM 679 CB ALA A 88 -21.716 -3.693 20.755 1.00 12.10 C ANISOU 679 CB ALA A 88 1393 1975 1227 -19 -25 70 C ATOM 680 N GLN A 89 -22.474 -5.417 23.344 1.00 18.73 N ANISOU 680 N GLN A 89 2246 2839 2030 -76 -31 111 N ATOM 681 CA GLN A 89 -21.967 -6.131 24.527 1.00 18.00 C ANISOU 681 CA GLN A 89 2179 2734 1925 -83 -42 148 C ATOM 682 C GLN A 89 -22.493 -7.551 24.568 1.00 19.78 C ANISOU 682 C GLN A 89 2449 2925 2141 -126 -32 173 C ATOM 683 O GLN A 89 -21.757 -8.484 24.920 1.00 22.35 O ANISOU 683 O GLN A 89 2815 3198 2479 -116 -46 210 O ATOM 684 CB GLN A 89 -22.357 -5.419 25.827 1.00 14.98 C ANISOU 684 CB GLN A 89 1782 2410 1499 -97 -47 146 C ATOM 685 CG GLN A 89 -21.466 -5.867 27.006 1.00 17.94 C ANISOU 685 CG GLN A 89 2190 2773 1855 -92 -76 189 C ATOM 686 CD GLN A 89 -20.004 -5.503 26.738 1.00 19.86 C ANISOU 686 CD GLN A 89 2415 2985 2146 -41 -110 194 C ATOM 687 OE1 GLN A 89 -19.718 -4.411 26.232 1.00 19.81 O ANISOU 687 OE1 GLN A 89 2371 2992 2165 -20 -110 162 O ATOM 688 NE2 GLN A 89 -19.089 -6.424 27.026 1.00 16.92 N ANISOU 688 NE2 GLN A 89 2065 2568 1795 -22 -140 236 N ATOM 689 N SER A 90 -23.782 -7.718 24.242 1.00 17.62 N ANISOU 689 N SER A 90 2165 2679 1852 -175 -13 153 N ATOM 690 CA SER A 90 -24.389 -9.040 24.173 1.00 18.12 C ANISOU 690 CA SER A 90 2271 2705 1911 -232 -3 172 C ATOM 691 C SER A 90 -23.698 -9.913 23.134 1.00 18.40 C ANISOU 691 C SER A 90 2355 2655 1982 -210 -10 170 C ATOM 692 O SER A 90 -23.506 -11.116 23.359 1.00 17.19 O ANISOU 692 O SER A 90 2261 2434 1836 -230 -14 200 O ATOM 693 CB SER A 90 -25.889 -8.898 23.871 1.00 18.99 C ANISOU 693 CB SER A 90 2338 2870 2009 -290 13 142 C ATOM 694 OG SER A 90 -26.492 -10.155 23.590 1.00 21.73 O ANISOU 694 OG SER A 90 2724 3175 2360 -359 18 153 O ATOM 695 N SER A 91 -23.330 -9.327 21.986 1.00 19.71 N ANISOU 695 N SER A 91 2504 2818 2167 -169 -9 133 N ATOM 696 CA SER A 91 -22.569 -10.047 20.959 1.00 18.56 C ANISOU 696 CA SER A 91 2404 2599 2049 -139 -1 119 C ATOM 697 C SER A 91 -21.243 -10.547 21.514 1.00 19.14 C ANISOU 697 C SER A 91 2497 2620 2157 -85 -5 152 C ATOM 698 O SER A 91 -20.838 -11.678 21.248 1.00 20.46 O ANISOU 698 O SER A 91 2718 2708 2349 -72 -2 156 O ATOM 699 CB SER A 91 -22.295 -9.122 19.752 1.00 19.70 C ANISOU 699 CB SER A 91 2527 2765 2192 -105 10 81 C ATOM 700 OG SER A 91 -23.496 -8.622 19.172 1.00 16.97 O ANISOU 700 OG SER A 91 2164 2466 1818 -144 -3 55 O ATOM 701 N ILE A 92 -20.538 -9.691 22.259 1.00 16.62 N ANISOU 701 N ILE A 92 2131 2339 1843 -49 -18 170 N ATOM 702 CA ILE A 92 -19.261 -10.059 22.870 1.00 18.20 C ANISOU 702 CA ILE A 92 2331 2502 2081 5 -39 203 C ATOM 703 C ILE A 92 -19.434 -11.223 23.837 1.00 17.07 C ANISOU 703 C ILE A 92 2247 2310 1929 -17 -65 253 C ATOM 704 O ILE A 92 -18.642 -12.166 23.830 1.00 20.78 O ANISOU 704 O ILE A 92 2750 2704 2442 27 -79 274 O ATOM 705 CB ILE A 92 -18.637 -8.832 23.570 1.00 22.21 C ANISOU 705 CB ILE A 92 2779 3070 2589 29 -61 211 C ATOM 706 CG1 ILE A 92 -18.030 -7.888 22.534 1.00 26.86 C ANISOU 706 CG1 ILE A 92 3321 3678 3207 59 -34 174 C ATOM 707 CG2 ILE A 92 -17.609 -9.266 24.630 1.00 17.81 C ANISOU 707 CG2 ILE A 92 2221 2490 2056 65 -107 257 C ATOM 708 CD1 ILE A 92 -17.896 -6.471 23.010 1.00 33.32 C ANISOU 708 CD1 ILE A 92 4090 4555 4014 55 -51 168 C ATOM 709 N PHE A 93 -20.448 -11.163 24.708 1.00 16.43 N ANISOU 709 N PHE A 93 2180 2270 1793 -82 -70 275 N ATOM 710 CA PHE A 93 -20.727 -12.300 25.597 1.00 18.87 C ANISOU 710 CA PHE A 93 2559 2530 2080 -121 -88 331 C ATOM 711 C PHE A 93 -21.019 -13.588 24.818 1.00 19.68 C ANISOU 711 C PHE A 93 2727 2538 2211 -142 -76 326 C ATOM 712 O PHE A 93 -20.555 -14.680 25.198 1.00 19.79 O ANISOU 712 O PHE A 93 2810 2463 2247 -127 -101 371 O ATOM 713 CB PHE A 93 -21.901 -11.968 26.536 1.00 19.91 C ANISOU 713 CB PHE A 93 2689 2736 2141 -201 -74 346 C ATOM 714 CG PHE A 93 -21.538 -10.971 27.641 1.00 24.77 C ANISOU 714 CG PHE A 93 3274 3424 2715 -183 -94 360 C ATOM 715 CD1 PHE A 93 -20.309 -11.053 28.302 1.00 33.68 C ANISOU 715 CD1 PHE A 93 4417 4525 3854 -128 -147 399 C ATOM 716 CD2 PHE A 93 -22.407 -9.964 28.010 1.00 20.07 C ANISOU 716 CD2 PHE A 93 2633 2920 2072 -217 -65 327 C ATOM 717 CE1 PHE A 93 -19.973 -10.148 29.327 1.00 34.12 C ANISOU 717 CE1 PHE A 93 4454 4646 3864 -120 -176 405 C ATOM 718 CE2 PHE A 93 -22.073 -9.066 29.042 1.00 23.30 C ANISOU 718 CE2 PHE A 93 3029 3388 2437 -202 -83 329 C ATOM 719 CZ PHE A 93 -20.864 -9.144 29.680 1.00 26.15 C ANISOU 719 CZ PHE A 93 3413 3723 2799 -159 -140 367 C ATOM 720 N SER A 94 -21.802 -13.496 23.740 1.00 18.33 N ANISOU 720 N SER A 94 2545 2378 2040 -177 -45 272 N ATOM 721 CA SER A 94 -22.079 -14.695 22.945 1.00 20.87 C ANISOU 721 CA SER A 94 2938 2607 2386 -204 -37 256 C ATOM 722 C SER A 94 -20.801 -15.248 22.319 1.00 20.92 C ANISOU 722 C SER A 94 2974 2525 2451 -111 -39 241 C ATOM 723 O SER A 94 -20.554 -16.458 22.348 1.00 22.97 O ANISOU 723 O SER A 94 3312 2676 2740 -103 -51 259 O ATOM 724 CB SER A 94 -23.111 -14.386 21.862 1.00 20.06 C ANISOU 724 CB SER A 94 2814 2544 2266 -257 -17 196 C ATOM 725 OG SER A 94 -24.345 -14.096 22.482 1.00 19.25 O ANISOU 725 OG SER A 94 2678 2514 2124 -341 -13 209 O ATOM 726 N LEU A 95 -19.991 -14.375 21.725 1.00 19.83 N ANISOU 726 N LEU A 95 2775 2428 2333 -42 -23 206 N ATOM 727 CA LEU A 95 -18.743 -14.814 21.092 1.00 23.01 C ANISOU 727 CA LEU A 95 3183 2762 2795 50 -9 183 C ATOM 728 C LEU A 95 -17.802 -15.461 22.106 1.00 23.59 C ANISOU 728 C LEU A 95 3270 2776 2916 110 -51 242 C ATOM 729 O LEU A 95 -17.167 -16.481 21.812 1.00 24.59 O ANISOU 729 O LEU A 95 3444 2800 3097 168 -52 236 O ATOM 730 CB LEU A 95 -18.058 -13.625 20.409 1.00 19.73 C ANISOU 730 CB LEU A 95 2688 2419 2389 97 22 145 C ATOM 731 CG LEU A 95 -18.764 -13.051 19.174 1.00 19.81 C ANISOU 731 CG LEU A 95 2699 2471 2356 58 59 88 C ATOM 732 CD1 LEU A 95 -18.150 -11.689 18.768 1.00 19.55 C ANISOU 732 CD1 LEU A 95 2591 2516 2322 89 83 73 C ATOM 733 CD2 LEU A 95 -18.692 -14.031 18.008 1.00 18.69 C ANISOU 733 CD2 LEU A 95 2630 2249 2221 70 93 34 C ATOM 734 N LEU A 96 -17.696 -14.880 23.302 1.00 20.14 N ANISOU 734 N LEU A 96 2798 2399 2457 102 -92 296 N ATOM 735 CA LEU A 96 -16.852 -15.476 24.331 1.00 23.05 C ANISOU 735 CA LEU A 96 3185 2715 2858 155 -150 361 C ATOM 736 C LEU A 96 -17.405 -16.820 24.786 1.00 24.42 C ANISOU 736 C LEU A 96 3472 2785 3020 115 -174 409 C ATOM 737 O LEU A 96 -16.643 -17.771 25.000 1.00 26.57 O ANISOU 737 O LEU A 96 3790 2955 3349 182 -211 441 O ATOM 738 CB LEU A 96 -16.723 -14.514 25.509 1.00 28.59 C ANISOU 738 CB LEU A 96 3837 3509 3516 140 -192 403 C ATOM 739 CG LEU A 96 -15.822 -14.893 26.689 1.00 34.47 C ANISOU 739 CG LEU A 96 4595 4225 4278 191 -272 475 C ATOM 740 CD1 LEU A 96 -14.420 -15.317 26.224 1.00 35.28 C ANISOU 740 CD1 LEU A 96 4653 4266 4487 308 -292 464 C ATOM 741 CD2 LEU A 96 -15.784 -13.730 27.744 1.00 32.71 C ANISOU 741 CD2 LEU A 96 4325 4110 3995 163 -309 496 C ATOM 742 N ALA A 97 -18.731 -16.927 24.919 1.00 24.83 N ANISOU 742 N ALA A 97 3569 2858 3009 5 -154 414 N ATOM 743 CA ALA A 97 -19.333 -18.206 25.279 1.00 23.90 C ANISOU 743 CA ALA A 97 3563 2638 2881 -55 -169 460 C ATOM 744 C ALA A 97 -19.058 -19.259 24.214 1.00 26.14 C ANISOU 744 C ALA A 97 3909 2792 3230 -15 -155 416 C ATOM 745 O ALA A 97 -18.811 -20.425 24.533 1.00 24.02 O ANISOU 745 O ALA A 97 3736 2397 2995 1 -188 460 O ATOM 746 CB ALA A 97 -20.835 -18.035 25.480 1.00 22.48 C ANISOU 746 CB ALA A 97 3392 2520 2629 -189 -138 462 C ATOM 747 N ILE A 98 -19.138 -18.880 22.936 1.00 25.18 N ANISOU 747 N ILE A 98 3749 2697 3122 -3 -106 328 N ATOM 748 CA ILE A 98 -18.898 -19.864 21.879 1.00 22.72 C ANISOU 748 CA ILE A 98 3507 2265 2859 33 -85 272 C ATOM 749 C ILE A 98 -17.466 -20.384 21.968 1.00 23.71 C ANISOU 749 C ILE A 98 3634 2305 3069 170 -104 281 C ATOM 750 O ILE A 98 -17.233 -21.595 21.914 1.00 24.95 O ANISOU 750 O ILE A 98 3887 2320 3275 203 -122 288 O ATOM 751 CB ILE A 98 -19.228 -19.268 20.494 1.00 20.83 C ANISOU 751 CB ILE A 98 3231 2084 2599 19 -30 177 C ATOM 752 CG1 ILE A 98 -20.751 -19.075 20.365 1.00 22.07 C ANISOU 752 CG1 ILE A 98 3400 2298 2690 -116 -28 168 C ATOM 753 CG2 ILE A 98 -18.740 -20.212 19.389 1.00 22.92 C ANISOU 753 CG2 ILE A 98 3569 2230 2910 77 -1 106 C ATOM 754 CD1 ILE A 98 -21.248 -18.054 19.313 1.00 22.12 C ANISOU 754 CD1 ILE A 98 3345 2408 2654 -141 3 99 C ATOM 755 N ALA A 99 -16.493 -19.486 22.170 1.00 22.27 N ANISOU 755 N ALA A 99 3345 2205 2911 252 -107 285 N ATOM 756 CA ALA A 99 -15.094 -19.910 22.293 1.00 25.11 C ANISOU 756 CA ALA A 99 3677 2499 3363 387 -130 294 C ATOM 757 C ALA A 99 -14.904 -20.891 23.453 1.00 26.76 C ANISOU 757 C ALA A 99 3966 2605 3598 408 -212 387 C ATOM 758 O ALA A 99 -14.259 -21.945 23.303 1.00 28.53 O ANISOU 758 O ALA A 99 4245 2694 3900 497 -232 386 O ATOM 759 CB ALA A 99 -14.199 -18.676 22.473 1.00 20.18 C ANISOU 759 CB ALA A 99 2913 1997 2756 443 -129 292 C ATOM 760 N ILE A 100 -15.479 -20.566 24.615 1.00 23.85 N ANISOU 760 N ILE A 100 3613 2292 3158 328 -261 467 N ATOM 761 CA ILE A 100 -15.324 -21.418 25.798 1.00 27.78 C ANISOU 761 CA ILE A 100 4198 2701 3657 336 -344 570 C ATOM 762 C ILE A 100 -15.982 -22.768 25.573 1.00 26.28 C ANISOU 762 C ILE A 100 4155 2356 3476 288 -342 583 C ATOM 763 O ILE A 100 -15.427 -23.811 25.939 1.00 28.19 O ANISOU 763 O ILE A 100 4479 2456 3776 356 -400 634 O ATOM 764 CB ILE A 100 -15.870 -20.697 27.050 1.00 28.05 C ANISOU 764 CB ILE A 100 4224 2844 3591 247 -380 645 C ATOM 765 CG1 ILE A 100 -15.003 -19.450 27.303 1.00 29.92 C ANISOU 765 CG1 ILE A 100 4325 3207 3836 310 -399 630 C ATOM 766 CG2 ILE A 100 -15.901 -21.649 28.272 1.00 25.90 C ANISOU 766 CG2 ILE A 100 4072 2476 3292 228 -462 762 C ATOM 767 CD1 ILE A 100 -15.488 -18.534 28.413 1.00 32.00 C ANISOU 767 CD1 ILE A 100 4570 3592 3997 230 -424 677 C ATOM 768 N ASP A 101 -17.159 -22.769 24.935 1.00 27.27 N ANISOU 768 N ASP A 101 4313 2498 3550 172 -282 535 N ATOM 769 CA ASP A 101 -17.852 -24.016 24.623 1.00 29.77 C ANISOU 769 CA ASP A 101 4768 2667 3876 106 -278 535 C ATOM 770 C ASP A 101 -16.984 -24.947 23.772 1.00 29.93 C ANISOU 770 C ASP A 101 4838 2535 3999 229 -276 477 C ATOM 771 O ASP A 101 -16.936 -26.156 24.016 1.00 29.43 O ANISOU 771 O ASP A 101 4901 2304 3976 240 -316 518 O ATOM 772 CB ASP A 101 -19.163 -23.706 23.905 1.00 29.11 C ANISOU 772 CB ASP A 101 4679 2650 3731 -30 -217 473 C ATOM 773 CG ASP A 101 -19.912 -24.959 23.505 1.00 36.17 C ANISOU 773 CG ASP A 101 5709 3396 4638 -114 -215 462 C ATOM 774 OD1 ASP A 101 -20.477 -25.609 24.404 1.00 37.84 O ANISOU 774 OD1 ASP A 101 6010 3547 4822 -205 -247 550 O ATOM 775 OD2 ASP A 101 -19.902 -25.315 22.306 1.00 37.70 O ANISOU 775 OD2 ASP A 101 5929 3529 4865 -93 -182 366 O ATOM 776 N ARG A 102 -16.299 -24.401 22.756 1.00 29.99 N ANISOU 776 N ARG A 102 4753 2594 4048 321 -223 381 N ATOM 777 CA ARG A 102 -15.445 -25.231 21.911 1.00 31.73 C ANISOU 777 CA ARG A 102 5010 2682 4364 446 -203 311 C ATOM 778 C ARG A 102 -14.182 -25.670 22.650 1.00 32.50 C ANISOU 778 C ARG A 102 5091 2703 4554 595 -270 372 C ATOM 779 O ARG A 102 -13.677 -26.777 22.417 1.00 34.42 O ANISOU 779 O ARG A 102 5416 2778 4882 688 -287 357 O ATOM 780 CB ARG A 102 -15.090 -24.475 20.623 1.00 36.36 C ANISOU 780 CB ARG A 102 5502 3360 4954 492 -115 193 C ATOM 781 CG ARG A 102 -16.271 -24.272 19.628 1.00 38.93 C ANISOU 781 CG ARG A 102 5867 3726 5198 365 -58 116 C ATOM 782 CD ARG A 102 -16.808 -25.635 19.118 1.00 42.81 C ANISOU 782 CD ARG A 102 6520 4041 5707 326 -60 76 C ATOM 783 NE ARG A 102 -17.773 -26.221 20.043 1.00 45.04 N ANISOU 783 NE ARG A 102 6894 4264 5957 202 -120 166 N ATOM 784 CZ ARG A 102 -18.072 -27.512 20.119 1.00 46.83 C ANISOU 784 CZ ARG A 102 7269 4310 6216 171 -151 179 C ATOM 785 NH1 ARG A 102 -17.472 -28.380 19.320 1.00 48.63 N ANISOU 785 NH1 ARG A 102 7574 4389 6513 267 -131 99 N ATOM 786 NH2 ARG A 102 -18.961 -27.931 21.012 1.00 44.32 N ANISOU 786 NH2 ARG A 102 7023 3955 5861 42 -196 271 N ATOM 787 N TYR A 103 -13.669 -24.836 23.553 1.00 27.52 N ANISOU 787 N TYR A 103 4357 2187 3912 624 -317 440 N ATOM 788 CA TYR A 103 -12.536 -25.260 24.363 1.00 30.17 C ANISOU 788 CA TYR A 103 4675 2455 4331 756 -404 510 C ATOM 789 C TYR A 103 -12.904 -26.453 25.249 1.00 34.11 C ANISOU 789 C TYR A 103 5340 2793 4827 727 -490 614 C ATOM 790 O TYR A 103 -12.165 -27.444 25.312 1.00 38.41 O ANISOU 790 O TYR A 103 5943 3181 5471 849 -541 632 O ATOM 791 CB TYR A 103 -12.010 -24.095 25.209 1.00 30.81 C ANISOU 791 CB TYR A 103 4622 2697 4386 769 -450 562 C ATOM 792 CG TYR A 103 -10.856 -24.531 26.082 1.00 38.73 C ANISOU 792 CG TYR A 103 5604 3638 5473 902 -560 639 C ATOM 793 CD1 TYR A 103 -9.657 -24.936 25.513 1.00 39.84 C ANISOU 793 CD1 TYR A 103 5672 3713 5751 1070 -556 586 C ATOM 794 CD2 TYR A 103 -10.982 -24.595 27.467 1.00 44.83 C ANISOU 794 CD2 TYR A 103 6433 4413 6186 862 -668 765 C ATOM 795 CE1 TYR A 103 -8.598 -25.359 26.295 1.00 45.11 C ANISOU 795 CE1 TYR A 103 6309 4323 6509 1202 -669 657 C ATOM 796 CE2 TYR A 103 -9.927 -25.032 28.263 1.00 49.33 C ANISOU 796 CE2 TYR A 103 6992 4922 6831 987 -787 842 C ATOM 797 CZ TYR A 103 -8.735 -25.403 27.666 1.00 51.03 C ANISOU 797 CZ TYR A 103 7119 5075 7197 1161 -792 787 C ATOM 798 OH TYR A 103 -7.670 -25.831 28.433 1.00 57.62 O ANISOU 798 OH TYR A 103 7925 5850 8118 1296 -921 862 O ATOM 799 N ILE A 104 -14.037 -26.369 25.958 1.00 32.77 N ANISOU 799 N ILE A 104 5248 2657 4546 568 -504 685 N ATOM 800 CA ILE A 104 -14.474 -27.492 26.793 1.00 35.46 C ANISOU 800 CA ILE A 104 5759 2845 4870 514 -575 793 C ATOM 801 C ILE A 104 -14.645 -28.752 25.953 1.00 34.02 C ANISOU 801 C ILE A 104 5705 2462 4758 533 -552 740 C ATOM 802 O ILE A 104 -14.261 -29.847 26.373 1.00 36.92 O ANISOU 802 O ILE A 104 6192 2648 5187 597 -624 805 O ATOM 803 CB ILE A 104 -15.771 -27.138 27.546 1.00 35.40 C ANISOU 803 CB ILE A 104 5800 2926 4725 321 -563 861 C ATOM 804 CG1 ILE A 104 -15.536 -25.991 28.534 1.00 34.28 C ANISOU 804 CG1 ILE A 104 5555 2959 4509 313 -597 917 C ATOM 805 CG2 ILE A 104 -16.321 -28.366 28.281 1.00 38.92 C ANISOU 805 CG2 ILE A 104 6435 3206 5148 241 -617 969 C ATOM 806 CD1 ILE A 104 -16.827 -25.489 29.207 1.00 32.97 C ANISOU 806 CD1 ILE A 104 5415 2905 4206 130 -562 962 C ATOM 807 N ALA A 105 -15.212 -28.619 24.749 1.00 33.13 N ANISOU 807 N ALA A 105 5579 2372 4637 480 -457 620 N ATOM 808 CA ALA A 105 -15.442 -29.798 23.915 1.00 35.54 C ANISOU 808 CA ALA A 105 6018 2486 4999 483 -435 556 C ATOM 809 C ALA A 105 -14.137 -30.484 23.525 1.00 39.54 C ANISOU 809 C ALA A 105 6528 2853 5640 691 -455 513 C ATOM 810 O ALA A 105 -14.086 -31.713 23.428 1.00 40.97 O ANISOU 810 O ALA A 105 6858 2824 5887 727 -487 517 O ATOM 811 CB ALA A 105 -16.230 -29.421 22.660 1.00 32.32 C ANISOU 811 CB ALA A 105 5586 2149 4546 392 -337 428 C ATOM 812 N ILE A 106 -13.075 -29.723 23.274 1.00 40.39 N ANISOU 812 N ILE A 106 6474 3071 5800 829 -434 466 N ATOM 813 CA ILE A 106 -11.832 -30.367 22.858 1.00 42.42 C ANISOU 813 CA ILE A 106 6714 3206 6198 1032 -442 415 C ATOM 814 C ILE A 106 -10.948 -30.762 24.043 1.00 43.75 C ANISOU 814 C ILE A 106 6881 3302 6439 1152 -568 538 C ATOM 815 O ILE A 106 -10.219 -31.752 23.962 1.00 42.95 O ANISOU 815 O ILE A 106 6840 3024 6457 1299 -608 532 O ATOM 816 CB ILE A 106 -11.054 -29.481 21.869 1.00 43.58 C ANISOU 816 CB ILE A 106 6685 3493 6380 1128 -345 292 C ATOM 817 CG1 ILE A 106 -10.024 -30.333 21.129 1.00 49.69 C ANISOU 817 CG1 ILE A 106 7465 4120 7293 1318 -314 201 C ATOM 818 CG2 ILE A 106 -10.336 -28.336 22.580 1.00 38.15 C ANISOU 818 CG2 ILE A 106 5818 2987 5693 1171 -381 350 C ATOM 819 CD1 ILE A 106 -9.341 -29.585 20.037 1.00 51.93 C ANISOU 819 CD1 ILE A 106 7596 4530 7603 1396 -196 72 C ATOM 820 N ALA A 107 -10.994 -30.021 25.150 1.00 44.33 N ANISOU 820 N ALA A 107 6895 3505 6443 1097 -636 649 N ATOM 821 CA ALA A 107 -10.094 -30.299 26.260 1.00 46.99 C ANISOU 821 CA ALA A 107 7222 3794 6839 1213 -768 765 C ATOM 822 C ALA A 107 -10.607 -31.425 27.146 1.00 54.20 C ANISOU 822 C ALA A 107 8346 4521 7728 1158 -866 893 C ATOM 823 O ALA A 107 -9.807 -32.198 27.694 1.00 60.16 O ANISOU 823 O ALA A 107 9100 5201 8559 1264 -931 950 O ATOM 824 CB ALA A 107 -9.882 -29.028 27.085 1.00 43.76 C ANISOU 824 CB ALA A 107 6672 3599 6357 1175 -807 824 C ATOM 825 N ILE A 108 -11.920 -31.541 27.302 1.00 52.55 N ANISOU 825 N ILE A 108 8258 4308 7400 960 -832 927 N ATOM 826 CA ILE A 108 -12.496 -32.571 28.160 1.00 51.77 C ANISOU 826 CA ILE A 108 8328 4085 7258 864 -888 1044 C ATOM 827 C ILE A 108 -13.731 -33.162 27.490 1.00 49.88 C ANISOU 827 C ILE A 108 8229 3746 6978 707 -814 996 C ATOM 828 O ILE A 108 -14.840 -33.062 28.032 1.00 50.69 O ANISOU 828 O ILE A 108 8405 3891 6963 517 -804 1065 O ATOM 829 CB ILE A 108 -12.825 -32.008 29.552 1.00 53.86 C ANISOU 829 CB ILE A 108 8592 4477 7394 759 -952 1182 C ATOM 830 CG1 ILE A 108 -13.586 -30.685 29.438 1.00 53.53 C ANISOU 830 CG1 ILE A 108 8472 4628 7239 632 -890 1151 C ATOM 831 CG2 ILE A 108 -11.545 -31.821 30.370 1.00 55.68 C ANISOU 831 CG2 ILE A 108 8717 4767 7673 912 -1048 1243 C ATOM 832 CD1 ILE A 108 -14.079 -30.165 30.776 1.00 56.59 C ANISOU 832 CD1 ILE A 108 8887 5131 7486 510 -939 1278 C ATOM 833 N PRO A 109 -13.591 -33.804 26.331 1.00 50.79 N ANISOU 833 N PRO A 109 8377 3737 7185 772 -757 874 N ATOM 834 CA PRO A 109 -14.783 -34.332 25.646 1.00 54.49 C ANISOU 834 CA PRO A 109 8971 4122 7611 610 -692 817 C ATOM 835 C PRO A 109 -15.612 -35.288 26.494 1.00 60.47 C ANISOU 835 C PRO A 109 9867 4793 8317 456 -726 929 C ATOM 836 O PRO A 109 -16.845 -35.284 26.381 1.00 59.51 O ANISOU 836 O PRO A 109 9810 4690 8111 260 -684 928 O ATOM 837 CB PRO A 109 -14.186 -35.042 24.424 1.00 54.30 C ANISOU 837 CB PRO A 109 8960 3966 7707 744 -642 673 C ATOM 838 CG PRO A 109 -12.767 -35.344 24.819 1.00 53.00 C ANISOU 838 CG PRO A 109 8711 3769 7658 959 -697 702 C ATOM 839 CD PRO A 109 -12.346 -34.171 25.636 1.00 49.40 C ANISOU 839 CD PRO A 109 8124 3491 7153 989 -746 782 C ATOM 840 N LEU A 110 -14.973 -36.096 27.352 1.00 66.08 N ANISOU 840 N LEU A 110 10616 5416 9074 538 -800 1027 N ATOM 841 CA LEU A 110 -15.687 -37.121 28.108 1.00 71.14 C ANISOU 841 CA LEU A 110 11400 5954 9675 405 -829 1130 C ATOM 842 C LEU A 110 -16.695 -36.540 29.096 1.00 74.51 C ANISOU 842 C LEU A 110 11841 6521 9949 209 -826 1237 C ATOM 843 O LEU A 110 -17.651 -37.235 29.464 1.00 76.87 O ANISOU 843 O LEU A 110 12250 6763 10196 45 -812 1292 O ATOM 844 CB LEU A 110 -14.695 -38.019 28.854 1.00 70.42 C ANISOU 844 CB LEU A 110 11346 5748 9663 549 -914 1217 C ATOM 845 CG LEU A 110 -13.674 -38.779 28.003 1.00 70.05 C ANISOU 845 CG LEU A 110 11288 5550 9778 749 -913 1121 C ATOM 846 CD1 LEU A 110 -12.698 -39.524 28.898 1.00 72.23 C ANISOU 846 CD1 LEU A 110 11585 5738 10123 888 -1007 1227 C ATOM 847 CD2 LEU A 110 -14.365 -39.734 27.041 1.00 69.46 C ANISOU 847 CD2 LEU A 110 11334 5314 9745 672 -854 1027 C ATOM 848 N ARG A 111 -16.512 -35.297 29.536 1.00 73.85 N ANISOU 848 N ARG A 111 11645 6621 9795 219 -834 1264 N ATOM 849 CA ARG A 111 -17.459 -34.666 30.447 1.00 75.31 C ANISOU 849 CA ARG A 111 11829 6953 9831 39 -816 1351 C ATOM 850 C ARG A 111 -18.140 -33.444 29.846 1.00 68.24 C ANISOU 850 C ARG A 111 10844 6212 8871 -53 -743 1276 C ATOM 851 O ARG A 111 -18.793 -32.695 30.583 1.00 65.48 O ANISOU 851 O ARG A 111 10461 6017 8403 -177 -722 1335 O ATOM 852 CB ARG A 111 -16.771 -34.285 31.760 1.00 82.35 C ANISOU 852 CB ARG A 111 12682 7937 10668 104 -895 1467 C ATOM 853 CG ARG A 111 -15.275 -34.140 31.651 1.00 89.35 C ANISOU 853 CG ARG A 111 13480 8807 11662 337 -967 1446 C ATOM 854 CD ARG A 111 -14.662 -33.824 33.005 1.00 96.51 C ANISOU 854 CD ARG A 111 14357 9809 12505 381 -1055 1563 C ATOM 855 NE ARG A 111 -13.203 -33.805 32.941 1.00101.90 N ANISOU 855 NE ARG A 111 14943 10471 13302 601 -1131 1546 N ATOM 856 CZ ARG A 111 -12.417 -33.270 33.869 1.00104.38 C ANISOU 856 CZ ARG A 111 15182 10894 13585 675 -1213 1612 C ATOM 857 NH1 ARG A 111 -12.947 -32.698 34.944 1.00104.17 N ANISOU 857 NH1 ARG A 111 15178 10998 13405 550 -1228 1694 N ATOM 858 NH2 ARG A 111 -11.099 -33.305 33.715 1.00106.28 N ANISOU 858 NH2 ARG A 111 15318 11116 13945 872 -1276 1587 N ATOM 859 N TYR A 112 -18.016 -33.222 28.533 1.00 62.60 N ANISOU 859 N TYR A 112 10093 5463 8228 5 -700 1144 N ATOM 860 CA TYR A 112 -18.658 -32.064 27.916 1.00 54.74 C ANISOU 860 CA TYR A 112 8968 4658 7171 -77 -614 1053 C ATOM 861 C TYR A 112 -20.176 -32.144 28.049 1.00 57.41 C ANISOU 861 C TYR A 112 9358 5038 7417 -316 -558 1074 C ATOM 862 O TYR A 112 -20.823 -31.187 28.491 1.00 54.84 O ANISOU 862 O TYR A 112 8933 4909 6994 -417 -514 1090 O ATOM 863 CB TYR A 112 -18.248 -31.947 26.445 1.00 46.73 C ANISOU 863 CB TYR A 112 7879 3634 6243 27 -558 887 C ATOM 864 CG TYR A 112 -19.005 -30.872 25.695 1.00 43.94 C ANISOU 864 CG TYR A 112 7389 3480 5826 -66 -467 784 C ATOM 865 CD1 TYR A 112 -18.556 -29.565 25.682 1.00 40.09 C ANISOU 865 CD1 TYR A 112 6726 3194 5312 1 -442 750 C ATOM 866 CD2 TYR A 112 -20.175 -31.169 24.999 1.00 47.82 C ANISOU 866 CD2 TYR A 112 7929 3953 6288 -223 -415 722 C ATOM 867 CE1 TYR A 112 -19.248 -28.570 25.010 1.00 38.16 C ANISOU 867 CE1 TYR A 112 6368 3121 5012 -77 -368 664 C ATOM 868 CE2 TYR A 112 -20.879 -30.181 24.321 1.00 45.75 C ANISOU 868 CE2 TYR A 112 7541 3872 5970 -300 -346 634 C ATOM 869 CZ TYR A 112 -20.407 -28.882 24.334 1.00 41.32 C ANISOU 869 CZ TYR A 112 6815 3501 5382 -222 -323 608 C ATOM 870 OH TYR A 112 -21.094 -27.900 23.663 1.00 40.21 O ANISOU 870 OH TYR A 112 6560 3528 5190 -290 -264 528 O ATOM 871 N ASN A 113 -20.765 -33.289 27.686 1.00 63.35 N ANISOU 871 N ASN A 113 10256 5610 8202 -408 -555 1069 N ATOM 872 CA ASN A 113 -22.223 -33.399 27.674 1.00 64.48 C ANISOU 872 CA ASN A 113 10417 5806 8275 -638 -494 1069 C ATOM 873 C ASN A 113 -22.820 -33.307 29.073 1.00 62.37 C ANISOU 873 C ASN A 113 10148 5645 7905 -761 -489 1199 C ATOM 874 O ASN A 113 -23.924 -32.775 29.238 1.00 60.63 O ANISOU 874 O ASN A 113 9870 5563 7603 -929 -426 1201 O ATOM 875 CB ASN A 113 -22.647 -34.696 26.985 1.00 67.50 C ANISOU 875 CB ASN A 113 10908 6013 8727 -694 -488 1012 C ATOM 876 CG ASN A 113 -22.618 -34.577 25.471 1.00 69.12 C ANISOU 876 CG ASN A 113 11100 6173 8989 -656 -457 853 C ATOM 877 OD1 ASN A 113 -22.606 -33.462 24.917 1.00 65.71 O ANISOU 877 OD1 ASN A 113 10528 5911 8530 -625 -414 772 O ATOM 878 ND2 ASN A 113 -22.614 -35.718 24.789 1.00 72.50 N ANISOU 878 ND2 ASN A 113 11626 6430 9492 -644 -465 787 N ATOM 879 N GLY A 114 -22.109 -33.798 30.088 1.00 62.41 N ANISOU 879 N GLY A 114 10207 5596 7907 -677 -552 1304 N ATOM 880 CA GLY A 114 -22.585 -33.642 31.451 1.00 63.19 C ANISOU 880 CA GLY A 114 10311 5805 7894 -781 -545 1421 C ATOM 881 C GLY A 114 -22.472 -32.223 31.979 1.00 60.78 C ANISOU 881 C GLY A 114 9887 5709 7496 -767 -530 1437 C ATOM 882 O GLY A 114 -23.244 -31.822 32.856 1.00 63.99 O ANISOU 882 O GLY A 114 10267 6253 7792 -896 -483 1491 O ATOM 883 N LEU A 115 -21.520 -31.447 31.466 1.00 52.79 N ANISOU 883 N LEU A 115 8800 4727 6530 -611 -565 1385 N ATOM 884 CA LEU A 115 -21.212 -30.134 32.013 1.00 50.82 C ANISOU 884 CA LEU A 115 8445 4662 6204 -574 -570 1404 C ATOM 885 C LEU A 115 -21.923 -29.005 31.283 1.00 52.10 C ANISOU 885 C LEU A 115 8438 5016 6341 -632 -473 1282 C ATOM 886 O LEU A 115 -22.405 -28.067 31.927 1.00 52.45 O ANISOU 886 O LEU A 115 8401 5241 6286 -701 -432 1298 O ATOM 887 CB LEU A 115 -19.697 -29.892 31.976 1.00 54.59 C ANISOU 887 CB LEU A 115 8874 5111 6756 -350 -658 1397 C ATOM 888 CG LEU A 115 -19.196 -28.450 32.161 1.00 59.11 C ANISOU 888 CG LEU A 115 9268 5900 7291 -273 -651 1350 C ATOM 889 CD1 LEU A 115 -19.583 -27.956 33.527 1.00 63.13 C ANISOU 889 CD1 LEU A 115 9802 6528 7656 -369 -662 1455 C ATOM 890 CD2 LEU A 115 -17.684 -28.322 31.967 1.00 59.78 C ANISOU 890 CD2 LEU A 115 9286 5949 7477 -57 -733 1328 C ATOM 891 N VAL A 116 -21.998 -29.072 29.955 1.00 49.88 N ANISOU 891 N VAL A 116 8105 4701 6145 -600 -436 1157 N ATOM 892 CA VAL A 116 -22.548 -28.005 29.131 1.00 46.80 C ANISOU 892 CA VAL A 116 7555 4485 5743 -629 -360 1036 C ATOM 893 C VAL A 116 -23.908 -28.486 28.637 1.00 49.87 C ANISOU 893 C VAL A 116 7978 4852 6119 -811 -301 1003 C ATOM 894 O VAL A 116 -23.995 -29.198 27.631 1.00 54.98 O ANISOU 894 O VAL A 116 8678 5373 6837 -812 -301 933 O ATOM 895 CB VAL A 116 -21.609 -27.646 27.973 1.00 44.46 C ANISOU 895 CB VAL A 116 7172 4184 5538 -462 -363 919 C ATOM 896 CG1 VAL A 116 -22.087 -26.418 27.253 1.00 39.84 C ANISOU 896 CG1 VAL A 116 6427 3784 4925 -484 -296 815 C ATOM 897 CG2 VAL A 116 -20.205 -27.420 28.487 1.00 46.48 C ANISOU 897 CG2 VAL A 116 7403 4429 5829 -287 -432 961 C ATOM 898 N THR A 117 -24.974 -28.107 29.344 1.00 45.48 N ANISOU 898 N THR A 117 7389 4419 5472 -967 -250 1049 N ATOM 899 CA THR A 117 -26.337 -28.511 29.033 1.00 42.73 C ANISOU 899 CA THR A 117 7051 4073 5111 -1158 -194 1029 C ATOM 900 C THR A 117 -27.125 -27.334 28.470 1.00 40.71 C ANISOU 900 C THR A 117 6613 4023 4831 -1199 -129 928 C ATOM 901 O THR A 117 -26.795 -26.165 28.701 1.00 37.03 O ANISOU 901 O THR A 117 6029 3711 4330 -1115 -116 905 O ATOM 902 CB THR A 117 -27.057 -29.040 30.282 1.00 47.43 C ANISOU 902 CB THR A 117 7742 4655 5625 -1322 -173 1161 C ATOM 903 OG1 THR A 117 -27.062 -28.016 31.287 1.00 52.15 O ANISOU 903 OG1 THR A 117 8256 5433 6124 -1314 -144 1204 O ATOM 904 CG2 THR A 117 -26.371 -30.292 30.841 1.00 42.94 C ANISOU 904 CG2 THR A 117 7355 3878 5082 -1281 -244 1261 C ATOM 905 N GLY A 118 -28.204 -27.662 27.752 1.00 40.10 N ANISOU 905 N GLY A 118 6518 3943 4776 -1334 -96 870 N ATOM 906 CA GLY A 118 -29.050 -26.622 27.188 1.00 40.22 C ANISOU 906 CA GLY A 118 6361 4144 4776 -1377 -47 778 C ATOM 907 C GLY A 118 -29.683 -25.746 28.251 1.00 42.17 C ANISOU 907 C GLY A 118 6509 4574 4939 -1443 12 826 C ATOM 908 O GLY A 118 -29.792 -24.526 28.087 1.00 45.84 O ANISOU 908 O GLY A 118 6828 5202 5385 -1385 38 765 O ATOM 909 N THR A 119 -30.107 -26.355 29.352 1.00 41.29 N ANISOU 909 N THR A 119 6481 4432 4773 -1566 38 935 N ATOM 910 CA THR A 119 -30.721 -25.610 30.444 1.00 43.62 C ANISOU 910 CA THR A 119 6698 4899 4976 -1637 107 980 C ATOM 911 C THR A 119 -29.748 -24.617 31.057 1.00 42.37 C ANISOU 911 C THR A 119 6505 4827 4768 -1481 88 992 C ATOM 912 O THR A 119 -30.105 -23.462 31.307 1.00 44.08 O ANISOU 912 O THR A 119 6588 5219 4941 -1465 137 949 O ATOM 913 CB THR A 119 -31.232 -26.590 31.505 1.00 47.82 C ANISOU 913 CB THR A 119 7353 5363 5452 -1791 138 1100 C ATOM 914 OG1 THR A 119 -32.421 -27.218 31.024 1.00 51.40 O ANISOU 914 OG1 THR A 119 7767 5809 5953 -1937 175 1058 O ATOM 915 CG2 THR A 119 -31.531 -25.883 32.789 1.00 48.85 C ANISOU 915 CG2 THR A 119 7423 5660 5479 -1803 202 1140 C ATOM 916 N ARG A 120 -28.509 -25.044 31.311 1.00 43.23 N ANISOU 916 N ARG A 120 6728 4810 4887 -1362 13 1048 N ATOM 917 CA ARG A 120 -27.515 -24.102 31.809 1.00 41.48 C ANISOU 917 CA ARG A 120 6464 4668 4630 -1214 -19 1051 C ATOM 918 C ARG A 120 -27.184 -23.038 30.771 1.00 41.13 C ANISOU 918 C ARG A 120 6274 4712 4643 -1093 -22 928 C ATOM 919 O ARG A 120 -26.898 -21.896 31.141 1.00 39.03 O ANISOU 919 O ARG A 120 5917 4577 4336 -1024 -13 904 O ATOM 920 CB ARG A 120 -26.243 -24.831 32.236 1.00 42.43 C ANISOU 920 CB ARG A 120 6723 4633 4765 -1107 -112 1135 C ATOM 921 CG ARG A 120 -26.434 -25.757 33.425 1.00 46.54 C ANISOU 921 CG ARG A 120 7404 5071 5210 -1212 -123 1277 C ATOM 922 CD ARG A 120 -25.231 -26.652 33.651 1.00 50.03 C ANISOU 922 CD ARG A 120 7991 5326 5692 -1101 -231 1358 C ATOM 923 NE ARG A 120 -25.401 -27.458 34.856 1.00 56.36 N ANISOU 923 NE ARG A 120 8907 6081 6426 -1166 -241 1467 N ATOM 924 CZ ARG A 120 -24.647 -28.503 35.174 1.00 57.59 C ANISOU 924 CZ ARG A 120 9186 6073 6624 -1093 -324 1536 C ATOM 925 NH1 ARG A 120 -24.885 -29.169 36.298 1.00 61.44 N ANISOU 925 NH1 ARG A 120 9759 6542 7043 -1154 -324 1625 N ATOM 926 NH2 ARG A 120 -23.666 -28.887 34.367 1.00 54.25 N ANISOU 926 NH2 ARG A 120 8797 5504 6310 -955 -403 1513 N ATOM 927 N ALA A 121 -27.212 -23.384 29.478 1.00 40.59 N ANISOU 927 N ALA A 121 6191 4570 4662 -1071 -35 850 N ATOM 928 CA ALA A 121 -26.914 -22.390 28.447 1.00 37.04 C ANISOU 928 CA ALA A 121 5618 4201 4256 -966 -35 740 C ATOM 929 C ALA A 121 -27.979 -21.301 28.408 1.00 35.32 C ANISOU 929 C ALA A 121 5256 4164 4001 -1031 26 684 C ATOM 930 O ALA A 121 -27.649 -20.116 28.299 1.00 35.62 O ANISOU 930 O ALA A 121 5193 4311 4029 -940 30 636 O ATOM 931 CB ALA A 121 -26.782 -23.055 27.079 1.00 34.58 C ANISOU 931 CB ALA A 121 5339 3771 4027 -942 -58 668 C ATOM 932 N ALA A 122 -29.259 -21.678 28.504 1.00 34.20 N ANISOU 932 N ALA A 122 5098 4053 3842 -1186 74 690 N ATOM 933 CA ALA A 122 -30.320 -20.673 28.497 1.00 34.02 C ANISOU 933 CA ALA A 122 4926 4204 3796 -1240 132 635 C ATOM 934 C ALA A 122 -30.164 -19.698 29.664 1.00 35.64 C ANISOU 934 C ALA A 122 5084 4534 3922 -1202 167 666 C ATOM 935 O ALA A 122 -30.314 -18.483 29.490 1.00 37.00 O ANISOU 935 O ALA A 122 5136 4831 4091 -1141 186 600 O ATOM 936 CB ALA A 122 -31.691 -21.345 28.536 1.00 33.26 C ANISOU 936 CB ALA A 122 4814 4121 3701 -1422 179 645 C ATOM 937 N GLY A 123 -29.813 -20.207 30.848 1.00 33.57 N ANISOU 937 N GLY A 123 4929 4231 3594 -1233 169 764 N ATOM 938 CA GLY A 123 -29.596 -19.329 31.981 1.00 31.86 C ANISOU 938 CA GLY A 123 4689 4126 3289 -1198 196 789 C ATOM 939 C GLY A 123 -28.386 -18.434 31.807 1.00 31.24 C ANISOU 939 C GLY A 123 4583 4062 3226 -1032 137 754 C ATOM 940 O GLY A 123 -28.404 -17.266 32.211 1.00 34.75 O ANISOU 940 O GLY A 123 4946 4629 3628 -987 161 715 O ATOM 941 N ILE A 124 -27.315 -18.959 31.207 1.00 28.34 N ANISOU 941 N ILE A 124 4279 3566 2923 -939 62 763 N ATOM 942 CA ILE A 124 -26.165 -18.111 30.910 1.00 26.68 C ANISOU 942 CA ILE A 124 4023 3373 2742 -789 11 723 C ATOM 943 C ILE A 124 -26.557 -17.000 29.936 1.00 26.96 C ANISOU 943 C ILE A 124 3921 3505 2816 -752 40 616 C ATOM 944 O ILE A 124 -26.147 -15.834 30.094 1.00 25.30 O ANISOU 944 O ILE A 124 3640 3380 2591 -676 36 580 O ATOM 945 CB ILE A 124 -25.001 -18.965 30.375 1.00 32.14 C ANISOU 945 CB ILE A 124 4795 3910 3507 -698 -62 745 C ATOM 946 CG1 ILE A 124 -24.454 -19.863 31.492 1.00 36.73 C ANISOU 946 CG1 ILE A 124 5510 4401 4046 -707 -110 860 C ATOM 947 CG2 ILE A 124 -23.887 -18.093 29.815 1.00 29.50 C ANISOU 947 CG2 ILE A 124 4387 3600 3222 -555 -99 689 C ATOM 948 CD1 ILE A 124 -23.562 -20.971 30.965 1.00 40.37 C ANISOU 948 CD1 ILE A 124 6063 4686 4591 -634 -175 887 C ATOM 949 N ILE A 125 -27.344 -17.342 28.910 1.00 22.95 N ANISOU 949 N ILE A 125 3382 2979 2359 -806 61 567 N ATOM 950 CA ILE A 125 -27.738 -16.355 27.908 1.00 25.69 C ANISOU 950 CA ILE A 125 3612 3408 2741 -770 74 474 C ATOM 951 C ILE A 125 -28.583 -15.252 28.541 1.00 22.57 C ANISOU 951 C ILE A 125 3115 3163 2297 -800 126 449 C ATOM 952 O ILE A 125 -28.343 -14.064 28.309 1.00 22.28 O ANISOU 952 O ILE A 125 3001 3198 2266 -719 122 397 O ATOM 953 CB ILE A 125 -28.455 -17.052 26.735 1.00 26.46 C ANISOU 953 CB ILE A 125 3709 3453 2891 -834 73 431 C ATOM 954 CG1 ILE A 125 -27.409 -17.825 25.896 1.00 26.75 C ANISOU 954 CG1 ILE A 125 3834 3348 2982 -761 24 425 C ATOM 955 CG2 ILE A 125 -29.210 -16.018 25.874 1.00 23.90 C ANISOU 955 CG2 ILE A 125 3258 3235 2585 -825 85 348 C ATOM 956 CD1 ILE A 125 -28.003 -18.864 24.926 1.00 26.24 C ANISOU 956 CD1 ILE A 125 3819 3192 2957 -838 16 395 C ATOM 957 N ALA A 126 -29.522 -15.623 29.417 1.00 24.08 N ANISOU 957 N ALA A 126 3312 3401 2438 -913 180 486 N ATOM 958 CA ALA A 126 -30.341 -14.633 30.117 1.00 25.93 C ANISOU 958 CA ALA A 126 3449 3779 2623 -938 244 457 C ATOM 959 C ALA A 126 -29.492 -13.712 30.997 1.00 26.82 C ANISOU 959 C ALA A 126 3576 3938 2678 -849 234 464 C ATOM 960 O ALA A 126 -29.706 -12.489 31.032 1.00 24.93 O ANISOU 960 O ALA A 126 3246 3794 2433 -796 254 402 O ATOM 961 CB ALA A 126 -31.408 -15.366 30.955 1.00 25.86 C ANISOU 961 CB ALA A 126 3456 3804 2564 -1086 316 505 C ATOM 962 N ILE A 127 -28.528 -14.280 31.731 1.00 25.84 N ANISOU 962 N ILE A 127 3565 3740 2511 -831 194 539 N ATOM 963 CA ILE A 127 -27.659 -13.455 32.565 1.00 24.08 C ANISOU 963 CA ILE A 127 3360 3557 2233 -754 168 545 C ATOM 964 C ILE A 127 -26.871 -12.487 31.702 1.00 22.69 C ANISOU 964 C ILE A 127 3117 3380 2122 -634 120 479 C ATOM 965 O ILE A 127 -26.730 -11.301 32.039 1.00 21.14 O ANISOU 965 O ILE A 127 2869 3262 1902 -583 126 434 O ATOM 966 CB ILE A 127 -26.719 -14.338 33.414 1.00 28.56 C ANISOU 966 CB ILE A 127 4063 4037 2752 -752 112 644 C ATOM 967 CG1 ILE A 127 -27.517 -15.099 34.476 1.00 31.63 C ANISOU 967 CG1 ILE A 127 4530 4443 3047 -880 168 717 C ATOM 968 CG2 ILE A 127 -25.608 -13.489 34.058 1.00 26.88 C ANISOU 968 CG2 ILE A 127 3860 3852 2501 -657 54 643 C ATOM 969 CD1 ILE A 127 -26.747 -16.252 35.125 1.00 34.44 C ANISOU 969 CD1 ILE A 127 5038 4680 3366 -894 104 831 C ATOM 970 N CYS A 128 -26.322 -12.983 30.587 1.00 20.67 N ANISOU 970 N CYS A 128 2871 3033 1950 -590 76 472 N ATOM 971 CA CYS A 128 -25.501 -12.142 29.728 1.00 21.02 C ANISOU 971 CA CYS A 128 2862 3073 2054 -485 39 419 C ATOM 972 C CYS A 128 -26.307 -10.999 29.114 1.00 20.50 C ANISOU 972 C CYS A 128 2689 3095 2004 -476 74 339 C ATOM 973 O CYS A 128 -25.760 -9.910 28.898 1.00 24.31 O ANISOU 973 O CYS A 128 3126 3607 2502 -402 55 299 O ATOM 974 CB CYS A 128 -24.847 -13.002 28.641 1.00 25.02 C ANISOU 974 CB CYS A 128 3405 3467 2635 -449 2 423 C ATOM 975 SG CYS A 128 -23.532 -14.073 29.300 1.00 30.30 S ANISOU 975 SG CYS A 128 4182 4021 3308 -405 -61 508 S ATOM 976 N TRP A 129 -27.594 -11.220 28.812 1.00 20.61 N ANISOU 976 N TRP A 129 2660 3149 2023 -551 119 316 N ATOM 977 CA TRP A 129 -28.432 -10.115 28.318 1.00 22.71 C ANISOU 977 CA TRP A 129 2818 3501 2308 -535 143 244 C ATOM 978 C TRP A 129 -28.676 -9.061 29.404 1.00 19.53 C ANISOU 978 C TRP A 129 2376 3193 1850 -518 179 223 C ATOM 979 O TRP A 129 -28.620 -7.855 29.133 1.00 18.68 O ANISOU 979 O TRP A 129 2211 3126 1761 -449 171 168 O ATOM 980 CB TRP A 129 -29.758 -10.657 27.772 1.00 22.90 C ANISOU 980 CB TRP A 129 2792 3550 2358 -621 173 226 C ATOM 981 CG TRP A 129 -29.662 -11.034 26.325 1.00 20.84 C ANISOU 981 CG TRP A 129 2535 3225 2158 -607 128 201 C ATOM 982 CD1 TRP A 129 -29.529 -12.291 25.810 1.00 20.35 C ANISOU 982 CD1 TRP A 129 2545 3069 2117 -655 109 227 C ATOM 983 CD2 TRP A 129 -29.666 -10.130 25.196 1.00 20.36 C ANISOU 983 CD2 TRP A 129 2416 3182 2136 -539 97 145 C ATOM 984 NE1 TRP A 129 -29.458 -12.229 24.421 1.00 22.34 N ANISOU 984 NE1 TRP A 129 2788 3289 2413 -623 71 182 N ATOM 985 CE2 TRP A 129 -29.539 -10.919 24.025 1.00 22.68 C ANISOU 985 CE2 TRP A 129 2754 3401 2463 -555 62 137 C ATOM 986 CE3 TRP A 129 -29.770 -8.731 25.068 1.00 18.33 C ANISOU 986 CE3 TRP A 129 2087 2992 1886 -469 92 101 C ATOM 987 CZ2 TRP A 129 -29.512 -10.357 22.739 1.00 25.84 C ANISOU 987 CZ2 TRP A 129 3129 3800 2890 -507 26 91 C ATOM 988 CZ3 TRP A 129 -29.748 -8.170 23.804 1.00 20.51 C ANISOU 988 CZ3 TRP A 129 2338 3259 2198 -420 52 63 C ATOM 989 CH2 TRP A 129 -29.614 -8.980 22.645 1.00 25.64 C ANISOU 989 CH2 TRP A 129 3034 3842 2867 -441 19 61 C ATOM 990 N VAL A 130 -28.913 -9.490 30.644 1.00 19.62 N ANISOU 990 N VAL A 130 2433 3235 1788 -580 219 264 N ATOM 991 CA VAL A 130 -29.036 -8.533 31.741 1.00 20.85 C ANISOU 991 CA VAL A 130 2572 3475 1874 -562 257 238 C ATOM 992 C VAL A 130 -27.741 -7.730 31.915 1.00 21.46 C ANISOU 992 C VAL A 130 2683 3525 1946 -470 194 230 C ATOM 993 O VAL A 130 -27.774 -6.504 32.090 1.00 23.41 O ANISOU 993 O VAL A 130 2884 3823 2187 -417 202 170 O ATOM 994 CB VAL A 130 -29.441 -9.261 33.043 1.00 23.82 C ANISOU 994 CB VAL A 130 3013 3884 2153 -656 312 294 C ATOM 995 CG1 VAL A 130 -29.490 -8.277 34.212 1.00 27.91 C ANISOU 995 CG1 VAL A 130 3532 4491 2583 -636 353 260 C ATOM 996 CG2 VAL A 130 -30.792 -9.938 32.882 1.00 22.43 C ANISOU 996 CG2 VAL A 130 2784 3747 1990 -760 384 296 C ATOM 997 N LEU A 131 -26.581 -8.398 31.880 1.00 21.31 N ANISOU 997 N LEU A 131 2741 3422 1936 -449 131 288 N ATOM 998 CA LEU A 131 -25.315 -7.676 32.041 1.00 21.00 C ANISOU 998 CA LEU A 131 2718 3361 1901 -370 67 281 C ATOM 999 C LEU A 131 -25.051 -6.717 30.877 1.00 22.40 C ANISOU 999 C LEU A 131 2822 3529 2159 -300 48 221 C ATOM 1000 O LEU A 131 -24.408 -5.676 31.069 1.00 20.63 O ANISOU 1000 O LEU A 131 2584 3318 1936 -248 19 189 O ATOM 1001 CB LEU A 131 -24.150 -8.659 32.172 1.00 18.87 C ANISOU 1001 CB LEU A 131 2525 3004 1640 -355 1 356 C ATOM 1002 CG LEU A 131 -24.161 -9.508 33.447 1.00 27.21 C ANISOU 1002 CG LEU A 131 3677 4057 2604 -414 -3 431 C ATOM 1003 CD1 LEU A 131 -23.080 -10.586 33.346 1.00 27.09 C ANISOU 1003 CD1 LEU A 131 3732 3937 2625 -385 -77 505 C ATOM 1004 CD2 LEU A 131 -24.004 -8.609 34.730 1.00 28.90 C ANISOU 1004 CD2 LEU A 131 3914 4349 2718 -412 -6 416 C ATOM 1005 N SER A 132 -25.481 -7.082 29.668 1.00 16.27 N ANISOU 1005 N SER A 132 2012 2723 1448 -304 56 208 N ATOM 1006 CA SER A 132 -25.338 -6.198 28.512 1.00 17.18 C ANISOU 1006 CA SER A 132 2071 2831 1625 -247 40 158 C ATOM 1007 C SER A 132 -26.144 -4.910 28.680 1.00 17.73 C ANISOU 1007 C SER A 132 2076 2972 1686 -228 67 96 C ATOM 1008 O SER A 132 -25.673 -3.831 28.300 1.00 19.22 O ANISOU 1008 O SER A 132 2244 3155 1903 -171 42 62 O ATOM 1009 CB SER A 132 -25.791 -6.936 27.245 1.00 15.72 C ANISOU 1009 CB SER A 132 1876 2607 1491 -267 43 157 C ATOM 1010 OG SER A 132 -24.959 -8.071 27.028 1.00 18.62 O ANISOU 1010 OG SER A 132 2307 2893 1875 -269 19 203 O ATOM 1011 N PHE A 133 -27.381 -5.014 29.196 1.00 17.16 N ANISOU 1011 N PHE A 133 1971 2966 1582 -275 121 79 N ATOM 1012 CA PHE A 133 -28.174 -3.816 29.493 1.00 20.78 C ANISOU 1012 CA PHE A 133 2365 3495 2036 -246 154 13 C ATOM 1013 C PHE A 133 -27.493 -2.963 30.557 1.00 20.99 C ANISOU 1013 C PHE A 133 2428 3535 2010 -212 147 -6 C ATOM 1014 O PHE A 133 -27.355 -1.744 30.389 1.00 20.39 O ANISOU 1014 O PHE A 133 2328 3460 1958 -152 131 -57 O ATOM 1015 CB PHE A 133 -29.600 -4.191 29.915 1.00 19.55 C ANISOU 1015 CB PHE A 133 2153 3414 1859 -306 224 -3 C ATOM 1016 CG PHE A 133 -30.545 -4.368 28.738 1.00 22.21 C ANISOU 1016 CG PHE A 133 2412 3760 2267 -316 219 -23 C ATOM 1017 CD1 PHE A 133 -31.253 -3.279 28.232 1.00 21.37 C ANISOU 1017 CD1 PHE A 133 2219 3692 2208 -257 216 -86 C ATOM 1018 CD2 PHE A 133 -30.712 -5.614 28.135 1.00 21.77 C ANISOU 1018 CD2 PHE A 133 2375 3666 2229 -382 209 19 C ATOM 1019 CE1 PHE A 133 -32.107 -3.420 27.132 1.00 24.25 C ANISOU 1019 CE1 PHE A 133 2512 4067 2634 -264 193 -101 C ATOM 1020 CE2 PHE A 133 -31.569 -5.779 27.027 1.00 24.13 C ANISOU 1020 CE2 PHE A 133 2607 3975 2587 -398 191 -3 C ATOM 1021 CZ PHE A 133 -32.270 -4.675 26.524 1.00 26.58 C ANISOU 1021 CZ PHE A 133 2825 4333 2941 -339 179 -62 C ATOM 1022 N ALA A 134 -27.024 -3.594 31.642 1.00 19.01 N ANISOU 1022 N ALA A 134 2248 3289 1685 -253 151 38 N ATOM 1023 CA ALA A 134 -26.351 -2.842 32.707 1.00 24.07 C ANISOU 1023 CA ALA A 134 2935 3947 2264 -230 133 19 C ATOM 1024 C ALA A 134 -25.102 -2.126 32.183 1.00 24.02 C ANISOU 1024 C ALA A 134 2936 3880 2309 -170 57 12 C ATOM 1025 O ALA A 134 -24.875 -0.955 32.505 1.00 24.12 O ANISOU 1025 O ALA A 134 2947 3903 2316 -133 44 -42 O ATOM 1026 CB ALA A 134 -25.986 -3.769 33.876 1.00 19.75 C ANISOU 1026 CB ALA A 134 2475 3408 1622 -287 132 82 C ATOM 1027 N ILE A 135 -24.285 -2.813 31.376 1.00 21.99 N ANISOU 1027 N ILE A 135 2689 3558 2108 -163 12 63 N ATOM 1028 CA ILE A 135 -23.066 -2.213 30.842 1.00 21.23 C ANISOU 1028 CA ILE A 135 2588 3411 2066 -116 -48 60 C ATOM 1029 C ILE A 135 -23.392 -1.142 29.799 1.00 19.17 C ANISOU 1029 C ILE A 135 2275 3141 1869 -76 -41 8 C ATOM 1030 O ILE A 135 -22.814 -0.047 29.809 1.00 16.87 O ANISOU 1030 O ILE A 135 1981 2834 1596 -45 -70 -23 O ATOM 1031 CB ILE A 135 -22.151 -3.301 30.246 1.00 22.29 C ANISOU 1031 CB ILE A 135 2740 3484 2245 -114 -84 122 C ATOM 1032 CG1 ILE A 135 -21.570 -4.196 31.349 1.00 21.87 C ANISOU 1032 CG1 ILE A 135 2748 3425 2136 -137 -117 181 C ATOM 1033 CG2 ILE A 135 -21.014 -2.677 29.440 1.00 17.92 C ANISOU 1033 CG2 ILE A 135 2158 2887 1762 -69 -124 114 C ATOM 1034 CD1 ILE A 135 -20.783 -5.392 30.789 1.00 21.80 C ANISOU 1034 CD1 ILE A 135 2757 3347 2180 -125 -149 240 C ATOM 1035 N GLY A 136 -24.277 -1.459 28.848 1.00 17.04 N ANISOU 1035 N GLY A 136 1969 2872 1633 -80 -11 4 N ATOM 1036 CA GLY A 136 -24.535 -0.519 27.763 1.00 16.51 C ANISOU 1036 CA GLY A 136 1863 2787 1621 -39 -19 -31 C ATOM 1037 C GLY A 136 -25.334 0.707 28.189 1.00 17.86 C ANISOU 1037 C GLY A 136 2007 2995 1785 -8 -2 -95 C ATOM 1038 O GLY A 136 -25.198 1.777 27.587 1.00 19.49 O ANISOU 1038 O GLY A 136 2203 3169 2032 34 -26 -122 O ATOM 1039 N LEU A 137 -26.206 0.567 29.191 1.00 15.58 N ANISOU 1039 N LEU A 137 1706 2768 1445 -28 44 -120 N ATOM 1040 CA LEU A 137 -26.987 1.694 29.704 1.00 17.17 C ANISOU 1040 CA LEU A 137 1879 3007 1640 11 72 -192 C ATOM 1041 C LEU A 137 -26.389 2.323 30.950 1.00 14.63 C ANISOU 1041 C LEU A 137 1610 2692 1257 14 69 -224 C ATOM 1042 O LEU A 137 -27.050 3.159 31.584 1.00 19.27 O ANISOU 1042 O LEU A 137 2185 3313 1823 44 104 -293 O ATOM 1043 CB LEU A 137 -28.424 1.261 29.997 1.00 19.27 C ANISOU 1043 CB LEU A 137 2084 3349 1890 -10 139 -215 C ATOM 1044 CG LEU A 137 -29.127 0.639 28.763 1.00 19.92 C ANISOU 1044 CG LEU A 137 2109 3429 2032 -22 131 -191 C ATOM 1045 CD1 LEU A 137 -30.593 0.343 29.070 1.00 17.68 C ANISOU 1045 CD1 LEU A 137 1742 3228 1747 -46 195 -222 C ATOM 1046 CD2 LEU A 137 -28.977 1.529 27.513 1.00 18.89 C ANISOU 1046 CD2 LEU A 137 1962 3242 1971 40 73 -204 C ATOM 1047 N THR A 138 -25.172 1.936 31.329 1.00 15.81 N ANISOU 1047 N THR A 138 1816 2812 1378 -13 25 -180 N ATOM 1048 CA THR A 138 -24.483 2.601 32.439 1.00 17.52 C ANISOU 1048 CA THR A 138 2088 3031 1539 -13 0 -211 C ATOM 1049 C THR A 138 -24.512 4.128 32.345 1.00 18.54 C ANISOU 1049 C THR A 138 2215 3129 1702 39 -15 -287 C ATOM 1050 O THR A 138 -24.666 4.775 33.394 1.00 21.95 O ANISOU 1050 O THR A 138 2683 3586 2073 44 0 -348 O ATOM 1051 CB THR A 138 -23.037 2.065 32.549 1.00 21.76 C ANISOU 1051 CB THR A 138 2665 3529 2073 -38 -70 -149 C ATOM 1052 OG1 THR A 138 -23.029 0.850 33.312 1.00 19.49 O ANISOU 1052 OG1 THR A 138 2414 3276 1716 -83 -60 -95 O ATOM 1053 CG2 THR A 138 -22.071 3.077 33.226 1.00 19.49 C ANISOU 1053 CG2 THR A 138 2417 3220 1768 -32 -128 -186 C ATOM 1054 N PRO A 139 -24.387 4.767 31.174 1.00 17.96 N ANISOU 1054 N PRO A 139 2112 2996 1714 75 -42 -288 N ATOM 1055 CA PRO A 139 -24.546 6.235 31.154 1.00 15.78 C ANISOU 1055 CA PRO A 139 1846 2679 1470 125 -55 -359 C ATOM 1056 C PRO A 139 -25.892 6.728 31.678 1.00 18.37 C ANISOU 1056 C PRO A 139 2148 3053 1779 169 7 -436 C ATOM 1057 O PRO A 139 -25.956 7.859 32.194 1.00 16.40 O ANISOU 1057 O PRO A 139 1929 2777 1525 207 4 -511 O ATOM 1058 CB PRO A 139 -24.350 6.588 29.678 1.00 17.77 C ANISOU 1058 CB PRO A 139 2075 2865 1811 149 -88 -325 C ATOM 1059 CG PRO A 139 -23.389 5.468 29.157 1.00 16.35 C ANISOU 1059 CG PRO A 139 1895 2679 1638 100 -110 -242 C ATOM 1060 CD PRO A 139 -23.856 4.243 29.890 1.00 14.42 C ANISOU 1060 CD PRO A 139 1643 2504 1331 68 -71 -222 C ATOM 1061 N AMET A 140 -26.966 5.922 31.560 0.64 16.89 N ANISOU 1061 N AMET A 140 1901 2933 1585 164 64 -425 N ATOM 1062 N BMET A 140 -26.963 5.934 31.568 0.36 17.03 N ANISOU 1062 N BMET A 140 1919 2950 1602 164 64 -426 N ATOM 1063 CA AMET A 140 -28.264 6.317 32.104 0.64 18.81 C ANISOU 1063 CA AMET A 140 2097 3235 1814 204 135 -501 C ATOM 1064 CA BMET A 140 -28.257 6.395 32.056 0.36 18.71 C ANISOU 1064 CA BMET A 140 2085 3218 1807 208 132 -503 C ATOM 1065 C AMET A 140 -28.237 6.412 33.621 0.64 21.58 C ANISOU 1065 C AMET A 140 2501 3639 2061 181 183 -554 C ATOM 1066 C BMET A 140 -28.314 6.483 33.572 0.36 21.56 C ANISOU 1066 C BMET A 140 2492 3635 2064 188 185 -559 C ATOM 1067 O AMET A 140 -29.141 7.019 34.206 0.64 24.32 O ANISOU 1067 O AMET A 140 2823 4027 2391 225 247 -639 O ATOM 1068 O BMET A 140 -29.238 7.110 34.100 0.36 24.11 O ANISOU 1068 O BMET A 140 2787 3998 2377 235 248 -644 O ATOM 1069 CB AMET A 140 -29.380 5.326 31.704 0.64 18.40 C ANISOU 1069 CB AMET A 140 1959 3255 1778 183 188 -473 C ATOM 1070 CB BMET A 140 -29.384 5.483 31.560 0.36 18.51 C ANISOU 1070 CB BMET A 140 1970 3258 1805 194 180 -477 C ATOM 1071 CG AMET A 140 -29.506 5.008 30.190 0.64 17.86 C ANISOU 1071 CG AMET A 140 1844 3148 1795 192 139 -419 C ATOM 1072 CG BMET A 140 -29.411 5.282 30.040 0.36 17.93 C ANISOU 1072 CG BMET A 140 1858 3138 1817 207 125 -424 C ATOM 1073 SD AMET A 140 -30.095 6.383 29.187 0.64 20.35 S ANISOU 1073 SD AMET A 140 2116 3406 2209 295 95 -466 S ATOM 1074 SD BMET A 140 -31.027 4.724 29.488 0.36 20.56 S ANISOU 1074 SD BMET A 140 2068 3547 2196 214 169 -433 S ATOM 1075 CE AMET A 140 -31.755 6.651 29.797 0.64 21.96 C ANISOU 1075 CE AMET A 140 2212 3703 2428 347 176 -552 C ATOM 1076 CE BMET A 140 -32.017 6.198 29.738 0.36 21.95 C ANISOU 1076 CE BMET A 140 2184 3731 2423 325 190 -538 C ATOM 1077 N ALEU A 141 -27.242 5.804 34.277 0.64 21.61 N ANISOU 1077 N ALEU A 141 2576 3645 1989 117 154 -507 N ATOM 1078 N BLEU A 141 -27.366 5.870 34.285 0.36 22.02 N ANISOU 1078 N BLEU A 141 2623 3701 2043 123 161 -515 N ATOM 1079 CA ALEU A 141 -27.140 5.875 35.734 0.64 23.25 C ANISOU 1079 CA ALEU A 141 2853 3903 2077 88 188 -551 C ATOM 1080 CA BLEU A 141 -27.341 5.986 35.740 0.36 23.28 C ANISOU 1080 CA BLEU A 141 2848 3912 2085 98 200 -564 C ATOM 1081 C ALEU A 141 -26.445 7.139 36.223 0.64 24.38 C ANISOU 1081 C ALEU A 141 3066 3990 2207 119 138 -624 C ATOM 1082 C BLEU A 141 -26.711 7.289 36.213 0.36 24.19 C ANISOU 1082 C BLEU A 141 3031 3971 2190 133 154 -642 C ATOM 1083 O ALEU A 141 -26.257 7.287 37.442 0.64 25.48 O ANISOU 1083 O ALEU A 141 3279 4166 2238 93 153 -668 O ATOM 1084 O BLEU A 141 -26.811 7.607 37.406 0.36 25.36 O ANISOU 1084 O BLEU A 141 3239 4160 2237 124 190 -708 O ATOM 1085 CB ALEU A 141 -26.418 4.640 36.274 0.64 21.58 C ANISOU 1085 CB ALEU A 141 2695 3718 1785 8 164 -462 C ATOM 1086 CB BLEU A 141 -26.608 4.794 36.370 0.36 21.70 C ANISOU 1086 CB BLEU A 141 2707 3742 1796 15 179 -481 C ATOM 1087 CG ALEU A 141 -26.920 3.303 35.705 0.64 21.65 C ANISOU 1087 CG ALEU A 141 2653 3758 1817 -33 197 -380 C ATOM 1088 CG BLEU A 141 -27.376 3.467 36.515 0.36 22.31 C ANISOU 1088 CG BLEU A 141 2755 3891 1833 -41 248 -422 C ATOM 1089 CD1ALEU A 141 -26.135 2.127 36.314 0.64 20.20 C ANISOU 1089 CD1ALEU A 141 2539 3581 1555 -104 164 -291 C ATOM 1090 CD1BLEU A 141 -27.889 2.921 35.169 0.36 21.29 C ANISOU 1090 CD1BLEU A 141 2535 3742 1813 -32 250 -376 C ATOM 1091 CD2ALEU A 141 -28.440 3.124 35.948 0.64 21.32 C ANISOU 1091 CD2ALEU A 141 2545 3800 1757 -36 310 -422 C ATOM 1092 CD2BLEU A 141 -26.528 2.406 37.241 0.36 19.59 C ANISOU 1092 CD2BLEU A 141 2494 3555 1396 -114 210 -337 C ATOM 1093 N GLY A 142 -26.084 8.053 35.319 1.00 19.51 N ANISOU 1093 N GLY A 142 2436 3283 1692 166 80 -638 N ATOM 1094 CA GLY A 142 -25.538 9.342 35.713 1.00 20.90 C ANISOU 1094 CA GLY A 142 2678 3393 1870 192 36 -715 C ATOM 1095 C GLY A 142 -24.204 9.697 35.076 1.00 24.47 C ANISOU 1095 C GLY A 142 3159 3754 2385 166 -66 -666 C ATOM 1096 O GLY A 142 -23.748 10.845 35.152 1.00 25.75 O ANISOU 1096 O GLY A 142 3369 3840 2575 182 -112 -723 O ATOM 1097 N TRP A 143 -23.543 8.714 34.470 1.00 21.58 N ANISOU 1097 N TRP A 143 2764 3392 2041 122 -100 -565 N ATOM 1098 CA TRP A 143 -22.285 8.964 33.779 1.00 19.81 C ANISOU 1098 CA TRP A 143 2547 3095 1885 95 -181 -516 C ATOM 1099 C TRP A 143 -22.605 9.481 32.373 1.00 17.44 C ANISOU 1099 C TRP A 143 2204 2730 1691 138 -180 -499 C ATOM 1100 O TRP A 143 -22.501 8.777 31.375 1.00 16.90 O ANISOU 1100 O TRP A 143 2091 2662 1668 130 -179 -425 O ATOM 1101 CB TRP A 143 -21.433 7.705 33.739 1.00 16.79 C ANISOU 1101 CB TRP A 143 2149 2745 1486 41 -211 -423 C ATOM 1102 CG TRP A 143 -19.958 7.953 33.357 1.00 21.60 C ANISOU 1102 CG TRP A 143 2759 3297 2152 5 -293 -384 C ATOM 1103 CD1 TRP A 143 -19.353 9.166 32.994 1.00 21.05 C ANISOU 1103 CD1 TRP A 143 2704 3149 2144 2 -337 -417 C ATOM 1104 CD2 TRP A 143 -18.915 6.972 33.336 1.00 17.03 C ANISOU 1104 CD2 TRP A 143 2159 2735 1578 -34 -337 -308 C ATOM 1105 NE1 TRP A 143 -18.006 8.952 32.727 1.00 16.10 N ANISOU 1105 NE1 TRP A 143 2055 2501 1561 -46 -399 -363 N ATOM 1106 CE2 TRP A 143 -17.721 7.623 32.930 1.00 17.65 C ANISOU 1106 CE2 TRP A 143 2224 2757 1727 -60 -401 -299 C ATOM 1107 CE3 TRP A 143 -18.882 5.600 33.590 1.00 18.10 C ANISOU 1107 CE3 TRP A 143 2284 2921 1672 -47 -329 -244 C ATOM 1108 CZ2 TRP A 143 -16.508 6.933 32.780 1.00 20.55 C ANISOU 1108 CZ2 TRP A 143 2550 3128 2128 -91 -452 -235 C ATOM 1109 CZ3 TRP A 143 -17.678 4.918 33.455 1.00 19.58 C ANISOU 1109 CZ3 TRP A 143 2446 3100 1892 -70 -388 -179 C ATOM 1110 CH2 TRP A 143 -16.506 5.588 33.053 1.00 19.27 C ANISOU 1110 CH2 TRP A 143 2377 3015 1929 -88 -447 -177 C ATOM 1111 N ASN A 144 -23.020 10.739 32.308 1.00 16.88 N ANISOU 1111 N ASN A 144 2159 2599 1657 187 -182 -570 N ATOM 1112 CA ASN A 144 -23.456 11.289 31.025 1.00 19.69 C ANISOU 1112 CA ASN A 144 2486 2890 2103 235 -188 -552 C ATOM 1113 C ASN A 144 -23.171 12.785 31.010 1.00 17.34 C ANISOU 1113 C ASN A 144 2250 2486 1852 259 -231 -609 C ATOM 1114 O ASN A 144 -22.790 13.369 32.018 1.00 18.06 O ANISOU 1114 O ASN A 144 2400 2560 1903 243 -248 -676 O ATOM 1115 CB ASN A 144 -24.945 10.994 30.747 1.00 17.61 C ANISOU 1115 CB ASN A 144 2162 2681 1850 299 -128 -570 C ATOM 1116 CG ASN A 144 -25.879 11.555 31.823 1.00 19.54 C ANISOU 1116 CG ASN A 144 2414 2958 2054 352 -77 -677 C ATOM 1117 OD1 ASN A 144 -25.996 12.758 31.994 1.00 24.31 O ANISOU 1117 OD1 ASN A 144 3059 3489 2687 403 -93 -748 O ATOM 1118 ND2 ASN A 144 -26.551 10.675 32.535 1.00 17.95 N ANISOU 1118 ND2 ASN A 144 2174 2861 1784 339 -9 -688 N ATOM 1119 N ASN A 145 -23.353 13.410 29.849 1.00 20.50 N ANISOU 1119 N ASN A 145 2648 2807 2332 294 -253 -581 N ATOM 1120 CA ASN A 145 -23.133 14.853 29.720 1.00 22.58 C ANISOU 1120 CA ASN A 145 2981 2949 2649 317 -297 -625 C ATOM 1121 C ASN A 145 -24.424 15.669 29.791 1.00 25.62 C ANISOU 1121 C ASN A 145 3370 3300 3064 426 -276 -703 C ATOM 1122 O ASN A 145 -24.422 16.828 29.355 1.00 27.48 O ANISOU 1122 O ASN A 145 3661 3416 3363 463 -317 -722 O ATOM 1123 CB ASN A 145 -22.431 15.192 28.399 1.00 23.60 C ANISOU 1123 CB ASN A 145 3127 2993 2847 284 -340 -541 C ATOM 1124 CG ASN A 145 -21.065 14.555 28.267 1.00 29.44 C ANISOU 1124 CG ASN A 145 3854 3756 3576 183 -358 -473 C ATOM 1125 OD1 ASN A 145 -20.345 14.400 29.239 1.00 28.64 O ANISOU 1125 OD1 ASN A 145 3763 3683 3434 133 -373 -500 O ATOM 1126 ND2 ASN A 145 -20.707 14.174 27.037 1.00 33.61 N ANISOU 1126 ND2 ASN A 145 4358 4274 4137 158 -358 -384 N ATOM 1127 N CYS A 146 -25.525 15.098 30.307 1.00 24.66 N ANISOU 1127 N CYS A 146 3187 3277 2907 478 -212 -747 N ATOM 1128 CA CYS A 146 -26.783 15.848 30.337 1.00 26.41 C ANISOU 1128 CA CYS A 146 3388 3475 3172 592 -188 -824 C ATOM 1129 C CYS A 146 -26.777 16.976 31.366 1.00 31.93 C ANISOU 1129 C CYS A 146 4165 4108 3859 631 -185 -944 C ATOM 1130 O CYS A 146 -27.595 17.897 31.255 1.00 32.50 O ANISOU 1130 O CYS A 146 4242 4114 3991 735 -184 -1010 O ATOM 1131 CB CYS A 146 -27.967 14.919 30.604 1.00 28.81 C ANISOU 1131 CB CYS A 146 3589 3912 3447 628 -111 -840 C ATOM 1132 SG CYS A 146 -28.327 13.796 29.203 1.00 30.16 S ANISOU 1132 SG CYS A 146 3669 4136 3654 608 -125 -720 S ATOM 1133 N GLY A 147 -25.892 16.928 32.359 1.00 31.75 N ANISOU 1133 N GLY A 147 4205 4097 3760 555 -189 -976 N ATOM 1134 CA GLY A 147 -25.727 18.072 33.249 1.00 29.64 C ANISOU 1134 CA GLY A 147 4034 3750 3480 578 -202 -1092 C ATOM 1135 C GLY A 147 -25.040 19.271 32.615 1.00 29.85 C ANISOU 1135 C GLY A 147 4144 3606 3590 572 -286 -1083 C ATOM 1136 O GLY A 147 -25.101 20.367 33.176 1.00 34.93 O ANISOU 1136 O GLY A 147 4872 4155 4246 612 -300 -1185 O ATOM 1137 N GLN A 148 -24.404 19.101 31.464 1.00 28.29 N ANISOU 1137 N GLN A 148 3935 3367 3448 521 -336 -966 N ATOM 1138 CA GLN A 148 -23.707 20.189 30.778 1.00 34.54 C ANISOU 1138 CA GLN A 148 4809 3999 4317 496 -410 -940 C ATOM 1139 C GLN A 148 -24.179 20.278 29.335 1.00 34.40 C ANISOU 1139 C GLN A 148 4761 3931 4377 545 -429 -849 C ATOM 1140 O GLN A 148 -23.412 20.029 28.401 1.00 35.05 O ANISOU 1140 O GLN A 148 4843 3993 4480 470 -460 -742 O ATOM 1141 CB GLN A 148 -22.198 19.984 30.852 1.00 43.17 C ANISOU 1141 CB GLN A 148 5930 5085 5389 356 -455 -884 C ATOM 1142 CG GLN A 148 -21.661 20.096 32.261 1.00 56.26 C ANISOU 1142 CG GLN A 148 7636 6769 6971 304 -464 -977 C ATOM 1143 CD GLN A 148 -20.239 19.604 32.376 1.00 70.31 C ANISOU 1143 CD GLN A 148 9406 8581 8728 171 -511 -914 C ATOM 1144 OE1 GLN A 148 -19.807 18.726 31.614 1.00 74.84 O ANISOU 1144 OE1 GLN A 148 9907 9214 9317 129 -505 -806 O ATOM 1145 NE2 GLN A 148 -19.491 20.167 33.330 1.00 75.54 N ANISOU 1145 NE2 GLN A 148 10139 9205 9357 107 -561 -986 N ATOM 1146 N PRO A 149 -25.450 20.618 29.116 1.00 34.35 N ANISOU 1146 N PRO A 149 4727 3911 4413 672 -412 -889 N ATOM 1147 CA PRO A 149 -25.962 20.652 27.744 1.00 32.18 C ANISOU 1147 CA PRO A 149 4424 3598 4203 723 -445 -799 C ATOM 1148 C PRO A 149 -25.303 21.761 26.930 1.00 36.13 C ANISOU 1148 C PRO A 149 5036 3924 4768 697 -521 -746 C ATOM 1149 O PRO A 149 -24.904 22.807 27.454 1.00 36.11 O ANISOU 1149 O PRO A 149 5130 3799 4790 691 -550 -811 O ATOM 1150 CB PRO A 149 -27.464 20.908 27.935 1.00 34.80 C ANISOU 1150 CB PRO A 149 4699 3950 4573 874 -418 -877 C ATOM 1151 CG PRO A 149 -27.556 21.672 29.240 1.00 34.96 C ANISOU 1151 CG PRO A 149 4775 3929 4578 914 -389 -1019 C ATOM 1152 CD PRO A 149 -26.450 21.095 30.100 1.00 34.24 C ANISOU 1152 CD PRO A 149 4711 3905 4394 781 -368 -1025 C ATOM 1153 N LYS A 150 -25.191 21.518 25.625 1.00 35.16 N ANISOU 1153 N LYS A 150 4906 3786 4667 674 -551 -627 N ATOM 1154 CA LYS A 150 -24.691 22.521 24.687 1.00 34.37 C ANISOU 1154 CA LYS A 150 4913 3523 4622 649 -618 -557 C ATOM 1155 C LYS A 150 -25.841 23.457 24.343 1.00 35.48 C ANISOU 1155 C LYS A 150 5088 3557 4835 797 -665 -587 C ATOM 1156 O LYS A 150 -26.596 23.258 23.383 1.00 33.64 O ANISOU 1156 O LYS A 150 4820 3339 4623 865 -693 -522 O ATOM 1157 CB LYS A 150 -24.084 21.860 23.458 1.00 35.05 C ANISOU 1157 CB LYS A 150 4987 3644 4685 561 -623 -420 C ATOM 1158 CG LYS A 150 -22.814 21.124 23.807 1.00 37.31 C ANISOU 1158 CG LYS A 150 5246 4009 4922 422 -585 -396 C ATOM 1159 CD LYS A 150 -22.000 20.794 22.600 1.00 40.47 C ANISOU 1159 CD LYS A 150 5659 4405 5312 327 -585 -272 C ATOM 1160 CE LYS A 150 -20.720 20.093 23.017 1.00 43.33 C ANISOU 1160 CE LYS A 150 5978 4844 5641 202 -547 -259 C ATOM 1161 NZ LYS A 150 -19.989 19.594 21.828 1.00 46.16 N ANISOU 1161 NZ LYS A 150 6328 5225 5986 120 -526 -147 N ATOM 1162 N GLU A 151 -25.951 24.513 25.145 1.00 40.51 N ANISOU 1162 N GLU A 151 5800 4080 5513 851 -681 -690 N ATOM 1163 CA GLU A 151 -27.108 25.396 25.078 1.00 46.78 C ANISOU 1163 CA GLU A 151 6614 4776 6383 1016 -717 -748 C ATOM 1164 C GLU A 151 -27.101 26.266 23.829 1.00 46.10 C ANISOU 1164 C GLU A 151 6630 4523 6363 1040 -808 -645 C ATOM 1165 O GLU A 151 -28.170 26.590 23.299 1.00 46.81 O ANISOU 1165 O GLU A 151 6700 4574 6511 1179 -853 -637 O ATOM 1166 CB GLU A 151 -27.153 26.265 26.331 1.00 55.47 C ANISOU 1166 CB GLU A 151 7778 5794 7503 1064 -701 -899 C ATOM 1167 CG GLU A 151 -28.530 26.376 26.919 1.00 61.82 C ANISOU 1167 CG GLU A 151 8505 6642 8341 1237 -664 -1016 C ATOM 1168 CD GLU A 151 -28.972 25.104 27.586 1.00 60.69 C ANISOU 1168 CD GLU A 151 8215 6721 8122 1228 -570 -1056 C ATOM 1169 OE1 GLU A 151 -29.664 24.292 26.937 1.00 62.33 O ANISOU 1169 OE1 GLU A 151 8309 7042 8333 1262 -560 -992 O ATOM 1170 OE2 GLU A 151 -28.626 24.923 28.764 1.00 61.05 O ANISOU 1170 OE2 GLU A 151 8269 6826 8101 1180 -509 -1150 O ATOM 1171 N GLY A 152 -25.925 26.673 23.353 1.00 44.47 N ANISOU 1171 N GLY A 152 6533 4216 6150 907 -840 -563 N ATOM 1172 CA GLY A 152 -25.875 27.425 22.110 1.00 44.74 C ANISOU 1172 CA GLY A 152 6675 4097 6228 911 -920 -447 C ATOM 1173 C GLY A 152 -26.385 26.622 20.932 1.00 43.33 C ANISOU 1173 C GLY A 152 6428 4017 6019 933 -935 -334 C ATOM 1174 O GLY A 152 -27.163 27.120 20.112 1.00 46.58 O ANISOU 1174 O GLY A 152 6878 4346 6475 1037 -1010 -281 O ATOM 1175 N LYS A 153 -25.967 25.360 20.843 1.00 39.41 N ANISOU 1175 N LYS A 153 5833 3694 5445 839 -872 -297 N ATOM 1176 CA LYS A 153 -26.455 24.490 19.783 1.00 36.21 C ANISOU 1176 CA LYS A 153 5363 3394 5002 853 -881 -204 C ATOM 1177 C LYS A 153 -27.957 24.241 19.927 1.00 36.25 C ANISOU 1177 C LYS A 153 5261 3470 5042 1017 -900 -264 C ATOM 1178 O LYS A 153 -28.702 24.275 18.937 1.00 36.85 O ANISOU 1178 O LYS A 153 5334 3532 5133 1089 -968 -195 O ATOM 1179 CB LYS A 153 -25.670 23.178 19.809 1.00 32.08 C ANISOU 1179 CB LYS A 153 4759 3034 4396 724 -803 -172 C ATOM 1180 CG LYS A 153 -25.885 22.281 18.628 1.00 33.90 C ANISOU 1180 CG LYS A 153 4950 3354 4574 703 -808 -71 C ATOM 1181 CD LYS A 153 -25.115 20.970 18.779 1.00 38.06 C ANISOU 1181 CD LYS A 153 5397 4033 5030 589 -725 -58 C ATOM 1182 CE LYS A 153 -23.615 21.181 18.948 1.00 43.70 C ANISOU 1182 CE LYS A 153 6170 4704 5731 448 -688 -32 C ATOM 1183 NZ LYS A 153 -22.858 19.912 18.624 1.00 46.01 N ANISOU 1183 NZ LYS A 153 6396 5128 5959 347 -622 16 N ATOM 1184 N ALA A 154 -28.419 24.007 21.157 1.00 34.41 N ANISOU 1184 N ALA A 154 4938 3315 4821 1073 -841 -393 N ATOM 1185 CA ALA A 154 -29.841 23.766 21.385 1.00 36.89 C ANISOU 1185 CA ALA A 154 5131 3711 5176 1222 -842 -460 C ATOM 1186 C ALA A 154 -30.676 24.993 21.020 1.00 37.29 C ANISOU 1186 C ALA A 154 5238 3604 5325 1378 -934 -473 C ATOM 1187 O ALA A 154 -31.726 24.871 20.373 1.00 36.21 O ANISOU 1187 O ALA A 154 5030 3500 5228 1486 -990 -446 O ATOM 1188 CB ALA A 154 -30.076 23.360 22.846 1.00 35.62 C ANISOU 1188 CB ALA A 154 4879 3658 4998 1239 -746 -598 C ATOM 1189 N HIS A 155 -30.220 26.189 21.412 1.00 37.89 N ANISOU 1189 N HIS A 155 5445 3503 5448 1392 -960 -513 N ATOM 1190 CA HIS A 155 -30.961 27.408 21.073 1.00 39.37 C ANISOU 1190 CA HIS A 155 5705 3517 5738 1546 -1054 -524 C ATOM 1191 C HIS A 155 -30.948 27.669 19.576 1.00 38.56 C ANISOU 1191 C HIS A 155 5686 3325 5639 1539 -1163 -365 C ATOM 1192 O HIS A 155 -31.966 28.066 19.002 1.00 41.58 O ANISOU 1192 O HIS A 155 6051 3659 6089 1686 -1251 -344 O ATOM 1193 CB HIS A 155 -30.380 28.613 21.806 1.00 42.57 C ANISOU 1193 CB HIS A 155 6253 3735 6188 1545 -1059 -600 C ATOM 1194 CG HIS A 155 -30.594 28.585 23.283 1.00 54.56 C ANISOU 1194 CG HIS A 155 7708 5314 7706 1588 -969 -773 C ATOM 1195 ND1 HIS A 155 -31.814 28.292 23.852 1.00 60.04 N ANISOU 1195 ND1 HIS A 155 8259 6117 8436 1736 -924 -879 N ATOM 1196 CD2 HIS A 155 -29.752 28.839 24.311 1.00 58.97 C ANISOU 1196 CD2 HIS A 155 8335 5841 8230 1499 -914 -859 C ATOM 1197 CE1 HIS A 155 -31.711 28.353 25.168 1.00 61.43 C ANISOU 1197 CE1 HIS A 155 8424 6329 8588 1735 -837 -1023 C ATOM 1198 NE2 HIS A 155 -30.469 28.685 25.473 1.00 59.44 N ANISOU 1198 NE2 HIS A 155 8303 5991 8290 1594 -837 -1014 N ATOM 1199 N ASER A 156 -29.800 27.468 18.925 0.55 39.10 N ANISOU 1199 N ASER A 156 5849 3373 5633 1371 -1159 -251 N ATOM 1200 N BSER A 156 -29.802 27.448 18.927 0.45 39.13 N ANISOU 1200 N BSER A 156 5851 3381 5637 1370 -1158 -252 N ATOM 1201 CA ASER A 156 -29.724 27.706 17.488 0.55 41.66 C ANISOU 1201 CA ASER A 156 6272 3618 5939 1348 -1252 -96 C ATOM 1202 CA BSER A 156 -29.694 27.687 17.491 0.45 41.61 C ANISOU 1202 CA BSER A 156 6266 3614 5931 1343 -1249 -95 C ATOM 1203 C ASER A 156 -30.699 26.820 16.722 0.55 43.92 C ANISOU 1203 C ASER A 156 6438 4048 6201 1416 -1289 -48 C ATOM 1204 C BSER A 156 -30.631 26.787 16.693 0.45 43.90 C ANISOU 1204 C BSER A 156 6440 4049 6193 1405 -1286 -42 C ATOM 1205 O ASER A 156 -31.207 27.221 15.671 0.55 46.34 O ANISOU 1205 O ASER A 156 6806 4279 6522 1482 -1400 47 O ATOM 1206 O BSER A 156 -31.033 27.143 15.580 0.45 46.19 O ANISOU 1206 O BSER A 156 6798 4265 6487 1453 -1393 63 O ATOM 1207 CB ASER A 156 -28.293 27.483 16.988 0.55 39.54 C ANISOU 1207 CB ASER A 156 6100 3339 5585 1143 -1211 6 C ATOM 1208 CB BSER A 156 -28.245 27.486 17.041 0.45 39.52 C ANISOU 1208 CB BSER A 156 6098 3336 5582 1137 -1206 2 C ATOM 1209 OG ASER A 156 -27.999 26.101 16.880 0.55 37.27 O ANISOU 1209 OG ASER A 156 5697 3254 5210 1048 -1133 25 O ATOM 1210 OG BSER A 156 -28.126 27.584 15.635 0.45 39.24 O ANISOU 1210 OG BSER A 156 6158 3248 5503 1097 -1276 155 O ATOM 1211 N GLN A 157 -30.977 25.621 17.229 1.00 44.18 N ANISOU 1211 N GLN A 157 6307 4284 6194 1396 -1206 -109 N ATOM 1212 CA GLN A 157 -31.941 24.728 16.600 1.00 41.12 C ANISOU 1212 CA GLN A 157 5794 4040 5789 1450 -1240 -79 C ATOM 1213 C GLN A 157 -33.351 24.918 17.125 1.00 39.46 C ANISOU 1213 C GLN A 157 5449 3865 5678 1636 -1269 -181 C ATOM 1214 O GLN A 157 -34.235 24.151 16.741 1.00 40.67 O ANISOU 1214 O GLN A 157 5471 4151 5831 1682 -1294 -173 O ATOM 1215 CB GLN A 157 -31.551 23.275 16.815 1.00 43.33 C ANISOU 1215 CB GLN A 157 5967 4516 5979 1327 -1138 -87 C ATOM 1216 CG GLN A 157 -30.263 22.879 16.183 1.00 52.27 C ANISOU 1216 CG GLN A 157 7197 5647 7017 1155 -1104 12 C ATOM 1217 CD GLN A 157 -30.123 21.395 16.170 1.00 56.28 C ANISOU 1217 CD GLN A 157 7595 6342 7447 1067 -1028 13 C ATOM 1218 OE1 GLN A 157 -31.090 20.679 16.455 1.00 57.65 O ANISOU 1218 OE1 GLN A 157 7628 6639 7635 1132 -1019 -42 O ATOM 1219 NE2 GLN A 157 -28.927 20.906 15.847 1.00 57.78 N ANISOU 1219 NE2 GLN A 157 7842 6553 7559 919 -971 74 N ATOM 1220 N GLY A 158 -33.573 25.875 18.019 1.00 37.16 N ANISOU 1220 N GLY A 158 5179 3467 5473 1738 -1259 -285 N ATOM 1221 CA GLY A 158 -34.895 26.072 18.581 1.00 41.68 C ANISOU 1221 CA GLY A 158 5605 4104 6129 1882 -1242 -388 C ATOM 1222 C GLY A 158 -35.370 24.990 19.530 1.00 44.61 C ANISOU 1222 C GLY A 158 5790 4670 6489 1896 -1138 -499 C ATOM 1223 O GLY A 158 -36.576 24.799 19.671 1.00 48.26 O ANISOU 1223 O GLY A 158 6098 5239 7000 1978 -1122 -546 O ATOM 1224 N CYS A 159 -34.463 24.280 20.200 1.00 41.67 N ANISOU 1224 N CYS A 159 5425 4376 6032 1760 -1034 -525 N ATOM 1225 CA CYS A 159 -34.924 23.280 21.153 1.00 40.10 C ANISOU 1225 CA CYS A 159 5062 4369 5807 1746 -918 -620 C ATOM 1226 C CYS A 159 -35.618 23.948 22.348 1.00 42.62 C ANISOU 1226 C CYS A 159 5323 4669 6201 1881 -860 -778 C ATOM 1227 O CYS A 159 -35.504 25.155 22.575 1.00 45.05 O ANISOU 1227 O CYS A 159 5739 4810 6568 1959 -894 -821 O ATOM 1228 CB CYS A 159 -33.759 22.394 21.600 1.00 33.39 C ANISOU 1228 CB CYS A 159 4243 3601 4842 1562 -825 -601 C ATOM 1229 SG CYS A 159 -32.950 21.509 20.189 1.00 33.78 S ANISOU 1229 SG CYS A 159 4348 3685 4802 1409 -872 -431 S ATOM 1230 N GLY A 160 -36.386 23.152 23.095 1.00 41.26 N ANISOU 1230 N GLY A 160 4982 4672 6024 1905 -764 -864 N ATOM 1231 CA GLY A 160 -37.090 23.631 24.263 1.00 41.13 C ANISOU 1231 CA GLY A 160 4898 4679 6051 1997 -673 -1008 C ATOM 1232 C GLY A 160 -36.366 23.268 25.548 1.00 43.90 C ANISOU 1232 C GLY A 160 5279 5086 6316 1917 -551 -1104 C ATOM 1233 O GLY A 160 -35.263 22.719 25.542 1.00 43.30 O ANISOU 1233 O GLY A 160 5283 5026 6142 1757 -535 -1038 O ATOM 1234 N GLU A 161 -37.019 23.564 26.672 1.00 44.72 N ANISOU 1234 N GLU A 161 5321 5237 6434 1981 -449 -1235 N ATOM 1235 CA GLU A 161 -36.387 23.347 27.966 1.00 48.05 C ANISOU 1235 CA GLU A 161 5789 5705 6765 1917 -338 -1339 C ATOM 1236 C GLU A 161 -36.095 21.870 28.209 1.00 46.35 C ANISOU 1236 C GLU A 161 5497 5676 6438 1767 -263 -1291 C ATOM 1237 O GLU A 161 -36.915 20.992 27.917 1.00 48.18 O ANISOU 1237 O GLU A 161 5574 6051 6681 1772 -236 -1264 O ATOM 1238 CB GLU A 161 -37.261 23.914 29.080 1.00 61.08 C ANISOU 1238 CB GLU A 161 7389 7386 8434 1990 -232 -1465 C ATOM 1239 CG GLU A 161 -37.282 25.443 29.079 1.00 74.26 C ANISOU 1239 CG GLU A 161 9179 8855 10182 2083 -287 -1503 C ATOM 1240 CD GLU A 161 -37.969 26.044 30.301 1.00 84.79 C ANISOU 1240 CD GLU A 161 10490 10206 11521 2151 -172 -1641 C ATOM 1241 OE1 GLU A 161 -39.142 25.683 30.579 1.00 87.91 O ANISOU 1241 OE1 GLU A 161 10723 10733 11946 2206 -91 -1675 O ATOM 1242 OE2 GLU A 161 -37.327 26.878 30.983 1.00 87.60 O ANISOU 1242 OE2 GLU A 161 10992 10440 11851 2143 -160 -1715 O ATOM 1243 N GLY A 162 -34.904 21.601 28.747 1.00 42.79 N ANISOU 1243 N GLY A 162 5159 5219 5881 1626 -234 -1275 N ATOM 1244 CA GLY A 162 -34.437 20.251 28.974 1.00 39.01 C ANISOU 1244 CA GLY A 162 4640 4889 5295 1476 -176 -1215 C ATOM 1245 C GLY A 162 -34.019 19.503 27.733 1.00 39.16 C ANISOU 1245 C GLY A 162 4650 4922 5306 1388 -251 -1062 C ATOM 1246 O GLY A 162 -33.571 18.345 27.846 1.00 41.03 O ANISOU 1246 O GLY A 162 4862 5269 5460 1265 -209 -1007 O ATOM 1247 N GLN A 163 -34.154 20.109 26.553 1.00 34.53 N ANISOU 1247 N GLN A 163 4094 4226 4800 1449 -359 -992 N ATOM 1248 CA GLN A 163 -33.814 19.450 25.298 1.00 32.35 C ANISOU 1248 CA GLN A 163 3820 3962 4510 1372 -429 -853 C ATOM 1249 C GLN A 163 -32.413 19.844 24.840 1.00 31.69 C ANISOU 1249 C GLN A 163 3896 3753 4391 1273 -484 -773 C ATOM 1250 O GLN A 163 -31.904 20.915 25.177 1.00 33.06 O ANISOU 1250 O GLN A 163 4182 3792 4588 1294 -506 -813 O ATOM 1251 CB GLN A 163 -34.822 19.784 24.195 1.00 31.79 C ANISOU 1251 CB GLN A 163 3686 3859 4531 1487 -522 -811 C ATOM 1252 CG GLN A 163 -36.213 19.247 24.433 1.00 32.67 C ANISOU 1252 CG GLN A 163 3611 4113 4689 1568 -479 -871 C ATOM 1253 CD GLN A 163 -37.111 19.408 23.209 1.00 37.79 C ANISOU 1253 CD GLN A 163 4192 4745 5422 1661 -594 -809 C ATOM 1254 OE1 GLN A 163 -36.925 20.316 22.399 1.00 38.10 O ANISOU 1254 OE1 GLN A 163 4331 4637 5507 1720 -704 -755 O ATOM 1255 NE2 GLN A 163 -38.091 18.520 23.071 1.00 40.61 N ANISOU 1255 NE2 GLN A 163 4380 5253 5797 1668 -574 -815 N ATOM 1256 N VAL A 164 -31.800 18.952 24.063 1.00 25.72 N ANISOU 1256 N VAL A 164 3146 3045 3581 1161 -500 -663 N ATOM 1257 CA VAL A 164 -30.518 19.171 23.410 1.00 26.42 C ANISOU 1257 CA VAL A 164 3360 3038 3639 1060 -545 -572 C ATOM 1258 C VAL A 164 -30.660 18.760 21.949 1.00 27.11 C ANISOU 1258 C VAL A 164 3443 3130 3726 1043 -611 -455 C ATOM 1259 O VAL A 164 -31.573 18.019 21.573 1.00 26.34 O ANISOU 1259 O VAL A 164 3240 3135 3633 1077 -614 -445 O ATOM 1260 CB VAL A 164 -29.382 18.353 24.060 1.00 27.04 C ANISOU 1260 CB VAL A 164 3455 3186 3634 921 -479 -564 C ATOM 1261 CG1 VAL A 164 -29.114 18.807 25.480 1.00 30.62 C ANISOU 1261 CG1 VAL A 164 3937 3627 4069 924 -428 -674 C ATOM 1262 CG2 VAL A 164 -29.747 16.860 24.030 1.00 27.99 C ANISOU 1262 CG2 VAL A 164 3463 3470 3702 875 -427 -538 C ATOM 1263 N ALA A 165 -29.734 19.235 21.123 1.00 26.22 N ANISOU 1263 N ALA A 165 3451 2910 3603 981 -662 -368 N ATOM 1264 CA ALA A 165 -29.571 18.640 19.797 1.00 27.55 C ANISOU 1264 CA ALA A 165 3633 3101 3734 927 -702 -254 C ATOM 1265 C ALA A 165 -28.988 17.239 19.973 1.00 25.32 C ANISOU 1265 C ALA A 165 3293 2951 3375 813 -627 -236 C ATOM 1266 O ALA A 165 -27.940 17.073 20.611 1.00 25.96 O ANISOU 1266 O ALA A 165 3404 3035 3424 727 -574 -248 O ATOM 1267 CB ALA A 165 -28.671 19.516 18.925 1.00 28.42 C ANISOU 1267 CB ALA A 165 3892 3065 3842 878 -757 -166 C ATOM 1268 N CYS A 166 -29.673 16.223 19.461 1.00 22.33 N ANISOU 1268 N CYS A 166 2830 2681 2974 815 -627 -212 N ATOM 1269 CA CYS A 166 -29.333 14.849 19.815 1.00 24.04 C ANISOU 1269 CA CYS A 166 2982 3022 3130 727 -553 -213 C ATOM 1270 C CYS A 166 -28.200 14.362 18.908 1.00 29.03 C ANISOU 1270 C CYS A 166 3687 3639 3705 621 -550 -123 C ATOM 1271 O CYS A 166 -28.411 14.098 17.713 1.00 32.42 O ANISOU 1271 O CYS A 166 4139 4069 4111 613 -594 -57 O ATOM 1272 CB CYS A 166 -30.553 13.930 19.733 1.00 24.35 C ANISOU 1272 CB CYS A 166 2899 3180 3173 762 -550 -234 C ATOM 1273 SG CYS A 166 -30.155 12.220 20.258 1.00 26.11 S ANISOU 1273 SG CYS A 166 3058 3536 3326 651 -459 -235 S ATOM 1274 N LEU A 167 -27.000 14.242 19.485 1.00 23.02 N ANISOU 1274 N LEU A 167 2959 2867 2919 540 -497 -125 N ATOM 1275 CA LEU A 167 -25.809 13.743 18.813 1.00 23.25 C ANISOU 1275 CA LEU A 167 3038 2894 2903 440 -472 -55 C ATOM 1276 C LEU A 167 -25.073 12.851 19.800 1.00 24.47 C ANISOU 1276 C LEU A 167 3144 3123 3032 376 -404 -86 C ATOM 1277 O LEU A 167 -25.022 13.177 20.988 1.00 23.02 O ANISOU 1277 O LEU A 167 2944 2940 2864 390 -387 -150 O ATOM 1278 CB LEU A 167 -24.902 14.891 18.357 1.00 25.07 C ANISOU 1278 CB LEU A 167 3375 3000 3150 406 -499 -10 C ATOM 1279 CG LEU A 167 -25.620 15.887 17.414 1.00 30.78 C ANISOU 1279 CG LEU A 167 4169 3630 3898 474 -579 31 C ATOM 1280 CD1 LEU A 167 -24.897 17.228 17.378 1.00 34.55 C ANISOU 1280 CD1 LEU A 167 4755 3965 4410 453 -606 53 C ATOM 1281 CD2 LEU A 167 -25.798 15.290 15.992 1.00 27.57 C ANISOU 1281 CD2 LEU A 167 3787 3253 3436 451 -603 113 C ATOM 1282 N PHE A 168 -24.516 11.734 19.301 1.00 20.83 N ANISOU 1282 N PHE A 168 2667 2720 2530 312 -368 -42 N ATOM 1283 CA PHE A 168 -23.920 10.721 20.173 1.00 18.21 C ANISOU 1283 CA PHE A 168 2285 2460 2175 263 -314 -63 C ATOM 1284 C PHE A 168 -22.866 11.345 21.087 1.00 19.71 C ANISOU 1284 C PHE A 168 2499 2609 2382 227 -305 -87 C ATOM 1285 O PHE A 168 -22.932 11.211 22.317 1.00 21.26 O ANISOU 1285 O PHE A 168 2664 2841 2571 233 -291 -142 O ATOM 1286 CB PHE A 168 -23.314 9.583 19.318 1.00 18.62 C ANISOU 1286 CB PHE A 168 2334 2551 2190 205 -282 -9 C ATOM 1287 CG PHE A 168 -22.825 8.388 20.123 1.00 18.75 C ANISOU 1287 CG PHE A 168 2299 2636 2187 168 -236 -24 C ATOM 1288 CD1 PHE A 168 -21.571 8.409 20.733 1.00 18.16 C ANISOU 1288 CD1 PHE A 168 2227 2552 2123 123 -217 -21 C ATOM 1289 CD2 PHE A 168 -23.601 7.247 20.245 1.00 16.13 C ANISOU 1289 CD2 PHE A 168 1921 2375 1833 175 -220 -35 C ATOM 1290 CE1 PHE A 168 -21.105 7.322 21.469 1.00 13.65 C ANISOU 1290 CE1 PHE A 168 1614 2035 1535 97 -189 -27 C ATOM 1291 CE2 PHE A 168 -23.146 6.149 20.992 1.00 17.45 C ANISOU 1291 CE2 PHE A 168 2056 2591 1982 142 -184 -39 C ATOM 1292 CZ PHE A 168 -21.877 6.187 21.586 1.00 16.89 C ANISOU 1292 CZ PHE A 168 1992 2505 1919 108 -171 -32 C ATOM 1293 N GLU A 169 -21.921 12.086 20.509 1.00 17.19 N ANISOU 1293 N GLU A 169 2239 2214 2080 183 -317 -46 N ATOM 1294 CA GLU A 169 -20.817 12.607 21.306 1.00 19.25 C ANISOU 1294 CA GLU A 169 2513 2439 2361 131 -315 -65 C ATOM 1295 C GLU A 169 -21.208 13.761 22.215 1.00 19.56 C ANISOU 1295 C GLU A 169 2587 2417 2428 172 -350 -132 C ATOM 1296 O GLU A 169 -20.415 14.117 23.091 1.00 21.26 O ANISOU 1296 O GLU A 169 2811 2613 2652 129 -356 -165 O ATOM 1297 CB GLU A 169 -19.669 13.046 20.398 1.00 26.06 C ANISOU 1297 CB GLU A 169 3419 3242 3240 58 -308 -2 C ATOM 1298 CG GLU A 169 -18.860 11.908 19.824 1.00 32.24 C ANISOU 1298 CG GLU A 169 4160 4090 4001 5 -258 45 C ATOM 1299 CD GLU A 169 -17.607 12.388 19.053 1.00 36.40 C ANISOU 1299 CD GLU A 169 4715 4568 4547 -76 -234 100 C ATOM 1300 OE1 GLU A 169 -17.017 13.453 19.409 1.00 39.73 O ANISOU 1300 OE1 GLU A 169 5168 4919 5008 -118 -257 93 O ATOM 1301 OE2 GLU A 169 -17.204 11.685 18.114 1.00 34.44 O ANISOU 1301 OE2 GLU A 169 4456 4354 4275 -104 -186 145 O ATOM 1302 N ASP A 170 -22.386 14.355 22.048 1.00 18.31 N ANISOU 1302 N ASP A 170 2446 2224 2285 255 -378 -158 N ATOM 1303 CA ASP A 170 -22.792 15.387 22.985 1.00 22.64 C ANISOU 1303 CA ASP A 170 3026 2715 2862 306 -402 -237 C ATOM 1304 C ASP A 170 -23.405 14.817 24.261 1.00 24.68 C ANISOU 1304 C ASP A 170 3223 3065 3089 342 -368 -317 C ATOM 1305 O ASP A 170 -23.431 15.526 25.271 1.00 26.69 O ANISOU 1305 O ASP A 170 3507 3287 3348 362 -373 -393 O ATOM 1306 CB ASP A 170 -23.783 16.365 22.327 1.00 23.90 C ANISOU 1306 CB ASP A 170 3229 2788 3065 395 -448 -237 C ATOM 1307 CG ASP A 170 -23.121 17.258 21.245 1.00 30.69 C ANISOU 1307 CG ASP A 170 4183 3527 3952 354 -489 -161 C ATOM 1308 OD1 ASP A 170 -21.891 17.144 21.080 1.00 30.50 O ANISOU 1308 OD1 ASP A 170 4180 3493 3917 252 -470 -118 O ATOM 1309 OD2 ASP A 170 -23.821 18.057 20.557 1.00 28.29 O ANISOU 1309 OD2 ASP A 170 3932 3139 3680 421 -540 -140 O ATOM 1310 N VAL A 171 -23.903 13.573 24.255 1.00 21.77 N ANISOU 1310 N VAL A 171 2782 2807 2685 345 -330 -303 N ATOM 1311 CA VAL A 171 -24.552 13.018 25.437 1.00 20.03 C ANISOU 1311 CA VAL A 171 2509 2675 2426 369 -290 -370 C ATOM 1312 C VAL A 171 -23.750 11.881 26.088 1.00 18.75 C ANISOU 1312 C VAL A 171 2323 2591 2210 294 -259 -351 C ATOM 1313 O VAL A 171 -23.763 11.769 27.319 1.00 19.31 O ANISOU 1313 O VAL A 171 2393 2704 2239 288 -239 -407 O ATOM 1314 CB VAL A 171 -26.017 12.576 25.141 1.00 21.16 C ANISOU 1314 CB VAL A 171 2581 2881 2576 440 -271 -384 C ATOM 1315 CG1 VAL A 171 -26.870 13.805 24.734 1.00 23.45 C ANISOU 1315 CG1 VAL A 171 2890 3092 2929 536 -311 -418 C ATOM 1316 CG2 VAL A 171 -26.129 11.522 24.048 1.00 15.42 C ANISOU 1316 CG2 VAL A 171 1818 2201 1841 410 -271 -307 C ATOM 1317 N VAL A 172 -23.030 11.057 25.328 1.00 18.02 N ANISOU 1317 N VAL A 172 2218 2516 2114 239 -257 -276 N ATOM 1318 CA VAL A 172 -22.265 9.942 25.894 1.00 18.94 C ANISOU 1318 CA VAL A 172 2310 2697 2191 181 -237 -253 C ATOM 1319 C VAL A 172 -20.849 10.440 26.199 1.00 18.47 C ANISOU 1319 C VAL A 172 2282 2590 2145 124 -268 -245 C ATOM 1320 O VAL A 172 -20.158 10.898 25.277 1.00 20.28 O ANISOU 1320 O VAL A 172 2531 2760 2416 96 -283 -202 O ATOM 1321 CB VAL A 172 -22.235 8.723 24.957 1.00 20.34 C ANISOU 1321 CB VAL A 172 2452 2914 2362 160 -216 -187 C ATOM 1322 CG1 VAL A 172 -21.647 7.458 25.673 1.00 19.62 C ANISOU 1322 CG1 VAL A 172 2336 2886 2233 117 -196 -168 C ATOM 1323 CG2 VAL A 172 -23.649 8.391 24.432 1.00 17.87 C ANISOU 1323 CG2 VAL A 172 2106 2636 2047 207 -201 -193 C ATOM 1324 N PRO A 173 -20.376 10.347 27.444 1.00 18.27 N ANISOU 1324 N PRO A 173 2264 2594 2084 98 -278 -281 N ATOM 1325 CA PRO A 173 -19.013 10.823 27.761 1.00 19.22 C ANISOU 1325 CA PRO A 173 2402 2675 2225 38 -321 -277 C ATOM 1326 C PRO A 173 -17.961 10.006 27.029 1.00 16.48 C ANISOU 1326 C PRO A 173 2011 2345 1906 -9 -317 -201 C ATOM 1327 O PRO A 173 -18.060 8.780 26.942 1.00 17.31 O ANISOU 1327 O PRO A 173 2078 2510 1987 -3 -291 -167 O ATOM 1328 CB PRO A 173 -18.895 10.615 29.282 1.00 19.59 C ANISOU 1328 CB PRO A 173 2463 2773 2208 25 -338 -328 C ATOM 1329 CG PRO A 173 -20.326 10.380 29.770 1.00 17.57 C ANISOU 1329 CG PRO A 173 2210 2567 1901 84 -291 -374 C ATOM 1330 CD PRO A 173 -21.047 9.734 28.613 1.00 18.03 C ANISOU 1330 CD PRO A 173 2223 2640 1986 114 -253 -323 C ATOM 1331 N MET A 174 -16.937 10.689 26.510 1.00 15.23 N ANISOU 1331 N MET A 174 1858 2129 1801 -58 -339 -179 N ATOM 1332 CA MET A 174 -15.889 9.958 25.788 1.00 17.06 C ANISOU 1332 CA MET A 174 2036 2381 2066 -99 -322 -115 C ATOM 1333 C MET A 174 -14.994 9.147 26.736 1.00 17.33 C ANISOU 1333 C MET A 174 2021 2473 2090 -125 -351 -111 C ATOM 1334 O MET A 174 -14.442 8.124 26.323 1.00 18.31 O ANISOU 1334 O MET A 174 2092 2634 2231 -128 -329 -66 O ATOM 1335 CB MET A 174 -15.054 10.934 24.954 1.00 21.34 C ANISOU 1335 CB MET A 174 2589 2852 2668 -153 -325 -89 C ATOM 1336 CG MET A 174 -14.242 10.252 23.872 1.00 24.71 C ANISOU 1336 CG MET A 174 2964 3299 3127 -182 -279 -25 C ATOM 1337 SD MET A 174 -15.252 9.339 22.679 1.00 29.45 S ANISOU 1337 SD MET A 174 3577 3925 3689 -126 -219 11 S ATOM 1338 CE MET A 174 -15.851 10.644 21.601 1.00 33.75 C ANISOU 1338 CE MET A 174 4202 4381 4239 -126 -219 28 C ATOM 1339 N ASN A 175 -14.836 9.566 28.008 1.00 15.94 N ANISOU 1339 N ASN A 175 1868 2303 1886 -140 -404 -161 N ATOM 1340 CA ASN A 175 -14.050 8.738 28.938 1.00 16.84 C ANISOU 1340 CA ASN A 175 1943 2475 1980 -159 -447 -150 C ATOM 1341 C ASN A 175 -14.758 7.409 29.244 1.00 16.86 C ANISOU 1341 C ASN A 175 1942 2540 1922 -115 -418 -129 C ATOM 1342 O ASN A 175 -14.104 6.357 29.298 1.00 17.85 O ANISOU 1342 O ASN A 175 2022 2701 2059 -116 -429 -83 O ATOM 1343 CB ASN A 175 -13.658 9.517 30.221 1.00 19.87 C ANISOU 1343 CB ASN A 175 2363 2852 2333 -195 -522 -209 C ATOM 1344 CG ASN A 175 -14.851 10.209 30.954 1.00 22.38 C ANISOU 1344 CG ASN A 175 2766 3156 2581 -162 -513 -284 C ATOM 1345 OD1 ASN A 175 -16.026 9.918 30.721 1.00 19.44 O ANISOU 1345 OD1 ASN A 175 2411 2800 2177 -108 -455 -290 O ATOM 1346 ND2 ASN A 175 -14.511 11.109 31.877 1.00 20.55 N ANISOU 1346 ND2 ASN A 175 2583 2899 2328 -196 -572 -347 N ATOM 1347 N TYR A 176 -16.092 7.409 29.342 1.00 15.56 N ANISOU 1347 N TYR A 176 1820 2386 1707 -75 -378 -156 N ATOM 1348 CA TYR A 176 -16.835 6.137 29.366 1.00 13.92 C ANISOU 1348 CA TYR A 176 1603 2229 1455 -45 -338 -128 C ATOM 1349 C TYR A 176 -16.585 5.316 28.092 1.00 16.01 C ANISOU 1349 C TYR A 176 1826 2486 1772 -37 -301 -69 C ATOM 1350 O TYR A 176 -16.338 4.096 28.151 1.00 16.18 O ANISOU 1350 O TYR A 176 1826 2535 1785 -32 -296 -29 O ATOM 1351 CB TYR A 176 -18.354 6.399 29.544 1.00 13.86 C ANISOU 1351 CB TYR A 176 1628 2236 1401 -9 -293 -172 C ATOM 1352 CG TYR A 176 -19.190 5.187 29.186 1.00 15.74 C ANISOU 1352 CG TYR A 176 1848 2515 1617 9 -244 -137 C ATOM 1353 CD1 TYR A 176 -19.461 4.203 30.146 1.00 16.47 C ANISOU 1353 CD1 TYR A 176 1954 2663 1643 -2 -237 -125 C ATOM 1354 CD2 TYR A 176 -19.671 4.997 27.880 1.00 13.73 C ANISOU 1354 CD2 TYR A 176 1571 2241 1404 27 -210 -114 C ATOM 1355 CE1 TYR A 176 -20.171 3.058 29.817 1.00 16.18 C ANISOU 1355 CE1 TYR A 176 1903 2653 1591 0 -195 -90 C ATOM 1356 CE2 TYR A 176 -20.383 3.848 27.534 1.00 16.30 C ANISOU 1356 CE2 TYR A 176 1881 2599 1712 32 -174 -86 C ATOM 1357 CZ TYR A 176 -20.617 2.871 28.522 1.00 19.50 C ANISOU 1357 CZ TYR A 176 2296 3052 2061 16 -165 -74 C ATOM 1358 OH TYR A 176 -21.334 1.728 28.211 1.00 22.15 O ANISOU 1358 OH TYR A 176 2621 3411 2383 9 -130 -46 O ATOM 1359 N MET A 177 -16.671 5.964 26.923 1.00 15.55 N ANISOU 1359 N MET A 177 1765 2385 1760 -34 -275 -65 N ATOM 1360 CA MET A 177 -16.557 5.238 25.653 1.00 15.95 C ANISOU 1360 CA MET A 177 1790 2429 1840 -27 -232 -20 C ATOM 1361 C MET A 177 -15.176 4.611 25.482 1.00 14.70 C ANISOU 1361 C MET A 177 1581 2278 1728 -47 -238 17 C ATOM 1362 O MET A 177 -15.047 3.508 24.934 1.00 15.77 O ANISOU 1362 O MET A 177 1696 2425 1871 -31 -206 48 O ATOM 1363 CB MET A 177 -16.877 6.174 24.482 1.00 16.15 C ANISOU 1363 CB MET A 177 1839 2407 1892 -26 -210 -19 C ATOM 1364 CG MET A 177 -18.392 6.472 24.294 1.00 16.01 C ANISOU 1364 CG MET A 177 1855 2388 1842 14 -200 -45 C ATOM 1365 SD MET A 177 -19.388 4.962 24.175 1.00 18.99 S ANISOU 1365 SD MET A 177 2215 2823 2178 37 -167 -31 S ATOM 1366 CE MET A 177 -18.706 4.167 22.735 1.00 17.77 C ANISOU 1366 CE MET A 177 2052 2654 2048 24 -134 19 C ATOM 1367 N VAL A 178 -14.126 5.290 25.932 1.00 15.84 N ANISOU 1367 N VAL A 178 1699 2410 1908 -82 -279 11 N ATOM 1368 CA VAL A 178 -12.773 4.769 25.722 1.00 17.85 C ANISOU 1368 CA VAL A 178 1882 2676 2223 -97 -285 43 C ATOM 1369 C VAL A 178 -12.351 3.813 26.846 1.00 18.00 C ANISOU 1369 C VAL A 178 1877 2734 2227 -81 -339 54 C ATOM 1370 O VAL A 178 -11.947 2.674 26.579 1.00 15.61 O ANISOU 1370 O VAL A 178 1537 2445 1949 -52 -323 87 O ATOM 1371 CB VAL A 178 -11.772 5.936 25.561 1.00 18.97 C ANISOU 1371 CB VAL A 178 1992 2791 2426 -153 -305 35 C ATOM 1372 CG1 VAL A 178 -10.359 5.415 25.513 1.00 21.32 C ANISOU 1372 CG1 VAL A 178 2193 3114 2795 -169 -315 61 C ATOM 1373 CG2 VAL A 178 -12.094 6.734 24.287 1.00 20.97 C ANISOU 1373 CG2 VAL A 178 2278 2997 2692 -171 -247 43 C ATOM 1374 N TYR A 179 -12.423 4.246 28.116 1.00 15.95 N ANISOU 1374 N TYR A 179 1646 2489 1924 -97 -406 27 N ATOM 1375 CA TYR A 179 -11.872 3.419 29.196 1.00 17.44 C ANISOU 1375 CA TYR A 179 1820 2713 2093 -88 -473 47 C ATOM 1376 C TYR A 179 -12.815 2.285 29.575 1.00 20.10 C ANISOU 1376 C TYR A 179 2208 3070 2360 -52 -453 68 C ATOM 1377 O TYR A 179 -12.376 1.150 29.796 1.00 21.97 O ANISOU 1377 O TYR A 179 2426 3316 2605 -27 -475 110 O ATOM 1378 CB TYR A 179 -11.589 4.261 30.448 1.00 17.07 C ANISOU 1378 CB TYR A 179 1800 2679 2008 -125 -557 9 C ATOM 1379 CG TYR A 179 -10.481 5.280 30.317 1.00 20.59 C ANISOU 1379 CG TYR A 179 2191 3105 2528 -176 -601 -9 C ATOM 1380 CD1 TYR A 179 -9.246 4.934 29.780 1.00 20.89 C ANISOU 1380 CD1 TYR A 179 2124 3150 2662 -184 -610 27 C ATOM 1381 CD2 TYR A 179 -10.673 6.602 30.730 1.00 20.54 C ANISOU 1381 CD2 TYR A 179 2234 3070 2499 -219 -628 -65 C ATOM 1382 CE1 TYR A 179 -8.229 5.884 29.673 1.00 26.74 C ANISOU 1382 CE1 TYR A 179 2804 3878 3476 -245 -646 11 C ATOM 1383 CE2 TYR A 179 -9.659 7.547 30.640 1.00 22.09 C ANISOU 1383 CE2 TYR A 179 2385 3242 2766 -281 -672 -81 C ATOM 1384 CZ TYR A 179 -8.444 7.187 30.098 1.00 27.35 C ANISOU 1384 CZ TYR A 179 2940 3923 3529 -300 -679 -40 C ATOM 1385 OH TYR A 179 -7.424 8.115 29.985 1.00 29.48 O ANISOU 1385 OH TYR A 179 3152 4173 3876 -375 -717 -54 O ATOM 1386 N PHE A 180 -14.104 2.584 29.706 1.00 18.13 N ANISOU 1386 N PHE A 180 2021 2824 2043 -50 -413 38 N ATOM 1387 CA PHE A 180 -15.047 1.615 30.246 1.00 20.85 C ANISOU 1387 CA PHE A 180 2413 3194 2314 -36 -394 54 C ATOM 1388 C PHE A 180 -15.602 0.741 29.124 1.00 18.83 C ANISOU 1388 C PHE A 180 2148 2922 2085 -13 -326 81 C ATOM 1389 O PHE A 180 -15.489 -0.490 29.165 1.00 22.35 O ANISOU 1389 O PHE A 180 2597 3365 2529 1 -326 123 O ATOM 1390 CB PHE A 180 -16.163 2.346 31.019 1.00 19.58 C ANISOU 1390 CB PHE A 180 2311 3057 2070 -47 -378 1 C ATOM 1391 CG PHE A 180 -17.132 1.429 31.791 1.00 18.45 C ANISOU 1391 CG PHE A 180 2217 2954 1840 -49 -352 16 C ATOM 1392 CD1 PHE A 180 -18.184 0.773 31.137 1.00 18.79 C ANISOU 1392 CD1 PHE A 180 2259 3000 1881 -40 -283 28 C ATOM 1393 CD2 PHE A 180 -17.037 1.303 33.178 1.00 18.08 C ANISOU 1393 CD2 PHE A 180 2222 2942 1705 -70 -396 15 C ATOM 1394 CE1 PHE A 180 -19.114 -0.024 31.858 1.00 20.42 C ANISOU 1394 CE1 PHE A 180 2505 3244 2009 -57 -251 42 C ATOM 1395 CE2 PHE A 180 -17.977 0.512 33.916 1.00 19.17 C ANISOU 1395 CE2 PHE A 180 2413 3120 1750 -85 -359 33 C ATOM 1396 CZ PHE A 180 -19.014 -0.146 33.246 1.00 17.42 C ANISOU 1396 CZ PHE A 180 2179 2900 1538 -81 -283 47 C ATOM 1397 N ASN A 181 -16.190 1.353 28.104 1.00 17.67 N ANISOU 1397 N ASN A 181 1996 2757 1961 -9 -275 57 N ATOM 1398 CA ASN A 181 -16.738 0.534 27.039 1.00 19.28 C ANISOU 1398 CA ASN A 181 2199 2948 2179 6 -221 76 C ATOM 1399 C ASN A 181 -15.626 -0.128 26.199 1.00 21.71 C ANISOU 1399 C ASN A 181 2466 3230 2554 21 -213 109 C ATOM 1400 O ASN A 181 -15.601 -1.348 26.054 1.00 25.90 O ANISOU 1400 O ASN A 181 3003 3750 3088 38 -201 137 O ATOM 1401 CB ASN A 181 -17.700 1.364 26.179 1.00 17.94 C ANISOU 1401 CB ASN A 181 2039 2769 2008 9 -183 45 C ATOM 1402 CG ASN A 181 -18.481 0.501 25.215 1.00 19.48 C ANISOU 1402 CG ASN A 181 2242 2960 2200 17 -140 59 C ATOM 1403 OD1 ASN A 181 -18.037 0.266 24.098 1.00 23.25 O ANISOU 1403 OD1 ASN A 181 2710 3411 2712 23 -117 73 O ATOM 1404 ND2 ASN A 181 -19.638 -0.008 25.657 1.00 19.03 N ANISOU 1404 ND2 ASN A 181 2202 2931 2098 11 -126 51 N ATOM 1405 N PHE A 182 -14.695 0.642 25.635 1.00 16.67 N ANISOU 1405 N PHE A 182 1787 2577 1972 14 -212 103 N ATOM 1406 CA PHE A 182 -13.735 0.028 24.711 1.00 19.04 C ANISOU 1406 CA PHE A 182 2040 2860 2335 30 -181 125 C ATOM 1407 C PHE A 182 -12.686 -0.815 25.453 1.00 18.28 C ANISOU 1407 C PHE A 182 1899 2770 2276 53 -228 152 C ATOM 1408 O PHE A 182 -12.597 -2.029 25.247 1.00 20.70 O ANISOU 1408 O PHE A 182 2208 3060 2595 88 -213 174 O ATOM 1409 CB PHE A 182 -13.048 1.097 23.849 1.00 17.62 C ANISOU 1409 CB PHE A 182 1825 2668 2202 5 -154 116 C ATOM 1410 CG PHE A 182 -12.081 0.532 22.790 1.00 21.29 C ANISOU 1410 CG PHE A 182 2238 3125 2727 19 -98 131 C ATOM 1411 CD1 PHE A 182 -12.393 -0.642 22.074 1.00 17.22 C ANISOU 1411 CD1 PHE A 182 1745 2597 2202 54 -49 136 C ATOM 1412 CD2 PHE A 182 -10.890 1.197 22.503 1.00 16.54 C ANISOU 1412 CD2 PHE A 182 1567 2528 2191 -7 -87 133 C ATOM 1413 CE1 PHE A 182 -11.537 -1.131 21.115 1.00 20.16 C ANISOU 1413 CE1 PHE A 182 2076 2962 2623 73 12 138 C ATOM 1414 CE2 PHE A 182 -10.029 0.730 21.527 1.00 20.99 C ANISOU 1414 CE2 PHE A 182 2076 3093 2808 5 -19 140 C ATOM 1415 CZ PHE A 182 -10.339 -0.453 20.824 1.00 20.13 C ANISOU 1415 CZ PHE A 182 1993 2972 2683 51 34 139 C ATOM 1416 N PHE A 183 -11.876 -0.195 26.313 1.00 16.18 N ANISOU 1416 N PHE A 183 1595 2522 2031 36 -293 150 N ATOM 1417 CA PHE A 183 -10.788 -0.939 26.954 1.00 20.08 C ANISOU 1417 CA PHE A 183 2035 3024 2571 63 -352 179 C ATOM 1418 C PHE A 183 -11.327 -2.094 27.807 1.00 22.96 C ANISOU 1418 C PHE A 183 2459 3385 2879 91 -389 210 C ATOM 1419 O PHE A 183 -10.973 -3.262 27.588 1.00 23.21 O ANISOU 1419 O PHE A 183 2479 3391 2947 137 -386 240 O ATOM 1420 CB PHE A 183 -9.908 -0.005 27.791 1.00 19.72 C ANISOU 1420 CB PHE A 183 1940 3002 2549 29 -432 169 C ATOM 1421 CG PHE A 183 -9.044 0.964 26.964 1.00 22.69 C ANISOU 1421 CG PHE A 183 2238 3377 3005 -6 -401 151 C ATOM 1422 CD1 PHE A 183 -9.002 0.898 25.576 1.00 21.04 C ANISOU 1422 CD1 PHE A 183 2008 3151 2836 1 -303 150 C ATOM 1423 CD2 PHE A 183 -8.274 1.931 27.596 1.00 23.30 C ANISOU 1423 CD2 PHE A 183 2271 3469 3111 -54 -470 135 C ATOM 1424 CE1 PHE A 183 -8.205 1.785 24.825 1.00 22.35 C ANISOU 1424 CE1 PHE A 183 2109 3318 3066 -43 -264 142 C ATOM 1425 CE2 PHE A 183 -7.472 2.822 26.852 1.00 26.20 C ANISOU 1425 CE2 PHE A 183 2567 3833 3556 -102 -437 124 C ATOM 1426 CZ PHE A 183 -7.452 2.736 25.459 1.00 24.53 C ANISOU 1426 CZ PHE A 183 2336 3606 3380 -97 -329 131 C ATOM 1427 N ALA A 184 -12.208 -1.794 28.769 1.00 20.02 N ANISOU 1427 N ALA A 184 2158 3032 2416 62 -418 203 N ATOM 1428 CA ALA A 184 -12.626 -2.823 29.727 1.00 20.70 C ANISOU 1428 CA ALA A 184 2307 3119 2438 73 -456 241 C ATOM 1429 C ALA A 184 -13.627 -3.813 29.128 1.00 22.51 C ANISOU 1429 C ALA A 184 2587 3321 2646 82 -388 255 C ATOM 1430 O ALA A 184 -13.503 -5.028 29.338 1.00 19.46 O ANISOU 1430 O ALA A 184 2228 2904 2263 108 -406 299 O ATOM 1431 CB ALA A 184 -13.223 -2.167 30.971 1.00 20.62 C ANISOU 1431 CB ALA A 184 2358 3148 2329 32 -497 223 C ATOM 1432 N CYS A 185 -14.622 -3.326 28.376 1.00 17.21 N ANISOU 1432 N CYS A 185 1931 2653 1954 61 -318 219 N ATOM 1433 CA CYS A 185 -15.749 -4.176 28.018 1.00 20.16 C ANISOU 1433 CA CYS A 185 2356 3012 2292 53 -267 227 C ATOM 1434 C CYS A 185 -15.654 -4.764 26.616 1.00 20.71 C ANISOU 1434 C CYS A 185 2409 3040 2419 77 -213 222 C ATOM 1435 O CYS A 185 -16.390 -5.711 26.307 1.00 20.60 O ANISOU 1435 O CYS A 185 2439 3001 2388 70 -184 233 O ATOM 1436 CB CYS A 185 -17.068 -3.403 28.168 1.00 20.93 C ANISOU 1436 CB CYS A 185 2480 3147 2326 16 -232 190 C ATOM 1437 SG CYS A 185 -17.445 -3.074 29.916 1.00 24.90 S ANISOU 1437 SG CYS A 185 3028 3699 2732 -15 -272 190 S ATOM 1438 N VAL A 186 -14.757 -4.257 25.777 1.00 17.40 N ANISOU 1438 N VAL A 186 1933 2613 2064 98 -197 206 N ATOM 1439 CA VAL A 186 -14.611 -4.788 24.434 1.00 20.59 C ANISOU 1439 CA VAL A 186 2330 2982 2510 120 -138 195 C ATOM 1440 C VAL A 186 -13.235 -5.407 24.230 1.00 20.92 C ANISOU 1440 C VAL A 186 2318 2998 2631 170 -144 210 C ATOM 1441 O VAL A 186 -13.122 -6.590 23.894 1.00 24.51 O ANISOU 1441 O VAL A 186 2796 3408 3110 206 -127 219 O ATOM 1442 CB VAL A 186 -14.869 -3.685 23.389 1.00 21.21 C ANISOU 1442 CB VAL A 186 2397 3077 2587 99 -91 161 C ATOM 1443 CG1 VAL A 186 -14.495 -4.209 21.987 1.00 17.69 C ANISOU 1443 CG1 VAL A 186 1947 2601 2174 120 -27 149 C ATOM 1444 CG2 VAL A 186 -16.302 -3.262 23.468 1.00 19.55 C ANISOU 1444 CG2 VAL A 186 2232 2885 2312 66 -87 145 C ATOM 1445 N ALEU A 187 -12.187 -4.619 24.473 0.39 19.72 N ANISOU 1445 N ALEU A 187 2094 2873 2528 174 -170 208 N ATOM 1446 N BLEU A 187 -12.175 -4.616 24.431 0.61 19.40 N ANISOU 1446 N BLEU A 187 2052 2832 2488 174 -168 207 N ATOM 1447 CA ALEU A 187 -10.833 -5.075 24.185 0.39 20.71 C ANISOU 1447 CA ALEU A 187 2140 2986 2745 224 -169 215 C ATOM 1448 CA BLEU A 187 -10.826 -5.114 24.179 0.61 20.78 C ANISOU 1448 CA BLEU A 187 2149 2993 2754 226 -168 215 C ATOM 1449 C ALEU A 187 -10.419 -6.233 25.089 0.39 22.33 C ANISOU 1449 C ALEU A 187 2350 3162 2973 275 -237 254 C ATOM 1450 C BLEU A 187 -10.486 -6.294 25.075 0.61 22.70 C ANISOU 1450 C BLEU A 187 2403 3206 3017 275 -235 255 C ATOM 1451 O ALEU A 187 -9.763 -7.176 24.630 0.39 22.81 O ANISOU 1451 O ALEU A 187 2383 3183 3101 337 -218 257 O ATOM 1452 O BLEU A 187 -9.919 -7.292 24.612 0.61 22.72 O ANISOU 1452 O BLEU A 187 2387 3166 3081 336 -215 258 O ATOM 1453 CB ALEU A 187 -9.857 -3.907 24.315 0.39 20.08 C ANISOU 1453 CB ALEU A 187 1969 2946 2713 201 -189 206 C ATOM 1454 CB BLEU A 187 -9.787 -4.011 24.373 0.61 20.07 C ANISOU 1454 CB BLEU A 187 1965 2943 2716 206 -193 208 C ATOM 1455 CG ALEU A 187 -8.447 -4.140 23.797 0.39 20.15 C ANISOU 1455 CG ALEU A 187 1868 2959 2829 242 -165 202 C ATOM 1456 CG BLEU A 187 -9.575 -3.099 23.185 0.61 18.84 C ANISOU 1456 CG BLEU A 187 1776 2800 2581 174 -112 179 C ATOM 1457 CD1ALEU A 187 -8.494 -4.633 22.364 0.39 19.89 C ANISOU 1457 CD1ALEU A 187 1844 2901 2812 266 -53 177 C ATOM 1458 CD1BLEU A 187 -8.384 -2.195 23.437 0.61 19.50 C ANISOU 1458 CD1BLEU A 187 1757 2917 2735 149 -140 178 C ATOM 1459 CD2ALEU A 187 -7.647 -2.853 23.900 0.39 20.06 C ANISOU 1459 CD2ALEU A 187 1772 2990 2860 192 -181 192 C ATOM 1460 CD2BLEU A 187 -9.374 -3.913 21.923 0.61 21.26 C ANISOU 1460 CD2BLEU A 187 2080 3081 2918 213 -20 164 C ATOM 1461 N VAL A 188 -10.785 -6.190 26.367 1.00 20.12 N ANISOU 1461 N VAL A 188 2113 2897 2636 253 -317 284 N ATOM 1462 CA VAL A 188 -10.396 -7.260 27.290 1.00 21.38 C ANISOU 1462 CA VAL A 188 2293 3024 2805 297 -395 335 C ATOM 1463 C VAL A 188 -11.081 -8.575 26.914 1.00 21.89 C ANISOU 1463 C VAL A 188 2441 3021 2855 320 -358 351 C ATOM 1464 O VAL A 188 -10.386 -9.587 26.757 1.00 24.58 O ANISOU 1464 O VAL A 188 2768 3306 3266 389 -373 370 O ATOM 1465 CB VAL A 188 -10.622 -6.842 28.756 1.00 22.73 C ANISOU 1465 CB VAL A 188 2505 3233 2898 258 -486 364 C ATOM 1466 CG1 VAL A 188 -10.563 -8.095 29.655 1.00 25.75 C ANISOU 1466 CG1 VAL A 188 2952 3571 3260 292 -560 429 C ATOM 1467 CG2 VAL A 188 -9.540 -5.824 29.182 1.00 19.79 C ANISOU 1467 CG2 VAL A 188 2040 2911 2571 252 -550 351 C ATOM 1468 N PRO A 189 -12.420 -8.617 26.725 1.00 22.74 N ANISOU 1468 N PRO A 189 2630 3125 2883 265 -310 340 N ATOM 1469 CA PRO A 189 -13.036 -9.876 26.242 1.00 25.04 C ANISOU 1469 CA PRO A 189 2998 3346 3171 274 -274 349 C ATOM 1470 C PRO A 189 -12.482 -10.379 24.913 1.00 22.34 C ANISOU 1470 C PRO A 189 2625 2957 2907 329 -210 311 C ATOM 1471 O PRO A 189 -12.300 -11.593 24.757 1.00 21.53 O ANISOU 1471 O PRO A 189 2564 2776 2842 375 -212 325 O ATOM 1472 CB PRO A 189 -14.534 -9.527 26.143 1.00 24.85 C ANISOU 1472 CB PRO A 189 3034 3351 3059 196 -231 331 C ATOM 1473 CG PRO A 189 -14.748 -8.452 27.169 1.00 24.46 C ANISOU 1473 CG PRO A 189 2970 3374 2950 155 -270 336 C ATOM 1474 CD PRO A 189 -13.460 -7.629 27.111 1.00 22.16 C ANISOU 1474 CD PRO A 189 2588 3110 2723 193 -299 322 C ATOM 1475 N LEU A 190 -12.182 -9.497 23.960 1.00 18.47 N ANISOU 1475 N LEU A 190 2072 2507 2440 325 -150 263 N ATOM 1476 CA LEU A 190 -11.620 -9.960 22.687 1.00 17.44 C ANISOU 1476 CA LEU A 190 1918 2340 2369 374 -76 222 C ATOM 1477 C LEU A 190 -10.258 -10.612 22.887 1.00 21.24 C ANISOU 1477 C LEU A 190 2329 2788 2953 465 -102 235 C ATOM 1478 O LEU A 190 -9.964 -11.648 22.278 1.00 25.61 O ANISOU 1478 O LEU A 190 2903 3273 3555 526 -66 215 O ATOM 1479 CB LEU A 190 -11.529 -8.801 21.690 1.00 18.76 C ANISOU 1479 CB LEU A 190 2037 2562 2528 342 -7 179 C ATOM 1480 CG LEU A 190 -12.874 -8.278 21.126 1.00 23.63 C ANISOU 1480 CG LEU A 190 2724 3199 3057 272 26 158 C ATOM 1481 CD1 LEU A 190 -12.662 -7.000 20.246 1.00 21.85 C ANISOU 1481 CD1 LEU A 190 2456 3023 2823 243 78 130 C ATOM 1482 CD2 LEU A 190 -13.636 -9.342 20.323 1.00 25.29 C ANISOU 1482 CD2 LEU A 190 3020 3351 3238 271 66 134 C ATOM 1483 N LEU A 191 -9.424 -10.044 23.769 1.00 19.50 N ANISOU 1483 N LEU A 191 2027 2613 2771 478 -172 264 N ATOM 1484 CA LEU A 191 -8.127 -10.641 24.054 1.00 23.11 C ANISOU 1484 CA LEU A 191 2400 3046 3336 570 -216 280 C ATOM 1485 C LEU A 191 -8.287 -11.973 24.773 1.00 25.30 C ANISOU 1485 C LEU A 191 2758 3238 3618 621 -286 329 C ATOM 1486 O LEU A 191 -7.560 -12.935 24.494 1.00 27.33 O ANISOU 1486 O LEU A 191 2991 3428 3963 715 -285 325 O ATOM 1487 CB LEU A 191 -7.284 -9.672 24.885 1.00 25.33 C ANISOU 1487 CB LEU A 191 2575 3400 3648 557 -292 300 C ATOM 1488 CG LEU A 191 -6.841 -8.392 24.162 1.00 31.02 C ANISOU 1488 CG LEU A 191 3202 4192 4392 511 -225 257 C ATOM 1489 CD1 LEU A 191 -6.129 -7.444 25.141 1.00 33.94 C ANISOU 1489 CD1 LEU A 191 3485 4625 4785 481 -319 278 C ATOM 1490 CD2 LEU A 191 -5.937 -8.728 22.967 1.00 31.59 C ANISOU 1490 CD2 LEU A 191 3187 4256 4562 572 -126 213 C ATOM 1491 N LEU A 192 -9.243 -12.056 25.696 1.00 24.34 N ANISOU 1491 N LEU A 192 2737 3111 3401 560 -344 375 N ATOM 1492 CA LEU A 192 -9.528 -13.340 26.323 1.00 23.52 C ANISOU 1492 CA LEU A 192 2734 2917 3287 590 -402 430 C ATOM 1493 C LEU A 192 -9.965 -14.365 25.284 1.00 24.76 C ANISOU 1493 C LEU A 192 2962 2982 3465 614 -323 394 C ATOM 1494 O LEU A 192 -9.543 -15.527 25.337 1.00 27.91 O ANISOU 1494 O LEU A 192 3396 3282 3926 692 -353 415 O ATOM 1495 CB LEU A 192 -10.591 -13.174 27.407 1.00 23.41 C ANISOU 1495 CB LEU A 192 2818 2926 3152 500 -452 480 C ATOM 1496 CG LEU A 192 -10.193 -12.443 28.692 1.00 31.28 C ANISOU 1496 CG LEU A 192 3784 3992 4110 481 -551 524 C ATOM 1497 CD1 LEU A 192 -11.438 -12.175 29.537 1.00 37.20 C ANISOU 1497 CD1 LEU A 192 4635 4776 4724 381 -558 551 C ATOM 1498 CD2 LEU A 192 -9.164 -13.242 29.502 1.00 30.70 C ANISOU 1498 CD2 LEU A 192 3700 3868 4096 566 -667 589 C ATOM 1499 N MET A 193 -10.794 -13.954 24.317 1.00 22.68 N ANISOU 1499 N MET A 193 2724 2743 3151 551 -230 338 N ATOM 1500 CA MET A 193 -11.177 -14.863 23.231 1.00 26.38 C ANISOU 1500 CA MET A 193 3261 3130 3632 567 -157 292 C ATOM 1501 C MET A 193 -9.959 -15.326 22.440 1.00 26.82 C ANISOU 1501 C MET A 193 3247 3144 3800 680 -114 247 C ATOM 1502 O MET A 193 -9.825 -16.512 22.110 1.00 29.87 O ANISOU 1502 O MET A 193 3693 3422 4233 742 -104 233 O ATOM 1503 CB MET A 193 -12.146 -14.182 22.271 1.00 28.48 C ANISOU 1503 CB MET A 193 3550 3447 3825 485 -77 237 C ATOM 1504 CG MET A 193 -13.517 -13.961 22.788 1.00 34.24 C ANISOU 1504 CG MET A 193 4352 4203 4457 382 -98 264 C ATOM 1505 SD MET A 193 -14.427 -13.168 21.460 1.00 34.68 S ANISOU 1505 SD MET A 193 4412 4314 4453 315 -13 194 S ATOM 1506 CE MET A 193 -15.408 -12.012 22.435 1.00 28.48 C ANISOU 1506 CE MET A 193 3612 3625 3585 227 -53 227 C ATOM 1507 N LEU A 194 -9.092 -14.384 22.069 1.00 24.69 N ANISOU 1507 N LEU A 194 2851 2957 3574 702 -78 216 N ATOM 1508 CA LEU A 194 -7.859 -14.762 21.393 1.00 27.35 C ANISOU 1508 CA LEU A 194 3096 3271 4023 809 -28 172 C ATOM 1509 C LEU A 194 -7.126 -15.836 22.187 1.00 28.23 C ANISOU 1509 C LEU A 194 3202 3298 4228 916 -116 216 C ATOM 1510 O LEU A 194 -6.661 -16.835 21.616 1.00 29.19 O ANISOU 1510 O LEU A 194 3335 3330 4426 1012 -78 179 O ATOM 1511 CB LEU A 194 -6.974 -13.530 21.179 1.00 24.06 C ANISOU 1511 CB LEU A 194 2530 2966 3647 802 5 153 C ATOM 1512 CG LEU A 194 -5.582 -13.819 20.608 1.00 30.89 C ANISOU 1512 CG LEU A 194 3265 3829 4641 911 60 110 C ATOM 1513 CD1 LEU A 194 -5.742 -14.460 19.239 1.00 30.91 C ANISOU 1513 CD1 LEU A 194 3327 3779 4639 942 189 31 C ATOM 1514 CD2 LEU A 194 -4.753 -12.548 20.503 1.00 32.02 C ANISOU 1514 CD2 LEU A 194 3256 4087 4823 880 87 101 C ATOM 1515 N GLY A 195 -7.050 -15.666 23.515 1.00 26.24 N ANISOU 1515 N GLY A 195 2941 3064 3964 904 -238 296 N ATOM 1516 CA GLY A 195 -6.359 -16.653 24.339 1.00 27.81 C ANISOU 1516 CA GLY A 195 3142 3182 4244 1006 -343 353 C ATOM 1517 C GLY A 195 -7.049 -18.007 24.344 1.00 29.79 C ANISOU 1517 C GLY A 195 3553 3289 4476 1024 -355 373 C ATOM 1518 O GLY A 195 -6.389 -19.049 24.374 1.00 35.64 O ANISOU 1518 O GLY A 195 4301 3926 5315 1140 -389 382 O ATOM 1519 N VAL A 196 -8.385 -18.015 24.324 1.00 28.54 N ANISOU 1519 N VAL A 196 3523 3121 4201 909 -330 381 N ATOM 1520 CA VAL A 196 -9.114 -19.284 24.307 1.00 29.03 C ANISOU 1520 CA VAL A 196 3742 3046 4244 903 -338 400 C ATOM 1521 C VAL A 196 -8.853 -20.034 22.998 1.00 26.98 C ANISOU 1521 C VAL A 196 3499 2698 4055 976 -242 310 C ATOM 1522 O VAL A 196 -8.567 -21.242 23.004 1.00 28.15 O ANISOU 1522 O VAL A 196 3718 2707 4273 1061 -270 317 O ATOM 1523 CB VAL A 196 -10.619 -19.046 24.560 1.00 25.01 C ANISOU 1523 CB VAL A 196 3341 2563 3598 751 -326 424 C ATOM 1524 CG1 VAL A 196 -11.395 -20.344 24.472 1.00 23.27 C ANISOU 1524 CG1 VAL A 196 3279 2201 3363 725 -328 440 C ATOM 1525 CG2 VAL A 196 -10.830 -18.427 25.946 1.00 24.39 C ANISOU 1525 CG2 VAL A 196 3259 2561 3447 690 -417 509 C ATOM 1526 N TYR A 197 -8.898 -19.325 21.867 1.00 26.48 N ANISOU 1526 N TYR A 197 3378 2711 3973 949 -131 223 N ATOM 1527 CA TYR A 197 -8.653 -19.958 20.571 1.00 26.78 C ANISOU 1527 CA TYR A 197 3438 2679 4057 1012 -28 127 C ATOM 1528 C TYR A 197 -7.219 -20.480 20.451 1.00 32.68 C ANISOU 1528 C TYR A 197 4087 3379 4950 1177 -24 101 C ATOM 1529 O TYR A 197 -6.998 -21.571 19.919 1.00 35.53 O ANISOU 1529 O TYR A 197 4513 3614 5374 1264 8 53 O ATOM 1530 CB TYR A 197 -9.001 -18.983 19.438 1.00 23.32 C ANISOU 1530 CB TYR A 197 2965 2347 3550 939 84 50 C ATOM 1531 CG TYR A 197 -10.496 -18.922 19.225 1.00 32.01 C ANISOU 1531 CG TYR A 197 4190 3447 4528 805 91 50 C ATOM 1532 CD1 TYR A 197 -11.201 -20.068 18.851 1.00 31.61 C ANISOU 1532 CD1 TYR A 197 4282 3270 4459 788 96 24 C ATOM 1533 CD2 TYR A 197 -11.222 -17.746 19.454 1.00 31.65 C ANISOU 1533 CD2 TYR A 197 4116 3520 4391 695 82 75 C ATOM 1534 CE1 TYR A 197 -12.578 -20.044 18.695 1.00 31.44 C ANISOU 1534 CE1 TYR A 197 4358 3253 4335 659 93 25 C ATOM 1535 CE2 TYR A 197 -12.622 -17.709 19.290 1.00 27.37 C ANISOU 1535 CE2 TYR A 197 3670 2982 3748 578 82 75 C ATOM 1536 CZ TYR A 197 -13.287 -18.869 18.918 1.00 30.48 C ANISOU 1536 CZ TYR A 197 4192 3260 4131 558 86 51 C ATOM 1537 OH TYR A 197 -14.665 -18.874 18.760 1.00 29.95 O ANISOU 1537 OH TYR A 197 4205 3201 3975 437 81 49 O ATOM 1538 N LEU A 198 -6.231 -19.741 20.958 1.00 30.46 N ANISOU 1538 N LEU A 198 3648 3193 4734 1225 -61 129 N ATOM 1539 CA LEU A 198 -4.872 -20.281 20.983 1.00 30.71 C ANISOU 1539 CA LEU A 198 3567 3182 4919 1387 -75 113 C ATOM 1540 C LEU A 198 -4.822 -21.608 21.727 1.00 29.09 C ANISOU 1540 C LEU A 198 3463 2817 4773 1475 -183 172 C ATOM 1541 O LEU A 198 -4.224 -22.583 21.249 1.00 30.89 O ANISOU 1541 O LEU A 198 3696 2932 5107 1607 -153 123 O ATOM 1542 CB LEU A 198 -3.916 -19.275 21.625 1.00 36.13 C ANISOU 1542 CB LEU A 198 4068 3999 5661 1404 -129 151 C ATOM 1543 CG LEU A 198 -3.664 -18.083 20.703 1.00 40.64 C ANISOU 1543 CG LEU A 198 4524 4706 6210 1345 -4 82 C ATOM 1544 CD1 LEU A 198 -2.832 -17.013 21.398 1.00 39.76 C ANISOU 1544 CD1 LEU A 198 4241 4721 6146 1332 -66 123 C ATOM 1545 CD2 LEU A 198 -2.987 -18.604 19.413 1.00 40.82 C ANISOU 1545 CD2 LEU A 198 4498 4695 6315 1445 139 -25 C ATOM 1546 N ARG A 199 -5.448 -21.660 22.907 1.00 28.69 N ANISOU 1546 N ARG A 199 3500 2749 4652 1404 -306 279 N ATOM 1547 CA ARG A 199 -5.491 -22.892 23.687 1.00 30.59 C ANISOU 1547 CA ARG A 199 3860 2832 4930 1467 -417 354 C ATOM 1548 C ARG A 199 -6.254 -24.010 22.967 1.00 30.65 C ANISOU 1548 C ARG A 199 4042 2683 4921 1458 -357 308 C ATOM 1549 O ARG A 199 -5.896 -25.182 23.112 1.00 33.77 O ANISOU 1549 O ARG A 199 4509 2917 5403 1568 -407 324 O ATOM 1550 CB ARG A 199 -6.124 -22.621 25.044 1.00 34.96 C ANISOU 1550 CB ARG A 199 4486 3416 5380 1365 -542 476 C ATOM 1551 CG ARG A 199 -5.313 -21.726 25.955 1.00 41.25 C ANISOU 1551 CG ARG A 199 5139 4337 6197 1385 -636 532 C ATOM 1552 CD ARG A 199 -5.940 -21.690 27.352 1.00 49.71 C ANISOU 1552 CD ARG A 199 6318 5413 7158 1295 -763 653 C ATOM 1553 NE ARG A 199 -5.074 -21.027 28.330 1.00 59.35 N ANISOU 1553 NE ARG A 199 7422 6728 8401 1329 -883 711 N ATOM 1554 CZ ARG A 199 -4.293 -21.666 29.197 1.00 67.47 C ANISOU 1554 CZ ARG A 199 8447 7689 9498 1435 -1028 792 C ATOM 1555 NH1 ARG A 199 -4.269 -22.994 29.223 1.00 71.09 N ANISOU 1555 NH1 ARG A 199 9021 7976 10015 1522 -1070 829 N ATOM 1556 NH2 ARG A 199 -3.533 -20.980 30.041 1.00 69.46 N ANISOU 1556 NH2 ARG A 199 8588 8041 9763 1453 -1142 836 N ATOM 1557 N ILE A 200 -7.304 -23.674 22.202 1.00 30.92 N ANISOU 1557 N ILE A 200 4147 2754 4846 1329 -260 251 N ATOM 1558 CA ILE A 200 -8.044 -24.688 21.441 1.00 33.64 C ANISOU 1558 CA ILE A 200 4654 2957 5172 1306 -205 194 C ATOM 1559 C ILE A 200 -7.154 -25.321 20.366 1.00 33.60 C ANISOU 1559 C ILE A 200 4615 2871 5280 1456 -117 82 C ATOM 1560 O ILE A 200 -7.065 -26.550 20.246 1.00 37.02 O ANISOU 1560 O ILE A 200 5159 3126 5780 1537 -135 65 O ATOM 1561 CB ILE A 200 -9.312 -24.075 20.814 1.00 33.85 C ANISOU 1561 CB ILE A 200 4740 3064 5059 1137 -129 153 C ATOM 1562 CG1 ILE A 200 -10.417 -23.833 21.857 1.00 30.83 C ANISOU 1562 CG1 ILE A 200 4434 2713 4568 991 -208 256 C ATOM 1563 CG2 ILE A 200 -9.817 -24.964 19.681 1.00 33.86 C ANISOU 1563 CG2 ILE A 200 4869 2943 5053 1130 -50 56 C ATOM 1564 CD1 ILE A 200 -11.589 -22.948 21.328 1.00 27.58 C ANISOU 1564 CD1 ILE A 200 4030 2419 4031 834 -141 218 C ATOM 1565 N PHE A 201 -6.495 -24.488 19.553 1.00 32.72 N ANISOU 1565 N PHE A 201 4355 2886 5191 1491 -14 -1 N ATOM 1566 CA PHE A 201 -5.680 -25.022 18.465 1.00 33.58 C ANISOU 1566 CA PHE A 201 4427 2936 5395 1625 95 -120 C ATOM 1567 C PHE A 201 -4.425 -25.715 18.981 1.00 34.90 C ANISOU 1567 C PHE A 201 4507 3020 5733 1818 32 -99 C ATOM 1568 O PHE A 201 -3.992 -26.717 18.400 1.00 36.30 O ANISOU 1568 O PHE A 201 4731 3061 6002 1945 78 -176 O ATOM 1569 CB PHE A 201 -5.334 -23.907 17.482 1.00 35.51 C ANISOU 1569 CB PHE A 201 4541 3347 5606 1596 230 -204 C ATOM 1570 CG PHE A 201 -6.537 -23.323 16.800 1.00 35.05 C ANISOU 1570 CG PHE A 201 4576 3353 5387 1428 293 -236 C ATOM 1571 CD1 PHE A 201 -7.346 -24.116 16.002 1.00 35.77 C ANISOU 1571 CD1 PHE A 201 4837 3335 5419 1389 340 -306 C ATOM 1572 CD2 PHE A 201 -6.877 -21.995 16.977 1.00 34.26 C ANISOU 1572 CD2 PHE A 201 4400 3417 5202 1312 293 -195 C ATOM 1573 CE1 PHE A 201 -8.476 -23.584 15.378 1.00 32.61 C ANISOU 1573 CE1 PHE A 201 4517 2998 4874 1235 381 -333 C ATOM 1574 CE2 PHE A 201 -8.003 -21.452 16.365 1.00 33.71 C ANISOU 1574 CE2 PHE A 201 4413 3403 4993 1169 337 -220 C ATOM 1575 CZ PHE A 201 -8.802 -22.251 15.562 1.00 33.44 C ANISOU 1575 CZ PHE A 201 4537 3269 4900 1131 378 -287 C ATOM 1576 N ALA A 202 -3.845 -25.226 20.080 1.00 35.21 N ANISOU 1576 N ALA A 202 4427 3132 5819 1845 -81 1 N ATOM 1577 CA ALA A 202 -2.730 -25.946 20.681 1.00 38.98 C ANISOU 1577 CA ALA A 202 4830 3522 6459 2028 -173 36 C ATOM 1578 C ALA A 202 -3.182 -27.309 21.194 1.00 40.86 C ANISOU 1578 C ALA A 202 5267 3541 6717 2070 -272 93 C ATOM 1579 O ALA A 202 -2.481 -28.309 21.013 1.00 41.92 O ANISOU 1579 O ALA A 202 5410 3549 6969 2221 -269 64 O ATOM 1580 CB ALA A 202 -2.100 -25.120 21.804 1.00 38.63 C ANISOU 1580 CB ALA A 202 4631 3603 6443 2030 -294 137 C ATOM 1581 N ALA A 203 -4.373 -27.375 21.801 1.00 40.06 N ANISOU 1581 N ALA A 203 5329 3408 6484 1915 -339 178 N ATOM 1582 CA ALA A 203 -4.872 -28.652 22.316 1.00 39.22 C ANISOU 1582 CA ALA A 203 5426 3091 6386 1928 -431 243 C ATOM 1583 C ALA A 203 -5.148 -29.646 21.187 1.00 39.50 C ANISOU 1583 C ALA A 203 5591 2964 6452 1969 -329 126 C ATOM 1584 O ALA A 203 -4.849 -30.835 21.315 1.00 43.35 O ANISOU 1584 O ALA A 203 6168 3277 7028 2064 -367 139 O ATOM 1585 CB ALA A 203 -6.131 -28.421 23.153 1.00 37.16 C ANISOU 1585 CB ALA A 203 5299 2853 5968 1732 -500 352 C ATOM 1586 N ALA A 204 -5.715 -29.174 20.074 1.00 39.01 N ANISOU 1586 N ALA A 204 5537 2981 6305 1873 -188 15 N ATOM 1587 CA ALA A 204 -5.927 -30.030 18.910 1.00 37.92 C ANISOU 1587 CA ALA A 204 5518 2706 6184 1909 -85 -115 C ATOM 1588 C ALA A 204 -4.609 -30.547 18.346 1.00 40.56 C ANISOU 1588 C ALA A 204 5753 2973 6683 2134 -27 -211 C ATOM 1589 O ALA A 204 -4.461 -31.749 18.092 1.00 41.68 O ANISOU 1589 O ALA A 204 5986 2951 6897 2188 -10 -243 O ATOM 1590 CB ALA A 204 -6.689 -29.263 17.833 1.00 37.95 C ANISOU 1590 CB ALA A 204 5527 2837 6054 1765 46 -211 C ATOM 1591 N ARG A 205 -3.648 -29.647 18.117 1.00 42.15 N ANISOU 1591 N ARG A 205 5734 3345 6938 2207 36 -248 N ATOM 1592 CA ARG A 205 -2.364 -30.052 17.547 1.00 50.24 C ANISOU 1592 CA ARG A 205 6627 4376 8087 2362 141 -319 C ATOM 1593 C ARG A 205 -1.669 -31.084 18.431 1.00 51.99 C ANISOU 1593 C ARG A 205 6858 4480 8414 2476 40 -219 C ATOM 1594 O ARG A 205 -1.094 -32.063 17.935 1.00 54.65 O ANISOU 1594 O ARG A 205 7223 4706 8835 2592 110 -277 O ATOM 1595 CB ARG A 205 -1.477 -28.819 17.338 1.00 55.89 C ANISOU 1595 CB ARG A 205 7109 5322 8804 2398 202 -348 C ATOM 1596 CG ARG A 205 -0.033 -29.146 16.982 1.00 67.96 C ANISOU 1596 CG ARG A 205 8500 6903 10418 2570 268 -400 C ATOM 1597 CD ARG A 205 0.873 -27.930 17.092 1.00 74.50 C ANISOU 1597 CD ARG A 205 9078 7961 11268 2571 283 -395 C ATOM 1598 NE ARG A 205 0.391 -26.983 18.094 1.00 79.63 N ANISOU 1598 NE ARG A 205 9677 8691 11886 2449 166 -278 N ATOM 1599 CZ ARG A 205 1.115 -25.986 18.594 1.00 83.43 C ANISOU 1599 CZ ARG A 205 9960 9345 12393 2434 129 -230 C ATOM 1600 NH1 ARG A 205 2.372 -25.815 18.196 1.00 86.28 N ANISOU 1600 NH1 ARG A 205 10144 9818 12821 2529 199 -283 N ATOM 1601 NH2 ARG A 205 0.587 -25.169 19.501 1.00 81.81 N ANISOU 1601 NH2 ARG A 205 9736 9201 12146 2321 19 -130 N ATOM 1602 N ARG A 206 -1.734 -30.892 19.747 1.00 51.54 N ANISOU 1602 N ARG A 206 6790 4446 8347 2443 -124 -69 N ATOM 1603 CA ARG A 206 -1.140 -31.840 20.682 1.00 51.45 C ANISOU 1603 CA ARG A 206 6803 4330 8417 2539 -236 39 C ATOM 1604 C ARG A 206 -1.843 -33.195 20.639 1.00 51.44 C ANISOU 1604 C ARG A 206 7027 4093 8424 2517 -257 46 C ATOM 1605 O ARG A 206 -1.187 -34.244 20.689 1.00 53.63 O ANISOU 1605 O ARG A 206 7327 4245 8805 2643 -261 53 O ATOM 1606 CB ARG A 206 -1.181 -31.235 22.080 1.00 54.26 C ANISOU 1606 CB ARG A 206 7114 4777 8726 2478 -403 193 C ATOM 1607 CG ARG A 206 -0.838 -32.148 23.206 1.00 63.00 C ANISOU 1607 CG ARG A 206 8284 5778 9876 2537 -543 325 C ATOM 1608 CD ARG A 206 -0.892 -31.364 24.507 1.00 73.27 C ANISOU 1608 CD ARG A 206 9534 7201 11102 2459 -692 461 C ATOM 1609 NE ARG A 206 -0.380 -32.144 25.630 1.00 84.32 N ANISOU 1609 NE ARG A 206 10972 8528 12537 2527 -830 588 N ATOM 1610 CZ ARG A 206 0.119 -31.612 26.742 1.00 87.60 C ANISOU 1610 CZ ARG A 206 11297 9060 12927 2524 -958 692 C ATOM 1611 NH1 ARG A 206 0.175 -30.289 26.874 1.00 86.09 N ANISOU 1611 NH1 ARG A 206 10970 9060 12681 2453 -962 682 N ATOM 1612 NH2 ARG A 206 0.573 -32.401 27.713 1.00 89.44 N ANISOU 1612 NH2 ARG A 206 11579 9216 13188 2590 -1082 803 N ATOM 1613 N GLN A 207 -3.174 -33.202 20.550 1.00 48.30 N ANISOU 1613 N GLN A 207 6801 3634 7918 2356 -274 46 N ATOM 1614 CA GLN A 207 -3.902 -34.467 20.551 1.00 46.83 C ANISOU 1614 CA GLN A 207 6833 3232 7728 2307 -303 58 C ATOM 1615 C GLN A 207 -3.669 -35.256 19.267 1.00 47.58 C ANISOU 1615 C GLN A 207 6966 3213 7898 2381 -165 -103 C ATOM 1616 O GLN A 207 -3.573 -36.491 19.300 1.00 49.81 O ANISOU 1616 O GLN A 207 7358 3313 8256 2434 -182 -98 O ATOM 1617 CB GLN A 207 -5.392 -34.213 20.764 1.00 44.85 C ANISOU 1617 CB GLN A 207 6750 2967 7325 2104 -349 98 C ATOM 1618 CG GLN A 207 -5.767 -33.961 22.208 1.00 47.13 C ANISOU 1618 CG GLN A 207 7073 3291 7543 2018 -498 278 C ATOM 1619 CD GLN A 207 -7.215 -33.546 22.353 1.00 51.38 C ANISOU 1619 CD GLN A 207 7752 3845 7924 1813 -518 312 C ATOM 1620 OE1 GLN A 207 -8.090 -34.068 21.655 1.00 55.66 O ANISOU 1620 OE1 GLN A 207 8442 4284 8420 1721 -462 243 O ATOM 1621 NE2 GLN A 207 -7.478 -32.583 23.245 1.00 49.26 N ANISOU 1621 NE2 GLN A 207 7434 3714 7570 1735 -594 415 N ATOM 1622 N LEU A 208 -3.589 -34.571 18.129 1.00 48.77 N ANISOU 1622 N LEU A 208 7035 3470 8027 2380 -27 -248 N ATOM 1623 CA LEU A 208 -3.338 -35.242 16.851 1.00 50.78 C ANISOU 1623 CA LEU A 208 7316 3636 8342 2440 112 -416 C ATOM 1624 C LEU A 208 -1.921 -35.787 16.784 1.00 51.17 C ANISOU 1624 C LEU A 208 7239 3657 8549 2644 172 -430 C ATOM 1625 O LEU A 208 -1.717 -36.941 16.397 1.00 54.84 O ANISOU 1625 O LEU A 208 7788 3949 9101 2716 208 -488 O ATOM 1626 CB LEU A 208 -3.580 -34.287 15.681 1.00 55.34 C ANISOU 1626 CB LEU A 208 7833 4360 8834 2378 240 -565 C ATOM 1627 CG LEU A 208 -5.031 -33.890 15.361 1.00 57.82 C ANISOU 1627 CG LEU A 208 8315 4692 8962 2190 228 -586 C ATOM 1628 CD1 LEU A 208 -5.079 -32.559 14.617 1.00 57.56 C ANISOU 1628 CD1 LEU A 208 8181 4869 8820 2147 334 -663 C ATOM 1629 CD2 LEU A 208 -5.731 -34.986 14.539 1.00 60.04 C ANISOU 1629 CD2 LEU A 208 8794 4804 9213 2131 264 -692 C ATOM 1630 N ALA A1001 -0.894 -35.209 17.461 1.00 72.93 N ANISOU 1630 N ALA A1001 10343 3720 13648 661 -323 -1235 N ATOM 1631 CA ALA A1001 0.469 -35.633 17.759 1.00 72.31 C ANISOU 1631 CA ALA A1001 10011 3652 13811 275 -324 -1228 C ATOM 1632 C ALA A1001 0.457 -36.907 18.592 1.00 70.73 C ANISOU 1632 C ALA A1001 9450 3798 13628 343 -329 -1354 C ATOM 1633 O ALA A1001 1.084 -37.898 18.219 1.00 67.35 O ANISOU 1633 O ALA A1001 8714 3540 13336 178 -199 -1246 O ATOM 1634 CB ALA A1001 1.237 -34.533 18.475 1.00 76.10 C ANISOU 1634 CB ALA A1001 10715 3821 14379 47 -534 -1336 C ATOM 1635 N ASP A1002 -0.277 -36.893 19.708 1.00 69.17 N ANISOU 1635 N ASP A1002 9320 3697 13264 618 -452 -1571 N ATOM 1636 CA ASP A1002 -0.340 -38.079 20.559 1.00 66.67 C ANISOU 1636 CA ASP A1002 8709 3707 12915 699 -449 -1686 C ATOM 1637 C ASP A1002 -0.971 -39.261 19.833 1.00 68.54 C ANISOU 1637 C ASP A1002 8684 4303 13056 805 -263 -1514 C ATOM 1638 O ASP A1002 -0.556 -40.409 20.031 1.00 66.77 O ANISOU 1638 O ASP A1002 8182 4366 12821 702 -213 -1488 O ATOM 1639 CB ASP A1002 -1.102 -37.771 21.846 1.00 67.84 C ANISOU 1639 CB ASP A1002 9042 3879 12854 1025 -559 -1919 C ATOM 1640 CG ASP A1002 -0.365 -36.788 22.738 1.00 83.23 C ANISOU 1640 CG ASP A1002 11303 5531 14787 895 -801 -2096 C ATOM 1641 OD1 ASP A1002 0.731 -36.327 22.346 1.00 83.96 O ANISOU 1641 OD1 ASP A1002 11406 5402 15092 514 -903 -2023 O ATOM 1642 OD2 ASP A1002 -0.883 -36.460 23.830 1.00 84.63 O ANISOU 1642 OD2 ASP A1002 11733 5693 14731 1176 -887 -2288 O ATOM 1643 N LEU A1003 -1.986 -39.012 19.002 1.00 69.24 N ANISOU 1643 N LEU A1003 8881 4359 13070 1017 -201 -1399 N ATOM 1644 CA LEU A1003 -2.535 -40.093 18.192 1.00 68.45 C ANISOU 1644 CA LEU A1003 8584 4530 12893 1069 -100 -1221 C ATOM 1645 C LEU A1003 -1.469 -40.684 17.283 1.00 73.08 C ANISOU 1645 C LEU A1003 9094 5115 13559 780 13 -1059 C ATOM 1646 O LEU A1003 -1.363 -41.909 17.145 1.00 67.01 O ANISOU 1646 O LEU A1003 8122 4614 12723 740 72 -990 O ATOM 1647 CB LEU A1003 -3.714 -39.590 17.359 1.00 67.89 C ANISOU 1647 CB LEU A1003 8672 4361 12761 1322 -122 -1111 C ATOM 1648 CG LEU A1003 -5.112 -39.495 17.970 1.00 67.44 C ANISOU 1648 CG LEU A1003 8541 4465 12617 1695 -170 -1167 C ATOM 1649 CD1 LEU A1003 -5.979 -38.701 17.038 1.00 64.35 C ANISOU 1649 CD1 LEU A1003 8352 3891 12206 1904 -229 -1049 C ATOM 1650 CD2 LEU A1003 -5.715 -40.880 18.197 1.00 60.20 C ANISOU 1650 CD2 LEU A1003 7269 3963 11641 1731 -145 -1090 C ATOM 1651 N GLU A1004 -0.660 -39.824 16.660 1.00 78.21 N ANISOU 1651 N GLU A1004 9920 5449 14345 588 63 -980 N ATOM 1652 CA GLU A1004 0.370 -40.302 15.746 1.00 82.14 C ANISOU 1652 CA GLU A1004 10346 5942 14922 355 246 -785 C ATOM 1653 C GLU A1004 1.522 -40.969 16.495 1.00 78.28 C ANISOU 1653 C GLU A1004 9543 5633 14567 142 266 -841 C ATOM 1654 O GLU A1004 2.119 -41.925 15.985 1.00 72.65 O ANISOU 1654 O GLU A1004 8668 5092 13843 71 427 -705 O ATOM 1655 CB GLU A1004 0.873 -39.140 14.885 1.00 90.36 C ANISOU 1655 CB GLU A1004 11653 6591 16089 208 332 -644 C ATOM 1656 CG GLU A1004 1.177 -39.516 13.437 1.00 95.87 C ANISOU 1656 CG GLU A1004 12466 7244 16715 173 576 -372 C ATOM 1657 CD GLU A1004 0.012 -40.222 12.741 1.00 96.82 C ANISOU 1657 CD GLU A1004 12726 7499 16563 452 532 -317 C ATOM 1658 OE1 GLU A1004 0.271 -41.184 11.984 1.00 95.83 O ANISOU 1658 OE1 GLU A1004 12603 7498 16309 460 675 -172 O ATOM 1659 OE2 GLU A1004 -1.157 -39.819 12.948 1.00 97.19 O ANISOU 1659 OE2 GLU A1004 12885 7515 16528 673 339 -411 O ATOM 1660 N ASP A1005 1.830 -40.492 17.706 1.00 77.10 N ANISOU 1660 N ASP A1005 9339 5431 14523 70 83 -1042 N ATOM 1661 CA ASP A1005 2.868 -41.118 18.518 1.00 74.34 C ANISOU 1661 CA ASP A1005 8696 5249 14300 -110 26 -1111 C ATOM 1662 C ASP A1005 2.513 -42.559 18.860 1.00 68.84 C ANISOU 1662 C ASP A1005 7805 4941 13412 45 60 -1143 C ATOM 1663 O ASP A1005 3.357 -43.454 18.759 1.00 68.22 O ANISOU 1663 O ASP A1005 7490 5039 13390 -62 147 -1062 O ATOM 1664 CB ASP A1005 3.097 -40.310 19.794 1.00 77.69 C ANISOU 1664 CB ASP A1005 9205 5502 14810 -173 -253 -1347 C ATOM 1665 CG ASP A1005 3.868 -39.033 19.539 1.00 86.62 C ANISOU 1665 CG ASP A1005 10473 6229 16209 -451 -336 -1294 C ATOM 1666 OD1 ASP A1005 4.431 -38.895 18.429 1.00 89.34 O ANISOU 1666 OD1 ASP A1005 10752 6479 16712 -631 -125 -1045 O ATOM 1667 OD2 ASP A1005 3.906 -38.164 20.443 1.00 91.39 O ANISOU 1667 OD2 ASP A1005 11287 6587 16851 -486 -610 -1489 O ATOM 1668 N ASN A1006 1.270 -42.805 19.285 1.00 65.95 N ANISOU 1668 N ASN A1006 7526 4705 12827 302 -3 -1242 N ATOM 1669 CA ASN A1006 0.899 -44.156 19.703 1.00 64.42 C ANISOU 1669 CA ASN A1006 7161 4852 12463 411 10 -1258 C ATOM 1670 C ASN A1006 0.918 -45.125 18.527 1.00 58.99 C ANISOU 1670 C ASN A1006 6434 4279 11701 401 163 -1049 C ATOM 1671 O ASN A1006 1.335 -46.279 18.675 1.00 59.82 O ANISOU 1671 O ASN A1006 6391 4597 11741 376 195 -1024 O ATOM 1672 CB ASN A1006 -0.474 -44.141 20.376 1.00 68.75 C ANISOU 1672 CB ASN A1006 7774 5511 12836 673 -54 -1356 C ATOM 1673 CG ASN A1006 -0.404 -43.705 21.828 1.00 74.26 C ANISOU 1673 CG ASN A1006 8526 6191 13498 745 -184 -1586 C ATOM 1674 OD1 ASN A1006 0.472 -44.145 22.579 1.00 79.95 O ANISOU 1674 OD1 ASN A1006 9151 6984 14242 625 -267 -1682 O ATOM 1675 ND2 ASN A1006 -1.320 -42.840 22.232 1.00 71.82 N ANISOU 1675 ND2 ASN A1006 8403 5772 13113 975 -212 -1676 N ATOM 1676 N TRP A1007 0.469 -44.668 17.358 1.00 55.08 N ANISOU 1676 N TRP A1007 6130 3615 11182 444 239 -903 N ATOM 1677 CA TRP A1007 0.557 -45.455 16.134 1.00 56.05 C ANISOU 1677 CA TRP A1007 6336 3767 11194 453 369 -704 C ATOM 1678 C TRP A1007 2.008 -45.790 15.788 1.00 56.64 C ANISOU 1678 C TRP A1007 6302 3841 11377 296 559 -604 C ATOM 1679 O TRP A1007 2.315 -46.931 15.428 1.00 57.20 O ANISOU 1679 O TRP A1007 6344 4066 11323 337 649 -519 O ATOM 1680 CB TRP A1007 -0.119 -44.680 15.002 1.00 59.79 C ANISOU 1680 CB TRP A1007 7101 3999 11618 538 385 -579 C ATOM 1681 CG TRP A1007 -0.124 -45.338 13.652 1.00 58.95 C ANISOU 1681 CG TRP A1007 7212 3847 11339 586 487 -378 C ATOM 1682 CD1 TRP A1007 0.549 -44.925 12.535 1.00 59.98 C ANISOU 1682 CD1 TRP A1007 7570 3756 11464 542 693 -205 C ATOM 1683 CD2 TRP A1007 -0.866 -46.498 13.267 1.00 57.46 C ANISOU 1683 CD2 TRP A1007 7097 3802 10934 697 375 -321 C ATOM 1684 NE1 TRP A1007 0.283 -45.770 11.486 1.00 60.50 N ANISOU 1684 NE1 TRP A1007 7893 3815 11280 660 723 -61 N ATOM 1685 CE2 TRP A1007 -0.585 -46.741 11.910 1.00 59.15 C ANISOU 1685 CE2 TRP A1007 7639 3851 10984 740 494 -137 C ATOM 1686 CE3 TRP A1007 -1.733 -47.362 13.943 1.00 57.39 C ANISOU 1686 CE3 TRP A1007 6929 4025 10852 752 183 -390 C ATOM 1687 CZ2 TRP A1007 -1.141 -47.806 11.217 1.00 62.53 C ANISOU 1687 CZ2 TRP A1007 8287 4309 11162 839 368 -50 C ATOM 1688 CZ3 TRP A1007 -2.288 -48.413 13.254 1.00 59.59 C ANISOU 1688 CZ3 TRP A1007 7363 4344 10933 804 60 -280 C ATOM 1689 CH2 TRP A1007 -1.989 -48.632 11.904 1.00 62.41 C ANISOU 1689 CH2 TRP A1007 8095 4506 11114 848 125 -126 C ATOM 1690 N GLU A1008 2.915 -44.815 15.905 1.00 60.42 N ANISOU 1690 N GLU A1008 6713 4143 12102 120 617 -597 N ATOM 1691 CA GLU A1008 4.324 -45.070 15.616 1.00 66.20 C ANISOU 1691 CA GLU A1008 7243 4898 13011 -37 817 -461 C ATOM 1692 C GLU A1008 4.939 -46.037 16.619 1.00 68.68 C ANISOU 1692 C GLU A1008 7250 5483 13364 -57 730 -570 C ATOM 1693 O GLU A1008 5.690 -46.938 16.232 1.00 70.29 O ANISOU 1693 O GLU A1008 7323 5830 13553 -28 906 -445 O ATOM 1694 CB GLU A1008 5.113 -43.769 15.608 1.00 71.16 C ANISOU 1694 CB GLU A1008 7819 5264 13953 -277 848 -408 C ATOM 1695 CG GLU A1008 4.762 -42.836 14.489 1.00 78.02 C ANISOU 1695 CG GLU A1008 9011 5837 14795 -275 988 -248 C ATOM 1696 CD GLU A1008 5.345 -41.459 14.714 1.00 89.70 C ANISOU 1696 CD GLU A1008 10487 7015 16582 -535 931 -235 C ATOM 1697 OE1 GLU A1008 6.416 -41.372 15.361 1.00 93.70 O ANISOU 1697 OE1 GLU A1008 10667 7551 17383 -773 881 -241 O ATOM 1698 OE2 GLU A1008 4.729 -40.466 14.262 1.00 94.53 O ANISOU 1698 OE2 GLU A1008 11429 7341 17148 -508 898 -215 O ATOM 1699 N THR A1009 4.652 -45.856 17.910 1.00 68.33 N ANISOU 1699 N THR A1009 7125 5493 13344 -72 467 -800 N ATOM 1700 CA THR A1009 5.169 -46.780 18.917 1.00 67.74 C ANISOU 1700 CA THR A1009 6817 5656 13265 -68 350 -913 C ATOM 1701 C THR A1009 4.707 -48.206 18.647 1.00 65.27 C ANISOU 1701 C THR A1009 6554 5574 12673 116 423 -865 C ATOM 1702 O THR A1009 5.495 -49.157 18.746 1.00 65.20 O ANISOU 1702 O THR A1009 6381 5729 12662 135 479 -822 O ATOM 1703 CB THR A1009 4.737 -46.331 20.312 1.00 69.11 C ANISOU 1703 CB THR A1009 7024 5816 13418 -57 64 -1169 C ATOM 1704 OG1 THR A1009 5.506 -45.188 20.702 1.00 75.96 O ANISOU 1704 OG1 THR A1009 7841 6454 14567 -267 -76 -1226 O ATOM 1705 CG2 THR A1009 4.935 -47.449 21.327 1.00 66.03 C ANISOU 1705 CG2 THR A1009 6501 5681 12907 16 -60 -1286 C ATOM 1706 N LEU A1010 3.434 -48.372 18.294 1.00 61.29 N ANISOU 1706 N LEU A1010 6275 5069 11943 251 401 -860 N ATOM 1707 CA LEU A1010 2.919 -49.698 17.980 1.00 57.40 C ANISOU 1707 CA LEU A1010 5873 4741 11196 380 413 -797 C ATOM 1708 C LEU A1010 3.709 -50.340 16.838 1.00 55.18 C ANISOU 1708 C LEU A1010 5664 4440 10862 416 633 -606 C ATOM 1709 O LEU A1010 4.176 -51.477 16.956 1.00 49.12 O ANISOU 1709 O LEU A1010 4856 3823 9985 486 661 -586 O ATOM 1710 CB LEU A1010 1.427 -49.586 17.657 1.00 56.76 C ANISOU 1710 CB LEU A1010 5983 4623 10960 477 319 -780 C ATOM 1711 CG LEU A1010 0.620 -50.680 16.967 1.00 57.34 C ANISOU 1711 CG LEU A1010 6230 4758 10797 565 270 -664 C ATOM 1712 CD1 LEU A1010 0.808 -52.021 17.625 1.00 56.49 C ANISOU 1712 CD1 LEU A1010 6050 4856 10559 577 211 -699 C ATOM 1713 CD2 LEU A1010 -0.851 -50.283 16.987 1.00 57.60 C ANISOU 1713 CD2 LEU A1010 6311 4776 10800 626 118 -662 C ATOM 1714 N ASN A1011 3.914 -49.606 15.741 1.00 58.49 N ANISOU 1714 N ASN A1011 6223 4660 11339 398 812 -456 N ATOM 1715 CA ASN A1011 4.600 -50.191 14.591 1.00 59.98 C ANISOU 1715 CA ASN A1011 6553 4815 11421 493 1079 -254 C ATOM 1716 C ASN A1011 6.102 -50.354 14.828 1.00 59.45 C ANISOU 1716 C ASN A1011 6160 4851 11579 442 1277 -186 C ATOM 1717 O ASN A1011 6.711 -51.306 14.320 1.00 56.07 O ANISOU 1717 O ASN A1011 5775 4508 11022 597 1469 -66 O ATOM 1718 CB ASN A1011 4.334 -49.345 13.350 1.00 64.21 C ANISOU 1718 CB ASN A1011 7385 5094 11917 511 1233 -95 C ATOM 1719 CG ASN A1011 2.919 -49.517 12.830 1.00 67.55 C ANISOU 1719 CG ASN A1011 8161 5428 12075 622 1031 -106 C ATOM 1720 OD1 ASN A1011 2.324 -50.592 12.960 1.00 67.34 O ANISOU 1720 OD1 ASN A1011 8228 5518 11839 708 865 -145 O ATOM 1721 ND2 ASN A1011 2.369 -48.459 12.239 1.00 70.80 N ANISOU 1721 ND2 ASN A1011 8768 5620 12513 611 1016 -56 N ATOM 1722 N ASP A1012 6.717 -49.445 15.588 1.00 59.95 N ANISOU 1722 N ASP A1012 5902 4894 11981 241 1212 -252 N ATOM 1723 CA ASP A1012 8.131 -49.588 15.919 1.00 60.56 C ANISOU 1723 CA ASP A1012 5582 5086 12343 161 1328 -178 C ATOM 1724 C ASP A1012 8.376 -50.827 16.769 1.00 58.20 C ANISOU 1724 C ASP A1012 5140 5037 11938 282 1183 -295 C ATOM 1725 O ASP A1012 9.312 -51.593 16.518 1.00 60.17 O ANISOU 1725 O ASP A1012 5225 5419 12219 401 1371 -168 O ATOM 1726 CB ASP A1012 8.626 -48.341 16.647 1.00 61.96 C ANISOU 1726 CB ASP A1012 5487 5146 12911 -122 1169 -245 C ATOM 1727 CG ASP A1012 8.694 -47.146 15.744 1.00 69.18 C ANISOU 1727 CG ASP A1012 6512 5795 13980 -263 1360 -74 C ATOM 1728 OD1 ASP A1012 8.897 -47.359 14.529 1.00 71.04 O ANISOU 1728 OD1 ASP A1012 6892 5989 14110 -148 1716 163 O ATOM 1729 OD2 ASP A1012 8.541 -46.004 16.241 1.00 73.85 O ANISOU 1729 OD2 ASP A1012 7101 6194 14764 -467 1156 -174 O ATOM 1730 N ASN A1013 7.550 -51.034 17.790 1.00 56.97 N ANISOU 1730 N ASN A1013 5055 4944 11648 279 869 -523 N ATOM 1731 CA ASN A1013 7.786 -52.154 18.692 1.00 58.58 C ANISOU 1731 CA ASN A1013 5155 5358 11745 377 714 -634 C ATOM 1732 C ASN A1013 7.485 -53.490 18.030 1.00 57.38 C ANISOU 1732 C ASN A1013 5265 5285 11251 605 833 -546 C ATOM 1733 O ASN A1013 8.067 -54.509 18.417 1.00 59.89 O ANISOU 1733 O ASN A1013 5501 5755 11500 729 812 -556 O ATOM 1734 CB ASN A1013 6.975 -51.965 19.972 1.00 59.49 C ANISOU 1734 CB ASN A1013 5316 5502 11786 323 393 -875 C ATOM 1735 CG ASN A1013 7.696 -51.086 20.978 1.00 62.29 C ANISOU 1735 CG ASN A1013 5415 5812 12441 149 187 -1003 C ATOM 1736 OD1 ASN A1013 8.878 -51.297 21.252 1.00 67.70 O ANISOU 1736 OD1 ASN A1013 5803 6575 13345 103 158 -965 O ATOM 1737 ND2 ASN A1013 7.004 -50.090 21.513 1.00 59.00 N ANISOU 1737 ND2 ASN A1013 5124 5255 12040 66 24 -1146 N ATOM 1738 N LEU A1014 6.594 -53.513 17.038 1.00 53.82 N ANISOU 1738 N LEU A1014 5166 4706 10575 671 919 -460 N ATOM 1739 CA LEU A1014 6.437 -54.714 16.226 1.00 53.95 C ANISOU 1739 CA LEU A1014 5507 4725 10265 881 1016 -354 C ATOM 1740 C LEU A1014 7.736 -55.064 15.512 1.00 55.40 C ANISOU 1740 C LEU A1014 5613 4936 10499 1043 1348 -175 C ATOM 1741 O LEU A1014 8.126 -56.239 15.454 1.00 53.77 O ANISOU 1741 O LEU A1014 5517 4817 10096 1252 1394 -145 O ATOM 1742 CB LEU A1014 5.305 -54.530 15.219 1.00 54.66 C ANISOU 1742 CB LEU A1014 6003 4629 10135 905 996 -284 C ATOM 1743 CG LEU A1014 3.916 -54.874 15.742 1.00 55.01 C ANISOU 1743 CG LEU A1014 6183 4696 10022 847 679 -396 C ATOM 1744 CD1 LEU A1014 2.838 -54.362 14.790 1.00 56.12 C ANISOU 1744 CD1 LEU A1014 6616 4647 10059 837 615 -318 C ATOM 1745 CD2 LEU A1014 3.806 -56.377 15.919 1.00 53.47 C ANISOU 1745 CD2 LEU A1014 6175 4581 9558 954 564 -400 C ATOM 1746 N LYS A1015 8.428 -54.057 14.973 1.00 56.96 N ANISOU 1746 N LYS A1015 5622 5057 10964 963 1601 -36 N ATOM 1747 CA LYS A1015 9.707 -54.312 14.314 1.00 60.33 C ANISOU 1747 CA LYS A1015 5892 5540 11492 1125 1987 183 C ATOM 1748 C LYS A1015 10.755 -54.807 15.307 1.00 64.73 C ANISOU 1748 C LYS A1015 5977 6329 12290 1144 1919 138 C ATOM 1749 O LYS A1015 11.581 -55.666 14.974 1.00 61.95 O ANISOU 1749 O LYS A1015 5577 6089 11873 1407 2152 269 O ATOM 1750 CB LYS A1015 10.194 -53.047 13.615 1.00 61.62 C ANISOU 1750 CB LYS A1015 5903 5567 11941 978 2273 373 C ATOM 1751 CG LYS A1015 9.354 -52.616 12.441 1.00 64.90 C ANISOU 1751 CG LYS A1015 6831 5738 12092 1030 2398 467 C ATOM 1752 CD LYS A1015 9.927 -51.336 11.834 1.00 74.50 C ANISOU 1752 CD LYS A1015 7891 6808 13609 865 2694 672 C ATOM 1753 CE LYS A1015 9.066 -50.804 10.691 1.00 80.30 C ANISOU 1753 CE LYS A1015 9175 7268 14070 920 2786 761 C ATOM 1754 NZ LYS A1015 8.933 -51.815 9.594 1.00 84.31 N ANISOU 1754 NZ LYS A1015 10211 7716 14106 1280 3003 885 N ATOM 1755 N VAL A1016 10.746 -54.258 16.524 1.00 64.84 N ANISOU 1755 N VAL A1016 5668 6401 12566 898 1592 -44 N ATOM 1756 CA VAL A1016 11.703 -54.671 17.551 1.00 64.55 C ANISOU 1756 CA VAL A1016 5205 6561 12760 901 1436 -105 C ATOM 1757 C VAL A1016 11.542 -56.158 17.854 1.00 61.45 C ANISOU 1757 C VAL A1016 5042 6294 12011 1176 1342 -185 C ATOM 1758 O VAL A1016 12.525 -56.905 17.931 1.00 61.14 O ANISOU 1758 O VAL A1016 4792 6406 12034 1382 1445 -100 O ATOM 1759 CB VAL A1016 11.527 -53.806 18.816 1.00 60.03 C ANISOU 1759 CB VAL A1016 4412 5964 12434 605 1035 -322 C ATOM 1760 CG1 VAL A1016 12.395 -54.311 19.945 1.00 61.74 C ANISOU 1760 CG1 VAL A1016 4278 6357 12824 623 782 -415 C ATOM 1761 CG2 VAL A1016 11.848 -52.344 18.517 1.00 62.40 C ANISOU 1761 CG2 VAL A1016 4496 6100 13112 323 1107 -227 C ATOM 1762 N ILE A1017 10.294 -56.609 18.013 1.00 55.64 N ANISOU 1762 N ILE A1017 4737 5490 10914 1186 1143 -329 N ATOM 1763 CA ILE A1017 10.015 -58.015 18.304 1.00 57.00 C ANISOU 1763 CA ILE A1017 5193 5733 10733 1398 1019 -394 C ATOM 1764 C ILE A1017 10.499 -58.906 17.167 1.00 56.55 C ANISOU 1764 C ILE A1017 5395 5647 10445 1723 1333 -207 C ATOM 1765 O ILE A1017 11.121 -59.951 17.403 1.00 59.13 O ANISOU 1765 O ILE A1017 5732 6077 10656 1969 1341 -195 O ATOM 1766 CB ILE A1017 8.509 -58.218 18.572 1.00 51.03 C ANISOU 1766 CB ILE A1017 4813 4888 9686 1291 770 -526 C ATOM 1767 CG1 ILE A1017 8.105 -57.555 19.893 1.00 49.84 C ANISOU 1767 CG1 ILE A1017 4446 4796 9697 1070 486 -720 C ATOM 1768 CG2 ILE A1017 8.151 -59.713 18.554 1.00 50.15 C ANISOU 1768 CG2 ILE A1017 5089 4781 9185 1484 674 -531 C ATOM 1769 CD1 ILE A1017 6.611 -57.375 20.056 1.00 49.28 C ANISOU 1769 CD1 ILE A1017 4628 4650 9446 953 334 -796 C ATOM 1770 N GLU A1018 10.229 -58.503 15.919 1.00 56.72 N ANISOU 1770 N GLU A1018 5679 5509 10365 1767 1596 -58 N ATOM 1771 CA GLU A1018 10.577 -59.330 14.769 1.00 61.06 C ANISOU 1771 CA GLU A1018 6612 5980 10606 2121 1903 115 C ATOM 1772 C GLU A1018 12.072 -59.600 14.705 1.00 68.68 C ANISOU 1772 C GLU A1018 7196 7118 11781 2372 2229 273 C ATOM 1773 O GLU A1018 12.494 -60.733 14.444 1.00 75.22 O ANISOU 1773 O GLU A1018 8265 7975 12342 2735 2345 327 O ATOM 1774 CB GLU A1018 10.100 -58.669 13.481 1.00 64.80 C ANISOU 1774 CB GLU A1018 7432 6237 10953 2118 2129 253 C ATOM 1775 CG GLU A1018 8.652 -58.939 13.168 1.00 68.25 C ANISOU 1775 CG GLU A1018 8420 6476 11035 2041 1830 157 C ATOM 1776 CD GLU A1018 8.005 -57.802 12.403 1.00 75.68 C ANISOU 1776 CD GLU A1018 9495 7236 12023 1882 1886 221 C ATOM 1777 OE1 GLU A1018 8.749 -56.944 11.874 1.00 80.68 O ANISOU 1777 OE1 GLU A1018 9927 7854 12875 1886 2235 376 O ATOM 1778 OE2 GLU A1018 6.755 -57.760 12.345 1.00 75.72 O ANISOU 1778 OE2 GLU A1018 9787 7115 11868 1748 1577 134 O ATOM 1779 N LYS A1019 12.893 -58.581 14.943 1.00 69.87 N ANISOU 1779 N LYS A1019 6745 7378 12424 2191 2367 363 N ATOM 1780 CA LYS A1019 14.335 -58.763 14.906 1.00 73.41 C ANISOU 1780 CA LYS A1019 6705 8021 13167 2399 2671 557 C ATOM 1781 C LYS A1019 14.935 -58.907 16.298 1.00 70.60 C ANISOU 1781 C LYS A1019 5818 7872 13135 2286 2323 419 C ATOM 1782 O LYS A1019 16.149 -58.752 16.466 1.00 72.92 O ANISOU 1782 O LYS A1019 5525 8344 13837 2341 2476 578 O ATOM 1783 CB LYS A1019 15.000 -57.619 14.142 1.00 80.53 C ANISOU 1783 CB LYS A1019 7255 8902 14441 2279 3084 822 C ATOM 1784 CG LYS A1019 14.698 -56.233 14.658 1.00 83.29 C ANISOU 1784 CG LYS A1019 7296 9175 15175 1786 2846 739 C ATOM 1785 CD LYS A1019 15.429 -55.198 13.815 1.00 91.61 C ANISOU 1785 CD LYS A1019 8039 10182 16585 1674 3290 1048 C ATOM 1786 CE LYS A1019 15.231 -55.465 12.326 1.00 95.37 C ANISOU 1786 CE LYS A1019 9062 10516 16660 1997 3792 1264 C ATOM 1787 NZ LYS A1019 16.009 -54.525 11.462 1.00101.23 N ANISOU 1787 NZ LYS A1019 9520 11217 17724 1924 4307 1616 N ATOM 1788 N ALA A1020 14.112 -59.212 17.293 1.00 65.35 N ANISOU 1788 N ALA A1020 5347 7186 12298 2140 1857 147 N ATOM 1789 CA ALA A1020 14.637 -59.553 18.602 1.00 65.74 C ANISOU 1789 CA ALA A1020 5044 7403 12532 2111 1508 4 C ATOM 1790 C ALA A1020 15.444 -60.849 18.520 1.00 78.17 C ANISOU 1790 C ALA A1020 6637 9113 13952 2555 1636 93 C ATOM 1791 O ALA A1020 15.284 -61.662 17.605 1.00 68.32 O ANISOU 1791 O ALA A1020 5850 7789 12321 2885 1907 191 O ATOM 1792 CB ALA A1020 13.502 -59.689 19.617 1.00 61.65 C ANISOU 1792 CB ALA A1020 4832 6817 11777 1914 1054 -279 C ATOM 1793 N ASP A1021 16.330 -61.032 19.496 1.00 78.06 N ANISOU 1793 N ASP A1021 6149 9282 14230 2583 1409 54 N ATOM 1794 CA ASP A1021 17.224 -62.175 19.510 1.00 82.06 C ANISOU 1794 CA ASP A1021 6581 9938 14661 3030 1513 148 C ATOM 1795 C ASP A1021 17.047 -63.085 20.713 1.00 79.58 C ANISOU 1795 C ASP A1021 6447 9660 14128 3109 1048 -80 C ATOM 1796 O ASP A1021 17.555 -64.207 20.689 1.00 83.22 O ANISOU 1796 O ASP A1021 7037 10191 14393 3524 1104 -32 O ATOM 1797 CB ASP A1021 18.681 -61.700 19.440 1.00 92.82 C ANISOU 1797 CB ASP A1021 7285 11547 16434 3004 1653 364 C ATOM 1798 CG ASP A1021 18.918 -60.760 18.278 1.00100.15 C ANISOU 1798 CG ASP A1021 8075 12439 17538 2870 2110 613 C ATOM 1799 OD1 ASP A1021 18.342 -61.003 17.195 1.00100.99 O ANISOU 1799 OD1 ASP A1021 8675 12392 17302 3066 2470 694 O ATOM 1800 OD2 ASP A1021 19.660 -59.771 18.449 1.00104.82 O ANISOU 1800 OD2 ASP A1021 8111 13121 18596 2560 2085 735 O ATOM 1801 N ASN A1022 16.343 -62.650 21.754 1.00 75.80 N ANISOU 1801 N ASN A1022 6027 9124 13650 2760 616 -315 N ATOM 1802 CA ASN A1022 16.068 -63.512 22.891 1.00 73.49 C ANISOU 1802 CA ASN A1022 5995 8839 13088 2831 206 -518 C ATOM 1803 C ASN A1022 14.697 -63.166 23.450 1.00 67.17 C ANISOU 1803 C ASN A1022 5588 7890 12042 2502 -42 -723 C ATOM 1804 O ASN A1022 14.113 -62.126 23.127 1.00 62.81 O ANISOU 1804 O ASN A1022 4996 7254 11614 2212 34 -731 O ATOM 1805 CB ASN A1022 17.148 -63.384 23.971 1.00 76.00 C ANISOU 1805 CB ASN A1022 5768 9323 13787 2838 -125 -562 C ATOM 1806 CG ASN A1022 17.371 -61.950 24.400 1.00 74.60 C ANISOU 1806 CG ASN A1022 5104 9146 14095 2423 -307 -599 C ATOM 1807 OD1 ASN A1022 16.473 -61.307 24.946 1.00 69.58 O ANISOU 1807 OD1 ASN A1022 4695 8382 13362 2114 -531 -784 O ATOM 1808 ND2 ASN A1022 18.575 -61.442 24.159 1.00 76.05 N ANISOU 1808 ND2 ASN A1022 4686 9476 14735 2392 -208 -400 N ATOM 1809 N ALA A1023 14.192 -64.057 24.308 1.00 65.22 N ANISOU 1809 N ALA A1023 5721 7614 11445 2570 -324 -871 N ATOM 1810 CA ALA A1023 12.855 -63.879 24.864 1.00 61.22 C ANISOU 1810 CA ALA A1023 5585 6992 10684 2305 -506 -1025 C ATOM 1811 C ALA A1023 12.756 -62.605 25.689 1.00 62.05 C ANISOU 1811 C ALA A1023 5391 7107 11079 1992 -719 -1159 C ATOM 1812 O ALA A1023 11.693 -61.970 25.722 1.00 61.70 O ANISOU 1812 O ALA A1023 5521 6970 10954 1760 -713 -1225 O ATOM 1813 CB ALA A1023 12.471 -65.096 25.705 1.00 60.70 C ANISOU 1813 CB ALA A1023 5947 6898 10217 2440 -745 -1119 C ATOM 1814 N ALA A1024 13.851 -62.196 26.338 1.00 63.15 N ANISOU 1814 N ALA A1024 5088 7341 11563 1991 -926 -1194 N ATOM 1815 CA ALA A1024 13.809 -60.992 27.161 1.00 61.34 C ANISOU 1815 CA ALA A1024 4656 7066 11584 1700 -1196 -1338 C ATOM 1816 C ALA A1024 13.566 -59.741 26.320 1.00 65.12 C ANISOU 1816 C ALA A1024 4946 7461 12335 1451 -968 -1260 C ATOM 1817 O ALA A1024 12.846 -58.832 26.751 1.00 59.65 O ANISOU 1817 O ALA A1024 4367 6656 11640 1221 -1091 -1390 O ATOM 1818 CB ALA A1024 15.101 -60.850 27.962 1.00 65.40 C ANISOU 1818 CB ALA A1024 4738 7670 12443 1734 -1537 -1373 C ATOM 1819 N GLN A1025 14.177 -59.661 25.132 1.00 66.70 N ANISOU 1819 N GLN A1025 4884 7704 12756 1522 -621 -1039 N ATOM 1820 CA GLN A1025 13.950 -58.506 24.266 1.00 62.18 C ANISOU 1820 CA GLN A1025 4184 7029 12412 1297 -380 -939 C ATOM 1821 C GLN A1025 12.503 -58.457 23.798 1.00 62.67 C ANISOU 1821 C GLN A1025 4738 6962 12111 1240 -241 -985 C ATOM 1822 O GLN A1025 11.866 -57.399 23.829 1.00 57.26 O ANISOU 1822 O GLN A1025 4092 6156 11507 1006 -277 -1051 O ATOM 1823 CB GLN A1025 14.895 -58.538 23.066 1.00 64.98 C ANISOU 1823 CB GLN A1025 4209 7458 13023 1432 24 -658 C ATOM 1824 CG GLN A1025 16.329 -58.176 23.400 1.00 72.79 C ANISOU 1824 CG GLN A1025 4540 8572 14544 1388 -84 -549 C ATOM 1825 CD GLN A1025 17.315 -58.610 22.329 1.00 73.14 C ANISOU 1825 CD GLN A1025 4263 8756 14769 1657 371 -240 C ATOM 1826 OE1 GLN A1025 16.973 -58.715 21.153 1.00 72.27 O ANISOU 1826 OE1 GLN A1025 4402 8591 14468 1785 814 -87 O ATOM 1827 NE2 GLN A1025 18.546 -58.866 22.737 1.00 77.44 N ANISOU 1827 NE2 GLN A1025 4417 9495 15514 1724 254 -132 N ATOM 1828 N VAL A1026 11.971 -59.600 23.353 1.00 61.77 N ANISOU 1828 N VAL A1026 5008 6857 11606 1457 -109 -942 N ATOM 1829 CA VAL A1026 10.566 -59.673 22.960 1.00 56.91 C ANISOU 1829 CA VAL A1026 4831 6124 10669 1387 -48 -968 C ATOM 1830 C VAL A1026 9.689 -59.127 24.076 1.00 55.11 C ANISOU 1830 C VAL A1026 4691 5864 10386 1191 -317 -1162 C ATOM 1831 O VAL A1026 8.816 -58.283 23.849 1.00 53.21 O ANISOU 1831 O VAL A1026 4529 5527 10160 1029 -273 -1184 O ATOM 1832 CB VAL A1026 10.186 -61.120 22.599 1.00 56.78 C ANISOU 1832 CB VAL A1026 5234 6097 10242 1617 2 -914 C ATOM 1833 CG1 VAL A1026 8.693 -61.228 22.377 1.00 54.95 C ANISOU 1833 CG1 VAL A1026 5398 5749 9731 1489 -33 -934 C ATOM 1834 CG2 VAL A1026 10.956 -61.590 21.364 1.00 54.13 C ANISOU 1834 CG2 VAL A1026 4917 5754 9896 1872 321 -718 C ATOM 1835 N LYS A1027 9.957 -59.568 25.312 1.00 58.10 N ANISOU 1835 N LYS A1027 5067 6317 10693 1238 -591 -1300 N ATOM 1836 CA LYS A1027 9.159 -59.156 26.464 1.00 59.52 C ANISOU 1836 CA LYS A1027 5401 6466 10750 1121 -813 -1479 C ATOM 1837 C LYS A1027 9.229 -57.650 26.691 1.00 60.76 C ANISOU 1837 C LYS A1027 5357 6531 11198 923 -892 -1566 C ATOM 1838 O LYS A1027 8.225 -57.020 27.046 1.00 58.44 O ANISOU 1838 O LYS A1027 5242 6163 10798 836 -911 -1654 O ATOM 1839 CB LYS A1027 9.619 -59.904 27.717 1.00 63.43 C ANISOU 1839 CB LYS A1027 5969 7033 11097 1243 -1096 -1599 C ATOM 1840 CG LYS A1027 8.985 -59.367 28.992 1.00 67.89 C ANISOU 1840 CG LYS A1027 6712 7552 11529 1164 -1314 -1786 C ATOM 1841 CD LYS A1027 9.614 -59.925 30.248 1.00 71.46 C ANISOU 1841 CD LYS A1027 7251 8044 11856 1289 -1635 -1915 C ATOM 1842 CE LYS A1027 8.982 -59.294 31.479 1.00 71.86 C ANISOU 1842 CE LYS A1027 7554 8017 11730 1248 -1819 -2099 C ATOM 1843 NZ LYS A1027 9.499 -59.895 32.737 1.00 74.69 N ANISOU 1843 NZ LYS A1027 8106 8387 11887 1394 -2145 -2226 N ATOM 1844 N ASP A1028 10.407 -57.056 26.505 1.00 67.74 N ANISOU 1844 N ASP A1028 5869 7408 12460 854 -941 -1528 N ATOM 1845 CA ASP A1028 10.549 -55.618 26.712 1.00 72.36 C ANISOU 1845 CA ASP A1028 6297 7857 13341 631 -1063 -1601 C ATOM 1846 C ASP A1028 9.622 -54.842 25.787 1.00 67.01 C ANISOU 1846 C ASP A1028 5746 7061 12655 531 -804 -1530 C ATOM 1847 O ASP A1028 8.850 -53.986 26.235 1.00 67.13 O ANISOU 1847 O ASP A1028 5933 6955 12616 443 -896 -1657 O ATOM 1848 CB ASP A1028 12.006 -55.201 26.502 1.00 83.71 C ANISOU 1848 CB ASP A1028 7254 9308 15244 534 -1138 -1502 C ATOM 1849 CG ASP A1028 12.872 -55.467 27.723 1.00 92.31 C ANISOU 1849 CG ASP A1028 8200 10447 16426 560 -1565 -1633 C ATOM 1850 OD1 ASP A1028 12.594 -54.870 28.785 1.00 95.28 O ANISOU 1850 OD1 ASP A1028 8769 10699 16736 467 -1905 -1844 O ATOM 1851 OD2 ASP A1028 13.823 -56.274 27.626 1.00 95.86 O ANISOU 1851 OD2 ASP A1028 8379 11047 16994 705 -1571 -1526 O ATOM 1852 N ALA A1029 9.673 -55.139 24.488 1.00 62.84 N ANISOU 1852 N ALA A1029 5175 6552 12149 581 -482 -1328 N ATOM 1853 CA ALA A1029 8.818 -54.436 23.542 1.00 59.35 C ANISOU 1853 CA ALA A1029 4882 5983 11684 505 -266 -1249 C ATOM 1854 C ALA A1029 7.339 -54.693 23.825 1.00 57.02 C ANISOU 1854 C ALA A1029 4935 5682 11049 558 -296 -1333 C ATOM 1855 O ALA A1029 6.518 -53.774 23.738 1.00 57.62 O ANISOU 1855 O ALA A1029 5112 5643 11136 479 -283 -1372 O ATOM 1856 CB ALA A1029 9.185 -54.843 22.115 1.00 58.83 C ANISOU 1856 CB ALA A1029 4791 5926 11638 597 71 -1013 C ATOM 1857 N LEU A1030 6.984 -55.927 24.196 1.00 48.65 N ANISOU 1857 N LEU A1030 4045 4740 9701 691 -338 -1345 N ATOM 1858 CA LEU A1030 5.577 -56.254 24.414 1.00 50.86 C ANISOU 1858 CA LEU A1030 4590 5031 9703 712 -343 -1364 C ATOM 1859 C LEU A1030 4.997 -55.494 25.602 1.00 51.50 C ANISOU 1859 C LEU A1030 4714 5094 9758 677 -490 -1536 C ATOM 1860 O LEU A1030 3.834 -55.073 25.566 1.00 50.04 O ANISOU 1860 O LEU A1030 4642 4881 9492 670 -426 -1528 O ATOM 1861 CB LEU A1030 5.405 -57.762 24.613 1.00 49.72 C ANISOU 1861 CB LEU A1030 4629 4989 9274 827 -375 -1318 C ATOM 1862 CG LEU A1030 5.428 -58.664 23.370 1.00 47.26 C ANISOU 1862 CG LEU A1030 4469 4645 8841 905 -232 -1143 C ATOM 1863 CD1 LEU A1030 5.614 -60.116 23.780 1.00 45.19 C ANISOU 1863 CD1 LEU A1030 4394 4451 8325 1030 -322 -1130 C ATOM 1864 CD2 LEU A1030 4.163 -58.501 22.529 1.00 43.97 C ANISOU 1864 CD2 LEU A1030 4235 4138 8333 832 -165 -1041 C ATOM 1865 N THR A1031 5.784 -55.313 26.666 1.00 55.86 N ANISOU 1865 N THR A1031 5200 5656 10369 683 -696 -1686 N ATOM 1866 CA THR A1031 5.279 -54.593 27.831 1.00 60.73 C ANISOU 1866 CA THR A1031 5959 6219 10898 700 -842 -1864 C ATOM 1867 C THR A1031 5.008 -53.130 27.501 1.00 62.66 C ANISOU 1867 C THR A1031 6182 6290 11335 609 -814 -1905 C ATOM 1868 O THR A1031 4.030 -52.549 27.990 1.00 62.81 O ANISOU 1868 O THR A1031 6382 6262 11220 680 -790 -1981 O ATOM 1869 CB THR A1031 6.263 -54.700 28.990 1.00 67.43 C ANISOU 1869 CB THR A1031 6803 7066 11750 729 -1137 -2024 C ATOM 1870 OG1 THR A1031 7.548 -54.260 28.546 1.00 78.16 O ANISOU 1870 OG1 THR A1031 7862 8365 13469 606 -1243 -1998 O ATOM 1871 CG2 THR A1031 6.364 -56.132 29.484 1.00 62.66 C ANISOU 1871 CG2 THR A1031 6307 6613 10889 858 -1178 -2000 C ATOM 1872 N LYS A1032 5.861 -52.516 26.675 1.00 63.69 N ANISOU 1872 N LYS A1032 6102 6318 11778 471 -796 -1836 N ATOM 1873 CA LYS A1032 5.566 -51.168 26.202 1.00 65.47 C ANISOU 1873 CA LYS A1032 6350 6349 12178 373 -752 -1841 C ATOM 1874 C LYS A1032 4.293 -51.149 25.368 1.00 64.41 C ANISOU 1874 C LYS A1032 6338 6224 11910 445 -516 -1725 C ATOM 1875 O LYS A1032 3.447 -50.261 25.537 1.00 68.54 O ANISOU 1875 O LYS A1032 7005 6640 12397 490 -508 -1788 O ATOM 1876 CB LYS A1032 6.734 -50.614 25.388 1.00 70.17 C ANISOU 1876 CB LYS A1032 6682 6836 13142 188 -730 -1731 C ATOM 1877 CG LYS A1032 7.973 -50.253 26.193 1.00 75.73 C ANISOU 1877 CG LYS A1032 7206 7475 14095 55 -1034 -1833 C ATOM 1878 CD LYS A1032 9.107 -49.862 25.263 1.00 79.67 C ANISOU 1878 CD LYS A1032 7352 7917 15003 -139 -938 -1642 C ATOM 1879 CE LYS A1032 10.307 -49.363 26.031 1.00 87.23 C ANISOU 1879 CE LYS A1032 8068 8783 16292 -330 -1296 -1714 C ATOM 1880 NZ LYS A1032 11.350 -48.815 25.116 1.00 93.00 N ANISOU 1880 NZ LYS A1032 8404 9446 17485 -561 -1169 -1481 N ATOM 1881 N MET A1033 4.140 -52.117 24.458 1.00 58.92 N ANISOU 1881 N MET A1033 5611 5639 11136 474 -352 -1553 N ATOM 1882 CA MET A1033 2.953 -52.150 23.608 1.00 55.76 C ANISOU 1882 CA MET A1033 5328 5230 10629 519 -204 -1429 C ATOM 1883 C MET A1033 1.687 -52.278 24.433 1.00 50.15 C ANISOU 1883 C MET A1033 4728 4609 9718 627 -231 -1486 C ATOM 1884 O MET A1033 0.651 -51.693 24.092 1.00 49.01 O ANISOU 1884 O MET A1033 4631 4418 9572 674 -166 -1439 O ATOM 1885 CB MET A1033 3.036 -53.304 22.611 1.00 57.95 C ANISOU 1885 CB MET A1033 5638 5578 10804 541 -95 -1254 C ATOM 1886 CG MET A1033 4.027 -53.082 21.508 1.00 61.48 C ANISOU 1886 CG MET A1033 6013 5928 11418 494 43 -1135 C ATOM 1887 SD MET A1033 4.172 -54.517 20.438 1.00 62.31 S ANISOU 1887 SD MET A1033 6276 6085 11313 603 169 -954 S ATOM 1888 CE MET A1033 2.705 -54.329 19.444 1.00 60.20 C ANISOU 1888 CE MET A1033 6266 5702 10907 607 179 -844 C ATOM 1889 N ARG A1034 1.749 -53.048 25.517 1.00 50.41 N ANISOU 1889 N ARG A1034 4794 4776 9583 687 -311 -1566 N ATOM 1890 CA ARG A1034 0.554 -53.285 26.312 1.00 51.44 C ANISOU 1890 CA ARG A1034 5015 5017 9515 799 -269 -1569 C ATOM 1891 C ARG A1034 0.098 -52.013 27.012 1.00 56.47 C ANISOU 1891 C ARG A1034 5734 5558 10165 908 -270 -1708 C ATOM 1892 O ARG A1034 -1.095 -51.690 27.008 1.00 57.93 O ANISOU 1892 O ARG A1034 5928 5782 10301 1017 -146 -1642 O ATOM 1893 CB ARG A1034 0.810 -54.393 27.326 1.00 51.57 C ANISOU 1893 CB ARG A1034 5104 5171 9320 844 -336 -1610 C ATOM 1894 CG ARG A1034 -0.446 -54.884 27.963 1.00 52.77 C ANISOU 1894 CG ARG A1034 5320 5459 9269 931 -227 -1529 C ATOM 1895 CD ARG A1034 -0.160 -55.802 29.102 1.00 55.18 C ANISOU 1895 CD ARG A1034 5764 5863 9341 991 -284 -1583 C ATOM 1896 NE ARG A1034 -1.381 -56.484 29.492 1.00 58.92 N ANISOU 1896 NE ARG A1034 6261 6478 9648 1024 -132 -1420 N ATOM 1897 CZ ARG A1034 -2.250 -56.007 30.369 1.00 65.96 C ANISOU 1897 CZ ARG A1034 7203 7433 10426 1177 21 -1427 C ATOM 1898 NH1 ARG A1034 -2.028 -54.834 30.953 1.00 70.80 N ANISOU 1898 NH1 ARG A1034 7925 7943 11031 1330 6 -1623 N ATOM 1899 NH2 ARG A1034 -3.344 -56.700 30.655 1.00 69.05 N ANISOU 1899 NH2 ARG A1034 7548 7976 10714 1180 194 -1221 N ATOM 1900 N ALA A1035 1.037 -51.276 27.612 1.00 58.78 N ANISOU 1900 N ALA A1035 6094 5711 10530 890 -427 -1893 N ATOM 1901 CA ALA A1035 0.697 -49.990 28.216 1.00 61.04 C ANISOU 1901 CA ALA A1035 6553 5832 10806 1004 -467 -2045 C ATOM 1902 C ALA A1035 0.179 -49.005 27.173 1.00 59.60 C ANISOU 1902 C ALA A1035 6338 5509 10798 987 -369 -1964 C ATOM 1903 O ALA A1035 -0.807 -48.300 27.415 1.00 60.92 O ANISOU 1903 O ALA A1035 6621 5635 10889 1172 -280 -1988 O ATOM 1904 CB ALA A1035 1.913 -49.417 28.947 1.00 61.90 C ANISOU 1904 CB ALA A1035 6765 5763 10991 929 -744 -2249 C ATOM 1905 N ALA A1036 0.825 -48.943 26.002 1.00 58.35 N ANISOU 1905 N ALA A1036 6041 5271 10857 799 -365 -1856 N ATOM 1906 CA ALA A1036 0.375 -48.025 24.958 1.00 59.93 C ANISOU 1906 CA ALA A1036 6261 5311 11198 785 -280 -1767 C ATOM 1907 C ALA A1036 -1.010 -48.393 24.428 1.00 66.08 C ANISOU 1907 C ALA A1036 7005 6223 11878 917 -134 -1611 C ATOM 1908 O ALA A1036 -1.792 -47.497 24.076 1.00 69.19 O ANISOU 1908 O ALA A1036 7468 6508 12314 1028 -90 -1588 O ATOM 1909 CB ALA A1036 1.378 -47.989 23.809 1.00 57.07 C ANISOU 1909 CB ALA A1036 5786 4845 11052 575 -258 -1650 C ATOM 1910 N ALA A1037 -1.334 -49.692 24.364 1.00 61.37 N ANISOU 1910 N ALA A1037 6307 5845 11167 902 -90 -1493 N ATOM 1911 CA ALA A1037 -2.659 -50.106 23.905 1.00 61.82 C ANISOU 1911 CA ALA A1037 6292 6024 11173 978 -14 -1319 C ATOM 1912 C ALA A1037 -3.747 -49.596 24.839 1.00 65.66 C ANISOU 1912 C ALA A1037 6772 6591 11583 1202 70 -1358 C ATOM 1913 O ALA A1037 -4.739 -49.015 24.391 1.00 68.62 O ANISOU 1913 O ALA A1037 7095 6948 12028 1322 122 -1264 O ATOM 1914 CB ALA A1037 -2.736 -51.630 23.785 1.00 59.05 C ANISOU 1914 CB ALA A1037 5874 5852 10711 884 -29 -1189 C ATOM 1915 N LEU A1038 -3.585 -49.822 26.146 1.00 67.67 N ANISOU 1915 N LEU A1038 7095 6936 11679 1297 93 -1483 N ATOM 1916 CA LEU A1038 -4.565 -49.334 27.112 1.00 73.95 C ANISOU 1916 CA LEU A1038 7935 7807 12354 1571 235 -1514 C ATOM 1917 C LEU A1038 -4.625 -47.813 27.110 1.00 82.10 C ANISOU 1917 C LEU A1038 9144 8605 13444 1739 222 -1653 C ATOM 1918 O LEU A1038 -5.703 -47.222 27.237 1.00 85.96 O ANISOU 1918 O LEU A1038 9614 9128 13920 1995 365 -1598 O ATOM 1919 CB LEU A1038 -4.217 -49.853 28.503 1.00 74.22 C ANISOU 1919 CB LEU A1038 8115 7934 12151 1654 254 -1637 C ATOM 1920 CG LEU A1038 -3.939 -51.352 28.547 1.00 74.07 C ANISOU 1920 CG LEU A1038 7995 8091 12056 1475 228 -1525 C ATOM 1921 CD1 LEU A1038 -3.474 -51.780 29.925 1.00 74.36 C ANISOU 1921 CD1 LEU A1038 8240 8176 11838 1571 212 -1664 C ATOM 1922 CD2 LEU A1038 -5.185 -52.112 28.139 1.00 76.27 C ANISOU 1922 CD2 LEU A1038 8035 8575 12369 1455 371 -1248 C ATOM 1923 N ASP A1039 -3.468 -47.166 26.962 1.00 86.03 N ANISOU 1923 N ASP A1039 9808 8856 14025 1600 48 -1817 N ATOM 1924 CA ASP A1039 -3.416 -45.712 26.872 1.00 90.90 C ANISOU 1924 CA ASP A1039 10645 9185 14710 1703 -13 -1943 C ATOM 1925 C ASP A1039 -4.178 -45.199 25.655 1.00 89.33 C ANISOU 1925 C ASP A1039 10348 8926 14666 1738 55 -1780 C ATOM 1926 O ASP A1039 -4.769 -44.114 25.707 1.00 91.61 O ANISOU 1926 O ASP A1039 10797 9060 14951 1967 87 -1830 O ATOM 1927 CB ASP A1039 -1.952 -45.265 26.837 1.00 96.25 C ANISOU 1927 CB ASP A1039 11449 9612 15512 1452 -241 -2091 C ATOM 1928 CG ASP A1039 -1.793 -43.769 26.915 1.00105.38 C ANISOU 1928 CG ASP A1039 12899 10415 16725 1515 -359 -2238 C ATOM 1929 OD1 ASP A1039 -2.130 -43.183 27.967 1.00109.42 O ANISOU 1929 OD1 ASP A1039 13706 10826 17042 1771 -391 -2410 O ATOM 1930 OD2 ASP A1039 -1.311 -43.180 25.924 1.00108.32 O ANISOU 1930 OD2 ASP A1039 13254 10584 17317 1317 -416 -2174 O ATOM 1931 N ALA A1040 -4.185 -45.961 24.556 1.00 84.67 N ANISOU 1931 N ALA A1040 9548 8436 14188 1544 59 -1589 N ATOM 1932 CA ALA A1040 -4.973 -45.586 23.386 1.00 82.60 C ANISOU 1932 CA ALA A1040 9224 8117 14041 1588 79 -1422 C ATOM 1933 C ALA A1040 -6.431 -46.008 23.506 1.00 84.26 C ANISOU 1933 C ALA A1040 9217 8574 14223 1794 182 -1258 C ATOM 1934 O ALA A1040 -7.276 -45.505 22.754 1.00 84.68 O ANISOU 1934 O ALA A1040 9217 8581 14376 1915 170 -1135 O ATOM 1935 CB ALA A1040 -4.369 -46.187 22.115 1.00 76.67 C ANISOU 1935 CB ALA A1040 8424 7325 13383 1323 18 -1285 C ATOM 1936 N GLN A1041 -6.741 -46.918 24.432 1.00 84.83 N ANISOU 1936 N GLN A1041 9150 8904 14179 1833 275 -1231 N ATOM 1937 CA GLN A1041 -8.128 -47.295 24.668 1.00 88.34 C ANISOU 1937 CA GLN A1041 9328 9601 14637 2014 407 -1037 C ATOM 1938 C GLN A1041 -8.906 -46.156 25.313 1.00 94.96 C ANISOU 1938 C GLN A1041 10228 10409 15441 2411 565 -1097 C ATOM 1939 O GLN A1041 -10.102 -45.991 25.044 1.00 99.38 O ANISOU 1939 O GLN A1041 10544 11101 16116 2605 649 -908 O ATOM 1940 CB GLN A1041 -8.179 -48.551 25.537 1.00 87.34 C ANISOU 1940 CB GLN A1041 9072 9731 14382 1935 498 -974 C ATOM 1941 CG GLN A1041 -9.531 -49.227 25.590 1.00 87.96 C ANISOU 1941 CG GLN A1041 8793 10088 14541 1994 614 -692 C ATOM 1942 CD GLN A1041 -9.431 -50.700 25.943 1.00 84.83 C ANISOU 1942 CD GLN A1041 8290 9877 14065 1761 611 -571 C ATOM 1943 OE1 GLN A1041 -8.338 -51.240 26.097 1.00 81.88 O ANISOU 1943 OE1 GLN A1041 8120 9429 13563 1587 517 -709 O ATOM 1944 NE2 GLN A1041 -10.577 -51.359 26.065 1.00 86.69 N ANISOU 1944 NE2 GLN A1041 8193 10349 14396 1754 705 -294 N ATOM 1945 N LYS A1042 -8.246 -45.357 26.145 1.00 95.77 N ANISOU 1945 N LYS A1042 10669 10327 15394 2551 584 -1351 N ATOM 1946 CA LYS A1042 -8.880 -44.211 26.779 1.00 98.93 C ANISOU 1946 CA LYS A1042 11253 10633 15702 2975 723 -1443 C ATOM 1947 C LYS A1042 -9.128 -43.088 25.771 1.00 99.58 C ANISOU 1947 C LYS A1042 11428 10467 15942 3062 618 -1433 C ATOM 1948 O LYS A1042 -10.117 -42.354 25.865 1.00101.71 O ANISOU 1948 O LYS A1042 11682 10744 16218 3444 747 -1379 O ATOM 1949 CB LYS A1042 -8.017 -43.702 27.932 1.00101.53 C ANISOU 1949 CB LYS A1042 12020 10764 15791 3072 689 -1738 C ATOM 1950 CG LYS A1042 -7.682 -44.755 28.979 1.00103.05 C ANISOU 1950 CG LYS A1042 12209 11161 15786 3010 761 -1770 C ATOM 1951 CD LYS A1042 -6.833 -44.148 30.089 1.00106.30 C ANISOU 1951 CD LYS A1042 13117 11323 15948 3124 647 -2077 C ATOM 1952 CE LYS A1042 -6.490 -45.161 31.170 1.00106.56 C ANISOU 1952 CE LYS A1042 13212 11532 15746 3099 693 -2118 C ATOM 1953 NZ LYS A1042 -5.694 -44.529 32.263 1.00108.97 N ANISOU 1953 NZ LYS A1042 14057 11559 15788 3230 515 -2426 N ATOM 1954 N MET A1058 -18.722 -48.317 18.449 1.00108.21 N ANISOU 1954 N MET A1058 8863 13057 19194 2209 -1012 1371 N ATOM 1955 CA MET A1058 -17.997 -48.416 19.713 1.00107.13 C ANISOU 1955 CA MET A1058 8812 13026 18865 2285 -560 1193 C ATOM 1956 C MET A1058 -17.787 -49.869 20.128 1.00104.30 C ANISOU 1956 C MET A1058 8300 12802 18529 1901 -576 1315 C ATOM 1957 O MET A1058 -16.775 -50.210 20.747 1.00 99.73 O ANISOU 1957 O MET A1058 8029 12177 17687 1811 -379 1104 O ATOM 1958 CB MET A1058 -18.737 -47.661 20.821 1.00113.52 C ANISOU 1958 CB MET A1058 9420 14123 19592 2682 -118 1207 C ATOM 1959 CG MET A1058 -18.236 -46.243 21.053 1.00116.08 C ANISOU 1959 CG MET A1058 10139 14250 19716 3100 81 916 C ATOM 1960 SD MET A1058 -16.537 -46.189 21.668 1.00113.03 S ANISOU 1960 SD MET A1058 10278 13593 19075 3045 261 539 S ATOM 1961 CE MET A1058 -16.705 -47.012 23.252 1.00113.50 C ANISOU 1961 CE MET A1058 10114 14011 19000 3061 676 602 C ATOM 1962 N LYS A1059 -18.757 -50.723 19.795 1.00105.60 N ANISOU 1962 N LYS A1059 8110 13125 18887 1627 -824 1631 N ATOM 1963 CA LYS A1059 -18.629 -52.138 20.126 1.00100.58 C ANISOU 1963 CA LYS A1059 7370 12578 18269 1228 -888 1775 C ATOM 1964 C LYS A1059 -17.521 -52.796 19.310 1.00 94.03 C ANISOU 1964 C LYS A1059 7064 11421 17241 922 -1225 1601 C ATOM 1965 O LYS A1059 -16.756 -53.609 19.839 1.00 90.09 O ANISOU 1965 O LYS A1059 6795 10920 16517 730 -1102 1500 O ATOM 1966 CB LYS A1059 -19.972 -52.843 19.920 1.00102.08 C ANISOU 1966 CB LYS A1059 7128 12961 18695 975 -1101 2151 C ATOM 1967 CG LYS A1059 -21.028 -52.405 20.929 1.00105.57 C ANISOU 1967 CG LYS A1059 7135 13774 19202 1242 -657 2312 C ATOM 1968 CD LYS A1059 -22.419 -52.281 20.310 1.00109.40 C ANISOU 1968 CD LYS A1059 7215 14373 19978 1206 -917 2602 C ATOM 1969 CE LYS A1059 -23.368 -51.579 21.262 1.00112.60 C ANISOU 1969 CE LYS A1059 7227 15125 20430 1592 -437 2709 C ATOM 1970 NZ LYS A1059 -24.692 -51.308 20.641 1.00119.25 N ANISOU 1970 NZ LYS A1059 7647 16082 21581 1620 -680 2969 N ATOM 1971 N ASP A1060 -17.414 -52.452 18.021 1.00 93.59 N ANISOU 1971 N ASP A1060 7301 11082 17177 894 -1622 1551 N ATOM 1972 CA ASP A1060 -16.285 -52.924 17.224 1.00 92.05 C ANISOU 1972 CA ASP A1060 7738 10567 16671 685 -1839 1352 C ATOM 1973 C ASP A1060 -14.983 -52.282 17.679 1.00 91.26 C ANISOU 1973 C ASP A1060 8035 10371 16269 868 -1462 1005 C ATOM 1974 O ASP A1060 -13.912 -52.882 17.537 1.00 90.52 O ANISOU 1974 O ASP A1060 8344 10131 15918 703 -1464 852 O ATOM 1975 CB ASP A1060 -16.519 -52.640 15.738 1.00 93.59 C ANISOU 1975 CB ASP A1060 8198 10468 16892 660 -2319 1399 C ATOM 1976 CG ASP A1060 -17.808 -53.261 15.214 1.00 99.03 C ANISOU 1976 CG ASP A1060 8506 11212 17911 449 -2805 1747 C ATOM 1977 OD1 ASP A1060 -18.094 -54.429 15.549 1.00 99.96 O ANISOU 1977 OD1 ASP A1060 8439 11432 18110 127 -2931 1926 O ATOM 1978 OD2 ASP A1060 -18.540 -52.576 14.464 1.00102.29 O ANISOU 1978 OD2 ASP A1060 8804 11547 18513 596 -3093 1855 O ATOM 1979 N PHE A1061 -15.057 -51.064 18.220 1.00 93.18 N ANISOU 1979 N PHE A1061 8175 10681 16549 1216 -1159 889 N ATOM 1980 CA PHE A1061 -13.881 -50.414 18.789 1.00 90.39 C ANISOU 1980 CA PHE A1061 8159 10232 15953 1362 -839 576 C ATOM 1981 C PHE A1061 -13.395 -51.160 20.022 1.00 85.70 C ANISOU 1981 C PHE A1061 7514 9826 15222 1276 -569 507 C ATOM 1982 O PHE A1061 -12.214 -51.510 20.125 1.00 81.34 O ANISOU 1982 O PHE A1061 7299 9158 14450 1151 -524 316 O ATOM 1983 CB PHE A1061 -14.209 -48.953 19.124 1.00 94.40 C ANISOU 1983 CB PHE A1061 8607 10733 16529 1760 -630 482 C ATOM 1984 CG PHE A1061 -13.365 -48.361 20.237 1.00 94.75 C ANISOU 1984 CG PHE A1061 8847 10775 16381 1935 -271 213 C ATOM 1985 CD1 PHE A1061 -12.141 -47.773 19.962 1.00 91.91 C ANISOU 1985 CD1 PHE A1061 8934 10139 15851 1906 -260 -40 C ATOM 1986 CD2 PHE A1061 -13.815 -48.365 21.553 1.00 97.07 C ANISOU 1986 CD2 PHE A1061 8889 11327 16668 2133 45 233 C ATOM 1987 CE1 PHE A1061 -11.381 -47.220 20.978 1.00 91.33 C ANISOU 1987 CE1 PHE A1061 9043 10030 15628 2033 -17 -280 C ATOM 1988 CE2 PHE A1061 -13.049 -47.821 22.570 1.00 95.74 C ANISOU 1988 CE2 PHE A1061 8981 11111 16287 2304 308 -27 C ATOM 1989 CZ PHE A1061 -11.833 -47.247 22.281 1.00 92.89 C ANISOU 1989 CZ PHE A1061 9056 10456 15783 2237 239 -289 C ATOM 1990 N ARG A1062 -14.299 -51.402 20.976 1.00 88.18 N ANISOU 1990 N ARG A1062 7404 10435 15667 1363 -373 680 N ATOM 1991 CA ARG A1062 -13.927 -52.111 22.193 1.00 87.80 C ANISOU 1991 CA ARG A1062 7339 10559 15461 1307 -105 638 C ATOM 1992 C ARG A1062 -13.502 -53.539 21.887 1.00 79.07 C ANISOU 1992 C ARG A1062 6366 9408 14268 912 -330 712 C ATOM 1993 O ARG A1062 -12.618 -54.081 22.560 1.00 74.57 O ANISOU 1993 O ARG A1062 6023 8839 13470 840 -201 564 O ATOM 1994 CB ARG A1062 -15.093 -52.080 23.191 1.00 98.56 C ANISOU 1994 CB ARG A1062 8217 12249 16984 1501 191 868 C ATOM 1995 CG ARG A1062 -14.916 -52.980 24.412 1.00104.75 C ANISOU 1995 CG ARG A1062 8972 13223 17607 1419 461 906 C ATOM 1996 CD ARG A1062 -15.678 -52.460 25.631 1.00113.03 C ANISOU 1996 CD ARG A1062 9740 14538 18668 1795 925 1003 C ATOM 1997 NE ARG A1062 -15.094 -51.227 26.160 1.00116.07 N ANISOU 1997 NE ARG A1062 10468 14800 18832 2191 1142 679 N ATOM 1998 CZ ARG A1062 -13.995 -51.176 26.911 1.00114.77 C ANISOU 1998 CZ ARG A1062 10748 14519 18340 2234 1246 381 C ATOM 1999 NH1 ARG A1062 -13.347 -52.292 27.224 1.00113.16 N ANISOU 1999 NH1 ARG A1062 10688 14324 17982 1942 1184 363 N ATOM 2000 NH2 ARG A1062 -13.539 -50.008 27.344 1.00114.36 N ANISOU 2000 NH2 ARG A1062 11016 14317 18119 2570 1373 103 N ATOM 2001 N HIS A1063 -14.097 -54.154 20.861 1.00 74.05 N ANISOU 2001 N HIS A1063 5641 8702 13794 669 -705 931 N ATOM 2002 CA HIS A1063 -13.687 -55.502 20.493 1.00 67.07 C ANISOU 2002 CA HIS A1063 4982 7712 12789 316 -960 989 C ATOM 2003 C HIS A1063 -12.264 -55.514 19.957 1.00 59.85 C ANISOU 2003 C HIS A1063 4618 6537 11587 303 -1009 709 C ATOM 2004 O HIS A1063 -11.478 -56.396 20.311 1.00 56.87 O ANISOU 2004 O HIS A1063 4469 6135 11004 172 -976 630 O ATOM 2005 CB HIS A1063 -14.654 -56.102 19.471 1.00 68.66 C ANISOU 2005 CB HIS A1063 5037 7838 13214 62 -1420 1278 C ATOM 2006 CG HIS A1063 -14.486 -57.580 19.283 1.00 69.91 C ANISOU 2006 CG HIS A1063 5398 7896 13267 -306 -1691 1390 C ATOM 2007 ND1 HIS A1063 -14.227 -58.440 20.330 1.00 70.27 N ANISOU 2007 ND1 HIS A1063 5419 8082 13199 -425 -1476 1414 N ATOM 2008 CD2 HIS A1063 -14.530 -58.350 18.169 1.00 71.09 C ANISOU 2008 CD2 HIS A1063 5853 7784 13375 -563 -2176 1477 C ATOM 2009 CE1 HIS A1063 -14.124 -59.675 19.870 1.00 70.61 C ANISOU 2009 CE1 HIS A1063 5724 7953 13151 -746 -1816 1516 C ATOM 2010 NE2 HIS A1063 -14.304 -59.648 18.561 1.00 70.84 N ANISOU 2010 NE2 HIS A1063 5971 7731 13215 -832 -2249 1550 N ATOM 2011 N GLY A1064 -11.909 -54.535 19.120 1.00 56.26 N ANISOU 2011 N GLY A1064 4368 5890 11119 454 -1065 576 N ATOM 2012 CA GLY A1064 -10.585 -54.524 18.516 1.00 53.42 C ANISOU 2012 CA GLY A1064 4481 5292 10525 441 -1075 367 C ATOM 2013 C GLY A1064 -9.467 -54.371 19.529 1.00 51.27 C ANISOU 2013 C GLY A1064 4298 5084 10098 529 -761 133 C ATOM 2014 O GLY A1064 -8.417 -55.007 19.408 1.00 49.37 O ANISOU 2014 O GLY A1064 4333 4751 9673 441 -763 32 O ATOM 2015 N PHE A1065 -9.677 -53.536 20.549 1.00 51.99 N ANISOU 2015 N PHE A1065 4177 5324 10254 727 -505 48 N ATOM 2016 CA PHE A1065 -8.666 -53.394 21.593 1.00 52.19 C ANISOU 2016 CA PHE A1065 4313 5388 10128 805 -276 -176 C ATOM 2017 C PHE A1065 -8.638 -54.605 22.525 1.00 54.57 C ANISOU 2017 C PHE A1065 4560 5863 10309 688 -222 -121 C ATOM 2018 O PHE A1065 -7.558 -55.014 22.982 1.00 50.87 O ANISOU 2018 O PHE A1065 4290 5366 9673 656 -176 -278 O ATOM 2019 CB PHE A1065 -8.898 -52.102 22.368 1.00 53.98 C ANISOU 2019 CB PHE A1065 4447 5658 10407 1079 -61 -300 C ATOM 2020 CG PHE A1065 -8.324 -50.891 21.689 1.00 53.42 C ANISOU 2020 CG PHE A1065 4577 5345 10374 1174 -86 -449 C ATOM 2021 CD1 PHE A1065 -6.951 -50.732 21.595 1.00 50.52 C ANISOU 2021 CD1 PHE A1065 4460 4816 9918 1096 -79 -635 C ATOM 2022 CD2 PHE A1065 -9.150 -49.922 21.130 1.00 55.86 C ANISOU 2022 CD2 PHE A1065 4812 5584 10829 1337 -121 -379 C ATOM 2023 CE1 PHE A1065 -6.408 -49.636 20.962 1.00 52.21 C ANISOU 2023 CE1 PHE A1065 4848 4796 10194 1139 -88 -732 C ATOM 2024 CE2 PHE A1065 -8.613 -48.812 20.499 1.00 55.64 C ANISOU 2024 CE2 PHE A1065 5016 5301 10822 1409 -143 -501 C ATOM 2025 CZ PHE A1065 -7.241 -48.669 20.413 1.00 55.57 C ANISOU 2025 CZ PHE A1065 5259 5125 10731 1291 -118 -669 C ATOM 2026 N ASP A1066 -9.806 -55.194 22.807 1.00 52.55 N ANISOU 2026 N ASP A1066 4027 5783 10156 617 -234 122 N ATOM 2027 CA ASP A1066 -9.857 -56.473 23.512 1.00 52.81 C ANISOU 2027 CA ASP A1066 4045 5941 10081 449 -217 231 C ATOM 2028 C ASP A1066 -8.987 -57.512 22.823 1.00 50.78 C ANISOU 2028 C ASP A1066 4121 5506 9666 239 -451 196 C ATOM 2029 O ASP A1066 -8.170 -58.183 23.464 1.00 52.99 O ANISOU 2029 O ASP A1066 4587 5798 9750 215 -390 91 O ATOM 2030 CB ASP A1066 -11.297 -56.979 23.593 1.00 60.05 C ANISOU 2030 CB ASP A1066 4582 7030 11203 326 -254 569 C ATOM 2031 CG ASP A1066 -12.093 -56.313 24.689 1.00 69.32 C ANISOU 2031 CG ASP A1066 5423 8452 12463 573 99 642 C ATOM 2032 OD1 ASP A1066 -11.471 -55.712 25.598 1.00 71.76 O ANISOU 2032 OD1 ASP A1066 5893 8786 12588 816 356 412 O ATOM 2033 OD2 ASP A1066 -13.345 -56.398 24.645 1.00 76.48 O ANISOU 2033 OD2 ASP A1066 5915 9522 13621 537 111 941 O ATOM 2034 N ILE A1067 -9.171 -57.677 21.512 1.00 50.76 N ANISOU 2034 N ILE A1067 4233 5326 9726 117 -728 287 N ATOM 2035 CA ILE A1067 -8.317 -58.579 20.748 1.00 49.27 C ANISOU 2035 CA ILE A1067 4440 4935 9345 -7 -926 245 C ATOM 2036 C ILE A1067 -6.858 -58.175 20.900 1.00 49.09 C ANISOU 2036 C ILE A1067 4635 4845 9171 150 -749 -19 C ATOM 2037 O ILE A1067 -5.988 -59.011 21.181 1.00 49.31 O ANISOU 2037 O ILE A1067 4871 4850 9015 126 -742 -92 O ATOM 2038 CB ILE A1067 -8.739 -58.603 19.269 1.00 50.10 C ANISOU 2038 CB ILE A1067 4714 4821 9501 -94 -1242 363 C ATOM 2039 CG1 ILE A1067 -10.221 -58.957 19.132 1.00 53.79 C ANISOU 2039 CG1 ILE A1067 4893 5357 10188 -279 -1484 648 C ATOM 2040 CG2 ILE A1067 -7.894 -59.614 18.506 1.00 49.18 C ANISOU 2040 CG2 ILE A1067 5081 4478 9128 -170 -1419 329 C ATOM 2041 CD1 ILE A1067 -10.745 -58.906 17.696 1.00 54.55 C ANISOU 2041 CD1 ILE A1067 5165 5218 10343 -358 -1876 766 C ATOM 2042 N LEU A1068 -6.575 -56.877 20.746 1.00 46.52 N ANISOU 2042 N LEU A1068 4248 4484 8942 311 -617 -151 N ATOM 2043 CA LEU A1068 -5.197 -56.402 20.746 1.00 44.97 C ANISOU 2043 CA LEU A1068 4212 4202 8675 412 -486 -361 C ATOM 2044 C LEU A1068 -4.500 -56.703 22.067 1.00 44.44 C ANISOU 2044 C LEU A1068 4105 4269 8509 456 -355 -502 C ATOM 2045 O LEU A1068 -3.387 -57.248 22.089 1.00 43.49 O ANISOU 2045 O LEU A1068 4143 4106 8274 456 -356 -589 O ATOM 2046 CB LEU A1068 -5.159 -54.905 20.464 1.00 47.43 C ANISOU 2046 CB LEU A1068 4456 4432 9133 538 -389 -450 C ATOM 2047 CG LEU A1068 -3.721 -54.423 20.308 1.00 44.29 C ANISOU 2047 CG LEU A1068 4193 3916 8718 579 -282 -614 C ATOM 2048 CD1 LEU A1068 -3.215 -54.862 18.953 1.00 43.97 C ANISOU 2048 CD1 LEU A1068 4408 3702 8598 538 -342 -526 C ATOM 2049 CD2 LEU A1068 -3.610 -52.908 20.505 1.00 44.96 C ANISOU 2049 CD2 LEU A1068 4206 3927 8951 679 -179 -734 C ATOM 2050 N VAL A1069 -5.133 -56.345 23.184 1.00 45.45 N ANISOU 2050 N VAL A1069 4043 4556 8669 528 -239 -520 N ATOM 2051 CA VAL A1069 -4.490 -56.569 24.472 1.00 50.10 C ANISOU 2051 CA VAL A1069 4667 5243 9124 597 -142 -665 C ATOM 2052 C VAL A1069 -4.371 -58.064 24.755 1.00 49.79 C ANISOU 2052 C VAL A1069 4746 5259 8913 480 -221 -572 C ATOM 2053 O VAL A1069 -3.347 -58.531 25.271 1.00 44.49 O ANISOU 2053 O VAL A1069 4217 4583 8106 514 -236 -698 O ATOM 2054 CB VAL A1069 -5.248 -55.819 25.581 1.00 52.01 C ANISOU 2054 CB VAL A1069 4764 5616 9380 756 30 -697 C ATOM 2055 CG1 VAL A1069 -4.637 -56.111 26.937 1.00 51.86 C ANISOU 2055 CG1 VAL A1069 4868 5671 9164 844 99 -843 C ATOM 2056 CG2 VAL A1069 -5.202 -54.305 25.301 1.00 53.08 C ANISOU 2056 CG2 VAL A1069 4874 5640 9655 896 78 -823 C ATOM 2057 N GLY A1070 -5.401 -58.840 24.401 1.00 48.12 N ANISOU 2057 N GLY A1070 4484 5081 8721 333 -307 -340 N ATOM 2058 CA GLY A1070 -5.315 -60.276 24.568 1.00 46.16 C ANISOU 2058 CA GLY A1070 4407 4826 8305 193 -419 -235 C ATOM 2059 C GLY A1070 -4.172 -60.887 23.779 1.00 51.83 C ANISOU 2059 C GLY A1070 5424 5372 8894 192 -555 -318 C ATOM 2060 O GLY A1070 -3.499 -61.813 24.254 1.00 44.52 O ANISOU 2060 O GLY A1070 4692 4441 7783 203 -589 -359 O ATOM 2061 N GLN A1071 -3.941 -60.390 22.560 1.00 44.13 N ANISOU 2061 N GLN A1071 4516 4251 7999 211 -616 -329 N ATOM 2062 CA GLN A1071 -2.865 -60.943 21.748 1.00 43.37 C ANISOU 2062 CA GLN A1071 4716 3998 7765 266 -679 -379 C ATOM 2063 C GLN A1071 -1.496 -60.543 22.277 1.00 42.58 C ANISOU 2063 C GLN A1071 4572 3945 7659 426 -530 -578 C ATOM 2064 O GLN A1071 -0.543 -61.320 22.149 1.00 47.92 O ANISOU 2064 O GLN A1071 5437 4574 8196 504 -549 -612 O ATOM 2065 CB GLN A1071 -3.024 -60.520 20.290 1.00 43.51 C ANISOU 2065 CB GLN A1071 4864 3834 7833 266 -753 -311 C ATOM 2066 CG GLN A1071 -4.194 -61.187 19.568 1.00 51.30 C ANISOU 2066 CG GLN A1071 5991 4707 8793 94 -1019 -105 C ATOM 2067 CD GLN A1071 -4.402 -60.632 18.169 1.00 50.57 C ANISOU 2067 CD GLN A1071 6067 4419 8730 124 -1121 -51 C ATOM 2068 OE1 GLN A1071 -4.278 -59.421 17.940 1.00 47.74 O ANISOU 2068 OE1 GLN A1071 5553 4070 8515 221 -976 -119 O ATOM 2069 NE2 GLN A1071 -4.704 -61.511 17.226 1.00 46.55 N ANISOU 2069 NE2 GLN A1071 5934 3694 8058 47 -1392 70 N ATOM 2070 N ILE A1072 -1.377 -59.355 22.882 1.00 42.48 N ANISOU 2070 N ILE A1072 4323 4014 7805 484 -408 -704 N ATOM 2071 CA ILE A1072 -0.135 -58.972 23.557 1.00 42.38 C ANISOU 2071 CA ILE A1072 4241 4039 7823 589 -343 -886 C ATOM 2072 C ILE A1072 0.102 -59.853 24.781 1.00 42.71 C ANISOU 2072 C ILE A1072 4347 4190 7692 622 -395 -941 C ATOM 2073 O ILE A1072 1.221 -60.309 25.027 1.00 42.83 O ANISOU 2073 O ILE A1072 4417 4208 7649 706 -434 -1023 O ATOM 2074 CB ILE A1072 -0.175 -57.476 23.935 1.00 49.77 C ANISOU 2074 CB ILE A1072 4985 4976 8948 621 -265 -1008 C ATOM 2075 CG1 ILE A1072 -0.257 -56.597 22.684 1.00 46.59 C ANISOU 2075 CG1 ILE A1072 4564 4434 8704 599 -213 -950 C ATOM 2076 CG2 ILE A1072 1.038 -57.091 24.772 1.00 50.11 C ANISOU 2076 CG2 ILE A1072 4961 5036 9042 685 -285 -1193 C ATOM 2077 CD1 ILE A1072 -0.574 -55.158 22.978 1.00 46.05 C ANISOU 2077 CD1 ILE A1072 4370 4327 8800 628 -160 -1041 C ATOM 2078 N ASP A1073 -0.953 -60.115 25.563 1.00 46.15 N ANISOU 2078 N ASP A1073 4771 4720 8044 572 -386 -874 N ATOM 2079 CA ASP A1073 -0.839 -61.035 26.695 1.00 46.28 C ANISOU 2079 CA ASP A1073 4914 4820 7852 599 -419 -889 C ATOM 2080 C ASP A1073 -0.420 -62.438 26.249 1.00 43.76 C ANISOU 2080 C ASP A1073 4840 4424 7362 567 -542 -801 C ATOM 2081 O ASP A1073 0.384 -63.093 26.922 1.00 44.11 O ANISOU 2081 O ASP A1073 5021 4486 7255 663 -602 -881 O ATOM 2082 CB ASP A1073 -2.169 -61.104 27.453 1.00 46.35 C ANISOU 2082 CB ASP A1073 4859 4941 7812 540 -323 -761 C ATOM 2083 CG ASP A1073 -2.497 -59.817 28.193 1.00 48.97 C ANISOU 2083 CG ASP A1073 5037 5347 8223 665 -177 -875 C ATOM 2084 OD1 ASP A1073 -1.576 -58.990 28.418 1.00 49.36 O ANISOU 2084 OD1 ASP A1073 5089 5343 8323 775 -208 -1086 O ATOM 2085 OD2 ASP A1073 -3.681 -59.651 28.563 1.00 49.29 O ANISOU 2085 OD2 ASP A1073 4959 5489 8279 659 -36 -738 O ATOM 2086 N ASP A1074 -0.998 -62.935 25.148 1.00 43.61 N ANISOU 2086 N ASP A1074 4926 4299 7344 450 -612 -635 N ATOM 2087 CA ASP A1074 -0.603 -64.234 24.600 1.00 43.84 C ANISOU 2087 CA ASP A1074 5282 4196 7178 449 -751 -560 C ATOM 2088 C ASP A1074 0.900 -64.283 24.361 1.00 43.53 C ANISOU 2088 C ASP A1074 5309 4123 7105 665 -722 -700 C ATOM 2089 O ASP A1074 1.589 -65.211 24.804 1.00 44.09 O ANISOU 2089 O ASP A1074 5570 4184 6998 776 -789 -733 O ATOM 2090 CB ASP A1074 -1.335 -64.511 23.275 1.00 44.09 C ANISOU 2090 CB ASP A1074 5469 4062 7222 318 -872 -395 C ATOM 2091 CG ASP A1074 -2.804 -64.861 23.456 1.00 48.75 C ANISOU 2091 CG ASP A1074 6001 4667 7853 68 -978 -192 C ATOM 2092 OD1 ASP A1074 -3.268 -64.889 24.608 1.00 52.46 O ANISOU 2092 OD1 ASP A1074 6309 5294 8331 17 -888 -162 O ATOM 2093 OD2 ASP A1074 -3.504 -65.117 22.439 1.00 46.02 O ANISOU 2093 OD2 ASP A1074 5778 4171 7536 -75 -1158 -43 O ATOM 2094 N ALA A1075 1.420 -63.288 23.637 1.00 43.04 N ANISOU 2094 N ALA A1075 5078 4043 7231 734 -615 -760 N ATOM 2095 CA ALA A1075 2.825 -63.306 23.248 1.00 50.35 C ANISOU 2095 CA ALA A1075 5997 4950 8185 929 -545 -831 C ATOM 2096 C ALA A1075 3.731 -63.092 24.456 1.00 47.41 C ANISOU 2096 C ALA A1075 5424 4712 7878 1023 -564 -986 C ATOM 2097 O ALA A1075 4.799 -63.704 24.558 1.00 44.82 O ANISOU 2097 O ALA A1075 5136 4399 7495 1196 -589 -1018 O ATOM 2098 CB ALA A1075 3.078 -62.246 22.172 1.00 43.27 C ANISOU 2098 CB ALA A1075 4960 3990 7490 942 -398 -812 C ATOM 2099 N LEU A1076 3.297 -62.249 25.392 1.00 43.74 N ANISOU 2099 N LEU A1076 4773 4333 7515 936 -574 -1080 N ATOM 2100 CA LEU A1076 4.078 -61.973 26.595 1.00 46.21 C ANISOU 2100 CA LEU A1076 4964 4732 7862 1017 -660 -1243 C ATOM 2101 C LEU A1076 4.221 -63.218 27.461 1.00 46.10 C ANISOU 2101 C LEU A1076 5188 4750 7576 1104 -786 -1248 C ATOM 2102 O LEU A1076 5.287 -63.470 28.035 1.00 46.51 O ANISOU 2102 O LEU A1076 5210 4839 7623 1246 -903 -1347 O ATOM 2103 CB LEU A1076 3.400 -60.847 27.377 1.00 49.75 C ANISOU 2103 CB LEU A1076 5292 5216 8395 939 -643 -1339 C ATOM 2104 CG LEU A1076 4.080 -60.181 28.559 1.00 53.40 C ANISOU 2104 CG LEU A1076 5676 5708 8908 1004 -770 -1534 C ATOM 2105 CD1 LEU A1076 5.347 -59.474 28.107 1.00 53.93 C ANISOU 2105 CD1 LEU A1076 5489 5732 9269 1010 -826 -1601 C ATOM 2106 CD2 LEU A1076 3.077 -59.207 29.166 1.00 54.40 C ANISOU 2106 CD2 LEU A1076 5812 5833 9024 969 -704 -1592 C ATOM 2107 N LYS A1077 3.152 -64.006 27.575 1.00 46.32 N ANISOU 2107 N LYS A1077 5448 4757 7394 1010 -785 -1126 N ATOM 2108 CA LYS A1077 3.228 -65.240 28.342 1.00 46.35 C ANISOU 2108 CA LYS A1077 5737 4756 7120 1070 -897 -1100 C ATOM 2109 C LYS A1077 4.215 -66.212 27.712 1.00 47.85 C ANISOU 2109 C LYS A1077 6098 4865 7215 1238 -974 -1077 C ATOM 2110 O LYS A1077 4.949 -66.911 28.423 1.00 48.54 O ANISOU 2110 O LYS A1077 6323 4966 7154 1400 -1096 -1138 O ATOM 2111 CB LYS A1077 1.844 -65.877 28.453 1.00 47.76 C ANISOU 2111 CB LYS A1077 6099 4907 7142 882 -870 -920 C ATOM 2112 CG LYS A1077 1.869 -67.160 29.252 1.00 55.17 C ANISOU 2112 CG LYS A1077 7373 5808 7781 913 -975 -864 C ATOM 2113 CD LYS A1077 0.533 -67.854 29.264 1.00 62.18 C ANISOU 2113 CD LYS A1077 8413 6649 8563 674 -954 -634 C ATOM 2114 CE LYS A1077 0.714 -69.354 29.451 1.00 67.48 C ANISOU 2114 CE LYS A1077 9513 7179 8946 679 -1108 -538 C ATOM 2115 NZ LYS A1077 1.536 -69.960 28.353 1.00 69.26 N ANISOU 2115 NZ LYS A1077 9949 7245 9123 811 -1239 -563 N ATOM 2116 N LEU A1078 4.244 -66.276 26.377 1.00 47.53 N ANISOU 2116 N LEU A1078 6092 4730 7235 1240 -901 -985 N ATOM 2117 CA LEU A1078 5.209 -67.139 25.702 1.00 49.28 C ANISOU 2117 CA LEU A1078 6507 4869 7347 1471 -918 -956 C ATOM 2118 C LEU A1078 6.628 -66.629 25.903 1.00 47.92 C ANISOU 2118 C LEU A1078 6013 4813 7382 1685 -882 -1068 C ATOM 2119 O LEU A1078 7.557 -67.421 26.099 1.00 49.46 O ANISOU 2119 O LEU A1078 6301 5015 7475 1929 -950 -1084 O ATOM 2120 CB LEU A1078 4.882 -67.231 24.212 1.00 48.78 C ANISOU 2120 CB LEU A1078 6616 4656 7263 1455 -830 -832 C ATOM 2121 CG LEU A1078 3.582 -67.931 23.843 1.00 46.39 C ANISOU 2121 CG LEU A1078 6667 4192 6767 1241 -954 -692 C ATOM 2122 CD1 LEU A1078 3.223 -67.626 22.389 1.00 46.22 C ANISOU 2122 CD1 LEU A1078 6762 4023 6778 1208 -903 -600 C ATOM 2123 CD2 LEU A1078 3.718 -69.438 24.074 1.00 47.79 C ANISOU 2123 CD2 LEU A1078 7314 4228 6615 1336 -1121 -640 C ATOM 2124 N ALA A1079 6.809 -65.306 25.859 1.00 50.61 N ANISOU 2124 N ALA A1079 5964 5233 8031 1592 -795 -1133 N ATOM 2125 CA ALA A1079 8.136 -64.726 26.033 1.00 52.76 C ANISOU 2125 CA ALA A1079 5865 5604 8576 1726 -794 -1207 C ATOM 2126 C ALA A1079 8.690 -65.016 27.425 1.00 57.95 C ANISOU 2126 C ALA A1079 6493 6343 9184 1812 -1038 -1339 C ATOM 2127 O ALA A1079 9.863 -65.377 27.566 1.00 63.34 O ANISOU 2127 O ALA A1079 7031 7086 9951 2025 -1117 -1352 O ATOM 2128 CB ALA A1079 8.083 -63.222 25.760 1.00 48.96 C ANISOU 2128 CB ALA A1079 5034 5140 8426 1549 -695 -1241 C ATOM 2129 N ASN A1080 7.851 -64.887 28.463 1.00 57.56 N ANISOU 2129 N ASN A1080 6593 6294 8984 1677 -1156 -1421 N ATOM 2130 CA ASN A1080 8.264 -65.207 29.828 1.00 57.38 C ANISOU 2130 CA ASN A1080 6661 6313 8830 1775 -1401 -1546 C ATOM 2131 C ASN A1080 8.609 -66.688 29.989 1.00 61.45 C ANISOU 2131 C ASN A1080 7498 6796 9056 1984 -1497 -1490 C ATOM 2132 O ASN A1080 9.458 -67.039 30.813 1.00 68.17 O ANISOU 2132 O ASN A1080 8353 7682 9865 2163 -1719 -1577 O ATOM 2133 CB ASN A1080 7.162 -64.813 30.814 1.00 54.92 C ANISOU 2133 CB ASN A1080 6525 5993 8350 1626 -1422 -1610 C ATOM 2134 CG ASN A1080 7.012 -63.308 30.961 1.00 58.94 C ANISOU 2134 CG ASN A1080 6771 6511 9111 1496 -1399 -1716 C ATOM 2135 OD1 ASN A1080 7.997 -62.581 31.059 1.00 66.90 O ANISOU 2135 OD1 ASN A1080 7507 7527 10383 1519 -1537 -1818 O ATOM 2136 ND2 ASN A1080 5.771 -62.834 30.982 1.00 56.09 N ANISOU 2136 ND2 ASN A1080 6487 6138 8684 1358 -1238 -1679 N ATOM 2137 N GLU A1081 7.952 -67.567 29.232 1.00 58.37 N ANISOU 2137 N GLU A1081 7415 6309 8454 1966 -1377 -1347 N ATOM 2138 CA GLU A1081 8.267 -68.990 29.202 1.00 60.07 C ANISOU 2138 CA GLU A1081 8007 6438 8380 2173 -1465 -1281 C ATOM 2139 C GLU A1081 9.534 -69.297 28.416 1.00 61.19 C ANISOU 2139 C GLU A1081 8006 6600 8643 2480 -1419 -1253 C ATOM 2140 O GLU A1081 9.901 -70.473 28.315 1.00 62.24 O ANISOU 2140 O GLU A1081 8473 6648 8529 2722 -1484 -1203 O ATOM 2141 CB GLU A1081 7.101 -69.781 28.596 1.00 62.11 C ANISOU 2141 CB GLU A1081 8678 6537 8385 2015 -1396 -1127 C ATOM 2142 CG GLU A1081 5.900 -69.943 29.503 1.00 67.67 C ANISOU 2142 CG GLU A1081 9583 7222 8908 1769 -1439 -1087 C ATOM 2143 CD GLU A1081 4.666 -70.456 28.771 1.00 73.18 C ANISOU 2143 CD GLU A1081 10536 7776 9492 1524 -1386 -901 C ATOM 2144 OE1 GLU A1081 4.720 -70.656 27.537 1.00 75.11 O ANISOU 2144 OE1 GLU A1081 10868 7908 9762 1551 -1351 -831 O ATOM 2145 OE2 GLU A1081 3.627 -70.655 29.433 1.00 75.43 O ANISOU 2145 OE2 GLU A1081 10939 8055 9666 1303 -1386 -809 O ATOM 2146 N GLY A1082 10.181 -68.288 27.836 1.00 59.66 N ANISOU 2146 N GLY A1082 7346 6507 8816 2487 -1286 -1262 N ATOM 2147 CA GLY A1082 11.373 -68.501 27.043 1.00 58.50 C ANISOU 2147 CA GLY A1082 6994 6410 8825 2789 -1161 -1189 C ATOM 2148 C GLY A1082 11.158 -69.010 25.635 1.00 56.75 C ANISOU 2148 C GLY A1082 7051 6062 8451 2909 -906 -1041 C ATOM 2149 O GLY A1082 12.113 -69.472 25.013 1.00 63.48 O ANISOU 2149 O GLY A1082 7865 6934 9319 3253 -769 -960 O ATOM 2150 N LYS A1083 9.946 -68.940 25.100 1.00 54.11 N ANISOU 2150 N LYS A1083 7006 5590 7964 2664 -845 -995 N ATOM 2151 CA LYS A1083 9.671 -69.439 23.749 1.00 54.01 C ANISOU 2151 CA LYS A1083 7360 5402 7758 2771 -673 -865 C ATOM 2152 C LYS A1083 9.728 -68.257 22.784 1.00 53.49 C ANISOU 2152 C LYS A1083 6969 5377 7979 2680 -413 -809 C ATOM 2153 O LYS A1083 8.706 -67.662 22.444 1.00 54.22 O ANISOU 2153 O LYS A1083 7108 5398 8094 2394 -403 -795 O ATOM 2154 CB LYS A1083 8.322 -70.148 23.703 1.00 52.62 C ANISOU 2154 CB LYS A1083 7716 5021 7256 2544 -832 -824 C ATOM 2155 CG LYS A1083 8.132 -71.169 24.822 1.00 56.30 C ANISOU 2155 CG LYS A1083 8482 5444 7466 2547 -1083 -862 C ATOM 2156 CD LYS A1083 6.746 -71.806 24.783 1.00 57.73 C ANISOU 2156 CD LYS A1083 9116 5425 7394 2249 -1234 -773 C ATOM 2157 CE LYS A1083 6.518 -72.700 26.008 1.00 57.04 C ANISOU 2157 CE LYS A1083 9293 5304 7076 2206 -1445 -785 C ATOM 2158 NZ LYS A1083 5.316 -73.583 25.854 1.00 54.47 N ANISOU 2158 NZ LYS A1083 9459 4739 6497 1935 -1601 -642 N ATOM 2159 N VAL A1084 10.938 -67.928 22.321 1.00 56.79 N ANISOU 2159 N VAL A1084 7045 5907 8625 2936 -191 -753 N ATOM 2160 CA VAL A1084 11.129 -66.724 21.505 1.00 57.85 C ANISOU 2160 CA VAL A1084 6824 6085 9070 2836 76 -680 C ATOM 2161 C VAL A1084 10.363 -66.833 20.191 1.00 56.65 C ANISOU 2161 C VAL A1084 7128 5722 8676 2833 239 -574 C ATOM 2162 O VAL A1084 9.539 -65.973 19.862 1.00 53.24 O ANISOU 2162 O VAL A1084 6658 5234 8337 2548 252 -574 O ATOM 2163 CB VAL A1084 12.621 -66.466 21.246 1.00 64.86 C ANISOU 2163 CB VAL A1084 7237 7139 10266 3118 314 -584 C ATOM 2164 CG1 VAL A1084 12.811 -65.039 20.721 1.00 64.59 C ANISOU 2164 CG1 VAL A1084 6748 7162 10632 2906 538 -512 C ATOM 2165 CG2 VAL A1084 13.440 -66.720 22.499 1.00 70.21 C ANISOU 2165 CG2 VAL A1084 7578 7988 11108 3203 64 -678 C ATOM 2166 N LYS A1085 10.647 -67.882 19.409 1.00 59.72 N ANISOU 2166 N LYS A1085 7988 5970 8732 3181 346 -484 N ATOM 2167 CA LYS A1085 10.009 -68.036 18.100 1.00 62.20 C ANISOU 2167 CA LYS A1085 8826 6037 8768 3224 462 -386 C ATOM 2168 C LYS A1085 8.490 -68.064 18.217 1.00 54.34 C ANISOU 2168 C LYS A1085 8144 4878 7623 2835 151 -437 C ATOM 2169 O LYS A1085 7.783 -67.502 17.374 1.00 53.64 O ANISOU 2169 O LYS A1085 8199 4660 7520 2683 189 -381 O ATOM 2170 CB LYS A1085 10.497 -69.314 17.417 1.00 59.90 C ANISOU 2170 CB LYS A1085 9122 5573 8064 3687 549 -312 C ATOM 2171 CG LYS A1085 11.964 -69.323 17.049 1.00 66.62 C ANISOU 2171 CG LYS A1085 9688 6581 9043 4153 943 -204 C ATOM 2172 CD LYS A1085 12.260 -68.441 15.844 1.00 64.94 C ANISOU 2172 CD LYS A1085 9369 6356 8948 4242 1368 -50 C ATOM 2173 CE LYS A1085 13.693 -68.675 15.381 1.00 73.35 C ANISOU 2173 CE LYS A1085 10188 7610 10070 4633 1758 103 C ATOM 2174 NZ LYS A1085 13.988 -68.009 14.089 1.00 78.86 N ANISOU 2174 NZ LYS A1085 10912 8288 10762 4711 2190 288 N ATOM 2175 N GLU A1086 7.969 -68.743 19.238 1.00 53.25 N ANISOU 2175 N GLU A1086 8119 4741 7374 2682 -157 -517 N ATOM 2176 CA GLU A1086 6.527 -68.795 19.411 1.00 53.72 C ANISOU 2176 CA GLU A1086 8388 4678 7344 2303 -425 -519 C ATOM 2177 C GLU A1086 5.984 -67.434 19.832 1.00 52.50 C ANISOU 2177 C GLU A1086 7712 4689 7547 1981 -394 -565 C ATOM 2178 O GLU A1086 4.892 -67.040 19.412 1.00 48.17 O ANISOU 2178 O GLU A1086 7247 4045 7012 1733 -483 -518 O ATOM 2179 CB GLU A1086 6.158 -69.867 20.429 1.00 55.96 C ANISOU 2179 CB GLU A1086 8911 4926 7427 2224 -705 -554 C ATOM 2180 CG GLU A1086 4.856 -70.560 20.101 1.00 58.92 C ANISOU 2180 CG GLU A1086 9776 5047 7563 1965 -979 -467 C ATOM 2181 CD GLU A1086 4.454 -71.575 21.149 1.00 64.11 C ANISOU 2181 CD GLU A1086 10649 5662 8047 1838 -1229 -464 C ATOM 2182 OE1 GLU A1086 5.359 -72.182 21.766 1.00 66.28 O ANISOU 2182 OE1 GLU A1086 10979 5992 8213 2101 -1216 -526 O ATOM 2183 OE2 GLU A1086 3.228 -71.753 21.359 1.00 67.10 O ANISOU 2183 OE2 GLU A1086 11124 5956 8414 1474 -1435 -380 O ATOM 2184 N ALA A1087 6.738 -66.700 20.651 1.00 49.00 N ANISOU 2184 N ALA A1087 6749 4475 7395 1996 -298 -655 N ATOM 2185 CA ALA A1087 6.319 -65.349 21.000 1.00 51.23 C ANISOU 2185 CA ALA A1087 6602 4871 7992 1737 -264 -710 C ATOM 2186 C ALA A1087 6.309 -64.452 19.768 1.00 47.68 C ANISOU 2186 C ALA A1087 6104 4341 7670 1732 -51 -626 C ATOM 2187 O ALA A1087 5.343 -63.720 19.541 1.00 46.42 O ANISOU 2187 O ALA A1087 5912 4133 7591 1509 -93 -615 O ATOM 2188 CB ALA A1087 7.223 -64.773 22.091 1.00 47.94 C ANISOU 2188 CB ALA A1087 5716 4658 7840 1760 -265 -829 C ATOM 2189 N GLN A1088 7.357 -64.520 18.943 1.00 53.97 N ANISOU 2189 N GLN A1088 6914 5118 8473 2003 196 -547 N ATOM 2190 CA GLN A1088 7.409 -63.677 17.750 1.00 55.92 C ANISOU 2190 CA GLN A1088 7162 5275 8812 2020 442 -442 C ATOM 2191 C GLN A1088 6.271 -64.004 16.786 1.00 55.13 C ANISOU 2191 C GLN A1088 7600 4930 8419 1960 328 -372 C ATOM 2192 O GLN A1088 5.650 -63.094 16.225 1.00 49.15 O ANISOU 2192 O GLN A1088 6814 4098 7763 1803 355 -336 O ATOM 2193 CB GLN A1088 8.764 -63.822 17.057 1.00 53.18 C ANISOU 2193 CB GLN A1088 6749 4962 8495 2366 786 -327 C ATOM 2194 CG GLN A1088 9.921 -63.208 17.818 1.00 54.42 C ANISOU 2194 CG GLN A1088 6260 5356 9061 2372 894 -350 C ATOM 2195 CD GLN A1088 11.267 -63.631 17.264 1.00 57.98 C ANISOU 2195 CD GLN A1088 6603 5881 9546 2757 1224 -203 C ATOM 2196 OE1 GLN A1088 11.512 -64.816 17.055 1.00 59.23 O ANISOU 2196 OE1 GLN A1088 7131 5988 9385 3079 1240 -175 O ATOM 2197 NE2 GLN A1088 12.143 -62.666 17.018 1.00 60.08 N ANISOU 2197 NE2 GLN A1088 6362 6261 10206 2735 1498 -90 N ATOM 2198 N ALA A1089 5.981 -65.296 16.580 1.00 54.54 N ANISOU 2198 N ALA A1089 8043 4700 7978 2080 156 -348 N ATOM 2199 CA ALA A1089 4.866 -65.659 15.711 1.00 53.22 C ANISOU 2199 CA ALA A1089 8406 4267 7548 1981 -54 -279 C ATOM 2200 C ALA A1089 3.544 -65.125 16.250 1.00 51.50 C ANISOU 2200 C ALA A1089 7978 4088 7503 1586 -315 -307 C ATOM 2201 O ALA A1089 2.706 -64.644 15.482 1.00 53.58 O ANISOU 2201 O ALA A1089 8384 4210 7763 1458 -408 -243 O ATOM 2202 CB ALA A1089 4.794 -67.174 15.533 1.00 51.97 C ANISOU 2202 CB ALA A1089 8862 3905 6981 2140 -258 -255 C ATOM 2203 N ALA A1090 3.337 -65.196 17.565 1.00 47.09 N ANISOU 2203 N ALA A1090 7090 3717 7085 1420 -427 -389 N ATOM 2204 CA ALA A1090 2.106 -64.662 18.145 1.00 45.68 C ANISOU 2204 CA ALA A1090 6672 3608 7076 1099 -600 -393 C ATOM 2205 C ALA A1090 2.014 -63.148 17.972 1.00 50.16 C ANISOU 2205 C ALA A1090 6858 4259 7940 1028 -436 -421 C ATOM 2206 O ALA A1090 0.925 -62.608 17.737 1.00 44.49 O ANISOU 2206 O ALA A1090 6092 3500 7312 848 -552 -372 O ATOM 2207 CB ALA A1090 2.020 -65.035 19.623 1.00 44.96 C ANISOU 2207 CB ALA A1090 6357 3699 7027 1000 -683 -467 C ATOM 2208 N ALA A1091 3.142 -62.442 18.107 1.00 45.02 N ANISOU 2208 N ALA A1091 5920 3718 7466 1161 -186 -488 N ATOM 2209 CA ALA A1091 3.127 -60.996 17.916 1.00 50.59 C ANISOU 2209 CA ALA A1091 6319 4455 8449 1082 -44 -508 C ATOM 2210 C ALA A1091 2.772 -60.632 16.481 1.00 51.17 C ANISOU 2210 C ALA A1091 6679 4322 8443 1118 14 -389 C ATOM 2211 O ALA A1091 2.134 -59.603 16.247 1.00 53.37 O ANISOU 2211 O ALA A1091 6836 4565 8879 998 6 -380 O ATOM 2212 CB ALA A1091 4.476 -60.388 18.308 1.00 45.40 C ANISOU 2212 CB ALA A1091 5305 3923 8023 1176 171 -571 C ATOM 2213 N GLU A1092 3.149 -61.467 15.514 1.00 53.15 N ANISOU 2213 N GLU A1092 7366 4411 8417 1314 62 -298 N ATOM 2214 CA GLU A1092 2.801 -61.189 14.124 1.00 57.34 C ANISOU 2214 CA GLU A1092 8281 4706 8800 1382 93 -185 C ATOM 2215 C GLU A1092 1.285 -61.144 13.922 1.00 55.61 C ANISOU 2215 C GLU A1092 8213 4370 8544 1164 -260 -152 C ATOM 2216 O GLU A1092 0.797 -60.426 13.040 1.00 56.04 O ANISOU 2216 O GLU A1092 8409 4276 8607 1148 -280 -86 O ATOM 2217 CB GLU A1092 3.453 -62.238 13.216 1.00 64.25 C ANISOU 2217 CB GLU A1092 9697 5406 9310 1682 188 -104 C ATOM 2218 CG GLU A1092 3.812 -61.757 11.814 1.00 74.26 C ANISOU 2218 CG GLU A1092 11305 6475 10436 1890 443 18 C ATOM 2219 CD GLU A1092 4.831 -60.614 11.799 1.00 78.93 C ANISOU 2219 CD GLU A1092 11442 7211 11337 1942 871 57 C ATOM 2220 OE1 GLU A1092 5.656 -60.511 12.735 1.00 80.23 O ANISOU 2220 OE1 GLU A1092 11110 7613 11761 1927 1006 -2 O ATOM 2221 OE2 GLU A1092 4.803 -59.817 10.839 1.00 80.81 O ANISOU 2221 OE2 GLU A1092 11837 7304 11564 1985 1048 158 O ATOM 2222 N GLN A1093 0.525 -61.877 14.747 1.00 51.71 N ANISOU 2222 N GLN A1093 7666 3946 8034 992 -539 -176 N ATOM 2223 CA GLN A1093 -0.934 -61.815 14.679 1.00 49.56 C ANISOU 2223 CA GLN A1093 7401 3612 7816 757 -867 -106 C ATOM 2224 C GLN A1093 -1.458 -60.418 14.981 1.00 50.16 C ANISOU 2224 C GLN A1093 7034 3815 8210 654 -790 -134 C ATOM 2225 O GLN A1093 -2.544 -60.052 14.518 1.00 53.14 O ANISOU 2225 O GLN A1093 7430 4107 8653 542 -1003 -51 O ATOM 2226 CB GLN A1093 -1.553 -62.815 15.655 1.00 49.13 C ANISOU 2226 CB GLN A1093 7283 3648 7737 577 -1102 -92 C ATOM 2227 CG GLN A1093 -0.963 -64.207 15.567 1.00 51.88 C ANISOU 2227 CG GLN A1093 8073 3870 7770 690 -1180 -86 C ATOM 2228 CD GLN A1093 -0.967 -64.728 14.153 1.00 58.86 C ANISOU 2228 CD GLN A1093 9599 4419 8346 819 -1331 -5 C ATOM 2229 OE1 GLN A1093 -1.952 -64.576 13.427 1.00 61.92 O ANISOU 2229 OE1 GLN A1093 10170 4631 8727 677 -1613 89 O ATOM 2230 NE2 GLN A1093 0.139 -65.335 13.744 1.00 63.11 N ANISOU 2230 NE2 GLN A1093 10503 4857 8618 1120 -1151 -35 N ATOM 2231 N LEU A1094 -0.709 -59.634 15.763 1.00 47.91 N ANISOU 2231 N LEU A1094 6365 3715 8125 698 -523 -249 N ATOM 2232 CA LEU A1094 -1.112 -58.265 16.072 1.00 47.74 C ANISOU 2232 CA LEU A1094 5995 3770 8373 634 -446 -294 C ATOM 2233 C LEU A1094 -1.328 -57.438 14.813 1.00 54.46 C ANISOU 2233 C LEU A1094 7045 4418 9230 687 -425 -214 C ATOM 2234 O LEU A1094 -2.145 -56.510 14.818 1.00 57.17 O ANISOU 2234 O LEU A1094 7222 4759 9740 629 -492 -205 O ATOM 2235 CB LEU A1094 -0.064 -57.593 16.960 1.00 44.40 C ANISOU 2235 CB LEU A1094 5244 3496 8128 678 -206 -432 C ATOM 2236 CG LEU A1094 0.191 -58.215 18.338 1.00 46.56 C ANISOU 2236 CG LEU A1094 5324 3968 8399 649 -236 -534 C ATOM 2237 CD1 LEU A1094 1.503 -57.715 18.902 1.00 43.27 C ANISOU 2237 CD1 LEU A1094 4684 3633 8126 715 -59 -651 C ATOM 2238 CD2 LEU A1094 -0.950 -57.892 19.289 1.00 50.80 C ANISOU 2238 CD2 LEU A1094 5638 4630 9032 541 -341 -560 C ATOM 2239 N LYS A1095 -0.615 -57.753 13.727 1.00 55.82 N ANISOU 2239 N LYS A1095 7602 4409 9198 831 -318 -148 N ATOM 2240 CA LYS A1095 -0.758 -56.963 12.506 1.00 57.41 C ANISOU 2240 CA LYS A1095 8062 4392 9357 906 -271 -60 C ATOM 2241 C LYS A1095 -2.119 -57.165 11.853 1.00 57.48 C ANISOU 2241 C LYS A1095 8330 4242 9269 832 -657 32 C ATOM 2242 O LYS A1095 -2.624 -56.250 11.191 1.00 59.37 O ANISOU 2242 O LYS A1095 8638 4351 9568 847 -707 82 O ATOM 2243 CB LYS A1095 0.363 -57.295 11.526 1.00 60.63 C ANISOU 2243 CB LYS A1095 8853 4649 9534 1122 -5 12 C ATOM 2244 CG LYS A1095 1.709 -56.771 11.978 1.00 64.22 C ANISOU 2244 CG LYS A1095 8965 5250 10186 1180 391 -25 C ATOM 2245 CD LYS A1095 2.814 -57.165 11.026 1.00 69.72 C ANISOU 2245 CD LYS A1095 9982 5835 10672 1431 715 91 C ATOM 2246 CE LYS A1095 4.082 -56.389 11.337 1.00 73.83 C ANISOU 2246 CE LYS A1095 10074 6490 11488 1442 1108 112 C ATOM 2247 NZ LYS A1095 5.214 -56.768 10.442 1.00 79.53 N ANISOU 2247 NZ LYS A1095 11025 7148 12046 1718 1505 271 N ATOM 2248 N THR A1096 -2.733 -58.337 12.032 1.00 55.53 N ANISOU 2248 N THR A1096 8222 3988 8891 739 -963 68 N ATOM 2249 CA THR A1096 -4.098 -58.518 11.550 1.00 55.26 C ANISOU 2249 CA THR A1096 8321 3825 8851 607 -1396 176 C ATOM 2250 C THR A1096 -5.070 -57.642 12.326 1.00 51.41 C ANISOU 2250 C THR A1096 7281 3538 8714 476 -1458 175 C ATOM 2251 O THR A1096 -5.962 -57.023 11.741 1.00 51.95 O ANISOU 2251 O THR A1096 7357 3506 8875 461 -1669 257 O ATOM 2252 CB THR A1096 -4.522 -59.980 11.664 1.00 58.87 C ANISOU 2252 CB THR A1096 9015 4219 9134 481 -1730 236 C ATOM 2253 OG1 THR A1096 -3.433 -60.833 11.295 1.00 63.50 O ANISOU 2253 OG1 THR A1096 10052 4679 9396 660 -1582 200 O ATOM 2254 CG2 THR A1096 -5.705 -60.251 10.750 1.00 60.08 C ANISOU 2254 CG2 THR A1096 9478 4126 9222 363 -2234 378 C ATOM 2255 N THR A1097 -4.924 -57.594 13.648 1.00 48.86 N ANISOU 2255 N THR A1097 6507 3489 8567 415 -1282 89 N ATOM 2256 CA THR A1097 -5.803 -56.759 14.455 1.00 50.08 C ANISOU 2256 CA THR A1097 6177 3837 9013 359 -1278 86 C ATOM 2257 C THR A1097 -5.609 -55.288 14.125 1.00 50.19 C ANISOU 2257 C THR A1097 6125 3790 9154 492 -1095 25 C ATOM 2258 O THR A1097 -6.571 -54.508 14.113 1.00 49.17 O ANISOU 2258 O THR A1097 5794 3683 9205 508 -1199 75 O ATOM 2259 CB THR A1097 -5.532 -57.000 15.936 1.00 51.55 C ANISOU 2259 CB THR A1097 6011 4291 9283 320 -1090 -11 C ATOM 2260 OG1 THR A1097 -5.547 -58.413 16.204 1.00 52.75 O ANISOU 2260 OG1 THR A1097 6299 4463 9280 202 -1237 48 O ATOM 2261 CG2 THR A1097 -6.578 -56.283 16.784 1.00 50.74 C ANISOU 2261 CG2 THR A1097 5463 4385 9429 305 -1073 15 C ATOM 2262 N ARG A1098 -4.364 -54.898 13.854 1.00 50.54 N ANISOU 2262 N ARG A1098 6328 3751 9122 592 -820 -63 N ATOM 2263 CA ARG A1098 -4.044 -53.501 13.599 1.00 53.53 C ANISOU 2263 CA ARG A1098 6664 4043 9630 679 -630 -110 C ATOM 2264 C ARG A1098 -4.690 -53.021 12.309 1.00 57.26 C ANISOU 2264 C ARG A1098 7447 4272 10038 743 -804 10 C ATOM 2265 O ARG A1098 -5.231 -51.911 12.256 1.00 60.13 O ANISOU 2265 O ARG A1098 7697 4592 10558 795 -820 9 O ATOM 2266 CB ARG A1098 -2.530 -53.327 13.545 1.00 53.30 C ANISOU 2266 CB ARG A1098 6706 3980 9567 726 -307 -177 C ATOM 2267 CG ARG A1098 -2.066 -51.902 13.395 1.00 57.71 C ANISOU 2267 CG ARG A1098 7201 4433 10292 758 -104 -213 C ATOM 2268 CD ARG A1098 -0.685 -51.898 12.780 1.00 61.02 C ANISOU 2268 CD ARG A1098 7783 4751 10651 798 187 -167 C ATOM 2269 NE ARG A1098 -0.665 -52.671 11.539 1.00 62.59 N ANISOU 2269 NE ARG A1098 8440 4783 10558 905 165 -28 N ATOM 2270 CZ ARG A1098 0.440 -52.994 10.878 1.00 63.60 C ANISOU 2270 CZ ARG A1098 8780 4834 10552 1009 442 54 C ATOM 2271 NH1 ARG A1098 1.626 -52.614 11.346 1.00 64.03 N ANISOU 2271 NH1 ARG A1098 8541 4988 10801 979 745 31 N ATOM 2272 NH2 ARG A1098 0.359 -53.703 9.758 1.00 64.12 N ANISOU 2272 NH2 ARG A1098 9356 4717 10290 1155 407 170 N ATOM 2273 N ASN A1099 -4.651 -53.846 11.263 1.00 54.51 N ANISOU 2273 N ASN A1099 7544 3734 9431 766 -959 111 N ATOM 2274 CA ASN A1099 -5.258 -53.453 10.000 1.00 57.84 C ANISOU 2274 CA ASN A1099 8348 3888 9741 843 -1176 224 C ATOM 2275 C ASN A1099 -6.774 -53.426 10.099 1.00 63.26 C ANISOU 2275 C ASN A1099 8827 4621 10590 765 -1592 304 C ATOM 2276 O ASN A1099 -7.417 -52.510 9.578 1.00 71.89 O ANISOU 2276 O ASN A1099 9949 5595 11769 845 -1720 356 O ATOM 2277 CB ASN A1099 -4.813 -54.400 8.890 1.00 62.34 C ANISOU 2277 CB ASN A1099 9533 4215 9938 921 -1255 302 C ATOM 2278 CG ASN A1099 -3.314 -54.443 8.738 1.00 64.20 C ANISOU 2278 CG ASN A1099 9928 4430 10034 1043 -796 267 C ATOM 2279 OD1 ASN A1099 -2.626 -53.474 9.055 1.00 64.49 O ANISOU 2279 OD1 ASN A1099 9713 4535 10254 1061 -455 222 O ATOM 2280 ND2 ASN A1099 -2.795 -55.571 8.254 1.00 64.38 N ANISOU 2280 ND2 ASN A1099 10367 4350 9745 1134 -792 302 N ATOM 2281 N ALA A1100 -7.367 -54.410 10.772 1.00 61.10 N ANISOU 2281 N ALA A1100 8317 4517 10379 612 -1803 338 N ATOM 2282 CA ALA A1100 -8.818 -54.542 10.749 1.00 60.95 C ANISOU 2282 CA ALA A1100 8077 4539 10541 511 -2222 476 C ATOM 2283 C ALA A1100 -9.504 -53.605 11.730 1.00 60.73 C ANISOU 2283 C ALA A1100 7450 4770 10854 550 -2094 460 C ATOM 2284 O ALA A1100 -10.643 -53.199 11.486 1.00 65.02 O ANISOU 2284 O ALA A1100 7798 5319 11588 570 -2365 583 O ATOM 2285 CB ALA A1100 -9.222 -55.991 11.041 1.00 61.02 C ANISOU 2285 CB ALA A1100 8077 4604 10503 296 -2504 565 C ATOM 2286 N TYR A1101 -8.840 -53.238 12.826 1.00 58.59 N ANISOU 2286 N TYR A1101 6906 4700 10656 592 -1702 314 N ATOM 2287 CA TYR A1101 -9.508 -52.487 13.885 1.00 59.02 C ANISOU 2287 CA TYR A1101 6455 4995 10975 666 -1568 292 C ATOM 2288 C TYR A1101 -8.788 -51.194 14.253 1.00 59.09 C ANISOU 2288 C TYR A1101 6457 4973 11020 834 -1233 118 C ATOM 2289 O TYR A1101 -9.379 -50.110 14.185 1.00 60.55 O ANISOU 2289 O TYR A1101 6538 5124 11346 991 -1237 125 O ATOM 2290 CB TYR A1101 -9.650 -53.352 15.140 1.00 59.56 C ANISOU 2290 CB TYR A1101 6187 5346 11098 547 -1473 295 C ATOM 2291 CG TYR A1101 -10.571 -54.537 14.983 1.00 63.11 C ANISOU 2291 CG TYR A1101 6542 5845 11592 340 -1815 504 C ATOM 2292 CD1 TYR A1101 -11.948 -54.390 15.127 1.00 64.88 C ANISOU 2292 CD1 TYR A1101 6352 6210 12092 319 -2007 699 C ATOM 2293 CD2 TYR A1101 -10.064 -55.811 14.706 1.00 63.61 C ANISOU 2293 CD2 TYR A1101 6923 5807 11440 167 -1957 523 C ATOM 2294 CE1 TYR A1101 -12.803 -55.472 14.988 1.00 68.84 C ANISOU 2294 CE1 TYR A1101 6723 6744 12690 73 -2357 926 C ATOM 2295 CE2 TYR A1101 -10.914 -56.903 14.564 1.00 65.73 C ANISOU 2295 CE2 TYR A1101 7147 6071 11756 -64 -2321 723 C ATOM 2296 CZ TYR A1101 -12.283 -56.724 14.705 1.00 70.59 C ANISOU 2296 CZ TYR A1101 7313 6823 12684 -139 -2533 932 C ATOM 2297 OH TYR A1101 -13.140 -57.792 14.573 1.00 76.42 O ANISOU 2297 OH TYR A1101 7959 7548 13527 -422 -2927 1164 O ATOM 2298 N ILE A1102 -7.516 -51.299 14.651 1.00 58.79 N ANISOU 2298 N ILE A1102 6533 4934 10872 802 -971 -29 N ATOM 2299 CA ILE A1102 -6.835 -50.168 15.278 1.00 57.53 C ANISOU 2299 CA ILE A1102 6303 4764 10791 899 -697 -194 C ATOM 2300 C ILE A1102 -6.691 -49.004 14.310 1.00 61.37 C ANISOU 2300 C ILE A1102 7047 4980 11292 999 -682 -183 C ATOM 2301 O ILE A1102 -6.892 -47.843 14.688 1.00 61.43 O ANISOU 2301 O ILE A1102 6973 4944 11422 1122 -600 -258 O ATOM 2302 CB ILE A1102 -5.465 -50.591 15.829 1.00 53.08 C ANISOU 2302 CB ILE A1102 5779 4245 10144 813 -486 -324 C ATOM 2303 CG1 ILE A1102 -5.594 -51.877 16.664 1.00 51.87 C ANISOU 2303 CG1 ILE A1102 5461 4322 9926 720 -530 -316 C ATOM 2304 CG2 ILE A1102 -4.847 -49.432 16.615 1.00 49.57 C ANISOU 2304 CG2 ILE A1102 5241 3778 9817 873 -290 -493 C ATOM 2305 CD1 ILE A1102 -6.626 -51.807 17.788 1.00 49.42 C ANISOU 2305 CD1 ILE A1102 4809 4240 9730 768 -535 -311 C ATOM 2306 N GLN A1103 -6.308 -49.283 13.061 1.00 63.45 N ANISOU 2306 N GLN A1103 7682 5029 11399 968 -747 -90 N ATOM 2307 CA GLN A1103 -6.133 -48.194 12.105 1.00 66.47 C ANISOU 2307 CA GLN A1103 8362 5129 11763 1063 -706 -55 C ATOM 2308 C GLN A1103 -7.456 -47.494 11.808 1.00 64.81 C ANISOU 2308 C GLN A1103 8103 4863 11657 1206 -952 19 C ATOM 2309 O GLN A1103 -7.478 -46.278 11.572 1.00 63.56 O ANISOU 2309 O GLN A1103 8060 4529 11561 1326 -889 -4 O ATOM 2310 CB GLN A1103 -5.500 -48.711 10.814 1.00 71.19 C ANISOU 2310 CB GLN A1103 9424 5506 12117 1045 -696 52 C ATOM 2311 CG GLN A1103 -5.026 -47.598 9.897 1.00 77.19 C ANISOU 2311 CG GLN A1103 10525 5971 12835 1126 -545 101 C ATOM 2312 CD GLN A1103 -4.615 -48.088 8.526 1.00 81.33 C ANISOU 2312 CD GLN A1103 11581 6256 13063 1175 -534 240 C ATOM 2313 OE1 GLN A1103 -4.380 -49.278 8.320 1.00 81.74 O ANISOU 2313 OE1 GLN A1103 11767 6360 12932 1150 -579 272 O ATOM 2314 NE2 GLN A1103 -4.529 -47.167 7.576 1.00 84.96 N ANISOU 2314 NE2 GLN A1103 12407 6429 13444 1272 -468 328 N ATOM 2315 N LYS A1104 -8.566 -48.239 11.830 1.00 64.06 N ANISOU 2315 N LYS A1104 7822 4911 11606 1193 -1245 125 N ATOM 2316 CA LYS A1104 -9.874 -47.619 11.650 1.00 66.15 C ANISOU 2316 CA LYS A1104 7926 5177 12032 1346 -1489 221 C ATOM 2317 C LYS A1104 -10.198 -46.669 12.798 1.00 61.12 C ANISOU 2317 C LYS A1104 6931 4700 11593 1508 -1288 117 C ATOM 2318 O LYS A1104 -10.755 -45.587 12.574 1.00 60.77 O ANISOU 2318 O LYS A1104 6911 4540 11638 1717 -1336 130 O ATOM 2319 CB LYS A1104 -10.956 -48.693 11.514 1.00 71.20 C ANISOU 2319 CB LYS A1104 8357 5958 12738 1248 -1858 390 C ATOM 2320 CG LYS A1104 -10.956 -49.400 10.173 1.00 75.20 C ANISOU 2320 CG LYS A1104 9333 6210 13032 1158 -2193 507 C ATOM 2321 CD LYS A1104 -12.004 -50.502 10.122 1.00 79.17 C ANISOU 2321 CD LYS A1104 9623 6825 13632 999 -2620 678 C ATOM 2322 CE LYS A1104 -11.965 -51.267 8.799 1.00 80.59 C ANISOU 2322 CE LYS A1104 10381 6694 13544 913 -3014 772 C ATOM 2323 NZ LYS A1104 -10.717 -52.071 8.630 1.00 77.85 N ANISOU 2323 NZ LYS A1104 10460 6244 12876 833 -2794 677 N ATOM 2324 N TYR A1105 -9.874 -47.060 14.035 1.00 59.21 N ANISOU 2324 N TYR A1105 6407 4701 11389 1446 -1072 12 N ATOM 2325 CA TYR A1105 -10.080 -46.159 15.164 1.00 62.90 C ANISOU 2325 CA TYR A1105 6645 5280 11972 1636 -864 -109 C ATOM 2326 C TYR A1105 -9.212 -44.914 15.029 1.00 62.37 C ANISOU 2326 C TYR A1105 6896 4936 11864 1708 -704 -260 C ATOM 2327 O TYR A1105 -9.666 -43.800 15.307 1.00 59.84 O ANISOU 2327 O TYR A1105 6580 4536 11621 1941 -666 -313 O ATOM 2328 CB TYR A1105 -9.790 -46.869 16.491 1.00 67.77 C ANISOU 2328 CB TYR A1105 7002 6171 12576 1558 -676 -198 C ATOM 2329 CG TYR A1105 -9.573 -45.898 17.644 1.00 75.04 C ANISOU 2329 CG TYR A1105 7881 7114 13515 1748 -438 -385 C ATOM 2330 CD1 TYR A1105 -10.648 -45.269 18.261 1.00 82.87 C ANISOU 2330 CD1 TYR A1105 8647 8230 14610 2041 -379 -355 C ATOM 2331 CD2 TYR A1105 -8.290 -45.589 18.098 1.00 74.97 C ANISOU 2331 CD2 TYR A1105 8079 6983 13421 1653 -290 -582 C ATOM 2332 CE1 TYR A1105 -10.455 -44.365 19.302 1.00 87.05 C ANISOU 2332 CE1 TYR A1105 9247 8730 15096 2262 -175 -539 C ATOM 2333 CE2 TYR A1105 -8.086 -44.684 19.139 1.00 78.02 C ANISOU 2333 CE2 TYR A1105 8512 7332 13802 1818 -148 -765 C ATOM 2334 CZ TYR A1105 -9.171 -44.081 19.739 1.00 85.54 C ANISOU 2334 CZ TYR A1105 9328 8377 14796 2135 -89 -755 C ATOM 2335 OH TYR A1105 -8.988 -43.182 20.772 1.00 90.89 O ANISOU 2335 OH TYR A1105 10149 8974 15409 2344 41 -949 O ATOM 2336 N LEU A1106 -7.962 -45.092 14.608 1.00 56.30 N ANISOU 2336 N LEU A1106 6394 4013 10986 1516 -604 -314 N ATOM 2337 CA LEU A1106 -7.010 -44.011 14.400 1.00 56.75 C ANISOU 2337 CA LEU A1106 6731 3791 11040 1500 -455 -409 C ATOM 2338 C LEU A1106 -7.547 -42.975 13.408 1.00 59.09 C ANISOU 2338 C LEU A1106 7303 3804 11342 1661 -567 -323 C ATOM 2339 O LEU A1106 -7.393 -41.765 13.605 1.00 60.59 O ANISOU 2339 O LEU A1106 7642 3791 11587 1762 -496 -409 O ATOM 2340 CB LEU A1106 -5.672 -44.588 13.905 1.00 60.88 C ANISOU 2340 CB LEU A1106 7426 4235 11472 1265 -322 -394 C ATOM 2341 CG LEU A1106 -4.614 -43.627 13.331 1.00 67.56 C ANISOU 2341 CG LEU A1106 8560 4771 12338 1182 -158 -396 C ATOM 2342 CD1 LEU A1106 -4.000 -42.723 14.409 1.00 70.72 C ANISOU 2342 CD1 LEU A1106 8871 5117 12883 1137 -55 -572 C ATOM 2343 CD2 LEU A1106 -3.513 -44.362 12.535 1.00 55.61 C ANISOU 2343 CD2 LEU A1106 7200 3210 10722 1017 -4 -290 C ATOM 2344 N GLU A 219 -8.082 -43.417 12.273 1.00 58.76 N ANISOU 2344 N GLU A 219 9703 3317 9306 1994 198 -1066 N ATOM 2345 CA GLU A 219 -8.590 -42.574 11.203 1.00 60.45 C ANISOU 2345 CA GLU A 219 9909 3693 9368 1898 278 -1196 C ATOM 2346 C GLU A 219 -9.827 -41.829 11.686 1.00 57.40 C ANISOU 2346 C GLU A 219 9585 3405 8819 1691 210 -1085 C ATOM 2347 O GLU A 219 -9.984 -40.630 11.421 1.00 58.93 O ANISOU 2347 O GLU A 219 9694 3795 8902 1645 253 -1097 O ATOM 2348 CB GLU A 219 -8.887 -43.411 9.951 1.00 64.18 C ANISOU 2348 CB GLU A 219 10507 4059 9818 1869 341 -1384 C ATOM 2349 CG GLU A 219 -7.623 -43.864 9.207 1.00 71.30 C ANISOU 2349 CG GLU A 219 11317 4920 10855 2076 442 -1537 C ATOM 2350 CD GLU A 219 -7.825 -45.099 8.324 1.00 80.00 C ANISOU 2350 CD GLU A 219 12572 5836 11987 2074 471 -1691 C ATOM 2351 OE1 GLU A 219 -8.902 -45.737 8.386 1.00 82.14 O ANISOU 2351 OE1 GLU A 219 13026 5987 12197 1918 400 -1664 O ATOM 2352 OE2 GLU A 219 -6.888 -45.444 7.569 1.00 83.82 O ANISOU 2352 OE2 GLU A 219 12989 6295 12562 2228 564 -1843 O ATOM 2353 N ARG A 220 -10.692 -42.511 12.439 1.00 55.90 N ANISOU 2353 N ARG A 220 9537 3084 8620 1564 107 -970 N ATOM 2354 CA ARG A 220 -11.898 -41.847 12.927 1.00 55.79 C ANISOU 2354 CA ARG A 220 9574 3162 8462 1358 46 -866 C ATOM 2355 C ARG A 220 -11.578 -40.839 14.029 1.00 56.38 C ANISOU 2355 C ARG A 220 9520 3373 8529 1391 0 -710 C ATOM 2356 O ARG A 220 -12.181 -39.761 14.084 1.00 57.50 O ANISOU 2356 O ARG A 220 9625 3675 8548 1281 3 -679 O ATOM 2357 CB ARG A 220 -12.919 -42.884 13.391 1.00 61.65 C ANISOU 2357 CB ARG A 220 10494 3736 9196 1200 -42 -794 C ATOM 2358 CG ARG A 220 -13.578 -43.609 12.216 1.00 71.78 C ANISOU 2358 CG ARG A 220 11909 4929 10436 1106 -4 -952 C ATOM 2359 CD ARG A 220 -14.738 -44.507 12.638 1.00 79.98 C ANISOU 2359 CD ARG A 220 13111 5826 11450 915 -89 -880 C ATOM 2360 NE ARG A 220 -15.740 -43.788 13.430 1.00 81.91 N ANISOU 2360 NE ARG A 220 13349 6186 11587 731 -148 -740 N ATOM 2361 CZ ARG A 220 -16.898 -44.314 13.818 1.00 80.03 C ANISOU 2361 CZ ARG A 220 13224 5880 11305 530 -213 -669 C ATOM 2362 NH1 ARG A 220 -17.202 -45.560 13.472 1.00 81.66 N ANISOU 2362 NH1 ARG A 220 13566 5900 11563 486 -231 -724 N ATOM 2363 NH2 ARG A 220 -17.749 -43.596 14.541 1.00 75.40 N ANISOU 2363 NH2 ARG A 220 12609 5416 10625 371 -254 -547 N ATOM 2364 N ALA A 221 -10.622 -41.155 14.906 1.00 56.43 N ANISOU 2364 N ALA A 221 9454 3322 8666 1541 -45 -613 N ATOM 2365 CA ALA A 221 -10.188 -40.175 15.900 1.00 53.79 C ANISOU 2365 CA ALA A 221 8983 3129 8326 1588 -91 -476 C ATOM 2366 C ALA A 221 -9.591 -38.943 15.232 1.00 50.69 C ANISOU 2366 C ALA A 221 8422 2936 7900 1667 3 -568 C ATOM 2367 O ALA A 221 -9.872 -37.804 15.636 1.00 51.10 O ANISOU 2367 O ALA A 221 8404 3149 7862 1605 -13 -500 O ATOM 2368 CB ALA A 221 -9.175 -40.813 16.852 1.00 57.68 C ANISOU 2368 CB ALA A 221 9425 3526 8967 1747 -156 -367 C ATOM 2369 N ARG A 222 -8.774 -39.154 14.197 1.00 50.07 N ANISOU 2369 N ARG A 222 8279 2852 7893 1798 108 -726 N ATOM 2370 CA ARG A 222 -8.172 -38.044 13.471 1.00 48.81 C ANISOU 2370 CA ARG A 222 7959 2886 7700 1867 214 -822 C ATOM 2371 C ARG A 222 -9.234 -37.194 12.789 1.00 46.77 C ANISOU 2371 C ARG A 222 7763 2753 7254 1698 259 -876 C ATOM 2372 O ARG A 222 -9.193 -35.959 12.850 1.00 44.83 O ANISOU 2372 O ARG A 222 7410 2688 6934 1682 290 -849 O ATOM 2373 CB ARG A 222 -7.182 -38.591 12.452 1.00 53.55 C ANISOU 2373 CB ARG A 222 8497 3445 8406 2019 322 -989 C ATOM 2374 CG ARG A 222 -6.406 -37.552 11.671 1.00 56.08 C ANISOU 2374 CG ARG A 222 8638 3965 8704 2099 440 -1095 C ATOM 2375 CD ARG A 222 -5.497 -38.263 10.681 1.00 62.93 C ANISOU 2375 CD ARG A 222 9461 4774 9676 2238 539 -1267 C ATOM 2376 NE ARG A 222 -4.681 -39.290 11.325 1.00 67.12 N ANISOU 2376 NE ARG A 222 9959 5134 10409 2382 497 -1218 N ATOM 2377 CZ ARG A 222 -4.253 -40.395 10.717 1.00 74.44 C ANISOU 2377 CZ ARG A 222 10935 5907 11443 2474 545 -1337 C ATOM 2378 NH1 ARG A 222 -4.574 -40.625 9.450 1.00 76.53 N ANISOU 2378 NH1 ARG A 222 11284 6172 11621 2432 624 -1520 N ATOM 2379 NH2 ARG A 222 -3.510 -41.276 11.375 1.00 76.69 N ANISOU 2379 NH2 ARG A 222 11193 6036 11909 2609 517 -1268 N ATOM 2380 N SER A 223 -10.203 -37.846 12.149 1.00 49.92 N ANISOU 2380 N SER A 223 8332 3057 7578 1566 261 -948 N ATOM 2381 CA SER A 223 -11.238 -37.135 11.410 1.00 46.56 C ANISOU 2381 CA SER A 223 7969 2743 6978 1399 302 -1006 C ATOM 2382 C SER A 223 -12.113 -36.310 12.344 1.00 49.48 C ANISOU 2382 C SER A 223 8346 3195 7258 1259 225 -858 C ATOM 2383 O SER A 223 -12.507 -35.182 12.009 1.00 51.85 O ANISOU 2383 O SER A 223 8602 3657 7441 1187 271 -872 O ATOM 2384 CB SER A 223 -12.061 -38.149 10.617 1.00 50.62 C ANISOU 2384 CB SER A 223 8659 3126 7450 1287 299 -1106 C ATOM 2385 OG SER A 223 -13.251 -37.572 10.126 1.00 53.39 O ANISOU 2385 OG SER A 223 9080 3568 7637 1096 301 -1129 O ATOM 2386 N THR A 224 -12.398 -36.828 13.540 1.00 43.73 N ANISOU 2386 N THR A 224 7669 2364 6583 1220 111 -711 N ATOM 2387 CA THR A 224 -13.169 -36.041 14.502 1.00 44.31 C ANISOU 2387 CA THR A 224 7740 2522 6574 1091 39 -567 C ATOM 2388 C THR A 224 -12.402 -34.797 14.945 1.00 44.11 C ANISOU 2388 C THR A 224 7545 2664 6552 1197 58 -514 C ATOM 2389 O THR A 224 -12.981 -33.711 15.067 1.00 43.56 O ANISOU 2389 O THR A 224 7382 2792 6377 1072 65 -469 O ATOM 2390 CB THR A 224 -13.545 -36.922 15.690 1.00 44.78 C ANISOU 2390 CB THR A 224 7886 2442 6684 1029 -79 -419 C ATOM 2391 OG1 THR A 224 -14.293 -38.034 15.203 1.00 49.11 O ANISOU 2391 OG1 THR A 224 8587 2843 7227 920 -88 -477 O ATOM 2392 CG2 THR A 224 -14.393 -36.172 16.694 1.00 42.93 C ANISOU 2392 CG2 THR A 224 7653 2300 6359 879 -148 -273 C ATOM 2393 N LEU A 225 -11.093 -34.926 15.168 1.00 45.53 N ANISOU 2393 N LEU A 225 7600 2840 6858 1393 67 -511 N ATOM 2394 CA LEU A 225 -10.308 -33.773 15.601 1.00 42.32 C ANISOU 2394 CA LEU A 225 7006 2607 6466 1488 79 -459 C ATOM 2395 C LEU A 225 -10.218 -32.721 14.503 1.00 42.04 C ANISOU 2395 C LEU A 225 6852 2774 6347 1462 210 -573 C ATOM 2396 O LEU A 225 -10.281 -31.520 14.785 1.00 43.47 O ANISOU 2396 O LEU A 225 6888 3165 6465 1397 215 -514 O ATOM 2397 CB LEU A 225 -8.912 -34.220 16.038 1.00 47.71 C ANISOU 2397 CB LEU A 225 7566 3245 7316 1692 56 -437 C ATOM 2398 CG LEU A 225 -8.756 -34.641 17.507 1.00 50.85 C ANISOU 2398 CG LEU A 225 7968 3572 7779 1708 -89 -260 C ATOM 2399 CD1 LEU A 225 -7.474 -35.420 17.738 1.00 54.05 C ANISOU 2399 CD1 LEU A 225 8283 3896 8358 1895 -101 -254 C ATOM 2400 CD2 LEU A 225 -8.825 -33.396 18.420 1.00 48.25 C ANISOU 2400 CD2 LEU A 225 7539 3410 7385 1671 -153 -142 C ATOM 2401 N GLN A 226 -10.082 -33.146 13.247 1.00 45.62 N ANISOU 2401 N GLN A 226 7378 3165 6792 1509 316 -735 N ATOM 2402 CA GLN A 226 -10.016 -32.176 12.160 1.00 47.60 C ANISOU 2402 CA GLN A 226 7538 3602 6946 1477 442 -838 C ATOM 2403 C GLN A 226 -11.337 -31.425 11.998 1.00 45.79 C ANISOU 2403 C GLN A 226 7342 3502 6555 1251 421 -805 C ATOM 2404 O GLN A 226 -11.337 -30.236 11.646 1.00 43.10 O ANISOU 2404 O GLN A 226 6877 3364 6133 1201 477 -809 O ATOM 2405 CB GLN A 226 -9.604 -32.876 10.867 1.00 52.36 C ANISOU 2405 CB GLN A 226 8201 4130 7563 1552 551 -1015 C ATOM 2406 CG GLN A 226 -8.189 -33.453 10.947 1.00 64.61 C ANISOU 2406 CG GLN A 226 9625 5637 9287 1752 572 -1050 C ATOM 2407 CD GLN A 226 -7.851 -34.422 9.809 1.00 76.27 C ANISOU 2407 CD GLN A 226 11161 7024 10794 1808 647 -1217 C ATOM 2408 OE1 GLN A 226 -8.704 -34.751 8.976 1.00 80.35 O ANISOU 2408 OE1 GLN A 226 11826 7502 11199 1692 672 -1302 O ATOM 2409 NE2 GLN A 226 -6.599 -34.888 9.777 1.00 80.22 N ANISOU 2409 NE2 GLN A 226 11538 7493 11447 1985 676 -1267 N ATOM 2410 N LYS A 227 -12.467 -32.087 12.272 1.00 45.14 N ANISOU 2410 N LYS A 227 7419 3305 6429 1111 338 -769 N ATOM 2411 CA LYS A 227 -13.752 -31.397 12.236 1.00 42.24 C ANISOU 2411 CA LYS A 227 7061 3062 5924 901 306 -729 C ATOM 2412 C LYS A 227 -13.884 -30.407 13.382 1.00 40.53 C ANISOU 2412 C LYS A 227 6701 3003 5696 849 243 -578 C ATOM 2413 O LYS A 227 -14.502 -29.346 13.211 1.00 41.08 O ANISOU 2413 O LYS A 227 6694 3250 5663 735 255 -561 O ATOM 2414 CB LYS A 227 -14.894 -32.404 12.273 1.00 43.02 C ANISOU 2414 CB LYS A 227 7354 2998 5996 762 235 -730 C ATOM 2415 CG LYS A 227 -14.916 -33.312 11.058 1.00 46.17 C ANISOU 2415 CG LYS A 227 7912 3247 6384 786 293 -895 C ATOM 2416 CD LYS A 227 -16.097 -34.233 11.097 1.00 53.23 C ANISOU 2416 CD LYS A 227 8990 3987 7248 624 216 -894 C ATOM 2417 CE LYS A 227 -15.968 -35.300 10.026 1.00 63.27 C ANISOU 2417 CE LYS A 227 10370 5134 8536 655 254 -1042 C ATOM 2418 NZ LYS A 227 -17.045 -36.324 10.161 1.00 69.53 N ANISOU 2418 NZ LYS A 227 11302 5792 9325 493 167 -1024 N ATOM 2419 N GLU A 228 -13.312 -30.726 14.546 1.00 37.36 N ANISOU 2419 N GLU A 228 6265 2536 5393 933 171 -469 N ATOM 2420 CA GLU A 228 -13.297 -29.767 15.647 1.00 37.35 C ANISOU 2420 CA GLU A 228 6129 2687 5377 898 115 -335 C ATOM 2421 C GLU A 228 -12.412 -28.573 15.327 1.00 36.44 C ANISOU 2421 C GLU A 228 5825 2758 5263 980 186 -363 C ATOM 2422 O GLU A 228 -12.735 -27.439 15.698 1.00 36.02 O ANISOU 2422 O GLU A 228 5667 2878 5142 898 175 -303 O ATOM 2423 CB GLU A 228 -12.824 -30.432 16.934 1.00 42.48 C ANISOU 2423 CB GLU A 228 6799 3217 6123 974 14 -213 C ATOM 2424 CG GLU A 228 -13.878 -31.236 17.655 1.00 47.46 C ANISOU 2424 CG GLU A 228 7589 3721 6724 838 -73 -126 C ATOM 2425 CD GLU A 228 -13.380 -31.725 18.999 1.00 52.57 C ANISOU 2425 CD GLU A 228 8254 4275 7446 908 -178 13 C ATOM 2426 OE1 GLU A 228 -12.864 -32.857 19.060 1.00 53.34 O ANISOU 2426 OE1 GLU A 228 8458 4167 7644 1018 -213 8 O ATOM 2427 OE2 GLU A 228 -13.474 -30.959 19.992 1.00 56.05 O ANISOU 2427 OE2 GLU A 228 8606 4848 7844 859 -229 126 O ATOM 2428 N VAL A 229 -11.276 -28.807 14.667 1.00 38.92 N ANISOU 2428 N VAL A 229 6092 3037 5659 1143 263 -454 N ATOM 2429 CA VAL A 229 -10.436 -27.688 14.244 1.00 41.10 C ANISOU 2429 CA VAL A 229 6190 3490 5935 1206 347 -489 C ATOM 2430 C VAL A 229 -11.193 -26.800 13.261 1.00 38.08 C ANISOU 2430 C VAL A 229 5809 3247 5411 1075 420 -552 C ATOM 2431 O VAL A 229 -11.186 -25.572 13.380 1.00 35.81 O ANISOU 2431 O VAL A 229 5399 3134 5073 1025 433 -510 O ATOM 2432 CB VAL A 229 -9.118 -28.205 13.642 1.00 43.56 C ANISOU 2432 CB VAL A 229 6451 3735 6364 1402 432 -587 C ATOM 2433 CG1 VAL A 229 -8.314 -27.038 13.058 1.00 44.72 C ANISOU 2433 CG1 VAL A 229 6419 4073 6500 1442 540 -632 C ATOM 2434 CG2 VAL A 229 -8.318 -28.939 14.692 1.00 41.66 C ANISOU 2434 CG2 VAL A 229 6183 3374 6273 1543 341 -511 C ATOM 2435 N HIS A 230 -11.880 -27.413 12.292 1.00 40.42 N ANISOU 2435 N HIS A 230 6255 3461 5640 1015 459 -650 N ATOM 2436 CA HIS A 230 -12.609 -26.654 11.283 1.00 40.86 C ANISOU 2436 CA HIS A 230 6330 3638 5557 896 515 -712 C ATOM 2437 C HIS A 230 -13.736 -25.841 11.913 1.00 36.22 C ANISOU 2437 C HIS A 230 5715 3162 4886 735 433 -610 C ATOM 2438 O HIS A 230 -13.980 -24.696 11.522 1.00 35.30 O ANISOU 2438 O HIS A 230 5522 3205 4684 672 464 -609 O ATOM 2439 CB HIS A 230 -13.155 -27.606 10.213 1.00 51.16 C ANISOU 2439 CB HIS A 230 7817 4815 6809 860 550 -836 C ATOM 2440 CG HIS A 230 -13.651 -26.912 8.980 1.00 61.26 C ANISOU 2440 CG HIS A 230 9121 6210 7945 771 618 -921 C ATOM 2441 ND1 HIS A 230 -14.948 -26.459 8.845 1.00 62.61 N ANISOU 2441 ND1 HIS A 230 9336 6451 8002 601 556 -893 N ATOM 2442 CD2 HIS A 230 -13.019 -26.584 7.827 1.00 64.15 C ANISOU 2442 CD2 HIS A 230 9476 6638 8261 830 742 -1029 C ATOM 2443 CE1 HIS A 230 -15.091 -25.883 7.664 1.00 62.43 C ANISOU 2443 CE1 HIS A 230 9334 6523 7864 562 625 -975 C ATOM 2444 NE2 HIS A 230 -13.935 -25.944 7.028 1.00 63.47 N ANISOU 2444 NE2 HIS A 230 9439 6651 8024 694 742 -1057 N ATOM 2445 N ALA A 231 -14.428 -26.416 12.895 1.00 33.89 N ANISOU 2445 N ALA A 231 5482 2782 4612 668 332 -524 N ATOM 2446 CA ALA A 231 -15.494 -25.690 13.565 1.00 38.95 C ANISOU 2446 CA ALA A 231 6089 3531 5182 522 264 -432 C ATOM 2447 C ALA A 231 -14.940 -24.528 14.382 1.00 37.14 C ANISOU 2447 C ALA A 231 5693 3450 4969 557 253 -344 C ATOM 2448 O ALA A 231 -15.535 -23.445 14.408 1.00 33.67 O ANISOU 2448 O ALA A 231 5185 3155 4452 468 248 -315 O ATOM 2449 CB ALA A 231 -16.301 -26.647 14.445 1.00 44.96 C ANISOU 2449 CB ALA A 231 6958 4162 5962 440 173 -360 C ATOM 2450 N ALA A 232 -13.796 -24.734 15.048 1.00 35.71 N ANISOU 2450 N ALA A 232 5445 3230 4892 690 242 -304 N ATOM 2451 CA ALA A 232 -13.200 -23.665 15.844 1.00 33.10 C ANISOU 2451 CA ALA A 232 4960 3036 4583 722 222 -227 C ATOM 2452 C ALA A 232 -12.711 -22.525 14.955 1.00 33.02 C ANISOU 2452 C ALA A 232 4839 3171 4537 740 313 -287 C ATOM 2453 O ALA A 232 -12.805 -21.354 15.339 1.00 30.05 O ANISOU 2453 O ALA A 232 4363 2933 4122 691 300 -236 O ATOM 2454 CB ALA A 232 -12.050 -24.210 16.696 1.00 31.61 C ANISOU 2454 CB ALA A 232 4724 2769 4519 864 178 -175 C ATOM 2455 N LYS A 233 -12.182 -22.846 13.765 1.00 34.32 N ANISOU 2455 N LYS A 233 5029 3301 4709 807 410 -398 N ATOM 2456 CA LYS A 233 -11.733 -21.791 12.862 1.00 36.68 C ANISOU 2456 CA LYS A 233 5239 3735 4961 812 507 -451 C ATOM 2457 C LYS A 233 -12.903 -20.940 12.389 1.00 32.70 C ANISOU 2457 C LYS A 233 4771 3331 4323 665 500 -449 C ATOM 2458 O LYS A 233 -12.794 -19.710 12.324 1.00 31.61 O ANISOU 2458 O LYS A 233 4536 3329 4145 633 520 -422 O ATOM 2459 CB LYS A 233 -10.991 -22.383 11.671 1.00 42.55 C ANISOU 2459 CB LYS A 233 6020 4421 5726 907 622 -575 C ATOM 2460 CG LYS A 233 -9.557 -22.727 11.989 1.00 49.70 C ANISOU 2460 CG LYS A 233 6818 5293 6775 1071 658 -583 C ATOM 2461 CD LYS A 233 -8.803 -23.262 10.774 1.00 50.84 C ANISOU 2461 CD LYS A 233 6986 5392 6939 1172 794 -717 C ATOM 2462 CE LYS A 233 -7.429 -23.765 11.184 1.00 51.41 C ANISOU 2462 CE LYS A 233 6943 5412 7176 1349 816 -726 C ATOM 2463 NZ LYS A 233 -6.733 -24.494 10.061 1.00 56.64 N ANISOU 2463 NZ LYS A 233 7643 6006 7872 1464 953 -870 N ATOM 2464 N SER A 234 -14.035 -21.580 12.078 1.00 32.07 N ANISOU 2464 N SER A 234 4826 3181 4178 576 463 -475 N ATOM 2465 CA SER A 234 -15.227 -20.837 11.687 1.00 32.11 C ANISOU 2465 CA SER A 234 4857 3277 4066 440 438 -469 C ATOM 2466 C SER A 234 -15.685 -19.907 12.801 1.00 32.00 C ANISOU 2466 C SER A 234 4749 3362 4049 380 366 -361 C ATOM 2467 O SER A 234 -16.030 -18.748 12.544 1.00 32.78 O ANISOU 2467 O SER A 234 4791 3584 4081 326 372 -347 O ATOM 2468 CB SER A 234 -16.335 -21.813 11.301 1.00 32.47 C ANISOU 2468 CB SER A 234 5052 3221 4065 353 397 -512 C ATOM 2469 OG SER A 234 -15.848 -22.706 10.321 1.00 35.78 O ANISOU 2469 OG SER A 234 5569 3537 4489 416 464 -621 O ATOM 2470 N ALA A 235 -15.682 -20.394 14.049 1.00 28.42 N ANISOU 2470 N ALA A 235 4286 2852 3661 391 297 -284 N ATOM 2471 CA ALA A 235 -16.061 -19.551 15.174 1.00 25.50 C ANISOU 2471 CA ALA A 235 3833 2574 3280 340 235 -189 C ATOM 2472 C ALA A 235 -15.075 -18.405 15.358 1.00 26.72 C ANISOU 2472 C ALA A 235 3854 2839 3461 403 265 -167 C ATOM 2473 O ALA A 235 -15.483 -17.272 15.646 1.00 26.62 O ANISOU 2473 O ALA A 235 3776 2937 3402 345 247 -130 O ATOM 2474 CB ALA A 235 -16.168 -20.391 16.457 1.00 23.40 C ANISOU 2474 CB ALA A 235 3604 2220 3068 341 161 -110 C ATOM 2475 N ALA A 236 -13.776 -18.678 15.177 1.00 27.51 N ANISOU 2475 N ALA A 236 3906 2905 3641 520 311 -194 N ATOM 2476 CA ALA A 236 -12.752 -17.636 15.304 1.00 26.24 C ANISOU 2476 CA ALA A 236 3607 2846 3517 574 343 -177 C ATOM 2477 C ALA A 236 -12.850 -16.585 14.195 1.00 26.14 C ANISOU 2477 C ALA A 236 3569 2934 3429 529 419 -225 C ATOM 2478 O ALA A 236 -12.546 -15.409 14.442 1.00 25.14 O ANISOU 2478 O ALA A 236 3346 2910 3297 512 420 -190 O ATOM 2479 CB ALA A 236 -11.354 -18.267 15.306 1.00 22.33 C ANISOU 2479 CB ALA A 236 3056 2293 3138 712 378 -202 C ATOM 2480 N ILE A 237 -13.227 -16.990 12.969 1.00 24.98 N ANISOU 2480 N ILE A 237 3517 2755 3220 509 479 -305 N ATOM 2481 CA ILE A 237 -13.441 -16.025 11.886 1.00 23.61 C ANISOU 2481 CA ILE A 237 3345 2672 2953 456 540 -341 C ATOM 2482 C ILE A 237 -14.530 -15.034 12.280 1.00 24.83 C ANISOU 2482 C ILE A 237 3490 2907 3039 353 469 -282 C ATOM 2483 O ILE A 237 -14.401 -13.821 12.058 1.00 24.59 O ANISOU 2483 O ILE A 237 3399 2971 2974 327 488 -262 O ATOM 2484 CB ILE A 237 -13.784 -16.752 10.564 1.00 25.75 C ANISOU 2484 CB ILE A 237 3743 2886 3153 443 600 -437 C ATOM 2485 CG1 ILE A 237 -12.557 -17.474 9.981 1.00 26.38 C ANISOU 2485 CG1 ILE A 237 3819 2909 3295 557 703 -512 C ATOM 2486 CG2 ILE A 237 -14.374 -15.779 9.512 1.00 25.29 C ANISOU 2486 CG2 ILE A 237 3720 2918 2968 362 628 -457 C ATOM 2487 CD1 ILE A 237 -12.904 -18.558 8.931 1.00 25.88 C ANISOU 2487 CD1 ILE A 237 3906 2749 3177 559 746 -615 C ATOM 2488 N ILE A 238 -15.610 -15.534 12.894 1.00 21.83 N ANISOU 2488 N ILE A 238 3164 2486 2642 294 388 -253 N ATOM 2489 CA ILE A 238 -16.727 -14.680 13.301 1.00 23.23 C ANISOU 2489 CA ILE A 238 3325 2738 2763 204 323 -206 C ATOM 2490 C ILE A 238 -16.274 -13.675 14.363 1.00 22.31 C ANISOU 2490 C ILE A 238 3096 2694 2687 221 296 -137 C ATOM 2491 O ILE A 238 -16.600 -12.483 14.304 1.00 24.81 O ANISOU 2491 O ILE A 238 3370 3095 2963 181 287 -117 O ATOM 2492 CB ILE A 238 -17.894 -15.551 13.815 1.00 27.68 C ANISOU 2492 CB ILE A 238 3958 3243 3315 137 255 -191 C ATOM 2493 CG1 ILE A 238 -18.399 -16.503 12.723 1.00 33.29 C ANISOU 2493 CG1 ILE A 238 4787 3879 3982 107 271 -267 C ATOM 2494 CG2 ILE A 238 -19.022 -14.692 14.377 1.00 25.19 C ANISOU 2494 CG2 ILE A 238 3603 3011 2957 55 195 -144 C ATOM 2495 CD1 ILE A 238 -19.386 -15.866 11.802 1.00 34.29 C ANISOU 2495 CD1 ILE A 238 4943 4074 4014 27 256 -296 C ATOM 2496 N ALA A 239 -15.527 -14.142 15.361 1.00 24.12 N ANISOU 2496 N ALA A 239 3284 2885 2996 279 275 -100 N ATOM 2497 CA ALA A 239 -14.985 -13.223 16.367 1.00 24.24 C ANISOU 2497 CA ALA A 239 3196 2966 3047 295 243 -42 C ATOM 2498 C ALA A 239 -14.016 -12.219 15.739 1.00 25.30 C ANISOU 2498 C ALA A 239 3252 3167 3196 326 305 -61 C ATOM 2499 O ALA A 239 -14.031 -11.024 16.080 1.00 24.47 O ANISOU 2499 O ALA A 239 3085 3136 3075 294 287 -31 O ATOM 2500 CB ALA A 239 -14.294 -14.013 17.487 1.00 23.86 C ANISOU 2500 CB ALA A 239 3128 2860 3079 357 197 1 C ATOM 2501 N GLY A 240 -13.173 -12.681 14.817 1.00 21.56 N ANISOU 2501 N GLY A 240 2779 2662 2749 383 384 -115 N ATOM 2502 CA GLY A 240 -12.227 -11.774 14.186 1.00 23.69 C ANISOU 2502 CA GLY A 240 2972 2998 3032 401 458 -131 C ATOM 2503 C GLY A 240 -12.907 -10.714 13.338 1.00 24.25 C ANISOU 2503 C GLY A 240 3078 3132 3005 324 482 -138 C ATOM 2504 O GLY A 240 -12.451 -9.566 13.287 1.00 26.78 O ANISOU 2504 O GLY A 240 3331 3517 3325 304 502 -116 O ATOM 2505 N LEU A 241 -14.018 -11.077 12.675 1.00 21.13 N ANISOU 2505 N LEU A 241 2790 2712 2525 276 471 -166 N ATOM 2506 CA LEU A 241 -14.768 -10.113 11.868 1.00 21.68 C ANISOU 2506 CA LEU A 241 2902 2837 2498 208 473 -167 C ATOM 2507 C LEU A 241 -15.519 -9.097 12.731 1.00 20.58 C ANISOU 2507 C LEU A 241 2723 2748 2350 160 391 -109 C ATOM 2508 O LEU A 241 -15.675 -7.943 12.329 1.00 21.24 O ANISOU 2508 O LEU A 241 2797 2882 2390 126 393 -92 O ATOM 2509 CB LEU A 241 -15.733 -10.847 10.942 1.00 25.34 C ANISOU 2509 CB LEU A 241 3485 3262 2880 172 468 -217 C ATOM 2510 CG LEU A 241 -15.015 -11.588 9.796 1.00 30.46 C ANISOU 2510 CG LEU A 241 4194 3873 3508 212 567 -290 C ATOM 2511 CD1 LEU A 241 -15.987 -12.472 9.046 1.00 31.28 C ANISOU 2511 CD1 LEU A 241 4425 3925 3535 173 545 -345 C ATOM 2512 CD2 LEU A 241 -14.258 -10.626 8.828 1.00 29.99 C ANISOU 2512 CD2 LEU A 241 4117 3877 3400 208 659 -299 C ATOM 2513 N PHE A 242 -16.024 -9.511 13.895 1.00 16.89 N ANISOU 2513 N PHE A 242 2239 2261 1917 157 320 -79 N ATOM 2514 CA PHE A 242 -16.571 -8.547 14.846 1.00 19.30 C ANISOU 2514 CA PHE A 242 2497 2616 2222 124 256 -32 C ATOM 2515 C PHE A 242 -15.521 -7.492 15.199 1.00 21.28 C ANISOU 2515 C PHE A 242 2662 2908 2515 145 274 -6 C ATOM 2516 O PHE A 242 -15.779 -6.279 15.134 1.00 19.63 O ANISOU 2516 O PHE A 242 2436 2744 2280 113 260 11 O ATOM 2517 CB PHE A 242 -17.079 -9.281 16.111 1.00 17.88 C ANISOU 2517 CB PHE A 242 2314 2409 2069 119 195 -4 C ATOM 2518 CG PHE A 242 -17.674 -8.358 17.162 1.00 16.93 C ANISOU 2518 CG PHE A 242 2151 2343 1940 88 140 35 C ATOM 2519 CD1 PHE A 242 -16.843 -7.676 18.054 1.00 17.90 C ANISOU 2519 CD1 PHE A 242 2205 2493 2105 113 125 65 C ATOM 2520 CD2 PHE A 242 -19.045 -8.126 17.214 1.00 17.48 C ANISOU 2520 CD2 PHE A 242 2243 2439 1960 35 105 34 C ATOM 2521 CE1 PHE A 242 -17.376 -6.787 19.017 1.00 19.29 C ANISOU 2521 CE1 PHE A 242 2351 2716 2264 86 78 88 C ATOM 2522 CE2 PHE A 242 -19.591 -7.246 18.196 1.00 21.07 C ANISOU 2522 CE2 PHE A 242 2654 2945 2408 16 65 59 C ATOM 2523 CZ PHE A 242 -18.759 -6.591 19.091 1.00 14.91 C ANISOU 2523 CZ PHE A 242 1821 2184 1659 41 55 83 C ATOM 2524 N ALA A 243 -14.303 -7.940 15.510 1.00 17.98 N ANISOU 2524 N ALA A 243 2188 2471 2170 199 302 -6 N ATOM 2525 CA ALA A 243 -13.236 -7.007 15.846 1.00 19.66 C ANISOU 2525 CA ALA A 243 2309 2726 2436 210 315 15 C ATOM 2526 C ALA A 243 -12.917 -6.076 14.674 1.00 19.46 C ANISOU 2526 C ALA A 243 2286 2734 2375 181 386 1 C ATOM 2527 O ALA A 243 -12.809 -4.855 14.847 1.00 22.82 O ANISOU 2527 O ALA A 243 2677 3197 2798 145 371 27 O ATOM 2528 CB ALA A 243 -11.998 -7.789 16.290 1.00 22.76 C ANISOU 2528 CB ALA A 243 2632 3093 2921 280 329 14 C ATOM 2529 N ALEU A 244 -12.771 -6.639 13.471 0.57 19.90 N ANISOU 2529 N ALEU A 244 2393 2772 2396 192 463 -40 N ATOM 2530 N BLEU A 244 -12.784 -6.632 13.472 0.43 19.94 N ANISOU 2530 N BLEU A 244 2398 2777 2400 192 463 -40 N ATOM 2531 CA ALEU A 244 -12.441 -5.833 12.297 0.57 21.63 C ANISOU 2531 CA ALEU A 244 2631 3023 2564 159 540 -49 C ATOM 2532 CA BLEU A 244 -12.438 -5.809 12.317 0.43 21.42 C ANISOU 2532 CA BLEU A 244 2603 2998 2539 159 539 -48 C ATOM 2533 C ALEU A 244 -13.491 -4.753 12.039 0.57 20.83 C ANISOU 2533 C ALEU A 244 2588 2944 2383 96 491 -20 C ATOM 2534 C BLEU A 244 -13.497 -4.745 12.036 0.43 20.78 C ANISOU 2534 C BLEU A 244 2582 2938 2376 96 490 -20 C ATOM 2535 O ALEU A 244 -13.147 -3.622 11.673 0.57 21.72 O ANISOU 2535 O ALEU A 244 2688 3085 2480 60 516 5 O ATOM 2536 O BLEU A 244 -13.162 -3.618 11.650 0.43 21.56 O ANISOU 2536 O BLEU A 244 2670 3065 2458 59 516 5 O ATOM 2537 CB ALEU A 244 -12.292 -6.728 11.055 0.57 21.11 C ANISOU 2537 CB ALEU A 244 2637 2934 2451 179 629 -106 C ATOM 2538 CB BLEU A 244 -12.237 -6.690 11.083 0.43 21.34 C ANISOU 2538 CB BLEU A 244 2660 2965 2484 180 630 -104 C ATOM 2539 CG ALEU A 244 -11.816 -6.053 9.757 0.57 23.13 C ANISOU 2539 CG ALEU A 244 2922 3225 2640 145 730 -118 C ATOM 2540 CG BLEU A 244 -10.860 -7.340 11.000 0.43 23.30 C ANISOU 2540 CG BLEU A 244 2829 3206 2817 246 718 -137 C ATOM 2541 CD1ALEU A 244 -10.336 -5.633 9.864 0.57 24.08 C ANISOU 2541 CD1ALEU A 244 2921 3381 2846 163 813 -111 C ATOM 2542 CD1BLEU A 244 -10.614 -7.852 9.601 0.43 24.34 C ANISOU 2542 CD1BLEU A 244 3033 3330 2884 256 832 -199 C ATOM 2543 CD2ALEU A 244 -12.035 -6.938 8.492 0.57 24.57 C ANISOU 2543 CD2ALEU A 244 3215 3383 2736 154 802 -183 C ATOM 2544 CD2BLEU A 244 -9.773 -6.341 11.420 0.43 24.49 C ANISOU 2544 CD2BLEU A 244 2854 3409 3042 236 742 -102 C ATOM 2545 N CYS A 245 -14.778 -5.091 12.194 1.00 17.38 N ANISOU 2545 N CYS A 245 2214 2490 1898 82 420 -23 N ATOM 2546 CA CYS A 245 -15.849 -4.144 11.879 1.00 18.44 C ANISOU 2546 CA CYS A 245 2399 2644 1964 37 366 -2 C ATOM 2547 C CYS A 245 -16.009 -3.065 12.944 1.00 20.51 C ANISOU 2547 C CYS A 245 2600 2925 2266 26 304 38 C ATOM 2548 O CYS A 245 -16.331 -1.914 12.619 1.00 18.42 O ANISOU 2548 O CYS A 245 2357 2673 1969 -2 284 62 O ATOM 2549 CB CYS A 245 -17.176 -4.886 11.695 1.00 22.40 C ANISOU 2549 CB CYS A 245 2968 3130 2414 24 310 -24 C ATOM 2550 SG CYS A 245 -17.232 -5.939 10.176 1.00 26.69 S ANISOU 2550 SG CYS A 245 3618 3646 2876 18 370 -81 S ATOM 2551 N TRP A 246 -15.820 -3.412 14.220 1.00 18.36 N ANISOU 2551 N TRP A 246 2266 2651 2059 49 268 45 N ATOM 2552 CA TRP A 246 -16.033 -2.462 15.308 1.00 19.38 C ANISOU 2552 CA TRP A 246 2350 2798 2216 39 208 71 C ATOM 2553 C TRP A 246 -14.815 -1.617 15.635 1.00 21.51 C ANISOU 2553 C TRP A 246 2554 3079 2541 34 228 89 C ATOM 2554 O TRP A 246 -14.972 -0.518 16.177 1.00 18.60 O ANISOU 2554 O TRP A 246 2170 2718 2180 14 187 105 O ATOM 2555 CB TRP A 246 -16.457 -3.208 16.578 1.00 19.86 C ANISOU 2555 CB TRP A 246 2387 2856 2302 56 156 72 C ATOM 2556 CG TRP A 246 -17.902 -3.556 16.503 1.00 22.44 C ANISOU 2556 CG TRP A 246 2762 3184 2578 38 120 61 C ATOM 2557 CD1 TRP A 246 -18.459 -4.745 16.095 1.00 23.10 C ANISOU 2557 CD1 TRP A 246 2892 3246 2640 34 126 42 C ATOM 2558 CD2 TRP A 246 -18.980 -2.663 16.742 1.00 20.08 C ANISOU 2558 CD2 TRP A 246 2466 2910 2252 20 73 65 C ATOM 2559 NE1 TRP A 246 -19.829 -4.648 16.114 1.00 21.86 N ANISOU 2559 NE1 TRP A 246 2755 3106 2444 6 82 37 N ATOM 2560 CE2 TRP A 246 -20.179 -3.380 16.510 1.00 21.34 C ANISOU 2560 CE2 TRP A 246 2658 3072 2377 4 50 50 C ATOM 2561 CE3 TRP A 246 -19.055 -1.326 17.156 1.00 17.98 C ANISOU 2561 CE3 TRP A 246 2178 2660 1994 18 46 76 C ATOM 2562 CZ2 TRP A 246 -21.448 -2.800 16.683 1.00 18.48 C ANISOU 2562 CZ2 TRP A 246 2288 2739 1994 -9 4 45 C ATOM 2563 CZ3 TRP A 246 -20.320 -0.749 17.339 1.00 15.82 C ANISOU 2563 CZ3 TRP A 246 1908 2404 1697 14 1 68 C ATOM 2564 CH2 TRP A 246 -21.498 -1.485 17.089 1.00 18.70 C ANISOU 2564 CH2 TRP A 246 2290 2783 2034 3 -18 54 C ATOM 2565 N LEU A 247 -13.608 -2.133 15.394 1.00 21.33 N ANISOU 2565 N LEU A 247 2484 3055 2565 54 288 81 N ATOM 2566 CA LEU A 247 -12.407 -1.420 15.824 1.00 21.96 C ANISOU 2566 CA LEU A 247 2478 3152 2713 44 300 97 C ATOM 2567 C LEU A 247 -12.262 -0.036 15.211 1.00 21.78 C ANISOU 2567 C LEU A 247 2471 3135 2669 -11 322 117 C ATOM 2568 O LEU A 247 -11.839 0.875 15.945 1.00 21.64 O ANISOU 2568 O LEU A 247 2405 3122 2694 -37 284 133 O ATOM 2569 CB LEU A 247 -11.148 -2.254 15.535 1.00 26.94 C ANISOU 2569 CB LEU A 247 3042 3787 3407 81 369 81 C ATOM 2570 CG LEU A 247 -10.726 -3.317 16.561 1.00 29.88 C ANISOU 2570 CG LEU A 247 3358 4148 3846 139 326 78 C ATOM 2571 CD1 LEU A 247 -9.557 -4.160 15.995 1.00 29.15 C ANISOU 2571 CD1 LEU A 247 3204 4054 3819 191 407 53 C ATOM 2572 CD2 LEU A 247 -10.317 -2.643 17.869 1.00 30.76 C ANISOU 2572 CD2 LEU A 247 3400 4280 4009 127 246 103 C ATOM 2573 N PRO A 248 -12.573 0.212 13.920 1.00 20.87 N ANISOU 2573 N PRO A 248 2430 3015 2486 -36 375 119 N ATOM 2574 CA PRO A 248 -12.351 1.579 13.397 1.00 18.39 C ANISOU 2574 CA PRO A 248 2138 2696 2154 -94 392 150 C ATOM 2575 C PRO A 248 -13.100 2.644 14.167 1.00 17.34 C ANISOU 2575 C PRO A 248 2024 2542 2021 -109 300 168 C ATOM 2576 O PRO A 248 -12.538 3.708 14.447 1.00 21.18 O ANISOU 2576 O PRO A 248 2486 3018 2545 -150 292 189 O ATOM 2577 CB PRO A 248 -12.829 1.479 11.942 1.00 15.12 C ANISOU 2577 CB PRO A 248 1825 2276 1642 -109 444 152 C ATOM 2578 CG PRO A 248 -12.493 0.065 11.582 1.00 17.77 C ANISOU 2578 CG PRO A 248 2149 2624 1978 -68 505 111 C ATOM 2579 CD PRO A 248 -12.933 -0.705 12.823 1.00 18.63 C ANISOU 2579 CD PRO A 248 2215 2725 2137 -20 428 94 C ATOM 2580 N LEU A 249 -14.350 2.382 14.536 1.00 19.25 N ANISOU 2580 N LEU A 249 2308 2778 2227 -79 234 156 N ATOM 2581 CA LEU A 249 -15.127 3.352 15.304 1.00 21.36 C ANISOU 2581 CA LEU A 249 2590 3029 2499 -80 154 161 C ATOM 2582 C LEU A 249 -14.524 3.572 16.694 1.00 19.08 C ANISOU 2582 C LEU A 249 2226 2747 2276 -79 118 152 C ATOM 2583 O LEU A 249 -14.427 4.715 17.158 1.00 17.50 O ANISOU 2583 O LEU A 249 2026 2524 2098 -103 82 157 O ATOM 2584 CB LEU A 249 -16.577 2.873 15.399 1.00 22.44 C ANISOU 2584 CB LEU A 249 2766 3171 2589 -46 104 144 C ATOM 2585 CG LEU A 249 -17.721 3.773 15.867 1.00 23.15 C ANISOU 2585 CG LEU A 249 2879 3248 2669 -32 32 141 C ATOM 2586 CD1 LEU A 249 -17.801 5.100 15.095 1.00 21.53 C ANISOU 2586 CD1 LEU A 249 2733 3001 2446 -52 19 171 C ATOM 2587 CD2 LEU A 249 -19.054 3.017 15.761 1.00 23.00 C ANISOU 2587 CD2 LEU A 249 2877 3250 2610 -5 1 122 C ATOM 2588 N HIS A 250 -14.113 2.493 17.372 1.00 14.69 N ANISOU 2588 N HIS A 250 1615 2216 1752 -52 119 137 N ATOM 2589 CA HIS A 250 -13.438 2.647 18.665 1.00 18.32 C ANISOU 2589 CA HIS A 250 2008 2687 2266 -53 75 132 C ATOM 2590 C HIS A 250 -12.132 3.416 18.545 1.00 19.47 C ANISOU 2590 C HIS A 250 2096 2830 2470 -97 98 145 C ATOM 2591 O HIS A 250 -11.821 4.268 19.394 1.00 18.34 O ANISOU 2591 O HIS A 250 1930 2680 2358 -124 46 141 O ATOM 2592 CB HIS A 250 -13.177 1.282 19.289 1.00 18.04 C ANISOU 2592 CB HIS A 250 1933 2671 2250 -12 69 126 C ATOM 2593 CG HIS A 250 -14.412 0.651 19.844 1.00 16.94 C ANISOU 2593 CG HIS A 250 1839 2535 2063 12 32 116 C ATOM 2594 ND1 HIS A 250 -15.074 1.167 20.942 1.00 17.75 N ANISOU 2594 ND1 HIS A 250 1952 2646 2145 8 -27 106 N ATOM 2595 CD2 HIS A 250 -15.105 -0.448 19.459 1.00 16.16 C ANISOU 2595 CD2 HIS A 250 1776 2433 1932 34 50 111 C ATOM 2596 CE1 HIS A 250 -16.126 0.407 21.211 1.00 17.05 C ANISOU 2596 CE1 HIS A 250 1895 2567 2015 24 -36 100 C ATOM 2597 NE2 HIS A 250 -16.172 -0.574 20.321 1.00 16.38 N ANISOU 2597 NE2 HIS A 250 1827 2472 1926 36 5 105 N ATOM 2598 N ILE A 251 -11.345 3.123 17.507 1.00 15.52 N ANISOU 2598 N ILE A 251 1573 2338 1986 -109 179 156 N ATOM 2599 CA ILE A 251 -10.080 3.829 17.305 1.00 15.93 C ANISOU 2599 CA ILE A 251 1558 2396 2100 -162 216 169 C ATOM 2600 C ILE A 251 -10.321 5.318 17.061 1.00 16.91 C ANISOU 2600 C ILE A 251 1739 2481 2207 -226 199 189 C ATOM 2601 O ILE A 251 -9.575 6.175 17.561 1.00 17.01 O ANISOU 2601 O ILE A 251 1704 2484 2274 -278 175 194 O ATOM 2602 CB ILE A 251 -9.294 3.169 16.154 1.00 21.30 C ANISOU 2602 CB ILE A 251 2205 3099 2791 -160 326 171 C ATOM 2603 CG1 ILE A 251 -8.808 1.765 16.574 1.00 20.38 C ANISOU 2603 CG1 ILE A 251 2015 3008 2721 -91 332 149 C ATOM 2604 CG2 ILE A 251 -8.113 4.052 15.702 1.00 18.86 C ANISOU 2604 CG2 ILE A 251 1833 2799 2534 -234 386 191 C ATOM 2605 CD1 ILE A 251 -8.318 0.887 15.404 1.00 19.54 C ANISOU 2605 CD1 ILE A 251 1898 2915 2610 -65 445 133 C ATOM 2606 N ILE A 252 -11.355 5.657 16.292 1.00 15.90 N ANISOU 2606 N ILE A 252 1714 2323 2005 -222 204 201 N ATOM 2607 CA ILE A 252 -11.677 7.071 16.070 1.00 17.02 C ANISOU 2607 CA ILE A 252 1925 2411 2132 -270 176 224 C ATOM 2608 C ILE A 252 -12.026 7.768 17.389 1.00 18.59 C ANISOU 2608 C ILE A 252 2119 2585 2359 -264 83 199 C ATOM 2609 O ILE A 252 -11.583 8.892 17.638 1.00 19.97 O ANISOU 2609 O ILE A 252 2300 2718 2570 -318 59 207 O ATOM 2610 CB ILE A 252 -12.806 7.210 15.029 1.00 17.99 C ANISOU 2610 CB ILE A 252 2159 2508 2169 -252 181 243 C ATOM 2611 CG1 ILE A 252 -12.307 6.809 13.626 1.00 17.10 C ANISOU 2611 CG1 ILE A 252 2072 2412 2012 -280 279 269 C ATOM 2612 CG2 ILE A 252 -13.344 8.663 15.004 1.00 15.34 C ANISOU 2612 CG2 ILE A 252 1902 2102 1825 -277 125 266 C ATOM 2613 CD1 ILE A 252 -13.424 6.712 12.590 1.00 19.31 C ANISOU 2613 CD1 ILE A 252 2463 2678 2195 -258 272 284 C ATOM 2614 N ASN A 253 -12.815 7.118 18.254 1.00 17.68 N ANISOU 2614 N ASN A 253 1999 2492 2226 -203 32 167 N ATOM 2615 CA ASN A 253 -13.086 7.685 19.579 1.00 23.47 C ANISOU 2615 CA ASN A 253 2729 3213 2976 -196 -45 135 C ATOM 2616 C ASN A 253 -11.793 7.922 20.354 1.00 22.89 C ANISOU 2616 C ASN A 253 2578 3151 2969 -244 -65 128 C ATOM 2617 O ASN A 253 -11.651 8.949 21.037 1.00 21.13 O ANISOU 2617 O ASN A 253 2369 2892 2767 -278 -118 110 O ATOM 2618 CB ASN A 253 -14.016 6.774 20.400 1.00 23.15 C ANISOU 2618 CB ASN A 253 2687 3209 2899 -134 -77 106 C ATOM 2619 CG ASN A 253 -15.408 6.644 19.799 1.00 26.37 C ANISOU 2619 CG ASN A 253 3159 3611 3252 -93 -74 105 C ATOM 2620 OD1 ASN A 253 -15.825 7.462 18.963 1.00 28.43 O ANISOU 2620 OD1 ASN A 253 3476 3829 3497 -100 -72 121 O ATOM 2621 ND2 ASN A 253 -16.146 5.609 20.224 1.00 21.88 N ANISOU 2621 ND2 ASN A 253 2579 3081 2653 -52 -79 89 N ATOM 2622 N CYS A 254 -10.840 6.976 20.267 1.00 18.92 N ANISOU 2622 N CYS A 254 1990 2696 2503 -242 -30 139 N ATOM 2623 CA CYS A 254 -9.543 7.156 20.917 1.00 17.95 C ANISOU 2623 CA CYS A 254 1774 2593 2455 -286 -56 135 C ATOM 2624 C CYS A 254 -8.830 8.408 20.404 1.00 16.41 C ANISOU 2624 C CYS A 254 1575 2358 2302 -375 -35 152 C ATOM 2625 O CYS A 254 -8.239 9.160 21.190 1.00 19.99 O ANISOU 2625 O CYS A 254 1997 2797 2802 -428 -94 137 O ATOM 2626 CB CYS A 254 -8.656 5.910 20.708 1.00 18.20 C ANISOU 2626 CB CYS A 254 1706 2678 2530 -256 -12 145 C ATOM 2627 SG CYS A 254 -9.207 4.442 21.635 1.00 19.01 S ANISOU 2627 SG CYS A 254 1807 2815 2602 -167 -60 132 S ATOM 2628 N PHE A 255 -8.861 8.650 19.091 1.00 16.74 N ANISOU 2628 N PHE A 255 1656 2380 2326 -401 47 186 N ATOM 2629 CA PHE A 255 -8.241 9.873 18.563 1.00 18.43 C ANISOU 2629 CA PHE A 255 1884 2547 2573 -498 72 212 C ATOM 2630 C PHE A 255 -8.955 11.118 19.091 1.00 19.44 C ANISOU 2630 C PHE A 255 2109 2595 2684 -517 -7 199 C ATOM 2631 O PHE A 255 -8.310 12.061 19.550 1.00 22.58 O ANISOU 2631 O PHE A 255 2492 2954 3135 -593 -44 193 O ATOM 2632 CB PHE A 255 -8.219 9.853 17.019 1.00 17.87 C ANISOU 2632 CB PHE A 255 1858 2470 2462 -522 178 257 C ATOM 2633 CG PHE A 255 -7.006 9.159 16.445 1.00 18.57 C ANISOU 2633 CG PHE A 255 1833 2623 2598 -549 276 268 C ATOM 2634 CD1 PHE A 255 -5.818 9.862 16.231 1.00 20.58 C ANISOU 2634 CD1 PHE A 255 2015 2881 2923 -651 320 288 C ATOM 2635 CD2 PHE A 255 -7.033 7.799 16.176 1.00 19.85 C ANISOU 2635 CD2 PHE A 255 1955 2844 2745 -472 323 251 C ATOM 2636 CE1 PHE A 255 -4.685 9.232 15.725 1.00 23.69 C ANISOU 2636 CE1 PHE A 255 2286 3344 3372 -670 419 291 C ATOM 2637 CE2 PHE A 255 -5.886 7.147 15.689 1.00 22.21 C ANISOU 2637 CE2 PHE A 255 2140 3201 3098 -482 417 250 C ATOM 2638 CZ PHE A 255 -4.720 7.867 15.454 1.00 24.04 C ANISOU 2638 CZ PHE A 255 2288 3445 3401 -578 469 269 C ATOM 2639 N THR A 256 -10.290 11.138 19.024 1.00 20.91 N ANISOU 2639 N THR A 256 2391 2751 2802 -450 -33 190 N ATOM 2640 CA THR A 256 -11.067 12.259 19.562 1.00 22.24 C ANISOU 2640 CA THR A 256 2649 2841 2959 -445 -106 167 C ATOM 2641 C THR A 256 -10.683 12.528 21.013 1.00 22.41 C ANISOU 2641 C THR A 256 2629 2867 3018 -459 -182 113 C ATOM 2642 O THR A 256 -10.418 13.674 21.401 1.00 23.25 O ANISOU 2642 O THR A 256 2772 2904 3157 -516 -227 97 O ATOM 2643 CB THR A 256 -12.564 11.936 19.454 1.00 21.38 C ANISOU 2643 CB THR A 256 2609 2730 2783 -350 -124 153 C ATOM 2644 OG1 THR A 256 -12.906 11.691 18.080 1.00 23.06 O ANISOU 2644 OG1 THR A 256 2868 2941 2953 -342 -66 202 O ATOM 2645 CG2 THR A 256 -13.467 13.073 20.055 1.00 16.31 C ANISOU 2645 CG2 THR A 256 2052 2009 2137 -323 -195 117 C ATOM 2646 N PHE A 257 -10.608 11.453 21.813 1.00 18.95 N ANISOU 2646 N PHE A 257 2121 2507 2572 -413 -201 87 N ATOM 2647 CA PHE A 257 -10.363 11.562 23.248 1.00 22.19 C ANISOU 2647 CA PHE A 257 2506 2933 2994 -417 -281 37 C ATOM 2648 C PHE A 257 -8.918 11.936 23.571 1.00 22.59 C ANISOU 2648 C PHE A 257 2473 2990 3121 -507 -308 39 C ATOM 2649 O PHE A 257 -8.666 12.869 24.355 1.00 22.61 O ANISOU 2649 O PHE A 257 2500 2948 3142 -559 -377 2 O ATOM 2650 CB PHE A 257 -10.727 10.233 23.918 1.00 18.18 C ANISOU 2650 CB PHE A 257 1961 2503 2445 -343 -292 24 C ATOM 2651 CG PHE A 257 -10.608 10.250 25.429 1.00 20.93 C ANISOU 2651 CG PHE A 257 2302 2874 2777 -342 -377 -24 C ATOM 2652 CD1 PHE A 257 -11.394 11.106 26.197 1.00 21.51 C ANISOU 2652 CD1 PHE A 257 2459 2905 2808 -333 -422 -78 C ATOM 2653 CD2 PHE A 257 -9.731 9.371 26.086 1.00 22.52 C ANISOU 2653 CD2 PHE A 257 2417 3141 3000 -344 -412 -16 C ATOM 2654 CE1 PHE A 257 -11.318 11.102 27.601 1.00 23.14 C ANISOU 2654 CE1 PHE A 257 2674 3137 2979 -334 -495 -127 C ATOM 2655 CE2 PHE A 257 -9.629 9.372 27.482 1.00 26.37 C ANISOU 2655 CE2 PHE A 257 2913 3652 3456 -346 -499 -54 C ATOM 2656 CZ PHE A 257 -10.427 10.257 28.246 1.00 25.96 C ANISOU 2656 CZ PHE A 257 2956 3561 3347 -346 -538 -112 C ATOM 2657 N PHE A 258 -7.948 11.185 23.027 1.00 21.36 N ANISOU 2657 N PHE A 258 2212 2891 3012 -527 -257 75 N ATOM 2658 CA PHE A 258 -6.556 11.337 23.451 1.00 20.66 C ANISOU 2658 CA PHE A 258 2010 2831 3007 -602 -289 74 C ATOM 2659 C PHE A 258 -5.809 12.430 22.707 1.00 23.15 C ANISOU 2659 C PHE A 258 2316 3095 3384 -715 -251 99 C ATOM 2660 O PHE A 258 -4.746 12.860 23.177 1.00 22.18 O ANISOU 2660 O PHE A 258 2109 2981 3335 -798 -295 89 O ATOM 2661 CB PHE A 258 -5.783 10.025 23.259 1.00 21.39 C ANISOU 2661 CB PHE A 258 1975 3012 3141 -564 -251 96 C ATOM 2662 CG PHE A 258 -6.162 8.951 24.219 1.00 21.18 C ANISOU 2662 CG PHE A 258 1940 3034 3075 -476 -311 77 C ATOM 2663 CD1 PHE A 258 -6.053 9.168 25.593 1.00 22.93 C ANISOU 2663 CD1 PHE A 258 2163 3263 3285 -485 -425 41 C ATOM 2664 CD2 PHE A 258 -6.596 7.706 23.758 1.00 21.61 C ANISOU 2664 CD2 PHE A 258 1991 3122 3098 -391 -255 96 C ATOM 2665 CE1 PHE A 258 -6.389 8.162 26.494 1.00 23.54 C ANISOU 2665 CE1 PHE A 258 2245 3386 3315 -412 -479 34 C ATOM 2666 CE2 PHE A 258 -6.942 6.700 24.643 1.00 21.30 C ANISOU 2666 CE2 PHE A 258 1954 3119 3022 -320 -309 88 C ATOM 2667 CZ PHE A 258 -6.839 6.927 26.022 1.00 23.42 C ANISOU 2667 CZ PHE A 258 2228 3397 3273 -330 -419 61 C ATOM 2668 N CYS A 259 -6.315 12.892 21.565 1.00 22.66 N ANISOU 2668 N CYS A 259 2338 2979 3292 -727 -176 136 N ATOM 2669 CA CYS A 259 -5.646 13.936 20.787 1.00 26.09 C ANISOU 2669 CA CYS A 259 2782 3357 3774 -843 -131 173 C ATOM 2670 C CYS A 259 -6.585 15.131 20.605 1.00 28.11 C ANISOU 2670 C CYS A 259 3200 3494 3987 -855 -160 175 C ATOM 2671 O CYS A 259 -7.138 15.340 19.518 1.00 27.28 O ANISOU 2671 O CYS A 259 3180 3348 3837 -846 -99 221 O ATOM 2672 CB CYS A 259 -5.168 13.407 19.434 1.00 30.06 C ANISOU 2672 CB CYS A 259 3236 3903 4281 -861 -1 228 C ATOM 2673 SG CYS A 259 -4.028 14.573 18.630 1.00 39.71 S ANISOU 2673 SG CYS A 259 4434 5081 5574 -1031 65 278 S ATOM 2674 N PRO A 260 -6.793 15.935 21.654 1.00 31.79 N ANISOU 2674 N PRO A 260 3717 3900 4464 -871 -259 123 N ATOM 2675 CA PRO A 260 -7.575 17.177 21.476 1.00 36.25 C ANISOU 2675 CA PRO A 260 4433 4334 5006 -883 -289 120 C ATOM 2676 C PRO A 260 -6.911 18.198 20.552 1.00 38.66 C ANISOU 2676 C PRO A 260 4776 4555 5356 -1009 -246 180 C ATOM 2677 O PRO A 260 -7.598 19.120 20.094 1.00 42.61 O ANISOU 2677 O PRO A 260 5415 4942 5835 -1009 -256 201 O ATOM 2678 CB PRO A 260 -7.713 17.728 22.908 1.00 35.94 C ANISOU 2678 CB PRO A 260 4423 4258 4975 -880 -399 37 C ATOM 2679 CG PRO A 260 -6.580 17.098 23.676 1.00 35.57 C ANISOU 2679 CG PRO A 260 4232 4308 4976 -927 -432 16 C ATOM 2680 CD PRO A 260 -6.415 15.716 23.061 1.00 31.14 C ANISOU 2680 CD PRO A 260 3570 3860 4402 -867 -353 59 C ATOM 2681 N ASP A 261 -5.607 18.076 20.275 1.00 34.46 N ANISOU 2681 N ASP A 261 4126 4075 4892 -1117 -198 210 N ATOM 2682 CA ASP A 261 -4.936 18.910 19.282 1.00 36.16 C ANISOU 2682 CA ASP A 261 4368 4228 5145 -1249 -131 278 C ATOM 2683 C ASP A 261 -5.174 18.452 17.846 1.00 31.97 C ANISOU 2683 C ASP A 261 3868 3724 4555 -1228 -11 353 C ATOM 2684 O ASP A 261 -4.838 19.194 16.917 1.00 31.77 O ANISOU 2684 O ASP A 261 3904 3635 4533 -1330 50 421 O ATOM 2685 CB ASP A 261 -3.427 18.938 19.542 1.00 45.84 C ANISOU 2685 CB ASP A 261 5434 5511 6471 -1379 -117 276 C ATOM 2686 CG ASP A 261 -3.077 19.594 20.859 1.00 56.52 C ANISOU 2686 CG ASP A 261 6772 6822 7882 -1433 -244 206 C ATOM 2687 OD1 ASP A 261 -4.002 20.188 21.458 1.00 59.93 O ANISOU 2687 OD1 ASP A 261 7339 7160 8271 -1379 -327 162 O ATOM 2688 OD2 ASP A 261 -1.893 19.514 21.297 1.00 60.08 O ANISOU 2688 OD2 ASP A 261 7074 7334 8418 -1526 -263 191 O ATOM 2689 N CYS A 262 -5.701 17.245 17.644 1.00 32.12 N ANISOU 2689 N CYS A 262 3852 3834 4516 -1108 24 345 N ATOM 2690 CA CYS A 262 -6.021 16.722 16.318 1.00 33.78 C ANISOU 2690 CA CYS A 262 4104 4074 4654 -1079 128 404 C ATOM 2691 C CYS A 262 -7.416 17.165 15.912 1.00 32.00 C ANISOU 2691 C CYS A 262 4051 3761 4345 -1003 86 423 C ATOM 2692 O CYS A 262 -8.349 17.116 16.718 1.00 30.52 O ANISOU 2692 O CYS A 262 3901 3554 4141 -905 -1 370 O ATOM 2693 CB CYS A 262 -5.969 15.191 16.304 1.00 36.66 C ANISOU 2693 CB CYS A 262 4359 4568 5000 -985 176 379 C ATOM 2694 SG CYS A 262 -4.348 14.427 16.602 1.00 44.78 S ANISOU 2694 SG CYS A 262 5167 5716 6132 -1041 233 360 S ATOM 2695 N SER A 263 -7.565 17.593 14.664 1.00 31.05 N ANISOU 2695 N SER A 263 4033 3592 4171 -1046 149 499 N ATOM 2696 CA SER A 263 -8.908 17.809 14.148 1.00 32.03 C ANISOU 2696 CA SER A 263 4305 3652 4212 -957 107 522 C ATOM 2697 C SER A 263 -9.725 16.528 14.267 1.00 28.04 C ANISOU 2697 C SER A 263 3758 3242 3653 -822 102 480 C ATOM 2698 O SER A 263 -9.199 15.419 14.112 1.00 26.78 O ANISOU 2698 O SER A 263 3494 3192 3491 -812 173 467 O ATOM 2699 CB SER A 263 -8.868 18.276 12.690 1.00 38.05 C ANISOU 2699 CB SER A 263 5183 4368 4907 -1024 179 619 C ATOM 2700 OG SER A 263 -8.602 19.667 12.638 1.00 46.03 O ANISOU 2700 OG SER A 263 6290 5244 5954 -1125 146 664 O ATOM 2701 N HIS A 264 -11.012 16.691 14.594 1.00 26.30 N ANISOU 2701 N HIS A 264 3615 2977 3400 -719 17 454 N ATOM 2702 CA HIS A 264 -11.933 15.565 14.682 1.00 28.75 C ANISOU 2702 CA HIS A 264 3897 3365 3659 -601 6 417 C ATOM 2703 C HIS A 264 -12.034 14.868 13.331 1.00 25.97 C ANISOU 2703 C HIS A 264 3578 3062 3226 -599 84 470 C ATOM 2704 O HIS A 264 -12.082 15.529 12.293 1.00 26.97 O ANISOU 2704 O HIS A 264 3811 3130 3306 -646 105 539 O ATOM 2705 CB HIS A 264 -13.309 16.074 15.112 1.00 29.70 C ANISOU 2705 CB HIS A 264 4099 3420 3765 -504 -92 389 C ATOM 2706 CG HIS A 264 -14.218 15.015 15.649 1.00 26.49 C ANISOU 2706 CG HIS A 264 3638 3095 3332 -395 -116 333 C ATOM 2707 ND1 HIS A 264 -14.819 14.070 14.843 1.00 26.82 N ANISOU 2707 ND1 HIS A 264 3684 3199 3307 -345 -86 351 N ATOM 2708 CD2 HIS A 264 -14.652 14.769 16.909 1.00 24.72 C ANISOU 2708 CD2 HIS A 264 3360 2898 3134 -335 -165 259 C ATOM 2709 CE1 HIS A 264 -15.571 13.275 15.588 1.00 26.31 C ANISOU 2709 CE1 HIS A 264 3566 3194 3238 -264 -116 294 C ATOM 2710 NE2 HIS A 264 -15.489 13.681 16.844 1.00 26.56 N ANISOU 2710 NE2 HIS A 264 3562 3208 3322 -256 -160 241 N ATOM 2711 N ALA A 265 -12.076 13.528 13.344 1.00 23.77 N ANISOU 2711 N ALA A 265 3220 2888 2925 -545 124 437 N ATOM 2712 CA ALA A 265 -12.368 12.753 12.132 1.00 24.58 C ANISOU 2712 CA ALA A 265 3364 3036 2938 -526 186 467 C ATOM 2713 C ALA A 265 -13.497 13.421 11.351 1.00 26.29 C ANISOU 2713 C ALA A 265 3725 3182 3082 -496 127 513 C ATOM 2714 O ALA A 265 -14.488 13.857 11.952 1.00 25.80 O ANISOU 2714 O ALA A 265 3693 3073 3037 -427 30 489 O ATOM 2715 CB ALA A 265 -12.773 11.320 12.469 1.00 22.27 C ANISOU 2715 CB ALA A 265 2998 2833 2632 -443 191 412 C ATOM 2716 N PRO A 266 -13.390 13.541 10.032 1.00 27.18 N ANISOU 2716 N PRO A 266 3929 3285 3112 -542 181 578 N ATOM 2717 CA PRO A 266 -14.418 14.283 9.284 1.00 26.77 C ANISOU 2717 CA PRO A 266 4023 3156 2991 -515 107 633 C ATOM 2718 C PRO A 266 -15.721 13.492 9.216 1.00 26.59 C ANISOU 2718 C PRO A 266 4007 3177 2921 -406 40 597 C ATOM 2719 O PRO A 266 -15.772 12.284 9.479 1.00 20.67 O ANISOU 2719 O PRO A 266 3170 2515 2167 -368 71 542 O ATOM 2720 CB PRO A 266 -13.785 14.476 7.903 1.00 26.00 C ANISOU 2720 CB PRO A 266 4019 3055 2805 -608 197 712 C ATOM 2721 CG PRO A 266 -12.790 13.350 7.788 1.00 25.10 C ANISOU 2721 CG PRO A 266 3796 3050 2691 -642 324 675 C ATOM 2722 CD PRO A 266 -12.274 13.101 9.174 1.00 23.37 C ANISOU 2722 CD PRO A 266 3425 2858 2595 -625 313 606 C ATOM 2723 N LEU A 267 -16.796 14.207 8.885 1.00 24.58 N ANISOU 2723 N LEU A 267 3851 2852 2635 -355 -61 630 N ATOM 2724 CA LEU A 267 -18.126 13.600 8.925 1.00 25.87 C ANISOU 2724 CA LEU A 267 4004 3053 2773 -252 -141 594 C ATOM 2725 C LEU A 267 -18.239 12.378 8.007 1.00 23.93 C ANISOU 2725 C LEU A 267 3766 2896 2432 -256 -92 591 C ATOM 2726 O LEU A 267 -18.856 11.369 8.382 1.00 25.02 O ANISOU 2726 O LEU A 267 3831 3102 2574 -198 -110 531 O ATOM 2727 CB LEU A 267 -19.189 14.642 8.562 1.00 29.22 C ANISOU 2727 CB LEU A 267 4534 3385 3185 -197 -259 639 C ATOM 2728 CG LEU A 267 -20.628 14.121 8.434 1.00 30.69 C ANISOU 2728 CG LEU A 267 4706 3610 3345 -95 -352 611 C ATOM 2729 CD1 LEU A 267 -21.126 13.476 9.744 1.00 28.21 C ANISOU 2729 CD1 LEU A 267 4251 3357 3110 -27 -364 514 C ATOM 2730 CD2 LEU A 267 -21.553 15.268 7.991 1.00 28.63 C ANISOU 2730 CD2 LEU A 267 4550 3249 3080 -37 -474 665 C ATOM 2731 N TRP A 268 -17.654 12.436 6.808 1.00 22.86 N ANISOU 2731 N TRP A 268 3723 2759 2203 -328 -26 652 N ATOM 2732 CA TRP A 268 -17.776 11.288 5.903 1.00 23.91 C ANISOU 2732 CA TRP A 268 3878 2971 2235 -331 21 639 C ATOM 2733 C TRP A 268 -17.134 10.045 6.507 1.00 23.44 C ANISOU 2733 C TRP A 268 3690 2996 2222 -328 110 562 C ATOM 2734 O TRP A 268 -17.597 8.923 6.270 1.00 22.04 O ANISOU 2734 O TRP A 268 3496 2877 2000 -292 112 518 O ATOM 2735 CB TRP A 268 -17.165 11.596 4.528 1.00 23.72 C ANISOU 2735 CB TRP A 268 3986 2936 2093 -416 93 714 C ATOM 2736 CG TRP A 268 -15.650 11.767 4.505 1.00 28.15 C ANISOU 2736 CG TRP A 268 4511 3507 2680 -513 237 730 C ATOM 2737 CD1 TRP A 268 -14.955 12.950 4.548 1.00 29.20 C ANISOU 2737 CD1 TRP A 268 4680 3566 2848 -589 260 793 C ATOM 2738 CD2 TRP A 268 -14.655 10.725 4.426 1.00 30.17 C ANISOU 2738 CD2 TRP A 268 4679 3847 2936 -545 376 680 C ATOM 2739 NE1 TRP A 268 -13.600 12.708 4.505 1.00 29.53 N ANISOU 2739 NE1 TRP A 268 4651 3654 2916 -673 405 786 N ATOM 2740 CE2 TRP A 268 -13.386 11.357 4.430 1.00 30.84 C ANISOU 2740 CE2 TRP A 268 4736 3917 3063 -640 478 716 C ATOM 2741 CE3 TRP A 268 -14.714 9.326 4.352 1.00 28.87 C ANISOU 2741 CE3 TRP A 268 4457 3764 2748 -501 421 608 C ATOM 2742 CZ2 TRP A 268 -12.189 10.640 4.360 1.00 32.87 C ANISOU 2742 CZ2 TRP A 268 4896 4249 3344 -684 625 680 C ATOM 2743 CZ3 TRP A 268 -13.522 8.608 4.288 1.00 32.42 C ANISOU 2743 CZ3 TRP A 268 4824 4275 3219 -537 565 571 C ATOM 2744 CH2 TRP A 268 -12.268 9.272 4.286 1.00 31.46 C ANISOU 2744 CH2 TRP A 268 4663 4148 3145 -624 667 606 C ATOM 2745 N LEU A 269 -16.088 10.229 7.317 1.00 23.14 N ANISOU 2745 N LEU A 269 3561 2957 2275 -363 174 546 N ATOM 2746 CA LEU A 269 -15.413 9.091 7.928 1.00 20.34 C ANISOU 2746 CA LEU A 269 3082 2673 1972 -353 248 481 C ATOM 2747 C LEU A 269 -16.212 8.547 9.108 1.00 19.17 C ANISOU 2747 C LEU A 269 2849 2544 1890 -273 168 419 C ATOM 2748 O LEU A 269 -16.276 7.328 9.305 1.00 20.08 O ANISOU 2748 O LEU A 269 2908 2716 2006 -241 194 370 O ATOM 2749 CB LEU A 269 -13.984 9.498 8.344 1.00 24.03 C ANISOU 2749 CB LEU A 269 3475 3140 2517 -422 333 489 C ATOM 2750 CG LEU A 269 -13.138 8.398 8.999 1.00 26.79 C ANISOU 2750 CG LEU A 269 3686 3558 2934 -408 403 429 C ATOM 2751 CD1 LEU A 269 -13.064 7.196 8.076 1.00 24.82 C ANISOU 2751 CD1 LEU A 269 3457 3366 2609 -392 483 404 C ATOM 2752 CD2 LEU A 269 -11.723 8.915 9.350 1.00 29.25 C ANISOU 2752 CD2 LEU A 269 3914 3872 3330 -482 475 442 C ATOM 2753 N MET A 270 -16.832 9.427 9.907 1.00 20.99 N ANISOU 2753 N MET A 270 3076 2724 2174 -242 77 420 N ATOM 2754 CA MET A 270 -17.764 8.961 10.930 1.00 18.30 C ANISOU 2754 CA MET A 270 2669 2407 1877 -168 7 365 C ATOM 2755 C MET A 270 -18.855 8.094 10.318 1.00 19.82 C ANISOU 2755 C MET A 270 2890 2639 2002 -125 -29 350 C ATOM 2756 O MET A 270 -19.161 7.017 10.831 1.00 19.88 O ANISOU 2756 O MET A 270 2833 2698 2024 -95 -25 301 O ATOM 2757 CB MET A 270 -18.406 10.151 11.665 1.00 18.57 C ANISOU 2757 CB MET A 270 2716 2377 1963 -134 -82 365 C ATOM 2758 CG MET A 270 -17.435 11.033 12.422 1.00 23.91 C ANISOU 2758 CG MET A 270 3366 3007 2711 -179 -65 368 C ATOM 2759 SD MET A 270 -16.481 10.069 13.607 1.00 29.89 S ANISOU 2759 SD MET A 270 3990 3835 3532 -191 -11 311 S ATOM 2760 CE MET A 270 -17.782 9.273 14.561 1.00 22.63 C ANISOU 2760 CE MET A 270 3020 2962 2616 -102 -72 249 C ATOM 2761 N TYR A 271 -19.483 8.572 9.234 1.00 18.81 N ANISOU 2761 N TYR A 271 2866 2483 1799 -125 -74 395 N ATOM 2762 CA TYR A 271 -20.528 7.792 8.566 1.00 16.42 C ANISOU 2762 CA TYR A 271 2593 2217 1427 -93 -122 381 C ATOM 2763 C TYR A 271 -20.013 6.420 8.162 1.00 21.90 C ANISOU 2763 C TYR A 271 3272 2971 2078 -119 -37 346 C ATOM 2764 O TYR A 271 -20.709 5.404 8.324 1.00 19.45 O ANISOU 2764 O TYR A 271 2926 2701 1763 -91 -63 300 O ATOM 2765 CB TYR A 271 -21.018 8.511 7.310 1.00 18.64 C ANISOU 2765 CB TYR A 271 3003 2460 1619 -103 -179 445 C ATOM 2766 CG TYR A 271 -21.915 9.715 7.495 1.00 23.73 C ANISOU 2766 CG TYR A 271 3678 3042 2298 -52 -294 477 C ATOM 2767 CD1 TYR A 271 -22.796 9.822 8.577 1.00 24.66 C ANISOU 2767 CD1 TYR A 271 3704 3164 2503 20 -362 429 C ATOM 2768 CD2 TYR A 271 -21.901 10.735 6.552 1.00 27.86 C ANISOU 2768 CD2 TYR A 271 4328 3498 2761 -73 -333 556 C ATOM 2769 CE1 TYR A 271 -23.632 10.931 8.705 1.00 27.33 C ANISOU 2769 CE1 TYR A 271 4067 3439 2878 81 -464 451 C ATOM 2770 CE2 TYR A 271 -22.726 11.829 6.664 1.00 30.68 C ANISOU 2770 CE2 TYR A 271 4720 3783 3154 -14 -446 588 C ATOM 2771 CZ TYR A 271 -23.583 11.934 7.735 1.00 33.12 C ANISOU 2771 CZ TYR A 271 4928 4096 3560 67 -510 531 C ATOM 2772 OH TYR A 271 -24.390 13.058 7.818 1.00 35.97 O ANISOU 2772 OH TYR A 271 5323 4379 3964 138 -619 557 O ATOM 2773 N LEU A 272 -18.819 6.393 7.568 1.00 19.00 N ANISOU 2773 N LEU A 272 2936 2604 1678 -175 65 367 N ATOM 2774 CA LEU A 272 -18.244 5.156 7.058 1.00 21.94 C ANISOU 2774 CA LEU A 272 3305 3024 2009 -193 157 330 C ATOM 2775 C LEU A 272 -17.976 4.180 8.188 1.00 17.83 C ANISOU 2775 C LEU A 272 2666 2532 1576 -161 181 271 C ATOM 2776 O LEU A 272 -18.305 2.995 8.077 1.00 16.78 O ANISOU 2776 O LEU A 272 2526 2428 1423 -142 189 226 O ATOM 2777 CB LEU A 272 -16.953 5.466 6.289 1.00 26.32 C ANISOU 2777 CB LEU A 272 3899 3577 2525 -257 275 363 C ATOM 2778 CG LEU A 272 -16.196 4.269 5.690 1.00 31.37 C ANISOU 2778 CG LEU A 272 4534 4262 3123 -270 392 318 C ATOM 2779 CD1 LEU A 272 -17.144 3.471 4.759 1.00 32.32 C ANISOU 2779 CD1 LEU A 272 4751 4399 3130 -256 354 292 C ATOM 2780 CD2 LEU A 272 -14.943 4.721 4.916 1.00 30.08 C ANISOU 2780 CD2 LEU A 272 4401 4105 2923 -337 520 352 C ATOM 2781 N ALA A 273 -17.407 4.675 9.299 1.00 15.91 N ANISOU 2781 N ALA A 273 2338 2278 1430 -157 185 272 N ATOM 2782 CA ALA A 273 -17.098 3.816 10.440 1.00 19.07 C ANISOU 2782 CA ALA A 273 2634 2703 1909 -128 198 226 C ATOM 2783 C ALA A 273 -18.371 3.289 11.106 1.00 18.54 C ANISOU 2783 C ALA A 273 2546 2649 1851 -83 115 195 C ATOM 2784 O ALA A 273 -18.394 2.153 11.603 1.00 16.69 O ANISOU 2784 O ALA A 273 2265 2437 1639 -64 128 159 O ATOM 2785 CB ALA A 273 -16.255 4.593 11.457 1.00 19.76 C ANISOU 2785 CB ALA A 273 2647 2776 2085 -142 203 237 C ATOM 2786 N ILE A 274 -19.430 4.107 11.139 1.00 16.21 N ANISOU 2786 N ILE A 274 2279 2336 1543 -66 30 211 N ATOM 2787 CA ILE A 274 -20.698 3.656 11.699 1.00 19.32 C ANISOU 2787 CA ILE A 274 2642 2752 1949 -29 -40 180 C ATOM 2788 C ILE A 274 -21.294 2.539 10.829 1.00 17.78 C ANISOU 2788 C ILE A 274 2487 2582 1688 -36 -43 160 C ATOM 2789 O ILE A 274 -21.718 1.493 11.336 1.00 15.88 O ANISOU 2789 O ILE A 274 2203 2365 1465 -28 -47 124 O ATOM 2790 CB ILE A 274 -21.660 4.853 11.854 1.00 19.05 C ANISOU 2790 CB ILE A 274 2619 2693 1925 1 -126 197 C ATOM 2791 CG1 ILE A 274 -21.148 5.819 12.945 1.00 17.47 C ANISOU 2791 CG1 ILE A 274 2377 2463 1796 9 -126 198 C ATOM 2792 CG2 ILE A 274 -23.040 4.371 12.211 1.00 17.37 C ANISOU 2792 CG2 ILE A 274 2365 2514 1719 36 -191 165 C ATOM 2793 CD1 ILE A 274 -21.914 7.209 12.950 1.00 19.93 C ANISOU 2793 CD1 ILE A 274 2722 2726 2123 44 -203 216 C ATOM 2794 N AVAL A 275 -21.311 2.717 9.506 0.54 15.81 N ANISOU 2794 N AVAL A 275 2329 2323 1357 -58 -41 183 N ATOM 2795 N BVAL A 275 -21.321 2.763 9.514 0.46 15.81 N ANISOU 2795 N BVAL A 275 2328 2322 1357 -57 -43 185 N ATOM 2796 CA AVAL A 275 -21.927 1.654 8.707 0.54 19.45 C ANISOU 2796 CA AVAL A 275 2834 2806 1749 -68 -56 155 C ATOM 2797 CA BVAL A 275 -21.823 1.768 8.568 0.46 19.27 C ANISOU 2797 CA BVAL A 275 2823 2780 1718 -72 -51 161 C ATOM 2798 C AVAL A 275 -21.035 0.409 8.632 0.54 18.86 C ANISOU 2798 C AVAL A 275 2756 2738 1673 -83 38 117 C ATOM 2799 C BVAL A 275 -21.040 0.461 8.691 0.46 18.94 C ANISOU 2799 C BVAL A 275 2762 2748 1687 -82 36 118 C ATOM 2800 O AVAL A 275 -21.545 -0.709 8.493 0.54 19.44 O ANISOU 2800 O AVAL A 275 2838 2822 1727 -86 27 76 O ATOM 2801 O BVAL A 275 -21.620 -0.628 8.751 0.46 19.25 O ANISOU 2801 O BVAL A 275 2796 2799 1721 -81 18 78 O ATOM 2802 CB AVAL A 275 -22.330 2.149 7.306 0.54 20.77 C ANISOU 2802 CB AVAL A 275 3114 2965 1812 -87 -97 187 C ATOM 2803 CB BVAL A 275 -21.764 2.336 7.139 0.46 21.15 C ANISOU 2803 CB BVAL A 275 3179 3004 1851 -99 -56 199 C ATOM 2804 CG1AVAL A 275 -23.346 3.313 7.413 0.54 20.57 C ANISOU 2804 CG1AVAL A 275 3088 2925 1802 -56 -209 224 C ATOM 2805 CG1BVAL A 275 -21.764 1.230 6.112 0.46 22.17 C ANISOU 2805 CG1BVAL A 275 3383 3152 1889 -126 -23 165 C ATOM 2806 CG2AVAL A 275 -21.108 2.513 6.456 0.54 22.54 C ANISOU 2806 CG2AVAL A 275 3413 3172 1977 -125 -3 218 C ATOM 2807 CG2BVAL A 275 -22.919 3.328 6.901 0.46 21.83 C ANISOU 2807 CG2BVAL A 275 3294 3078 1921 -76 -177 236 C ATOM 2808 N LEU A 276 -19.711 0.556 8.737 1.00 18.94 N ANISOU 2808 N LEU A 276 2747 2739 1711 -90 129 126 N ATOM 2809 CA LEU A 276 -18.865 -0.634 8.870 1.00 20.34 C ANISOU 2809 CA LEU A 276 2897 2919 1913 -84 212 85 C ATOM 2810 C LEU A 276 -19.216 -1.444 10.128 1.00 18.62 C ANISOU 2810 C LEU A 276 2600 2703 1772 -57 179 59 C ATOM 2811 O LEU A 276 -19.356 -2.669 10.070 1.00 18.13 O ANISOU 2811 O LEU A 276 2550 2634 1705 -51 193 21 O ATOM 2812 CB LEU A 276 -17.396 -0.235 8.891 1.00 21.06 C ANISOU 2812 CB LEU A 276 2952 3009 2041 -92 308 102 C ATOM 2813 CG LEU A 276 -16.419 -1.407 9.066 1.00 23.90 C ANISOU 2813 CG LEU A 276 3266 3370 2445 -69 393 59 C ATOM 2814 CD1 LEU A 276 -16.503 -2.403 7.858 1.00 19.78 C ANISOU 2814 CD1 LEU A 276 2834 2845 1836 -72 446 14 C ATOM 2815 CD2 LEU A 276 -15.000 -0.887 9.265 1.00 24.86 C ANISOU 2815 CD2 LEU A 276 3317 3501 2628 -75 474 77 C ATOM 2816 N ALA A 277 -19.349 -0.777 11.279 1.00 16.73 N ANISOU 2816 N ALA A 277 2291 2468 1598 -43 137 79 N ATOM 2817 CA ALA A 277 -19.755 -1.478 12.489 1.00 18.06 C ANISOU 2817 CA ALA A 277 2398 2643 1822 -25 106 61 C ATOM 2818 C ALA A 277 -21.082 -2.200 12.275 1.00 19.93 C ANISOU 2818 C ALA A 277 2661 2888 2023 -36 52 38 C ATOM 2819 O ALA A 277 -21.232 -3.373 12.654 1.00 17.75 O ANISOU 2819 O ALA A 277 2377 2604 1763 -39 59 14 O ATOM 2820 CB ALA A 277 -19.869 -0.493 13.661 1.00 15.41 C ANISOU 2820 CB ALA A 277 2001 2316 1539 -14 65 80 C ATOM 2821 N HIS A 278 -22.049 -1.522 11.643 1.00 17.23 N ANISOU 2821 N HIS A 278 2352 2559 1636 -45 -7 47 N ATOM 2822 CA HIS A 278 -23.356 -2.130 11.433 1.00 18.70 C ANISOU 2822 CA HIS A 278 2546 2762 1797 -61 -69 24 C ATOM 2823 C HIS A 278 -23.296 -3.303 10.457 1.00 17.94 C ANISOU 2823 C HIS A 278 2522 2650 1645 -88 -46 -9 C ATOM 2824 O HIS A 278 -24.058 -4.262 10.622 1.00 19.57 O ANISOU 2824 O HIS A 278 2722 2857 1855 -111 -75 -37 O ATOM 2825 CB HIS A 278 -24.367 -1.079 10.942 1.00 19.67 C ANISOU 2825 CB HIS A 278 2678 2903 1893 -54 -151 43 C ATOM 2826 CG HIS A 278 -24.664 -0.023 11.964 1.00 19.66 C ANISOU 2826 CG HIS A 278 2606 2911 1952 -20 -180 59 C ATOM 2827 ND1 HIS A 278 -25.287 1.165 11.651 1.00 19.80 N ANISOU 2827 ND1 HIS A 278 2632 2928 1965 6 -245 81 N ATOM 2828 CD2 HIS A 278 -24.379 0.037 13.290 1.00 20.35 C ANISOU 2828 CD2 HIS A 278 2626 3005 2103 -6 -154 54 C ATOM 2829 CE1 HIS A 278 -25.406 1.899 12.747 1.00 22.18 C ANISOU 2829 CE1 HIS A 278 2868 3230 2328 38 -252 80 C ATOM 2830 NE2 HIS A 278 -24.862 1.241 13.758 1.00 21.19 N ANISOU 2830 NE2 HIS A 278 2699 3114 2238 27 -197 63 N ATOM 2831 N ATHR A 279 -22.403 -3.245 9.456 0.77 16.99 N ANISOU 2831 N ATHR A 279 2472 2512 1471 -91 12 -9 N ATOM 2832 N BTHR A 279 -22.418 -3.250 9.444 0.23 17.28 N ANISOU 2832 N BTHR A 279 2510 2549 1507 -91 11 -9 N ATOM 2833 CA ATHR A 279 -22.289 -4.329 8.469 0.77 18.95 C ANISOU 2833 CA ATHR A 279 2803 2741 1655 -113 44 -52 C ATOM 2834 CA BTHR A 279 -22.349 -4.350 8.479 0.23 18.91 C ANISOU 2834 CA BTHR A 279 2798 2738 1651 -114 40 -53 C ATOM 2835 C ATHR A 279 -21.928 -5.655 9.130 0.77 18.88 C ANISOU 2835 C ATHR A 279 2770 2701 1702 -105 85 -88 C ATOM 2836 C BTHR A 279 -21.930 -5.659 9.126 0.23 18.57 C ANISOU 2836 C BTHR A 279 2731 2662 1662 -105 85 -88 C ATOM 2837 O ATHR A 279 -22.217 -6.728 8.579 0.77 19.52 O ANISOU 2837 O ATHR A 279 2913 2757 1748 -127 86 -133 O ATOM 2838 O BTHR A 279 -22.167 -6.726 8.546 0.23 19.08 O ANISOU 2838 O BTHR A 279 2860 2700 1691 -126 89 -134 O ATOM 2839 CB ATHR A 279 -21.241 -3.969 7.399 0.77 20.82 C ANISOU 2839 CB ATHR A 279 3112 2972 1826 -113 123 -48 C ATOM 2840 CB BTHR A 279 -21.373 -4.056 7.332 0.23 21.01 C ANISOU 2840 CB BTHR A 279 3143 2996 1844 -116 116 -52 C ATOM 2841 OG1ATHR A 279 -21.641 -2.777 6.718 0.77 23.81 O ANISOU 2841 OG1ATHR A 279 3535 3369 2142 -127 75 -5 O ATOM 2842 OG1BTHR A 279 -20.056 -3.846 7.853 0.23 21.40 O ANISOU 2842 OG1BTHR A 279 3138 3037 1955 -90 205 -38 O ATOM 2843 CG2ATHR A 279 -21.069 -5.079 6.360 0.77 21.27 C ANISOU 2843 CG2ATHR A 279 3264 3008 1808 -130 169 -105 C ATOM 2844 CG2BTHR A 279 -21.812 -2.855 6.519 0.23 22.92 C ANISOU 2844 CG2BTHR A 279 3439 3257 2012 -132 64 -10 C ATOM 2845 N ASN A 280 -21.293 -5.609 10.296 1.00 15.65 N ANISOU 2845 N ASN A 280 2282 2286 1377 -76 114 -68 N ATOM 2846 CA ASN A 280 -20.988 -6.853 10.993 1.00 21.21 C ANISOU 2846 CA ASN A 280 2970 2953 2135 -64 139 -90 C ATOM 2847 C ASN A 280 -22.259 -7.652 11.301 1.00 22.77 C ANISOU 2847 C ASN A 280 3176 3143 2331 -105 73 -107 C ATOM 2848 O ASN A 280 -22.211 -8.889 11.380 1.00 23.08 O ANISOU 2848 O ASN A 280 3250 3134 2385 -114 88 -135 O ATOM 2849 CB ASN A 280 -20.217 -6.595 12.294 1.00 19.07 C ANISOU 2849 CB ASN A 280 2614 2684 1948 -30 156 -57 C ATOM 2850 CG ASN A 280 -19.811 -7.896 12.963 1.00 23.74 C ANISOU 2850 CG ASN A 280 3202 3227 2591 -11 175 -70 C ATOM 2851 OD1 ASN A 280 -18.968 -8.632 12.436 1.00 26.98 O ANISOU 2851 OD1 ASN A 280 3645 3597 3010 18 233 -100 O ATOM 2852 ND2 ASN A 280 -20.459 -8.223 14.069 1.00 19.96 N ANISOU 2852 ND2 ASN A 280 2692 2749 2144 -27 128 -50 N ATOM 2853 N SER A 281 -23.406 -6.974 11.437 1.00 17.49 N ANISOU 2853 N SER A 281 2476 2521 1650 -131 2 -91 N ATOM 2854 CA SER A 281 -24.668 -7.678 11.660 1.00 21.60 C ANISOU 2854 CA SER A 281 2988 3047 2172 -181 -57 -108 C ATOM 2855 C SER A 281 -25.180 -8.388 10.416 1.00 22.92 C ANISOU 2855 C SER A 281 3241 3193 2272 -223 -84 -153 C ATOM 2856 O SER A 281 -26.149 -9.147 10.520 1.00 23.99 O ANISOU 2856 O SER A 281 3376 3326 2414 -277 -132 -174 O ATOM 2857 CB SER A 281 -25.726 -6.710 12.183 1.00 18.16 C ANISOU 2857 CB SER A 281 2474 2673 1754 -187 -120 -84 C ATOM 2858 OG SER A 281 -25.361 -6.297 13.493 1.00 23.54 O ANISOU 2858 OG SER A 281 3085 3367 2492 -159 -95 -55 O ATOM 2859 N VAL A 282 -24.544 -8.176 9.262 1.00 21.35 N ANISOU 2859 N VAL A 282 3120 2983 2007 -208 -53 -170 N ATOM 2860 CA VAL A 282 -24.892 -8.890 8.033 1.00 22.37 C ANISOU 2860 CA VAL A 282 3353 3091 2056 -248 -73 -222 C ATOM 2861 C VAL A 282 -24.044 -10.152 7.816 1.00 25.32 C ANISOU 2861 C VAL A 282 3798 3390 2433 -238 3 -272 C ATOM 2862 O VAL A 282 -24.505 -11.090 7.157 1.00 29.88 O ANISOU 2862 O VAL A 282 4456 3931 2967 -282 -20 -326 O ATOM 2863 CB VAL A 282 -24.760 -7.938 6.814 1.00 23.09 C ANISOU 2863 CB VAL A 282 3509 3214 2051 -241 -82 -214 C ATOM 2864 CG1 VAL A 282 -25.143 -8.661 5.481 1.00 21.44 C ANISOU 2864 CG1 VAL A 282 3424 2987 1736 -288 -109 -273 C ATOM 2865 CG2 VAL A 282 -25.613 -6.694 7.007 1.00 21.12 C ANISOU 2865 CG2 VAL A 282 3195 3021 1807 -238 -167 -164 C ATOM 2866 N VAL A 283 -22.807 -10.204 8.333 1.00 21.58 N ANISOU 2866 N VAL A 283 3296 2890 2013 -180 89 -259 N ATOM 2867 CA VAL A 283 -21.831 -11.147 7.768 1.00 24.54 C ANISOU 2867 CA VAL A 283 3746 3201 2377 -149 173 -314 C ATOM 2868 C VAL A 283 -21.935 -12.564 8.353 1.00 28.01 C ANISOU 2868 C VAL A 283 4207 3559 2877 -155 170 -344 C ATOM 2869 O VAL A 283 -21.567 -13.536 7.673 1.00 32.78 O ANISOU 2869 O VAL A 283 4902 4096 3458 -147 212 -408 O ATOM 2870 CB VAL A 283 -20.381 -10.628 7.907 1.00 29.54 C ANISOU 2870 CB VAL A 283 4334 3842 3046 -80 270 -294 C ATOM 2871 CG1 VAL A 283 -20.190 -9.263 7.225 1.00 32.20 C ANISOU 2871 CG1 VAL A 283 4670 4245 3318 -85 284 -263 C ATOM 2872 CG2 VAL A 283 -19.946 -10.548 9.371 1.00 31.07 C ANISOU 2872 CG2 VAL A 283 4421 4033 3352 -43 268 -244 C ATOM 2873 N ASN A 284 -22.411 -12.739 9.584 1.00 30.33 N ANISOU 2873 N ASN A 284 4430 3849 3243 -171 125 -300 N ATOM 2874 CA ASN A 284 -22.401 -14.084 10.174 1.00 32.77 C ANISOU 2874 CA ASN A 284 4773 4069 3610 -178 125 -316 C ATOM 2875 C ASN A 284 -23.186 -15.128 9.372 1.00 31.74 C ANISOU 2875 C ASN A 284 4749 3879 3434 -245 91 -381 C ATOM 2876 O ASN A 284 -22.630 -16.214 9.123 1.00 31.45 O ANISOU 2876 O ASN A 284 4791 3744 3414 -220 132 -429 O ATOM 2877 CB ASN A 284 -22.867 -14.027 11.637 1.00 33.90 C ANISOU 2877 CB ASN A 284 4832 4228 3820 -198 84 -250 C ATOM 2878 CG ASN A 284 -21.893 -13.254 12.513 1.00 33.67 C ANISOU 2878 CG ASN A 284 4717 4233 3842 -128 118 -196 C ATOM 2879 OD1 ASN A 284 -20.770 -12.924 12.075 1.00 32.07 O ANISOU 2879 OD1 ASN A 284 4510 4031 3643 -63 178 -209 O ATOM 2880 ND2 ASN A 284 -22.290 -12.983 13.755 1.00 31.55 N ANISOU 2880 ND2 ASN A 284 4381 3996 3612 -145 84 -141 N ATOM 2881 N PRO A 285 -24.424 -14.879 8.911 1.00 29.58 N ANISOU 2881 N PRO A 285 4482 3652 3105 -326 14 -391 N ATOM 2882 CA PRO A 285 -25.119 -15.916 8.125 1.00 29.65 C ANISOU 2882 CA PRO A 285 4596 3601 3071 -398 -26 -460 C ATOM 2883 C PRO A 285 -24.330 -16.376 6.910 1.00 34.79 C ANISOU 2883 C PRO A 285 5369 4196 3654 -361 34 -540 C ATOM 2884 O PRO A 285 -24.448 -17.545 6.520 1.00 35.91 O ANISOU 2884 O PRO A 285 5613 4244 3788 -393 32 -606 O ATOM 2885 CB PRO A 285 -26.433 -15.236 7.711 1.00 26.10 C ANISOU 2885 CB PRO A 285 4110 3240 2568 -475 -122 -453 C ATOM 2886 CG PRO A 285 -26.648 -14.180 8.787 1.00 28.11 C ANISOU 2886 CG PRO A 285 4225 3577 2877 -452 -134 -372 C ATOM 2887 CD PRO A 285 -25.261 -13.677 9.087 1.00 32.43 C ANISOU 2887 CD PRO A 285 4755 4120 3448 -353 -46 -345 C ATOM 2888 N PHE A 286 -23.505 -15.498 6.316 1.00 33.83 N ANISOU 2888 N PHE A 286 5244 4127 3483 -298 96 -538 N ATOM 2889 CA PHE A 286 -22.654 -15.918 5.201 1.00 34.55 C ANISOU 2889 CA PHE A 286 5446 4174 3507 -258 178 -616 C ATOM 2890 C PHE A 286 -21.545 -16.855 5.657 1.00 36.57 C ANISOU 2890 C PHE A 286 5714 4333 3849 -178 266 -643 C ATOM 2891 O PHE A 286 -21.268 -17.861 4.987 1.00 39.32 O ANISOU 2891 O PHE A 286 6175 4593 4172 -167 305 -730 O ATOM 2892 CB PHE A 286 -22.075 -14.694 4.495 1.00 35.42 C ANISOU 2892 CB PHE A 286 5543 4372 3542 -223 229 -596 C ATOM 2893 CG PHE A 286 -23.089 -13.976 3.698 1.00 35.18 C ANISOU 2893 CG PHE A 286 5550 4414 3405 -292 141 -589 C ATOM 2894 CD1 PHE A 286 -23.352 -14.368 2.391 1.00 40.59 C ANISOU 2894 CD1 PHE A 286 6374 5085 3963 -333 130 -665 C ATOM 2895 CD2 PHE A 286 -23.858 -12.987 4.276 1.00 30.34 C ANISOU 2895 CD2 PHE A 286 4835 3874 2817 -317 57 -512 C ATOM 2896 CE1 PHE A 286 -24.341 -13.733 1.650 1.00 43.48 C ANISOU 2896 CE1 PHE A 286 6777 5518 4228 -398 27 -653 C ATOM 2897 CE2 PHE A 286 -24.842 -12.356 3.552 1.00 33.82 C ANISOU 2897 CE2 PHE A 286 5304 4377 3170 -371 -39 -503 C ATOM 2898 CZ PHE A 286 -25.089 -12.733 2.238 1.00 38.48 C ANISOU 2898 CZ PHE A 286 6031 4956 3632 -413 -61 -570 C ATOM 2899 N ILE A 287 -20.894 -16.546 6.784 1.00 33.20 N ANISOU 2899 N ILE A 287 5175 3915 3523 -117 292 -575 N ATOM 2900 CA ILE A 287 -19.868 -17.449 7.297 1.00 35.59 C ANISOU 2900 CA ILE A 287 5480 4123 3920 -34 356 -592 C ATOM 2901 C ILE A 287 -20.462 -18.819 7.592 1.00 37.64 C ANISOU 2901 C ILE A 287 5823 4262 4218 -74 307 -623 C ATOM 2902 O ILE A 287 -19.854 -19.855 7.280 1.00 41.82 O ANISOU 2902 O ILE A 287 6434 4681 4774 -21 357 -690 O ATOM 2903 CB ILE A 287 -19.192 -16.850 8.539 1.00 38.17 C ANISOU 2903 CB ILE A 287 5670 4488 4344 25 366 -504 C ATOM 2904 CG1 ILE A 287 -18.716 -15.430 8.238 1.00 38.26 C ANISOU 2904 CG1 ILE A 287 5606 4614 4318 45 405 -472 C ATOM 2905 CG2 ILE A 287 -18.035 -17.746 8.986 1.00 39.27 C ANISOU 2905 CG2 ILE A 287 5805 4533 4582 126 424 -521 C ATOM 2906 CD1 ILE A 287 -17.806 -15.374 7.051 1.00 38.94 C ANISOU 2906 CD1 ILE A 287 5740 4705 4350 91 510 -539 C ATOM 2907 N TYR A 288 -21.663 -18.858 8.183 1.00 35.62 N ANISOU 2907 N TYR A 288 5547 4020 3966 -170 212 -578 N ATOM 2908 CA TYR A 288 -22.259 -20.161 8.476 1.00 35.35 C ANISOU 2908 CA TYR A 288 5595 3866 3969 -227 166 -601 C ATOM 2909 C TYR A 288 -22.580 -20.910 7.193 1.00 35.45 C ANISOU 2909 C TYR A 288 5753 3813 3905 -270 164 -711 C ATOM 2910 O TYR A 288 -22.361 -22.120 7.112 1.00 35.93 O ANISOU 2910 O TYR A 288 5916 3736 4001 -258 178 -766 O ATOM 2911 CB TYR A 288 -23.519 -20.021 9.329 1.00 31.89 C ANISOU 2911 CB TYR A 288 5098 3470 3548 -334 75 -533 C ATOM 2912 CG TYR A 288 -23.315 -19.328 10.644 1.00 29.52 C ANISOU 2912 CG TYR A 288 4671 3234 3311 -303 74 -432 C ATOM 2913 CD1 TYR A 288 -22.235 -19.640 11.471 1.00 31.30 C ANISOU 2913 CD1 TYR A 288 4876 3402 3615 -210 116 -394 C ATOM 2914 CD2 TYR A 288 -24.218 -18.357 11.068 1.00 27.05 C ANISOU 2914 CD2 TYR A 288 4260 3039 2978 -363 24 -379 C ATOM 2915 CE1 TYR A 288 -22.056 -18.983 12.713 1.00 34.46 C ANISOU 2915 CE1 TYR A 288 5168 3865 4061 -188 105 -303 C ATOM 2916 CE2 TYR A 288 -24.049 -17.689 12.261 1.00 27.94 C ANISOU 2916 CE2 TYR A 288 4269 3211 3137 -336 26 -297 C ATOM 2917 CZ TYR A 288 -22.976 -17.998 13.090 1.00 34.15 C ANISOU 2917 CZ TYR A 288 5044 3943 3989 -254 64 -259 C ATOM 2918 OH TYR A 288 -22.849 -17.299 14.282 1.00 33.81 O ANISOU 2918 OH TYR A 288 4904 3965 3978 -236 56 -181 O ATOM 2919 N ALA A 289 -23.078 -20.201 6.174 1.00 34.95 N ANISOU 2919 N ALA A 289 5709 3840 3731 -317 143 -746 N ATOM 2920 CA ALA A 289 -23.440 -20.859 4.922 1.00 37.67 C ANISOU 2920 CA ALA A 289 6199 4131 3981 -368 130 -854 C ATOM 2921 C ALA A 289 -22.210 -21.381 4.193 1.00 42.41 C ANISOU 2921 C ALA A 289 6894 4657 4564 -265 245 -941 C ATOM 2922 O ALA A 289 -22.238 -22.484 3.632 1.00 46.76 O ANISOU 2922 O ALA A 289 7580 5090 5097 -279 253 -1037 O ATOM 2923 CB ALA A 289 -24.234 -19.906 4.023 1.00 34.54 C ANISOU 2923 CB ALA A 289 5804 3857 3464 -436 70 -859 C ATOM 2924 N TYR A 290 -21.123 -20.609 4.182 1.00 42.42 N ANISOU 2924 N TYR A 290 6822 4722 4573 -164 340 -916 N ATOM 2925 CA TYR A 290 -19.937 -21.039 3.456 1.00 46.88 C ANISOU 2925 CA TYR A 290 7455 5233 5123 -64 464 -1004 C ATOM 2926 C TYR A 290 -19.141 -22.093 4.207 1.00 47.94 C ANISOU 2926 C TYR A 290 7588 5234 5394 29 508 -1017 C ATOM 2927 O TYR A 290 -18.451 -22.890 3.563 1.00 46.72 O ANISOU 2927 O TYR A 290 7528 4988 5236 99 590 -1118 O ATOM 2928 CB TYR A 290 -19.043 -19.837 3.119 1.00 52.32 C ANISOU 2928 CB TYR A 290 8061 6043 5774 0 556 -974 C ATOM 2929 CG TYR A 290 -19.524 -19.087 1.895 1.00 62.70 C ANISOU 2929 CG TYR A 290 9447 7451 6923 -68 549 -1004 C ATOM 2930 CD1 TYR A 290 -19.231 -19.554 0.612 1.00 70.03 C ANISOU 2930 CD1 TYR A 290 10522 8350 7737 -62 621 -1120 C ATOM 2931 CD2 TYR A 290 -20.294 -17.934 2.013 1.00 65.45 C ANISOU 2931 CD2 TYR A 290 9729 7913 7227 -136 465 -918 C ATOM 2932 CE1 TYR A 290 -19.685 -18.888 -0.523 1.00 73.86 C ANISOU 2932 CE1 TYR A 290 11091 8920 8054 -130 605 -1141 C ATOM 2933 CE2 TYR A 290 -20.754 -17.258 0.888 1.00 69.84 C ANISOU 2933 CE2 TYR A 290 10361 8547 7629 -195 442 -936 C ATOM 2934 CZ TYR A 290 -20.447 -17.740 -0.380 1.00 75.47 C ANISOU 2934 CZ TYR A 290 11226 9233 8218 -195 509 -1044 C ATOM 2935 OH TYR A 290 -20.902 -17.079 -1.506 1.00 79.71 O ANISOU 2935 OH TYR A 290 11853 9846 8586 -257 478 -1056 O ATOM 2936 N ARG A 291 -19.254 -22.162 5.541 1.00 45.82 N ANISOU 2936 N ARG A 291 7225 4944 5240 34 452 -919 N ATOM 2937 CA ARG A 291 -18.356 -23.012 6.312 1.00 45.50 C ANISOU 2937 CA ARG A 291 7171 4786 5330 140 488 -912 C ATOM 2938 C ARG A 291 -19.007 -24.172 7.061 1.00 42.02 C ANISOU 2938 C ARG A 291 6802 4203 4960 89 404 -893 C ATOM 2939 O ARG A 291 -18.278 -25.002 7.604 1.00 42.53 O ANISOU 2939 O ARG A 291 6883 4146 5129 181 426 -892 O ATOM 2940 CB ARG A 291 -17.555 -22.161 7.315 1.00 45.02 C ANISOU 2940 CB ARG A 291 6943 4808 5353 217 508 -810 C ATOM 2941 CG ARG A 291 -16.624 -21.144 6.647 1.00 44.95 C ANISOU 2941 CG ARG A 291 6859 4916 5304 282 610 -829 C ATOM 2942 CD ARG A 291 -15.605 -20.587 7.619 1.00 46.89 C ANISOU 2942 CD ARG A 291 6950 5210 5658 373 637 -749 C ATOM 2943 NE ARG A 291 -14.901 -21.668 8.293 1.00 53.09 N ANISOU 2943 NE ARG A 291 7738 5865 6569 473 640 -754 N ATOM 2944 CZ ARG A 291 -13.742 -22.181 7.889 1.00 56.04 C ANISOU 2944 CZ ARG A 291 8106 6183 7003 599 737 -824 C ATOM 2945 NH1 ARG A 291 -13.142 -21.689 6.814 1.00 52.99 N ANISOU 2945 NH1 ARG A 291 7710 5870 6555 629 852 -897 N ATOM 2946 NH2 ARG A 291 -13.188 -23.187 8.566 1.00 58.96 N ANISOU 2946 NH2 ARG A 291 8481 6424 7496 695 719 -820 N ATOM 2947 N ILE A 292 -20.329 -24.268 7.133 1.00 39.63 N ANISOU 2947 N ILE A 292 6539 3908 4611 -53 309 -874 N ATOM 2948 CA ILE A 292 -20.965 -25.302 7.944 1.00 40.30 C ANISOU 2948 CA ILE A 292 6681 3865 4766 -119 234 -839 C ATOM 2949 C ILE A 292 -22.045 -25.959 7.103 1.00 39.76 C ANISOU 2949 C ILE A 292 6746 3738 4623 -248 178 -922 C ATOM 2950 O ILE A 292 -23.103 -25.363 6.878 1.00 37.00 O ANISOU 2950 O ILE A 292 6362 3494 4202 -366 113 -905 O ATOM 2951 CB ILE A 292 -21.549 -24.748 9.254 1.00 40.63 C ANISOU 2951 CB ILE A 292 6602 3984 4850 -179 168 -705 C ATOM 2952 CG1 ILE A 292 -20.506 -23.896 9.988 1.00 37.84 C ANISOU 2952 CG1 ILE A 292 6113 3715 4551 -62 214 -629 C ATOM 2953 CG2 ILE A 292 -22.021 -25.910 10.158 1.00 42.32 C ANISOU 2953 CG2 ILE A 292 6886 4053 5140 -239 109 -660 C ATOM 2954 CD1 ILE A 292 -21.023 -23.226 11.245 1.00 36.50 C ANISOU 2954 CD1 ILE A 292 5829 3634 4406 -115 158 -508 C ATOM 2955 N ARG A 293 -21.784 -27.197 6.654 1.00 45.23 N ANISOU 2955 N ARG A 293 7589 4257 5339 -225 196 -1015 N ATOM 2956 CA ARG A 293 -22.692 -27.895 5.740 1.00 50.24 C ANISOU 2956 CA ARG A 293 8370 4821 5899 -345 144 -1116 C ATOM 2957 C ARG A 293 -24.122 -27.916 6.258 1.00 46.87 C ANISOU 2957 C ARG A 293 7914 4424 5468 -522 29 -1050 C ATOM 2958 O ARG A 293 -25.069 -27.652 5.510 1.00 46.50 O ANISOU 2958 O ARG A 293 7889 4448 5329 -638 -31 -1095 O ATOM 2959 CB ARG A 293 -22.231 -29.339 5.508 1.00 58.13 C ANISOU 2959 CB ARG A 293 9537 5597 6954 -296 169 -1208 C ATOM 2960 CG ARG A 293 -20.859 -29.510 4.925 1.00 66.22 C ANISOU 2960 CG ARG A 293 10597 6571 7990 -119 290 -1296 C ATOM 2961 CD ARG A 293 -20.687 -30.917 4.337 1.00 73.62 C ANISOU 2961 CD ARG A 293 11724 7298 8950 -95 305 -1423 C ATOM 2962 NE ARG A 293 -19.293 -31.184 3.990 1.00 80.19 N ANISOU 2962 NE ARG A 293 12541 8093 9836 97 422 -1486 N ATOM 2963 CZ ARG A 293 -18.858 -32.302 3.416 1.00 87.59 C ANISOU 2963 CZ ARG A 293 13556 8909 10815 162 450 -1581 C ATOM 2964 NH1 ARG A 293 -19.710 -33.276 3.114 1.00 90.80 N ANISOU 2964 NH1 ARG A 293 14075 9212 11214 50 370 -1623 N ATOM 2965 NH2 ARG A 293 -17.567 -32.447 3.141 1.00 90.06 N ANISOU 2965 NH2 ARG A 293 13828 9208 11185 340 560 -1636 N ATOM 2966 N GLU A 294 -24.299 -28.250 7.540 1.00 44.31 N ANISOU 2966 N GLU A 294 7541 4049 5244 -546 -4 -944 N ATOM 2967 CA GLU A 294 -25.642 -28.436 8.077 1.00 44.82 C ANISOU 2967 CA GLU A 294 7584 4128 5317 -721 -97 -887 C ATOM 2968 C GLU A 294 -26.458 -27.144 8.035 1.00 42.08 C ANISOU 2968 C GLU A 294 7089 3995 4905 -792 -136 -839 C ATOM 2969 O GLU A 294 -27.675 -27.186 7.815 1.00 41.32 O ANISOU 2969 O GLU A 294 6984 3939 4775 -942 -215 -850 O ATOM 2970 CB GLU A 294 -25.561 -28.979 9.502 1.00 50.62 C ANISOU 2970 CB GLU A 294 8298 4776 6160 -726 -108 -773 C ATOM 2971 CG GLU A 294 -26.901 -29.465 10.045 1.00 55.84 C ANISOU 2971 CG GLU A 294 8966 5414 6838 -919 -188 -724 C ATOM 2972 CD GLU A 294 -27.290 -30.821 9.510 1.00 59.41 C ANISOU 2972 CD GLU A 294 9598 5670 7303 -1011 -226 -809 C ATOM 2973 OE1 GLU A 294 -26.384 -31.633 9.228 1.00 61.64 O ANISOU 2973 OE1 GLU A 294 10012 5787 7622 -905 -188 -869 O ATOM 2974 OE2 GLU A 294 -28.502 -31.077 9.366 1.00 60.91 O ANISOU 2974 OE2 GLU A 294 9797 5873 7474 -1190 -297 -820 O ATOM 2975 N PHE A 295 -25.815 -25.984 8.256 1.00 38.22 N ANISOU 2975 N PHE A 295 6476 3641 4405 -685 -87 -787 N ATOM 2976 CA PHE A 295 -26.514 -24.717 8.048 1.00 38.76 C ANISOU 2976 CA PHE A 295 6422 3898 4407 -733 -123 -756 C ATOM 2977 C PHE A 295 -26.805 -24.499 6.566 1.00 39.31 C ANISOU 2977 C PHE A 295 6565 4008 4363 -763 -145 -861 C ATOM 2978 O PHE A 295 -27.922 -24.132 6.184 1.00 39.52 O ANISOU 2978 O PHE A 295 6558 4121 4337 -875 -228 -867 O ATOM 2979 CB PHE A 295 -25.693 -23.541 8.594 1.00 36.77 C ANISOU 2979 CB PHE A 295 6039 3762 4170 -614 -65 -682 C ATOM 2980 CG PHE A 295 -25.992 -23.182 10.031 1.00 38.03 C ANISOU 2980 CG PHE A 295 6077 3974 4399 -635 -82 -563 C ATOM 2981 CD1 PHE A 295 -27.201 -22.571 10.379 1.00 36.71 C ANISOU 2981 CD1 PHE A 295 5810 3921 4216 -743 -144 -518 C ATOM 2982 CD2 PHE A 295 -25.040 -23.391 11.030 1.00 35.90 C ANISOU 2982 CD2 PHE A 295 5787 3647 4205 -541 -37 -500 C ATOM 2983 CE1 PHE A 295 -27.466 -22.206 11.701 1.00 31.11 C ANISOU 2983 CE1 PHE A 295 4993 3268 3559 -760 -146 -417 C ATOM 2984 CE2 PHE A 295 -25.297 -23.011 12.351 1.00 33.17 C ANISOU 2984 CE2 PHE A 295 5341 3358 3904 -562 -52 -394 C ATOM 2985 CZ PHE A 295 -26.512 -22.423 12.679 1.00 29.70 C ANISOU 2985 CZ PHE A 295 4813 3033 3440 -674 -99 -356 C ATOM 2986 N ARG A 296 -25.796 -24.714 5.719 1.00 38.43 N ANISOU 2986 N ARG A 296 6552 3841 4210 -662 -70 -944 N ATOM 2987 CA ARG A 296 -25.945 -24.459 4.292 1.00 37.84 C ANISOU 2987 CA ARG A 296 6562 3810 4005 -682 -79 -1042 C ATOM 2988 C ARG A 296 -27.075 -25.295 3.694 1.00 37.91 C ANISOU 2988 C ARG A 296 6681 3754 3970 -831 -179 -1117 C ATOM 2989 O ARG A 296 -27.883 -24.792 2.901 1.00 37.91 O ANISOU 2989 O ARG A 296 6681 3849 3872 -912 -255 -1146 O ATOM 2990 CB ARG A 296 -24.608 -24.737 3.601 1.00 41.32 C ANISOU 2990 CB ARG A 296 7097 4183 4418 -548 39 -1125 C ATOM 2991 CG ARG A 296 -24.653 -24.812 2.095 1.00 47.00 C ANISOU 2991 CG ARG A 296 7956 4909 4994 -569 48 -1248 C ATOM 2992 CD ARG A 296 -23.241 -24.773 1.522 1.00 48.43 C ANISOU 2992 CD ARG A 296 8183 5068 5148 -422 192 -1311 C ATOM 2993 NE ARG A 296 -22.481 -26.013 1.687 1.00 45.75 N ANISOU 2993 NE ARG A 296 7938 4551 4892 -343 260 -1381 N ATOM 2994 CZ ARG A 296 -21.412 -26.153 2.471 1.00 46.50 C ANISOU 2994 CZ ARG A 296 7962 4598 5108 -211 342 -1340 C ATOM 2995 NH1 ARG A 296 -20.783 -27.321 2.534 1.00 48.39 N ANISOU 2995 NH1 ARG A 296 8298 4666 5424 -134 392 -1410 N ATOM 2996 NH2 ARG A 296 -20.966 -25.137 3.197 1.00 46.00 N ANISOU 2996 NH2 ARG A 296 7733 4653 5093 -154 369 -1229 N ATOM 2997 N GLN A 297 -27.168 -26.567 4.090 1.00 40.15 N ANISOU 2997 N GLN A 297 7054 3871 4328 -874 -190 -1145 N ATOM 2998 CA GLN A 297 -28.214 -27.436 3.554 1.00 42.99 C ANISOU 2998 CA GLN A 297 7524 4154 4657 -1028 -287 -1220 C ATOM 2999 C GLN A 297 -29.586 -27.065 4.100 1.00 44.54 C ANISOU 2999 C GLN A 297 7592 4452 4878 -1178 -396 -1143 C ATOM 3000 O GLN A 297 -30.592 -27.197 3.393 1.00 45.18 O ANISOU 3000 O GLN A 297 7689 4572 4906 -1296 -492 -1190 O ATOM 3001 CB GLN A 297 -27.890 -28.903 3.861 1.00 47.10 C ANISOU 3001 CB GLN A 297 8179 4455 5262 -1029 -265 -1264 C ATOM 3002 CG GLN A 297 -26.590 -29.399 3.207 1.00 54.89 C ANISOU 3002 CG GLN A 297 9271 5345 6238 -868 -156 -1351 C ATOM 3003 CD GLN A 297 -26.282 -30.869 3.502 1.00 63.60 C ANISOU 3003 CD GLN A 297 10479 6241 7444 -846 -142 -1380 C ATOM 3004 OE1 GLN A 297 -26.606 -31.382 4.572 1.00 68.94 O ANISOU 3004 OE1 GLN A 297 11146 6827 8220 -904 -178 -1302 O ATOM 3005 NE2 GLN A 297 -25.649 -31.548 2.548 1.00 63.76 N ANISOU 3005 NE2 GLN A 297 10599 6188 7439 -761 -88 -1488 N ATOM 3006 N THR A 298 -29.649 -26.592 5.348 1.00 42.40 N ANISOU 3006 N THR A 298 7171 4243 4696 -1162 -379 -1019 N ATOM 3007 CA THR A 298 -30.924 -26.169 5.913 1.00 40.38 C ANISOU 3007 CA THR A 298 6775 4099 4469 -1292 -464 -948 C ATOM 3008 C THR A 298 -31.386 -24.849 5.304 1.00 38.00 C ANISOU 3008 C THR A 298 6366 3987 4085 -1284 -511 -941 C ATOM 3009 O THR A 298 -32.567 -24.695 4.973 1.00 39.47 O ANISOU 3009 O THR A 298 6500 4248 4247 -1407 -615 -953 O ATOM 3010 CB THR A 298 -30.814 -26.059 7.434 1.00 41.86 C ANISOU 3010 CB THR A 298 6849 4295 4762 -1273 -421 -824 C ATOM 3011 OG1 THR A 298 -30.300 -27.284 7.958 1.00 42.35 O ANISOU 3011 OG1 THR A 298 7028 4169 4894 -1268 -383 -823 O ATOM 3012 CG2 THR A 298 -32.180 -25.799 8.052 1.00 45.15 C ANISOU 3012 CG2 THR A 298 7127 4813 5213 -1419 -493 -762 C ATOM 3013 N PHE A 299 -30.472 -23.875 5.175 1.00 35.88 N ANISOU 3013 N PHE A 299 6058 3795 3779 -1141 -441 -915 N ATOM 3014 CA PHE A 299 -30.763 -22.672 4.395 1.00 39.06 C ANISOU 3014 CA PHE A 299 6402 4350 4088 -1122 -484 -917 C ATOM 3015 C PHE A 299 -31.364 -23.035 3.032 1.00 43.56 C ANISOU 3015 C PHE A 299 7094 4909 4548 -1209 -572 -1023 C ATOM 3016 O PHE A 299 -32.375 -22.463 2.610 1.00 47.51 O ANISOU 3016 O PHE A 299 7529 5520 5004 -1285 -680 -1018 O ATOM 3017 CB PHE A 299 -29.493 -21.827 4.188 1.00 38.11 C ANISOU 3017 CB PHE A 299 6281 4272 3928 -965 -381 -900 C ATOM 3018 CG PHE A 299 -28.915 -21.196 5.459 1.00 36.98 C ANISOU 3018 CG PHE A 299 6003 4171 3878 -877 -312 -793 C ATOM 3019 CD1 PHE A 299 -29.601 -21.210 6.663 1.00 34.94 C ANISOU 3019 CD1 PHE A 299 5628 3936 3712 -935 -343 -715 C ATOM 3020 CD2 PHE A 299 -27.656 -20.589 5.424 1.00 34.56 C ANISOU 3020 CD2 PHE A 299 5690 3881 3561 -741 -213 -777 C ATOM 3021 CE1 PHE A 299 -29.035 -20.622 7.814 1.00 34.70 C ANISOU 3021 CE1 PHE A 299 5489 3945 3750 -855 -282 -624 C ATOM 3022 CE2 PHE A 299 -27.098 -20.010 6.565 1.00 31.92 C ANISOU 3022 CE2 PHE A 299 5238 3584 3307 -666 -161 -686 C ATOM 3023 CZ PHE A 299 -27.785 -20.030 7.751 1.00 30.28 C ANISOU 3023 CZ PHE A 299 4929 3397 3179 -721 -198 -612 C ATOM 3024 N ARG A 300 -30.755 -23.994 2.330 1.00 45.77 N ANISOU 3024 N ARG A 300 7554 5056 4783 -1195 -532 -1124 N ATOM 3025 CA ARG A 300 -31.266 -24.353 1.008 1.00 54.70 C ANISOU 3025 CA ARG A 300 8766 6193 5824 -1242 -599 -1204 C ATOM 3026 C ARG A 300 -32.684 -24.908 1.090 1.00 55.41 C ANISOU 3026 C ARG A 300 8794 6292 5967 -1390 -723 -1199 C ATOM 3027 O ARG A 300 -33.547 -24.540 0.284 1.00 53.61 O ANISOU 3027 O ARG A 300 8524 6163 5683 -1437 -821 -1210 O ATOM 3028 CB ARG A 300 -30.342 -25.361 0.330 1.00 62.70 C ANISOU 3028 CB ARG A 300 9944 7068 6810 -1174 -512 -1299 C ATOM 3029 CG ARG A 300 -29.004 -24.789 -0.095 1.00 68.38 C ANISOU 3029 CG ARG A 300 10715 7805 7461 -1026 -387 -1320 C ATOM 3030 CD ARG A 300 -28.219 -25.810 -0.918 1.00 74.44 C ANISOU 3030 CD ARG A 300 11630 8453 8200 -962 -307 -1426 C ATOM 3031 NE ARG A 300 -26.962 -25.242 -1.388 1.00 76.96 N ANISOU 3031 NE ARG A 300 11976 8807 8457 -825 -178 -1446 N ATOM 3032 CZ ARG A 300 -26.837 -24.547 -2.512 1.00 79.45 C ANISOU 3032 CZ ARG A 300 12312 9231 8645 -800 -167 -1465 C ATOM 3033 NH1 ARG A 300 -25.655 -24.064 -2.858 1.00 82.50 N ANISOU 3033 NH1 ARG A 300 12711 9648 8987 -683 -35 -1476 N ATOM 3034 NH2 ARG A 300 -27.888 -24.340 -3.297 1.00 79.25 N ANISOU 3034 NH2 ARG A 300 12289 9283 8540 -892 -287 -1469 N ATOM 3035 N LYS A 301 -32.949 -25.788 2.061 1.00 54.87 N ANISOU 3035 N LYS A 301 8715 6122 6011 -1463 -719 -1177 N ATOM 3036 CA LYS A 301 -34.293 -26.339 2.194 1.00 55.35 C ANISOU 3036 CA LYS A 301 8705 6195 6132 -1611 -823 -1167 C ATOM 3037 C LYS A 301 -35.302 -25.252 2.531 1.00 52.30 C ANISOU 3037 C LYS A 301 8125 5985 5762 -1661 -904 -1094 C ATOM 3038 O LYS A 301 -36.423 -25.260 2.014 1.00 54.81 O ANISOU 3038 O LYS A 301 8373 6375 6078 -1744 -1009 -1108 O ATOM 3039 CB LYS A 301 -34.320 -27.440 3.256 1.00 58.96 C ANISOU 3039 CB LYS A 301 9187 6509 6707 -1679 -788 -1140 C ATOM 3040 CG LYS A 301 -33.563 -28.692 2.863 1.00 65.45 C ANISOU 3040 CG LYS A 301 10193 7143 7533 -1640 -733 -1218 C ATOM 3041 CD LYS A 301 -33.713 -29.805 3.899 1.00 68.74 C ANISOU 3041 CD LYS A 301 10636 7412 8070 -1715 -715 -1177 C ATOM 3042 CE LYS A 301 -32.925 -31.041 3.470 1.00 72.88 C ANISOU 3042 CE LYS A 301 11345 7742 8605 -1657 -664 -1258 C ATOM 3043 NZ LYS A 301 -32.856 -32.087 4.534 1.00 75.26 N ANISOU 3043 NZ LYS A 301 11689 7883 9023 -1701 -638 -1205 N ATOM 3044 N ILE A 302 -34.924 -24.309 3.397 1.00 51.48 N ANISOU 3044 N ILE A 302 7929 5953 5680 -1607 -858 -1019 N ATOM 3045 CA ILE A 302 -35.828 -23.217 3.762 1.00 52.95 C ANISOU 3045 CA ILE A 302 7922 6308 5888 -1636 -926 -951 C ATOM 3046 C ILE A 302 -36.130 -22.344 2.551 1.00 57.33 C ANISOU 3046 C ILE A 302 8461 6978 6345 -1585 -1003 -974 C ATOM 3047 O ILE A 302 -37.281 -21.959 2.310 1.00 58.32 O ANISOU 3047 O ILE A 302 8460 7208 6489 -1638 -1107 -959 O ATOM 3048 CB ILE A 302 -35.234 -22.365 4.900 1.00 46.58 C ANISOU 3048 CB ILE A 302 7011 5555 5131 -1546 -838 -859 C ATOM 3049 CG1 ILE A 302 -35.091 -23.167 6.190 1.00 43.80 C ANISOU 3049 CG1 ILE A 302 6640 5112 4891 -1581 -763 -806 C ATOM 3050 CG2 ILE A 302 -36.108 -21.149 5.140 1.00 43.75 C ANISOU 3050 CG2 ILE A 302 6457 5374 4791 -1546 -903 -798 C ATOM 3051 CD1 ILE A 302 -34.398 -22.397 7.300 1.00 36.02 C ANISOU 3051 CD1 ILE A 302 5552 4177 3956 -1460 -664 -708 C ATOM 3052 N ILE A 303 -35.091 -21.972 1.803 1.00 59.12 N ANISOU 3052 N ILE A 303 8807 7187 6467 -1475 -947 -1006 N ATOM 3053 CA ILE A 303 -35.285 -21.064 0.677 1.00 61.00 C ANISOU 3053 CA ILE A 303 9042 7531 6602 -1421 -1010 -1012 C ATOM 3054 C ILE A 303 -36.089 -21.752 -0.425 1.00 64.75 C ANISOU 3054 C ILE A 303 9572 7994 7037 -1492 -1107 -1081 C ATOM 3055 O ILE A 303 -37.069 -21.196 -0.933 1.00 64.75 O ANISOU 3055 O ILE A 303 9482 8100 7022 -1519 -1222 -1067 O ATOM 3056 CB ILE A 303 -33.926 -20.541 0.171 1.00 58.17 C ANISOU 3056 CB ILE A 303 8801 7159 6143 -1294 -907 -1024 C ATOM 3057 CG1 ILE A 303 -33.289 -19.612 1.213 1.00 53.65 C ANISOU 3057 CG1 ILE A 303 8147 6630 5606 -1225 -836 -948 C ATOM 3058 CG2 ILE A 303 -34.081 -19.804 -1.149 1.00 57.66 C ANISOU 3058 CG2 ILE A 303 8771 7180 5959 -1251 -964 -1034 C ATOM 3059 CD1 ILE A 303 -31.783 -19.651 1.223 1.00 50.95 C ANISOU 3059 CD1 ILE A 303 7904 6219 5237 -1108 -685 -960 C ATOM 3060 N ARG A 304 -35.715 -22.984 -0.784 1.00 69.22 N ANISOU 3060 N ARG A 304 10283 8426 7591 -1522 -1067 -1160 N ATOM 3061 CA ARG A 304 -36.426 -23.722 -1.830 1.00 74.70 C ANISOU 3061 CA ARG A 304 11042 9097 8242 -1595 -1156 -1236 C ATOM 3062 C ARG A 304 -37.898 -23.919 -1.486 1.00 77.73 C ANISOU 3062 C ARG A 304 11278 9536 8719 -1720 -1278 -1215 C ATOM 3063 O ARG A 304 -38.773 -23.331 -2.128 1.00 80.56 O ANISOU 3063 O ARG A 304 11558 10006 9046 -1737 -1392 -1210 O ATOM 3064 CB ARG A 304 -35.773 -25.086 -2.088 1.00 76.93 C ANISOU 3064 CB ARG A 304 11499 9213 8520 -1607 -1086 -1323 C ATOM 3065 CG ARG A 304 -34.419 -25.000 -2.774 1.00 79.98 C ANISOU 3065 CG ARG A 304 12035 9552 8803 -1484 -972 -1371 C ATOM 3066 CD ARG A 304 -33.779 -26.367 -2.987 1.00 85.32 C ANISOU 3066 CD ARG A 304 12870 10058 9489 -1481 -899 -1463 C ATOM 3067 NE ARG A 304 -32.335 -26.238 -3.190 1.00 88.87 N ANISOU 3067 NE ARG A 304 13419 10461 9886 -1345 -756 -1490 N ATOM 3068 CZ ARG A 304 -31.500 -27.257 -3.374 1.00 91.92 C ANISOU 3068 CZ ARG A 304 13938 10705 10281 -1297 -665 -1569 C ATOM 3069 NH1 ARG A 304 -30.202 -27.026 -3.545 1.00 90.48 N ANISOU 3069 NH1 ARG A 304 13816 10502 10060 -1165 -530 -1590 N ATOM 3070 NH2 ARG A 304 -31.958 -28.505 -3.391 1.00 94.45 N ANISOU 3070 NH2 ARG A 304 14325 10904 10656 -1377 -706 -1628 N ATOM 3071 N SER A 305 -38.176 -24.739 -0.478 1.00 78.92 N ANISOU 3071 N SER A 305 11388 9610 8987 -1804 -1253 -1200 N ATOM 3072 CA SER A 305 -39.545 -25.047 -0.066 1.00 81.85 C ANISOU 3072 CA SER A 305 11612 10026 9459 -1932 -1347 -1181 C ATOM 3073 C SER A 305 -40.391 -23.796 0.153 1.00 79.61 C ANISOU 3073 C SER A 305 11124 9918 9205 -1917 -1423 -1113 C ATOM 3074 O SER A 305 -39.941 -22.838 0.779 1.00 77.81 O ANISOU 3074 O SER A 305 10826 9753 8984 -1836 -1370 -1046 O ATOM 3075 CB SER A 305 -39.525 -25.885 1.214 1.00 85.74 C ANISOU 3075 CB SER A 305 12082 10422 10074 -2007 -1276 -1144 C ATOM 3076 OG SER A 305 -38.618 -26.972 1.097 1.00 88.76 O ANISOU 3076 OG SER A 305 12655 10629 10439 -1994 -1198 -1199 O TER 3077 SER A 305 HETATM 3078 C10 9Y2 A1201 -22.185 8.360 16.124 1.00 19.79 C ANISOU 3078 C10 9Y2 A1201 2577 2695 2249 109 -240 126 C HETATM 3079 C13 9Y2 A1201 -22.474 6.241 17.209 1.00 15.85 C ANISOU 3079 C13 9Y2 A1201 1974 2308 1740 103 -192 75 C HETATM 3080 C15 9Y2 A1201 -24.336 7.298 16.169 1.00 15.01 C ANISOU 3080 C15 9Y2 A1201 1903 2176 1626 173 -289 82 C HETATM 3081 C17 9Y2 A1201 -21.899 5.041 17.902 1.00 18.28 C ANISOU 3081 C17 9Y2 A1201 2239 2659 2048 78 -147 63 C HETATM 3082 C20 9Y2 A1201 -19.950 4.048 18.928 1.00 16.74 C ANISOU 3082 C20 9Y2 A1201 1999 2479 1881 35 -89 68 C HETATM 3083 C22 9Y2 A1201 -18.235 2.837 19.708 1.00 16.77 C ANISOU 3083 C22 9Y2 A1201 1950 2502 1919 12 -50 79 C HETATM 3084 C01 9Y2 A1201 -22.926 11.047 12.461 1.00 21.80 C ANISOU 3084 C01 9Y2 A1201 3115 2757 2410 122 -379 297 C HETATM 3085 C02 9Y2 A1201 -23.522 12.192 13.266 1.00 21.02 C ANISOU 3085 C02 9Y2 A1201 3009 2595 2381 187 -441 271 C HETATM 3086 C03 9Y2 A1201 -22.377 12.812 14.026 1.00 19.69 C ANISOU 3086 C03 9Y2 A1201 2846 2379 2258 139 -396 263 C HETATM 3087 C04 9Y2 A1201 -24.098 13.213 12.282 1.00 18.00 C ANISOU 3087 C04 9Y2 A1201 2727 2132 1982 223 -525 331 C HETATM 3088 C05 9Y2 A1201 -24.602 11.735 14.261 1.00 18.15 C ANISOU 3088 C05 9Y2 A1201 2543 2294 2060 258 -464 198 C HETATM 3089 C06 9Y2 A1201 -24.042 10.795 15.333 1.00 21.67 C ANISOU 3089 C06 9Y2 A1201 2907 2809 2517 223 -391 148 C HETATM 3090 C09 9Y2 A1201 -23.551 8.368 15.827 1.00 17.39 C ANISOU 3090 C09 9Y2 A1201 2267 2407 1936 161 -293 115 C HETATM 3091 C12 9Y2 A1201 -21.630 7.284 16.823 1.00 16.98 C ANISOU 3091 C12 9Y2 A1201 2164 2391 1895 84 -191 104 C HETATM 3092 C14 9Y2 A1201 -23.813 6.211 16.860 1.00 13.22 C ANISOU 3092 C14 9Y2 A1201 1632 1994 1395 140 -235 64 C HETATM 3093 C23 9Y2 A1201 -19.200 1.862 19.828 1.00 18.48 C ANISOU 3093 C23 9Y2 A1201 2171 2745 2107 26 -52 69 C HETATM 3094 F11 9Y2 A1201 -21.412 9.401 15.755 1.00 22.05 F ANISOU 3094 F11 9Y2 A1201 2920 2912 2546 81 -240 160 F HETATM 3095 F16 9Y2 A1201 -25.617 7.316 15.868 1.00 18.91 F ANISOU 3095 F16 9Y2 A1201 2374 2691 2120 217 -341 70 F HETATM 3096 N08 9Y2 A1201 -24.082 9.428 15.043 1.00 18.29 N ANISOU 3096 N08 9Y2 A1201 2441 2460 2047 194 -355 145 N HETATM 3097 N19 9Y2 A1201 -20.586 5.148 18.366 1.00 14.52 N ANISOU 3097 N19 9Y2 A1201 1754 2168 1595 50 -119 72 N HETATM 3098 N21 9Y2 A1201 -18.657 4.002 19.211 1.00 17.00 N ANISOU 3098 N21 9Y2 A1201 2011 2505 1943 12 -67 80 N HETATM 3099 O07 9Y2 A1201 -23.630 11.147 16.426 1.00 20.38 O ANISOU 3099 O07 9Y2 A1201 2716 2633 2394 222 -370 109 O HETATM 3100 O18 9Y2 A1201 -22.549 4.002 17.919 1.00 19.95 O ANISOU 3100 O18 9Y2 A1201 2429 2911 2241 79 -142 51 O HETATM 3101 S24 9Y2 A1201 -20.688 2.530 19.264 1.00 18.67 S ANISOU 3101 S24 9Y2 A1201 2221 2770 2103 41 -79 56 S HETATM 3102 NA NA A1202 -23.245 -8.560 16.581 1.00 44.50 NA HETATM 3103 C1 CLR A1203 -38.038 9.563 31.059 1.00 63.97 C HETATM 3104 C2 CLR A1203 -37.897 11.099 30.966 1.00 64.39 C HETATM 3105 C3 CLR A1203 -36.634 11.523 30.264 1.00 61.65 C HETATM 3106 C4 CLR A1203 -36.497 10.842 28.886 1.00 59.49 C HETATM 3107 C5 CLR A1203 -36.657 9.343 29.000 1.00 59.91 C HETATM 3108 C6 CLR A1203 -35.709 8.544 28.481 1.00 59.80 C HETATM 3109 C7 CLR A1203 -35.793 7.030 28.399 1.00 60.64 C HETATM 3110 C8 CLR A1203 -37.172 6.522 28.791 1.00 63.54 C HETATM 3111 C9 CLR A1203 -37.686 7.306 30.007 1.00 64.97 C HETATM 3112 C10 CLR A1203 -37.876 8.809 29.730 1.00 63.46 C HETATM 3113 C11 CLR A1203 -38.901 6.629 30.650 1.00 64.67 C HETATM 3114 C12 CLR A1203 -38.712 5.125 30.872 1.00 66.40 C HETATM 3115 C13 CLR A1203 -38.340 4.383 29.619 1.00 68.67 C HETATM 3116 C14 CLR A1203 -37.054 5.055 29.142 1.00 67.96 C HETATM 3117 C15 CLR A1203 -36.494 4.131 28.062 1.00 70.88 C HETATM 3118 C16 CLR A1203 -36.978 2.745 28.493 1.00 73.42 C HETATM 3119 C17 CLR A1203 -37.903 2.909 29.706 1.00 73.73 C HETATM 3120 C18 CLR A1203 -39.516 4.462 28.599 1.00 65.51 C HETATM 3121 C19 CLR A1203 -39.134 9.063 28.843 1.00 60.43 C HETATM 3122 C20 CLR A1203 -38.983 1.813 29.767 1.00 76.00 C HETATM 3123 C21 CLR A1203 -39.404 1.529 31.212 1.00 75.69 C HETATM 3124 C22 CLR A1203 -38.540 0.504 29.061 1.00 77.20 C HETATM 3125 C23 CLR A1203 -39.364 -0.748 29.414 1.00 78.07 C HETATM 3126 C24 CLR A1203 -39.620 -1.650 28.200 1.00 79.31 C HETATM 3127 C25 CLR A1203 -40.810 -2.616 28.374 1.00 81.08 C HETATM 3128 C26 CLR A1203 -40.523 -4.007 27.808 1.00 80.27 C HETATM 3129 C27 CLR A1203 -41.298 -2.728 29.820 1.00 81.76 C HETATM 3130 O1 CLR A1203 -36.633 12.950 30.105 1.00 61.06 O HETATM 3131 C1 CLR A1204 -38.100 10.947 21.610 1.00 21.11 C HETATM 3132 C2 CLR A1204 -37.736 12.432 21.822 1.00 23.73 C HETATM 3133 C3 CLR A1204 -38.026 12.840 23.256 1.00 26.51 C HETATM 3134 C4 CLR A1204 -37.251 11.974 24.274 1.00 24.19 C HETATM 3135 C5 CLR A1204 -37.482 10.513 24.023 1.00 24.42 C HETATM 3136 C6 CLR A1204 -37.761 9.758 25.100 1.00 20.86 C HETATM 3137 C7 CLR A1204 -37.967 8.259 25.030 1.00 22.13 C HETATM 3138 C8 CLR A1204 -37.651 7.659 23.637 1.00 22.94 C HETATM 3139 C9 CLR A1204 -38.076 8.601 22.504 1.00 24.72 C HETATM 3140 C10 CLR A1204 -37.404 9.972 22.584 1.00 25.18 C HETATM 3141 C11 CLR A1204 -37.886 7.912 21.138 1.00 24.99 C HETATM 3142 C12 CLR A1204 -38.594 6.549 21.078 1.00 22.09 C HETATM 3143 C13 CLR A1204 -38.148 5.598 22.154 1.00 24.43 C HETATM 3144 C14 CLR A1204 -38.408 6.354 23.462 1.00 23.46 C HETATM 3145 C15 CLR A1204 -38.224 5.291 24.553 1.00 25.82 C HETATM 3146 C16 CLR A1204 -38.609 3.978 23.863 1.00 25.79 C HETATM 3147 C17 CLR A1204 -38.927 4.284 22.394 1.00 23.05 C HETATM 3148 C18 CLR A1204 -36.638 5.234 21.973 1.00 24.52 C HETATM 3149 C19 CLR A1204 -35.905 9.754 22.152 1.00 22.78 C HETATM 3150 C20 CLR A1204 -38.687 3.069 21.490 1.00 23.96 C HETATM 3151 C21 CLR A1204 -38.870 3.379 19.994 1.00 23.15 C HETATM 3152 C22 CLR A1204 -39.646 1.914 21.875 1.00 29.59 C HETATM 3153 C23 CLR A1204 -39.375 0.591 21.121 1.00 30.54 C HETATM 3154 C24 CLR A1204 -40.384 -0.485 21.544 1.00 37.15 C HETATM 3155 C25 CLR A1204 -39.962 -1.893 21.085 1.00 45.97 C HETATM 3156 C26 CLR A1204 -40.478 -2.991 22.002 1.00 48.54 C HETATM 3157 C27 CLR A1204 -40.414 -2.181 19.655 1.00 49.55 C HETATM 3158 O1 CLR A1204 -37.667 14.211 23.472 1.00 26.92 O HETATM 3159 C1 CLR A1205 -8.344 11.001 13.260 1.00 28.28 C HETATM 3160 C2 CLR A1205 -8.373 12.554 13.260 1.00 27.67 C HETATM 3161 C3 CLR A1205 -7.009 13.132 12.952 1.00 30.23 C HETATM 3162 C4 CLR A1205 -6.528 12.640 11.580 1.00 28.40 C HETATM 3163 C5 CLR A1205 -6.510 11.132 11.557 1.00 29.82 C HETATM 3164 C6 CLR A1205 -5.397 10.492 11.139 1.00 29.57 C HETATM 3165 C7 CLR A1205 -5.321 8.996 10.864 1.00 28.72 C HETATM 3166 C8 CLR A1205 -6.694 8.320 10.965 1.00 29.43 C HETATM 3167 C9 CLR A1205 -7.487 8.914 12.140 1.00 27.67 C HETATM 3168 C10 CLR A1205 -7.780 10.406 11.962 1.00 29.68 C HETATM 3169 C11 CLR A1205 -8.757 8.111 12.393 1.00 25.79 C HETATM 3170 C12 CLR A1205 -8.502 6.606 12.507 1.00 24.52 C HETATM 3171 C13 CLR A1205 -7.826 6.017 11.291 1.00 27.73 C HETATM 3172 C14 CLR A1205 -6.523 6.817 11.152 1.00 30.10 C HETATM 3173 C15 CLR A1205 -5.687 6.040 10.122 1.00 31.96 C HETATM 3174 C16 CLR A1205 -6.103 4.582 10.362 1.00 32.88 C HETATM 3175 C17 CLR A1205 -7.295 4.568 11.341 1.00 31.30 C HETATM 3176 C18 CLR A1205 -8.731 6.200 10.038 1.00 25.11 C HETATM 3177 C19 CLR A1205 -8.792 10.632 10.790 1.00 27.28 C HETATM 3178 C20 CLR A1205 -8.241 3.379 11.083 1.00 31.25 C HETATM 3179 C21 CLR A1205 -9.499 3.415 11.963 1.00 31.69 C HETATM 3180 C22 CLR A1205 -7.530 2.045 11.360 1.00 30.40 C HETATM 3181 C23 CLR A1205 -8.313 0.762 11.007 1.00 31.76 C HETATM 3182 C24 CLR A1205 -7.426 -0.426 11.390 1.00 36.91 C HETATM 3183 C25 CLR A1205 -8.086 -1.811 11.249 1.00 40.87 C HETATM 3184 C26 CLR A1205 -8.980 -2.095 12.453 1.00 34.59 C HETATM 3185 C27 CLR A1205 -8.928 -1.851 9.977 1.00 47.84 C HETATM 3186 O1 CLR A1205 -7.102 14.560 12.906 1.00 32.30 O HETATM 3187 C1 CLR A1206 -3.079 8.408 21.210 1.00 21.19 C HETATM 3188 C2 CLR A1206 -2.850 9.946 21.145 1.00 23.53 C HETATM 3189 C3 CLR A1206 -1.942 10.303 20.002 1.00 26.40 C HETATM 3190 C4 CLR A1206 -2.458 9.745 18.654 1.00 24.99 C HETATM 3191 C5 CLR A1206 -2.643 8.244 18.749 1.00 21.86 C HETATM 3192 C6 CLR A1206 -2.102 7.437 17.804 1.00 22.01 C HETATM 3193 C7 CLR A1206 -2.299 5.926 17.712 1.00 21.70 C HETATM 3194 C8 CLR A1206 -3.452 5.499 18.624 1.00 23.26 C HETATM 3195 C9 CLR A1206 -3.399 6.227 19.981 1.00 21.35 C HETATM 3196 C10 CLR A1206 -3.516 7.752 19.882 1.00 21.25 C HETATM 3197 C11 CLR A1206 -4.421 5.643 20.963 1.00 23.02 C HETATM 3198 C12 CLR A1206 -4.429 4.119 21.025 1.00 22.13 C HETATM 3199 C13 CLR A1206 -4.573 3.459 19.672 1.00 25.73 C HETATM 3200 C14 CLR A1206 -3.409 3.998 18.851 1.00 24.32 C HETATM 3201 C15 CLR A1206 -3.388 3.121 17.608 1.00 23.95 C HETATM 3202 C16 CLR A1206 -4.023 1.804 18.080 1.00 27.04 C HETATM 3203 C17 CLR A1206 -4.365 1.937 19.566 1.00 27.73 C HETATM 3204 C18 CLR A1206 -5.952 3.801 19.022 1.00 20.70 C HETATM 3205 C19 CLR A1206 -4.988 8.188 19.551 1.00 18.09 C HETATM 3206 C20 CLR A1206 -5.483 0.950 19.990 1.00 27.93 C HETATM 3207 C21 CLR A1206 -5.995 1.122 21.425 1.00 21.67 C HETATM 3208 C22 CLR A1206 -5.001 -0.515 19.816 1.00 32.20 C HETATM 3209 C23 CLR A1206 -6.036 -1.596 20.175 1.00 38.10 C HETATM 3210 C24 CLR A1206 -5.851 -2.810 19.251 1.00 44.21 C HETATM 3211 C25 CLR A1206 -5.430 -4.109 19.951 1.00 50.78 C HETATM 3212 C26 CLR A1206 -4.879 -5.137 18.960 1.00 51.20 C HETATM 3213 C27 CLR A1206 -4.459 -3.914 21.115 1.00 54.13 C HETATM 3214 O1 CLR A1206 -1.873 11.721 19.892 1.00 25.62 O HETATM 3215 C1 OLA A1207 -8.452 14.809 7.755 1.00 71.22 C HETATM 3216 O1 OLA A1207 -8.277 15.918 7.173 1.00 74.48 O HETATM 3217 O2 OLA A1207 -8.200 14.732 8.973 1.00 74.14 O HETATM 3218 C2 OLA A1207 -8.957 13.601 7.000 1.00 64.16 C HETATM 3219 C3 OLA A1207 -8.083 12.379 7.246 1.00 58.69 C HETATM 3220 C4 OLA A1207 -8.688 11.150 6.596 1.00 57.31 C HETATM 3221 C5 OLA A1207 -7.802 9.934 6.695 1.00 57.00 C HETATM 3222 C6 OLA A1207 -8.343 8.754 5.911 1.00 57.61 C HETATM 3223 C7 OLA A1207 -7.702 7.452 6.369 1.00 58.66 C HETATM 3224 C8 OLA A1207 -8.692 6.311 6.461 1.00 61.17 C HETATM 3225 C9 OLA A1207 -8.426 5.328 5.329 1.00 61.87 C HETATM 3226 C10 OLA A1207 -9.322 4.907 4.402 1.00 60.98 C HETATM 3227 C11 OLA A1207 -10.767 5.355 4.315 1.00 57.36 C HETATM 3228 C12 OLA A1207 -11.656 4.298 3.625 1.00 54.00 C HETATM 3229 C13 OLA A1207 -11.301 3.980 2.158 1.00 52.43 C HETATM 3230 C1 OLA A1208 -20.344 -22.301 28.118 1.00 58.16 C HETATM 3231 O1 OLA A1208 -20.835 -21.922 27.030 1.00 64.32 O HETATM 3232 O2 OLA A1208 -20.285 -23.525 28.289 1.00 63.60 O HETATM 3233 C2 OLA A1208 -19.856 -21.330 29.172 1.00 48.19 C HETATM 3234 C3 OLA A1208 -20.173 -19.877 28.814 1.00 43.37 C HETATM 3235 C4 OLA A1208 -19.359 -18.874 29.614 1.00 40.53 C HETATM 3236 C5 OLA A1208 -19.942 -17.477 29.596 1.00 39.50 C HETATM 3237 C6 OLA A1208 -19.081 -16.438 28.903 1.00 38.29 C HETATM 3238 C7 OLA A1208 -19.612 -15.023 29.111 1.00 38.53 C HETATM 3239 C1 OLA A1209 -21.497 -8.785 3.383 1.00 65.39 C HETATM 3240 O1 OLA A1209 -20.929 -9.543 2.535 1.00 69.36 O HETATM 3241 O2 OLA A1209 -22.352 -9.301 4.121 1.00 68.53 O HETATM 3242 C2 OLA A1209 -21.163 -7.312 3.530 1.00 57.67 C HETATM 3243 C3 OLA A1209 -21.919 -6.415 2.546 1.00 53.89 C HETATM 3244 C4 OLA A1209 -23.087 -5.625 3.134 1.00 49.52 C HETATM 3245 C5 OLA A1209 -23.127 -4.190 2.644 1.00 47.89 C HETATM 3246 C6 OLA A1209 -24.507 -3.616 2.342 1.00 47.13 C HETATM 3247 C7 OLA A1209 -24.409 -2.134 1.989 1.00 46.99 C HETATM 3248 C1 OLA A1210 -20.770 12.969 3.073 1.00 64.01 C HETATM 3249 O1 OLA A1210 -19.529 13.070 2.904 1.00 66.54 O HETATM 3250 O2 OLA A1210 -21.294 13.779 3.850 1.00 65.93 O HETATM 3251 C2 OLA A1210 -21.598 11.921 2.360 1.00 61.08 C HETATM 3252 C3 OLA A1210 -20.875 10.577 2.231 1.00 58.58 C HETATM 3253 C4 OLA A1210 -21.511 9.486 3.082 1.00 56.32 C HETATM 3254 C5 OLA A1210 -20.737 8.188 3.089 1.00 56.32 C HETATM 3255 C6 OLA A1210 -21.513 6.992 3.628 1.00 57.12 C HETATM 3256 C7 OLA A1210 -20.708 5.710 3.471 1.00 56.63 C HETATM 3257 C8 OLA A1210 -21.496 4.543 2.920 1.00 55.53 C HETATM 3258 C9 OLA A1210 -20.972 4.161 1.544 1.00 55.26 C HETATM 3259 C10 OLA A1210 -20.435 2.962 1.221 1.00 57.61 C HETATM 3260 C11 OLA A1210 -20.251 1.826 2.210 1.00 61.58 C HETATM 3261 C12 OLA A1210 -21.015 0.529 1.847 1.00 64.76 C HETATM 3262 C13 OLA A1210 -20.735 -0.638 2.827 1.00 63.02 C HETATM 3263 C14 OLA A1210 -19.665 -0.288 3.878 1.00 59.78 C HETATM 3264 C15 OLA A1210 -18.889 -1.481 4.475 1.00 58.34 C HETATM 3265 C16 OLA A1210 -18.432 -2.539 3.453 1.00 58.38 C HETATM 3266 C1 OLA A1211 -28.019 -20.503 40.006 1.00 68.60 C HETATM 3267 O1 OLA A1211 -27.044 -21.296 39.860 1.00 67.76 O HETATM 3268 O2 OLA A1211 -28.999 -20.923 40.653 1.00 67.09 O HETATM 3269 C2 OLA A1211 -28.013 -19.099 39.406 1.00 69.12 C HETATM 3270 C3 OLA A1211 -27.500 -18.001 40.351 1.00 68.61 C HETATM 3271 C4 OLA A1211 -27.253 -16.646 39.683 1.00 66.15 C HETATM 3272 C5 OLA A1211 -25.793 -16.233 39.544 1.00 63.76 C HETATM 3273 C6 OLA A1211 -25.536 -15.148 38.499 1.00 61.90 C HETATM 3274 C7 OLA A1211 -24.397 -14.186 38.838 1.00 62.82 C HETATM 3275 C8 OLA A1211 -24.708 -12.709 38.611 1.00 65.37 C HETATM 3276 C9 OLA A1211 -23.726 -11.841 39.391 1.00 66.21 C HETATM 3277 C10 OLA A1211 -23.757 -10.499 39.594 1.00 67.05 C HETATM 3278 C11 OLA A1211 -24.805 -9.537 39.068 1.00 66.59 C HETATM 3279 C12 OLA A1211 -24.417 -8.039 39.218 1.00 62.59 C HETATM 3280 C13 OLA A1211 -22.995 -7.756 39.756 1.00 56.46 C HETATM 3281 C14 OLA A1211 -22.131 -6.902 38.810 1.00 55.13 C HETATM 3282 C15 OLA A1211 -22.899 -5.948 37.867 1.00 55.71 C HETATM 3283 C16 OLA A1211 -22.101 -5.554 36.602 1.00 56.20 C HETATM 3284 C17 OLA A1211 -21.748 -4.061 36.452 1.00 53.60 C HETATM 3285 C18 OLA A1211 -22.945 -3.168 36.093 1.00 51.61 C HETATM 3286 C1 OLA A1212 -36.126 -15.625 5.261 1.00 74.86 C HETATM 3287 O1 OLA A1212 -35.623 -16.608 5.831 1.00 75.31 O HETATM 3288 O2 OLA A1212 -36.848 -14.847 5.945 1.00 73.72 O HETATM 3289 C2 OLA A1212 -35.858 -15.387 3.788 1.00 75.17 C HETATM 3290 C3 OLA A1212 -34.589 -14.551 3.589 1.00 75.03 C HETATM 3291 C4 OLA A1212 -33.405 -15.339 3.041 1.00 70.71 C HETATM 3292 C5 OLA A1212 -32.821 -14.708 1.797 1.00 64.48 C HETATM 3293 C6 OLA A1212 -31.328 -14.464 1.879 1.00 57.83 C HETATM 3294 C7 OLA A1212 -31.002 -13.246 2.729 1.00 53.40 C HETATM 3295 C8 OLA A1212 -29.563 -13.232 3.202 1.00 50.85 C HETATM 3296 C9 OLA A1212 -29.038 -11.809 3.121 1.00 50.02 C HETATM 3297 C10 OLA A1212 -27.934 -11.365 3.758 1.00 50.70 C HETATM 3298 C1 OLA A1213 -15.045 12.810 0.528 1.00 62.94 C HETATM 3299 O1 OLA A1213 -13.936 13.370 0.297 1.00 64.80 O HETATM 3300 O2 OLA A1213 -16.000 13.537 0.865 1.00 62.24 O HETATM 3301 C2 OLA A1213 -15.202 11.305 0.402 1.00 61.91 C HETATM 3302 C3 OLA A1213 -16.650 10.865 0.634 1.00 63.24 C HETATM 3303 C4 OLA A1213 -16.845 9.351 0.599 1.00 61.69 C HETATM 3304 C5 OLA A1213 -15.557 8.557 0.668 1.00 59.90 C HETATM 3305 C6 OLA A1213 -15.740 7.043 0.613 1.00 58.59 C HETATM 3306 C1 OLA A1214 -39.715 12.291 9.187 1.00 71.38 C HETATM 3307 O1 OLA A1214 -40.846 12.807 8.936 1.00 71.87 O HETATM 3308 O2 OLA A1214 -38.705 13.014 9.135 1.00 72.86 O HETATM 3309 C2 OLA A1214 -39.567 10.829 9.549 1.00 69.58 C HETATM 3310 C3 OLA A1214 -40.822 10.045 9.168 1.00 68.40 C HETATM 3311 C4 OLA A1214 -40.537 8.978 8.128 1.00 66.70 C HETATM 3312 C5 OLA A1214 -41.734 8.114 7.815 1.00 66.64 C HETATM 3313 C6 OLA A1214 -41.520 6.642 8.125 1.00 65.93 C HETATM 3314 C7 OLA A1214 -42.204 5.770 7.080 1.00 67.05 C HETATM 3315 C8 OLA A1214 -41.963 4.285 7.256 1.00 69.18 C HETATM 3316 C9 OLA A1214 -43.294 3.620 7.565 1.00 70.61 C HETATM 3317 C10 OLA A1214 -43.467 2.500 8.303 1.00 69.85 C HETATM 3318 C11 OLA A1214 -42.342 1.721 8.944 1.00 67.08 C HETATM 3319 C12 OLA A1214 -42.621 0.206 8.888 1.00 65.92 C HETATM 3320 C13 OLA A1214 -43.066 -0.403 10.232 1.00 66.20 C HETATM 3321 C1 OLA A1215 -43.468 -23.910 13.519 1.00 66.16 C HETATM 3322 O1 OLA A1215 -44.259 -24.357 12.646 1.00 64.22 O HETATM 3323 O2 OLA A1215 -42.632 -24.706 14.005 1.00 64.96 O HETATM 3324 C2 OLA A1215 -43.524 -22.457 13.969 1.00 67.32 C HETATM 3325 C3 OLA A1215 -42.314 -22.123 14.847 1.00 69.38 C HETATM 3326 C4 OLA A1215 -42.096 -20.649 15.181 1.00 72.67 C HETATM 3327 C5 OLA A1215 -40.781 -20.395 15.909 1.00 74.35 C HETATM 3328 C6 OLA A1215 -40.152 -19.008 15.740 1.00 73.62 C HETATM 3329 C7 OLA A1215 -38.676 -19.036 15.319 1.00 70.34 C HETATM 3330 C8 OLA A1215 -38.342 -18.093 14.171 1.00 68.89 C HETATM 3331 C9 OLA A1215 -37.077 -17.306 14.477 1.00 68.88 C HETATM 3332 C10 OLA A1215 -36.858 -15.968 14.367 1.00 66.11 C HETATM 3333 C11 OLA A1215 -37.854 -14.925 13.913 1.00 62.93 C HETATM 3334 C12 OLA A1215 -37.685 -13.616 14.713 1.00 63.15 C HETATM 3335 C13 OLA A1215 -38.036 -12.340 13.918 1.00 66.08 C HETATM 3336 C14 OLA A1215 -38.350 -11.132 14.824 1.00 67.97 C HETATM 3337 C15 OLA A1215 -38.393 -9.748 14.133 1.00 67.70 C HETATM 3338 C16 OLA A1215 -38.787 -9.779 12.642 1.00 64.97 C HETATM 3339 C17 OLA A1215 -38.648 -8.416 11.947 1.00 62.07 C HETATM 3340 C1 OLA A1216 -36.571 15.052 12.631 1.00 58.63 C HETATM 3341 O1 OLA A1216 -36.001 16.175 12.471 1.00 58.86 O HETATM 3342 O2 OLA A1216 -37.504 14.967 13.447 1.00 59.13 O HETATM 3343 C2 OLA A1216 -36.172 13.809 11.863 1.00 55.12 C HETATM 3344 C3 OLA A1216 -36.863 12.592 12.470 1.00 48.51 C HETATM 3345 C4 OLA A1216 -36.058 11.323 12.258 1.00 43.41 C HETATM 3346 C5 OLA A1216 -36.888 10.162 11.768 1.00 42.89 C HETATM 3347 C6 OLA A1216 -36.504 8.807 12.345 1.00 45.63 C HETATM 3348 C7 OLA A1216 -36.103 7.824 11.250 1.00 45.74 C HETATM 3349 C8 OLA A1216 -36.659 6.421 11.387 1.00 45.38 C HETATM 3350 C9 OLA A1216 -35.932 5.527 10.390 1.00 48.60 C HETATM 3351 C10 OLA A1216 -36.408 4.400 9.802 1.00 52.63 C HETATM 3352 C11 OLA A1216 -37.788 3.812 10.047 1.00 53.66 C HETATM 3353 C12 OLA A1216 -37.749 2.279 10.201 1.00 55.66 C HETATM 3354 C13 OLA A1216 -38.718 1.735 11.282 1.00 58.73 C HETATM 3355 C14 OLA A1216 -39.301 0.335 10.986 1.00 59.08 C HETATM 3356 C15 OLA A1216 -39.180 -0.658 12.165 1.00 57.77 C HETATM 3357 C16 OLA A1216 -38.796 -2.098 11.773 1.00 55.25 C HETATM 3358 C17 OLA A1216 -39.972 -3.090 11.781 1.00 54.32 C HETATM 3359 C18 OLA A1216 -39.592 -4.491 11.260 1.00 54.27 C HETATM 3360 C1 OLA A1217 -9.767 -14.176 17.274 1.00 59.01 C HETATM 3361 O1 OLA A1217 -9.034 -14.898 16.569 1.00 59.88 O HETATM 3362 O2 OLA A1217 -10.464 -14.725 18.161 1.00 62.39 O HETATM 3363 C2 OLA A1217 -9.830 -12.679 17.092 1.00 53.95 C HETATM 3364 C3 OLA A1217 -9.978 -11.949 18.424 1.00 48.45 C HETATM 3365 C4 OLA A1217 -9.850 -10.447 18.230 1.00 48.00 C HETATM 3366 C5 OLA A1217 -8.679 -9.802 18.949 1.00 49.88 C HETATM 3367 C6 OLA A1217 -8.294 -8.413 18.446 1.00 52.65 C HETATM 3368 C7 OLA A1217 -8.086 -7.405 19.582 1.00 53.29 C HETATM 3369 C10 OLC A1218 -6.059 -4.231 27.704 1.00 63.69 C HETATM 3370 C9 OLC A1218 -6.442 -2.967 27.667 1.00 65.33 C HETATM 3371 C8 OLC A1218 -6.207 -2.070 28.853 1.00 69.04 C HETATM 3372 C24 OLC A1218 -4.844 10.082 29.008 1.00 69.99 C HETATM 3373 C7 OLC A1218 -5.191 -1.003 28.450 1.00 69.86 C HETATM 3374 C6 OLC A1218 -4.562 -0.260 29.626 1.00 66.37 C HETATM 3375 C5 OLC A1218 -4.435 1.192 29.210 1.00 61.61 C HETATM 3376 C4 OLC A1218 -4.277 2.179 30.344 1.00 59.20 C HETATM 3377 C3 OLC A1218 -4.262 3.584 29.768 1.00 59.32 C HETATM 3378 C2 OLC A1218 -3.772 4.640 30.732 1.00 59.66 C HETATM 3379 C21 OLC A1218 -4.249 8.250 30.520 1.00 67.57 C HETATM 3380 C1 OLC A1218 -3.725 5.961 30.029 1.00 64.78 C HETATM 3381 C22 OLC A1218 -3.688 9.371 29.693 1.00 68.73 C HETATM 3382 O19 OLC A1218 -4.048 6.057 28.889 1.00 70.18 O HETATM 3383 O25 OLC A1218 -4.999 11.465 29.343 1.00 69.67 O HETATM 3384 O23 OLC A1218 -3.037 10.249 30.587 1.00 70.75 O HETATM 3385 O20 OLC A1218 -3.335 7.192 30.640 1.00 66.70 O HETATM 3386 C10 OLC A1219 -36.795 6.049 5.682 1.00 66.06 C HETATM 3387 C9 OLC A1219 -36.928 7.314 6.026 1.00 64.29 C HETATM 3388 C11 OLC A1219 -37.851 5.371 4.846 1.00 67.96 C HETATM 3389 C8 OLC A1219 -35.882 7.978 6.863 1.00 64.30 C HETATM 3390 C24 OLC A1219 -28.921 18.381 8.726 1.00 88.87 C HETATM 3391 C7 OLC A1219 -36.302 9.413 7.052 1.00 65.89 C HETATM 3392 C6 OLC A1219 -35.215 10.208 7.730 1.00 68.01 C HETATM 3393 C5 OLC A1219 -35.540 11.682 7.648 1.00 71.52 C HETATM 3394 C4 OLC A1219 -34.407 12.507 8.218 1.00 73.37 C HETATM 3395 C3 OLC A1219 -34.397 13.894 7.608 1.00 75.57 C HETATM 3396 C2 OLC A1219 -32.968 14.264 7.226 1.00 77.96 C HETATM 3397 C21 OLC A1219 -30.414 16.440 9.120 1.00 88.38 C HETATM 3398 C1 OLC A1219 -32.457 15.394 8.084 1.00 83.07 C HETATM 3399 C22 OLC A1219 -29.092 16.885 8.512 1.00 88.02 C HETATM 3400 O19 OLC A1219 -33.205 16.161 8.667 1.00 83.37 O HETATM 3401 O25 OLC A1219 -28.295 18.664 9.976 1.00 89.33 O HETATM 3402 O23 OLC A1219 -28.008 16.184 9.124 1.00 85.68 O HETATM 3403 O20 OLC A1219 -31.030 15.551 8.205 1.00 87.12 O HETATM 3404 C10 OLC A1220 -42.072 4.103 12.732 1.00 44.94 C HETATM 3405 C9 OLC A1220 -41.365 5.177 12.483 1.00 45.53 C HETATM 3406 C11 OLC A1220 -43.036 3.995 13.858 1.00 41.95 C HETATM 3407 C8 OLC A1220 -41.465 6.389 13.326 1.00 45.02 C HETATM 3408 C24 OLC A1220 -41.403 19.648 14.401 1.00 86.32 C HETATM 3409 C12 OLC A1220 -43.821 2.732 13.618 1.00 42.86 C HETATM 3410 C7 OLC A1220 -40.905 7.531 12.533 1.00 44.00 C HETATM 3411 C15 OLC A1220 -43.761 -0.931 14.426 1.00 49.76 C HETATM 3412 C13 OLC A1220 -43.209 1.513 14.261 1.00 44.85 C HETATM 3413 C6 OLC A1220 -40.644 8.729 13.414 1.00 43.63 C HETATM 3414 C14 OLC A1220 -43.580 0.261 13.499 1.00 47.59 C HETATM 3415 C5 OLC A1220 -41.622 9.847 13.111 1.00 44.16 C HETATM 3416 C4 OLC A1220 -40.982 11.128 13.558 1.00 47.62 C HETATM 3417 C3 OLC A1220 -41.731 12.363 13.157 1.00 50.75 C HETATM 3418 C2 OLC A1220 -41.066 13.475 13.915 1.00 55.20 C HETATM 3419 C21 OLC A1220 -41.666 17.259 13.802 1.00 78.01 C HETATM 3420 C1 OLC A1220 -41.679 14.779 13.526 1.00 64.26 C HETATM 3421 C22 OLC A1220 -40.837 18.255 14.590 1.00 82.82 C HETATM 3422 O19 OLC A1220 -42.601 14.822 12.750 1.00 64.20 O HETATM 3423 O25 OLC A1220 -42.817 19.552 14.421 1.00 89.09 O HETATM 3424 O23 OLC A1220 -40.919 17.903 15.959 1.00 82.83 O HETATM 3425 O20 OLC A1220 -41.145 15.985 14.108 1.00 71.51 O HETATM 3426 C18 OLC A1221 -33.392 -17.373 27.035 1.00 52.07 C HETATM 3427 C10 OLC A1221 -33.714 -8.177 29.576 1.00 54.81 C HETATM 3428 C9 OLC A1221 -33.520 -7.407 30.642 1.00 55.26 C HETATM 3429 C17 OLC A1221 -33.956 -15.980 27.128 1.00 51.69 C HETATM 3430 C11 OLC A1221 -33.403 -9.644 29.726 1.00 53.40 C HETATM 3431 C8 OLC A1221 -33.804 -5.932 30.619 1.00 52.49 C HETATM 3432 C16 OLC A1221 -32.887 -14.908 27.077 1.00 48.57 C HETATM 3433 C12 OLC A1221 -33.547 -10.379 28.417 1.00 54.18 C HETATM 3434 C7 OLC A1221 -33.729 -5.346 32.014 1.00 48.52 C HETATM 3435 C15 OLC A1221 -33.513 -13.527 27.098 1.00 48.68 C HETATM 3436 C13 OLC A1221 -34.327 -11.672 28.579 1.00 54.99 C HETATM 3437 C6 OLC A1221 -32.288 -5.274 32.478 1.00 49.11 C HETATM 3438 C14 OLC A1221 -33.465 -12.908 28.480 1.00 51.75 C HETATM 3439 C5 OLC A1221 -32.027 -3.900 33.074 1.00 52.85 C HETATM 3440 C4 OLC A1221 -30.649 -3.728 33.680 1.00 54.96 C HETATM 3441 C3 OLC A1221 -30.123 -2.333 33.349 1.00 57.91 C HETATM 3442 C2 OLC A1221 -31.259 -1.318 33.371 1.00 59.94 C HETATM 3443 C1 OLC A1221 -30.716 0.078 33.387 1.00 59.85 C HETATM 3444 O19 OLC A1221 -29.546 0.231 33.597 1.00 63.69 O HETATM 3445 O20 OLC A1221 -31.571 1.227 33.156 1.00 57.00 O HETATM 3446 C18 OLC A1222 -41.975 -5.154 14.771 1.00 59.98 C HETATM 3447 C10 OLC A1222 -38.484 3.083 14.811 1.00 36.02 C HETATM 3448 C9 OLC A1222 -37.867 4.239 14.823 1.00 34.77 C HETATM 3449 C17 OLC A1222 -41.693 -3.791 15.356 1.00 58.46 C HETATM 3450 C11 OLC A1222 -38.646 2.210 16.010 1.00 37.44 C HETATM 3451 C8 OLC A1222 -37.221 4.813 16.032 1.00 37.04 C HETATM 3452 C24 OLC A1222 -40.325 16.828 17.377 1.00 74.44 C HETATM 3453 C16 OLC A1222 -40.600 -3.803 16.409 1.00 56.17 C HETATM 3454 C12 OLC A1222 -39.303 0.936 15.529 1.00 40.16 C HETATM 3455 C7 OLC A1222 -37.286 6.301 15.826 1.00 41.20 C HETATM 3456 C15 OLC A1222 -40.429 -2.434 17.053 1.00 55.05 C HETATM 3457 C13 OLC A1222 -39.539 -0.082 16.629 1.00 46.57 C HETATM 3458 C6 OLC A1222 -36.907 7.071 17.059 1.00 43.21 C HETATM 3459 C14 OLC A1222 -40.113 -1.359 16.031 1.00 52.24 C HETATM 3460 C5 OLC A1222 -37.875 8.191 17.336 1.00 41.52 C HETATM 3461 C4 OLC A1222 -37.795 9.347 16.379 1.00 42.44 C HETATM 3462 C3 OLC A1222 -38.011 10.613 17.164 1.00 43.50 C HETATM 3463 C2 OLC A1222 -38.504 11.817 16.374 1.00 47.28 C HETATM 3464 C21 OLC A1222 -39.049 15.005 18.190 1.00 59.36 C HETATM 3465 C1 OLC A1222 -39.121 12.787 17.349 1.00 48.68 C HETATM 3466 C22 OLC A1222 -38.908 16.390 17.667 1.00 69.75 C HETATM 3467 O19 OLC A1222 -39.435 12.418 18.437 1.00 48.91 O HETATM 3468 O25 OLC A1222 -41.005 16.922 18.634 1.00 76.77 O HETATM 3469 O23 OLC A1222 -38.349 17.211 18.685 1.00 74.20 O HETATM 3470 O20 OLC A1222 -39.325 14.174 17.092 1.00 52.35 O HETATM 3471 C10 OLC A1223 -33.832 -8.463 24.857 1.00 49.72 C HETATM 3472 C9 OLC A1223 -33.441 -9.723 24.768 1.00 45.35 C HETATM 3473 C17 OLC A1223 -36.604 -0.870 24.245 1.00 59.94 C HETATM 3474 C11 OLC A1223 -34.634 -7.777 23.797 1.00 54.72 C HETATM 3475 C8 OLC A1223 -33.732 -10.635 23.610 1.00 41.54 C HETATM 3476 C24 OLC A1223 -32.044 -23.612 24.869 1.00 69.47 C HETATM 3477 C16 OLC A1223 -35.678 -1.935 23.682 1.00 62.57 C HETATM 3478 C12 OLC A1223 -35.055 -6.380 24.244 1.00 57.50 C HETATM 3479 C7 OLC A1223 -32.887 -11.871 23.812 1.00 40.49 C HETATM 3480 C15 OLC A1223 -36.158 -3.337 24.049 1.00 63.50 C HETATM 3481 C13 OLC A1223 -36.122 -5.778 23.337 1.00 58.51 C HETATM 3482 C6 OLC A1223 -33.271 -13.028 22.916 1.00 41.75 C HETATM 3483 C14 OLC A1223 -35.782 -4.344 22.967 1.00 60.76 C HETATM 3484 C5 OLC A1223 -32.315 -14.172 23.155 1.00 42.94 C HETATM 3485 C4 OLC A1223 -32.727 -15.436 22.435 1.00 45.61 C HETATM 3486 C3 OLC A1223 -31.773 -16.602 22.677 1.00 47.43 C HETATM 3487 C2 OLC A1223 -32.560 -17.864 22.403 1.00 56.43 C HETATM 3488 C21 OLC A1223 -31.903 -21.305 23.965 1.00 65.58 C HETATM 3489 C1 OLC A1223 -31.844 -19.128 22.742 1.00 63.75 C HETATM 3490 C22 OLC A1223 -32.791 -22.533 24.108 1.00 66.83 C HETATM 3491 O19 OLC A1223 -30.660 -19.201 22.609 1.00 67.48 O HETATM 3492 O25 OLC A1223 -32.954 -24.569 25.411 1.00 70.45 O HETATM 3493 O23 OLC A1223 -33.994 -22.227 24.795 1.00 66.59 O HETATM 3494 O20 OLC A1223 -32.564 -20.283 23.241 1.00 65.84 O HETATM 3495 C10 OLC A1224 -35.583 -10.033 19.052 1.00 59.02 C HETATM 3496 C9 OLC A1224 -35.127 -10.999 18.260 1.00 55.51 C HETATM 3497 C11 OLC A1224 -36.885 -10.217 19.795 1.00 59.88 C HETATM 3498 C8 OLC A1224 -35.911 -12.280 18.103 1.00 51.44 C HETATM 3499 C24 OLC A1224 -35.223 -25.049 20.588 1.00 72.91 C HETATM 3500 C7 OLC A1224 -34.951 -13.463 18.076 1.00 48.88 C HETATM 3501 C6 OLC A1224 -35.563 -14.680 18.758 1.00 45.92 C HETATM 3502 C5 OLC A1224 -34.779 -15.944 18.428 1.00 46.60 C HETATM 3503 C4 OLC A1224 -35.557 -17.191 18.832 1.00 49.52 C HETATM 3504 C3 OLC A1224 -35.209 -18.368 17.928 1.00 48.75 C HETATM 3505 C2 OLC A1224 -35.584 -19.691 18.586 1.00 52.86 C HETATM 3506 C21 OLC A1224 -35.017 -22.957 19.255 1.00 67.34 C HETATM 3507 C1 OLC A1224 -34.649 -20.775 18.105 1.00 58.12 C HETATM 3508 C22 OLC A1224 -34.277 -23.931 20.166 1.00 71.88 C HETATM 3509 O19 OLC A1224 -34.260 -20.794 16.949 1.00 60.08 O HETATM 3510 O25 OLC A1224 -34.575 -25.880 21.558 1.00 73.57 O HETATM 3511 O23 OLC A1224 -33.162 -24.489 19.462 1.00 74.65 O HETATM 3512 O20 OLC A1224 -34.200 -21.812 19.021 1.00 61.18 O HETATM 3513 C10 OLC A1225 -3.204 1.109 25.446 1.00 51.70 C HETATM 3514 C9 OLC A1225 -2.766 2.347 25.248 1.00 46.79 C HETATM 3515 C11 OLC A1225 -4.655 0.726 25.494 1.00 54.04 C HETATM 3516 C8 OLC A1225 -3.591 3.588 25.053 1.00 39.96 C HETATM 3517 C24 OLC A1225 -0.651 17.076 25.287 1.00 53.13 C HETATM 3518 C12 OLC A1225 -4.891 -0.613 24.811 1.00 50.35 C HETATM 3519 C7 OLC A1225 -2.887 4.790 25.667 1.00 33.56 C HETATM 3520 C6 OLC A1225 -3.111 6.124 24.980 1.00 28.12 C HETATM 3521 C5 OLC A1225 -2.532 7.259 25.799 1.00 26.71 C HETATM 3522 C4 OLC A1225 -2.548 8.574 25.056 1.00 26.97 C HETATM 3523 C3 OLC A1225 -2.039 9.725 25.895 1.00 29.50 C HETATM 3524 C2 OLC A1225 -2.110 11.010 25.102 1.00 37.34 C HETATM 3525 C21 OLC A1225 -1.131 14.673 25.710 1.00 49.67 C HETATM 3526 C1 OLC A1225 -1.569 12.242 25.777 1.00 45.55 C HETATM 3527 C22 OLC A1225 -1.281 15.818 24.716 1.00 53.67 C HETATM 3528 O19 OLC A1225 -0.918 12.200 26.777 1.00 49.07 O HETATM 3529 O25 OLC A1225 0.756 16.939 25.372 1.00 51.34 O HETATM 3530 O23 OLC A1225 -0.669 15.483 23.463 1.00 56.88 O HETATM 3531 O20 OLC A1225 -1.816 13.540 25.224 1.00 45.60 O HETATM 3532 C10 OLC A1226 -29.145 -3.548 37.852 1.00 54.78 C HETATM 3533 C9 OLC A1226 -30.072 -2.591 37.744 1.00 55.40 C HETATM 3534 C11 OLC A1226 -28.824 -4.434 36.672 1.00 47.12 C HETATM 3535 C8 OLC A1226 -30.497 -1.633 38.833 1.00 50.74 C HETATM 3536 C24 OLC A1226 -29.184 9.481 36.011 1.00 56.64 C HETATM 3537 C12 OLC A1226 -28.223 -5.771 37.051 1.00 41.58 C HETATM 3538 C7 OLC A1226 -30.335 -0.242 38.253 1.00 48.39 C HETATM 3539 C13 OLC A1226 -26.736 -5.740 37.296 1.00 39.82 C HETATM 3540 C6 OLC A1226 -31.191 0.799 38.925 1.00 45.62 C HETATM 3541 C5 OLC A1226 -31.993 1.662 37.966 1.00 47.84 C HETATM 3542 C4 OLC A1226 -31.375 3.011 37.687 1.00 46.56 C HETATM 3543 C3 OLC A1226 -32.388 4.096 37.359 1.00 45.52 C HETATM 3544 C2 OLC A1226 -31.703 5.137 36.492 1.00 49.88 C HETATM 3545 C21 OLC A1226 -31.594 8.952 36.575 1.00 55.46 C HETATM 3546 C1 OLC A1226 -32.146 6.546 36.729 1.00 54.15 C HETATM 3547 C22 OLC A1226 -30.393 9.828 36.879 1.00 59.03 C HETATM 3548 O19 OLC A1226 -33.294 6.837 36.872 1.00 57.00 O HETATM 3549 O25 OLC A1226 -28.955 10.437 34.977 1.00 55.61 O HETATM 3550 O23 OLC A1226 -30.772 11.189 36.738 1.00 64.67 O HETATM 3551 O20 OLC A1226 -31.192 7.618 36.805 1.00 55.97 O HETATM 3552 C1 OLA A1227 -33.788 9.469 2.093 0.67 68.31 C HETATM 3553 O1 OLA A1227 -34.429 10.419 2.631 0.67 68.75 O HETATM 3554 O2 OLA A1227 -32.552 9.452 2.241 0.67 68.52 O HETATM 3555 C2 OLA A1227 -34.487 8.389 1.283 0.67 67.38 C HETATM 3556 C3 OLA A1227 -34.123 6.964 1.718 0.67 66.26 C HETATM 3557 C4 OLA A1227 -34.894 5.891 0.956 0.67 65.19 C HETATM 3558 C5 OLA A1227 -34.025 4.767 0.429 0.67 65.24 C HETATM 3559 C6 OLA A1227 -34.576 3.357 0.617 0.67 65.62 C HETATM 3560 C7 OLA A1227 -33.527 2.295 0.289 0.67 65.90 C HETATM 3561 C8 OLA A1227 -33.744 0.918 0.896 0.67 65.69 C HETATM 3562 C9 OLA A1227 -32.697 -0.020 0.314 0.67 65.40 C HETATM 3563 C10 OLA A1227 -32.826 -1.343 0.070 0.67 65.64 C HETATM 3564 C11 OLA A1227 -34.073 -2.162 0.338 0.67 65.94 C HETATM 3565 C12 OLA A1227 -34.303 -3.217 -0.764 0.67 65.61 C HETATM 3566 C13 OLA A1227 -35.025 -4.494 -0.287 0.67 65.17 C HETATM 3567 C14 OLA A1227 -34.572 -5.754 -1.040 0.67 65.18 C HETATM 3568 C15 OLA A1227 -35.019 -7.070 -0.379 0.67 65.98 C HETATM 3569 C16 OLA A1227 -34.204 -8.286 -0.854 0.67 67.30 C HETATM 3570 C17 OLA A1227 -34.044 -8.363 -2.382 0.67 67.88 C HETATM 3571 C18 OLA A1227 -33.917 -9.810 -2.887 0.67 68.74 C HETATM 3572 C1 OLA A1228 -34.407 11.209 33.777 1.00 60.37 C HETATM 3573 O1 OLA A1228 -34.913 12.308 33.454 1.00 64.48 O HETATM 3574 O2 OLA A1228 -33.351 11.236 34.468 1.00 64.79 O HETATM 3575 C2 OLA A1228 -35.029 9.891 33.355 1.00 51.26 C HETATM 3576 C3 OLA A1228 -33.997 8.761 33.325 1.00 47.76 C HETATM 3577 C4 OLA A1228 -34.605 7.424 32.937 1.00 46.70 C HETATM 3578 C5 OLA A1228 -33.668 6.248 33.070 1.00 46.10 C HETATM 3579 C6 OLA A1228 -34.215 4.915 32.575 1.00 47.63 C HETATM 3580 C7 OLA A1228 -33.162 3.801 32.668 1.00 50.56 C HETATM 3581 C24 OLC A1229 -8.853 -16.849 11.432 1.00 67.99 C HETATM 3582 C6 OLC A1229 -8.015 -8.267 14.590 1.00 61.47 C HETATM 3583 C5 OLC A1229 -8.850 -9.219 13.741 1.00 59.62 C HETATM 3584 C4 OLC A1229 -8.289 -9.324 12.328 1.00 60.48 C HETATM 3585 C3 OLC A1229 -9.170 -10.210 11.455 1.00 61.73 C HETATM 3586 C2 OLC A1229 -9.421 -11.558 12.123 1.00 66.81 C HETATM 3587 C21 OLC A1229 -10.326 -14.887 11.853 1.00 71.96 C HETATM 3588 C1 OLC A1229 -9.839 -12.566 11.080 1.00 70.72 C HETATM 3589 C22 OLC A1229 -9.506 -15.991 12.510 1.00 70.35 C HETATM 3590 O19 OLC A1229 -10.506 -12.225 10.116 1.00 69.92 O HETATM 3591 O25 OLC A1229 -8.703 -18.189 11.915 1.00 67.42 O HETATM 3592 O23 OLC A1229 -8.492 -15.406 13.334 1.00 73.02 O HETATM 3593 O20 OLC A1229 -9.450 -13.960 11.214 1.00 72.96 O HETATM 3594 O HOH A1301 -34.191 17.543 10.090 1.00 59.70 O HETATM 3595 O HOH A1302 -11.122 -13.154 8.076 1.00 51.03 O HETATM 3596 O HOH A1303 1.673 -47.083 20.852 1.00 60.49 O HETATM 3597 O HOH A1304 -22.768 -27.997 21.886 1.00 48.51 O HETATM 3598 O HOH A1305 -27.838 3.369 19.631 1.00 26.58 O HETATM 3599 O HOH A1306 -20.662 16.659 18.965 1.00 64.63 O HETATM 3600 O HOH A1307 -38.266 21.063 20.380 1.00 59.55 O HETATM 3601 O HOH A1308 -4.225 -63.970 26.774 1.00 51.62 O HETATM 3602 O HOH A1309 -7.807 10.507 30.788 1.00 39.56 O HETATM 3603 O HOH A1310 -16.813 -25.045 9.867 1.00 46.47 O HETATM 3604 O HOH A1311 -21.901 -6.623 15.480 1.00 27.07 O HETATM 3605 O HOH A1312 -16.447 -29.171 11.529 1.00 44.97 O HETATM 3606 O HOH A1313 -18.794 10.261 23.176 1.00 24.26 O HETATM 3607 O HOH A1314 -18.687 -11.363 13.249 1.00 27.93 O HETATM 3608 O HOH A1315 4.079 -47.835 26.272 1.00 57.38 O HETATM 3609 O HOH A1316 -13.180 17.696 11.329 1.00 49.12 O HETATM 3610 O HOH A1317 -36.469 -31.267 17.712 1.00 54.77 O HETATM 3611 O HOH A1318 0.288 13.688 28.559 1.00 46.59 O HETATM 3612 O HOH A1319 -16.263 -16.842 19.187 1.00 23.85 O HETATM 3613 O HOH A1320 -26.183 18.556 21.868 1.00 27.82 O HETATM 3614 O HOH A1321 -15.237 9.956 17.935 1.00 22.70 O HETATM 3615 O HOH A1322 -19.387 -35.625 26.966 1.00 52.43 O HETATM 3616 O HOH A1323 -14.611 -27.048 17.503 1.00 38.34 O HETATM 3617 O HOH A1324 -11.339 15.406 23.173 1.00 32.84 O HETATM 3618 O HOH A1325 -21.726 12.585 17.594 1.00 23.07 O HETATM 3619 O HOH A1326 -23.730 15.560 33.211 1.00 38.79 O HETATM 3620 O HOH A1327 -25.935 -12.080 21.728 1.00 22.90 O HETATM 3621 O HOH A1328 -25.308 -13.282 13.776 1.00 22.79 O HETATM 3622 O HOH A1329 8.454 -67.203 14.794 1.00 43.17 O HETATM 3623 O HOH A1330 -25.018 -15.793 14.826 1.00 29.19 O HETATM 3624 O HOH A1331 -12.595 -35.823 28.603 1.00 52.99 O HETATM 3625 O HOH A1332 -16.157 0.786 12.693 1.00 15.56 O HETATM 3626 O HOH A1333 -23.280 -4.744 14.259 1.00 22.93 O HETATM 3627 O HOH A1334 -0.803 -63.056 19.775 1.00 41.80 O HETATM 3628 O HOH A1335 -25.791 8.480 12.856 1.00 17.53 O HETATM 3629 O HOH A1336 -26.017 -11.638 25.839 1.00 31.32 O HETATM 3630 O HOH A1337 -5.597 -61.564 28.163 1.00 54.32 O HETATM 3631 O HOH A1338 -11.369 12.157 15.861 1.00 22.06 O HETATM 3632 O HOH A1339 0.360 -67.625 25.217 1.00 35.69 O HETATM 3633 O HOH A1340 -5.444 -31.559 24.771 1.00 46.74 O HETATM 3634 O HOH A1341 3.706 -73.484 23.632 1.00 48.07 O HETATM 3635 O HOH A1342 -15.058 3.794 21.974 1.00 14.96 O HETATM 3636 O HOH A1343 -34.134 14.094 29.930 1.00 30.79 O HETATM 3637 O HOH A1344 -4.361 -25.967 25.265 1.00 40.07 O HETATM 3638 O HOH A1345 -29.548 12.890 8.680 1.00 45.01 O HETATM 3639 O HOH A1346 -2.190 13.474 22.017 1.00 30.98 O HETATM 3640 O HOH A1347 -21.093 -27.476 18.165 1.00 52.48 O HETATM 3641 O HOH A1348 -23.796 -11.158 11.639 1.00 27.25 O HETATM 3642 O HOH A1349 -21.526 -33.095 22.376 1.00 53.81 O HETATM 3643 O HOH A1350 -25.762 -14.377 24.880 1.00 32.25 O HETATM 3644 O HOH A1351 -20.404 -35.999 29.794 1.00 55.19 O HETATM 3645 O HOH A1352 -20.655 -2.435 24.472 1.00 21.49 O HETATM 3646 O HOH A1353 -20.509 -11.469 15.312 1.00 43.90 O HETATM 3647 O HOH A1354 -9.851 15.450 18.786 1.00 34.47 O HETATM 3648 O HOH A1355 -17.914 13.011 23.768 1.00 32.45 O HETATM 3649 O HOH A1356 -29.904 18.246 29.673 1.00 43.40 O HETATM 3650 O HOH A1357 -13.924 -28.046 19.909 1.00 39.81 O HETATM 3651 O HOH A1358 7.350 -61.025 15.306 1.00 48.38 O HETATM 3652 O HOH A1359 -27.958 -28.613 33.909 1.00 61.33 O HETATM 3653 O HOH A1360 -25.004 -6.659 17.789 1.00 50.04 O HETATM 3654 O HOH A1361 -19.260 12.352 16.268 1.00 40.67 O HETATM 3655 O HOH A1362 -25.594 16.844 26.570 1.00 34.31 O HETATM 3656 O HOH A1363 -24.172 16.746 1.991 1.00 44.86 O HETATM 3657 O HOH A1364 -17.547 13.950 29.553 1.00 34.08 O HETATM 3658 O HOH A1365 -17.981 -17.378 17.030 1.00 29.30 O HETATM 3659 O HOH A1366 9.336 -70.841 20.619 1.00 34.99 O HETATM 3660 O HOH A1367 -27.176 3.221 16.976 1.00 20.60 O HETATM 3661 O HOH A1368 -25.674 18.870 24.645 1.00 22.92 O HETATM 3662 O HOH A1369 -27.316 -11.625 6.927 1.00 36.14 O HETATM 3663 O HOH A1370 -24.474 2.843 16.126 1.00 19.41 O HETATM 3664 O HOH A1371 -27.597 20.836 22.188 1.00 25.18 O HETATM 3665 O HOH A1372 -19.400 -1.450 22.235 1.00 20.08 O HETATM 3666 O HOH A1373 15.865 -66.294 24.995 1.00 62.30 O HETATM 3667 O HOH A1374 -10.168 15.145 25.296 1.00 34.47 O HETATM 3668 O HOH A1375 5.674 -76.335 26.644 1.00 33.01 O HETATM 3669 O HOH A1376 -4.321 -64.319 17.774 1.00 41.26 O HETATM 3670 O HOH A1377 -17.314 13.553 26.369 1.00 29.34 O HETATM 3671 O HOH A1378 -22.334 -10.237 15.263 1.00 40.51 O HETATM 3672 O HOH A1379 -18.271 -2.578 20.195 1.00 19.85 O HETATM 3673 O HOH A1380 -24.600 23.843 30.164 1.00 45.57 O HETATM 3674 O HOH A1381 -16.326 17.069 8.504 1.00 37.34 O HETATM 3675 O HOH A1382 -32.387 23.757 25.709 1.00 49.76 O HETATM 3676 O HOH A1383 -18.747 7.437 18.446 1.00 22.49 O HETATM 3677 O HOH A1384 -17.999 16.222 19.371 1.00 51.40 O HETATM 3678 O HOH A1385 -27.281 19.216 14.078 1.00 64.33 O HETATM 3679 O HOH A1386 -31.137 20.719 28.061 1.00 48.10 O HETATM 3680 O HOH A1387 -15.121 12.483 28.619 1.00 25.32 O HETATM 3681 O HOH A1388 -23.076 -15.527 26.590 1.00 47.24 O HETATM 3682 O HOH A1389 -16.707 15.853 12.285 1.00 50.40 O HETATM 3683 O HOH A1390 -17.308 15.213 5.679 1.00 34.91 O HETATM 3684 O HOH A1391 -3.422 16.451 21.585 1.00 38.67 O HETATM 3685 O HOH A1392 -37.032 17.959 27.921 1.00 41.35 O HETATM 3686 O HOH A1393 18.059 -57.179 18.584 1.00 57.04 O HETATM 3687 O HOH A1394 -36.135 18.790 16.049 1.00 46.90 O HETATM 3688 O HOH A1395 -18.580 -23.489 14.183 1.00 55.50 O HETATM 3689 O HOH A1396 -9.212 13.529 16.605 1.00 30.75 O HETATM 3690 O HOH A1397 -25.641 -29.754 23.088 1.00 50.19 O HETATM 3691 O HOH A1398 -27.901 29.461 27.176 1.00 52.93 O HETATM 3692 O HOH A1399 -7.359 12.768 27.568 1.00 52.00 O HETATM 3693 O HOH A1400 -16.112 14.354 22.412 1.00 42.79 O HETATM 3694 O HOH A1401 -13.178 13.513 30.094 1.00 61.58 O HETATM 3695 O HOH A1402 8.452 -62.236 13.275 1.00 55.18 O HETATM 3696 O HOH A1403 -26.533 16.872 12.436 1.00 53.84 O HETATM 3697 O HOH A1404 -20.135 -18.512 15.885 1.00 39.71 O HETATM 3698 O HOH A1405 -25.936 20.704 11.567 1.00 58.51 O HETATM 3699 O HOH A1406 -16.744 -30.823 15.576 1.00 55.81 O HETATM 3700 O HOH A1407 -11.905 16.763 18.094 1.00 42.47 O HETATM 3701 O HOH A1408 -18.785 14.605 15.390 1.00 49.94 O HETATM 3702 O HOH A1409 6.265 -76.646 23.881 1.00 31.17 O HETATM 3703 O HOH A1410 -31.215 16.863 31.311 1.00 51.32 O HETATM 3704 O HOH A1411 8.546 -75.617 27.393 1.00 42.83 O HETATM 3705 O HOH A1412 -21.315 15.140 16.788 1.00 34.37 O HETATM 3706 O HOH A1413 -24.242 16.831 11.755 1.00 55.21 O HETATM 3707 O HOH A1414 -20.249 -21.632 15.256 1.00 52.18 O HETATM 3708 O HOH A1415 -21.817 16.638 14.951 1.00 43.01 O CONECT 423 3102 CONECT 559 1229 CONECT 575 1132 CONECT 595 1273 CONECT 700 3102 CONECT 1132 575 CONECT 1229 559 CONECT 1273 595 CONECT 2673 2694 CONECT 2694 2673 CONECT 3078 3090 3091 3094 CONECT 3079 3081 3091 3092 CONECT 3080 3090 3092 3095 CONECT 3081 3079 3097 3100 CONECT 3082 3097 3098 3101 CONECT 3083 3093 3098 CONECT 3084 3085 CONECT 3085 3084 3086 3087 3088 CONECT 3086 3085 CONECT 3087 3085 CONECT 3088 3085 3089 CONECT 3089 3088 3096 3099 CONECT 3090 3078 3080 3096 CONECT 3091 3078 3079 CONECT 3092 3079 3080 CONECT 3093 3083 3101 CONECT 3094 3078 CONECT 3095 3080 CONECT 3096 3089 3090 CONECT 3097 3081 3082 CONECT 3098 3082 3083 CONECT 3099 3089 CONECT 3100 3081 CONECT 3101 3082 3093 CONECT 3102 423 700 3604 3653 CONECT 3102 3671 CONECT 3103 3104 3112 CONECT 3104 3103 3105 CONECT 3105 3104 3106 3130 CONECT 3106 3105 3107 CONECT 3107 3106 3108 3112 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3109 3111 3116 CONECT 3111 3110 3112 3113 CONECT 3112 3103 3107 3111 3121 CONECT 3113 3111 3114 CONECT 3114 3113 3115 CONECT 3115 3114 3116 3119 3120 CONECT 3116 3110 3115 3117 CONECT 3117 3116 3118 CONECT 3118 3117 3119 CONECT 3119 3115 3118 3122 CONECT 3120 3115 CONECT 3121 3112 CONECT 3122 3119 3123 3124 CONECT 3123 3122 CONECT 3124 3122 3125 CONECT 3125 3124 3126 CONECT 3126 3125 3127 CONECT 3127 3126 3128 3129 CONECT 3128 3127 CONECT 3129 3127 CONECT 3130 3105 CONECT 3131 3132 3140 CONECT 3132 3131 3133 CONECT 3133 3132 3134 3158 CONECT 3134 3133 3135 CONECT 3135 3134 3136 3140 CONECT 3136 3135 3137 CONECT 3137 3136 3138 CONECT 3138 3137 3139 3144 CONECT 3139 3138 3140 3141 CONECT 3140 3131 3135 3139 3149 CONECT 3141 3139 3142 CONECT 3142 3141 3143 CONECT 3143 3142 3144 3147 3148 CONECT 3144 3138 3143 3145 CONECT 3145 3144 3146 CONECT 3146 3145 3147 CONECT 3147 3143 3146 3150 CONECT 3148 3143 CONECT 3149 3140 CONECT 3150 3147 3151 3152 CONECT 3151 3150 CONECT 3152 3150 3153 CONECT 3153 3152 3154 CONECT 3154 3153 3155 CONECT 3155 3154 3156 3157 CONECT 3156 3155 CONECT 3157 3155 CONECT 3158 3133 CONECT 3159 3160 3168 CONECT 3160 3159 3161 CONECT 3161 3160 3162 3186 CONECT 3162 3161 3163 CONECT 3163 3162 3164 3168 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3165 3167 3172 CONECT 3167 3166 3168 3169 CONECT 3168 3159 3163 3167 3177 CONECT 3169 3167 3170 CONECT 3170 3169 3171 CONECT 3171 3170 3172 3175 3176 CONECT 3172 3166 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 CONECT 3175 3171 3174 3178 CONECT 3176 3171 CONECT 3177 3168 CONECT 3178 3175 3179 3180 CONECT 3179 3178 CONECT 3180 3178 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3184 3185 CONECT 3184 3183 CONECT 3185 3183 CONECT 3186 3161 CONECT 3187 3188 3196 CONECT 3188 3187 3189 CONECT 3189 3188 3190 3214 CONECT 3190 3189 3191 CONECT 3191 3190 3192 3196 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 3200 CONECT 3195 3194 3196 3197 CONECT 3196 3187 3191 3195 3205 CONECT 3197 3195 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 3203 3204 CONECT 3200 3194 3199 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 CONECT 3203 3199 3202 3206 CONECT 3204 3199 CONECT 3205 3196 CONECT 3206 3203 3207 3208 CONECT 3207 3206 CONECT 3208 3206 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 3213 CONECT 3212 3211 CONECT 3213 3211 CONECT 3214 3189 CONECT 3215 3216 3217 3218 CONECT 3216 3215 CONECT 3217 3215 CONECT 3218 3215 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 3225 CONECT 3225 3224 3226 CONECT 3226 3225 3227 CONECT 3227 3226 3228 CONECT 3228 3227 3229 CONECT 3229 3228 CONECT 3230 3231 3232 3233 CONECT 3231 3230 CONECT 3232 3230 CONECT 3233 3230 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 CONECT 3239 3240 3241 3242 CONECT 3240 3239 CONECT 3241 3239 CONECT 3242 3239 3243 CONECT 3243 3242 3244 CONECT 3244 3243 3245 CONECT 3245 3244 3246 CONECT 3246 3245 3247 CONECT 3247 3246 CONECT 3248 3249 3250 3251 CONECT 3249 3248 CONECT 3250 3248 CONECT 3251 3248 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3264 CONECT 3266 3267 3268 3269 CONECT 3267 3266 CONECT 3268 3266 CONECT 3269 3266 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 3276 CONECT 3276 3275 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 CONECT 3286 3287 3288 3289 CONECT 3287 3286 CONECT 3288 3286 CONECT 3289 3286 3290 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 CONECT 3298 3299 3300 3301 CONECT 3299 3298 CONECT 3300 3298 CONECT 3301 3298 3302 CONECT 3302 3301 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 CONECT 3306 3307 3308 3309 CONECT 3307 3306 CONECT 3308 3306 CONECT 3309 3306 3310 CONECT 3310 3309 3311 CONECT 3311 3310 3312 CONECT 3312 3311 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 CONECT 3321 3322 3323 3324 CONECT 3322 3321 CONECT 3323 3321 CONECT 3324 3321 3325 CONECT 3325 3324 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 3329 CONECT 3329 3328 3330 CONECT 3330 3329 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 CONECT 3340 3341 3342 3343 CONECT 3341 3340 CONECT 3342 3340 CONECT 3343 3340 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 CONECT 3355 3354 3356 CONECT 3356 3355 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 CONECT 3360 3361 3362 3363 CONECT 3361 3360 CONECT 3362 3360 CONECT 3363 3360 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 CONECT 3369 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3373 CONECT 3372 3381 3383 CONECT 3373 3371 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3380 CONECT 3379 3381 3385 CONECT 3380 3378 3382 3385 CONECT 3381 3372 3379 3384 CONECT 3382 3380 CONECT 3383 3372 CONECT 3384 3381 CONECT 3385 3379 3380 CONECT 3386 3387 3388 CONECT 3387 3386 3389 CONECT 3388 3386 CONECT 3389 3387 3391 CONECT 3390 3399 3401 CONECT 3391 3389 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3398 CONECT 3397 3399 3403 CONECT 3398 3396 3400 3403 CONECT 3399 3390 3397 3402 CONECT 3400 3398 CONECT 3401 3390 CONECT 3402 3399 CONECT 3403 3397 3398 CONECT 3404 3405 3406 CONECT 3405 3404 3407 CONECT 3406 3404 3409 CONECT 3407 3405 3410 CONECT 3408 3421 3423 CONECT 3409 3406 3412 CONECT 3410 3407 3413 CONECT 3411 3414 CONECT 3412 3409 3414 CONECT 3413 3410 3415 CONECT 3414 3411 3412 CONECT 3415 3413 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3420 CONECT 3419 3421 3425 CONECT 3420 3418 3422 3425 CONECT 3421 3408 3419 3424 CONECT 3422 3420 CONECT 3423 3408 CONECT 3424 3421 CONECT 3425 3419 3420 CONECT 3426 3429 CONECT 3427 3428 3430 CONECT 3428 3427 3431 CONECT 3429 3426 3432 CONECT 3430 3427 3433 CONECT 3431 3428 3434 CONECT 3432 3429 3435 CONECT 3433 3430 3436 CONECT 3434 3431 3437 CONECT 3435 3432 3438 CONECT 3436 3433 3438 CONECT 3437 3434 3439 CONECT 3438 3435 3436 CONECT 3439 3437 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 3445 CONECT 3444 3443 CONECT 3445 3443 CONECT 3446 3449 CONECT 3447 3448 3450 CONECT 3448 3447 3451 CONECT 3449 3446 3453 CONECT 3450 3447 3454 CONECT 3451 3448 3455 CONECT 3452 3466 3468 CONECT 3453 3449 3456 CONECT 3454 3450 3457 CONECT 3455 3451 3458 CONECT 3456 3453 3459 CONECT 3457 3454 3459 CONECT 3458 3455 3460 CONECT 3459 3456 3457 CONECT 3460 3458 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3465 CONECT 3464 3466 3470 CONECT 3465 3463 3467 3470 CONECT 3466 3452 3464 3469 CONECT 3467 3465 CONECT 3468 3452 CONECT 3469 3466 CONECT 3470 3464 3465 CONECT 3471 3472 3474 CONECT 3472 3471 3475 CONECT 3473 3477 CONECT 3474 3471 3478 CONECT 3475 3472 3479 CONECT 3476 3490 3492 CONECT 3477 3473 3480 CONECT 3478 3474 3481 CONECT 3479 3475 3482 CONECT 3480 3477 3483 CONECT 3481 3478 3483 CONECT 3482 3479 3484 CONECT 3483 3480 3481 CONECT 3484 3482 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3489 CONECT 3488 3490 3494 CONECT 3489 3487 3491 3494 CONECT 3490 3476 3488 3493 CONECT 3491 3489 CONECT 3492 3476 CONECT 3493 3490 CONECT 3494 3488 3489 CONECT 3495 3496 3497 CONECT 3496 3495 3498 CONECT 3497 3495 CONECT 3498 3496 3500 CONECT 3499 3508 3510 CONECT 3500 3498 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 CONECT 3504 3503 3505 CONECT 3505 3504 3507 CONECT 3506 3508 3512 CONECT 3507 3505 3509 3512 CONECT 3508 3499 3506 3511 CONECT 3509 3507 CONECT 3510 3499 CONECT 3511 3508 CONECT 3512 3506 3507 CONECT 3513 3514 3515 CONECT 3514 3513 3516 CONECT 3515 3513 3518 CONECT 3516 3514 3519 CONECT 3517 3527 3529 CONECT 3518 3515 CONECT 3519 3516 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3526 CONECT 3525 3527 3531 CONECT 3526 3524 3528 3531 CONECT 3527 3517 3525 3530 CONECT 3528 3526 CONECT 3529 3517 CONECT 3530 3527 CONECT 3531 3525 3526 CONECT 3532 3533 3534 CONECT 3533 3532 3535 CONECT 3534 3532 3537 CONECT 3535 3533 3538 CONECT 3536 3547 3549 CONECT 3537 3534 3539 CONECT 3538 3535 3540 CONECT 3539 3537 CONECT 3540 3538 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3546 CONECT 3545 3547 3551 CONECT 3546 3544 3548 3551 CONECT 3547 3536 3545 3550 CONECT 3548 3546 CONECT 3549 3536 CONECT 3550 3547 CONECT 3551 3545 3546 CONECT 3552 3553 3554 3555 CONECT 3553 3552 CONECT 3554 3552 CONECT 3555 3552 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 CONECT 3562 3561 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 3567 CONECT 3567 3566 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3571 CONECT 3571 3570 CONECT 3572 3573 3574 3575 CONECT 3573 3572 CONECT 3574 3572 CONECT 3575 3572 3576 CONECT 3576 3575 3577 CONECT 3577 3576 3578 CONECT 3578 3577 3579 CONECT 3579 3578 3580 CONECT 3580 3579 CONECT 3581 3589 3591 CONECT 3582 3583 CONECT 3583 3582 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3588 CONECT 3587 3589 3593 CONECT 3588 3586 3590 3593 CONECT 3589 3581 3587 3592 CONECT 3590 3588 CONECT 3591 3581 CONECT 3592 3589 CONECT 3593 3587 3588 CONECT 3604 3102 CONECT 3653 3102 CONECT 3671 3102 MASTER 508 0 29 19 2 0 44 6 3629 1 530 34 END