HEADER MEMBRANE PROTEIN 28-JUL-17 5OLZ TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-COMPOUND 4E COMPLEX AT 1.9A TITLE 2 OBTAINED FROM BESPOKE CO-CRYSTALLISATION 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 5OLZ 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. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.090 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 39432 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.196 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 3713 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 33.7113 - 5.6912 0.98 2622 112 0.1823 0.2164 REMARK 3 2 5.6912 - 4.5208 0.99 2664 125 0.1710 0.1785 REMARK 3 3 4.5208 - 3.9503 0.99 2625 129 0.1440 0.1651 REMARK 3 4 3.9503 - 3.5896 1.00 2644 134 0.1416 0.1765 REMARK 3 5 3.5896 - 3.3325 0.99 2648 133 0.1473 0.1485 REMARK 3 6 3.3325 - 3.1362 1.00 2701 118 0.1503 0.1787 REMARK 3 7 3.1362 - 2.9792 0.99 2628 111 0.1508 0.1795 REMARK 3 8 2.9792 - 2.8496 0.99 2604 170 0.1541 0.2039 REMARK 3 9 2.8496 - 2.7400 1.00 2648 171 0.1521 0.1734 REMARK 3 10 2.7400 - 2.6455 1.00 2586 145 0.1497 0.1791 REMARK 3 11 2.6455 - 2.5628 1.00 2709 123 0.1563 0.1712 REMARK 3 12 2.5628 - 2.4895 1.00 2639 128 0.1580 0.1761 REMARK 3 13 2.4895 - 2.4240 1.00 2596 189 0.1561 0.2142 REMARK 3 14 2.4240 - 2.3649 1.00 2690 116 0.1628 0.2013 REMARK 3 15 2.3649 - 2.3112 0.99 2600 138 0.1720 0.2078 REMARK 3 16 2.3112 - 2.2620 0.99 2656 127 0.1843 0.1847 REMARK 3 17 2.2620 - 2.2167 0.99 2635 140 0.1871 0.1889 REMARK 3 18 2.2167 - 2.1749 0.99 2548 158 0.1960 0.2027 REMARK 3 19 2.1749 - 2.1361 0.99 2687 116 0.2190 0.2183 REMARK 3 20 2.1361 - 2.0999 0.99 2613 166 0.2253 0.2252 REMARK 3 21 2.0999 - 2.0660 0.99 2593 133 0.2389 0.2784 REMARK 3 22 2.0660 - 2.0342 0.99 2631 169 0.2435 0.2660 REMARK 3 23 2.0342 - 2.0043 0.99 2641 129 0.2545 0.2817 REMARK 3 24 2.0043 - 1.9761 0.99 2621 157 0.2814 0.3002 REMARK 3 25 1.9761 - 1.9494 0.99 2641 129 0.2907 0.3132 REMARK 3 26 1.9494 - 1.9241 0.99 2687 135 0.3200 0.3393 REMARK 3 27 1.9241 - 1.9000 1.00 2669 112 0.3213 0.3279 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.140 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3758 REMARK 3 ANGLE : 0.989 5004 REMARK 3 CHIRALITY : 0.039 549 REMARK 3 PLANARITY : 0.003 598 REMARK 3 DIHEDRAL : 12.783 1946 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): -22.0383 -6.9663 17.7169 REMARK 3 T TENSOR REMARK 3 T11: 0.1614 T22: 0.2322 REMARK 3 T33: 0.1207 T12: -0.0126 REMARK 3 T13: 0.0075 T23: 0.0040 REMARK 3 L TENSOR REMARK 3 L11: 1.3287 L22: 2.1932 REMARK 3 L33: 1.6786 L12: 0.1783 REMARK 3 L13: 0.2393 L23: 0.1935 REMARK 3 S TENSOR REMARK 3 S11: -0.0147 S12: 0.0308 S13: -0.1271 REMARK 3 S21: -0.1141 S22: 0.0056 S23: -0.0257 REMARK 3 S31: 0.2043 S32: -0.0771 S33: 0.0175 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ 1001:1106)) REMARK 3 ORIGIN FOR THE GROUP (A): 0.8327 -54.4924 19.8816 REMARK 3 T TENSOR REMARK 3 T11: 0.5633 T22: 0.3896 REMARK 3 T33: 0.9296 T12: 0.0758 REMARK 3 T13: 0.0521 T23: -0.0624 REMARK 3 L TENSOR REMARK 3 L11: 1.9910 L22: 9.2899 REMARK 3 L33: 6.6243 L12: -2.5931 REMARK 3 L13: 2.1205 L23: -3.1172 REMARK 3 S TENSOR REMARK 3 S11: 0.3427 S12: -0.1198 S13: 0.7642 REMARK 3 S21: -0.8635 S22: -0.2495 S23: -0.6562 REMARK 3 S31: 0.1190 S32: 0.1095 S33: -0.0861 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 5OLZ 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_1200006024. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-NOV-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 : 39460 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 33.710 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.80 REMARK 200 R MERGE FOR SHELL (I) : 1.17400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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 (%): 52.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.L M TRI-SODIUM CITRATE PH 5.3-5.4, REMARK 280 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2% (V/V) 2,5- REMARK 280 HEXANEDIOL AND 0.005 MM COMPOUND 4E., LIPIDIC CUBIC PHASE, REMARK 280 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 70.03300 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 70.03300 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 19.68450 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.62350 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.68450 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.62350 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.03300 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.68450 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.62350 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.03300 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.68450 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.62350 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: 10090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 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 MET A 1058 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 O HOH A 1329 O HOH A 1359 2.18 REMARK 500 O HOH A 1398 O HOH A 1406 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 208 CA - C - N ANGL. DEV. = 14.9 DEGREES REMARK 500 LEU A 208 O - C - N ANGL. DEV. = -19.5 DEGREES 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 -51.19 -122.07 REMARK 500 TYR A1101 -55.56 -126.95 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 -15.63 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 1209 REMARK 610 OLA A 1210 REMARK 610 OLA A 1211 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1217 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLC A 1220 REMARK 610 OLC A 1221 REMARK 610 OLC A 1222 REMARK 610 OLC A 1223 REMARK 610 OLC A 1226 REMARK 610 OLC A 1227 REMARK 610 OLC A 1229 REMARK 610 OLC A 1230 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 A1234 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 127.8 REMARK 620 3 HOH A1376 O 82.1 118.1 REMARK 620 4 HOH A1343 O 104.6 120.9 91.3 REMARK 620 5 HOH A1368 O 88.3 65.4 169.8 94.7 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 T4E A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR 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 OLA 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 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1228 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1229 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1230 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TAR A 1231 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1232 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 1233 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1234 DBREF 5OLZ A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5OLZ A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5OLZ A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5OLZ ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5OLZ TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5OLZ LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5OLZ GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5OLZ ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5OLZ PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5OLZ LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5OLZ ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5OLZ ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5OLZ ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5OLZ ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5OLZ ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5OLZ TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5OLZ ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5OLZ LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5OLZ ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5OLZ ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5OLZ ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5OLZ ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5OLZ HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5OLZ 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 T4E A1201 21 HET CLR A1202 28 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET OLA A1206 20 HET OLA A1207 9 HET OLA A1208 20 HET OLA A1209 18 HET OLA A1210 15 HET OLA A1211 12 HET OLA A1212 12 HET OLA A1213 10 HET OLA A1214 10 HET OLA A1215 9 HET OLA A1216 19 HET OLA A1217 12 HET OLA A1218 9 HET OLA A1219 16 HET OLC A1220 17 HET OLC A1221 19 HET OLC A1222 16 HET OLC A1223 22 HET OLC A1224 25 HET OLC A1225 25 HET OLC A1226 24 HET OLC A1227 18 HET OLC A1228 25 HET OLC A1229 17 HET OLC A1230 14 HET TAR A1231 10 HET OLA A1232 20 HET PGE A1233 10 HET NA A1234 1 HETNAM T4E 4-(3-AMINO-5-PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM TAR D(-)-TARTARIC ACID HETNAM PGE TRIETHYLENE GLYCOL HETNAM NA SODIUM ION HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 T4E C15 H11 CL N4 O FORMUL 3 CLR 4(C27 H46 O) FORMUL 7 OLA 15(C18 H34 O2) FORMUL 21 OLC 11(C21 H40 O4) FORMUL 32 TAR C4 H6 O6 FORMUL 34 PGE C6 H14 O4 FORMUL 35 NA NA 1+ FORMUL 36 HOH *118(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 ASP A 1060 GLU A 1081 1 22 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 TYR A 1101 CYS A 259 1 47 HELIX 17 AB8 PRO A 266 ILE A 292 1 27 HELIX 18 AB9 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 2.04 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.04 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04 LINK OD1 ASP A 52 NA NA A1234 1555 1555 2.43 LINK OG SER A 91 NA NA A1234 1555 1555 2.65 LINK NA NA A1234 O HOH A1376 1555 1555 2.39 LINK NA NA A1234 O HOH A1343 1555 1555 2.53 LINK NA NA A1234 O HOH A1368 1555 1555 2.64 SITE 1 AC1 12 ALA A 63 VAL A 84 LEU A 85 PHE A 168 SITE 2 AC1 12 GLU A 169 MET A 177 TRP A 246 HIS A 250 SITE 3 AC1 12 ASN A 253 HIS A 278 HOH A1309 HOH A1355 SITE 1 AC2 5 HIS A 75 GLY A 76 OLC A1229 HOH A1305 SITE 2 AC2 5 HOH A1326 SITE 1 AC3 8 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC3 8 CLR A1205 OLC A1221 OLC A1225 OLC A1226 SITE 1 AC4 5 PRO A 248 CYS A 262 SER A 263 OLA A1218 SITE 2 AC4 5 OLC A1223 SITE 1 AC5 7 CYS A 254 PHE A 255 PHE A 258 CYS A 259 SITE 2 AC5 7 CLR A1203 OLC A1225 HOH A1344 SITE 1 AC6 1 THR A 65 SITE 1 AC7 3 PHE A 44 ALA A 97 VAL A 116 SITE 1 AC8 5 GLY A 123 LEU A 131 VAL A 188 OLC A1224 SITE 2 AC8 5 HOH A1356 SITE 1 AC9 5 GLY A 5 TYR A 271 VAL A 275 OLA A1213 SITE 2 AC9 5 OLA A1214 SITE 1 AD1 1 OLC A1228 SITE 1 AD2 3 SER A 7 LEU A 26 PHE A 286 SITE 1 AD3 2 TRP A 268 LEU A 272 SITE 1 AD4 2 OLA A1209 OLA A1214 SITE 1 AD5 4 THR A 279 VAL A 283 OLA A1209 OLA A1213 SITE 1 AD6 3 LEU A 190 ALA A 236 OLA A1217 SITE 1 AD7 4 TRP A 29 TRP A 32 PHE A 201 LYS A 233 SITE 1 AD8 2 LEU A 244 OLA A1215 SITE 1 AD9 2 LEU A 244 CLR A1204 SITE 1 AE1 2 TRP A 268 LEU A 272 SITE 1 AE2 4 TYR A 179 OLC A1221 OLC A1222 OLC A1229 SITE 1 AE3 8 GLN A 163 PHE A 183 PHE A 258 CLR A1203 SITE 2 AE3 8 OLC A1220 HOH A1305 HOH A1348 HOH A1380 SITE 1 AE4 10 HIS A 75 MET A 140 LEU A 141 GLY A 142 SITE 2 AE4 10 ASN A 144 TYR A 179 OLC A1220 OLC A1229 SITE 3 AE4 10 HOH A1301 HOH A1311 SITE 1 AE5 6 ASP A 261 SER A 263 LYS A1085 CLR A1204 SITE 2 AE5 6 OLC A1225 HOH A1302 SITE 1 AE6 3 ARG A 120 PHE A 180 OLA A1208 SITE 1 AE7 7 THR A 65 PHE A 70 CYS A 71 CLR A1203 SITE 2 AE7 7 CLR A1205 OLC A1223 HOH A1375 SITE 1 AE8 7 TYR A 43 LEU A 58 PHE A 83 ILE A 125 SITE 2 AE8 7 TRP A 129 PHE A 133 CLR A1203 SITE 1 AE9 5 CYS A 28 VAL A 31 TYR A 43 LEU A 54 SITE 2 AE9 5 ARG A 205 SITE 1 AF1 6 SER A 6 ILE A 10 SER A 67 THR A 68 SITE 2 AF1 6 GLN A 157 OLA A1210 SITE 1 AF2 6 HIS A 75 MET A 140 CLR A1202 OLC A1220 SITE 2 AF2 6 OLC A1222 OLC A1230 SITE 1 AF3 1 OLC A1229 SITE 1 AF4 5 GLY A 142 TRP A 143 ASN A 144 ASN A 145 SITE 2 AF4 5 ASN A 175 SITE 1 AF5 2 SER A 7 THR A 11 SITE 1 AF6 5 HIS A 264 ALA A 265 PRO A 266 LEU A 267 SITE 2 AF6 5 HOH A1308 SITE 1 AF7 5 ASP A 52 SER A 91 HOH A1343 HOH A1368 SITE 2 AF7 5 HOH A1376 CRYST1 39.369 179.247 140.066 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 0.025401 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005579 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007139 0.00000 ATOM 1 N GLY A -1 -20.621 24.470 1.213 1.00 97.34 N ANISOU 1 N GLY A -1 14706 11055 11225 -441 -717 1853 N ATOM 2 CA GLY A -1 -21.350 23.570 2.087 1.00 96.20 C ANISOU 2 CA GLY A -1 14420 11002 11131 -325 -791 1745 C ATOM 3 C GLY A -1 -22.613 23.013 1.456 1.00 96.36 C ANISOU 3 C GLY A -1 14426 11115 11073 -190 -928 1727 C ATOM 4 O GLY A -1 -23.674 23.636 1.519 1.00 98.66 O ANISOU 4 O GLY A -1 14729 11325 11434 -52 -1097 1731 O ATOM 5 N ALA A 0 -22.492 21.834 0.849 1.00 92.38 N ANISOU 5 N ALA A 0 13885 10781 10435 -231 -852 1698 N ATOM 6 CA ALA A 0 -23.624 21.211 0.182 1.00 88.44 C ANISOU 6 CA ALA A 0 13368 10378 9858 -128 -975 1674 C ATOM 7 C ALA A 0 -24.740 20.923 1.185 1.00 83.94 C ANISOU 7 C ALA A 0 12652 9828 9415 27 -1119 1583 C ATOM 8 O ALA A 0 -24.475 20.710 2.373 1.00 82.62 O ANISOU 8 O ALA A 0 12382 9660 9350 36 -1083 1517 O ATOM 9 CB ALA A 0 -23.188 19.920 -0.506 1.00 87.12 C ANISOU 9 CB ALA A 0 13179 10382 9539 -208 -852 1636 C ATOM 10 N PRO A 1 -25.996 20.919 0.735 1.00 82.84 N ANISOU 10 N PRO A 1 12491 9710 9274 149 -1282 1575 N ATOM 11 CA PRO A 1 -27.127 20.699 1.649 1.00 80.41 C ANISOU 11 CA PRO A 1 12020 9428 9103 302 -1413 1483 C ATOM 12 C PRO A 1 -26.933 19.437 2.469 1.00 77.39 C ANISOU 12 C PRO A 1 11489 9184 8730 283 -1337 1379 C ATOM 13 O PRO A 1 -26.574 18.381 1.926 1.00 77.40 O ANISOU 13 O PRO A 1 11490 9314 8605 199 -1251 1360 O ATOM 14 CB PRO A 1 -28.328 20.566 0.700 1.00 81.14 C ANISOU 14 CB PRO A 1 12110 9572 9147 387 -1562 1494 C ATOM 15 CG PRO A 1 -27.931 21.334 -0.509 1.00 83.06 C ANISOU 15 CG PRO A 1 12552 9733 9274 318 -1556 1616 C ATOM 16 CD PRO A 1 -26.445 21.151 -0.651 1.00 83.43 C ANISOU 16 CD PRO A 1 12687 9787 9227 150 -1354 1651 C ATOM 17 N PRO A 2 -27.150 19.511 3.785 1.00 72.42 N ANISOU 17 N PRO A 2 10712 8541 8261 359 -1341 1288 N ATOM 18 CA PRO A 2 -26.897 18.334 4.630 1.00 65.25 C ANISOU 18 CA PRO A 2 9611 7787 7395 327 -1212 1154 C ATOM 19 C PRO A 2 -27.772 17.147 4.279 1.00 56.98 C ANISOU 19 C PRO A 2 8471 6889 6290 365 -1275 1101 C ATOM 20 O PRO A 2 -27.356 16.004 4.497 1.00 52.76 O ANISOU 20 O PRO A 2 7847 6479 5719 297 -1158 1029 O ATOM 21 CB PRO A 2 -27.186 18.850 6.049 1.00 67.72 C ANISOU 21 CB PRO A 2 9777 8053 7902 418 -1211 1056 C ATOM 22 CG PRO A 2 -27.149 20.347 5.944 1.00 70.08 C ANISOU 22 CG PRO A 2 10216 8155 8257 457 -1290 1140 C ATOM 23 CD PRO A 2 -27.638 20.659 4.566 1.00 73.07 C ANISOU 23 CD PRO A 2 10768 8482 8512 475 -1429 1273 C ATOM 24 N ILE A 3 -28.964 17.382 3.724 1.00 56.33 N ANISOU 24 N ILE A 3 8410 6790 6202 470 -1465 1137 N ATOM 25 CA ILE A 3 -29.879 16.291 3.411 1.00 57.74 C ANISOU 25 CA ILE A 3 8484 7108 6346 500 -1539 1078 C ATOM 26 C ILE A 3 -29.344 15.387 2.303 1.00 58.25 C ANISOU 26 C ILE A 3 8647 7261 6225 376 -1461 1100 C ATOM 27 O ILE A 3 -29.828 14.261 2.141 1.00 55.74 O ANISOU 27 O ILE A 3 8241 7066 5872 366 -1475 1031 O ATOM 28 CB ILE A 3 -31.261 16.851 3.025 1.00 56.72 C ANISOU 28 CB ILE A 3 8298 6955 6296 625 -1709 1083 C ATOM 29 CG1 ILE A 3 -32.330 15.757 3.111 1.00 58.53 C ANISOU 29 CG1 ILE A 3 8348 7331 6560 664 -1773 990 C ATOM 30 CG2 ILE A 3 -31.215 17.444 1.633 1.00 60.70 C ANISOU 30 CG2 ILE A 3 8984 7399 6679 589 -1759 1190 C ATOM 31 CD1 ILE A 3 -33.582 16.041 2.301 1.00 62.68 C ANISOU 31 CD1 ILE A 3 8844 7864 7106 741 -1932 1011 C ATOM 32 N MET A 4 -28.354 15.841 1.532 1.00 53.19 N ANISOU 32 N MET A 4 8181 6559 5469 280 -1369 1187 N ATOM 33 CA MET A 4 -27.851 15.034 0.424 1.00 49.04 C ANISOU 33 CA MET A 4 7749 6117 4770 175 -1283 1196 C ATOM 34 C MET A 4 -26.903 13.945 0.915 1.00 46.37 C ANISOU 34 C MET A 4 7361 5867 4391 84 -1115 1129 C ATOM 35 O MET A 4 -27.130 12.755 0.669 1.00 46.49 O ANISOU 35 O MET A 4 7321 5994 4348 64 -1099 1056 O ATOM 36 CB MET A 4 -27.168 15.932 -0.609 1.00 48.51 C ANISOU 36 CB MET A 4 7874 5960 4598 108 -1235 1309 C ATOM 37 CG MET A 4 -28.122 16.881 -1.308 1.00 46.98 C ANISOU 37 CG MET A 4 7751 5687 4415 191 -1407 1380 C ATOM 38 SD MET A 4 -27.303 17.869 -2.566 1.00 56.05 S ANISOU 38 SD MET A 4 9137 6735 5424 99 -1346 1517 S ATOM 39 CE MET A 4 -26.872 16.616 -3.774 1.00 56.74 C ANISOU 39 CE MET A 4 9292 6964 5301 -3 -1243 1488 C ATOM 40 N GLY A 5 -25.822 14.336 1.598 1.00 41.12 N ANISOU 40 N GLY A 5 6713 5149 3763 26 -989 1150 N ATOM 41 CA GLY A 5 -24.964 13.344 2.226 1.00 40.10 C ANISOU 41 CA GLY A 5 6460 5111 3665 -41 -807 1054 C ATOM 42 C GLY A 5 -25.714 12.511 3.243 1.00 45.14 C ANISOU 42 C GLY A 5 6889 5832 4429 32 -841 931 C ATOM 43 O GLY A 5 -25.455 11.312 3.392 1.00 43.95 O ANISOU 43 O GLY A 5 6662 5780 4256 -6 -754 852 O ATOM 44 N ASER A 6 -26.672 13.129 3.939 0.53 43.95 N ANISOU 44 N ASER A 6 6649 5640 4412 139 -965 914 N ATOM 45 N BSER A 6 -26.638 13.137 3.978 0.47 43.84 N ANISOU 45 N BSER A 6 6630 5624 4401 138 -960 913 N ATOM 46 CA ASER A 6 -27.572 12.383 4.809 0.53 41.36 C ANISOU 46 CA ASER A 6 6128 5395 4193 209 -1006 808 C ATOM 47 CA BSER A 6 -27.477 12.379 4.901 0.47 41.09 C ANISOU 47 CA BSER A 6 6087 5360 4166 204 -991 804 C ATOM 48 C ASER A 6 -28.334 11.316 4.030 0.53 36.71 C ANISOU 48 C ASER A 6 5537 4901 3509 203 -1088 783 C ATOM 49 C BSER A 6 -28.258 11.301 4.164 0.47 36.72 C ANISOU 49 C BSER A 6 5526 4904 3523 201 -1072 776 C ATOM 50 O ASER A 6 -28.512 10.195 4.517 0.53 35.28 O ANISOU 50 O ASER A 6 5232 4813 3360 186 -1040 693 O ATOM 51 O BSER A 6 -28.403 10.179 4.663 0.47 34.75 O ANISOU 51 O BSER A 6 5152 4746 3304 183 -1020 686 O ATOM 52 CB ASER A 6 -28.543 13.347 5.494 0.53 43.51 C ANISOU 52 CB ASER A 6 6319 5601 4611 333 -1129 801 C ATOM 53 CB BSER A 6 -28.436 13.313 5.642 0.47 43.37 C ANISOU 53 CB BSER A 6 6289 5586 4604 328 -1108 792 C ATOM 54 OG ASER A 6 -29.493 12.662 6.290 0.53 45.11 O ANISOU 54 OG ASER A 6 6333 5891 4916 396 -1162 702 O ATOM 55 OG BSER A 6 -27.738 14.223 6.472 0.47 44.67 O ANISOU 55 OG BSER A 6 6452 5661 4861 329 -1032 793 O ATOM 56 N ASER A 7 -28.786 11.646 2.816 0.53 37.59 N ANISOU 56 N ASER A 7 5798 4985 3499 210 -1219 864 N ATOM 57 N BSER A 7 -28.760 11.622 2.968 0.47 37.32 N ANISOU 57 N BSER A 7 5743 4953 3482 212 -1206 854 N ATOM 58 CA ASER A 7 -29.595 10.706 2.043 0.53 37.65 C ANISOU 58 CA ASER A 7 5804 5079 3423 204 -1317 833 C ATOM 59 CA BSER A 7 -29.559 10.667 2.209 0.47 37.61 C ANISOU 59 CA BSER A 7 5784 5077 3431 205 -1310 826 C ATOM 60 C ASER A 7 -28.806 9.461 1.657 0.53 34.91 C ANISOU 60 C ASER A 7 5501 4809 2953 98 -1182 784 C ATOM 61 C BSER A 7 -28.753 9.425 1.852 0.47 34.56 C ANISOU 61 C BSER A 7 5438 4767 2927 99 -1169 776 C ATOM 62 O ASER A 7 -29.378 8.369 1.569 0.53 33.17 O ANISOU 62 O ASER A 7 5206 4671 2725 87 -1214 707 O ATOM 63 O BSER A 7 -29.257 8.300 1.960 0.47 32.35 O ANISOU 63 O BSER A 7 5066 4571 2655 87 -1187 692 O ATOM 64 CB ASER A 7 -30.150 11.386 0.792 0.53 40.47 C ANISOU 64 CB ASER A 7 6271 5394 3713 230 -1426 905 C ATOM 65 CB BSER A 7 -30.105 11.328 0.944 0.47 39.92 C ANISOU 65 CB BSER A 7 6186 5327 3653 230 -1416 897 C ATOM 66 OG ASER A 7 -31.176 12.308 1.123 0.53 42.35 O ANISOU 66 OG ASER A 7 6431 5577 4083 346 -1574 926 O ATOM 67 OG BSER A 7 -29.052 11.777 0.111 0.47 39.57 O ANISOU 67 OG BSER A 7 6326 5229 3479 153 -1314 974 O ATOM 68 N VAL A 8 -27.501 9.606 1.422 1.00 31.23 N ANISOU 68 N VAL A 8 5149 4314 2403 19 -1024 822 N ATOM 69 CA VAL A 8 -26.663 8.457 1.090 1.00 32.96 C ANISOU 69 CA VAL A 8 5399 4601 2525 -69 -874 765 C ATOM 70 C VAL A 8 -26.454 7.590 2.321 1.00 34.85 C ANISOU 70 C VAL A 8 5445 4892 2904 -65 -772 660 C ATOM 71 O VAL A 8 -26.626 6.366 2.280 1.00 29.65 O ANISOU 71 O VAL A 8 4742 4301 2221 -89 -753 581 O ATOM 72 CB VAL A 8 -25.319 8.916 0.497 1.00 29.80 C ANISOU 72 CB VAL A 8 5129 4159 2033 -145 -709 825 C ATOM 73 CG1 VAL A 8 -24.337 7.744 0.451 1.00 28.38 C ANISOU 73 CG1 VAL A 8 4937 4047 1798 -217 -529 751 C ATOM 74 CG2 VAL A 8 -25.525 9.496 -0.885 1.00 32.18 C ANISOU 74 CG2 VAL A 8 5575 4426 2224 -150 -760 895 C ATOM 75 N TYR A 9 -26.087 8.223 3.438 1.00 28.09 N ANISOU 75 N TYR A 9 4484 3997 2194 -37 -713 657 N ATOM 76 CA TYR A 9 -25.896 7.500 4.686 1.00 25.47 C ANISOU 76 CA TYR A 9 3980 3708 1989 -29 -627 567 C ATOM 77 C TYR A 9 -27.165 6.753 5.088 1.00 24.85 C ANISOU 77 C TYR A 9 3779 3690 1974 16 -733 500 C ATOM 78 O TYR A 9 -27.115 5.569 5.440 1.00 25.26 O ANISOU 78 O TYR A 9 3759 3800 2041 -13 -675 427 O ATOM 79 CB TYR A 9 -25.455 8.479 5.778 1.00 25.02 C ANISOU 79 CB TYR A 9 3850 3592 2064 0 -581 579 C ATOM 80 CG TYR A 9 -25.529 7.904 7.170 1.00 26.59 C ANISOU 80 CG TYR A 9 3877 3834 2394 25 -532 494 C ATOM 81 CD1 TYR A 9 -24.700 6.852 7.552 1.00 22.55 C ANISOU 81 CD1 TYR A 9 3317 3370 1882 -25 -408 439 C ATOM 82 CD2 TYR A 9 -26.421 8.412 8.106 1.00 26.87 C ANISOU 82 CD2 TYR A 9 3804 3857 2547 103 -607 467 C ATOM 83 CE1 TYR A 9 -24.762 6.319 8.825 1.00 24.02 C ANISOU 83 CE1 TYR A 9 3366 3589 2172 -5 -370 373 C ATOM 84 CE2 TYR A 9 -26.490 7.885 9.382 1.00 25.93 C ANISOU 84 CE2 TYR A 9 3546 3782 2526 118 -553 394 C ATOM 85 CZ TYR A 9 -25.659 6.837 9.735 1.00 26.76 C ANISOU 85 CZ TYR A 9 3619 3931 2617 60 -440 352 C ATOM 86 OH TYR A 9 -25.723 6.302 11.004 1.00 29.09 O ANISOU 86 OH TYR A 9 3794 4263 2995 73 -394 290 O ATOM 87 N ILE A 10 -28.318 7.424 5.010 1.00 25.34 N ANISOU 87 N ILE A 10 3814 3734 2079 87 -889 526 N ATOM 88 CA ILE A 10 -29.580 6.811 5.420 1.00 29.20 C ANISOU 88 CA ILE A 10 4161 4284 2648 128 -988 463 C ATOM 89 C ILE A 10 -29.956 5.655 4.494 1.00 29.52 C ANISOU 89 C ILE A 10 4252 4385 2580 71 -1041 432 C ATOM 90 O ILE A 10 -30.412 4.601 4.951 1.00 28.37 O ANISOU 90 O ILE A 10 3996 4299 2486 48 -1031 358 O ATOM 91 CB ILE A 10 -30.695 7.873 5.467 1.00 32.86 C ANISOU 91 CB ILE A 10 4577 4714 3193 227 -1147 498 C ATOM 92 CG1 ILE A 10 -30.486 8.821 6.652 1.00 34.06 C ANISOU 92 CG1 ILE A 10 4647 4813 3481 290 -1089 493 C ATOM 93 CG2 ILE A 10 -32.061 7.218 5.537 1.00 29.00 C ANISOU 93 CG2 ILE A 10 3951 4299 2768 257 -1269 443 C ATOM 94 CD1 ILE A 10 -31.444 9.996 6.658 1.00 32.92 C ANISOU 94 CD1 ILE A 10 4475 4611 3420 402 -1234 527 C ATOM 95 N THR A 11 -29.799 5.841 3.181 1.00 28.33 N ANISOU 95 N THR A 11 4278 4215 2272 43 -1100 488 N ATOM 96 CA THR A 11 -30.152 4.784 2.236 1.00 30.29 C ANISOU 96 CA THR A 11 4597 4514 2398 -13 -1161 451 C ATOM 97 C THR A 11 -29.307 3.540 2.459 1.00 28.46 C ANISOU 97 C THR A 11 4361 4313 2138 -85 -998 376 C ATOM 98 O THR A 11 -29.823 2.416 2.445 1.00 31.66 O ANISOU 98 O THR A 11 4718 4764 2549 -119 -1030 302 O ATOM 99 CB THR A 11 -29.980 5.282 0.806 1.00 28.31 C ANISOU 99 CB THR A 11 4531 4231 1995 -24 -1198 515 C ATOM 100 OG1 THR A 11 -30.796 6.441 0.598 1.00 31.87 O ANISOU 100 OG1 THR A 11 4969 4641 2499 54 -1339 583 O ATOM 101 CG2 THR A 11 -30.384 4.189 -0.184 1.00 27.44 C ANISOU 101 CG2 THR A 11 4468 4168 1789 -70 -1233 452 C ATOM 102 N VAL A 12 -28.005 3.726 2.678 1.00 23.15 N ANISOU 102 N VAL A 12 3735 3611 1449 -109 -828 392 N ATOM 103 CA VAL A 12 -27.118 2.601 2.948 1.00 25.17 C ANISOU 103 CA VAL A 12 3976 3888 1697 -159 -673 323 C ATOM 104 C VAL A 12 -27.501 1.921 4.256 1.00 28.07 C ANISOU 104 C VAL A 12 4160 4282 2224 -143 -653 257 C ATOM 105 O VAL A 12 -27.543 0.687 4.339 1.00 24.91 O ANISOU 105 O VAL A 12 3736 3906 1823 -179 -621 187 O ATOM 106 CB VAL A 12 -25.653 3.079 2.950 1.00 24.26 C ANISOU 106 CB VAL A 12 3924 3740 1554 -181 -504 359 C ATOM 107 CG1 VAL A 12 -24.719 1.989 3.469 1.00 26.52 C ANISOU 107 CG1 VAL A 12 4154 4045 1879 -209 -349 286 C ATOM 108 CG2 VAL A 12 -25.252 3.521 1.535 1.00 23.44 C ANISOU 108 CG2 VAL A 12 4022 3620 1264 -219 -499 420 C ATOM 109 N GLU A 13 -27.798 2.714 5.295 1.00 24.70 N ANISOU 109 N GLU A 13 3613 3844 1930 -89 -668 278 N ATOM 110 CA GLU A 13 -28.217 2.145 6.575 1.00 23.94 C ANISOU 110 CA GLU A 13 3352 3776 1970 -76 -644 223 C ATOM 111 C GLU A 13 -29.466 1.288 6.419 1.00 19.98 C ANISOU 111 C GLU A 13 2786 3320 1485 -94 -753 175 C ATOM 112 O GLU A 13 -29.545 0.189 6.979 1.00 23.63 O ANISOU 112 O GLU A 13 3181 3805 1991 -132 -705 118 O ATOM 113 CB GLU A 13 -28.468 3.258 7.598 1.00 25.13 C ANISOU 113 CB GLU A 13 3402 3908 2239 -10 -656 248 C ATOM 114 CG GLU A 13 -27.206 3.921 8.128 1.00 25.94 C ANISOU 114 CG GLU A 13 3528 3966 2362 -7 -537 275 C ATOM 115 CD GLU A 13 -26.582 3.138 9.258 1.00 29.97 C ANISOU 115 CD GLU A 13 3951 4495 2939 -25 -424 225 C ATOM 116 OE1 GLU A 13 -26.593 3.649 10.396 1.00 31.34 O ANISOU 116 OE1 GLU A 13 4039 4663 3207 10 -402 217 O ATOM 117 OE2 GLU A 13 -26.102 2.005 9.019 1.00 30.84 O ANISOU 117 OE2 GLU A 13 4088 4623 3007 -71 -363 191 O ATOM 118 N LEU A 14 -30.455 1.773 5.664 1.00 22.23 N ANISOU 118 N LEU A 14 3091 3616 1741 -71 -909 200 N ATOM 119 CA LEU A 14 -31.684 1.004 5.482 1.00 23.43 C ANISOU 119 CA LEU A 14 3165 3815 1921 -95 -1028 153 C ATOM 120 C LEU A 14 -31.426 -0.294 4.722 1.00 27.72 C ANISOU 120 C LEU A 14 3808 4366 2358 -179 -1013 101 C ATOM 121 O LEU A 14 -31.997 -1.339 5.057 1.00 26.96 O ANISOU 121 O LEU A 14 3630 4295 2316 -228 -1027 41 O ATOM 122 CB LEU A 14 -32.733 1.849 4.763 1.00 27.74 C ANISOU 122 CB LEU A 14 3711 4369 2458 -45 -1216 195 C ATOM 123 CG LEU A 14 -33.222 3.057 5.568 1.00 31.38 C ANISOU 123 CG LEU A 14 4052 4819 3052 52 -1248 229 C ATOM 124 CD1 LEU A 14 -34.217 3.878 4.766 1.00 36.91 C ANISOU 124 CD1 LEU A 14 4763 5516 3746 115 -1448 274 C ATOM 125 CD2 LEU A 14 -33.831 2.599 6.885 1.00 33.98 C ANISOU 125 CD2 LEU A 14 4177 5196 3539 57 -1194 168 C ATOM 126 N ALA A 15 -30.581 -0.247 3.688 1.00 25.24 N ANISOU 126 N ALA A 15 3676 4024 1890 -201 -979 121 N ATOM 127 CA ALA A 15 -30.226 -1.466 2.968 1.00 27.63 C ANISOU 127 CA ALA A 15 4088 4324 2084 -272 -944 59 C ATOM 128 C ALA A 15 -29.560 -2.480 3.894 1.00 22.95 C ANISOU 128 C ALA A 15 3431 3719 1570 -298 -794 2 C ATOM 129 O ALA A 15 -29.861 -3.678 3.839 1.00 24.74 O ANISOU 129 O ALA A 15 3656 3944 1799 -352 -805 -66 O ATOM 130 CB ALA A 15 -29.311 -1.127 1.791 1.00 24.44 C ANISOU 130 CB ALA A 15 3890 3897 1500 -283 -897 91 C ATOM 131 N ILE A 16 -28.655 -2.019 4.753 1.00 22.20 N ANISOU 131 N ILE A 16 3287 3605 1541 -261 -664 31 N ATOM 132 CA ILE A 16 -28.001 -2.928 5.691 1.00 22.79 C ANISOU 132 CA ILE A 16 3302 3665 1694 -275 -538 -12 C ATOM 133 C ILE A 16 -29.020 -3.534 6.653 1.00 25.66 C ANISOU 133 C ILE A 16 3521 4050 2180 -294 -588 -42 C ATOM 134 O ILE A 16 -28.966 -4.732 6.960 1.00 23.24 O ANISOU 134 O ILE A 16 3206 3726 1899 -338 -547 -93 O ATOM 135 CB ILE A 16 -26.878 -2.194 6.440 1.00 22.64 C ANISOU 135 CB ILE A 16 3251 3628 1725 -232 -414 29 C ATOM 136 CG1 ILE A 16 -25.741 -1.858 5.476 1.00 24.02 C ANISOU 136 CG1 ILE A 16 3563 3782 1783 -236 -332 49 C ATOM 137 CG2 ILE A 16 -26.366 -3.030 7.614 1.00 22.80 C ANISOU 137 CG2 ILE A 16 3186 3635 1842 -234 -317 -4 C ATOM 138 CD1 ILE A 16 -24.754 -0.884 6.060 1.00 25.67 C ANISOU 138 CD1 ILE A 16 3737 3974 2041 -204 -238 100 C ATOM 139 N ALA A 17 -29.965 -2.717 7.137 1.00 22.73 N ANISOU 139 N ALA A 17 3036 3713 1888 -260 -670 -11 N ATOM 140 CA ALA A 17 -30.970 -3.206 8.079 1.00 23.13 C ANISOU 140 CA ALA A 17 2936 3795 2057 -282 -700 -37 C ATOM 141 C ALA A 17 -31.807 -4.329 7.473 1.00 24.94 C ANISOU 141 C ALA A 17 3175 4035 2268 -361 -788 -90 C ATOM 142 O ALA A 17 -32.088 -5.330 8.143 1.00 24.45 O ANISOU 142 O ALA A 17 3049 3968 2273 -416 -752 -126 O ATOM 143 CB ALA A 17 -31.863 -2.052 8.549 1.00 21.78 C ANISOU 143 CB ALA A 17 2642 3663 1971 -221 -772 -4 C ATOM 144 N AVAL A 18 -32.223 -4.165 6.213 0.95 23.93 N ANISOU 144 N AVAL A 18 3133 3914 2045 -372 -910 -94 N ATOM 145 N BVAL A 18 -32.200 -4.206 6.203 0.05 25.35 N ANISOU 145 N BVAL A 18 3316 4092 2223 -374 -908 -96 N ATOM 146 CA AVAL A 18 -32.988 -5.201 5.522 0.95 28.76 C ANISOU 146 CA AVAL A 18 3770 4530 2627 -454 -1013 -153 C ATOM 147 CA BVAL A 18 -33.035 -5.260 5.630 0.05 27.73 C ANISOU 147 CA BVAL A 18 3626 4401 2510 -458 -1009 -155 C ATOM 148 C AVAL A 18 -32.205 -6.507 5.502 0.95 27.43 C ANISOU 148 C AVAL A 18 3698 4305 2418 -513 -910 -209 C ATOM 149 C BVAL A 18 -32.230 -6.540 5.410 0.05 27.08 C ANISOU 149 C BVAL A 18 3663 4261 2366 -517 -918 -212 C ATOM 150 O AVAL A 18 -32.730 -7.579 5.828 0.95 24.73 O ANISOU 150 O AVAL A 18 3310 3950 2137 -587 -923 -257 O ATOM 151 O BVAL A 18 -32.775 -7.644 5.520 0.05 26.93 O ANISOU 151 O BVAL A 18 3618 4227 2389 -596 -947 -266 O ATOM 152 CB AVAL A 18 -33.336 -4.740 4.095 0.95 30.38 C ANISOU 152 CB AVAL A 18 4093 4747 2702 -450 -1161 -144 C ATOM 153 CB BVAL A 18 -33.726 -4.781 4.336 0.05 30.55 C ANISOU 153 CB BVAL A 18 4053 4782 2771 -456 -1186 -148 C ATOM 154 CG1AVAL A 18 -33.929 -5.892 3.279 0.95 31.01 C ANISOU 154 CG1AVAL A 18 4237 4822 2724 -544 -1265 -219 C ATOM 155 CG1BVAL A 18 -34.516 -3.503 4.594 0.05 30.92 C ANISOU 155 CG1BVAL A 18 3976 4875 2898 -380 -1282 -91 C ATOM 156 CG2AVAL A 18 -34.289 -3.553 4.131 0.95 31.97 C ANISOU 156 CG2AVAL A 18 4184 4995 2966 -387 -1292 -92 C ATOM 157 CG2BVAL A 18 -32.729 -4.585 3.210 0.05 30.98 C ANISOU 157 CG2BVAL A 18 4324 4802 2646 -444 -1156 -138 C ATOM 158 N LEU A 19 -30.929 -6.429 5.124 1.00 25.83 N ANISOU 158 N LEU A 19 3630 4064 2122 -481 -802 -204 N ATOM 159 CA LEU A 19 -30.104 -7.626 4.987 1.00 26.16 C ANISOU 159 CA LEU A 19 3772 4044 2123 -516 -704 -264 C ATOM 160 C LEU A 19 -29.809 -8.262 6.341 1.00 23.48 C ANISOU 160 C LEU A 19 3333 3676 1912 -519 -601 -264 C ATOM 161 O LEU A 19 -29.737 -9.492 6.451 1.00 27.38 O ANISOU 161 O LEU A 19 3863 4114 2424 -570 -574 -317 O ATOM 162 CB LEU A 19 -28.801 -7.271 4.276 1.00 24.61 C ANISOU 162 CB LEU A 19 3718 3825 1807 -471 -602 -257 C ATOM 163 CG LEU A 19 -28.901 -6.912 2.797 1.00 26.17 C ANISOU 163 CG LEU A 19 4070 4038 1836 -482 -679 -264 C ATOM 164 CD1 LEU A 19 -27.562 -6.365 2.311 1.00 30.04 C ANISOU 164 CD1 LEU A 19 4671 4517 2227 -438 -544 -239 C ATOM 165 CD2 LEU A 19 -29.324 -8.132 1.987 1.00 30.33 C ANISOU 165 CD2 LEU A 19 4703 4535 2286 -554 -746 -357 C ATOM 166 N ALA A 20 -29.608 -7.443 7.374 1.00 24.54 N ANISOU 166 N ALA A 20 3359 3838 2129 -465 -545 -205 N ATOM 167 CA ALA A 20 -29.344 -7.992 8.700 1.00 26.09 C ANISOU 167 CA ALA A 20 3473 4011 2428 -469 -457 -198 C ATOM 168 C ALA A 20 -30.558 -8.742 9.225 1.00 29.52 C ANISOU 168 C ALA A 20 3814 4456 2946 -546 -517 -217 C ATOM 169 O ALA A 20 -30.424 -9.830 9.801 1.00 26.20 O ANISOU 169 O ALA A 20 3401 3983 2569 -592 -467 -236 O ATOM 170 CB ALA A 20 -28.942 -6.880 9.667 1.00 20.62 C ANISOU 170 CB ALA A 20 2693 3351 1791 -399 -398 -138 C ATOM 171 N ILE A 21 -31.752 -8.180 9.024 1.00 28.72 N ANISOU 171 N ILE A 21 3622 4417 2872 -563 -627 -209 N ATOM 172 CA ILE A 21 -32.975 -8.853 9.454 1.00 27.30 C ANISOU 172 CA ILE A 21 3332 4260 2782 -648 -683 -230 C ATOM 173 C ILE A 21 -33.167 -10.149 8.677 1.00 29.27 C ANISOU 173 C ILE A 21 3679 4450 2992 -742 -735 -294 C ATOM 174 O ILE A 21 -33.355 -11.223 9.264 1.00 31.39 O ANISOU 174 O ILE A 21 3932 4673 3321 -819 -699 -312 O ATOM 175 CB ILE A 21 -34.183 -7.911 9.304 1.00 28.28 C ANISOU 175 CB ILE A 21 3323 4469 2954 -632 -797 -215 C ATOM 176 CG1 ILE A 21 -34.047 -6.724 10.263 1.00 26.08 C ANISOU 176 CG1 ILE A 21 2944 4234 2731 -541 -732 -163 C ATOM 177 CG2 ILE A 21 -35.488 -8.661 9.552 1.00 30.61 C ANISOU 177 CG2 ILE A 21 3491 4794 3344 -735 -864 -245 C ATOM 178 CD1 ILE A 21 -35.026 -5.606 9.999 1.00 31.48 C ANISOU 178 CD1 ILE A 21 3517 4985 3457 -488 -842 -147 C ATOM 179 N LEU A 22 -33.103 -10.071 7.345 1.00 26.33 N ANISOU 179 N LEU A 22 3424 4071 2510 -742 -822 -329 N ATOM 180 CA LEU A 22 -33.394 -11.236 6.512 1.00 26.12 C ANISOU 180 CA LEU A 22 3499 3989 2435 -834 -892 -404 C ATOM 181 C LEU A 22 -32.429 -12.381 6.796 1.00 30.19 C ANISOU 181 C LEU A 22 4124 4401 2945 -850 -774 -438 C ATOM 182 O LEU A 22 -32.850 -13.526 6.995 1.00 30.35 O ANISOU 182 O LEU A 22 4153 4362 3018 -943 -790 -479 O ATOM 183 CB LEU A 22 -33.341 -10.854 5.031 1.00 30.69 C ANISOU 183 CB LEU A 22 4213 4581 2867 -818 -993 -434 C ATOM 184 CG LEU A 22 -34.506 -10.030 4.478 1.00 38.13 C ANISOU 184 CG LEU A 22 5073 5606 3808 -822 -1166 -416 C ATOM 185 CD1 LEU A 22 -34.341 -9.830 2.979 1.00 37.88 C ANISOU 185 CD1 LEU A 22 5220 5572 3601 -815 -1265 -446 C ATOM 186 CD2 LEU A 22 -35.830 -10.697 4.800 1.00 41.12 C ANISOU 186 CD2 LEU A 22 5311 6008 4307 -927 -1270 -448 C ATOM 187 N GLY A 23 -31.127 -12.095 6.809 1.00 28.37 N ANISOU 187 N GLY A 23 3976 4142 2659 -761 -659 -423 N ATOM 188 CA GLY A 23 -30.156 -13.162 6.970 1.00 26.16 C ANISOU 188 CA GLY A 23 3801 3762 2378 -756 -557 -461 C ATOM 189 C GLY A 23 -30.199 -13.798 8.342 1.00 29.31 C ANISOU 189 C GLY A 23 4116 4118 2901 -783 -494 -426 C ATOM 190 O GLY A 23 -30.020 -15.013 8.477 1.00 29.70 O ANISOU 190 O GLY A 23 4238 4069 2979 -828 -470 -465 O ATOM 191 N ASN A 24 -30.452 -13.003 9.377 1.00 25.87 N ANISOU 191 N ASN A 24 3540 3751 2536 -756 -468 -353 N ATOM 192 CA ASN A 24 -30.401 -13.557 10.722 1.00 27.94 C ANISOU 192 CA ASN A 24 3743 3979 2893 -778 -397 -312 C ATOM 193 C ASN A 24 -31.726 -14.185 11.138 1.00 27.21 C ANISOU 193 C ASN A 24 3567 3892 2879 -900 -455 -313 C ATOM 194 O ASN A 24 -31.731 -15.106 11.961 1.00 29.50 O ANISOU 194 O ASN A 24 3866 4115 3228 -955 -407 -295 O ATOM 195 CB ASN A 24 -29.944 -12.480 11.704 1.00 25.16 C ANISOU 195 CB ASN A 24 3300 3692 2569 -693 -328 -241 C ATOM 196 CG ASN A 24 -28.458 -12.203 11.585 1.00 26.85 C ANISOU 196 CG ASN A 24 3592 3873 2738 -592 -249 -237 C ATOM 197 OD1 ASN A 24 -27.629 -13.024 11.989 1.00 26.12 O ANISOU 197 OD1 ASN A 24 3560 3700 2666 -574 -187 -240 O ATOM 198 ND2 ASN A 24 -28.111 -11.064 10.994 1.00 21.50 N ANISOU 198 ND2 ASN A 24 2911 3252 2004 -529 -254 -228 N ATOM 199 N VAL A 25 -32.847 -13.722 10.583 1.00 26.16 N ANISOU 199 N VAL A 25 3352 3837 2751 -948 -559 -330 N ATOM 200 CA VAL A 25 -34.090 -14.479 10.706 1.00 31.10 C ANISOU 200 CA VAL A 25 3904 4460 3452 -1083 -626 -350 C ATOM 201 C VAL A 25 -33.914 -15.872 10.110 1.00 33.00 C ANISOU 201 C VAL A 25 4292 4575 3671 -1165 -652 -415 C ATOM 202 O VAL A 25 -34.400 -16.866 10.661 1.00 33.22 O ANISOU 202 O VAL A 25 4307 4541 3774 -1275 -642 -414 O ATOM 203 CB VAL A 25 -35.250 -13.712 10.043 1.00 30.24 C ANISOU 203 CB VAL A 25 3679 4457 3354 -1105 -755 -367 C ATOM 204 CG1 VAL A 25 -36.409 -14.634 9.755 1.00 33.83 C ANISOU 204 CG1 VAL A 25 4086 4897 3872 -1255 -852 -413 C ATOM 205 CG2 VAL A 25 -35.705 -12.560 10.939 1.00 30.28 C ANISOU 205 CG2 VAL A 25 3507 4571 3426 -1046 -719 -306 C ATOM 206 N LEU A 26 -33.186 -15.969 8.992 1.00 31.09 N ANISOU 206 N LEU A 26 4203 4287 3324 -1115 -677 -474 N ATOM 207 CA LEU A 26 -32.919 -17.267 8.379 1.00 31.22 C ANISOU 207 CA LEU A 26 4379 4172 3312 -1176 -694 -552 C ATOM 208 C LEU A 26 -32.095 -18.162 9.301 1.00 29.06 C ANISOU 208 C LEU A 26 4168 3781 3091 -1160 -580 -526 C ATOM 209 O LEU A 26 -32.344 -19.370 9.384 1.00 33.14 O ANISOU 209 O LEU A 26 4755 4184 3654 -1255 -595 -559 O ATOM 210 CB LEU A 26 -32.210 -17.069 7.038 1.00 35.63 C ANISOU 210 CB LEU A 26 5090 4717 3730 -1107 -718 -621 C ATOM 211 CG LEU A 26 -31.950 -18.277 6.137 1.00 45.09 C ANISOU 211 CG LEU A 26 6475 5789 4870 -1155 -746 -728 C ATOM 212 CD1 LEU A 26 -33.258 -18.885 5.643 1.00 47.33 C ANISOU 212 CD1 LEU A 26 6746 6060 5176 -1307 -896 -785 C ATOM 213 CD2 LEU A 26 -31.062 -17.881 4.964 1.00 45.61 C ANISOU 213 CD2 LEU A 26 6684 5862 4782 -1062 -724 -784 C ATOM 214 N VAL A 27 -31.106 -17.590 9.994 1.00 27.01 N ANISOU 214 N VAL A 27 3890 3541 2831 -1043 -475 -466 N ATOM 215 CA VAL A 27 -30.319 -18.365 10.955 1.00 30.95 C ANISOU 215 CA VAL A 27 4439 3936 3384 -1016 -383 -430 C ATOM 216 C VAL A 27 -31.222 -18.940 12.044 1.00 32.05 C ANISOU 216 C VAL A 27 4502 4056 3620 -1134 -383 -372 C ATOM 217 O VAL A 27 -31.131 -20.125 12.389 1.00 30.83 O ANISOU 217 O VAL A 27 4435 3769 3511 -1193 -368 -374 O ATOM 218 CB VAL A 27 -29.201 -17.496 11.559 1.00 30.78 C ANISOU 218 CB VAL A 27 4383 3962 3349 -877 -292 -371 C ATOM 219 CG1 VAL A 27 -28.562 -18.193 12.761 1.00 25.85 C ANISOU 219 CG1 VAL A 27 3783 3249 2790 -855 -220 -314 C ATOM 220 CG2 VAL A 27 -28.147 -17.174 10.515 1.00 29.08 C ANISOU 220 CG2 VAL A 27 4261 3740 3047 -774 -265 -429 C ATOM 221 N CYS A 28 -32.100 -18.103 12.607 1.00 31.31 N ANISOU 221 N CYS A 28 4247 4090 3561 -1168 -393 -320 N ATOM 222 CA CYS A 28 -32.973 -18.551 13.691 1.00 33.04 C ANISOU 222 CA CYS A 28 4378 4311 3865 -1282 -368 -261 C ATOM 223 C CYS A 28 -33.974 -19.591 13.204 1.00 35.31 C ANISOU 223 C CYS A 28 4685 4531 4200 -1445 -446 -311 C ATOM 224 O CYS A 28 -34.263 -20.565 13.912 1.00 39.44 O ANISOU 224 O CYS A 28 5235 4966 4786 -1551 -414 -276 O ATOM 225 CB CYS A 28 -33.703 -17.356 14.310 1.00 30.35 C ANISOU 225 CB CYS A 28 3851 4130 3550 -1270 -352 -212 C ATOM 226 SG CYS A 28 -32.630 -16.164 15.137 1.00 32.69 S ANISOU 226 SG CYS A 28 4121 4495 3806 -1104 -260 -150 S ATOM 227 N ATRP A 29 -34.535 -19.396 12.006 0.43 35.77 N ANISOU 227 N ATRP A 29 4734 4629 4228 -1477 -555 -389 N ATOM 228 N BTRP A 29 -34.508 -19.401 11.995 0.57 35.79 N ANISOU 228 N BTRP A 29 4741 4629 4229 -1474 -555 -389 N ATOM 229 CA ATRP A 29 -35.460 -20.389 11.466 0.43 37.38 C ANISOU 229 CA ATRP A 29 4961 4765 4477 -1639 -648 -448 C ATOM 230 CA BTRP A 29 -35.452 -20.356 11.423 0.57 37.18 C ANISOU 230 CA BTRP A 29 4936 4743 4448 -1635 -651 -450 C ATOM 231 C ATRP A 29 -34.765 -21.728 11.252 0.43 37.86 C ANISOU 231 C ATRP A 29 5226 4632 4528 -1666 -634 -491 C ATOM 232 C BTRP A 29 -34.786 -21.708 11.186 0.57 37.91 C ANISOU 232 C BTRP A 29 5232 4641 4531 -1666 -639 -495 C ATOM 233 O ATRP A 29 -35.353 -22.787 11.498 0.43 39.11 O ANISOU 233 O ATRP A 29 5412 4689 4757 -1813 -654 -496 O ATOM 234 O BTRP A 29 -35.411 -22.759 11.375 0.57 39.58 O ANISOU 234 O BTRP A 29 5470 4755 4814 -1816 -666 -505 O ATOM 235 CB ATRP A 29 -36.075 -19.898 10.154 0.43 40.74 C ANISOU 235 CB ATRP A 29 5361 5267 4853 -1652 -787 -528 C ATOM 236 CB BTRP A 29 -36.018 -19.774 10.124 0.57 40.47 C ANISOU 236 CB BTRP A 29 5324 5243 4810 -1637 -786 -527 C ATOM 237 CG ATRP A 29 -37.349 -19.109 10.304 0.43 44.75 C ANISOU 237 CG ATRP A 29 5648 5927 5427 -1709 -853 -505 C ATOM 238 CG BTRP A 29 -37.267 -20.410 9.561 0.57 45.74 C ANISOU 238 CG BTRP A 29 5945 5902 5534 -1808 -917 -587 C ATOM 239 CD1ATRP A 29 -37.505 -17.769 10.117 0.43 45.43 C ANISOU 239 CD1ATRP A 29 5621 6154 5485 -1606 -881 -484 C ATOM 240 CD1BTRP A 29 -37.490 -20.739 8.258 0.57 47.81 C ANISOU 240 CD1BTRP A 29 6307 6129 5731 -1851 -1051 -687 C ATOM 241 CD2ATRP A 29 -38.645 -19.616 10.654 0.43 49.11 C ANISOU 241 CD2ATRP A 29 6060 6503 6097 -1880 -899 -502 C ATOM 242 CD2BTRP A 29 -38.470 -20.757 10.269 0.57 50.17 C ANISOU 242 CD2BTRP A 29 6342 6497 6224 -1965 -928 -553 C ATOM 243 NE1ATRP A 29 -38.812 -17.406 10.331 0.43 45.27 N ANISOU 243 NE1ATRP A 29 5395 6243 5562 -1686 -944 -473 N ATOM 244 NE1BTRP A 29 -38.742 -21.277 8.107 0.57 50.50 N ANISOU 244 NE1BTRP A 29 6553 6475 6159 -2025 -1161 -720 N ATOM 245 CE2ATRP A 29 -39.533 -18.521 10.665 0.43 50.17 C ANISOU 245 CE2ATRP A 29 5985 6803 6276 -1858 -951 -485 C ATOM 246 CE2BTRP A 29 -39.365 -21.301 9.326 0.57 52.44 C ANISOU 246 CE2BTRP A 29 6628 6765 6533 -2101 -1082 -638 C ATOM 247 CE3ATRP A 29 -39.140 -20.887 10.963 0.43 52.38 C ANISOU 247 CE3ATRP A 29 6502 6808 6592 -2052 -899 -512 C ATOM 248 CE3BTRP A 29 -38.873 -20.667 11.606 0.57 51.94 C ANISOU 248 CE3BTRP A 29 6422 6768 6543 -2010 -818 -462 C ATOM 249 CZ2ATRP A 29 -40.887 -18.658 10.972 0.43 53.33 C ANISOU 249 CZ2ATRP A 29 6185 7275 6802 -1998 -997 -483 C ATOM 250 CZ2BTRP A 29 -40.637 -21.755 9.677 0.57 56.82 C ANISOU 250 CZ2BTRP A 29 7024 7346 7219 -2278 -1127 -632 C ATOM 251 CZ3ATRP A 29 -40.484 -21.021 11.268 0.43 54.47 C ANISOU 251 CZ3ATRP A 29 6575 7143 6977 -2207 -941 -504 C ATOM 252 CZ3BTRP A 29 -40.137 -21.119 11.952 0.57 53.84 C ANISOU 252 CZ3BTRP A 29 6513 7039 6903 -2189 -848 -455 C ATOM 253 CH2ATRP A 29 -41.341 -19.913 11.270 0.43 54.48 C ANISOU 253 CH2ATRP A 29 6351 7324 7025 -2177 -987 -492 C ATOM 254 CH2BTRP A 29 -41.003 -21.656 10.991 0.57 56.29 C ANISOU 254 CH2BTRP A 29 6807 7329 7250 -2325 -1003 -540 C ATOM 255 N ALA A 30 -33.508 -21.700 10.796 1.00 37.51 N ANISOU 255 N ALA A 30 5321 4527 4402 -1526 -594 -524 N ATOM 256 CA ALA A 30 -32.788 -22.946 10.548 1.00 36.47 C ANISOU 256 CA ALA A 30 5383 4205 4268 -1527 -578 -576 C ATOM 257 C ALA A 30 -32.566 -23.730 11.837 1.00 36.75 C ANISOU 257 C ALA A 30 5442 4132 4389 -1560 -499 -489 C ATOM 258 O ALA A 30 -32.772 -24.950 11.872 1.00 35.73 O ANISOU 258 O ALA A 30 5421 3843 4311 -1663 -521 -512 O ATOM 259 CB ALA A 30 -31.453 -22.654 9.863 1.00 32.70 C ANISOU 259 CB ALA A 30 5022 3706 3697 -1355 -531 -628 C ATOM 260 N VAL A 31 -32.144 -23.051 12.907 1.00 35.52 N ANISOU 260 N VAL A 31 5200 4052 4244 -1478 -413 -388 N ATOM 261 CA VAL A 31 -31.944 -23.743 14.177 1.00 35.30 C ANISOU 261 CA VAL A 31 5205 3929 4277 -1510 -345 -293 C ATOM 262 C VAL A 31 -33.274 -24.252 14.720 1.00 37.25 C ANISOU 262 C VAL A 31 5378 4175 4600 -1710 -363 -251 C ATOM 263 O VAL A 31 -33.357 -25.363 15.257 1.00 37.83 O ANISOU 263 O VAL A 31 5548 4099 4728 -1804 -348 -212 O ATOM 264 CB VAL A 31 -31.229 -22.824 15.183 1.00 32.77 C ANISOU 264 CB VAL A 31 4811 3705 3935 -1381 -261 -201 C ATOM 265 CG1 VAL A 31 -31.132 -23.504 16.549 1.00 33.49 C ANISOU 265 CG1 VAL A 31 4943 3710 4073 -1426 -203 -92 C ATOM 266 CG2 VAL A 31 -29.836 -22.463 14.672 1.00 27.60 C ANISOU 266 CG2 VAL A 31 4229 3033 3226 -1197 -239 -242 C ATOM 267 N TRP A 32 -34.339 -23.463 14.567 1.00 39.09 N ANISOU 267 N TRP A 32 5437 4569 4845 -1780 -396 -257 N ATOM 268 CA TRP A 32 -35.651 -23.892 15.040 1.00 43.11 C ANISOU 268 CA TRP A 32 5844 5097 5439 -1976 -405 -224 C ATOM 269 C TRP A 32 -36.104 -25.170 14.343 1.00 48.32 C ANISOU 269 C TRP A 32 6617 5598 6146 -2127 -488 -294 C ATOM 270 O TRP A 32 -36.729 -26.037 14.965 1.00 46.67 O ANISOU 270 O TRP A 32 6415 5305 6013 -2290 -467 -246 O ATOM 271 CB TRP A 32 -36.675 -22.776 14.827 1.00 44.33 C ANISOU 271 CB TRP A 32 5778 5456 5610 -2000 -441 -238 C ATOM 272 CG TRP A 32 -38.071 -23.145 15.256 1.00 55.74 C ANISOU 272 CG TRP A 32 7079 6943 7157 -2201 -445 -214 C ATOM 273 CD1 TRP A 32 -38.972 -23.912 14.565 1.00 58.53 C ANISOU 273 CD1 TRP A 32 7422 7243 7575 -2371 -545 -279 C ATOM 274 CD2 TRP A 32 -38.726 -22.757 16.470 1.00 60.96 C ANISOU 274 CD2 TRP A 32 7581 7713 7870 -2259 -340 -123 C ATOM 275 NE1 TRP A 32 -40.139 -24.029 15.280 1.00 61.99 N ANISOU 275 NE1 TRP A 32 7688 7752 8114 -2535 -505 -229 N ATOM 276 CE2 TRP A 32 -40.015 -23.329 16.452 1.00 64.84 C ANISOU 276 CE2 TRP A 32 7957 8216 8465 -2468 -371 -135 C ATOM 277 CE3 TRP A 32 -38.346 -21.984 17.573 1.00 59.50 C ANISOU 277 CE3 TRP A 32 7341 7618 7650 -2159 -221 -40 C ATOM 278 CZ2 TRP A 32 -40.927 -23.149 17.493 1.00 67.82 C ANISOU 278 CZ2 TRP A 32 8158 8697 8913 -2576 -269 -64 C ATOM 279 CZ3 TRP A 32 -39.253 -21.808 18.607 1.00 61.61 C ANISOU 279 CZ3 TRP A 32 7452 7984 7973 -2261 -125 26 C ATOM 280 CH2 TRP A 32 -40.528 -22.387 18.559 1.00 65.39 C ANISOU 280 CH2 TRP A 32 7810 8478 8556 -2466 -141 15 C ATOM 281 N LEU A 33 -35.788 -25.311 13.057 1.00 51.23 N ANISOU 281 N LEU A 33 7087 5917 6462 -2081 -580 -409 N ATOM 282 CA LEU A 33 -36.346 -26.390 12.250 1.00 52.94 C ANISOU 282 CA LEU A 33 7401 6000 6713 -2230 -680 -500 C ATOM 283 C LEU A 33 -35.489 -27.649 12.223 1.00 51.89 C ANISOU 283 C LEU A 33 7506 5626 6585 -2215 -662 -525 C ATOM 284 O LEU A 33 -36.029 -28.742 12.030 1.00 54.48 O ANISOU 284 O LEU A 33 7919 5806 6974 -2376 -718 -563 O ATOM 285 CB LEU A 33 -36.564 -25.913 10.811 1.00 57.49 C ANISOU 285 CB LEU A 33 7976 6649 7217 -2201 -803 -623 C ATOM 286 CG LEU A 33 -37.674 -24.893 10.546 1.00 64.39 C ANISOU 286 CG LEU A 33 8628 7730 8106 -2251 -878 -624 C ATOM 287 CD1 LEU A 33 -37.632 -24.436 9.096 1.00 66.92 C ANISOU 287 CD1 LEU A 33 9001 8101 8324 -2191 -1002 -736 C ATOM 288 CD2 LEU A 33 -39.037 -25.474 10.886 1.00 64.62 C ANISOU 288 CD2 LEU A 33 8531 7761 8262 -2478 -927 -611 C ATOM 289 N ASN A 34 -34.174 -27.536 12.396 1.00 46.71 N ANISOU 289 N ASN A 34 6955 4918 5874 -2028 -590 -509 N ATOM 290 CA ASN A 34 -33.263 -28.663 12.215 1.00 46.03 C ANISOU 290 CA ASN A 34 7092 4603 5794 -1975 -581 -552 C ATOM 291 C ASN A 34 -32.726 -29.103 13.573 1.00 45.15 C ANISOU 291 C ASN A 34 7023 4397 5736 -1945 -491 -420 C ATOM 292 O ASN A 34 -31.974 -28.363 14.219 1.00 40.46 O ANISOU 292 O ASN A 34 6374 3891 5109 -1799 -418 -346 O ATOM 293 CB ASN A 34 -32.123 -28.292 11.270 1.00 43.95 C ANISOU 293 CB ASN A 34 6920 4343 5436 -1779 -572 -648 C ATOM 294 CG ASN A 34 -31.327 -29.500 10.815 1.00 48.20 C ANISOU 294 CG ASN A 34 7684 4644 5985 -1729 -575 -733 C ATOM 295 OD1 ASN A 34 -31.428 -30.583 11.394 1.00 49.94 O ANISOU 295 OD1 ASN A 34 8006 4682 6289 -1812 -576 -696 O ATOM 296 ND2 ASN A 34 -30.527 -29.319 9.774 1.00 49.75 N ANISOU 296 ND2 ASN A 34 7968 4838 6097 -1592 -571 -848 N ATOM 297 N SER A 35 -33.089 -30.322 13.987 1.00 44.44 N ANISOU 297 N SER A 35 7044 4117 5724 -2086 -504 -389 N ATOM 298 CA SER A 35 -32.612 -30.842 15.266 1.00 45.43 C ANISOU 298 CA SER A 35 7239 4130 5890 -2069 -433 -254 C ATOM 299 C SER A 35 -31.103 -31.055 15.260 1.00 49.24 C ANISOU 299 C SER A 35 7862 4499 6349 -1845 -405 -266 C ATOM 300 O SER A 35 -30.460 -30.924 16.308 1.00 50.53 O ANISOU 300 O SER A 35 8028 4658 6513 -1754 -347 -150 O ATOM 301 CB SER A 35 -33.333 -32.148 15.612 1.00 49.41 C ANISOU 301 CB SER A 35 7855 4436 6484 -2278 -460 -219 C ATOM 302 OG SER A 35 -32.935 -33.196 14.748 1.00 53.36 O ANISOU 302 OG SER A 35 8556 4711 7008 -2268 -526 -333 O ATOM 303 N ASN A 36 -30.518 -31.369 14.098 1.00 47.43 N ANISOU 303 N ASN A 36 7744 4182 6097 -1752 -445 -409 N ATOM 304 CA ASN A 36 -29.065 -31.464 13.991 1.00 49.88 C ANISOU 304 CA ASN A 36 8152 4410 6391 -1525 -407 -438 C ATOM 305 C ASN A 36 -28.362 -30.140 14.268 1.00 49.75 C ANISOU 305 C ASN A 36 7988 4603 6313 -1360 -346 -394 C ATOM 306 O ASN A 36 -27.149 -30.140 14.504 1.00 52.09 O ANISOU 306 O ASN A 36 8327 4851 6614 -1178 -306 -381 O ATOM 307 CB ASN A 36 -28.661 -31.958 12.603 1.00 52.32 C ANISOU 307 CB ASN A 36 8594 4613 6674 -1463 -444 -616 C ATOM 308 CG ASN A 36 -29.171 -33.351 12.305 1.00 56.60 C ANISOU 308 CG ASN A 36 9314 4910 7282 -1605 -509 -676 C ATOM 309 OD1 ASN A 36 -29.468 -34.126 13.213 1.00 56.30 O ANISOU 309 OD1 ASN A 36 9337 4729 7324 -1706 -515 -573 O ATOM 310 ND2 ASN A 36 -29.271 -33.678 11.024 1.00 58.38 N ANISOU 310 ND2 ASN A 36 9635 5080 7467 -1620 -560 -844 N ATOM 311 N LEU A 37 -29.079 -29.021 14.228 1.00 46.14 N ANISOU 311 N LEU A 37 7356 4369 5806 -1416 -343 -375 N ATOM 312 CA LEU A 37 -28.513 -27.719 14.546 1.00 43.52 C ANISOU 312 CA LEU A 37 6886 4230 5421 -1279 -289 -328 C ATOM 313 C LEU A 37 -28.802 -27.285 15.976 1.00 43.70 C ANISOU 313 C LEU A 37 6807 4337 5460 -1318 -246 -176 C ATOM 314 O LEU A 37 -28.342 -26.218 16.391 1.00 37.85 O ANISOU 314 O LEU A 37 5957 3745 4679 -1212 -205 -131 O ATOM 315 CB LEU A 37 -29.039 -26.661 13.570 1.00 41.24 C ANISOU 315 CB LEU A 37 6480 4128 5060 -1292 -315 -405 C ATOM 316 CG LEU A 37 -28.498 -26.710 12.138 1.00 43.31 C ANISOU 316 CG LEU A 37 6834 4361 5261 -1209 -336 -552 C ATOM 317 CD1 LEU A 37 -29.225 -25.709 11.253 1.00 40.23 C ANISOU 317 CD1 LEU A 37 6341 4151 4795 -1253 -382 -606 C ATOM 318 CD2 LEU A 37 -26.996 -26.452 12.122 1.00 36.26 C ANISOU 318 CD2 LEU A 37 5975 3454 4349 -999 -263 -562 C ATOM 319 N GLN A 38 -29.542 -28.081 16.740 1.00 45.76 N ANISOU 319 N GLN A 38 7109 4505 5774 -1472 -251 -97 N ATOM 320 CA GLN A 38 -29.961 -27.701 18.087 1.00 44.18 C ANISOU 320 CA GLN A 38 6821 4392 5572 -1533 -199 44 C ATOM 321 C GLN A 38 -28.954 -28.250 19.092 1.00 44.20 C ANISOU 321 C GLN A 38 6944 4263 5586 -1434 -176 144 C ATOM 322 O GLN A 38 -29.019 -29.414 19.491 1.00 48.52 O ANISOU 322 O GLN A 38 7635 4618 6182 -1509 -192 194 O ATOM 323 CB GLN A 38 -31.381 -28.182 18.357 1.00 40.94 C ANISOU 323 CB GLN A 38 6374 3976 5207 -1769 -204 79 C ATOM 324 CG GLN A 38 -32.403 -27.377 17.580 1.00 43.14 C ANISOU 324 CG GLN A 38 6484 4432 5476 -1849 -232 1 C ATOM 325 CD GLN A 38 -33.778 -27.996 17.590 1.00 50.22 C ANISOU 325 CD GLN A 38 7339 5304 6439 -2087 -256 5 C ATOM 326 OE1 GLN A 38 -34.028 -28.970 18.295 1.00 52.62 O ANISOU 326 OE1 GLN A 38 7735 5467 6791 -2209 -232 82 O ATOM 327 NE2 GLN A 38 -34.682 -27.434 16.798 1.00 50.55 N ANISOU 327 NE2 GLN A 38 7239 5480 6487 -2158 -307 -74 N ATOM 328 N ASN A 39 -28.020 -27.393 19.490 1.00 46.38 N ANISOU 328 N ASN A 39 7162 4640 5819 -1267 -148 175 N ATOM 329 CA ASN A 39 -26.968 -27.714 20.441 1.00 42.03 C ANISOU 329 CA ASN A 39 6700 3997 5274 -1147 -143 267 C ATOM 330 C ASN A 39 -26.558 -26.408 21.101 1.00 40.74 C ANISOU 330 C ASN A 39 6401 4029 5049 -1049 -106 318 C ATOM 331 O ASN A 39 -26.896 -25.326 20.616 1.00 40.39 O ANISOU 331 O ASN A 39 6216 4163 4969 -1043 -86 261 O ATOM 332 CB ASN A 39 -25.774 -28.386 19.757 1.00 44.38 C ANISOU 332 CB ASN A 39 7115 4130 5616 -987 -179 191 C ATOM 333 CG ASN A 39 -25.306 -27.622 18.523 1.00 44.68 C ANISOU 333 CG ASN A 39 7072 4274 5630 -876 -170 54 C ATOM 334 OD1 ASN A 39 -24.829 -26.493 18.624 1.00 43.04 O ANISOU 334 OD1 ASN A 39 6742 4230 5380 -778 -142 59 O ATOM 335 ND2 ASN A 39 -25.438 -28.241 17.354 1.00 45.44 N ANISOU 335 ND2 ASN A 39 7247 4271 5746 -898 -194 -69 N ATOM 336 N VAL A 40 -25.805 -26.521 22.199 1.00 39.65 N ANISOU 336 N VAL A 40 6317 3848 4898 -968 -109 423 N ATOM 337 CA VAL A 40 -25.483 -25.348 23.012 1.00 37.48 C ANISOU 337 CA VAL A 40 5933 3748 4559 -897 -81 480 C ATOM 338 C VAL A 40 -24.758 -24.290 22.188 1.00 39.11 C ANISOU 338 C VAL A 40 6024 4077 4757 -755 -79 381 C ATOM 339 O VAL A 40 -25.041 -23.090 22.308 1.00 41.32 O ANISOU 339 O VAL A 40 6172 4539 4989 -754 -47 375 O ATOM 340 CB VAL A 40 -24.661 -25.758 24.246 1.00 37.26 C ANISOU 340 CB VAL A 40 6007 3633 4516 -823 -109 601 C ATOM 341 CG1 VAL A 40 -24.043 -24.530 24.883 1.00 37.84 C ANISOU 341 CG1 VAL A 40 5974 3873 4529 -716 -100 628 C ATOM 342 CG2 VAL A 40 -25.546 -26.491 25.241 1.00 37.16 C ANISOU 342 CG2 VAL A 40 6092 3551 4477 -990 -88 723 C ATOM 343 N THR A 41 -23.805 -24.711 21.352 1.00 35.65 N ANISOU 343 N THR A 41 5638 3539 4368 -633 -105 303 N ATOM 344 CA THR A 41 -23.091 -23.759 20.506 1.00 35.92 C ANISOU 344 CA THR A 41 5571 3683 4393 -510 -89 211 C ATOM 345 C THR A 41 -24.062 -22.902 19.703 1.00 36.43 C ANISOU 345 C THR A 41 5532 3896 4414 -597 -64 144 C ATOM 346 O THR A 41 -23.908 -21.677 19.620 1.00 33.24 O ANISOU 346 O THR A 41 5009 3648 3971 -548 -42 131 O ATOM 347 CB THR A 41 -22.142 -24.499 19.560 1.00 41.96 C ANISOU 347 CB THR A 41 6414 4310 5217 -393 -101 118 C ATOM 348 OG1 THR A 41 -21.637 -25.678 20.204 1.00 47.15 O ANISOU 348 OG1 THR A 41 7203 4777 5935 -352 -142 178 O ATOM 349 CG2 THR A 41 -20.981 -23.604 19.171 1.00 40.06 C ANISOU 349 CG2 THR A 41 6076 4166 4977 -234 -76 69 C ATOM 350 N ASN A 42 -25.089 -23.526 19.127 1.00 34.44 N ANISOU 350 N ASN A 42 5322 3591 4172 -731 -77 104 N ATOM 351 CA ASN A 42 -25.998 -22.795 18.259 1.00 33.14 C ANISOU 351 CA ASN A 42 5063 3556 3973 -806 -76 34 C ATOM 352 C ASN A 42 -27.077 -22.036 19.021 1.00 30.44 C ANISOU 352 C ASN A 42 4601 3359 3605 -911 -56 101 C ATOM 353 O ASN A 42 -27.770 -21.211 18.420 1.00 29.76 O ANISOU 353 O ASN A 42 4410 3401 3495 -947 -61 54 O ATOM 354 CB ASN A 42 -26.628 -23.749 17.245 1.00 30.79 C ANISOU 354 CB ASN A 42 4853 3147 3699 -904 -114 -51 C ATOM 355 CG ASN A 42 -25.649 -24.162 16.162 1.00 34.44 C ANISOU 355 CG ASN A 42 5408 3513 4163 -787 -120 -157 C ATOM 356 OD1 ASN A 42 -24.606 -23.530 15.985 1.00 36.60 O ANISOU 356 OD1 ASN A 42 5645 3841 4419 -642 -88 -176 O ATOM 357 ND2 ASN A 42 -25.981 -25.215 15.427 1.00 33.29 N ANISOU 357 ND2 ASN A 42 5381 3226 4040 -855 -155 -232 N ATOM 358 N TYR A 43 -27.247 -22.289 20.317 1.00 30.47 N ANISOU 358 N TYR A 43 4621 3346 3610 -957 -32 208 N ATOM 359 CA TYR A 43 -28.092 -21.397 21.102 1.00 30.73 C ANISOU 359 CA TYR A 43 4531 3536 3609 -1024 10 262 C ATOM 360 C TYR A 43 -27.430 -20.037 21.267 1.00 27.89 C ANISOU 360 C TYR A 43 4076 3316 3207 -893 26 257 C ATOM 361 O TYR A 43 -28.106 -19.004 21.241 1.00 27.41 O ANISOU 361 O TYR A 43 3890 3402 3124 -915 46 241 O ATOM 362 CB TYR A 43 -28.405 -22.023 22.458 1.00 31.01 C ANISOU 362 CB TYR A 43 4627 3520 3637 -1110 44 379 C ATOM 363 CG TYR A 43 -29.089 -23.361 22.313 1.00 38.84 C ANISOU 363 CG TYR A 43 5717 4362 4678 -1258 30 392 C ATOM 364 CD1 TYR A 43 -29.890 -23.628 21.207 1.00 41.49 C ANISOU 364 CD1 TYR A 43 6020 4688 5056 -1351 -1 302 C ATOM 365 CD2 TYR A 43 -28.918 -24.361 23.256 1.00 38.76 C ANISOU 365 CD2 TYR A 43 5843 4213 4671 -1306 38 494 C ATOM 366 CE1 TYR A 43 -30.510 -24.850 21.050 1.00 39.92 C ANISOU 366 CE1 TYR A 43 5913 4344 4910 -1497 -21 307 C ATOM 367 CE2 TYR A 43 -29.541 -25.590 23.111 1.00 43.66 C ANISOU 367 CE2 TYR A 43 6564 4681 5344 -1452 25 508 C ATOM 368 CZ TYR A 43 -30.336 -25.826 22.005 1.00 45.75 C ANISOU 368 CZ TYR A 43 6785 4938 5659 -1550 -4 410 C ATOM 369 OH TYR A 43 -30.959 -27.044 21.846 1.00 54.91 O ANISOU 369 OH TYR A 43 8046 5939 6878 -1706 -24 417 O ATOM 370 N PHE A 44 -26.105 -20.022 21.435 1.00 24.41 N ANISOU 370 N PHE A 44 3688 2824 2762 -756 14 267 N ATOM 371 CA PHE A 44 -25.373 -18.760 21.444 1.00 26.34 C ANISOU 371 CA PHE A 44 3845 3186 2977 -638 22 250 C ATOM 372 C PHE A 44 -25.336 -18.125 20.060 1.00 26.40 C ANISOU 372 C PHE A 44 3796 3250 2984 -600 14 152 C ATOM 373 O PHE A 44 -25.338 -16.893 19.947 1.00 25.18 O ANISOU 373 O PHE A 44 3544 3221 2801 -560 26 137 O ATOM 374 CB PHE A 44 -23.959 -18.981 21.976 1.00 28.93 C ANISOU 374 CB PHE A 44 4232 3444 3318 -510 3 286 C ATOM 375 CG PHE A 44 -23.921 -19.345 23.433 1.00 31.48 C ANISOU 375 CG PHE A 44 4612 3735 3615 -534 -1 394 C ATOM 376 CD1 PHE A 44 -24.218 -18.391 24.400 1.00 35.50 C ANISOU 376 CD1 PHE A 44 5054 4371 4063 -549 25 442 C ATOM 377 CD2 PHE A 44 -23.610 -20.630 23.835 1.00 31.45 C ANISOU 377 CD2 PHE A 44 4741 3570 3641 -540 -31 449 C ATOM 378 CE1 PHE A 44 -24.196 -18.720 25.745 1.00 34.21 C ANISOU 378 CE1 PHE A 44 4961 4184 3852 -576 24 542 C ATOM 379 CE2 PHE A 44 -23.583 -20.969 25.181 1.00 34.26 C ANISOU 379 CE2 PHE A 44 5168 3893 3955 -566 -41 560 C ATOM 380 CZ PHE A 44 -23.876 -20.015 26.136 1.00 33.79 C ANISOU 380 CZ PHE A 44 5047 3972 3819 -587 -11 607 C ATOM 381 N VAL A 45 -25.298 -18.943 19.004 1.00 25.15 N ANISOU 381 N VAL A 45 3711 2995 2850 -613 -7 84 N ATOM 382 CA VAL A 45 -25.418 -18.425 17.644 1.00 25.71 C ANISOU 382 CA VAL A 45 3752 3120 2898 -598 -18 -7 C ATOM 383 C VAL A 45 -26.748 -17.698 17.470 1.00 23.76 C ANISOU 383 C VAL A 45 3405 2993 2630 -695 -33 -12 C ATOM 384 O VAL A 45 -26.806 -16.603 16.895 1.00 23.24 O ANISOU 384 O VAL A 45 3265 3034 2531 -655 -38 -43 O ATOM 385 CB VAL A 45 -25.253 -19.572 16.627 1.00 28.96 C ANISOU 385 CB VAL A 45 4282 3394 3326 -609 -39 -84 C ATOM 386 CG1 VAL A 45 -25.796 -19.177 15.254 1.00 26.55 C ANISOU 386 CG1 VAL A 45 3964 3147 2977 -643 -65 -174 C ATOM 387 CG2 VAL A 45 -23.789 -19.982 16.528 1.00 29.61 C ANISOU 387 CG2 VAL A 45 4432 3385 3435 -472 -16 -104 C ATOM 388 N VAL A 46 -27.834 -18.287 17.981 1.00 26.71 N ANISOU 388 N VAL A 46 3770 3350 3029 -822 -40 21 N ATOM 389 CA VAL A 46 -29.148 -17.658 17.881 1.00 26.10 C ANISOU 389 CA VAL A 46 3574 3389 2952 -913 -54 14 C ATOM 390 C VAL A 46 -29.202 -16.377 18.708 1.00 24.63 C ANISOU 390 C VAL A 46 3273 3338 2745 -860 -15 60 C ATOM 391 O VAL A 46 -29.789 -15.376 18.285 1.00 25.32 O ANISOU 391 O VAL A 46 3259 3538 2825 -853 -33 32 O ATOM 392 CB VAL A 46 -30.241 -18.653 18.305 1.00 30.35 C ANISOU 392 CB VAL A 46 4120 3876 3537 -1071 -57 41 C ATOM 393 CG1 VAL A 46 -31.565 -17.926 18.555 1.00 31.67 C ANISOU 393 CG1 VAL A 46 4127 4183 3722 -1155 -50 49 C ATOM 394 CG2 VAL A 46 -30.413 -19.727 17.244 1.00 30.56 C ANISOU 394 CG2 VAL A 46 4245 3781 3584 -1137 -115 -30 C ATOM 395 N SER A 47 -28.609 -16.388 19.905 1.00 24.46 N ANISOU 395 N SER A 47 3276 3304 2714 -822 30 129 N ATOM 396 CA SER A 47 -28.530 -15.160 20.691 1.00 23.22 C ANISOU 396 CA SER A 47 3031 3265 2528 -763 65 160 C ATOM 397 C SER A 47 -27.796 -14.069 19.920 1.00 23.87 C ANISOU 397 C SER A 47 3080 3400 2590 -649 44 114 C ATOM 398 O SER A 47 -28.219 -12.905 19.911 1.00 22.63 O ANISOU 398 O SER A 47 2827 3349 2422 -626 47 102 O ATOM 399 CB SER A 47 -27.839 -15.436 22.027 1.00 25.01 C ANISOU 399 CB SER A 47 3318 3454 2731 -734 100 237 C ATOM 400 OG SER A 47 -27.800 -14.262 22.818 1.00 29.50 O ANISOU 400 OG SER A 47 3813 4133 3263 -685 130 256 O ATOM 401 N LEU A 48 -26.702 -14.434 19.253 1.00 21.65 N ANISOU 401 N LEU A 48 2878 3041 2308 -579 28 86 N ATOM 402 CA LEU A 48 -25.971 -13.487 18.420 1.00 20.89 C ANISOU 402 CA LEU A 48 2760 2988 2191 -487 21 45 C ATOM 403 C LEU A 48 -26.826 -13.009 17.248 1.00 24.08 C ANISOU 403 C LEU A 48 3125 3448 2578 -524 -16 -9 C ATOM 404 O LEU A 48 -26.805 -11.822 16.893 1.00 24.89 O ANISOU 404 O LEU A 48 3170 3629 2658 -477 -23 -18 O ATOM 405 CB LEU A 48 -24.687 -14.157 17.932 1.00 23.65 C ANISOU 405 CB LEU A 48 3196 3240 2549 -415 28 20 C ATOM 406 CG LEU A 48 -23.622 -13.413 17.142 1.00 29.16 C ANISOU 406 CG LEU A 48 3885 3962 3231 -320 45 -17 C ATOM 407 CD1 LEU A 48 -23.159 -12.174 17.893 1.00 24.48 C ANISOU 407 CD1 LEU A 48 3213 3453 2635 -266 58 22 C ATOM 408 CD2 LEU A 48 -22.455 -14.367 16.873 1.00 25.70 C ANISOU 408 CD2 LEU A 48 3524 3418 2822 -254 65 -42 C ATOM 409 N ALA A 49 -27.582 -13.920 16.632 1.00 24.28 N ANISOU 409 N ALA A 49 3188 3425 2613 -609 -50 -42 N ATOM 410 CA ALA A 49 -28.437 -13.535 15.513 1.00 22.94 C ANISOU 410 CA ALA A 49 2986 3306 2423 -649 -108 -93 C ATOM 411 C ALA A 49 -29.565 -12.618 15.970 1.00 25.39 C ANISOU 411 C ALA A 49 3163 3730 2755 -680 -124 -69 C ATOM 412 O ALA A 49 -29.989 -11.727 15.223 1.00 23.83 O ANISOU 412 O ALA A 49 2915 3602 2539 -659 -172 -93 O ATOM 413 CB ALA A 49 -29.001 -14.780 14.831 1.00 22.63 C ANISOU 413 CB ALA A 49 3019 3184 2394 -744 -152 -140 C ATOM 414 N ALA A 50 -30.081 -12.837 17.186 1.00 22.03 N ANISOU 414 N ALA A 50 2681 3322 2368 -730 -82 -22 N ATOM 415 CA ALA A 50 -31.101 -11.946 17.737 1.00 24.27 C ANISOU 415 CA ALA A 50 2827 3718 2678 -747 -75 -7 C ATOM 416 C ALA A 50 -30.552 -10.541 17.955 1.00 21.15 C ANISOU 416 C ALA A 50 2391 3388 2257 -634 -59 3 C ATOM 417 O ALA A 50 -31.252 -9.553 17.711 1.00 23.59 O ANISOU 417 O ALA A 50 2606 3777 2580 -611 -89 -12 O ATOM 418 CB ALA A 50 -31.649 -12.503 19.052 1.00 22.34 C ANISOU 418 CB ALA A 50 2547 3478 2463 -824 -8 41 C ATOM 419 N ALA A 51 -29.315 -10.430 18.450 1.00 22.21 N ANISOU 419 N ALA A 51 2592 3483 2363 -563 -18 28 N ATOM 420 CA ALA A 51 -28.689 -9.116 18.572 1.00 24.65 C ANISOU 420 CA ALA A 51 2875 3840 2652 -467 -10 32 C ATOM 421 C ALA A 51 -28.588 -8.434 17.215 1.00 24.45 C ANISOU 421 C ALA A 51 2858 3827 2605 -427 -64 -3 C ATOM 422 O ALA A 51 -28.804 -7.222 17.102 1.00 24.20 O ANISOU 422 O ALA A 51 2771 3852 2573 -379 -82 -3 O ATOM 423 CB ALA A 51 -27.305 -9.241 19.209 1.00 23.12 C ANISOU 423 CB ALA A 51 2748 3597 2440 -408 27 59 C ATOM 424 N ASP A 52 -28.272 -9.201 16.170 1.00 19.80 N ANISOU 424 N ASP A 52 2350 3179 1993 -448 -91 -32 N ATOM 425 CA ASP A 52 -28.121 -8.621 14.839 1.00 21.87 C ANISOU 425 CA ASP A 52 2648 3452 2211 -417 -136 -61 C ATOM 426 C ASP A 52 -29.470 -8.272 14.221 1.00 23.67 C ANISOU 426 C ASP A 52 2813 3735 2445 -458 -218 -79 C ATOM 427 O ASP A 52 -29.572 -7.285 13.483 1.00 21.82 O ANISOU 427 O ASP A 52 2574 3537 2180 -416 -265 -80 O ATOM 428 CB ASP A 52 -27.329 -9.578 13.949 1.00 24.58 C ANISOU 428 CB ASP A 52 3108 3716 2515 -422 -127 -96 C ATOM 429 CG ASP A 52 -25.855 -9.618 14.319 1.00 30.11 C ANISOU 429 CG ASP A 52 3851 4374 3216 -353 -55 -83 C ATOM 430 OD1 ASP A 52 -25.350 -8.589 14.822 1.00 29.54 O ANISOU 430 OD1 ASP A 52 3732 4342 3150 -299 -31 -51 O ATOM 431 OD2 ASP A 52 -25.206 -10.669 14.115 1.00 35.70 O ANISOU 431 OD2 ASP A 52 4634 5005 3924 -352 -28 -107 O ATOM 432 N ILE A 53 -30.514 -9.049 14.520 1.00 22.25 N ANISOU 432 N ILE A 53 2581 3562 2310 -542 -241 -89 N ATOM 433 CA ILE A 53 -31.860 -8.659 14.107 1.00 22.38 C ANISOU 433 CA ILE A 53 2499 3646 2358 -578 -323 -106 C ATOM 434 C ILE A 53 -32.242 -7.324 14.736 1.00 24.14 C ANISOU 434 C ILE A 53 2609 3946 2616 -510 -314 -81 C ATOM 435 O ILE A 53 -32.798 -6.443 14.071 1.00 24.32 O ANISOU 435 O ILE A 53 2587 4012 2641 -472 -391 -88 O ATOM 436 CB ILE A 53 -32.871 -9.764 14.468 1.00 25.53 C ANISOU 436 CB ILE A 53 2843 4041 2817 -694 -332 -119 C ATOM 437 CG1 ILE A 53 -32.640 -11.007 13.606 1.00 29.28 C ANISOU 437 CG1 ILE A 53 3439 4428 3258 -763 -369 -158 C ATOM 438 CG2 ILE A 53 -34.300 -9.254 14.312 1.00 26.76 C ANISOU 438 CG2 ILE A 53 2849 4285 3035 -725 -406 -133 C ATOM 439 CD1 ILE A 53 -33.465 -12.207 14.043 1.00 31.87 C ANISOU 439 CD1 ILE A 53 3736 4725 3650 -891 -369 -165 C ATOM 440 N LEU A 54 -31.943 -7.147 16.027 1.00 20.57 N ANISOU 440 N LEU A 54 2123 3506 2189 -488 -224 -53 N ATOM 441 CA LEU A 54 -32.252 -5.889 16.699 1.00 20.30 C ANISOU 441 CA LEU A 54 1995 3534 2184 -418 -205 -43 C ATOM 442 C LEU A 54 -31.381 -4.735 16.217 1.00 21.65 C ANISOU 442 C LEU A 54 2223 3689 2314 -323 -225 -33 C ATOM 443 O LEU A 54 -31.769 -3.576 16.378 1.00 23.14 O ANISOU 443 O LEU A 54 2347 3917 2530 -260 -244 -32 O ATOM 444 CB LEU A 54 -32.115 -6.061 18.211 1.00 21.17 C ANISOU 444 CB LEU A 54 2077 3657 2310 -427 -104 -21 C ATOM 445 CG LEU A 54 -33.111 -7.046 18.830 1.00 28.86 C ANISOU 445 CG LEU A 54 2982 4656 3327 -530 -67 -21 C ATOM 446 CD1 LEU A 54 -32.799 -7.271 20.303 1.00 32.08 C ANISOU 446 CD1 LEU A 54 3402 5067 3718 -542 38 11 C ATOM 447 CD2 LEU A 54 -34.534 -6.539 18.650 1.00 30.56 C ANISOU 447 CD2 LEU A 54 3041 4956 3614 -542 -105 -49 C ATOM 448 N VAL A 55 -30.209 -5.013 15.642 1.00 21.13 N ANISOU 448 N VAL A 55 2275 3563 2191 -312 -214 -26 N ATOM 449 CA VAL A 55 -29.473 -3.949 14.968 1.00 19.44 C ANISOU 449 CA VAL A 55 2115 3335 1937 -243 -234 -14 C ATOM 450 C VAL A 55 -30.284 -3.416 13.793 1.00 21.66 C ANISOU 450 C VAL A 55 2390 3638 2201 -236 -336 -21 C ATOM 451 O VAL A 55 -30.384 -2.201 13.590 1.00 23.51 O ANISOU 451 O VAL A 55 2610 3885 2439 -174 -373 -3 O ATOM 452 CB VAL A 55 -28.083 -4.446 14.529 1.00 23.39 C ANISOU 452 CB VAL A 55 2727 3775 2383 -241 -188 -11 C ATOM 453 CG1 VAL A 55 -27.457 -3.471 13.529 1.00 19.08 C ANISOU 453 CG1 VAL A 55 2245 3218 1786 -197 -208 3 C ATOM 454 CG2 VAL A 55 -27.174 -4.600 15.753 1.00 18.85 C ANISOU 454 CG2 VAL A 55 2148 3182 1832 -221 -109 6 C ATOM 455 N GLY A 56 -30.914 -4.312 13.031 1.00 22.18 N ANISOU 455 N GLY A 56 2471 3705 2252 -299 -395 -46 N ATOM 456 CA GLY A 56 -31.708 -3.867 11.896 1.00 18.38 C ANISOU 456 CA GLY A 56 1990 3247 1747 -294 -515 -52 C ATOM 457 C GLY A 56 -33.010 -3.211 12.314 1.00 25.35 C ANISOU 457 C GLY A 56 2722 4193 2718 -270 -576 -53 C ATOM 458 O GLY A 56 -33.421 -2.202 11.736 1.00 25.00 O ANISOU 458 O GLY A 56 2663 4163 2672 -211 -663 -38 O ATOM 459 N VAL A 57 -33.667 -3.760 13.334 1.00 22.22 N ANISOU 459 N VAL A 57 2212 3832 2400 -313 -528 -70 N ATOM 460 CA VAL A 57 -34.984 -3.264 13.720 1.00 26.93 C ANISOU 460 CA VAL A 57 2641 4498 3092 -295 -572 -83 C ATOM 461 C VAL A 57 -34.880 -1.995 14.568 1.00 24.56 C ANISOU 461 C VAL A 57 2285 4216 2832 -194 -521 -70 C ATOM 462 O VAL A 57 -35.719 -1.093 14.455 1.00 27.00 O ANISOU 462 O VAL A 57 2495 4561 3201 -129 -588 -76 O ATOM 463 CB VAL A 57 -35.763 -4.380 14.443 1.00 30.70 C ANISOU 463 CB VAL A 57 3018 5011 3636 -396 -525 -106 C ATOM 464 CG1 VAL A 57 -37.057 -3.837 15.055 1.00 33.83 C ANISOU 464 CG1 VAL A 57 3218 5492 4145 -375 -531 -123 C ATOM 465 CG2 VAL A 57 -36.070 -5.513 13.473 1.00 28.79 C ANISOU 465 CG2 VAL A 57 2824 4745 3369 -496 -606 -129 C ATOM 466 N LEU A 58 -33.866 -1.892 15.426 1.00 22.52 N ANISOU 466 N LEU A 58 2087 3925 2543 -176 -413 -55 N ATOM 467 CA LEU A 58 -33.809 -0.793 16.386 1.00 25.35 C ANISOU 467 CA LEU A 58 2395 4298 2938 -93 -359 -57 C ATOM 468 C LEU A 58 -32.551 0.055 16.270 1.00 23.63 C ANISOU 468 C LEU A 58 2295 4018 2665 -33 -343 -30 C ATOM 469 O LEU A 58 -32.651 1.285 16.179 1.00 21.38 O ANISOU 469 O LEU A 58 2000 3721 2403 48 -381 -26 O ATOM 470 CB LEU A 58 -33.947 -1.335 17.823 1.00 27.24 C ANISOU 470 CB LEU A 58 2574 4573 3203 -132 -240 -70 C ATOM 471 CG LEU A 58 -35.325 -1.887 18.208 1.00 29.31 C ANISOU 471 CG LEU A 58 2685 4910 3541 -186 -226 -97 C ATOM 472 CD1 LEU A 58 -35.319 -2.436 19.627 1.00 26.90 C ANISOU 472 CD1 LEU A 58 2354 4633 3234 -234 -93 -98 C ATOM 473 CD2 LEU A 58 -36.409 -0.823 18.055 1.00 30.81 C ANISOU 473 CD2 LEU A 58 2737 5152 3817 -104 -284 -126 C ATOM 474 N ALA A 59 -31.361 -0.557 16.268 1.00 19.77 N ANISOU 474 N ALA A 59 1913 3485 2114 -71 -291 -13 N ATOM 475 CA ALA A 59 -30.141 0.244 16.343 1.00 22.27 C ANISOU 475 CA ALA A 59 2314 3752 2396 -25 -262 8 C ATOM 476 C ALA A 59 -29.968 1.123 15.111 1.00 21.47 C ANISOU 476 C ALA A 59 2278 3615 2264 12 -340 33 C ATOM 477 O ALA A 59 -29.524 2.271 15.225 1.00 21.87 O ANISOU 477 O ALA A 59 2356 3632 2321 67 -341 50 O ATOM 478 CB ALA A 59 -28.909 -0.645 16.528 1.00 19.76 C ANISOU 478 CB ALA A 59 2077 3399 2033 -69 -196 19 C ATOM 479 N ILE A 60 -30.308 0.616 13.930 1.00 21.42 N ANISOU 479 N ILE A 60 2311 3611 2217 -22 -408 39 N ATOM 480 CA ILE A 60 -30.107 1.392 12.707 1.00 22.28 C ANISOU 480 CA ILE A 60 2508 3685 2271 6 -481 73 C ATOM 481 C ILE A 60 -31.142 2.514 12.604 1.00 21.69 C ANISOU 481 C ILE A 60 2369 3620 2252 78 -576 82 C ATOM 482 O ILE A 60 -30.760 3.650 12.296 1.00 22.13 O ANISOU 482 O ILE A 60 2487 3628 2296 130 -602 118 O ATOM 483 CB ILE A 60 -30.095 0.478 11.470 1.00 25.13 C ANISOU 483 CB ILE A 60 2953 4045 2550 -54 -525 70 C ATOM 484 CG1 ILE A 60 -28.737 -0.233 11.387 1.00 23.88 C ANISOU 484 CG1 ILE A 60 2888 3853 2333 -94 -424 68 C ATOM 485 CG2 ILE A 60 -30.390 1.273 10.189 1.00 23.08 C ANISOU 485 CG2 ILE A 60 2772 3770 2229 -26 -635 106 C ATOM 486 CD1 ILE A 60 -28.646 -1.310 10.307 1.00 22.20 C ANISOU 486 CD1 ILE A 60 2765 3634 2038 -152 -442 45 C ATOM 487 N PRO A 61 -32.438 2.283 12.855 1.00 20.61 N ANISOU 487 N PRO A 61 2106 3539 2187 87 -630 51 N ATOM 488 CA PRO A 61 -33.348 3.438 12.998 1.00 22.80 C ANISOU 488 CA PRO A 61 2298 3822 2542 180 -704 51 C ATOM 489 C PRO A 61 -32.895 4.450 14.044 1.00 21.88 C ANISOU 489 C PRO A 61 2170 3672 2471 247 -629 45 C ATOM 490 O PRO A 61 -33.056 5.658 13.834 1.00 23.24 O ANISOU 490 O PRO A 61 2360 3798 2673 330 -690 64 O ATOM 491 CB PRO A 61 -34.681 2.781 13.376 1.00 25.56 C ANISOU 491 CB PRO A 61 2482 4252 2977 161 -729 5 C ATOM 492 CG PRO A 61 -34.620 1.432 12.711 1.00 23.82 C ANISOU 492 CG PRO A 61 2308 4049 2695 54 -745 0 C ATOM 493 CD PRO A 61 -33.181 1.004 12.866 1.00 19.96 C ANISOU 493 CD PRO A 61 1952 3511 2122 12 -639 16 C ATOM 494 N PHE A 62 -32.333 3.992 15.168 1.00 20.22 N ANISOU 494 N PHE A 62 1943 3475 2263 214 -508 19 N ATOM 495 CA PHE A 62 -31.814 4.923 16.168 1.00 20.02 C ANISOU 495 CA PHE A 62 1925 3415 2265 269 -445 5 C ATOM 496 C PHE A 62 -30.606 5.694 15.638 1.00 24.85 C ANISOU 496 C PHE A 62 2674 3943 2826 275 -453 50 C ATOM 497 O PHE A 62 -30.463 6.892 15.912 1.00 21.90 O ANISOU 497 O PHE A 62 2322 3514 2486 340 -466 52 O ATOM 498 CB PHE A 62 -31.421 4.181 17.450 1.00 18.43 C ANISOU 498 CB PHE A 62 1694 3250 2058 223 -327 -27 C ATOM 499 CG PHE A 62 -32.585 3.626 18.242 1.00 21.88 C ANISOU 499 CG PHE A 62 1996 3768 2551 214 -289 -70 C ATOM 500 CD1 PHE A 62 -33.900 3.875 17.874 1.00 24.43 C ANISOU 500 CD1 PHE A 62 2204 4132 2945 255 -355 -90 C ATOM 501 CD2 PHE A 62 -32.346 2.855 19.372 1.00 23.25 C ANISOU 501 CD2 PHE A 62 2155 3976 2704 163 -185 -88 C ATOM 502 CE1 PHE A 62 -34.962 3.353 18.615 1.00 28.40 C ANISOU 502 CE1 PHE A 62 2564 4717 3508 237 -303 -132 C ATOM 503 CE2 PHE A 62 -33.395 2.331 20.121 1.00 21.29 C ANISOU 503 CE2 PHE A 62 1789 3804 2498 140 -131 -122 C ATOM 504 CZ PHE A 62 -34.707 2.580 19.743 1.00 27.18 C ANISOU 504 CZ PHE A 62 2405 4598 3324 173 -182 -147 C ATOM 505 N ALA A 63 -29.705 5.015 14.911 1.00 21.29 N ANISOU 505 N ALA A 63 2314 3477 2297 206 -435 84 N ATOM 506 CA ALA A 63 -28.535 5.687 14.345 1.00 21.55 C ANISOU 506 CA ALA A 63 2467 3439 2282 197 -426 129 C ATOM 507 C ALA A 63 -28.935 6.734 13.310 1.00 24.71 C ANISOU 507 C ALA A 63 2928 3788 2673 244 -528 176 C ATOM 508 O ALA A 63 -28.323 7.806 13.229 1.00 22.52 O ANISOU 508 O ALA A 63 2722 3437 2398 265 -530 209 O ATOM 509 CB ALA A 63 -27.581 4.663 13.720 1.00 19.46 C ANISOU 509 CB ALA A 63 2273 3180 1940 119 -375 145 C ATOM 510 N ILE A 64 -29.945 6.430 12.494 1.00 21.94 N ANISOU 510 N ILE A 64 2557 3469 2309 254 -622 183 N ATOM 511 CA ILE A 64 -30.457 7.411 11.541 1.00 26.22 C ANISOU 511 CA ILE A 64 3157 3962 2841 310 -742 233 C ATOM 512 C ILE A 64 -31.034 8.613 12.281 1.00 30.26 C ANISOU 512 C ILE A 64 3606 4433 3459 412 -777 217 C ATOM 513 O ILE A 64 -30.817 9.769 11.895 1.00 27.80 O ANISOU 513 O ILE A 64 3381 4033 3149 458 -828 265 O ATOM 514 CB ILE A 64 -31.506 6.749 10.630 1.00 26.49 C ANISOU 514 CB ILE A 64 3165 4052 2850 302 -853 233 C ATOM 515 CG1 ILE A 64 -30.836 5.716 9.718 1.00 25.82 C ANISOU 515 CG1 ILE A 64 3184 3984 2642 206 -825 247 C ATOM 516 CG2 ILE A 64 -32.294 7.796 9.839 1.00 27.22 C ANISOU 516 CG2 ILE A 64 3287 4100 2955 383 -1006 280 C ATOM 517 CD1 ILE A 64 -31.825 4.836 8.956 1.00 23.69 C ANISOU 517 CD1 ILE A 64 2886 3773 2342 177 -928 227 C ATOM 518 N THR A 65 -31.763 8.355 13.368 1.00 23.95 N ANISOU 518 N THR A 65 2662 3692 2747 446 -740 148 N ATOM 519 CA THR A 65 -32.389 9.428 14.132 1.00 27.40 C ANISOU 519 CA THR A 65 3029 4097 3286 553 -759 113 C ATOM 520 C THR A 65 -31.347 10.356 14.749 1.00 24.44 C ANISOU 520 C THR A 65 2741 3633 2914 563 -695 116 C ATOM 521 O THR A 65 -31.448 11.583 14.634 1.00 28.38 O ANISOU 521 O THR A 65 3287 4040 3456 640 -754 133 O ATOM 522 CB THR A 65 -33.295 8.822 15.204 1.00 29.61 C ANISOU 522 CB THR A 65 3139 4472 3641 569 -700 34 C ATOM 523 OG1 THR A 65 -34.313 8.044 14.568 1.00 29.58 O ANISOU 523 OG1 THR A 65 3045 4543 3652 552 -774 32 O ATOM 524 CG2 THR A 65 -33.964 9.897 16.011 1.00 30.99 C ANISOU 524 CG2 THR A 65 3235 4619 3919 688 -702 -18 C ATOM 525 N ILE A 66 -30.324 9.791 15.396 1.00 25.99 N ANISOU 525 N ILE A 66 2961 3847 3067 486 -585 100 N ATOM 526 CA ILE A 66 -29.318 10.616 16.053 1.00 28.30 C ANISOU 526 CA ILE A 66 3321 4062 3368 484 -533 94 C ATOM 527 C ILE A 66 -28.327 11.239 15.082 1.00 34.85 C ANISOU 527 C ILE A 66 4292 4800 4147 442 -560 172 C ATOM 528 O ILE A 66 -27.477 12.030 15.508 1.00 38.78 O ANISOU 528 O ILE A 66 4851 5222 4662 430 -529 173 O ATOM 529 CB ILE A 66 -28.526 9.824 17.115 1.00 24.75 C ANISOU 529 CB ILE A 66 2846 3664 2894 419 -422 52 C ATOM 530 CG1 ILE A 66 -27.634 8.773 16.456 1.00 29.25 C ANISOU 530 CG1 ILE A 66 3463 4263 3386 321 -386 95 C ATOM 531 CG2 ILE A 66 -29.463 9.175 18.129 1.00 27.74 C ANISOU 531 CG2 ILE A 66 3101 4133 3306 444 -378 -17 C ATOM 532 CD1 ILE A 66 -27.047 7.767 17.458 1.00 32.57 C ANISOU 532 CD1 ILE A 66 3844 4742 3790 268 -297 58 C ATOM 533 N SER A 67 -28.385 10.888 13.798 1.00 31.52 N ANISOU 533 N SER A 67 3930 4386 3659 409 -611 236 N ATOM 534 CA SER A 67 -27.587 11.615 12.818 1.00 30.70 C ANISOU 534 CA SER A 67 3970 4193 3501 373 -634 318 C ATOM 535 C SER A 67 -28.199 12.965 12.474 1.00 32.86 C ANISOU 535 C SER A 67 4299 4363 3822 460 -741 356 C ATOM 536 O SER A 67 -27.496 13.831 11.945 1.00 30.67 O ANISOU 536 O SER A 67 4148 3985 3520 432 -752 423 O ATOM 537 CB SER A 67 -27.413 10.788 11.536 1.00 28.60 C ANISOU 537 CB SER A 67 3772 3969 3125 306 -645 371 C ATOM 538 OG SER A 67 -28.596 10.791 10.746 1.00 27.08 O ANISOU 538 OG SER A 67 3576 3792 2919 360 -769 392 O ATOM 539 N THR A 68 -29.486 13.164 12.774 1.00 31.93 N ANISOU 539 N THR A 68 4088 4265 3781 565 -818 315 N ATOM 540 CA THR A 68 -30.163 14.412 12.447 1.00 33.29 C ANISOU 540 CA THR A 68 4302 4333 4013 670 -935 347 C ATOM 541 C THR A 68 -29.924 15.510 13.474 1.00 33.14 C ANISOU 541 C THR A 68 4290 4217 4086 727 -904 300 C ATOM 542 O THR A 68 -30.173 16.678 13.169 1.00 29.15 O ANISOU 542 O THR A 68 3862 3588 3628 802 -991 337 O ATOM 543 CB THR A 68 -31.673 14.190 12.314 1.00 37.07 C ANISOU 543 CB THR A 68 4657 4875 4553 770 -1037 316 C ATOM 544 OG1 THR A 68 -32.217 13.805 13.585 1.00 34.34 O ANISOU 544 OG1 THR A 68 4149 4608 4292 810 -962 209 O ATOM 545 CG2 THR A 68 -31.967 13.113 11.288 1.00 34.85 C ANISOU 545 CG2 THR A 68 4376 4685 4182 708 -1085 353 C ATOM 546 N GLY A 69 -29.467 15.167 14.677 1.00 28.85 N ANISOU 546 N GLY A 69 3679 3718 3565 696 -793 219 N ATOM 547 CA GLY A 69 -29.346 16.160 15.726 1.00 29.07 C ANISOU 547 CA GLY A 69 3711 3660 3672 755 -769 155 C ATOM 548 C GLY A 69 -30.658 16.753 16.178 1.00 32.68 C ANISOU 548 C GLY A 69 4081 4103 4235 906 -827 90 C ATOM 549 O GLY A 69 -30.681 17.891 16.657 1.00 32.71 O ANISOU 549 O GLY A 69 4130 3988 4309 981 -848 56 O ATOM 550 N PHE A 70 -31.758 16.014 16.033 1.00 32.43 N ANISOU 550 N PHE A 70 3917 4183 4221 953 -853 67 N ATOM 551 CA PHE A 70 -33.080 16.525 16.368 1.00 31.49 C ANISOU 551 CA PHE A 70 3684 4064 4217 1103 -908 5 C ATOM 552 C PHE A 70 -33.175 16.836 17.862 1.00 30.54 C ANISOU 552 C PHE A 70 3498 3952 4155 1155 -803 -117 C ATOM 553 O PHE A 70 -32.438 16.288 18.689 1.00 31.42 O ANISOU 553 O PHE A 70 3614 4116 4209 1066 -690 -157 O ATOM 554 CB PHE A 70 -34.157 15.504 15.981 1.00 31.30 C ANISOU 554 CB PHE A 70 3509 4181 4203 1113 -942 -1 C ATOM 555 CG PHE A 70 -34.294 14.374 16.966 1.00 31.54 C ANISOU 555 CG PHE A 70 3410 4354 4218 1052 -811 -79 C ATOM 556 CD1 PHE A 70 -33.273 13.463 17.147 1.00 29.33 C ANISOU 556 CD1 PHE A 70 3185 4123 3837 915 -720 -61 C ATOM 557 CD2 PHE A 70 -35.450 14.230 17.719 1.00 35.81 C ANISOU 557 CD2 PHE A 70 3775 4979 4851 1135 -775 -168 C ATOM 558 CE1 PHE A 70 -33.394 12.438 18.062 1.00 33.06 C ANISOU 558 CE1 PHE A 70 3557 4712 4292 861 -608 -121 C ATOM 559 CE2 PHE A 70 -35.573 13.197 18.631 1.00 30.30 C ANISOU 559 CE2 PHE A 70 2975 4408 4130 1067 -647 -228 C ATOM 560 CZ PHE A 70 -34.555 12.303 18.800 1.00 32.51 C ANISOU 560 CZ PHE A 70 3328 4723 4301 931 -570 -200 C ATOM 561 N CYS A 71 -34.108 17.721 18.203 1.00 27.81 N ANISOU 561 N CYS A 71 3093 3552 3923 1307 -844 -179 N ATOM 562 CA CYS A 71 -34.301 18.123 19.592 1.00 33.37 C ANISOU 562 CA CYS A 71 3744 4257 4678 1373 -743 -307 C ATOM 563 C CYS A 71 -34.940 16.993 20.389 1.00 34.00 C ANISOU 563 C CYS A 71 3653 4518 4746 1349 -629 -381 C ATOM 564 O CYS A 71 -35.959 16.427 19.982 1.00 33.52 O ANISOU 564 O CYS A 71 3450 4555 4732 1383 -661 -376 O ATOM 565 CB CYS A 71 -35.174 19.378 19.668 1.00 41.03 C ANISOU 565 CB CYS A 71 4695 5114 5782 1557 -815 -359 C ATOM 566 SG CYS A 71 -34.435 20.879 18.958 1.00 44.21 S ANISOU 566 SG CYS A 71 5321 5266 6209 1592 -940 -281 S ATOM 567 N ALA A 72 -34.347 16.670 21.535 1.00 29.61 N ANISOU 567 N ALA A 72 3116 4007 4129 1285 -501 -448 N ATOM 568 CA ALA A 72 -34.847 15.574 22.349 1.00 30.60 C ANISOU 568 CA ALA A 72 3106 4295 4224 1243 -382 -506 C ATOM 569 C ALA A 72 -34.515 15.838 23.807 1.00 32.45 C ANISOU 569 C ALA A 72 3373 4535 4422 1249 -259 -613 C ATOM 570 O ALA A 72 -33.503 16.472 24.122 1.00 32.25 O ANISOU 570 O ALA A 72 3492 4406 4357 1221 -266 -620 O ATOM 571 CB ALA A 72 -34.237 14.231 21.911 1.00 29.76 C ANISOU 571 CB ALA A 72 3012 4279 4017 1087 -365 -424 C ATOM 572 N ALA A 73 -35.378 15.349 24.694 1.00 30.82 N ANISOU 572 N ALA A 73 3034 4451 4227 1278 -147 -696 N ATOM 573 CA ALA A 73 -35.019 15.294 26.104 1.00 32.21 C ANISOU 573 CA ALA A 73 3251 4662 4324 1252 -16 -787 C ATOM 574 C ALA A 73 -33.703 14.542 26.250 1.00 29.42 C ANISOU 574 C ALA A 73 3015 4320 3842 1096 -5 -722 C ATOM 575 O ALA A 73 -33.491 13.508 25.612 1.00 28.01 O ANISOU 575 O ALA A 73 2812 4204 3627 999 -25 -634 O ATOM 576 CB ALA A 73 -36.124 14.611 26.913 1.00 33.78 C ANISOU 576 CB ALA A 73 3289 5016 4532 1271 118 -861 C ATOM 577 N CYS A 74 -32.801 15.078 27.077 1.00 27.64 N ANISOU 577 N CYS A 74 2919 4028 3554 1077 18 -772 N ATOM 578 CA CYS A 74 -31.425 14.588 27.047 1.00 27.13 C ANISOU 578 CA CYS A 74 2966 3946 3397 945 -7 -704 C ATOM 579 C CYS A 74 -31.348 13.102 27.373 1.00 25.50 C ANISOU 579 C CYS A 74 2708 3877 3102 839 65 -664 C ATOM 580 O CYS A 74 -30.604 12.360 26.725 1.00 26.78 O ANISOU 580 O CYS A 74 2899 4047 3230 745 24 -572 O ATOM 581 CB CYS A 74 -30.538 15.386 27.999 1.00 33.61 C ANISOU 581 CB CYS A 74 3918 4683 4168 938 -1 -776 C ATOM 582 SG CYS A 74 -28.776 15.008 27.722 1.00 37.62 S ANISOU 582 SG CYS A 74 4542 5147 4606 788 -65 -685 S ATOM 583 N HIS A 75 -32.120 12.639 28.357 1.00 25.60 N ANISOU 583 N HIS A 75 2651 3997 3079 854 178 -731 N ATOM 584 CA HIS A 75 -32.029 11.230 28.728 1.00 26.37 C ANISOU 584 CA HIS A 75 2720 4210 3090 747 247 -686 C ATOM 585 C HIS A 75 -32.730 10.324 27.719 1.00 28.28 C ANISOU 585 C HIS A 75 2844 4516 3387 715 227 -612 C ATOM 586 O HIS A 75 -32.366 9.149 27.592 1.00 25.57 O ANISOU 586 O HIS A 75 2505 4225 2986 612 239 -544 O ATOM 587 CB HIS A 75 -32.583 11.033 30.135 1.00 31.40 C ANISOU 587 CB HIS A 75 3340 4937 3655 757 383 -774 C ATOM 588 CG HIS A 75 -31.677 11.566 31.200 1.00 36.73 C ANISOU 588 CG HIS A 75 4160 5566 4232 748 394 -834 C ATOM 589 ND1 HIS A 75 -31.691 12.885 31.601 1.00 40.37 N ANISOU 589 ND1 HIS A 75 4678 5940 4720 843 383 -934 N ATOM 590 CD2 HIS A 75 -30.695 10.967 31.915 1.00 36.97 C ANISOU 590 CD2 HIS A 75 4294 5615 4139 655 398 -809 C ATOM 591 CE1 HIS A 75 -30.773 13.070 32.532 1.00 40.57 C ANISOU 591 CE1 HIS A 75 4838 5939 4638 801 381 -973 C ATOM 592 NE2 HIS A 75 -30.153 11.923 32.740 1.00 37.34 N ANISOU 592 NE2 HIS A 75 4455 5596 4136 688 386 -896 N ATOM 593 N GLY A 76 -33.722 10.844 26.995 1.00 28.89 N ANISOU 593 N GLY A 76 2819 4584 3576 804 187 -626 N ATOM 594 CA GLY A 76 -34.267 10.096 25.874 1.00 26.51 C ANISOU 594 CA GLY A 76 2423 4325 3326 770 131 -553 C ATOM 595 C GLY A 76 -33.262 9.953 24.749 1.00 24.19 C ANISOU 595 C GLY A 76 2228 3955 3009 711 21 -457 C ATOM 596 O GLY A 76 -33.106 8.871 24.176 1.00 24.02 O ANISOU 596 O GLY A 76 2194 3977 2955 622 7 -391 O ATOM 597 N CYS A 77 -32.564 11.043 24.420 1.00 25.82 N ANISOU 597 N CYS A 77 2537 4043 3230 756 -51 -451 N ATOM 598 CA CYS A 77 -31.464 10.969 23.466 1.00 26.71 C ANISOU 598 CA CYS A 77 2754 4085 3310 690 -129 -364 C ATOM 599 C CYS A 77 -30.418 9.962 23.926 1.00 26.31 C ANISOU 599 C CYS A 77 2759 4072 3164 576 -78 -335 C ATOM 600 O CYS A 77 -29.885 9.193 23.118 1.00 22.28 O ANISOU 600 O CYS A 77 2272 3568 2624 502 -107 -263 O ATOM 601 CB CYS A 77 -30.829 12.350 23.300 1.00 29.64 C ANISOU 601 CB CYS A 77 3232 4321 3711 742 -191 -370 C ATOM 602 SG CYS A 77 -29.425 12.390 22.170 1.00 29.59 S ANISOU 602 SG CYS A 77 3350 4228 3665 651 -263 -265 S ATOM 603 N ALEU A 78 -30.117 9.954 25.226 0.70 25.76 N ANISOU 603 N ALEU A 78 2716 4027 3044 566 -5 -393 N ATOM 604 N BLEU A 78 -30.102 9.965 25.225 0.30 25.66 N ANISOU 604 N BLEU A 78 2705 4012 3031 566 -5 -393 N ATOM 605 CA ALEU A 78 -29.126 9.029 25.764 0.70 22.74 C ANISOU 605 CA ALEU A 78 2389 3676 2576 470 29 -364 C ATOM 606 CA BLEU A 78 -29.127 9.021 25.765 0.30 23.03 C ANISOU 606 CA BLEU A 78 2425 3713 2611 470 29 -364 C ATOM 607 C ALEU A 78 -29.527 7.579 25.514 0.70 21.77 C ANISOU 607 C ALEU A 78 2204 3641 2427 403 64 -317 C ATOM 608 C BLEU A 78 -29.533 7.583 25.476 0.30 22.21 C ANISOU 608 C BLEU A 78 2259 3696 2485 403 62 -315 C ATOM 609 O ALEU A 78 -28.686 6.752 25.145 0.70 23.21 O ANISOU 609 O ALEU A 78 2427 3820 2572 330 47 -257 O ATOM 610 O BLEU A 78 -28.703 6.764 25.067 0.30 22.25 O ANISOU 610 O BLEU A 78 2304 3696 2453 331 43 -255 O ATOM 611 CB ALEU A 78 -28.945 9.294 27.256 0.70 22.04 C ANISOU 611 CB ALEU A 78 2343 3606 2426 480 93 -439 C ATOM 612 CB BLEU A 78 -28.972 9.229 27.270 0.30 22.11 C ANISOU 612 CB BLEU A 78 2349 3620 2433 477 96 -438 C ATOM 613 CG ALEU A 78 -27.745 8.686 27.964 0.70 18.43 C ANISOU 613 CG ALEU A 78 1967 3155 1880 400 97 -417 C ATOM 614 CG BLEU A 78 -27.944 10.212 27.818 0.30 20.68 C ANISOU 614 CG BLEU A 78 2274 3353 2231 485 59 -476 C ATOM 615 CD1ALEU A 78 -26.462 8.969 27.185 0.70 17.51 C ANISOU 615 CD1ALEU A 78 1911 2954 1786 362 14 -363 C ATOM 616 CD1BLEU A 78 -28.051 10.207 29.327 0.30 19.03 C ANISOU 616 CD1BLEU A 78 2100 3192 1938 491 131 -555 C ATOM 617 CD2ALEU A 78 -27.673 9.271 29.359 0.70 18.40 C ANISOU 617 CD2ALEU A 78 2023 3155 1814 426 138 -504 C ATOM 618 CD2BLEU A 78 -26.538 9.836 27.372 0.30 17.29 C ANISOU 618 CD2BLEU A 78 1906 2884 1781 403 0 -406 C ATOM 619 N PHE A 79 -30.810 7.254 25.691 1.00 21.04 N ANISOU 619 N PHE A 79 2006 3624 2364 426 114 -345 N ATOM 620 CA PHE A 79 -31.253 5.878 25.494 1.00 20.75 C ANISOU 620 CA PHE A 79 1910 3663 2310 349 146 -304 C ATOM 621 C PHE A 79 -31.071 5.439 24.043 1.00 23.36 C ANISOU 621 C PHE A 79 2243 3964 2670 316 62 -237 C ATOM 622 O PHE A 79 -30.504 4.374 23.775 1.00 22.26 O ANISOU 622 O PHE A 79 2141 3830 2487 237 62 -188 O ATOM 623 CB PHE A 79 -32.710 5.697 25.928 1.00 21.49 C ANISOU 623 CB PHE A 79 1873 3846 2447 372 219 -350 C ATOM 624 CG PHE A 79 -33.209 4.295 25.717 1.00 27.44 C ANISOU 624 CG PHE A 79 2565 4667 3194 277 249 -307 C ATOM 625 CD1 PHE A 79 -32.863 3.284 26.608 1.00 26.63 C ANISOU 625 CD1 PHE A 79 2511 4601 3008 192 328 -286 C ATOM 626 CD2 PHE A 79 -33.966 3.968 24.601 1.00 30.62 C ANISOU 626 CD2 PHE A 79 2877 5086 3669 268 187 -284 C ATOM 627 CE1 PHE A 79 -33.282 1.987 26.409 1.00 30.24 C ANISOU 627 CE1 PHE A 79 2927 5101 3462 97 353 -242 C ATOM 628 CE2 PHE A 79 -34.390 2.666 24.391 1.00 34.41 C ANISOU 628 CE2 PHE A 79 3310 5617 4146 170 207 -250 C ATOM 629 CZ PHE A 79 -34.049 1.673 25.300 1.00 38.08 C ANISOU 629 CZ PHE A 79 3825 6108 4535 83 295 -228 C ATOM 630 N ILE A 80 -31.539 6.246 23.086 1.00 21.49 N ANISOU 630 N ILE A 80 1976 3690 2498 380 -15 -235 N ATOM 631 CA ILE A 80 -31.399 5.812 21.698 1.00 22.12 C ANISOU 631 CA ILE A 80 2074 3747 2582 345 -95 -174 C ATOM 632 C ILE A 80 -29.950 5.840 21.243 1.00 20.49 C ANISOU 632 C ILE A 80 1991 3471 2323 305 -120 -127 C ATOM 633 O ILE A 80 -29.582 5.089 20.334 1.00 22.76 O ANISOU 633 O ILE A 80 2312 3755 2582 249 -147 -80 O ATOM 634 CB ILE A 80 -32.259 6.636 20.724 1.00 24.54 C ANISOU 634 CB ILE A 80 2333 4031 2960 421 -188 -172 C ATOM 635 CG1 ILE A 80 -31.900 8.118 20.762 1.00 24.79 C ANISOU 635 CG1 ILE A 80 2427 3973 3021 508 -225 -185 C ATOM 636 CG2 ILE A 80 -33.723 6.428 21.007 1.00 28.50 C ANISOU 636 CG2 ILE A 80 2681 4616 3532 453 -170 -216 C ATOM 637 CD1 ILE A 80 -32.634 8.910 19.694 1.00 32.42 C ANISOU 637 CD1 ILE A 80 3371 4897 4051 586 -337 -165 C ATOM 638 N ALA A 81 -29.110 6.675 21.860 1.00 18.66 N ANISOU 638 N ALA A 81 1825 3185 2079 328 -107 -144 N ATOM 639 CA ALA A 81 -27.685 6.646 21.550 1.00 22.18 C ANISOU 639 CA ALA A 81 2364 3576 2488 280 -118 -103 C ATOM 640 C ALA A 81 -27.017 5.395 22.113 1.00 23.59 C ANISOU 640 C ALA A 81 2554 3796 2615 210 -67 -90 C ATOM 641 O ALA A 81 -26.186 4.772 21.442 1.00 20.62 O ANISOU 641 O ALA A 81 2216 3402 2216 162 -75 -48 O ATOM 642 CB ALA A 81 -26.999 7.902 22.096 1.00 22.38 C ANISOU 642 CB ALA A 81 2447 3530 2528 314 -129 -130 C ATOM 643 N CYS A 82 -27.355 5.017 23.349 1.00 22.25 N ANISOU 643 N CYS A 82 2357 3677 2422 206 -11 -126 N ATOM 644 CA CYS A 82 -26.659 3.928 24.022 1.00 19.91 C ANISOU 644 CA CYS A 82 2090 3404 2072 147 25 -108 C ATOM 645 C CYS A 82 -27.171 2.547 23.635 1.00 22.97 C ANISOU 645 C CYS A 82 2446 3833 2450 94 46 -76 C ATOM 646 O CYS A 82 -26.500 1.552 23.927 1.00 18.65 O ANISOU 646 O CYS A 82 1935 3283 1866 48 62 -48 O ATOM 647 CB CYS A 82 -26.774 4.085 25.542 1.00 21.56 C ANISOU 647 CB CYS A 82 2308 3645 2238 157 75 -151 C ATOM 648 SG CYS A 82 -25.808 5.453 26.196 1.00 26.17 S ANISOU 648 SG CYS A 82 2959 4167 2816 195 41 -194 S ATOM 649 N PHE A 83 -28.339 2.448 23.003 1.00 19.89 N ANISOU 649 N PHE A 83 1987 3474 2095 100 37 -82 N ATOM 650 CA PHE A 83 -28.914 1.120 22.827 1.00 19.59 C ANISOU 650 CA PHE A 83 1918 3475 2051 36 59 -62 C ATOM 651 C PHE A 83 -28.008 0.224 21.985 1.00 19.38 C ANISOU 651 C PHE A 83 1956 3405 2003 -10 31 -21 C ATOM 652 O PHE A 83 -27.924 -0.983 22.241 1.00 21.27 O ANISOU 652 O PHE A 83 2212 3648 2220 -66 59 -1 O ATOM 653 CB PHE A 83 -30.319 1.213 22.224 1.00 20.70 C ANISOU 653 CB PHE A 83 1960 3658 2246 45 37 -80 C ATOM 654 CG PHE A 83 -31.004 -0.118 22.127 1.00 23.44 C ANISOU 654 CG PHE A 83 2264 4044 2597 -36 59 -67 C ATOM 655 CD1 PHE A 83 -31.499 -0.737 23.269 1.00 28.31 C ANISOU 655 CD1 PHE A 83 2846 4710 3199 -81 143 -73 C ATOM 656 CD2 PHE A 83 -31.122 -0.771 20.906 1.00 22.24 C ANISOU 656 CD2 PHE A 83 2122 3873 2454 -75 -3 -47 C ATOM 657 CE1 PHE A 83 -32.110 -1.978 23.199 1.00 32.46 C ANISOU 657 CE1 PHE A 83 3340 5260 3733 -170 165 -55 C ATOM 658 CE2 PHE A 83 -31.731 -2.018 20.826 1.00 25.11 C ANISOU 658 CE2 PHE A 83 2455 4259 2825 -160 11 -39 C ATOM 659 CZ PHE A 83 -32.226 -2.620 21.970 1.00 27.89 C ANISOU 659 CZ PHE A 83 2766 4653 3176 -211 95 -40 C ATOM 660 N VAL A 84 -27.282 0.795 21.017 1.00 16.98 N ANISOU 660 N VAL A 84 1696 3054 1703 14 -15 -7 N ATOM 661 CA VAL A 84 -26.392 -0.029 20.202 1.00 17.32 C ANISOU 661 CA VAL A 84 1796 3060 1723 -21 -23 21 C ATOM 662 C VAL A 84 -25.287 -0.640 21.059 1.00 18.63 C ANISOU 662 C VAL A 84 2002 3207 1870 -36 12 33 C ATOM 663 O VAL A 84 -24.761 -1.711 20.734 1.00 21.04 O ANISOU 663 O VAL A 84 2341 3488 2164 -66 21 50 O ATOM 664 CB VAL A 84 -25.813 0.783 19.028 1.00 17.90 C ANISOU 664 CB VAL A 84 1912 3094 1796 2 -60 35 C ATOM 665 CG1 VAL A 84 -24.841 1.854 19.533 1.00 16.96 C ANISOU 665 CG1 VAL A 84 1816 2942 1687 33 -54 36 C ATOM 666 CG2 VAL A 84 -25.129 -0.150 18.016 1.00 15.95 C ANISOU 666 CG2 VAL A 84 1719 2821 1519 -34 -55 52 C ATOM 667 N LEU A 85 -24.932 0.013 22.172 1.00 18.68 N ANISOU 667 N LEU A 85 2008 3219 1871 -12 24 22 N ATOM 668 CA LEU A 85 -23.926 -0.538 23.076 1.00 18.62 C ANISOU 668 CA LEU A 85 2037 3197 1841 -22 36 36 C ATOM 669 C LEU A 85 -24.414 -1.816 23.747 1.00 18.38 C ANISOU 669 C LEU A 85 2015 3185 1782 -63 66 54 C ATOM 670 O LEU A 85 -23.611 -2.713 24.028 1.00 19.37 O ANISOU 670 O LEU A 85 2182 3281 1896 -76 62 81 O ATOM 671 CB LEU A 85 -23.550 0.498 24.136 1.00 18.58 C ANISOU 671 CB LEU A 85 2039 3197 1825 8 29 13 C ATOM 672 CG LEU A 85 -23.040 1.848 23.621 1.00 22.15 C ANISOU 672 CG LEU A 85 2491 3613 2310 39 -2 -3 C ATOM 673 CD1 LEU A 85 -22.906 2.844 24.759 1.00 16.58 C ANISOU 673 CD1 LEU A 85 1800 2908 1592 64 -11 -41 C ATOM 674 CD2 LEU A 85 -21.705 1.670 22.910 1.00 24.15 C ANISOU 674 CD2 LEU A 85 2761 3826 2587 25 -17 23 C ATOM 675 N VAL A 86 -25.713 -1.897 24.038 1.00 16.61 N ANISOU 675 N VAL A 86 1751 3008 1553 -83 96 41 N ATOM 676 CA VAL A 86 -26.299 -3.120 24.580 1.00 19.62 C ANISOU 676 CA VAL A 86 2140 3404 1911 -141 133 65 C ATOM 677 C VAL A 86 -26.129 -4.271 23.594 1.00 20.57 C ANISOU 677 C VAL A 86 2286 3479 2053 -179 114 87 C ATOM 678 O VAL A 86 -25.736 -5.385 23.966 1.00 19.73 O ANISOU 678 O VAL A 86 2232 3334 1929 -212 122 120 O ATOM 679 CB VAL A 86 -27.786 -2.892 24.911 1.00 21.13 C ANISOU 679 CB VAL A 86 2256 3661 2111 -162 178 40 C ATOM 680 CG1 VAL A 86 -28.426 -4.188 25.421 1.00 22.46 C ANISOU 680 CG1 VAL A 86 2430 3843 2260 -244 226 71 C ATOM 681 CG2 VAL A 86 -27.954 -1.765 25.927 1.00 17.09 C ANISOU 681 CG2 VAL A 86 1729 3191 1575 -114 209 4 C ATOM 682 N LEU A 87 -26.431 -4.015 22.317 1.00 18.30 N ANISOU 682 N LEU A 87 1971 3186 1796 -173 83 68 N ATOM 683 CA LEU A 87 -26.396 -5.069 21.310 1.00 21.27 C ANISOU 683 CA LEU A 87 2379 3520 2181 -212 65 74 C ATOM 684 C LEU A 87 -24.965 -5.505 21.016 1.00 20.94 C ANISOU 684 C LEU A 87 2405 3417 2135 -185 59 86 C ATOM 685 O LEU A 87 -24.697 -6.700 20.833 1.00 20.35 O ANISOU 685 O LEU A 87 2378 3291 2062 -212 63 96 O ATOM 686 CB LEU A 87 -27.091 -4.589 20.034 1.00 19.39 C ANISOU 686 CB LEU A 87 2108 3300 1960 -210 24 49 C ATOM 687 CG LEU A 87 -28.567 -4.207 20.206 1.00 21.07 C ANISOU 687 CG LEU A 87 2230 3577 2200 -228 19 31 C ATOM 688 CD1 LEU A 87 -29.194 -3.869 18.854 1.00 20.66 C ANISOU 688 CD1 LEU A 87 2153 3534 2162 -225 -49 12 C ATOM 689 CD2 LEU A 87 -29.333 -5.328 20.903 1.00 17.29 C ANISOU 689 CD2 LEU A 87 1727 3113 1729 -307 58 41 C ATOM 690 N ALA A 88 -24.036 -4.550 20.957 1.00 18.62 N ANISOU 690 N ALA A 88 2110 3120 1844 -132 51 83 N ATOM 691 CA ALA A 88 -22.637 -4.911 20.771 1.00 19.77 C ANISOU 691 CA ALA A 88 2293 3219 2002 -104 53 91 C ATOM 692 C ALA A 88 -22.128 -5.728 21.951 1.00 17.41 C ANISOU 692 C ALA A 88 2020 2894 1699 -103 54 119 C ATOM 693 O ALA A 88 -21.394 -6.706 21.766 1.00 20.35 O ANISOU 693 O ALA A 88 2430 3213 2091 -92 52 129 O ATOM 694 CB ALA A 88 -21.786 -3.657 20.579 1.00 19.67 C ANISOU 694 CB ALA A 88 2259 3213 2002 -63 47 84 C ATOM 695 N GLN A 89 -22.513 -5.345 23.174 1.00 18.16 N ANISOU 695 N GLN A 89 2107 3026 1768 -109 54 132 N ATOM 696 CA GLN A 89 -22.053 -6.082 24.346 1.00 18.82 C ANISOU 696 CA GLN A 89 2235 3087 1828 -110 45 168 C ATOM 697 C GLN A 89 -22.618 -7.492 24.366 1.00 21.00 C ANISOU 697 C GLN A 89 2558 3323 2099 -160 60 196 C ATOM 698 O GLN A 89 -21.903 -8.445 24.696 1.00 20.10 O ANISOU 698 O GLN A 89 2499 3148 1991 -148 39 229 O ATOM 699 CB GLN A 89 -22.442 -5.362 25.634 1.00 18.91 C ANISOU 699 CB GLN A 89 2245 3151 1788 -114 51 170 C ATOM 700 CG GLN A 89 -21.586 -5.811 26.812 1.00 21.83 C ANISOU 700 CG GLN A 89 2674 3499 2123 -99 16 208 C ATOM 701 CD GLN A 89 -20.114 -5.506 26.565 1.00 23.70 C ANISOU 701 CD GLN A 89 2894 3704 2408 -43 -39 202 C ATOM 702 OE1 GLN A 89 -19.776 -4.423 26.096 1.00 24.09 O ANISOU 702 OE1 GLN A 89 2894 3772 2486 -22 -44 166 O ATOM 703 NE2 GLN A 89 -19.238 -6.468 26.854 1.00 22.69 N ANISOU 703 NE2 GLN A 89 2802 3524 2296 -21 -80 239 N ATOM 704 N SER A 90 -23.909 -7.635 24.042 1.00 19.47 N ANISOU 704 N SER A 90 2341 3158 1900 -217 90 185 N ATOM 705 CA SER A 90 -24.512 -8.959 23.950 1.00 17.63 C ANISOU 705 CA SER A 90 2148 2879 1671 -283 103 208 C ATOM 706 C SER A 90 -23.770 -9.825 22.943 1.00 21.68 C ANISOU 706 C SER A 90 2707 3307 2221 -264 79 197 C ATOM 707 O SER A 90 -23.554 -11.017 23.184 1.00 21.71 O ANISOU 707 O SER A 90 2780 3235 2234 -283 72 227 O ATOM 708 CB SER A 90 -25.992 -8.842 23.571 1.00 19.80 C ANISOU 708 CB SER A 90 2363 3207 1954 -349 129 185 C ATOM 709 OG SER A 90 -26.594 -10.128 23.479 1.00 26.71 O ANISOU 709 OG SER A 90 3276 4033 2841 -431 139 206 O ATOM 710 N SER A 91 -23.366 -9.239 21.809 1.00 21.25 N ANISOU 710 N SER A 91 2625 3262 2188 -223 69 154 N ATOM 711 CA SER A 91 -22.616 -9.986 20.803 1.00 20.78 C ANISOU 711 CA SER A 91 2610 3130 2155 -198 64 130 C ATOM 712 C SER A 91 -21.285 -10.472 21.364 1.00 21.95 C ANISOU 712 C SER A 91 2790 3221 2330 -134 53 153 C ATOM 713 O SER A 91 -20.881 -11.617 21.133 1.00 24.09 O ANISOU 713 O SER A 91 3119 3405 2628 -123 48 153 O ATOM 714 CB SER A 91 -22.384 -9.113 19.568 1.00 22.94 C ANISOU 714 CB SER A 91 2853 3436 2426 -169 68 85 C ATOM 715 OG SER A 91 -23.616 -8.655 19.041 1.00 23.56 O ANISOU 715 OG SER A 91 2902 3565 2485 -217 57 68 O ATOM 716 N ILE A 92 -20.588 -9.605 22.105 1.00 19.57 N ANISOU 716 N ILE A 92 2449 2959 2027 -89 39 170 N ATOM 717 CA ILE A 92 -19.311 -9.976 22.715 1.00 21.79 C ANISOU 717 CA ILE A 92 2742 3197 2342 -26 9 194 C ATOM 718 C ILE A 92 -19.486 -11.152 23.674 1.00 22.94 C ANISOU 718 C ILE A 92 2965 3278 2475 -44 -17 249 C ATOM 719 O ILE A 92 -18.681 -12.092 23.685 1.00 21.47 O ANISOU 719 O ILE A 92 2818 3008 2332 5 -43 262 O ATOM 720 CB ILE A 92 -18.697 -8.755 23.421 1.00 24.39 C ANISOU 720 CB ILE A 92 3014 3587 2665 6 -15 200 C ATOM 721 CG1 ILE A 92 -18.135 -7.779 22.387 1.00 22.62 C ANISOU 721 CG1 ILE A 92 2727 3395 2474 32 9 156 C ATOM 722 CG2 ILE A 92 -17.621 -9.180 24.419 1.00 22.16 C ANISOU 722 CG2 ILE A 92 2746 3269 2404 58 -73 237 C ATOM 723 CD1 ILE A 92 -17.857 -6.411 22.953 1.00 30.66 C ANISOU 723 CD1 ILE A 92 3696 4471 3484 38 -11 153 C ATOM 724 N PHE A 93 -20.526 -11.108 24.510 1.00 22.05 N ANISOU 724 N PHE A 93 2875 3200 2303 -111 -8 283 N ATOM 725 CA PHE A 93 -20.775 -12.218 25.427 1.00 22.86 C ANISOU 725 CA PHE A 93 3067 3240 2380 -146 -23 347 C ATOM 726 C PHE A 93 -21.064 -13.512 24.669 1.00 26.05 C ANISOU 726 C PHE A 93 3531 3543 2824 -177 -14 342 C ATOM 727 O PHE A 93 -20.573 -14.585 25.046 1.00 23.69 O ANISOU 727 O PHE A 93 3313 3143 2546 -156 -48 385 O ATOM 728 CB PHE A 93 -21.932 -11.874 26.368 1.00 24.27 C ANISOU 728 CB PHE A 93 3251 3487 2482 -225 12 377 C ATOM 729 CG PHE A 93 -21.567 -10.886 27.449 1.00 28.75 C ANISOU 729 CG PHE A 93 3805 4125 2993 -194 -6 390 C ATOM 730 CD1 PHE A 93 -20.349 -10.974 28.112 1.00 39.23 C ANISOU 730 CD1 PHE A 93 5166 5419 4319 -126 -77 422 C ATOM 731 CD2 PHE A 93 -22.434 -9.862 27.795 1.00 25.86 C ANISOU 731 CD2 PHE A 93 3389 3857 2580 -228 40 364 C ATOM 732 CE1 PHE A 93 -20.011 -10.062 29.111 1.00 39.83 C ANISOU 732 CE1 PHE A 93 5239 5558 4336 -105 -107 426 C ATOM 733 CE2 PHE A 93 -22.104 -8.945 28.794 1.00 25.48 C ANISOU 733 CE2 PHE A 93 3343 3866 2473 -199 23 363 C ATOM 734 CZ PHE A 93 -20.893 -9.045 29.450 1.00 28.35 C ANISOU 734 CZ PHE A 93 3752 4196 2824 -144 -53 393 C ATOM 735 N SER A 94 -21.856 -13.435 23.593 1.00 20.69 N ANISOU 735 N SER A 94 2821 2883 2156 -225 20 289 N ATOM 736 CA SER A 94 -22.147 -14.635 22.813 1.00 22.45 C ANISOU 736 CA SER A 94 3109 3007 2414 -262 22 270 C ATOM 737 C SER A 94 -20.888 -15.177 22.147 1.00 22.86 C ANISOU 737 C SER A 94 3191 2972 2523 -165 4 237 C ATOM 738 O SER A 94 -20.657 -16.390 22.138 1.00 24.97 O ANISOU 738 O SER A 94 3544 3118 2824 -158 -14 250 O ATOM 739 CB SER A 94 -23.214 -14.340 21.760 1.00 24.45 C ANISOU 739 CB SER A 94 3320 3309 2662 -330 45 213 C ATOM 740 OG SER A 94 -24.476 -14.120 22.366 1.00 29.18 O ANISOU 740 OG SER A 94 3885 3973 3231 -424 66 241 O ATOM 741 N LEU A 95 -20.064 -14.291 21.582 1.00 22.83 N ANISOU 741 N LEU A 95 3116 3023 2534 -90 14 193 N ATOM 742 CA LEU A 95 -18.822 -14.730 20.952 1.00 23.40 C ANISOU 742 CA LEU A 95 3194 3029 2668 6 15 155 C ATOM 743 C LEU A 95 -17.901 -15.402 21.963 1.00 22.58 C ANISOU 743 C LEU A 95 3122 2849 2607 76 -36 210 C ATOM 744 O LEU A 95 -17.296 -16.439 21.669 1.00 24.17 O ANISOU 744 O LEU A 95 3376 2940 2868 135 -46 195 O ATOM 745 CB LEU A 95 -18.126 -13.541 20.291 1.00 22.61 C ANISOU 745 CB LEU A 95 3001 3015 2574 56 46 110 C ATOM 746 CG LEU A 95 -18.834 -12.976 19.056 1.00 24.41 C ANISOU 746 CG LEU A 95 3217 3297 2759 7 87 54 C ATOM 747 CD1 LEU A 95 -18.217 -11.641 18.621 1.00 25.55 C ANISOU 747 CD1 LEU A 95 3279 3528 2899 41 115 35 C ATOM 748 CD2 LEU A 95 -18.802 -13.984 17.919 1.00 22.82 C ANISOU 748 CD2 LEU A 95 3088 3014 2569 12 114 -8 C ATOM 749 N LEU A 96 -17.785 -14.827 23.161 1.00 21.74 N ANISOU 749 N LEU A 96 2992 2798 2471 77 -74 272 N ATOM 750 CA LEU A 96 -16.934 -15.418 24.186 1.00 23.92 C ANISOU 750 CA LEU A 96 3306 3008 2776 143 -145 334 C ATOM 751 C LEU A 96 -17.478 -16.770 24.628 1.00 27.72 C ANISOU 751 C LEU A 96 3917 3368 3248 102 -168 390 C ATOM 752 O LEU A 96 -16.714 -17.724 24.819 1.00 28.54 O ANISOU 752 O LEU A 96 4076 3356 3411 177 -218 414 O ATOM 753 CB LEU A 96 -16.815 -14.459 25.373 1.00 24.82 C ANISOU 753 CB LEU A 96 3384 3213 2833 137 -186 382 C ATOM 754 CG LEU A 96 -15.950 -14.887 26.563 1.00 32.81 C ANISOU 754 CG LEU A 96 4438 4176 3852 201 -282 453 C ATOM 755 CD1 LEU A 96 -14.547 -15.260 26.110 1.00 32.69 C ANISOU 755 CD1 LEU A 96 4366 4101 3953 325 -323 424 C ATOM 756 CD2 LEU A 96 -15.900 -13.778 27.611 1.00 30.12 C ANISOU 756 CD2 LEU A 96 4066 3941 3439 184 -319 480 C ATOM 757 N ALA A 97 -18.802 -16.872 24.775 1.00 26.50 N ANISOU 757 N ALA A 97 3808 3233 3029 -19 -132 411 N ATOM 758 CA ALA A 97 -19.415 -18.137 25.150 1.00 26.00 C ANISOU 758 CA ALA A 97 3868 3051 2958 -85 -143 468 C ATOM 759 C ALA A 97 -19.157 -19.205 24.098 1.00 26.78 C ANISOU 759 C ALA A 97 4023 3017 3136 -53 -140 413 C ATOM 760 O ALA A 97 -18.856 -20.355 24.432 1.00 24.77 O ANISOU 760 O ALA A 97 3876 2618 2919 -28 -183 457 O ATOM 761 CB ALA A 97 -20.913 -17.946 25.364 1.00 25.70 C ANISOU 761 CB ALA A 97 3836 3078 2852 -231 -89 486 C ATOM 762 N ILE A 98 -19.272 -18.844 22.818 1.00 28.64 N ANISOU 762 N ILE A 98 4199 3292 3391 -51 -92 315 N ATOM 763 CA ILE A 98 -19.020 -19.807 21.748 1.00 27.41 C ANISOU 763 CA ILE A 98 4104 3014 3296 -18 -82 245 C ATOM 764 C ILE A 98 -17.588 -20.323 21.831 1.00 28.35 C ANISOU 764 C ILE A 98 4232 3041 3498 134 -116 239 C ATOM 765 O ILE A 98 -17.337 -21.527 21.727 1.00 28.83 O ANISOU 765 O ILE A 98 4394 2945 3617 170 -141 237 O ATOM 766 CB ILE A 98 -19.321 -19.173 20.378 1.00 23.08 C ANISOU 766 CB ILE A 98 3495 2545 2730 -37 -26 142 C ATOM 767 CG1 ILE A 98 -20.831 -18.977 20.206 1.00 24.12 C ANISOU 767 CG1 ILE A 98 3628 2733 2802 -184 -12 143 C ATOM 768 CG2 ILE A 98 -18.759 -20.027 19.252 1.00 22.96 C ANISOU 768 CG2 ILE A 98 3539 2418 2767 27 -6 52 C ATOM 769 CD1 ILE A 98 -21.207 -18.048 19.052 1.00 22.09 C ANISOU 769 CD1 ILE A 98 3299 2585 2508 -204 22 64 C ATOM 770 N ALA A 99 -16.628 -19.416 22.032 1.00 27.72 N ANISOU 770 N ALA A 99 4043 3054 3437 224 -122 236 N ATOM 771 CA ALA A 99 -15.227 -19.820 22.130 1.00 26.99 C ANISOU 771 CA ALA A 99 3924 2891 3439 374 -159 228 C ATOM 772 C ALA A 99 -15.009 -20.770 23.302 1.00 29.94 C ANISOU 772 C ALA A 99 4397 3142 3837 405 -253 328 C ATOM 773 O ALA A 99 -14.327 -21.797 23.172 1.00 28.33 O ANISOU 773 O ALA A 99 4249 2795 3721 504 -287 318 O ATOM 774 CB ALA A 99 -14.346 -18.578 22.267 1.00 22.06 C ANISOU 774 CB ALA A 99 3151 2402 2829 436 -157 216 C ATOM 775 N ILE A 100 -15.581 -20.437 24.463 1.00 28.49 N ANISOU 775 N ILE A 100 4244 3009 3569 327 -294 425 N ATOM 776 CA ILE A 100 -15.420 -21.282 25.642 1.00 31.87 C ANISOU 776 CA ILE A 100 4788 3329 3994 345 -386 536 C ATOM 777 C ILE A 100 -16.085 -22.634 25.421 1.00 30.48 C ANISOU 777 C ILE A 100 4766 2981 3834 287 -381 555 C ATOM 778 O ILE A 100 -15.541 -23.678 25.798 1.00 32.54 O ANISOU 778 O ILE A 100 5126 3082 4155 362 -454 604 O ATOM 779 CB ILE A 100 -15.969 -20.560 26.889 1.00 32.56 C ANISOU 779 CB ILE A 100 4887 3523 3963 259 -411 627 C ATOM 780 CG1 ILE A 100 -15.070 -19.365 27.236 1.00 31.80 C ANISOU 780 CG1 ILE A 100 4657 3558 3867 336 -447 611 C ATOM 781 CG2 ILE A 100 -16.088 -21.530 28.064 1.00 31.75 C ANISOU 781 CG2 ILE A 100 4942 3300 3820 239 -491 754 C ATOM 782 CD1 ILE A 100 -15.584 -18.508 28.370 1.00 33.88 C ANISOU 782 CD1 ILE A 100 4928 3937 4006 257 -463 674 C ATOM 783 N ASP A 101 -17.256 -22.637 24.776 1.00 29.56 N ANISOU 783 N ASP A 101 4670 2888 3674 155 -305 513 N ATOM 784 CA ASP A 101 -17.934 -23.891 24.462 1.00 33.45 C ANISOU 784 CA ASP A 101 5303 3217 4189 81 -299 518 C ATOM 785 C ASP A 101 -17.062 -24.788 23.591 1.00 33.30 C ANISOU 785 C ASP A 101 5324 3044 4284 209 -314 438 C ATOM 786 O ASP A 101 -16.977 -25.998 23.823 1.00 33.57 O ANISOU 786 O ASP A 101 5497 2888 4369 226 -362 478 O ATOM 787 CB ASP A 101 -19.268 -23.612 23.769 1.00 33.31 C ANISOU 787 CB ASP A 101 5266 3271 4118 -77 -223 465 C ATOM 788 CG ASP A 101 -20.013 -24.888 23.404 1.00 39.40 C ANISOU 788 CG ASP A 101 6176 3874 4919 -174 -223 461 C ATOM 789 OD1 ASP A 101 -20.611 -25.505 24.303 1.00 42.11 O ANISOU 789 OD1 ASP A 101 6622 4143 5233 -272 -244 566 O ATOM 790 OD2 ASP A 101 -19.994 -25.282 22.221 1.00 40.95 O ANISOU 790 OD2 ASP A 101 6387 4008 5163 -157 -201 352 O ATOM 791 N ARG A 102 -16.403 -24.212 22.583 1.00 31.32 N ANISOU 791 N ARG A 102 4959 2867 4075 300 -265 324 N ATOM 792 CA ARG A 102 -15.549 -25.019 21.718 1.00 32.11 C ANISOU 792 CA ARG A 102 5087 2833 4280 430 -258 232 C ATOM 793 C ARG A 102 -14.317 -25.522 22.462 1.00 31.36 C ANISOU 793 C ARG A 102 4996 2639 4280 595 -343 287 C ATOM 794 O ARG A 102 -13.830 -26.626 22.189 1.00 35.83 O ANISOU 794 O ARG A 102 5649 3023 4941 690 -369 257 O ATOM 795 CB ARG A 102 -15.153 -24.213 20.479 1.00 32.39 C ANISOU 795 CB ARG A 102 4999 2990 4320 477 -168 101 C ATOM 796 CG ARG A 102 -16.322 -23.852 19.544 1.00 34.91 C ANISOU 796 CG ARG A 102 5330 3382 4552 333 -100 34 C ATOM 797 CD ARG A 102 -16.918 -25.086 18.867 1.00 43.12 C ANISOU 797 CD ARG A 102 6522 4252 5610 279 -97 -24 C ATOM 798 NE ARG A 102 -17.863 -25.791 19.730 1.00 50.63 N ANISOU 798 NE ARG A 102 7586 5108 6542 154 -154 76 N ATOM 799 CZ ARG A 102 -17.988 -27.112 19.779 1.00 55.31 C ANISOU 799 CZ ARG A 102 8333 5492 7189 145 -192 83 C ATOM 800 NH1 ARG A 102 -17.221 -27.881 19.017 1.00 59.44 N ANISOU 800 NH1 ARG A 102 8915 5876 7794 268 -182 -14 N ATOM 801 NH2 ARG A 102 -18.870 -27.667 20.600 1.00 56.41 N ANISOU 801 NH2 ARG A 102 8572 5557 7306 12 -233 187 N ATOM 802 N TYR A 103 -13.798 -24.735 23.411 1.00 31.78 N ANISOU 802 N TYR A 103 4959 2804 4314 634 -397 364 N ATOM 803 CA TYR A 103 -12.645 -25.194 24.180 1.00 32.48 C ANISOU 803 CA TYR A 103 5045 2803 4491 790 -503 424 C ATOM 804 C TYR A 103 -13.011 -26.356 25.096 1.00 36.18 C ANISOU 804 C TYR A 103 5705 3088 4952 762 -597 545 C ATOM 805 O TYR A 103 -12.237 -27.310 25.236 1.00 36.37 O ANISOU 805 O TYR A 103 5792 2943 5084 898 -673 561 O ATOM 806 CB TYR A 103 -12.042 -24.053 24.998 1.00 35.51 C ANISOU 806 CB TYR A 103 5294 3352 4847 824 -555 476 C ATOM 807 CG TYR A 103 -10.946 -24.541 25.923 1.00 44.14 C ANISOU 807 CG TYR A 103 6393 4358 6023 971 -694 553 C ATOM 808 CD1 TYR A 103 -9.693 -24.878 25.427 1.00 46.26 C ANISOU 808 CD1 TYR A 103 6563 4566 6447 1155 -714 482 C ATOM 809 CD2 TYR A 103 -11.174 -24.695 27.287 1.00 50.59 C ANISOU 809 CD2 TYR A 103 7314 5148 6759 930 -807 697 C ATOM 810 CE1 TYR A 103 -8.690 -25.341 26.266 1.00 51.88 C ANISOU 810 CE1 TYR A 103 7268 5196 7249 1301 -859 553 C ATOM 811 CE2 TYR A 103 -10.177 -25.158 28.133 1.00 53.39 C ANISOU 811 CE2 TYR A 103 7685 5418 7183 1069 -956 774 C ATOM 812 CZ TYR A 103 -8.938 -25.478 27.618 1.00 55.96 C ANISOU 812 CZ TYR A 103 7899 5685 7679 1257 -990 703 C ATOM 813 OH TYR A 103 -7.946 -25.937 28.459 1.00 60.58 O ANISOU 813 OH TYR A 103 8487 6186 8346 1405 -1155 780 O ATOM 814 N ILE A 104 -14.176 -26.295 25.743 1.00 36.12 N ANISOU 814 N ILE A 104 5794 3107 4823 589 -591 634 N ATOM 815 CA ILE A 104 -14.600 -27.422 26.570 1.00 38.68 C ANISOU 815 CA ILE A 104 6316 3250 5129 538 -664 756 C ATOM 816 C ILE A 104 -14.723 -28.681 25.721 1.00 39.24 C ANISOU 816 C ILE A 104 6508 3107 5295 557 -647 693 C ATOM 817 O ILE A 104 -14.316 -29.773 26.136 1.00 39.63 O ANISOU 817 O ILE A 104 6694 2951 5413 633 -735 758 O ATOM 818 CB ILE A 104 -15.918 -27.093 27.293 1.00 38.05 C ANISOU 818 CB ILE A 104 6301 3254 4900 330 -626 848 C ATOM 819 CG1 ILE A 104 -15.704 -25.963 28.300 1.00 37.66 C ANISOU 819 CG1 ILE A 104 6166 3387 4754 330 -658 915 C ATOM 820 CG2 ILE A 104 -16.471 -28.330 27.998 1.00 44.35 C ANISOU 820 CG2 ILE A 104 7317 3855 5678 246 -676 972 C ATOM 821 CD1 ILE A 104 -16.999 -25.334 28.796 1.00 38.14 C ANISOU 821 CD1 ILE A 104 6237 3582 4672 138 -582 962 C ATOM 822 N ALA A 105 -15.258 -28.541 24.506 1.00 38.23 N ANISOU 822 N ALA A 105 6339 3017 5171 493 -543 563 N ATOM 823 CA ALA A 105 -15.462 -29.698 23.640 1.00 38.91 C ANISOU 823 CA ALA A 105 6550 2903 5332 494 -524 485 C ATOM 824 C ALA A 105 -14.140 -30.331 23.222 1.00 41.34 C ANISOU 824 C ALA A 105 6850 3072 5785 720 -562 414 C ATOM 825 O ALA A 105 -14.027 -31.560 23.166 1.00 44.15 O ANISOU 825 O ALA A 105 7360 3193 6221 768 -609 418 O ATOM 826 CB ALA A 105 -16.275 -29.292 22.412 1.00 38.87 C ANISOU 826 CB ALA A 105 6493 2991 5283 382 -415 353 C ATOM 827 N ILE A 106 -13.128 -29.515 22.918 1.00 43.08 N ANISOU 827 N ILE A 106 6889 3430 6049 862 -539 346 N ATOM 828 CA ILE A 106 -11.852 -30.086 22.494 1.00 46.70 C ANISOU 828 CA ILE A 106 7311 3772 6659 1084 -561 269 C ATOM 829 C ILE A 106 -11.032 -30.568 23.689 1.00 48.43 C ANISOU 829 C ILE A 106 7565 3883 6952 1216 -709 398 C ATOM 830 O ILE A 106 -10.288 -31.550 23.578 1.00 49.66 O ANISOU 830 O ILE A 106 7781 3846 7243 1377 -764 374 O ATOM 831 CB ILE A 106 -11.053 -29.078 21.647 1.00 46.71 C ANISOU 831 CB ILE A 106 7097 3958 6693 1178 -467 142 C ATOM 832 CG1 ILE A 106 -9.912 -29.782 20.914 1.00 52.94 C ANISOU 832 CG1 ILE A 106 7853 4622 7641 1390 -444 24 C ATOM 833 CG2 ILE A 106 -10.478 -27.964 22.506 1.00 45.18 C ANISOU 833 CG2 ILE A 106 6741 3949 6477 1209 -518 222 C ATOM 834 CD1 ILE A 106 -10.345 -30.479 19.650 1.00 58.18 C ANISOU 834 CD1 ILE A 106 8624 5173 8310 1366 -343 -121 C ATOM 835 N ALA A 107 -11.146 -29.907 24.840 1.00 48.48 N ANISOU 835 N ALA A 107 7544 4006 6871 1156 -782 533 N ATOM 836 CA ALA A 107 -10.251 -30.187 25.956 1.00 49.73 C ANISOU 836 CA ALA A 107 7714 4096 7086 1292 -937 651 C ATOM 837 C ALA A 107 -10.768 -31.298 26.861 1.00 59.56 C ANISOU 837 C ALA A 107 9202 5128 8299 1237 -1043 801 C ATOM 838 O ALA A 107 -9.981 -32.128 27.330 1.00 63.57 O ANISOU 838 O ALA A 107 9783 5460 8912 1393 -1169 861 O ATOM 839 CB ALA A 107 -10.015 -28.916 26.774 1.00 48.21 C ANISOU 839 CB ALA A 107 7381 4130 6807 1264 -977 717 C ATOM 840 N ILE A 108 -12.071 -31.335 27.123 1.00 60.37 N ANISOU 840 N ILE A 108 9432 5239 8265 1018 -994 867 N ATOM 841 CA ILE A 108 -12.640 -32.381 27.970 1.00 60.25 C ANISOU 841 CA ILE A 108 9658 5024 8211 935 -1075 1017 C ATOM 842 C ILE A 108 -13.898 -32.945 27.317 1.00 57.01 C ANISOU 842 C ILE A 108 9372 4525 7764 745 -972 977 C ATOM 843 O ILE A 108 -14.997 -32.811 27.872 1.00 56.13 O ANISOU 843 O ILE A 108 9340 4464 7523 539 -937 1070 O ATOM 844 CB ILE A 108 -12.932 -31.849 29.381 1.00 60.92 C ANISOU 844 CB ILE A 108 9786 5217 8144 842 -1144 1189 C ATOM 845 CG1 ILE A 108 -13.617 -30.480 29.312 1.00 58.53 C ANISOU 845 CG1 ILE A 108 9334 5194 7711 698 -1031 1146 C ATOM 846 CG2 ILE A 108 -11.644 -31.772 30.193 1.00 60.74 C ANISOU 846 CG2 ILE A 108 9719 5184 8175 1040 -1305 1261 C ATOM 847 CD1 ILE A 108 -14.310 -30.080 30.600 1.00 61.69 C ANISOU 847 CD1 ILE A 108 9819 5686 7935 550 -1054 1300 C ATOM 848 N PRO A 109 -13.788 -33.598 26.156 1.00 57.76 N ANISOU 848 N PRO A 109 9488 4488 7970 802 -921 836 N ATOM 849 CA PRO A 109 -15.002 -34.092 25.483 1.00 59.22 C ANISOU 849 CA PRO A 109 9784 4598 8120 610 -835 785 C ATOM 850 C PRO A 109 -15.789 -35.108 26.297 1.00 63.75 C ANISOU 850 C PRO A 109 10594 4970 8658 464 -892 938 C ATOM 851 O PRO A 109 -17.011 -35.205 26.129 1.00 62.49 O ANISOU 851 O PRO A 109 10494 4821 8426 243 -821 944 O ATOM 852 CB PRO A 109 -14.450 -34.710 24.189 1.00 58.35 C ANISOU 852 CB PRO A 109 9673 4352 8146 747 -798 605 C ATOM 853 CG PRO A 109 -13.030 -35.061 24.515 1.00 58.59 C ANISOU 853 CG PRO A 109 9676 4279 8305 1008 -896 619 C ATOM 854 CD PRO A 109 -12.561 -33.971 25.431 1.00 59.13 C ANISOU 854 CD PRO A 109 9593 4566 8308 1044 -942 715 C ATOM 855 N LEU A 110 -15.132 -35.861 27.185 1.00 68.17 N ANISOU 855 N LEU A 110 11248 5392 9263 569 -1002 1056 N ATOM 856 CA LEU A 110 -15.841 -36.897 27.930 1.00 76.52 C ANISOU 856 CA LEU A 110 12466 6326 10282 421 -1017 1182 C ATOM 857 C LEU A 110 -16.800 -36.310 28.958 1.00 78.54 C ANISOU 857 C LEU A 110 12743 6734 10364 213 -987 1326 C ATOM 858 O LEU A 110 -17.784 -36.963 29.323 1.00 80.73 O ANISOU 858 O LEU A 110 13134 6948 10590 22 -947 1401 O ATOM 859 CB LEU A 110 -14.846 -37.839 28.610 1.00 78.74 C ANISOU 859 CB LEU A 110 12800 6470 10649 591 -1125 1257 C ATOM 860 CG LEU A 110 -13.977 -38.675 27.668 1.00 79.81 C ANISOU 860 CG LEU A 110 12929 6430 10967 785 -1141 1121 C ATOM 861 CD1 LEU A 110 -13.031 -39.572 28.452 1.00 80.56 C ANISOU 861 CD1 LEU A 110 13070 6397 11141 945 -1253 1215 C ATOM 862 CD2 LEU A 110 -14.850 -39.497 26.733 1.00 80.16 C ANISOU 862 CD2 LEU A 110 13087 6318 11050 654 -1065 1025 C ATOM 863 N ARG A 111 -16.545 -35.092 29.435 1.00 77.20 N ANISOU 863 N ARG A 111 12461 6769 10105 243 -996 1361 N ATOM 864 CA ARG A 111 -17.435 -34.448 30.393 1.00 77.20 C ANISOU 864 CA ARG A 111 12467 6935 9933 55 -949 1480 C ATOM 865 C ARG A 111 -18.185 -33.263 29.801 1.00 68.87 C ANISOU 865 C ARG A 111 11284 6078 8807 -64 -840 1398 C ATOM 866 O ARG A 111 -18.861 -32.542 30.542 1.00 64.61 O ANISOU 866 O ARG A 111 10711 5710 8127 -200 -788 1474 O ATOM 867 CB ARG A 111 -16.662 -34.009 31.638 1.00 84.79 C ANISOU 867 CB ARG A 111 13395 8004 10817 157 -1040 1593 C ATOM 868 CG ARG A 111 -15.162 -33.908 31.460 1.00 91.92 C ANISOU 868 CG ARG A 111 14204 8883 11838 424 -1152 1539 C ATOM 869 CD ARG A 111 -14.490 -33.638 32.797 1.00 99.34 C ANISOU 869 CD ARG A 111 15130 9917 12697 496 -1254 1659 C ATOM 870 NE ARG A 111 -13.034 -33.618 32.697 1.00104.76 N ANISOU 870 NE ARG A 111 15706 10586 13511 744 -1368 1613 N ATOM 871 CZ ARG A 111 -12.224 -33.275 33.693 1.00108.03 C ANISOU 871 CZ ARG A 111 16071 11093 13883 838 -1476 1686 C ATOM 872 NH1 ARG A 111 -12.731 -32.920 34.867 1.00109.16 N ANISOU 872 NH1 ARG A 111 16282 11348 13847 710 -1482 1804 N ATOM 873 NH2 ARG A 111 -10.910 -33.284 33.518 1.00109.22 N ANISOU 873 NH2 ARG A 111 16096 11231 14170 1056 -1572 1632 N ATOM 874 N TYR A 112 -18.094 -33.049 28.485 1.00 66.20 N ANISOU 874 N TYR A 112 10818 5776 8557 -14 -779 1217 N ATOM 875 CA TYR A 112 -18.784 -31.920 27.868 1.00 61.05 C ANISOU 875 CA TYR A 112 9982 5371 7845 -115 -662 1111 C ATOM 876 C TYR A 112 -20.294 -32.037 28.038 1.00 64.29 C ANISOU 876 C TYR A 112 10446 5809 8171 -376 -577 1159 C ATOM 877 O TYR A 112 -20.956 -31.088 28.474 1.00 62.65 O ANISOU 877 O TYR A 112 10137 5812 7855 -485 -509 1186 O ATOM 878 CB TYR A 112 -18.417 -31.822 26.384 1.00 53.15 C ANISOU 878 CB TYR A 112 8874 4375 6946 -19 -618 917 C ATOM 879 CG TYR A 112 -19.197 -30.767 25.628 1.00 50.97 C ANISOU 879 CG TYR A 112 8434 4324 6610 -129 -510 809 C ATOM 880 CD1 TYR A 112 -20.416 -31.067 25.026 1.00 53.16 C ANISOU 880 CD1 TYR A 112 8745 4582 6871 -316 -446 763 C ATOM 881 CD2 TYR A 112 -18.716 -29.470 25.512 1.00 46.74 C ANISOU 881 CD2 TYR A 112 7709 4012 6038 -46 -481 757 C ATOM 882 CE1 TYR A 112 -21.133 -30.104 24.340 1.00 50.56 C ANISOU 882 CE1 TYR A 112 8266 4454 6491 -406 -366 671 C ATOM 883 CE2 TYR A 112 -19.425 -28.503 24.827 1.00 42.79 C ANISOU 883 CE2 TYR A 112 7071 3702 5484 -137 -393 668 C ATOM 884 CZ TYR A 112 -20.631 -28.825 24.243 1.00 47.15 C ANISOU 884 CZ TYR A 112 7660 4234 6021 -311 -340 627 C ATOM 885 OH TYR A 112 -21.340 -27.863 23.559 1.00 46.86 O ANISOU 885 OH TYR A 112 7485 4384 5935 -391 -270 543 O ATOM 886 N ASN A 113 -20.858 -33.198 27.693 1.00 68.09 N ANISOU 886 N ASN A 113 11082 6079 8712 -480 -577 1163 N ATOM 887 CA ASN A 113 -22.311 -33.343 27.701 1.00 71.79 C ANISOU 887 CA ASN A 113 11575 6574 9127 -739 -493 1189 C ATOM 888 C ASN A 113 -22.889 -33.218 29.106 1.00 72.86 C ANISOU 888 C ASN A 113 11778 6768 9136 -877 -470 1372 C ATOM 889 O ASN A 113 -24.047 -32.813 29.262 1.00 72.48 O ANISOU 889 O ASN A 113 11664 6855 9019 -1073 -372 1386 O ATOM 890 CB ASN A 113 -22.708 -34.676 27.067 1.00 75.58 C ANISOU 890 CB ASN A 113 12219 6790 9706 -824 -512 1157 C ATOM 891 CG ASN A 113 -22.441 -34.709 25.574 1.00 77.48 C ANISOU 891 CG ASN A 113 12388 7008 10042 -737 -504 953 C ATOM 892 OD1 ASN A 113 -22.378 -33.666 24.920 1.00 74.17 O ANISOU 892 OD1 ASN A 113 11783 6801 9598 -687 -455 840 O ATOM 893 ND2 ASN A 113 -22.286 -35.908 25.025 1.00 81.29 N ANISOU 893 ND2 ASN A 113 13032 7226 10628 -719 -551 907 N ATOM 894 N GLY A 114 -22.103 -33.544 30.136 1.00 73.08 N ANISOU 894 N GLY A 114 11908 6726 9133 -767 -552 1497 N ATOM 895 CA GLY A 114 -22.564 -33.374 31.502 1.00 74.59 C ANISOU 895 CA GLY A 114 12114 7037 9189 -864 -515 1635 C ATOM 896 C GLY A 114 -22.384 -31.979 32.061 1.00 73.31 C ANISOU 896 C GLY A 114 11836 7113 8905 -829 -494 1654 C ATOM 897 O GLY A 114 -23.109 -31.597 32.986 1.00 75.96 O ANISOU 897 O GLY A 114 12149 7595 9116 -952 -416 1726 O ATOM 898 N LEU A 115 -21.436 -31.211 31.525 1.00 66.40 N ANISOU 898 N LEU A 115 10853 6304 8071 -649 -548 1565 N ATOM 899 CA LEU A 115 -21.165 -29.851 31.975 1.00 62.00 C ANISOU 899 CA LEU A 115 10141 5996 7419 -590 -530 1546 C ATOM 900 C LEU A 115 -21.924 -28.800 31.179 1.00 56.51 C ANISOU 900 C LEU A 115 9239 5515 6718 -666 -411 1410 C ATOM 901 O LEU A 115 -22.477 -27.865 31.766 1.00 53.03 O ANISOU 901 O LEU A 115 8717 5266 6164 -744 -341 1431 O ATOM 902 CB LEU A 115 -19.662 -29.557 31.893 1.00 65.39 C ANISOU 902 CB LEU A 115 10511 6420 7913 -343 -650 1507 C ATOM 903 CG LEU A 115 -19.221 -28.090 31.933 1.00 67.81 C ANISOU 903 CG LEU A 115 10620 6973 8172 -260 -635 1433 C ATOM 904 CD1 LEU A 115 -19.596 -27.429 33.248 1.00 69.12 C ANISOU 904 CD1 LEU A 115 10820 7279 8164 -344 -621 1543 C ATOM 905 CD2 LEU A 115 -17.725 -27.973 31.689 1.00 68.57 C ANISOU 905 CD2 LEU A 115 10647 7038 8371 -26 -751 1383 C ATOM 906 N VAL A 116 -21.967 -28.934 29.858 1.00 54.08 N ANISOU 906 N VAL A 116 8852 5173 6525 -641 -390 1270 N ATOM 907 CA VAL A 116 -22.552 -27.930 28.980 1.00 52.41 C ANISOU 907 CA VAL A 116 8446 5151 6314 -685 -302 1137 C ATOM 908 C VAL A 116 -23.905 -28.466 28.521 1.00 55.76 C ANISOU 908 C VAL A 116 8895 5537 6755 -893 -226 1119 C ATOM 909 O VAL A 116 -23.983 -29.316 27.630 1.00 61.00 O ANISOU 909 O VAL A 116 9617 6045 7513 -909 -245 1054 O ATOM 910 CB VAL A 116 -21.630 -27.611 27.800 1.00 49.71 C ANISOU 910 CB VAL A 116 7998 4819 6071 -514 -332 991 C ATOM 911 CG1 VAL A 116 -22.112 -26.377 27.079 1.00 46.93 C ANISOU 911 CG1 VAL A 116 7455 4682 5694 -544 -255 879 C ATOM 912 CG2 VAL A 116 -20.199 -27.423 28.283 1.00 47.61 C ANISOU 912 CG2 VAL A 116 7729 4537 5825 -312 -425 1021 C ATOM 913 N THR A 117 -24.977 -27.971 29.135 1.00 50.22 N ANISOU 913 N THR A 117 8143 4975 5964 -1053 -138 1171 N ATOM 914 CA THR A 117 -26.332 -28.396 28.821 1.00 47.94 C ANISOU 914 CA THR A 117 7846 4675 5695 -1267 -62 1162 C ATOM 915 C THR A 117 -27.128 -27.219 28.276 1.00 46.30 C ANISOU 915 C THR A 117 7422 4698 5471 -1317 16 1058 C ATOM 916 O THR A 117 -26.744 -26.055 28.430 1.00 45.06 O ANISOU 916 O THR A 117 7146 4712 5263 -1213 26 1025 O ATOM 917 CB THR A 117 -27.044 -28.974 30.054 1.00 51.82 C ANISOU 917 CB THR A 117 8465 5118 6106 -1437 -11 1323 C ATOM 918 OG1 THR A 117 -27.199 -27.949 31.043 1.00 52.99 O ANISOU 918 OG1 THR A 117 8540 5466 6127 -1439 51 1377 O ATOM 919 CG2 THR A 117 -26.246 -30.122 30.650 1.00 52.72 C ANISOU 919 CG2 THR A 117 8812 4993 6228 -1381 -103 1443 C ATOM 920 N GLY A 118 -28.254 -27.537 27.633 1.00 43.10 N ANISOU 920 N GLY A 118 6968 4290 5117 -1481 61 1008 N ATOM 921 CA GLY A 118 -29.091 -26.490 27.070 1.00 44.27 C ANISOU 921 CA GLY A 118 6911 4644 5264 -1530 119 912 C ATOM 922 C GLY A 118 -29.721 -25.606 28.130 1.00 45.87 C ANISOU 922 C GLY A 118 7021 5037 5372 -1593 213 978 C ATOM 923 O GLY A 118 -29.858 -24.394 27.938 1.00 44.63 O ANISOU 923 O GLY A 118 6702 5066 5191 -1533 242 909 O ATOM 924 N THR A 119 -30.110 -26.198 29.261 1.00 48.64 N ANISOU 924 N THR A 119 7482 5336 5664 -1714 267 1110 N ATOM 925 CA THR A 119 -30.733 -25.427 30.333 1.00 48.60 C ANISOU 925 CA THR A 119 7404 5507 5554 -1781 375 1171 C ATOM 926 C THR A 119 -29.748 -24.449 30.957 1.00 43.68 C ANISOU 926 C THR A 119 6775 4984 4836 -1602 348 1180 C ATOM 927 O THR A 119 -30.093 -23.289 31.209 1.00 48.85 O ANISOU 927 O THR A 119 7290 5832 5439 -1580 412 1136 O ATOM 928 CB THR A 119 -31.302 -26.371 31.391 1.00 52.66 C ANISOU 928 CB THR A 119 8058 5934 6016 -1946 442 1312 C ATOM 929 OG1 THR A 119 -32.351 -27.149 30.808 1.00 57.50 O ANISOU 929 OG1 THR A 119 8623 6488 6736 -2106 472 1277 O ATOM 930 CG2 THR A 119 -31.860 -25.587 32.567 1.00 53.98 C ANISOU 930 CG2 THR A 119 8137 6296 6076 -1955 556 1343 C ATOM 931 N ARG A 120 -28.517 -24.895 31.211 1.00 41.93 N ANISOU 931 N ARG A 120 6700 4630 4599 -1471 247 1231 N ATOM 932 CA ARG A 120 -27.489 -23.975 31.686 1.00 45.30 C ANISOU 932 CA ARG A 120 7109 5147 4957 -1297 198 1225 C ATOM 933 C ARG A 120 -27.164 -22.921 30.634 1.00 44.02 C ANISOU 933 C ARG A 120 6769 5100 4858 -1175 175 1080 C ATOM 934 O ARG A 120 -26.900 -21.760 30.969 1.00 41.81 O ANISOU 934 O ARG A 120 6398 4969 4518 -1095 187 1048 O ATOM 935 CB ARG A 120 -26.233 -24.752 32.075 1.00 47.14 C ANISOU 935 CB ARG A 120 7519 5205 5188 -1179 78 1305 C ATOM 936 CG ARG A 120 -26.442 -25.686 33.256 1.00 54.66 C ANISOU 936 CG ARG A 120 8672 6044 6050 -1284 88 1470 C ATOM 937 CD ARG A 120 -25.271 -26.634 33.441 1.00 54.48 C ANISOU 937 CD ARG A 120 8828 5811 6060 -1164 -51 1545 C ATOM 938 NE ARG A 120 -25.481 -27.523 34.577 1.00 58.59 N ANISOU 938 NE ARG A 120 9514 6241 6509 -1238 -46 1683 N ATOM 939 CZ ARG A 120 -24.692 -28.548 34.878 1.00 60.23 C ANISOU 939 CZ ARG A 120 9874 6259 6752 -1153 -157 1756 C ATOM 940 NH1 ARG A 120 -24.963 -29.303 35.933 1.00 60.70 N ANISOU 940 NH1 ARG A 120 10046 6268 6750 -1212 -141 1861 N ATOM 941 NH2 ARG A 120 -23.635 -28.820 34.123 1.00 58.44 N ANISOU 941 NH2 ARG A 120 9684 5894 6628 -1002 -280 1721 N ATOM 942 N ALA A 121 -27.176 -23.308 29.355 1.00 43.08 N ANISOU 942 N ALA A 121 6610 4905 4851 -1164 140 990 N ATOM 943 CA ALA A 121 -26.901 -22.353 28.285 1.00 38.82 C ANISOU 943 CA ALA A 121 5920 4469 4362 -1061 122 860 C ATOM 944 C ALA A 121 -27.960 -21.258 28.237 1.00 38.67 C ANISOU 944 C ALA A 121 5733 4644 4315 -1131 205 809 C ATOM 945 O ALA A 121 -27.635 -20.076 28.075 1.00 34.17 O ANISOU 945 O ALA A 121 5054 4202 3725 -1031 203 749 O ATOM 946 CB ALA A 121 -26.817 -23.078 26.941 1.00 37.10 C ANISOU 946 CB ALA A 121 5718 4129 4250 -1054 76 775 C ATOM 947 N ALA A 122 -29.234 -21.631 28.385 1.00 39.37 N ANISOU 947 N ALA A 122 5794 4754 4410 -1302 279 831 N ATOM 948 CA ALA A 122 -30.300 -20.634 28.369 1.00 38.17 C ANISOU 948 CA ALA A 122 5469 4786 4248 -1363 359 781 C ATOM 949 C ALA A 122 -30.178 -19.677 29.549 1.00 40.12 C ANISOU 949 C ALA A 122 5692 5164 4386 -1316 418 822 C ATOM 950 O ALA A 122 -30.468 -18.481 29.421 1.00 39.17 O ANISOU 950 O ALA A 122 5430 5194 4257 -1267 449 753 O ATOM 951 CB ALA A 122 -31.662 -21.324 28.377 1.00 37.95 C ANISOU 951 CB ALA A 122 5407 4750 4261 -1564 429 803 C ATOM 952 N GLY A 123 -29.752 -20.186 30.707 1.00 40.27 N ANISOU 952 N GLY A 123 5861 5122 4317 -1330 427 932 N ATOM 953 CA GLY A 123 -29.537 -19.315 31.849 1.00 35.51 C ANISOU 953 CA GLY A 123 5264 4635 3592 -1281 471 966 C ATOM 954 C GLY A 123 -28.384 -18.355 31.635 1.00 35.59 C ANISOU 954 C GLY A 123 5241 4687 3596 -1098 386 906 C ATOM 955 O GLY A 123 -28.470 -17.179 31.997 1.00 37.58 O ANISOU 955 O GLY A 123 5406 5078 3795 -1049 423 862 O ATOM 956 N ILE A 124 -27.292 -18.841 31.040 1.00 31.38 N ANISOU 956 N ILE A 124 4772 4030 3122 -997 276 900 N ATOM 957 CA ILE A 124 -26.155 -17.974 30.740 1.00 30.87 C ANISOU 957 CA ILE A 124 4659 4001 3069 -834 199 841 C ATOM 958 C ILE A 124 -26.560 -16.882 29.758 1.00 31.13 C ANISOU 958 C ILE A 124 4520 4151 3158 -805 226 725 C ATOM 959 O ILE A 124 -26.160 -15.718 29.898 1.00 29.74 O ANISOU 959 O ILE A 124 4272 4073 2953 -719 218 681 O ATOM 960 CB ILE A 124 -24.981 -18.812 30.200 1.00 31.72 C ANISOU 960 CB ILE A 124 4850 3952 3250 -738 93 850 C ATOM 961 CG1 ILE A 124 -24.422 -19.712 31.305 1.00 40.50 C ANISOU 961 CG1 ILE A 124 6137 4950 4300 -735 42 974 C ATOM 962 CG2 ILE A 124 -23.893 -17.918 29.625 1.00 29.83 C ANISOU 962 CG2 ILE A 124 4525 3758 3052 -586 32 773 C ATOM 963 CD1 ILE A 124 -23.316 -20.643 30.832 1.00 44.39 C ANISOU 963 CD1 ILE A 124 6713 5273 4880 -632 -64 985 C ATOM 964 N ILE A 125 -27.350 -17.242 28.744 1.00 29.59 N ANISOU 964 N ILE A 125 4263 3938 3041 -876 248 676 N ATOM 965 CA ILE A 125 -27.780 -16.265 27.747 1.00 30.48 C ANISOU 965 CA ILE A 125 4225 4152 3203 -849 257 575 C ATOM 966 C ILE A 125 -28.614 -15.169 28.400 1.00 26.84 C ANISOU 966 C ILE A 125 3661 3847 2692 -876 335 559 C ATOM 967 O ILE A 125 -28.431 -13.979 28.123 1.00 26.07 O ANISOU 967 O ILE A 125 3472 3838 2595 -791 326 497 O ATOM 968 CB ILE A 125 -28.547 -16.966 26.611 1.00 32.24 C ANISOU 968 CB ILE A 125 4418 4323 3509 -935 251 530 C ATOM 969 CG1 ILE A 125 -27.578 -17.795 25.765 1.00 31.56 C ANISOU 969 CG1 ILE A 125 4424 4092 3475 -872 174 511 C ATOM 970 CG2 ILE A 125 -29.290 -15.948 25.745 1.00 27.76 C ANISOU 970 CG2 ILE A 125 3693 3876 2978 -931 262 442 C ATOM 971 CD1 ILE A 125 -28.264 -18.799 24.851 1.00 28.39 C ANISOU 971 CD1 ILE A 125 4047 3600 3139 -973 161 479 C ATOM 972 N ALA A 126 -29.544 -15.557 29.279 1.00 29.33 N ANISOU 972 N ALA A 126 3990 4192 2962 -994 420 614 N ATOM 973 CA ALA A 126 -30.357 -14.577 29.998 1.00 29.64 C ANISOU 973 CA ALA A 126 3933 4379 2949 -1015 513 594 C ATOM 974 C ALA A 126 -29.487 -13.644 30.836 1.00 30.32 C ANISOU 974 C ALA A 126 4061 4516 2945 -904 498 596 C ATOM 975 O ALA A 126 -29.679 -12.422 30.837 1.00 26.15 O ANISOU 975 O ALA A 126 3432 4093 2410 -843 521 528 O ATOM 976 CB ALA A 126 -31.377 -15.302 30.882 1.00 27.24 C ANISOU 976 CB ALA A 126 3658 4090 2604 -1169 622 664 C ATOM 977 N ILE A 127 -28.521 -14.210 31.562 1.00 30.47 N ANISOU 977 N ILE A 127 4230 4453 2895 -875 449 671 N ATOM 978 CA ILE A 127 -27.635 -13.398 32.393 1.00 27.80 C ANISOU 978 CA ILE A 127 3939 4155 2468 -778 413 673 C ATOM 979 C ILE A 127 -26.830 -12.440 31.531 1.00 26.88 C ANISOU 979 C ILE A 127 3738 4055 2419 -653 335 590 C ATOM 980 O ILE A 127 -26.619 -11.276 31.896 1.00 25.63 O ANISOU 980 O ILE A 127 3537 3979 2221 -590 337 543 O ATOM 981 CB ILE A 127 -26.715 -14.304 33.232 1.00 29.16 C ANISOU 981 CB ILE A 127 4288 4224 2568 -768 347 775 C ATOM 982 CG1 ILE A 127 -27.526 -15.039 34.299 1.00 33.11 C ANISOU 982 CG1 ILE A 127 4890 4724 2965 -898 439 868 C ATOM 983 CG2 ILE A 127 -25.580 -13.492 33.864 1.00 29.94 C ANISOU 983 CG2 ILE A 127 4424 4351 2600 -653 267 766 C ATOM 984 CD1 ILE A 127 -26.793 -16.215 34.912 1.00 36.53 C ANISOU 984 CD1 ILE A 127 5512 5020 3348 -908 365 987 C ATOM 985 N CYS A 128 -26.370 -12.909 30.370 1.00 24.09 N ANISOU 985 N CYS A 128 3366 3620 2165 -621 272 568 N ATOM 986 CA CYS A 128 -25.542 -12.064 29.522 1.00 24.48 C ANISOU 986 CA CYS A 128 3347 3682 2274 -513 209 499 C ATOM 987 C CYS A 128 -26.349 -10.915 28.922 1.00 23.92 C ANISOU 987 C CYS A 128 3141 3713 2233 -509 253 419 C ATOM 988 O CYS A 128 -25.823 -9.811 28.760 1.00 22.91 O ANISOU 988 O CYS A 128 2966 3629 2112 -428 225 371 O ATOM 989 CB CYS A 128 -24.874 -12.909 28.438 1.00 32.19 C ANISOU 989 CB CYS A 128 4347 4547 3336 -482 148 493 C ATOM 990 SG CYS A 128 -23.541 -13.962 29.094 1.00 33.28 S ANISOU 990 SG CYS A 128 4625 4558 3462 -425 65 573 S ATOM 991 N TRP A 129 -27.629 -11.141 28.607 1.00 24.45 N ANISOU 991 N TRP A 129 3146 3817 2328 -595 316 405 N ATOM 992 CA TRP A 129 -28.457 -10.036 28.125 1.00 25.67 C ANISOU 992 CA TRP A 129 3168 4069 2517 -581 347 334 C ATOM 993 C TRP A 129 -28.701 -9.006 29.224 1.00 23.27 C ANISOU 993 C TRP A 129 2841 3858 2142 -554 404 317 C ATOM 994 O TRP A 129 -28.699 -7.799 28.958 1.00 22.50 O ANISOU 994 O TRP A 129 2671 3815 2064 -482 394 256 O ATOM 995 CB TRP A 129 -29.783 -10.561 27.570 1.00 23.52 C ANISOU 995 CB TRP A 129 2817 3818 2302 -681 389 321 C ATOM 996 CG TRP A 129 -29.686 -10.971 26.132 1.00 25.80 C ANISOU 996 CG TRP A 129 3088 4046 2667 -680 320 290 C ATOM 997 CD1 TRP A 129 -29.546 -12.237 25.646 1.00 25.91 C ANISOU 997 CD1 TRP A 129 3176 3959 2710 -738 290 315 C ATOM 998 CD2 TRP A 129 -29.696 -10.099 24.988 1.00 26.10 C ANISOU 998 CD2 TRP A 129 3048 4115 2753 -616 270 225 C ATOM 999 NE1 TRP A 129 -29.477 -12.210 24.269 1.00 26.55 N ANISOU 999 NE1 TRP A 129 3228 4013 2845 -715 230 261 N ATOM 1000 CE2 TRP A 129 -29.568 -10.912 23.842 1.00 25.67 C ANISOU 1000 CE2 TRP A 129 3027 3985 2740 -643 215 211 C ATOM 1001 CE3 TRP A 129 -29.805 -8.712 24.824 1.00 22.91 C ANISOU 1001 CE3 TRP A 129 2563 3788 2355 -539 264 178 C ATOM 1002 CZ2 TRP A 129 -29.550 -10.383 22.546 1.00 26.17 C ANISOU 1002 CZ2 TRP A 129 3049 4057 2836 -600 158 157 C ATOM 1003 CZ3 TRP A 129 -29.786 -8.187 23.535 1.00 24.77 C ANISOU 1003 CZ3 TRP A 129 2757 4023 2634 -496 202 133 C ATOM 1004 CH2 TRP A 129 -29.659 -9.023 22.416 1.00 27.57 C ANISOU 1004 CH2 TRP A 129 3150 4312 3014 -529 151 125 C ATOM 1005 N VAL A 130 -28.909 -9.456 30.465 1.00 23.24 N ANISOU 1005 N VAL A 130 2911 3869 2050 -609 465 371 N ATOM 1006 CA VAL A 130 -29.087 -8.508 31.562 1.00 25.66 C ANISOU 1006 CA VAL A 130 3218 4263 2269 -581 524 346 C ATOM 1007 C VAL A 130 -27.819 -7.683 31.749 1.00 25.60 C ANISOU 1007 C VAL A 130 3260 4237 2231 -475 439 324 C ATOM 1008 O VAL A 130 -27.866 -6.452 31.869 1.00 22.88 O ANISOU 1008 O VAL A 130 2862 3949 1881 -413 447 257 O ATOM 1009 CB VAL A 130 -29.485 -9.241 32.856 1.00 26.35 C ANISOU 1009 CB VAL A 130 3402 4366 2244 -671 609 417 C ATOM 1010 CG1 VAL A 130 -29.422 -8.285 34.058 1.00 26.93 C ANISOU 1010 CG1 VAL A 130 3514 4519 2198 -630 659 387 C ATOM 1011 CG2 VAL A 130 -30.884 -9.825 32.726 1.00 27.17 C ANISOU 1011 CG2 VAL A 130 3424 4511 2389 -788 716 426 C ATOM 1012 N LEU A 131 -26.662 -8.350 31.750 1.00 25.11 N ANISOU 1012 N LEU A 131 3292 4087 2161 -451 351 376 N ATOM 1013 CA LEU A 131 -25.399 -7.634 31.895 1.00 25.42 C ANISOU 1013 CA LEU A 131 3361 4108 2189 -360 262 356 C ATOM 1014 C LEU A 131 -25.140 -6.696 30.721 1.00 24.94 C ANISOU 1014 C LEU A 131 3197 4053 2227 -295 225 286 C ATOM 1015 O LEU A 131 -24.512 -5.645 30.893 1.00 22.68 O ANISOU 1015 O LEU A 131 2899 3785 1933 -233 185 244 O ATOM 1016 CB LEU A 131 -24.250 -8.633 32.042 1.00 22.77 C ANISOU 1016 CB LEU A 131 3124 3678 1849 -342 173 427 C ATOM 1017 CG LEU A 131 -24.251 -9.456 33.330 1.00 30.35 C ANISOU 1017 CG LEU A 131 4220 4620 2693 -392 180 511 C ATOM 1018 CD1 LEU A 131 -23.203 -10.553 33.258 1.00 33.72 C ANISOU 1018 CD1 LEU A 131 4731 4933 3147 -364 81 583 C ATOM 1019 CD2 LEU A 131 -24.013 -8.557 34.538 1.00 28.67 C ANISOU 1019 CD2 LEU A 131 4060 4476 2360 -367 175 494 C ATOM 1020 N SER A 132 -25.601 -7.061 29.525 1.00 22.48 N ANISOU 1020 N SER A 132 2821 3719 2001 -315 232 274 N ATOM 1021 CA SER A 132 -25.422 -6.193 28.365 1.00 21.80 C ANISOU 1021 CA SER A 132 2654 3637 1993 -262 200 217 C ATOM 1022 C SER A 132 -26.222 -4.901 28.512 1.00 22.54 C ANISOU 1022 C SER A 132 2672 3807 2083 -238 241 157 C ATOM 1023 O SER A 132 -25.738 -3.817 28.159 1.00 19.69 O ANISOU 1023 O SER A 132 2284 3447 1748 -177 204 116 O ATOM 1024 CB SER A 132 -25.830 -6.933 27.092 1.00 20.12 C ANISOU 1024 CB SER A 132 2408 3388 1851 -295 195 217 C ATOM 1025 OG SER A 132 -24.982 -8.045 26.869 1.00 21.89 O ANISOU 1025 OG SER A 132 2703 3526 2087 -297 156 258 O ATOM 1026 N PHE A 133 -27.453 -4.997 29.021 1.00 22.09 N ANISOU 1026 N PHE A 133 2579 3811 2003 -287 320 150 N ATOM 1027 CA PHE A 133 -28.220 -3.787 29.297 1.00 23.19 C ANISOU 1027 CA PHE A 133 2646 4022 2143 -250 366 85 C ATOM 1028 C PHE A 133 -27.543 -2.943 30.369 1.00 22.70 C ANISOU 1028 C PHE A 133 2649 3972 2005 -201 360 61 C ATOM 1029 O PHE A 133 -27.474 -1.715 30.245 1.00 23.14 O ANISOU 1029 O PHE A 133 2671 4038 2083 -136 343 1 O ATOM 1030 CB PHE A 133 -29.648 -4.144 29.711 1.00 21.33 C ANISOU 1030 CB PHE A 133 2345 3857 1904 -314 468 80 C ATOM 1031 CG PHE A 133 -30.586 -4.301 28.550 1.00 25.89 C ANISOU 1031 CG PHE A 133 2807 4448 2582 -337 461 62 C ATOM 1032 CD1 PHE A 133 -31.282 -3.205 28.052 1.00 26.17 C ANISOU 1032 CD1 PHE A 133 2734 4528 2683 -276 458 -1 C ATOM 1033 CD2 PHE A 133 -30.764 -5.541 27.942 1.00 27.66 C ANISOU 1033 CD2 PHE A 133 3039 4632 2838 -417 445 108 C ATOM 1034 CE1 PHE A 133 -32.146 -3.340 26.969 1.00 27.38 C ANISOU 1034 CE1 PHE A 133 2782 4695 2926 -294 429 -15 C ATOM 1035 CE2 PHE A 133 -31.624 -5.687 26.857 1.00 27.09 C ANISOU 1035 CE2 PHE A 133 2866 4573 2853 -444 421 86 C ATOM 1036 CZ PHE A 133 -32.316 -4.582 26.369 1.00 28.22 C ANISOU 1036 CZ PHE A 133 2896 4770 3056 -382 409 26 C ATOM 1037 N ALA A 134 -27.031 -3.583 31.425 1.00 22.55 N ANISOU 1037 N ALA A 134 2733 3944 1890 -232 364 107 N ATOM 1038 CA ALA A 134 -26.369 -2.846 32.498 1.00 22.17 C ANISOU 1038 CA ALA A 134 2761 3908 1753 -193 343 82 C ATOM 1039 C ALA A 134 -25.136 -2.108 31.980 1.00 26.89 C ANISOU 1039 C ALA A 134 3361 4452 2403 -129 236 60 C ATOM 1040 O ALA A 134 -24.922 -0.932 32.299 1.00 25.01 O ANISOU 1040 O ALA A 134 3124 4226 2154 -83 219 -2 O ATOM 1041 CB ALA A 134 -25.990 -3.799 33.634 1.00 23.91 C ANISOU 1041 CB ALA A 134 3106 4122 1857 -241 345 151 C ATOM 1042 N ILE A 135 -24.315 -2.785 31.174 1.00 22.61 N ANISOU 1042 N ILE A 135 2818 3849 1922 -130 169 105 N ATOM 1043 CA ILE A 135 -23.104 -2.167 30.640 1.00 24.52 C ANISOU 1043 CA ILE A 135 3049 4045 2222 -81 82 89 C ATOM 1044 C ILE A 135 -23.450 -1.096 29.609 1.00 22.62 C ANISOU 1044 C ILE A 135 2727 3806 2062 -48 89 36 C ATOM 1045 O ILE A 135 -22.910 0.019 29.637 1.00 20.66 O ANISOU 1045 O ILE A 135 2474 3544 1831 -12 51 -6 O ATOM 1046 CB ILE A 135 -22.189 -3.248 30.037 1.00 25.65 C ANISOU 1046 CB ILE A 135 3205 4128 2414 -85 28 146 C ATOM 1047 CG1 ILE A 135 -21.502 -4.043 31.152 1.00 25.29 C ANISOU 1047 CG1 ILE A 135 3252 4063 2295 -93 -19 200 C ATOM 1048 CG2 ILE A 135 -21.165 -2.638 29.077 1.00 20.98 C ANISOU 1048 CG2 ILE A 135 2563 3499 1910 -44 -27 124 C ATOM 1049 CD1 ILE A 135 -20.922 -5.366 30.677 1.00 27.51 C ANISOU 1049 CD1 ILE A 135 3554 4277 2622 -95 -53 261 C ATOM 1050 N GLY A 136 -24.328 -1.429 28.658 1.00 19.12 N ANISOU 1050 N GLY A 136 2224 3370 1669 -65 128 40 N ATOM 1051 CA GLY A 136 -24.616 -0.505 27.573 1.00 19.32 C ANISOU 1051 CA GLY A 136 2186 3388 1767 -32 117 4 C ATOM 1052 C GLY A 136 -25.380 0.727 28.012 1.00 22.27 C ANISOU 1052 C GLY A 136 2531 3796 2136 7 145 -57 C ATOM 1053 O GLY A 136 -25.230 1.798 27.414 1.00 20.58 O ANISOU 1053 O GLY A 136 2295 3553 1970 49 112 -87 O ATOM 1054 N LEU A 137 -26.206 0.603 29.052 1.00 18.26 N ANISOU 1054 N LEU A 137 2025 3343 1568 -6 212 -77 N ATOM 1055 CA LEU A 137 -26.985 1.729 29.551 1.00 20.31 C ANISOU 1055 CA LEU A 137 2255 3637 1825 41 254 -148 C ATOM 1056 C LEU A 137 -26.378 2.354 30.800 1.00 21.30 C ANISOU 1056 C LEU A 137 2464 3762 1867 61 250 -187 C ATOM 1057 O LEU A 137 -27.040 3.157 31.464 1.00 21.56 O ANISOU 1057 O LEU A 137 2491 3826 1874 98 302 -256 O ATOM 1058 CB LEU A 137 -28.431 1.292 29.836 1.00 22.10 C ANISOU 1058 CB LEU A 137 2412 3938 2048 18 350 -160 C ATOM 1059 CG LEU A 137 -29.170 0.726 28.614 1.00 19.26 C ANISOU 1059 CG LEU A 137 1961 3584 1773 -7 342 -133 C ATOM 1060 CD1 LEU A 137 -30.630 0.428 28.941 1.00 23.78 C ANISOU 1060 CD1 LEU A 137 2438 4236 2361 -33 435 -155 C ATOM 1061 CD2 LEU A 137 -29.066 1.674 27.421 1.00 19.03 C ANISOU 1061 CD2 LEU A 137 1893 3510 1828 55 267 -152 C ATOM 1062 N THR A 138 -25.136 2.010 31.131 1.00 19.54 N ANISOU 1062 N THR A 138 2316 3503 1605 40 184 -152 N ATOM 1063 CA THR A 138 -24.459 2.663 32.249 1.00 21.61 C ANISOU 1063 CA THR A 138 2661 3760 1791 55 152 -193 C ATOM 1064 C THR A 138 -24.479 4.189 32.155 1.00 18.83 C ANISOU 1064 C THR A 138 2299 3375 1480 111 132 -276 C ATOM 1065 O THR A 138 -24.653 4.836 33.202 1.00 22.74 O ANISOU 1065 O THR A 138 2852 3889 1901 132 155 -343 O ATOM 1066 CB THR A 138 -23.024 2.116 32.361 1.00 20.87 C ANISOU 1066 CB THR A 138 2621 3625 1685 31 55 -140 C ATOM 1067 OG1 THR A 138 -23.045 0.860 33.060 1.00 24.43 O ANISOU 1067 OG1 THR A 138 3127 4103 2052 -11 73 -79 O ATOM 1068 CG2 THR A 138 -22.111 3.080 33.111 1.00 24.38 C ANISOU 1068 CG2 THR A 138 3126 4044 2094 49 -20 -192 C ATOM 1069 N PRO A 139 -24.335 4.825 30.981 1.00 20.23 N ANISOU 1069 N PRO A 139 2421 3499 1765 137 92 -276 N ATOM 1070 CA PRO A 139 -24.493 6.291 30.940 1.00 17.50 C ANISOU 1070 CA PRO A 139 2078 3109 1460 192 77 -351 C ATOM 1071 C PRO A 139 -25.837 6.778 31.459 1.00 19.45 C ANISOU 1071 C PRO A 139 2300 3399 1689 244 164 -423 C ATOM 1072 O PRO A 139 -25.903 7.886 32.003 1.00 20.22 O ANISOU 1072 O PRO A 139 2437 3466 1778 292 162 -505 O ATOM 1073 CB PRO A 139 -24.304 6.621 29.452 1.00 19.41 C ANISOU 1073 CB PRO A 139 2268 3294 1813 201 32 -313 C ATOM 1074 CG PRO A 139 -23.379 5.543 28.957 1.00 18.91 C ANISOU 1074 CG PRO A 139 2202 3230 1753 145 -1 -235 C ATOM 1075 CD PRO A 139 -23.841 4.302 29.687 1.00 17.73 C ANISOU 1075 CD PRO A 139 2060 3149 1527 116 52 -209 C ATOM 1076 N AMET A 140 -26.909 5.994 31.324 0.53 19.64 N ANISOU 1076 N AMET A 140 2254 3493 1714 235 242 -401 N ATOM 1077 N BMET A 140 -26.903 5.979 31.311 0.47 19.48 N ANISOU 1077 N BMET A 140 2234 3473 1694 234 242 -400 N ATOM 1078 CA AMET A 140 -28.188 6.427 31.878 0.53 20.75 C ANISOU 1078 CA AMET A 140 2349 3688 1846 285 339 -475 C ATOM 1079 CA BMET A 140 -28.213 6.354 31.840 0.47 21.05 C ANISOU 1079 CA BMET A 140 2383 3729 1886 281 341 -470 C ATOM 1080 C AMET A 140 -28.210 6.399 33.399 0.53 24.10 C ANISOU 1080 C AMET A 140 2857 4163 2138 274 408 -528 C ATOM 1081 C BMET A 140 -28.206 6.489 33.353 0.47 24.04 C ANISOU 1081 C BMET A 140 2847 4149 2136 279 404 -532 C ATOM 1082 O AMET A 140 -29.158 6.921 33.999 0.53 24.77 O ANISOU 1082 O AMET A 140 2917 4291 2205 323 501 -609 O ATOM 1083 O BMET A 140 -29.070 7.179 33.908 0.47 25.29 O ANISOU 1083 O BMET A 140 2986 4339 2286 337 484 -620 O ATOM 1084 CB AMET A 140 -29.324 5.561 31.336 0.53 23.82 C ANISOU 1084 CB AMET A 140 2624 4145 2280 263 404 -437 C ATOM 1085 CB BMET A 140 -29.277 5.321 31.449 0.47 22.96 C ANISOU 1085 CB BMET A 140 2523 4045 2154 247 412 -426 C ATOM 1086 CG AMET A 140 -29.438 5.589 29.826 0.53 24.97 C ANISOU 1086 CG AMET A 140 2697 4250 2543 276 333 -393 C ATOM 1087 CG BMET A 140 -29.389 5.037 29.960 0.47 25.40 C ANISOU 1087 CG BMET A 140 2757 4325 2570 241 348 -368 C ATOM 1088 SD AMET A 140 -30.891 4.698 29.269 0.53 28.33 S ANISOU 1088 SD AMET A 140 2981 4757 3027 250 395 -369 S ATOM 1089 SD BMET A 140 -30.103 6.402 29.031 0.47 25.44 S ANISOU 1089 SD BMET A 140 2684 4284 2700 345 306 -421 S ATOM 1090 CE AMET A 140 -32.196 5.825 29.743 0.53 28.12 C ANISOU 1090 CE AMET A 140 2859 4772 3056 353 470 -475 C ATOM 1091 CE BMET A 140 -31.721 6.534 29.773 0.47 27.49 C ANISOU 1091 CE BMET A 140 2830 4640 2976 393 431 -499 C ATOM 1092 N ALEU A 141 -27.204 5.807 34.036 0.53 23.66 N ANISOU 1092 N ALEU A 141 2901 4103 1985 215 365 -486 N ATOM 1093 N BLEU A 141 -27.269 5.833 34.035 0.47 23.73 N ANISOU 1093 N BLEU A 141 2907 4115 1996 217 369 -489 N ATOM 1094 CA ALEU A 141 -27.115 5.847 35.488 0.53 25.59 C ANISOU 1094 CA ALEU A 141 3254 4390 2081 202 410 -533 C ATOM 1095 CA BLEU A 141 -27.217 5.901 35.487 0.47 25.57 C ANISOU 1095 CA BLEU A 141 3245 4390 2081 207 418 -540 C ATOM 1096 C ALEU A 141 -26.415 7.099 35.997 0.53 26.40 C ANISOU 1096 C ALEU A 141 3443 4430 2158 246 341 -622 C ATOM 1097 C BLEU A 141 -26.519 7.156 35.993 0.47 26.33 C ANISOU 1097 C BLEU A 141 3428 4423 2153 251 350 -629 C ATOM 1098 O ALEU A 141 -26.295 7.270 37.215 0.53 27.59 O ANISOU 1098 O ALEU A 141 3701 4610 2174 240 366 -677 O ATOM 1099 O BLEU A 141 -26.497 7.384 37.208 0.47 27.31 O ANISOU 1099 O BLEU A 141 3654 4578 2145 251 384 -691 O ATOM 1100 CB ALEU A 141 -26.401 4.592 35.998 0.53 27.65 C ANISOU 1100 CB ALEU A 141 3592 4673 2241 122 379 -442 C ATOM 1101 CB BLEU A 141 -26.528 4.652 36.055 0.47 27.49 C ANISOU 1101 CB BLEU A 141 3569 4659 2217 126 392 -450 C ATOM 1102 CG ALEU A 141 -26.997 3.297 35.438 0.53 26.03 C ANISOU 1102 CG ALEU A 141 3314 4506 2069 69 433 -350 C ATOM 1103 CG BLEU A 141 -27.333 3.344 36.118 0.47 27.47 C ANISOU 1103 CG BLEU A 141 3531 4726 2182 66 489 -377 C ATOM 1104 CD1ALEU A 141 -26.214 2.074 35.885 0.53 20.28 C ANISOU 1104 CD1ALEU A 141 2675 3775 1257 0 387 -255 C ATOM 1105 CD1BLEU A 141 -27.763 2.840 34.739 0.47 25.73 C ANISOU 1105 CD1BLEU A 141 3181 4490 2104 56 483 -322 C ATOM 1106 CD2ALEU A 141 -28.467 3.172 35.829 0.53 26.77 C ANISOU 1106 CD2ALEU A 141 3347 4686 2139 66 588 -386 C ATOM 1107 CD2BLEU A 141 -26.558 2.255 36.851 0.47 24.65 C ANISOU 1107 CD2BLEU A 141 3289 4372 1705 -3 448 -292 C ATOM 1108 N GLY A 142 -25.958 7.974 35.104 1.00 21.77 N ANISOU 1108 N GLY A 142 2824 3756 1692 282 256 -637 N ATOM 1109 CA GLY A 142 -25.390 9.243 35.519 1.00 23.19 C ANISOU 1109 CA GLY A 142 3082 3861 1868 317 193 -727 C ATOM 1110 C GLY A 142 -24.072 9.610 34.869 1.00 24.14 C ANISOU 1110 C GLY A 142 3218 3890 2064 285 56 -688 C ATOM 1111 O GLY A 142 -23.628 10.759 34.970 1.00 26.25 O ANISOU 1111 O GLY A 142 3535 4075 2363 306 -4 -758 O ATOM 1112 N TRP A 143 -23.431 8.645 34.208 1.00 22.81 N ANISOU 1112 N TRP A 143 3007 3730 1929 231 11 -583 N ATOM 1113 CA TRP A 143 -22.167 8.889 33.513 1.00 21.15 C ANISOU 1113 CA TRP A 143 2789 3447 1800 195 -99 -541 C ATOM 1114 C TRP A 143 -22.498 9.405 32.116 1.00 18.29 C ANISOU 1114 C TRP A 143 2350 3030 1571 223 -94 -516 C ATOM 1115 O TRP A 143 -22.382 8.705 31.107 1.00 20.39 O ANISOU 1115 O TRP A 143 2552 3304 1892 201 -94 -435 O ATOM 1116 CB TRP A 143 -21.321 7.623 33.471 1.00 20.31 C ANISOU 1116 CB TRP A 143 2672 3375 1670 138 -141 -448 C ATOM 1117 CG TRP A 143 -19.870 7.845 33.097 1.00 22.96 C ANISOU 1117 CG TRP A 143 2998 3651 2073 98 -252 -421 C ATOM 1118 CD1 TRP A 143 -19.281 9.023 32.715 1.00 24.64 C ANISOU 1118 CD1 TRP A 143 3211 3783 2367 92 -310 -460 C ATOM 1119 CD2 TRP A 143 -18.830 6.856 33.090 1.00 20.21 C ANISOU 1119 CD2 TRP A 143 2632 3319 1727 58 -315 -350 C ATOM 1120 NE1 TRP A 143 -17.936 8.817 32.459 1.00 20.09 N ANISOU 1120 NE1 TRP A 143 2605 3184 1846 41 -396 -417 N ATOM 1121 CE2 TRP A 143 -17.638 7.497 32.686 1.00 21.16 C ANISOU 1121 CE2 TRP A 143 2723 3379 1937 28 -402 -353 C ATOM 1122 CE3 TRP A 143 -18.793 5.489 33.387 1.00 19.85 C ANISOU 1122 CE3 TRP A 143 2592 3327 1624 45 -305 -283 C ATOM 1123 CZ2 TRP A 143 -16.422 6.812 32.569 1.00 22.81 C ANISOU 1123 CZ2 TRP A 143 2889 3590 2187 -5 -476 -298 C ATOM 1124 CZ3 TRP A 143 -17.588 4.811 33.267 1.00 23.21 C ANISOU 1124 CZ3 TRP A 143 2990 3742 2088 22 -388 -226 C ATOM 1125 CH2 TRP A 143 -16.420 5.473 32.864 1.00 22.75 C ANISOU 1125 CH2 TRP A 143 2885 3634 2126 1 -470 -238 C ATOM 1126 N ASN A 144 -22.927 10.662 32.067 1.00 23.04 N ANISOU 1126 N ASN A 144 2971 3568 2216 276 -93 -590 N ATOM 1127 CA ASN A 144 -23.377 11.258 30.819 1.00 22.95 C ANISOU 1127 CA ASN A 144 2905 3496 2318 313 -96 -567 C ATOM 1128 C ASN A 144 -23.100 12.755 30.861 1.00 23.08 C ANISOU 1128 C ASN A 144 2983 3397 2388 342 -149 -636 C ATOM 1129 O ASN A 144 -22.677 13.302 31.880 1.00 25.29 O ANISOU 1129 O ASN A 144 3341 3649 2616 336 -176 -714 O ATOM 1130 CB ASN A 144 -24.866 10.968 30.561 1.00 20.85 C ANISOU 1130 CB ASN A 144 2567 3291 2065 376 -10 -574 C ATOM 1131 CG ASN A 144 -25.779 11.521 31.650 1.00 24.54 C ANISOU 1131 CG ASN A 144 3058 3783 2482 444 60 -683 C ATOM 1132 OD1 ASN A 144 -25.862 12.729 31.854 1.00 26.68 O ANISOU 1132 OD1 ASN A 144 3376 3975 2788 501 39 -763 O ATOM 1133 ND2 ASN A 144 -26.489 10.631 32.336 1.00 24.68 N ANISOU 1133 ND2 ASN A 144 3047 3909 2420 438 150 -689 N ATOM 1134 N ASN A 145 -23.336 13.417 29.731 1.00 22.77 N ANISOU 1134 N ASN A 145 2920 3282 2451 371 -171 -605 N ATOM 1135 CA ASN A 145 -23.106 14.850 29.618 1.00 26.52 C ANISOU 1135 CA ASN A 145 3461 3624 2992 396 -225 -655 C ATOM 1136 C ASN A 145 -24.398 15.659 29.672 1.00 30.59 C ANISOU 1136 C ASN A 145 3975 4103 3547 513 -189 -727 C ATOM 1137 O ASN A 145 -24.418 16.811 29.220 1.00 31.90 O ANISOU 1137 O ASN A 145 4186 4141 3792 551 -237 -745 O ATOM 1138 CB ASN A 145 -22.340 15.157 28.333 1.00 28.90 C ANISOU 1138 CB ASN A 145 3758 3844 3378 341 -282 -563 C ATOM 1139 CG ASN A 145 -20.944 14.561 28.336 1.00 32.85 C ANISOU 1139 CG ASN A 145 4252 4367 3863 232 -318 -510 C ATOM 1140 OD1 ASN A 145 -20.305 14.469 29.381 1.00 35.52 O ANISOU 1140 OD1 ASN A 145 4622 4725 4149 196 -344 -561 O ATOM 1141 ND2 ASN A 145 -20.470 14.140 27.169 1.00 30.96 N ANISOU 1141 ND2 ASN A 145 3969 4129 3666 184 -320 -413 N ATOM 1142 N CYS A 146 -25.472 15.092 30.235 1.00 29.42 N ANISOU 1142 N CYS A 146 3772 4058 3348 571 -103 -769 N ATOM 1143 CA CYS A 146 -26.748 15.806 30.281 1.00 32.06 C ANISOU 1143 CA CYS A 146 4075 4370 3735 694 -60 -843 C ATOM 1144 C CYS A 146 -26.732 16.949 31.287 1.00 33.88 C ANISOU 1144 C CYS A 146 4403 4517 3951 750 -60 -976 C ATOM 1145 O CYS A 146 -27.502 17.908 31.145 1.00 34.47 O ANISOU 1145 O CYS A 146 4479 4514 4105 859 -57 -1040 O ATOM 1146 CB CYS A 146 -27.885 14.833 30.595 1.00 32.47 C ANISOU 1146 CB CYS A 146 4024 4567 3748 727 44 -851 C ATOM 1147 SG CYS A 146 -28.262 13.728 29.218 1.00 33.89 S ANISOU 1147 SG CYS A 146 4084 4815 3976 690 33 -716 S ATOM 1148 N GLY A 147 -25.868 16.876 32.300 1.00 33.91 N ANISOU 1148 N GLY A 147 4495 4531 3858 682 -72 -1024 N ATOM 1149 CA GLY A 147 -25.743 17.980 33.235 1.00 34.70 C ANISOU 1149 CA GLY A 147 4708 4541 3935 723 -86 -1157 C ATOM 1150 C GLY A 147 -25.078 19.207 32.648 1.00 38.28 C ANISOU 1150 C GLY A 147 5238 4813 4493 715 -192 -1160 C ATOM 1151 O GLY A 147 -25.203 20.297 33.214 1.00 42.99 O ANISOU 1151 O GLY A 147 5927 5303 5105 773 -206 -1277 O ATOM 1152 N GLN A 148 -24.379 19.058 31.526 1.00 35.45 N ANISOU 1152 N GLN A 148 4851 4414 4205 641 -260 -1035 N ATOM 1153 CA GLN A 148 -23.656 20.158 30.886 1.00 43.22 C ANISOU 1153 CA GLN A 148 5910 5226 5287 606 -355 -1014 C ATOM 1154 C GLN A 148 -24.026 20.235 29.410 1.00 40.05 C ANISOU 1154 C GLN A 148 5453 4781 4985 631 -373 -897 C ATOM 1155 O GLN A 148 -23.177 20.065 28.533 1.00 44.03 O ANISOU 1155 O GLN A 148 5952 5258 5520 535 -418 -789 O ATOM 1156 CB GLN A 148 -22.147 19.980 31.057 1.00 56.00 C ANISOU 1156 CB GLN A 148 7566 6831 6880 460 -425 -977 C ATOM 1157 CG GLN A 148 -21.699 19.592 32.460 1.00 65.27 C ANISOU 1157 CG GLN A 148 8784 8082 7932 420 -424 -1066 C ATOM 1158 CD GLN A 148 -21.696 18.087 32.682 1.00 67.79 C ANISOU 1158 CD GLN A 148 9022 8579 8157 387 -372 -1002 C ATOM 1159 OE1 GLN A 148 -21.235 17.322 31.834 1.00 66.90 O ANISOU 1159 OE1 GLN A 148 8831 8511 8076 328 -381 -884 O ATOM 1160 NE2 GLN A 148 -22.216 17.656 33.826 1.00 69.68 N ANISOU 1160 NE2 GLN A 148 9286 8912 8275 425 -313 -1081 N ATOM 1161 N PRO A 149 -25.290 20.502 29.098 1.00 39.22 N ANISOU 1161 N PRO A 149 5305 4669 4930 761 -340 -919 N ATOM 1162 CA PRO A 149 -25.718 20.459 27.696 1.00 39.61 C ANISOU 1162 CA PRO A 149 5302 4693 5054 787 -371 -803 C ATOM 1163 C PRO A 149 -25.099 21.574 26.863 1.00 40.60 C ANISOU 1163 C PRO A 149 5529 4632 5266 757 -462 -747 C ATOM 1164 O PRO A 149 -24.740 22.643 27.367 1.00 40.24 O ANISOU 1164 O PRO A 149 5589 4446 5256 762 -502 -822 O ATOM 1165 CB PRO A 149 -27.239 20.621 27.790 1.00 42.11 C ANISOU 1165 CB PRO A 149 5547 5039 5413 946 -327 -865 C ATOM 1166 CG PRO A 149 -27.449 21.395 29.036 1.00 41.03 C ANISOU 1166 CG PRO A 149 5476 4850 5264 1016 -295 -1021 C ATOM 1167 CD PRO A 149 -26.381 20.936 29.992 1.00 40.26 C ANISOU 1167 CD PRO A 149 5434 4807 5055 894 -279 -1055 C ATOM 1168 N LYS A 150 -24.966 21.304 25.565 1.00 38.03 N ANISOU 1168 N LYS A 150 5180 4303 4967 716 -493 -612 N ATOM 1169 CA LYS A 150 -24.556 22.330 24.615 1.00 37.00 C ANISOU 1169 CA LYS A 150 5149 3998 4912 692 -571 -536 C ATOM 1170 C LYS A 150 -25.719 23.280 24.349 1.00 40.43 C ANISOU 1170 C LYS A 150 5612 4317 5431 851 -614 -567 C ATOM 1171 O LYS A 150 -26.481 23.100 23.392 1.00 35.74 O ANISOU 1171 O LYS A 150 4974 3743 4863 915 -640 -489 O ATOM 1172 CB LYS A 150 -24.045 21.696 23.323 1.00 34.66 C ANISOU 1172 CB LYS A 150 4830 3743 4594 596 -579 -384 C ATOM 1173 CG LYS A 150 -22.763 20.902 23.525 1.00 38.40 C ANISOU 1173 CG LYS A 150 5278 4302 5010 444 -543 -354 C ATOM 1174 CD LYS A 150 -22.076 20.596 22.214 1.00 42.77 C ANISOU 1174 CD LYS A 150 5839 4854 5556 344 -546 -215 C ATOM 1175 CE LYS A 150 -20.765 19.874 22.455 1.00 47.61 C ANISOU 1175 CE LYS A 150 6411 5544 6133 207 -509 -197 C ATOM 1176 NZ LYS A 150 -19.897 20.629 23.396 1.00 51.27 N ANISOU 1176 NZ LYS A 150 6925 5921 6632 144 -539 -272 N ATOM 1177 N GLU A 151 -25.855 24.299 25.201 1.00 45.74 N ANISOU 1177 N GLU A 151 6362 4867 6149 919 -629 -686 N ATOM 1178 CA GLU A 151 -27.036 25.156 25.162 1.00 55.08 C ANISOU 1178 CA GLU A 151 7557 5949 7421 1098 -660 -745 C ATOM 1179 C GLU A 151 -27.058 26.039 23.922 1.00 52.83 C ANISOU 1179 C GLU A 151 7364 5487 7221 1118 -762 -629 C ATOM 1180 O GLU A 151 -28.138 26.360 23.414 1.00 52.64 O ANISOU 1180 O GLU A 151 7309 5425 7266 1265 -805 -616 O ATOM 1181 CB GLU A 151 -27.098 26.014 26.425 1.00 65.14 C ANISOU 1181 CB GLU A 151 8906 7129 8715 1164 -643 -916 C ATOM 1182 CG GLU A 151 -28.486 26.157 27.023 1.00 74.73 C ANISOU 1182 CG GLU A 151 10043 8384 9967 1357 -590 -1040 C ATOM 1183 CD GLU A 151 -29.038 24.843 27.536 1.00 77.02 C ANISOU 1183 CD GLU A 151 10176 8919 10170 1361 -480 -1068 C ATOM 1184 OE1 GLU A 151 -29.651 24.102 26.738 1.00 78.91 O ANISOU 1184 OE1 GLU A 151 10297 9266 10421 1382 -478 -976 O ATOM 1185 OE2 GLU A 151 -28.856 24.550 28.737 1.00 78.42 O ANISOU 1185 OE2 GLU A 151 10357 9176 10261 1336 -401 -1181 O ATOM 1186 N GLY A 152 -25.889 26.446 23.426 1.00 53.41 N ANISOU 1186 N GLY A 152 7550 5449 7292 973 -805 -543 N ATOM 1187 CA GLY A 152 -25.858 27.214 22.192 1.00 53.80 C ANISOU 1187 CA GLY A 152 7703 5336 7402 972 -894 -412 C ATOM 1188 C GLY A 152 -26.309 26.398 20.999 1.00 50.47 C ANISOU 1188 C GLY A 152 7208 5029 6940 977 -906 -276 C ATOM 1189 O GLY A 152 -27.027 26.897 20.127 1.00 50.40 O ANISOU 1189 O GLY A 152 7239 4930 6981 1074 -987 -202 O ATOM 1190 N LYS A 153 -25.897 25.129 20.944 1.00 45.23 N ANISOU 1190 N LYS A 153 6443 4560 6184 876 -834 -243 N ATOM 1191 CA LYS A 153 -26.372 24.242 19.890 1.00 42.78 C ANISOU 1191 CA LYS A 153 6060 4371 5825 880 -841 -136 C ATOM 1192 C LYS A 153 -27.871 23.997 20.021 1.00 41.88 C ANISOU 1192 C LYS A 153 5830 4333 5748 1056 -857 -194 C ATOM 1193 O LYS A 153 -28.597 23.977 19.020 1.00 41.65 O ANISOU 1193 O LYS A 153 5791 4300 5735 1123 -929 -110 O ATOM 1194 CB LYS A 153 -25.598 22.923 19.933 1.00 42.94 C ANISOU 1194 CB LYS A 153 5998 4572 5747 742 -755 -110 C ATOM 1195 CG LYS A 153 -25.655 22.134 18.639 1.00 44.44 C ANISOU 1195 CG LYS A 153 6167 4846 5874 695 -764 20 C ATOM 1196 CD LYS A 153 -24.965 20.777 18.755 1.00 45.20 C ANISOU 1196 CD LYS A 153 6175 5115 5883 581 -676 28 C ATOM 1197 CE LYS A 153 -23.452 20.904 18.827 1.00 44.07 C ANISOU 1197 CE LYS A 153 6090 4931 5723 425 -636 58 C ATOM 1198 NZ LYS A 153 -22.791 19.588 18.609 1.00 46.66 N ANISOU 1198 NZ LYS A 153 6341 5414 5975 327 -563 91 N ATOM 1199 N ALA A 154 -28.354 23.818 21.252 1.00 38.97 N ANISOU 1199 N ALA A 154 5374 4037 5394 1129 -792 -338 N ATOM 1200 CA ALA A 154 -29.777 23.574 21.463 1.00 41.34 C ANISOU 1200 CA ALA A 154 5542 4423 5742 1290 -786 -404 C ATOM 1201 C ALA A 154 -30.613 24.776 21.039 1.00 45.99 C ANISOU 1201 C ALA A 154 6182 4843 6450 1453 -890 -405 C ATOM 1202 O ALA A 154 -31.652 24.621 20.385 1.00 45.12 O ANISOU 1202 O ALA A 154 5985 4772 6386 1561 -949 -368 O ATOM 1203 CB ALA A 154 -30.033 23.232 22.931 1.00 36.83 C ANISOU 1203 CB ALA A 154 4887 3954 5151 1324 -676 -560 C ATOM 1204 N HIS A 155 -30.173 25.985 21.404 1.00 45.13 N ANISOU 1204 N HIS A 155 6214 4536 6398 1475 -924 -449 N ATOM 1205 CA HIS A 155 -30.917 27.187 21.035 1.00 50.48 C ANISOU 1205 CA HIS A 155 6959 5025 7198 1639 -1029 -451 C ATOM 1206 C HIS A 155 -30.946 27.386 19.525 1.00 47.36 C ANISOU 1206 C HIS A 155 6639 4550 6806 1624 -1152 -271 C ATOM 1207 O HIS A 155 -31.987 27.744 18.962 1.00 47.98 O ANISOU 1207 O HIS A 155 6684 4582 6966 1780 -1248 -244 O ATOM 1208 CB HIS A 155 -30.313 28.414 21.718 1.00 54.04 C ANISOU 1208 CB HIS A 155 7569 5263 7702 1641 -1042 -531 C ATOM 1209 CG HIS A 155 -30.528 28.454 23.198 1.00 60.80 C ANISOU 1209 CG HIS A 155 8373 6166 8562 1703 -941 -726 C ATOM 1210 ND1 HIS A 155 -31.713 28.072 23.789 1.00 64.53 N ANISOU 1210 ND1 HIS A 155 8683 6768 9066 1856 -877 -838 N ATOM 1211 CD2 HIS A 155 -29.709 28.832 24.207 1.00 62.98 C ANISOU 1211 CD2 HIS A 155 8741 6381 8806 1626 -893 -831 C ATOM 1212 CE1 HIS A 155 -31.614 28.213 25.099 1.00 65.78 C ANISOU 1212 CE1 HIS A 155 8849 6945 9200 1873 -782 -1002 C ATOM 1213 NE2 HIS A 155 -30.407 28.672 25.379 1.00 64.37 N ANISOU 1213 NE2 HIS A 155 8828 6651 8980 1737 -799 -1002 N ATOM 1214 N SER A 156 -29.814 27.159 18.851 1.00 41.93 N ANISOU 1214 N SER A 156 6054 3848 6031 1439 -1152 -147 N ATOM 1215 CA SER A 156 -29.760 27.366 17.408 1.00 48.68 C ANISOU 1215 CA SER A 156 7008 4626 6862 1409 -1257 29 C ATOM 1216 C SER A 156 -30.674 26.410 16.655 1.00 52.14 C ANISOU 1216 C SER A 156 7315 5233 7263 1464 -1293 85 C ATOM 1217 O SER A 156 -31.065 26.706 15.521 1.00 51.51 O ANISOU 1217 O SER A 156 7304 5084 7183 1507 -1413 207 O ATOM 1218 CB SER A 156 -28.324 27.224 16.902 1.00 48.11 C ANISOU 1218 CB SER A 156 7055 4530 6695 1188 -1217 138 C ATOM 1219 OG SER A 156 -27.919 25.867 16.881 1.00 54.87 O ANISOU 1219 OG SER A 156 7798 5606 7445 1073 -1122 147 O ATOM 1220 N GLN A 157 -31.021 25.274 17.253 1.00 52.47 N ANISOU 1220 N GLN A 157 7179 5488 7269 1458 -1200 2 N ATOM 1221 CA GLN A 157 -31.944 24.323 16.652 1.00 51.85 C ANISOU 1221 CA GLN A 157 6959 5573 7167 1504 -1232 35 C ATOM 1222 C GLN A 157 -33.378 24.512 17.127 1.00 48.62 C ANISOU 1222 C GLN A 157 6396 5197 6880 1707 -1266 -68 C ATOM 1223 O GLN A 157 -34.252 23.727 16.744 1.00 49.49 O ANISOU 1223 O GLN A 157 6361 5450 6991 1750 -1295 -58 O ATOM 1224 CB GLN A 157 -31.493 22.891 16.945 1.00 54.36 C ANISOU 1224 CB GLN A 157 7173 6103 7378 1367 -1111 16 C ATOM 1225 CG GLN A 157 -30.086 22.574 16.474 1.00 62.04 C ANISOU 1225 CG GLN A 157 8265 7068 8240 1174 -1065 109 C ATOM 1226 CD GLN A 157 -29.880 21.092 16.256 1.00 72.62 C ANISOU 1226 CD GLN A 157 9509 8606 9478 1068 -993 129 C ATOM 1227 OE1 GLN A 157 -28.753 20.626 16.090 1.00 78.44 O ANISOU 1227 OE1 GLN A 157 10299 9371 10132 920 -928 174 O ATOM 1228 NE2 GLN A 157 -30.975 20.341 16.250 1.00 75.66 N ANISOU 1228 NE2 GLN A 157 9745 9123 9878 1143 -1006 93 N ATOM 1229 N GLY A 158 -33.637 25.520 17.955 1.00 47.22 N ANISOU 1229 N GLY A 158 6242 4891 6808 1829 -1261 -174 N ATOM 1230 CA GLY A 158 -34.972 25.775 18.453 1.00 50.21 C ANISOU 1230 CA GLY A 158 6467 5295 7316 2033 -1276 -286 C ATOM 1231 C GLY A 158 -35.466 24.814 19.508 1.00 51.87 C ANISOU 1231 C GLY A 158 6477 5717 7515 2037 -1129 -419 C ATOM 1232 O GLY A 158 -36.676 24.762 19.751 1.00 56.17 O ANISOU 1232 O GLY A 158 6851 6332 8160 2188 -1131 -496 O ATOM 1233 N CYS A 159 -34.575 24.059 20.150 1.00 48.29 N ANISOU 1233 N CYS A 159 6037 5366 6947 1876 -1001 -445 N ATOM 1234 CA CYS A 159 -34.999 23.064 21.123 1.00 47.99 C ANISOU 1234 CA CYS A 159 5828 5528 6877 1860 -859 -552 C ATOM 1235 C CYS A 159 -35.680 23.724 22.316 1.00 52.48 C ANISOU 1235 C CYS A 159 6334 6070 7535 2012 -782 -722 C ATOM 1236 O CYS A 159 -35.453 24.894 22.629 1.00 49.69 O ANISOU 1236 O CYS A 159 6104 5535 7239 2089 -813 -775 O ATOM 1237 CB CYS A 159 -33.806 22.235 21.596 1.00 43.65 C ANISOU 1237 CB CYS A 159 5335 5064 6186 1666 -756 -540 C ATOM 1238 SG CYS A 159 -32.951 21.373 20.267 1.00 39.23 S ANISOU 1238 SG CYS A 159 4840 4549 5518 1489 -814 -361 S ATOM 1239 N GLY A 160 -36.536 22.953 22.982 1.00 53.04 N ANISOU 1239 N GLY A 160 6215 6322 7616 2051 -674 -810 N ATOM 1240 CA GLY A 160 -37.200 23.404 24.183 1.00 52.34 C ANISOU 1240 CA GLY A 160 6052 6246 7590 2182 -564 -982 C ATOM 1241 C GLY A 160 -36.311 23.254 25.399 1.00 53.80 C ANISOU 1241 C GLY A 160 6333 6454 7654 2077 -431 -1070 C ATOM 1242 O GLY A 160 -35.150 22.851 25.317 1.00 50.25 O ANISOU 1242 O GLY A 160 6000 6002 7089 1909 -434 -997 O ATOM 1243 N GLU A 161 -36.876 23.588 26.553 1.00 57.43 N ANISOU 1243 N GLU A 161 6741 6940 8141 2183 -312 -1233 N ATOM 1244 CA GLU A 161 -36.132 23.475 27.796 1.00 60.64 C ANISOU 1244 CA GLU A 161 7244 7375 8421 2095 -190 -1330 C ATOM 1245 C GLU A 161 -35.988 22.012 28.193 1.00 57.74 C ANISOU 1245 C GLU A 161 6788 7226 7923 1946 -79 -1298 C ATOM 1246 O GLU A 161 -36.889 21.195 27.981 1.00 58.04 O ANISOU 1246 O GLU A 161 6645 7418 7992 1962 -33 -1278 O ATOM 1247 CB GLU A 161 -36.816 24.277 28.903 1.00 75.59 C ANISOU 1247 CB GLU A 161 9123 9231 10367 2256 -88 -1521 C ATOM 1248 CG GLU A 161 -36.666 25.780 28.709 1.00 86.56 C ANISOU 1248 CG GLU A 161 10663 10374 11854 2350 -190 -1545 C ATOM 1249 CD GLU A 161 -37.291 26.594 29.824 1.00 98.11 C ANISOU 1249 CD GLU A 161 12137 11801 13340 2439 -74 -1692 C ATOM 1250 OE1 GLU A 161 -38.331 26.169 30.368 1.00102.45 O ANISOU 1250 OE1 GLU A 161 12524 12503 13899 2479 61 -1743 O ATOM 1251 OE2 GLU A 161 -36.738 27.666 30.152 1.00102.13 O ANISOU 1251 OE2 GLU A 161 12823 12122 13859 2462 -115 -1754 O ATOM 1252 N GLY A 162 -34.830 21.683 28.763 1.00 53.20 N ANISOU 1252 N GLY A 162 6345 6660 7210 1798 -47 -1290 N ATOM 1253 CA GLY A 162 -34.486 20.307 29.038 1.00 50.08 C ANISOU 1253 CA GLY A 162 5901 6440 6688 1646 30 -1235 C ATOM 1254 C GLY A 162 -34.112 19.489 27.823 1.00 49.31 C ANISOU 1254 C GLY A 162 5774 6379 6582 1536 -59 -1068 C ATOM 1255 O GLY A 162 -33.751 18.314 27.974 1.00 49.58 O ANISOU 1255 O GLY A 162 5779 6541 6517 1408 -6 -1015 O ATOM 1256 N GLN A 163 -34.187 20.062 26.627 1.00 47.24 N ANISOU 1256 N GLN A 163 5530 6004 6415 1584 -191 -984 N ATOM 1257 CA GLN A 163 -33.849 19.358 25.401 1.00 43.13 C ANISOU 1257 CA GLN A 163 4999 5511 5877 1486 -276 -832 C ATOM 1258 C GLN A 163 -32.441 19.716 24.941 1.00 40.06 C ANISOU 1258 C GLN A 163 4785 4999 5436 1375 -351 -750 C ATOM 1259 O GLN A 163 -31.904 20.783 25.249 1.00 42.46 O ANISOU 1259 O GLN A 163 5216 5154 5763 1400 -383 -793 O ATOM 1260 CB GLN A 163 -34.849 19.680 24.286 1.00 40.78 C ANISOU 1260 CB GLN A 163 4613 5182 5700 1599 -382 -779 C ATOM 1261 CG GLN A 163 -36.241 19.116 24.509 1.00 40.40 C ANISOU 1261 CG GLN A 163 4352 5281 5717 1684 -320 -836 C ATOM 1262 CD GLN A 163 -37.103 19.212 23.266 1.00 46.95 C ANISOU 1262 CD GLN A 163 5088 6098 6652 1765 -453 -760 C ATOM 1263 OE1 GLN A 163 -37.023 20.182 22.514 1.00 46.06 O ANISOU 1263 OE1 GLN A 163 5066 5830 6603 1842 -584 -712 O ATOM 1264 NE2 GLN A 163 -37.926 18.197 23.037 1.00 51.49 N ANISOU 1264 NE2 GLN A 163 5488 6833 7243 1742 -429 -745 N ATOM 1265 N VAL A 164 -31.849 18.795 24.185 1.00 32.69 N ANISOU 1265 N VAL A 164 3854 4129 4438 1248 -375 -634 N ATOM 1266 CA VAL A 164 -30.565 19.000 23.533 1.00 33.79 C ANISOU 1266 CA VAL A 164 4129 4173 4537 1135 -437 -539 C ATOM 1267 C VAL A 164 -30.715 18.609 22.072 1.00 32.19 C ANISOU 1267 C VAL A 164 3911 3980 4341 1108 -518 -409 C ATOM 1268 O VAL A 164 -31.635 17.883 21.691 1.00 30.16 O ANISOU 1268 O VAL A 164 3533 3832 4095 1141 -519 -393 O ATOM 1269 CB VAL A 164 -29.434 18.180 24.192 1.00 31.51 C ANISOU 1269 CB VAL A 164 3873 3960 4141 990 -368 -539 C ATOM 1270 CG1 VAL A 164 -29.321 18.505 25.674 1.00 34.91 C ANISOU 1270 CG1 VAL A 164 4329 4392 4541 1013 -296 -669 C ATOM 1271 CG2 VAL A 164 -29.668 16.686 23.988 1.00 33.86 C ANISOU 1271 CG2 VAL A 164 4064 4425 4376 924 -317 -491 C ATOM 1272 N ALA A 165 -29.800 19.107 21.247 1.00 30.51 N ANISOU 1272 N ALA A 165 3825 3652 4115 1040 -585 -317 N ATOM 1273 CA ALA A 165 -29.612 18.523 19.925 1.00 32.36 C ANISOU 1273 CA ALA A 165 4072 3916 4307 971 -637 -190 C ATOM 1274 C ALA A 165 -29.067 17.107 20.098 1.00 31.90 C ANISOU 1274 C ALA A 165 3957 4007 4157 850 -555 -176 C ATOM 1275 O ALA A 165 -28.007 16.910 20.704 1.00 26.67 O ANISOU 1275 O ALA A 165 3336 3349 3448 759 -498 -192 O ATOM 1276 CB ALA A 165 -28.668 19.384 19.090 1.00 32.32 C ANISOU 1276 CB ALA A 165 4225 3757 4297 910 -701 -97 C ATOM 1277 N CYS A 166 -29.800 16.113 19.607 1.00 29.66 N ANISOU 1277 N CYS A 166 3575 3841 3853 852 -556 -149 N ATOM 1278 CA CYS A 166 -29.468 14.728 19.938 1.00 29.55 C ANISOU 1278 CA CYS A 166 3499 3963 3765 756 -475 -153 C ATOM 1279 C CYS A 166 -28.359 14.231 19.019 1.00 31.59 C ANISOU 1279 C CYS A 166 3838 4213 3953 638 -481 -58 C ATOM 1280 O CYS A 166 -28.596 13.902 17.854 1.00 32.70 O ANISOU 1280 O CYS A 166 3991 4366 4068 623 -533 14 O ATOM 1281 CB CYS A 166 -30.695 13.833 19.845 1.00 29.36 C ANISOU 1281 CB CYS A 166 3338 4063 3756 793 -468 -171 C ATOM 1282 SG CYS A 166 -30.302 12.160 20.348 1.00 30.96 S ANISOU 1282 SG CYS A 166 3484 4407 3874 675 -368 -175 S ATOM 1283 N LEU A 167 -27.140 14.172 19.557 1.00 25.91 N ANISOU 1283 N LEU A 167 3171 3476 3199 556 -428 -65 N ATOM 1284 CA LEU A 167 -25.961 13.699 18.849 1.00 25.83 C ANISOU 1284 CA LEU A 167 3217 3464 3132 445 -411 9 C ATOM 1285 C LEU A 167 -25.182 12.812 19.803 1.00 25.16 C ANISOU 1285 C LEU A 167 3094 3455 3011 377 -335 -31 C ATOM 1286 O LEU A 167 -25.056 13.141 20.986 1.00 24.77 O ANISOU 1286 O LEU A 167 3036 3398 2976 395 -312 -102 O ATOM 1287 CB LEU A 167 -25.080 14.867 18.373 1.00 26.00 C ANISOU 1287 CB LEU A 167 3354 3349 3174 411 -445 57 C ATOM 1288 CG LEU A 167 -25.769 15.798 17.372 1.00 29.63 C ANISOU 1288 CG LEU A 167 3881 3713 3663 476 -533 115 C ATOM 1289 CD1 LEU A 167 -25.016 17.110 17.235 1.00 32.04 C ANISOU 1289 CD1 LEU A 167 4306 3863 4006 449 -563 147 C ATOM 1290 CD2 LEU A 167 -25.893 15.095 16.030 1.00 29.00 C ANISOU 1290 CD2 LEU A 167 3820 3684 3516 438 -554 202 C ATOM 1291 N PHE A 168 -24.666 11.693 19.282 1.00 23.29 N ANISOU 1291 N PHE A 168 2841 3286 2722 305 -301 13 N ATOM 1292 CA PHE A 168 -24.035 10.685 20.133 1.00 18.55 C ANISOU 1292 CA PHE A 168 2199 2759 2090 254 -241 -16 C ATOM 1293 C PHE A 168 -22.938 11.296 21.000 1.00 21.11 C ANISOU 1293 C PHE A 168 2557 3033 2431 220 -234 -46 C ATOM 1294 O PHE A 168 -22.948 11.150 22.227 1.00 21.31 O ANISOU 1294 O PHE A 168 2560 3091 2447 232 -216 -109 O ATOM 1295 CB PHE A 168 -23.479 9.547 19.267 1.00 23.08 C ANISOU 1295 CB PHE A 168 2769 3382 2619 188 -213 39 C ATOM 1296 CG PHE A 168 -22.934 8.381 20.062 1.00 18.60 C ANISOU 1296 CG PHE A 168 2157 2884 2024 150 -163 17 C ATOM 1297 CD1 PHE A 168 -21.641 8.418 20.582 1.00 20.70 C ANISOU 1297 CD1 PHE A 168 2434 3131 2298 103 -146 13 C ATOM 1298 CD2 PHE A 168 -23.708 7.258 20.281 1.00 19.96 C ANISOU 1298 CD2 PHE A 168 2279 3133 2171 157 -142 3 C ATOM 1299 CE1 PHE A 168 -21.137 7.346 21.313 1.00 18.97 C ANISOU 1299 CE1 PHE A 168 2181 2969 2058 78 -118 0 C ATOM 1300 CE2 PHE A 168 -23.214 6.175 21.012 1.00 21.55 C ANISOU 1300 CE2 PHE A 168 2458 3383 2347 123 -103 -6 C ATOM 1301 CZ PHE A 168 -21.921 6.221 21.526 1.00 19.82 C ANISOU 1301 CZ PHE A 168 2255 3143 2132 91 -96 -6 C ATOM 1302 N GLU A 169 -21.983 11.995 20.381 1.00 20.88 N ANISOU 1302 N GLU A 169 2585 2924 2423 169 -249 -3 N ATOM 1303 CA GLU A 169 -20.842 12.495 21.142 1.00 25.70 C ANISOU 1303 CA GLU A 169 3214 3491 3060 117 -251 -30 C ATOM 1304 C GLU A 169 -21.195 13.651 22.066 1.00 25.00 C ANISOU 1304 C GLU A 169 3164 3327 3006 166 -289 -101 C ATOM 1305 O GLU A 169 -20.395 13.978 22.946 1.00 25.73 O ANISOU 1305 O GLU A 169 3270 3395 3110 127 -300 -146 O ATOM 1306 CB GLU A 169 -19.714 12.913 20.193 1.00 28.74 C ANISOU 1306 CB GLU A 169 3638 3815 3468 33 -245 38 C ATOM 1307 CG GLU A 169 -19.112 11.737 19.449 1.00 26.71 C ANISOU 1307 CG GLU A 169 3341 3633 3176 -18 -191 87 C ATOM 1308 CD GLU A 169 -17.897 12.107 18.622 1.00 28.49 C ANISOU 1308 CD GLU A 169 3589 3813 3425 -108 -160 145 C ATOM 1309 OE1 GLU A 169 -17.231 13.118 18.943 1.00 29.50 O ANISOU 1309 OE1 GLU A 169 3741 3861 3606 -153 -181 138 O ATOM 1310 OE2 GLU A 169 -17.611 11.375 17.651 1.00 28.88 O ANISOU 1310 OE2 GLU A 169 3630 3905 3437 -137 -109 192 O ATOM 1311 N ASP A 170 -22.362 14.273 21.901 1.00 22.63 N ANISOU 1311 N ASP A 170 2882 2990 2726 253 -314 -119 N ATOM 1312 CA ASP A 170 -22.753 15.331 22.822 1.00 25.29 C ANISOU 1312 CA ASP A 170 3257 3255 3099 315 -340 -202 C ATOM 1313 C ASP A 170 -23.350 14.799 24.121 1.00 25.46 C ANISOU 1313 C ASP A 170 3228 3366 3079 363 -300 -292 C ATOM 1314 O ASP A 170 -23.367 15.528 25.118 1.00 28.42 O ANISOU 1314 O ASP A 170 3643 3695 3460 394 -308 -378 O ATOM 1315 CB ASP A 170 -23.748 16.284 22.148 1.00 25.43 C ANISOU 1315 CB ASP A 170 3311 3184 3168 405 -386 -190 C ATOM 1316 CG ASP A 170 -23.082 17.199 21.119 1.00 34.92 C ANISOU 1316 CG ASP A 170 4605 4256 4408 355 -433 -109 C ATOM 1317 OD1 ASP A 170 -21.855 17.075 20.920 1.00 37.46 O ANISOU 1317 OD1 ASP A 170 4948 4567 4720 244 -416 -68 O ATOM 1318 OD2 ASP A 170 -23.780 18.048 20.515 1.00 34.37 O ANISOU 1318 OD2 ASP A 170 4586 4092 4380 425 -487 -84 O ATOM 1319 N VAL A 171 -23.843 13.560 24.145 1.00 21.50 N ANISOU 1319 N VAL A 171 2652 2986 2530 365 -255 -277 N ATOM 1320 CA VAL A 171 -24.473 13.031 25.344 1.00 23.55 C ANISOU 1320 CA VAL A 171 2872 3333 2743 401 -204 -351 C ATOM 1321 C VAL A 171 -23.679 11.890 25.980 1.00 21.96 C ANISOU 1321 C VAL A 171 2657 3214 2473 325 -175 -338 C ATOM 1322 O VAL A 171 -23.676 11.773 27.210 1.00 23.70 O ANISOU 1322 O VAL A 171 2893 3471 2639 330 -151 -402 O ATOM 1323 CB VAL A 171 -25.934 12.597 25.079 1.00 23.92 C ANISOU 1323 CB VAL A 171 2838 3450 2801 473 -171 -357 C ATOM 1324 CG1 VAL A 171 -26.785 13.803 24.681 1.00 29.71 C ANISOU 1324 CG1 VAL A 171 3579 4099 3611 573 -210 -385 C ATOM 1325 CG2 VAL A 171 -26.010 11.508 24.023 1.00 20.60 C ANISOU 1325 CG2 VAL A 171 2369 3090 2369 427 -170 -271 C ATOM 1326 N VAL A 172 -22.999 11.062 25.194 1.00 20.44 N ANISOU 1326 N VAL A 172 2443 3046 2276 261 -178 -260 N ATOM 1327 CA VAL A 172 -22.245 9.927 25.719 1.00 18.95 C ANISOU 1327 CA VAL A 172 2240 2926 2036 203 -161 -242 C ATOM 1328 C VAL A 172 -20.809 10.395 25.986 1.00 20.44 C ANISOU 1328 C VAL A 172 2464 3059 2244 145 -207 -243 C ATOM 1329 O VAL A 172 -20.136 10.827 25.043 1.00 21.35 O ANISOU 1329 O VAL A 172 2584 3116 2411 109 -227 -198 O ATOM 1330 CB VAL A 172 -22.257 8.738 24.752 1.00 21.13 C ANISOU 1330 CB VAL A 172 2470 3251 2306 173 -137 -170 C ATOM 1331 CG1 VAL A 172 -21.608 7.506 25.412 1.00 19.44 C ANISOU 1331 CG1 VAL A 172 2244 3097 2044 131 -122 -156 C ATOM 1332 CG2 VAL A 172 -23.680 8.429 24.290 1.00 18.53 C ANISOU 1332 CG2 VAL A 172 2099 2964 1977 219 -112 -168 C ATOM 1333 N PRO A 173 -20.319 10.311 27.223 1.00 23.60 N ANISOU 1333 N PRO A 173 2887 3479 2599 130 -225 -291 N ATOM 1334 CA PRO A 173 -18.957 10.793 27.498 1.00 21.87 C ANISOU 1334 CA PRO A 173 2688 3209 2410 70 -286 -298 C ATOM 1335 C PRO A 173 -17.918 9.947 26.781 1.00 20.07 C ANISOU 1335 C PRO A 173 2405 3006 2216 14 -287 -225 C ATOM 1336 O PRO A 173 -18.054 8.726 26.669 1.00 17.18 O ANISOU 1336 O PRO A 173 2002 2708 1816 20 -255 -188 O ATOM 1337 CB PRO A 173 -18.819 10.650 29.023 1.00 23.27 C ANISOU 1337 CB PRO A 173 2906 3424 2511 73 -312 -364 C ATOM 1338 CG PRO A 173 -20.211 10.418 29.542 1.00 25.20 C ANISOU 1338 CG PRO A 173 3165 3723 2688 139 -248 -402 C ATOM 1339 CD PRO A 173 -20.971 9.764 28.424 1.00 23.59 C ANISOU 1339 CD PRO A 173 2898 3550 2513 159 -194 -338 C ATOM 1340 N MET A 174 -16.854 10.607 26.321 1.00 19.72 N ANISOU 1340 N MET A 174 2351 2900 2242 -43 -320 -209 N ATOM 1341 CA AMET A 174 -15.821 9.870 25.608 0.75 20.87 C ANISOU 1341 CA AMET A 174 2430 3071 2430 -93 -307 -148 C ATOM 1342 CA BMET A 174 -15.783 9.909 25.613 0.25 20.83 C ANISOU 1342 CA BMET A 174 2425 3063 2427 -95 -309 -149 C ATOM 1343 C MET A 174 -14.924 9.078 26.554 1.00 19.83 C ANISOU 1343 C MET A 174 2259 2990 2286 -110 -353 -160 C ATOM 1344 O MET A 174 -14.356 8.063 26.138 1.00 19.39 O ANISOU 1344 O MET A 174 2142 2976 2248 -118 -332 -115 O ATOM 1345 CB AMET A 174 -14.994 10.823 24.743 0.75 22.19 C ANISOU 1345 CB AMET A 174 2589 3162 2681 -157 -310 -121 C ATOM 1346 CB BMET A 174 -14.903 10.906 24.864 0.25 21.92 C ANISOU 1346 CB BMET A 174 2555 3123 2649 -162 -318 -127 C ATOM 1347 CG AMET A 174 -14.293 10.137 23.576 0.75 23.06 C ANISOU 1347 CG AMET A 174 2636 3299 2827 -195 -252 -53 C ATOM 1348 CG BMET A 174 -15.572 11.549 23.675 0.25 21.24 C ANISOU 1348 CG BMET A 174 2512 2981 2576 -153 -277 -87 C ATOM 1349 SD AMET A 174 -15.390 9.223 22.458 0.75 23.48 S ANISOU 1349 SD AMET A 174 2703 3396 2820 -142 -177 -5 S ATOM 1350 SD BMET A 174 -16.010 10.380 22.378 0.25 25.28 S ANISOU 1350 SD BMET A 174 2995 3558 3054 -132 -199 -17 S ATOM 1351 CE AMET A 174 -15.888 10.494 21.306 0.75 26.85 C ANISOU 1351 CE AMET A 174 3202 3737 3263 -156 -163 32 C ATOM 1352 CE BMET A 174 -14.390 9.932 21.780 0.25 25.00 C ANISOU 1352 CE BMET A 174 2882 3539 3077 -213 -163 24 C ATOM 1353 N ASN A 175 -14.784 9.501 27.820 1.00 17.16 N ANISOU 1353 N ASN A 175 1962 2646 1913 -111 -421 -220 N ATOM 1354 CA ASN A 175 -14.029 8.657 28.741 1.00 20.19 C ANISOU 1354 CA ASN A 175 2320 3082 2268 -119 -480 -222 C ATOM 1355 C ASN A 175 -14.781 7.355 29.020 1.00 19.76 C ANISOU 1355 C ASN A 175 2279 3097 2131 -69 -439 -194 C ATOM 1356 O ASN A 175 -14.163 6.292 29.131 1.00 20.04 O ANISOU 1356 O ASN A 175 2274 3170 2171 -67 -459 -155 O ATOM 1357 CB ASN A 175 -13.662 9.403 30.041 1.00 20.50 C ANISOU 1357 CB ASN A 175 2416 3101 2273 -139 -576 -295 C ATOM 1358 CG ASN A 175 -14.838 10.130 30.701 1.00 23.17 C ANISOU 1358 CG ASN A 175 2856 3420 2528 -97 -555 -364 C ATOM 1359 OD1 ASN A 175 -16.008 9.830 30.467 1.00 21.92 O ANISOU 1359 OD1 ASN A 175 2717 3288 2323 -44 -475 -356 O ATOM 1360 ND2 ASN A 175 -14.508 11.089 31.562 1.00 23.58 N ANISOU 1360 ND2 ASN A 175 2968 3425 2565 -121 -630 -441 N ATOM 1361 N TYR A 176 -16.116 7.405 29.089 1.00 18.57 N ANISOU 1361 N TYR A 176 2179 2961 1916 -27 -379 -210 N ATOM 1362 CA TYR A 176 -16.882 6.162 29.113 1.00 19.59 C ANISOU 1362 CA TYR A 176 2309 3149 1985 2 -325 -173 C ATOM 1363 C TYR A 176 -16.607 5.327 27.865 1.00 21.09 C ANISOU 1363 C TYR A 176 2435 3343 2235 -4 -284 -109 C ATOM 1364 O TYR A 176 -16.375 4.114 27.953 1.00 19.80 O ANISOU 1364 O TYR A 176 2257 3211 2057 1 -282 -71 O ATOM 1365 CB TYR A 176 -18.385 6.447 29.236 1.00 19.87 C ANISOU 1365 CB TYR A 176 2381 3203 1967 41 -259 -205 C ATOM 1366 CG TYR A 176 -19.206 5.211 28.927 1.00 19.72 C ANISOU 1366 CG TYR A 176 2343 3236 1915 53 -195 -159 C ATOM 1367 CD1 TYR A 176 -19.453 4.259 29.913 1.00 19.15 C ANISOU 1367 CD1 TYR A 176 2306 3214 1757 50 -186 -147 C ATOM 1368 CD2 TYR A 176 -19.694 4.971 27.646 1.00 18.36 C ANISOU 1368 CD2 TYR A 176 2126 3058 1793 57 -151 -124 C ATOM 1369 CE1 TYR A 176 -20.170 3.116 29.639 1.00 19.91 C ANISOU 1369 CE1 TYR A 176 2389 3346 1832 46 -129 -103 C ATOM 1370 CE2 TYR A 176 -20.409 3.819 27.357 1.00 18.22 C ANISOU 1370 CE2 TYR A 176 2092 3080 1751 56 -103 -88 C ATOM 1371 CZ TYR A 176 -20.641 2.895 28.360 1.00 21.29 C ANISOU 1371 CZ TYR A 176 2511 3511 2067 48 -91 -78 C ATOM 1372 OH TYR A 176 -21.349 1.747 28.093 1.00 23.67 O ANISOU 1372 OH TYR A 176 2801 3841 2351 34 -44 -41 O ATOM 1373 N MET A 177 -16.624 5.960 26.690 1.00 18.79 N ANISOU 1373 N MET A 177 2119 3014 2007 -15 -253 -97 N ATOM 1374 CA MET A 177 -16.518 5.196 25.452 1.00 19.86 C ANISOU 1374 CA MET A 177 2213 3156 2176 -20 -203 -46 C ATOM 1375 C MET A 177 -15.144 4.547 25.302 1.00 18.77 C ANISOU 1375 C MET A 177 2017 3022 2093 -41 -221 -21 C ATOM 1376 O MET A 177 -15.040 3.426 24.792 1.00 18.87 O ANISOU 1376 O MET A 177 2006 3054 2109 -27 -187 11 O ATOM 1377 CB MET A 177 -16.825 6.094 24.254 1.00 18.33 C ANISOU 1377 CB MET A 177 2026 2921 2019 -30 -170 -35 C ATOM 1378 CG MET A 177 -18.318 6.390 24.066 1.00 18.75 C ANISOU 1378 CG MET A 177 2114 2977 2032 9 -147 -47 C ATOM 1379 SD MET A 177 -19.293 4.873 23.904 1.00 20.05 S ANISOU 1379 SD MET A 177 2266 3207 2145 30 -104 -25 S ATOM 1380 CE MET A 177 -18.698 4.254 22.318 1.00 19.76 C ANISOU 1380 CE MET A 177 2211 3160 2139 4 -70 25 C ATOM 1381 N VAL A 178 -14.084 5.220 25.741 1.00 19.52 N ANISOU 1381 N VAL A 178 2082 3096 2239 -71 -277 -39 N ATOM 1382 CA VAL A 178 -12.727 4.695 25.558 1.00 18.86 C ANISOU 1382 CA VAL A 178 1915 3020 2231 -88 -296 -20 C ATOM 1383 C VAL A 178 -12.328 3.752 26.692 1.00 19.44 C ANISOU 1383 C VAL A 178 1983 3125 2279 -58 -369 -19 C ATOM 1384 O VAL A 178 -11.916 2.613 26.451 1.00 18.96 O ANISOU 1384 O VAL A 178 1882 3079 2243 -29 -357 11 O ATOM 1385 CB VAL A 178 -11.715 5.855 25.416 1.00 18.62 C ANISOU 1385 CB VAL A 178 1836 2954 2287 -148 -326 -37 C ATOM 1386 CG1 VAL A 178 -10.291 5.323 25.438 1.00 21.43 C ANISOU 1386 CG1 VAL A 178 2079 3329 2734 -162 -356 -26 C ATOM 1387 CG2 VAL A 178 -11.969 6.639 24.130 1.00 20.06 C ANISOU 1387 CG2 VAL A 178 2031 3097 2495 -182 -248 -16 C ATOM 1388 N TYR A 179 -12.426 4.206 27.944 1.00 18.65 N ANISOU 1388 N TYR A 179 1934 3028 2125 -61 -448 -52 N ATOM 1389 CA TYR A 179 -11.929 3.410 29.067 1.00 22.94 C ANISOU 1389 CA TYR A 179 2485 3596 2633 -38 -537 -44 C ATOM 1390 C TYR A 179 -12.885 2.281 29.436 1.00 22.17 C ANISOU 1390 C TYR A 179 2460 3524 2438 2 -504 -13 C ATOM 1391 O TYR A 179 -12.461 1.139 29.637 1.00 20.81 O ANISOU 1391 O TYR A 179 2276 3358 2272 31 -534 27 O ATOM 1392 CB TYR A 179 -11.700 4.293 30.293 1.00 21.38 C ANISOU 1392 CB TYR A 179 2337 3395 2390 -62 -638 -95 C ATOM 1393 CG TYR A 179 -10.534 5.250 30.198 1.00 23.29 C ANISOU 1393 CG TYR A 179 2503 3610 2737 -114 -705 -125 C ATOM 1394 CD1 TYR A 179 -9.310 4.850 29.668 1.00 25.28 C ANISOU 1394 CD1 TYR A 179 2628 3867 3112 -124 -727 -98 C ATOM 1395 CD2 TYR A 179 -10.656 6.558 30.649 1.00 26.12 C ANISOU 1395 CD2 TYR A 179 2912 3933 3078 -156 -743 -185 C ATOM 1396 CE1 TYR A 179 -8.245 5.735 29.587 1.00 25.88 C ANISOU 1396 CE1 TYR A 179 2617 3921 3294 -187 -782 -126 C ATOM 1397 CE2 TYR A 179 -9.602 7.445 30.574 1.00 28.23 C ANISOU 1397 CE2 TYR A 179 3111 4166 3448 -220 -808 -213 C ATOM 1398 CZ TYR A 179 -8.400 7.031 30.043 1.00 28.86 C ANISOU 1398 CZ TYR A 179 3054 4259 3652 -241 -826 -180 C ATOM 1399 OH TYR A 179 -7.355 7.923 29.971 1.00 34.91 O ANISOU 1399 OH TYR A 179 3738 4996 4531 -319 -885 -207 O ATOM 1400 N PHE A 180 -14.170 2.596 29.584 1.00 20.44 N ANISOU 1400 N PHE A 180 2315 3314 2136 2 -446 -31 N ATOM 1401 CA PHE A 180 -15.126 1.619 30.081 1.00 20.44 C ANISOU 1401 CA PHE A 180 2383 3343 2042 21 -410 -3 C ATOM 1402 C PHE A 180 -15.631 0.732 28.951 1.00 22.76 C ANISOU 1402 C PHE A 180 2647 3630 2369 31 -328 35 C ATOM 1403 O PHE A 180 -15.530 -0.497 29.023 1.00 24.39 O ANISOU 1403 O PHE A 180 2866 3835 2567 46 -330 79 O ATOM 1404 CB PHE A 180 -16.288 2.337 30.782 1.00 19.66 C ANISOU 1404 CB PHE A 180 2358 3266 1847 18 -375 -48 C ATOM 1405 CG PHE A 180 -17.209 1.423 31.565 1.00 21.97 C ANISOU 1405 CG PHE A 180 2723 3596 2029 21 -337 -23 C ATOM 1406 CD1 PHE A 180 -18.253 0.759 30.939 1.00 21.36 C ANISOU 1406 CD1 PHE A 180 2635 3532 1949 20 -246 4 C ATOM 1407 CD2 PHE A 180 -17.046 1.265 32.937 1.00 24.78 C ANISOU 1407 CD2 PHE A 180 3163 3975 2279 17 -393 -26 C ATOM 1408 CE1 PHE A 180 -19.109 -0.064 31.661 1.00 21.73 C ANISOU 1408 CE1 PHE A 180 2743 3612 1902 6 -201 31 C ATOM 1409 CE2 PHE A 180 -17.901 0.440 33.668 1.00 24.88 C ANISOU 1409 CE2 PHE A 180 3252 4021 2179 8 -343 6 C ATOM 1410 CZ PHE A 180 -18.931 -0.223 33.030 1.00 21.96 C ANISOU 1410 CZ PHE A 180 2860 3662 1821 -1 -242 35 C ATOM 1411 N ASN A 181 -16.149 1.335 27.884 1.00 21.09 N ANISOU 1411 N ASN A 181 2407 3410 2196 23 -263 20 N ATOM 1412 CA ASN A 181 -16.733 0.524 26.828 1.00 21.52 C ANISOU 1412 CA ASN A 181 2448 3462 2265 27 -194 48 C ATOM 1413 C ASN A 181 -15.649 -0.178 26.016 1.00 26.56 C ANISOU 1413 C ASN A 181 3033 4076 2980 36 -195 73 C ATOM 1414 O ASN A 181 -15.635 -1.410 25.916 1.00 24.54 O ANISOU 1414 O ASN A 181 2789 3812 2723 52 -185 102 O ATOM 1415 CB ASN A 181 -17.631 1.370 25.932 1.00 21.97 C ANISOU 1415 CB ASN A 181 2500 3517 2330 20 -142 28 C ATOM 1416 CG ASN A 181 -18.445 0.518 24.976 1.00 25.03 C ANISOU 1416 CG ASN A 181 2887 3910 2712 18 -87 50 C ATOM 1417 OD1 ASN A 181 -18.074 0.335 23.814 1.00 24.56 O ANISOU 1417 OD1 ASN A 181 2805 3832 2694 14 -63 62 O ATOM 1418 ND2 ASN A 181 -19.549 -0.031 25.470 1.00 24.55 N ANISOU 1418 ND2 ASN A 181 2853 3877 2597 14 -63 53 N ATOM 1419 N PHE A 182 -14.719 0.585 25.443 1.00 22.14 N ANISOU 1419 N PHE A 182 2417 3503 2494 25 -200 60 N ATOM 1420 CA PHE A 182 -13.726 -0.018 24.563 1.00 17.38 C ANISOU 1420 CA PHE A 182 1750 2885 1968 36 -174 74 C ATOM 1421 C PHE A 182 -12.723 -0.870 25.336 1.00 19.83 C ANISOU 1421 C PHE A 182 2026 3192 2316 69 -241 88 C ATOM 1422 O PHE A 182 -12.663 -2.088 25.136 1.00 23.44 O ANISOU 1422 O PHE A 182 2490 3634 2781 104 -227 109 O ATOM 1423 CB PHE A 182 -12.991 1.053 23.748 1.00 18.21 C ANISOU 1423 CB PHE A 182 1797 2981 2141 3 -147 61 C ATOM 1424 CG PHE A 182 -11.993 0.487 22.765 1.00 21.89 C ANISOU 1424 CG PHE A 182 2191 3442 2683 11 -93 69 C ATOM 1425 CD1 PHE A 182 -12.259 -0.717 22.108 1.00 20.03 C ANISOU 1425 CD1 PHE A 182 1975 3202 2433 45 -40 78 C ATOM 1426 CD2 PHE A 182 -10.806 1.163 22.483 1.00 21.36 C ANISOU 1426 CD2 PHE A 182 2035 3375 2705 -18 -87 61 C ATOM 1427 CE1 PHE A 182 -11.358 -1.244 21.197 1.00 21.61 C ANISOU 1427 CE1 PHE A 182 2114 3397 2699 62 23 71 C ATOM 1428 CE2 PHE A 182 -9.895 0.650 21.573 1.00 25.40 C ANISOU 1428 CE2 PHE A 182 2471 3892 3290 -8 -17 61 C ATOM 1429 CZ PHE A 182 -10.170 -0.563 20.927 1.00 26.95 C ANISOU 1429 CZ PHE A 182 2692 4084 3463 38 42 63 C ATOM 1430 N PHE A 183 -11.919 -0.251 26.202 1.00 21.47 N ANISOU 1430 N PHE A 183 2199 3406 2550 61 -325 76 N ATOM 1431 CA PHE A 183 -10.831 -0.991 26.837 1.00 19.33 C ANISOU 1431 CA PHE A 183 1879 3133 2333 99 -407 91 C ATOM 1432 C PHE A 183 -11.365 -2.155 27.671 1.00 22.98 C ANISOU 1432 C PHE A 183 2428 3587 2718 136 -447 127 C ATOM 1433 O PHE A 183 -10.969 -3.310 27.472 1.00 23.71 O ANISOU 1433 O PHE A 183 2505 3652 2851 184 -451 154 O ATOM 1434 CB PHE A 183 -9.980 -0.057 27.703 1.00 22.23 C ANISOU 1434 CB PHE A 183 2202 3512 2733 74 -511 67 C ATOM 1435 CG PHE A 183 -9.092 0.890 26.916 1.00 27.78 C ANISOU 1435 CG PHE A 183 2796 4214 3546 31 -482 42 C ATOM 1436 CD1 PHE A 183 -9.025 0.835 25.531 1.00 28.73 C ANISOU 1436 CD1 PHE A 183 2869 4329 3720 23 -364 46 C ATOM 1437 CD2 PHE A 183 -8.307 1.825 27.577 1.00 29.04 C ANISOU 1437 CD2 PHE A 183 2906 4376 3750 -10 -575 14 C ATOM 1438 CE1 PHE A 183 -8.196 1.705 24.815 1.00 27.72 C ANISOU 1438 CE1 PHE A 183 2646 4199 3685 -28 -324 31 C ATOM 1439 CE2 PHE A 183 -7.480 2.693 26.869 1.00 32.82 C ANISOU 1439 CE2 PHE A 183 3282 4850 4339 -66 -543 -4 C ATOM 1440 CZ PHE A 183 -7.429 2.630 25.481 1.00 28.92 C ANISOU 1440 CZ PHE A 183 2743 4352 3895 -76 -410 9 C ATOM 1441 N ALA A 184 -12.281 -1.873 28.599 1.00 20.91 N ANISOU 1441 N ALA A 184 2263 3341 2343 114 -469 128 N ATOM 1442 CA ALA A 184 -12.689 -2.892 29.563 1.00 24.11 C ANISOU 1442 CA ALA A 184 2760 3740 2663 134 -512 172 C ATOM 1443 C ALA A 184 -13.721 -3.860 28.989 1.00 22.40 C ANISOU 1443 C ALA A 184 2596 3504 2412 132 -422 199 C ATOM 1444 O ALA A 184 -13.625 -5.071 29.216 1.00 22.57 O ANISOU 1444 O ALA A 184 2657 3489 2429 160 -444 245 O ATOM 1445 CB ALA A 184 -13.237 -2.232 30.831 1.00 19.70 C ANISOU 1445 CB ALA A 184 2288 3213 1983 105 -557 158 C ATOM 1446 N CYS A 185 -14.719 -3.362 28.260 1.00 20.71 N ANISOU 1446 N CYS A 185 2385 3307 2178 99 -330 174 N ATOM 1447 CA CYS A 185 -15.852 -4.198 27.878 1.00 21.92 C ANISOU 1447 CA CYS A 185 2590 3451 2290 82 -259 194 C ATOM 1448 C CYS A 185 -15.757 -4.778 26.469 1.00 23.85 C ANISOU 1448 C CYS A 185 2794 3662 2605 93 -200 189 C ATOM 1449 O CYS A 185 -16.511 -5.702 26.149 1.00 23.18 O ANISOU 1449 O CYS A 185 2754 3555 2499 79 -160 207 O ATOM 1450 CB CYS A 185 -17.156 -3.406 28.022 1.00 26.37 C ANISOU 1450 CB CYS A 185 3179 4057 2782 43 -204 168 C ATOM 1451 SG CYS A 185 -17.539 -3.005 29.750 1.00 28.42 S ANISOU 1451 SG CYS A 185 3518 4357 2925 28 -242 169 S ATOM 1452 N VAL A 186 -14.854 -4.281 25.627 1.00 20.87 N ANISOU 1452 N VAL A 186 2340 3281 2308 111 -190 163 N ATOM 1453 CA VAL A 186 -14.734 -4.790 24.264 1.00 23.29 C ANISOU 1453 CA VAL A 186 2622 3562 2664 121 -124 150 C ATOM 1454 C VAL A 186 -13.357 -5.409 24.071 1.00 23.15 C ANISOU 1454 C VAL A 186 2545 3513 2739 176 -144 150 C ATOM 1455 O VAL A 186 -13.234 -6.590 23.723 1.00 22.67 O ANISOU 1455 O VAL A 186 2506 3405 2703 211 -128 157 O ATOM 1456 CB VAL A 186 -14.984 -3.679 23.228 1.00 23.77 C ANISOU 1456 CB VAL A 186 2652 3649 2730 91 -67 120 C ATOM 1457 CG1 VAL A 186 -14.629 -4.166 21.816 1.00 21.85 C ANISOU 1457 CG1 VAL A 186 2391 3385 2526 102 3 103 C ATOM 1458 CG2 VAL A 186 -16.425 -3.211 23.289 1.00 21.42 C ANISOU 1458 CG2 VAL A 186 2403 3376 2359 54 -49 116 C ATOM 1459 N LEU A 187 -12.315 -4.617 24.319 1.00 23.53 N ANISOU 1459 N LEU A 187 2511 3583 2846 185 -182 138 N ATOM 1460 CA LEU A 187 -10.950 -5.046 24.026 1.00 22.16 C ANISOU 1460 CA LEU A 187 2244 3392 2782 238 -191 129 C ATOM 1461 C LEU A 187 -10.526 -6.222 24.899 1.00 25.58 C ANISOU 1461 C LEU A 187 2699 3784 3238 301 -276 162 C ATOM 1462 O LEU A 187 -9.962 -7.207 24.404 1.00 25.66 O ANISOU 1462 O LEU A 187 2681 3750 3319 363 -255 157 O ATOM 1463 CB LEU A 187 -9.997 -3.864 24.205 1.00 25.02 C ANISOU 1463 CB LEU A 187 2506 3792 3209 215 -223 111 C ATOM 1464 CG LEU A 187 -8.574 -3.998 23.676 1.00 31.80 C ANISOU 1464 CG LEU A 187 3229 4652 4202 252 -205 91 C ATOM 1465 CD1 LEU A 187 -8.601 -4.559 22.266 1.00 36.16 C ANISOU 1465 CD1 LEU A 187 3775 5189 4774 270 -75 68 C ATOM 1466 CD2 LEU A 187 -7.883 -2.634 23.707 1.00 29.83 C ANISOU 1466 CD2 LEU A 187 2888 4440 4006 195 -218 73 C ATOM 1467 N VAL A 188 -10.768 -6.133 26.209 1.00 23.00 N ANISOU 1467 N VAL A 188 2427 3464 2846 292 -372 195 N ATOM 1468 CA VAL A 188 -10.379 -7.230 27.105 1.00 24.32 C ANISOU 1468 CA VAL A 188 2636 3585 3020 350 -468 241 C ATOM 1469 C VAL A 188 -11.090 -8.528 26.756 1.00 27.84 C ANISOU 1469 C VAL A 188 3175 3965 3438 367 -421 267 C ATOM 1470 O VAL A 188 -10.415 -9.576 26.678 1.00 24.93 O ANISOU 1470 O VAL A 188 2796 3531 3144 441 -454 281 O ATOM 1471 CB VAL A 188 -10.583 -6.811 28.572 1.00 23.86 C ANISOU 1471 CB VAL A 188 2646 3554 2868 325 -575 273 C ATOM 1472 CG1 VAL A 188 -10.593 -8.043 29.481 1.00 30.33 C ANISOU 1472 CG1 VAL A 188 3563 4317 3646 368 -660 340 C ATOM 1473 CG2 VAL A 188 -9.491 -5.844 29.003 1.00 21.64 C ANISOU 1473 CG2 VAL A 188 2262 3313 2647 328 -662 247 C ATOM 1474 N PRO A 189 -12.414 -8.567 26.535 1.00 26.33 N ANISOU 1474 N PRO A 189 3071 3778 3155 304 -352 270 N ATOM 1475 CA PRO A 189 -13.041 -9.832 26.114 1.00 28.05 C ANISOU 1475 CA PRO A 189 3371 3925 3362 307 -310 288 C ATOM 1476 C PRO A 189 -12.550 -10.344 24.768 1.00 25.08 C ANISOU 1476 C PRO A 189 2944 3507 3076 351 -240 240 C ATOM 1477 O PRO A 189 -12.422 -11.561 24.589 1.00 26.52 O ANISOU 1477 O PRO A 189 3175 3604 3295 396 -245 251 O ATOM 1478 CB PRO A 189 -14.539 -9.486 26.080 1.00 29.61 C ANISOU 1478 CB PRO A 189 3634 4159 3457 218 -249 289 C ATOM 1479 CG PRO A 189 -14.689 -8.352 27.028 1.00 25.33 C ANISOU 1479 CG PRO A 189 3083 3689 2851 187 -286 294 C ATOM 1480 CD PRO A 189 -13.437 -7.543 26.854 1.00 25.55 C ANISOU 1480 CD PRO A 189 3005 3743 2959 228 -323 262 C ATOM 1481 N LEU A 190 -12.279 -9.455 23.808 1.00 20.38 N ANISOU 1481 N LEU A 190 2266 2965 2512 339 -172 188 N ATOM 1482 CA LEU A 190 -11.728 -9.907 22.531 1.00 22.42 C ANISOU 1482 CA LEU A 190 2483 3193 2843 381 -92 137 C ATOM 1483 C LEU A 190 -10.356 -10.546 22.718 1.00 25.59 C ANISOU 1483 C LEU A 190 2808 3553 3364 482 -134 132 C ATOM 1484 O LEU A 190 -10.040 -11.563 22.086 1.00 24.72 O ANISOU 1484 O LEU A 190 2711 3373 3309 544 -95 104 O ATOM 1485 CB LEU A 190 -11.651 -8.740 21.547 1.00 21.88 C ANISOU 1485 CB LEU A 190 2348 3193 2771 339 -10 94 C ATOM 1486 CG LEU A 190 -12.975 -8.242 20.964 1.00 24.92 C ANISOU 1486 CG LEU A 190 2804 3608 3058 260 40 87 C ATOM 1487 CD1 LEU A 190 -12.736 -7.025 20.079 1.00 27.19 C ANISOU 1487 CD1 LEU A 190 3035 3953 3345 226 103 59 C ATOM 1488 CD2 LEU A 190 -13.670 -9.360 20.188 1.00 27.86 C ANISOU 1488 CD2 LEU A 190 3262 3922 3400 256 83 66 C ATOM 1489 N LEU A 191 -9.535 -9.975 23.601 1.00 22.49 N ANISOU 1489 N LEU A 191 2333 3195 3015 505 -219 154 N ATOM 1490 CA LEU A 191 -8.225 -10.550 23.874 1.00 24.66 C ANISOU 1490 CA LEU A 191 2516 3436 3417 607 -281 153 C ATOM 1491 C LEU A 191 -8.352 -11.881 24.603 1.00 25.74 C ANISOU 1491 C LEU A 191 2753 3475 3553 670 -368 204 C ATOM 1492 O LEU A 191 -7.578 -12.810 24.350 1.00 29.33 O ANISOU 1492 O LEU A 191 3171 3860 4113 772 -379 189 O ATOM 1493 CB LEU A 191 -7.384 -9.559 24.678 1.00 26.67 C ANISOU 1493 CB LEU A 191 2660 3758 3715 602 -372 164 C ATOM 1494 CG LEU A 191 -6.937 -8.327 23.887 1.00 34.37 C ANISOU 1494 CG LEU A 191 3516 4811 4733 550 -286 114 C ATOM 1495 CD1 LEU A 191 -6.214 -7.333 24.784 1.00 35.95 C ANISOU 1495 CD1 LEU A 191 3623 5067 4971 525 -392 124 C ATOM 1496 CD2 LEU A 191 -6.059 -8.739 22.709 1.00 34.28 C ANISOU 1496 CD2 LEU A 191 3396 4790 4839 610 -178 59 C ATOM 1497 N LEU A 192 -9.324 -11.991 25.511 1.00 24.92 N ANISOU 1497 N LEU A 192 2778 3360 3331 611 -425 264 N ATOM 1498 CA LEU A 192 -9.600 -13.275 26.145 1.00 29.08 C ANISOU 1498 CA LEU A 192 3429 3783 3838 649 -493 325 C ATOM 1499 C LEU A 192 -10.030 -14.306 25.109 1.00 27.13 C ANISOU 1499 C LEU A 192 3246 3447 3616 664 -402 291 C ATOM 1500 O LEU A 192 -9.573 -15.455 25.130 1.00 29.65 O ANISOU 1500 O LEU A 192 3601 3657 4007 751 -441 303 O ATOM 1501 CB LEU A 192 -10.672 -13.102 27.221 1.00 29.59 C ANISOU 1501 CB LEU A 192 3621 3866 3755 560 -537 393 C ATOM 1502 CG LEU A 192 -10.206 -12.409 28.504 1.00 36.78 C ANISOU 1502 CG LEU A 192 4516 4834 4625 560 -659 435 C ATOM 1503 CD1 LEU A 192 -11.388 -12.019 29.377 1.00 38.68 C ANISOU 1503 CD1 LEU A 192 4875 5117 4703 459 -656 478 C ATOM 1504 CD2 LEU A 192 -9.255 -13.321 29.267 1.00 37.16 C ANISOU 1504 CD2 LEU A 192 4581 4804 4736 662 -799 492 C ATOM 1505 N MET A 193 -10.910 -13.905 24.188 1.00 24.58 N ANISOU 1505 N MET A 193 2942 3163 3233 583 -289 245 N ATOM 1506 CA MET A 193 -11.305 -14.785 23.089 1.00 28.21 C ANISOU 1506 CA MET A 193 3462 3548 3708 588 -205 196 C ATOM 1507 C MET A 193 -10.097 -15.268 22.301 1.00 29.52 C ANISOU 1507 C MET A 193 3543 3669 4004 705 -168 132 C ATOM 1508 O MET A 193 -9.992 -16.457 21.972 1.00 32.07 O ANISOU 1508 O MET A 193 3933 3876 4377 767 -162 113 O ATOM 1509 CB MET A 193 -12.259 -14.058 22.147 1.00 29.26 C ANISOU 1509 CB MET A 193 3603 3752 3762 490 -104 150 C ATOM 1510 CG MET A 193 -13.711 -14.117 22.511 1.00 35.18 C ANISOU 1510 CG MET A 193 4458 4506 4403 383 -108 189 C ATOM 1511 SD MET A 193 -14.597 -13.140 21.286 1.00 37.63 S ANISOU 1511 SD MET A 193 4744 4906 4648 297 -11 128 S ATOM 1512 CE MET A 193 -15.401 -11.934 22.346 1.00 39.34 C ANISOU 1512 CE MET A 193 4944 5225 4780 219 -48 180 C ATOM 1513 N LEU A 194 -9.189 -14.350 21.964 1.00 30.58 N ANISOU 1513 N LEU A 194 3530 3891 4199 733 -134 93 N ATOM 1514 CA LEU A 194 -7.972 -14.736 21.258 1.00 32.30 C ANISOU 1514 CA LEU A 194 3640 4084 4550 845 -84 28 C ATOM 1515 C LEU A 194 -7.182 -15.763 22.055 1.00 29.63 C ANISOU 1515 C LEU A 194 3293 3645 4318 969 -196 62 C ATOM 1516 O LEU A 194 -6.665 -16.733 21.490 1.00 29.38 O ANISOU 1516 O LEU A 194 3260 3524 4380 1072 -160 13 O ATOM 1517 CB LEU A 194 -7.118 -13.500 20.970 1.00 30.08 C ANISOU 1517 CB LEU A 194 3188 3920 4320 836 -39 -4 C ATOM 1518 CG LEU A 194 -5.704 -13.723 20.423 1.00 33.65 C ANISOU 1518 CG LEU A 194 3482 4373 4930 949 13 -66 C ATOM 1519 CD1 LEU A 194 -5.744 -14.390 19.060 1.00 34.23 C ANISOU 1519 CD1 LEU A 194 3594 4401 5009 984 162 -152 C ATOM 1520 CD2 LEU A 194 -4.945 -12.405 20.356 1.00 33.63 C ANISOU 1520 CD2 LEU A 194 3312 4491 4975 908 41 -78 C ATOM 1521 N GLY A 195 -7.086 -15.573 23.373 1.00 27.93 N ANISOU 1521 N GLY A 195 3083 3440 4087 967 -338 146 N ATOM 1522 CA GLY A 195 -6.405 -16.557 24.198 1.00 27.15 C ANISOU 1522 CA GLY A 195 3000 3240 4077 1084 -469 195 C ATOM 1523 C GLY A 195 -7.094 -17.909 24.184 1.00 29.96 C ANISOU 1523 C GLY A 195 3535 3444 4404 1102 -478 222 C ATOM 1524 O GLY A 195 -6.436 -18.952 24.157 1.00 29.83 O ANISOU 1524 O GLY A 195 3525 3310 4500 1229 -521 215 O ATOM 1525 N VAL A 196 -8.429 -17.910 24.195 1.00 29.47 N ANISOU 1525 N VAL A 196 3616 3378 4202 975 -440 250 N ATOM 1526 CA VAL A 196 -9.173 -19.167 24.184 1.00 32.16 C ANISOU 1526 CA VAL A 196 4132 3573 4514 963 -446 278 C ATOM 1527 C VAL A 196 -8.942 -19.909 22.873 1.00 30.11 C ANISOU 1527 C VAL A 196 3874 3230 4336 1029 -343 175 C ATOM 1528 O VAL A 196 -8.699 -21.122 22.859 1.00 30.62 O ANISOU 1528 O VAL A 196 4020 3139 4474 1116 -378 176 O ATOM 1529 CB VAL A 196 -10.672 -18.908 24.433 1.00 28.27 C ANISOU 1529 CB VAL A 196 3762 3115 3865 799 -416 323 C ATOM 1530 CG1 VAL A 196 -11.476 -20.185 24.220 1.00 26.98 C ANISOU 1530 CG1 VAL A 196 3766 2801 3684 765 -404 337 C ATOM 1531 CG2 VAL A 196 -10.883 -18.386 25.844 1.00 29.23 C ANISOU 1531 CG2 VAL A 196 3911 3295 3900 749 -518 425 C ATOM 1532 N TYR A 197 -8.995 -19.188 21.749 1.00 29.87 N ANISOU 1532 N TYR A 197 3765 3296 4290 991 -213 83 N ATOM 1533 CA TYR A 197 -8.806 -19.846 20.460 1.00 32.37 C ANISOU 1533 CA TYR A 197 4097 3544 4657 1046 -103 -25 C ATOM 1534 C TYR A 197 -7.383 -20.367 20.307 1.00 34.26 C ANISOU 1534 C TYR A 197 4226 3726 5064 1224 -108 -74 C ATOM 1535 O TYR A 197 -7.169 -21.439 19.732 1.00 36.08 O ANISOU 1535 O TYR A 197 4520 3826 5363 1312 -73 -137 O ATOM 1536 CB TYR A 197 -9.180 -18.896 19.322 1.00 27.44 C ANISOU 1536 CB TYR A 197 3426 3042 3956 959 31 -101 C ATOM 1537 CG TYR A 197 -10.674 -18.852 19.117 1.00 33.27 C ANISOU 1537 CG TYR A 197 4300 3786 4556 812 47 -84 C ATOM 1538 CD1 TYR A 197 -11.361 -19.983 18.686 1.00 34.02 C ANISOU 1538 CD1 TYR A 197 4545 3750 4632 791 56 -114 C ATOM 1539 CD2 TYR A 197 -11.403 -17.696 19.381 1.00 31.91 C ANISOU 1539 CD2 TYR A 197 4101 3742 4283 695 45 -42 C ATOM 1540 CE1 TYR A 197 -12.730 -19.963 18.509 1.00 31.55 C ANISOU 1540 CE1 TYR A 197 4335 3444 4207 649 62 -100 C ATOM 1541 CE2 TYR A 197 -12.777 -17.665 19.209 1.00 29.53 C ANISOU 1541 CE2 TYR A 197 3901 3449 3873 568 55 -29 C ATOM 1542 CZ TYR A 197 -13.434 -18.803 18.773 1.00 32.30 C ANISOU 1542 CZ TYR A 197 4384 3678 4211 542 62 -57 C ATOM 1543 OH TYR A 197 -14.798 -18.782 18.602 1.00 34.83 O ANISOU 1543 OH TYR A 197 4784 4012 4436 410 64 -47 O ATOM 1544 N LEU A 198 -6.397 -19.637 20.833 1.00 35.72 N ANISOU 1544 N LEU A 198 4243 4004 5326 1281 -155 -52 N ATOM 1545 CA LEU A 198 -5.034 -20.161 20.838 1.00 35.49 C ANISOU 1545 CA LEU A 198 4085 3923 5476 1458 -181 -90 C ATOM 1546 C LEU A 198 -4.958 -21.468 21.617 1.00 33.58 C ANISOU 1546 C LEU A 198 3960 3501 5297 1559 -317 -28 C ATOM 1547 O LEU A 198 -4.271 -22.407 21.201 1.00 34.73 O ANISOU 1547 O LEU A 198 4091 3531 5575 1706 -301 -89 O ATOM 1548 CB LEU A 198 -4.071 -19.126 21.419 1.00 42.36 C ANISOU 1548 CB LEU A 198 4752 4926 6418 1481 -238 -63 C ATOM 1549 CG LEU A 198 -3.820 -17.877 20.566 1.00 47.41 C ANISOU 1549 CG LEU A 198 5248 5726 7040 1407 -97 -131 C ATOM 1550 CD1 LEU A 198 -2.962 -16.867 21.316 1.00 44.17 C ANISOU 1550 CD1 LEU A 198 4654 5431 6698 1407 -181 -92 C ATOM 1551 CD2 LEU A 198 -3.177 -18.247 19.234 1.00 50.57 C ANISOU 1551 CD2 LEU A 198 5573 6114 7528 1492 72 -255 C ATOM 1552 N ARG A 199 -5.675 -21.553 22.743 1.00 35.62 N ANISOU 1552 N ARG A 199 4346 3729 5459 1481 -446 93 N ATOM 1553 CA ARG A 199 -5.707 -22.793 23.513 1.00 39.67 C ANISOU 1553 CA ARG A 199 5002 4060 6009 1557 -577 171 C ATOM 1554 C ARG A 199 -6.428 -23.902 22.754 1.00 36.34 C ANISOU 1554 C ARG A 199 4755 3480 5572 1543 -503 122 C ATOM 1555 O ARG A 199 -6.013 -25.065 22.810 1.00 40.83 O ANISOU 1555 O ARG A 199 5395 3872 6246 1670 -558 120 O ATOM 1556 CB ARG A 199 -6.371 -22.558 24.869 1.00 42.26 C ANISOU 1556 CB ARG A 199 5440 4405 6211 1455 -710 314 C ATOM 1557 CG ARG A 199 -5.553 -21.711 25.830 1.00 51.03 C ANISOU 1557 CG ARG A 199 6413 5630 7346 1491 -832 370 C ATOM 1558 CD ARG A 199 -6.286 -21.527 27.154 1.00 59.25 C ANISOU 1558 CD ARG A 199 7592 6684 8234 1386 -950 504 C ATOM 1559 NE ARG A 199 -5.437 -20.926 28.181 1.00 70.71 N ANISOU 1559 NE ARG A 199 8944 8213 9708 1437 -1102 562 N ATOM 1560 CZ ARG A 199 -4.719 -21.623 29.058 1.00 80.86 C ANISOU 1560 CZ ARG A 199 10261 9402 11061 1558 -1278 641 C ATOM 1561 NH1 ARG A 199 -4.748 -22.950 29.036 1.00 84.47 N ANISOU 1561 NH1 ARG A 199 10851 9670 11575 1643 -1320 677 N ATOM 1562 NH2 ARG A 199 -3.971 -20.996 29.958 1.00 83.90 N ANISOU 1562 NH2 ARG A 199 10550 9870 11457 1593 -1425 685 N ATOM 1563 N ILE A 200 -7.507 -23.566 22.041 1.00 32.34 N ANISOU 1563 N ILE A 200 4321 3026 4939 1393 -388 80 N ATOM 1564 CA ILE A 200 -8.243 -24.576 21.279 1.00 33.63 C ANISOU 1564 CA ILE A 200 4651 3045 5081 1361 -324 24 C ATOM 1565 C ILE A 200 -7.347 -25.198 20.214 1.00 34.98 C ANISOU 1565 C ILE A 200 4770 3136 5386 1517 -237 -112 C ATOM 1566 O ILE A 200 -7.268 -26.425 20.079 1.00 37.58 O ANISOU 1566 O ILE A 200 5220 3271 5789 1601 -264 -136 O ATOM 1567 CB ILE A 200 -9.505 -23.962 20.649 1.00 33.02 C ANISOU 1567 CB ILE A 200 4630 3066 4851 1173 -226 -5 C ATOM 1568 CG1 ILE A 200 -10.571 -23.715 21.713 1.00 34.20 C ANISOU 1568 CG1 ILE A 200 4872 3244 4879 1024 -305 124 C ATOM 1569 CG2 ILE A 200 -10.039 -24.864 19.547 1.00 33.87 C ANISOU 1569 CG2 ILE A 200 4869 3050 4952 1153 -144 -105 C ATOM 1570 CD1 ILE A 200 -11.721 -22.845 21.229 1.00 30.52 C ANISOU 1570 CD1 ILE A 200 4407 2911 4276 853 -222 102 C ATOM 1571 N PHE A 201 -6.664 -24.356 19.434 1.00 36.26 N ANISOU 1571 N PHE A 201 4756 3441 5579 1554 -124 -205 N ATOM 1572 CA PHE A 201 -5.840 -24.877 18.349 1.00 37.64 C ANISOU 1572 CA PHE A 201 4876 3561 5866 1694 -10 -347 C ATOM 1573 C PHE A 201 -4.576 -25.544 18.873 1.00 37.81 C ANISOU 1573 C PHE A 201 4800 3484 6083 1906 -94 -342 C ATOM 1574 O PHE A 201 -4.087 -26.498 18.261 1.00 41.05 O ANISOU 1574 O PHE A 201 5239 3757 6601 2044 -44 -439 O ATOM 1575 CB PHE A 201 -5.506 -23.756 17.364 1.00 40.16 C ANISOU 1575 CB PHE A 201 5042 4069 6150 1657 149 -438 C ATOM 1576 CG PHE A 201 -6.716 -23.164 16.694 1.00 39.63 C ANISOU 1576 CG PHE A 201 5075 4085 5899 1471 229 -455 C ATOM 1577 CD1 PHE A 201 -7.572 -23.965 15.955 1.00 41.73 C ANISOU 1577 CD1 PHE A 201 5525 4238 6091 1418 273 -519 C ATOM 1578 CD2 PHE A 201 -6.998 -21.817 16.800 1.00 38.58 C ANISOU 1578 CD2 PHE A 201 4852 4133 5672 1351 248 -410 C ATOM 1579 CE1 PHE A 201 -8.688 -23.427 15.340 1.00 38.29 C ANISOU 1579 CE1 PHE A 201 5172 3881 5495 1251 327 -534 C ATOM 1580 CE2 PHE A 201 -8.110 -21.275 16.190 1.00 39.44 C ANISOU 1580 CE2 PHE A 201 5049 4313 5625 1194 306 -422 C ATOM 1581 CZ PHE A 201 -8.958 -22.085 15.457 1.00 39.99 C ANISOU 1581 CZ PHE A 201 5290 4279 5624 1145 342 -483 C ATOM 1582 N ALA A 202 -4.040 -25.072 20.001 1.00 39.25 N ANISOU 1582 N ALA A 202 4871 3728 6314 1938 -229 -234 N ATOM 1583 CA ALA A 202 -2.923 -25.775 20.623 1.00 42.55 C ANISOU 1583 CA ALA A 202 5211 4040 6918 2140 -349 -211 C ATOM 1584 C ALA A 202 -3.362 -27.137 21.146 1.00 43.52 C ANISOU 1584 C ALA A 202 5557 3922 7057 2189 -468 -146 C ATOM 1585 O ALA A 202 -2.622 -28.122 21.030 1.00 45.89 O ANISOU 1585 O ALA A 202 5856 4063 7517 2375 -501 -191 O ATOM 1586 CB ALA A 202 -2.327 -24.933 21.750 1.00 40.47 C ANISOU 1586 CB ALA A 202 4793 3900 6682 2146 -490 -106 C ATOM 1587 N ALA A 203 -4.568 -27.215 21.717 1.00 43.25 N ANISOU 1587 N ALA A 203 5716 3852 6864 2022 -529 -41 N ATOM 1588 CA ALA A 203 -5.067 -28.492 22.219 1.00 44.18 C ANISOU 1588 CA ALA A 203 6064 3736 6986 2037 -634 32 C ATOM 1589 C ALA A 203 -5.315 -29.475 21.082 1.00 43.34 C ANISOU 1589 C ALA A 203 6079 3468 6922 2077 -521 -98 C ATOM 1590 O ALA A 203 -5.044 -30.673 21.219 1.00 47.34 O ANISOU 1590 O ALA A 203 6701 3749 7535 2202 -593 -95 O ATOM 1591 CB ALA A 203 -6.347 -28.272 23.027 1.00 45.36 C ANISOU 1591 CB ALA A 203 6377 3907 6950 1827 -693 167 C ATOM 1592 N ALA A 204 -5.825 -28.988 19.950 1.00 43.66 N ANISOU 1592 N ALA A 204 6103 3611 6873 1973 -353 -215 N ATOM 1593 CA ALA A 204 -6.085 -29.872 18.819 1.00 46.08 C ANISOU 1593 CA ALA A 204 6536 3773 7198 1999 -246 -354 C ATOM 1594 C ALA A 204 -4.789 -30.376 18.195 1.00 49.27 C ANISOU 1594 C ALA A 204 6825 4107 7788 2238 -185 -484 C ATOM 1595 O ALA A 204 -4.677 -31.561 17.859 1.00 54.07 O ANISOU 1595 O ALA A 204 7564 4496 8484 2345 -188 -552 O ATOM 1596 CB ALA A 204 -6.937 -29.151 17.780 1.00 41.45 C ANISOU 1596 CB ALA A 204 5962 3331 6457 1827 -95 -441 C ATOM 1597 N AARG A 205 -3.805 -29.491 18.026 0.50 48.94 N ANISOU 1597 N AARG A 205 6536 4245 7815 2321 -123 -527 N ATOM 1598 N BARG A 205 -3.802 -29.491 18.022 0.50 48.93 N ANISOU 1598 N BARG A 205 6534 4244 7814 2321 -122 -528 N ATOM 1599 CA AARG A 205 -2.516 -29.913 17.491 0.50 52.66 C ANISOU 1599 CA AARG A 205 6860 4669 8478 2553 -55 -651 C ATOM 1600 CA BARG A 205 -2.513 -29.919 17.485 0.50 52.67 C ANISOU 1600 CA BARG A 205 6862 4669 8480 2554 -54 -652 C ATOM 1601 C AARG A 205 -1.859 -30.949 18.394 0.50 54.52 C ANISOU 1601 C AARG A 205 7122 4749 8846 2682 -197 -550 C ATOM 1602 C BARG A 205 -1.853 -30.949 18.393 0.50 54.51 C ANISOU 1602 C BARG A 205 7119 4747 8845 2682 -197 -550 C ATOM 1603 O AARG A 205 -1.243 -31.907 17.910 0.50 57.42 O ANISOU 1603 O AARG A 205 7503 5000 9313 2805 -130 -621 O ATOM 1604 O BARG A 205 -1.226 -31.901 17.913 0.50 57.42 O ANISOU 1604 O BARG A 205 7500 5002 9314 2806 -129 -621 O ATOM 1605 CB AARG A 205 -1.602 -28.702 17.313 0.50 54.61 C ANISOU 1605 CB AARG A 205 6819 5158 8772 2582 28 -683 C ATOM 1606 CB BARG A 205 -1.587 -28.714 17.291 0.50 54.65 C ANISOU 1606 CB BARG A 205 6823 5162 8780 2586 31 -687 C ATOM 1607 CG AARG A 205 -0.172 -29.054 16.943 0.50 57.74 C ANISOU 1607 CG AARG A 205 7039 5586 9314 2746 121 -741 C ATOM 1608 CG BARG A 205 -2.052 -27.680 16.266 0.50 54.95 C ANISOU 1608 CG BARG A 205 6823 5395 8661 2424 219 -766 C ATOM 1609 CD AARG A 205 0.723 -27.831 17.010 0.50 59.95 C ANISOU 1609 CD AARG A 205 7041 6110 9629 2741 169 -730 C ATOM 1610 CD BARG A 205 -1.960 -28.188 14.832 0.50 59.19 C ANISOU 1610 CD BARG A 205 7415 5879 9194 2479 417 -953 C ATOM 1611 NE AARG A 205 0.604 -27.152 18.297 0.50 61.45 N ANISOU 1611 NE AARG A 205 7172 6368 9809 2677 -24 -579 N ATOM 1612 NE BARG A 205 -0.625 -28.677 14.496 0.50 64.39 N ANISOU 1612 NE BARG A 205 7933 6527 10006 2666 500 -1021 N ATOM 1613 CZ AARG A 205 1.161 -25.979 18.578 0.50 63.05 C ANISOU 1613 CZ AARG A 205 7161 6773 10023 2631 -25 -546 C ATOM 1614 CZ BARG A 205 -0.239 -29.008 13.267 0.50 66.16 C ANISOU 1614 CZ BARG A 205 8172 6760 10205 2719 695 -1164 C ATOM 1615 NH1AARG A 205 1.880 -25.348 17.661 0.50 65.26 N ANISOU 1615 NH1AARG A 205 7264 7209 10324 2634 158 -644 N ATOM 1616 NH1BARG A 205 -1.085 -28.895 12.252 0.50 64.73 N ANISOU 1616 NH1BARG A 205 8134 6583 9877 2614 818 -1275 N ATOM 1617 NH2AARG A 205 0.996 -25.435 19.776 0.50 62.49 N ANISOU 1617 NH2AARG A 205 7068 6749 9927 2571 -209 -412 N ATOM 1618 NH2BARG A 205 0.993 -29.449 13.049 0.50 69.05 N ANISOU 1618 NH2BARG A 205 8416 7139 10680 2880 760 -1198 N ATOM 1619 N ARG A 206 -1.984 -30.777 19.712 1.00 50.33 N ANISOU 1619 N ARG A 206 6606 4218 8298 2646 -389 -378 N ATOM 1620 CA ARG A 206 -1.387 -31.730 20.642 1.00 49.43 C ANISOU 1620 CA ARG A 206 6528 3973 8281 2750 -531 -264 C ATOM 1621 C ARG A 206 -2.048 -33.100 20.536 1.00 54.49 C ANISOU 1621 C ARG A 206 7432 4354 8916 2741 -555 -259 C ATOM 1622 O ARG A 206 -1.364 -34.129 20.569 1.00 55.45 O ANISOU 1622 O ARG A 206 7571 4340 9158 2875 -569 -264 O ATOM 1623 CB ARG A 206 -1.479 -31.204 22.073 1.00 51.60 C ANISOU 1623 CB ARG A 206 6791 4317 8499 2687 -726 -80 C ATOM 1624 CG ARG A 206 -1.006 -32.216 23.101 1.00 60.47 C ANISOU 1624 CG ARG A 206 7989 5298 9688 2774 -887 50 C ATOM 1625 CD ARG A 206 -0.698 -31.593 24.452 1.00 70.36 C ANISOU 1625 CD ARG A 206 9171 6667 10897 2744 -1062 207 C ATOM 1626 NE ARG A 206 0.088 -32.515 25.271 1.00 83.28 N ANISOU 1626 NE ARG A 206 10825 8196 12623 2868 -1197 300 N ATOM 1627 CZ ARG A 206 0.517 -32.258 26.503 1.00 88.68 C ANISOU 1627 CZ ARG A 206 11469 8947 13280 2871 -1367 436 C ATOM 1628 NH1 ARG A 206 0.238 -31.097 27.079 1.00 89.11 N ANISOU 1628 NH1 ARG A 206 11463 9175 13219 2752 -1421 493 N ATOM 1629 NH2 ARG A 206 1.228 -33.166 27.160 1.00 92.48 N ANISOU 1629 NH2 ARG A 206 11976 9318 13845 2993 -1487 511 N ATOM 1630 N GLN A 207 -3.375 -33.135 20.401 1.00 54.56 N ANISOU 1630 N GLN A 207 7650 4291 8788 2579 -558 -249 N ATOM 1631 CA GLN A 207 -4.071 -34.415 20.323 1.00 56.42 C ANISOU 1631 CA GLN A 207 8141 4283 9013 2536 -582 -239 C ATOM 1632 C GLN A 207 -3.804 -35.111 18.995 1.00 58.01 C ANISOU 1632 C GLN A 207 8362 4391 9287 2617 -417 -430 C ATOM 1633 O GLN A 207 -3.628 -36.335 18.954 1.00 62.46 O ANISOU 1633 O GLN A 207 9040 4755 9935 2686 -433 -438 O ATOM 1634 CB GLN A 207 -5.569 -34.208 20.541 1.00 53.60 C ANISOU 1634 CB GLN A 207 7992 3891 8484 2320 -623 -172 C ATOM 1635 CG GLN A 207 -5.915 -33.739 21.941 1.00 54.76 C ANISOU 1635 CG GLN A 207 8165 4095 8545 2229 -782 32 C ATOM 1636 CD GLN A 207 -7.395 -33.460 22.116 1.00 59.34 C ANISOU 1636 CD GLN A 207 8915 4693 8939 1982 -777 102 C ATOM 1637 OE1 GLN A 207 -8.233 -34.026 21.413 1.00 63.42 O ANISOU 1637 OE1 GLN A 207 9585 5102 9409 1876 -703 33 O ATOM 1638 NE2 GLN A 207 -7.724 -32.576 23.053 1.00 56.70 N ANISOU 1638 NE2 GLN A 207 8528 4526 8488 1864 -836 236 N ATOM 1639 N LEU A 208 -3.775 -34.356 17.902 1.00 58.07 N ANISOU 1639 N LEU A 208 8268 4542 9253 2605 -254 -584 N ATOM 1640 CA LEU A 208 -3.391 -34.906 16.608 1.00 57.06 C ANISOU 1640 CA LEU A 208 8141 4361 9180 2686 -77 -773 C ATOM 1641 C LEU A 208 -1.927 -35.330 16.634 1.00 57.53 C ANISOU 1641 C LEU A 208 8027 4417 9414 2899 -40 -793 C ATOM 1642 O LEU A 208 -1.600 -36.480 16.333 1.00 60.68 O ANISOU 1642 O LEU A 208 8512 4636 9907 2998 -11 -846 O ATOM 1643 CB LEU A 208 -3.628 -33.887 15.492 1.00 61.59 C ANISOU 1643 CB LEU A 208 8636 5120 9645 2618 93 -919 C ATOM 1644 CG LEU A 208 -5.072 -33.630 15.055 1.00 64.67 C ANISOU 1644 CG LEU A 208 9227 5498 9847 2423 101 -952 C ATOM 1645 CD1 LEU A 208 -5.168 -32.348 14.240 1.00 66.18 C ANISOU 1645 CD1 LEU A 208 9286 5948 9911 2335 250 -1032 C ATOM 1646 CD2 LEU A 208 -5.608 -34.809 14.257 1.00 67.52 C ANISOU 1646 CD2 LEU A 208 9804 5657 10192 2383 153 -1062 C ATOM 1647 N ALA A1001 -0.869 -34.883 17.341 1.00 87.32 N ANISOU 1647 N ALA A1001 12852 4343 15981 938 140 -629 N ATOM 1648 CA ALA A1001 0.470 -35.367 17.659 1.00 85.43 C ANISOU 1648 CA ALA A1001 12222 4095 16143 494 180 -506 C ATOM 1649 C ALA A1001 0.412 -36.635 18.505 1.00 81.43 C ANISOU 1649 C ALA A1001 11328 3999 15614 540 157 -707 C ATOM 1650 O ALA A1001 1.097 -37.615 18.213 1.00 79.60 O ANISOU 1650 O ALA A1001 10726 3951 15568 363 381 -535 O ATOM 1651 CB ALA A1001 1.268 -34.290 18.375 1.00 90.14 C ANISOU 1651 CB ALA A1001 12968 4284 16996 178 -149 -550 C ATOM 1652 N ASP A1002 -0.418 -36.606 19.552 1.00 80.56 N ANISOU 1652 N ASP A1002 11337 4023 15248 816 -83 -1054 N ATOM 1653 CA ASP A1002 -0.517 -37.752 20.451 1.00 77.31 C ANISOU 1653 CA ASP A1002 10612 3982 14780 870 -121 -1252 C ATOM 1654 C ASP A1002 -1.039 -38.987 19.727 1.00 73.44 C ANISOU 1654 C ASP A1002 9867 3910 14127 1006 169 -1121 C ATOM 1655 O ASP A1002 -0.566 -40.103 19.971 1.00 70.81 O ANISOU 1655 O ASP A1002 9211 3887 13808 860 241 -1093 O ATOM 1656 CB ASP A1002 -1.411 -37.411 21.644 1.00 85.11 C ANISOU 1656 CB ASP A1002 11839 5041 15456 1216 -356 -1601 C ATOM 1657 CG ASP A1002 -0.734 -36.483 22.634 1.00 93.15 C ANISOU 1657 CG ASP A1002 13149 5701 16544 1055 -715 -1771 C ATOM 1658 OD1 ASP A1002 0.512 -36.489 22.696 1.00 96.92 O ANISOU 1658 OD1 ASP A1002 13453 5993 17380 609 -847 -1655 O ATOM 1659 OD2 ASP A1002 -1.448 -35.751 23.353 1.00 97.62 O ANISOU 1659 OD2 ASP A1002 14118 6173 16800 1387 -868 -1998 O ATOM 1660 N LEU A1003 -2.018 -38.810 18.835 1.00 74.14 N ANISOU 1660 N LEU A1003 10137 4034 14001 1284 285 -1026 N ATOM 1661 CA LEU A1003 -2.525 -39.939 18.059 1.00 72.29 C ANISOU 1661 CA LEU A1003 9749 4168 13549 1381 463 -873 C ATOM 1662 C LEU A1003 -1.452 -40.504 17.139 1.00 69.50 C ANISOU 1662 C LEU A1003 9311 3763 13334 1124 720 -587 C ATOM 1663 O LEU A1003 -1.304 -41.727 17.024 1.00 66.97 O ANISOU 1663 O LEU A1003 8790 3757 12899 1086 819 -528 O ATOM 1664 CB LEU A1003 -3.746 -39.514 17.244 1.00 76.74 C ANISOU 1664 CB LEU A1003 10560 4701 13895 1718 445 -810 C ATOM 1665 CG LEU A1003 -5.080 -39.332 17.966 1.00 78.19 C ANISOU 1665 CG LEU A1003 10708 5108 13891 2086 278 -1007 C ATOM 1666 CD1 LEU A1003 -6.061 -38.625 17.052 1.00 81.15 C ANISOU 1666 CD1 LEU A1003 11343 5332 14157 2399 228 -904 C ATOM 1667 CD2 LEU A1003 -5.635 -40.677 18.406 1.00 74.88 C ANISOU 1667 CD2 LEU A1003 9919 5210 13320 2110 273 -1024 C ATOM 1668 N GLU A1004 -0.703 -39.628 16.467 1.00 74.53 N ANISOU 1668 N GLU A1004 10118 3994 14205 970 853 -380 N ATOM 1669 CA GLU A1004 0.345 -40.085 15.563 1.00 78.85 C ANISOU 1669 CA GLU A1004 10577 4493 14889 786 1196 -45 C ATOM 1670 C GLU A1004 1.495 -40.732 16.324 1.00 77.59 C ANISOU 1670 C GLU A1004 9979 4484 15020 499 1219 -41 C ATOM 1671 O GLU A1004 2.111 -41.679 15.823 1.00 77.79 O ANISOU 1671 O GLU A1004 9835 4694 15027 472 1495 162 O ATOM 1672 CB GLU A1004 0.842 -38.912 14.715 1.00 89.18 C ANISOU 1672 CB GLU A1004 12145 5373 16365 678 1353 227 C ATOM 1673 CG GLU A1004 1.720 -39.302 13.539 1.00 96.56 C ANISOU 1673 CG GLU A1004 13082 6254 17353 614 1823 647 C ATOM 1674 CD GLU A1004 1.070 -40.336 12.638 1.00 98.95 C ANISOU 1674 CD GLU A1004 13619 6796 17181 936 1981 705 C ATOM 1675 OE1 GLU A1004 1.701 -41.383 12.386 1.00 98.17 O ANISOU 1675 OE1 GLU A1004 13363 6879 17060 941 2250 854 O ATOM 1676 OE2 GLU A1004 -0.073 -40.106 12.186 1.00100.15 O ANISOU 1676 OE2 GLU A1004 14127 6965 16960 1189 1784 605 O ATOM 1677 N ASP A1005 1.785 -40.251 17.537 1.00 75.53 N ANISOU 1677 N ASP A1005 9574 4127 14996 323 904 -267 N ATOM 1678 CA ASP A1005 2.841 -40.856 18.342 1.00 78.27 C ANISOU 1678 CA ASP A1005 9510 4603 15628 58 829 -282 C ATOM 1679 C ASP A1005 2.475 -42.274 18.762 1.00 75.51 C ANISOU 1679 C ASP A1005 8989 4735 14968 208 831 -433 C ATOM 1680 O ASP A1005 3.321 -43.174 18.732 1.00 75.08 O ANISOU 1680 O ASP A1005 8634 4862 15032 97 978 -297 O ATOM 1681 CB ASP A1005 3.134 -39.994 19.571 1.00 84.36 C ANISOU 1681 CB ASP A1005 10296 5101 16656 -134 388 -524 C ATOM 1682 CG ASP A1005 4.039 -38.818 19.257 1.00 96.42 C ANISOU 1682 CG ASP A1005 11842 6132 18662 -465 337 -283 C ATOM 1683 OD1 ASP A1005 4.843 -38.924 18.308 1.00100.40 O ANISOU 1683 OD1 ASP A1005 12125 6578 19443 -632 703 124 O ATOM 1684 OD2 ASP A1005 3.950 -37.791 19.964 1.00101.94 O ANISOU 1684 OD2 ASP A1005 12802 6580 19350 -537 -61 -471 O ATOM 1685 N ASN A1006 1.218 -42.493 19.164 1.00 74.16 N ANISOU 1685 N ASN A1006 8989 4772 14418 468 676 -683 N ATOM 1686 CA ASN A1006 0.797 -43.837 19.546 1.00 72.25 C ANISOU 1686 CA ASN A1006 8598 4961 13893 574 663 -784 C ATOM 1687 C ASN A1006 0.750 -44.765 18.339 1.00 67.22 C ANISOU 1687 C ASN A1006 8012 4468 13060 667 937 -539 C ATOM 1688 O ASN A1006 1.090 -45.949 18.445 1.00 60.50 O ANISOU 1688 O ASN A1006 7009 3864 12113 645 989 -512 O ATOM 1689 CB ASN A1006 -0.561 -43.784 20.246 1.00 72.66 C ANISOU 1689 CB ASN A1006 8764 5199 13643 819 468 -1032 C ATOM 1690 CG ASN A1006 -0.442 -43.421 21.714 1.00 74.95 C ANISOU 1690 CG ASN A1006 9031 5464 13981 795 209 -1315 C ATOM 1691 OD1 ASN A1006 0.572 -43.706 22.351 1.00 79.22 O ANISOU 1691 OD1 ASN A1006 9407 5977 14718 574 102 -1360 O ATOM 1692 ND2 ASN A1006 -1.477 -42.791 22.258 1.00 68.92 N ANISOU 1692 ND2 ASN A1006 8463 4701 13025 1062 99 -1498 N ATOM 1693 N TRP A1007 0.334 -44.244 17.182 1.00 66.83 N ANISOU 1693 N TRP A1007 8253 4228 12912 800 1085 -365 N ATOM 1694 CA TRP A1007 0.383 -45.027 15.952 1.00 64.42 C ANISOU 1694 CA TRP A1007 8137 3964 12375 925 1329 -124 C ATOM 1695 C TRP A1007 1.820 -45.384 15.591 1.00 67.73 C ANISOU 1695 C TRP A1007 8389 4329 13014 800 1661 123 C ATOM 1696 O TRP A1007 2.107 -46.522 15.195 1.00 63.71 O ANISOU 1696 O TRP A1007 7908 3991 12306 901 1813 224 O ATOM 1697 CB TRP A1007 -0.291 -44.246 14.822 1.00 68.36 C ANISOU 1697 CB TRP A1007 9048 4206 12720 1107 1390 13 C ATOM 1698 CG TRP A1007 -0.274 -44.913 13.475 1.00 72.95 C ANISOU 1698 CG TRP A1007 9985 4739 12994 1288 1609 259 C ATOM 1699 CD1 TRP A1007 0.421 -44.508 12.371 1.00 77.07 C ANISOU 1699 CD1 TRP A1007 10778 4983 13522 1350 1979 563 C ATOM 1700 CD2 TRP A1007 -0.996 -46.088 13.083 1.00 71.30 C ANISOU 1700 CD2 TRP A1007 9974 4722 12393 1450 1452 238 C ATOM 1701 NE1 TRP A1007 0.178 -45.358 11.320 1.00 76.53 N ANISOU 1701 NE1 TRP A1007 11131 4917 13031 1596 2075 705 N ATOM 1702 CE2 TRP A1007 -0.688 -46.336 11.731 1.00 72.91 C ANISOU 1702 CE2 TRP A1007 10647 4723 12333 1641 1708 498 C ATOM 1703 CE3 TRP A1007 -1.874 -46.953 13.745 1.00 60.84 C ANISOU 1703 CE3 TRP A1007 8503 3697 10917 1445 1111 50 C ATOM 1704 CZ2 TRP A1007 -1.223 -47.414 11.029 1.00 70.78 C ANISOU 1704 CZ2 TRP A1007 10768 4495 11630 1830 1558 535 C ATOM 1705 CZ3 TRP A1007 -2.404 -48.019 13.046 1.00 68.42 C ANISOU 1705 CZ3 TRP A1007 9767 4711 11517 1569 960 122 C ATOM 1706 CH2 TRP A1007 -2.076 -48.241 11.702 1.00 68.58 C ANISOU 1706 CH2 TRP A1007 10319 4481 11257 1763 1146 342 C ATOM 1707 N GLU A1008 2.741 -44.427 15.734 1.00 67.69 N ANISOU 1707 N GLU A1008 8203 4075 13440 588 1766 245 N ATOM 1708 CA GLU A1008 4.151 -44.707 15.476 1.00 77.28 C ANISOU 1708 CA GLU A1008 9120 5270 14975 454 2097 541 C ATOM 1709 C GLU A1008 4.704 -45.726 16.463 1.00 72.91 C ANISOU 1709 C GLU A1008 8178 5011 14514 364 1955 402 C ATOM 1710 O GLU A1008 5.494 -46.597 16.085 1.00 73.18 O ANISOU 1710 O GLU A1008 8061 5185 14559 442 2244 610 O ATOM 1711 CB GLU A1008 4.968 -43.418 15.541 1.00 79.31 C ANISOU 1711 CB GLU A1008 9191 5179 15764 165 2144 728 C ATOM 1712 CG GLU A1008 4.781 -42.488 14.362 1.00 86.40 C ANISOU 1712 CG GLU A1008 10460 5748 16618 244 2420 997 C ATOM 1713 CD GLU A1008 5.462 -41.153 14.579 1.00 96.69 C ANISOU 1713 CD GLU A1008 11610 6661 18466 -101 2358 1156 C ATOM 1714 OE1 GLU A1008 6.495 -41.119 15.280 1.00101.07 O ANISOU 1714 OE1 GLU A1008 11676 7205 19522 -415 2268 1237 O ATOM 1715 OE2 GLU A1008 4.959 -40.135 14.059 1.00101.65 O ANISOU 1715 OE2 GLU A1008 12619 6966 19036 -69 2348 1206 O ATOM 1716 N THR A1009 4.310 -45.626 17.735 1.00 69.28 N ANISOU 1716 N THR A1009 7596 4636 14093 245 1526 60 N ATOM 1717 CA THR A1009 4.815 -46.556 18.739 1.00 70.26 C ANISOU 1717 CA THR A1009 7406 5010 14279 164 1349 -83 C ATOM 1718 C THR A1009 4.354 -47.981 18.454 1.00 68.84 C ANISOU 1718 C THR A1009 7369 5138 13649 395 1435 -112 C ATOM 1719 O THR A1009 5.106 -48.939 18.674 1.00 66.27 O ANISOU 1719 O THR A1009 6833 4983 13365 404 1500 -54 O ATOM 1720 CB THR A1009 4.376 -46.107 20.134 1.00 69.84 C ANISOU 1720 CB THR A1009 7332 4947 14258 52 886 -445 C ATOM 1721 OG1 THR A1009 5.003 -44.858 20.451 1.00 73.19 O ANISOU 1721 OG1 THR A1009 7663 5017 15127 -194 726 -415 O ATOM 1722 CG2 THR A1009 4.765 -47.139 21.182 1.00 67.78 C ANISOU 1722 CG2 THR A1009 6843 4944 13968 8 680 -609 C ATOM 1723 N ALEU A1010 3.126 -48.135 17.953 0.40 67.28 N ANISOU 1723 N ALEU A1010 7536 4987 13040 582 1394 -184 N ATOM 1724 N BLEU A1010 3.127 -48.147 17.956 0.60 67.42 N ANISOU 1724 N BLEU A1010 7554 5008 13057 582 1393 -184 N ATOM 1725 CA ALEU A1010 2.618 -49.460 17.611 0.40 64.24 C ANISOU 1725 CA ALEU A1010 7351 4820 12237 758 1389 -188 C ATOM 1726 CA BLEU A1010 2.654 -49.489 17.630 0.60 64.20 C ANISOU 1726 CA BLEU A1010 7337 4821 12237 755 1391 -188 C ATOM 1727 C ALEU A1010 3.408 -50.074 16.462 0.40 64.43 C ANISOU 1727 C ALEU A1010 7531 4784 12164 929 1771 108 C ATOM 1728 C BLEU A1010 3.433 -50.083 16.462 0.60 64.50 C ANISOU 1728 C BLEU A1010 7536 4793 12177 929 1776 111 C ATOM 1729 O ALEU A1010 3.762 -51.258 16.504 0.40 63.12 O ANISOU 1729 O ALEU A1010 7382 4776 11825 1028 1804 126 O ATOM 1730 O BLEU A1010 3.804 -51.261 16.493 0.60 62.72 O ANISOU 1730 O BLEU A1010 7325 4723 11781 1030 1815 133 O ATOM 1731 CB ALEU A1010 1.135 -49.368 17.250 0.40 63.71 C ANISOU 1731 CB ALEU A1010 7601 4769 11837 882 1202 -273 C ATOM 1732 CB BLEU A1010 1.158 -49.462 17.319 0.60 63.60 C ANISOU 1732 CB BLEU A1010 7571 4777 11818 877 1192 -282 C ATOM 1733 CG ALEU A1010 0.374 -50.679 17.041 0.40 62.09 C ANISOU 1733 CG ALEU A1010 7604 4753 11233 986 1039 -291 C ATOM 1734 CG BLEU A1010 0.231 -49.191 18.505 0.60 61.99 C ANISOU 1734 CG BLEU A1010 7215 4729 11609 811 874 -547 C ATOM 1735 CD1ALEU A1010 0.156 -51.380 18.368 0.40 59.66 C ANISOU 1735 CD1ALEU A1010 7034 4720 10914 861 795 -494 C ATOM 1736 CD1BLEU A1010 -1.226 -49.361 18.101 0.60 61.45 C ANISOU 1736 CD1BLEU A1010 7350 4746 11253 946 704 -552 C ATOM 1737 CD2ALEU A1010 -0.953 -50.427 16.343 0.40 62.38 C ANISOU 1737 CD2ALEU A1010 7936 4729 11038 1101 863 -265 C ATOM 1738 CD2BLEU A1010 0.580 -50.101 19.672 0.60 59.96 C ANISOU 1738 CD2BLEU A1010 6722 4714 11347 707 733 -696 C ATOM 1739 N ASN A1011 3.697 -49.283 15.428 1.00 65.77 N ANISOU 1739 N ASN A1011 7867 4710 12414 1005 2086 355 N ATOM 1740 CA ASN A1011 4.412 -49.795 14.265 1.00 69.67 C ANISOU 1740 CA ASN A1011 8589 5129 12753 1254 2536 674 C ATOM 1741 C ASN A1011 5.902 -49.967 14.541 1.00 70.69 C ANISOU 1741 C ASN A1011 8235 5327 13297 1192 2848 885 C ATOM 1742 O ASN A1011 6.500 -50.960 14.110 1.00 68.65 O ANISOU 1742 O ASN A1011 8056 5167 12861 1443 3121 1043 O ATOM 1743 CB ASN A1011 4.193 -48.870 13.069 1.00 75.27 C ANISOU 1743 CB ASN A1011 9678 5546 13377 1380 2802 901 C ATOM 1744 CG ASN A1011 2.762 -48.893 12.575 1.00 79.05 C ANISOU 1744 CG ASN A1011 10676 5952 13405 1520 2491 751 C ATOM 1745 OD1 ASN A1011 2.088 -49.919 12.654 1.00 78.29 O ANISOU 1745 OD1 ASN A1011 10787 6001 12960 1613 2214 603 O ATOM 1746 ND2 ASN A1011 2.288 -47.761 12.065 1.00 84.09 N ANISOU 1746 ND2 ASN A1011 11519 6350 14080 1521 2499 810 N ATOM 1747 N ASP A1012 6.517 -49.015 15.248 1.00 69.57 N ANISOU 1747 N ASP A1012 7603 5113 13718 878 2781 904 N ATOM 1748 CA ASP A1012 7.942 -49.121 15.552 1.00 72.29 C ANISOU 1748 CA ASP A1012 7386 5517 14566 770 3003 1146 C ATOM 1749 C ASP A1012 8.237 -50.370 16.370 1.00 72.72 C ANISOU 1749 C ASP A1012 7242 5855 14534 831 2803 971 C ATOM 1750 O ASP A1012 9.159 -51.132 16.055 1.00 72.56 O ANISOU 1750 O ASP A1012 7044 5953 14572 1033 3134 1212 O ATOM 1751 CB ASP A1012 8.422 -47.876 16.300 1.00 80.54 C ANISOU 1751 CB ASP A1012 7985 6378 16239 353 2775 1152 C ATOM 1752 CG ASP A1012 8.413 -46.632 15.436 1.00 85.01 C ANISOU 1752 CG ASP A1012 8697 6623 16980 273 3035 1420 C ATOM 1753 OD1 ASP A1012 8.576 -46.762 14.205 1.00 87.37 O ANISOU 1753 OD1 ASP A1012 9249 6869 17079 538 3562 1752 O ATOM 1754 OD2 ASP A1012 8.247 -45.525 15.991 1.00 86.23 O ANISOU 1754 OD2 ASP A1012 8778 6547 17437 -31 2707 1301 O ATOM 1755 N ASN A1013 7.461 -50.597 17.431 1.00 66.53 N ANISOU 1755 N ASN A1013 6504 5179 13596 694 2289 572 N ATOM 1756 CA ASN A1013 7.756 -51.713 18.321 1.00 73.21 C ANISOU 1756 CA ASN A1013 7176 6263 14377 715 2062 406 C ATOM 1757 C ASN A1013 7.428 -53.055 17.681 1.00 69.83 C ANISOU 1757 C ASN A1013 7169 5964 13397 1059 2209 427 C ATOM 1758 O ASN A1013 7.999 -54.078 18.073 1.00 63.45 O ANISOU 1758 O ASN A1013 6242 5318 12549 1170 2183 418 O ATOM 1759 CB ASN A1013 7.009 -51.538 19.641 1.00 69.07 C ANISOU 1759 CB ASN A1013 6635 5799 13808 497 1522 11 C ATOM 1760 CG ASN A1013 7.744 -50.634 20.609 1.00 72.08 C ANISOU 1760 CG ASN A1013 6588 6059 14738 189 1259 -44 C ATOM 1761 OD1 ASN A1013 8.932 -50.823 20.869 1.00 75.96 O ANISOU 1761 OD1 ASN A1013 6651 6573 15638 109 1283 118 O ATOM 1762 ND2 ASN A1013 7.044 -49.640 21.141 1.00 70.82 N ANISOU 1762 ND2 ASN A1013 6562 5748 14599 34 974 -262 N ATOM 1763 N LEU A1014 6.518 -53.076 16.703 1.00 66.21 N ANISOU 1763 N LEU A1014 7249 5403 12506 1237 2307 454 N ATOM 1764 CA LEU A1014 6.329 -54.280 15.899 1.00 67.35 C ANISOU 1764 CA LEU A1014 7897 5567 12125 1584 2436 525 C ATOM 1765 C LEU A1014 7.612 -54.655 15.168 1.00 73.08 C ANISOU 1765 C LEU A1014 8551 6280 12936 1895 2979 870 C ATOM 1766 O LEU A1014 7.984 -55.833 15.111 1.00 75.02 O ANISOU 1766 O LEU A1014 8965 6618 12920 2164 3037 890 O ATOM 1767 CB LEU A1014 5.188 -54.076 14.901 1.00 65.99 C ANISOU 1767 CB LEU A1014 8333 5218 11522 1707 2391 526 C ATOM 1768 CG LEU A1014 3.787 -54.512 15.326 1.00 65.05 C ANISOU 1768 CG LEU A1014 8467 5165 11085 1584 1867 253 C ATOM 1769 CD1 LEU A1014 2.753 -53.982 14.345 1.00 65.35 C ANISOU 1769 CD1 LEU A1014 8967 5003 10861 1665 1795 299 C ATOM 1770 CD2 LEU A1014 3.705 -56.029 15.421 1.00 63.24 C ANISOU 1770 CD2 LEU A1014 8533 5023 10474 1720 1683 191 C ATOM 1771 N LYS A1015 8.304 -53.661 14.604 1.00 76.36 N ANISOU 1771 N LYS A1015 8718 6576 13721 1884 3402 1175 N ATOM 1772 CA LYS A1015 9.569 -53.927 13.927 1.00 82.14 C ANISOU 1772 CA LYS A1015 9272 7330 14609 2197 4012 1585 C ATOM 1773 C LYS A1015 10.636 -54.383 14.913 1.00 81.93 C ANISOU 1773 C LYS A1015 8557 7524 15050 2106 3948 1611 C ATOM 1774 O LYS A1015 11.451 -55.256 14.592 1.00 82.29 O ANISOU 1774 O LYS A1015 8568 7680 15020 2484 4300 1825 O ATOM 1775 CB LYS A1015 10.034 -52.680 13.175 1.00 87.49 C ANISOU 1775 CB LYS A1015 9768 7826 15647 2134 4476 1956 C ATOM 1776 CG LYS A1015 9.110 -52.240 12.051 1.00 92.43 C ANISOU 1776 CG LYS A1015 11130 8205 15785 2306 4600 1989 C ATOM 1777 CD LYS A1015 9.546 -50.892 11.490 1.00101.89 C ANISOU 1777 CD LYS A1015 12114 9203 17397 2160 4995 2342 C ATOM 1778 CE LYS A1015 8.663 -50.438 10.336 1.00104.47 C ANISOU 1778 CE LYS A1015 13223 9258 17214 2369 5116 2391 C ATOM 1779 NZ LYS A1015 8.876 -51.258 9.111 1.00108.81 N ANISOU 1779 NZ LYS A1015 14436 9740 17166 2966 5625 2643 N ATOM 1780 N VAL A1016 10.647 -53.805 16.117 1.00 79.61 N ANISOU 1780 N VAL A1016 7755 7275 15218 1648 3482 1397 N ATOM 1781 CA VAL A1016 11.632 -54.186 17.126 1.00 80.17 C ANISOU 1781 CA VAL A1016 7193 7520 15747 1532 3304 1401 C ATOM 1782 C VAL A1016 11.493 -55.663 17.477 1.00 79.65 C ANISOU 1782 C VAL A1016 7417 7629 15219 1810 3127 1196 C ATOM 1783 O VAL A1016 12.491 -56.376 17.645 1.00 79.73 O ANISOU 1783 O VAL A1016 7102 7782 15409 2025 3281 1361 O ATOM 1784 CB VAL A1016 11.486 -53.296 18.374 1.00 74.55 C ANISOU 1784 CB VAL A1016 6096 6751 15477 1014 2728 1140 C ATOM 1785 CG1 VAL A1016 12.465 -53.723 19.453 1.00 76.32 C ANISOU 1785 CG1 VAL A1016 5741 7118 16140 895 2436 1118 C ATOM 1786 CG2 VAL A1016 11.684 -51.831 18.011 1.00 78.44 C ANISOU 1786 CG2 VAL A1016 6352 7011 16442 731 2867 1361 C ATOM 1787 N ILE A1017 10.254 -56.146 17.581 1.00 76.24 N ANISOU 1787 N ILE A1017 7585 7175 14208 1810 2792 865 N ATOM 1788 CA ILE A1017 10.021 -57.533 17.967 1.00 75.55 C ANISOU 1788 CA ILE A1017 7822 7205 13678 2002 2551 670 C ATOM 1789 C ILE A1017 10.496 -58.485 16.875 1.00 80.80 C ANISOU 1789 C ILE A1017 8898 7842 13962 2549 3008 918 C ATOM 1790 O ILE A1017 11.074 -59.540 17.164 1.00 84.73 O ANISOU 1790 O ILE A1017 9396 8446 14353 2802 2997 922 O ATOM 1791 CB ILE A1017 8.533 -57.742 18.302 1.00 67.14 C ANISOU 1791 CB ILE A1017 7243 6111 12157 1817 2088 331 C ATOM 1792 CG1 ILE A1017 8.179 -57.024 19.607 1.00 62.07 C ANISOU 1792 CG1 ILE A1017 6220 5535 11830 1387 1654 70 C ATOM 1793 CG2 ILE A1017 8.201 -59.228 18.392 1.00 65.19 C ANISOU 1793 CG2 ILE A1017 7473 5911 11387 2027 1883 209 C ATOM 1794 CD1 ILE A1017 6.694 -56.878 19.840 1.00 58.77 C ANISOU 1794 CD1 ILE A1017 6150 5103 11077 1215 1330 -171 C ATOM 1795 N GLU A1018 10.279 -58.124 15.607 1.00 81.62 N ANISOU 1795 N GLU A1018 9416 7777 13820 2786 3418 1130 N ATOM 1796 CA GLU A1018 10.624 -59.024 14.511 1.00 85.52 C ANISOU 1796 CA GLU A1018 10486 8188 13820 3383 3851 1346 C ATOM 1797 C GLU A1018 12.126 -59.267 14.435 1.00 91.88 C ANISOU 1797 C GLU A1018 10768 9154 14988 3704 4368 1698 C ATOM 1798 O GLU A1018 12.567 -60.394 14.180 1.00 96.00 O ANISOU 1798 O GLU A1018 11634 9763 15079 4072 4440 1740 O ATOM 1799 CB GLU A1018 10.110 -58.465 13.186 1.00 86.36 C ANISOU 1799 CB GLU A1018 11178 8052 13581 3578 4179 1514 C ATOM 1800 CG GLU A1018 8.604 -58.490 13.049 1.00 86.63 C ANISOU 1800 CG GLU A1018 11846 7920 13150 3378 3649 1209 C ATOM 1801 CD GLU A1018 8.125 -57.736 11.828 1.00 94.54 C ANISOU 1801 CD GLU A1018 13346 8670 13903 3520 3908 1375 C ATOM 1802 OE1 GLU A1018 8.812 -57.788 10.785 1.00100.16 O ANISOU 1802 OE1 GLU A1018 14341 9339 14375 3910 4449 1689 O ATOM 1803 OE2 GLU A1018 7.068 -57.080 11.915 1.00 93.30 O ANISOU 1803 OE2 GLU A1018 13282 8431 13738 3192 3529 1195 O ATOM 1804 N LYS A1019 12.928 -58.225 14.645 1.00 91.22 N ANISOU 1804 N LYS A1019 9872 9152 15636 3461 4621 1959 N ATOM 1805 CA LYS A1019 14.378 -58.344 14.585 1.00 96.51 C ANISOU 1805 CA LYS A1019 9967 10033 16668 3588 4989 2345 C ATOM 1806 C LYS A1019 15.013 -58.522 15.957 1.00 91.21 C ANISOU 1806 C LYS A1019 8538 9553 16564 3301 4551 2217 C ATOM 1807 O LYS A1019 16.239 -58.431 16.077 1.00 93.53 O ANISOU 1807 O LYS A1019 8217 10007 17313 3289 4733 2539 O ATOM 1808 CB LYS A1019 14.979 -57.127 13.877 1.00105.42 C ANISOU 1808 CB LYS A1019 10693 11100 18261 3470 5510 2803 C ATOM 1809 CG LYS A1019 14.516 -55.790 14.418 1.00105.96 C ANISOU 1809 CG LYS A1019 10302 11022 18935 2924 5259 2700 C ATOM 1810 CD LYS A1019 14.970 -54.658 13.515 1.00114.59 C ANISOU 1810 CD LYS A1019 11196 11983 20361 2857 5811 3174 C ATOM 1811 CE LYS A1019 14.588 -54.925 12.067 1.00118.96 C ANISOU 1811 CE LYS A1019 12627 12401 20172 3377 6363 3358 C ATOM 1812 NZ LYS A1019 15.028 -53.827 11.163 1.00125.66 N ANISOU 1812 NZ LYS A1019 13331 13096 21318 3347 6946 3856 N ATOM 1813 N ALA A1020 14.215 -58.769 16.991 1.00 84.80 N ANISOU 1813 N ALA A1020 7783 8706 15732 3073 3955 1775 N ATOM 1814 CA ALA A1020 14.770 -59.130 18.283 1.00 87.18 C ANISOU 1814 CA ALA A1020 7536 9163 16427 2880 3494 1623 C ATOM 1815 C ALA A1020 15.433 -60.503 18.204 1.00 89.72 C ANISOU 1815 C ALA A1020 8071 9645 16373 3344 3586 1684 C ATOM 1816 O ALA A1020 15.174 -61.297 17.295 1.00 87.96 O ANISOU 1816 O ALA A1020 8570 9374 15478 3784 3866 1719 O ATOM 1817 CB ALA A1020 13.682 -59.128 19.357 1.00 76.64 C ANISOU 1817 CB ALA A1020 6471 7785 14864 2452 2763 1115 C ATOM 1818 N ASP A1021 16.311 -60.779 19.169 1.00 96.72 N ANISOU 1818 N ASP A1021 8369 10698 17681 3246 3294 1687 N ATOM 1819 CA ASP A1021 16.976 -62.073 19.226 1.00107.48 C ANISOU 1819 CA ASP A1021 9884 12209 18745 3695 3329 1722 C ATOM 1820 C ASP A1021 16.829 -62.789 20.561 1.00105.84 C ANISOU 1820 C ASP A1021 9609 12028 18579 3610 2694 1376 C ATOM 1821 O ASP A1021 17.283 -63.932 20.673 1.00109.28 O ANISOU 1821 O ASP A1021 10245 12550 18726 4005 2667 1364 O ATOM 1822 CB ASP A1021 18.472 -61.934 18.893 1.00120.82 C ANISOU 1822 CB ASP A1021 10949 14095 20861 3830 3708 2177 C ATOM 1823 CG ASP A1021 19.281 -61.354 20.038 1.00127.06 C ANISOU 1823 CG ASP A1021 10847 14981 22449 3390 3267 2216 C ATOM 1824 OD1 ASP A1021 18.794 -60.414 20.701 1.00125.28 O ANISOU 1824 OD1 ASP A1021 10383 14624 22592 2866 2865 2039 O ATOM 1825 OD2 ASP A1021 20.408 -61.845 20.272 1.00133.26 O ANISOU 1825 OD2 ASP A1021 11213 15947 23473 3576 3286 2417 O ATOM 1826 N ASN A1022 16.214 -62.168 21.566 1.00101.24 N ANISOU 1826 N ASN A1022 8811 11354 18302 3125 2171 1089 N ATOM 1827 CA ASN A1022 15.955 -62.821 22.841 1.00 97.76 C ANISOU 1827 CA ASN A1022 8516 10937 17690 2952 1503 722 C ATOM 1828 C ASN A1022 14.578 -62.405 23.339 1.00 92.81 C ANISOU 1828 C ASN A1022 8363 10199 16704 2499 1094 337 C ATOM 1829 O ASN A1022 13.956 -61.476 22.816 1.00 91.34 O ANISOU 1829 O ASN A1022 8249 9923 16533 2280 1259 352 O ATOM 1830 CB ASN A1022 17.033 -62.488 23.882 1.00 98.56 C ANISOU 1830 CB ASN A1022 7785 11129 18533 2752 1132 789 C ATOM 1831 CG ASN A1022 17.128 -61.005 24.169 1.00 97.97 C ANISOU 1831 CG ASN A1022 7162 10970 19091 2221 968 838 C ATOM 1832 OD1 ASN A1022 16.331 -60.456 24.929 1.00 92.76 O ANISOU 1832 OD1 ASN A1022 6733 10198 18315 1802 497 499 O ATOM 1833 ND2 ASN A1022 18.108 -60.346 23.562 1.00103.09 N ANISOU 1833 ND2 ASN A1022 7317 11686 20166 2160 1322 1251 N ATOM 1834 N ALA A1023 14.104 -63.109 24.370 1.00 89.32 N ANISOU 1834 N ALA A1023 8240 9766 15933 2386 577 17 N ATOM 1835 CA ALA A1023 12.761 -62.870 24.887 1.00 83.40 C ANISOU 1835 CA ALA A1023 7937 8949 14803 2025 245 -303 C ATOM 1836 C ALA A1023 12.644 -61.547 25.632 1.00 83.33 C ANISOU 1836 C ALA A1023 7535 8899 15226 1580 -26 -425 C ATOM 1837 O ALA A1023 11.539 -61.004 25.728 1.00 83.28 O ANISOU 1837 O ALA A1023 7818 8838 14988 1337 -113 -601 O ATOM 1838 CB ALA A1023 12.338 -64.018 25.803 1.00 80.25 C ANISOU 1838 CB ALA A1023 7980 8571 13939 2044 -176 -548 C ATOM 1839 N ALA A1024 13.749 -61.017 26.160 1.00 84.32 N ANISOU 1839 N ALA A1024 7027 9029 15981 1479 -194 -325 N ATOM 1840 CA ALA A1024 13.684 -59.772 26.916 1.00 82.30 C ANISOU 1840 CA ALA A1024 6500 8657 16113 1060 -551 -460 C ATOM 1841 C ALA A1024 13.462 -58.562 26.017 1.00 82.81 C ANISOU 1841 C ALA A1024 6412 8615 16439 901 -203 -291 C ATOM 1842 O ALA A1024 12.794 -57.606 26.428 1.00 81.37 O ANISOU 1842 O ALA A1024 6350 8302 16264 604 -427 -483 O ATOM 1843 CB ALA A1024 14.957 -59.587 27.742 1.00 85.59 C ANISOU 1843 CB ALA A1024 6309 9053 17160 964 -948 -385 C ATOM 1844 N GLN A1025 14.013 -58.577 24.801 1.00 83.59 N ANISOU 1844 N GLN A1025 6289 8749 16722 1133 360 76 N ATOM 1845 CA GLN A1025 13.740 -57.498 23.857 1.00 80.31 C ANISOU 1845 CA GLN A1025 5827 8216 16472 1016 734 259 C ATOM 1846 C GLN A1025 12.288 -57.529 23.399 1.00 75.53 C ANISOU 1846 C GLN A1025 5916 7568 15214 1039 828 51 C ATOM 1847 O GLN A1025 11.653 -56.479 23.249 1.00 73.26 O ANISOU 1847 O GLN A1025 5709 7147 14978 807 815 -11 O ATOM 1848 CB GLN A1025 14.680 -57.596 22.658 1.00 82.08 C ANISOU 1848 CB GLN A1025 5708 8496 16981 1325 1380 740 C ATOM 1849 CG GLN A1025 16.140 -57.378 22.996 1.00 88.83 C ANISOU 1849 CG GLN A1025 5708 9405 18638 1267 1339 1056 C ATOM 1850 CD GLN A1025 17.052 -57.698 21.832 1.00 96.47 C ANISOU 1850 CD GLN A1025 6525 10504 19625 1630 2027 1546 C ATOM 1851 OE1 GLN A1025 16.593 -58.064 20.751 1.00 95.25 O ANISOU 1851 OE1 GLN A1025 6840 10356 18995 1995 2560 1645 O ATOM 1852 NE2 GLN A1025 18.355 -57.565 22.047 1.00104.03 N ANISOU 1852 NE2 GLN A1025 6904 11550 21073 1543 1989 1854 N ATOM 1853 N VAL A1026 11.750 -58.728 23.163 1.00 76.32 N ANISOU 1853 N VAL A1026 6522 7758 14718 1315 887 -41 N ATOM 1854 CA VAL A1026 10.336 -58.851 22.825 1.00 71.83 C ANISOU 1854 CA VAL A1026 6564 7148 13579 1290 865 -219 C ATOM 1855 C VAL A1026 9.475 -58.348 23.974 1.00 72.08 C ANISOU 1855 C VAL A1026 6660 7176 13551 955 405 -543 C ATOM 1856 O VAL A1026 8.516 -57.594 23.767 1.00 71.65 O ANISOU 1856 O VAL A1026 6786 7052 13384 814 412 -624 O ATOM 1857 CB VAL A1026 9.999 -60.308 22.459 1.00 69.04 C ANISOU 1857 CB VAL A1026 6743 6844 12645 1600 902 -238 C ATOM 1858 CG1 VAL A1026 8.530 -60.441 22.112 1.00 64.35 C ANISOU 1858 CG1 VAL A1026 6715 6192 11545 1515 798 -376 C ATOM 1859 CG2 VAL A1026 10.869 -60.783 21.302 1.00 71.33 C ANISOU 1859 CG2 VAL A1026 7065 7113 12923 2037 1403 82 C ATOM 1860 N LYS A1027 9.814 -58.743 25.205 1.00 74.91 N ANISOU 1860 N LYS A1027 6898 7600 13965 870 13 -721 N ATOM 1861 CA LYS A1027 9.048 -58.298 26.365 1.00 75.43 C ANISOU 1861 CA LYS A1027 7095 7655 13911 629 -382 -1017 C ATOM 1862 C LYS A1027 9.049 -56.779 26.475 1.00 76.40 C ANISOU 1862 C LYS A1027 6995 7617 14418 402 -439 -1048 C ATOM 1863 O LYS A1027 7.999 -56.162 26.683 1.00 74.06 O ANISOU 1863 O LYS A1027 6943 7283 13915 306 -499 -1207 O ATOM 1864 CB LYS A1027 9.603 -58.922 27.645 1.00 77.16 C ANISOU 1864 CB LYS A1027 7256 7925 14136 614 -796 -1177 C ATOM 1865 CG LYS A1027 8.914 -58.402 28.898 1.00 78.52 C ANISOU 1865 CG LYS A1027 7623 8058 14152 429 -1174 -1470 C ATOM 1866 CD LYS A1027 9.588 -58.885 30.167 1.00 82.89 C ANISOU 1866 CD LYS A1027 8160 8606 14728 426 -1623 -1623 C ATOM 1867 CE LYS A1027 8.805 -58.435 31.388 1.00 84.29 C ANISOU 1867 CE LYS A1027 8677 8732 14616 326 -1935 -1908 C ATOM 1868 NZ LYS A1027 9.397 -58.944 32.653 1.00 88.58 N ANISOU 1868 NZ LYS A1027 9329 9239 15089 353 -2402 -2070 N ATOM 1869 N ASP A1028 10.224 -56.160 26.337 1.00 82.16 N ANISOU 1869 N ASP A1028 7249 8236 15730 318 -430 -871 N ATOM 1870 CA ASP A1028 10.317 -54.707 26.437 1.00 82.98 C ANISOU 1870 CA ASP A1028 7170 8119 16239 63 -546 -877 C ATOM 1871 C ASP A1028 9.419 -54.025 25.412 1.00 75.38 C ANISOU 1871 C ASP A1028 6440 7089 15113 82 -187 -802 C ATOM 1872 O ASP A1028 8.617 -53.149 25.757 1.00 77.94 O ANISOU 1872 O ASP A1028 6982 7293 15340 -35 -344 -990 O ATOM 1873 CB ASP A1028 11.769 -54.260 26.259 1.00 95.23 C ANISOU 1873 CB ASP A1028 8106 9565 18513 -61 -553 -589 C ATOM 1874 CG ASP A1028 12.441 -53.921 27.574 1.00104.40 C ANISOU 1874 CG ASP A1028 9054 10585 20027 -293 -1194 -755 C ATOM 1875 OD1 ASP A1028 11.786 -53.291 28.431 1.00105.54 O ANISOU 1875 OD1 ASP A1028 9545 10573 19983 -432 -1582 -1069 O ATOM 1876 OD2 ASP A1028 13.625 -54.282 27.749 1.00109.82 O ANISOU 1876 OD2 ASP A1028 9251 11306 21170 -304 -1323 -563 O ATOM 1877 N ALA A1029 9.537 -54.419 24.142 1.00 69.30 N ANISOU 1877 N ALA A1029 5677 6379 14275 278 292 -528 N ATOM 1878 CA ALA A1029 8.758 -53.773 23.091 1.00 66.80 C ANISOU 1878 CA ALA A1029 5611 5964 13804 317 607 -432 C ATOM 1879 C ALA A1029 7.266 -54.049 23.234 1.00 61.96 C ANISOU 1879 C ALA A1029 5479 5431 12630 373 490 -673 C ATOM 1880 O ALA A1029 6.444 -53.233 22.802 1.00 63.15 O ANISOU 1880 O ALA A1029 5814 5479 12701 342 558 -694 O ATOM 1881 CB ALA A1029 9.255 -54.227 21.719 1.00 65.64 C ANISOU 1881 CB ALA A1029 5468 5840 13633 576 1137 -82 C ATOM 1882 N LEU A1030 6.894 -55.183 23.832 1.00 57.58 N ANISOU 1882 N LEU A1030 5107 5056 11714 452 310 -822 N ATOM 1883 CA LEU A1030 5.481 -55.501 24.004 1.00 54.53 C ANISOU 1883 CA LEU A1030 5086 4768 10866 468 201 -977 C ATOM 1884 C LEU A1030 4.840 -54.664 25.104 1.00 55.42 C ANISOU 1884 C LEU A1030 5200 4866 10991 330 -65 -1220 C ATOM 1885 O LEU A1030 3.690 -54.232 24.967 1.00 51.22 O ANISOU 1885 O LEU A1030 4847 4351 10263 347 -40 -1270 O ATOM 1886 CB LEU A1030 5.310 -56.988 24.307 1.00 55.03 C ANISOU 1886 CB LEU A1030 5350 4997 10562 562 91 -1011 C ATOM 1887 CG LEU A1030 5.355 -57.976 23.145 1.00 53.92 C ANISOU 1887 CG LEU A1030 5479 4847 10161 770 307 -818 C ATOM 1888 CD1 LEU A1030 5.490 -59.378 23.702 1.00 54.39 C ANISOU 1888 CD1 LEU A1030 5708 5014 9943 838 119 -873 C ATOM 1889 CD2 LEU A1030 4.107 -57.850 22.280 1.00 49.76 C ANISOU 1889 CD2 LEU A1030 5286 4271 9348 783 357 -767 C ATOM 1890 N THR A1031 5.560 -54.432 26.205 1.00 61.14 N ANISOU 1890 N THR A1031 5758 5543 11927 230 -338 -1364 N ATOM 1891 CA THR A1031 5.010 -53.602 27.272 1.00 65.42 C ANISOU 1891 CA THR A1031 6423 6017 12416 170 -594 -1609 C ATOM 1892 C THR A1031 4.796 -52.171 26.797 1.00 63.47 C ANISOU 1892 C THR A1031 6172 5543 12399 117 -522 -1592 C ATOM 1893 O THR A1031 3.802 -51.531 27.158 1.00 60.24 O ANISOU 1893 O THR A1031 5983 5115 11790 186 -561 -1736 O ATOM 1894 CB THR A1031 5.926 -53.622 28.496 1.00 71.11 C ANISOU 1894 CB THR A1031 7057 6657 13303 85 -980 -1769 C ATOM 1895 OG1 THR A1031 7.175 -53.000 28.170 1.00 78.74 O ANISOU 1895 OG1 THR A1031 7677 7414 14828 -63 -1048 -1635 O ATOM 1896 CG2 THR A1031 6.171 -55.051 28.958 1.00 67.26 C ANISOU 1896 CG2 THR A1031 6607 6373 12576 160 -1061 -1778 C ATOM 1897 N LYS A1032 5.718 -51.655 25.980 1.00 67.35 N ANISOU 1897 N LYS A1032 6419 5858 13314 18 -389 -1388 N ATOM 1898 CA LYS A1032 5.542 -50.322 25.411 1.00 71.33 C ANISOU 1898 CA LYS A1032 6953 6110 14037 -48 -303 -1328 C ATOM 1899 C LYS A1032 4.342 -50.277 24.473 1.00 68.85 C ANISOU 1899 C LYS A1032 6883 5876 13401 116 -19 -1261 C ATOM 1900 O LYS A1032 3.605 -49.284 24.443 1.00 70.36 O ANISOU 1900 O LYS A1032 7250 5932 13552 151 -45 -1343 O ATOM 1901 CB LYS A1032 6.813 -49.893 24.679 1.00 76.76 C ANISOU 1901 CB LYS A1032 7289 6612 15264 -205 -161 -1040 C ATOM 1902 CG LYS A1032 7.997 -49.614 25.591 1.00 80.96 C ANISOU 1902 CG LYS A1032 7514 6987 16261 -433 -545 -1071 C ATOM 1903 CD LYS A1032 9.231 -49.269 24.775 1.00 86.00 C ANISOU 1903 CD LYS A1032 7686 7490 17499 -594 -334 -683 C ATOM 1904 CE LYS A1032 10.413 -48.923 25.663 1.00 91.84 C ANISOU 1904 CE LYS A1032 8044 8045 18806 -878 -803 -667 C ATOM 1905 NZ LYS A1032 11.615 -48.556 24.863 1.00 97.41 N ANISOU 1905 NZ LYS A1032 8183 8642 20187 -1061 -562 -205 N ATOM 1906 N MET A1033 4.131 -51.342 23.693 1.00 64.37 N ANISOU 1906 N MET A1033 6364 5498 12596 236 208 -1110 N ATOM 1907 CA MET A1033 2.943 -51.416 22.848 1.00 60.92 C ANISOU 1907 CA MET A1033 6182 5121 11844 374 361 -1047 C ATOM 1908 C MET A1033 1.670 -51.474 23.675 1.00 55.67 C ANISOU 1908 C MET A1033 5647 4622 10883 432 179 -1242 C ATOM 1909 O MET A1033 0.640 -50.926 23.266 1.00 54.97 O ANISOU 1909 O MET A1033 5685 4519 10681 525 223 -1227 O ATOM 1910 CB MET A1033 3.012 -52.636 21.933 1.00 64.87 C ANISOU 1910 CB MET A1033 6802 5732 12113 490 538 -864 C ATOM 1911 CG MET A1033 3.957 -52.485 20.774 1.00 67.74 C ANISOU 1911 CG MET A1033 7137 5937 12665 557 864 -599 C ATOM 1912 SD MET A1033 4.075 -53.992 19.796 1.00 66.91 S ANISOU 1912 SD MET A1033 7326 5915 12180 794 1049 -422 S ATOM 1913 CE MET A1033 2.472 -53.995 19.009 1.00 65.09 C ANISOU 1913 CE MET A1033 7542 5647 11543 873 940 -429 C ATOM 1914 N ARG A1034 1.718 -52.138 24.831 1.00 54.38 N ANISOU 1914 N ARG A1034 5447 4622 10593 405 -5 -1394 N ATOM 1915 CA ARG A1034 0.519 -52.284 25.646 1.00 54.64 C ANISOU 1915 CA ARG A1034 5580 4848 10331 489 -93 -1514 C ATOM 1916 C ARG A1034 0.102 -50.953 26.255 1.00 61.27 C ANISOU 1916 C ARG A1034 6499 5555 11226 580 -153 -1680 C ATOM 1917 O ARG A1034 -1.095 -50.662 26.363 1.00 61.64 O ANISOU 1917 O ARG A1034 6612 5720 11089 735 -88 -1686 O ATOM 1918 CB ARG A1034 0.750 -53.326 26.738 1.00 54.79 C ANISOU 1918 CB ARG A1034 5601 5046 10169 456 -243 -1610 C ATOM 1919 CG ARG A1034 -0.530 -53.843 27.358 1.00 57.47 C ANISOU 1919 CG ARG A1034 6014 5643 10177 532 -236 -1609 C ATOM 1920 CD ARG A1034 -0.250 -54.805 28.494 1.00 59.27 C ANISOU 1920 CD ARG A1034 6302 6011 10206 502 -371 -1692 C ATOM 1921 NE ARG A1034 -1.449 -55.556 28.850 1.00 63.79 N ANISOU 1921 NE ARG A1034 6899 6849 10490 523 -307 -1576 N ATOM 1922 CZ ARG A1034 -2.414 -55.093 29.636 1.00 68.84 C ANISOU 1922 CZ ARG A1034 7555 7627 10972 669 -209 -1603 C ATOM 1923 NH1 ARG A1034 -2.324 -53.877 30.156 1.00 72.98 N ANISOU 1923 NH1 ARG A1034 8175 8015 11541 841 -201 -1794 N ATOM 1924 NH2 ARG A1034 -3.472 -55.847 29.902 1.00 69.23 N ANISOU 1924 NH2 ARG A1034 7538 7939 10825 656 -118 -1413 N ATOM 1925 N ALA A1035 1.074 -50.131 26.659 1.00 62.95 N ANISOU 1925 N ALA A1035 6710 5503 11705 496 -300 -1797 N ATOM 1926 CA ALA A1035 0.747 -48.815 27.198 1.00 62.31 C ANISOU 1926 CA ALA A1035 6818 5204 11652 598 -412 -1971 C ATOM 1927 C ALA A1035 0.291 -47.869 26.095 1.00 63.75 C ANISOU 1927 C ALA A1035 7045 5220 11958 653 -248 -1849 C ATOM 1928 O ALA A1035 -0.645 -47.086 26.290 1.00 66.53 O ANISOU 1928 O ALA A1035 7577 5535 12168 865 -230 -1937 O ATOM 1929 CB ALA A1035 1.949 -48.237 27.944 1.00 62.75 C ANISOU 1929 CB ALA A1035 6907 4956 11981 441 -731 -2120 C ATOM 1930 N ALA A1036 0.943 -47.924 24.930 1.00 64.37 N ANISOU 1930 N ALA A1036 6991 5190 12278 509 -104 -1632 N ATOM 1931 CA ALA A1036 0.485 -47.136 23.791 1.00 62.65 C ANISOU 1931 CA ALA A1036 6871 4810 12122 577 66 -1488 C ATOM 1932 C ALA A1036 -0.925 -47.540 23.381 1.00 63.25 C ANISOU 1932 C ALA A1036 7017 5134 11879 786 170 -1433 C ATOM 1933 O ALA A1036 -1.735 -46.690 22.990 1.00 65.18 O ANISOU 1933 O ALA A1036 7395 5283 12089 947 203 -1423 O ATOM 1934 CB ALA A1036 1.450 -47.294 22.617 1.00 57.79 C ANISOU 1934 CB ALA A1036 6140 4065 11753 431 268 -1223 C ATOM 1935 N ALA A1037 -1.241 -48.835 23.479 1.00 58.50 N ANISOU 1935 N ALA A1037 6321 4838 11070 776 182 -1378 N ATOM 1936 CA ALA A1037 -2.568 -49.308 23.102 1.00 56.28 C ANISOU 1936 CA ALA A1037 6044 4783 10557 905 206 -1273 C ATOM 1937 C ALA A1037 -3.631 -48.814 24.074 1.00 59.17 C ANISOU 1937 C ALA A1037 6384 5301 10798 1105 174 -1395 C ATOM 1938 O ALA A1037 -4.710 -48.382 23.654 1.00 62.35 O ANISOU 1938 O ALA A1037 6775 5757 11157 1279 208 -1308 O ATOM 1939 CB ALA A1037 -2.583 -50.835 23.024 1.00 50.89 C ANISOU 1939 CB ALA A1037 5301 4330 9703 799 170 -1168 C ATOM 1940 N LEU A1038 -3.346 -48.870 25.378 1.00 64.01 N ANISOU 1940 N LEU A1038 7005 5981 11336 1126 114 -1581 N ATOM 1941 CA LEU A1038 -4.315 -48.398 26.363 1.00 69.80 C ANISOU 1941 CA LEU A1038 7779 6855 11887 1402 157 -1683 C ATOM 1942 C LEU A1038 -4.453 -46.882 26.322 1.00 76.10 C ANISOU 1942 C LEU A1038 8791 7360 12764 1616 150 -1809 C ATOM 1943 O LEU A1038 -5.555 -46.349 26.500 1.00 78.13 O ANISOU 1943 O LEU A1038 9061 7723 12901 1931 256 -1793 O ATOM 1944 CB LEU A1038 -3.915 -48.865 27.761 1.00 72.60 C ANISOU 1944 CB LEU A1038 8210 7307 12066 1409 89 -1854 C ATOM 1945 CG LEU A1038 -3.961 -50.374 28.003 1.00 74.69 C ANISOU 1945 CG LEU A1038 8313 7874 12193 1245 97 -1729 C ATOM 1946 CD1 LEU A1038 -3.574 -50.695 29.438 1.00 77.48 C ANISOU 1946 CD1 LEU A1038 8823 8280 12336 1300 22 -1909 C ATOM 1947 CD2 LEU A1038 -5.339 -50.930 27.676 1.00 75.61 C ANISOU 1947 CD2 LEU A1038 8207 8313 12209 1316 238 -1475 C ATOM 1948 N ASP A1039 -3.346 -46.171 26.093 1.00 78.16 N ANISOU 1948 N ASP A1039 9209 7241 13247 1457 22 -1908 N ATOM 1949 CA ASP A1039 -3.418 -44.719 25.966 1.00 82.71 C ANISOU 1949 CA ASP A1039 10048 7462 13915 1614 -33 -2009 C ATOM 1950 C ASP A1039 -4.232 -44.320 24.742 1.00 78.88 C ANISOU 1950 C ASP A1039 9526 6969 13474 1735 102 -1818 C ATOM 1951 O ASP A1039 -5.013 -43.361 24.790 1.00 81.80 O ANISOU 1951 O ASP A1039 10067 7240 13774 2045 123 -1872 O ATOM 1952 CB ASP A1039 -2.009 -44.129 25.894 1.00 91.60 C ANISOU 1952 CB ASP A1039 11288 8166 15349 1324 -230 -2077 C ATOM 1953 CG ASP A1039 -1.987 -42.641 26.177 1.00105.06 C ANISOU 1953 CG ASP A1039 13369 9434 17114 1460 -400 -2241 C ATOM 1954 OD1 ASP A1039 -2.168 -42.259 27.352 1.00110.38 O ANISOU 1954 OD1 ASP A1039 14333 10029 17580 1675 -562 -2487 O ATOM 1955 OD2 ASP A1039 -1.790 -41.853 25.227 1.00109.44 O ANISOU 1955 OD2 ASP A1039 13996 9696 17891 1374 -379 -2121 O ATOM 1956 N ALA A1040 -4.072 -45.052 23.637 1.00 73.64 N ANISOU 1956 N ALA A1040 8695 6390 12897 1537 175 -1596 N ATOM 1957 CA ALA A1040 -4.864 -44.776 22.443 1.00 74.05 C ANISOU 1957 CA ALA A1040 8769 6417 12949 1657 240 -1409 C ATOM 1958 C ALA A1040 -6.321 -45.176 22.633 1.00 76.05 C ANISOU 1958 C ALA A1040 8833 7034 13029 1904 263 -1325 C ATOM 1959 O ALA A1040 -7.209 -44.596 21.997 1.00 76.22 O ANISOU 1959 O ALA A1040 8880 7024 13057 2121 259 -1225 O ATOM 1960 CB ALA A1040 -4.266 -45.496 21.235 1.00 69.94 C ANISOU 1960 CB ALA A1040 8232 5847 12495 1425 294 -1200 C ATOM 1961 N GLN A1041 -6.587 -46.159 23.497 1.00 77.23 N ANISOU 1961 N GLN A1041 8768 7527 13050 1871 282 -1330 N ATOM 1962 CA GLN A1041 -7.967 -46.546 23.773 1.00 81.47 C ANISOU 1962 CA GLN A1041 9036 8434 13486 2077 335 -1183 C ATOM 1963 C GLN A1041 -8.722 -45.416 24.461 1.00 84.00 C ANISOU 1963 C GLN A1041 9420 8756 13741 2512 448 -1285 C ATOM 1964 O GLN A1041 -9.892 -45.161 24.152 1.00 86.13 O ANISOU 1964 O GLN A1041 9494 9194 14037 2771 495 -1116 O ATOM 1965 CB GLN A1041 -7.993 -47.817 24.624 1.00 83.30 C ANISOU 1965 CB GLN A1041 9056 8999 13593 1925 362 -1139 C ATOM 1966 CG GLN A1041 -9.369 -48.449 24.777 1.00 87.64 C ANISOU 1966 CG GLN A1041 9234 9951 14115 2023 412 -877 C ATOM 1967 CD GLN A1041 -9.299 -49.856 25.343 1.00 89.85 C ANISOU 1967 CD GLN A1041 9345 10496 14298 1767 394 -771 C ATOM 1968 OE1 GLN A1041 -8.234 -50.323 25.746 1.00 89.91 O ANISOU 1968 OE1 GLN A1041 9536 10404 14222 1581 358 -933 O ATOM 1969 NE2 GLN A1041 -10.436 -50.542 25.368 1.00 92.10 N ANISOU 1969 NE2 GLN A1041 9262 11107 14623 1744 395 -471 N ATOM 1970 N LYS A1042 -8.067 -44.723 25.388 1.00 84.08 N ANISOU 1970 N LYS A1042 9727 8555 13665 2624 463 -1554 N ATOM 1971 CA LYS A1042 -8.678 -43.594 26.079 1.00 88.14 C ANISOU 1971 CA LYS A1042 10455 8988 14045 3102 558 -1693 C ATOM 1972 C LYS A1042 -8.823 -42.400 25.141 1.00 86.67 C ANISOU 1972 C LYS A1042 10487 8452 13992 3250 482 -1695 C ATOM 1973 O LYS A1042 -9.878 -41.766 25.084 1.00 87.03 O ANISOU 1973 O LYS A1042 10502 8577 13988 3676 581 -1629 O ATOM 1974 CB LYS A1042 -7.852 -43.200 27.306 1.00 92.74 C ANISOU 1974 CB LYS A1042 11433 9345 14460 3163 491 -2004 C ATOM 1975 CG LYS A1042 -7.695 -44.301 28.342 1.00 95.89 C ANISOU 1975 CG LYS A1042 11712 10051 14670 3073 557 -2022 C ATOM 1976 CD LYS A1042 -6.938 -43.801 29.563 1.00101.56 C ANISOU 1976 CD LYS A1042 12919 10486 15182 3191 416 -2348 C ATOM 1977 CE LYS A1042 -6.662 -44.927 30.546 1.00102.92 C ANISOU 1977 CE LYS A1042 13033 10921 15153 3080 444 -2368 C ATOM 1978 NZ LYS A1042 -5.895 -44.451 31.731 1.00106.58 N ANISOU 1978 NZ LYS A1042 14044 11061 15392 3199 220 -2697 N ATOM 1979 N LYS A1059 -18.247 -50.248 20.098 1.00113.36 N ANISOU 1979 N LYS A1059 9618 14420 19035 1938 -1294 1699 N ATOM 1980 CA LYS A1059 -18.358 -51.702 20.060 1.00114.37 C ANISOU 1980 CA LYS A1059 9601 14616 19239 1404 -1628 1946 C ATOM 1981 C LYS A1059 -17.299 -52.297 19.141 1.00111.65 C ANISOU 1981 C LYS A1059 10016 13804 18602 1085 -1980 1703 C ATOM 1982 O LYS A1059 -16.432 -53.046 19.591 1.00108.09 O ANISOU 1982 O LYS A1059 9836 13314 17921 856 -1853 1546 O ATOM 1983 CB LYS A1059 -19.758 -52.119 19.612 1.00119.25 C ANISOU 1983 CB LYS A1059 9564 15427 20319 1243 -2095 2471 C ATOM 1984 CG LYS A1059 -20.848 -51.671 20.569 1.00123.23 C ANISOU 1984 CG LYS A1059 9206 16463 21154 1575 -1674 2808 C ATOM 1985 CD LYS A1059 -22.233 -51.933 20.010 1.00128.70 C ANISOU 1985 CD LYS A1059 9415 17298 22185 1389 -2100 3250 C ATOM 1986 CE LYS A1059 -23.300 -51.347 20.917 1.00132.68 C ANISOU 1986 CE LYS A1059 9331 18293 22790 1763 -1545 3459 C ATOM 1987 NZ LYS A1059 -24.664 -51.538 20.361 1.00139.77 N ANISOU 1987 NZ LYS A1059 9745 19312 24050 1593 -1940 3881 N ATOM 1988 N ASP A1060 -17.371 -51.965 17.849 1.00115.14 N ANISOU 1988 N ASP A1060 10828 13888 19030 1118 -2408 1686 N ATOM 1989 CA ASP A1060 -16.288 -52.320 16.940 1.00116.07 C ANISOU 1989 CA ASP A1060 11757 13544 18800 964 -2609 1440 C ATOM 1990 C ASP A1060 -14.984 -51.646 17.340 1.00114.07 C ANISOU 1990 C ASP A1060 11906 13169 18266 1169 -2060 1035 C ATOM 1991 O ASP A1060 -13.904 -52.148 17.008 1.00111.32 O ANISOU 1991 O ASP A1060 12085 12564 17647 1021 -2045 854 O ATOM 1992 CB ASP A1060 -16.658 -51.943 15.505 1.00121.13 C ANISOU 1992 CB ASP A1060 12777 13815 19433 1051 -3116 1509 C ATOM 1993 CG ASP A1060 -18.102 -52.266 15.172 1.00130.33 C ANISOU 1993 CG ASP A1060 13414 15117 20988 920 -3697 1933 C ATOM 1994 OD1 ASP A1060 -18.671 -53.183 15.803 1.00133.43 O ANISOU 1994 OD1 ASP A1060 13281 15797 21619 606 -3829 2212 O ATOM 1995 OD2 ASP A1060 -18.670 -51.601 14.279 1.00134.11 O ANISOU 1995 OD2 ASP A1060 13988 15407 21561 1120 -4039 2014 O ATOM 1996 N PHE A1061 -15.069 -50.515 18.044 1.00115.65 N ANISOU 1996 N PHE A1061 11871 13530 18541 1520 -1633 910 N ATOM 1997 CA PHE A1061 -13.886 -49.878 18.609 1.00111.27 C ANISOU 1997 CA PHE A1061 11631 12861 17785 1663 -1177 554 C ATOM 1998 C PHE A1061 -13.352 -50.674 19.794 1.00107.12 C ANISOU 1998 C PHE A1061 10964 12569 17168 1478 -929 474 C ATOM 1999 O PHE A1061 -12.150 -50.952 19.878 1.00104.18 O ANISOU 1999 O PHE A1061 10958 12018 16606 1348 -811 252 O ATOM 2000 CB PHE A1061 -14.230 -48.441 19.013 1.00113.07 C ANISOU 2000 CB PHE A1061 11736 13129 18095 2106 -889 449 C ATOM 2001 CG PHE A1061 -13.398 -47.898 20.144 1.00111.11 C ANISOU 2001 CG PHE A1061 11598 12904 17714 2250 -450 151 C ATOM 2002 CD1 PHE A1061 -12.173 -47.305 19.898 1.00108.12 C ANISOU 2002 CD1 PHE A1061 11719 12160 17203 2238 -335 -128 C ATOM 2003 CD2 PHE A1061 -13.860 -47.951 21.451 1.00112.73 C ANISOU 2003 CD2 PHE A1061 11423 13476 17933 2410 -168 178 C ATOM 2004 CE1 PHE A1061 -11.415 -46.793 20.934 1.00107.17 C ANISOU 2004 CE1 PHE A1061 11715 12009 16997 2334 -46 -392 C ATOM 2005 CE2 PHE A1061 -13.103 -47.445 22.491 1.00111.34 C ANISOU 2005 CE2 PHE A1061 11456 13260 17588 2564 154 -114 C ATOM 2006 CZ PHE A1061 -11.880 -46.864 22.231 1.00108.50 C ANISOU 2006 CZ PHE A1061 11593 12503 17128 2505 165 -408 C ATOM 2007 N ARG A1062 -14.238 -51.058 20.717 1.00107.58 N ANISOU 2007 N ARG A1062 10477 13030 17368 1481 -836 686 N ATOM 2008 CA ARG A1062 -13.803 -51.784 21.906 1.00106.19 C ANISOU 2008 CA ARG A1062 10203 13075 17071 1342 -586 629 C ATOM 2009 C ARG A1062 -13.333 -53.191 21.557 1.00 98.62 C ANISOU 2009 C ARG A1062 9445 12014 16013 899 -888 700 C ATOM 2010 O ARG A1062 -12.373 -53.696 22.151 1.00 94.70 O ANISOU 2010 O ARG A1062 9173 11488 15322 783 -739 510 O ATOM 2011 CB ARG A1062 -14.931 -51.829 22.937 1.00115.08 C ANISOU 2011 CB ARG A1062 10710 14661 18355 1495 -350 902 C ATOM 2012 CG ARG A1062 -14.678 -52.779 24.098 1.00119.65 C ANISOU 2012 CG ARG A1062 11183 15479 18800 1312 -142 940 C ATOM 2013 CD ARG A1062 -15.511 -52.416 25.317 1.00127.80 C ANISOU 2013 CD ARG A1062 11759 16929 19869 1652 313 1112 C ATOM 2014 NE ARG A1062 -15.038 -51.190 25.955 1.00130.42 N ANISOU 2014 NE ARG A1062 12391 17175 19989 2131 681 757 N ATOM 2015 CZ ARG A1062 -14.013 -51.136 26.802 1.00129.39 C ANISOU 2015 CZ ARG A1062 12678 16930 19556 2179 871 420 C ATOM 2016 NH1 ARG A1062 -13.348 -52.241 27.112 1.00126.92 N ANISOU 2016 NH1 ARG A1062 12501 16605 19116 1809 770 392 N ATOM 2017 NH2 ARG A1062 -13.650 -49.978 27.336 1.00129.96 N ANISOU 2017 NH2 ARG A1062 13065 16862 19453 2601 1107 110 N ATOM 2018 N HIS A1063 -13.990 -53.839 20.591 1.00 94.84 N ANISOU 2018 N HIS A1063 8936 11444 15656 667 -1361 967 N ATOM 2019 CA HIS A1063 -13.565 -55.175 20.192 1.00 89.99 C ANISOU 2019 CA HIS A1063 8635 10658 14899 283 -1705 1025 C ATOM 2020 C HIS A1063 -12.178 -55.142 19.563 1.00 79.79 C ANISOU 2020 C HIS A1063 8013 8990 13311 325 -1655 705 C ATOM 2021 O HIS A1063 -11.362 -56.042 19.795 1.00 76.84 O ANISOU 2021 O HIS A1063 7906 8545 12743 153 -1651 612 O ATOM 2022 CB HIS A1063 -14.580 -55.792 19.229 1.00 95.22 C ANISOU 2022 CB HIS A1063 9219 11218 15741 39 -2319 1370 C ATOM 2023 CG HIS A1063 -14.373 -57.256 18.990 1.00 97.01 C ANISOU 2023 CG HIS A1063 9745 11278 15835 -367 -2730 1483 C ATOM 2024 ND1 HIS A1063 -14.227 -58.164 20.017 1.00 96.58 N ANISOU 2024 ND1 HIS A1063 9514 11435 15747 -598 -2594 1554 N ATOM 2025 CD2 HIS A1063 -14.290 -57.971 17.843 1.00 98.26 C ANISOU 2025 CD2 HIS A1063 10452 11037 15844 -555 -3296 1533 C ATOM 2026 CE1 HIS A1063 -14.061 -59.374 19.513 1.00 97.02 C ANISOU 2026 CE1 HIS A1063 9975 11226 15663 -926 -3066 1643 C ATOM 2027 NE2 HIS A1063 -14.095 -59.285 18.196 1.00 97.70 N ANISOU 2027 NE2 HIS A1063 10526 10932 15663 -894 -3504 1624 N ATOM 2028 N GLY A1064 -11.887 -54.105 18.775 1.00 72.66 N ANISOU 2028 N GLY A1064 7376 7849 12384 573 -1589 564 N ATOM 2029 CA GLY A1064 -10.585 -54.019 18.132 1.00 64.90 C ANISOU 2029 CA GLY A1064 6967 6528 11164 631 -1472 338 C ATOM 2030 C GLY A1064 -9.450 -53.840 19.122 1.00 59.65 C ANISOU 2030 C GLY A1064 6285 5942 10438 673 -1048 85 C ATOM 2031 O GLY A1064 -8.367 -54.406 18.945 1.00 57.17 O ANISOU 2031 O GLY A1064 6297 5468 9957 603 -987 -21 O ATOM 2032 N PHE A1065 -9.678 -53.055 20.176 1.00 59.65 N ANISOU 2032 N PHE A1065 5929 6169 10565 820 -773 -7 N ATOM 2033 CA PHE A1065 -8.652 -52.868 21.194 1.00 62.99 C ANISOU 2033 CA PHE A1065 6369 6631 10932 851 -470 -252 C ATOM 2034 C PHE A1065 -8.586 -54.040 22.165 1.00 65.69 C ANISOU 2034 C PHE A1065 6572 7206 11179 656 -486 -217 C ATOM 2035 O PHE A1065 -7.507 -54.335 22.693 1.00 63.78 O ANISOU 2035 O PHE A1065 6477 6915 10842 606 -374 -395 O ATOM 2036 CB PHE A1065 -8.890 -51.562 21.954 1.00 65.18 C ANISOU 2036 CB PHE A1065 6475 6983 11307 1125 -221 -391 C ATOM 2037 CG PHE A1065 -8.345 -50.349 21.254 1.00 65.50 C ANISOU 2037 CG PHE A1065 6777 6699 11409 1285 -142 -525 C ATOM 2038 CD1 PHE A1065 -6.997 -50.042 21.327 1.00 63.33 C ANISOU 2038 CD1 PHE A1065 6734 6194 11136 1230 -14 -716 C ATOM 2039 CD2 PHE A1065 -9.179 -49.515 20.526 1.00 70.01 C ANISOU 2039 CD2 PHE A1065 7344 7188 12070 1479 -213 -426 C ATOM 2040 CE1 PHE A1065 -6.489 -48.927 20.686 1.00 63.88 C ANISOU 2040 CE1 PHE A1065 7023 5947 11300 1329 67 -782 C ATOM 2041 CE2 PHE A1065 -8.677 -48.396 19.881 1.00 68.29 C ANISOU 2041 CE2 PHE A1065 7412 6639 11896 1614 -138 -527 C ATOM 2042 CZ PHE A1065 -7.331 -48.102 19.962 1.00 65.49 C ANISOU 2042 CZ PHE A1065 7285 6049 11549 1520 14 -693 C ATOM 2043 N ASP A1066 -9.716 -54.712 22.411 1.00 68.64 N ANISOU 2043 N ASP A1066 6649 7825 11605 535 -638 41 N ATOM 2044 CA ASP A1066 -9.695 -55.930 23.217 1.00 67.69 C ANISOU 2044 CA ASP A1066 6449 7886 11385 307 -683 131 C ATOM 2045 C ASP A1066 -8.873 -57.019 22.544 1.00 62.53 C ANISOU 2045 C ASP A1066 6210 6986 10564 93 -928 107 C ATOM 2046 O ASP A1066 -8.098 -57.721 23.206 1.00 62.86 O ANISOU 2046 O ASP A1066 6378 7047 10459 9 -868 0 O ATOM 2047 CB ASP A1066 -11.118 -56.429 23.469 1.00 77.48 C ANISOU 2047 CB ASP A1066 7248 9411 12780 173 -814 498 C ATOM 2048 CG ASP A1066 -11.813 -55.673 24.577 1.00 88.39 C ANISOU 2048 CG ASP A1066 8206 11129 14247 434 -439 547 C ATOM 2049 OD1 ASP A1066 -11.113 -55.070 25.418 1.00 91.20 O ANISOU 2049 OD1 ASP A1066 8703 11492 14457 659 -128 265 O ATOM 2050 OD2 ASP A1066 -13.061 -55.689 24.610 1.00 95.58 O ANISOU 2050 OD2 ASP A1066 8656 12287 15374 432 -469 885 O ATOM 2051 N ILE A1067 -9.041 -57.187 21.230 1.00 59.97 N ANISOU 2051 N ILE A1067 6152 6410 10224 46 -1221 208 N ATOM 2052 CA ILE A1067 -8.196 -58.119 20.491 1.00 53.41 C ANISOU 2052 CA ILE A1067 5834 5294 9165 -43 -1408 167 C ATOM 2053 C ILE A1067 -6.736 -57.705 20.603 1.00 56.23 C ANISOU 2053 C ILE A1067 6394 5532 9439 138 -1071 -101 C ATOM 2054 O ILE A1067 -5.849 -58.545 20.797 1.00 54.83 O ANISOU 2054 O ILE A1067 6438 5292 9104 96 -1060 -174 O ATOM 2055 CB ILE A1067 -8.647 -58.201 19.021 1.00 55.09 C ANISOU 2055 CB ILE A1067 6405 5209 9317 -39 -1770 306 C ATOM 2056 CG1 ILE A1067 -10.092 -58.694 18.923 1.00 66.34 C ANISOU 2056 CG1 ILE A1067 7572 6733 10899 -282 -2213 616 C ATOM 2057 CG2 ILE A1067 -7.735 -59.125 18.235 1.00 54.54 C ANISOU 2057 CG2 ILE A1067 6976 4814 8932 -25 -1909 254 C ATOM 2058 CD1 ILE A1067 -10.664 -58.624 17.519 1.00 64.39 C ANISOU 2058 CD1 ILE A1067 7671 6174 10622 -267 -2663 752 C ATOM 2059 N LEU A1068 -6.466 -56.400 20.510 1.00 53.63 N ANISOU 2059 N LEU A1068 5967 5162 9248 336 -813 -228 N ATOM 2060 CA LEU A1068 -5.088 -55.923 20.498 1.00 50.18 C ANISOU 2060 CA LEU A1068 5667 4577 8822 460 -534 -416 C ATOM 2061 C LEU A1068 -4.390 -56.201 21.824 1.00 48.10 C ANISOU 2061 C LEU A1068 5221 4482 8575 406 -409 -573 C ATOM 2062 O LEU A1068 -3.305 -56.793 21.850 1.00 47.27 O ANISOU 2062 O LEU A1068 5265 4294 8402 399 -361 -636 O ATOM 2063 CB LEU A1068 -5.048 -54.430 20.180 1.00 49.71 C ANISOU 2063 CB LEU A1068 5543 4404 8939 629 -342 -486 C ATOM 2064 CG LEU A1068 -3.639 -53.952 19.832 1.00 49.21 C ANISOU 2064 CG LEU A1068 5630 4123 8945 706 -91 -578 C ATOM 2065 CD1 LEU A1068 -3.214 -54.540 18.498 1.00 49.70 C ANISOU 2065 CD1 LEU A1068 6107 3953 8823 776 -95 -437 C ATOM 2066 CD2 LEU A1068 -3.556 -52.437 19.810 1.00 52.68 C ANISOU 2066 CD2 LEU A1068 5981 4439 9597 813 75 -654 C ATOM 2067 N VAL A1069 -4.994 -55.774 22.936 1.00 48.61 N ANISOU 2067 N VAL A1069 4988 4772 8708 413 -351 -629 N ATOM 2068 CA VAL A1069 -4.357 -55.960 24.237 1.00 50.60 C ANISOU 2068 CA VAL A1069 5155 5145 8927 398 -268 -794 C ATOM 2069 C VAL A1069 -4.260 -57.440 24.581 1.00 48.84 C ANISOU 2069 C VAL A1069 5026 5014 8517 232 -421 -712 C ATOM 2070 O VAL A1069 -3.258 -57.896 25.145 1.00 50.14 O ANISOU 2070 O VAL A1069 5275 5153 8624 221 -413 -839 O ATOM 2071 CB VAL A1069 -5.113 -55.170 25.321 1.00 53.74 C ANISOU 2071 CB VAL A1069 5329 5738 9352 521 -147 -858 C ATOM 2072 CG1 VAL A1069 -4.502 -55.427 26.693 1.00 53.13 C ANISOU 2072 CG1 VAL A1069 5276 5749 9162 531 -109 -1030 C ATOM 2073 CG2 VAL A1069 -5.088 -53.687 24.997 1.00 53.74 C ANISOU 2073 CG2 VAL A1069 5327 5578 9513 708 -30 -968 C ATOM 2074 N GLY A1070 -5.291 -58.217 24.240 1.00 48.65 N ANISOU 2074 N GLY A1070 4994 5072 8417 90 -607 -482 N ATOM 2075 CA GLY A1070 -5.224 -59.651 24.464 1.00 48.57 C ANISOU 2075 CA GLY A1070 5148 5082 8226 -96 -805 -380 C ATOM 2076 C GLY A1070 -4.080 -60.303 23.714 1.00 47.97 C ANISOU 2076 C GLY A1070 5456 4750 8022 -54 -881 -450 C ATOM 2077 O GLY A1070 -3.377 -61.160 24.255 1.00 47.04 O ANISOU 2077 O GLY A1070 5476 4629 7768 -83 -924 -511 O ATOM 2078 N GLN A1071 -3.876 -59.907 22.455 1.00 47.49 N ANISOU 2078 N GLN A1071 5596 4467 7981 61 -874 -427 N ATOM 2079 CA GLN A1071 -2.784 -60.477 21.672 1.00 47.25 C ANISOU 2079 CA GLN A1071 5951 4199 7801 193 -853 -456 C ATOM 2080 C GLN A1071 -1.430 -60.028 22.206 1.00 46.40 C ANISOU 2080 C GLN A1071 5689 4110 7830 333 -574 -631 C ATOM 2081 O GLN A1071 -0.458 -60.792 22.168 1.00 47.04 O ANISOU 2081 O GLN A1071 5950 4115 7806 428 -551 -653 O ATOM 2082 CB GLN A1071 -2.941 -60.097 20.202 1.00 49.22 C ANISOU 2082 CB GLN A1071 6504 4201 7997 328 -866 -360 C ATOM 2083 CG GLN A1071 -4.102 -60.783 19.504 1.00 51.38 C ANISOU 2083 CG GLN A1071 7055 4359 8107 187 -1280 -174 C ATOM 2084 CD GLN A1071 -4.379 -60.215 18.124 1.00 54.09 C ANISOU 2084 CD GLN A1071 7715 4447 8390 341 -1332 -95 C ATOM 2085 OE1 GLN A1071 -4.259 -59.006 17.896 1.00 54.80 O ANISOU 2085 OE1 GLN A1071 7622 4545 8657 473 -1069 -143 O ATOM 2086 NE2 GLN A1071 -4.753 -61.083 17.196 1.00 53.08 N ANISOU 2086 NE2 GLN A1071 8132 4049 7986 332 -1709 28 N ATOM 2087 N ILE A1072 -1.346 -58.793 22.704 1.00 46.13 N ANISOU 2087 N ILE A1072 5329 4154 8044 357 -396 -742 N ATOM 2088 CA ILE A1072 -0.129 -58.343 23.374 1.00 50.27 C ANISOU 2088 CA ILE A1072 5664 4677 8759 417 -247 -895 C ATOM 2089 C ILE A1072 0.120 -59.177 24.627 1.00 45.78 C ANISOU 2089 C ILE A1072 5055 4257 8083 341 -388 -990 C ATOM 2090 O ILE A1072 1.249 -59.603 24.898 1.00 46.04 O ANISOU 2090 O ILE A1072 5085 4250 8158 402 -385 -1048 O ATOM 2091 CB ILE A1072 -0.221 -56.840 23.698 1.00 50.53 C ANISOU 2091 CB ILE A1072 5452 4696 9051 432 -128 -1000 C ATOM 2092 CG1 ILE A1072 -0.217 -56.017 22.406 1.00 49.21 C ANISOU 2092 CG1 ILE A1072 5367 4334 8997 523 33 -892 C ATOM 2093 CG2 ILE A1072 0.918 -56.412 24.617 1.00 47.04 C ANISOU 2093 CG2 ILE A1072 4821 4228 8824 425 -116 -1162 C ATOM 2094 CD1 ILE A1072 -0.546 -54.562 22.609 1.00 47.71 C ANISOU 2094 CD1 ILE A1072 5020 4089 9017 540 102 -974 C ATOM 2095 N ASP A1073 -0.937 -59.429 25.405 1.00 45.77 N ANISOU 2095 N ASP A1073 5010 4433 7948 226 -502 -977 N ATOM 2096 CA ASP A1073 -0.799 -60.256 26.601 1.00 53.91 C ANISOU 2096 CA ASP A1073 6070 5594 8821 161 -621 -1037 C ATOM 2097 C ASP A1073 -0.391 -61.682 26.246 1.00 51.35 C ANISOU 2097 C ASP A1073 6031 5189 8290 133 -775 -946 C ATOM 2098 O ASP A1073 0.432 -62.291 26.942 1.00 50.80 O ANISOU 2098 O ASP A1073 6027 5124 8153 171 -849 -1036 O ATOM 2099 CB ASP A1073 -2.105 -60.258 27.394 1.00 54.05 C ANISOU 2099 CB ASP A1073 5982 5828 8727 65 -630 -957 C ATOM 2100 CG ASP A1073 -2.392 -58.921 28.049 1.00 58.79 C ANISOU 2100 CG ASP A1073 6385 6502 9449 187 -469 -1090 C ATOM 2101 OD1 ASP A1073 -1.453 -58.110 28.187 1.00 61.22 O ANISOU 2101 OD1 ASP A1073 6674 6674 9914 286 -438 -1283 O ATOM 2102 OD2 ASP A1073 -3.558 -58.686 28.433 1.00 61.45 O ANISOU 2102 OD2 ASP A1073 6591 7022 9733 194 -382 -981 O ATOM 2103 N ASP A1074 -0.973 -62.236 25.178 1.00 49.92 N ANISOU 2103 N ASP A1074 6078 4902 7988 87 -872 -772 N ATOM 2104 CA ASP A1074 -0.568 -63.558 24.706 1.00 48.22 C ANISOU 2104 CA ASP A1074 6260 4531 7530 113 -1047 -697 C ATOM 2105 C ASP A1074 0.929 -63.603 24.449 1.00 47.34 C ANISOU 2105 C ASP A1074 6206 4308 7474 372 -892 -797 C ATOM 2106 O ASP A1074 1.622 -64.529 24.886 1.00 47.82 O ANISOU 2106 O ASP A1074 6425 4345 7400 445 -987 -832 O ATOM 2107 CB ASP A1074 -1.327 -63.922 23.429 1.00 47.76 C ANISOU 2107 CB ASP A1074 6526 4287 7335 72 -1215 -520 C ATOM 2108 CG ASP A1074 -2.781 -64.256 23.681 1.00 50.20 C ANISOU 2108 CG ASP A1074 6768 4692 7616 -230 -1471 -340 C ATOM 2109 OD1 ASP A1074 -3.201 -64.248 24.856 1.00 53.43 O ANISOU 2109 OD1 ASP A1074 6886 5336 8078 -375 -1436 -332 O ATOM 2110 OD2 ASP A1074 -3.503 -64.529 22.695 1.00 49.95 O ANISOU 2110 OD2 ASP A1074 6978 4489 7512 -313 -1714 -180 O ATOM 2111 N ALA A1075 1.447 -62.599 23.737 1.00 46.62 N ANISOU 2111 N ALA A1075 5960 4148 7605 521 -642 -810 N ATOM 2112 CA ALA A1075 2.862 -62.588 23.389 1.00 49.43 C ANISOU 2112 CA ALA A1075 6275 4418 8088 770 -435 -818 C ATOM 2113 C ALA A1075 3.731 -62.356 24.617 1.00 49.06 C ANISOU 2113 C ALA A1075 5869 4495 8277 745 -460 -962 C ATOM 2114 O ALA A1075 4.799 -62.964 24.750 1.00 49.14 O ANISOU 2114 O ALA A1075 5874 4483 8315 915 -449 -958 O ATOM 2115 CB ALA A1075 3.129 -61.526 22.323 1.00 48.23 C ANISOU 2115 CB ALA A1075 6030 4156 8140 897 -137 -734 C ATOM 2116 N LEU A1076 3.284 -61.489 25.531 1.00 50.13 N ANISOU 2116 N LEU A1076 5740 4740 8566 570 -522 -1088 N ATOM 2117 CA LEU A1076 4.055 -61.219 26.741 1.00 53.36 C ANISOU 2117 CA LEU A1076 5907 5209 9159 546 -638 -1247 C ATOM 2118 C LEU A1076 4.201 -62.468 27.598 1.00 53.64 C ANISOU 2118 C LEU A1076 6145 5308 8929 551 -867 -1292 C ATOM 2119 O LEU A1076 5.269 -62.715 28.172 1.00 55.66 O ANISOU 2119 O LEU A1076 6290 5551 9309 640 -978 -1363 O ATOM 2120 CB LEU A1076 3.398 -60.095 27.542 1.00 54.91 C ANISOU 2120 CB LEU A1076 5949 5462 9452 416 -679 -1384 C ATOM 2121 CG LEU A1076 3.824 -58.685 27.144 1.00 57.76 C ANISOU 2121 CG LEU A1076 6053 5700 10191 416 -548 -1406 C ATOM 2122 CD1 LEU A1076 2.896 -57.649 27.753 1.00 61.05 C ANISOU 2122 CD1 LEU A1076 6461 6143 10592 354 -576 -1531 C ATOM 2123 CD2 LEU A1076 5.262 -58.440 27.574 1.00 59.43 C ANISOU 2123 CD2 LEU A1076 6010 5821 10750 431 -652 -1458 C ATOM 2124 N LYS A1077 3.137 -63.266 27.704 1.00 54.04 N ANISOU 2124 N LYS A1077 6480 5415 8640 442 -968 -1227 N ATOM 2125 CA LYS A1077 3.223 -64.513 28.456 1.00 56.83 C ANISOU 2125 CA LYS A1077 7089 5792 8712 428 -1186 -1234 C ATOM 2126 C LYS A1077 4.271 -65.440 27.853 1.00 58.87 C ANISOU 2126 C LYS A1077 7532 5918 8918 652 -1210 -1183 C ATOM 2127 O LYS A1077 5.085 -66.029 28.574 1.00 59.79 O ANISOU 2127 O LYS A1077 7679 6035 9004 757 -1359 -1255 O ATOM 2128 CB LYS A1077 1.859 -65.200 28.499 1.00 58.01 C ANISOU 2128 CB LYS A1077 7482 5992 8566 222 -1284 -1093 C ATOM 2129 CG LYS A1077 1.909 -66.571 29.141 1.00 62.21 C ANISOU 2129 CG LYS A1077 8349 6497 8791 177 -1514 -1050 C ATOM 2130 CD LYS A1077 0.535 -67.188 29.276 1.00 67.85 C ANISOU 2130 CD LYS A1077 9224 7262 9292 -99 -1621 -849 C ATOM 2131 CE LYS A1077 0.641 -68.589 29.844 1.00 72.88 C ANISOU 2131 CE LYS A1077 10250 7816 9624 -166 -1867 -779 C ATOM 2132 NZ LYS A1077 1.424 -69.485 28.951 1.00 75.43 N ANISOU 2132 NZ LYS A1077 10955 7886 9817 19 -2015 -776 N ATOM 2133 N LEU A1078 4.263 -65.581 26.525 1.00 56.83 N ANISOU 2133 N LEU A1078 7440 5533 8619 779 -1063 -1052 N ATOM 2134 CA LEU A1078 5.287 -66.378 25.855 1.00 56.56 C ANISOU 2134 CA LEU A1078 7616 5367 8506 1099 -998 -984 C ATOM 2135 C LEU A1078 6.672 -65.786 26.075 1.00 55.95 C ANISOU 2135 C LEU A1078 7080 5345 8831 1294 -836 -1018 C ATOM 2136 O LEU A1078 7.641 -66.521 26.300 1.00 58.03 O ANISOU 2136 O LEU A1078 7365 5593 9090 1530 -887 -1009 O ATOM 2137 CB LEU A1078 4.981 -66.477 24.361 1.00 50.85 C ANISOU 2137 CB LEU A1078 7227 4470 7622 1249 -836 -837 C ATOM 2138 CG LEU A1078 3.695 -67.202 23.968 1.00 58.68 C ANISOU 2138 CG LEU A1078 8718 5335 8241 1058 -1101 -760 C ATOM 2139 CD1 LEU A1078 3.384 -66.966 22.499 1.00 51.17 C ANISOU 2139 CD1 LEU A1078 8075 4189 7178 1201 -977 -641 C ATOM 2140 CD2 LEU A1078 3.824 -68.688 24.263 1.00 51.72 C ANISOU 2140 CD2 LEU A1078 8330 4321 6999 1121 -1388 -746 C ATOM 2141 N ALA A1079 6.784 -64.456 26.016 1.00 55.51 N ANISOU 2141 N ALA A1079 6593 5339 9157 1190 -671 -1036 N ATOM 2142 CA ALA A1079 8.074 -63.809 26.234 1.00 59.90 C ANISOU 2142 CA ALA A1079 6649 5922 10189 1291 -578 -1021 C ATOM 2143 C ALA A1079 8.589 -64.060 27.647 1.00 63.61 C ANISOU 2143 C ALA A1079 6970 6456 10743 1221 -932 -1181 C ATOM 2144 O ALA A1079 9.776 -64.350 27.839 1.00 64.42 O ANISOU 2144 O ALA A1079 6822 6564 11090 1406 -978 -1132 O ATOM 2145 CB ALA A1079 7.961 -62.308 25.962 1.00 58.64 C ANISOU 2145 CB ALA A1079 6133 5744 10404 1125 -412 -1009 C ATOM 2146 N ASN A1080 7.709 -63.960 28.648 1.00 65.36 N ANISOU 2146 N ASN A1080 7350 6725 10757 988 -1178 -1352 N ATOM 2147 CA ASN A1080 8.115 -64.194 30.029 1.00 69.47 C ANISOU 2147 CA ASN A1080 7856 7274 11267 947 -1533 -1515 C ATOM 2148 C ASN A1080 8.571 -65.627 30.266 1.00 71.71 C ANISOU 2148 C ASN A1080 8419 7546 11280 1139 -1693 -1487 C ATOM 2149 O ASN A1080 9.326 -65.877 31.211 1.00 74.40 O ANISOU 2149 O ASN A1080 8685 7881 11700 1199 -1986 -1583 O ATOM 2150 CB ASN A1080 6.969 -63.851 30.983 1.00 71.14 C ANISOU 2150 CB ASN A1080 8276 7541 11214 731 -1665 -1663 C ATOM 2151 CG ASN A1080 6.689 -62.363 31.047 1.00 74.39 C ANISOU 2151 CG ASN A1080 8442 7929 11895 602 -1593 -1744 C ATOM 2152 OD1 ASN A1080 7.599 -61.542 30.931 1.00 76.83 O ANISOU 2152 OD1 ASN A1080 8405 8146 12640 605 -1630 -1757 O ATOM 2153 ND2 ASN A1080 5.424 -62.007 31.235 1.00 75.09 N ANISOU 2153 ND2 ASN A1080 8697 8087 11745 492 -1497 -1773 N ATOM 2154 N GLU A1081 8.130 -66.570 29.437 1.00 70.06 N ANISOU 2154 N GLU A1081 8584 7296 10739 1245 -1560 -1361 N ATOM 2155 CA GLU A1081 8.568 -67.955 29.521 1.00 69.88 C ANISOU 2155 CA GLU A1081 8914 7207 10429 1469 -1708 -1324 C ATOM 2156 C GLU A1081 9.805 -68.230 28.675 1.00 69.78 C ANISOU 2156 C GLU A1081 8727 7153 10634 1867 -1506 -1187 C ATOM 2157 O GLU A1081 10.202 -69.392 28.539 1.00 71.67 O ANISOU 2157 O GLU A1081 9311 7312 10610 2148 -1577 -1138 O ATOM 2158 CB GLU A1081 7.434 -68.891 29.099 1.00 71.15 C ANISOU 2158 CB GLU A1081 9659 7281 10095 1372 -1745 -1248 C ATOM 2159 CG GLU A1081 6.182 -68.781 29.952 1.00 74.17 C ANISOU 2159 CG GLU A1081 10170 7740 10272 1004 -1894 -1297 C ATOM 2160 CD GLU A1081 5.020 -69.566 29.377 1.00 78.88 C ANISOU 2160 CD GLU A1081 11217 8241 10512 836 -1945 -1148 C ATOM 2161 OE1 GLU A1081 5.113 -69.995 28.207 1.00 81.19 O ANISOU 2161 OE1 GLU A1081 11766 8376 10707 997 -1878 -1047 O ATOM 2162 OE2 GLU A1081 4.014 -69.756 30.092 1.00 80.97 O ANISOU 2162 OE2 GLU A1081 11594 8574 10598 549 -2062 -1109 O ATOM 2163 N GLY A1082 10.413 -67.194 28.098 1.00 66.80 N ANISOU 2163 N GLY A1082 7837 6820 10725 1918 -1232 -1096 N ATOM 2164 CA GLY A1082 11.613 -67.365 27.303 1.00 69.80 C ANISOU 2164 CA GLY A1082 7954 7200 11369 2319 -946 -896 C ATOM 2165 C GLY A1082 11.401 -67.911 25.910 1.00 69.06 C ANISOU 2165 C GLY A1082 8295 7000 10946 2632 -578 -727 C ATOM 2166 O GLY A1082 12.381 -68.248 25.241 1.00 73.78 O ANISOU 2166 O GLY A1082 8787 7595 11652 3076 -282 -538 O ATOM 2167 N LYS A1083 10.156 -68.004 25.446 1.00 65.16 N ANISOU 2167 N LYS A1083 8299 6406 10054 2443 -597 -771 N ATOM 2168 CA LYS A1083 9.847 -68.571 24.133 1.00 60.76 C ANISOU 2168 CA LYS A1083 8310 5672 9102 2728 -366 -639 C ATOM 2169 C LYS A1083 9.790 -67.432 23.125 1.00 60.81 C ANISOU 2169 C LYS A1083 8072 5681 9351 2731 43 -503 C ATOM 2170 O LYS A1083 8.743 -66.824 22.898 1.00 60.11 O ANISOU 2170 O LYS A1083 8082 5560 9197 2420 -8 -551 O ATOM 2171 CB LYS A1083 8.540 -69.349 24.183 1.00 58.63 C ANISOU 2171 CB LYS A1083 8717 5253 8309 2487 -712 -727 C ATOM 2172 CG LYS A1083 8.440 -70.316 25.351 1.00 63.15 C ANISOU 2172 CG LYS A1083 9496 5827 8672 2365 -1131 -847 C ATOM 2173 CD LYS A1083 7.102 -71.031 25.347 1.00 60.32 C ANISOU 2173 CD LYS A1083 9738 5313 7870 2058 -1457 -855 C ATOM 2174 CE LYS A1083 7.017 -72.055 26.463 1.00 59.85 C ANISOU 2174 CE LYS A1083 9943 5225 7574 1943 -1837 -925 C ATOM 2175 NZ LYS A1083 5.722 -72.789 26.434 1.00 57.81 N ANISOU 2175 NZ LYS A1083 10225 4799 6942 1598 -2157 -859 N ATOM 2176 N VAL A1084 10.933 -67.151 22.496 1.00 64.19 N ANISOU 2176 N VAL A1084 8169 6150 10071 3109 474 -298 N ATOM 2177 CA VAL A1084 11.045 -65.969 21.646 1.00 68.92 C ANISOU 2177 CA VAL A1084 8447 6758 10980 3095 897 -127 C ATOM 2178 C VAL A1084 10.312 -66.179 20.326 1.00 66.43 C ANISOU 2178 C VAL A1084 8843 6232 10166 3296 1101 -44 C ATOM 2179 O VAL A1084 9.529 -65.326 19.893 1.00 64.35 O ANISOU 2179 O VAL A1084 8608 5916 9924 3044 1141 -52 O ATOM 2180 CB VAL A1084 12.523 -65.611 21.416 1.00 72.42 C ANISOU 2180 CB VAL A1084 8246 7324 11948 3415 1324 143 C ATOM 2181 CG1 VAL A1084 12.648 -64.148 21.001 1.00 71.66 C ANISOU 2181 CG1 VAL A1084 7618 7259 12351 3189 1631 301 C ATOM 2182 CG2 VAL A1084 13.337 -65.900 22.667 1.00 73.91 C ANISOU 2182 CG2 VAL A1084 7927 7660 12495 3352 998 65 C ATOM 2183 N LYS A1085 10.562 -67.310 19.661 1.00 69.18 N ANISOU 2183 N LYS A1085 9827 6422 10036 3784 1199 32 N ATOM 2184 CA LYS A1085 9.954 -67.553 18.354 1.00 71.43 C ANISOU 2184 CA LYS A1085 10907 6439 9793 4039 1343 111 C ATOM 2185 C LYS A1085 8.433 -67.587 18.440 1.00 68.01 C ANISOU 2185 C LYS A1085 10908 5866 9066 3566 833 -73 C ATOM 2186 O LYS A1085 7.742 -67.063 17.558 1.00 64.43 O ANISOU 2186 O LYS A1085 10751 5266 8462 3518 899 -21 O ATOM 2187 CB LYS A1085 10.483 -68.858 17.760 1.00 72.90 C ANISOU 2187 CB LYS A1085 11780 6470 9447 4606 1426 186 C ATOM 2188 CG LYS A1085 11.909 -68.781 17.242 1.00 78.77 C ANISOU 2188 CG LYS A1085 12124 7425 10381 5034 2014 454 C ATOM 2189 CD LYS A1085 11.998 -67.992 15.941 1.00 81.49 C ANISOU 2189 CD LYS A1085 12551 7764 10647 5158 2519 688 C ATOM 2190 CE LYS A1085 13.352 -68.203 15.274 1.00 90.68 C ANISOU 2190 CE LYS A1085 13540 9104 11808 5640 3102 1004 C ATOM 2191 NZ LYS A1085 13.433 -67.571 13.928 1.00 95.49 N ANISOU 2191 NZ LYS A1085 14402 9675 12204 5826 3621 1276 N ATOM 2192 N GLU A1086 7.891 -68.206 19.491 1.00 62.34 N ANISOU 2192 N GLU A1086 10221 5191 8276 3222 326 -255 N ATOM 2193 CA GLU A1086 6.442 -68.243 19.637 1.00 62.95 C ANISOU 2193 CA GLU A1086 10583 5178 8156 2754 -129 -360 C ATOM 2194 C GLU A1086 5.891 -66.861 19.970 1.00 59.51 C ANISOU 2194 C GLU A1086 9521 4938 8154 2342 -66 -397 C ATOM 2195 O GLU A1086 4.795 -66.502 19.527 1.00 55.71 O ANISOU 2195 O GLU A1086 9233 4368 7567 2109 -229 -390 O ATOM 2196 CB GLU A1086 6.042 -69.261 20.703 1.00 65.55 C ANISOU 2196 CB GLU A1086 11077 5514 8313 2502 -615 -482 C ATOM 2197 CG GLU A1086 4.615 -69.764 20.545 1.00 72.13 C ANISOU 2197 CG GLU A1086 12424 6158 8826 2140 -1096 -486 C ATOM 2198 CD GLU A1086 4.227 -70.797 21.584 1.00 77.36 C ANISOU 2198 CD GLU A1086 13256 6812 9328 1870 -1539 -543 C ATOM 2199 OE1 GLU A1086 5.117 -71.533 22.063 1.00 79.46 O ANISOU 2199 OE1 GLU A1086 13615 7074 9503 2129 -1533 -587 O ATOM 2200 OE2 GLU A1086 3.026 -70.869 21.924 1.00 78.01 O ANISOU 2200 OE2 GLU A1086 13356 6894 9389 1405 -1882 -513 O ATOM 2201 N ALA A1087 6.642 -66.071 20.744 1.00 56.34 N ANISOU 2201 N ALA A1087 8390 4775 8243 2262 126 -431 N ATOM 2202 CA ALA A1087 6.231 -64.699 21.025 1.00 60.74 C ANISOU 2202 CA ALA A1087 8425 5462 9192 1935 195 -473 C ATOM 2203 C ALA A1087 6.190 -63.871 19.747 1.00 59.69 C ANISOU 2203 C ALA A1087 8382 5203 9093 2091 550 -318 C ATOM 2204 O ALA A1087 5.251 -63.099 19.525 1.00 56.39 O ANISOU 2204 O ALA A1087 7952 4763 8711 1854 476 -342 O ATOM 2205 CB ALA A1087 7.174 -64.063 22.049 1.00 54.70 C ANISOU 2205 CB ALA A1087 6964 4891 8930 1846 260 -533 C ATOM 2206 N GLN A1088 7.201 -64.027 18.888 1.00 60.56 N ANISOU 2206 N GLN A1088 8598 5231 9179 2530 962 -133 N ATOM 2207 CA GLN A1088 7.263 -63.244 17.658 1.00 61.88 C ANISOU 2207 CA GLN A1088 8892 5268 9351 2725 1369 55 C ATOM 2208 C GLN A1088 6.122 -63.607 16.716 1.00 61.49 C ANISOU 2208 C GLN A1088 9631 4965 8768 2767 1154 45 C ATOM 2209 O GLN A1088 5.494 -62.728 16.114 1.00 62.53 O ANISOU 2209 O GLN A1088 9815 5013 8932 2656 1207 87 O ATOM 2210 CB GLN A1088 8.615 -63.448 16.977 1.00 64.89 C ANISOU 2210 CB GLN A1088 9231 5637 9788 3247 1923 309 C ATOM 2211 CG GLN A1088 9.771 -62.760 17.678 1.00 66.30 C ANISOU 2211 CG GLN A1088 8503 6041 10646 3164 2165 413 C ATOM 2212 CD GLN A1088 11.122 -63.236 17.176 1.00 71.28 C ANISOU 2212 CD GLN A1088 9010 6716 11358 3709 2677 701 C ATOM 2213 OE1 GLN A1088 11.391 -64.437 17.129 1.00 72.70 O ANISOU 2213 OE1 GLN A1088 9607 6857 11159 4083 2635 683 O ATOM 2214 NE2 GLN A1088 11.977 -62.295 16.795 1.00 74.53 N ANISOU 2214 NE2 GLN A1088 8842 7201 12277 3770 3176 998 N ATOM 2215 N ALA A1089 5.847 -64.905 16.565 1.00 66.06 N ANISOU 2215 N ALA A1089 10863 5381 8855 2926 858 -4 N ATOM 2216 CA ALA A1089 4.702 -65.322 15.763 1.00 65.36 C ANISOU 2216 CA ALA A1089 11539 5004 8289 2890 491 -16 C ATOM 2217 C ALA A1089 3.406 -64.761 16.333 1.00 64.04 C ANISOU 2217 C ALA A1089 11071 4939 8321 2329 74 -122 C ATOM 2218 O ALA A1089 2.533 -64.309 15.582 1.00 67.51 O ANISOU 2218 O ALA A1089 11781 5222 8646 2250 -68 -77 O ATOM 2219 CB ALA A1089 4.642 -66.846 15.685 1.00 63.26 C ANISOU 2219 CB ALA A1089 12014 4514 7508 3082 140 -56 C ATOM 2220 N ALA A1090 3.268 -64.775 17.662 1.00 59.99 N ANISOU 2220 N ALA A1090 10008 4688 8097 1978 -113 -248 N ATOM 2221 CA ALA A1090 2.090 -64.189 18.292 1.00 56.82 C ANISOU 2221 CA ALA A1090 9257 4431 7901 1518 -402 -316 C ATOM 2222 C ALA A1090 2.019 -62.689 18.038 1.00 56.49 C ANISOU 2222 C ALA A1090 8794 4468 8202 1471 -112 -298 C ATOM 2223 O ALA A1090 0.935 -62.144 17.803 1.00 56.70 O ANISOU 2223 O ALA A1090 8815 4474 8254 1276 -298 -284 O ATOM 2224 CB ALA A1090 2.097 -64.482 19.792 1.00 51.89 C ANISOU 2224 CB ALA A1090 8194 4063 7460 1246 -567 -440 C ATOM 2225 N ALA A1091 3.167 -62.005 18.083 1.00 57.74 N ANISOU 2225 N ALA A1091 8582 4702 8655 1643 321 -274 N ATOM 2226 CA ALA A1091 3.188 -60.572 17.810 1.00 58.84 C ANISOU 2226 CA ALA A1091 8373 4857 9126 1588 586 -234 C ATOM 2227 C ALA A1091 2.790 -60.270 16.373 1.00 64.47 C ANISOU 2227 C ALA A1091 9590 5317 9588 1794 704 -87 C ATOM 2228 O ALA A1091 2.213 -59.211 16.101 1.00 65.74 O ANISOU 2228 O ALA A1091 9626 5448 9905 1677 728 -74 O ATOM 2229 CB ALA A1091 4.572 -59.994 18.106 1.00 59.53 C ANISOU 2229 CB ALA A1091 7964 5034 9622 1691 980 -177 C ATOM 2230 N GLU A1092 3.086 -61.184 15.445 1.00 65.45 N ANISOU 2230 N GLU A1092 10354 5229 9286 2138 762 19 N ATOM 2231 CA GLU A1092 2.709 -60.979 14.051 1.00 70.84 C ANISOU 2231 CA GLU A1092 11664 5618 9634 2386 833 152 C ATOM 2232 C GLU A1092 1.197 -60.910 13.887 1.00 67.77 C ANISOU 2232 C GLU A1092 11509 5133 9109 2108 288 90 C ATOM 2233 O GLU A1092 0.701 -60.233 12.979 1.00 68.73 O ANISOU 2233 O GLU A1092 11908 5070 9137 2187 296 171 O ATOM 2234 CB GLU A1092 3.291 -62.097 13.184 1.00 81.20 C ANISOU 2234 CB GLU A1092 13741 6686 10427 2864 947 253 C ATOM 2235 CG GLU A1092 3.752 -61.639 11.813 1.00 91.68 C ANISOU 2235 CG GLU A1092 15461 7873 11498 3235 1388 454 C ATOM 2236 CD GLU A1092 4.879 -60.627 11.889 1.00 96.90 C ANISOU 2236 CD GLU A1092 15518 8661 12638 3372 2077 628 C ATOM 2237 OE1 GLU A1092 5.810 -60.827 12.699 1.00 98.53 O ANISOU 2237 OE1 GLU A1092 15191 9056 13189 3402 2304 640 O ATOM 2238 OE2 GLU A1092 4.828 -59.627 11.144 1.00 99.10 O ANISOU 2238 OE2 GLU A1092 15814 8873 12968 3400 2345 767 O ATOM 2239 N GLN A1093 0.453 -61.594 14.761 1.00 65.27 N ANISOU 2239 N GLN A1093 11058 4940 8803 1784 -184 -20 N ATOM 2240 CA GLN A1093 -1.004 -61.541 14.708 1.00 68.21 C ANISOU 2240 CA GLN A1093 11492 5272 9151 1485 -701 -17 C ATOM 2241 C GLN A1093 -1.526 -60.131 14.943 1.00 65.99 C ANISOU 2241 C GLN A1093 10661 5153 9257 1321 -579 -34 C ATOM 2242 O GLN A1093 -2.637 -59.803 14.511 1.00 68.89 O ANISOU 2242 O GLN A1093 11123 5440 9612 1206 -901 22 O ATOM 2243 CB GLN A1093 -1.597 -62.499 15.742 1.00 72.23 C ANISOU 2243 CB GLN A1093 11831 5933 9678 1150 -1125 -69 C ATOM 2244 CG GLN A1093 -1.120 -63.922 15.584 1.00 80.62 C ANISOU 2244 CG GLN A1093 13483 6799 10349 1298 -1305 -64 C ATOM 2245 CD GLN A1093 -1.253 -64.404 14.159 1.00 90.15 C ANISOU 2245 CD GLN A1093 15611 7565 11076 1590 -1509 26 C ATOM 2246 OE1 GLN A1093 -2.357 -64.485 13.621 1.00 94.54 O ANISOU 2246 OE1 GLN A1093 16474 7924 11524 1411 -2010 98 O ATOM 2247 NE2 GLN A1093 -0.125 -64.714 13.532 1.00 94.64 N ANISOU 2247 NE2 GLN A1093 16641 7966 11352 2072 -1126 41 N ATOM 2248 N LEU A1094 -0.744 -59.292 15.627 1.00 63.82 N ANISOU 2248 N LEU A1094 9831 5082 9336 1315 -166 -103 N ATOM 2249 CA LEU A1094 -1.169 -57.923 15.901 1.00 62.24 C ANISOU 2249 CA LEU A1094 9182 4988 9477 1193 -60 -139 C ATOM 2250 C LEU A1094 -1.397 -57.143 14.613 1.00 64.66 C ANISOU 2250 C LEU A1094 9851 5034 9682 1386 42 -19 C ATOM 2251 O LEU A1094 -2.300 -56.302 14.541 1.00 64.19 O ANISOU 2251 O LEU A1094 9650 4983 9758 1294 -102 -20 O ATOM 2252 CB LEU A1094 -0.128 -57.221 16.771 1.00 51.31 C ANISOU 2252 CB LEU A1094 7269 3767 8461 1162 300 -228 C ATOM 2253 CG LEU A1094 0.052 -57.784 18.180 1.00 51.77 C ANISOU 2253 CG LEU A1094 6959 4078 8633 975 171 -372 C ATOM 2254 CD1 LEU A1094 1.363 -57.325 18.779 1.00 49.80 C ANISOU 2254 CD1 LEU A1094 6338 3890 8695 1003 466 -425 C ATOM 2255 CD2 LEU A1094 -1.104 -57.350 19.051 1.00 50.90 C ANISOU 2255 CD2 LEU A1094 6540 4155 8643 752 -63 -462 C ATOM 2256 N LYS A1095 -0.588 -57.412 13.583 1.00 66.69 N ANISOU 2256 N LYS A1095 10607 5055 9677 1699 313 102 N ATOM 2257 CA LYS A1095 -0.698 -56.664 12.335 1.00 74.53 C ANISOU 2257 CA LYS A1095 12024 5773 10522 1927 471 239 C ATOM 2258 C LYS A1095 -2.073 -56.819 11.698 1.00 74.68 C ANISOU 2258 C LYS A1095 12466 5616 10293 1878 -79 257 C ATOM 2259 O LYS A1095 -2.585 -55.870 11.095 1.00 74.09 O ANISOU 2259 O LYS A1095 12486 5409 10258 1929 -95 314 O ATOM 2260 CB LYS A1095 0.393 -57.107 11.362 1.00 81.49 C ANISOU 2260 CB LYS A1095 13444 6438 11082 2338 894 400 C ATOM 2261 CG LYS A1095 1.780 -56.620 11.734 1.00 85.60 C ANISOU 2261 CG LYS A1095 13466 7102 11957 2411 1506 484 C ATOM 2262 CD LYS A1095 2.818 -57.151 10.767 1.00 93.05 C ANISOU 2262 CD LYS A1095 14908 7871 12576 2883 1987 701 C ATOM 2263 CE LYS A1095 4.155 -56.464 10.963 1.00 97.04 C ANISOU 2263 CE LYS A1095 14833 8505 13531 2942 2630 887 C ATOM 2264 NZ LYS A1095 5.214 -57.077 10.112 1.00103.13 N ANISOU 2264 NZ LYS A1095 15939 9266 13979 3382 3126 1129 N ATOM 2265 N THR A1096 -2.685 -57.999 11.822 1.00 72.66 N ANISOU 2265 N THR A1096 12464 5335 9808 1762 -575 230 N ATOM 2266 CA THR A1096 -4.036 -58.183 11.302 1.00 73.30 C ANISOU 2266 CA THR A1096 12848 5252 9750 1641 -1202 284 C ATOM 2267 C THR A1096 -5.042 -57.339 12.075 1.00 68.63 C ANISOU 2267 C THR A1096 11534 4939 9602 1349 -1371 255 C ATOM 2268 O THR A1096 -5.945 -56.738 11.480 1.00 71.45 O ANISOU 2268 O THR A1096 11987 5176 9987 1360 -1647 329 O ATOM 2269 CB THR A1096 -4.421 -59.662 11.349 1.00 77.71 C ANISOU 2269 CB THR A1096 13799 5700 10029 1516 -1734 295 C ATOM 2270 OG1 THR A1096 -3.494 -60.421 10.562 1.00 81.74 O ANISOU 2270 OG1 THR A1096 14988 6017 10053 1843 -1532 304 O ATOM 2271 CG2 THR A1096 -5.828 -59.868 10.803 1.00 80.90 C ANISOU 2271 CG2 THR A1096 14466 5907 10364 1330 -2476 397 C ATOM 2272 N THR A1097 -4.900 -57.279 13.402 1.00 62.57 N ANISOU 2272 N THR A1097 10080 4534 9160 1135 -1209 155 N ATOM 2273 CA THR A1097 -5.760 -56.412 14.203 1.00 59.19 C ANISOU 2273 CA THR A1097 9002 4379 9110 959 -1258 126 C ATOM 2274 C THR A1097 -5.537 -54.946 13.853 1.00 59.12 C ANISOU 2274 C THR A1097 8905 4294 9263 1139 -920 100 C ATOM 2275 O THR A1097 -6.488 -54.156 13.805 1.00 58.11 O ANISOU 2275 O THR A1097 8572 4206 9301 1133 -1081 134 O ATOM 2276 CB THR A1097 -5.499 -56.645 15.691 1.00 56.34 C ANISOU 2276 CB THR A1097 8066 4371 8969 771 -1099 12 C ATOM 2277 OG1 THR A1097 -5.565 -58.049 15.975 1.00 62.90 O ANISOU 2277 OG1 THR A1097 9053 5227 9620 611 -1381 51 O ATOM 2278 CG2 THR A1097 -6.528 -55.915 16.535 1.00 55.25 C ANISOU 2278 CG2 THR A1097 7343 4512 9136 652 -1161 10 C ATOM 2279 N ARG A1098 -4.283 -54.567 13.605 1.00 57.38 N ANISOU 2279 N ARG A1098 8821 3959 9021 1304 -453 70 N ATOM 2280 CA ARG A1098 -3.976 -53.182 13.269 1.00 59.89 C ANISOU 2280 CA ARG A1098 9082 4159 9513 1431 -130 80 C ATOM 2281 C ARG A1098 -4.592 -52.788 11.932 1.00 62.89 C ANISOU 2281 C ARG A1098 10001 4229 9666 1623 -301 214 C ATOM 2282 O ARG A1098 -5.132 -51.684 11.790 1.00 62.56 O ANISOU 2282 O ARG A1098 9850 4136 9784 1667 -316 220 O ATOM 2283 CB ARG A1098 -2.463 -52.982 13.246 1.00 56.73 C ANISOU 2283 CB ARG A1098 8672 3696 9187 1522 392 99 C ATOM 2284 CG ARG A1098 -2.026 -51.551 13.008 1.00 62.11 C ANISOU 2284 CG ARG A1098 9249 4235 10116 1579 729 144 C ATOM 2285 CD ARG A1098 -0.630 -51.534 12.429 1.00 64.59 C ANISOU 2285 CD ARG A1098 9717 4398 10426 1722 1229 308 C ATOM 2286 NE ARG A1098 -0.524 -52.457 11.304 1.00 69.25 N ANISOU 2286 NE ARG A1098 10956 4806 10550 1991 1262 454 N ATOM 2287 CZ ARG A1098 0.616 -52.771 10.698 1.00 75.40 C ANISOU 2287 CZ ARG A1098 11963 5478 11207 2223 1724 637 C ATOM 2288 NH1 ARG A1098 1.755 -52.232 11.109 1.00 78.08 N ANISOU 2288 NH1 ARG A1098 11831 5896 11942 2155 2169 730 N ATOM 2289 NH2 ARG A1098 0.616 -53.625 9.683 1.00 77.95 N ANISOU 2289 NH2 ARG A1098 12984 5621 11014 2527 1718 744 N ATOM 2290 N ASN A1099 -4.531 -53.683 10.942 1.00 66.25 N ANISOU 2290 N ASN A1099 11080 4411 9682 1772 -465 315 N ATOM 2291 CA ASN A1099 -5.031 -53.353 9.612 1.00 72.85 C ANISOU 2291 CA ASN A1099 12563 4891 10226 1996 -657 441 C ATOM 2292 C ASN A1099 -6.553 -53.318 9.565 1.00 75.13 C ANISOU 2292 C ASN A1099 12758 5199 10588 1862 -1308 460 C ATOM 2293 O ASN A1099 -7.127 -52.582 8.754 1.00 80.94 O ANISOU 2293 O ASN A1099 13782 5712 11258 2013 -1477 536 O ATOM 2294 CB ASN A1099 -4.503 -54.356 8.584 1.00 78.15 C ANISOU 2294 CB ASN A1099 13980 5348 10367 2203 -650 524 C ATOM 2295 CG ASN A1099 -2.995 -54.318 8.451 1.00 77.88 C ANISOU 2295 CG ASN A1099 13959 5362 10270 2379 47 573 C ATOM 2296 OD1 ASN A1099 -2.357 -53.314 8.765 1.00 76.82 O ANISOU 2296 OD1 ASN A1099 13469 5253 10466 2394 514 606 O ATOM 2297 ND2 ASN A1099 -2.415 -55.416 7.977 1.00 78.83 N ANISOU 2297 ND2 ASN A1099 14483 5492 9978 2517 102 599 N ATOM 2298 N ALA A1100 -7.223 -54.095 10.415 1.00 72.06 N ANISOU 2298 N ALA A1100 11950 5072 10357 1586 -1678 427 N ATOM 2299 CA ALA A1100 -8.672 -54.218 10.348 1.00 71.70 C ANISOU 2299 CA ALA A1100 11746 5064 10435 1434 -2318 524 C ATOM 2300 C ALA A1100 -9.413 -53.360 11.364 1.00 69.09 C ANISOU 2300 C ALA A1100 10574 5105 10573 1320 -2253 500 C ATOM 2301 O ALA A1100 -10.589 -53.052 11.142 1.00 72.60 O ANISOU 2301 O ALA A1100 10840 5568 11178 1303 -2673 620 O ATOM 2302 CB ALA A1100 -9.088 -55.683 10.533 1.00 72.53 C ANISOU 2302 CB ALA A1100 11952 5181 10425 1184 -2828 588 C ATOM 2303 N TYR A1101 -8.770 -52.963 12.464 1.00 67.45 N ANISOU 2303 N TYR A1101 9875 5174 10578 1277 -1762 358 N ATOM 2304 CA TYR A1101 -9.455 -52.189 13.495 1.00 66.54 C ANISOU 2304 CA TYR A1101 9065 5390 10828 1242 -1676 321 C ATOM 2305 C TYR A1101 -8.726 -50.900 13.851 1.00 65.29 C ANISOU 2305 C TYR A1101 8793 5212 10801 1407 -1173 166 C ATOM 2306 O TYR A1101 -9.312 -49.813 13.795 1.00 61.84 O ANISOU 2306 O TYR A1101 8222 4757 10516 1567 -1168 169 O ATOM 2307 CB TYR A1101 -9.629 -53.015 14.770 1.00 63.59 C ANISOU 2307 CB TYR A1101 8182 5388 10590 1002 -1679 304 C ATOM 2308 CG TYR A1101 -10.469 -54.262 14.628 1.00 66.71 C ANISOU 2308 CG TYR A1101 8571 5827 10948 761 -2209 498 C ATOM 2309 CD1 TYR A1101 -9.883 -55.485 14.326 1.00 64.62 C ANISOU 2309 CD1 TYR A1101 8753 5395 10407 628 -2369 501 C ATOM 2310 CD2 TYR A1101 -11.845 -54.223 14.823 1.00 68.81 C ANISOU 2310 CD2 TYR A1101 8370 6293 11483 666 -2562 705 C ATOM 2311 CE1 TYR A1101 -10.643 -56.630 14.207 1.00 67.23 C ANISOU 2311 CE1 TYR A1101 9135 5700 10708 366 -2922 686 C ATOM 2312 CE2 TYR A1101 -12.615 -55.366 14.706 1.00 72.14 C ANISOU 2312 CE2 TYR A1101 8739 6729 11942 373 -3101 934 C ATOM 2313 CZ TYR A1101 -12.008 -56.566 14.398 1.00 72.98 C ANISOU 2313 CZ TYR A1101 9364 6614 11753 203 -3307 913 C ATOM 2314 OH TYR A1101 -12.765 -57.708 14.279 1.00 79.40 O ANISOU 2314 OH TYR A1101 10189 7373 12604 -125 -3911 1147 O ATOM 2315 N ILE A1102 -7.452 -51.017 14.236 1.00 60.47 N ANISOU 2315 N ILE A1102 8233 4587 10157 1365 -790 46 N ATOM 2316 CA ILE A1102 -6.765 -49.919 14.911 1.00 60.90 C ANISOU 2316 CA ILE A1102 8062 4656 10419 1417 -401 -101 C ATOM 2317 C ILE A1102 -6.573 -48.733 13.975 1.00 62.94 C ANISOU 2317 C ILE A1102 8650 4584 10681 1606 -259 -53 C ATOM 2318 O ILE A1102 -6.766 -47.578 14.371 1.00 64.11 O ANISOU 2318 O ILE A1102 8632 4708 11019 1694 -161 -132 O ATOM 2319 CB ILE A1102 -5.424 -50.402 15.490 1.00 58.78 C ANISOU 2319 CB ILE A1102 7735 4431 10166 1296 -109 -196 C ATOM 2320 CG1 ILE A1102 -5.636 -51.642 16.365 1.00 56.20 C ANISOU 2320 CG1 ILE A1102 7169 4398 9788 1122 -276 -232 C ATOM 2321 CG2 ILE A1102 -4.755 -49.285 16.281 1.00 58.75 C ANISOU 2321 CG2 ILE A1102 7489 4410 10423 1292 167 -342 C ATOM 2322 CD1 ILE A1102 -6.672 -51.462 17.459 1.00 54.35 C ANISOU 2322 CD1 ILE A1102 6476 4472 9703 1080 -402 -280 C ATOM 2323 N GLN A1103 -6.176 -48.991 12.727 1.00 64.86 N ANISOU 2323 N GLN A1103 9427 4537 10678 1699 -235 84 N ATOM 2324 CA GLN A1103 -6.016 -47.895 11.778 1.00 67.16 C ANISOU 2324 CA GLN A1103 10091 4491 10934 1885 -82 171 C ATOM 2325 C GLN A1103 -7.344 -47.204 11.499 1.00 64.92 C ANISOU 2325 C GLN A1103 9805 4171 10689 2027 -431 198 C ATOM 2326 O GLN A1103 -7.373 -45.999 11.225 1.00 66.08 O ANISOU 2326 O GLN A1103 10069 4115 10924 2169 -312 203 O ATOM 2327 CB GLN A1103 -5.395 -48.410 10.480 1.00 72.39 C ANISOU 2327 CB GLN A1103 11405 4856 11245 2021 37 341 C ATOM 2328 CG GLN A1103 -5.016 -47.311 9.507 1.00 82.16 C ANISOU 2328 CG GLN A1103 13065 5729 12422 2212 311 476 C ATOM 2329 CD GLN A1103 -4.632 -47.847 8.147 1.00 87.93 C ANISOU 2329 CD GLN A1103 14459 6249 12701 2384 388 654 C ATOM 2330 OE1 GLN A1103 -4.039 -48.919 8.035 1.00 90.79 O ANISOU 2330 OE1 GLN A1103 14957 6686 12854 2384 485 682 O ATOM 2331 NE2 GLN A1103 -4.978 -47.106 7.100 1.00 92.40 N ANISOU 2331 NE2 GLN A1103 15377 6658 13072 2502 327 755 N ATOM 2332 N LYS A1104 -8.453 -47.946 11.572 1.00 65.35 N ANISOU 2332 N LYS A1104 9707 4411 10711 1987 -882 241 N ATOM 2333 CA LYS A1104 -9.765 -47.331 11.413 1.00 72.99 C ANISOU 2333 CA LYS A1104 10529 5407 11798 2130 -1233 302 C ATOM 2334 C LYS A1104 -10.082 -46.399 12.575 1.00 69.25 C ANISOU 2334 C LYS A1104 9510 5172 11630 2197 -1045 173 C ATOM 2335 O LYS A1104 -10.696 -45.343 12.379 1.00 69.05 O ANISOU 2335 O LYS A1104 9492 5047 11699 2427 -1106 185 O ATOM 2336 CB LYS A1104 -10.842 -48.406 11.277 1.00 77.50 C ANISOU 2336 CB LYS A1104 10964 6133 12347 2015 -1784 437 C ATOM 2337 CG LYS A1104 -10.900 -49.054 9.905 1.00 84.05 C ANISOU 2337 CG LYS A1104 12501 6603 12831 2053 -2160 572 C ATOM 2338 CD LYS A1104 -11.893 -50.204 9.884 1.00 90.20 C ANISOU 2338 CD LYS A1104 13133 7501 13637 1851 -2788 713 C ATOM 2339 CE LYS A1104 -11.703 -51.079 8.654 1.00 93.68 C ANISOU 2339 CE LYS A1104 14417 7532 13645 1868 -3172 797 C ATOM 2340 NZ LYS A1104 -10.367 -51.738 8.650 1.00 91.81 N ANISOU 2340 NZ LYS A1104 14574 7203 13108 1858 -2743 697 N ATOM 2341 N TYR A1105 -9.675 -46.765 13.793 1.00 64.99 N ANISOU 2341 N TYR A1105 8562 4920 11210 2041 -831 44 N ATOM 2342 CA TYR A1105 -9.882 -45.860 14.918 1.00 68.55 C ANISOU 2342 CA TYR A1105 8640 5540 11867 2163 -638 -102 C ATOM 2343 C TYR A1105 -8.996 -44.625 14.794 1.00 65.10 C ANISOU 2343 C TYR A1105 8500 4767 11469 2253 -354 -220 C ATOM 2344 O TYR A1105 -9.453 -43.499 15.015 1.00 67.06 O ANISOU 2344 O TYR A1105 8735 4930 11813 2485 -336 -282 O ATOM 2345 CB TYR A1105 -9.619 -46.567 16.247 1.00 70.98 C ANISOU 2345 CB TYR A1105 8546 6191 12233 1994 -502 -213 C ATOM 2346 CG TYR A1105 -9.664 -45.601 17.409 1.00 81.51 C ANISOU 2346 CG TYR A1105 9662 7618 13689 2169 -287 -395 C ATOM 2347 CD1 TYR A1105 -10.860 -45.006 17.792 1.00 88.19 C ANISOU 2347 CD1 TYR A1105 10243 8643 14623 2463 -343 -354 C ATOM 2348 CD2 TYR A1105 -8.510 -45.258 18.103 1.00 82.79 C ANISOU 2348 CD2 TYR A1105 9917 7663 13878 2073 -53 -595 C ATOM 2349 CE1 TYR A1105 -10.910 -44.110 18.842 1.00 92.00 C ANISOU 2349 CE1 TYR A1105 10649 9168 15139 2706 -139 -532 C ATOM 2350 CE2 TYR A1105 -8.551 -44.360 19.157 1.00 86.23 C ANISOU 2350 CE2 TYR A1105 10285 8107 14370 2255 66 -782 C ATOM 2351 CZ TYR A1105 -9.754 -43.791 19.522 1.00 92.09 C ANISOU 2351 CZ TYR A1105 10858 9009 15123 2597 39 -763 C ATOM 2352 OH TYR A1105 -9.804 -42.898 20.568 1.00 96.46 O ANISOU 2352 OH TYR A1105 11458 9534 15658 2858 168 -961 O ATOM 2353 N LEU A1106 -7.725 -44.821 14.453 1.00 63.79 N ANISOU 2353 N LEU A1106 8591 4398 11248 2079 -129 -223 N ATOM 2354 CA LEU A1106 -6.791 -43.723 14.254 1.00 64.80 C ANISOU 2354 CA LEU A1106 8967 4179 11474 2083 131 -256 C ATOM 2355 C LEU A1106 -7.298 -42.747 13.199 1.00 72.37 C ANISOU 2355 C LEU A1106 10319 4811 12369 2312 53 -142 C ATOM 2356 O LEU A1106 -7.491 -41.565 13.480 1.00 69.39 O ANISOU 2356 O LEU A1106 9985 4268 12112 2454 71 -224 O ATOM 2357 CB LEU A1106 -5.416 -44.257 13.851 1.00 67.50 C ANISOU 2357 CB LEU A1106 9463 4393 11792 1877 400 -170 C ATOM 2358 CG LEU A1106 -4.507 -43.268 13.111 1.00 74.41 C ANISOU 2358 CG LEU A1106 10664 4856 12753 1870 678 -42 C ATOM 2359 CD1 LEU A1106 -3.766 -42.349 14.075 1.00 75.27 C ANISOU 2359 CD1 LEU A1106 10561 4855 13184 1715 796 -172 C ATOM 2360 CD2 LEU A1106 -3.538 -44.010 12.206 1.00 73.94 C ANISOU 2360 CD2 LEU A1106 10846 4696 12553 1812 950 170 C ATOM 2361 N GLU A 219 -7.830 -43.185 12.056 1.00 69.28 N ANISOU 2361 N GLU A 219 11223 4387 10712 2234 72 -1455 N ATOM 2362 CA GLU A 219 -8.322 -42.341 10.975 1.00 67.75 C ANISOU 2362 CA GLU A 219 11008 4376 10358 2125 178 -1602 C ATOM 2363 C GLU A 219 -9.586 -41.586 11.383 1.00 67.93 C ANISOU 2363 C GLU A 219 11103 4501 10206 1893 92 -1487 C ATOM 2364 O GLU A 219 -9.706 -40.390 11.121 1.00 64.31 O ANISOU 2364 O GLU A 219 10545 4264 9627 1850 147 -1501 O ATOM 2365 CB GLU A 219 -8.583 -43.175 9.719 1.00 70.05 C ANISOU 2365 CB GLU A 219 11428 4554 10635 2092 261 -1815 C ATOM 2366 CG GLU A 219 -7.344 -43.393 8.861 1.00 78.25 C ANISOU 2366 CG GLU A 219 12344 5605 11782 2303 420 -1997 C ATOM 2367 CD GLU A 219 -7.423 -44.651 8.013 1.00 86.10 C ANISOU 2367 CD GLU A 219 13491 6391 12833 2316 460 -2169 C ATOM 2368 OE1 GLU A 219 -8.532 -45.206 7.861 1.00 87.94 O ANISOU 2368 OE1 GLU A 219 13919 6507 12985 2137 377 -2175 O ATOM 2369 OE2 GLU A 219 -6.370 -45.092 7.504 1.00 90.60 O ANISOU 2369 OE2 GLU A 219 13980 6910 13533 2504 580 -2299 O ATOM 2370 N ARG A 220 -10.523 -42.281 12.038 1.00 60.39 N ANISOU 2370 N ARG A 220 10318 3385 9242 1740 -34 -1367 N ATOM 2371 CA ARG A 220 -11.756 -41.618 12.454 1.00 63.72 C ANISOU 2371 CA ARG A 220 10803 3898 9511 1508 -106 -1254 C ATOM 2372 C ARG A 220 -11.502 -40.620 13.578 1.00 61.09 C ANISOU 2372 C ARG A 220 10342 3708 9162 1538 -164 -1072 C ATOM 2373 O ARG A 220 -12.144 -39.564 13.630 1.00 56.22 O ANISOU 2373 O ARG A 220 9693 3260 8409 1411 -160 -1032 O ATOM 2374 CB ARG A 220 -12.801 -42.647 12.874 1.00 66.84 C ANISOU 2374 CB ARG A 220 11394 4091 9910 1324 -212 -1170 C ATOM 2375 CG ARG A 220 -13.657 -43.138 11.724 1.00 76.01 C ANISOU 2375 CG ARG A 220 12685 5198 10998 1174 -175 -1335 C ATOM 2376 CD ARG A 220 -14.688 -44.150 12.187 1.00 87.56 C ANISOU 2376 CD ARG A 220 14322 6467 12479 984 -278 -1245 C ATOM 2377 NE ARG A 220 -15.179 -44.962 11.078 1.00 94.85 N ANISOU 2377 NE ARG A 220 15369 7279 13390 903 -251 -1423 N ATOM 2378 CZ ARG A 220 -16.077 -45.933 11.201 1.00101.19 C ANISOU 2378 CZ ARG A 220 16325 7908 14215 733 -325 -1392 C ATOM 2379 NH1 ARG A 220 -16.593 -46.216 12.389 1.00103.90 N ANISOU 2379 NH1 ARG A 220 16717 8171 14589 621 -419 -1184 N ATOM 2380 NH2 ARG A 220 -16.460 -46.621 10.134 1.00104.17 N ANISOU 2380 NH2 ARG A 220 16804 8195 14580 671 -303 -1568 N ATOM 2381 N ALA A 221 -10.579 -40.935 14.490 1.00 57.17 N ANISOU 2381 N ALA A 221 9774 3147 8802 1703 -223 -960 N ATOM 2382 CA ALA A 221 -10.221 -39.975 15.529 1.00 57.48 C ANISOU 2382 CA ALA A 221 9676 3334 8827 1748 -284 -799 C ATOM 2383 C ALA A 221 -9.575 -38.736 14.925 1.00 53.36 C ANISOU 2383 C ALA A 221 8957 3051 8267 1847 -173 -900 C ATOM 2384 O ALA A 221 -9.842 -37.610 15.360 1.00 50.98 O ANISOU 2384 O ALA A 221 8579 2920 7870 1785 -195 -818 O ATOM 2385 CB ALA A 221 -9.289 -40.626 16.550 1.00 61.10 C ANISOU 2385 CB ALA A 221 10094 3683 9439 1913 -376 -670 C ATOM 2386 N ARG A 222 -8.719 -38.927 13.917 1.00 59.63 N ANISOU 2386 N ARG A 222 9666 3858 9132 1997 -45 -1079 N ATOM 2387 CA ARG A 222 -8.137 -37.798 13.200 1.00 58.12 C ANISOU 2387 CA ARG A 222 9291 3898 8893 2071 88 -1189 C ATOM 2388 C ARG A 222 -9.213 -36.981 12.495 1.00 58.46 C ANISOU 2388 C ARG A 222 9406 4073 8732 1881 142 -1250 C ATOM 2389 O ARG A 222 -9.189 -35.745 12.529 1.00 57.11 O ANISOU 2389 O ARG A 222 9118 4108 8472 1865 180 -1226 O ATOM 2390 CB ARG A 222 -7.106 -38.313 12.197 1.00 65.36 C ANISOU 2390 CB ARG A 222 10127 4787 9920 2239 233 -1372 C ATOM 2391 CG ARG A 222 -6.322 -37.240 11.471 1.00 68.01 C ANISOU 2391 CG ARG A 222 10251 5360 10229 2325 390 -1480 C ATOM 2392 CD ARG A 222 -5.434 -37.878 10.419 1.00 72.48 C ANISOU 2392 CD ARG A 222 10766 5879 10895 2461 548 -1669 C ATOM 2393 NE ARG A 222 -4.750 -39.051 10.953 1.00 81.50 N ANISOU 2393 NE ARG A 222 11929 6809 12229 2610 497 -1625 N ATOM 2394 CZ ARG A 222 -4.160 -39.980 10.206 1.00 88.24 C ANISOU 2394 CZ ARG A 222 12806 7532 13187 2722 604 -1770 C ATOM 2395 NH1 ARG A 222 -4.170 -39.879 8.883 1.00 88.77 N ANISOU 2395 NH1 ARG A 222 12874 7668 13186 2693 761 -1979 N ATOM 2396 NH2 ARG A 222 -3.563 -41.013 10.782 1.00 91.57 N ANISOU 2396 NH2 ARG A 222 13257 7760 13776 2863 547 -1709 N ATOM 2397 N SER A 223 -10.170 -37.659 11.855 1.00 62.36 N ANISOU 2397 N SER A 223 10091 4452 9151 1731 141 -1327 N ATOM 2398 CA SER A 223 -11.245 -36.967 11.150 1.00 57.13 C ANISOU 2398 CA SER A 223 9503 3909 8294 1537 182 -1384 C ATOM 2399 C SER A 223 -12.110 -36.156 12.107 1.00 56.26 C ANISOU 2399 C SER A 223 9374 3909 8094 1367 89 -1198 C ATOM 2400 O SER A 223 -12.546 -35.049 11.770 1.00 54.04 O ANISOU 2400 O SER A 223 8982 3874 7678 1247 144 -1191 O ATOM 2401 CB SER A 223 -12.096 -37.979 10.382 1.00 63.73 C ANISOU 2401 CB SER A 223 10531 4595 9090 1400 170 -1489 C ATOM 2402 OG SER A 223 -13.437 -37.534 10.266 1.00 67.71 O ANISOU 2402 OG SER A 223 11132 5159 9437 1160 126 -1455 O ATOM 2403 N THR A 224 -12.372 -36.691 13.302 1.00 55.27 N ANISOU 2403 N THR A 224 9317 3643 8039 1333 -46 -1031 N ATOM 2404 CA THR A 224 -13.151 -35.948 14.290 1.00 52.06 C ANISOU 2404 CA THR A 224 8843 3386 7549 1155 -118 -839 C ATOM 2405 C THR A 224 -12.389 -34.723 14.782 1.00 50.13 C ANISOU 2405 C THR A 224 8356 3392 7301 1242 -90 -764 C ATOM 2406 O THR A 224 -12.978 -33.652 14.971 1.00 46.33 O ANISOU 2406 O THR A 224 7768 3131 6702 1100 -76 -694 O ATOM 2407 CB THR A 224 -13.523 -36.863 15.458 1.00 50.88 C ANISOU 2407 CB THR A 224 8842 3018 7470 1105 -257 -678 C ATOM 2408 OG1 THR A 224 -14.365 -37.917 14.978 1.00 58.94 O ANISOU 2408 OG1 THR A 224 10089 3817 8488 982 -283 -745 O ATOM 2409 CG2 THR A 224 -14.269 -36.100 16.535 1.00 54.34 C ANISOU 2409 CG2 THR A 224 9211 3617 7817 932 -315 -483 C ATOM 2410 N LEU A 225 -11.076 -34.859 14.987 1.00 52.18 N ANISOU 2410 N LEU A 225 8518 3613 7695 1478 -84 -782 N ATOM 2411 CA LEU A 225 -10.269 -33.718 15.408 1.00 51.55 C ANISOU 2411 CA LEU A 225 8199 3763 7626 1562 -61 -724 C ATOM 2412 C LEU A 225 -10.229 -32.641 14.332 1.00 48.96 C ANISOU 2412 C LEU A 225 7738 3672 7194 1522 88 -843 C ATOM 2413 O LEU A 225 -10.304 -31.446 14.638 1.00 48.10 O ANISOU 2413 O LEU A 225 7475 3789 7010 1450 101 -768 O ATOM 2414 CB LEU A 225 -8.856 -34.180 15.761 1.00 57.33 C ANISOU 2414 CB LEU A 225 8845 4393 8543 1827 -90 -735 C ATOM 2415 CG LEU A 225 -8.597 -34.408 17.251 1.00 63.03 C ANISOU 2415 CG LEU A 225 9567 5040 9341 1875 -258 -540 C ATOM 2416 CD1 LEU A 225 -7.333 -35.220 17.474 1.00 67.32 C ANISOU 2416 CD1 LEU A 225 10072 5423 10085 2134 -306 -564 C ATOM 2417 CD2 LEU A 225 -8.509 -33.074 17.974 1.00 64.40 C ANISOU 2417 CD2 LEU A 225 9550 5477 9442 1810 -280 -423 C ATOM 2418 N GLN A 226 -10.117 -33.044 13.065 1.00 52.10 N ANISOU 2418 N GLN A 226 8205 4014 7578 1566 200 -1028 N ATOM 2419 CA GLN A 226 -10.064 -32.064 11.985 1.00 53.03 C ANISOU 2419 CA GLN A 226 8221 4347 7580 1527 344 -1138 C ATOM 2420 C GLN A 226 -11.379 -31.304 11.862 1.00 52.07 C ANISOU 2420 C GLN A 226 8133 4370 7281 1281 325 -1081 C ATOM 2421 O GLN A 226 -11.384 -30.107 11.552 1.00 44.52 O ANISOU 2421 O GLN A 226 7042 3641 6232 1227 392 -1074 O ATOM 2422 CB GLN A 226 -9.704 -32.755 10.671 1.00 53.74 C ANISOU 2422 CB GLN A 226 8411 4331 7675 1623 467 -1352 C ATOM 2423 CG GLN A 226 -8.244 -33.165 10.590 1.00 61.81 C ANISOU 2423 CG GLN A 226 9331 5285 8871 1887 536 -1435 C ATOM 2424 CD GLN A 226 -7.978 -34.209 9.520 1.00 71.57 C ANISOU 2424 CD GLN A 226 10689 6362 10141 1973 626 -1631 C ATOM 2425 OE1 GLN A 226 -8.883 -34.619 8.793 1.00 76.76 O ANISOU 2425 OE1 GLN A 226 11525 6958 10681 1835 631 -1712 O ATOM 2426 NE2 GLN A 226 -6.727 -34.648 9.424 1.00 73.96 N ANISOU 2426 NE2 GLN A 226 10847 6637 10616 2160 688 -1694 N ATOM 2427 N LYS A 227 -12.505 -31.977 12.110 1.00 54.21 N ANISOU 2427 N LYS A 227 8576 4508 7512 1131 231 -1037 N ATOM 2428 CA LYS A 227 -13.792 -31.292 12.059 1.00 48.40 C ANISOU 2428 CA LYS A 227 7853 3908 6629 902 203 -980 C ATOM 2429 C LYS A 227 -13.937 -30.307 13.210 1.00 46.48 C ANISOU 2429 C LYS A 227 7461 3830 6370 844 147 -803 C ATOM 2430 O LYS A 227 -14.509 -29.224 13.038 1.00 44.86 O ANISOU 2430 O LYS A 227 7169 3824 6052 727 171 -775 O ATOM 2431 CB LYS A 227 -14.928 -32.314 12.066 1.00 48.77 C ANISOU 2431 CB LYS A 227 8105 3766 6657 752 119 -980 C ATOM 2432 CG LYS A 227 -15.016 -33.101 10.773 1.00 56.50 C ANISOU 2432 CG LYS A 227 9243 4615 7611 764 173 -1174 C ATOM 2433 CD LYS A 227 -15.993 -34.253 10.866 1.00 63.64 C ANISOU 2433 CD LYS A 227 10356 5293 8531 629 78 -1176 C ATOM 2434 CE LYS A 227 -15.972 -35.062 9.580 1.00 70.81 C ANISOU 2434 CE LYS A 227 11432 6056 9415 657 128 -1386 C ATOM 2435 NZ LYS A 227 -16.800 -36.294 9.671 1.00 76.61 N ANISOU 2435 NZ LYS A 227 12382 6536 10190 536 30 -1399 N ATOM 2436 N GLU A 228 -13.423 -30.660 14.390 1.00 45.99 N ANISOU 2436 N GLU A 228 7377 3682 6414 930 65 -683 N ATOM 2437 CA GLU A 228 -13.437 -29.717 15.504 1.00 44.77 C ANISOU 2437 CA GLU A 228 7088 3684 6239 891 13 -527 C ATOM 2438 C GLU A 228 -12.572 -28.498 15.207 1.00 41.60 C ANISOU 2438 C GLU A 228 6482 3496 5827 978 95 -559 C ATOM 2439 O GLU A 228 -12.943 -27.369 15.547 1.00 41.25 O ANISOU 2439 O GLU A 228 6332 3641 5702 884 94 -486 O ATOM 2440 CB GLU A 228 -12.971 -30.405 16.786 1.00 52.63 C ANISOU 2440 CB GLU A 228 8121 4534 7341 976 -100 -397 C ATOM 2441 CG GLU A 228 -14.094 -31.026 17.593 1.00 62.20 C ANISOU 2441 CG GLU A 228 9489 5631 8515 813 -192 -276 C ATOM 2442 CD GLU A 228 -13.604 -31.645 18.886 1.00 65.10 C ANISOU 2442 CD GLU A 228 9907 5860 8966 896 -307 -133 C ATOM 2443 OE1 GLU A 228 -13.049 -32.764 18.837 1.00 65.14 O ANISOU 2443 OE1 GLU A 228 10023 5640 9086 1022 -348 -163 O ATOM 2444 OE2 GLU A 228 -13.763 -31.006 19.950 1.00 62.70 O ANISOU 2444 OE2 GLU A 228 9542 5670 8611 840 -361 7 O ATOM 2445 N VAL A 229 -11.408 -28.707 14.584 1.00 44.03 N ANISOU 2445 N VAL A 229 6730 3775 6225 1156 170 -669 N ATOM 2446 CA VAL A 229 -10.577 -27.580 14.169 1.00 43.79 C ANISOU 2446 CA VAL A 229 6506 3944 6189 1224 268 -710 C ATOM 2447 C VAL A 229 -11.323 -26.718 13.161 1.00 40.44 C ANISOU 2447 C VAL A 229 6082 3676 5606 1082 357 -773 C ATOM 2448 O VAL A 229 -11.321 -25.485 13.253 1.00 38.72 O ANISOU 2448 O VAL A 229 5733 3651 5327 1028 383 -725 O ATOM 2449 CB VAL A 229 -9.238 -28.078 13.595 1.00 46.37 C ANISOU 2449 CB VAL A 229 6770 4202 6647 1437 352 -832 C ATOM 2450 CG1 VAL A 229 -8.413 -26.903 13.083 1.00 45.77 C ANISOU 2450 CG1 VAL A 229 6491 4337 6561 1483 473 -877 C ATOM 2451 CG2 VAL A 229 -8.474 -28.846 14.642 1.00 48.74 C ANISOU 2451 CG2 VAL A 229 7052 4354 7112 1590 242 -757 C ATOM 2452 N HIS A 230 -11.979 -27.353 12.186 1.00 42.02 N ANISOU 2452 N HIS A 230 6440 3789 5738 1021 394 -882 N ATOM 2453 CA HIS A 230 -12.731 -26.607 11.182 1.00 45.21 C ANISOU 2453 CA HIS A 230 6864 4329 5983 888 459 -942 C ATOM 2454 C HIS A 230 -13.850 -25.793 11.822 1.00 40.98 C ANISOU 2454 C HIS A 230 6299 3913 5359 714 377 -814 C ATOM 2455 O HIS A 230 -14.089 -24.641 11.439 1.00 39.86 O ANISOU 2455 O HIS A 230 6074 3951 5121 646 419 -805 O ATOM 2456 CB HIS A 230 -13.291 -27.568 10.133 1.00 52.70 C ANISOU 2456 CB HIS A 230 8007 5140 6875 847 482 -1079 C ATOM 2457 CG HIS A 230 -13.875 -26.884 8.936 1.00 64.06 C ANISOU 2457 CG HIS A 230 9479 6712 8148 741 549 -1161 C ATOM 2458 ND1 HIS A 230 -15.224 -26.633 8.805 1.00 66.16 N ANISOU 2458 ND1 HIS A 230 9813 7022 8302 555 473 -1127 N ATOM 2459 CD2 HIS A 230 -13.291 -26.397 7.815 1.00 66.37 C ANISOU 2459 CD2 HIS A 230 9748 7103 8367 795 683 -1274 C ATOM 2460 CE1 HIS A 230 -15.447 -26.022 7.655 1.00 65.98 C ANISOU 2460 CE1 HIS A 230 9813 7115 8141 506 540 -1211 C ATOM 2461 NE2 HIS A 230 -14.290 -25.866 7.035 1.00 65.87 N ANISOU 2461 NE2 HIS A 230 9754 7135 8137 644 672 -1298 N ATOM 2462 N ALA A 231 -14.540 -26.369 12.809 1.00 37.04 N ANISOU 2462 N ALA A 231 5867 3312 4893 642 265 -713 N ATOM 2463 CA ALA A 231 -15.618 -25.644 13.474 1.00 39.14 C ANISOU 2463 CA ALA A 231 6097 3690 5082 482 200 -598 C ATOM 2464 C ALA A 231 -15.078 -24.500 14.326 1.00 37.56 C ANISOU 2464 C ALA A 231 5727 3649 4896 522 196 -496 C ATOM 2465 O ALA A 231 -15.694 -23.431 14.405 1.00 33.66 O ANISOU 2465 O ALA A 231 5159 3312 4317 423 196 -450 O ATOM 2466 CB ALA A 231 -16.448 -26.606 14.324 1.00 41.44 C ANISOU 2466 CB ALA A 231 6509 3831 5406 390 101 -516 C ATOM 2467 N ALA A 232 -13.933 -24.708 14.982 1.00 38.44 N ANISOU 2467 N ALA A 232 5773 3715 5118 669 183 -463 N ATOM 2468 CA ALA A 232 -13.340 -23.631 15.767 1.00 35.23 C ANISOU 2468 CA ALA A 232 5205 3454 4729 706 170 -379 C ATOM 2469 C ALA A 232 -12.834 -22.506 14.876 1.00 35.66 C ANISOU 2469 C ALA A 232 5136 3673 4741 727 274 -448 C ATOM 2470 O ALA A 232 -12.892 -21.333 15.266 1.00 34.75 O ANISOU 2470 O ALA A 232 4911 3708 4584 680 269 -386 O ATOM 2471 CB ALA A 232 -12.205 -24.170 16.637 1.00 31.08 C ANISOU 2471 CB ALA A 232 4636 2836 4338 862 113 -332 C ATOM 2472 N LYS A 233 -12.336 -22.836 13.681 1.00 33.92 N ANISOU 2472 N LYS A 233 4940 3421 4526 795 375 -577 N ATOM 2473 CA LYS A 233 -11.899 -21.792 12.762 1.00 35.25 C ANISOU 2473 CA LYS A 233 5012 3743 4637 798 488 -638 C ATOM 2474 C LYS A 233 -13.077 -20.964 12.267 1.00 34.96 C ANISOU 2474 C LYS A 233 5015 3818 4450 639 487 -625 C ATOM 2475 O LYS A 233 -12.964 -19.741 12.131 1.00 32.87 O ANISOU 2475 O LYS A 233 4650 3703 4135 604 524 -596 O ATOM 2476 CB LYS A 233 -11.134 -22.403 11.589 1.00 37.56 C ANISOU 2476 CB LYS A 233 5340 3975 4954 904 609 -784 C ATOM 2477 CG LYS A 233 -9.742 -22.861 11.972 1.00 48.05 C ANISOU 2477 CG LYS A 233 6563 5245 6449 1085 634 -805 C ATOM 2478 CD LYS A 233 -8.936 -23.339 10.779 1.00 53.94 C ANISOU 2478 CD LYS A 233 7320 5953 7220 1197 783 -961 C ATOM 2479 CE LYS A 233 -7.550 -23.775 11.226 1.00 58.07 C ANISOU 2479 CE LYS A 233 7708 6423 7933 1389 801 -979 C ATOM 2480 NZ LYS A 233 -6.778 -24.442 10.140 1.00 65.34 N ANISOU 2480 NZ LYS A 233 8648 7281 8897 1518 951 -1143 N ATOM 2481 N SER A 234 -14.213 -21.610 11.990 1.00 33.27 N ANISOU 2481 N SER A 234 4944 3526 4170 539 439 -644 N ATOM 2482 CA SER A 234 -15.411 -20.872 11.599 1.00 32.59 C ANISOU 2482 CA SER A 234 4885 3542 3956 391 414 -626 C ATOM 2483 C SER A 234 -15.840 -19.905 12.695 1.00 33.06 C ANISOU 2483 C SER A 234 4839 3708 4012 329 349 -498 C ATOM 2484 O SER A 234 -16.169 -18.744 12.424 1.00 33.45 O ANISOU 2484 O SER A 234 4826 3895 3987 272 365 -477 O ATOM 2485 CB SER A 234 -16.543 -21.844 11.270 1.00 32.37 C ANISOU 2485 CB SER A 234 5012 3402 3886 292 355 -665 C ATOM 2486 OG SER A 234 -16.195 -22.671 10.178 1.00 36.12 O ANISOU 2486 OG SER A 234 5600 3779 4346 344 416 -798 O ATOM 2487 N ALA A 235 -15.844 -20.370 13.946 1.00 28.98 N ANISOU 2487 N ALA A 235 4315 3125 3572 342 275 -412 N ATOM 2488 CA ALA A 235 -16.205 -19.494 15.056 1.00 29.48 C ANISOU 2488 CA ALA A 235 4291 3287 3624 290 220 -300 C ATOM 2489 C ALA A 235 -15.212 -18.344 15.200 1.00 31.24 C ANISOU 2489 C ALA A 235 4371 3630 3868 360 260 -282 C ATOM 2490 O ALA A 235 -15.610 -17.197 15.440 1.00 27.77 O ANISOU 2490 O ALA A 235 3863 3314 3376 300 252 -236 O ATOM 2491 CB ALA A 235 -16.290 -20.300 16.351 1.00 27.53 C ANISOU 2491 CB ALA A 235 4085 2936 3440 295 139 -212 C ATOM 2492 N ALA A 236 -13.915 -18.631 15.050 1.00 31.36 N ANISOU 2492 N ALA A 236 4336 3608 3970 488 304 -323 N ATOM 2493 CA ALA A 236 -12.905 -17.589 15.209 1.00 31.29 C ANISOU 2493 CA ALA A 236 4179 3709 3999 547 341 -307 C ATOM 2494 C ALA A 236 -12.994 -16.548 14.098 1.00 26.23 C ANISOU 2494 C ALA A 236 3506 3186 3274 497 431 -356 C ATOM 2495 O ALA A 236 -12.690 -15.372 14.320 1.00 28.14 O ANISOU 2495 O ALA A 236 3644 3538 3510 480 442 -316 O ATOM 2496 CB ALA A 236 -11.508 -18.207 15.244 1.00 29.53 C ANISOU 2496 CB ALA A 236 3894 3421 3906 697 370 -347 C ATOM 2497 N ILE A 237 -13.360 -16.971 12.885 1.00 26.07 N ANISOU 2497 N ILE A 237 3585 3136 3185 474 494 -442 N ATOM 2498 CA ILE A 237 -13.576 -16.027 11.791 1.00 27.32 C ANISOU 2498 CA ILE A 237 3745 3398 3237 416 567 -478 C ATOM 2499 C ILE A 237 -14.675 -15.038 12.160 1.00 28.84 C ANISOU 2499 C ILE A 237 3928 3677 3352 304 496 -401 C ATOM 2500 O ILE A 237 -14.550 -13.829 11.933 1.00 28.98 O ANISOU 2500 O ILE A 237 3882 3799 3330 277 525 -375 O ATOM 2501 CB ILE A 237 -13.916 -16.785 10.493 1.00 30.59 C ANISOU 2501 CB ILE A 237 4298 3754 3572 403 624 -584 C ATOM 2502 CG1 ILE A 237 -12.682 -17.503 9.948 1.00 32.20 C ANISOU 2502 CG1 ILE A 237 4494 3897 3844 527 731 -678 C ATOM 2503 CG2 ILE A 237 -14.494 -15.838 9.447 1.00 30.44 C ANISOU 2503 CG2 ILE A 237 4319 3837 3409 317 659 -600 C ATOM 2504 CD1 ILE A 237 -12.991 -18.467 8.814 1.00 32.39 C ANISOU 2504 CD1 ILE A 237 4676 3834 3796 527 779 -796 C ATOM 2505 N ILE A 238 -15.771 -15.545 12.732 1.00 25.30 N ANISOU 2505 N ILE A 238 3542 3180 2888 239 405 -365 N ATOM 2506 CA ILE A 238 -16.880 -14.688 13.150 1.00 28.26 C ANISOU 2506 CA ILE A 238 3897 3635 3205 142 340 -300 C ATOM 2507 C ILE A 238 -16.419 -13.680 14.200 1.00 30.16 C ANISOU 2507 C ILE A 238 4019 3950 3490 164 321 -223 C ATOM 2508 O ILE A 238 -16.743 -12.486 14.131 1.00 25.51 O ANISOU 2508 O ILE A 238 3383 3456 2856 122 318 -194 O ATOM 2509 CB ILE A 238 -18.038 -15.552 13.680 1.00 33.23 C ANISOU 2509 CB ILE A 238 4598 4195 3832 70 262 -277 C ATOM 2510 CG1 ILE A 238 -18.593 -16.443 12.568 1.00 39.97 C ANISOU 2510 CG1 ILE A 238 5573 4978 4636 29 267 -361 C ATOM 2511 CG2 ILE A 238 -19.129 -14.682 14.273 1.00 27.60 C ANISOU 2511 CG2 ILE A 238 3836 3569 3080 -16 206 -210 C ATOM 2512 CD1 ILE A 238 -19.527 -15.730 11.653 1.00 42.58 C ANISOU 2512 CD1 ILE A 238 5925 5392 4863 -53 251 -383 C ATOM 2513 N ALA A 239 -15.679 -14.152 15.207 1.00 27.54 N ANISOU 2513 N ALA A 239 3648 3570 3248 230 295 -189 N ATOM 2514 CA ALA A 239 -15.149 -13.245 16.223 1.00 27.62 C ANISOU 2514 CA ALA A 239 3553 3646 3297 251 265 -126 C ATOM 2515 C ALA A 239 -14.164 -12.249 15.619 1.00 27.05 C ANISOU 2515 C ALA A 239 3390 3648 3241 285 335 -151 C ATOM 2516 O ALA A 239 -14.146 -11.071 15.998 1.00 24.75 O ANISOU 2516 O ALA A 239 3031 3437 2937 256 320 -112 O ATOM 2517 CB ALA A 239 -14.478 -14.041 17.342 1.00 25.40 C ANISOU 2517 CB ALA A 239 3257 3290 3101 321 209 -87 C ATOM 2518 N GLY A 240 -13.332 -12.705 14.681 1.00 25.84 N ANISOU 2518 N GLY A 240 3236 3467 3116 345 419 -219 N ATOM 2519 CA GLY A 240 -12.371 -11.807 14.063 1.00 29.44 C ANISOU 2519 CA GLY A 240 3603 3995 3589 365 505 -241 C ATOM 2520 C GLY A 240 -13.032 -10.746 13.204 1.00 27.05 C ANISOU 2520 C GLY A 240 3335 3768 3175 280 541 -239 C ATOM 2521 O GLY A 240 -12.564 -9.605 13.142 1.00 22.69 O ANISOU 2521 O GLY A 240 2708 3286 2627 260 572 -213 O ATOM 2522 N LEU A 241 -14.121 -11.109 12.517 1.00 22.24 N ANISOU 2522 N LEU A 241 2842 3138 2468 227 528 -263 N ATOM 2523 CA LEU A 241 -14.862 -10.134 11.722 1.00 23.98 C ANISOU 2523 CA LEU A 241 3107 3424 2580 152 535 -253 C ATOM 2524 C LEU A 241 -15.581 -9.125 12.611 1.00 23.29 C ANISOU 2524 C LEU A 241 2973 3387 2490 103 450 -178 C ATOM 2525 O LEU A 241 -15.713 -7.951 12.248 1.00 24.90 O ANISOU 2525 O LEU A 241 3163 3650 2648 67 460 -151 O ATOM 2526 CB LEU A 241 -15.855 -10.850 10.806 1.00 23.14 C ANISOU 2526 CB LEU A 241 3131 3282 2378 109 521 -302 C ATOM 2527 CG LEU A 241 -15.232 -11.612 9.632 1.00 30.89 C ANISOU 2527 CG LEU A 241 4188 4226 3323 147 620 -392 C ATOM 2528 CD1 LEU A 241 -16.290 -12.396 8.883 1.00 32.96 C ANISOU 2528 CD1 LEU A 241 4588 4441 3493 97 577 -446 C ATOM 2529 CD2 LEU A 241 -14.504 -10.658 8.692 1.00 34.29 C ANISOU 2529 CD2 LEU A 241 4604 4728 3695 144 727 -401 C ATOM 2530 N PHE A 242 -16.058 -9.558 13.776 1.00 22.23 N ANISOU 2530 N PHE A 242 2822 3225 2399 103 372 -144 N ATOM 2531 CA PHE A 242 -16.598 -8.597 14.728 1.00 23.78 C ANISOU 2531 CA PHE A 242 2968 3470 2597 70 308 -84 C ATOM 2532 C PHE A 242 -15.547 -7.551 15.084 1.00 23.29 C ANISOU 2532 C PHE A 242 2814 3452 2585 95 331 -61 C ATOM 2533 O PHE A 242 -15.814 -6.346 15.058 1.00 21.29 O ANISOU 2533 O PHE A 242 2539 3246 2303 61 320 -34 O ATOM 2534 CB PHE A 242 -17.101 -9.309 15.987 1.00 19.84 C ANISOU 2534 CB PHE A 242 2471 2936 2131 68 240 -52 C ATOM 2535 CG PHE A 242 -17.715 -8.370 16.998 1.00 19.46 C ANISOU 2535 CG PHE A 242 2380 2941 2072 37 187 -2 C ATOM 2536 CD1 PHE A 242 -16.924 -7.699 17.917 1.00 19.16 C ANISOU 2536 CD1 PHE A 242 2274 2927 2078 67 170 27 C ATOM 2537 CD2 PHE A 242 -19.086 -8.143 17.003 1.00 23.21 C ANISOU 2537 CD2 PHE A 242 2879 3444 2496 -22 154 7 C ATOM 2538 CE1 PHE A 242 -17.484 -6.805 18.841 1.00 24.30 C ANISOU 2538 CE1 PHE A 242 2898 3624 2710 42 127 59 C ATOM 2539 CE2 PHE A 242 -19.660 -7.259 17.930 1.00 21.70 C ANISOU 2539 CE2 PHE A 242 2644 3302 2297 -40 119 41 C ATOM 2540 CZ PHE A 242 -18.856 -6.590 18.849 1.00 22.55 C ANISOU 2540 CZ PHE A 242 2703 3428 2438 -7 109 64 C ATOM 2541 N ALA A 243 -14.338 -8.000 15.423 1.00 20.37 N ANISOU 2541 N ALA A 243 2385 3058 2299 156 357 -72 N ATOM 2542 CA ALA A 243 -13.277 -7.059 15.770 1.00 24.40 C ANISOU 2542 CA ALA A 243 2791 3608 2871 171 372 -54 C ATOM 2543 C ALA A 243 -12.945 -6.136 14.600 1.00 21.65 C ANISOU 2543 C ALA A 243 2437 3302 2485 136 459 -67 C ATOM 2544 O ALA A 243 -12.738 -4.933 14.788 1.00 22.11 O ANISOU 2544 O ALA A 243 2449 3399 2552 101 452 -36 O ATOM 2545 CB ALA A 243 -12.037 -7.826 16.224 1.00 22.91 C ANISOU 2545 CB ALA A 243 2527 3387 2790 249 380 -70 C ATOM 2546 N ALEU A 244 -12.895 -6.688 13.386 0.60 22.25 N ANISOU 2546 N ALEU A 244 2575 3365 2514 141 541 -113 N ATOM 2547 N BLEU A 244 -12.900 -6.674 13.380 0.40 22.22 N ANISOU 2547 N BLEU A 244 2572 3362 2510 141 541 -113 N ATOM 2548 CA ALEU A 244 -12.550 -5.894 12.211 0.60 23.34 C ANISOU 2548 CA ALEU A 244 2729 3543 2596 104 635 -121 C ATOM 2549 CA BLEU A 244 -12.534 -5.846 12.234 0.40 23.12 C ANISOU 2549 CA BLEU A 244 2698 3516 2571 103 635 -119 C ATOM 2550 C ALEU A 244 -13.588 -4.809 11.943 0.60 22.95 C ANISOU 2550 C ALEU A 244 2743 3520 2455 35 587 -76 C ATOM 2551 C BLEU A 244 -13.594 -4.792 11.936 0.40 22.70 C ANISOU 2551 C BLEU A 244 2712 3489 2423 34 587 -76 C ATOM 2552 O ALEU A 244 -13.235 -3.677 11.594 0.60 21.51 O ANISOU 2552 O ALEU A 244 2543 3368 2260 -4 623 -45 O ATOM 2553 O BLEU A 244 -13.263 -3.665 11.550 0.40 21.82 O ANISOU 2553 O BLEU A 244 2587 3409 2296 -6 624 -45 O ATOM 2554 CB ALEU A 244 -12.408 -6.809 10.994 0.60 23.05 C ANISOU 2554 CB ALEU A 244 2772 3485 2502 125 729 -187 C ATOM 2555 CB BLEU A 244 -12.294 -6.717 11.003 0.40 23.38 C ANISOU 2555 CB BLEU A 244 2802 3531 2550 125 736 -185 C ATOM 2556 CG ALEU A 244 -12.043 -6.190 9.642 0.60 25.55 C ANISOU 2556 CG ALEU A 244 3134 3841 2732 85 847 -200 C ATOM 2557 CG BLEU A 244 -10.891 -7.312 10.893 0.40 25.69 C ANISOU 2557 CG BLEU A 244 3004 3816 2942 194 837 -233 C ATOM 2558 CD1ALEU A 244 -10.627 -5.634 9.660 0.60 24.86 C ANISOU 2558 CD1ALEU A 244 2920 3789 2736 96 949 -197 C ATOM 2559 CD1BLEU A 244 -10.695 -7.973 9.539 0.40 26.47 C ANISOU 2559 CD1BLEU A 244 3189 3904 2964 210 959 -308 C ATOM 2560 CD2ALEU A 244 -12.203 -7.224 8.531 0.60 28.88 C ANISOU 2560 CD2ALEU A 244 3671 4236 3067 105 917 -277 C ATOM 2561 CD2BLEU A 244 -9.839 -6.239 11.132 0.40 25.42 C ANISOU 2561 CD2BLEU A 244 2838 3834 2987 176 884 -200 C ATOM 2562 N CYS A 245 -14.872 -5.136 12.096 1.00 20.67 N ANISOU 2562 N CYS A 245 2526 3217 2111 19 504 -71 N ATOM 2563 CA CYS A 245 -15.929 -4.183 11.773 1.00 22.19 C ANISOU 2563 CA CYS A 245 2772 3433 2225 -31 450 -35 C ATOM 2564 C CYS A 245 -16.108 -3.112 12.846 1.00 22.91 C ANISOU 2564 C CYS A 245 2797 3541 2367 -40 385 13 C ATOM 2565 O CYS A 245 -16.523 -1.990 12.529 1.00 22.94 O ANISOU 2565 O CYS A 245 2826 3559 2333 -71 363 46 O ATOM 2566 CB CYS A 245 -17.245 -4.930 11.547 1.00 21.16 C ANISOU 2566 CB CYS A 245 2719 3289 2033 -46 383 -55 C ATOM 2567 SG CYS A 245 -17.239 -5.959 10.051 1.00 28.85 S ANISOU 2567 SG CYS A 245 3809 4239 2912 -52 445 -120 S ATOM 2568 N TRP A 246 -15.797 -3.423 14.104 1.00 19.09 N ANISOU 2568 N TRP A 246 2242 3049 1963 -11 349 15 N ATOM 2569 CA TRP A 246 -16.015 -2.483 15.198 1.00 17.92 C ANISOU 2569 CA TRP A 246 2045 2913 1849 -18 284 48 C ATOM 2570 C TRP A 246 -14.778 -1.685 15.580 1.00 20.39 C ANISOU 2570 C TRP A 246 2281 3233 2233 -19 307 60 C ATOM 2571 O TRP A 246 -14.916 -0.591 16.131 1.00 18.12 O ANISOU 2571 O TRP A 246 1976 2951 1959 -39 265 81 O ATOM 2572 CB TRP A 246 -16.525 -3.222 16.441 1.00 19.57 C ANISOU 2572 CB TRP A 246 2240 3115 2082 3 222 48 C ATOM 2573 CG TRP A 246 -17.979 -3.578 16.332 1.00 23.19 C ANISOU 2573 CG TRP A 246 2753 3577 2483 -18 183 46 C ATOM 2574 CD1 TRP A 246 -18.513 -4.772 15.944 1.00 22.17 C ANISOU 2574 CD1 TRP A 246 2671 3425 2328 -24 185 25 C ATOM 2575 CD2 TRP A 246 -19.082 -2.706 16.592 1.00 20.01 C ANISOU 2575 CD2 TRP A 246 2352 3200 2052 -37 135 61 C ATOM 2576 NE1 TRP A 246 -19.893 -4.699 15.957 1.00 22.03 N ANISOU 2576 NE1 TRP A 246 2674 3425 2272 -56 139 29 N ATOM 2577 CE2 TRP A 246 -20.263 -3.439 16.354 1.00 20.94 C ANISOU 2577 CE2 TRP A 246 2502 3320 2134 -58 110 51 C ATOM 2578 CE3 TRP A 246 -19.184 -1.371 17.003 1.00 16.40 C ANISOU 2578 CE3 TRP A 246 1869 2757 1606 -37 110 78 C ATOM 2579 CZ2 TRP A 246 -21.534 -2.880 16.520 1.00 20.26 C ANISOU 2579 CZ2 TRP A 246 2404 3263 2030 -72 64 57 C ATOM 2580 CZ3 TRP A 246 -20.446 -0.818 17.170 1.00 17.10 C ANISOU 2580 CZ3 TRP A 246 1961 2865 1672 -41 66 81 C ATOM 2581 CH2 TRP A 246 -21.605 -1.571 16.926 1.00 18.85 C ANISOU 2581 CH2 TRP A 246 2197 3101 1866 -56 45 70 C ATOM 2582 N LEU A 247 -13.581 -2.210 15.334 1.00 22.11 N ANISOU 2582 N LEU A 247 2446 3448 2507 3 370 40 N ATOM 2583 CA LEU A 247 -12.373 -1.501 15.750 1.00 25.75 C ANISOU 2583 CA LEU A 247 2810 3921 3055 -6 384 48 C ATOM 2584 C LEU A 247 -12.224 -0.101 15.156 1.00 24.52 C ANISOU 2584 C LEU A 247 2663 3773 2882 -68 417 76 C ATOM 2585 O LEU A 247 -11.768 0.794 15.889 1.00 23.60 O ANISOU 2585 O LEU A 247 2488 3654 2825 -92 377 91 O ATOM 2586 CB LEU A 247 -11.135 -2.350 15.431 1.00 28.03 C ANISOU 2586 CB LEU A 247 3023 4210 3416 35 458 17 C ATOM 2587 CG LEU A 247 -10.761 -3.347 16.533 1.00 32.32 C ANISOU 2587 CG LEU A 247 3512 4735 4034 101 392 5 C ATOM 2588 CD1 LEU A 247 -9.662 -4.302 16.066 1.00 33.77 C ANISOU 2588 CD1 LEU A 247 3628 4910 4295 160 467 -34 C ATOM 2589 CD2 LEU A 247 -10.346 -2.602 17.795 1.00 30.42 C ANISOU 2589 CD2 LEU A 247 3198 4506 3854 90 300 28 C ATOM 2590 N PRO A 248 -12.551 0.168 13.880 1.00 23.20 N ANISOU 2590 N PRO A 248 2574 3606 2634 -100 483 86 N ATOM 2591 CA PRO A 248 -12.383 1.549 13.382 1.00 21.07 C ANISOU 2591 CA PRO A 248 2326 3330 2349 -164 507 127 C ATOM 2592 C PRO A 248 -13.133 2.593 14.197 1.00 18.97 C ANISOU 2592 C PRO A 248 2081 3041 2088 -177 403 153 C ATOM 2593 O PRO A 248 -12.567 3.650 14.486 1.00 22.58 O ANISOU 2593 O PRO A 248 2503 3479 2598 -219 397 174 O ATOM 2594 CB PRO A 248 -12.892 1.457 11.937 1.00 19.13 C ANISOU 2594 CB PRO A 248 2195 3087 1986 -185 569 138 C ATOM 2595 CG PRO A 248 -12.548 0.047 11.536 1.00 18.30 C ANISOU 2595 CG PRO A 248 2082 2999 1874 -142 635 86 C ATOM 2596 CD PRO A 248 -12.868 -0.761 12.777 1.00 22.45 C ANISOU 2596 CD PRO A 248 2555 3514 2460 -86 546 61 C ATOM 2597 N LEU A 249 -14.380 2.322 14.595 1.00 20.64 N ANISOU 2597 N LEU A 249 2341 3249 2252 -143 326 147 N ATOM 2598 CA LEU A 249 -15.100 3.264 15.452 1.00 24.85 C ANISOU 2598 CA LEU A 249 2884 3763 2796 -140 239 158 C ATOM 2599 C LEU A 249 -14.351 3.503 16.759 1.00 21.52 C ANISOU 2599 C LEU A 249 2380 3338 2458 -138 200 140 C ATOM 2600 O LEU A 249 -14.184 4.648 17.195 1.00 19.09 O ANISOU 2600 O LEU A 249 2068 3002 2184 -165 165 148 O ATOM 2601 CB LEU A 249 -16.503 2.741 15.758 1.00 18.67 C ANISOU 2601 CB LEU A 249 2139 2993 1963 -102 179 144 C ATOM 2602 CG LEU A 249 -17.643 3.076 14.797 1.00 21.43 C ANISOU 2602 CG LEU A 249 2569 3335 2238 -103 156 164 C ATOM 2603 CD1 LEU A 249 -18.867 2.252 15.167 1.00 21.07 C ANISOU 2603 CD1 LEU A 249 2524 3315 2167 -72 108 141 C ATOM 2604 CD2 LEU A 249 -17.951 4.561 14.846 1.00 19.44 C ANISOU 2604 CD2 LEU A 249 2345 3045 1996 -111 113 193 C ATOM 2605 N HIS A 250 -13.928 2.422 17.420 1.00 20.47 N ANISOU 2605 N HIS A 250 2192 3229 2358 -104 194 116 N ATOM 2606 CA HIS A 250 -13.257 2.564 18.707 1.00 20.96 C ANISOU 2606 CA HIS A 250 2185 3292 2485 -97 136 101 C ATOM 2607 C HIS A 250 -11.932 3.296 18.559 1.00 18.57 C ANISOU 2607 C HIS A 250 1808 2981 2265 -144 162 105 C ATOM 2608 O HIS A 250 -11.552 4.090 19.427 1.00 19.88 O ANISOU 2608 O HIS A 250 1942 3133 2477 -167 100 97 O ATOM 2609 CB HIS A 250 -13.050 1.189 19.334 1.00 21.44 C ANISOU 2609 CB HIS A 250 2215 3371 2560 -48 118 86 C ATOM 2610 CG HIS A 250 -14.319 0.545 19.801 1.00 18.67 C ANISOU 2610 CG HIS A 250 1928 3025 2140 -20 83 84 C ATOM 2611 ND1 HIS A 250 -15.070 1.057 20.837 1.00 19.13 N ANISOU 2611 ND1 HIS A 250 2012 3088 2168 -18 21 79 N ATOM 2612 CD2 HIS A 250 -14.962 -0.572 19.380 1.00 18.26 C ANISOU 2612 CD2 HIS A 250 1916 2974 2047 1 106 82 C ATOM 2613 CE1 HIS A 250 -16.126 0.287 21.031 1.00 19.69 C ANISOU 2613 CE1 HIS A 250 2127 3170 2186 -2 17 80 C ATOM 2614 NE2 HIS A 250 -16.084 -0.709 20.160 1.00 19.78 N ANISOU 2614 NE2 HIS A 250 2147 3175 2192 6 61 84 N ATOM 2615 N ILE A 251 -11.212 3.037 17.467 1.00 19.25 N ANISOU 2615 N ILE A 251 1866 3078 2371 -163 258 113 N ATOM 2616 CA ILE A 251 -9.939 3.712 17.229 1.00 17.78 C ANISOU 2616 CA ILE A 251 1593 2891 2272 -220 304 120 C ATOM 2617 C ILE A 251 -10.161 5.201 16.994 1.00 18.86 C ANISOU 2617 C ILE A 251 1784 2985 2396 -292 294 150 C ATOM 2618 O ILE A 251 -9.408 6.045 17.495 1.00 18.85 O ANISOU 2618 O ILE A 251 1724 2965 2475 -345 264 149 O ATOM 2619 CB ILE A 251 -9.211 3.042 16.049 1.00 21.39 C ANISOU 2619 CB ILE A 251 2013 3376 2740 -222 433 117 C ATOM 2620 CG1 ILE A 251 -8.771 1.630 16.456 1.00 26.02 C ANISOU 2620 CG1 ILE A 251 2529 3987 3372 -143 429 81 C ATOM 2621 CG2 ILE A 251 -8.007 3.866 15.594 1.00 22.87 C ANISOU 2621 CG2 ILE A 251 2114 3567 3008 -301 510 131 C ATOM 2622 CD1 ILE A 251 -8.307 0.768 15.284 1.00 29.35 C ANISOU 2622 CD1 ILE A 251 2939 4428 3786 -120 559 60 C ATOM 2623 N ILE A 252 -11.193 5.550 16.225 1.00 17.91 N ANISOU 2623 N ILE A 252 1780 2842 2182 -294 310 177 N ATOM 2624 CA ILE A 252 -11.519 6.957 16.013 1.00 21.95 C ANISOU 2624 CA ILE A 252 2361 3295 2682 -348 286 211 C ATOM 2625 C ILE A 252 -11.826 7.632 17.346 1.00 20.22 C ANISOU 2625 C ILE A 252 2138 3044 2501 -335 174 184 C ATOM 2626 O ILE A 252 -11.365 8.743 17.616 1.00 19.34 O ANISOU 2626 O ILE A 252 2023 2882 2445 -393 148 190 O ATOM 2627 CB ILE A 252 -12.696 7.097 15.031 1.00 23.57 C ANISOU 2627 CB ILE A 252 2693 3483 2778 -331 295 245 C ATOM 2628 CG1 ILE A 252 -12.268 6.702 13.616 1.00 25.20 C ANISOU 2628 CG1 ILE A 252 2931 3713 2932 -364 411 275 C ATOM 2629 CG2 ILE A 252 -13.226 8.527 15.036 1.00 18.78 C ANISOU 2629 CG2 ILE A 252 2167 2802 2167 -359 239 278 C ATOM 2630 CD1 ILE A 252 -13.452 6.481 12.677 1.00 22.81 C ANISOU 2630 CD1 ILE A 252 2751 3409 2507 -335 401 297 C ATOM 2631 N ASN A 253 -12.623 6.974 18.195 1.00 19.43 N ANISOU 2631 N ASN A 253 2045 2969 2367 -264 112 150 N ATOM 2632 CA ASN A 253 -12.920 7.546 19.506 1.00 22.85 C ANISOU 2632 CA ASN A 253 2484 3381 2817 -249 18 115 C ATOM 2633 C ASN A 253 -11.645 7.758 20.313 1.00 21.84 C ANISOU 2633 C ASN A 253 2267 3253 2778 -290 -18 91 C ATOM 2634 O ASN A 253 -11.517 8.753 21.034 1.00 22.11 O ANISOU 2634 O ASN A 253 2316 3243 2843 -320 -83 68 O ATOM 2635 CB ASN A 253 -13.902 6.655 20.272 1.00 17.94 C ANISOU 2635 CB ASN A 253 1881 2799 2137 -176 -21 87 C ATOM 2636 CG ASN A 253 -15.339 6.811 19.779 1.00 18.05 C ANISOU 2636 CG ASN A 253 1973 2805 2082 -139 -19 97 C ATOM 2637 OD1 ASN A 253 -15.664 7.768 19.081 1.00 22.59 O ANISOU 2637 OD1 ASN A 253 2600 3331 2651 -157 -15 121 O ATOM 2638 ND2 ASN A 253 -16.204 5.872 20.152 1.00 18.78 N ANISOU 2638 ND2 ASN A 253 2070 2940 2126 -91 -27 82 N ATOM 2639 N CYS A 254 -10.678 6.847 20.181 1.00 19.56 N ANISOU 2639 N CYS A 254 1883 3011 2537 -290 18 92 N ATOM 2640 CA CYS A 254 -9.403 7.030 20.866 1.00 21.84 C ANISOU 2640 CA CYS A 254 2066 3307 2926 -330 -26 71 C ATOM 2641 C CYS A 254 -8.679 8.287 20.376 1.00 20.81 C ANISOU 2641 C CYS A 254 1913 3127 2866 -430 1 88 C ATOM 2642 O CYS A 254 -8.055 9.001 21.170 1.00 21.05 O ANISOU 2642 O CYS A 254 1901 3132 2965 -479 -75 62 O ATOM 2643 CB CYS A 254 -8.527 5.787 20.681 1.00 22.18 C ANISOU 2643 CB CYS A 254 2000 3406 3021 -296 14 69 C ATOM 2644 SG CYS A 254 -9.016 4.324 21.643 1.00 22.59 S ANISOU 2644 SG CYS A 254 2065 3495 3022 -193 -54 51 S ATOM 2645 N PHE A 255 -8.736 8.572 19.070 1.00 20.95 N ANISOU 2645 N PHE A 255 1967 3129 2865 -469 106 133 N ATOM 2646 CA PHE A 255 -8.119 9.797 18.559 1.00 21.13 C ANISOU 2646 CA PHE A 255 1989 3094 2945 -577 141 163 C ATOM 2647 C PHE A 255 -8.851 11.036 19.069 1.00 24.44 C ANISOU 2647 C PHE A 255 2518 3425 3343 -595 55 157 C ATOM 2648 O PHE A 255 -8.226 12.005 19.514 1.00 25.83 O ANISOU 2648 O PHE A 255 2672 3545 3597 -674 8 144 O ATOM 2649 CB PHE A 255 -8.092 9.790 17.028 1.00 21.56 C ANISOU 2649 CB PHE A 255 2085 3151 2956 -614 277 221 C ATOM 2650 CG PHE A 255 -6.889 9.097 16.443 1.00 22.96 C ANISOU 2650 CG PHE A 255 2130 3393 3200 -645 389 222 C ATOM 2651 CD1 PHE A 255 -5.715 9.794 16.232 1.00 24.48 C ANISOU 2651 CD1 PHE A 255 2228 3576 3499 -756 442 237 C ATOM 2652 CD2 PHE A 255 -6.940 7.744 16.121 1.00 23.52 C ANISOU 2652 CD2 PHE A 255 2168 3533 3236 -563 443 203 C ATOM 2653 CE1 PHE A 255 -4.604 9.161 15.704 1.00 30.63 C ANISOU 2653 CE1 PHE A 255 2864 4422 4351 -778 557 231 C ATOM 2654 CE2 PHE A 255 -5.831 7.102 15.589 1.00 23.96 C ANISOU 2654 CE2 PHE A 255 2098 3646 3361 -576 553 192 C ATOM 2655 CZ PHE A 255 -4.664 7.810 15.380 1.00 26.61 C ANISOU 2655 CZ PHE A 255 2324 3982 3806 -680 615 205 C ATOM 2656 N THR A 256 -10.181 11.025 18.994 1.00 21.26 N ANISOU 2656 N THR A 256 2230 3004 2844 -522 32 160 N ATOM 2657 CA THR A 256 -10.968 12.132 19.526 1.00 24.00 C ANISOU 2657 CA THR A 256 2677 3267 3175 -513 -48 143 C ATOM 2658 C THR A 256 -10.627 12.398 20.988 1.00 23.77 C ANISOU 2658 C THR A 256 2610 3229 3192 -514 -151 72 C ATOM 2659 O THR A 256 -10.466 13.553 21.399 1.00 25.54 O ANISOU 2659 O THR A 256 2877 3368 3460 -565 -207 51 O ATOM 2660 CB THR A 256 -12.458 11.816 19.370 1.00 26.14 C ANISOU 2660 CB THR A 256 3037 3548 3348 -415 -60 144 C ATOM 2661 OG1 THR A 256 -12.767 11.621 17.981 1.00 26.87 O ANISOU 2661 OG1 THR A 256 3177 3645 3389 -420 17 208 O ATOM 2662 CG2 THR A 256 -13.325 12.934 19.955 1.00 26.05 C ANISOU 2662 CG2 THR A 256 3118 3450 3330 -385 -137 114 C ATOM 2663 N PHE A 257 -10.490 11.332 21.781 1.00 21.27 N ANISOU 2663 N PHE A 257 2228 2994 2861 -461 -182 36 N ATOM 2664 CA PHE A 257 -10.293 11.444 23.224 1.00 20.29 C ANISOU 2664 CA PHE A 257 2090 2873 2746 -450 -289 -30 C ATOM 2665 C PHE A 257 -8.849 11.779 23.585 1.00 24.02 C ANISOU 2665 C PHE A 257 2460 3340 3329 -539 -334 -46 C ATOM 2666 O PHE A 257 -8.593 12.725 24.341 1.00 25.89 O ANISOU 2666 O PHE A 257 2722 3516 3598 -588 -419 -92 O ATOM 2667 CB PHE A 257 -10.721 10.137 23.892 1.00 22.15 C ANISOU 2667 CB PHE A 257 2309 3194 2914 -362 -307 -48 C ATOM 2668 CG PHE A 257 -10.601 10.150 25.383 1.00 24.97 C ANISOU 2668 CG PHE A 257 2675 3563 3249 -346 -415 -109 C ATOM 2669 CD1 PHE A 257 -11.368 11.020 26.148 1.00 23.99 C ANISOU 2669 CD1 PHE A 257 2652 3390 3072 -330 -466 -162 C ATOM 2670 CD2 PHE A 257 -9.733 9.279 26.023 1.00 24.79 C ANISOU 2670 CD2 PHE A 257 2568 3599 3252 -340 -469 -115 C ATOM 2671 CE1 PHE A 257 -11.260 11.031 27.533 1.00 26.19 C ANISOU 2671 CE1 PHE A 257 2958 3684 3308 -317 -562 -223 C ATOM 2672 CE2 PHE A 257 -9.625 9.278 27.401 1.00 29.92 C ANISOU 2672 CE2 PHE A 257 3246 4262 3862 -327 -580 -165 C ATOM 2673 CZ PHE A 257 -10.392 10.162 28.160 1.00 28.92 C ANISOU 2673 CZ PHE A 257 3232 4092 3666 -320 -623 -221 C ATOM 2674 N PHE A 258 -7.890 11.010 23.064 1.00 24.56 N ANISOU 2674 N PHE A 258 2404 3468 3460 -562 -281 -17 N ATOM 2675 CA PHE A 258 -6.498 11.156 23.480 1.00 22.88 C ANISOU 2675 CA PHE A 258 2058 3269 3367 -636 -332 -36 C ATOM 2676 C PHE A 258 -5.746 12.254 22.737 1.00 27.41 C ANISOU 2676 C PHE A 258 2596 3780 4038 -765 -281 -9 C ATOM 2677 O PHE A 258 -4.678 12.673 23.204 1.00 26.08 O ANISOU 2677 O PHE A 258 2325 3604 3980 -848 -343 -35 O ATOM 2678 CB PHE A 258 -5.741 9.841 23.291 1.00 23.55 C ANISOU 2678 CB PHE A 258 2005 3446 3498 -594 -296 -23 C ATOM 2679 CG PHE A 258 -6.163 8.755 24.234 1.00 27.44 C ANISOU 2679 CG PHE A 258 2515 3990 3920 -488 -372 -46 C ATOM 2680 CD1 PHE A 258 -6.043 8.925 25.611 1.00 29.90 C ANISOU 2680 CD1 PHE A 258 2842 4300 4217 -481 -517 -94 C ATOM 2681 CD2 PHE A 258 -6.652 7.548 23.746 1.00 21.31 C ANISOU 2681 CD2 PHE A 258 1749 3260 3086 -403 -300 -19 C ATOM 2682 CE1 PHE A 258 -6.422 7.917 26.487 1.00 28.19 C ANISOU 2682 CE1 PHE A 258 2659 4130 3923 -392 -584 -104 C ATOM 2683 CE2 PHE A 258 -7.031 6.533 24.614 1.00 24.61 C ANISOU 2683 CE2 PHE A 258 2193 3715 3442 -317 -367 -31 C ATOM 2684 CZ PHE A 258 -6.918 6.721 25.989 1.00 25.94 C ANISOU 2684 CZ PHE A 258 2383 3883 3589 -312 -506 -68 C ATOM 2685 N CYS A 259 -6.241 12.718 21.587 1.00 26.48 N ANISOU 2685 N CYS A 259 2560 3616 3886 -790 -176 46 N ATOM 2686 CA CYS A 259 -5.569 13.768 20.819 1.00 31.19 C ANISOU 2686 CA CYS A 259 3145 4144 4562 -923 -115 87 C ATOM 2687 C CYS A 259 -6.521 14.942 20.603 1.00 34.59 C ANISOU 2687 C CYS A 259 3751 4453 4936 -938 -134 106 C ATOM 2688 O CYS A 259 -7.035 15.144 19.495 1.00 32.68 O ANISOU 2688 O CYS A 259 3597 4181 4639 -940 -44 172 O ATOM 2689 CB CYS A 259 -5.051 13.251 19.477 1.00 36.36 C ANISOU 2689 CB CYS A 259 3732 4852 5233 -956 46 151 C ATOM 2690 SG CYS A 259 -4.002 14.463 18.625 1.00 43.78 S ANISOU 2690 SG CYS A 259 4631 5721 6281 -1144 135 207 S ATOM 2691 N PRO A 260 -6.768 15.747 21.640 1.00 40.40 N ANISOU 2691 N PRO A 260 4551 5115 5683 -943 -256 46 N ATOM 2692 CA PRO A 260 -7.578 16.964 21.440 1.00 38.86 C ANISOU 2692 CA PRO A 260 4520 4786 5460 -955 -278 58 C ATOM 2693 C PRO A 260 -6.924 17.980 20.523 1.00 40.34 C ANISOU 2693 C PRO A 260 4727 4876 5723 -1097 -217 126 C ATOM 2694 O PRO A 260 -7.607 18.903 20.064 1.00 45.10 O ANISOU 2694 O PRO A 260 5476 5361 6297 -1102 -217 162 O ATOM 2695 CB PRO A 260 -7.745 17.515 22.864 1.00 40.42 C ANISOU 2695 CB PRO A 260 4761 4932 5664 -937 -419 -41 C ATOM 2696 CG PRO A 260 -6.591 16.938 23.636 1.00 43.20 C ANISOU 2696 CG PRO A 260 4959 5369 6088 -982 -476 -85 C ATOM 2697 CD PRO A 260 -6.367 15.575 23.048 1.00 38.62 C ANISOU 2697 CD PRO A 260 4267 4919 5488 -929 -385 -39 C ATOM 2698 N ASP A 261 -5.626 17.846 20.241 1.00 37.76 N ANISOU 2698 N ASP A 261 4257 4593 5499 -1213 -164 147 N ATOM 2699 CA ASP A 261 -4.963 18.698 19.263 1.00 41.79 C ANISOU 2699 CA ASP A 261 4776 5026 6077 -1364 -75 224 C ATOM 2700 C ASP A 261 -5.145 18.212 17.830 1.00 39.01 C ANISOU 2700 C ASP A 261 4450 4721 5650 -1356 84 320 C ATOM 2701 O ASP A 261 -4.748 18.922 16.900 1.00 40.75 O ANISOU 2701 O ASP A 261 4713 4875 5894 -1476 174 400 O ATOM 2702 CB ASP A 261 -3.466 18.797 19.572 1.00 49.27 C ANISOU 2702 CB ASP A 261 5538 6005 7176 -1503 -76 202 C ATOM 2703 CG ASP A 261 -3.187 19.447 20.914 1.00 58.61 C ANISOU 2703 CG ASP A 261 6712 7125 8434 -1541 -245 109 C ATOM 2704 OD1 ASP A 261 -4.070 20.169 21.424 1.00 60.59 O ANISOU 2704 OD1 ASP A 261 7126 7266 8629 -1495 -336 73 O ATOM 2705 OD2 ASP A 261 -2.079 19.242 21.456 1.00 61.58 O ANISOU 2705 OD2 ASP A 261 6914 7559 8925 -1615 -291 67 O ATOM 2706 N CYS A 262 -5.707 17.021 17.633 1.00 38.63 N ANISOU 2706 N CYS A 262 4385 4783 5508 -1226 121 313 N ATOM 2707 CA CYS A 262 -6.004 16.496 16.307 1.00 36.01 C ANISOU 2707 CA CYS A 262 4100 4498 5083 -1205 257 389 C ATOM 2708 C CYS A 262 -7.402 16.939 15.891 1.00 35.26 C ANISOU 2708 C CYS A 262 4204 4323 4869 -1127 220 428 C ATOM 2709 O CYS A 262 -8.341 16.866 16.691 1.00 32.53 O ANISOU 2709 O CYS A 262 3911 3965 4486 -1016 112 373 O ATOM 2710 CB CYS A 262 -5.931 14.966 16.294 1.00 39.06 C ANISOU 2710 CB CYS A 262 4375 5032 5434 -1105 305 355 C ATOM 2711 SG CYS A 262 -4.318 14.180 16.631 1.00 46.75 S ANISOU 2711 SG CYS A 262 5093 6118 6551 -1158 356 311 S ATOM 2712 N SER A 263 -7.539 17.390 14.644 1.00 34.04 N ANISOU 2712 N SER A 263 4159 4119 4654 -1183 309 524 N ATOM 2713 CA SER A 263 -8.867 17.622 14.088 1.00 36.86 C ANISOU 2713 CA SER A 263 4692 4420 4891 -1094 273 569 C ATOM 2714 C SER A 263 -9.715 16.364 14.213 1.00 31.37 C ANISOU 2714 C SER A 263 3972 3838 4108 -946 256 523 C ATOM 2715 O SER A 263 -9.229 15.247 14.019 1.00 30.74 O ANISOU 2715 O SER A 263 3784 3877 4017 -933 334 503 O ATOM 2716 CB SER A 263 -8.773 18.038 12.618 1.00 40.02 C ANISOU 2716 CB SER A 263 5210 4780 5218 -1177 381 687 C ATOM 2717 OG SER A 263 -8.464 19.414 12.493 1.00 50.19 O ANISOU 2717 OG SER A 263 6590 5916 6563 -1293 362 746 O ATOM 2718 N HIS A 264 -10.989 16.552 14.555 1.00 30.26 N ANISOU 2718 N HIS A 264 3926 3656 3916 -835 155 503 N ATOM 2719 CA HIS A 264 -11.907 15.427 14.664 1.00 26.85 C ANISOU 2719 CA HIS A 264 3476 3321 3404 -707 135 464 C ATOM 2720 C HIS A 264 -11.959 14.684 13.336 1.00 28.21 C ANISOU 2720 C HIS A 264 3681 3560 3476 -712 236 525 C ATOM 2721 O HIS A 264 -11.863 15.295 12.268 1.00 30.50 O ANISOU 2721 O HIS A 264 4075 3795 3719 -778 287 610 O ATOM 2722 CB HIS A 264 -13.302 15.927 15.047 1.00 28.50 C ANISOU 2722 CB HIS A 264 3783 3465 3580 -600 24 445 C ATOM 2723 CG HIS A 264 -14.207 14.867 15.596 1.00 27.22 C ANISOU 2723 CG HIS A 264 3572 3399 3370 -480 -11 382 C ATOM 2724 ND1 HIS A 264 -14.764 13.876 14.813 1.00 27.60 N ANISOU 2724 ND1 HIS A 264 3628 3529 3330 -433 27 405 N ATOM 2725 CD2 HIS A 264 -14.675 14.662 16.851 1.00 25.51 C ANISOU 2725 CD2 HIS A 264 3307 3206 3178 -407 -79 298 C ATOM 2726 CE1 HIS A 264 -15.524 13.099 15.565 1.00 26.26 C ANISOU 2726 CE1 HIS A 264 3408 3425 3145 -342 -15 342 C ATOM 2727 NE2 HIS A 264 -15.488 13.555 16.805 1.00 25.71 N ANISOU 2727 NE2 HIS A 264 3305 3325 3138 -324 -74 279 N ATOM 2728 N ALA A 265 -12.072 13.359 13.405 1.00 26.90 N ANISOU 2728 N ALA A 265 3439 3509 3273 -647 266 480 N ATOM 2729 CA ALA A 265 -12.321 12.582 12.201 1.00 26.34 C ANISOU 2729 CA ALA A 265 3418 3498 3092 -634 345 519 C ATOM 2730 C ALA A 265 -13.498 13.193 11.444 1.00 28.77 C ANISOU 2730 C ALA A 265 3886 3741 3304 -597 284 580 C ATOM 2731 O ALA A 265 -14.506 13.562 12.065 1.00 27.06 O ANISOU 2731 O ALA A 265 3700 3482 3101 -518 171 555 O ATOM 2732 CB ALA A 265 -12.617 11.121 12.555 1.00 25.84 C ANISOU 2732 CB ALA A 265 3273 3540 3004 -547 347 452 C ATOM 2733 N PRO A 266 -13.405 13.342 10.125 1.00 25.81 N ANISOU 2733 N PRO A 266 3617 3355 2833 -650 354 658 N ATOM 2734 CA PRO A 266 -14.468 14.030 9.386 1.00 28.39 C ANISOU 2734 CA PRO A 266 4106 3608 3072 -618 275 729 C ATOM 2735 C PRO A 266 -15.761 13.228 9.389 1.00 26.06 C ANISOU 2735 C PRO A 266 3821 3370 2712 -499 189 689 C ATOM 2736 O PRO A 266 -15.785 12.022 9.642 1.00 24.32 O ANISOU 2736 O PRO A 266 3511 3249 2482 -460 218 624 O ATOM 2737 CB PRO A 266 -13.893 14.170 7.971 1.00 28.94 C ANISOU 2737 CB PRO A 266 4285 3676 3035 -714 388 820 C ATOM 2738 CG PRO A 266 -12.894 13.083 7.857 1.00 31.51 C ANISOU 2738 CG PRO A 266 4493 4114 3365 -752 528 770 C ATOM 2739 CD PRO A 266 -12.325 12.872 9.241 1.00 26.25 C ANISOU 2739 CD PRO A 266 3652 3470 2853 -738 510 685 C ATOM 2740 N LEU A 267 -16.857 13.937 9.108 1.00 27.01 N ANISOU 2740 N LEU A 267 4048 3419 2797 -442 76 732 N ATOM 2741 CA LEU A 267 -18.182 13.338 9.238 1.00 29.27 C ANISOU 2741 CA LEU A 267 4321 3751 3049 -329 -24 691 C ATOM 2742 C LEU A 267 -18.370 12.163 8.282 1.00 28.66 C ANISOU 2742 C LEU A 267 4269 3770 2851 -330 19 691 C ATOM 2743 O LEU A 267 -19.004 11.163 8.641 1.00 24.68 O ANISOU 2743 O LEU A 267 3691 3342 2345 -268 -12 624 O ATOM 2744 CB LEU A 267 -19.262 14.395 9.005 1.00 36.15 C ANISOU 2744 CB LEU A 267 5296 4522 3917 -264 -156 742 C ATOM 2745 CG LEU A 267 -20.713 13.911 9.079 1.00 39.43 C ANISOU 2745 CG LEU A 267 5685 4983 4314 -148 -269 704 C ATOM 2746 CD1 LEU A 267 -21.054 13.426 10.483 1.00 36.96 C ANISOU 2746 CD1 LEU A 267 5219 4723 4100 -85 -281 597 C ATOM 2747 CD2 LEU A 267 -21.668 15.008 8.631 1.00 44.81 C ANISOU 2747 CD2 LEU A 267 6475 5560 4992 -83 -401 769 C ATOM 2748 N TRP A 268 -17.832 12.259 7.060 1.00 28.36 N ANISOU 2748 N TRP A 268 4345 3727 2705 -406 93 763 N ATOM 2749 CA TRP A 268 -17.977 11.140 6.131 1.00 30.67 C ANISOU 2749 CA TRP A 268 4676 4106 2869 -408 138 750 C ATOM 2750 C TRP A 268 -17.296 9.888 6.667 1.00 28.35 C ANISOU 2750 C TRP A 268 4246 3906 2621 -411 238 659 C ATOM 2751 O TRP A 268 -17.775 8.771 6.436 1.00 25.23 O ANISOU 2751 O TRP A 268 3838 3579 2169 -372 229 608 O ATOM 2752 CB TRP A 268 -17.427 11.497 4.744 1.00 27.55 C ANISOU 2752 CB TRP A 268 4441 3692 2336 -495 220 841 C ATOM 2753 CG TRP A 268 -15.933 11.721 4.671 1.00 29.54 C ANISOU 2753 CG TRP A 268 4660 3943 2620 -603 390 860 C ATOM 2754 CD1 TRP A 268 -15.283 12.919 4.708 1.00 32.40 C ANISOU 2754 CD1 TRP A 268 5061 4217 3034 -682 423 933 C ATOM 2755 CD2 TRP A 268 -14.913 10.720 4.523 1.00 30.94 C ANISOU 2755 CD2 TRP A 268 4752 4211 2791 -645 550 802 C ATOM 2756 NE1 TRP A 268 -13.927 12.730 4.604 1.00 30.81 N ANISOU 2756 NE1 TRP A 268 4790 4054 2863 -779 595 925 N ATOM 2757 CE2 TRP A 268 -13.673 11.390 4.490 1.00 33.14 C ANISOU 2757 CE2 TRP A 268 5004 4461 3127 -750 677 844 C ATOM 2758 CE3 TRP A 268 -14.927 9.324 4.421 1.00 31.92 C ANISOU 2758 CE3 TRP A 268 4820 4431 2879 -602 598 717 C ATOM 2759 CZ2 TRP A 268 -12.463 10.715 4.360 1.00 31.32 C ANISOU 2759 CZ2 TRP A 268 4673 4305 2922 -804 850 801 C ATOM 2760 CZ3 TRP A 268 -13.724 8.656 4.295 1.00 34.41 C ANISOU 2760 CZ3 TRP A 268 5052 4807 3216 -647 766 673 C ATOM 2761 CH2 TRP A 268 -12.509 9.353 4.263 1.00 34.98 C ANISOU 2761 CH2 TRP A 268 5082 4861 3350 -743 892 714 C ATOM 2762 N LEU A 269 -16.191 10.053 7.398 1.00 27.22 N ANISOU 2762 N LEU A 269 3999 3758 2585 -455 322 637 N ATOM 2763 CA LEU A 269 -15.494 8.900 7.958 1.00 23.84 C ANISOU 2763 CA LEU A 269 3437 3409 2214 -446 404 555 C ATOM 2764 C LEU A 269 -16.264 8.310 9.132 1.00 22.67 C ANISOU 2764 C LEU A 269 3192 3286 2138 -360 307 484 C ATOM 2765 O LEU A 269 -16.295 7.085 9.309 1.00 21.04 O ANISOU 2765 O LEU A 269 2927 3143 1926 -327 331 424 O ATOM 2766 CB LEU A 269 -14.078 9.297 8.383 1.00 25.53 C ANISOU 2766 CB LEU A 269 3558 3613 2529 -520 505 556 C ATOM 2767 CG LEU A 269 -13.219 8.163 8.948 1.00 29.21 C ANISOU 2767 CG LEU A 269 3876 4153 3068 -505 584 479 C ATOM 2768 CD1 LEU A 269 -13.098 7.032 7.936 1.00 30.39 C ANISOU 2768 CD1 LEU A 269 4065 4368 3115 -496 680 455 C ATOM 2769 CD2 LEU A 269 -11.846 8.684 9.348 1.00 28.33 C ANISOU 2769 CD2 LEU A 269 3661 4032 3071 -581 665 484 C ATOM 2770 N MET A 270 -16.883 9.166 9.952 1.00 24.37 N ANISOU 2770 N MET A 270 3394 3446 2419 -325 204 488 N ATOM 2771 CA MET A 270 -17.751 8.674 11.017 1.00 23.50 C ANISOU 2771 CA MET A 270 3206 3364 2358 -247 122 425 C ATOM 2772 C MET A 270 -18.875 7.827 10.441 1.00 21.10 C ANISOU 2772 C MET A 270 2939 3105 1971 -200 73 411 C ATOM 2773 O MET A 270 -19.145 6.720 10.920 1.00 24.25 O ANISOU 2773 O MET A 270 3270 3561 2382 -169 74 354 O ATOM 2774 CB MET A 270 -18.333 9.840 11.823 1.00 22.23 C ANISOU 2774 CB MET A 270 3047 3133 2266 -211 29 428 C ATOM 2775 CG MET A 270 -17.309 10.773 12.445 1.00 27.02 C ANISOU 2775 CG MET A 270 3628 3679 2958 -264 55 434 C ATOM 2776 SD MET A 270 -16.196 9.899 13.550 1.00 28.26 S ANISOU 2776 SD MET A 270 3641 3901 3194 -284 115 365 S ATOM 2777 CE MET A 270 -17.330 9.129 14.703 1.00 26.59 C ANISOU 2777 CE MET A 270 3370 3740 2991 -188 40 293 C ATOM 2778 N TYR A 271 -19.538 8.338 9.400 1.00 23.40 N ANISOU 2778 N TYR A 271 3344 3368 2179 -198 20 467 N ATOM 2779 CA TYR A 271 -20.603 7.587 8.743 1.00 22.21 C ANISOU 2779 CA TYR A 271 3232 3260 1947 -164 -43 456 C ATOM 2780 C TYR A 271 -20.088 6.260 8.200 1.00 23.21 C ANISOU 2780 C TYR A 271 3362 3450 2008 -196 45 417 C ATOM 2781 O TYR A 271 -20.752 5.227 8.334 1.00 22.05 O ANISOU 2781 O TYR A 271 3178 3348 1850 -167 12 365 O ATOM 2782 CB TYR A 271 -21.209 8.408 7.603 1.00 24.17 C ANISOU 2782 CB TYR A 271 3619 3462 2103 -164 -120 532 C ATOM 2783 CG TYR A 271 -22.129 9.543 8.003 1.00 32.41 C ANISOU 2783 CG TYR A 271 4666 4440 3208 -101 -244 562 C ATOM 2784 CD1 TYR A 271 -22.771 9.558 9.233 1.00 34.58 C ANISOU 2784 CD1 TYR A 271 4821 4724 3595 -35 -294 502 C ATOM 2785 CD2 TYR A 271 -22.374 10.595 7.122 1.00 41.56 C ANISOU 2785 CD2 TYR A 271 5959 5524 4309 -103 -310 650 C ATOM 2786 CE1 TYR A 271 -23.627 10.601 9.582 1.00 40.57 C ANISOU 2786 CE1 TYR A 271 5579 5420 4415 35 -398 517 C ATOM 2787 CE2 TYR A 271 -23.223 11.638 7.459 1.00 46.54 C ANISOU 2787 CE2 TYR A 271 6595 6082 5007 -30 -430 674 C ATOM 2788 CZ TYR A 271 -23.847 11.636 8.689 1.00 47.04 C ANISOU 2788 CZ TYR A 271 6525 6158 5191 43 -470 601 C ATOM 2789 OH TYR A 271 -24.691 12.677 9.020 1.00 49.88 O ANISOU 2789 OH TYR A 271 6885 6442 5623 128 -579 613 O ATOM 2790 N LEU A 272 -18.914 6.271 7.561 1.00 23.40 N ANISOU 2790 N LEU A 272 3429 3473 1989 -256 164 439 N ATOM 2791 CA LEU A 272 -18.361 5.035 7.017 1.00 22.67 C ANISOU 2791 CA LEU A 272 3342 3434 1838 -276 261 392 C ATOM 2792 C LEU A 272 -18.071 4.031 8.126 1.00 21.71 C ANISOU 2792 C LEU A 272 3085 3344 1818 -242 286 318 C ATOM 2793 O LEU A 272 -18.353 2.835 7.983 1.00 22.31 O ANISOU 2793 O LEU A 272 3159 3453 1865 -224 291 264 O ATOM 2794 CB LEU A 272 -17.098 5.339 6.210 1.00 26.30 C ANISOU 2794 CB LEU A 272 3854 3891 2249 -344 402 426 C ATOM 2795 CG LEU A 272 -16.362 4.163 5.559 1.00 33.90 C ANISOU 2795 CG LEU A 272 4825 4904 3152 -359 531 371 C ATOM 2796 CD1 LEU A 272 -17.266 3.433 4.573 1.00 36.60 C ANISOU 2796 CD1 LEU A 272 5290 5268 3350 -346 481 349 C ATOM 2797 CD2 LEU A 272 -15.081 4.647 4.871 1.00 29.97 C ANISOU 2797 CD2 LEU A 272 4354 4408 2625 -431 689 407 C ATOM 2798 N ALA A 273 -17.515 4.499 9.246 1.00 21.06 N ANISOU 2798 N ALA A 273 2902 3245 1853 -238 294 315 N ATOM 2799 CA ALA A 273 -17.213 3.599 10.353 1.00 20.98 C ANISOU 2799 CA ALA A 273 2778 3262 1933 -205 304 255 C ATOM 2800 C ALA A 273 -18.489 3.030 10.969 1.00 18.23 C ANISOU 2800 C ALA A 273 2409 2928 1590 -158 206 225 C ATOM 2801 O ALA A 273 -18.513 1.873 11.407 1.00 19.52 O ANISOU 2801 O ALA A 273 2528 3115 1774 -138 217 179 O ATOM 2802 CB ALA A 273 -16.391 4.333 11.414 1.00 17.79 C ANISOU 2802 CB ALA A 273 2283 2836 1639 -215 313 261 C ATOM 2803 N ILE A 274 -19.559 3.825 11.012 1.00 20.15 N ANISOU 2803 N ILE A 274 2680 3153 1822 -139 112 251 N ATOM 2804 CA ILE A 274 -20.814 3.328 11.564 1.00 18.53 C ANISOU 2804 CA ILE A 274 2439 2972 1631 -101 31 220 C ATOM 2805 C ILE A 274 -21.424 2.279 10.640 1.00 21.32 C ANISOU 2805 C ILE A 274 2845 3353 1904 -111 15 199 C ATOM 2806 O ILE A 274 -21.891 1.230 11.097 1.00 21.41 O ANISOU 2806 O ILE A 274 2812 3388 1934 -104 3 157 O ATOM 2807 CB ILE A 274 -21.777 4.500 11.829 1.00 23.08 C ANISOU 2807 CB ILE A 274 3016 3523 2232 -67 -61 246 C ATOM 2808 CG1 ILE A 274 -21.271 5.346 13.001 1.00 22.68 C ANISOU 2808 CG1 ILE A 274 2907 3442 2266 -54 -52 242 C ATOM 2809 CG2 ILE A 274 -23.178 3.988 12.136 1.00 18.60 C ANISOU 2809 CG2 ILE A 274 2403 2991 1673 -33 -139 215 C ATOM 2810 CD1 ILE A 274 -22.007 6.670 13.164 1.00 23.49 C ANISOU 2810 CD1 ILE A 274 3028 3498 2398 -16 -128 264 C ATOM 2811 N AVAL A 275 -21.437 2.564 9.332 0.59 19.85 N ANISOU 2811 N AVAL A 275 2764 3158 1621 -134 13 230 N ATOM 2812 N BVAL A 275 -21.428 2.523 9.326 0.41 20.14 N ANISOU 2812 N BVAL A 275 2801 3195 1657 -135 14 229 N ATOM 2813 CA AVAL A 275 -21.923 1.612 8.334 0.59 21.21 C ANISOU 2813 CA AVAL A 275 3009 3352 1698 -151 -6 204 C ATOM 2814 CA BVAL A 275 -22.026 1.510 8.457 0.41 21.18 C ANISOU 2814 CA BVAL A 275 2993 3351 1704 -148 -12 198 C ATOM 2815 C AVAL A 275 -21.156 0.300 8.430 0.59 21.58 C ANISOU 2815 C AVAL A 275 3039 3411 1752 -163 88 146 C ATOM 2816 C BVAL A 275 -21.155 0.258 8.394 0.41 21.45 C ANISOU 2816 C BVAL A 275 3024 3394 1731 -164 89 145 C ATOM 2817 O AVAL A 275 -21.741 -0.789 8.385 0.59 20.66 O ANISOU 2817 O AVAL A 275 2923 3305 1622 -165 58 99 O ATOM 2818 O BVAL A 275 -21.674 -0.847 8.204 0.41 20.82 O ANISOU 2818 O BVAL A 275 2959 3325 1627 -169 65 97 O ATOM 2819 CB AVAL A 275 -21.808 2.231 6.927 0.59 24.90 C ANISOU 2819 CB AVAL A 275 3614 3806 2040 -180 -8 252 C ATOM 2820 CB BVAL A 275 -22.326 2.062 7.049 0.41 24.43 C ANISOU 2820 CB BVAL A 275 3538 3754 1990 -169 -54 241 C ATOM 2821 CG1AVAL A 275 -21.905 1.166 5.854 0.59 26.76 C ANISOU 2821 CG1AVAL A 275 3944 4064 2159 -207 8 211 C ATOM 2822 CG1BVAL A 275 -23.373 3.170 7.115 0.41 26.39 C ANISOU 2822 CG1BVAL A 275 3785 3985 2257 -136 -182 290 C ATOM 2823 CG2AVAL A 275 -22.868 3.303 6.721 0.59 26.02 C ANISOU 2823 CG2AVAL A 275 3786 3929 2171 -155 -139 306 C ATOM 2824 CG2BVAL A 275 -21.061 2.541 6.368 0.41 25.66 C ANISOU 2824 CG2BVAL A 275 3769 3892 2087 -206 61 277 C ATOM 2825 N LEU A 276 -19.834 0.388 8.564 1.00 22.07 N ANISOU 2825 N LEU A 276 3079 3464 1844 -170 198 148 N ATOM 2826 CA LEU A 276 -19.000 -0.806 8.661 1.00 23.62 C ANISOU 2826 CA LEU A 276 3249 3663 2062 -164 288 93 C ATOM 2827 C LEU A 276 -19.375 -1.635 9.883 1.00 23.15 C ANISOU 2827 C LEU A 276 3101 3601 2092 -135 246 60 C ATOM 2828 O LEU A 276 -19.522 -2.861 9.796 1.00 21.84 O ANISOU 2828 O LEU A 276 2952 3428 1919 -131 253 13 O ATOM 2829 CB LEU A 276 -17.520 -0.417 8.708 1.00 21.61 C ANISOU 2829 CB LEU A 276 2954 3407 1852 -171 404 104 C ATOM 2830 CG LEU A 276 -16.562 -1.561 9.053 1.00 25.07 C ANISOU 2830 CG LEU A 276 3329 3844 2352 -142 488 48 C ATOM 2831 CD1 LEU A 276 -16.619 -2.665 7.997 1.00 25.26 C ANISOU 2831 CD1 LEU A 276 3445 3867 2286 -141 538 -9 C ATOM 2832 CD2 LEU A 276 -15.140 -1.041 9.224 1.00 27.80 C ANISOU 2832 CD2 LEU A 276 3598 4197 2769 -149 589 61 C ATOM 2833 N ALA A 277 -19.541 -0.978 11.036 1.00 19.67 N ANISOU 2833 N ALA A 277 2580 3162 1732 -119 203 86 N ATOM 2834 CA ALA A 277 -19.978 -1.686 12.232 1.00 20.13 C ANISOU 2834 CA ALA A 277 2570 3222 1857 -100 165 65 C ATOM 2835 C ALA A 277 -21.307 -2.386 11.995 1.00 19.81 C ANISOU 2835 C ALA A 277 2557 3190 1780 -115 97 44 C ATOM 2836 O ALA A 277 -21.483 -3.548 12.380 1.00 21.02 O ANISOU 2836 O ALA A 277 2700 3332 1953 -119 99 14 O ATOM 2837 CB ALA A 277 -20.088 -0.716 13.408 1.00 18.13 C ANISOU 2837 CB ALA A 277 2246 2974 1668 -84 128 90 C ATOM 2838 N HIS A 278 -22.248 -1.702 11.338 1.00 19.25 N ANISOU 2838 N HIS A 278 2521 3135 1660 -125 30 62 N ATOM 2839 CA HIS A 278 -23.558 -2.295 11.090 1.00 21.16 C ANISOU 2839 CA HIS A 278 2769 3392 1880 -145 -49 41 C ATOM 2840 C HIS A 278 -23.480 -3.466 10.111 1.00 21.73 C ANISOU 2840 C HIS A 278 2924 3448 1884 -175 -33 -2 C ATOM 2841 O HIS A 278 -24.263 -4.415 10.232 1.00 24.65 O ANISOU 2841 O HIS A 278 3286 3816 2265 -203 -76 -34 O ATOM 2842 CB HIS A 278 -24.526 -1.228 10.576 1.00 22.73 C ANISOU 2842 CB HIS A 278 2977 3609 2051 -137 -139 72 C ATOM 2843 CG HIS A 278 -24.910 -0.218 11.613 1.00 23.78 C ANISOU 2843 CG HIS A 278 3024 3751 2261 -100 -167 96 C ATOM 2844 ND1 HIS A 278 -25.400 1.029 11.294 1.00 23.54 N ANISOU 2844 ND1 HIS A 278 3002 3715 2225 -70 -231 132 N ATOM 2845 CD2 HIS A 278 -24.877 -0.273 12.966 1.00 24.90 C ANISOU 2845 CD2 HIS A 278 3082 3901 2479 -84 -139 86 C ATOM 2846 CE1 HIS A 278 -25.656 1.698 12.406 1.00 24.49 C ANISOU 2846 CE1 HIS A 278 3042 3838 2424 -34 -236 133 C ATOM 2847 NE2 HIS A 278 -25.345 0.931 13.435 1.00 23.91 N ANISOU 2847 NE2 HIS A 278 2914 3778 2392 -45 -178 104 N ATOM 2848 N ATHR A 279 -22.548 -3.415 9.153 0.57 21.45 N ANISOU 2848 N ATHR A 279 2972 3400 1779 -176 33 -7 N ATOM 2849 N BTHR A 279 -22.564 -3.425 9.131 0.43 21.47 N ANISOU 2849 N BTHR A 279 2976 3403 1780 -177 32 -8 N ATOM 2850 CA ATHR A 279 -22.407 -4.497 8.181 0.57 22.06 C ANISOU 2850 CA ATHR A 279 3144 3458 1780 -199 59 -62 C ATOM 2851 CA BTHR A 279 -22.466 -4.538 8.185 0.43 21.94 C ANISOU 2851 CA BTHR A 279 3129 3443 1765 -200 55 -64 C ATOM 2852 C ATHR A 279 -22.046 -5.815 8.860 0.57 22.19 C ANISOU 2852 C ATHR A 279 3130 3438 1863 -192 103 -109 C ATOM 2853 C BTHR A 279 -22.047 -5.833 8.862 0.43 22.15 C ANISOU 2853 C BTHR A 279 3125 3432 1859 -192 103 -110 C ATOM 2854 O ATHR A 279 -22.361 -6.889 8.337 0.57 23.95 O ANISOU 2854 O ATHR A 279 3418 3632 2049 -216 90 -163 O ATOM 2855 O BTHR A 279 -22.295 -6.911 8.314 0.43 23.86 O ANISOU 2855 O BTHR A 279 3410 3620 2037 -214 96 -165 O ATOM 2856 CB ATHR A 279 -21.355 -4.116 7.132 0.57 23.34 C ANISOU 2856 CB ATHR A 279 3393 3620 1856 -197 152 -60 C ATOM 2857 CB BTHR A 279 -21.472 -4.249 7.052 0.43 23.28 C ANISOU 2857 CB BTHR A 279 3395 3611 1840 -201 143 -67 C ATOM 2858 OG1ATHR A 279 -21.759 -2.916 6.458 0.57 24.85 O ANISOU 2858 OG1ATHR A 279 3636 3832 1973 -211 100 -4 O ATOM 2859 OG1BTHR A 279 -20.181 -3.945 7.596 0.43 21.17 O ANISOU 2859 OG1BTHR A 279 3065 3337 1640 -172 251 -52 O ATOM 2860 CG2ATHR A 279 -21.177 -5.222 6.104 0.57 22.83 C ANISOU 2860 CG2ATHR A 279 3439 3535 1699 -214 192 -131 C ATOM 2861 CG2BTHR A 279 -21.954 -3.112 6.165 0.43 24.27 C ANISOU 2861 CG2BTHR A 279 3593 3759 1870 -219 84 -16 C ATOM 2862 N ASN A 280 -21.405 -5.757 10.030 1.00 19.50 N ANISOU 2862 N ASN A 280 2700 3089 1619 -160 144 -88 N ATOM 2863 CA ASN A 280 -21.105 -6.982 10.765 1.00 22.34 C ANISOU 2863 CA ASN A 280 3038 3405 2046 -147 169 -118 C ATOM 2864 C ASN A 280 -22.373 -7.761 11.100 1.00 26.33 C ANISOU 2864 C ASN A 280 3544 3897 2562 -192 89 -131 C ATOM 2865 O ASN A 280 -22.337 -8.992 11.203 1.00 28.51 O ANISOU 2865 O ASN A 280 3855 4119 2859 -202 99 -168 O ATOM 2866 CB ASN A 280 -20.334 -6.674 12.046 1.00 24.08 C ANISOU 2866 CB ASN A 280 3166 3627 2358 -108 197 -83 C ATOM 2867 CG ASN A 280 -19.876 -7.934 12.751 1.00 27.97 C ANISOU 2867 CG ASN A 280 3651 4063 2912 -85 217 -104 C ATOM 2868 OD1 ASN A 280 -19.002 -8.646 12.258 1.00 29.28 O ANISOU 2868 OD1 ASN A 280 3851 4189 3084 -52 278 -144 O ATOM 2869 ND2 ASN A 280 -20.479 -8.230 13.891 1.00 21.53 N ANISOU 2869 ND2 ASN A 280 2797 3242 2142 -98 169 -76 N ATOM 2870 N SER A 281 -23.499 -7.070 11.259 1.00 22.19 N ANISOU 2870 N SER A 281 2978 3419 2034 -219 13 -103 N ATOM 2871 CA SER A 281 -24.771 -7.740 11.493 1.00 25.00 C ANISOU 2871 CA SER A 281 3316 3776 2409 -274 -58 -117 C ATOM 2872 C SER A 281 -25.317 -8.422 10.246 1.00 25.92 C ANISOU 2872 C SER A 281 3523 3873 2454 -321 -107 -169 C ATOM 2873 O SER A 281 -26.359 -9.080 10.328 1.00 31.01 O ANISOU 2873 O SER A 281 4153 4512 3119 -380 -171 -188 O ATOM 2874 CB SER A 281 -25.801 -6.741 12.035 1.00 23.27 C ANISOU 2874 CB SER A 281 3003 3618 2220 -278 -119 -79 C ATOM 2875 OG SER A 281 -25.471 -6.344 13.354 1.00 26.25 O ANISOU 2875 OG SER A 281 3306 4008 2662 -248 -79 -45 O ATOM 2876 N VAL A 282 -24.640 -8.294 9.103 1.00 24.75 N ANISOU 2876 N VAL A 282 3470 3715 2218 -303 -75 -195 N ATOM 2877 CA VAL A 282 -25.039 -8.962 7.869 1.00 24.53 C ANISOU 2877 CA VAL A 282 3555 3666 2100 -346 -118 -256 C ATOM 2878 C VAL A 282 -24.196 -10.215 7.629 1.00 30.11 C ANISOU 2878 C VAL A 282 4345 4295 2800 -336 -40 -321 C ATOM 2879 O VAL A 282 -24.665 -11.174 7.007 1.00 31.48 O ANISOU 2879 O VAL A 282 4603 4425 2934 -383 -81 -385 O ATOM 2880 CB VAL A 282 -24.930 -8.002 6.663 1.00 25.72 C ANISOU 2880 CB VAL A 282 3784 3857 2131 -336 -135 -244 C ATOM 2881 CG1 VAL A 282 -25.303 -8.707 5.358 1.00 26.55 C ANISOU 2881 CG1 VAL A 282 4026 3943 2118 -382 -184 -313 C ATOM 2882 CG2 VAL A 282 -25.803 -6.774 6.860 1.00 25.83 C ANISOU 2882 CG2 VAL A 282 3723 3931 2161 -333 -226 -180 C ATOM 2883 N VAL A 283 -22.955 -10.235 8.129 1.00 25.26 N ANISOU 2883 N VAL A 283 3706 3659 2234 -273 66 -311 N ATOM 2884 CA VAL A 283 -21.977 -11.177 7.574 1.00 30.21 C ANISOU 2884 CA VAL A 283 4419 4220 2839 -240 154 -381 C ATOM 2885 C VAL A 283 -22.099 -12.595 8.139 1.00 32.41 C ANISOU 2885 C VAL A 283 4716 4405 3192 -249 143 -420 C ATOM 2886 O VAL A 283 -21.767 -13.558 7.441 1.00 33.88 O ANISOU 2886 O VAL A 283 5006 4522 3345 -241 177 -500 O ATOM 2887 CB VAL A 283 -20.541 -10.654 7.754 1.00 32.89 C ANISOU 2887 CB VAL A 283 4713 4574 3210 -165 272 -362 C ATOM 2888 CG1 VAL A 283 -20.346 -9.356 6.989 1.00 35.92 C ANISOU 2888 CG1 VAL A 283 5110 5030 3506 -169 296 -328 C ATOM 2889 CG2 VAL A 283 -20.203 -10.487 9.226 1.00 35.33 C ANISOU 2889 CG2 VAL A 283 4899 4882 3645 -131 272 -302 C ATOM 2890 N ASN A 284 -22.533 -12.770 9.388 1.00 33.47 N ANISOU 2890 N ASN A 284 4766 4529 3422 -265 103 -368 N ATOM 2891 CA ASN A 284 -22.541 -14.114 9.974 1.00 35.19 C ANISOU 2891 CA ASN A 284 5015 4644 3710 -275 99 -390 C ATOM 2892 C ASN A 284 -23.349 -15.138 9.178 1.00 31.86 C ANISOU 2892 C ASN A 284 4702 4156 3247 -349 42 -464 C ATOM 2893 O ASN A 284 -22.826 -16.238 8.938 1.00 28.64 O ANISOU 2893 O ASN A 284 4383 3643 2855 -325 77 -526 O ATOM 2894 CB ASN A 284 -23.015 -14.042 11.433 1.00 37.90 C ANISOU 2894 CB ASN A 284 5262 4998 4139 -299 64 -310 C ATOM 2895 CG ASN A 284 -22.007 -13.351 12.332 1.00 39.35 C ANISOU 2895 CG ASN A 284 5362 5214 4373 -219 117 -253 C ATOM 2896 OD1 ASN A 284 -20.940 -12.933 11.878 1.00 37.83 O ANISOU 2896 OD1 ASN A 284 5168 5037 4168 -151 180 -271 O ATOM 2897 ND2 ASN A 284 -22.342 -13.218 13.609 1.00 41.30 N ANISOU 2897 ND2 ASN A 284 5541 5477 4674 -234 92 -187 N ATOM 2898 N PRO A 285 -24.585 -14.860 8.726 1.00 31.90 N ANISOU 2898 N PRO A 285 4706 4211 3204 -436 -50 -468 N ATOM 2899 CA PRO A 285 -25.298 -15.870 7.920 1.00 33.28 C ANISOU 2899 CA PRO A 285 4989 4317 3339 -514 -115 -548 C ATOM 2900 C PRO A 285 -24.504 -16.360 6.722 1.00 38.83 C ANISOU 2900 C PRO A 285 5837 4966 3952 -472 -61 -646 C ATOM 2901 O PRO A 285 -24.597 -17.540 6.365 1.00 42.59 O ANISOU 2901 O PRO A 285 6420 5335 4429 -503 -75 -725 O ATOM 2902 CB PRO A 285 -26.575 -15.138 7.488 1.00 32.34 C ANISOU 2902 CB PRO A 285 4823 4292 3173 -592 -227 -532 C ATOM 2903 CG PRO A 285 -26.803 -14.135 8.566 1.00 33.14 C ANISOU 2903 CG PRO A 285 4771 4477 3342 -571 -222 -435 C ATOM 2904 CD PRO A 285 -25.427 -13.674 8.975 1.00 33.27 C ANISOU 2904 CD PRO A 285 4775 4496 3372 -465 -111 -404 C ATOM 2905 N PHE A 286 -23.702 -15.490 6.104 1.00 34.71 N ANISOU 2905 N PHE A 286 5326 4510 3353 -403 10 -646 N ATOM 2906 CA PHE A 286 -22.877 -15.925 4.983 1.00 34.73 C ANISOU 2906 CA PHE A 286 5463 4470 3262 -358 90 -742 C ATOM 2907 C PHE A 286 -21.753 -16.840 5.443 1.00 37.30 C ANISOU 2907 C PHE A 286 5801 4694 3677 -273 194 -780 C ATOM 2908 O PHE A 286 -21.415 -17.809 4.753 1.00 38.94 O ANISOU 2908 O PHE A 286 6133 4811 3851 -254 232 -884 O ATOM 2909 CB PHE A 286 -22.316 -14.716 4.244 1.00 37.80 C ANISOU 2909 CB PHE A 286 5857 4961 3546 -319 152 -720 C ATOM 2910 CG PHE A 286 -23.342 -13.988 3.460 1.00 41.13 C ANISOU 2910 CG PHE A 286 6318 5459 3851 -390 42 -704 C ATOM 2911 CD1 PHE A 286 -23.609 -14.352 2.149 1.00 45.82 C ANISOU 2911 CD1 PHE A 286 7074 6041 4296 -429 11 -791 C ATOM 2912 CD2 PHE A 286 -24.076 -12.970 4.040 1.00 39.59 C ANISOU 2912 CD2 PHE A 286 6005 5343 3696 -415 -40 -608 C ATOM 2913 CE1 PHE A 286 -24.573 -13.696 1.419 1.00 46.75 C ANISOU 2913 CE1 PHE A 286 7233 6226 4303 -491 -113 -772 C ATOM 2914 CE2 PHE A 286 -25.040 -12.310 3.320 1.00 42.34 C ANISOU 2914 CE2 PHE A 286 6383 5754 3949 -469 -156 -592 C ATOM 2915 CZ PHE A 286 -25.295 -12.680 2.003 1.00 45.22 C ANISOU 2915 CZ PHE A 286 6909 6109 4164 -508 -201 -670 C ATOM 2916 N ILE A 287 -21.159 -16.551 6.603 1.00 36.14 N ANISOU 2916 N ILE A 287 5529 4556 3646 -215 234 -701 N ATOM 2917 CA ILE A 287 -20.099 -17.417 7.110 1.00 39.33 C ANISOU 2917 CA ILE A 287 5933 4861 4149 -123 311 -727 C ATOM 2918 C ILE A 287 -20.649 -18.806 7.418 1.00 38.95 C ANISOU 2918 C ILE A 287 5967 4673 4160 -165 248 -766 C ATOM 2919 O ILE A 287 -20.041 -19.823 7.064 1.00 40.75 O ANISOU 2919 O ILE A 287 6289 4785 4410 -108 297 -851 O ATOM 2920 CB ILE A 287 -19.428 -16.786 8.339 1.00 38.05 C ANISOU 2920 CB ILE A 287 5623 4743 4093 -62 338 -628 C ATOM 2921 CG1 ILE A 287 -18.955 -15.366 8.020 1.00 37.17 C ANISOU 2921 CG1 ILE A 287 5436 4760 3928 -40 392 -589 C ATOM 2922 CG2 ILE A 287 -18.266 -17.654 8.803 1.00 37.93 C ANISOU 2922 CG2 ILE A 287 5601 4627 4183 46 404 -655 C ATOM 2923 CD1 ILE A 287 -17.926 -15.300 6.914 1.00 41.64 C ANISOU 2923 CD1 ILE A 287 6053 5338 4431 22 515 -665 C ATOM 2924 N TYR A 288 -21.816 -18.869 8.071 1.00 34.60 N ANISOU 2924 N TYR A 288 5382 4125 3638 -266 144 -706 N ATOM 2925 CA TYR A 288 -22.438 -20.164 8.341 1.00 37.42 C ANISOU 2925 CA TYR A 288 5822 4346 4050 -333 83 -734 C ATOM 2926 C TYR A 288 -22.769 -20.892 7.047 1.00 39.47 C ANISOU 2926 C TYR A 288 6237 4537 4223 -378 60 -862 C ATOM 2927 O TYR A 288 -22.569 -22.107 6.942 1.00 42.00 O ANISOU 2927 O TYR A 288 6669 4706 4585 -368 64 -932 O ATOM 2928 CB TYR A 288 -23.706 -19.992 9.181 1.00 36.12 C ANISOU 2928 CB TYR A 288 5579 4220 3924 -452 -11 -649 C ATOM 2929 CG TYR A 288 -23.507 -19.262 10.486 1.00 35.19 C ANISOU 2929 CG TYR A 288 5324 4174 3873 -419 7 -530 C ATOM 2930 CD1 TYR A 288 -22.436 -19.554 11.320 1.00 37.54 C ANISOU 2930 CD1 TYR A 288 5604 4414 4248 -319 63 -491 C ATOM 2931 CD2 TYR A 288 -24.393 -18.269 10.881 1.00 37.73 C ANISOU 2931 CD2 TYR A 288 5534 4621 4180 -481 -37 -462 C ATOM 2932 CE1 TYR A 288 -22.257 -18.875 12.518 1.00 39.08 C ANISOU 2932 CE1 TYR A 288 5686 4675 4487 -294 68 -388 C ATOM 2933 CE2 TYR A 288 -24.224 -17.586 12.068 1.00 35.22 C ANISOU 2933 CE2 TYR A 288 5105 4367 3911 -451 -17 -366 C ATOM 2934 CZ TYR A 288 -23.158 -17.890 12.884 1.00 36.99 C ANISOU 2934 CZ TYR A 288 5326 4534 4196 -363 33 -329 C ATOM 2935 OH TYR A 288 -23.000 -17.203 14.068 1.00 33.01 O ANISOU 2935 OH TYR A 288 4723 4094 3725 -339 41 -239 O ATOM 2936 N ALA A 289 -23.272 -20.164 6.047 1.00 39.62 N ANISOU 2936 N ALA A 289 6278 4658 4117 -425 28 -895 N ATOM 2937 CA ALA A 289 -23.653 -20.801 4.791 1.00 38.71 C ANISOU 2937 CA ALA A 289 6323 4488 3898 -477 -10 -1020 C ATOM 2938 C ALA A 289 -22.440 -21.367 4.068 1.00 45.24 C ANISOU 2938 C ALA A 289 7268 5236 4686 -366 111 -1129 C ATOM 2939 O ALA A 289 -22.500 -22.469 3.507 1.00 47.05 O ANISOU 2939 O ALA A 289 7644 5337 4897 -383 99 -1242 O ATOM 2940 CB ALA A 289 -24.391 -19.805 3.898 1.00 35.86 C ANISOU 2940 CB ALA A 289 5963 4262 3400 -541 -79 -1019 C ATOM 2941 N TYR A 290 -21.327 -20.636 4.076 1.00 43.67 N ANISOU 2941 N TYR A 290 7002 5111 4481 -254 232 -1103 N ATOM 2942 CA TYR A 290 -20.149 -21.071 3.340 1.00 50.95 C ANISOU 2942 CA TYR A 290 8011 5980 5367 -143 367 -1211 C ATOM 2943 C TYR A 290 -19.314 -22.097 4.093 1.00 50.10 C ANISOU 2943 C TYR A 290 7893 5729 5414 -42 422 -1231 C ATOM 2944 O TYR A 290 -18.547 -22.830 3.458 1.00 49.18 O ANISOU 2944 O TYR A 290 7876 5524 5286 43 514 -1350 O ATOM 2945 CB TYR A 290 -19.283 -19.863 2.977 1.00 58.29 C ANISOU 2945 CB TYR A 290 8865 7050 6232 -75 482 -1176 C ATOM 2946 CG TYR A 290 -19.749 -19.154 1.728 1.00 69.71 C ANISOU 2946 CG TYR A 290 10407 8596 7483 -140 469 -1211 C ATOM 2947 CD1 TYR A 290 -19.476 -19.681 0.472 1.00 77.28 C ANISOU 2947 CD1 TYR A 290 11539 9518 8304 -127 534 -1348 C ATOM 2948 CD2 TYR A 290 -20.464 -17.965 1.800 1.00 73.27 C ANISOU 2948 CD2 TYR A 290 10785 9174 7882 -210 388 -1108 C ATOM 2949 CE1 TYR A 290 -19.899 -19.045 -0.679 1.00 81.02 C ANISOU 2949 CE1 TYR A 290 12122 10082 8580 -190 513 -1374 C ATOM 2950 CE2 TYR A 290 -20.892 -17.318 0.653 1.00 77.17 C ANISOU 2950 CE2 TYR A 290 11378 9750 8193 -265 359 -1129 C ATOM 2951 CZ TYR A 290 -20.606 -17.865 -0.584 1.00 81.11 C ANISOU 2951 CZ TYR A 290 12059 10214 8544 -258 419 -1258 C ATOM 2952 OH TYR A 290 -21.026 -17.236 -1.734 1.00 82.93 O ANISOU 2952 OH TYR A 290 12375 10531 8603 -306 375 -1257 O ATOM 2953 N ARG A 291 -19.452 -22.190 5.419 1.00 45.30 N ANISOU 2953 N ARG A 291 7177 5091 4944 -45 367 -1121 N ATOM 2954 CA ARG A 291 -18.539 -23.003 6.210 1.00 47.72 C ANISOU 2954 CA ARG A 291 7461 5273 5397 69 412 -1116 C ATOM 2955 C ARG A 291 -19.184 -24.164 6.956 1.00 47.37 C ANISOU 2955 C ARG A 291 7485 5064 5448 12 313 -1096 C ATOM 2956 O ARG A 291 -18.459 -25.078 7.364 1.00 46.76 O ANISOU 2956 O ARG A 291 7444 4845 5480 110 341 -1119 O ATOM 2957 CB ARG A 291 -17.784 -22.124 7.221 1.00 45.90 C ANISOU 2957 CB ARG A 291 7050 5138 5252 145 449 -998 C ATOM 2958 CG ARG A 291 -16.866 -21.093 6.567 1.00 43.49 C ANISOU 2958 CG ARG A 291 6671 4968 4886 216 569 -1018 C ATOM 2959 CD ARG A 291 -15.783 -20.624 7.524 1.00 46.20 C ANISOU 2959 CD ARG A 291 6851 5351 5352 322 618 -939 C ATOM 2960 NE ARG A 291 -15.097 -21.745 8.163 1.00 48.06 N ANISOU 2960 NE ARG A 291 7095 5437 5729 428 618 -958 N ATOM 2961 CZ ARG A 291 -13.910 -22.214 7.793 1.00 51.23 C ANISOU 2961 CZ ARG A 291 7486 5786 6194 567 724 -1043 C ATOM 2962 NH1 ARG A 291 -13.255 -21.657 6.784 1.00 51.59 N ANISOU 2962 NH1 ARG A 291 7512 5924 6168 607 856 -1118 N ATOM 2963 NH2 ARG A 291 -13.376 -23.241 8.441 1.00 50.59 N ANISOU 2963 NH2 ARG A 291 7414 5557 6252 668 700 -1050 N ATOM 2964 N ILE A 292 -20.500 -24.171 7.147 1.00 45.70 N ANISOU 2964 N ILE A 292 7290 4865 5209 -142 201 -1052 N ATOM 2965 CA ILE A 292 -21.169 -25.218 7.915 1.00 45.59 C ANISOU 2965 CA ILE A 292 7332 4702 5287 -220 114 -1016 C ATOM 2966 C ILE A 292 -22.221 -25.862 7.022 1.00 45.62 C ANISOU 2966 C ILE A 292 7475 4638 5221 -355 37 -1113 C ATOM 2967 O ILE A 292 -23.272 -25.265 6.758 1.00 41.77 O ANISOU 2967 O ILE A 292 6948 4262 4663 -481 -36 -1091 O ATOM 2968 CB ILE A 292 -21.791 -24.679 9.209 1.00 44.17 C ANISOU 2968 CB ILE A 292 7020 4598 5164 -293 57 -858 C ATOM 2969 CG1 ILE A 292 -20.757 -23.874 9.995 1.00 44.65 C ANISOU 2969 CG1 ILE A 292 6946 4747 5272 -167 122 -772 C ATOM 2970 CG2 ILE A 292 -22.308 -25.827 10.069 1.00 46.29 C ANISOU 2970 CG2 ILE A 292 7358 4700 5530 -367 -9 -810 C ATOM 2971 CD1 ILE A 292 -21.334 -23.099 11.151 1.00 44.55 C ANISOU 2971 CD1 ILE A 292 6804 4842 5282 -232 78 -632 C ATOM 2972 N ARG A 293 -21.944 -27.093 6.578 1.00 49.63 N ANISOU 2972 N ARG A 293 8143 4958 5757 -327 43 -1225 N ATOM 2973 CA ARG A 293 -22.822 -27.774 5.629 1.00 49.99 C ANISOU 2973 CA ARG A 293 8341 4922 5730 -450 -32 -1342 C ATOM 2974 C ARG A 293 -24.245 -27.907 6.165 1.00 44.39 C ANISOU 2974 C ARG A 293 7597 4215 5055 -644 -161 -1265 C ATOM 2975 O ARG A 293 -25.215 -27.743 5.415 1.00 43.38 O ANISOU 2975 O ARG A 293 7499 4144 4840 -772 -244 -1318 O ATOM 2976 CB ARG A 293 -22.249 -29.151 5.287 1.00 54.43 C ANISOU 2976 CB ARG A 293 9084 5252 6345 -381 -4 -1467 C ATOM 2977 CG ARG A 293 -23.049 -29.925 4.248 1.00 66.93 C ANISOU 2977 CG ARG A 293 10849 6733 7850 -502 -82 -1611 C ATOM 2978 CD ARG A 293 -22.521 -31.349 4.070 1.00 75.20 C ANISOU 2978 CD ARG A 293 12080 7520 8971 -434 -61 -1729 C ATOM 2979 NE ARG A 293 -21.104 -31.374 3.711 1.00 83.88 N ANISOU 2979 NE ARG A 293 13199 8599 10073 -219 84 -1809 N ATOM 2980 CZ ARG A 293 -20.464 -32.456 3.276 1.00 93.81 C ANISOU 2980 CZ ARG A 293 14600 9667 11376 -116 131 -1941 C ATOM 2981 NH1 ARG A 293 -21.114 -33.604 3.137 1.00 97.36 N ANISOU 2981 NH1 ARG A 293 15154 9956 11881 -210 36 -1985 N ATOM 2982 NH2 ARG A 293 -19.173 -32.390 2.973 1.00 96.84 N ANISOU 2982 NH2 ARG A 293 14950 10067 11776 85 272 -2004 N ATOM 2983 N GLU A 294 -24.394 -28.202 7.458 1.00 43.43 N ANISOU 2983 N GLU A 294 7409 4035 5056 -671 -180 -1139 N ATOM 2984 CA GLU A 294 -25.731 -28.402 8.012 1.00 48.12 C ANISOU 2984 CA GLU A 294 7965 4627 5692 -863 -280 -1066 C ATOM 2985 C GLU A 294 -26.562 -27.124 7.941 1.00 46.00 C ANISOU 2985 C GLU A 294 7537 4588 5355 -941 -318 -1007 C ATOM 2986 O GLU A 294 -27.774 -27.177 7.695 1.00 45.70 O ANISOU 2986 O GLU A 294 7480 4580 5304 -1103 -413 -1018 O ATOM 2987 CB GLU A 294 -25.636 -28.905 9.452 1.00 51.62 C ANISOU 2987 CB GLU A 294 8377 4973 6263 -869 -272 -931 C ATOM 2988 CG GLU A 294 -26.946 -29.458 9.997 1.00 55.05 C ANISOU 2988 CG GLU A 294 8811 5352 6754 -1078 -357 -871 C ATOM 2989 CD GLU A 294 -27.313 -30.798 9.385 1.00 62.06 C ANISOU 2989 CD GLU A 294 9887 6021 7673 -1174 -419 -981 C ATOM 2990 OE1 GLU A 294 -26.400 -31.619 9.162 1.00 66.15 O ANISOU 2990 OE1 GLU A 294 10550 6361 8221 -1057 -385 -1051 O ATOM 2991 OE2 GLU A 294 -28.513 -31.032 9.124 1.00 63.63 O ANISOU 2991 OE2 GLU A 294 10083 6221 7871 -1364 -505 -1002 O ATOM 2992 N PHE A 295 -25.932 -25.964 8.154 1.00 41.40 N ANISOU 2992 N PHE A 295 6832 4163 4736 -827 -250 -947 N ATOM 2993 CA PHE A 295 -26.630 -24.695 7.961 1.00 41.12 C ANISOU 2993 CA PHE A 295 6660 4333 4631 -878 -285 -903 C ATOM 2994 C PHE A 295 -26.948 -24.470 6.489 1.00 43.00 C ANISOU 2994 C PHE A 295 6979 4621 4739 -908 -333 -1023 C ATOM 2995 O PHE A 295 -28.078 -24.114 6.131 1.00 41.44 O ANISOU 2995 O PHE A 295 6734 4507 4504 -1029 -434 -1025 O ATOM 2996 CB PHE A 295 -25.787 -23.533 8.495 1.00 39.94 C ANISOU 2996 CB PHE A 295 6384 4318 4475 -747 -200 -819 C ATOM 2997 CG PHE A 295 -26.100 -23.141 9.911 1.00 40.46 C ANISOU 2997 CG PHE A 295 6311 4437 4623 -774 -198 -678 C ATOM 2998 CD1 PHE A 295 -27.302 -22.527 10.225 1.00 37.29 C ANISOU 2998 CD1 PHE A 295 5794 4152 4222 -890 -259 -620 C ATOM 2999 CD2 PHE A 295 -25.176 -23.354 10.923 1.00 40.65 C ANISOU 2999 CD2 PHE A 295 6321 4404 4720 -676 -136 -608 C ATOM 3000 CE1 PHE A 295 -27.587 -22.152 11.529 1.00 33.38 C ANISOU 3000 CE1 PHE A 295 5180 3713 3791 -913 -241 -501 C ATOM 3001 CE2 PHE A 295 -25.453 -22.979 12.227 1.00 38.02 C ANISOU 3001 CE2 PHE A 295 5881 4125 4440 -703 -134 -483 C ATOM 3002 CZ PHE A 295 -26.660 -22.375 12.530 1.00 35.87 C ANISOU 3002 CZ PHE A 295 5502 3969 4158 -822 -177 -432 C ATOM 3003 N ARG A 296 -25.948 -24.665 5.625 1.00 43.16 N ANISOU 3003 N ARG A 296 7119 4594 4687 -795 -262 -1125 N ATOM 3004 CA ARG A 296 -26.102 -24.432 4.193 1.00 44.70 C ANISOU 3004 CA ARG A 296 7417 4837 4729 -811 -292 -1241 C ATOM 3005 C ARG A 296 -27.251 -25.250 3.613 1.00 47.19 C ANISOU 3005 C ARG A 296 7835 5072 5023 -971 -428 -1325 C ATOM 3006 O ARG A 296 -28.103 -24.724 2.888 1.00 48.68 O ANISOU 3006 O ARG A 296 8015 5365 5118 -1058 -529 -1348 O ATOM 3007 CB ARG A 296 -24.781 -24.760 3.490 1.00 45.42 C ANISOU 3007 CB ARG A 296 7634 4862 4762 -665 -167 -1345 C ATOM 3008 CG ARG A 296 -24.831 -24.757 1.978 1.00 54.76 C ANISOU 3008 CG ARG A 296 8973 6065 5770 -679 -179 -1484 C ATOM 3009 CD ARG A 296 -23.424 -24.807 1.385 1.00 60.63 C ANISOU 3009 CD ARG A 296 9797 6786 6455 -518 -15 -1569 C ATOM 3010 NE ARG A 296 -22.719 -26.054 1.677 1.00 61.68 N ANISOU 3010 NE ARG A 296 10018 6724 6694 -440 49 -1643 N ATOM 3011 CZ ARG A 296 -21.703 -26.167 2.529 1.00 61.68 C ANISOU 3011 CZ ARG A 296 9933 6681 6824 -308 150 -1588 C ATOM 3012 NH1 ARG A 296 -21.128 -27.348 2.718 1.00 64.74 N ANISOU 3012 NH1 ARG A 296 10413 6875 7308 -233 189 -1661 N ATOM 3013 NH2 ARG A 296 -21.257 -25.106 3.187 1.00 59.17 N ANISOU 3013 NH2 ARG A 296 9439 6502 6540 -250 202 -1463 N ATOM 3014 N GLN A 297 -27.291 -26.547 3.931 1.00 45.56 N ANISOU 3014 N GLN A 297 7728 4674 4910 -1015 -442 -1369 N ATOM 3015 CA GLN A 297 -28.355 -27.404 3.421 1.00 50.34 C ANISOU 3015 CA GLN A 297 8434 5182 5510 -1181 -574 -1454 C ATOM 3016 C GLN A 297 -29.710 -27.034 4.010 1.00 46.83 C ANISOU 3016 C GLN A 297 7829 4832 5132 -1344 -688 -1355 C ATOM 3017 O GLN A 297 -30.734 -27.161 3.330 1.00 48.14 O ANISOU 3017 O GLN A 297 8018 5018 5255 -1483 -821 -1418 O ATOM 3018 CB GLN A 297 -28.027 -28.870 3.706 1.00 57.27 C ANISOU 3018 CB GLN A 297 9460 5813 6487 -1187 -556 -1515 C ATOM 3019 CG GLN A 297 -26.771 -29.359 3.001 1.00 66.28 C ANISOU 3019 CG GLN A 297 10767 6845 7570 -1026 -449 -1642 C ATOM 3020 CD GLN A 297 -26.382 -30.767 3.408 1.00 76.50 C ANISOU 3020 CD GLN A 297 12199 7882 8985 -1006 -430 -1689 C ATOM 3021 OE1 GLN A 297 -26.666 -31.204 4.523 1.00 82.09 O ANISOU 3021 OE1 GLN A 297 12851 8507 9833 -1062 -453 -1578 O ATOM 3022 NE2 GLN A 297 -25.727 -31.487 2.502 1.00 74.11 N ANISOU 3022 NE2 GLN A 297 12024 7486 8646 -904 -379 -1823 N ATOM 3023 N THR A 298 -29.740 -26.580 5.265 1.00 43.02 N ANISOU 3023 N THR A 298 7180 4411 4754 -1330 -640 -1208 N ATOM 3024 CA THR A 298 -30.999 -26.135 5.851 1.00 43.44 C ANISOU 3024 CA THR A 298 7061 4573 4870 -1471 -724 -1117 C ATOM 3025 C THR A 298 -31.451 -24.817 5.237 1.00 43.47 C ANISOU 3025 C THR A 298 6954 4785 4777 -1458 -779 -1106 C ATOM 3026 O THR A 298 -32.646 -24.620 4.986 1.00 44.89 O ANISOU 3026 O THR A 298 7052 5039 4965 -1588 -902 -1110 O ATOM 3027 CB THR A 298 -30.858 -26.000 7.367 1.00 43.43 C ANISOU 3027 CB THR A 298 6932 4582 4988 -1452 -643 -969 C ATOM 3028 OG1 THR A 298 -30.254 -27.186 7.893 1.00 43.35 O ANISOU 3028 OG1 THR A 298 7048 4367 5056 -1435 -591 -971 O ATOM 3029 CG2 THR A 298 -32.221 -25.806 8.015 1.00 42.59 C ANISOU 3029 CG2 THR A 298 6662 4558 4962 -1617 -712 -890 C ATOM 3030 N PHE A 299 -30.509 -23.899 4.997 1.00 41.35 N ANISOU 3030 N PHE A 299 6679 4609 4424 -1301 -693 -1090 N ATOM 3031 CA PHE A 299 -30.837 -22.669 4.283 1.00 45.72 C ANISOU 3031 CA PHE A 299 7166 5337 4869 -1279 -748 -1083 C ATOM 3032 C PHE A 299 -31.441 -22.974 2.918 1.00 49.47 C ANISOU 3032 C PHE A 299 7768 5800 5226 -1362 -878 -1206 C ATOM 3033 O PHE A 299 -32.432 -22.352 2.517 1.00 49.98 O ANISOU 3033 O PHE A 299 7751 5979 5259 -1437 -1006 -1194 O ATOM 3034 CB PHE A 299 -29.591 -21.796 4.113 1.00 40.25 C ANISOU 3034 CB PHE A 299 6486 4712 4096 -1108 -623 -1059 C ATOM 3035 CG PHE A 299 -29.093 -21.164 5.387 1.00 38.00 C ANISOU 3035 CG PHE A 299 6051 4481 3906 -1028 -525 -932 C ATOM 3036 CD1 PHE A 299 -29.861 -21.165 6.541 1.00 36.26 C ANISOU 3036 CD1 PHE A 299 5688 4282 3809 -1104 -551 -839 C ATOM 3037 CD2 PHE A 299 -27.847 -20.551 5.417 1.00 38.33 C ANISOU 3037 CD2 PHE A 299 6096 4557 3910 -881 -403 -909 C ATOM 3038 CE1 PHE A 299 -29.387 -20.571 7.708 1.00 33.67 C ANISOU 3038 CE1 PHE A 299 5241 4005 3549 -1029 -463 -730 C ATOM 3039 CE2 PHE A 299 -27.370 -19.958 6.575 1.00 35.12 C ANISOU 3039 CE2 PHE A 299 5559 4200 3586 -811 -327 -800 C ATOM 3040 CZ PHE A 299 -28.141 -19.970 7.721 1.00 34.55 C ANISOU 3040 CZ PHE A 299 5362 4144 3620 -883 -361 -713 C ATOM 3041 N AARG A 300 -30.851 -23.926 2.189 0.50 53.51 N ANISOU 3041 N AARG A 300 8486 6173 5673 -1345 -853 -1330 N ATOM 3042 N BARG A 300 -30.857 -23.929 2.191 0.50 53.52 N ANISOU 3042 N BARG A 300 8487 6173 5675 -1346 -853 -1330 N ATOM 3043 CA AARG A 300 -31.353 -24.269 0.862 0.50 57.39 C ANISOU 3043 CA AARG A 300 9087 6659 6061 -1392 -958 -1438 C ATOM 3044 CA BARG A 300 -31.362 -24.258 0.861 0.50 57.39 C ANISOU 3044 CA BARG A 300 9084 6660 6060 -1392 -959 -1437 C ATOM 3045 C AARG A 300 -32.790 -24.770 0.922 0.50 58.54 C ANISOU 3045 C AARG A 300 9138 6798 6306 -1551 -1112 -1434 C ATOM 3046 C BARG A 300 -32.795 -24.770 0.921 0.50 58.53 C ANISOU 3046 C BARG A 300 9137 6798 6305 -1551 -1112 -1434 C ATOM 3047 O AARG A 300 -33.625 -24.381 0.098 0.50 59.13 O ANISOU 3047 O AARG A 300 9164 6974 6328 -1585 -1232 -1449 O ATOM 3048 O BARG A 300 -33.632 -24.389 0.095 0.50 59.14 O ANISOU 3048 O BARG A 300 9166 6975 6330 -1586 -1233 -1449 O ATOM 3049 CB AARG A 300 -30.449 -25.316 0.207 0.50 61.39 C ANISOU 3049 CB AARG A 300 9791 7014 6521 -1319 -873 -1559 C ATOM 3050 CB BARG A 300 -30.454 -25.290 0.192 0.50 61.39 C ANISOU 3050 CB BARG A 300 9788 7018 6518 -1318 -874 -1558 C ATOM 3051 CG AARG A 300 -29.159 -24.760 -0.385 0.50 64.18 C ANISOU 3051 CG AARG A 300 10230 7412 6743 -1155 -732 -1590 C ATOM 3052 CG BARG A 300 -29.076 -24.765 -0.170 0.50 63.82 C ANISOU 3052 CG BARG A 300 10176 7357 6716 -1151 -718 -1580 C ATOM 3053 CD AARG A 300 -28.519 -25.744 -1.366 0.50 67.17 C ANISOU 3053 CD AARG A 300 10784 7677 7060 -1091 -673 -1727 C ATOM 3054 CD BARG A 300 -28.318 -25.757 -1.038 0.50 66.85 C ANISOU 3054 CD BARG A 300 10734 7618 7048 -1076 -643 -1713 C ATOM 3055 NE AARG A 300 -27.642 -26.713 -0.712 0.50 67.94 N ANISOU 3055 NE AARG A 300 10957 7598 7259 -1028 -561 -1768 N ATOM 3056 NE BARG A 300 -27.076 -25.191 -1.555 0.50 66.95 N ANISOU 3056 NE BARG A 300 10797 7689 6951 -923 -488 -1735 N ATOM 3057 CZ AARG A 300 -26.314 -26.631 -0.701 0.50 67.76 C ANISOU 3057 CZ AARG A 300 10983 7550 7212 -874 -396 -1795 C ATOM 3058 CZ BARG A 300 -27.001 -24.426 -2.639 0.50 67.37 C ANISOU 3058 CZ BARG A 300 10871 7876 6852 -885 -485 -1745 C ATOM 3059 NH1AARG A 300 -25.707 -25.623 -1.312 0.50 67.56 N ANISOU 3059 NH1AARG A 300 10939 7670 7061 -783 -313 -1782 N ATOM 3060 NH1BARG A 300 -28.099 -24.129 -3.320 0.50 67.01 N ANISOU 3060 NH1BARG A 300 10806 7914 6741 -977 -639 -1737 N ATOM 3061 NH2AARG A 300 -25.592 -27.556 -0.083 0.50 67.31 N ANISOU 3061 NH2AARG A 300 10985 7321 7269 -808 -313 -1830 N ATOM 3062 NH2BARG A 300 -25.828 -23.955 -3.039 0.50 69.41 N ANISOU 3062 NH2BARG A 300 11162 8183 7027 -755 -326 -1757 N ATOM 3063 N LYS A 301 -33.098 -25.633 1.894 1.00 58.46 N ANISOU 3063 N LYS A 301 9098 6670 6446 -1649 -1107 -1409 N ATOM 3064 CA LYS A 301 -34.457 -26.155 2.016 1.00 60.48 C ANISOU 3064 CA LYS A 301 9247 6919 6814 -1808 -1233 -1400 C ATOM 3065 C LYS A 301 -35.448 -25.055 2.370 1.00 56.27 C ANISOU 3065 C LYS A 301 8486 6572 6322 -1857 -1312 -1305 C ATOM 3066 O LYS A 301 -36.551 -25.005 1.817 1.00 57.95 O ANISOU 3066 O LYS A 301 8608 6854 6556 -1931 -1443 -1326 O ATOM 3067 CB LYS A 301 -34.505 -27.268 3.062 1.00 64.45 C ANISOU 3067 CB LYS A 301 9766 7254 7469 -1901 -1188 -1373 C ATOM 3068 CG LYS A 301 -33.818 -28.554 2.645 1.00 73.89 C ANISOU 3068 CG LYS A 301 11174 8243 8659 -1869 -1145 -1476 C ATOM 3069 CD LYS A 301 -34.050 -29.643 3.679 1.00 78.10 C ANISOU 3069 CD LYS A 301 11712 8607 9354 -1974 -1121 -1430 C ATOM 3070 CE LYS A 301 -33.267 -30.901 3.352 1.00 82.44 C ANISOU 3070 CE LYS A 301 12475 8937 9912 -1918 -1072 -1526 C ATOM 3071 NZ LYS A 301 -33.428 -31.932 4.415 1.00 86.94 N ANISOU 3071 NZ LYS A 301 13062 9331 10639 -2009 -1046 -1460 N ATOM 3072 N ILE A 302 -35.074 -24.164 3.292 1.00 52.57 N ANISOU 3072 N ILE A 302 7917 6187 5871 -1812 -1236 -1206 N ATOM 3073 CA ILE A 302 -35.973 -23.082 3.690 1.00 55.40 C ANISOU 3073 CA ILE A 302 8048 6722 6278 -1840 -1298 -1117 C ATOM 3074 C ILE A 302 -36.310 -22.198 2.495 1.00 59.13 C ANISOU 3074 C ILE A 302 8507 7323 6636 -1769 -1400 -1145 C ATOM 3075 O ILE A 302 -37.471 -21.825 2.285 1.00 59.76 O ANISOU 3075 O ILE A 302 8432 7501 6772 -1820 -1520 -1127 O ATOM 3076 CB ILE A 302 -35.353 -22.260 4.835 1.00 48.14 C ANISOU 3076 CB ILE A 302 7016 5873 5402 -1738 -1158 -997 C ATOM 3077 CG1 ILE A 302 -35.214 -23.109 6.099 1.00 46.20 C ANISOU 3077 CG1 ILE A 302 6745 5517 5292 -1788 -1053 -936 C ATOM 3078 CG2 ILE A 302 -36.188 -21.022 5.112 1.00 46.69 C ANISOU 3078 CG2 ILE A 302 6611 5875 5255 -1733 -1213 -917 C ATOM 3079 CD1 ILE A 302 -34.521 -22.385 7.238 1.00 45.54 C ANISOU 3079 CD1 ILE A 302 6563 5495 5246 -1664 -908 -818 C ATOM 3080 N ILE A 303 -35.303 -21.851 1.693 1.00 58.05 N ANISOU 3080 N ILE A 303 8529 7186 6342 -1645 -1349 -1186 N ATOM 3081 CA ILE A 303 -35.533 -20.949 0.570 1.00 61.14 C ANISOU 3081 CA ILE A 303 8924 7695 6610 -1572 -1432 -1195 C ATOM 3082 C ILE A 303 -36.308 -21.654 -0.538 1.00 65.44 C ANISOU 3082 C ILE A 303 9530 8207 7126 -1635 -1562 -1289 C ATOM 3083 O ILE A 303 -37.244 -21.086 -1.112 1.00 65.39 O ANISOU 3083 O ILE A 303 9429 8306 7111 -1648 -1696 -1279 O ATOM 3084 CB ILE A 303 -34.194 -20.382 0.069 1.00 59.90 C ANISOU 3084 CB ILE A 303 8916 7549 6295 -1429 -1313 -1201 C ATOM 3085 CG1 ILE A 303 -33.563 -19.517 1.162 1.00 55.45 C ANISOU 3085 CG1 ILE A 303 8263 7042 5764 -1371 -1206 -1103 C ATOM 3086 CG2 ILE A 303 -34.395 -19.578 -1.208 1.00 61.16 C ANISOU 3086 CG2 ILE A 303 9114 7809 6313 -1363 -1392 -1209 C ATOM 3087 CD1 ILE A 303 -32.055 -19.480 1.131 1.00 54.92 C ANISOU 3087 CD1 ILE A 303 8332 6925 5611 -1251 -1035 -1119 C ATOM 3088 N ARG A 304 -35.945 -22.901 -0.847 1.00 71.92 N ANISOU 3088 N ARG A 304 10508 8880 7936 -1673 -1530 -1386 N ATOM 3089 CA ARG A 304 -36.665 -23.651 -1.873 1.00 78.73 C ANISOU 3089 CA ARG A 304 11436 9705 8772 -1744 -1654 -1486 C ATOM 3090 C ARG A 304 -38.121 -23.860 -1.475 1.00 83.36 C ANISOU 3090 C ARG A 304 11830 10326 9516 -1881 -1789 -1464 C ATOM 3091 O ARG A 304 -39.042 -23.448 -2.190 1.00 86.75 O ANISOU 3091 O ARG A 304 12182 10854 9924 -1903 -1930 -1478 O ATOM 3092 CB ARG A 304 -35.977 -24.993 -2.131 1.00 81.89 C ANISOU 3092 CB ARG A 304 12035 9925 9154 -1756 -1583 -1594 C ATOM 3093 CG ARG A 304 -34.668 -24.883 -2.897 1.00 86.61 C ANISOU 3093 CG ARG A 304 12826 10499 9582 -1617 -1464 -1650 C ATOM 3094 CD ARG A 304 -33.949 -26.223 -2.978 1.00 92.99 C ANISOU 3094 CD ARG A 304 13808 11119 10403 -1613 -1378 -1755 C ATOM 3095 NE ARG A 304 -32.587 -26.070 -3.482 1.00 98.56 N ANISOU 3095 NE ARG A 304 14663 11808 10978 -1465 -1228 -1800 N ATOM 3096 CZ ARG A 304 -31.692 -27.052 -3.539 1.00103.21 C ANISOU 3096 CZ ARG A 304 15400 12245 11571 -1412 -1119 -1888 C ATOM 3097 NH1 ARG A 304 -30.475 -26.814 -4.013 1.00103.57 N ANISOU 3097 NH1 ARG A 304 15548 12298 11505 -1271 -974 -1926 N ATOM 3098 NH2 ARG A 304 -32.009 -28.270 -3.121 1.00105.50 N ANISOU 3098 NH2 ARG A 304 15725 12374 11987 -1497 -1149 -1936 N ATOM 3099 N SER A 305 -38.348 -24.495 -0.330 1.00 86.61 N ANISOU 3099 N SER A 305 12158 10661 10089 -1975 -1741 -1426 N ATOM 3100 CA SER A 305 -39.702 -24.756 0.146 1.00 91.87 C ANISOU 3100 CA SER A 305 12626 11358 10922 -2114 -1838 -1402 C ATOM 3101 C SER A 305 -40.419 -23.460 0.510 1.00 93.54 C ANISOU 3101 C SER A 305 12606 11751 11183 -2083 -1889 -1308 C ATOM 3102 O SER A 305 -40.670 -23.188 1.684 1.00 94.73 O ANISOU 3102 O SER A 305 12593 11939 11461 -2118 -1827 -1219 O ATOM 3103 CB SER A 305 -39.675 -25.697 1.353 1.00 92.21 C ANISOU 3103 CB SER A 305 12643 11273 11118 -2217 -1746 -1365 C ATOM 3104 OG SER A 305 -39.045 -26.925 1.030 1.00 93.88 O ANISOU 3104 OG SER A 305 13069 11301 11301 -2236 -1705 -1453 O TER 3105 SER A 305 HETATM 3106 N2 T4E A1201 -20.301 8.216 17.337 1.00 27.39 N ANISOU 3106 N2 T4E A1201 3368 3932 3108 0 -103 155 N HETATM 3107 N1 T4E A1201 -21.216 7.384 17.046 1.00 21.49 N ANISOU 3107 N1 T4E A1201 2606 3235 2324 26 -110 150 N HETATM 3108 C6 T4E A1201 -21.221 6.054 17.423 1.00 20.07 C ANISOU 3108 C6 T4E A1201 2380 3119 2127 20 -79 127 C HETATM 3109 C5 T4E A1201 -20.072 5.632 18.200 1.00 17.61 C ANISOU 3109 C5 T4E A1201 2035 2817 1840 -6 -44 111 C HETATM 3110 N4 T4E A1201 -19.077 6.525 18.516 1.00 20.90 N ANISOU 3110 N4 T4E A1201 2453 3189 2298 -31 -45 114 N HETATM 3111 C3 T4E A1201 -19.179 7.825 18.086 1.00 18.41 C ANISOU 3111 C3 T4E A1201 2185 2810 1998 -35 -70 134 C HETATM 3112 C10 T4E A1201 -24.450 3.359 16.126 1.00 17.71 C ANISOU 3112 C10 T4E A1201 2037 2953 1739 38 -136 106 C HETATM 3113 C11 T4E A1201 -24.753 4.615 16.717 1.00 18.33 C ANISOU 3113 C11 T4E A1201 2097 3007 1858 83 -163 99 C HETATM 3114 C12 T4E A1201 -23.705 5.497 17.138 1.00 20.62 C ANISOU 3114 C12 T4E A1201 2415 3249 2170 82 -143 106 C HETATM 3115 C7 T4E A1201 -22.341 5.146 16.993 1.00 20.17 C ANISOU 3115 C7 T4E A1201 2381 3179 2103 36 -93 122 C HETATM 3116 C8 T4E A1201 -22.092 3.896 16.376 1.00 18.53 C ANISOU 3116 C8 T4E A1201 2181 3001 1858 5 -60 127 C HETATM 3117 C9 T4E A1201 -23.115 3.052 15.985 1.00 19.52 C ANISOU 3117 C9 T4E A1201 2298 3162 1955 7 -81 117 C HETATM 3118 C16 T4E A1201 -19.300 1.598 19.735 1.00 19.51 C ANISOU 3118 C16 T4E A1201 2192 3161 2060 -12 18 78 C HETATM 3119 C17 T4E A1201 -20.621 2.115 19.752 1.00 19.77 C ANISOU 3119 C17 T4E A1201 2233 3206 2071 1 -5 70 C HETATM 3120 C18 T4E A1201 -20.880 3.429 19.263 1.00 19.69 C ANISOU 3120 C18 T4E A1201 2242 3170 2071 11 -27 75 C HETATM 3121 C13 T4E A1201 -19.843 4.225 18.725 1.00 19.04 C ANISOU 3121 C13 T4E A1201 2177 3046 2010 -10 -18 95 C HETATM 3122 C14 T4E A1201 -18.541 3.687 18.730 1.00 19.49 C ANISOU 3122 C14 T4E A1201 2212 3103 2090 -35 18 100 C HETATM 3123 C15 T4E A1201 -18.261 2.390 19.218 1.00 20.01 C ANISOU 3123 C15 T4E A1201 2251 3196 2155 -28 32 90 C HETATM 3124 N3 T4E A1201 -18.179 8.731 18.397 1.00 24.16 N ANISOU 3124 N3 T4E A1201 2918 3486 2776 -75 -72 135 N HETATM 3125 CL1 T4E A1201 -22.599 1.505 15.262 1.00 20.40 CL ANISOU 3125 CL1 T4E A1201 2439 3288 2024 -34 -36 112 CL HETATM 3126 O1 T4E A1201 -25.425 2.518 15.725 1.00 19.99 O ANISOU 3126 O1 T4E A1201 2306 3280 2011 26 -163 95 O HETATM 3127 C1 CLR A1202 -38.104 9.405 31.021 1.00 78.07 C HETATM 3128 C2 CLR A1202 -37.848 10.931 30.946 1.00 77.65 C HETATM 3129 C3 CLR A1202 -36.537 11.276 30.285 1.00 76.24 C HETATM 3130 C4 CLR A1202 -36.428 10.598 28.910 1.00 74.72 C HETATM 3131 C5 CLR A1202 -36.640 9.113 29.036 1.00 74.17 C HETATM 3132 C6 CLR A1202 -35.685 8.287 28.573 1.00 70.38 C HETATM 3133 C7 CLR A1202 -35.848 6.791 28.385 1.00 69.70 C HETATM 3134 C8 CLR A1202 -37.256 6.335 28.746 1.00 73.98 C HETATM 3135 C9 CLR A1202 -37.781 7.114 29.963 1.00 76.73 C HETATM 3136 C10 CLR A1202 -37.907 8.629 29.709 1.00 77.45 C HETATM 3137 C11 CLR A1202 -39.047 6.457 30.522 1.00 76.72 C HETATM 3138 C12 CLR A1202 -38.953 4.930 30.668 1.00 78.32 C HETATM 3139 C13 CLR A1202 -38.539 4.216 29.409 1.00 78.53 C HETATM 3140 C14 CLR A1202 -37.202 4.851 29.053 1.00 76.16 C HETATM 3141 C15 CLR A1202 -36.601 3.946 27.976 1.00 76.06 C HETATM 3142 C16 CLR A1202 -37.311 2.607 28.177 1.00 77.21 C HETATM 3143 C17 CLR A1202 -38.162 2.726 29.440 1.00 78.81 C HETATM 3144 C18 CLR A1202 -39.635 4.408 28.320 1.00 77.65 C HETATM 3145 C19 CLR A1202 -39.097 8.942 28.755 1.00 76.56 C HETATM 3146 C20 CLR A1202 -39.263 1.653 29.508 1.00 78.45 C HETATM 3147 C21 CLR A1202 -39.761 1.452 30.940 1.00 79.27 C HETATM 3148 C22 CLR A1202 -38.822 0.282 28.938 1.00 77.09 C HETATM 3149 C23 CLR A1202 -39.803 -0.862 29.251 1.00 76.39 C HETATM 3150 C24 CLR A1202 -39.764 -1.961 28.185 1.00 77.02 C HETATM 3151 C25 CLR A1202 -40.966 -2.919 28.229 1.00 77.28 C HETATM 3152 C26 CLR A1202 -40.771 -4.115 27.300 1.00 77.03 C HETATM 3153 C27 CLR A1202 -41.268 -3.408 29.644 1.00 76.99 C HETATM 3154 O1 CLR A1202 -36.425 12.696 30.097 1.00 75.38 O HETATM 3155 C1 CLR A1203 -38.065 10.883 21.627 1.00 27.35 C HETATM 3156 C2 CLR A1203 -37.761 12.376 21.888 1.00 29.59 C HETATM 3157 C3 CLR A1203 -37.990 12.748 23.331 1.00 30.82 C HETATM 3158 C4 CLR A1203 -37.176 11.833 24.268 1.00 26.75 C HETATM 3159 C5 CLR A1203 -37.446 10.378 24.000 1.00 27.87 C HETATM 3160 C6 CLR A1203 -37.746 9.582 25.045 1.00 26.46 C HETATM 3161 C7 CLR A1203 -38.011 8.089 24.958 1.00 26.53 C HETATM 3162 C8 CLR A1203 -37.681 7.519 23.578 1.00 27.65 C HETATM 3163 C9 CLR A1203 -38.054 8.517 22.470 1.00 28.16 C HETATM 3164 C10 CLR A1203 -37.371 9.884 22.568 1.00 29.70 C HETATM 3165 C11 CLR A1203 -37.873 7.864 21.096 1.00 27.39 C HETATM 3166 C12 CLR A1203 -38.546 6.494 20.976 1.00 26.87 C HETATM 3167 C13 CLR A1203 -38.186 5.505 22.052 1.00 28.60 C HETATM 3168 C14 CLR A1203 -38.460 6.231 23.363 1.00 26.14 C HETATM 3169 C15 CLR A1203 -38.283 5.133 24.408 1.00 30.37 C HETATM 3170 C16 CLR A1203 -38.828 3.894 23.696 1.00 32.66 C HETATM 3171 C17 CLR A1203 -39.009 4.214 22.207 1.00 28.61 C HETATM 3172 C18 CLR A1203 -36.697 5.078 21.935 1.00 29.65 C HETATM 3173 C19 CLR A1203 -35.872 9.759 22.154 1.00 29.00 C HETATM 3174 C20 CLR A1203 -38.714 2.965 21.348 1.00 28.57 C HETATM 3175 C21 CLR A1203 -38.801 3.200 19.836 1.00 29.26 C HETATM 3176 C22 CLR A1203 -39.679 1.813 21.711 1.00 33.28 C HETATM 3177 C23 CLR A1203 -39.424 0.452 21.036 1.00 37.43 C HETATM 3178 C24 CLR A1203 -40.486 -0.533 21.538 1.00 48.49 C HETATM 3179 C25 CLR A1203 -40.307 -2.009 21.149 1.00 56.89 C HETATM 3180 C26 CLR A1203 -41.407 -2.864 21.775 1.00 61.25 C HETATM 3181 C27 CLR A1203 -40.317 -2.218 19.637 1.00 56.87 C HETATM 3182 O1 CLR A1203 -37.591 14.110 23.554 1.00 32.33 O HETATM 3183 C1 CLR A1204 -8.297 10.819 13.201 1.00 32.97 C HETATM 3184 C2 CLR A1204 -8.312 12.358 13.296 1.00 35.55 C HETATM 3185 C3 CLR A1204 -6.965 12.968 12.988 1.00 34.20 C HETATM 3186 C4 CLR A1204 -6.413 12.475 11.639 1.00 29.32 C HETATM 3187 C5 CLR A1204 -6.451 10.973 11.528 1.00 30.04 C HETATM 3188 C6 CLR A1204 -5.348 10.317 11.113 1.00 28.99 C HETATM 3189 C7 CLR A1204 -5.272 8.822 10.847 1.00 30.48 C HETATM 3190 C8 CLR A1204 -6.659 8.180 10.877 1.00 32.13 C HETATM 3191 C9 CLR A1204 -7.488 8.779 12.025 1.00 29.29 C HETATM 3192 C10 CLR A1204 -7.747 10.272 11.877 1.00 32.65 C HETATM 3193 C11 CLR A1204 -8.778 7.992 12.256 1.00 29.83 C HETATM 3194 C12 CLR A1204 -8.550 6.486 12.350 1.00 33.86 C HETATM 3195 C13 CLR A1204 -7.834 5.908 11.161 1.00 33.48 C HETATM 3196 C14 CLR A1204 -6.524 6.684 11.078 1.00 33.02 C HETATM 3197 C15 CLR A1204 -5.722 5.916 10.029 1.00 35.28 C HETATM 3198 C16 CLR A1204 -6.128 4.467 10.289 1.00 34.85 C HETATM 3199 C17 CLR A1204 -7.336 4.460 11.231 1.00 33.58 C HETATM 3200 C18 CLR A1204 -8.703 6.079 9.881 1.00 34.00 C HETATM 3201 C19 CLR A1204 -8.770 10.552 10.735 1.00 33.59 C HETATM 3202 C20 CLR A1204 -8.282 3.290 10.906 1.00 36.06 C HETATM 3203 C21 CLR A1204 -9.538 3.235 11.783 1.00 35.92 C HETATM 3204 C22 CLR A1204 -7.548 1.947 11.071 1.00 36.81 C HETATM 3205 C23 CLR A1204 -8.462 0.720 10.935 1.00 36.87 C HETATM 3206 C24 CLR A1204 -7.642 -0.549 11.163 1.00 41.15 C HETATM 3207 C25 CLR A1204 -8.406 -1.852 10.895 1.00 43.83 C HETATM 3208 C26 CLR A1204 -7.432 -2.982 10.566 1.00 45.91 C HETATM 3209 C27 CLR A1204 -9.283 -2.253 12.081 1.00 40.82 C HETATM 3210 O1 CLR A1204 -7.092 14.395 12.925 1.00 31.82 O HETATM 3211 C1 CLR A1205 -3.035 8.274 21.142 1.00 24.53 C HETATM 3212 C2 CLR A1205 -2.808 9.798 21.091 1.00 23.97 C HETATM 3213 C3 CLR A1205 -1.881 10.198 19.978 1.00 27.93 C HETATM 3214 C4 CLR A1205 -2.301 9.605 18.618 1.00 30.04 C HETATM 3215 C5 CLR A1205 -2.585 8.126 18.702 1.00 27.25 C HETATM 3216 C6 CLR A1205 -2.050 7.298 17.781 1.00 27.63 C HETATM 3217 C7 CLR A1205 -2.338 5.809 17.663 1.00 30.20 C HETATM 3218 C8 CLR A1205 -3.495 5.391 18.565 1.00 27.50 C HETATM 3219 C9 CLR A1205 -3.414 6.117 19.918 1.00 25.42 C HETATM 3220 C10 CLR A1205 -3.485 7.646 19.817 1.00 27.36 C HETATM 3221 C11 CLR A1205 -4.429 5.544 20.909 1.00 27.40 C HETATM 3222 C12 CLR A1205 -4.412 4.019 20.975 1.00 27.81 C HETATM 3223 C13 CLR A1205 -4.595 3.354 19.634 1.00 31.22 C HETATM 3224 C14 CLR A1205 -3.458 3.892 18.777 1.00 29.31 C HETATM 3225 C15 CLR A1205 -3.481 3.015 17.525 1.00 31.48 C HETATM 3226 C16 CLR A1205 -4.031 1.682 18.030 1.00 32.27 C HETATM 3227 C17 CLR A1205 -4.383 1.841 19.512 1.00 31.81 C HETATM 3228 C18 CLR A1205 -5.989 3.707 19.036 1.00 25.43 C HETATM 3229 C19 CLR A1205 -4.931 8.130 19.500 1.00 27.64 C HETATM 3230 C20 CLR A1205 -5.486 0.848 19.910 1.00 34.06 C HETATM 3231 C21 CLR A1205 -5.942 0.957 21.369 1.00 29.49 C HETATM 3232 C22 CLR A1205 -4.974 -0.584 19.670 1.00 40.85 C HETATM 3233 C23 CLR A1205 -6.000 -1.696 19.925 1.00 44.80 C HETATM 3234 C24 CLR A1205 -5.262 -3.030 20.066 1.00 51.65 C HETATM 3235 C25 CLR A1205 -5.776 -4.147 19.146 1.00 57.14 C HETATM 3236 C26 CLR A1205 -6.260 -3.607 17.802 1.00 58.15 C HETATM 3237 C27 CLR A1205 -4.711 -5.215 18.917 1.00 58.32 C HETATM 3238 O1 CLR A1205 -1.887 11.625 19.876 1.00 28.15 O HETATM 3239 C1 OLA A1206 -36.237 14.787 12.746 1.00 66.73 C HETATM 3240 O1 OLA A1206 -35.551 15.823 12.519 1.00 69.17 O HETATM 3241 O2 OLA A1206 -37.106 14.842 13.632 1.00 69.47 O HETATM 3242 C2 OLA A1206 -36.024 13.503 11.973 1.00 60.70 C HETATM 3243 C3 OLA A1206 -36.452 12.276 12.779 1.00 54.60 C HETATM 3244 C4 OLA A1206 -35.749 11.000 12.332 1.00 48.18 C HETATM 3245 C5 OLA A1206 -36.682 9.828 12.094 1.00 43.13 C HETATM 3246 C6 OLA A1206 -35.990 8.474 12.148 1.00 42.05 C HETATM 3247 C7 OLA A1206 -36.581 7.456 11.181 1.00 40.28 C HETATM 3248 C8 OLA A1206 -36.144 6.027 11.435 1.00 41.94 C HETATM 3249 C9 OLA A1206 -35.791 5.362 10.111 1.00 47.09 C HETATM 3250 C10 OLA A1206 -36.520 4.412 9.481 1.00 52.32 C HETATM 3251 C11 OLA A1206 -37.826 3.866 10.020 1.00 55.03 C HETATM 3252 C12 OLA A1206 -37.906 2.330 9.921 1.00 57.23 C HETATM 3253 C13 OLA A1206 -38.355 1.653 11.233 1.00 60.40 C HETATM 3254 C14 OLA A1206 -39.178 0.371 11.019 1.00 61.74 C HETATM 3255 C15 OLA A1206 -38.977 -0.686 12.123 1.00 61.59 C HETATM 3256 C16 OLA A1206 -38.683 -2.094 11.577 1.00 61.90 C HETATM 3257 C17 OLA A1206 -39.839 -3.087 11.779 1.00 61.55 C HETATM 3258 C18 OLA A1206 -39.607 -4.411 11.034 1.00 59.73 C HETATM 3259 C1 OLA A1207 -20.474 -22.058 27.869 1.00 58.27 C HETATM 3260 O1 OLA A1207 -20.871 -21.599 26.764 1.00 63.63 O HETATM 3261 O2 OLA A1207 -20.521 -23.287 28.029 1.00 61.52 O HETATM 3262 C2 OLA A1207 -19.958 -21.159 28.973 1.00 54.58 C HETATM 3263 C3 OLA A1207 -20.252 -19.686 28.684 1.00 49.42 C HETATM 3264 C4 OLA A1207 -19.378 -18.730 29.484 1.00 47.36 C HETATM 3265 C5 OLA A1207 -19.909 -17.313 29.508 1.00 46.42 C HETATM 3266 C6 OLA A1207 -19.030 -16.288 28.807 1.00 44.51 C HETATM 3267 C7 OLA A1207 -19.728 -14.938 28.673 1.00 47.93 C HETATM 3268 C1 OLA A1208 -28.404 -21.059 34.953 1.00 76.54 C HETATM 3269 O1 OLA A1208 -27.282 -20.481 34.889 1.00 75.26 O HETATM 3270 O2 OLA A1208 -28.415 -22.303 34.953 1.00 75.49 O HETATM 3271 C2 OLA A1208 -29.714 -20.293 35.022 1.00 76.75 C HETATM 3272 C3 OLA A1208 -29.645 -19.000 35.843 1.00 74.19 C HETATM 3273 C4 OLA A1208 -30.902 -18.143 35.704 1.00 72.80 C HETATM 3274 C5 OLA A1208 -30.738 -16.706 36.167 1.00 73.34 C HETATM 3275 C6 OLA A1208 -31.414 -15.653 35.293 1.00 72.77 C HETATM 3276 C7 OLA A1208 -31.580 -14.320 36.025 1.00 72.84 C HETATM 3277 C8 OLA A1208 -30.625 -13.216 35.599 1.00 73.13 C HETATM 3278 C9 OLA A1208 -30.551 -12.164 36.700 1.00 70.91 C HETATM 3279 C10 OLA A1208 -29.522 -11.317 36.943 1.00 68.82 C HETATM 3280 C11 OLA A1208 -28.238 -11.272 36.138 1.00 67.04 C HETATM 3281 C12 OLA A1208 -27.014 -10.858 36.982 1.00 63.43 C HETATM 3282 C13 OLA A1208 -27.177 -9.515 37.727 1.00 63.97 C HETATM 3283 C14 OLA A1208 -26.734 -8.294 36.902 1.00 61.41 C HETATM 3284 C15 OLA A1208 -26.352 -7.061 37.747 1.00 55.73 C HETATM 3285 C16 OLA A1208 -26.764 -5.728 37.100 1.00 47.54 C HETATM 3286 C17 OLA A1208 -28.250 -5.679 36.719 1.00 46.39 C HETATM 3287 C18 OLA A1208 -28.799 -4.248 36.650 1.00 46.76 C HETATM 3288 C1 OLA A1209 -21.342 12.601 3.717 1.00 73.84 C HETATM 3289 O1 OLA A1209 -20.603 13.242 2.951 1.00 75.66 O HETATM 3290 O2 OLA A1209 -21.356 12.927 4.936 1.00 75.24 O HETATM 3291 C2 OLA A1209 -22.190 11.464 3.184 1.00 68.84 C HETATM 3292 C3 OLA A1209 -21.325 10.322 2.647 1.00 63.72 C HETATM 3293 C4 OLA A1209 -21.623 8.979 3.300 1.00 60.21 C HETATM 3294 C5 OLA A1209 -20.419 8.061 3.373 1.00 58.72 C HETATM 3295 C6 OLA A1209 -20.639 6.792 4.185 1.00 55.17 C HETATM 3296 C7 OLA A1209 -21.836 6.002 3.664 1.00 54.00 C HETATM 3297 C8 OLA A1209 -21.507 4.602 3.186 1.00 56.54 C HETATM 3298 C9 OLA A1209 -20.780 4.691 1.852 1.00 58.09 C HETATM 3299 C10 OLA A1209 -20.471 3.637 1.066 1.00 59.65 C HETATM 3300 C11 OLA A1209 -20.821 2.210 1.427 1.00 61.87 C HETATM 3301 C12 OLA A1209 -19.667 1.513 2.173 1.00 64.64 C HETATM 3302 C13 OLA A1209 -20.078 0.199 2.873 1.00 66.75 C HETATM 3303 C14 OLA A1209 -19.185 -0.144 4.078 1.00 66.21 C HETATM 3304 C15 OLA A1209 -18.979 -1.654 4.294 1.00 65.84 C HETATM 3305 C16 OLA A1209 -17.777 -2.221 3.519 1.00 64.37 C HETATM 3306 C1 OLA A1210 -39.122 12.311 9.024 1.00 83.76 C HETATM 3307 O1 OLA A1210 -40.232 12.894 8.873 1.00 86.26 O HETATM 3308 O2 OLA A1210 -38.087 12.984 8.887 1.00 85.82 O HETATM 3309 C2 OLA A1210 -39.036 10.838 9.363 1.00 78.46 C HETATM 3310 C3 OLA A1210 -40.304 10.087 8.952 1.00 74.56 C HETATM 3311 C4 OLA A1210 -40.124 8.576 8.956 1.00 72.46 C HETATM 3312 C5 OLA A1210 -41.168 7.827 8.155 1.00 69.97 C HETATM 3313 C6 OLA A1210 -41.076 6.314 8.294 1.00 68.50 C HETATM 3314 C7 OLA A1210 -42.156 5.587 7.499 1.00 69.58 C HETATM 3315 C8 OLA A1210 -41.866 4.116 7.261 1.00 73.15 C HETATM 3316 C9 OLA A1210 -43.177 3.342 7.255 1.00 75.75 C HETATM 3317 C10 OLA A1210 -43.440 2.233 7.984 1.00 74.57 C HETATM 3318 C11 OLA A1210 -42.439 1.600 8.928 1.00 72.09 C HETATM 3319 C12 OLA A1210 -42.422 0.064 8.816 1.00 71.40 C HETATM 3320 C13 OLA A1210 -43.363 -0.636 9.817 1.00 72.09 C HETATM 3321 C1 OLA A1211 -36.176 -15.391 5.147 1.00 81.12 C HETATM 3322 O1 OLA A1211 -36.746 -14.452 5.766 1.00 81.94 O HETATM 3323 O2 OLA A1211 -35.962 -16.446 5.766 1.00 82.55 O HETATM 3324 C2 OLA A1211 -35.763 -15.256 3.695 1.00 78.49 C HETATM 3325 C3 OLA A1211 -34.261 -15.474 3.493 1.00 74.78 C HETATM 3326 C4 OLA A1211 -33.877 -15.601 2.024 1.00 70.78 C HETATM 3327 C5 OLA A1211 -33.077 -14.425 1.499 1.00 66.38 C HETATM 3328 C6 OLA A1211 -31.584 -14.495 1.787 1.00 62.08 C HETATM 3329 C7 OLA A1211 -31.155 -13.395 2.753 1.00 57.03 C HETATM 3330 C8 OLA A1211 -29.690 -13.427 3.147 1.00 55.95 C HETATM 3331 C9 OLA A1211 -29.164 -12.000 3.125 1.00 57.80 C HETATM 3332 C10 OLA A1211 -28.039 -11.567 3.734 1.00 58.09 C HETATM 3333 C1 OLA A1212 -15.791 13.064 0.849 1.00 67.32 C HETATM 3334 O1 OLA A1212 -14.639 12.699 0.484 1.00 68.32 O HETATM 3335 O2 OLA A1212 -15.914 14.202 1.331 1.00 65.65 O HETATM 3336 C2 OLA A1212 -16.995 12.153 0.714 1.00 67.70 C HETATM 3337 C3 OLA A1212 -16.751 10.798 1.383 1.00 69.01 C HETATM 3338 C4 OLA A1212 -17.089 9.603 0.500 1.00 69.61 C HETATM 3339 C5 OLA A1212 -15.971 8.584 0.396 1.00 69.56 C HETATM 3340 C6 OLA A1212 -16.272 7.223 1.010 1.00 69.95 C HETATM 3341 C7 OLA A1212 -15.364 6.138 0.433 1.00 71.08 C HETATM 3342 C8 OLA A1212 -15.334 4.837 1.215 1.00 70.29 C HETATM 3343 C9 OLA A1212 -15.503 3.677 0.244 1.00 68.22 C HETATM 3344 C10 OLA A1212 -15.264 2.375 0.521 1.00 66.21 C HETATM 3345 C3 OLA A1213 -18.007 -14.655 3.161 1.00 68.40 C HETATM 3346 C4 OLA A1213 -18.307 -13.180 2.926 1.00 69.65 C HETATM 3347 C5 OLA A1213 -18.168 -12.324 4.170 1.00 70.87 C HETATM 3348 C6 OLA A1213 -16.889 -11.498 4.247 1.00 70.81 C HETATM 3349 C7 OLA A1213 -17.129 -10.046 3.838 1.00 71.88 C HETATM 3350 C8 OLA A1213 -16.170 -9.036 4.447 1.00 71.95 C HETATM 3351 C9 OLA A1213 -16.810 -8.425 5.687 1.00 70.51 C HETATM 3352 C10 OLA A1213 -16.818 -7.116 6.036 1.00 67.42 C HETATM 3353 C11 OLA A1213 -16.170 -6.020 5.218 1.00 67.01 C HETATM 3354 C12 OLA A1213 -17.191 -5.274 4.337 1.00 68.46 C HETATM 3355 C9 OLA A1214 -21.233 -11.829 0.481 1.00 63.43 C HETATM 3356 C10 OLA A1214 -20.819 -11.208 1.610 1.00 63.48 C HETATM 3357 C11 OLA A1214 -21.099 -9.752 1.920 1.00 61.13 C HETATM 3358 C12 OLA A1214 -21.788 -9.580 3.289 1.00 58.85 C HETATM 3359 C13 OLA A1214 -21.642 -8.171 3.903 1.00 55.67 C HETATM 3360 C14 OLA A1214 -21.838 -7.026 2.896 1.00 53.29 C HETATM 3361 C15 OLA A1214 -23.035 -6.102 3.203 1.00 50.51 C HETATM 3362 C16 OLA A1214 -22.946 -4.742 2.487 1.00 51.50 C HETATM 3363 C17 OLA A1214 -24.275 -3.971 2.436 1.00 52.33 C HETATM 3364 C18 OLA A1214 -24.082 -2.491 2.070 1.00 55.30 C HETATM 3365 C2 OLA A1215 -8.765 -15.403 16.830 1.00 47.71 C HETATM 3366 C3 OLA A1215 -10.211 -14.897 16.816 1.00 47.05 C HETATM 3367 C4 OLA A1215 -10.483 -13.826 17.864 1.00 48.66 C HETATM 3368 C5 OLA A1215 -10.139 -12.432 17.383 1.00 49.07 C HETATM 3369 C6 OLA A1215 -10.102 -11.357 18.457 1.00 45.46 C HETATM 3370 C7 OLA A1215 -9.237 -10.180 18.021 1.00 49.49 C HETATM 3371 C8 OLA A1215 -8.382 -9.567 19.113 1.00 53.10 C HETATM 3372 C9 OLA A1215 -8.064 -8.135 18.710 1.00 57.97 C HETATM 3373 C10 OLA A1215 -8.241 -7.041 19.485 1.00 59.67 C HETATM 3374 C1 OLA A1216 -43.693 -24.146 13.150 1.00 70.99 C HETATM 3375 O1 OLA A1216 -44.034 -24.837 12.152 1.00 73.02 O HETATM 3376 O2 OLA A1216 -42.923 -24.668 13.972 1.00 71.77 O HETATM 3377 C2 OLA A1216 -44.190 -22.728 13.358 1.00 70.26 C HETATM 3378 C3 OLA A1216 -43.193 -21.912 14.184 1.00 72.74 C HETATM 3379 C4 OLA A1216 -43.706 -20.545 14.623 1.00 76.46 C HETATM 3380 C5 OLA A1216 -42.686 -19.770 15.433 1.00 77.39 C HETATM 3381 C6 OLA A1216 -41.255 -20.265 15.263 1.00 77.69 C HETATM 3382 C7 OLA A1216 -40.274 -19.534 16.178 1.00 76.42 C HETATM 3383 C8 OLA A1216 -39.510 -18.398 15.522 1.00 72.58 C HETATM 3384 C9 OLA A1216 -38.271 -18.952 14.832 1.00 67.65 C HETATM 3385 C10 OLA A1216 -37.553 -18.319 13.876 1.00 63.50 C HETATM 3386 C11 OLA A1216 -37.880 -16.941 13.336 1.00 59.52 C HETATM 3387 C12 OLA A1216 -37.472 -15.804 14.295 1.00 56.87 C HETATM 3388 C13 OLA A1216 -37.724 -14.395 13.720 1.00 57.01 C HETATM 3389 C14 OLA A1216 -37.689 -13.275 14.773 1.00 58.62 C HETATM 3390 C15 OLA A1216 -38.235 -11.921 14.270 1.00 59.01 C HETATM 3391 C16 OLA A1216 -38.509 -10.910 15.399 1.00 59.09 C HETATM 3392 C17 OLA A1216 -38.430 -9.442 14.945 1.00 55.75 C HETATM 3393 C1 OLA A1217 -9.767 -15.090 7.456 1.00 61.49 C HETATM 3394 C2 OLA A1217 -11.121 -14.413 7.531 1.00 61.52 C HETATM 3395 C3 OLA A1217 -10.990 -12.902 7.730 1.00 61.21 C HETATM 3396 C4 OLA A1217 -11.130 -12.469 9.184 1.00 61.70 C HETATM 3397 C5 OLA A1217 -10.743 -13.548 10.176 1.00 62.81 C HETATM 3398 C6 OLA A1217 -9.979 -13.038 11.390 1.00 63.25 C HETATM 3399 C7 OLA A1217 -9.731 -11.534 11.291 1.00 64.58 C HETATM 3400 C8 OLA A1217 -8.736 -10.985 12.299 1.00 66.42 C HETATM 3401 C9 OLA A1217 -8.626 -9.481 12.106 1.00 66.54 C HETATM 3402 C10 OLA A1217 -8.390 -8.573 13.078 1.00 67.12 C HETATM 3403 C11 OLA A1217 -8.196 -8.936 14.535 1.00 67.60 C HETATM 3404 C12 OLA A1217 -7.590 -7.765 15.335 1.00 66.74 C HETATM 3405 C10 OLA A1218 -12.512 -3.927 6.923 1.00 65.15 C HETATM 3406 C11 OLA A1218 -12.055 -2.937 7.973 1.00 64.27 C HETATM 3407 C12 OLA A1218 -10.727 -2.259 7.587 1.00 65.51 C HETATM 3408 C13 OLA A1218 -10.582 -0.829 8.145 1.00 66.43 C HETATM 3409 C14 OLA A1218 -11.256 0.238 7.267 1.00 63.73 C HETATM 3410 C15 OLA A1218 -10.601 1.630 7.372 1.00 59.56 C HETATM 3411 C16 OLA A1218 -11.487 2.662 8.091 1.00 54.78 C HETATM 3412 C17 OLA A1218 -12.983 2.492 7.785 1.00 51.23 C HETATM 3413 C18 OLA A1218 -13.876 3.322 8.718 1.00 47.39 C HETATM 3414 C1 OLA A1219 -8.731 14.771 8.465 1.00 71.81 C HETATM 3415 O1 OLA A1219 -9.228 15.670 7.730 1.00 73.60 O HETATM 3416 O2 OLA A1219 -8.875 14.875 9.696 1.00 73.26 O HETATM 3417 C2 OLA A1219 -7.979 13.593 7.881 1.00 65.74 C HETATM 3418 C3 OLA A1219 -8.881 12.712 7.016 1.00 61.61 C HETATM 3419 C4 OLA A1219 -8.460 11.248 7.018 1.00 61.95 C HETATM 3420 C5 OLA A1219 -9.064 10.436 5.891 1.00 62.39 C HETATM 3421 C6 OLA A1219 -9.540 9.050 6.299 1.00 65.45 C HETATM 3422 C7 OLA A1219 -8.372 8.083 6.473 1.00 68.73 C HETATM 3423 C8 OLA A1219 -8.300 6.987 5.426 1.00 72.48 C HETATM 3424 C9 OLA A1219 -8.999 5.749 5.968 1.00 74.99 C HETATM 3425 C10 OLA A1219 -10.046 5.106 5.403 1.00 75.48 C HETATM 3426 C11 OLA A1219 -10.707 5.525 4.107 1.00 73.14 C HETATM 3427 C12 OLA A1219 -11.779 4.511 3.660 1.00 71.30 C HETATM 3428 C13 OLA A1219 -11.313 3.585 2.519 1.00 72.38 C HETATM 3429 C14 OLA A1219 -10.897 2.186 3.002 1.00 74.81 C HETATM 3430 C10 OLC A1220 -5.993 -3.926 27.004 1.00 71.20 C HETATM 3431 C9 OLC A1220 -6.306 -3.094 27.983 1.00 72.29 C HETATM 3432 C8 OLC A1220 -5.751 -1.700 27.957 1.00 74.39 C HETATM 3433 C24 OLC A1220 -3.218 10.687 29.738 1.00 83.67 C HETATM 3434 C7 OLC A1220 -5.652 -1.173 29.382 1.00 75.51 C HETATM 3435 C6 OLC A1220 -4.486 -0.210 29.578 1.00 75.16 C HETATM 3436 C5 OLC A1220 -4.930 1.214 29.328 1.00 74.94 C HETATM 3437 C4 OLC A1220 -3.935 2.190 29.916 1.00 75.46 C HETATM 3438 C3 OLC A1220 -4.440 3.610 29.766 1.00 76.36 C HETATM 3439 C2 OLC A1220 -3.824 4.587 30.761 1.00 79.30 C HETATM 3440 C21 OLC A1220 -3.902 8.368 30.103 1.00 82.63 C HETATM 3441 C1 OLC A1220 -3.750 5.944 30.117 1.00 81.10 C HETATM 3442 C22 OLC A1220 -3.045 9.484 30.630 1.00 82.46 C HETATM 3443 O19 OLC A1220 -3.789 6.019 28.926 1.00 82.42 O HETATM 3444 O25 OLC A1220 -4.607 10.834 29.479 1.00 82.33 O HETATM 3445 O23 OLC A1220 -3.500 9.808 31.934 1.00 82.53 O HETATM 3446 O20 OLC A1220 -3.635 7.186 30.838 1.00 82.60 O HETATM 3447 C10 OLC A1221 -3.891 2.044 25.678 1.00 57.34 C HETATM 3448 C9 OLC A1221 -3.730 3.356 25.660 1.00 56.51 C HETATM 3449 C11 OLC A1221 -3.133 1.146 24.764 1.00 55.62 C HETATM 3450 C8 OLC A1221 -2.812 4.042 24.716 1.00 49.72 C HETATM 3451 C24 OLC A1221 -0.126 16.696 24.665 1.00 69.25 C HETATM 3452 C12 OLC A1221 -3.739 -0.237 24.874 1.00 58.03 C HETATM 3453 C7 OLC A1221 -3.270 5.477 24.557 1.00 40.88 C HETATM 3454 C6 OLC A1221 -2.708 6.431 25.572 1.00 33.22 C HETATM 3455 C5 OLC A1221 -2.673 7.792 24.955 1.00 32.12 C HETATM 3456 C4 OLC A1221 -2.189 8.820 25.919 1.00 37.48 C HETATM 3457 C3 OLC A1221 -1.991 10.128 25.223 1.00 37.08 C HETATM 3458 C2 OLC A1221 -2.566 11.216 26.085 1.00 48.23 C HETATM 3459 C21 OLC A1221 -0.784 14.433 25.188 1.00 64.50 C HETATM 3460 C1 OLC A1221 -1.655 12.387 26.108 1.00 55.59 C HETATM 3461 C22 OLC A1221 -1.245 15.870 25.258 1.00 68.09 C HETATM 3462 O19 OLC A1221 -0.739 12.403 26.870 1.00 58.86 O HETATM 3463 O25 OLC A1221 0.663 17.217 25.718 1.00 67.52 O HETATM 3464 O23 OLC A1221 -2.445 16.089 24.526 1.00 68.74 O HETATM 3465 O20 OLC A1221 -1.847 13.516 25.255 1.00 59.17 O HETATM 3466 C9 OLC A1222 -30.640 -1.638 38.755 1.00 49.16 C HETATM 3467 C8 OLC A1222 -30.067 -0.499 37.979 1.00 47.05 C HETATM 3468 C24 OLC A1222 -28.716 10.314 34.569 1.00 61.46 C HETATM 3469 C7 OLC A1222 -30.636 0.828 38.430 1.00 49.65 C HETATM 3470 C6 OLC A1222 -31.891 1.257 37.712 1.00 53.91 C HETATM 3471 C5 OLC A1222 -32.254 2.713 37.957 1.00 54.61 C HETATM 3472 C4 OLC A1222 -31.735 3.593 36.845 1.00 53.43 C HETATM 3473 C3 OLC A1222 -32.380 4.961 36.809 1.00 55.05 C HETATM 3474 C2 OLC A1222 -31.517 5.905 35.999 1.00 58.68 C HETATM 3475 C21 OLC A1222 -30.536 9.482 36.068 1.00 64.36 C HETATM 3476 C1 OLC A1222 -31.793 7.324 36.376 1.00 62.40 C HETATM 3477 C22 OLC A1222 -29.038 9.589 35.868 1.00 64.97 C HETATM 3478 O19 OLC A1222 -32.912 7.721 36.464 1.00 65.64 O HETATM 3479 O25 OLC A1222 -28.232 11.638 34.764 1.00 61.80 O HETATM 3480 O23 OLC A1222 -28.479 10.259 36.995 1.00 67.31 O HETATM 3481 O20 OLC A1222 -30.712 8.223 36.677 1.00 65.66 O HETATM 3482 C10 OLC A1223 -42.151 4.251 12.469 1.00 56.08 C HETATM 3483 C9 OLC A1223 -41.489 5.361 12.234 1.00 55.14 C HETATM 3484 C11 OLC A1223 -42.741 3.899 13.791 1.00 53.83 C HETATM 3485 C8 OLC A1223 -41.205 6.403 13.262 1.00 52.28 C HETATM 3486 C24 OLC A1223 -45.026 17.988 12.567 1.00 84.18 C HETATM 3487 C12 OLC A1223 -43.647 2.711 13.589 1.00 52.80 C HETATM 3488 C7 OLC A1223 -40.950 7.698 12.532 1.00 49.59 C HETATM 3489 C15 OLC A1223 -43.668 -0.974 14.354 1.00 53.54 C HETATM 3490 C13 OLC A1223 -43.036 1.419 14.068 1.00 50.80 C HETATM 3491 C6 OLC A1223 -40.931 8.873 13.481 1.00 48.98 C HETATM 3492 C14 OLC A1223 -43.774 0.255 13.475 1.00 49.89 C HETATM 3493 C5 OLC A1223 -41.173 10.168 12.742 1.00 50.90 C HETATM 3494 C4 OLC A1223 -41.078 11.321 13.694 1.00 51.76 C HETATM 3495 C3 OLC A1223 -41.494 12.635 13.086 1.00 55.50 C HETATM 3496 C2 OLC A1223 -40.888 13.692 13.974 1.00 62.01 C HETATM 3497 C21 OLC A1223 -42.987 16.565 12.652 1.00 80.78 C HETATM 3498 C1 OLC A1223 -41.394 15.061 13.660 1.00 69.87 C HETATM 3499 C22 OLC A1223 -44.486 16.573 12.497 1.00 82.69 C HETATM 3500 O19 OLC A1223 -40.855 16.057 14.116 1.00 69.81 O HETATM 3501 O25 OLC A1223 -44.202 18.791 13.382 1.00 83.08 O HETATM 3502 O23 OLC A1223 -44.803 16.043 11.204 1.00 78.87 O HETATM 3503 O20 OLC A1223 -42.540 15.221 12.819 1.00 75.88 O HETATM 3504 C18 OLC A1224 -21.740 -3.174 35.354 1.00 53.48 C HETATM 3505 C10 OLC A1224 -23.145 -11.023 38.515 1.00 70.04 C HETATM 3506 C9 OLC A1224 -23.370 -12.303 38.204 1.00 71.40 C HETATM 3507 C17 OLC A1224 -22.742 -3.977 36.123 1.00 54.56 C HETATM 3508 C11 OLC A1224 -24.082 -10.135 39.306 1.00 67.20 C HETATM 3509 C8 OLC A1224 -24.625 -13.062 38.567 1.00 70.98 C HETATM 3510 C24 OLC A1224 -24.488 -24.231 38.187 1.00 91.76 C HETATM 3511 C16 OLC A1224 -22.101 -5.210 36.721 1.00 55.88 C HETATM 3512 C12 OLC A1224 -23.994 -8.704 38.770 1.00 64.93 C HETATM 3513 C7 OLC A1224 -24.481 -14.563 38.353 1.00 69.86 C HETATM 3514 C15 OLC A1224 -23.002 -5.891 37.747 1.00 56.30 C HETATM 3515 C13 OLC A1224 -23.068 -7.756 39.528 1.00 57.74 C HETATM 3516 C6 OLC A1224 -25.824 -15.206 38.664 1.00 69.97 C HETATM 3517 C14 OLC A1224 -22.232 -6.886 38.606 1.00 56.02 C HETATM 3518 C5 OLC A1224 -25.821 -16.635 39.164 1.00 70.39 C HETATM 3519 C4 OLC A1224 -27.262 -17.138 39.139 1.00 75.34 C HETATM 3520 C3 OLC A1224 -27.518 -18.409 39.948 1.00 80.11 C HETATM 3521 C2 OLC A1224 -27.074 -19.676 39.239 1.00 83.31 C HETATM 3522 C21 OLC A1224 -26.091 -22.979 39.713 1.00 90.20 C HETATM 3523 C1 OLC A1224 -27.651 -20.935 39.837 1.00 86.03 C HETATM 3524 C22 OLC A1224 -25.925 -24.036 38.620 1.00 91.65 C HETATM 3525 O19 OLC A1224 -28.473 -20.906 40.720 1.00 86.52 O HETATM 3526 O25 OLC A1224 -24.499 -25.119 37.071 1.00 91.56 O HETATM 3527 O23 OLC A1224 -26.420 -25.316 39.017 1.00 93.67 O HETATM 3528 O20 OLC A1224 -27.224 -22.218 39.321 1.00 87.84 O HETATM 3529 C18 OLC A1225 -41.296 -4.982 14.730 1.00 68.35 C HETATM 3530 C10 OLC A1225 -38.341 3.157 14.735 1.00 49.19 C HETATM 3531 C9 OLC A1225 -37.792 4.348 14.818 1.00 44.89 C HETATM 3532 C17 OLC A1225 -41.491 -3.702 15.510 1.00 68.27 C HETATM 3533 C11 OLC A1225 -38.578 2.287 15.919 1.00 49.15 C HETATM 3534 C8 OLC A1225 -37.312 4.935 16.096 1.00 40.27 C HETATM 3535 C24 OLC A1225 -37.682 16.492 18.092 1.00 80.61 C HETATM 3536 C16 OLC A1225 -40.452 -3.574 16.602 1.00 66.41 C HETATM 3537 C12 OLC A1225 -39.248 1.036 15.403 1.00 51.98 C HETATM 3538 C7 OLC A1225 -37.160 6.406 15.868 1.00 40.44 C HETATM 3539 C15 OLC A1225 -40.419 -2.161 17.148 1.00 65.85 C HETATM 3540 C13 OLC A1225 -39.689 0.156 16.555 1.00 56.79 C HETATM 3541 C6 OLC A1225 -37.493 7.143 17.129 1.00 44.08 C HETATM 3542 C14 OLC A1225 -40.169 -1.177 16.027 1.00 62.93 C HETATM 3543 C5 OLC A1225 -37.097 8.589 17.106 1.00 42.52 C HETATM 3544 C4 OLC A1225 -38.100 9.503 16.467 1.00 47.01 C HETATM 3545 C3 OLC A1225 -37.845 10.888 17.001 1.00 47.18 C HETATM 3546 C2 OLC A1225 -38.506 12.013 16.224 1.00 54.91 C HETATM 3547 C21 OLC A1225 -39.789 15.200 17.985 1.00 70.82 C HETATM 3548 C1 OLC A1225 -39.052 13.003 17.206 1.00 58.60 C HETATM 3549 C22 OLC A1225 -38.710 15.734 18.910 1.00 79.01 C HETATM 3550 O19 OLC A1225 -39.379 12.610 18.271 1.00 60.25 O HETATM 3551 O25 OLC A1225 -37.995 17.871 18.012 1.00 80.60 O HETATM 3552 O23 OLC A1225 -39.247 16.578 19.940 1.00 82.85 O HETATM 3553 O20 OLC A1225 -39.199 14.414 16.972 1.00 63.27 O HETATM 3554 C10 OLC A1226 -33.768 -8.096 24.668 1.00 50.11 C HETATM 3555 C9 OLC A1226 -33.531 -9.387 24.612 1.00 47.23 C HETATM 3556 C17 OLC A1226 -37.306 -0.538 23.263 1.00 66.52 C HETATM 3557 C11 OLC A1226 -34.496 -7.326 23.616 1.00 56.45 C HETATM 3558 C8 OLC A1226 -33.922 -10.288 23.488 1.00 44.87 C HETATM 3559 C24 OLC A1226 -31.832 -23.346 24.710 1.00 76.26 C HETATM 3560 C16 OLC A1226 -36.020 -1.351 23.231 1.00 66.94 C HETATM 3561 C12 OLC A1226 -34.810 -5.922 24.122 1.00 61.28 C HETATM 3562 C7 OLC A1226 -33.081 -11.529 23.658 1.00 43.21 C HETATM 3563 C15 OLC A1226 -36.241 -2.753 23.782 1.00 68.24 C HETATM 3564 C13 OLC A1226 -35.899 -5.238 23.308 1.00 64.91 C HETATM 3565 C6 OLC A1226 -33.515 -12.715 22.835 1.00 45.76 C HETATM 3566 C14 OLC A1226 -35.499 -3.808 22.970 1.00 67.76 C HETATM 3567 C5 OLC A1226 -32.560 -13.852 23.111 1.00 48.81 C HETATM 3568 C4 OLC A1226 -32.845 -15.070 22.269 1.00 52.00 C HETATM 3569 C3 OLC A1226 -32.007 -16.266 22.654 1.00 52.54 C HETATM 3570 C2 OLC A1226 -32.835 -17.519 22.499 1.00 60.88 C HETATM 3571 C21 OLC A1226 -31.738 -21.018 23.712 1.00 73.10 C HETATM 3572 C1 OLC A1226 -31.992 -18.729 22.738 1.00 67.99 C HETATM 3573 C22 OLC A1226 -32.520 -22.324 23.814 1.00 76.12 C HETATM 3574 O19 OLC A1226 -30.813 -18.621 22.650 1.00 72.86 O HETATM 3575 O25 OLC A1226 -32.773 -24.324 25.159 1.00 75.71 O HETATM 3576 O23 OLC A1226 -33.794 -22.032 24.354 1.00 78.11 O HETATM 3577 O20 OLC A1226 -32.537 -20.024 23.079 1.00 70.61 O HETATM 3578 C10 OLC A1227 -35.612 -9.870 18.202 1.00 60.95 C HETATM 3579 C9 OLC A1227 -35.508 -11.064 17.680 1.00 55.88 C HETATM 3580 C11 OLC A1227 -35.658 -9.748 19.694 1.00 64.43 C HETATM 3581 C8 OLC A1227 -35.442 -12.193 18.638 1.00 53.33 C HETATM 3582 C24 OLC A1227 -35.043 -24.740 20.573 1.00 75.14 C HETATM 3583 C7 OLC A1227 -35.465 -13.462 17.844 1.00 52.95 C HETATM 3584 C6 OLC A1227 -35.203 -14.645 18.738 1.00 54.29 C HETATM 3585 C5 OLC A1227 -35.435 -15.880 17.912 1.00 56.79 C HETATM 3586 C4 OLC A1227 -35.544 -17.106 18.773 1.00 57.67 C HETATM 3587 C3 OLC A1227 -35.566 -18.341 17.909 1.00 59.39 C HETATM 3588 C2 OLC A1227 -35.349 -19.537 18.797 1.00 60.87 C HETATM 3589 C21 OLC A1227 -34.884 -22.765 19.057 1.00 71.14 C HETATM 3590 C1 OLC A1227 -34.533 -20.560 18.080 1.00 62.84 C HETATM 3591 C22 OLC A1227 -34.165 -23.622 20.057 1.00 74.10 C HETATM 3592 O19 OLC A1227 -34.332 -20.450 16.918 1.00 65.10 O HETATM 3593 O25 OLC A1227 -34.197 -25.749 21.126 1.00 75.31 O HETATM 3594 O23 OLC A1227 -33.071 -24.161 19.348 1.00 76.72 O HETATM 3595 O20 OLC A1227 -34.005 -21.703 18.759 1.00 66.18 O HETATM 3596 C18 OLC A1228 -37.191 6.970 4.667 1.00 65.88 C HETATM 3597 C10 OLC A1228 -34.731 14.861 8.588 1.00 75.81 C HETATM 3598 C9 OLC A1228 -33.695 15.630 8.883 1.00 76.95 C HETATM 3599 C17 OLC A1228 -36.441 7.137 5.964 1.00 64.41 C HETATM 3600 C11 OLC A1228 -34.549 13.656 7.702 1.00 73.63 C HETATM 3601 C8 OLC A1228 -32.332 15.300 8.331 1.00 77.06 C HETATM 3602 C24 OLC A1228 -25.418 20.870 12.133 1.00 98.71 C HETATM 3603 C16 OLC A1228 -36.718 8.512 6.524 1.00 63.44 C HETATM 3604 C12 OLC A1228 -34.544 12.416 8.579 1.00 71.95 C HETATM 3605 C7 OLC A1228 -31.536 16.582 8.168 1.00 76.75 C HETATM 3606 C15 OLC A1228 -35.605 8.972 7.429 1.00 63.18 C HETATM 3607 C13 OLC A1228 -34.488 11.149 7.763 1.00 68.18 C HETATM 3608 C6 OLC A1228 -30.089 16.289 7.805 1.00 76.29 C HETATM 3609 C14 OLC A1228 -35.810 10.426 7.784 1.00 65.60 C HETATM 3610 C5 OLC A1228 -29.245 15.978 9.022 1.00 75.84 C HETATM 3611 C4 OLC A1228 -27.965 16.799 9.033 1.00 77.85 C HETATM 3612 C3 OLC A1228 -27.131 16.569 10.291 1.00 80.20 C HETATM 3613 C2 OLC A1228 -27.437 17.548 11.420 1.00 82.22 C HETATM 3614 C21 OLC A1228 -26.976 19.696 13.665 1.00 91.96 C HETATM 3615 C1 OLC A1228 -26.321 17.592 12.438 1.00 83.75 C HETATM 3616 C22 OLC A1228 -25.848 20.712 13.589 1.00 96.46 C HETATM 3617 O19 OLC A1228 -25.274 17.005 12.256 1.00 82.39 O HETATM 3618 O25 OLC A1228 -24.137 21.501 12.081 1.00 98.95 O HETATM 3619 O23 OLC A1228 -26.269 21.974 14.123 1.00 95.36 O HETATM 3620 O20 OLC A1228 -26.463 18.373 13.646 1.00 87.31 O HETATM 3621 C10 OLC A1229 -30.031 -1.708 33.289 1.00 62.22 C HETATM 3622 C9 OLC A1229 -30.996 -0.808 33.263 1.00 60.24 C HETATM 3623 C8 OLC A1229 -30.679 0.658 33.264 1.00 58.87 C HETATM 3624 C24 OLC A1229 -35.076 12.733 33.723 1.00 88.30 C HETATM 3625 C7 OLC A1229 -32.006 1.379 33.183 1.00 61.70 C HETATM 3626 C6 OLC A1229 -31.936 2.749 32.548 1.00 64.03 C HETATM 3627 C5 OLC A1229 -33.317 3.117 32.021 1.00 67.15 C HETATM 3628 C4 OLC A1229 -34.014 4.156 32.892 1.00 69.73 C HETATM 3629 C3 OLC A1229 -33.797 5.577 32.407 1.00 71.54 C HETATM 3630 C2 OLC A1229 -34.658 6.562 33.171 1.00 76.65 C HETATM 3631 C21 OLC A1229 -35.075 10.313 33.208 1.00 86.61 C HETATM 3632 C1 OLC A1229 -34.161 7.969 32.967 1.00 81.89 C HETATM 3633 C22 OLC A1229 -34.314 11.437 33.878 1.00 87.84 C HETATM 3634 O19 OLC A1229 -33.306 8.202 32.165 1.00 83.90 O HETATM 3635 O25 OLC A1229 -34.137 13.795 33.894 1.00 88.49 O HETATM 3636 O23 OLC A1229 -34.145 11.165 35.267 1.00 89.66 O HETATM 3637 O20 OLC A1229 -34.663 9.071 33.753 1.00 85.23 O HETATM 3638 C10 OLC A1230 -34.494 -10.446 28.761 1.00 63.59 C HETATM 3639 C9 OLC A1230 -34.487 -11.627 28.174 1.00 61.22 C HETATM 3640 C17 OLC A1230 -31.834 -4.247 33.199 1.00 56.93 C HETATM 3641 C11 OLC A1230 -33.316 -9.684 29.292 1.00 61.68 C HETATM 3642 C8 OLC A1230 -33.284 -12.466 27.911 1.00 56.21 C HETATM 3643 C16 OLC A1230 -32.540 -5.444 32.568 1.00 56.95 C HETATM 3644 C12 OLC A1230 -33.505 -8.174 29.129 1.00 58.73 C HETATM 3645 C7 OLC A1230 -33.730 -13.576 26.964 1.00 52.30 C HETATM 3646 C15 OLC A1230 -33.348 -5.056 31.335 1.00 55.70 C HETATM 3647 C13 OLC A1230 -33.228 -7.446 30.416 1.00 57.85 C HETATM 3648 C6 OLC A1230 -32.971 -14.893 27.076 1.00 49.55 C HETATM 3649 C14 OLC A1230 -34.071 -6.185 30.585 1.00 56.26 C HETATM 3650 C5 OLC A1230 -33.827 -16.119 27.229 1.00 48.61 C HETATM 3651 C4 OLC A1230 -33.294 -17.425 26.714 1.00 51.32 C HETATM 3652 O1 TAR A1231 -21.562 12.070 37.334 0.49 92.28 O HETATM 3653 O11 TAR A1231 -19.586 12.990 37.373 0.49 92.47 O1- HETATM 3654 C1 TAR A1231 -20.516 12.432 36.733 0.49 92.34 C HETATM 3655 C2 TAR A1231 -20.382 12.201 35.243 0.49 92.02 C HETATM 3656 O2 TAR A1231 -21.036 13.259 34.580 0.49 92.06 O HETATM 3657 C3 TAR A1231 -18.941 12.171 34.778 0.49 92.02 C HETATM 3658 O3 TAR A1231 -18.253 13.214 35.428 0.49 92.03 O HETATM 3659 C4 TAR A1231 -18.798 12.381 33.286 0.49 92.37 C HETATM 3660 O4 TAR A1231 -19.769 12.814 32.612 0.49 92.40 O HETATM 3661 O41 TAR A1231 -17.704 12.123 32.717 0.49 92.21 O1- HETATM 3662 C1 OLA A1232 -34.274 8.807 1.748 0.60 68.80 C HETATM 3663 O1 OLA A1232 -34.513 9.728 2.577 0.60 69.15 O HETATM 3664 O2 OLA A1232 -33.096 8.435 1.627 0.60 69.11 O HETATM 3665 C2 OLA A1232 -35.370 8.164 0.918 0.60 68.20 C HETATM 3666 C3 OLA A1232 -35.598 6.695 1.290 0.60 67.16 C HETATM 3667 C4 OLA A1232 -34.503 5.760 0.787 0.60 65.87 C HETATM 3668 C5 OLA A1232 -34.988 4.357 0.475 0.60 65.28 C HETATM 3669 C6 OLA A1232 -34.145 3.234 1.069 0.60 65.28 C HETATM 3670 C7 OLA A1232 -33.798 2.162 0.036 0.60 65.04 C HETATM 3671 C8 OLA A1232 -33.404 0.815 0.617 0.60 64.73 C HETATM 3672 C9 OLA A1232 -32.741 -0.027 -0.464 0.60 64.47 C HETATM 3673 C10 OLA A1232 -32.940 -1.349 -0.672 0.60 64.75 C HETATM 3674 C11 OLA A1232 -33.876 -2.200 0.161 0.60 65.06 C HETATM 3675 C12 OLA A1232 -34.682 -3.190 -0.703 0.60 65.44 C HETATM 3676 C13 OLA A1232 -34.450 -4.670 -0.333 0.60 65.22 C HETATM 3677 C14 OLA A1232 -34.996 -5.654 -1.380 0.60 65.94 C HETATM 3678 C15 OLA A1232 -34.985 -7.126 -0.922 0.60 67.31 C HETATM 3679 C16 OLA A1232 -33.862 -7.960 -1.564 0.60 68.47 C HETATM 3680 C17 OLA A1232 -34.355 -8.913 -2.666 0.60 68.83 C HETATM 3681 C18 OLA A1232 -33.462 -10.155 -2.817 0.60 68.66 C HETATM 3682 C1 PGE A1233 -18.558 16.722 16.815 1.00109.46 C HETATM 3683 O1 PGE A1233 -19.454 16.450 17.885 1.00109.59 O HETATM 3684 C2 PGE A1233 -18.541 15.532 15.878 1.00108.55 C HETATM 3685 O2 PGE A1233 -17.855 15.871 14.690 1.00107.53 O HETATM 3686 C3 PGE A1233 -18.281 15.119 13.573 1.00105.50 C HETATM 3687 C4 PGE A1233 -17.249 15.241 12.469 1.00103.57 C HETATM 3688 O4 PGE A1233 -13.396 17.560 11.417 1.00 99.00 O HETATM 3689 C6 PGE A1233 -14.655 17.763 12.044 1.00102.55 C HETATM 3690 C5 PGE A1233 -15.596 16.664 11.598 1.00103.83 C HETATM 3691 O3 PGE A1233 -16.647 16.517 12.530 1.00102.92 O HETATM 3692 NA NA A1234 -23.539 -8.309 16.414 1.00 40.48 NA HETATM 3693 O HOH A1301 -26.777 13.346 34.404 1.00 71.40 O HETATM 3694 O HOH A1302 -40.592 17.718 15.723 1.00 74.19 O HETATM 3695 O HOH A1303 -4.280 -63.297 26.737 1.00 62.71 O HETATM 3696 O HOH A1304 -24.801 16.760 2.016 1.00 47.05 O HETATM 3697 O HOH A1305 0.414 13.634 28.590 1.00 64.86 O HETATM 3698 O HOH A1306 -18.419 12.745 23.772 1.00 48.83 O HETATM 3699 O HOH A1307 -23.473 15.626 33.108 1.00 42.83 O HETATM 3700 O HOH A1308 -21.409 15.116 17.086 1.00 55.74 O HETATM 3701 O HOH A1309 -27.582 3.109 16.852 1.00 18.95 O HETATM 3702 O HOH A1310 -27.790 3.499 19.557 1.00 27.67 O HETATM 3703 O HOH A1311 -27.947 12.152 38.659 1.00 50.68 O HETATM 3704 O HOH A1312 -16.373 -16.797 19.079 1.00 27.00 O HETATM 3705 O HOH A1313 -13.114 -33.359 21.355 1.00 47.50 O HETATM 3706 O HOH A1314 -24.789 13.514 11.471 1.00 42.73 O HETATM 3707 O HOH A1315 -11.374 12.113 15.845 1.00 27.65 O HETATM 3708 O HOH A1316 -14.687 -26.941 17.424 1.00 41.80 O HETATM 3709 O HOH A1317 3.852 -72.613 24.065 1.00 55.69 O HETATM 3710 O HOH A1318 -16.398 14.882 20.667 1.00 43.92 O HETATM 3711 O HOH A1319 -23.374 -28.782 0.544 1.00 73.19 O HETATM 3712 O HOH A1320 -23.478 -4.766 14.003 1.00 24.62 O HETATM 3713 O HOH A1321 -19.527 -35.406 26.867 1.00 58.84 O HETATM 3714 O HOH A1322 -22.859 -27.917 21.413 1.00 57.62 O HETATM 3715 O HOH A1323 -16.307 0.645 12.730 1.00 18.84 O HETATM 3716 O HOH A1324 -25.417 -13.269 13.588 1.00 29.76 O HETATM 3717 O HOH A1325 -18.931 -11.399 13.071 1.00 24.56 O HETATM 3718 O HOH A1326 -34.156 14.102 29.953 1.00 39.88 O HETATM 3719 O HOH A1327 -25.172 -15.795 14.740 1.00 31.02 O HETATM 3720 O HOH A1328 -23.960 -11.115 11.411 1.00 35.32 O HETATM 3721 O HOH A1329 -11.303 15.341 23.215 1.00 38.31 O HETATM 3722 O HOH A1330 -24.480 13.216 35.653 1.00 64.30 O HETATM 3723 O HOH A1331 -24.502 11.399 16.606 1.00 27.48 O HETATM 3724 O HOH A1332 -25.844 -14.264 24.686 1.00 31.03 O HETATM 3725 O HOH A1333 -12.689 -35.660 28.318 1.00 54.92 O HETATM 3726 O HOH A1334 3.377 -43.293 21.936 1.00 58.92 O HETATM 3727 O HOH A1335 -25.984 -11.885 21.519 1.00 25.40 O HETATM 3728 O HOH A1336 -9.708 -28.937 9.784 1.00 61.22 O HETATM 3729 O HOH A1337 -25.624 7.926 13.299 1.00 31.78 O HETATM 3730 O HOH A1338 -18.736 10.093 22.845 1.00 35.83 O HETATM 3731 O HOH A1339 -25.562 18.838 24.604 1.00 31.94 O HETATM 3732 O HOH A1340 -26.143 18.486 21.892 1.00 26.37 O HETATM 3733 O HOH A1341 -15.109 10.233 17.822 1.00 25.14 O HETATM 3734 O HOH A1342 -24.516 23.753 29.850 1.00 47.69 O HETATM 3735 O HOH A1343 -22.042 -6.552 15.376 1.00 30.84 O HETATM 3736 O HOH A1344 -2.238 13.421 21.936 1.00 34.38 O HETATM 3737 O HOH A1345 0.325 -66.940 25.209 1.00 58.59 O HETATM 3738 O HOH A1346 -27.497 20.767 22.315 1.00 30.85 O HETATM 3739 O HOH A1347 -26.165 -11.746 25.681 1.00 32.94 O HETATM 3740 O HOH A1348 2.208 17.710 27.972 1.00 48.95 O HETATM 3741 O HOH A1349 -4.525 -25.893 25.009 1.00 57.18 O HETATM 3742 O HOH A1350 4.540 -47.015 25.753 1.00 60.48 O HETATM 3743 O HOH A1351 5.399 -73.197 19.833 1.00 51.68 O HETATM 3744 O HOH A1352 -16.584 -29.069 11.167 1.00 53.35 O HETATM 3745 O HOH A1353 -0.874 -62.669 19.875 1.00 45.42 O HETATM 3746 O HOH A1354 -20.792 -2.476 24.354 1.00 23.39 O HETATM 3747 O HOH A1355 -20.291 10.805 16.249 1.00 37.24 O HETATM 3748 O HOH A1356 -29.926 -23.726 36.849 1.00 74.03 O HETATM 3749 O HOH A1357 -27.471 -11.378 6.894 1.00 42.10 O HETATM 3750 O HOH A1358 -19.494 -1.383 22.092 1.00 24.26 O HETATM 3751 O HOH A1359 -10.205 14.925 25.046 1.00 39.11 O HETATM 3752 O HOH A1360 -9.657 14.992 18.449 1.00 62.57 O HETATM 3753 O HOH A1361 -7.893 10.456 31.113 1.00 53.41 O HETATM 3754 O HOH A1362 -14.038 -27.930 19.684 1.00 58.76 O HETATM 3755 O HOH A1363 -18.020 -17.203 16.929 1.00 31.11 O HETATM 3756 O HOH A1364 9.328 -70.178 20.936 1.00 47.41 O HETATM 3757 O HOH A1365 -29.994 18.157 29.792 1.00 44.93 O HETATM 3758 O HOH A1366 -15.100 3.726 21.827 1.00 20.32 O HETATM 3759 O HOH A1367 5.672 -75.641 26.561 1.00 44.74 O HETATM 3760 O HOH A1368 -25.046 -6.575 17.705 1.00 52.45 O HETATM 3761 O HOH A1369 7.281 -60.658 15.271 1.00 62.83 O HETATM 3762 O HOH A1370 -16.662 16.749 8.584 1.00 41.53 O HETATM 3763 O HOH A1371 -4.423 -63.883 17.762 1.00 55.45 O HETATM 3764 O HOH A1372 -25.551 16.832 26.566 1.00 37.76 O HETATM 3765 O HOH A1373 -22.102 12.489 17.537 1.00 27.98 O HETATM 3766 O HOH A1374 -5.597 -31.390 24.624 1.00 54.02 O HETATM 3767 O HOH A1375 -35.776 18.884 16.131 1.00 54.14 O HETATM 3768 O HOH A1376 -22.541 -10.023 15.082 1.00 41.97 O HETATM 3769 O HOH A1377 -18.306 -2.588 20.067 1.00 23.56 O HETATM 3770 O HOH A1378 -22.180 -29.279 9.047 1.00 45.67 O HETATM 3771 O HOH A1379 -17.078 13.550 26.380 1.00 38.59 O HETATM 3772 O HOH A1380 -3.422 16.337 21.741 1.00 37.97 O HETATM 3773 O HOH A1381 -32.451 24.085 25.671 1.00 59.83 O HETATM 3774 O HOH A1382 -11.959 19.384 14.789 1.00 45.80 O HETATM 3775 O HOH A1383 0.608 -61.516 29.841 1.00 56.98 O HETATM 3776 O HOH A1384 -28.254 -28.622 33.778 1.00 60.44 O HETATM 3777 O HOH A1385 -19.004 16.523 21.745 1.00 59.73 O HETATM 3778 O HOH A1386 -17.351 13.842 29.289 1.00 54.34 O HETATM 3779 O HOH A1387 -22.978 -26.700 -2.077 1.00 69.19 O HETATM 3780 O HOH A1388 -11.663 14.751 4.559 1.00 49.23 O HETATM 3781 O HOH A1389 -18.619 -26.809 4.342 1.00 60.42 O HETATM 3782 O HOH A1390 -15.253 12.439 28.454 1.00 30.54 O HETATM 3783 O HOH A1391 -24.991 -29.386 22.877 1.00 58.89 O HETATM 3784 O HOH A1392 -20.554 -11.330 15.212 1.00 46.85 O HETATM 3785 O HOH A1393 -21.707 22.926 27.111 1.00 49.71 O HETATM 3786 O HOH A1394 -17.482 15.094 5.864 1.00 36.63 O HETATM 3787 O HOH A1395 -37.277 23.355 16.161 1.00 70.09 O HETATM 3788 O HOH A1396 -8.945 13.490 16.865 1.00 33.98 O HETATM 3789 O HOH A1397 -19.320 16.530 24.449 1.00 61.23 O HETATM 3790 O HOH A1398 -18.366 -28.211 6.995 1.00 50.25 O HETATM 3791 O HOH A1399 -23.779 8.665 15.652 1.00 30.09 O HETATM 3792 O HOH A1400 -23.733 -26.968 13.948 1.00 60.83 O HETATM 3793 O HOH A1401 -20.008 -30.681 20.956 1.00 57.36 O HETATM 3794 O HOH A1402 -34.208 16.292 30.493 1.00 60.97 O HETATM 3795 O HOH A1403 -31.012 20.716 28.424 1.00 46.99 O HETATM 3796 O HOH A1404 -7.125 12.303 27.893 1.00 53.58 O HETATM 3797 O HOH A1405 -15.259 -29.890 7.926 1.00 73.43 O HETATM 3798 O HOH A1406 -19.684 -28.520 8.701 1.00 49.56 O HETATM 3799 O HOH A1407 -30.757 20.290 3.511 1.00 56.38 O HETATM 3800 O HOH A1408 -31.276 -22.305 -2.768 1.00 59.63 O HETATM 3801 O HOH A1409 4.348 -75.109 22.918 1.00 60.06 O HETATM 3802 O HOH A1410 -10.893 -37.799 18.982 1.00 62.50 O HETATM 3803 O HOH A1411 6.502 -75.807 24.157 1.00 40.63 O HETATM 3804 O HOH A1412 -31.358 16.735 31.304 1.00 67.32 O HETATM 3805 O HOH A1413 -18.487 -27.379 10.915 1.00 60.40 O HETATM 3806 O HOH A1414 11.488 -72.961 26.965 1.00 60.90 O HETATM 3807 O HOH A1415 -18.024 -33.049 22.342 1.00 65.39 O HETATM 3808 O HOH A1416 -20.186 -23.867 14.817 1.00 65.90 O HETATM 3809 O HOH A1417 -21.546 10.782 13.528 1.00 55.87 O HETATM 3810 O HOH A1418 -20.371 -21.402 15.192 1.00 56.70 O CONECT 430 3692 CONECT 566 1238 CONECT 582 1147 CONECT 602 1282 CONECT 715 3692 CONECT 1147 582 CONECT 1238 566 CONECT 1282 602 CONECT 2690 2711 CONECT 2711 2690 CONECT 3106 3107 3111 CONECT 3107 3106 3108 CONECT 3108 3107 3109 3115 CONECT 3109 3108 3110 3121 CONECT 3110 3109 3111 CONECT 3111 3106 3110 3124 CONECT 3112 3113 3117 3126 CONECT 3113 3112 3114 CONECT 3114 3113 3115 CONECT 3115 3108 3114 3116 CONECT 3116 3115 3117 CONECT 3117 3112 3116 3125 CONECT 3118 3119 3123 CONECT 3119 3118 3120 CONECT 3120 3119 3121 CONECT 3121 3109 3120 3122 CONECT 3122 3121 3123 CONECT 3123 3118 3122 CONECT 3124 3111 CONECT 3125 3117 CONECT 3126 3112 CONECT 3127 3128 3136 CONECT 3128 3127 3129 CONECT 3129 3128 3130 3154 CONECT 3130 3129 3131 CONECT 3131 3130 3132 3136 CONECT 3132 3131 3133 CONECT 3133 3132 3134 CONECT 3134 3133 3135 3140 CONECT 3135 3134 3136 3137 CONECT 3136 3127 3131 3135 3145 CONECT 3137 3135 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3140 3143 3144 CONECT 3140 3134 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 3143 CONECT 3143 3139 3142 3146 CONECT 3144 3139 CONECT 3145 3136 CONECT 3146 3143 3147 3148 CONECT 3147 3146 CONECT 3148 3146 3149 CONECT 3149 3148 3150 CONECT 3150 3149 3151 CONECT 3151 3150 3152 3153 CONECT 3152 3151 CONECT 3153 3151 CONECT 3154 3129 CONECT 3155 3156 3164 CONECT 3156 3155 3157 CONECT 3157 3156 3158 3182 CONECT 3158 3157 3159 CONECT 3159 3158 3160 3164 CONECT 3160 3159 3161 CONECT 3161 3160 3162 CONECT 3162 3161 3163 3168 CONECT 3163 3162 3164 3165 CONECT 3164 3155 3159 3163 3173 CONECT 3165 3163 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 3171 3172 CONECT 3168 3162 3167 3169 CONECT 3169 3168 3170 CONECT 3170 3169 3171 CONECT 3171 3167 3170 3174 CONECT 3172 3167 CONECT 3173 3164 CONECT 3174 3171 3175 3176 CONECT 3175 3174 CONECT 3176 3174 3177 CONECT 3177 3176 3178 CONECT 3178 3177 3179 CONECT 3179 3178 3180 3181 CONECT 3180 3179 CONECT 3181 3179 CONECT 3182 3157 CONECT 3183 3184 3192 CONECT 3184 3183 3185 CONECT 3185 3184 3186 3210 CONECT 3186 3185 3187 CONECT 3187 3186 3188 3192 CONECT 3188 3187 3189 CONECT 3189 3188 3190 CONECT 3190 3189 3191 3196 CONECT 3191 3190 3192 3193 CONECT 3192 3183 3187 3191 3201 CONECT 3193 3191 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 3199 3200 CONECT 3196 3190 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3195 3198 3202 CONECT 3200 3195 CONECT 3201 3192 CONECT 3202 3199 3203 3204 CONECT 3203 3202 CONECT 3204 3202 3205 CONECT 3205 3204 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 3209 CONECT 3208 3207 CONECT 3209 3207 CONECT 3210 3185 CONECT 3211 3212 3220 CONECT 3212 3211 3213 CONECT 3213 3212 3214 3238 CONECT 3214 3213 3215 CONECT 3215 3214 3216 3220 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 3224 CONECT 3219 3218 3220 3221 CONECT 3220 3211 3215 3219 3229 CONECT 3221 3219 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 3227 3228 CONECT 3224 3218 3223 3225 CONECT 3225 3224 3226 CONECT 3226 3225 3227 CONECT 3227 3223 3226 3230 CONECT 3228 3223 CONECT 3229 3220 CONECT 3230 3227 3231 3232 CONECT 3231 3230 CONECT 3232 3230 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 3237 CONECT 3236 3235 CONECT 3237 3235 CONECT 3238 3213 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 3248 CONECT 3248 3247 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 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 CONECT 3259 3260 3261 3262 CONECT 3260 3259 CONECT 3261 3259 CONECT 3262 3259 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3264 3266 CONECT 3266 3265 3267 CONECT 3267 3266 CONECT 3268 3269 3270 3271 CONECT 3269 3268 CONECT 3270 3268 CONECT 3271 3268 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 3286 CONECT 3286 3285 3287 CONECT 3287 3286 CONECT 3288 3289 3290 3291 CONECT 3289 3288 CONECT 3290 3288 CONECT 3291 3288 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 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 CONECT 3333 3334 3335 3336 CONECT 3334 3333 CONECT 3335 3333 CONECT 3336 3333 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 CONECT 3344 3343 CONECT 3345 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 CONECT 3355 3356 CONECT 3356 3355 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 CONECT 3365 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 CONECT 3374 3375 3376 3377 CONECT 3375 3374 CONECT 3376 3374 CONECT 3377 3374 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 CONECT 3393 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 CONECT 3405 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 CONECT 3414 3415 3416 3417 CONECT 3415 3414 CONECT 3416 3414 CONECT 3417 3414 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 CONECT 3430 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3434 CONECT 3433 3442 3444 CONECT 3434 3432 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3441 CONECT 3440 3442 3446 CONECT 3441 3439 3443 3446 CONECT 3442 3433 3440 3445 CONECT 3443 3441 CONECT 3444 3433 CONECT 3445 3442 CONECT 3446 3440 3441 CONECT 3447 3448 3449 CONECT 3448 3447 3450 CONECT 3449 3447 3452 CONECT 3450 3448 3453 CONECT 3451 3461 3463 CONECT 3452 3449 CONECT 3453 3450 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3460 CONECT 3459 3461 3465 CONECT 3460 3458 3462 3465 CONECT 3461 3451 3459 3464 CONECT 3462 3460 CONECT 3463 3451 CONECT 3464 3461 CONECT 3465 3459 3460 CONECT 3466 3467 CONECT 3467 3466 3469 CONECT 3468 3477 3479 CONECT 3469 3467 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3476 CONECT 3475 3477 3481 CONECT 3476 3474 3478 3481 CONECT 3477 3468 3475 3480 CONECT 3478 3476 CONECT 3479 3468 CONECT 3480 3477 CONECT 3481 3475 3476 CONECT 3482 3483 3484 CONECT 3483 3482 3485 CONECT 3484 3482 3487 CONECT 3485 3483 3488 CONECT 3486 3499 3501 CONECT 3487 3484 3490 CONECT 3488 3485 3491 CONECT 3489 3492 CONECT 3490 3487 3492 CONECT 3491 3488 3493 CONECT 3492 3489 3490 CONECT 3493 3491 3494 CONECT 3494 3493 3495 CONECT 3495 3494 3496 CONECT 3496 3495 3498 CONECT 3497 3499 3503 CONECT 3498 3496 3500 3503 CONECT 3499 3486 3497 3502 CONECT 3500 3498 CONECT 3501 3486 CONECT 3502 3499 CONECT 3503 3497 3498 CONECT 3504 3507 CONECT 3505 3506 3508 CONECT 3506 3505 3509 CONECT 3507 3504 3511 CONECT 3508 3505 3512 CONECT 3509 3506 3513 CONECT 3510 3524 3526 CONECT 3511 3507 3514 CONECT 3512 3508 3515 CONECT 3513 3509 3516 CONECT 3514 3511 3517 CONECT 3515 3512 3517 CONECT 3516 3513 3518 CONECT 3517 3514 3515 CONECT 3518 3516 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3523 CONECT 3522 3524 3528 CONECT 3523 3521 3525 3528 CONECT 3524 3510 3522 3527 CONECT 3525 3523 CONECT 3526 3510 CONECT 3527 3524 CONECT 3528 3522 3523 CONECT 3529 3532 CONECT 3530 3531 3533 CONECT 3531 3530 3534 CONECT 3532 3529 3536 CONECT 3533 3530 3537 CONECT 3534 3531 3538 CONECT 3535 3549 3551 CONECT 3536 3532 3539 CONECT 3537 3533 3540 CONECT 3538 3534 3541 CONECT 3539 3536 3542 CONECT 3540 3537 3542 CONECT 3541 3538 3543 CONECT 3542 3539 3540 CONECT 3543 3541 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3548 CONECT 3547 3549 3553 CONECT 3548 3546 3550 3553 CONECT 3549 3535 3547 3552 CONECT 3550 3548 CONECT 3551 3535 CONECT 3552 3549 CONECT 3553 3547 3548 CONECT 3554 3555 3557 CONECT 3555 3554 3558 CONECT 3556 3560 CONECT 3557 3554 3561 CONECT 3558 3555 3562 CONECT 3559 3573 3575 CONECT 3560 3556 3563 CONECT 3561 3557 3564 CONECT 3562 3558 3565 CONECT 3563 3560 3566 CONECT 3564 3561 3566 CONECT 3565 3562 3567 CONECT 3566 3563 3564 CONECT 3567 3565 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3572 CONECT 3571 3573 3577 CONECT 3572 3570 3574 3577 CONECT 3573 3559 3571 3576 CONECT 3574 3572 CONECT 3575 3559 CONECT 3576 3573 CONECT 3577 3571 3572 CONECT 3578 3579 3580 CONECT 3579 3578 3581 CONECT 3580 3578 CONECT 3581 3579 3583 CONECT 3582 3591 3593 CONECT 3583 3581 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3587 3590 CONECT 3589 3591 3595 CONECT 3590 3588 3592 3595 CONECT 3591 3582 3589 3594 CONECT 3592 3590 CONECT 3593 3582 CONECT 3594 3591 CONECT 3595 3589 3590 CONECT 3596 3599 CONECT 3597 3598 3600 CONECT 3598 3597 3601 CONECT 3599 3596 3603 CONECT 3600 3597 3604 CONECT 3601 3598 3605 CONECT 3602 3616 3618 CONECT 3603 3599 3606 CONECT 3604 3600 3607 CONECT 3605 3601 3608 CONECT 3606 3603 3609 CONECT 3607 3604 3609 CONECT 3608 3605 3610 CONECT 3609 3606 3607 CONECT 3610 3608 3611 CONECT 3611 3610 3612 CONECT 3612 3611 3613 CONECT 3613 3612 3615 CONECT 3614 3616 3620 CONECT 3615 3613 3617 3620 CONECT 3616 3602 3614 3619 CONECT 3617 3615 CONECT 3618 3602 CONECT 3619 3616 CONECT 3620 3614 3615 CONECT 3621 3622 CONECT 3622 3621 3623 CONECT 3623 3622 3625 CONECT 3624 3633 3635 CONECT 3625 3623 3626 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3629 CONECT 3629 3628 3630 CONECT 3630 3629 3632 CONECT 3631 3633 3637 CONECT 3632 3630 3634 3637 CONECT 3633 3624 3631 3636 CONECT 3634 3632 CONECT 3635 3624 CONECT 3636 3633 CONECT 3637 3631 3632 CONECT 3638 3639 3641 CONECT 3639 3638 3642 CONECT 3640 3643 CONECT 3641 3638 3644 CONECT 3642 3639 3645 CONECT 3643 3640 3646 CONECT 3644 3641 3647 CONECT 3645 3642 3648 CONECT 3646 3643 3649 CONECT 3647 3644 3649 CONECT 3648 3645 3650 CONECT 3649 3646 3647 CONECT 3650 3648 3651 CONECT 3651 3650 CONECT 3652 3654 CONECT 3653 3654 CONECT 3654 3652 3653 3655 CONECT 3655 3654 3656 3657 CONECT 3656 3655 CONECT 3657 3655 3658 3659 CONECT 3658 3657 CONECT 3659 3657 3660 3661 CONECT 3660 3659 CONECT 3661 3659 CONECT 3662 3663 3664 3665 CONECT 3663 3662 CONECT 3664 3662 CONECT 3665 3662 3666 CONECT 3666 3665 3667 CONECT 3667 3666 3668 CONECT 3668 3667 3669 CONECT 3669 3668 3670 CONECT 3670 3669 3671 CONECT 3671 3670 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3674 CONECT 3674 3673 3675 CONECT 3675 3674 3676 CONECT 3676 3675 3677 CONECT 3677 3676 3678 CONECT 3678 3677 3679 CONECT 3679 3678 3680 CONECT 3680 3679 3681 CONECT 3681 3680 CONECT 3682 3683 3684 CONECT 3683 3682 CONECT 3684 3682 3685 CONECT 3685 3684 3686 CONECT 3686 3685 3687 CONECT 3687 3686 3691 CONECT 3688 3689 CONECT 3689 3688 3690 CONECT 3690 3689 3691 CONECT 3691 3687 3690 CONECT 3692 430 715 3735 3760 CONECT 3692 3768 CONECT 3735 3692 CONECT 3760 3692 CONECT 3768 3692 MASTER 562 0 34 18 2 0 54 6 3695 1 601 34 END