HEADER MEMBRANE PROTEIN 24-AUG-18 6M9T TITLE CRYSTAL STRUCTURE OF EP3 RECEPTOR BOUND TO MISOPROSTOL-FA COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROSTAGLANDIN E2 RECEPTOR EP3 SUBTYPE, ENDOLYSIN CHIMERA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: EP3 UNP RESIDUES 2-259,273-353 WITH INTERVENING LYSOZYME; COMPND 5 SYNONYM: PGE2 RECEPTOR EP3 SUBTYPE,PGE2-R,PROSTANOID EP3 RECEPTOR, COMPND 6 LYSIS PROTEIN,LYSOZYME,MURAMIDASE; COMPND 7 EC: 3.2.1.17; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: PTGER3; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, PROSTAGLANDIN E2 RECEPTOR 3 (EP3), PROSTAGLANDIN ANALOGUE, KEYWDS 2 MEMBRANE PROTEIN, MISOPROSTOL-FA (BIOLOGICALLY ACTIVE FREE ACID), KEYWDS 3 XFEL, LCP, T4L EXPDTA X-RAY DIFFRACTION AUTHOR M.AUDET,K.L.WHITE,B.BRETON,B.ZARZYCKA,G.W.HAN,Y.LU,C.GATI,A.BATYUK, AUTHOR 2 P.POPOV,J.VELASQUEZ,D.MANAHAN,H.HU,U.WEIERSTALL,W.LIU,W.SHUI, AUTHOR 3 V.KATRICH,V.CHEREZOV,M.A.HANSON,R.C.STEVENS REVDAT 3 29-APR-20 6M9T 1 REMARK REVDAT 2 13-FEB-19 6M9T 1 JRNL REVDAT 1 05-DEC-18 6M9T 0 JRNL AUTH M.AUDET,K.L.WHITE,B.BRETON,B.ZARZYCKA,G.W.HAN,Y.LU,C.GATI, JRNL AUTH 2 A.BATYUK,P.POPOV,J.VELASQUEZ,D.MANAHAN,H.HU,U.WEIERSTALL, JRNL AUTH 3 W.LIU,W.SHUI,V.KATRITCH,V.CHEREZOV,M.A.HANSON,R.C.STEVENS JRNL TITL CRYSTAL STRUCTURE OF MISOPROSTOL BOUND TO THE LABOR INDUCER JRNL TITL 2 PROSTAGLANDIN E2RECEPTOR. JRNL REF NAT. CHEM. BIOL. V. 15 11 2019 JRNL REFN ESSN 1552-4469 JRNL PMID 30510194 JRNL DOI 10.1038/S41589-018-0160-Y REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.27 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 22101 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.750 REMARK 3 FREE R VALUE TEST SET COUNT : 1050 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 11 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.62 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2925 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2820 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2798 REMARK 3 BIN R VALUE (WORKING SET) : 0.2790 REMARK 3 BIN FREE R VALUE : 0.3410 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.34 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3416 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 127 REMARK 3 SOLVENT ATOMS : 5 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 74.95 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 128.8 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.05720 REMARK 3 B22 (A**2) : -3.09750 REMARK 3 B33 (A**2) : 8.15470 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 20.02750 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.560 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.315 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.234 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.337 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.242 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3630 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4909 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1257 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 530 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3630 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 479 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3985 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.95 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.88 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.66 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|46 - A|259 A|273 - A|353 } REMARK 3 ORIGIN FOR THE GROUP (A): 126.1788 -10.9319 145.6804 REMARK 3 T TENSOR REMARK 3 T11: -1.0475 T22: -0.8036 REMARK 3 T33: -1.1661 T12: 0.0099 REMARK 3 T13: -0.0409 T23: 0.0578 REMARK 3 L TENSOR REMARK 3 L11: 2.9504 L22: 2.5618 REMARK 3 L33: 4.3817 L12: 0.0481 REMARK 3 L13: 1.1550 L23: 0.8426 REMARK 3 S TENSOR REMARK 3 S11: -0.1590 S12: -0.2316 S13: 0.1667 REMARK 3 S21: 0.0543 S22: 0.1092 S23: 0.3195 REMARK 3 S31: -0.1149 S32: -0.5722 S33: 0.0498 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1000 - A|1163 } REMARK 3 ORIGIN FOR THE GROUP (A): 119.9708 -17.1007 102.9829 REMARK 3 T TENSOR REMARK 3 T11: -0.7657 T22: -0.6251 REMARK 3 T33: -1.3404 T12: -0.1645 REMARK 3 T13: -0.2056 T23: 0.0782 REMARK 3 L TENSOR REMARK 3 L11: 6.1972 L22: 4.1803 REMARK 3 L33: 12.5595 L12: -0.2125 REMARK 3 L13: 5.0948 L23: -0.4859 REMARK 3 S TENSOR REMARK 3 S11: -0.1528 S12: 0.3283 S13: 0.3114 REMARK 3 S21: -0.4009 S22: -0.1887 S23: -0.2772 REMARK 3 S31: -0.6020 S32: 0.9801 S33: 0.3415 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6M9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-18. REMARK 100 THE DEPOSITION ID IS D_1000233952. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-AUG-17 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.302 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL 0.6.2 REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL 0.6.2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22151 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 30.030 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 223.9 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 90.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.250 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: PDB ENTRIES 3P0G & 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.72 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, PH 3.8-4.2, 10 REMARK 280 -35 MM MAGNESIUM SULFATE, 20-23% V/V PEG400, 2.5% JEFFAMINE M- REMARK 280 600, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.40000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.42500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.40000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.42500 REMARK 290 SMTRY3 4 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 VAL A -11 REMARK 465 PHE A -10 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 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 LYS A 2 REMARK 465 GLU A 3 REMARK 465 THR A 4 REMARK 465 ARG A 5 REMARK 465 GLY A 6 REMARK 465 TYR A 7 REMARK 465 GLY A 8 REMARK 465 GLY A 9 REMARK 465 ASP A 10 REMARK 465 ALA A 11 REMARK 465 PRO A 12 REMARK 465 PHE A 13 REMARK 465 CYS A 14 REMARK 465 THR A 15 REMARK 465 ARG A 16 REMARK 465 LEU A 17 REMARK 465 ASN A 18 REMARK 465 HIS A 19 REMARK 465 SER A 20 REMARK 465 TYR A 21 REMARK 465 THR A 22 REMARK 465 GLY A 23 REMARK 465 MET A 24 REMARK 465 TRP A 25 REMARK 465 ALA A 26 REMARK 465 PRO A 27 REMARK 465 GLU A 28 REMARK 465 ARG A 29 REMARK 465 SER A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ALA A 33 REMARK 465 ARG A 34 REMARK 465 GLY A 35 REMARK 465 ASN A 36 REMARK 465 LEU A 37 REMARK 465 THR A 38 REMARK 465 ARG A 39 REMARK 465 PRO A 40 REMARK 465 PRO A 41 REMARK 465 GLY A 42 REMARK 465 SER A 43 REMARK 465 GLY A 44 REMARK 465 GLU A 45 REMARK 465 GLY A 213 REMARK 465 ARG A 214 REMARK 465 GLY A 215 REMARK 465 GLY A 216 REMARK 465 ASN A 217 REMARK 465 GLY A 218 REMARK 465 THR A 219 REMARK 465 SER A 220 REMARK 465 SER A 221 REMARK 465 SER A 222 REMARK 465 HIS A 223 REMARK 465 GLN A 309 REMARK 465 THR A 310 REMARK 465 SER A 311 REMARK 465 VAL A 312 REMARK 465 GLU A 313 REMARK 465 HIS A 314 REMARK 465 CYS A 315 REMARK 465 LYS A 316 REMARK 465 THR A 317 REMARK 465 HIS A 318 REMARK 465 THR A 319 REMARK 465 PHE A 2007 REMARK 465 GLN A 2008 REMARK 465 GLY A 2009 REMARK 465 PRO A 2010 REMARK 465 HIS A 2011 REMARK 465 HIS A 2012 REMARK 465 HIS A 2013 REMARK 465 HIS A 2014 REMARK 465 HIS A 2015 REMARK 465 HIS A 2016 REMARK 465 HIS A 2017 REMARK 465 HIS A 2018 REMARK 465 HIS A 2019 REMARK 465 HIS A 2020 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 CYS A 47 SG REMARK 470 TYR A 77 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 80 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 81 CG CD OE1 OE2 REMARK 470 SER A 82 OG REMARK 470 ARG A 84 NE CZ NH1 NH2 REMARK 470 PHE A 88 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 119 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 122 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 179 CG CD1 CD2 REMARK 470 ASN A 224 CG OD1 ND2 REMARK 470 ARG A 275 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 304 CG CD CE NZ REMARK 470 GLU A 320 CG CD OE1 OE2 REMARK 470 LYS A 321 CG CD CE NZ REMARK 470 LYS A 323 CG CD CE NZ REMARK 470 ARG A2001 CD NE CZ NH1 NH2 REMARK 470 GLU A2004 CG CD OE1 OE2 REMARK 470 VAL A2005 CG1 CG2 REMARK 470 LEU A2006 CG CD1 CD2 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 ARG A 80 73.66 55.61 REMARK 500 GLU A 81 -107.45 -101.94 REMARK 500 SER A 82 -43.67 -136.17 REMARK 500 LYS A 85 23.71 -78.74 REMARK 500 LYS A 117 59.86 74.34 REMARK 500 GLN A 118 -146.81 51.79 REMARK 500 ARG A 119 72.79 59.83 REMARK 500 MET A 169 -60.91 -157.39 REMARK 500 LYS A 170 -9.28 61.94 REMARK 500 THR A 171 -31.61 68.75 REMARK 500 PRO A 204 37.16 -95.87 REMARK 500 PHE A1114 47.34 -91.21 REMARK 500 SER A1163 -77.61 -83.63 REMARK 500 LEU A 347 -63.11 -142.99 REMARK 500 LEU A 353 45.67 -90.90 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 OLC A 2106 REMARK 610 OLA A 2107 REMARK 610 OLA A 2108 REMARK 610 OLA A 2109 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue J9P A 2101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2103 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2104 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2106 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2110 DBREF 6M9T A 2 259 UNP P43115 PE2R3_HUMAN 2 259 DBREF 6M9T A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 6M9T A 273 353 UNP P43115 PE2R3_HUMAN 273 353 SEQADV 6M9T VAL A -11 UNP P43115 EXPRESSION TAG SEQADV 6M9T PHE A -10 UNP P43115 EXPRESSION TAG SEQADV 6M9T ALA A -9 UNP P43115 EXPRESSION TAG SEQADV 6M9T ASP A -8 UNP P43115 EXPRESSION TAG SEQADV 6M9T TYR A -7 UNP P43115 EXPRESSION TAG SEQADV 6M9T LYS A -6 UNP P43115 EXPRESSION TAG SEQADV 6M9T ASP A -5 UNP P43115 EXPRESSION TAG SEQADV 6M9T ASP A -4 UNP P43115 EXPRESSION TAG SEQADV 6M9T ASP A -3 UNP P43115 EXPRESSION TAG SEQADV 6M9T ASP A -2 UNP P43115 EXPRESSION TAG SEQADV 6M9T GLY A -1 UNP P43115 EXPRESSION TAG SEQADV 6M9T ALA A 0 UNP P43115 EXPRESSION TAG SEQADV 6M9T PRO A 1 UNP P43115 EXPRESSION TAG SEQADV 6M9T GLY A 1000 UNP P43115 LINKER SEQADV 6M9T SER A 1001 UNP P43115 LINKER SEQADV 6M9T GLY A 1012 UNP P00720 ARG 12 VARIANT SEQADV 6M9T THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 6M9T THR A 1074 UNP P00720 ALA 74 ENGINEERED MUTATION SEQADV 6M9T ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 6M9T ARG A 1137 UNP P00720 ILE 137 VARIANT SEQADV 6M9T GLY A 1162 UNP P00720 LINKER SEQADV 6M9T SER A 1163 UNP P00720 LINKER SEQADV 6M9T ALA A 286 UNP P43115 GLY 286 ENGINEERED MUTATION SEQADV 6M9T GLY A 2000 UNP P43115 EXPRESSION TAG SEQADV 6M9T ARG A 2001 UNP P43115 EXPRESSION TAG SEQADV 6M9T PRO A 2002 UNP P43115 EXPRESSION TAG SEQADV 6M9T LEU A 2003 UNP P43115 EXPRESSION TAG SEQADV 6M9T GLU A 2004 UNP P43115 EXPRESSION TAG SEQADV 6M9T VAL A 2005 UNP P43115 EXPRESSION TAG SEQADV 6M9T LEU A 2006 UNP P43115 EXPRESSION TAG SEQADV 6M9T PHE A 2007 UNP P43115 EXPRESSION TAG SEQADV 6M9T GLN A 2008 UNP P43115 EXPRESSION TAG SEQADV 6M9T GLY A 2009 UNP P43115 EXPRESSION TAG SEQADV 6M9T PRO A 2010 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2011 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2012 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2013 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2014 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2015 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2016 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2017 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2018 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2019 UNP P43115 EXPRESSION TAG SEQADV 6M9T HIS A 2020 UNP P43115 EXPRESSION TAG SEQRES 1 A 537 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 2 A 537 LYS GLU THR ARG GLY TYR GLY GLY ASP ALA PRO PHE CYS SEQRES 3 A 537 THR ARG LEU ASN HIS SER TYR THR GLY MET TRP ALA PRO SEQRES 4 A 537 GLU ARG SER ALA GLU ALA ARG GLY ASN LEU THR ARG PRO SEQRES 5 A 537 PRO GLY SER GLY GLU ASP CYS GLY SER VAL SER VAL ALA SEQRES 6 A 537 PHE PRO ILE THR MET LEU LEU THR GLY PHE VAL GLY ASN SEQRES 7 A 537 ALA LEU ALA MET LEU LEU VAL SER ARG SER TYR ARG ARG SEQRES 8 A 537 ARG GLU SER LYS ARG LYS LYS SER PHE LEU LEU CYS ILE SEQRES 9 A 537 GLY TRP LEU ALA LEU THR ASP LEU VAL GLY GLN LEU LEU SEQRES 10 A 537 THR THR PRO VAL VAL ILE VAL VAL TYR LEU SER LYS GLN SEQRES 11 A 537 ARG TRP GLU HIS ILE ASP PRO SER GLY ARG LEU CYS THR SEQRES 12 A 537 PHE PHE GLY LEU THR MET THR VAL PHE GLY LEU SER SER SEQRES 13 A 537 LEU PHE ILE ALA SER ALA MET ALA VAL GLU ARG ALA LEU SEQRES 14 A 537 ALA ILE ARG ALA PRO HIS TRP TYR ALA SER HIS MET LYS SEQRES 15 A 537 THR ARG ALA THR ARG ALA VAL LEU LEU GLY VAL TRP LEU SEQRES 16 A 537 ALA VAL LEU ALA PHE ALA LEU LEU PRO VAL LEU GLY VAL SEQRES 17 A 537 GLY GLN TYR THR VAL GLN TRP PRO GLY THR TRP CYS PHE SEQRES 18 A 537 ILE SER THR GLY ARG GLY GLY ASN GLY THR SER SER SER SEQRES 19 A 537 HIS ASN TRP GLY ASN LEU PHE PHE ALA SER ALA PHE ALA SEQRES 20 A 537 PHE LEU GLY LEU LEU ALA LEU THR VAL THR PHE SER CYS SEQRES 21 A 537 ASN LEU ALA THR ILE LYS ALA LEU VAL SER ARG GLY SER SEQRES 22 A 537 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG SEQRES 23 A 537 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE SEQRES 24 A 537 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN SEQRES 25 A 537 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN SEQRES 26 A 537 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU SEQRES 27 A 537 PHE ASN GLN ASP VAL ASP ALA THR VAL ARG GLY ILE LEU SEQRES 28 A 537 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP SEQRES 29 A 537 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN SEQRES 30 A 537 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU SEQRES 31 A 537 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL SEQRES 32 A 537 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN SEQRES 33 A 537 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR SEQRES 34 A 537 TRP ASP ALA TYR GLY SER TRP GLY ARG ILE THR THR GLU SEQRES 35 A 537 THR ALA ILE GLN LEU MET ALA ILE MET CYS VAL LEU SER SEQRES 36 A 537 VAL CYS TRP SER PRO LEU LEU ILE MET MET LEU LYS MET SEQRES 37 A 537 ILE PHE ASN GLN THR SER VAL GLU HIS CYS LYS THR HIS SEQRES 38 A 537 THR GLU LYS GLN LYS GLU CYS ASN PHE PHE LEU ILE ALA SEQRES 39 A 537 VAL ARG LEU ALA SER LEU ASN GLN ILE LEU ASP PRO TRP SEQRES 40 A 537 VAL TYR LEU LEU LEU ARG LYS ILE LEU GLY ARG PRO LEU SEQRES 41 A 537 GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS SEQRES 42 A 537 HIS HIS HIS HIS HET J9P A2101 26 HET SO4 A2102 5 HET SO4 A2103 5 HET SO4 A2104 5 HET SO4 A2105 5 HET OLC A2106 21 HET OLA A2107 15 HET OLA A2108 9 HET OLA A2109 16 HET OLA A2110 20 HETNAM J9P (11ALPHA,12ALPHA,13E,16S)-11,16-DIHYDROXY-16-METHYL-9- HETNAM 2 J9P OXOPROST-13-EN-1-OIC ACID HETNAM SO4 SULFATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 J9P C21 H36 O5 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 OLC C21 H40 O4 FORMUL 8 OLA 4(C18 H34 O2) FORMUL 12 HOH *5(H2 O) HELIX 1 AA1 VAL A 52 ARG A 78 1 27 HELIX 2 AA2 LYS A 85 SER A 116 1 32 HELIX 3 AA3 ARG A 119 ASP A 124 1 6 HELIX 4 AA4 GLY A 127 ALA A 161 1 35 HELIX 5 AA5 ALA A 161 HIS A 168 1 8 HELIX 6 AA6 THR A 171 LEU A 190 1 20 HELIX 7 AA7 LEU A 190 GLY A 195 1 6 HELIX 8 AA8 TRP A 225 ARG A 259 1 35 HELIX 9 AA9 SER A 1001 GLY A 1012 1 12 HELIX 10 AB1 SER A 1038 GLY A 1051 1 14 HELIX 11 AB2 THR A 1059 ASN A 1081 1 23 HELIX 12 AB3 LYS A 1083 LEU A 1091 1 9 HELIX 13 AB4 ASP A 1092 GLY A 1107 1 16 HELIX 14 AB5 GLY A 1107 GLY A 1113 1 7 HELIX 15 AB6 PHE A 1114 GLN A 1123 1 10 HELIX 16 AB7 ARG A 1125 LYS A 1135 1 11 HELIX 17 AB8 SER A 1136 THR A 1142 1 7 HELIX 18 AB9 THR A 1142 GLY A 1156 1 15 HELIX 19 AC1 ARG A 275 PHE A 307 1 33 HELIX 20 AC2 LYS A 323 LEU A 347 1 25 HELIX 21 AC3 LEU A 347 LEU A 353 1 7 HELIX 22 AC4 GLY A 2000 LEU A 2006 1 7 SHEET 1 AA1 2 TYR A 199 GLN A 202 0 SHEET 2 AA1 2 TRP A 207 ILE A 210 -1 O TRP A 207 N GLN A 202 SHEET 1 AA2 3 ARG A1014 LYS A1019 0 SHEET 2 AA2 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA2 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 130 CYS A 208 1555 1555 2.03 CISPEP 1 TRP A 203 PRO A 204 0 3.90 SITE 1 AC1 14 PRO A 55 THR A 106 THR A 107 TYR A 114 SITE 2 AC1 14 MET A 137 PHE A 140 GLY A 141 THR A 206 SITE 3 AC1 14 TRP A 207 TRP A 295 ARG A 333 SER A 336 SITE 4 AC1 14 GLN A 339 HOH A2202 SITE 1 AC2 7 ALA A 161 PRO A 162 HIS A 163 TRP A 164 SITE 2 AC2 7 ARG A1008 LEU A1013 HOH A2204 SITE 1 AC3 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC4 1 TYR A1088 SITE 1 AC5 2 MET A 70 GLY A 93 SITE 1 AC6 3 GLN A 283 ALA A 286 VAL A 345 SITE 1 AC7 2 ALA A 286 CYS A 289 SITE 1 AC8 4 PHE A 54 MET A 58 ILE A 330 ARG A 333 CRYST1 120.800 54.850 96.800 90.00 95.83 90.00 C 1 2 1 4 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 0.008278 0.000000 0.000845 0.00000 SCALE2 0.000000 0.018232 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010384 0.00000 ATOM 1 N ASP A 46 139.250 -14.776 168.661 1.00149.01 N ANISOU 1 N ASP A 46 20504 22045 14068 1580 -1649 157 N ATOM 2 CA ASP A 46 140.331 -14.688 167.682 1.00146.97 C ANISOU 2 CA ASP A 46 20069 21634 14140 1616 -1807 33 C ATOM 3 C ASP A 46 140.734 -13.227 167.422 1.00148.73 C ANISOU 3 C ASP A 46 20093 21895 14523 1609 -1832 -277 C ATOM 4 O ASP A 46 140.021 -12.499 166.724 1.00146.71 O ANISOU 4 O ASP A 46 19727 21597 14419 1508 -1650 -344 O ATOM 5 CB ASP A 46 139.954 -15.426 166.375 1.00146.64 C ANISOU 5 CB ASP A 46 19958 21395 14365 1509 -1688 186 C ATOM 6 CG ASP A 46 141.060 -15.552 165.335 1.00156.86 C ANISOU 6 CG ASP A 46 21083 22555 15963 1551 -1833 87 C ATOM 7 OD1 ASP A 46 140.732 -15.712 164.139 1.00155.80 O ANISOU 7 OD1 ASP A 46 20846 22288 16063 1453 -1714 132 O ATOM 8 OD2 ASP A 46 142.253 -15.531 165.721 1.00164.03 O ANISOU 8 OD2 ASP A 46 21952 23513 16860 1684 -2066 -39 O ATOM 9 N CYS A 47 141.887 -12.811 167.996 1.00145.44 N ANISOU 9 N CYS A 47 19639 21549 14071 1714 -2077 -464 N ATOM 10 CA CYS A 47 142.467 -11.461 167.884 1.00143.98 C ANISOU 10 CA CYS A 47 19291 21386 14028 1688 -2153 -764 C ATOM 11 C CYS A 47 142.789 -11.052 166.432 1.00141.82 C ANISOU 11 C CYS A 47 18791 20955 14142 1564 -2099 -833 C ATOM 12 O CYS A 47 142.801 -9.858 166.113 1.00140.91 O ANISOU 12 O CYS A 47 18573 20801 14165 1478 -2068 -1022 O ATOM 13 CB CYS A 47 143.689 -11.326 168.791 1.00146.76 C ANISOU 13 CB CYS A 47 19648 21863 14251 1810 -2449 -927 C ATOM 14 N GLY A 48 143.041 -12.048 165.583 1.00134.09 N ANISOU 14 N GLY A 48 17755 19878 13316 1557 -2095 -680 N ATOM 15 CA GLY A 48 143.354 -11.863 164.173 1.00130.18 C ANISOU 15 CA GLY A 48 17057 19259 13146 1443 -2034 -717 C ATOM 16 C GLY A 48 142.150 -11.467 163.348 1.00127.80 C ANISOU 16 C GLY A 48 16749 18853 12957 1310 -1784 -641 C ATOM 17 O GLY A 48 142.197 -10.452 162.650 1.00127.30 O ANISOU 17 O GLY A 48 16559 18725 13085 1198 -1733 -766 O ATOM 18 N SER A 49 141.061 -12.267 163.429 1.00119.45 N ANISOU 18 N SER A 49 15831 17778 11777 1311 -1636 -430 N ATOM 19 CA SER A 49 139.809 -12.050 162.693 1.00115.33 C ANISOU 19 CA SER A 49 15294 17186 11342 1200 -1407 -342 C ATOM 20 C SER A 49 139.125 -10.738 163.034 1.00114.12 C ANISOU 20 C SER A 49 15129 17079 11151 1182 -1320 -491 C ATOM 21 O SER A 49 138.534 -10.123 162.147 1.00112.43 O ANISOU 21 O SER A 49 14832 16777 11111 1099 -1203 -513 O ATOM 22 CB SER A 49 138.845 -13.209 162.902 1.00119.26 C ANISOU 22 CB SER A 49 15934 17689 11691 1188 -1289 -94 C ATOM 23 OG SER A 49 139.285 -14.344 162.177 1.00128.90 O ANISOU 23 OG SER A 49 17163 18791 13022 1186 -1346 38 O ATOM 24 N VAL A 50 139.202 -10.309 164.305 1.00108.26 N ANISOU 24 N VAL A 50 14485 16473 10178 1276 -1391 -601 N ATOM 25 CA VAL A 50 138.603 -9.056 164.762 1.00106.76 C ANISOU 25 CA VAL A 50 14305 16329 9930 1301 -1331 -785 C ATOM 26 C VAL A 50 139.634 -7.940 164.538 1.00108.41 C ANISOU 26 C VAL A 50 14428 16450 10313 1272 -1496 -1026 C ATOM 27 O VAL A 50 140.583 -7.807 165.312 1.00110.55 O ANISOU 27 O VAL A 50 14725 16797 10483 1327 -1683 -1158 O ATOM 28 CB VAL A 50 138.099 -9.138 166.231 1.00112.11 C ANISOU 28 CB VAL A 50 15136 17214 10245 1412 -1305 -802 C ATOM 29 CG1 VAL A 50 137.259 -7.917 166.598 1.00112.56 C ANISOU 29 CG1 VAL A 50 15195 17323 10250 1464 -1204 -998 C ATOM 30 CG2 VAL A 50 137.315 -10.423 166.478 1.00111.94 C ANISOU 30 CG2 VAL A 50 15210 17280 10042 1393 -1166 -523 C ATOM 31 N SER A 51 139.469 -7.179 163.443 1.00100.83 N ANISOU 31 N SER A 51 13368 15327 9614 1167 -1437 -1071 N ATOM 32 CA SER A 51 140.357 -6.083 163.048 1.00 99.81 C ANISOU 32 CA SER A 51 13163 15079 9681 1078 -1569 -1265 C ATOM 33 C SER A 51 139.634 -5.099 162.133 1.00101.25 C ANISOU 33 C SER A 51 13329 15084 10057 1001 -1464 -1295 C ATOM 34 O SER A 51 138.899 -5.521 161.242 1.00 99.50 O ANISOU 34 O SER A 51 13073 14813 9919 967 -1316 -1128 O ATOM 35 CB SER A 51 141.596 -6.628 162.340 1.00102.00 C ANISOU 35 CB SER A 51 13301 15335 10119 983 -1672 -1223 C ATOM 36 OG SER A 51 142.427 -5.593 161.840 1.00110.32 O ANISOU 36 OG SER A 51 14260 16293 11362 847 -1778 -1391 O ATOM 37 N VAL A 52 139.885 -3.793 162.321 1.00 97.85 N ANISOU 37 N VAL A 52 12935 14542 9703 970 -1565 -1509 N ATOM 38 CA VAL A 52 139.298 -2.722 161.512 1.00 96.89 C ANISOU 38 CA VAL A 52 12837 14209 9768 911 -1515 -1552 C ATOM 39 C VAL A 52 139.899 -2.714 160.095 1.00 99.97 C ANISOU 39 C VAL A 52 13119 14456 10410 706 -1510 -1438 C ATOM 40 O VAL A 52 139.316 -2.120 159.194 1.00 99.36 O ANISOU 40 O VAL A 52 13063 14209 10478 649 -1445 -1387 O ATOM 41 CB VAL A 52 139.374 -1.344 162.231 1.00103.02 C ANISOU 41 CB VAL A 52 13731 14877 10533 954 -1643 -1825 C ATOM 42 CG1 VAL A 52 140.739 -0.680 162.062 1.00104.03 C ANISOU 42 CG1 VAL A 52 13824 14893 10810 767 -1834 -1959 C ATOM 43 CG2 VAL A 52 138.250 -0.414 161.790 1.00102.87 C ANISOU 43 CG2 VAL A 52 13796 14678 10612 1020 -1568 -1864 C ATOM 44 N ALA A 53 141.042 -3.403 159.896 1.00 96.52 N ANISOU 44 N ALA A 53 12562 14106 10007 610 -1579 -1400 N ATOM 45 CA ALA A 53 141.727 -3.499 158.603 1.00 95.09 C ANISOU 45 CA ALA A 53 12250 13855 10027 418 -1560 -1308 C ATOM 46 C ALA A 53 140.894 -4.215 157.539 1.00 97.15 C ANISOU 46 C ALA A 53 12487 14088 10337 415 -1388 -1091 C ATOM 47 O ALA A 53 141.037 -3.895 156.356 1.00 96.22 O ANISOU 47 O ALA A 53 12320 13860 10378 259 -1344 -1023 O ATOM 48 CB ALA A 53 143.076 -4.179 158.766 1.00 96.23 C ANISOU 48 CB ALA A 53 12243 14154 10165 376 -1666 -1344 C ATOM 49 N PHE A 54 140.018 -5.163 157.948 1.00 93.45 N ANISOU 49 N PHE A 54 12061 13724 9723 566 -1295 -979 N ATOM 50 CA PHE A 54 139.153 -5.890 157.009 1.00 91.96 C ANISOU 50 CA PHE A 54 11852 13518 9572 558 -1145 -785 C ATOM 51 C PHE A 54 138.089 -4.972 156.374 1.00 95.53 C ANISOU 51 C PHE A 54 12356 13825 10114 542 -1071 -767 C ATOM 52 O PHE A 54 138.161 -4.793 155.155 1.00 93.82 O ANISOU 52 O PHE A 54 12100 13506 10042 416 -1039 -687 O ATOM 53 CB PHE A 54 138.537 -7.160 157.625 1.00 93.58 C ANISOU 53 CB PHE A 54 12091 13861 9604 681 -1076 -664 C ATOM 54 CG PHE A 54 139.522 -8.280 157.829 1.00 95.56 C ANISOU 54 CG PHE A 54 12300 14204 9806 700 -1152 -623 C ATOM 55 CD1 PHE A 54 139.811 -9.169 156.801 1.00 97.88 C ANISOU 55 CD1 PHE A 54 12520 14475 10197 643 -1113 -506 C ATOM 56 CD2 PHE A 54 140.165 -8.449 159.050 1.00 99.48 C ANISOU 56 CD2 PHE A 54 12837 14809 10153 798 -1279 -713 C ATOM 57 CE1 PHE A 54 140.733 -10.203 156.989 1.00 99.41 C ANISOU 57 CE1 PHE A 54 12678 14738 10355 703 -1203 -489 C ATOM 58 CE2 PHE A 54 141.089 -9.481 159.236 1.00102.60 C ANISOU 58 CE2 PHE A 54 13197 15279 10509 851 -1379 -678 C ATOM 59 CZ PHE A 54 141.363 -10.353 158.207 1.00 99.46 C ANISOU 59 CZ PHE A 54 12723 14842 10225 813 -1341 -569 C ATOM 60 N PRO A 55 137.167 -4.305 157.137 1.00 92.57 N ANISOU 60 N PRO A 55 12071 13443 9657 675 -1056 -856 N ATOM 61 CA PRO A 55 136.197 -3.410 156.476 1.00 91.76 C ANISOU 61 CA PRO A 55 12010 13194 9661 694 -1014 -851 C ATOM 62 C PRO A 55 136.821 -2.249 155.689 1.00 95.14 C ANISOU 62 C PRO A 55 12485 13390 10272 553 -1115 -906 C ATOM 63 O PRO A 55 136.301 -1.921 154.629 1.00 94.06 O ANISOU 63 O PRO A 55 12365 13126 10247 507 -1081 -809 O ATOM 64 CB PRO A 55 135.307 -2.932 157.625 1.00 95.16 C ANISOU 64 CB PRO A 55 12510 13697 9952 894 -995 -986 C ATOM 65 CG PRO A 55 136.106 -3.145 158.857 1.00100.76 C ANISOU 65 CG PRO A 55 13251 14528 10504 933 -1073 -1108 C ATOM 66 CD PRO A 55 136.923 -4.362 158.597 1.00 95.05 C ANISOU 66 CD PRO A 55 12450 13900 9766 832 -1073 -967 C ATOM 67 N ILE A 56 137.946 -1.664 156.165 1.00 92.76 N ANISOU 67 N ILE A 56 12209 13039 9998 464 -1244 -1049 N ATOM 68 CA ILE A 56 138.625 -0.552 155.477 1.00 93.58 C ANISOU 68 CA ILE A 56 12367 12917 10271 275 -1342 -1093 C ATOM 69 C ILE A 56 139.086 -0.953 154.067 1.00 96.11 C ANISOU 69 C ILE A 56 12595 13220 10702 70 -1279 -912 C ATOM 70 O ILE A 56 138.730 -0.279 153.102 1.00 95.89 O ANISOU 70 O ILE A 56 12643 13009 10782 -19 -1273 -828 O ATOM 71 CB ILE A 56 139.772 0.078 156.319 1.00 98.50 C ANISOU 71 CB ILE A 56 13011 13518 10897 190 -1499 -1295 C ATOM 72 CG1 ILE A 56 139.221 0.768 157.569 1.00100.54 C ANISOU 72 CG1 ILE A 56 13406 13746 11050 391 -1575 -1502 C ATOM 73 CG2 ILE A 56 140.607 1.071 155.489 1.00100.75 C ANISOU 73 CG2 ILE A 56 13330 13585 11365 -82 -1586 -1304 C ATOM 74 CD1 ILE A 56 140.217 0.941 158.604 1.00109.50 C ANISOU 74 CD1 ILE A 56 14535 14957 12114 362 -1717 -1697 C ATOM 75 N THR A 57 139.865 -2.038 153.953 1.00 91.53 N ANISOU 75 N THR A 57 11864 12831 10082 13 -1239 -859 N ATOM 76 CA THR A 57 140.377 -2.516 152.667 1.00 90.43 C ANISOU 76 CA THR A 57 11617 12724 10019 -160 -1167 -721 C ATOM 77 C THR A 57 139.257 -3.053 151.768 1.00 92.74 C ANISOU 77 C THR A 57 11930 13003 10306 -101 -1047 -547 C ATOM 78 O THR A 57 139.325 -2.886 150.546 1.00 92.40 O ANISOU 78 O THR A 57 11881 12893 10335 -249 -1005 -438 O ATOM 79 CB THR A 57 141.506 -3.527 152.866 1.00 98.88 C ANISOU 79 CB THR A 57 12515 14006 11049 -184 -1175 -753 C ATOM 80 OG1 THR A 57 141.028 -4.578 153.698 1.00101.06 O ANISOU 80 OG1 THR A 57 12794 14413 11191 29 -1154 -739 O ATOM 81 CG2 THR A 57 142.754 -2.903 153.485 1.00 98.63 C ANISOU 81 CG2 THR A 57 12418 14003 11054 -299 -1306 -923 C ATOM 82 N MET A 58 138.216 -3.665 152.377 1.00 86.81 N ANISOU 82 N MET A 58 11201 12327 9455 98 -996 -522 N ATOM 83 CA MET A 58 137.073 -4.208 151.651 1.00 84.45 C ANISOU 83 CA MET A 58 10902 12038 9147 155 -895 -376 C ATOM 84 C MET A 58 136.246 -3.107 151.017 1.00 88.68 C ANISOU 84 C MET A 58 11539 12392 9764 158 -917 -346 C ATOM 85 O MET A 58 135.883 -3.221 149.843 1.00 89.01 O ANISOU 85 O MET A 58 11576 12394 9851 91 -875 -214 O ATOM 86 CB MET A 58 136.222 -5.115 152.543 1.00 86.06 C ANISOU 86 CB MET A 58 11090 12388 9221 329 -833 -361 C ATOM 87 CG MET A 58 136.844 -6.479 152.735 1.00 88.81 C ANISOU 87 CG MET A 58 11366 12879 9498 323 -809 -314 C ATOM 88 SD MET A 58 135.990 -7.481 153.954 1.00 92.98 S ANISOU 88 SD MET A 58 11922 13558 9848 482 -750 -277 S ATOM 89 CE MET A 58 134.970 -8.431 152.900 1.00 88.43 C ANISOU 89 CE MET A 58 11306 12992 9303 437 -639 -99 C ATOM 90 N LEU A 59 135.974 -2.031 151.774 1.00 85.21 N ANISOU 90 N LEU A 59 11204 11832 9339 249 -999 -478 N ATOM 91 CA LEU A 59 135.226 -0.876 151.288 1.00 85.50 C ANISOU 91 CA LEU A 59 11367 11656 9464 291 -1058 -474 C ATOM 92 C LEU A 59 136.025 -0.188 150.199 1.00 89.82 C ANISOU 92 C LEU A 59 11985 12020 10123 53 -1116 -395 C ATOM 93 O LEU A 59 135.457 0.134 149.160 1.00 90.17 O ANISOU 93 O LEU A 59 12093 11951 10218 25 -1119 -266 O ATOM 94 CB LEU A 59 134.906 0.111 152.435 1.00 87.31 C ANISOU 94 CB LEU A 59 11706 11787 9681 460 -1149 -673 C ATOM 95 CG LEU A 59 134.256 1.462 152.079 1.00 93.41 C ANISOU 95 CG LEU A 59 12644 12287 10559 545 -1254 -712 C ATOM 96 CD1 LEU A 59 132.893 1.283 151.383 1.00 92.92 C ANISOU 96 CD1 LEU A 59 12541 12263 10501 707 -1197 -605 C ATOM 97 CD2 LEU A 59 134.116 2.332 153.310 1.00 96.72 C ANISOU 97 CD2 LEU A 59 13174 12617 10958 712 -1351 -953 C ATOM 98 N LEU A 60 137.342 0.009 150.419 1.00 86.13 N ANISOU 98 N LEU A 60 11497 11546 9681 -129 -1162 -465 N ATOM 99 CA LEU A 60 138.215 0.670 149.448 1.00 86.26 C ANISOU 99 CA LEU A 60 11562 11425 9790 -406 -1198 -391 C ATOM 100 C LEU A 60 138.214 -0.030 148.087 1.00 87.33 C ANISOU 100 C LEU A 60 11620 11655 9908 -531 -1089 -199 C ATOM 101 O LEU A 60 137.947 0.630 147.087 1.00 87.34 O ANISOU 101 O LEU A 60 11740 11492 9953 -638 -1110 -72 O ATOM 102 CB LEU A 60 139.653 0.850 149.982 1.00 87.03 C ANISOU 102 CB LEU A 60 11586 11571 9910 -589 -1253 -519 C ATOM 103 CG LEU A 60 140.599 1.643 149.068 1.00 93.02 C ANISOU 103 CG LEU A 60 12378 12205 10760 -925 -1279 -450 C ATOM 104 CD1 LEU A 60 140.264 3.118 149.063 1.00 95.28 C ANISOU 104 CD1 LEU A 60 12919 12138 11143 -986 -1416 -468 C ATOM 105 CD2 LEU A 60 142.028 1.456 149.472 1.00 97.27 C ANISOU 105 CD2 LEU A 60 12740 12913 11307 -1106 -1292 -564 C ATOM 106 N THR A 61 138.486 -1.352 148.065 1.00 81.19 N ANISOU 106 N THR A 61 10664 11127 9056 -503 -987 -182 N ATOM 107 CA THR A 61 138.554 -2.162 146.849 1.00 79.82 C ANISOU 107 CA THR A 61 10407 11071 8850 -599 -883 -41 C ATOM 108 C THR A 61 137.179 -2.237 146.172 1.00 84.17 C ANISOU 108 C THR A 61 11040 11557 9384 -485 -864 86 C ATOM 109 O THR A 61 137.078 -1.988 144.966 1.00 83.85 O ANISOU 109 O THR A 61 11053 11461 9343 -612 -847 218 O ATOM 110 CB THR A 61 139.210 -3.528 147.114 1.00 85.70 C ANISOU 110 CB THR A 61 10968 12061 9534 -560 -811 -88 C ATOM 111 OG1 THR A 61 138.576 -4.165 148.220 1.00 89.64 O ANISOU 111 OG1 THR A 61 11458 12622 9977 -335 -820 -148 O ATOM 112 CG2 THR A 61 140.705 -3.420 147.389 1.00 82.16 C ANISOU 112 CG2 THR A 61 10398 11708 9111 -710 -834 -197 C ATOM 113 N GLY A 62 136.136 -2.476 146.967 1.00 80.69 N ANISOU 113 N GLY A 62 10607 11133 8920 -256 -874 42 N ATOM 114 CA GLY A 62 134.760 -2.531 146.481 1.00 80.15 C ANISOU 114 CA GLY A 62 10574 11038 8843 -123 -868 132 C ATOM 115 C GLY A 62 134.304 -1.235 145.838 1.00 85.50 C ANISOU 115 C GLY A 62 11419 11480 9589 -134 -969 192 C ATOM 116 O GLY A 62 133.704 -1.264 144.762 1.00 85.14 O ANISOU 116 O GLY A 62 11406 11410 9534 -150 -973 325 O ATOM 117 N PHE A 63 134.631 -0.086 146.472 1.00 83.78 N ANISOU 117 N PHE A 63 11326 11070 9435 -127 -1070 92 N ATOM 118 CA PHE A 63 134.257 1.251 145.998 1.00 85.73 C ANISOU 118 CA PHE A 63 11783 11029 9762 -123 -1202 138 C ATOM 119 C PHE A 63 134.869 1.595 144.647 1.00 90.87 C ANISOU 119 C PHE A 63 12531 11576 10419 -394 -1211 317 C ATOM 120 O PHE A 63 134.134 1.976 143.741 1.00 91.52 O ANISOU 120 O PHE A 63 12725 11547 10502 -361 -1268 454 O ATOM 121 CB PHE A 63 134.568 2.346 147.048 1.00 89.14 C ANISOU 121 CB PHE A 63 12345 11260 10263 -68 -1318 -35 C ATOM 122 CG PHE A 63 134.129 3.739 146.658 1.00 92.81 C ANISOU 122 CG PHE A 63 13063 11375 10824 -33 -1482 -6 C ATOM 123 CD1 PHE A 63 132.802 4.131 146.794 1.00 96.58 C ANISOU 123 CD1 PHE A 63 13601 11769 11326 271 -1558 -41 C ATOM 124 CD2 PHE A 63 135.041 4.658 146.155 1.00 96.48 C ANISOU 124 CD2 PHE A 63 13709 11593 11357 -303 -1569 55 C ATOM 125 CE1 PHE A 63 132.392 5.413 146.421 1.00100.04 C ANISOU 125 CE1 PHE A 63 14297 11855 11861 341 -1738 -18 C ATOM 126 CE2 PHE A 63 134.634 5.948 145.803 1.00102.02 C ANISOU 126 CE2 PHE A 63 14691 11922 12150 -271 -1744 97 C ATOM 127 CZ PHE A 63 133.311 6.314 145.929 1.00100.87 C ANISOU 127 CZ PHE A 63 14623 11671 12033 68 -1838 59 C ATOM 128 N VAL A 64 136.201 1.460 144.515 1.00 87.84 N ANISOU 128 N VAL A 64 12093 11256 10027 -658 -1154 315 N ATOM 129 CA VAL A 64 136.952 1.761 143.290 1.00 89.07 C ANISOU 129 CA VAL A 64 12311 11371 10161 -962 -1127 475 C ATOM 130 C VAL A 64 136.417 0.941 142.113 1.00 92.50 C ANISOU 130 C VAL A 64 12690 11960 10495 -958 -1042 630 C ATOM 131 O VAL A 64 136.004 1.518 141.112 1.00 93.45 O ANISOU 131 O VAL A 64 12974 11943 10590 -1033 -1096 795 O ATOM 132 CB VAL A 64 138.481 1.571 143.484 1.00 93.44 C ANISOU 132 CB VAL A 64 12727 12062 10714 -1220 -1052 402 C ATOM 133 CG1 VAL A 64 139.250 1.972 142.230 1.00 94.91 C ANISOU 133 CG1 VAL A 64 12960 12242 10860 -1559 -998 566 C ATOM 134 CG2 VAL A 64 138.985 2.355 144.689 1.00 94.65 C ANISOU 134 CG2 VAL A 64 12933 12067 10961 -1229 -1159 232 C ATOM 135 N GLY A 65 136.395 -0.382 142.277 1.00 87.13 N ANISOU 135 N GLY A 65 11803 11547 9756 -863 -930 572 N ATOM 136 CA GLY A 65 135.921 -1.323 141.276 1.00 85.88 C ANISOU 136 CA GLY A 65 11574 11552 9502 -851 -853 675 C ATOM 137 C GLY A 65 134.528 -1.024 140.767 1.00 91.56 C ANISOU 137 C GLY A 65 12404 12169 10215 -691 -942 776 C ATOM 138 O GLY A 65 134.345 -0.835 139.559 1.00 92.66 O ANISOU 138 O GLY A 65 12633 12288 10284 -791 -956 928 O ATOM 139 N ASN A 66 133.545 -0.931 141.689 1.00 87.60 N ANISOU 139 N ASN A 66 11890 11618 9775 -437 -1006 688 N ATOM 140 CA ASN A 66 132.140 -0.682 141.337 1.00 87.51 C ANISOU 140 CA ASN A 66 11930 11548 9772 -241 -1098 749 C ATOM 141 C ASN A 66 131.874 0.735 140.795 1.00 93.30 C ANISOU 141 C ASN A 66 12908 11991 10551 -240 -1260 850 C ATOM 142 O ASN A 66 131.051 0.867 139.888 1.00 92.82 O ANISOU 142 O ASN A 66 12910 11899 10457 -168 -1341 969 O ATOM 143 CB ASN A 66 131.201 -1.036 142.488 1.00 84.39 C ANISOU 143 CB ASN A 66 11408 11242 9415 21 -1092 611 C ATOM 144 CG ASN A 66 131.130 -2.530 142.719 1.00 98.74 C ANISOU 144 CG ASN A 66 13023 13323 11169 21 -959 577 C ATOM 145 OD1 ASN A 66 130.638 -3.298 141.882 1.00 94.43 O ANISOU 145 OD1 ASN A 66 12412 12896 10570 -7 -930 659 O ATOM 146 ND2 ASN A 66 131.670 -2.987 143.832 1.00 82.83 N ANISOU 146 ND2 ASN A 66 10926 11392 9152 43 -889 457 N ATOM 147 N ALA A 67 132.575 1.779 141.307 1.00 91.49 N ANISOU 147 N ALA A 67 12828 11537 10396 -324 -1325 807 N ATOM 148 CA ALA A 67 132.380 3.140 140.785 1.00 94.22 C ANISOU 148 CA ALA A 67 13456 11551 10793 -342 -1498 915 C ATOM 149 C ALA A 67 132.952 3.266 139.369 1.00 99.31 C ANISOU 149 C ALA A 67 14229 12163 11339 -633 -1484 1142 C ATOM 150 O ALA A 67 132.383 3.981 138.543 1.00100.61 O ANISOU 150 O ALA A 67 14608 12132 11489 -604 -1626 1300 O ATOM 151 CB ALA A 67 133.005 4.177 141.707 1.00 96.45 C ANISOU 151 CB ALA A 67 13877 11585 11184 -379 -1579 795 C ATOM 152 N LEU A 68 134.054 2.539 139.081 1.00 95.12 N ANISOU 152 N LEU A 68 13567 11846 10730 -896 -1317 1155 N ATOM 153 CA LEU A 68 134.681 2.564 137.760 1.00 96.03 C ANISOU 153 CA LEU A 68 13768 12001 10717 -1191 -1261 1350 C ATOM 154 C LEU A 68 133.911 1.723 136.744 1.00 99.20 C ANISOU 154 C LEU A 68 14107 12599 10984 -1115 -1229 1450 C ATOM 155 O LEU A 68 133.777 2.154 135.599 1.00100.55 O ANISOU 155 O LEU A 68 14453 12709 11043 -1247 -1276 1646 O ATOM 156 CB LEU A 68 136.175 2.204 137.810 1.00 95.63 C ANISOU 156 CB LEU A 68 13580 12121 10632 -1493 -1095 1301 C ATOM 157 CG LEU A 68 137.089 3.292 138.400 1.00102.18 C ANISOU 157 CG LEU A 68 14529 12726 11568 -1692 -1150 1267 C ATOM 158 CD1 LEU A 68 138.460 2.756 138.685 1.00101.50 C ANISOU 158 CD1 LEU A 68 14214 12881 11469 -1920 -991 1156 C ATOM 159 CD2 LEU A 68 137.194 4.499 137.482 1.00108.75 C ANISOU 159 CD2 LEU A 68 15675 13275 12369 -1927 -1252 1495 C ATOM 160 N ALA A 69 133.353 0.563 137.173 1.00 92.92 N ANISOU 160 N ALA A 69 13085 12028 10193 -911 -1165 1320 N ATOM 161 CA ALA A 69 132.534 -0.315 136.330 1.00 91.24 C ANISOU 161 CA ALA A 69 12796 12000 9874 -827 -1153 1377 C ATOM 162 C ALA A 69 131.337 0.466 135.798 1.00 98.52 C ANISOU 162 C ALA A 69 13891 12743 10801 -658 -1351 1498 C ATOM 163 O ALA A 69 131.048 0.379 134.608 1.00 99.43 O ANISOU 163 O ALA A 69 14088 12907 10783 -717 -1393 1645 O ATOM 164 CB ALA A 69 132.061 -1.528 137.123 1.00 89.01 C ANISOU 164 CB ALA A 69 12264 11925 9630 -650 -1072 1212 C ATOM 165 N MET A 70 130.690 1.279 136.665 1.00 97.24 N ANISOU 165 N MET A 70 13793 12372 10782 -438 -1483 1429 N ATOM 166 CA MET A 70 129.552 2.139 136.326 1.00100.32 C ANISOU 166 CA MET A 70 14342 12564 11210 -216 -1700 1508 C ATOM 167 C MET A 70 129.947 3.209 135.302 1.00108.95 C ANISOU 167 C MET A 70 15762 13398 12234 -394 -1825 1735 C ATOM 168 O MET A 70 129.168 3.503 134.391 1.00110.23 O ANISOU 168 O MET A 70 16057 13499 12328 -298 -1981 1881 O ATOM 169 CB MET A 70 129.009 2.820 137.586 1.00103.52 C ANISOU 169 CB MET A 70 14742 12808 11785 54 -1791 1341 C ATOM 170 CG MET A 70 127.806 2.136 138.182 1.00106.83 C ANISOU 170 CG MET A 70 14914 13429 12246 353 -1790 1201 C ATOM 171 SD MET A 70 127.451 2.733 139.856 1.00112.42 S ANISOU 171 SD MET A 70 15564 14041 13110 635 -1817 955 S ATOM 172 CE MET A 70 126.861 4.398 139.496 1.00112.97 C ANISOU 172 CE MET A 70 15956 13697 13271 840 -2108 1022 C ATOM 173 N LEU A 71 131.158 3.787 135.459 1.00107.65 N ANISOU 173 N LEU A 71 15729 13090 12082 -665 -1764 1771 N ATOM 174 CA LEU A 71 131.700 4.829 134.581 1.00110.84 C ANISOU 174 CA LEU A 71 16460 13238 12417 -912 -1855 2002 C ATOM 175 C LEU A 71 131.969 4.300 133.172 1.00113.75 C ANISOU 175 C LEU A 71 16853 13813 12553 -1142 -1769 2195 C ATOM 176 O LEU A 71 131.726 5.021 132.205 1.00116.13 O ANISOU 176 O LEU A 71 17434 13939 12750 -1214 -1909 2425 O ATOM 177 CB LEU A 71 132.982 5.431 135.188 1.00112.01 C ANISOU 177 CB LEU A 71 16679 13236 12643 -1185 -1783 1961 C ATOM 178 CG LEU A 71 133.430 6.779 134.624 1.00120.96 C ANISOU 178 CG LEU A 71 18196 13996 13768 -1424 -1921 2179 C ATOM 179 CD1 LEU A 71 132.997 7.919 135.530 1.00123.12 C ANISOU 179 CD1 LEU A 71 18678 13858 14244 -1214 -2140 2090 C ATOM 180 CD2 LEU A 71 134.934 6.813 134.443 1.00124.48 C ANISOU 180 CD2 LEU A 71 18619 14524 14152 -1879 -1740 2230 C ATOM 181 N LEU A 72 132.461 3.050 133.058 1.00107.03 N ANISOU 181 N LEU A 72 15729 13326 11613 -1243 -1552 2098 N ATOM 182 CA LEU A 72 132.772 2.423 131.773 1.00107.36 C ANISOU 182 CA LEU A 72 15761 13610 11419 -1443 -1446 2227 C ATOM 183 C LEU A 72 131.517 1.945 131.028 1.00112.38 C ANISOU 183 C LEU A 72 16393 14348 11960 -1221 -1569 2279 C ATOM 184 O LEU A 72 131.467 2.035 129.796 1.00112.68 O ANISOU 184 O LEU A 72 16586 14437 11790 -1348 -1604 2466 O ATOM 185 CB LEU A 72 133.812 1.303 131.930 1.00105.06 C ANISOU 185 CB LEU A 72 15192 13649 11078 -1607 -1186 2076 C ATOM 186 CG LEU A 72 135.242 1.773 132.238 1.00110.77 C ANISOU 186 CG LEU A 72 15916 14355 11818 -1923 -1050 2073 C ATOM 187 CD1 LEU A 72 136.001 0.734 133.025 1.00108.35 C ANISOU 187 CD1 LEU A 72 15288 14310 11572 -1921 -863 1838 C ATOM 188 CD2 LEU A 72 136.003 2.131 130.973 1.00115.42 C ANISOU 188 CD2 LEU A 72 16657 15017 12180 -2269 -967 2287 C ATOM 189 N VAL A 73 130.499 1.473 131.785 1.00108.62 N ANISOU 189 N VAL A 73 15734 13912 11623 -903 -1638 2116 N ATOM 190 CA VAL A 73 129.202 1.023 131.279 1.00108.92 C ANISOU 190 CA VAL A 73 15713 14059 11614 -673 -1772 2127 C ATOM 191 C VAL A 73 128.446 2.204 130.638 1.00119.26 C ANISOU 191 C VAL A 73 17314 15103 12896 -553 -2041 2324 C ATOM 192 O VAL A 73 127.897 2.042 129.550 1.00120.18 O ANISOU 192 O VAL A 73 17509 15308 12844 -544 -2144 2455 O ATOM 193 CB VAL A 73 128.394 0.293 132.386 1.00109.91 C ANISOU 193 CB VAL A 73 15547 14309 11905 -406 -1751 1900 C ATOM 194 CG1 VAL A 73 126.888 0.347 132.140 1.00110.66 C ANISOU 194 CG1 VAL A 73 15601 14417 12026 -119 -1957 1908 C ATOM 195 CG2 VAL A 73 128.860 -1.149 132.533 1.00107.00 C ANISOU 195 CG2 VAL A 73 14928 14241 11486 -514 -1538 1764 C ATOM 196 N SER A 74 128.458 3.386 131.297 1.00120.07 N ANISOU 196 N SER A 74 17596 14870 13154 -462 -2167 2341 N ATOM 197 CA SER A 74 127.818 4.630 130.841 1.00124.71 C ANISOU 197 CA SER A 74 18503 15129 13752 -319 -2451 2518 C ATOM 198 C SER A 74 128.428 5.130 129.529 1.00135.19 C ANISOU 198 C SER A 74 20154 16363 14850 -622 -2487 2816 C ATOM 199 O SER A 74 127.703 5.623 128.661 1.00137.48 O ANISOU 199 O SER A 74 20660 16540 15036 -510 -2714 2999 O ATOM 200 CB SER A 74 127.941 5.717 131.905 1.00129.27 C ANISOU 200 CB SER A 74 19218 15352 14548 -198 -2549 2440 C ATOM 201 OG SER A 74 127.485 5.273 133.172 1.00136.77 O ANISOU 201 OG SER A 74 19876 16413 15677 63 -2492 2164 O ATOM 202 N ARG A 75 129.761 4.993 129.391 1.00134.30 N ANISOU 202 N ARG A 75 20060 16321 14647 -1005 -2261 2862 N ATOM 203 CA ARG A 75 130.523 5.393 128.207 1.00138.22 C ANISOU 203 CA ARG A 75 20827 16792 14900 -1363 -2225 3135 C ATOM 204 C ARG A 75 130.283 4.423 127.030 1.00145.14 C ANISOU 204 C ARG A 75 21614 18029 15503 -1420 -2158 3197 C ATOM 205 O ARG A 75 130.317 4.844 125.874 1.00147.47 O ANISOU 205 O ARG A 75 22181 18293 15559 -1585 -2232 3454 O ATOM 206 CB ARG A 75 132.024 5.462 128.557 1.00138.00 C ANISOU 206 CB ARG A 75 20761 16793 14881 -1746 -1979 3111 C ATOM 207 CG ARG A 75 132.860 6.381 127.665 1.00152.45 C ANISOU 207 CG ARG A 75 22935 18460 16530 -2144 -1973 3412 C ATOM 208 CD ARG A 75 132.931 7.802 128.200 1.00165.68 C ANISOU 208 CD ARG A 75 24936 19631 18383 -2173 -2168 3517 C ATOM 209 NE ARG A 75 132.056 8.709 127.455 1.00178.30 N ANISOU 209 NE ARG A 75 26929 20906 19911 -2027 -2477 3772 N ATOM 210 CZ ARG A 75 131.430 9.756 127.986 1.00194.63 C ANISOU 210 CZ ARG A 75 29249 22520 22180 -1787 -2756 3790 C ATOM 211 NH1 ARG A 75 131.562 10.035 129.277 1.00180.80 N ANISOU 211 NH1 ARG A 75 27396 20596 20704 -1672 -2755 3556 N ATOM 212 NH2 ARG A 75 130.657 10.526 127.231 1.00184.01 N ANISOU 212 NH2 ARG A 75 28266 20893 20756 -1638 -3051 4030 N ATOM 213 N SER A 76 130.040 3.134 127.333 1.00141.50 N ANISOU 213 N SER A 76 20796 17899 15070 -1291 -2025 2964 N ATOM 214 CA SER A 76 129.827 2.066 126.353 1.00142.26 C ANISOU 214 CA SER A 76 20774 18344 14933 -1330 -1955 2956 C ATOM 215 C SER A 76 128.360 1.834 125.936 1.00149.97 C ANISOU 215 C SER A 76 21723 19367 15893 -1016 -2197 2952 C ATOM 216 O SER A 76 128.136 1.190 124.908 1.00150.33 O ANISOU 216 O SER A 76 21752 19656 15711 -1064 -2198 2987 O ATOM 217 CB SER A 76 130.440 0.758 126.851 1.00142.97 C ANISOU 217 CB SER A 76 20519 18747 15056 -1402 -1683 2705 C ATOM 218 OG SER A 76 131.831 0.875 127.103 1.00153.03 O ANISOU 218 OG SER A 76 21783 20049 16311 -1699 -1460 2702 O ATOM 219 N TYR A 77 127.373 2.328 126.722 1.00148.73 N ANISOU 219 N TYR A 77 21541 19003 15966 -693 -2401 2889 N ATOM 220 CA TYR A 77 125.944 2.132 126.432 1.00150.09 C ANISOU 220 CA TYR A 77 21631 19244 16153 -375 -2638 2860 C ATOM 221 C TYR A 77 125.285 3.294 125.682 1.00160.41 C ANISOU 221 C TYR A 77 23277 20288 17381 -237 -2962 3103 C ATOM 222 O TYR A 77 124.570 3.057 124.705 1.00161.59 O ANISOU 222 O TYR A 77 23464 20574 17360 -150 -3131 3188 O ATOM 223 CB TYR A 77 125.156 1.801 127.711 1.00148.92 C ANISOU 223 CB TYR A 77 21171 19124 16287 -80 -2645 2604 C ATOM 224 N ARG A 78 125.530 4.540 126.132 1.00160.66 N ANISOU 224 N ARG A 78 23574 19933 17536 -214 -3067 3213 N ATOM 225 CA ARG A 78 124.959 5.770 125.562 1.00165.57 C ANISOU 225 CA ARG A 78 24572 20217 18120 -60 -3401 3450 C ATOM 226 C ARG A 78 125.426 6.089 124.121 1.00174.40 C ANISOU 226 C ARG A 78 26052 21314 18897 -347 -3454 3781 C ATOM 227 O ARG A 78 124.968 7.078 123.537 1.00177.91 O ANISOU 227 O ARG A 78 26858 21463 19275 -242 -3747 4018 O ATOM 228 CB ARG A 78 125.221 6.964 126.504 1.00167.45 C ANISOU 228 CB ARG A 78 25008 20016 18599 21 -3485 3447 C ATOM 229 CG ARG A 78 124.416 6.916 127.801 1.00178.06 C ANISOU 229 CG ARG A 78 26065 21341 20247 412 -3536 3150 C ATOM 230 CD ARG A 78 124.716 8.097 128.706 1.00192.42 C ANISOU 230 CD ARG A 78 28105 22724 22283 489 -3622 3123 C ATOM 231 NE ARG A 78 123.903 8.072 129.925 1.00201.15 N ANISOU 231 NE ARG A 78 28938 23843 23648 881 -3663 2825 N ATOM 232 CZ ARG A 78 123.943 9.000 130.878 1.00217.05 C ANISOU 232 CZ ARG A 78 31078 25518 25872 1044 -3751 2716 C ATOM 233 NH1 ARG A 78 124.758 10.042 130.768 1.00206.76 N ANISOU 233 NH1 ARG A 78 30183 23801 24575 834 -3824 2887 N ATOM 234 NH2 ARG A 78 123.167 8.893 131.948 1.00203.25 N ANISOU 234 NH2 ARG A 78 29053 23850 24321 1406 -3764 2429 N ATOM 235 N ARG A 79 126.302 5.237 123.548 1.00170.78 N ANISOU 235 N ARG A 79 25502 21175 18211 -689 -3180 3790 N ATOM 236 CA ARG A 79 126.895 5.376 122.215 1.00173.95 C ANISOU 236 CA ARG A 79 26198 21649 18246 -1010 -3152 4073 C ATOM 237 C ARG A 79 125.873 5.389 121.053 1.00181.61 C ANISOU 237 C ARG A 79 27326 22699 18980 -832 -3445 4233 C ATOM 238 O ARG A 79 126.115 6.085 120.063 1.00185.26 O ANISOU 238 O ARG A 79 28182 23033 19174 -1005 -3560 4550 O ATOM 239 CB ARG A 79 127.991 4.297 121.992 1.00172.18 C ANISOU 239 CB ARG A 79 25756 21810 17855 -1358 -2768 3963 C ATOM 240 CG ARG A 79 127.567 2.957 121.350 1.00181.17 C ANISOU 240 CG ARG A 79 26636 23386 18814 -1304 -2700 3808 C ATOM 241 CD ARG A 79 126.693 2.081 122.235 1.00187.94 C ANISOU 241 CD ARG A 79 27098 24372 19937 -989 -2721 3493 C ATOM 242 NE ARG A 79 126.184 0.912 121.517 1.00196.11 N ANISOU 242 NE ARG A 79 27950 25766 20798 -946 -2720 3375 N ATOM 243 CZ ARG A 79 126.632 -0.329 121.682 1.00207.00 C ANISOU 243 CZ ARG A 79 29047 27438 22166 -1048 -2472 3145 C ATOM 244 NH1 ARG A 79 127.597 -0.584 122.558 1.00188.67 N ANISOU 244 NH1 ARG A 79 26573 25115 19996 -1182 -2205 3011 N ATOM 245 NH2 ARG A 79 126.112 -1.326 120.979 1.00195.52 N ANISOU 245 NH2 ARG A 79 27468 26267 20554 -1007 -2510 3039 N ATOM 246 N ARG A 80 124.749 4.630 121.180 1.00176.95 N ANISOU 246 N ARG A 80 26430 22324 18479 -505 -3567 4022 N ATOM 247 CA ARG A 80 123.694 4.458 120.163 1.00179.12 C ANISOU 247 CA ARG A 80 26762 22743 18554 -309 -3853 4107 C ATOM 248 C ARG A 80 124.294 3.948 118.830 1.00184.19 C ANISOU 248 C ARG A 80 27561 23660 18761 -637 -3737 4265 C ATOM 249 O ARG A 80 124.446 4.718 117.875 1.00187.81 O ANISOU 249 O ARG A 80 28430 23980 18950 -757 -3889 4585 O ATOM 250 CB ARG A 80 122.839 5.733 119.994 1.00183.45 C ANISOU 250 CB ARG A 80 27625 22914 19164 -4 -4269 4313 C ATOM 251 N GLU A 81 124.680 2.651 118.803 1.00177.33 N ANISOU 251 N GLU A 81 26380 23176 17822 -787 -3459 4037 N ATOM 252 CA GLU A 81 125.332 2.010 117.656 1.00177.92 C ANISOU 252 CA GLU A 81 26542 23564 17495 -1087 -3295 4106 C ATOM 253 C GLU A 81 124.391 1.126 116.808 1.00181.41 C ANISOU 253 C GLU A 81 26863 24323 17741 -939 -3465 4004 C ATOM 254 O GLU A 81 123.567 1.669 116.063 1.00184.50 O ANISOU 254 O GLU A 81 27475 24646 17981 -776 -3801 4190 O ATOM 255 CB GLU A 81 126.582 1.231 118.110 1.00176.24 C ANISOU 255 CB GLU A 81 26113 23546 17305 -1375 -2867 3923 C ATOM 256 N SER A 82 124.536 -0.219 116.891 1.00173.79 N ANISOU 256 N SER A 82 25570 23690 16772 -998 -3254 3713 N ATOM 257 CA SER A 82 123.745 -1.171 116.108 1.00173.44 C ANISOU 257 CA SER A 82 25399 23953 16546 -904 -3393 3578 C ATOM 258 C SER A 82 123.235 -2.372 116.908 1.00171.39 C ANISOU 258 C SER A 82 24699 23855 16567 -766 -3321 3218 C ATOM 259 O SER A 82 122.075 -2.753 116.737 1.00171.52 O ANISOU 259 O SER A 82 24569 23969 16634 -553 -3573 3122 O ATOM 260 CB SER A 82 124.531 -1.641 114.888 1.00179.11 C ANISOU 260 CB SER A 82 26287 24956 16812 -1193 -3232 3635 C ATOM 261 N LYS A 83 124.090 -2.978 117.763 1.00162.71 N ANISOU 261 N LYS A 83 23390 22788 15642 -896 -2992 3026 N ATOM 262 CA LYS A 83 123.695 -4.141 118.563 1.00158.05 C ANISOU 262 CA LYS A 83 22420 22325 15307 -801 -2905 2708 C ATOM 263 C LYS A 83 122.777 -3.767 119.720 1.00159.03 C ANISOU 263 C LYS A 83 22344 22264 15816 -536 -3043 2646 C ATOM 264 O LYS A 83 122.960 -2.724 120.349 1.00158.29 O ANISOU 264 O LYS A 83 22352 21908 15882 -474 -3049 2770 O ATOM 265 CB LYS A 83 124.908 -4.958 119.043 1.00156.77 C ANISOU 265 CB LYS A 83 22124 22259 15183 -1005 -2534 2531 C ATOM 266 CG LYS A 83 124.556 -6.412 119.364 1.00158.28 C ANISOU 266 CG LYS A 83 22009 22632 15497 -964 -2466 2221 C ATOM 267 CD LYS A 83 125.781 -7.274 119.620 1.00162.40 C ANISOU 267 CD LYS A 83 22436 23256 16011 -1138 -2134 2047 C ATOM 268 CE LYS A 83 125.423 -8.676 120.056 1.00166.43 C ANISOU 268 CE LYS A 83 22686 23882 16669 -1090 -2091 1757 C ATOM 269 NZ LYS A 83 124.759 -9.455 118.977 1.00174.72 N ANISOU 269 NZ LYS A 83 23759 25137 17490 -1098 -2247 1661 N ATOM 270 N ARG A 84 121.776 -4.623 119.976 1.00154.16 N ANISOU 270 N ARG A 84 21439 21797 15337 -392 -3152 2443 N ATOM 271 CA ARG A 84 120.797 -4.463 121.049 1.00152.71 C ANISOU 271 CA ARG A 84 20999 21529 15496 -145 -3263 2343 C ATOM 272 C ARG A 84 121.262 -5.156 122.343 1.00152.18 C ANISOU 272 C ARG A 84 20679 21448 15696 -198 -2981 2141 C ATOM 273 O ARG A 84 120.460 -5.351 123.261 1.00150.55 O ANISOU 273 O ARG A 84 20208 21247 15747 -36 -3020 2013 O ATOM 274 CB ARG A 84 119.404 -4.950 120.599 1.00154.75 C ANISOU 274 CB ARG A 84 21061 21984 15752 13 -3539 2245 C ATOM 275 CG ARG A 84 118.659 -3.971 119.691 1.00168.20 C ANISOU 275 CG ARG A 84 22969 23641 17299 195 -3898 2450 C ATOM 276 CD ARG A 84 117.711 -3.075 120.467 1.00177.84 C ANISOU 276 CD ARG A 84 24080 24696 18795 517 -4097 2475 C ATOM 277 N LYS A 85 122.577 -5.478 122.434 1.00146.68 N ANISOU 277 N LYS A 85 20063 20742 14926 -420 -2699 2120 N ATOM 278 CA LYS A 85 123.196 -6.083 123.620 1.00142.94 C ANISOU 278 CA LYS A 85 19397 20242 14672 -475 -2438 1952 C ATOM 279 C LYS A 85 123.454 -5.006 124.701 1.00144.43 C ANISOU 279 C LYS A 85 19620 20179 15079 -375 -2400 2027 C ATOM 280 O LYS A 85 124.299 -5.178 125.585 1.00141.81 O ANISOU 280 O LYS A 85 19222 19787 14871 -453 -2179 1947 O ATOM 281 CB LYS A 85 124.476 -6.868 123.248 1.00144.75 C ANISOU 281 CB LYS A 85 19679 20584 14736 -715 -2181 1878 C ATOM 282 CG LYS A 85 124.835 -8.009 124.215 1.00155.93 C ANISOU 282 CG LYS A 85 20858 22050 16337 -750 -1976 1649 C ATOM 283 CD LYS A 85 123.925 -9.233 124.068 1.00166.63 C ANISOU 283 CD LYS A 85 22027 23561 17723 -720 -2061 1472 C ATOM 284 CE LYS A 85 124.142 -10.244 125.167 1.00173.60 C ANISOU 284 CE LYS A 85 22708 24435 18818 -739 -1890 1286 C ATOM 285 NZ LYS A 85 123.187 -11.380 125.065 1.00181.55 N ANISOU 285 NZ LYS A 85 23546 25557 19876 -740 -1989 1135 N ATOM 286 N LYS A 86 122.677 -3.903 124.630 1.00141.87 N ANISOU 286 N LYS A 86 19397 19706 14802 -180 -2642 2164 N ATOM 287 CA LYS A 86 122.669 -2.785 125.570 1.00141.19 C ANISOU 287 CA LYS A 86 19366 19358 14922 -30 -2676 2219 C ATOM 288 C LYS A 86 122.123 -3.304 126.904 1.00140.85 C ANISOU 288 C LYS A 86 18994 19367 15156 118 -2596 2004 C ATOM 289 O LYS A 86 122.468 -2.761 127.954 1.00139.83 O ANISOU 289 O LYS A 86 18857 19071 15201 181 -2510 1971 O ATOM 290 CB LYS A 86 121.779 -1.647 125.029 1.00147.50 C ANISOU 290 CB LYS A 86 20352 20003 15689 188 -3001 2393 C ATOM 291 CG LYS A 86 122.065 -0.274 125.639 1.00167.54 C ANISOU 291 CG LYS A 86 23097 22197 18363 290 -3057 2506 C ATOM 292 CD LYS A 86 121.039 0.127 126.699 1.00178.60 C ANISOU 292 CD LYS A 86 24297 23522 20041 634 -3190 2371 C ATOM 293 CE LYS A 86 121.379 1.451 127.341 1.00189.61 C ANISOU 293 CE LYS A 86 25917 24553 21574 745 -3251 2448 C ATOM 294 NZ LYS A 86 120.341 1.877 128.315 1.00198.49 N ANISOU 294 NZ LYS A 86 26843 25628 22947 1114 -3382 2289 N ATOM 295 N SER A 87 121.290 -4.375 126.850 1.00134.79 N ANISOU 295 N SER A 87 17965 18838 14413 151 -2623 1860 N ATOM 296 CA SER A 87 120.699 -5.047 128.007 1.00131.93 C ANISOU 296 CA SER A 87 17278 18578 14271 240 -2534 1668 C ATOM 297 C SER A 87 121.762 -5.764 128.858 1.00130.39 C ANISOU 297 C SER A 87 17031 18372 14141 69 -2241 1567 C ATOM 298 O SER A 87 121.580 -5.872 130.073 1.00129.32 O ANISOU 298 O SER A 87 16723 18222 14191 153 -2144 1461 O ATOM 299 CB SER A 87 119.598 -6.013 127.576 1.00136.07 C ANISOU 299 CB SER A 87 17569 19355 14776 248 -2643 1565 C ATOM 300 OG SER A 87 120.104 -7.063 126.770 1.00144.78 O ANISOU 300 OG SER A 87 18733 20577 15698 17 -2566 1537 O ATOM 301 N PHE A 88 122.869 -6.238 128.233 1.00123.30 N ANISOU 301 N PHE A 88 16276 17496 13078 -156 -2105 1592 N ATOM 302 CA PHE A 88 123.974 -6.887 128.951 1.00119.36 C ANISOU 302 CA PHE A 88 15738 16989 12624 -300 -1849 1495 C ATOM 303 C PHE A 88 124.745 -5.823 129.727 1.00119.73 C ANISOU 303 C PHE A 88 15897 16831 12766 -275 -1774 1556 C ATOM 304 O PHE A 88 125.171 -6.082 130.848 1.00116.98 O ANISOU 304 O PHE A 88 15437 16453 12556 -270 -1628 1453 O ATOM 305 CB PHE A 88 124.903 -7.644 127.997 1.00121.05 C ANISOU 305 CB PHE A 88 16057 17309 12627 -510 -1742 1485 C ATOM 306 N LEU A 89 124.882 -4.613 129.143 1.00116.45 N ANISOU 306 N LEU A 89 15715 16261 12272 -262 -1893 1727 N ATOM 307 CA LEU A 89 125.525 -3.463 129.778 1.00115.46 C ANISOU 307 CA LEU A 89 15734 15898 12237 -251 -1867 1795 C ATOM 308 C LEU A 89 124.636 -2.957 130.905 1.00117.35 C ANISOU 308 C LEU A 89 15852 16038 12698 10 -1959 1715 C ATOM 309 O LEU A 89 125.142 -2.625 131.981 1.00116.58 O ANISOU 309 O LEU A 89 15737 15825 12734 32 -1859 1645 O ATOM 310 CB LEU A 89 125.777 -2.338 128.764 1.00118.20 C ANISOU 310 CB LEU A 89 16396 16085 12431 -322 -1999 2021 C ATOM 311 CG LEU A 89 126.980 -2.509 127.842 1.00123.43 C ANISOU 311 CG LEU A 89 17209 16826 12865 -618 -1855 2115 C ATOM 312 CD1 LEU A 89 126.853 -1.620 126.627 1.00126.60 C ANISOU 312 CD1 LEU A 89 17904 17143 13054 -675 -2026 2356 C ATOM 313 CD2 LEU A 89 128.297 -2.225 128.575 1.00125.46 C ANISOU 313 CD2 LEU A 89 17492 16987 13190 -789 -1655 2091 C ATOM 314 N LEU A 90 123.309 -2.940 130.664 1.00113.03 N ANISOU 314 N LEU A 90 15200 15567 12181 212 -2146 1704 N ATOM 315 CA LEU A 90 122.268 -2.521 131.604 1.00112.74 C ANISOU 315 CA LEU A 90 14997 15505 12332 493 -2243 1605 C ATOM 316 C LEU A 90 122.302 -3.359 132.892 1.00113.28 C ANISOU 316 C LEU A 90 14803 15705 12533 491 -2041 1420 C ATOM 317 O LEU A 90 122.162 -2.794 133.978 1.00112.66 O ANISOU 317 O LEU A 90 14667 15542 12595 652 -2021 1336 O ATOM 318 CB LEU A 90 120.891 -2.629 130.934 1.00114.71 C ANISOU 318 CB LEU A 90 15126 15898 12560 669 -2467 1614 C ATOM 319 CG LEU A 90 119.857 -1.597 131.344 1.00121.80 C ANISOU 319 CG LEU A 90 15980 16701 13598 1009 -2673 1589 C ATOM 320 CD1 LEU A 90 119.160 -1.017 130.128 1.00125.07 C ANISOU 320 CD1 LEU A 90 16535 17078 13906 1139 -2970 1732 C ATOM 321 CD2 LEU A 90 118.842 -2.192 132.298 1.00124.15 C ANISOU 321 CD2 LEU A 90 15893 17233 14044 1163 -2619 1391 C ATOM 322 N CYS A 91 122.512 -4.691 132.769 1.00107.40 N ANISOU 322 N CYS A 91 13924 15154 11730 310 -1899 1356 N ATOM 323 CA CYS A 91 122.587 -5.621 133.902 1.00104.96 C ANISOU 323 CA CYS A 91 13403 14959 11516 273 -1714 1212 C ATOM 324 C CYS A 91 123.888 -5.427 134.728 1.00106.33 C ANISOU 324 C CYS A 91 13679 15001 11722 184 -1543 1186 C ATOM 325 O CYS A 91 123.818 -5.404 135.959 1.00104.60 O ANISOU 325 O CYS A 91 13348 14785 11611 269 -1455 1087 O ATOM 326 CB CYS A 91 122.411 -7.070 133.444 1.00104.49 C ANISOU 326 CB CYS A 91 13215 15095 11389 113 -1655 1161 C ATOM 327 SG CYS A 91 120.745 -7.481 132.840 1.00110.39 S ANISOU 327 SG CYS A 91 13746 16052 12146 206 -1842 1135 S ATOM 328 N ILE A 92 125.061 -5.283 134.047 1.00102.07 N ANISOU 328 N ILE A 92 13336 14373 11074 9 -1495 1268 N ATOM 329 CA ILE A 92 126.385 -5.062 134.659 1.00100.06 C ANISOU 329 CA ILE A 92 13166 14014 10840 -102 -1352 1246 C ATOM 330 C ILE A 92 126.382 -3.728 135.402 1.00105.18 C ANISOU 330 C ILE A 92 13913 14454 11598 33 -1421 1254 C ATOM 331 O ILE A 92 126.862 -3.659 136.534 1.00104.59 O ANISOU 331 O ILE A 92 13787 14340 11611 57 -1325 1155 O ATOM 332 CB ILE A 92 127.543 -5.150 133.616 1.00103.08 C ANISOU 332 CB ILE A 92 13700 14399 11065 -330 -1287 1330 C ATOM 333 CG1 ILE A 92 127.698 -6.584 133.072 1.00102.50 C ANISOU 333 CG1 ILE A 92 13521 14527 10896 -440 -1195 1260 C ATOM 334 CG2 ILE A 92 128.878 -4.646 134.193 1.00103.00 C ANISOU 334 CG2 ILE A 92 13768 14280 11087 -446 -1170 1317 C ATOM 335 CD1 ILE A 92 128.411 -6.693 131.681 1.00108.42 C ANISOU 335 CD1 ILE A 92 14406 15347 11441 -621 -1169 1337 C ATOM 336 N GLY A 93 125.831 -2.698 134.760 1.00103.63 N ANISOU 336 N GLY A 93 13869 14116 11388 130 -1604 1366 N ATOM 337 CA GLY A 93 125.710 -1.357 135.318 1.00104.83 C ANISOU 337 CA GLY A 93 14158 14024 11648 286 -1717 1374 C ATOM 338 C GLY A 93 124.863 -1.342 136.569 1.00108.05 C ANISOU 338 C GLY A 93 14373 14483 12198 536 -1717 1207 C ATOM 339 O GLY A 93 125.220 -0.686 137.551 1.00107.54 O ANISOU 339 O GLY A 93 14356 14277 12225 609 -1694 1123 O ATOM 340 N TRP A 94 123.751 -2.103 136.548 1.00104.55 N ANISOU 340 N TRP A 94 13699 14265 11762 649 -1732 1150 N ATOM 341 CA TRP A 94 122.834 -2.257 137.678 1.00104.59 C ANISOU 341 CA TRP A 94 13467 14401 11871 861 -1700 993 C ATOM 342 C TRP A 94 123.502 -3.085 138.780 1.00100.85 C ANISOU 342 C TRP A 94 12882 14028 11409 747 -1479 886 C ATOM 343 O TRP A 94 123.329 -2.763 139.951 1.00101.22 O ANISOU 343 O TRP A 94 12861 14071 11526 891 -1432 765 O ATOM 344 CB TRP A 94 121.507 -2.888 137.223 1.00105.64 C ANISOU 344 CB TRP A 94 13366 14775 11996 951 -1772 977 C ATOM 345 CG TRP A 94 120.448 -2.975 138.283 1.00108.50 C ANISOU 345 CG TRP A 94 13454 15316 12453 1163 -1737 823 C ATOM 346 CD1 TRP A 94 119.999 -4.105 138.899 1.00110.61 C ANISOU 346 CD1 TRP A 94 13460 15845 12723 1086 -1583 740 C ATOM 347 CD2 TRP A 94 119.674 -1.893 138.815 1.00111.28 C ANISOU 347 CD2 TRP A 94 13767 15613 12902 1483 -1856 730 C ATOM 348 NE1 TRP A 94 119.002 -3.793 139.795 1.00112.02 N ANISOU 348 NE1 TRP A 94 13417 16169 12977 1317 -1575 607 N ATOM 349 CE2 TRP A 94 118.788 -2.440 139.770 1.00115.71 C ANISOU 349 CE2 TRP A 94 14005 16454 13507 1584 -1741 581 C ATOM 350 CE3 TRP A 94 119.644 -0.507 138.581 1.00115.33 C ANISOU 350 CE3 TRP A 94 14498 15856 13468 1698 -2053 755 C ATOM 351 CZ2 TRP A 94 117.881 -1.651 140.489 1.00117.66 C ANISOU 351 CZ2 TRP A 94 14108 16759 13838 1911 -1801 433 C ATOM 352 CZ3 TRP A 94 118.744 0.272 139.295 1.00119.52 C ANISOU 352 CZ3 TRP A 94 14912 16399 14100 2042 -2140 604 C ATOM 353 CH2 TRP A 94 117.880 -0.299 140.240 1.00120.35 C ANISOU 353 CH2 TRP A 94 14664 16826 14239 2156 -2006 433 C ATOM 354 N LEU A 95 124.296 -4.114 138.407 1.00 91.00 N ANISOU 354 N LEU A 95 11633 12862 10081 505 -1357 926 N ATOM 355 CA LEU A 95 125.030 -4.957 139.350 1.00 86.86 C ANISOU 355 CA LEU A 95 11035 12412 9555 397 -1176 845 C ATOM 356 C LEU A 95 126.088 -4.128 140.109 1.00 90.71 C ANISOU 356 C LEU A 95 11666 12722 10078 391 -1142 805 C ATOM 357 O LEU A 95 126.191 -4.260 141.329 1.00 89.62 O ANISOU 357 O LEU A 95 11452 12626 9974 452 -1055 697 O ATOM 358 CB LEU A 95 125.663 -6.175 138.639 1.00 84.43 C ANISOU 358 CB LEU A 95 10720 12200 9159 175 -1090 887 C ATOM 359 CG LEU A 95 126.423 -7.206 139.508 1.00 85.76 C ANISOU 359 CG LEU A 95 10823 12439 9323 78 -931 813 C ATOM 360 CD1 LEU A 95 125.509 -7.902 140.482 1.00 85.36 C ANISOU 360 CD1 LEU A 95 10587 12538 9306 146 -871 749 C ATOM 361 CD2 LEU A 95 127.112 -8.250 138.647 1.00 85.42 C ANISOU 361 CD2 LEU A 95 10817 12441 9198 -103 -879 840 C ATOM 362 N ALA A 96 126.836 -3.254 139.397 1.00 87.72 N ANISOU 362 N ALA A 96 11496 12150 9682 305 -1216 894 N ATOM 363 CA ALA A 96 127.851 -2.387 139.999 1.00 87.74 C ANISOU 363 CA ALA A 96 11644 11967 9727 259 -1208 861 C ATOM 364 C ALA A 96 127.211 -1.445 141.014 1.00 93.46 C ANISOU 364 C ALA A 96 12382 12577 10550 501 -1288 752 C ATOM 365 O ALA A 96 127.722 -1.328 142.129 1.00 94.01 O ANISOU 365 O ALA A 96 12448 12618 10654 518 -1227 635 O ATOM 366 CB ALA A 96 128.581 -1.594 138.927 1.00 89.72 C ANISOU 366 CB ALA A 96 12117 12039 9934 93 -1281 1004 C ATOM 367 N LEU A 97 126.065 -0.834 140.655 1.00 90.86 N ANISOU 367 N LEU A 97 12057 12208 10260 708 -1430 770 N ATOM 368 CA LEU A 97 125.296 0.062 141.525 1.00 92.41 C ANISOU 368 CA LEU A 97 12247 12316 10547 994 -1519 640 C ATOM 369 C LEU A 97 124.812 -0.694 142.775 1.00 95.29 C ANISOU 369 C LEU A 97 12363 12934 10910 1104 -1373 477 C ATOM 370 O LEU A 97 125.047 -0.225 143.890 1.00 94.59 O ANISOU 370 O LEU A 97 12295 12792 10853 1213 -1346 335 O ATOM 371 CB LEU A 97 124.115 0.697 140.753 1.00 94.61 C ANISOU 371 CB LEU A 97 12550 12536 10860 1210 -1714 695 C ATOM 372 CG LEU A 97 123.290 1.773 141.468 1.00101.98 C ANISOU 372 CG LEU A 97 13492 13359 11898 1557 -1843 549 C ATOM 373 CD1 LEU A 97 124.095 3.036 141.705 1.00104.04 C ANISOU 373 CD1 LEU A 97 14065 13241 12223 1567 -1958 538 C ATOM 374 CD2 LEU A 97 122.060 2.132 140.662 1.00107.13 C ANISOU 374 CD2 LEU A 97 14088 14041 12576 1788 -2028 594 C ATOM 375 N THR A 98 124.187 -1.886 142.582 1.00 90.78 N ANISOU 375 N THR A 98 11572 12632 10287 1049 -1278 503 N ATOM 376 CA THR A 98 123.697 -2.767 143.654 1.00 89.59 C ANISOU 376 CA THR A 98 11190 12742 10110 1092 -1125 396 C ATOM 377 C THR A 98 124.840 -3.101 144.622 1.00 91.55 C ANISOU 377 C THR A 98 11496 12971 10317 973 -996 338 C ATOM 378 O THR A 98 124.647 -3.017 145.832 1.00 92.99 O ANISOU 378 O THR A 98 11609 13238 10486 1097 -927 208 O ATOM 379 CB THR A 98 123.062 -4.045 143.060 1.00 96.41 C ANISOU 379 CB THR A 98 11868 13837 10928 966 -1064 472 C ATOM 380 OG1 THR A 98 122.041 -3.685 142.135 1.00 98.85 O ANISOU 380 OG1 THR A 98 12118 14172 11270 1081 -1211 516 O ATOM 381 CG2 THR A 98 122.481 -4.975 144.117 1.00 93.92 C ANISOU 381 CG2 THR A 98 11326 13783 10577 968 -906 394 C ATOM 382 N ASP A 99 126.024 -3.445 144.094 1.00 84.84 N ANISOU 382 N ASP A 99 10767 12030 9438 749 -972 424 N ATOM 383 CA ASP A 99 127.176 -3.787 144.920 1.00 83.30 C ANISOU 383 CA ASP A 99 10613 11828 9209 641 -877 370 C ATOM 384 C ASP A 99 127.734 -2.588 145.695 1.00 88.48 C ANISOU 384 C ASP A 99 11407 12302 9909 728 -939 261 C ATOM 385 O ASP A 99 128.023 -2.720 146.889 1.00 88.18 O ANISOU 385 O ASP A 99 11337 12331 9837 775 -873 146 O ATOM 386 CB ASP A 99 128.267 -4.492 144.086 1.00 83.12 C ANISOU 386 CB ASP A 99 10644 11788 9149 401 -838 468 C ATOM 387 CG ASP A 99 127.859 -5.845 143.510 1.00 84.41 C ANISOU 387 CG ASP A 99 10689 12120 9262 310 -774 539 C ATOM 388 OD1 ASP A 99 126.793 -6.368 143.907 1.00 83.23 O ANISOU 388 OD1 ASP A 99 10399 12118 9106 392 -740 520 O ATOM 389 OD2 ASP A 99 128.581 -6.357 142.638 1.00 86.57 O ANISOU 389 OD2 ASP A 99 11008 12384 9502 150 -759 604 O ATOM 390 N LEU A 100 127.855 -1.424 145.030 1.00 85.96 N ANISOU 390 N LEU A 100 11258 11746 9657 748 -1077 298 N ATOM 391 CA LEU A 100 128.388 -0.193 145.617 1.00 87.32 C ANISOU 391 CA LEU A 100 11603 11686 9890 806 -1170 198 C ATOM 392 C LEU A 100 127.541 0.331 146.779 1.00 93.42 C ANISOU 392 C LEU A 100 12325 12491 10681 1094 -1190 13 C ATOM 393 O LEU A 100 128.103 0.667 147.827 1.00 94.23 O ANISOU 393 O LEU A 100 12476 12554 10773 1123 -1176 -130 O ATOM 394 CB LEU A 100 128.571 0.882 144.536 1.00 88.91 C ANISOU 394 CB LEU A 100 12024 11603 10154 746 -1326 314 C ATOM 395 CG LEU A 100 129.291 2.152 144.961 1.00 95.48 C ANISOU 395 CG LEU A 100 13081 12135 11061 726 -1439 241 C ATOM 396 CD1 LEU A 100 130.514 2.394 144.106 1.00 95.77 C ANISOU 396 CD1 LEU A 100 13266 12029 11095 404 -1450 384 C ATOM 397 CD2 LEU A 100 128.367 3.333 144.873 1.00100.77 C ANISOU 397 CD2 LEU A 100 13899 12572 11816 977 -1621 207 C ATOM 398 N VAL A 101 126.202 0.403 146.594 1.00 90.38 N ANISOU 398 N VAL A 101 11829 12199 10314 1310 -1224 -1 N ATOM 399 CA VAL A 101 125.254 0.902 147.602 1.00 91.87 C ANISOU 399 CA VAL A 101 11928 12467 10510 1614 -1231 -194 C ATOM 400 C VAL A 101 125.246 -0.017 148.837 1.00 94.36 C ANISOU 400 C VAL A 101 12068 13074 10712 1608 -1042 -296 C ATOM 401 O VAL A 101 125.253 0.486 149.965 1.00 95.09 O ANISOU 401 O VAL A 101 12185 13174 10773 1760 -1029 -481 O ATOM 402 CB VAL A 101 123.834 1.183 147.021 1.00 97.27 C ANISOU 402 CB VAL A 101 12494 13219 11245 1851 -1318 -189 C ATOM 403 CG1 VAL A 101 122.857 1.639 148.102 1.00 99.24 C ANISOU 403 CG1 VAL A 101 12608 13606 11492 2183 -1300 -420 C ATOM 404 CG2 VAL A 101 123.899 2.227 145.910 1.00 98.62 C ANISOU 404 CG2 VAL A 101 12898 13060 11512 1883 -1537 -84 C ATOM 405 N GLY A 102 125.305 -1.333 148.605 1.00 88.28 N ANISOU 405 N GLY A 102 11155 12517 9871 1422 -911 -174 N ATOM 406 CA GLY A 102 125.351 -2.348 149.656 1.00 86.79 C ANISOU 406 CA GLY A 102 10834 12583 9560 1371 -741 -214 C ATOM 407 C GLY A 102 126.568 -2.240 150.562 1.00 88.85 C ANISOU 407 C GLY A 102 11226 12767 9765 1298 -724 -292 C ATOM 408 O GLY A 102 126.508 -2.608 151.735 1.00 88.01 O ANISOU 408 O GLY A 102 11058 12837 9543 1354 -624 -385 O ATOM 409 N GLN A 103 127.673 -1.720 150.022 1.00 84.96 N ANISOU 409 N GLN A 103 10909 12029 9344 1165 -825 -252 N ATOM 410 CA GLN A 103 128.922 -1.520 150.749 1.00 84.60 C ANISOU 410 CA GLN A 103 10976 11899 9269 1076 -843 -333 C ATOM 411 C GLN A 103 128.912 -0.169 151.479 1.00 91.54 C ANISOU 411 C GLN A 103 11989 12606 10186 1251 -952 -526 C ATOM 412 O GLN A 103 129.357 -0.092 152.627 1.00 91.42 O ANISOU 412 O GLN A 103 11999 12646 10091 1295 -935 -671 O ATOM 413 CB GLN A 103 130.122 -1.643 149.797 1.00 84.30 C ANISOU 413 CB GLN A 103 11025 11718 9289 825 -886 -209 C ATOM 414 CG GLN A 103 130.393 -3.087 149.359 1.00 87.12 C ANISOU 414 CG GLN A 103 11266 12249 9586 668 -778 -76 C ATOM 415 CD GLN A 103 131.064 -3.210 148.007 1.00104.41 C ANISOU 415 CD GLN A 103 13501 14340 11830 467 -806 59 C ATOM 416 OE1 GLN A 103 131.517 -2.233 147.396 1.00 97.89 O ANISOU 416 OE1 GLN A 103 12801 13317 11077 395 -897 78 O ATOM 417 NE2 GLN A 103 131.156 -4.434 147.510 1.00 96.06 N ANISOU 417 NE2 GLN A 103 12353 13417 10728 363 -725 153 N ATOM 418 N LEU A 104 128.376 0.881 150.825 1.00 90.71 N ANISOU 418 N LEU A 104 11983 12285 10195 1363 -1080 -534 N ATOM 419 CA LEU A 104 128.275 2.228 151.391 1.00 93.81 C ANISOU 419 CA LEU A 104 12538 12456 10650 1554 -1215 -723 C ATOM 420 C LEU A 104 127.322 2.302 152.588 1.00 98.94 C ANISOU 420 C LEU A 104 13075 13311 11208 1848 -1149 -936 C ATOM 421 O LEU A 104 127.544 3.117 153.483 1.00100.64 O ANISOU 421 O LEU A 104 13411 13413 11415 1984 -1222 -1147 O ATOM 422 CB LEU A 104 127.848 3.256 150.320 1.00 95.82 C ANISOU 422 CB LEU A 104 12943 12417 11047 1625 -1384 -653 C ATOM 423 CG LEU A 104 128.921 3.760 149.342 1.00101.07 C ANISOU 423 CG LEU A 104 13826 12772 11803 1356 -1500 -507 C ATOM 424 CD1 LEU A 104 128.314 4.723 148.341 1.00103.56 C ANISOU 424 CD1 LEU A 104 14307 12812 12229 1459 -1672 -418 C ATOM 425 CD2 LEU A 104 130.063 4.476 150.067 1.00104.62 C ANISOU 425 CD2 LEU A 104 14449 13019 12282 1255 -1578 -650 C ATOM 426 N LEU A 105 126.264 1.468 152.598 1.00 94.18 N ANISOU 426 N LEU A 105 12239 13017 10529 1934 -1010 -890 N ATOM 427 CA LEU A 105 125.256 1.441 153.665 1.00 95.54 C ANISOU 427 CA LEU A 105 12254 13457 10590 2192 -907 -1075 C ATOM 428 C LEU A 105 125.657 0.582 154.875 1.00 99.12 C ANISOU 428 C LEU A 105 12636 14178 10847 2114 -746 -1124 C ATOM 429 O LEU A 105 125.193 0.852 155.982 1.00100.60 O ANISOU 429 O LEU A 105 12784 14525 10916 2317 -688 -1329 O ATOM 430 CB LEU A 105 123.911 0.957 153.098 1.00 95.74 C ANISOU 430 CB LEU A 105 12039 13708 10629 2295 -835 -998 C ATOM 431 CG LEU A 105 122.861 2.006 152.666 1.00102.85 C ANISOU 431 CG LEU A 105 12920 14512 11647 2612 -969 -1116 C ATOM 432 CD1 LEU A 105 123.452 3.109 151.791 1.00103.70 C ANISOU 432 CD1 LEU A 105 13315 14163 11922 2613 -1209 -1076 C ATOM 433 CD2 LEU A 105 121.723 1.341 151.914 1.00103.37 C ANISOU 433 CD2 LEU A 105 12724 14818 11734 2639 -913 -1000 C ATOM 434 N THR A 106 126.513 -0.440 154.669 1.00 93.13 N ANISOU 434 N THR A 106 11872 13470 10042 1840 -681 -945 N ATOM 435 CA THR A 106 126.916 -1.358 155.732 1.00 92.25 C ANISOU 435 CA THR A 106 11718 13593 9740 1759 -553 -949 C ATOM 436 C THR A 106 128.254 -0.988 156.419 1.00 96.91 C ANISOU 436 C THR A 106 12487 14045 10290 1695 -645 -1054 C ATOM 437 O THR A 106 128.261 -0.806 157.638 1.00 98.08 O ANISOU 437 O THR A 106 12659 14324 10284 1818 -613 -1224 O ATOM 438 CB THR A 106 126.914 -2.824 155.234 1.00 93.86 C ANISOU 438 CB THR A 106 11809 13947 9906 1536 -440 -711 C ATOM 439 OG1 THR A 106 127.750 -2.962 154.084 1.00 87.57 O ANISOU 439 OG1 THR A 106 11094 12929 9248 1348 -534 -570 O ATOM 440 CG2 THR A 106 125.513 -3.350 154.937 1.00 90.75 C ANISOU 440 CG2 THR A 106 11204 13784 9493 1582 -319 -638 C ATOM 441 N THR A 107 129.364 -0.895 155.652 1.00 92.38 N ANISOU 441 N THR A 107 12020 13240 9839 1498 -753 -960 N ATOM 442 CA THR A 107 130.732 -0.655 156.148 1.00 92.11 C ANISOU 442 CA THR A 107 12113 13094 9793 1384 -850 -1037 C ATOM 443 C THR A 107 130.903 0.563 157.095 1.00 98.62 C ANISOU 443 C THR A 107 13077 13800 10596 1542 -963 -1304 C ATOM 444 O THR A 107 131.537 0.357 158.130 1.00 98.44 O ANISOU 444 O THR A 107 13084 13885 10433 1536 -971 -1409 O ATOM 445 CB THR A 107 131.756 -0.585 155.008 1.00 98.82 C ANISOU 445 CB THR A 107 13019 13729 10800 1148 -937 -903 C ATOM 446 OG1 THR A 107 131.346 -1.433 153.934 1.00 99.86 O ANISOU 446 OG1 THR A 107 13043 13929 10969 1052 -852 -691 O ATOM 447 CG2 THR A 107 133.147 -0.976 155.460 1.00 94.21 C ANISOU 447 CG2 THR A 107 12459 13163 10174 988 -982 -925 C ATOM 448 N PRO A 108 130.401 1.805 156.828 1.00 97.20 N ANISOU 448 N PRO A 108 12999 13392 10539 1693 -1070 -1429 N ATOM 449 CA PRO A 108 130.636 2.910 157.787 1.00 99.51 C ANISOU 449 CA PRO A 108 13449 13553 10807 1842 -1192 -1710 C ATOM 450 C PRO A 108 130.158 2.634 159.210 1.00105.09 C ANISOU 450 C PRO A 108 14092 14564 11273 2045 -1089 -1897 C ATOM 451 O PRO A 108 130.817 3.066 160.159 1.00106.61 O ANISOU 451 O PRO A 108 14399 14730 11377 2072 -1174 -2096 O ATOM 452 CB PRO A 108 129.907 4.099 157.154 1.00102.90 C ANISOU 452 CB PRO A 108 13988 13700 11409 2011 -1311 -1781 C ATOM 453 CG PRO A 108 129.858 3.776 155.714 1.00105.34 C ANISOU 453 CG PRO A 108 14259 13906 11861 1838 -1308 -1507 C ATOM 454 CD PRO A 108 129.643 2.291 155.659 1.00 98.45 C ANISOU 454 CD PRO A 108 13164 13381 10862 1745 -1114 -1332 C ATOM 455 N VAL A 109 129.044 1.879 159.355 1.00101.05 N ANISOU 455 N VAL A 109 13394 14359 10640 2160 -903 -1827 N ATOM 456 CA VAL A 109 128.469 1.477 160.649 1.00102.04 C ANISOU 456 CA VAL A 109 13434 14836 10500 2323 -757 -1961 C ATOM 457 C VAL A 109 129.468 0.545 161.373 1.00103.82 C ANISOU 457 C VAL A 109 13683 15220 10544 2142 -724 -1883 C ATOM 458 O VAL A 109 129.789 0.788 162.540 1.00104.91 O ANISOU 458 O VAL A 109 13899 15474 10489 2236 -742 -2073 O ATOM 459 CB VAL A 109 127.062 0.831 160.499 1.00105.87 C ANISOU 459 CB VAL A 109 13688 15620 10918 2430 -558 -1872 C ATOM 460 CG1 VAL A 109 126.432 0.573 161.863 1.00107.88 C ANISOU 460 CG1 VAL A 109 13855 16255 10879 2592 -391 -2025 C ATOM 461 CG2 VAL A 109 126.138 1.694 159.642 1.00106.72 C ANISOU 461 CG2 VAL A 109 13758 15566 11227 2619 -626 -1933 C ATOM 462 N VAL A 110 129.984 -0.485 160.648 1.00 96.75 N ANISOU 462 N VAL A 110 12733 14317 9709 1900 -697 -1616 N ATOM 463 CA VAL A 110 130.980 -1.464 161.121 1.00 95.08 C ANISOU 463 CA VAL A 110 12543 14217 9367 1734 -696 -1508 C ATOM 464 C VAL A 110 132.259 -0.733 161.584 1.00 99.28 C ANISOU 464 C VAL A 110 13224 14577 9919 1695 -890 -1683 C ATOM 465 O VAL A 110 132.808 -1.076 162.630 1.00100.52 O ANISOU 465 O VAL A 110 13426 14890 9876 1704 -913 -1750 O ATOM 466 CB VAL A 110 131.281 -2.555 160.048 1.00 96.28 C ANISOU 466 CB VAL A 110 12614 14337 9632 1517 -656 -1221 C ATOM 467 CG1 VAL A 110 132.337 -3.548 160.530 1.00 95.37 C ANISOU 467 CG1 VAL A 110 12527 14313 9397 1389 -683 -1127 C ATOM 468 CG2 VAL A 110 130.012 -3.292 159.634 1.00 95.44 C ANISOU 468 CG2 VAL A 110 12359 14399 9504 1531 -481 -1064 C ATOM 469 N ILE A 111 132.710 0.291 160.825 1.00 94.83 N ANISOU 469 N ILE A 111 12744 13698 9590 1639 -1039 -1752 N ATOM 470 CA ILE A 111 133.886 1.097 161.175 1.00 95.22 C ANISOU 470 CA ILE A 111 12925 13560 9692 1562 -1234 -1926 C ATOM 471 C ILE A 111 133.628 1.835 162.506 1.00102.50 C ANISOU 471 C ILE A 111 13957 14549 10441 1779 -1286 -2229 C ATOM 472 O ILE A 111 134.442 1.723 163.423 1.00103.22 O ANISOU 472 O ILE A 111 14101 14729 10389 1750 -1373 -2347 O ATOM 473 CB ILE A 111 134.325 2.040 160.008 1.00 97.38 C ANISOU 473 CB ILE A 111 13277 13469 10253 1414 -1364 -1899 C ATOM 474 CG1 ILE A 111 134.784 1.226 158.781 1.00 94.81 C ANISOU 474 CG1 ILE A 111 12842 13132 10049 1181 -1310 -1620 C ATOM 475 CG2 ILE A 111 135.425 3.023 160.442 1.00 99.37 C ANISOU 475 CG2 ILE A 111 13675 13512 10570 1320 -1572 -2108 C ATOM 476 CD1 ILE A 111 134.639 1.962 157.426 1.00103.52 C ANISOU 476 CD1 ILE A 111 14001 13945 11387 1072 -1361 -1515 C ATOM 477 N VAL A 112 132.468 2.522 162.622 1.00100.31 N ANISOU 477 N VAL A 112 13697 14259 10157 2014 -1233 -2363 N ATOM 478 CA VAL A 112 132.054 3.293 163.800 1.00102.99 C ANISOU 478 CA VAL A 112 14134 14668 10331 2268 -1265 -2683 C ATOM 479 C VAL A 112 132.020 2.436 165.080 1.00107.47 C ANISOU 479 C VAL A 112 14652 15633 10547 2332 -1147 -2718 C ATOM 480 O VAL A 112 132.528 2.888 166.108 1.00109.23 O ANISOU 480 O VAL A 112 14998 15890 10616 2405 -1254 -2960 O ATOM 481 CB VAL A 112 130.722 4.043 163.536 1.00108.50 C ANISOU 481 CB VAL A 112 14814 15309 11103 2535 -1211 -2800 C ATOM 482 CG1 VAL A 112 130.046 4.497 164.828 1.00111.60 C ANISOU 482 CG1 VAL A 112 15232 15919 11251 2840 -1157 -3115 C ATOM 483 CG2 VAL A 112 130.945 5.230 162.604 1.00109.06 C ANISOU 483 CG2 VAL A 112 15042 14916 11481 2512 -1411 -2854 C ATOM 484 N VAL A 113 131.467 1.205 165.018 1.00102.70 N ANISOU 484 N VAL A 113 13894 15315 9814 2286 -944 -2473 N ATOM 485 CA VAL A 113 131.401 0.338 166.205 1.00103.64 C ANISOU 485 CA VAL A 113 13995 15803 9582 2321 -827 -2458 C ATOM 486 C VAL A 113 132.814 -0.095 166.663 1.00108.54 C ANISOU 486 C VAL A 113 14708 16410 10123 2161 -982 -2424 C ATOM 487 O VAL A 113 133.052 -0.156 167.868 1.00110.39 O ANISOU 487 O VAL A 113 15024 16850 10071 2245 -1004 -2558 O ATOM 488 CB VAL A 113 130.404 -0.850 166.123 1.00106.27 C ANISOU 488 CB VAL A 113 14162 16437 9778 2294 -573 -2206 C ATOM 489 CG1 VAL A 113 128.964 -0.354 166.091 1.00107.52 C ANISOU 489 CG1 VAL A 113 14200 16727 9924 2505 -417 -2324 C ATOM 490 CG2 VAL A 113 130.680 -1.753 164.933 1.00103.00 C ANISOU 490 CG2 VAL A 113 13664 15903 9569 2064 -557 -1884 C ATOM 491 N TYR A 114 133.761 -0.313 165.719 1.00103.53 N ANISOU 491 N TYR A 114 14057 15550 9731 1949 -1100 -2272 N ATOM 492 CA TYR A 114 135.155 -0.663 166.048 1.00102.89 C ANISOU 492 CA TYR A 114 14022 15458 9615 1810 -1267 -2262 C ATOM 493 C TYR A 114 135.863 0.499 166.766 1.00109.76 C ANISOU 493 C TYR A 114 15028 16208 10469 1861 -1479 -2589 C ATOM 494 O TYR A 114 136.592 0.269 167.733 1.00110.40 O ANISOU 494 O TYR A 114 15166 16434 10346 1868 -1589 -2682 O ATOM 495 CB TYR A 114 135.942 -1.027 164.779 1.00100.68 C ANISOU 495 CB TYR A 114 13657 14983 9612 1585 -1325 -2058 C ATOM 496 CG TYR A 114 135.956 -2.496 164.425 1.00 99.27 C ANISOU 496 CG TYR A 114 13381 14954 9382 1497 -1211 -1761 C ATOM 497 CD1 TYR A 114 136.845 -3.374 165.040 1.00100.96 C ANISOU 497 CD1 TYR A 114 13608 15310 9441 1460 -1291 -1696 C ATOM 498 CD2 TYR A 114 135.157 -2.992 163.400 1.00 97.93 C ANISOU 498 CD2 TYR A 114 13117 14750 9340 1448 -1056 -1551 C ATOM 499 CE1 TYR A 114 136.902 -4.719 164.676 1.00 99.89 C ANISOU 499 CE1 TYR A 114 13414 15259 9279 1391 -1215 -1429 C ATOM 500 CE2 TYR A 114 135.211 -4.333 163.021 1.00 96.89 C ANISOU 500 CE2 TYR A 114 12919 14714 9183 1355 -974 -1294 C ATOM 501 CZ TYR A 114 136.084 -5.194 163.663 1.00103.81 C ANISOU 501 CZ TYR A 114 13830 15705 9908 1331 -1053 -1234 C ATOM 502 OH TYR A 114 136.131 -6.516 163.291 1.00101.52 O ANISOU 502 OH TYR A 114 13504 15466 9601 1259 -992 -989 O ATOM 503 N LEU A 115 135.641 1.741 166.281 1.00108.29 N ANISOU 503 N LEU A 115 14908 15741 10496 1896 -1555 -2762 N ATOM 504 CA LEU A 115 136.221 2.974 166.819 1.00111.61 C ANISOU 504 CA LEU A 115 15484 15972 10952 1927 -1770 -3088 C ATOM 505 C LEU A 115 135.706 3.283 168.223 1.00120.30 C ANISOU 505 C LEU A 115 16686 17293 11732 2183 -1753 -3362 C ATOM 506 O LEU A 115 136.456 3.817 169.044 1.00122.33 O ANISOU 506 O LEU A 115 17061 17528 11890 2190 -1941 -3611 O ATOM 507 CB LEU A 115 135.938 4.169 165.874 1.00112.14 C ANISOU 507 CB LEU A 115 15630 15647 11333 1910 -1846 -3165 C ATOM 508 CG LEU A 115 137.000 4.580 164.814 1.00115.81 C ANISOU 508 CG LEU A 115 16108 15788 12108 1610 -2005 -3077 C ATOM 509 CD1 LEU A 115 138.296 5.085 165.445 1.00117.94 C ANISOU 509 CD1 LEU A 115 16457 15989 12368 1467 -2239 -3290 C ATOM 510 CD2 LEU A 115 137.249 3.496 163.774 1.00114.28 C ANISOU 510 CD2 LEU A 115 15737 15665 12019 1416 -1887 -2728 C ATOM 511 N SER A 116 134.434 2.935 168.497 1.00118.62 N ANISOU 511 N SER A 116 16412 17314 11344 2382 -1526 -3324 N ATOM 512 CA SER A 116 133.770 3.141 169.787 1.00122.46 C ANISOU 512 CA SER A 116 16962 18079 11489 2636 -1450 -3569 C ATOM 513 C SER A 116 134.150 2.072 170.837 1.00129.63 C ANISOU 513 C SER A 116 17868 19363 12023 2608 -1396 -3470 C ATOM 514 O SER A 116 133.740 2.180 171.996 1.00131.88 O ANISOU 514 O SER A 116 18216 19926 11966 2793 -1327 -3655 O ATOM 515 CB SER A 116 132.255 3.190 169.596 1.00125.79 C ANISOU 515 CB SER A 116 17279 18630 11883 2844 -1216 -3567 C ATOM 516 OG SER A 116 131.714 1.905 169.339 1.00130.49 O ANISOU 516 OG SER A 116 17705 19479 12396 2753 -988 -3229 O ATOM 517 N LYS A 117 134.946 1.058 170.416 1.00126.09 N ANISOU 517 N LYS A 117 17357 18917 11633 2387 -1438 -3184 N ATOM 518 CA LYS A 117 135.441 -0.100 171.181 1.00127.05 C ANISOU 518 CA LYS A 117 17490 19323 11459 2333 -1429 -3018 C ATOM 519 C LYS A 117 134.314 -1.129 171.408 1.00133.85 C ANISOU 519 C LYS A 117 18279 20494 12083 2383 -1141 -2781 C ATOM 520 O LYS A 117 133.964 -1.459 172.549 1.00135.63 O ANISOU 520 O LYS A 117 18574 21038 11920 2490 -1053 -2825 O ATOM 521 CB LYS A 117 136.188 0.295 172.477 1.00132.20 C ANISOU 521 CB LYS A 117 18296 20102 11830 2417 -1624 -3291 C ATOM 522 CG LYS A 117 137.383 1.236 172.261 1.00144.04 C ANISOU 522 CG LYS A 117 19852 21306 13570 2317 -1925 -3519 C ATOM 523 CD LYS A 117 138.610 0.546 171.649 1.00150.41 C ANISOU 523 CD LYS A 117 20564 22017 14569 2087 -2072 -3308 C ATOM 524 CE LYS A 117 139.614 0.067 172.672 1.00162.16 C ANISOU 524 CE LYS A 117 22105 23715 15793 2087 -2262 -3351 C ATOM 525 NZ LYS A 117 140.338 1.196 173.317 1.00175.20 N ANISOU 525 NZ LYS A 117 23862 25283 17424 2100 -2525 -3727 N ATOM 526 N GLN A 118 133.767 -1.634 170.266 1.00129.74 N ANISOU 526 N GLN A 118 17619 19878 11800 2280 -996 -2524 N ATOM 527 CA GLN A 118 132.666 -2.601 170.115 1.00129.58 C ANISOU 527 CA GLN A 118 17490 20082 11662 2261 -726 -2267 C ATOM 528 C GLN A 118 131.396 -2.201 170.913 1.00136.94 C ANISOU 528 C GLN A 118 18394 21301 12335 2463 -520 -2442 C ATOM 529 O GLN A 118 131.111 -1.004 171.020 1.00138.62 O ANISOU 529 O GLN A 118 18624 21421 12623 2638 -568 -2751 O ATOM 530 CB GLN A 118 133.116 -4.045 170.405 1.00130.43 C ANISOU 530 CB GLN A 118 17635 20343 11578 2122 -707 -1962 C ATOM 531 CG GLN A 118 133.537 -4.806 169.153 1.00139.52 C ANISOU 531 CG GLN A 118 18700 21283 13026 1933 -732 -1678 C ATOM 532 CD GLN A 118 135.028 -4.754 168.946 1.00161.11 C ANISOU 532 CD GLN A 118 21483 23823 15908 1854 -994 -1703 C ATOM 533 OE1 GLN A 118 135.588 -3.745 168.507 1.00157.11 O ANISOU 533 OE1 GLN A 118 20964 23098 15634 1846 -1144 -1898 O ATOM 534 NE2 GLN A 118 135.708 -5.845 169.268 1.00154.48 N ANISOU 534 NE2 GLN A 118 20698 23060 14937 1790 -1061 -1507 N ATOM 535 N ARG A 119 130.629 -3.197 171.431 1.00133.86 N ANISOU 535 N ARG A 119 17958 21255 11649 2433 -290 -2248 N ATOM 536 CA ARG A 119 129.365 -3.029 172.156 1.00136.31 C ANISOU 536 CA ARG A 119 18191 21921 11678 2588 -42 -2370 C ATOM 537 C ARG A 119 128.332 -2.328 171.267 1.00139.07 C ANISOU 537 C ARG A 119 18350 22191 12302 2697 71 -2472 C ATOM 538 O ARG A 119 128.054 -1.139 171.444 1.00140.38 O ANISOU 538 O ARG A 119 18520 22314 12503 2929 29 -2812 O ATOM 539 CB ARG A 119 129.555 -2.334 173.519 1.00140.18 C ANISOU 539 CB ARG A 119 18832 22608 11820 2785 -101 -2700 C ATOM 540 N TRP A 120 127.814 -3.074 170.266 1.00133.13 N ANISOU 540 N TRP A 120 17440 21391 11752 2535 185 -2182 N ATOM 541 CA TRP A 120 126.810 -2.619 169.293 1.00132.28 C ANISOU 541 CA TRP A 120 17129 21220 11912 2608 282 -2210 C ATOM 542 C TRP A 120 125.564 -2.113 170.009 1.00140.75 C ANISOU 542 C TRP A 120 18055 22660 12764 2837 499 -2436 C ATOM 543 O TRP A 120 125.000 -1.094 169.607 1.00141.38 O ANISOU 543 O TRP A 120 18042 22647 13031 3054 476 -2669 O ATOM 544 CB TRP A 120 126.435 -3.763 168.329 1.00128.14 C ANISOU 544 CB TRP A 120 16469 20679 11541 2362 387 -1836 C ATOM 545 CG TRP A 120 125.329 -3.435 167.364 1.00128.65 C ANISOU 545 CG TRP A 120 16304 20735 11843 2420 489 -1837 C ATOM 546 CD1 TRP A 120 123.992 -3.392 167.632 1.00134.00 C ANISOU 546 CD1 TRP A 120 16758 21761 12393 2519 724 -1895 C ATOM 547 CD2 TRP A 120 125.466 -3.152 165.965 1.00125.68 C ANISOU 547 CD2 TRP A 120 15884 20011 11856 2375 356 -1767 C ATOM 548 NE1 TRP A 120 123.293 -3.041 166.504 1.00132.41 N ANISOU 548 NE1 TRP A 120 16375 21442 12494 2566 720 -1887 N ATOM 549 CE2 TRP A 120 124.171 -2.902 165.460 1.00130.56 C ANISOU 549 CE2 TRP A 120 16264 20773 12569 2476 494 -1797 C ATOM 550 CE3 TRP A 120 126.560 -3.074 165.087 1.00123.96 C ANISOU 550 CE3 TRP A 120 15798 19398 11903 2257 135 -1685 C ATOM 551 CZ2 TRP A 120 123.938 -2.588 164.115 1.00127.88 C ANISOU 551 CZ2 TRP A 120 15843 20177 12570 2471 398 -1737 C ATOM 552 CZ3 TRP A 120 126.328 -2.755 163.758 1.00123.55 C ANISOU 552 CZ3 TRP A 120 15667 19102 12173 2236 67 -1623 C ATOM 553 CH2 TRP A 120 125.029 -2.523 163.283 1.00125.07 C ANISOU 553 CH2 TRP A 120 15651 19427 12444 2345 188 -1642 C ATOM 554 N GLU A 121 125.145 -2.839 171.067 1.00140.20 N ANISOU 554 N GLU A 121 17970 23013 12289 2790 708 -2363 N ATOM 555 CA GLU A 121 123.978 -2.564 171.907 1.00144.12 C ANISOU 555 CA GLU A 121 18305 23964 12490 2971 966 -2554 C ATOM 556 C GLU A 121 124.063 -1.203 172.612 1.00151.16 C ANISOU 556 C GLU A 121 19284 24857 13293 3317 871 -3023 C ATOM 557 O GLU A 121 123.027 -0.648 172.983 1.00154.10 O ANISOU 557 O GLU A 121 19480 25527 13543 3550 1049 -3265 O ATOM 558 CB GLU A 121 123.765 -3.702 172.926 1.00147.51 C ANISOU 558 CB GLU A 121 18761 24815 12470 2786 1187 -2330 C ATOM 559 CG GLU A 121 123.444 -5.057 172.303 1.00155.49 C ANISOU 559 CG GLU A 121 19672 25860 13547 2452 1317 -1889 C ATOM 560 CD GLU A 121 124.611 -5.966 171.952 1.00170.08 C ANISOU 560 CD GLU A 121 21738 27387 15499 2207 1120 -1577 C ATOM 561 OE1 GLU A 121 125.763 -5.480 171.868 1.00161.84 O ANISOU 561 OE1 GLU A 121 20880 26021 14592 2279 847 -1690 O ATOM 562 OE2 GLU A 121 124.363 -7.174 171.739 1.00161.99 O ANISOU 562 OE2 GLU A 121 20689 26433 14427 1940 1235 -1225 O ATOM 563 N HIS A 122 125.289 -0.670 172.794 1.00147.06 N ANISOU 563 N HIS A 122 19024 24013 12837 3351 586 -3164 N ATOM 564 CA HIS A 122 125.516 0.635 173.416 1.00149.84 C ANISOU 564 CA HIS A 122 19511 24284 13138 3651 441 -3617 C ATOM 565 C HIS A 122 125.235 1.734 172.396 1.00152.44 C ANISOU 565 C HIS A 122 19794 24221 13904 3825 289 -3802 C ATOM 566 O HIS A 122 124.514 2.686 172.701 1.00155.46 O ANISOU 566 O HIS A 122 20136 24664 14268 4145 309 -4160 O ATOM 567 CB HIS A 122 126.949 0.747 173.966 1.00150.49 C ANISOU 567 CB HIS A 122 19882 24184 13112 3577 182 -3682 C ATOM 568 N ILE A 123 125.776 1.578 171.175 1.00144.33 N ANISOU 568 N ILE A 123 18783 22799 13258 3624 136 -3557 N ATOM 569 CA ILE A 123 125.602 2.511 170.062 1.00143.02 C ANISOU 569 CA ILE A 123 18605 22225 13512 3732 -25 -3650 C ATOM 570 C ILE A 123 124.155 2.468 169.514 1.00146.94 C ANISOU 570 C ILE A 123 18814 22919 14099 3875 178 -3623 C ATOM 571 O ILE A 123 123.674 3.467 168.970 1.00147.73 O ANISOU 571 O ILE A 123 18892 22802 14436 4115 77 -3829 O ATOM 572 CB ILE A 123 126.710 2.263 168.982 1.00142.02 C ANISOU 572 CB ILE A 123 18589 21666 13705 3441 -236 -3383 C ATOM 573 CG1 ILE A 123 127.633 3.506 168.804 1.00143.27 C ANISOU 573 CG1 ILE A 123 18993 21371 14073 3497 -548 -3629 C ATOM 574 CG2 ILE A 123 126.186 1.738 167.636 1.00139.32 C ANISOU 574 CG2 ILE A 123 18071 21209 13654 3308 -175 -3087 C ATOM 575 CD1 ILE A 123 126.973 4.891 168.363 1.00154.26 C ANISOU 575 CD1 ILE A 123 20431 22463 15718 3780 -671 -3915 C ATOM 576 N ASP A 124 123.469 1.321 169.687 1.00142.40 N ANISOU 576 N ASP A 124 18024 22753 13327 3726 450 -3376 N ATOM 577 CA ASP A 124 122.102 1.097 169.226 1.00142.63 C ANISOU 577 CA ASP A 124 17734 23047 13411 3806 664 -3324 C ATOM 578 C ASP A 124 121.241 0.427 170.337 1.00149.23 C ANISOU 578 C ASP A 124 18380 24502 13818 3820 995 -3344 C ATOM 579 O ASP A 124 121.004 -0.786 170.273 1.00147.30 O ANISOU 579 O ASP A 124 18021 24492 13455 3531 1178 -3010 O ATOM 580 CB ASP A 124 122.130 0.275 167.917 1.00140.28 C ANISOU 580 CB ASP A 124 17340 22567 13394 3515 647 -2931 C ATOM 581 CG ASP A 124 120.804 0.135 167.202 1.00149.00 C ANISOU 581 CG ASP A 124 18117 23861 14635 3584 797 -2879 C ATOM 582 OD1 ASP A 124 120.113 1.163 167.023 1.00151.82 O ANISOU 582 OD1 ASP A 124 18380 24185 15121 3914 745 -3160 O ATOM 583 OD2 ASP A 124 120.478 -0.993 166.775 1.00151.69 O ANISOU 583 OD2 ASP A 124 18302 24360 14973 3311 939 -2562 O ATOM 584 N PRO A 125 120.785 1.191 171.375 1.00150.22 N ANISOU 584 N PRO A 125 18486 24899 13691 4141 1079 -3731 N ATOM 585 CA PRO A 125 119.962 0.573 172.440 1.00153.42 C ANISOU 585 CA PRO A 125 18701 25937 13654 4138 1420 -3750 C ATOM 586 C PRO A 125 118.601 0.089 171.938 1.00157.92 C ANISOU 586 C PRO A 125 18864 26859 14281 4106 1682 -3628 C ATOM 587 O PRO A 125 118.118 -0.947 172.395 1.00158.57 O ANISOU 587 O PRO A 125 18794 27372 14084 3867 1958 -3401 O ATOM 588 CB PRO A 125 119.849 1.673 173.498 1.00159.63 C ANISOU 588 CB PRO A 125 19571 26872 14210 4531 1407 -4245 C ATOM 589 CG PRO A 125 120.055 2.936 172.761 1.00163.64 C ANISOU 589 CG PRO A 125 20187 26871 15119 4804 1109 -4507 C ATOM 590 CD PRO A 125 120.979 2.636 171.617 1.00154.07 C ANISOU 590 CD PRO A 125 19130 25134 14278 4513 870 -4174 C ATOM 591 N SER A 126 118.007 0.827 170.979 1.00153.92 N ANISOU 591 N SER A 126 18192 26154 14138 4330 1577 -3764 N ATOM 592 CA SER A 126 116.763 0.473 170.295 1.00154.31 C ANISOU 592 CA SER A 126 17838 26476 14319 4318 1758 -3665 C ATOM 593 C SER A 126 117.161 -0.465 169.151 1.00153.77 C ANISOU 593 C SER A 126 17793 26115 14518 3927 1670 -3216 C ATOM 594 O SER A 126 118.339 -0.524 168.797 1.00150.20 O ANISOU 594 O SER A 126 17654 25213 14203 3769 1441 -3065 O ATOM 595 CB SER A 126 116.074 1.721 169.751 1.00159.65 C ANISOU 595 CB SER A 126 18368 27027 15266 4766 1629 -4019 C ATOM 596 OG SER A 126 116.988 2.553 169.057 1.00166.12 O ANISOU 596 OG SER A 126 19509 27203 16406 4877 1265 -4091 O ATOM 597 N GLY A 127 116.205 -1.203 168.599 1.00150.12 N ANISOU 597 N GLY A 127 16996 25925 14119 3768 1850 -3020 N ATOM 598 CA GLY A 127 116.494 -2.161 167.534 1.00145.41 C ANISOU 598 CA GLY A 127 16409 25092 13749 3395 1783 -2612 C ATOM 599 C GLY A 127 116.544 -1.634 166.113 1.00145.02 C ANISOU 599 C GLY A 127 16373 24584 14144 3479 1516 -2585 C ATOM 600 O GLY A 127 116.637 -2.443 165.188 1.00141.50 O ANISOU 600 O GLY A 127 15923 23968 13871 3179 1468 -2266 O ATOM 601 N ARG A 128 116.504 -0.288 165.917 1.00141.85 N ANISOU 601 N ARG A 128 16015 23962 13920 3881 1329 -2912 N ATOM 602 CA ARG A 128 116.492 0.356 164.588 1.00139.21 C ANISOU 602 CA ARG A 128 15714 23191 13987 3999 1062 -2900 C ATOM 603 C ARG A 128 117.711 0.031 163.702 1.00135.81 C ANISOU 603 C ARG A 128 15590 22249 13761 3703 842 -2609 C ATOM 604 O ARG A 128 117.513 -0.550 162.637 1.00133.24 O ANISOU 604 O ARG A 128 15162 21841 13621 3498 813 -2353 O ATOM 605 CB ARG A 128 116.268 1.890 164.625 1.00142.89 C ANISOU 605 CB ARG A 128 16252 23451 14589 4485 871 -3300 C ATOM 606 CG ARG A 128 116.143 2.552 165.989 1.00158.45 C ANISOU 606 CG ARG A 128 18266 25661 16278 4782 967 -3678 C ATOM 607 CD ARG A 128 114.700 2.833 166.356 1.00174.28 C ANISOU 607 CD ARG A 128 19865 28173 18180 5116 1168 -3954 C ATOM 608 NE ARG A 128 114.592 3.948 167.298 1.00188.22 N ANISOU 608 NE ARG A 128 21726 29978 19813 5555 1131 -4417 N ATOM 609 CZ ARG A 128 114.184 5.171 166.973 1.00205.51 C ANISOU 609 CZ ARG A 128 23910 31959 22217 6014 936 -4743 C ATOM 610 NH1 ARG A 128 113.824 5.450 165.725 1.00192.56 N ANISOU 610 NH1 ARG A 128 22168 30073 20923 6096 759 -4641 N ATOM 611 NH2 ARG A 128 114.120 6.123 167.895 1.00195.37 N ANISOU 611 NH2 ARG A 128 22735 30704 20793 6407 904 -5179 N ATOM 612 N LEU A 129 118.944 0.407 164.112 1.00129.03 N ANISOU 612 N LEU A 129 15084 21071 12870 3682 686 -2663 N ATOM 613 CA LEU A 129 120.142 0.153 163.298 1.00123.79 C ANISOU 613 CA LEU A 129 14682 19957 12397 3417 486 -2420 C ATOM 614 C LEU A 129 120.430 -1.318 163.036 1.00122.85 C ANISOU 614 C LEU A 129 14525 19942 12210 3013 604 -2049 C ATOM 615 O LEU A 129 120.904 -1.635 161.952 1.00119.40 O ANISOU 615 O LEU A 129 14158 19215 11993 2824 476 -1832 O ATOM 616 CB LEU A 129 121.397 0.834 163.856 1.00123.54 C ANISOU 616 CB LEU A 129 14993 19614 12333 3458 302 -2570 C ATOM 617 CG LEU A 129 121.829 2.138 163.188 1.00128.48 C ANISOU 617 CG LEU A 129 15820 19758 13238 3652 18 -2743 C ATOM 618 CD1 LEU A 129 122.966 2.775 163.955 1.00129.22 C ANISOU 618 CD1 LEU A 129 16222 19613 13263 3657 -137 -2911 C ATOM 619 CD2 LEU A 129 122.257 1.919 161.744 1.00127.63 C ANISOU 619 CD2 LEU A 129 15758 19304 13430 3452 -131 -2472 C ATOM 620 N CYS A 130 120.155 -2.210 164.007 1.00119.31 N ANISOU 620 N CYS A 130 13986 19892 11454 2881 839 -1977 N ATOM 621 CA CYS A 130 120.390 -3.647 163.848 1.00116.09 C ANISOU 621 CA CYS A 130 13574 19562 10971 2503 942 -1624 C ATOM 622 C CYS A 130 119.434 -4.280 162.836 1.00119.85 C ANISOU 622 C CYS A 130 13782 20147 11610 2361 1024 -1437 C ATOM 623 O CYS A 130 119.893 -5.041 161.986 1.00116.34 O ANISOU 623 O CYS A 130 13404 19496 11304 2101 954 -1176 O ATOM 624 CB CYS A 130 120.364 -4.374 165.188 1.00117.67 C ANISOU 624 CB CYS A 130 13797 20128 10784 2395 1151 -1582 C ATOM 625 SG CYS A 130 120.849 -6.117 165.096 1.00118.82 S ANISOU 625 SG CYS A 130 14037 20276 10832 1945 1223 -1144 S ATOM 626 N THR A 131 118.120 -3.957 162.907 1.00120.14 N ANISOU 626 N THR A 131 13503 20514 11632 2542 1162 -1592 N ATOM 627 CA THR A 131 117.136 -4.480 161.945 1.00120.28 C ANISOU 627 CA THR A 131 13226 20666 11811 2427 1221 -1451 C ATOM 628 C THR A 131 117.417 -3.905 160.562 1.00121.33 C ANISOU 628 C THR A 131 13434 20373 12291 2504 955 -1428 C ATOM 629 O THR A 131 117.388 -4.650 159.582 1.00119.34 O ANISOU 629 O THR A 131 13128 20031 12185 2269 917 -1197 O ATOM 630 CB THR A 131 115.681 -4.251 162.392 1.00135.10 C ANISOU 630 CB THR A 131 14708 23045 13578 2613 1432 -1644 C ATOM 631 OG1 THR A 131 115.461 -2.861 162.631 1.00138.98 O ANISOU 631 OG1 THR A 131 15199 23496 14111 3057 1336 -2003 O ATOM 632 CG2 THR A 131 115.292 -5.089 163.613 1.00135.91 C ANISOU 632 CG2 THR A 131 14694 23628 13318 2420 1742 -1576 C ATOM 633 N PHE A 132 117.753 -2.594 160.495 1.00117.35 N ANISOU 633 N PHE A 132 13091 19592 11906 2814 762 -1662 N ATOM 634 CA PHE A 132 118.106 -1.914 159.250 1.00114.95 C ANISOU 634 CA PHE A 132 12916 18855 11905 2889 498 -1636 C ATOM 635 C PHE A 132 119.329 -2.558 158.619 1.00113.43 C ANISOU 635 C PHE A 132 12981 18323 11792 2573 387 -1375 C ATOM 636 O PHE A 132 119.293 -2.839 157.428 1.00112.11 O ANISOU 636 O PHE A 132 12799 17983 11814 2448 284 -1205 O ATOM 637 CB PHE A 132 118.333 -0.404 159.456 1.00118.79 C ANISOU 637 CB PHE A 132 13565 19092 12479 3262 316 -1935 C ATOM 638 CG PHE A 132 118.991 0.282 158.280 1.00118.80 C ANISOU 638 CG PHE A 132 13802 18584 12754 3276 33 -1870 C ATOM 639 CD1 PHE A 132 118.297 0.479 157.090 1.00122.28 C ANISOU 639 CD1 PHE A 132 14119 18938 13405 3349 -82 -1798 C ATOM 640 CD2 PHE A 132 120.312 0.708 158.353 1.00119.90 C ANISOU 640 CD2 PHE A 132 14281 18347 12928 3196 -118 -1870 C ATOM 641 CE1 PHE A 132 118.913 1.088 155.995 1.00121.92 C ANISOU 641 CE1 PHE A 132 14314 18432 13579 3335 -334 -1710 C ATOM 642 CE2 PHE A 132 120.928 1.319 157.256 1.00121.46 C ANISOU 642 CE2 PHE A 132 14693 18097 13361 3163 -357 -1789 C ATOM 643 CZ PHE A 132 120.223 1.507 156.086 1.00119.65 C ANISOU 643 CZ PHE A 132 14365 17781 13317 3231 -459 -1700 C ATOM 644 N PHE A 133 120.397 -2.792 159.416 1.00107.44 N ANISOU 644 N PHE A 133 12448 17492 10880 2459 401 -1358 N ATOM 645 CA PHE A 133 121.648 -3.427 158.984 1.00103.11 C ANISOU 645 CA PHE A 133 12126 16666 10384 2186 304 -1144 C ATOM 646 C PHE A 133 121.372 -4.831 158.472 1.00105.84 C ANISOU 646 C PHE A 133 12353 17138 10722 1886 413 -863 C ATOM 647 O PHE A 133 121.912 -5.209 157.440 1.00102.49 O ANISOU 647 O PHE A 133 12014 16470 10458 1720 301 -696 O ATOM 648 CB PHE A 133 122.688 -3.464 160.117 1.00104.16 C ANISOU 648 CB PHE A 133 12473 16781 10323 2157 305 -1207 C ATOM 649 CG PHE A 133 124.090 -3.810 159.675 1.00101.70 C ANISOU 649 CG PHE A 133 12386 16160 10096 1951 160 -1058 C ATOM 650 CD1 PHE A 133 124.505 -5.133 159.595 1.00102.07 C ANISOU 650 CD1 PHE A 133 12454 16260 10069 1688 226 -815 C ATOM 651 CD2 PHE A 133 125.006 -2.811 159.373 1.00102.21 C ANISOU 651 CD2 PHE A 133 12641 15884 10312 2020 -44 -1170 C ATOM 652 CE1 PHE A 133 125.802 -5.452 159.196 1.00100.15 C ANISOU 652 CE1 PHE A 133 12387 15760 9904 1534 93 -706 C ATOM 653 CE2 PHE A 133 126.304 -3.131 158.972 1.00102.16 C ANISOU 653 CE2 PHE A 133 12795 15642 10377 1823 -160 -1047 C ATOM 654 CZ PHE A 133 126.689 -4.449 158.878 1.00 98.36 C ANISOU 654 CZ PHE A 133 12303 15246 9823 1600 -90 -827 C ATOM 655 N GLY A 134 120.524 -5.571 159.189 1.00104.99 N ANISOU 655 N GLY A 134 12056 17413 10424 1813 630 -821 N ATOM 656 CA GLY A 134 120.105 -6.912 158.809 1.00104.30 C ANISOU 656 CA GLY A 134 11851 17462 10316 1514 743 -567 C ATOM 657 C GLY A 134 119.384 -6.886 157.477 1.00108.17 C ANISOU 657 C GLY A 134 12159 17903 11038 1495 673 -510 C ATOM 658 O GLY A 134 119.699 -7.683 156.588 1.00105.58 O ANISOU 658 O GLY A 134 11874 17432 10811 1258 622 -307 O ATOM 659 N LEU A 135 118.454 -5.913 157.314 1.00107.10 N ANISOU 659 N LEU A 135 11834 17874 10988 1771 648 -709 N ATOM 660 CA LEU A 135 117.690 -5.695 156.084 1.00106.89 C ANISOU 660 CA LEU A 135 11625 17814 11173 1819 546 -690 C ATOM 661 C LEU A 135 118.629 -5.365 154.913 1.00107.45 C ANISOU 661 C LEU A 135 11940 17439 11446 1785 309 -601 C ATOM 662 O LEU A 135 118.611 -6.101 153.925 1.00105.54 O ANISOU 662 O LEU A 135 11672 17126 11302 1578 262 -421 O ATOM 663 CB LEU A 135 116.622 -4.594 156.273 1.00110.22 C ANISOU 663 CB LEU A 135 11817 18431 11632 2185 543 -951 C ATOM 664 CG LEU A 135 115.716 -4.305 155.065 1.00115.86 C ANISOU 664 CG LEU A 135 12324 19142 12556 2288 412 -951 C ATOM 665 CD1 LEU A 135 114.256 -4.259 155.475 1.00120.12 C ANISOU 665 CD1 LEU A 135 12435 20166 13038 2409 571 -1080 C ATOM 666 CD2 LEU A 135 116.111 -3.007 154.366 1.00117.67 C ANISOU 666 CD2 LEU A 135 12742 19004 12964 2592 154 -1081 C ATOM 667 N THR A 136 119.471 -4.299 155.041 1.00103.04 N ANISOU 667 N THR A 136 11624 16592 10935 1964 165 -726 N ATOM 668 CA THR A 136 120.398 -3.856 153.988 1.00100.69 C ANISOU 668 CA THR A 136 11562 15886 10810 1922 -46 -648 C ATOM 669 C THR A 136 121.387 -4.984 153.585 1.00101.17 C ANISOU 669 C THR A 136 11763 15822 10854 1592 -35 -426 C ATOM 670 O THR A 136 121.695 -5.105 152.400 1.00 99.29 O ANISOU 670 O THR A 136 11600 15377 10747 1483 -153 -305 O ATOM 671 CB THR A 136 121.075 -2.495 154.308 1.00110.89 C ANISOU 671 CB THR A 136 13077 16905 12152 2148 -193 -834 C ATOM 672 OG1 THR A 136 121.863 -2.081 153.195 1.00110.72 O ANISOU 672 OG1 THR A 136 13254 16518 12298 2077 -385 -735 O ATOM 673 CG2 THR A 136 121.949 -2.522 155.528 1.00111.68 C ANISOU 673 CG2 THR A 136 13334 17004 12097 2118 -133 -916 C ATOM 674 N MET A 137 121.806 -5.843 154.539 1.00 96.76 N ANISOU 674 N MET A 137 11236 15404 10126 1447 103 -373 N ATOM 675 CA MET A 137 122.689 -6.980 154.255 1.00 93.59 C ANISOU 675 CA MET A 137 10960 14895 9703 1175 107 -180 C ATOM 676 C MET A 137 121.964 -8.047 153.423 1.00 97.20 C ANISOU 676 C MET A 137 11269 15455 10210 976 156 -10 C ATOM 677 O MET A 137 122.545 -8.560 152.471 1.00 95.29 O ANISOU 677 O MET A 137 11123 15026 10058 821 73 114 O ATOM 678 CB MET A 137 123.235 -7.599 155.551 1.00 95.82 C ANISOU 678 CB MET A 137 11334 15295 9779 1107 216 -167 C ATOM 679 CG MET A 137 124.372 -6.814 156.166 1.00 98.63 C ANISOU 679 CG MET A 137 11893 15480 10101 1221 119 -298 C ATOM 680 SD MET A 137 126.023 -7.437 155.784 1.00 99.80 S ANISOU 680 SD MET A 137 12259 15364 10295 1034 1 -173 S ATOM 681 CE MET A 137 126.030 -8.945 156.724 1.00 96.77 C ANISOU 681 CE MET A 137 11895 15179 9694 875 136 -20 C ATOM 682 N THR A 138 120.698 -8.360 153.772 1.00 95.30 N ANISOU 682 N THR A 138 10781 15522 9907 979 290 -22 N ATOM 683 CA THR A 138 119.888 -9.376 153.098 1.00 95.32 C ANISOU 683 CA THR A 138 10611 15658 9949 769 341 119 C ATOM 684 C THR A 138 119.392 -8.914 151.721 1.00 98.55 C ANISOU 684 C THR A 138 10925 15974 10545 831 192 111 C ATOM 685 O THR A 138 119.521 -9.683 150.769 1.00 96.55 O ANISOU 685 O THR A 138 10700 15622 10362 633 133 245 O ATOM 686 CB THR A 138 118.746 -9.865 154.017 1.00106.87 C ANISOU 686 CB THR A 138 11825 17516 11266 715 549 109 C ATOM 687 OG1 THR A 138 119.312 -10.358 155.230 1.00104.95 O ANISOU 687 OG1 THR A 138 11720 17336 10819 645 670 144 O ATOM 688 CG2 THR A 138 117.887 -10.969 153.377 1.00105.85 C ANISOU 688 CG2 THR A 138 11516 17529 11175 440 604 261 C ATOM 689 N VAL A 139 118.818 -7.692 151.607 1.00 96.74 N ANISOU 689 N VAL A 139 10598 15772 10388 1114 117 -49 N ATOM 690 CA VAL A 139 118.297 -7.194 150.322 1.00 96.92 C ANISOU 690 CA VAL A 139 10544 15710 10571 1204 -49 -50 C ATOM 691 C VAL A 139 119.428 -7.086 149.273 1.00 99.18 C ANISOU 691 C VAL A 139 11106 15631 10946 1118 -213 52 C ATOM 692 O VAL A 139 119.273 -7.635 148.185 1.00 98.44 O ANISOU 692 O VAL A 139 10990 15497 10916 974 -287 163 O ATOM 693 CB VAL A 139 117.407 -5.908 150.405 1.00103.13 C ANISOU 693 CB VAL A 139 11176 16589 11419 1560 -119 -244 C ATOM 694 CG1 VAL A 139 118.143 -4.713 150.998 1.00102.99 C ANISOU 694 CG1 VAL A 139 11385 16344 11403 1798 -194 -387 C ATOM 695 CG2 VAL A 139 116.811 -5.547 149.050 1.00103.49 C ANISOU 695 CG2 VAL A 139 11131 16579 11613 1638 -304 -214 C ATOM 696 N PHE A 140 120.572 -6.470 149.620 1.00 94.80 N ANISOU 696 N PHE A 140 10799 14841 10381 1177 -259 12 N ATOM 697 CA PHE A 140 121.688 -6.319 148.684 1.00 92.41 C ANISOU 697 CA PHE A 140 10732 14231 10146 1079 -389 100 C ATOM 698 C PHE A 140 122.464 -7.632 148.439 1.00 94.40 C ANISOU 698 C PHE A 140 11065 14451 10352 800 -329 241 C ATOM 699 O PHE A 140 123.112 -7.759 147.398 1.00 92.41 O ANISOU 699 O PHE A 140 10936 14024 10152 692 -418 323 O ATOM 700 CB PHE A 140 122.610 -5.161 149.104 1.00 93.77 C ANISOU 700 CB PHE A 140 11115 14174 10339 1218 -468 -1 C ATOM 701 CG PHE A 140 121.958 -3.821 148.851 1.00 96.88 C ANISOU 701 CG PHE A 140 11505 14481 10823 1487 -600 -114 C ATOM 702 CD1 PHE A 140 121.973 -3.249 147.585 1.00 99.75 C ANISOU 702 CD1 PHE A 140 11972 14635 11292 1503 -771 -37 C ATOM 703 CD2 PHE A 140 121.267 -3.164 149.860 1.00100.86 C ANISOU 703 CD2 PHE A 140 11908 15119 11296 1737 -558 -298 C ATOM 704 CE1 PHE A 140 121.346 -2.023 147.344 1.00102.69 C ANISOU 704 CE1 PHE A 140 12373 14893 11751 1771 -922 -129 C ATOM 705 CE2 PHE A 140 120.626 -1.945 149.613 1.00105.85 C ANISOU 705 CE2 PHE A 140 12544 15650 12023 2024 -702 -420 C ATOM 706 CZ PHE A 140 120.669 -1.384 148.356 1.00103.76 C ANISOU 706 CZ PHE A 140 12405 15141 11877 2043 -894 -326 C ATOM 707 N GLY A 141 122.353 -8.590 149.368 1.00 90.89 N ANISOU 707 N GLY A 141 10556 14176 9801 695 -184 266 N ATOM 708 CA GLY A 141 122.978 -9.907 149.272 1.00 89.05 C ANISOU 708 CA GLY A 141 10407 13905 9522 461 -137 391 C ATOM 709 C GLY A 141 122.280 -10.801 148.266 1.00 93.41 C ANISOU 709 C GLY A 141 10855 14511 10124 293 -154 492 C ATOM 710 O GLY A 141 122.938 -11.402 147.418 1.00 91.63 O ANISOU 710 O GLY A 141 10748 14137 9931 159 -214 565 O ATOM 711 N LEU A 142 120.934 -10.889 148.351 1.00 92.55 N ANISOU 711 N LEU A 142 10510 14634 10019 303 -104 477 N ATOM 712 CA LEU A 142 120.102 -11.685 147.444 1.00 93.28 C ANISOU 712 CA LEU A 142 10466 14813 10162 136 -132 551 C ATOM 713 C LEU A 142 120.024 -11.043 146.060 1.00 97.75 C ANISOU 713 C LEU A 142 11046 15264 10830 213 -305 540 C ATOM 714 O LEU A 142 120.027 -11.770 145.066 1.00 96.65 O ANISOU 714 O LEU A 142 10933 15070 10720 51 -372 611 O ATOM 715 CB LEU A 142 118.679 -11.909 148.002 1.00 95.89 C ANISOU 715 CB LEU A 142 10499 15470 10463 109 -21 527 C ATOM 716 CG LEU A 142 118.522 -12.838 149.214 1.00101.62 C ANISOU 716 CG LEU A 142 11195 16355 11060 -62 166 589 C ATOM 717 CD1 LEU A 142 117.145 -12.686 149.832 1.00104.73 C ANISOU 717 CD1 LEU A 142 11266 17117 11409 -28 296 525 C ATOM 718 CD2 LEU A 142 118.759 -14.303 148.846 1.00103.58 C ANISOU 718 CD2 LEU A 142 11543 16507 11305 -375 168 738 C ATOM 719 N SER A 143 119.968 -9.687 145.990 1.00 95.36 N ANISOU 719 N SER A 143 10751 14910 10572 461 -388 453 N ATOM 720 CA SER A 143 119.909 -8.949 144.719 1.00 95.13 C ANISOU 720 CA SER A 143 10775 14751 10620 550 -568 465 C ATOM 721 C SER A 143 121.108 -9.286 143.833 1.00 97.62 C ANISOU 721 C SER A 143 11331 14834 10925 401 -628 552 C ATOM 722 O SER A 143 120.906 -9.611 142.664 1.00 97.71 O ANISOU 722 O SER A 143 11346 14829 10951 310 -723 610 O ATOM 723 CB SER A 143 119.809 -7.444 144.948 1.00 98.46 C ANISOU 723 CB SER A 143 11231 15093 11086 838 -653 367 C ATOM 724 OG SER A 143 118.590 -7.110 145.588 1.00106.38 O ANISOU 724 OG SER A 143 11977 16341 12102 1015 -614 259 O ATOM 725 N SER A 144 122.336 -9.304 144.410 1.00 92.12 N ANISOU 725 N SER A 144 10814 13995 10193 368 -568 548 N ATOM 726 CA SER A 144 123.567 -9.662 143.690 1.00 89.61 C ANISOU 726 CA SER A 144 10690 13500 9859 234 -598 606 C ATOM 727 C SER A 144 123.458 -11.064 143.082 1.00 90.27 C ANISOU 727 C SER A 144 10750 13630 9919 33 -579 667 C ATOM 728 O SER A 144 123.739 -11.224 141.897 1.00 89.93 O ANISOU 728 O SER A 144 10784 13515 9872 -41 -658 704 O ATOM 729 CB SER A 144 124.782 -9.590 144.610 1.00 92.98 C ANISOU 729 CB SER A 144 11247 13830 10253 237 -529 570 C ATOM 730 OG SER A 144 124.832 -8.357 145.308 1.00106.86 O ANISOU 730 OG SER A 144 13034 15537 12032 412 -551 490 O ATOM 731 N LEU A 145 122.983 -12.050 143.869 1.00 85.16 N ANISOU 731 N LEU A 145 10006 13104 9246 -59 -481 678 N ATOM 732 CA LEU A 145 122.820 -13.436 143.424 1.00 84.68 C ANISOU 732 CA LEU A 145 9944 13057 9175 -262 -473 730 C ATOM 733 C LEU A 145 121.754 -13.602 142.352 1.00 91.79 C ANISOU 733 C LEU A 145 10714 14053 10110 -324 -566 742 C ATOM 734 O LEU A 145 121.978 -14.376 141.422 1.00 92.04 O ANISOU 734 O LEU A 145 10821 14016 10134 -457 -626 761 O ATOM 735 CB LEU A 145 122.575 -14.404 144.599 1.00 84.89 C ANISOU 735 CB LEU A 145 9932 13165 9160 -368 -351 764 C ATOM 736 CG LEU A 145 123.728 -14.595 145.599 1.00 87.83 C ANISOU 736 CG LEU A 145 10463 13434 9474 -337 -284 766 C ATOM 737 CD1 LEU A 145 123.237 -15.220 146.871 1.00 89.33 C ANISOU 737 CD1 LEU A 145 10600 13748 9593 -407 -165 813 C ATOM 738 CD2 LEU A 145 124.852 -15.433 145.016 1.00 87.66 C ANISOU 738 CD2 LEU A 145 10624 13230 9453 -420 -332 782 C ATOM 739 N PHE A 146 120.618 -12.870 142.452 1.00 90.55 N ANISOU 739 N PHE A 146 10357 14061 9987 -213 -591 713 N ATOM 740 CA PHE A 146 119.534 -12.960 141.461 1.00 92.39 C ANISOU 740 CA PHE A 146 10431 14418 10256 -249 -705 713 C ATOM 741 C PHE A 146 119.857 -12.218 140.155 1.00 95.53 C ANISOU 741 C PHE A 146 10949 14699 10650 -160 -867 723 C ATOM 742 O PHE A 146 119.434 -12.682 139.097 1.00 95.73 O ANISOU 742 O PHE A 146 10945 14762 10666 -258 -974 738 O ATOM 743 CB PHE A 146 118.165 -12.554 142.037 1.00 96.84 C ANISOU 743 CB PHE A 146 10700 15237 10857 -152 -679 665 C ATOM 744 CG PHE A 146 117.564 -13.626 142.921 1.00100.42 C ANISOU 744 CG PHE A 146 10996 15867 11294 -349 -533 684 C ATOM 745 CD1 PHE A 146 116.990 -14.768 142.370 1.00105.32 C ANISOU 745 CD1 PHE A 146 11532 16555 11931 -601 -564 721 C ATOM 746 CD2 PHE A 146 117.582 -13.502 144.306 1.00103.61 C ANISOU 746 CD2 PHE A 146 11352 16364 11650 -301 -368 668 C ATOM 747 CE1 PHE A 146 116.457 -15.768 143.189 1.00107.77 C ANISOU 747 CE1 PHE A 146 11722 17004 12223 -827 -429 763 C ATOM 748 CE2 PHE A 146 117.050 -14.503 145.124 1.00108.05 C ANISOU 748 CE2 PHE A 146 11793 17092 12170 -514 -224 716 C ATOM 749 CZ PHE A 146 116.487 -15.627 144.560 1.00107.32 C ANISOU 749 CZ PHE A 146 11624 17046 12106 -787 -254 772 C ATOM 750 N ILE A 147 120.640 -11.111 140.212 1.00 90.62 N ANISOU 750 N ILE A 147 10480 13931 10023 -1 -889 722 N ATOM 751 CA ILE A 147 121.088 -10.389 139.008 1.00 89.77 C ANISOU 751 CA ILE A 147 10531 13691 9886 49 -1027 764 C ATOM 752 C ILE A 147 122.097 -11.311 138.283 1.00 92.16 C ANISOU 752 C ILE A 147 10998 13900 10119 -144 -1003 793 C ATOM 753 O ILE A 147 122.016 -11.458 137.061 1.00 92.24 O ANISOU 753 O ILE A 147 11062 13911 10074 -203 -1109 821 O ATOM 754 CB ILE A 147 121.663 -8.968 139.322 1.00 92.47 C ANISOU 754 CB ILE A 147 11007 13879 10247 231 -1053 763 C ATOM 755 CG1 ILE A 147 120.560 -8.026 139.861 1.00 94.44 C ANISOU 755 CG1 ILE A 147 11101 14216 10567 468 -1115 706 C ATOM 756 CG2 ILE A 147 122.339 -8.341 138.085 1.00 92.96 C ANISOU 756 CG2 ILE A 147 11285 13782 10254 208 -1166 841 C ATOM 757 CD1 ILE A 147 121.059 -6.903 140.770 1.00 98.59 C ANISOU 757 CD1 ILE A 147 11726 14606 11128 642 -1088 651 C ATOM 758 N ALA A 148 122.991 -11.988 139.051 1.00 87.49 N ANISOU 758 N ALA A 148 10475 13247 9519 -226 -871 773 N ATOM 759 CA ALA A 148 123.959 -12.943 138.497 1.00 86.50 C ANISOU 759 CA ALA A 148 10485 13042 9339 -370 -843 767 C ATOM 760 C ALA A 148 123.229 -14.091 137.770 1.00 92.16 C ANISOU 760 C ALA A 148 11141 13833 10042 -515 -898 755 C ATOM 761 O ALA A 148 123.711 -14.565 136.741 1.00 91.18 O ANISOU 761 O ALA A 148 11123 13669 9852 -594 -947 738 O ATOM 762 CB ALA A 148 124.836 -13.500 139.597 1.00 85.99 C ANISOU 762 CB ALA A 148 10476 12914 9284 -391 -720 741 C ATOM 763 N SER A 149 122.057 -14.506 138.304 1.00 90.01 N ANISOU 763 N SER A 149 10690 13686 9826 -557 -890 755 N ATOM 764 CA SER A 149 121.208 -15.551 137.743 1.00 90.97 C ANISOU 764 CA SER A 149 10724 13885 9953 -723 -953 740 C ATOM 765 C SER A 149 120.447 -15.067 136.522 1.00 96.82 C ANISOU 765 C SER A 149 11400 14720 10669 -691 -1117 737 C ATOM 766 O SER A 149 120.321 -15.832 135.564 1.00 97.72 O ANISOU 766 O SER A 149 11556 14833 10739 -820 -1204 707 O ATOM 767 CB SER A 149 120.245 -16.090 138.791 1.00 94.44 C ANISOU 767 CB SER A 149 10972 14455 10455 -806 -877 752 C ATOM 768 OG SER A 149 120.882 -17.096 139.556 1.00100.17 O ANISOU 768 OG SER A 149 11809 15073 11177 -915 -767 770 O ATOM 769 N ALA A 150 119.947 -13.806 136.542 1.00 93.51 N ANISOU 769 N ALA A 150 10893 14368 10268 -506 -1177 760 N ATOM 770 CA ALA A 150 119.217 -13.209 135.413 1.00 94.62 C ANISOU 770 CA ALA A 150 10985 14589 10378 -431 -1362 772 C ATOM 771 C ALA A 150 120.110 -13.147 134.171 1.00 98.07 C ANISOU 771 C ALA A 150 11661 14911 10690 -468 -1435 799 C ATOM 772 O ALA A 150 119.666 -13.509 133.078 1.00 98.58 O ANISOU 772 O ALA A 150 11726 15045 10685 -534 -1573 788 O ATOM 773 CB ALA A 150 118.713 -11.820 135.776 1.00 96.03 C ANISOU 773 CB ALA A 150 11076 14805 10606 -187 -1416 791 C ATOM 774 N MET A 151 121.386 -12.747 134.362 1.00 93.34 N ANISOU 774 N MET A 151 11254 14160 10052 -440 -1337 825 N ATOM 775 CA MET A 151 122.395 -12.686 133.305 1.00 93.06 C ANISOU 775 CA MET A 151 11431 14043 9883 -493 -1355 847 C ATOM 776 C MET A 151 122.657 -14.086 132.765 1.00 94.60 C ANISOU 776 C MET A 151 11670 14255 10017 -661 -1336 766 C ATOM 777 O MET A 151 122.647 -14.266 131.549 1.00 95.86 O ANISOU 777 O MET A 151 11920 14454 10049 -715 -1429 756 O ATOM 778 CB MET A 151 123.702 -12.062 133.817 1.00 94.60 C ANISOU 778 CB MET A 151 11766 14104 10074 -453 -1231 873 C ATOM 779 CG MET A 151 123.669 -10.561 133.872 1.00100.11 C ANISOU 779 CG MET A 151 12522 14732 10784 -312 -1293 958 C ATOM 780 SD MET A 151 125.254 -9.848 134.382 1.00104.81 S ANISOU 780 SD MET A 151 13283 15170 11370 -324 -1163 981 S ATOM 781 CE MET A 151 126.191 -10.027 132.856 1.00101.96 C ANISOU 781 CE MET A 151 13095 14829 10817 -479 -1161 1018 C ATOM 782 N ALA A 152 122.849 -15.083 133.663 1.00 88.19 N ANISOU 782 N ALA A 152 10812 13407 9288 -739 -1229 708 N ATOM 783 CA ALA A 152 123.082 -16.482 133.296 1.00 87.51 C ANISOU 783 CA ALA A 152 10790 13288 9174 -884 -1224 619 C ATOM 784 C ALA A 152 121.960 -17.011 132.384 1.00 91.71 C ANISOU 784 C ALA A 152 11245 13924 9677 -986 -1382 580 C ATOM 785 O ALA A 152 122.264 -17.590 131.342 1.00 90.75 O ANISOU 785 O ALA A 152 11239 13795 9446 -1058 -1444 507 O ATOM 786 CB ALA A 152 123.202 -17.346 134.542 1.00 87.42 C ANISOU 786 CB ALA A 152 10747 13199 9269 -939 -1114 599 C ATOM 787 N VAL A 153 120.679 -16.760 132.762 1.00 89.19 N ANISOU 787 N VAL A 153 10717 13726 9447 -982 -1448 615 N ATOM 788 CA VAL A 153 119.466 -17.162 132.032 1.00 91.26 C ANISOU 788 CA VAL A 153 10843 14127 9706 -1079 -1613 577 C ATOM 789 C VAL A 153 119.391 -16.462 130.673 1.00 96.20 C ANISOU 789 C VAL A 153 11547 14818 10184 -1002 -1776 590 C ATOM 790 O VAL A 153 119.090 -17.122 129.679 1.00 97.00 O ANISOU 790 O VAL A 153 11690 14967 10199 -1113 -1900 516 O ATOM 791 CB VAL A 153 118.173 -16.948 132.879 1.00 96.07 C ANISOU 791 CB VAL A 153 11162 14893 10448 -1071 -1622 605 C ATOM 792 CG1 VAL A 153 116.902 -17.125 132.044 1.00 98.27 C ANISOU 792 CG1 VAL A 153 11257 15358 10722 -1137 -1821 563 C ATOM 793 CG2 VAL A 153 118.147 -17.870 134.092 1.00 95.41 C ANISOU 793 CG2 VAL A 153 11018 14765 10467 -1217 -1471 600 C ATOM 794 N GLU A 154 119.681 -15.143 130.630 1.00 92.59 N ANISOU 794 N GLU A 154 11138 14351 9690 -822 -1784 685 N ATOM 795 CA GLU A 154 119.642 -14.362 129.394 1.00 93.82 C ANISOU 795 CA GLU A 154 11407 14551 9690 -743 -1940 741 C ATOM 796 C GLU A 154 120.661 -14.835 128.346 1.00 96.97 C ANISOU 796 C GLU A 154 12044 14903 9898 -838 -1918 702 C ATOM 797 O GLU A 154 120.277 -15.024 127.185 1.00 98.22 O ANISOU 797 O GLU A 154 12257 15156 9907 -879 -2074 679 O ATOM 798 CB GLU A 154 119.763 -12.862 129.668 1.00 95.20 C ANISOU 798 CB GLU A 154 11619 14671 9881 -545 -1951 863 C ATOM 799 CG GLU A 154 118.865 -12.050 128.750 1.00112.44 C ANISOU 799 CG GLU A 154 13785 16948 11990 -422 -2191 932 C ATOM 800 CD GLU A 154 118.516 -10.656 129.234 1.00145.27 C ANISOU 800 CD GLU A 154 17921 21047 16230 -192 -2249 1027 C ATOM 801 OE1 GLU A 154 118.778 -9.690 128.481 1.00145.08 O ANISOU 801 OE1 GLU A 154 18098 20939 16086 -103 -2357 1144 O ATOM 802 OE2 GLU A 154 117.960 -10.531 130.351 1.00142.73 O ANISOU 802 OE2 GLU A 154 17390 20760 16080 -99 -2191 983 O ATOM 803 N ARG A 155 121.936 -15.058 128.759 1.00 90.92 N ANISOU 803 N ARG A 155 11402 14017 9127 -866 -1728 679 N ATOM 804 CA ARG A 155 123.012 -15.559 127.891 1.00 90.50 C ANISOU 804 CA ARG A 155 11540 13947 8901 -939 -1667 610 C ATOM 805 C ARG A 155 122.633 -16.924 127.317 1.00 95.08 C ANISOU 805 C ARG A 155 12120 14565 9442 -1066 -1742 454 C ATOM 806 O ARG A 155 122.777 -17.131 126.111 1.00 97.13 O ANISOU 806 O ARG A 155 12502 14899 9504 -1108 -1815 395 O ATOM 807 CB ARG A 155 124.346 -15.677 128.644 1.00 90.04 C ANISOU 807 CB ARG A 155 11547 13775 8889 -928 -1457 586 C ATOM 808 CG ARG A 155 125.126 -14.381 128.798 1.00104.97 C ANISOU 808 CG ARG A 155 13518 15629 10736 -854 -1379 710 C ATOM 809 CD ARG A 155 126.595 -14.673 129.060 1.00115.28 C ANISOU 809 CD ARG A 155 14898 16887 12016 -879 -1195 644 C ATOM 810 NE ARG A 155 127.355 -13.467 129.393 1.00125.43 N ANISOU 810 NE ARG A 155 16232 18124 13302 -843 -1113 756 N ATOM 811 CZ ARG A 155 127.774 -13.157 130.618 1.00143.42 C ANISOU 811 CZ ARG A 155 18453 20308 15732 -790 -1018 768 C ATOM 812 NH1 ARG A 155 127.518 -13.963 131.642 1.00126.46 N ANISOU 812 NH1 ARG A 155 16204 18113 13732 -762 -983 691 N ATOM 813 NH2 ARG A 155 128.460 -12.040 130.825 1.00136.32 N ANISOU 813 NH2 ARG A 155 17611 19356 14828 -780 -965 859 N ATOM 814 N ALA A 156 122.102 -17.829 128.168 1.00 90.30 N ANISOU 814 N ALA A 156 11389 13908 9012 -1140 -1732 391 N ATOM 815 CA ALA A 156 121.673 -19.168 127.770 1.00 91.71 C ANISOU 815 CA ALA A 156 11576 14076 9193 -1288 -1818 244 C ATOM 816 C ALA A 156 120.568 -19.123 126.703 1.00100.01 C ANISOU 816 C ALA A 156 12567 15284 10148 -1341 -2043 219 C ATOM 817 O ALA A 156 120.655 -19.869 125.728 1.00101.27 O ANISOU 817 O ALA A 156 12839 15461 10177 -1426 -2133 85 O ATOM 818 CB ALA A 156 121.219 -19.963 128.980 1.00 91.76 C ANISOU 818 CB ALA A 156 11465 13989 9410 -1381 -1762 232 C ATOM 819 N LEU A 157 119.576 -18.211 126.855 1.00 98.51 N ANISOU 819 N LEU A 157 12204 15215 10012 -1268 -2146 333 N ATOM 820 CA LEU A 157 118.469 -18.031 125.903 1.00101.57 C ANISOU 820 CA LEU A 157 12500 15774 10316 -1284 -2388 320 C ATOM 821 C LEU A 157 118.959 -17.512 124.545 1.00107.17 C ANISOU 821 C LEU A 157 13420 16547 10752 -1222 -2483 339 C ATOM 822 O LEU A 157 118.470 -17.956 123.502 1.00109.55 O ANISOU 822 O LEU A 157 13750 16959 10914 -1294 -2668 251 O ATOM 823 CB LEU A 157 117.410 -17.060 126.459 1.00102.45 C ANISOU 823 CB LEU A 157 12368 16000 10557 -1162 -2470 432 C ATOM 824 CG LEU A 157 116.496 -17.533 127.591 1.00107.84 C ANISOU 824 CG LEU A 157 12772 16730 11471 -1248 -2426 406 C ATOM 825 CD1 LEU A 157 115.576 -16.407 128.028 1.00108.83 C ANISOU 825 CD1 LEU A 157 12669 16988 11696 -1063 -2482 499 C ATOM 826 CD2 LEU A 157 115.652 -18.736 127.176 1.00112.81 C ANISOU 826 CD2 LEU A 157 13280 17455 12128 -1470 -2574 276 C ATOM 827 N ALA A 158 119.917 -16.569 124.570 1.00102.17 N ANISOU 827 N ALA A 158 12935 15854 10033 -1106 -2360 457 N ATOM 828 CA ALA A 158 120.510 -15.941 123.393 1.00103.00 C ANISOU 828 CA ALA A 158 13256 16019 9861 -1066 -2406 519 C ATOM 829 C ALA A 158 121.229 -16.925 122.466 1.00108.10 C ANISOU 829 C ALA A 158 14074 16698 10302 -1178 -2367 354 C ATOM 830 O ALA A 158 121.199 -16.741 121.243 1.00111.12 O ANISOU 830 O ALA A 158 14594 17206 10419 -1187 -2485 356 O ATOM 831 CB ALA A 158 121.469 -14.843 123.824 1.00102.22 C ANISOU 831 CB ALA A 158 13262 15824 9753 -970 -2248 678 C ATOM 832 N ILE A 159 121.846 -17.972 123.039 1.00102.30 N ANISOU 832 N ILE A 159 13341 15852 9677 -1247 -2215 206 N ATOM 833 CA ILE A 159 122.631 -18.957 122.295 1.00102.95 C ANISOU 833 CA ILE A 159 13582 15941 9592 -1313 -2162 12 C ATOM 834 C ILE A 159 121.831 -20.256 121.999 1.00107.96 C ANISOU 834 C ILE A 159 14182 16563 10273 -1436 -2322 -187 C ATOM 835 O ILE A 159 121.954 -20.798 120.894 1.00109.05 O ANISOU 835 O ILE A 159 14455 16786 10194 -1479 -2410 -340 O ATOM 836 CB ILE A 159 123.990 -19.193 123.034 1.00104.45 C ANISOU 836 CB ILE A 159 13828 16007 9851 -1273 -1904 -30 C ATOM 837 CG1 ILE A 159 124.839 -17.897 123.003 1.00104.31 C ANISOU 837 CG1 ILE A 159 13870 16036 9728 -1198 -1770 147 C ATOM 838 CG2 ILE A 159 124.802 -20.339 122.425 1.00106.24 C ANISOU 838 CG2 ILE A 159 14192 16229 9946 -1302 -1847 -273 C ATOM 839 CD1 ILE A 159 125.577 -17.561 124.256 1.00106.92 C ANISOU 839 CD1 ILE A 159 14138 16237 10251 -1143 -1579 210 C ATOM 840 N ARG A 160 121.006 -20.734 122.951 1.00104.33 N ANISOU 840 N ARG A 160 13550 16009 10080 -1507 -2361 -187 N ATOM 841 CA ARG A 160 120.232 -21.972 122.766 1.00106.09 C ANISOU 841 CA ARG A 160 13739 16195 10376 -1670 -2513 -362 C ATOM 842 C ARG A 160 118.995 -21.789 121.887 1.00112.03 C ANISOU 842 C ARG A 160 14395 17138 11033 -1730 -2781 -372 C ATOM 843 O ARG A 160 118.589 -22.741 121.215 1.00114.29 O ANISOU 843 O ARG A 160 14732 17435 11257 -1861 -2937 -558 O ATOM 844 CB ARG A 160 119.877 -22.637 124.107 1.00106.67 C ANISOU 844 CB ARG A 160 13678 16103 10749 -1769 -2442 -348 C ATOM 845 CG ARG A 160 121.106 -23.080 124.914 1.00116.41 C ANISOU 845 CG ARG A 160 15039 17129 12062 -1716 -2225 -379 C ATOM 846 CD ARG A 160 120.762 -24.091 125.988 1.00128.88 C ANISOU 846 CD ARG A 160 16567 18519 13882 -1856 -2201 -401 C ATOM 847 NE ARG A 160 120.692 -25.451 125.450 1.00142.72 N ANISOU 847 NE ARG A 160 18467 20134 15627 -1999 -2321 -611 N ATOM 848 CZ ARG A 160 121.698 -26.322 125.466 1.00158.53 C ANISOU 848 CZ ARG A 160 20681 21933 17619 -1954 -2255 -758 C ATOM 849 NH1 ARG A 160 121.541 -27.535 124.953 1.00154.84 N ANISOU 849 NH1 ARG A 160 20362 21317 17151 -2077 -2392 -963 N ATOM 850 NH2 ARG A 160 122.868 -25.987 125.997 1.00136.77 N ANISOU 850 NH2 ARG A 160 17990 19119 14859 -1777 -2066 -714 N ATOM 851 N ALA A 161 118.405 -20.574 121.881 1.00108.02 N ANISOU 851 N ALA A 161 13756 16772 10513 -1623 -2855 -187 N ATOM 852 CA ALA A 161 117.248 -20.214 121.047 1.00109.98 C ANISOU 852 CA ALA A 161 13899 17225 10664 -1627 -3132 -174 C ATOM 853 C ALA A 161 117.498 -18.820 120.392 1.00113.72 C ANISOU 853 C ALA A 161 14476 17809 10923 -1440 -3173 10 C ATOM 854 O ALA A 161 116.832 -17.844 120.756 1.00113.32 O ANISOU 854 O ALA A 161 14273 17815 10967 -1318 -3245 171 O ATOM 855 CB ALA A 161 115.979 -20.211 121.887 1.00111.05 C ANISOU 855 CB ALA A 161 13711 17420 11064 -1684 -3224 -133 C ATOM 856 N PRO A 162 118.474 -18.706 119.446 1.00110.64 N ANISOU 856 N PRO A 162 14354 17445 10238 -1415 -3123 -10 N ATOM 857 CA PRO A 162 118.796 -17.388 118.859 1.00111.22 C ANISOU 857 CA PRO A 162 14565 17596 10097 -1277 -3143 197 C ATOM 858 C PRO A 162 117.702 -16.694 118.049 1.00119.24 C ANISOU 858 C PRO A 162 15541 18783 10982 -1201 -3455 295 C ATOM 859 O PRO A 162 117.712 -15.464 117.973 1.00118.88 O ANISOU 859 O PRO A 162 15554 18739 10877 -1060 -3494 514 O ATOM 860 CB PRO A 162 120.017 -17.675 117.978 1.00113.32 C ANISOU 860 CB PRO A 162 15102 17895 10059 -1319 -3008 116 C ATOM 861 CG PRO A 162 120.551 -18.967 118.445 1.00116.53 C ANISOU 861 CG PRO A 162 15500 18186 10591 -1416 -2862 -116 C ATOM 862 CD PRO A 162 119.373 -19.747 118.908 1.00112.49 C ANISOU 862 CD PRO A 162 14781 17639 10319 -1507 -3029 -220 C ATOM 863 N HIS A 163 116.793 -17.459 117.419 1.00119.45 N ANISOU 863 N HIS A 163 15484 18944 10958 -1291 -3694 134 N ATOM 864 CA HIS A 163 115.718 -16.876 116.625 1.00123.12 C ANISOU 864 CA HIS A 163 15889 19596 11295 -1210 -4026 203 C ATOM 865 C HIS A 163 114.667 -16.203 117.507 1.00127.65 C ANISOU 865 C HIS A 163 16158 20184 12159 -1085 -4132 318 C ATOM 866 O HIS A 163 114.330 -15.043 117.265 1.00128.10 O ANISOU 866 O HIS A 163 16238 20291 12144 -896 -4282 504 O ATOM 867 CB HIS A 163 115.099 -17.916 115.685 1.00127.16 C ANISOU 867 CB HIS A 163 16390 20259 11664 -1355 -4259 -29 C ATOM 868 CG HIS A 163 114.023 -17.372 114.808 1.00134.14 C ANISOU 868 CG HIS A 163 17215 21361 12391 -1267 -4627 26 C ATOM 869 ND1 HIS A 163 114.311 -16.513 113.767 1.00138.03 N ANISOU 869 ND1 HIS A 163 17972 21954 12521 -1153 -4746 174 N ATOM 870 CD2 HIS A 163 112.689 -17.585 114.846 1.00138.22 C ANISOU 870 CD2 HIS A 163 17433 22021 13064 -1282 -4899 -45 C ATOM 871 CE1 HIS A 163 113.149 -16.240 113.195 1.00140.69 C ANISOU 871 CE1 HIS A 163 18180 22476 12800 -1078 -5107 188 C ATOM 872 NE2 HIS A 163 112.144 -16.862 113.811 1.00141.29 N ANISOU 872 NE2 HIS A 163 17897 22596 13189 -1148 -5211 47 N ATOM 873 N TRP A 164 114.176 -16.918 118.536 1.00124.47 N ANISOU 873 N TRP A 164 15482 19738 12075 -1185 -4050 207 N ATOM 874 CA TRP A 164 113.192 -16.410 119.496 1.00125.22 C ANISOU 874 CA TRP A 164 15242 19882 12455 -1082 -4102 277 C ATOM 875 C TRP A 164 113.744 -15.211 120.302 1.00127.70 C ANISOU 875 C TRP A 164 15608 20054 12856 -874 -3929 482 C ATOM 876 O TRP A 164 112.976 -14.303 120.636 1.00128.82 O ANISOU 876 O TRP A 164 15576 20263 13106 -679 -4060 583 O ATOM 877 CB TRP A 164 112.721 -17.542 120.435 1.00123.71 C ANISOU 877 CB TRP A 164 14788 19671 12544 -1290 -3997 122 C ATOM 878 CG TRP A 164 111.761 -17.100 121.503 1.00124.96 C ANISOU 878 CG TRP A 164 14577 19921 12983 -1208 -4000 173 C ATOM 879 CD1 TRP A 164 110.400 -17.120 121.440 1.00130.82 C ANISOU 879 CD1 TRP A 164 14976 20902 13827 -1211 -4235 112 C ATOM 880 CD2 TRP A 164 112.097 -16.539 122.781 1.00122.19 C ANISOU 880 CD2 TRP A 164 14146 19451 12828 -1101 -3753 279 C ATOM 881 NE1 TRP A 164 109.865 -16.607 122.599 1.00129.79 N ANISOU 881 NE1 TRP A 164 14547 20826 13943 -1104 -4133 169 N ATOM 882 CE2 TRP A 164 110.885 -16.234 123.436 1.00127.77 C ANISOU 882 CE2 TRP A 164 14461 20346 13741 -1032 -3840 272 C ATOM 883 CE3 TRP A 164 113.309 -16.243 123.428 1.00120.22 C ANISOU 883 CE3 TRP A 164 14107 18977 12594 -1051 -3472 367 C ATOM 884 CZ2 TRP A 164 110.847 -15.667 124.715 1.00125.54 C ANISOU 884 CZ2 TRP A 164 14011 20030 13660 -912 -3646 342 C ATOM 885 CZ3 TRP A 164 113.271 -15.671 124.690 1.00120.05 C ANISOU 885 CZ3 TRP A 164 13929 18905 12777 -939 -3302 443 C ATOM 886 CH2 TRP A 164 112.053 -15.390 125.321 1.00122.30 C ANISOU 886 CH2 TRP A 164 13844 19376 13248 -867 -3384 428 C ATOM 887 N TYR A 165 115.054 -15.227 120.638 1.00121.01 N ANISOU 887 N TYR A 165 14988 19017 11975 -910 -3647 524 N ATOM 888 CA TYR A 165 115.701 -14.158 121.401 1.00118.63 C ANISOU 888 CA TYR A 165 14762 18559 11752 -753 -3473 698 C ATOM 889 C TYR A 165 115.709 -12.820 120.651 1.00124.92 C ANISOU 889 C TYR A 165 15747 19360 12358 -563 -3640 897 C ATOM 890 O TYR A 165 115.393 -11.792 121.249 1.00124.37 O ANISOU 890 O TYR A 165 15606 19225 12423 -369 -3674 1023 O ATOM 891 CB TYR A 165 117.126 -14.561 121.837 1.00116.63 C ANISOU 891 CB TYR A 165 14696 18132 11484 -858 -3158 675 C ATOM 892 CG TYR A 165 117.767 -13.589 122.808 1.00115.79 C ANISOU 892 CG TYR A 165 14626 17863 11506 -734 -2969 819 C ATOM 893 CD1 TYR A 165 117.542 -13.689 124.177 1.00115.96 C ANISOU 893 CD1 TYR A 165 14433 17819 11807 -707 -2836 793 C ATOM 894 CD2 TYR A 165 118.607 -12.575 122.357 1.00116.34 C ANISOU 894 CD2 TYR A 165 14952 17848 11402 -665 -2922 979 C ATOM 895 CE1 TYR A 165 118.117 -12.789 125.072 1.00115.36 C ANISOU 895 CE1 TYR A 165 14396 17597 11837 -590 -2680 903 C ATOM 896 CE2 TYR A 165 119.187 -11.668 123.243 1.00115.54 C ANISOU 896 CE2 TYR A 165 14890 17583 11425 -571 -2769 1098 C ATOM 897 CZ TYR A 165 118.943 -11.781 124.601 1.00122.43 C ANISOU 897 CZ TYR A 165 15547 18391 12578 -523 -2654 1047 C ATOM 898 OH TYR A 165 119.524 -10.894 125.476 1.00123.30 O ANISOU 898 OH TYR A 165 15704 18343 12800 -429 -2515 1142 O ATOM 899 N ALA A 166 116.080 -12.836 119.360 1.00124.44 N ANISOU 899 N ALA A 166 15942 19366 11973 -615 -3746 924 N ATOM 900 CA ALA A 166 116.164 -11.643 118.514 1.00127.14 C ANISOU 900 CA ALA A 166 16527 19703 12076 -476 -3911 1139 C ATOM 901 C ALA A 166 114.824 -10.921 118.313 1.00136.59 C ANISOU 901 C ALA A 166 17570 21002 13328 -261 -4258 1212 C ATOM 902 O ALA A 166 114.804 -9.689 118.287 1.00136.83 O ANISOU 902 O ALA A 166 17736 20926 13328 -68 -4359 1416 O ATOM 903 CB ALA A 166 116.784 -11.994 117.171 1.00129.38 C ANISOU 903 CB ALA A 166 17096 20088 11973 -608 -3940 1126 C ATOM 904 N SER A 167 113.712 -11.680 118.188 1.00137.40 N ANISOU 904 N SER A 167 17387 21301 13519 -292 -4447 1039 N ATOM 905 CA SER A 167 112.375 -11.114 117.973 1.00141.55 C ANISOU 905 CA SER A 167 17698 21979 14105 -84 -4794 1064 C ATOM 906 C SER A 167 111.638 -10.749 119.268 1.00148.29 C ANISOU 906 C SER A 167 18195 22823 15327 76 -4755 1037 C ATOM 907 O SER A 167 110.954 -9.724 119.295 1.00150.07 O ANISOU 907 O SER A 167 18349 23065 15608 354 -4971 1138 O ATOM 908 CB SER A 167 111.522 -12.024 117.089 1.00147.04 C ANISOU 908 CB SER A 167 18251 22931 14686 -204 -5049 889 C ATOM 909 OG SER A 167 111.449 -13.356 117.567 1.00152.43 O ANISOU 909 OG SER A 167 18723 23659 15536 -453 -4890 663 O ATOM 910 N HIS A 168 111.780 -11.564 120.331 1.00145.04 N ANISOU 910 N HIS A 168 17573 22386 15150 -84 -4486 899 N ATOM 911 CA HIS A 168 111.121 -11.325 121.618 1.00145.58 C ANISOU 911 CA HIS A 168 17294 22480 15541 33 -4402 855 C ATOM 912 C HIS A 168 112.106 -10.820 122.683 1.00149.60 C ANISOU 912 C HIS A 168 17935 22739 16166 79 -4089 943 C ATOM 913 O HIS A 168 112.806 -11.634 123.291 1.00147.13 O ANISOU 913 O HIS A 168 17640 22342 15921 -128 -3814 872 O ATOM 914 CB HIS A 168 110.401 -12.599 122.112 1.00146.59 C ANISOU 914 CB HIS A 168 17060 22791 15846 -196 -4349 648 C ATOM 915 CG HIS A 168 109.402 -13.162 121.150 1.00153.57 C ANISOU 915 CG HIS A 168 17777 23931 16642 -273 -4661 533 C ATOM 916 ND1 HIS A 168 109.759 -14.118 120.218 1.00155.92 N ANISOU 916 ND1 HIS A 168 18266 24243 16734 -510 -4716 445 N ATOM 917 CD2 HIS A 168 108.078 -12.907 121.028 1.00158.78 C ANISOU 917 CD2 HIS A 168 18082 24850 17397 -139 -4933 474 C ATOM 918 CE1 HIS A 168 108.652 -14.404 119.551 1.00158.94 C ANISOU 918 CE1 HIS A 168 18423 24880 17088 -528 -5027 341 C ATOM 919 NE2 HIS A 168 107.614 -13.700 120.003 1.00161.11 N ANISOU 919 NE2 HIS A 168 18352 25319 17545 -311 -5170 358 N ATOM 920 N MET A 169 112.166 -9.482 122.905 1.00148.80 N ANISOU 920 N MET A 169 17942 22506 16090 354 -4152 1094 N ATOM 921 CA MET A 169 113.033 -8.844 123.917 1.00147.12 C ANISOU 921 CA MET A 169 17856 22052 15993 422 -3899 1173 C ATOM 922 C MET A 169 112.538 -7.452 124.349 1.00152.90 C ANISOU 922 C MET A 169 18558 22696 16840 773 -4044 1264 C ATOM 923 O MET A 169 112.269 -7.245 125.534 1.00151.48 O ANISOU 923 O MET A 169 18155 22514 16888 886 -3917 1190 O ATOM 924 CB MET A 169 114.515 -8.799 123.482 1.00148.00 C ANISOU 924 CB MET A 169 18373 21955 15905 264 -3722 1286 C ATOM 925 CG MET A 169 115.384 -9.862 124.144 1.00149.25 C ANISOU 925 CG MET A 169 18515 22066 16128 17 -3397 1176 C ATOM 926 SD MET A 169 115.672 -9.626 125.927 1.00151.64 S ANISOU 926 SD MET A 169 18651 22242 16723 87 -3127 1139 S ATOM 927 CE MET A 169 114.657 -10.955 126.602 1.00148.36 C ANISOU 927 CE MET A 169 17838 22048 16483 -67 -3073 940 C ATOM 928 N LYS A 170 112.455 -6.498 123.387 1.00152.23 N ANISOU 928 N LYS A 170 18726 22529 16585 948 -4312 1425 N ATOM 929 CA LYS A 170 111.997 -5.101 123.534 1.00154.13 C ANISOU 929 CA LYS A 170 19028 22636 16900 1310 -4526 1533 C ATOM 930 C LYS A 170 112.848 -4.215 124.500 1.00154.00 C ANISOU 930 C LYS A 170 19200 22308 17005 1398 -4325 1610 C ATOM 931 O LYS A 170 112.636 -2.997 124.522 1.00155.62 O ANISOU 931 O LYS A 170 19548 22332 17250 1686 -4511 1715 O ATOM 932 CB LYS A 170 110.502 -5.042 123.917 1.00159.69 C ANISOU 932 CB LYS A 170 19282 23593 17800 1566 -4731 1381 C ATOM 933 CG LYS A 170 109.721 -3.934 123.212 1.00181.16 C ANISOU 933 CG LYS A 170 22076 26287 20468 1933 -5138 1485 C ATOM 934 CD LYS A 170 108.234 -3.944 123.585 1.00195.90 C ANISOU 934 CD LYS A 170 23436 28462 22536 2196 -5334 1300 C ATOM 935 CE LYS A 170 107.896 -3.094 124.792 1.00207.64 C ANISOU 935 CE LYS A 170 24747 29868 24279 2519 -5271 1222 C ATOM 936 NZ LYS A 170 107.837 -1.647 124.455 1.00219.36 N ANISOU 936 NZ LYS A 170 26539 31072 25737 2905 -5556 1376 N ATOM 937 N THR A 171 113.805 -4.811 125.272 1.00145.17 N ANISOU 937 N THR A 171 18097 21117 15944 1160 -3971 1554 N ATOM 938 CA THR A 171 114.711 -4.159 126.250 1.00142.26 C ANISOU 938 CA THR A 171 17882 20483 15686 1184 -3753 1595 C ATOM 939 C THR A 171 113.957 -3.638 127.492 1.00145.00 C ANISOU 939 C THR A 171 17953 20844 16298 1465 -3747 1469 C ATOM 940 O THR A 171 114.525 -3.634 128.586 1.00142.47 O ANISOU 940 O THR A 171 17609 20422 16100 1427 -3501 1407 O ATOM 941 CB THR A 171 115.613 -3.073 125.605 1.00152.16 C ANISOU 941 CB THR A 171 19601 21433 16779 1192 -3827 1826 C ATOM 942 OG1 THR A 171 116.042 -3.517 124.318 1.00156.10 O ANISOU 942 OG1 THR A 171 20313 21999 16997 975 -3877 1934 O ATOM 943 CG2 THR A 171 116.836 -2.725 126.455 1.00146.17 C ANISOU 943 CG2 THR A 171 19016 20430 16091 1078 -3554 1856 C ATOM 944 N ARG A 172 112.688 -3.218 127.326 1.00143.49 N ANISOU 944 N ARG A 172 17539 20800 16180 1755 -4017 1415 N ATOM 945 CA ARG A 172 111.806 -2.736 128.394 1.00143.92 C ANISOU 945 CA ARG A 172 17280 20936 16467 2061 -4035 1264 C ATOM 946 C ARG A 172 111.519 -3.857 129.401 1.00143.74 C ANISOU 946 C ARG A 172 16858 21183 16575 1890 -3760 1071 C ATOM 947 O ARG A 172 111.325 -3.578 130.586 1.00143.10 O ANISOU 947 O ARG A 172 16592 21122 16656 2038 -3620 953 O ATOM 948 CB ARG A 172 110.487 -2.222 127.797 1.00149.31 C ANISOU 948 CB ARG A 172 17780 21778 17174 2395 -4407 1238 C ATOM 949 CG ARG A 172 110.307 -0.713 127.891 1.00163.76 C ANISOU 949 CG ARG A 172 19805 23339 19078 2809 -4632 1301 C ATOM 950 CD ARG A 172 108.905 -0.292 127.481 1.00180.53 C ANISOU 950 CD ARG A 172 21663 25668 21263 3188 -4994 1226 C ATOM 951 NE ARG A 172 107.904 -0.637 128.495 1.00192.21 N ANISOU 951 NE ARG A 172 22590 27490 22952 3340 -4895 964 N ATOM 952 CZ ARG A 172 106.589 -0.565 128.311 1.00211.60 C ANISOU 952 CZ ARG A 172 24655 30253 25490 3623 -5144 831 C ATOM 953 NH1 ARG A 172 106.094 -0.169 127.145 1.00201.73 N ANISOU 953 NH1 ARG A 172 23518 28996 24133 3808 -5537 937 N ATOM 954 NH2 ARG A 172 105.759 -0.896 129.291 1.00201.28 N ANISOU 954 NH2 ARG A 172 22831 29284 24361 3719 -5003 592 N ATOM 955 N ALA A 173 111.501 -5.119 128.922 1.00137.76 N ANISOU 955 N ALA A 173 15988 20621 15732 1574 -3688 1040 N ATOM 956 CA ALA A 173 111.270 -6.317 129.725 1.00135.60 C ANISOU 956 CA ALA A 173 15390 20575 15557 1346 -3444 892 C ATOM 957 C ALA A 173 112.429 -6.581 130.686 1.00135.67 C ANISOU 957 C ALA A 173 15554 20398 15595 1176 -3112 900 C ATOM 958 O ALA A 173 112.183 -6.988 131.817 1.00134.57 O ANISOU 958 O ALA A 173 15167 20381 15583 1151 -2913 788 O ATOM 959 CB ALA A 173 111.058 -7.521 128.824 1.00136.41 C ANISOU 959 CB ALA A 173 15422 20858 15551 1052 -3498 870 C ATOM 960 N THR A 174 113.681 -6.340 130.247 1.00130.21 N ANISOU 960 N THR A 174 15262 19435 14775 1060 -3054 1031 N ATOM 961 CA THR A 174 114.879 -6.550 131.070 1.00127.05 C ANISOU 961 CA THR A 174 15024 18857 14392 907 -2768 1039 C ATOM 962 C THR A 174 114.991 -5.489 132.175 1.00130.93 C ANISOU 962 C THR A 174 15528 19204 15013 1150 -2704 1013 C ATOM 963 O THR A 174 115.413 -5.812 133.286 1.00128.03 O ANISOU 963 O THR A 174 15097 18827 14720 1078 -2468 942 O ATOM 964 CB THR A 174 116.146 -6.677 130.211 1.00133.81 C ANISOU 964 CB THR A 174 16249 19524 15070 704 -2726 1165 C ATOM 965 OG1 THR A 174 116.328 -5.489 129.445 1.00136.52 O ANISOU 965 OG1 THR A 174 16863 19687 15322 860 -2924 1311 O ATOM 966 CG2 THR A 174 116.107 -7.886 129.289 1.00131.81 C ANISOU 966 CG2 THR A 174 15975 19421 14687 456 -2746 1140 C ATOM 967 N ARG A 175 114.568 -4.242 131.879 1.00130.51 N ANISOU 967 N ARG A 175 15568 19037 14983 1449 -2933 1062 N ATOM 968 CA ARG A 175 114.552 -3.121 132.825 1.00131.03 C ANISOU 968 CA ARG A 175 15668 18943 15175 1728 -2930 1014 C ATOM 969 C ARG A 175 113.484 -3.367 133.905 1.00135.09 C ANISOU 969 C ARG A 175 15751 19739 15839 1891 -2850 817 C ATOM 970 O ARG A 175 113.709 -3.037 135.070 1.00133.99 O ANISOU 970 O ARG A 175 15575 19548 15786 1988 -2691 723 O ATOM 971 CB ARG A 175 114.271 -1.801 132.083 1.00135.30 C ANISOU 971 CB ARG A 175 16439 19271 15697 2014 -3241 1122 C ATOM 972 CG ARG A 175 114.753 -0.563 132.833 1.00148.27 C ANISOU 972 CG ARG A 175 18302 20601 17434 2226 -3243 1118 C ATOM 973 CD ARG A 175 114.422 0.721 132.095 1.00163.88 C ANISOU 973 CD ARG A 175 20533 22332 19402 2517 -3580 1234 C ATOM 974 NE ARG A 175 115.339 0.982 130.982 1.00173.48 N ANISOU 974 NE ARG A 175 22171 23303 20440 2303 -3662 1478 N ATOM 975 CZ ARG A 175 116.441 1.723 131.070 1.00187.32 C ANISOU 975 CZ ARG A 175 24299 24708 22168 2203 -3612 1599 C ATOM 976 NH1 ARG A 175 116.784 2.282 132.224 1.00173.43 N ANISOU 976 NH1 ARG A 175 22563 22778 20555 2305 -3499 1488 N ATOM 977 NH2 ARG A 175 117.209 1.908 130.005 1.00175.03 N ANISOU 977 NH2 ARG A 175 23092 22985 20427 1983 -3673 1827 N ATOM 978 N ALA A 176 112.332 -3.958 133.509 1.00132.78 N ANISOU 978 N ALA A 176 15126 19764 15562 1904 -2958 749 N ATOM 979 CA ALA A 176 111.220 -4.299 134.399 1.00133.50 C ANISOU 979 CA ALA A 176 14753 20195 15775 2011 -2877 567 C ATOM 980 C ALA A 176 111.581 -5.469 135.326 1.00133.96 C ANISOU 980 C ALA A 176 14669 20390 15839 1691 -2548 512 C ATOM 981 O ALA A 176 111.207 -5.442 136.500 1.00134.03 O ANISOU 981 O ALA A 176 14434 20562 15929 1777 -2380 385 O ATOM 982 CB ALA A 176 109.980 -4.632 133.586 1.00137.07 C ANISOU 982 CB ALA A 176 14899 20948 16235 2069 -3105 524 C ATOM 983 N VAL A 177 112.322 -6.478 134.804 1.00127.34 N ANISOU 983 N VAL A 177 13999 19481 14902 1337 -2460 606 N ATOM 984 CA VAL A 177 112.774 -7.661 135.548 1.00124.61 C ANISOU 984 CA VAL A 177 13591 19204 14550 1024 -2184 582 C ATOM 985 C VAL A 177 113.707 -7.260 136.707 1.00126.41 C ANISOU 985 C VAL A 177 13982 19250 14797 1068 -1971 572 C ATOM 986 O VAL A 177 113.491 -7.712 137.829 1.00125.68 O ANISOU 986 O VAL A 177 13693 19312 14747 1014 -1770 492 O ATOM 987 CB VAL A 177 113.374 -8.749 134.609 1.00126.70 C ANISOU 987 CB VAL A 177 14028 19405 14708 691 -2187 663 C ATOM 988 CG1 VAL A 177 114.323 -9.697 135.344 1.00123.63 C ANISOU 988 CG1 VAL A 177 13750 18923 14299 427 -1923 672 C ATOM 989 CG2 VAL A 177 112.268 -9.538 133.922 1.00128.64 C ANISOU 989 CG2 VAL A 177 13996 19923 14958 568 -2322 613 C ATOM 990 N LEU A 178 114.695 -6.378 136.449 1.00122.13 N ANISOU 990 N LEU A 178 13791 18396 14217 1161 -2023 653 N ATOM 991 CA LEU A 178 115.641 -5.887 137.464 1.00120.37 C ANISOU 991 CA LEU A 178 13744 17979 14012 1205 -1861 636 C ATOM 992 C LEU A 178 114.942 -5.061 138.556 1.00127.60 C ANISOU 992 C LEU A 178 14471 18987 15023 1507 -1836 497 C ATOM 993 O LEU A 178 115.428 -5.008 139.689 1.00125.73 O ANISOU 993 O LEU A 178 14257 18718 14796 1508 -1652 433 O ATOM 994 CB LEU A 178 116.789 -5.087 136.822 1.00119.16 C ANISOU 994 CB LEU A 178 13989 17485 13801 1209 -1947 756 C ATOM 995 CG LEU A 178 117.731 -5.860 135.893 1.00121.40 C ANISOU 995 CG LEU A 178 14480 17681 13966 912 -1913 870 C ATOM 996 CD1 LEU A 178 118.464 -4.920 134.965 1.00121.72 C ANISOU 996 CD1 LEU A 178 14854 17463 13932 940 -2054 1002 C ATOM 997 CD2 LEU A 178 118.719 -6.718 136.677 1.00120.73 C ANISOU 997 CD2 LEU A 178 14437 17570 13867 696 -1667 844 C ATOM 998 N LEU A 179 113.794 -4.436 138.211 1.00128.73 N ANISOU 998 N LEU A 179 14421 19263 15228 1777 -2029 435 N ATOM 999 CA LEU A 179 112.959 -3.658 139.131 1.00131.56 C ANISOU 999 CA LEU A 179 14551 19758 15677 2113 -2029 266 C ATOM 1000 C LEU A 179 112.093 -4.617 139.962 1.00137.15 C ANISOU 1000 C LEU A 179 14830 20882 16400 2006 -1829 150 C ATOM 1001 O LEU A 179 111.982 -4.439 141.176 1.00137.22 O ANISOU 1001 O LEU A 179 14706 21008 16423 2112 -1654 23 O ATOM 1002 CB LEU A 179 112.074 -2.667 138.358 1.00134.94 C ANISOU 1002 CB LEU A 179 14938 20168 16166 2465 -2338 242 C ATOM 1003 N GLY A 180 111.516 -5.624 139.294 1.00134.37 N ANISOU 1003 N GLY A 180 14279 20746 16029 1775 -1857 196 N ATOM 1004 CA GLY A 180 110.676 -6.657 139.895 1.00135.38 C ANISOU 1004 CA GLY A 180 14009 21262 16167 1587 -1683 121 C ATOM 1005 C GLY A 180 111.420 -7.542 140.877 1.00137.28 C ANISOU 1005 C GLY A 180 14325 21489 16345 1294 -1389 156 C ATOM 1006 O GLY A 180 110.920 -7.803 141.974 1.00138.21 O ANISOU 1006 O GLY A 180 14179 21876 16460 1270 -1190 67 O ATOM 1007 N VAL A 181 112.634 -7.989 140.497 1.00130.91 N ANISOU 1007 N VAL A 181 13881 20381 15476 1079 -1362 286 N ATOM 1008 CA VAL A 181 113.517 -8.818 141.325 1.00128.62 C ANISOU 1008 CA VAL A 181 13728 20017 15124 826 -1126 335 C ATOM 1009 C VAL A 181 113.816 -8.082 142.644 1.00133.06 C ANISOU 1009 C VAL A 181 14319 20562 15675 1027 -980 246 C ATOM 1010 O VAL A 181 113.724 -8.680 143.713 1.00132.88 O ANISOU 1010 O VAL A 181 14181 20705 15604 904 -765 220 O ATOM 1011 CB VAL A 181 114.805 -9.224 140.540 1.00129.72 C ANISOU 1011 CB VAL A 181 14241 19839 15209 631 -1168 463 C ATOM 1012 CG1 VAL A 181 115.974 -9.559 141.467 1.00127.12 C ANISOU 1012 CG1 VAL A 181 14123 19350 14827 515 -976 492 C ATOM 1013 CG2 VAL A 181 114.525 -10.383 139.586 1.00129.61 C ANISOU 1013 CG2 VAL A 181 14175 19894 15177 352 -1231 522 C ATOM 1014 N TRP A 182 114.105 -6.774 142.550 1.00129.97 N ANISOU 1014 N TRP A 182 14087 19975 15319 1333 -1110 197 N ATOM 1015 CA TRP A 182 114.408 -5.885 143.667 1.00129.89 C ANISOU 1015 CA TRP A 182 14146 19901 15306 1566 -1026 85 C ATOM 1016 C TRP A 182 113.276 -5.827 144.684 1.00132.95 C ANISOU 1016 C TRP A 182 14160 20661 15693 1721 -894 -78 C ATOM 1017 O TRP A 182 113.504 -6.086 145.867 1.00132.29 O ANISOU 1017 O TRP A 182 14054 20677 15534 1675 -683 -132 O ATOM 1018 CB TRP A 182 114.666 -4.478 143.136 1.00130.23 C ANISOU 1018 CB TRP A 182 14415 19655 15412 1863 -1249 63 C ATOM 1019 CG TRP A 182 115.502 -3.649 144.046 1.00131.37 C ANISOU 1019 CG TRP A 182 14782 19586 15546 2006 -1191 -14 C ATOM 1020 CD1 TRP A 182 115.088 -2.944 145.139 1.00136.49 C ANISOU 1020 CD1 TRP A 182 15316 20338 16206 2283 -1132 -202 C ATOM 1021 CD2 TRP A 182 116.907 -3.439 143.937 1.00129.07 C ANISOU 1021 CD2 TRP A 182 14856 18959 15227 1873 -1192 75 C ATOM 1022 NE1 TRP A 182 116.159 -2.316 145.728 1.00135.16 N ANISOU 1022 NE1 TRP A 182 15442 19896 16019 2322 -1108 -235 N ATOM 1023 CE2 TRP A 182 117.290 -2.597 145.006 1.00134.07 C ANISOU 1023 CE2 TRP A 182 15588 19489 15862 2065 -1146 -62 C ATOM 1024 CE3 TRP A 182 117.891 -3.895 143.045 1.00128.09 C ANISOU 1024 CE3 TRP A 182 14968 18633 15069 1608 -1222 242 C ATOM 1025 CZ2 TRP A 182 118.612 -2.180 145.189 1.00131.92 C ANISOU 1025 CZ2 TRP A 182 15636 18912 15573 1982 -1146 -29 C ATOM 1026 CZ3 TRP A 182 119.197 -3.475 143.221 1.00128.24 C ANISOU 1026 CZ3 TRP A 182 15282 18374 15069 1538 -1205 275 C ATOM 1027 CH2 TRP A 182 119.550 -2.632 144.284 1.00129.67 C ANISOU 1027 CH2 TRP A 182 15550 18453 15266 1711 -1173 145 C ATOM 1028 N LEU A 183 112.061 -5.475 144.216 1.00129.58 N ANISOU 1028 N LEU A 183 13432 20463 15340 1913 -1022 -162 N ATOM 1029 CA LEU A 183 110.863 -5.345 145.042 1.00131.15 C ANISOU 1029 CA LEU A 183 13212 21075 15545 2091 -908 -342 C ATOM 1030 C LEU A 183 110.488 -6.658 145.720 1.00132.34 C ANISOU 1030 C LEU A 183 13107 21563 15612 1739 -644 -305 C ATOM 1031 O LEU A 183 110.147 -6.641 146.901 1.00134.04 O ANISOU 1031 O LEU A 183 13126 22045 15757 1799 -434 -421 O ATOM 1032 CB LEU A 183 109.690 -4.763 144.239 1.00134.27 C ANISOU 1032 CB LEU A 183 13329 21640 16046 2369 -1138 -433 C ATOM 1033 CG LEU A 183 109.909 -3.362 143.649 1.00139.59 C ANISOU 1033 CG LEU A 183 14250 21984 16802 2767 -1420 -475 C ATOM 1034 CD1 LEU A 183 108.938 -3.087 142.527 1.00142.27 C ANISOU 1034 CD1 LEU A 183 14401 22428 17228 2938 -1697 -479 C ATOM 1035 CD2 LEU A 183 109.824 -2.276 144.715 1.00143.98 C ANISOU 1035 CD2 LEU A 183 14787 22544 17374 3159 -1372 -691 C ATOM 1036 N ALA A 184 110.621 -7.794 145.004 1.00124.51 N ANISOU 1036 N ALA A 184 12153 20543 14614 1365 -654 -141 N ATOM 1037 CA ALA A 184 110.357 -9.136 145.534 1.00123.19 C ANISOU 1037 CA ALA A 184 11815 20617 14376 975 -433 -67 C ATOM 1038 C ALA A 184 111.334 -9.487 146.677 1.00122.57 C ANISOU 1038 C ALA A 184 11979 20417 14174 839 -211 -11 C ATOM 1039 O ALA A 184 110.921 -10.071 147.681 1.00123.27 O ANISOU 1039 O ALA A 184 11882 20786 14171 680 19 -18 O ATOM 1040 CB ALA A 184 110.462 -10.164 144.419 1.00122.56 C ANISOU 1040 CB ALA A 184 11806 20433 14328 643 -546 80 C ATOM 1041 N VAL A 185 112.618 -9.096 146.522 1.00114.48 N ANISOU 1041 N VAL A 185 11363 18994 13139 900 -285 45 N ATOM 1042 CA VAL A 185 113.704 -9.316 147.485 1.00111.15 C ANISOU 1042 CA VAL A 185 11208 18414 12609 812 -131 90 C ATOM 1043 C VAL A 185 113.538 -8.391 148.708 1.00115.28 C ANISOU 1043 C VAL A 185 11656 19079 13067 1102 -17 -79 C ATOM 1044 O VAL A 185 113.677 -8.855 149.843 1.00114.83 O ANISOU 1044 O VAL A 185 11589 19164 12875 993 192 -76 O ATOM 1045 CB VAL A 185 115.086 -9.206 146.787 1.00111.31 C ANISOU 1045 CB VAL A 185 11638 18000 12654 769 -264 191 C ATOM 1046 CG1 VAL A 185 116.221 -9.043 147.788 1.00109.80 C ANISOU 1046 CG1 VAL A 185 11702 17643 12372 788 -157 186 C ATOM 1047 CG2 VAL A 185 115.339 -10.417 145.894 1.00109.45 C ANISOU 1047 CG2 VAL A 185 11482 17672 12431 438 -305 342 C ATOM 1048 N LEU A 186 113.204 -7.099 148.470 1.00112.56 N ANISOU 1048 N LEU A 186 11265 18696 12807 1478 -165 -232 N ATOM 1049 CA LEU A 186 112.950 -6.088 149.509 1.00113.85 C ANISOU 1049 CA LEU A 186 11352 18979 12927 1814 -96 -440 C ATOM 1050 C LEU A 186 111.771 -6.518 150.400 1.00119.09 C ANISOU 1050 C LEU A 186 11593 20157 13497 1794 131 -542 C ATOM 1051 O LEU A 186 111.858 -6.373 151.618 1.00119.41 O ANISOU 1051 O LEU A 186 11620 20351 13400 1863 318 -643 O ATOM 1052 CB LEU A 186 112.658 -4.717 148.865 1.00115.42 C ANISOU 1052 CB LEU A 186 11577 19015 13262 2218 -343 -574 C ATOM 1053 CG LEU A 186 112.466 -3.540 149.826 1.00122.43 C ANISOU 1053 CG LEU A 186 12453 19937 14129 2616 -324 -819 C ATOM 1054 CD1 LEU A 186 113.677 -2.640 149.829 1.00121.05 C ANISOU 1054 CD1 LEU A 186 12719 19289 13986 2732 -466 -822 C ATOM 1055 CD2 LEU A 186 111.233 -2.745 149.472 1.00127.42 C ANISOU 1055 CD2 LEU A 186 12781 20764 14867 2990 -458 -1000 C ATOM 1056 N ALA A 187 110.684 -7.053 149.783 1.00116.37 N ANISOU 1056 N ALA A 187 10900 20097 13217 1680 117 -518 N ATOM 1057 CA ALA A 187 109.480 -7.542 150.471 1.00118.98 C ANISOU 1057 CA ALA A 187 10773 20961 13472 1600 335 -599 C ATOM 1058 C ALA A 187 109.823 -8.714 151.390 1.00120.66 C ANISOU 1058 C ALA A 187 11045 21294 13508 1199 606 -451 C ATOM 1059 O ALA A 187 109.356 -8.741 152.532 1.00122.62 O ANISOU 1059 O ALA A 187 11077 21907 13607 1208 846 -542 O ATOM 1060 CB ALA A 187 108.419 -7.956 149.460 1.00121.40 C ANISOU 1060 CB ALA A 187 10733 21491 13902 1503 223 -578 C ATOM 1061 N PHE A 188 110.671 -9.657 150.906 1.00112.93 N ANISOU 1061 N PHE A 188 10373 20002 12532 863 561 -226 N ATOM 1062 CA PHE A 188 111.129 -10.802 151.693 1.00111.61 C ANISOU 1062 CA PHE A 188 10343 19856 12209 491 766 -57 C ATOM 1063 C PHE A 188 111.952 -10.303 152.885 1.00114.57 C ANISOU 1063 C PHE A 188 10958 20151 12423 650 882 -116 C ATOM 1064 O PHE A 188 111.729 -10.759 154.005 1.00115.42 O ANISOU 1064 O PHE A 188 10991 20521 12341 508 1118 -90 O ATOM 1065 CB PHE A 188 111.935 -11.803 150.832 1.00110.10 C ANISOU 1065 CB PHE A 188 10445 19307 12081 171 646 161 C ATOM 1066 CG PHE A 188 112.583 -12.922 151.621 1.00110.66 C ANISOU 1066 CG PHE A 188 10739 19302 12004 -162 805 341 C ATOM 1067 CD1 PHE A 188 111.837 -14.011 152.056 1.00115.93 C ANISOU 1067 CD1 PHE A 188 11216 20243 12588 -520 981 455 C ATOM 1068 CD2 PHE A 188 113.933 -12.871 151.951 1.00110.02 C ANISOU 1068 CD2 PHE A 188 11060 18878 11866 -120 767 399 C ATOM 1069 CE1 PHE A 188 112.427 -15.027 152.814 1.00116.43 C ANISOU 1069 CE1 PHE A 188 11525 20206 12506 -816 1108 641 C ATOM 1070 CE2 PHE A 188 114.525 -13.890 152.707 1.00112.38 C ANISOU 1070 CE2 PHE A 188 11573 19102 12023 -390 886 565 C ATOM 1071 CZ PHE A 188 113.768 -14.963 153.129 1.00112.84 C ANISOU 1071 CZ PHE A 188 11478 19401 11995 -730 1049 693 C ATOM 1072 N ALA A 189 112.865 -9.336 152.638 1.00109.43 N ANISOU 1072 N ALA A 189 10590 19150 11838 933 710 -197 N ATOM 1073 CA ALA A 189 113.738 -8.717 153.641 1.00108.83 C ANISOU 1073 CA ALA A 189 10763 18950 11636 1110 762 -283 C ATOM 1074 C ALA A 189 112.963 -7.942 154.713 1.00117.14 C ANISOU 1074 C ALA A 189 11568 20370 12569 1392 916 -518 C ATOM 1075 O ALA A 189 113.477 -7.761 155.818 1.00117.57 O ANISOU 1075 O ALA A 189 11769 20452 12449 1458 1032 -582 O ATOM 1076 CB ALA A 189 114.751 -7.806 152.964 1.00106.89 C ANISOU 1076 CB ALA A 189 10835 18256 11523 1317 522 -320 C ATOM 1077 N LEU A 190 111.726 -7.507 154.396 1.00116.76 N ANISOU 1077 N LEU A 190 11135 20623 12606 1569 911 -662 N ATOM 1078 CA LEU A 190 110.864 -6.767 155.319 1.00120.52 C ANISOU 1078 CA LEU A 190 11313 21498 12982 1874 1056 -922 C ATOM 1079 C LEU A 190 110.063 -7.667 156.279 1.00127.54 C ANISOU 1079 C LEU A 190 11885 22917 13658 1616 1382 -885 C ATOM 1080 O LEU A 190 109.334 -7.135 157.119 1.00131.22 O ANISOU 1080 O LEU A 190 12073 23780 14004 1847 1545 -1109 O ATOM 1081 CB LEU A 190 109.926 -5.816 154.545 1.00122.75 C ANISOU 1081 CB LEU A 190 11319 21860 13461 2236 877 -1115 C ATOM 1082 CG LEU A 190 110.527 -4.483 154.089 1.00126.50 C ANISOU 1082 CG LEU A 190 12076 21907 14080 2640 603 -1256 C ATOM 1083 CD1 LEU A 190 109.815 -3.959 152.862 1.00127.91 C ANISOU 1083 CD1 LEU A 190 12087 22030 14482 2851 353 -1300 C ATOM 1084 CD2 LEU A 190 110.488 -3.439 155.199 1.00131.59 C ANISOU 1084 CD2 LEU A 190 12724 22659 14616 3029 678 -1548 C ATOM 1085 N LEU A 191 110.196 -9.014 156.169 1.00122.56 N ANISOU 1085 N LEU A 191 11305 22291 12971 1138 1479 -610 N ATOM 1086 CA LEU A 191 109.472 -9.967 157.026 1.00125.28 C ANISOU 1086 CA LEU A 191 11394 23098 13108 811 1784 -519 C ATOM 1087 C LEU A 191 109.749 -9.786 158.544 1.00131.12 C ANISOU 1087 C LEU A 191 12226 24051 13544 882 2022 -596 C ATOM 1088 O LEU A 191 108.761 -9.732 159.276 1.00134.99 O ANISOU 1088 O LEU A 191 12346 25067 13877 904 2265 -719 O ATOM 1089 CB LEU A 191 109.667 -11.433 156.595 1.00123.69 C ANISOU 1089 CB LEU A 191 11313 22764 12919 283 1800 -197 C ATOM 1090 CG LEU A 191 108.824 -11.909 155.400 1.00128.45 C ANISOU 1090 CG LEU A 191 11641 23428 13738 98 1684 -136 C ATOM 1091 CD1 LEU A 191 109.401 -13.168 154.794 1.00126.02 C ANISOU 1091 CD1 LEU A 191 11610 22792 13480 -338 1607 150 C ATOM 1092 CD2 LEU A 191 107.378 -12.158 155.794 1.00134.94 C ANISOU 1092 CD2 LEU A 191 11916 24861 14496 -29 1906 -211 C ATOM 1093 N PRO A 192 111.009 -9.622 159.057 1.00125.34 N ANISOU 1093 N PRO A 192 11942 22972 12711 941 1962 -556 N ATOM 1094 CA PRO A 192 111.189 -9.414 160.512 1.00127.01 C ANISOU 1094 CA PRO A 192 12225 23426 12609 1025 2176 -651 C ATOM 1095 C PRO A 192 110.534 -8.146 161.067 1.00133.64 C ANISOU 1095 C PRO A 192 12813 24575 13391 1490 2242 -1022 C ATOM 1096 O PRO A 192 110.187 -8.114 162.250 1.00136.39 O ANISOU 1096 O PRO A 192 13051 25322 13449 1522 2494 -1124 O ATOM 1097 CB PRO A 192 112.711 -9.377 160.680 1.00124.93 C ANISOU 1097 CB PRO A 192 12479 22670 12317 1033 2015 -558 C ATOM 1098 CG PRO A 192 113.239 -10.096 159.500 1.00126.08 C ANISOU 1098 CG PRO A 192 12798 22415 12693 787 1818 -322 C ATOM 1099 CD PRO A 192 112.325 -9.669 158.388 1.00122.44 C ANISOU 1099 CD PRO A 192 12016 22019 12484 916 1709 -426 C ATOM 1100 N VAL A 193 110.354 -7.114 160.211 1.00129.39 N ANISOU 1100 N VAL A 193 12196 23851 13116 1858 2010 -1223 N ATOM 1101 CA VAL A 193 109.691 -5.850 160.552 1.00132.51 C ANISOU 1101 CA VAL A 193 12358 24473 13516 2356 2013 -1598 C ATOM 1102 C VAL A 193 108.219 -6.172 160.875 1.00142.00 C ANISOU 1102 C VAL A 193 12989 26343 14620 2308 2278 -1691 C ATOM 1103 O VAL A 193 107.690 -5.679 161.875 1.00145.71 O ANISOU 1103 O VAL A 193 13246 27230 14885 2548 2480 -1947 O ATOM 1104 CB VAL A 193 109.840 -4.791 159.417 1.00134.50 C ANISOU 1104 CB VAL A 193 12702 24308 14095 2717 1664 -1732 C ATOM 1105 CG1 VAL A 193 109.073 -3.507 159.731 1.00138.20 C ANISOU 1105 CG1 VAL A 193 12936 24985 14588 3261 1639 -2128 C ATOM 1106 CG2 VAL A 193 111.307 -4.478 159.140 1.00129.85 C ANISOU 1106 CG2 VAL A 193 12651 23101 13586 2713 1432 -1633 C ATOM 1107 N LEU A 194 107.589 -7.048 160.058 1.00138.66 N ANISOU 1107 N LEU A 194 12320 26036 14328 1974 2287 -1486 N ATOM 1108 CA LEU A 194 106.209 -7.497 160.250 1.00143.07 C ANISOU 1108 CA LEU A 194 12311 27230 14820 1835 2530 -1534 C ATOM 1109 C LEU A 194 106.111 -8.485 161.422 1.00149.95 C ANISOU 1109 C LEU A 194 13142 28489 15341 1422 2897 -1369 C ATOM 1110 O LEU A 194 105.229 -8.329 162.270 1.00154.32 O ANISOU 1110 O LEU A 194 13309 29635 15689 1496 3177 -1548 O ATOM 1111 CB LEU A 194 105.616 -8.106 158.961 1.00142.27 C ANISOU 1111 CB LEU A 194 11982 27090 14983 1593 2382 -1374 C ATOM 1112 CG LEU A 194 105.635 -7.245 157.685 1.00144.99 C ANISOU 1112 CG LEU A 194 12352 27080 15657 1955 2011 -1493 C ATOM 1113 CD1 LEU A 194 105.220 -8.058 156.484 1.00143.87 C ANISOU 1113 CD1 LEU A 194 12075 26870 15719 1626 1871 -1283 C ATOM 1114 CD2 LEU A 194 104.734 -6.026 157.806 1.00151.66 C ANISOU 1114 CD2 LEU A 194 12807 28254 16562 2502 1984 -1874 C ATOM 1115 N GLY A 195 107.022 -9.464 161.473 1.00143.81 N ANISOU 1115 N GLY A 195 12768 27382 14489 1007 2888 -1034 N ATOM 1116 CA GLY A 195 107.059 -10.460 162.540 1.00145.77 C ANISOU 1116 CA GLY A 195 13078 27905 14403 589 3192 -819 C ATOM 1117 C GLY A 195 107.768 -11.767 162.236 1.00147.21 C ANISOU 1117 C GLY A 195 13624 27715 14594 79 3133 -413 C ATOM 1118 O GLY A 195 108.263 -12.416 163.161 1.00147.06 O ANISOU 1118 O GLY A 195 13879 27700 14296 -159 3282 -229 O ATOM 1119 N VAL A 196 107.804 -12.184 160.950 1.00141.68 N ANISOU 1119 N VAL A 196 12935 26697 14200 -82 2907 -277 N ATOM 1120 CA VAL A 196 108.432 -13.444 160.515 1.00138.96 C ANISOU 1120 CA VAL A 196 12922 25973 13904 -541 2819 79 C ATOM 1121 C VAL A 196 109.963 -13.319 160.516 1.00138.52 C ANISOU 1121 C VAL A 196 13435 25342 13853 -413 2613 155 C ATOM 1122 O VAL A 196 110.525 -12.597 159.695 1.00134.75 O ANISOU 1122 O VAL A 196 13101 24493 13606 -126 2348 44 O ATOM 1123 CB VAL A 196 107.867 -13.964 159.160 1.00142.07 C ANISOU 1123 CB VAL A 196 13119 26260 14600 -754 2653 166 C ATOM 1124 CG1 VAL A 196 108.480 -15.312 158.781 1.00139.75 C ANISOU 1124 CG1 VAL A 196 13174 25585 14339 -1226 2575 509 C ATOM 1125 CG2 VAL A 196 106.345 -14.064 159.197 1.00146.77 C ANISOU 1125 CG2 VAL A 196 13109 27465 15193 -883 2851 72 C ATOM 1126 N GLY A 197 110.609 -14.025 161.443 1.00135.62 N ANISOU 1126 N GLY A 197 13379 24927 13224 -636 2734 350 N ATOM 1127 CA GLY A 197 112.059 -14.001 161.618 1.00131.83 C ANISOU 1127 CA GLY A 197 13409 23971 12709 -538 2560 426 C ATOM 1128 C GLY A 197 112.526 -12.753 162.342 1.00135.27 C ANISOU 1128 C GLY A 197 13928 24443 13027 -86 2547 149 C ATOM 1129 O GLY A 197 111.702 -11.904 162.700 1.00137.91 O ANISOU 1129 O GLY A 197 13933 25164 13303 173 2676 -111 O ATOM 1130 N GLN A 198 113.847 -12.639 162.594 1.00128.20 N ANISOU 1130 N GLN A 198 13464 23154 12092 16 2386 187 N ATOM 1131 CA GLN A 198 114.415 -11.463 163.268 1.00127.64 C ANISOU 1131 CA GLN A 198 13524 23054 11920 420 2335 -77 C ATOM 1132 C GLN A 198 115.898 -11.258 162.978 1.00126.49 C ANISOU 1132 C GLN A 198 13801 22373 11885 521 2063 -44 C ATOM 1133 O GLN A 198 116.600 -12.208 162.630 1.00124.21 O ANISOU 1133 O GLN A 198 13756 21798 11642 259 1969 213 O ATOM 1134 CB GLN A 198 114.137 -11.442 164.792 1.00132.98 C ANISOU 1134 CB GLN A 198 14175 24166 12183 429 2603 -134 C ATOM 1135 CG GLN A 198 114.757 -12.564 165.617 1.00149.45 C ANISOU 1135 CG GLN A 198 16580 26215 13989 94 2683 171 C ATOM 1136 CD GLN A 198 114.527 -12.326 167.090 1.00170.73 C ANISOU 1136 CD GLN A 198 19266 29346 16256 158 2927 79 C ATOM 1137 OE1 GLN A 198 115.274 -11.595 167.750 1.00165.09 O ANISOU 1137 OE1 GLN A 198 18765 28561 15400 437 2850 -100 O ATOM 1138 NE2 GLN A 198 113.472 -12.915 167.633 1.00166.29 N ANISOU 1138 NE2 GLN A 198 18448 29267 15467 -110 3231 190 N ATOM 1139 N TYR A 199 116.359 -10.000 163.108 1.00121.14 N ANISOU 1139 N TYR A 199 13201 21565 11260 902 1933 -318 N ATOM 1140 CA TYR A 199 117.753 -9.619 162.912 1.00117.04 C ANISOU 1140 CA TYR A 199 13042 20589 10840 1014 1685 -332 C ATOM 1141 C TYR A 199 118.394 -9.385 164.281 1.00121.00 C ANISOU 1141 C TYR A 199 13757 21190 11027 1117 1740 -420 C ATOM 1142 O TYR A 199 117.913 -8.556 165.064 1.00122.83 O ANISOU 1142 O TYR A 199 13870 21701 11099 1367 1847 -677 O ATOM 1143 CB TYR A 199 117.880 -8.377 162.008 1.00116.51 C ANISOU 1143 CB TYR A 199 12947 20254 11067 1323 1471 -556 C ATOM 1144 CG TYR A 199 117.326 -8.544 160.607 1.00117.00 C ANISOU 1144 CG TYR A 199 12827 20203 11423 1246 1381 -473 C ATOM 1145 CD1 TYR A 199 117.856 -9.490 159.732 1.00116.28 C ANISOU 1145 CD1 TYR A 199 12869 19843 11470 964 1280 -218 C ATOM 1146 CD2 TYR A 199 116.327 -7.702 160.128 1.00119.37 C ANISOU 1146 CD2 TYR A 199 12842 20648 11865 1488 1370 -671 C ATOM 1147 CE1 TYR A 199 117.376 -9.621 158.428 1.00115.93 C ANISOU 1147 CE1 TYR A 199 12675 19698 11674 900 1183 -158 C ATOM 1148 CE2 TYR A 199 115.848 -7.814 158.822 1.00119.16 C ANISOU 1148 CE2 TYR A 199 12664 20516 12096 1434 1257 -599 C ATOM 1149 CZ TYR A 199 116.366 -8.784 157.981 1.00123.27 C ANISOU 1149 CZ TYR A 199 13320 20788 12728 1127 1169 -341 C ATOM 1150 OH TYR A 199 115.889 -8.904 156.701 1.00122.72 O ANISOU 1150 OH TYR A 199 13110 20634 12885 1072 1053 -282 O ATOM 1151 N THR A 200 119.454 -10.157 164.578 1.00115.21 N ANISOU 1151 N THR A 200 13336 20245 10192 934 1660 -214 N ATOM 1152 CA THR A 200 120.175 -10.110 165.852 1.00115.88 C ANISOU 1152 CA THR A 200 13659 20407 9962 996 1677 -254 C ATOM 1153 C THR A 200 121.633 -9.707 165.686 1.00115.94 C ANISOU 1153 C THR A 200 13967 20001 10085 1113 1401 -309 C ATOM 1154 O THR A 200 122.192 -9.840 164.597 1.00112.13 O ANISOU 1154 O THR A 200 13546 19166 9894 1054 1222 -224 O ATOM 1155 CB THR A 200 120.072 -11.456 166.586 1.00124.45 C ANISOU 1155 CB THR A 200 14846 21685 10755 673 1841 50 C ATOM 1156 OG1 THR A 200 120.438 -12.510 165.695 1.00118.76 O ANISOU 1156 OG1 THR A 200 14236 20658 10228 404 1730 336 O ATOM 1157 CG2 THR A 200 118.689 -11.701 167.179 1.00128.00 C ANISOU 1157 CG2 THR A 200 15002 22651 10980 561 2160 62 C ATOM 1158 N VAL A 201 122.251 -9.234 166.788 1.00113.64 N ANISOU 1158 N VAL A 201 13852 19779 9547 1268 1371 -457 N ATOM 1159 CA VAL A 201 123.663 -8.842 166.842 1.00110.84 C ANISOU 1159 CA VAL A 201 13764 19093 9256 1369 1114 -533 C ATOM 1160 C VAL A 201 124.500 -10.126 166.795 1.00113.15 C ANISOU 1160 C VAL A 201 14270 19213 9508 1121 1029 -219 C ATOM 1161 O VAL A 201 124.235 -11.063 167.556 1.00115.11 O ANISOU 1161 O VAL A 201 14591 19674 9472 957 1164 -22 O ATOM 1162 CB VAL A 201 124.000 -7.968 168.081 1.00116.21 C ANISOU 1162 CB VAL A 201 14560 19929 9667 1606 1098 -807 C ATOM 1163 CG1 VAL A 201 125.399 -7.373 167.961 1.00113.80 C ANISOU 1163 CG1 VAL A 201 14471 19264 9501 1713 809 -935 C ATOM 1164 CG2 VAL A 201 122.973 -6.859 168.273 1.00118.39 C ANISOU 1164 CG2 VAL A 201 14614 20445 9923 1859 1228 -1115 C ATOM 1165 N GLN A 202 125.472 -10.181 165.873 1.00105.75 N ANISOU 1165 N GLN A 202 13432 17896 8854 1094 809 -171 N ATOM 1166 CA GLN A 202 126.335 -11.350 165.681 1.00103.78 C ANISOU 1166 CA GLN A 202 13372 17443 8617 909 695 89 C ATOM 1167 C GLN A 202 127.731 -11.115 166.254 1.00107.16 C ANISOU 1167 C GLN A 202 14023 17724 8971 1023 480 1 C ATOM 1168 O GLN A 202 128.146 -9.965 166.376 1.00106.54 O ANISOU 1168 O GLN A 202 13937 17593 8949 1212 380 -263 O ATOM 1169 CB GLN A 202 126.445 -11.701 164.185 1.00101.68 C ANISOU 1169 CB GLN A 202 13035 16891 8706 794 608 200 C ATOM 1170 CG GLN A 202 125.121 -11.835 163.427 1.00107.19 C ANISOU 1170 CG GLN A 202 13489 17708 9531 692 772 255 C ATOM 1171 CD GLN A 202 124.351 -13.078 163.781 1.00122.99 C ANISOU 1171 CD GLN A 202 15476 19899 11357 441 947 511 C ATOM 1172 OE1 GLN A 202 124.860 -14.202 163.722 1.00117.28 O ANISOU 1172 OE1 GLN A 202 14930 19018 10613 263 884 742 O ATOM 1173 NE2 GLN A 202 123.093 -12.897 164.137 1.00118.45 N ANISOU 1173 NE2 GLN A 202 14683 19663 10660 419 1168 471 N ATOM 1174 N TRP A 203 128.458 -12.204 166.582 1.00103.65 N ANISOU 1174 N TRP A 203 13775 17198 8408 910 392 217 N ATOM 1175 CA TRP A 203 129.832 -12.165 167.097 1.00103.06 C ANISOU 1175 CA TRP A 203 13897 16998 8263 1008 164 161 C ATOM 1176 C TRP A 203 130.757 -11.547 166.033 1.00104.33 C ANISOU 1176 C TRP A 203 14004 16859 8779 1073 -34 21 C ATOM 1177 O TRP A 203 130.615 -11.907 164.863 1.00101.58 O ANISOU 1177 O TRP A 203 13567 16339 8692 970 -29 122 O ATOM 1178 CB TRP A 203 130.311 -13.588 167.425 1.00102.31 C ANISOU 1178 CB TRP A 203 14008 16841 8022 875 99 456 C ATOM 1179 CG TRP A 203 131.654 -13.639 168.095 1.00103.79 C ANISOU 1179 CG TRP A 203 14388 16954 8092 994 -142 411 C ATOM 1180 CD1 TRP A 203 131.900 -13.585 169.435 1.00109.41 C ANISOU 1180 CD1 TRP A 203 15263 17867 8441 1077 -175 386 C ATOM 1181 CD2 TRP A 203 132.935 -13.736 167.454 1.00101.55 C ANISOU 1181 CD2 TRP A 203 14136 16403 8046 1048 -389 375 C ATOM 1182 NE1 TRP A 203 133.254 -13.641 169.670 1.00108.63 N ANISOU 1182 NE1 TRP A 203 15293 17633 8349 1185 -448 335 N ATOM 1183 CE2 TRP A 203 133.914 -13.730 168.472 1.00106.97 C ANISOU 1183 CE2 TRP A 203 14989 17145 8512 1170 -577 322 C ATOM 1184 CE3 TRP A 203 133.354 -13.819 166.114 1.00 99.76 C ANISOU 1184 CE3 TRP A 203 13799 15923 8184 1007 -467 372 C ATOM 1185 CZ2 TRP A 203 135.284 -13.816 168.194 1.00105.12 C ANISOU 1185 CZ2 TRP A 203 14784 16729 8427 1254 -840 260 C ATOM 1186 CZ3 TRP A 203 134.711 -13.900 165.841 1.00100.16 C ANISOU 1186 CZ3 TRP A 203 13884 15804 8368 1084 -704 311 C ATOM 1187 CH2 TRP A 203 135.659 -13.897 166.872 1.00102.57 C ANISOU 1187 CH2 TRP A 203 14326 16177 8468 1207 -889 252 C ATOM 1188 N PRO A 204 131.689 -10.620 166.367 1.00101.67 N ANISOU 1188 N PRO A 204 13715 16461 8454 1219 -206 -209 N ATOM 1189 CA PRO A 204 132.064 -10.095 167.694 1.00104.23 C ANISOU 1189 CA PRO A 204 14158 16959 8486 1356 -268 -376 C ATOM 1190 C PRO A 204 131.390 -8.776 168.117 1.00110.18 C ANISOU 1190 C PRO A 204 14831 17854 9178 1506 -179 -663 C ATOM 1191 O PRO A 204 132.013 -7.945 168.790 1.00110.72 O ANISOU 1191 O PRO A 204 14976 17937 9155 1640 -312 -901 O ATOM 1192 CB PRO A 204 133.583 -9.957 167.559 1.00104.97 C ANISOU 1192 CB PRO A 204 14324 16854 8705 1398 -543 -459 C ATOM 1193 CG PRO A 204 133.784 -9.562 166.099 1.00106.58 C ANISOU 1193 CG PRO A 204 14382 16803 9309 1339 -583 -497 C ATOM 1194 CD PRO A 204 132.582 -10.076 165.325 1.00101.01 C ANISOU 1194 CD PRO A 204 13572 16107 8700 1230 -377 -317 C ATOM 1195 N GLY A 205 130.118 -8.616 167.756 1.00107.67 N ANISOU 1195 N GLY A 205 14359 17646 8907 1493 33 -650 N ATOM 1196 CA GLY A 205 129.324 -7.430 168.071 1.00109.30 C ANISOU 1196 CA GLY A 205 14464 17990 9074 1667 130 -924 C ATOM 1197 C GLY A 205 129.598 -6.260 167.146 1.00111.28 C ANISOU 1197 C GLY A 205 14654 17960 9669 1760 -9 -1132 C ATOM 1198 O GLY A 205 129.380 -5.105 167.521 1.00112.73 O ANISOU 1198 O GLY A 205 14837 18162 9834 1945 -35 -1418 O ATOM 1199 N THR A 206 130.085 -6.561 165.932 1.00104.27 N ANISOU 1199 N THR A 206 13729 16802 9086 1630 -102 -989 N ATOM 1200 CA THR A 206 130.441 -5.585 164.901 1.00102.26 C ANISOU 1200 CA THR A 206 13438 16255 9161 1661 -237 -1120 C ATOM 1201 C THR A 206 129.450 -5.588 163.730 1.00104.90 C ANISOU 1201 C THR A 206 13610 16529 9719 1623 -129 -1023 C ATOM 1202 O THR A 206 129.615 -4.794 162.798 1.00103.80 O ANISOU 1202 O THR A 206 13451 16150 9838 1647 -230 -1103 O ATOM 1203 CB THR A 206 131.871 -5.858 164.399 1.00106.92 C ANISOU 1203 CB THR A 206 14109 16608 9906 1542 -439 -1056 C ATOM 1204 OG1 THR A 206 131.936 -7.181 163.854 1.00101.73 O ANISOU 1204 OG1 THR A 206 13425 15942 9285 1383 -393 -776 O ATOM 1205 CG2 THR A 206 132.920 -5.681 165.487 1.00107.13 C ANISOU 1205 CG2 THR A 206 14275 16685 9743 1599 -591 -1194 C ATOM 1206 N TRP A 207 128.430 -6.481 163.769 1.00101.34 N ANISOU 1206 N TRP A 207 13049 16296 9161 1549 66 -844 N ATOM 1207 CA TRP A 207 127.435 -6.633 162.701 1.00 99.91 C ANISOU 1207 CA TRP A 207 12691 16102 9167 1496 164 -742 C ATOM 1208 C TRP A 207 126.151 -7.350 163.129 1.00105.34 C ANISOU 1208 C TRP A 207 13230 17124 9672 1449 401 -636 C ATOM 1209 O TRP A 207 126.150 -8.083 164.119 1.00106.06 O ANISOU 1209 O TRP A 207 13383 17428 9485 1386 500 -551 O ATOM 1210 CB TRP A 207 128.063 -7.381 161.507 1.00 95.61 C ANISOU 1210 CB TRP A 207 12167 15320 8842 1303 74 -530 C ATOM 1211 CG TRP A 207 128.461 -8.804 161.790 1.00 95.88 C ANISOU 1211 CG TRP A 207 12280 15406 8745 1131 103 -298 C ATOM 1212 CD1 TRP A 207 129.389 -9.238 162.691 1.00 99.23 C ANISOU 1212 CD1 TRP A 207 12865 15846 8990 1125 25 -277 C ATOM 1213 CD2 TRP A 207 127.996 -9.971 161.100 1.00 94.69 C ANISOU 1213 CD2 TRP A 207 12072 15255 8650 945 183 -59 C ATOM 1214 NE1 TRP A 207 129.497 -10.607 162.638 1.00 98.04 N ANISOU 1214 NE1 TRP A 207 12775 15699 8777 965 53 -29 N ATOM 1215 CE2 TRP A 207 128.664 -11.083 161.660 1.00 98.50 C ANISOU 1215 CE2 TRP A 207 12708 15735 8984 843 151 104 C ATOM 1216 CE3 TRP A 207 127.074 -10.187 160.061 1.00 94.99 C ANISOU 1216 CE3 TRP A 207 11953 15290 8850 859 260 28 C ATOM 1217 CZ2 TRP A 207 128.423 -12.393 161.232 1.00 97.37 C ANISOU 1217 CZ2 TRP A 207 12585 15556 8854 654 197 347 C ATOM 1218 CZ3 TRP A 207 126.857 -11.482 159.621 1.00 95.83 C ANISOU 1218 CZ3 TRP A 207 12062 15382 8969 655 308 257 C ATOM 1219 CH2 TRP A 207 127.506 -12.569 160.218 1.00 96.84 C ANISOU 1219 CH2 TRP A 207 12362 15481 8950 552 280 414 C ATOM 1220 N CYS A 208 125.080 -7.175 162.326 1.00102.41 N ANISOU 1220 N CYS A 208 12657 16798 9457 1461 483 -627 N ATOM 1221 CA CYS A 208 123.765 -7.797 162.501 1.00104.21 C ANISOU 1221 CA CYS A 208 12676 17350 9570 1390 707 -536 C ATOM 1222 C CYS A 208 123.382 -8.628 161.277 1.00106.71 C ANISOU 1222 C CYS A 208 12884 17574 10088 1181 715 -313 C ATOM 1223 O CYS A 208 123.692 -8.238 160.148 1.00104.46 O ANISOU 1223 O CYS A 208 12601 17026 10063 1202 570 -324 O ATOM 1224 CB CYS A 208 122.704 -6.744 162.799 1.00107.15 C ANISOU 1224 CB CYS A 208 12858 17937 9916 1642 798 -792 C ATOM 1225 SG CYS A 208 122.778 -6.067 164.474 1.00114.40 S ANISOU 1225 SG CYS A 208 13858 19122 10487 1858 881 -1048 S ATOM 1226 N PHE A 209 122.687 -9.761 161.501 1.00104.36 N ANISOU 1226 N PHE A 209 12500 17494 9657 967 882 -113 N ATOM 1227 CA PHE A 209 122.224 -10.671 160.443 1.00102.94 C ANISOU 1227 CA PHE A 209 12219 17252 9642 740 897 92 C ATOM 1228 C PHE A 209 121.023 -11.523 160.909 1.00110.31 C ANISOU 1228 C PHE A 209 12967 18538 10407 548 1130 224 C ATOM 1229 O PHE A 209 120.564 -11.367 162.045 1.00112.88 O ANISOU 1229 O PHE A 209 13237 19176 10476 600 1295 157 O ATOM 1230 CB PHE A 209 123.393 -11.550 159.925 1.00102.00 C ANISOU 1230 CB PHE A 209 12333 16812 9609 574 747 277 C ATOM 1231 CG PHE A 209 123.186 -12.222 158.582 1.00101.73 C ANISOU 1231 CG PHE A 209 12239 16613 9799 399 690 421 C ATOM 1232 CD1 PHE A 209 122.940 -11.470 157.437 1.00103.28 C ANISOU 1232 CD1 PHE A 209 12319 16689 10232 496 596 322 C ATOM 1233 CD2 PHE A 209 123.250 -13.604 158.462 1.00103.75 C ANISOU 1233 CD2 PHE A 209 12585 16815 10021 143 713 652 C ATOM 1234 CE1 PHE A 209 122.725 -12.093 156.205 1.00102.87 C ANISOU 1234 CE1 PHE A 209 12219 16509 10357 337 539 443 C ATOM 1235 CE2 PHE A 209 123.051 -14.225 157.226 1.00105.19 C ANISOU 1235 CE2 PHE A 209 12723 16842 10401 -12 651 756 C ATOM 1236 CZ PHE A 209 122.791 -13.465 156.105 1.00101.94 C ANISOU 1236 CZ PHE A 209 12178 16351 10202 86 568 646 C ATOM 1237 N ILE A 210 120.499 -12.391 160.010 1.00106.60 N ANISOU 1237 N ILE A 210 12395 18031 10076 314 1145 401 N ATOM 1238 CA ILE A 210 119.378 -13.313 160.224 1.00108.84 C ANISOU 1238 CA ILE A 210 12496 18606 10253 55 1344 556 C ATOM 1239 C ILE A 210 119.673 -14.243 161.414 1.00115.76 C ANISOU 1239 C ILE A 210 13569 19585 10828 -135 1461 742 C ATOM 1240 O ILE A 210 120.683 -14.951 161.408 1.00114.15 O ANISOU 1240 O ILE A 210 13658 19098 10616 -227 1333 892 O ATOM 1241 CB ILE A 210 119.083 -14.103 158.911 1.00110.15 C ANISOU 1241 CB ILE A 210 12594 18600 10657 -171 1264 707 C ATOM 1242 CG1 ILE A 210 118.589 -13.166 157.788 1.00109.26 C ANISOU 1242 CG1 ILE A 210 12278 18434 10803 21 1152 534 C ATOM 1243 CG2 ILE A 210 118.096 -15.248 159.141 1.00113.36 C ANISOU 1243 CG2 ILE A 210 12846 19263 10962 -508 1449 894 C ATOM 1244 CD1 ILE A 210 119.005 -13.574 156.374 1.00111.74 C ANISOU 1244 CD1 ILE A 210 12676 18422 11360 -90 967 629 C ATOM 1245 N SER A 211 118.799 -14.216 162.434 1.00116.34 N ANISOU 1245 N SER A 211 13482 20076 10644 -178 1699 725 N ATOM 1246 CA SER A 211 118.919 -15.048 163.632 1.00118.99 C ANISOU 1246 CA SER A 211 13997 20568 10644 -373 1838 916 C ATOM 1247 C SER A 211 118.602 -16.512 163.300 1.00125.19 C ANISOU 1247 C SER A 211 14843 21276 11446 -787 1880 1238 C ATOM 1248 O SER A 211 117.769 -16.774 162.428 1.00125.54 O ANISOU 1248 O SER A 211 14647 21374 11678 -944 1918 1267 O ATOM 1249 CB SER A 211 117.979 -14.544 164.721 1.00126.14 C ANISOU 1249 CB SER A 211 14681 21987 11261 -302 2104 785 C ATOM 1250 OG SER A 211 118.232 -15.187 165.959 1.00137.77 O ANISOU 1250 OG SER A 211 16369 23613 12365 -458 2227 958 O ATOM 1251 N THR A 212 119.276 -17.459 163.982 1.00122.87 N ANISOU 1251 N THR A 212 14887 20842 10958 -958 1850 1475 N ATOM 1252 CA THR A 212 119.088 -18.901 163.778 1.00152.54 C ANISOU 1252 CA THR A 212 18787 24459 14713 -1352 1861 1797 C ATOM 1253 C THR A 212 118.762 -19.614 165.088 1.00184.84 C ANISOU 1253 C THR A 212 23015 28806 18410 -1590 2058 2021 C ATOM 1254 O THR A 212 117.684 -19.416 165.649 1.00150.20 O ANISOU 1254 O THR A 212 18362 24872 13836 -1693 2324 1993 O ATOM 1255 CB THR A 212 120.289 -19.530 163.044 1.00156.34 C ANISOU 1255 CB THR A 212 19592 24416 15396 -1342 1575 1900 C ATOM 1256 OG1 THR A 212 121.511 -19.069 163.624 1.00154.25 O ANISOU 1256 OG1 THR A 212 19574 24011 15022 -1072 1433 1818 O ATOM 1257 CG2 THR A 212 120.282 -19.240 161.548 1.00150.72 C ANISOU 1257 CG2 THR A 212 18725 23480 15062 -1263 1427 1766 C ATOM 1258 N ASN A 224 110.571 -19.213 167.574 1.00181.81 N ANISOU 1258 N ASN A 224 20167 31852 17061 -2720 4015 1849 N ATOM 1259 CA ASN A 224 110.776 -20.655 167.468 1.00181.99 C ANISOU 1259 CA ASN A 224 20534 31536 17078 -3221 3949 2270 C ATOM 1260 C ASN A 224 110.599 -21.137 166.026 1.00182.86 C ANISOU 1260 C ASN A 224 20559 31283 17635 -3379 3730 2315 C ATOM 1261 O ASN A 224 111.545 -21.679 165.455 1.00178.86 O ANISOU 1261 O ASN A 224 20457 30197 17306 -3399 3449 2460 O ATOM 1262 CB ASN A 224 109.853 -21.415 168.430 1.00189.37 C ANISOU 1262 CB ASN A 224 21372 32939 17641 -3725 4305 2537 C ATOM 1263 N TRP A 225 109.402 -20.926 165.436 1.00181.10 N ANISOU 1263 N TRP A 225 19806 31419 17587 -3473 3850 2172 N ATOM 1264 CA TRP A 225 109.101 -21.318 164.057 1.00178.87 C ANISOU 1264 CA TRP A 225 19387 30867 17708 -3621 3650 2181 C ATOM 1265 C TRP A 225 109.463 -20.216 163.046 1.00175.80 C ANISOU 1265 C TRP A 225 18885 30264 17647 -3099 3392 1851 C ATOM 1266 O TRP A 225 110.042 -20.520 162.000 1.00171.62 O ANISOU 1266 O TRP A 225 18563 29240 17403 -3091 3108 1895 O ATOM 1267 CB TRP A 225 107.631 -21.767 163.902 1.00182.93 C ANISOU 1267 CB TRP A 225 19391 31873 18239 -4044 3886 2224 C ATOM 1268 CG TRP A 225 107.194 -21.911 162.470 1.00182.67 C ANISOU 1268 CG TRP A 225 19123 31666 18616 -4119 3679 2148 C ATOM 1269 CD1 TRP A 225 107.603 -22.861 161.581 1.00183.76 C ANISOU 1269 CD1 TRP A 225 19550 31288 18981 -4407 3440 2349 C ATOM 1270 CD2 TRP A 225 106.337 -21.020 161.740 1.00182.86 C ANISOU 1270 CD2 TRP A 225 18598 32018 18864 -3860 3663 1829 C ATOM 1271 NE1 TRP A 225 107.041 -22.630 160.346 1.00182.34 N ANISOU 1271 NE1 TRP A 225 19034 31112 19135 -4363 3285 2177 N ATOM 1272 CE2 TRP A 225 106.256 -21.507 160.415 1.00185.04 C ANISOU 1272 CE2 TRP A 225 18860 31965 19483 -4029 3411 1868 C ATOM 1273 CE3 TRP A 225 105.615 -19.862 162.081 1.00186.07 C ANISOU 1273 CE3 TRP A 225 18527 32964 19208 -3481 3826 1502 C ATOM 1274 CZ2 TRP A 225 105.480 -20.880 159.431 1.00184.29 C ANISOU 1274 CZ2 TRP A 225 18292 32072 19656 -3845 3309 1613 C ATOM 1275 CZ3 TRP A 225 104.849 -19.240 161.105 1.00187.58 C ANISOU 1275 CZ3 TRP A 225 18252 33336 19685 -3279 3719 1246 C ATOM 1276 CH2 TRP A 225 104.787 -19.748 159.798 1.00186.33 C ANISOU 1276 CH2 TRP A 225 18092 32850 19853 -3466 3460 1313 C ATOM 1277 N GLY A 226 109.106 -18.969 163.368 1.00171.16 N ANISOU 1277 N GLY A 226 17984 30048 17002 -2678 3493 1529 N ATOM 1278 CA GLY A 226 109.340 -17.791 162.536 1.00166.46 C ANISOU 1278 CA GLY A 226 17271 29294 16681 -2169 3270 1210 C ATOM 1279 C GLY A 226 110.790 -17.534 162.175 1.00162.50 C ANISOU 1279 C GLY A 226 17257 28187 16297 -1903 2971 1212 C ATOM 1280 O GLY A 226 111.089 -17.215 161.021 1.00158.54 O ANISOU 1280 O GLY A 226 16774 27356 16107 -1732 2716 1119 O ATOM 1281 N ASN A 227 111.697 -17.679 163.164 1.00156.73 N ANISOU 1281 N ASN A 227 16916 27330 15304 -1879 3000 1321 N ATOM 1282 CA ASN A 227 113.141 -17.488 163.002 1.00151.25 C ANISOU 1282 CA ASN A 227 16677 26111 14679 -1649 2735 1328 C ATOM 1283 C ASN A 227 113.745 -18.553 162.087 1.00150.37 C ANISOU 1283 C ASN A 227 16856 25496 14780 -1913 2516 1570 C ATOM 1284 O ASN A 227 114.521 -18.211 161.189 1.00145.68 O ANISOU 1284 O ASN A 227 16416 24506 14431 -1696 2259 1483 O ATOM 1285 CB ASN A 227 113.849 -17.500 164.365 1.00152.44 C ANISOU 1285 CB ASN A 227 17135 26319 14464 -1591 2829 1392 C ATOM 1286 CG ASN A 227 113.740 -16.223 165.170 1.00171.85 C ANISOU 1286 CG ASN A 227 19442 29106 16747 -1185 2938 1078 C ATOM 1287 OD1 ASN A 227 112.802 -15.427 165.032 1.00166.39 O ANISOU 1287 OD1 ASN A 227 18336 28770 16113 -1004 3055 831 O ATOM 1288 ND2 ASN A 227 114.691 -16.024 166.069 1.00162.34 N ANISOU 1288 ND2 ASN A 227 18573 27797 15312 -1027 2893 1071 N ATOM 1289 N LEU A 228 113.379 -19.836 162.312 1.00147.91 N ANISOU 1289 N LEU A 228 16627 25202 14369 -2385 2618 1868 N ATOM 1290 CA LEU A 228 113.866 -20.976 161.534 1.00145.27 C ANISOU 1290 CA LEU A 228 16586 24394 14215 -2662 2419 2099 C ATOM 1291 C LEU A 228 113.356 -20.987 160.099 1.00145.61 C ANISOU 1291 C LEU A 228 16390 24322 14611 -2705 2277 2005 C ATOM 1292 O LEU A 228 114.125 -21.328 159.198 1.00141.95 O ANISOU 1292 O LEU A 228 16174 23400 14359 -2669 2027 2035 O ATOM 1293 CB LEU A 228 113.582 -22.318 162.232 1.00149.08 C ANISOU 1293 CB LEU A 228 17261 24901 14483 -3163 2557 2448 C ATOM 1294 CG LEU A 228 114.449 -22.652 163.455 1.00154.89 C ANISOU 1294 CG LEU A 228 18418 25545 14888 -3156 2587 2630 C ATOM 1295 CD1 LEU A 228 113.884 -23.835 164.212 1.00159.91 C ANISOU 1295 CD1 LEU A 228 19168 26317 15274 -3673 2779 2974 C ATOM 1296 CD2 LEU A 228 115.894 -22.944 163.063 1.00153.69 C ANISOU 1296 CD2 LEU A 228 18728 24806 14864 -2973 2271 2683 C ATOM 1297 N PHE A 229 112.081 -20.602 159.878 1.00143.10 N ANISOU 1297 N PHE A 229 15585 24439 14347 -2766 2428 1879 N ATOM 1298 CA PHE A 229 111.491 -20.543 158.538 1.00141.19 C ANISOU 1298 CA PHE A 229 15075 24153 14419 -2794 2288 1773 C ATOM 1299 C PHE A 229 112.160 -19.466 157.676 1.00138.47 C ANISOU 1299 C PHE A 229 14764 23559 14289 -2323 2050 1533 C ATOM 1300 O PHE A 229 112.485 -19.739 156.522 1.00135.85 O ANISOU 1300 O PHE A 229 14540 22886 14191 -2344 1825 1542 O ATOM 1301 CB PHE A 229 109.964 -20.344 158.596 1.00147.34 C ANISOU 1301 CB PHE A 229 15291 25506 15184 -2943 2504 1679 C ATOM 1302 CG PHE A 229 109.319 -20.039 157.261 1.00148.42 C ANISOU 1302 CG PHE A 229 15098 25668 15628 -2881 2343 1519 C ATOM 1303 CD1 PHE A 229 109.161 -21.033 156.301 1.00151.68 C ANISOU 1303 CD1 PHE A 229 15563 25842 16227 -3238 2198 1658 C ATOM 1304 CD2 PHE A 229 108.874 -18.756 156.963 1.00150.51 C ANISOU 1304 CD2 PHE A 229 15014 26187 15985 -2456 2319 1222 C ATOM 1305 CE1 PHE A 229 108.575 -20.747 155.062 1.00152.16 C ANISOU 1305 CE1 PHE A 229 15327 25942 16546 -3176 2033 1505 C ATOM 1306 CE2 PHE A 229 108.288 -18.471 155.724 1.00153.08 C ANISOU 1306 CE2 PHE A 229 15053 26535 16576 -2385 2146 1087 C ATOM 1307 CZ PHE A 229 108.141 -19.469 154.784 1.00151.01 C ANISOU 1307 CZ PHE A 229 14838 26061 16480 -2749 2006 1231 C ATOM 1308 N PHE A 230 112.365 -18.257 158.239 1.00132.26 N ANISOU 1308 N PHE A 230 13902 22938 13410 -1913 2100 1321 N ATOM 1309 CA PHE A 230 112.999 -17.120 157.564 1.00127.46 C ANISOU 1309 CA PHE A 230 13345 22104 12979 -1470 1891 1098 C ATOM 1310 C PHE A 230 114.459 -17.406 157.204 1.00126.69 C ANISOU 1310 C PHE A 230 13716 21471 12948 -1413 1672 1190 C ATOM 1311 O PHE A 230 114.906 -16.999 156.133 1.00123.55 O ANISOU 1311 O PHE A 230 13377 20796 12768 -1238 1459 1100 O ATOM 1312 CB PHE A 230 112.876 -15.851 158.421 1.00129.87 C ANISOU 1312 CB PHE A 230 13502 22699 13145 -1084 2005 858 C ATOM 1313 CG PHE A 230 113.405 -14.580 157.803 1.00127.95 C ANISOU 1313 CG PHE A 230 13301 22235 13080 -641 1796 625 C ATOM 1314 CD1 PHE A 230 112.757 -13.988 156.726 1.00130.64 C ANISOU 1314 CD1 PHE A 230 13369 22616 13654 -482 1675 478 C ATOM 1315 CD2 PHE A 230 114.517 -13.941 158.335 1.00127.50 C ANISOU 1315 CD2 PHE A 230 13556 21941 12946 -389 1715 554 C ATOM 1316 CE1 PHE A 230 113.239 -12.803 156.166 1.00129.25 C ANISOU 1316 CE1 PHE A 230 13269 22210 13629 -92 1476 291 C ATOM 1317 CE2 PHE A 230 114.994 -12.753 157.777 1.00127.91 C ANISOU 1317 CE2 PHE A 230 13661 21777 13163 -20 1525 352 C ATOM 1318 CZ PHE A 230 114.357 -12.195 156.694 1.00125.95 C ANISOU 1318 CZ PHE A 230 13174 21540 13142 121 1408 233 C ATOM 1319 N ALA A 231 115.188 -18.122 158.081 1.00122.93 N ANISOU 1319 N ALA A 231 13564 20867 12275 -1562 1723 1372 N ATOM 1320 CA ALA A 231 116.584 -18.501 157.849 1.00119.25 C ANISOU 1320 CA ALA A 231 13523 19931 11855 -1511 1523 1460 C ATOM 1321 C ALA A 231 116.674 -19.569 156.760 1.00121.31 C ANISOU 1321 C ALA A 231 13903 19878 12309 -1777 1373 1607 C ATOM 1322 O ALA A 231 117.467 -19.405 155.833 1.00117.93 O ANISOU 1322 O ALA A 231 13637 19114 12055 -1632 1165 1551 O ATOM 1323 CB ALA A 231 117.229 -18.988 159.139 1.00121.21 C ANISOU 1323 CB ALA A 231 14062 20170 11822 -1576 1607 1609 C ATOM 1324 N SER A 232 115.824 -20.625 156.834 1.00120.22 N ANISOU 1324 N SER A 232 13674 19864 12139 -2172 1480 1781 N ATOM 1325 CA SER A 232 115.761 -21.699 155.835 1.00119.76 C ANISOU 1325 CA SER A 232 13722 19523 12260 -2458 1340 1906 C ATOM 1326 C SER A 232 115.416 -21.147 154.455 1.00122.11 C ANISOU 1326 C SER A 232 13789 19793 12814 -2333 1196 1727 C ATOM 1327 O SER A 232 116.043 -21.548 153.470 1.00119.52 O ANISOU 1327 O SER A 232 13653 19112 12648 -2342 996 1734 O ATOM 1328 CB SER A 232 114.745 -22.762 156.236 1.00127.26 C ANISOU 1328 CB SER A 232 14585 20652 13117 -2929 1498 2113 C ATOM 1329 OG SER A 232 115.242 -23.578 157.282 1.00138.03 O ANISOU 1329 OG SER A 232 16285 21903 14257 -3099 1567 2341 O ATOM 1330 N ALA A 233 114.449 -20.199 154.395 1.00119.75 N ANISOU 1330 N ALA A 233 13086 19874 12541 -2188 1289 1558 N ATOM 1331 CA ALA A 233 114.009 -19.542 153.160 1.00118.31 C ANISOU 1331 CA ALA A 233 12663 19713 12577 -2034 1147 1387 C ATOM 1332 C ALA A 233 115.167 -18.825 152.468 1.00117.86 C ANISOU 1332 C ALA A 233 12838 19313 12630 -1700 940 1278 C ATOM 1333 O ALA A 233 115.310 -18.967 151.254 1.00116.41 O ANISOU 1333 O ALA A 233 12686 18929 12616 -1709 761 1249 O ATOM 1334 CB ALA A 233 112.875 -18.570 153.445 1.00121.31 C ANISOU 1334 CB ALA A 233 12595 20562 12935 -1872 1281 1218 C ATOM 1335 N PHE A 234 116.018 -18.109 153.241 1.00112.00 N ANISOU 1335 N PHE A 234 12267 18509 11778 -1434 966 1223 N ATOM 1336 CA PHE A 234 117.201 -17.415 152.721 1.00107.87 C ANISOU 1336 CA PHE A 234 11967 17678 11341 -1150 792 1128 C ATOM 1337 C PHE A 234 118.221 -18.439 152.202 1.00110.23 C ANISOU 1337 C PHE A 234 12602 17589 11692 -1297 655 1255 C ATOM 1338 O PHE A 234 118.774 -18.246 151.120 1.00107.11 O ANISOU 1338 O PHE A 234 12293 16966 11438 -1198 489 1194 O ATOM 1339 CB PHE A 234 117.832 -16.512 153.802 1.00108.68 C ANISOU 1339 CB PHE A 234 12159 17833 11300 -880 859 1037 C ATOM 1340 CG PHE A 234 119.086 -15.783 153.374 1.00106.42 C ANISOU 1340 CG PHE A 234 12094 17247 11095 -624 691 943 C ATOM 1341 CD1 PHE A 234 120.341 -16.357 153.552 1.00107.26 C ANISOU 1341 CD1 PHE A 234 12517 17075 11161 -656 616 1029 C ATOM 1342 CD2 PHE A 234 119.014 -14.516 152.808 1.00107.15 C ANISOU 1342 CD2 PHE A 234 12072 17337 11301 -356 603 771 C ATOM 1343 CE1 PHE A 234 121.499 -15.684 153.154 1.00105.40 C ANISOU 1343 CE1 PHE A 234 12444 16602 11001 -449 474 935 C ATOM 1344 CE2 PHE A 234 120.175 -13.841 152.416 1.00107.17 C ANISOU 1344 CE2 PHE A 234 12279 17067 11372 -169 459 701 C ATOM 1345 CZ PHE A 234 121.408 -14.433 152.587 1.00103.55 C ANISOU 1345 CZ PHE A 234 12097 16372 10874 -230 405 779 C ATOM 1346 N ALA A 235 118.458 -19.522 152.978 1.00108.71 N ANISOU 1346 N ALA A 235 12605 17327 11373 -1524 724 1429 N ATOM 1347 CA ALA A 235 119.389 -20.601 152.633 1.00107.41 C ANISOU 1347 CA ALA A 235 12772 16793 11247 -1648 592 1547 C ATOM 1348 C ALA A 235 119.028 -21.275 151.297 1.00110.47 C ANISOU 1348 C ALA A 235 13130 17032 11813 -1829 466 1553 C ATOM 1349 O ALA A 235 119.909 -21.423 150.446 1.00107.37 O ANISOU 1349 O ALA A 235 12919 16354 11522 -1738 305 1506 O ATOM 1350 CB ALA A 235 119.455 -21.626 153.760 1.00110.41 C ANISOU 1350 CB ALA A 235 13351 17152 11448 -1870 687 1751 C ATOM 1351 N APHE A 236 117.746 -21.654 151.108 0.50109.66 N ANISOU 1351 N APHE A 236 12782 17144 11740 -2081 539 1592 N ATOM 1352 N BPHE A 236 117.743 -21.653 151.113 0.50109.37 N ANISOU 1352 N BPHE A 236 12744 17108 11702 -2081 540 1592 N ATOM 1353 CA APHE A 236 117.275 -22.301 149.882 0.50110.00 C ANISOU 1353 CA APHE A 236 12773 17081 11940 -2278 413 1583 C ATOM 1354 CA BPHE A 236 117.241 -22.283 149.890 0.50109.60 C ANISOU 1354 CA BPHE A 236 12712 17042 11888 -2279 417 1582 C ATOM 1355 C APHE A 236 117.173 -21.331 148.696 0.50112.62 C ANISOU 1355 C APHE A 236 12930 17454 12407 -2048 290 1402 C ATOM 1356 C BPHE A 236 117.262 -21.309 148.710 0.50112.22 C ANISOU 1356 C BPHE A 236 12896 17389 12354 -2033 287 1401 C ATOM 1357 O APHE A 236 117.382 -21.759 147.560 0.50111.93 O ANISOU 1357 O APHE A 236 12931 17168 12431 -2102 132 1368 O ATOM 1358 O BPHE A 236 117.615 -21.712 147.600 0.50111.23 O ANISOU 1358 O BPHE A 236 12886 17040 12335 -2066 126 1366 O ATOM 1359 CB APHE A 236 115.965 -23.069 150.119 0.50115.44 C ANISOU 1359 CB APHE A 236 13254 17993 12613 -2662 523 1690 C ATOM 1360 CB BPHE A 236 115.824 -22.860 150.106 0.50114.84 C ANISOU 1360 CB BPHE A 236 13114 17982 12539 -2632 537 1666 C ATOM 1361 CG APHE A 236 116.170 -24.409 150.792 0.50118.90 C ANISOU 1361 CG APHE A 236 13978 18232 12967 -2985 558 1905 C ATOM 1362 CG BPHE A 236 115.034 -23.167 148.851 0.50116.88 C ANISOU 1362 CG BPHE A 236 13186 18261 12960 -2803 414 1602 C ATOM 1363 CD1APHE A 236 116.364 -25.562 150.039 0.50122.39 C ANISOU 1363 CD1APHE A 236 14648 18338 13517 -3214 400 1967 C ATOM 1364 CD1BPHE A 236 115.339 -24.275 148.068 0.50119.75 C ANISOU 1364 CD1BPHE A 236 13789 18296 13414 -3021 258 1653 C ATOM 1365 CD2APHE A 236 116.182 -24.516 152.178 0.50122.60 C ANISOU 1365 CD2APHE A 236 14515 18833 13236 -3052 737 2046 C ATOM 1366 CD2BPHE A 236 113.975 -22.354 148.460 0.50119.66 C ANISOU 1366 CD2BPHE A 236 13126 18967 13371 -2732 438 1476 C ATOM 1367 CE1APHE A 236 116.567 -26.797 150.661 0.50125.47 C ANISOU 1367 CE1APHE A 236 15344 18493 13837 -3501 406 2174 C ATOM 1368 CE1BPHE A 236 114.611 -24.553 146.908 0.50121.50 C ANISOU 1368 CE1BPHE A 236 13847 18546 13772 -3181 129 1576 C ATOM 1369 CE2APHE A 236 116.382 -25.753 152.799 0.50127.58 C ANISOU 1369 CE2APHE A 236 15449 19251 13774 -3352 750 2273 C ATOM 1370 CE2BPHE A 236 113.246 -22.636 147.302 0.50123.24 C ANISOU 1370 CE2BPHE A 236 13404 19456 13964 -2884 300 1411 C ATOM 1371 CZ APHE A 236 116.573 -26.884 152.037 0.50126.20 C ANISOU 1371 CZ APHE A 236 15513 18709 13729 -3573 578 2341 C ATOM 1372 CZ BPHE A 236 113.568 -23.733 146.535 0.50121.31 C ANISOU 1372 CZ BPHE A 236 13407 18890 13796 -3119 148 1462 C ATOM 1373 N LEU A 237 116.887 -20.034 148.955 1.00108.45 N ANISOU 1373 N LEU A 237 12182 17166 11857 -1782 352 1285 N ATOM 1374 CA LEU A 237 116.826 -18.968 147.932 1.00106.42 C ANISOU 1374 CA LEU A 237 11794 16931 11711 -1531 225 1133 C ATOM 1375 C LEU A 237 118.217 -18.702 147.338 1.00106.73 C ANISOU 1375 C LEU A 237 12127 16643 11782 -1342 91 1094 C ATOM 1376 O LEU A 237 118.339 -18.468 146.137 1.00105.80 O ANISOU 1376 O LEU A 237 12018 16425 11756 -1279 -54 1030 O ATOM 1377 CB LEU A 237 116.265 -17.674 148.547 1.00107.20 C ANISOU 1377 CB LEU A 237 11635 17325 11770 -1276 321 1021 C ATOM 1378 CG LEU A 237 114.945 -17.132 147.996 1.00113.98 C ANISOU 1378 CG LEU A 237 12117 18478 12714 -1236 292 923 C ATOM 1379 CD1 LEU A 237 113.784 -18.081 148.271 1.00117.42 C ANISOU 1379 CD1 LEU A 237 12302 19182 13130 -1573 408 997 C ATOM 1380 CD2 LEU A 237 114.633 -15.785 148.610 1.00116.95 C ANISOU 1380 CD2 LEU A 237 12312 19063 13061 -898 350 783 C ATOM 1381 N GLY A 238 119.238 -18.773 148.190 1.00101.36 N ANISOU 1381 N GLY A 238 11674 15824 11014 -1268 141 1136 N ATOM 1382 CA GLY A 238 120.634 -18.588 147.824 1.00 98.42 C ANISOU 1382 CA GLY A 238 11556 15179 10660 -1108 38 1099 C ATOM 1383 C GLY A 238 121.193 -19.757 147.040 1.00101.91 C ANISOU 1383 C GLY A 238 12204 15363 11156 -1264 -73 1144 C ATOM 1384 O GLY A 238 121.943 -19.544 146.090 1.00100.33 O ANISOU 1384 O GLY A 238 12099 15009 11013 -1159 -185 1071 O ATOM 1385 N LEU A 239 120.851 -21.002 147.431 1.00100.14 N ANISOU 1385 N LEU A 239 12060 15085 10904 -1518 -42 1261 N ATOM 1386 CA LEU A 239 121.319 -22.202 146.729 1.00 99.90 C ANISOU 1386 CA LEU A 239 12249 14780 10930 -1666 -161 1291 C ATOM 1387 C LEU A 239 120.621 -22.351 145.371 1.00104.59 C ANISOU 1387 C LEU A 239 12721 15391 11627 -1773 -266 1218 C ATOM 1388 O LEU A 239 121.238 -22.848 144.424 1.00103.47 O ANISOU 1388 O LEU A 239 12743 15037 11535 -1766 -392 1158 O ATOM 1389 CB LEU A 239 121.149 -23.472 147.578 1.00102.06 C ANISOU 1389 CB LEU A 239 12684 14949 11146 -1916 -117 1451 C ATOM 1390 CG LEU A 239 122.031 -23.603 148.828 1.00106.71 C ANISOU 1390 CG LEU A 239 13488 15443 11615 -1815 -68 1538 C ATOM 1391 CD1 LEU A 239 121.549 -24.733 149.702 1.00109.65 C ANISOU 1391 CD1 LEU A 239 13985 15775 11903 -2099 -4 1733 C ATOM 1392 CD2 LEU A 239 123.497 -23.830 148.471 1.00107.50 C ANISOU 1392 CD2 LEU A 239 13846 15250 11749 -1625 -206 1473 C ATOM 1393 N LEU A 240 119.352 -21.890 145.268 1.00102.26 N ANISOU 1393 N LEU A 240 12128 15371 11356 -1852 -220 1206 N ATOM 1394 CA LEU A 240 118.602 -21.912 144.013 1.00102.94 C ANISOU 1394 CA LEU A 240 12064 15521 11528 -1938 -337 1131 C ATOM 1395 C LEU A 240 119.262 -20.970 143.011 1.00104.37 C ANISOU 1395 C LEU A 240 12278 15648 11730 -1676 -444 1016 C ATOM 1396 O LEU A 240 119.365 -21.317 141.835 1.00104.03 O ANISOU 1396 O LEU A 240 12300 15503 11724 -1721 -578 954 O ATOM 1397 CB LEU A 240 117.131 -21.523 144.217 1.00105.31 C ANISOU 1397 CB LEU A 240 12000 16168 11846 -2037 -269 1132 C ATOM 1398 CG LEU A 240 116.213 -21.828 143.033 1.00112.00 C ANISOU 1398 CG LEU A 240 12675 17102 12779 -2194 -405 1070 C ATOM 1399 CD1 LEU A 240 115.671 -23.256 143.108 1.00115.15 C ANISOU 1399 CD1 LEU A 240 13110 17435 13207 -2590 -410 1150 C ATOM 1400 CD2 LEU A 240 115.075 -20.825 142.950 1.00115.72 C ANISOU 1400 CD2 LEU A 240 12761 17932 13275 -2084 -387 1004 C ATOM 1401 N ALA A 241 119.729 -19.795 143.488 1.00 98.99 N ANISOU 1401 N ALA A 241 11572 15028 11013 -1419 -386 988 N ATOM 1402 CA ALA A 241 120.418 -18.801 142.669 1.00 96.95 C ANISOU 1402 CA ALA A 241 11365 14708 10762 -1191 -470 907 C ATOM 1403 C ALA A 241 121.686 -19.404 142.063 1.00 99.73 C ANISOU 1403 C ALA A 241 11985 14805 11102 -1183 -537 880 C ATOM 1404 O ALA A 241 121.878 -19.288 140.849 1.00 99.32 O ANISOU 1404 O ALA A 241 11972 14706 11057 -1153 -641 819 O ATOM 1405 CB ALA A 241 120.758 -17.572 143.498 1.00 96.70 C ANISOU 1405 CB ALA A 241 11293 14751 10700 -958 -391 888 C ATOM 1406 N LEU A 242 122.505 -20.108 142.888 1.00 95.11 N ANISOU 1406 N LEU A 242 11580 14071 10489 -1209 -482 923 N ATOM 1407 CA LEU A 242 123.748 -20.753 142.448 1.00 93.72 C ANISOU 1407 CA LEU A 242 11637 13666 10305 -1171 -543 878 C ATOM 1408 C LEU A 242 123.498 -21.899 141.473 1.00 98.29 C ANISOU 1408 C LEU A 242 12302 14126 10918 -1341 -648 842 C ATOM 1409 O LEU A 242 124.242 -22.032 140.503 1.00 97.56 O ANISOU 1409 O LEU A 242 12314 13936 10817 -1273 -724 746 O ATOM 1410 CB LEU A 242 124.610 -21.239 143.627 1.00 93.76 C ANISOU 1410 CB LEU A 242 11805 13546 10272 -1131 -488 932 C ATOM 1411 CG LEU A 242 124.909 -20.259 144.771 1.00 97.69 C ANISOU 1411 CG LEU A 242 12250 14150 10717 -981 -391 959 C ATOM 1412 CD1 LEU A 242 125.787 -20.905 145.821 1.00 98.02 C ANISOU 1412 CD1 LEU A 242 12478 14059 10705 -951 -375 1012 C ATOM 1413 CD2 LEU A 242 125.558 -18.997 144.274 1.00 98.69 C ANISOU 1413 CD2 LEU A 242 12333 14315 10851 -787 -407 869 C ATOM 1414 N THR A 243 122.444 -22.703 141.706 1.00 96.11 N ANISOU 1414 N THR A 243 11975 13869 10672 -1572 -650 908 N ATOM 1415 CA THR A 243 122.086 -23.824 140.831 1.00 97.44 C ANISOU 1415 CA THR A 243 12229 13911 10883 -1769 -766 866 C ATOM 1416 C THR A 243 121.626 -23.321 139.454 1.00100.82 C ANISOU 1416 C THR A 243 12533 14457 11315 -1752 -867 762 C ATOM 1417 O THR A 243 122.026 -23.899 138.443 1.00100.79 O ANISOU 1417 O THR A 243 12670 14321 11305 -1771 -975 661 O ATOM 1418 CB THR A 243 121.088 -24.763 141.525 1.00109.21 C ANISOU 1418 CB THR A 243 13687 15402 12406 -2060 -736 979 C ATOM 1419 OG1 THR A 243 121.563 -25.051 142.845 1.00109.30 O ANISOU 1419 OG1 THR A 243 13824 15328 12375 -2049 -638 1097 O ATOM 1420 CG2 THR A 243 120.879 -26.069 140.763 1.00108.82 C ANISOU 1420 CG2 THR A 243 13792 15145 12411 -2284 -872 935 C ATOM 1421 N VAL A 244 120.833 -22.227 139.415 1.00 96.97 N ANISOU 1421 N VAL A 244 11800 14218 10827 -1692 -842 780 N ATOM 1422 CA VAL A 244 120.349 -21.598 138.175 1.00 97.05 C ANISOU 1422 CA VAL A 244 11692 14358 10825 -1646 -954 706 C ATOM 1423 C VAL A 244 121.535 -20.991 137.372 1.00 99.63 C ANISOU 1423 C VAL A 244 12173 14600 11082 -1444 -987 637 C ATOM 1424 O VAL A 244 121.562 -21.105 136.142 1.00100.70 O ANISOU 1424 O VAL A 244 12361 14730 11172 -1459 -1100 558 O ATOM 1425 CB VAL A 244 119.183 -20.598 138.449 1.00101.50 C ANISOU 1425 CB VAL A 244 11955 15196 11413 -1598 -932 743 C ATOM 1426 CG1 VAL A 244 118.967 -19.619 137.299 1.00100.96 C ANISOU 1426 CG1 VAL A 244 11814 15234 11313 -1447 -1054 690 C ATOM 1427 CG2 VAL A 244 117.889 -21.343 138.758 1.00103.92 C ANISOU 1427 CG2 VAL A 244 12065 15640 11779 -1854 -934 774 C ATOM 1428 N THR A 245 122.528 -20.409 138.078 1.00 93.23 N ANISOU 1428 N THR A 245 11436 13737 10251 -1276 -887 664 N ATOM 1429 CA THR A 245 123.734 -19.825 137.481 1.00 90.99 C ANISOU 1429 CA THR A 245 11277 13392 9904 -1116 -887 610 C ATOM 1430 C THR A 245 124.617 -20.922 136.858 1.00 95.51 C ANISOU 1430 C THR A 245 12045 13799 10445 -1154 -927 513 C ATOM 1431 O THR A 245 124.966 -20.800 135.680 1.00 95.65 O ANISOU 1431 O THR A 245 12120 13836 10388 -1121 -985 434 O ATOM 1432 CB THR A 245 124.464 -18.904 138.493 1.00 89.31 C ANISOU 1432 CB THR A 245 11061 13180 9694 -957 -779 655 C ATOM 1433 OG1 THR A 245 123.671 -17.731 138.686 1.00 86.18 O ANISOU 1433 OG1 THR A 245 10497 12932 9315 -886 -773 704 O ATOM 1434 CG2 THR A 245 125.862 -18.491 138.027 1.00 82.79 C ANISOU 1434 CG2 THR A 245 10355 12291 8811 -837 -764 600 C ATOM 1435 N APHE A 246 124.967 -21.973 137.636 0.50 92.56 N ANISOU 1435 N APHE A 246 11784 13269 10115 -1211 -903 517 N ATOM 1436 N BPHE A 246 124.947 -21.982 137.633 0.50 92.07 N ANISOU 1436 N BPHE A 246 11721 13207 10054 -1213 -904 518 N ATOM 1437 CA APHE A 246 125.789 -23.099 137.175 0.50 92.74 C ANISOU 1437 CA APHE A 246 12006 13105 10127 -1211 -957 408 C ATOM 1438 CA BPHE A 246 125.783 -23.113 137.203 0.50 92.00 C ANISOU 1438 CA BPHE A 246 11912 13009 10034 -1212 -956 410 C ATOM 1439 C APHE A 246 125.156 -23.812 135.977 0.50 96.71 C ANISOU 1439 C APHE A 246 12545 13587 10613 -1349 -1082 313 C ATOM 1440 C BPHE A 246 125.170 -23.897 136.039 0.50 96.42 C ANISOU 1440 C BPHE A 246 12517 13536 10581 -1353 -1082 314 C ATOM 1441 O APHE A 246 125.871 -24.148 135.032 0.50 96.40 O ANISOU 1441 O APHE A 246 12620 13499 10509 -1283 -1129 175 O ATOM 1442 O BPHE A 246 125.908 -24.345 135.162 0.50 96.17 O ANISOU 1442 O BPHE A 246 12612 13436 10491 -1289 -1130 174 O ATOM 1443 CB APHE A 246 126.083 -24.102 138.321 0.50 95.24 C ANISOU 1443 CB APHE A 246 12456 13231 10502 -1244 -938 459 C ATOM 1444 CB BPHE A 246 126.108 -24.066 138.375 0.50 94.14 C ANISOU 1444 CB BPHE A 246 12315 13092 10362 -1237 -933 462 C ATOM 1445 CG APHE A 246 126.395 -25.513 137.859 0.50 98.71 C ANISOU 1445 CG APHE A 246 13106 13435 10964 -1299 -1042 357 C ATOM 1446 CG BPHE A 246 126.787 -23.493 139.602 0.50 94.26 C ANISOU 1446 CG BPHE A 246 12317 13123 10373 -1099 -832 541 C ATOM 1447 CD1APHE A 246 127.640 -25.831 137.327 0.50101.66 C ANISOU 1447 CD1APHE A 246 13611 13715 11302 -1123 -1069 206 C ATOM 1448 CD1BPHE A 246 127.590 -22.359 139.513 0.50 95.48 C ANISOU 1448 CD1BPHE A 246 12407 13386 10486 -924 -775 505 C ATOM 1449 CD2APHE A 246 125.423 -26.509 137.904 0.50103.11 C ANISOU 1449 CD2APHE A 246 13725 13870 11580 -1530 -1119 396 C ATOM 1450 CD2BPHE A 246 126.661 -24.114 140.839 0.50 97.17 C ANISOU 1450 CD2BPHE A 246 12758 13394 10768 -1158 -803 651 C ATOM 1451 CE1APHE A 246 127.917 -27.125 136.873 0.50104.49 C ANISOU 1451 CE1APHE A 246 14173 13842 11684 -1137 -1180 81 C ATOM 1452 CE1BPHE A 246 128.216 -21.836 140.644 0.50 95.43 C ANISOU 1452 CE1BPHE A 246 12389 13393 10475 -807 -701 557 C ATOM 1453 CE2APHE A 246 125.697 -27.800 137.439 0.50107.75 C ANISOU 1453 CE2APHE A 246 14541 14199 12198 -1578 -1239 288 C ATOM 1454 CE2BPHE A 246 127.290 -23.590 141.971 0.50 98.91 C ANISOU 1454 CE2BPHE A 246 12976 13643 10961 -1025 -725 712 C ATOM 1455 CZ APHE A 246 126.943 -28.100 136.931 0.50105.58 C ANISOU 1455 CZ APHE A 246 14410 13817 11889 -1361 -1274 123 C ATOM 1456 CZ BPHE A 246 128.067 -22.459 141.864 0.50 95.32 C ANISOU 1456 CZ BPHE A 246 12442 13298 10477 -846 -681 652 C ATOM 1457 N SER A 247 123.833 -24.066 136.032 1.00 93.89 N ANISOU 1457 N SER A 247 12081 13286 10308 -1543 -1134 372 N ATOM 1458 CA SER A 247 123.109 -24.771 134.958 1.00 95.87 C ANISOU 1458 CA SER A 247 12351 13524 10551 -1707 -1275 277 C ATOM 1459 C SER A 247 123.159 -24.004 133.633 1.00 98.65 C ANISOU 1459 C SER A 247 12654 14038 10790 -1617 -1339 193 C ATOM 1460 O SER A 247 123.623 -24.559 132.638 1.00 99.15 O ANISOU 1460 O SER A 247 12856 14036 10780 -1614 -1421 48 O ATOM 1461 CB SER A 247 121.671 -25.083 135.366 1.00101.29 C ANISOU 1461 CB SER A 247 12878 14288 11321 -1947 -1309 365 C ATOM 1462 OG SER A 247 121.643 -25.903 136.523 1.00112.39 O ANISOU 1462 OG SER A 247 14363 15537 12802 -2068 -1248 460 O ATOM 1463 N CYS A 248 122.771 -22.716 133.645 1.00 93.72 N ANISOU 1463 N CYS A 248 11859 13613 10139 -1527 -1302 283 N ATOM 1464 CA CYS A 248 122.783 -21.858 132.463 1.00 93.88 C ANISOU 1464 CA CYS A 248 11852 13781 10038 -1442 -1368 250 C ATOM 1465 C CYS A 248 124.185 -21.616 131.900 1.00 97.88 C ANISOU 1465 C CYS A 248 12517 14247 10426 -1298 -1309 177 C ATOM 1466 O CYS A 248 124.336 -21.563 130.677 1.00 99.61 O ANISOU 1466 O CYS A 248 12802 14537 10509 -1293 -1382 95 O ATOM 1467 CB CYS A 248 122.054 -20.549 132.733 1.00 93.68 C ANISOU 1467 CB CYS A 248 11631 13931 10030 -1364 -1360 372 C ATOM 1468 SG CYS A 248 120.304 -20.751 133.139 1.00 99.50 S ANISOU 1468 SG CYS A 248 12110 14816 10878 -1522 -1443 419 S ATOM 1469 N ASN A 249 125.202 -21.479 132.772 1.00 91.78 N ANISOU 1469 N ASN A 249 11794 13387 9690 -1190 -1178 202 N ATOM 1470 CA ASN A 249 126.580 -21.274 132.333 1.00 90.79 C ANISOU 1470 CA ASN A 249 11776 13255 9466 -1066 -1105 123 C ATOM 1471 C ASN A 249 127.152 -22.538 131.682 1.00 97.17 C ANISOU 1471 C ASN A 249 12737 13959 10225 -1076 -1149 -61 C ATOM 1472 O ASN A 249 127.809 -22.433 130.646 1.00 97.67 O ANISOU 1472 O ASN A 249 12861 14106 10143 -1023 -1140 -167 O ATOM 1473 CB ASN A 249 127.460 -20.778 133.471 1.00 89.66 C ANISOU 1473 CB ASN A 249 11614 13067 9385 -952 -977 185 C ATOM 1474 CG ASN A 249 127.315 -19.307 133.807 1.00109.21 C ANISOU 1474 CG ASN A 249 13983 15649 11862 -894 -928 317 C ATOM 1475 OD1 ASN A 249 126.490 -18.575 133.252 1.00 98.95 O ANISOU 1475 OD1 ASN A 249 12617 14451 10529 -920 -993 383 O ATOM 1476 ND2 ASN A 249 128.132 -18.834 134.736 1.00102.44 N ANISOU 1476 ND2 ASN A 249 13117 14757 11047 -803 -829 348 N ATOM 1477 N LEU A 250 126.854 -23.731 132.246 1.00 94.90 N ANISOU 1477 N LEU A 250 12522 13488 10048 -1150 -1201 -101 N ATOM 1478 CA LEU A 250 127.301 -25.009 131.676 1.00 96.22 C ANISOU 1478 CA LEU A 250 12863 13503 10193 -1148 -1274 -292 C ATOM 1479 C LEU A 250 126.627 -25.247 130.337 1.00100.68 C ANISOU 1479 C LEU A 250 13454 14150 10647 -1250 -1399 -403 C ATOM 1480 O LEU A 250 127.282 -25.722 129.412 1.00102.25 O ANISOU 1480 O LEU A 250 13771 14349 10730 -1180 -1423 -591 O ATOM 1481 CB LEU A 250 127.051 -26.192 132.639 1.00 97.35 C ANISOU 1481 CB LEU A 250 13112 13389 10489 -1229 -1324 -275 C ATOM 1482 CG LEU A 250 127.316 -27.618 132.110 1.00104.63 C ANISOU 1482 CG LEU A 250 14251 14083 11422 -1243 -1443 -472 C ATOM 1483 CD1 LEU A 250 128.793 -27.850 131.812 1.00104.89 C ANISOU 1483 CD1 LEU A 250 14388 14074 11392 -998 -1394 -646 C ATOM 1484 CD2 LEU A 250 126.805 -28.660 133.077 1.00108.81 C ANISOU 1484 CD2 LEU A 250 14893 14347 12104 -1389 -1512 -391 C ATOM 1485 N ALA A 251 125.329 -24.892 130.228 1.00 96.20 N ANISOU 1485 N ALA A 251 12765 13681 10106 -1401 -1480 -300 N ATOM 1486 CA ALA A 251 124.541 -25.031 129.005 1.00 97.12 C ANISOU 1486 CA ALA A 251 12880 13904 10117 -1507 -1629 -388 C ATOM 1487 C ALA A 251 125.091 -24.123 127.906 1.00 99.57 C ANISOU 1487 C ALA A 251 13197 14421 10213 -1391 -1601 -418 C ATOM 1488 O ALA A 251 125.173 -24.550 126.754 1.00100.78 O ANISOU 1488 O ALA A 251 13450 14628 10213 -1409 -1690 -575 O ATOM 1489 CB ALA A 251 123.085 -24.702 129.281 1.00 98.29 C ANISOU 1489 CB ALA A 251 12842 14148 10354 -1665 -1714 -257 C ATOM 1490 N THR A 252 125.507 -22.892 128.273 1.00 93.30 N ANISOU 1490 N THR A 252 12317 13734 9398 -1284 -1479 -269 N ATOM 1491 CA THR A 252 126.077 -21.911 127.348 1.00 92.88 C ANISOU 1491 CA THR A 252 12285 13862 9144 -1204 -1435 -248 C ATOM 1492 C THR A 252 127.403 -22.397 126.763 1.00 97.79 C ANISOU 1492 C THR A 252 13037 14491 9627 -1117 -1342 -426 C ATOM 1493 O THR A 252 127.551 -22.386 125.538 1.00 99.79 O ANISOU 1493 O THR A 252 13367 14885 9666 -1124 -1378 -521 O ATOM 1494 CB THR A 252 126.184 -20.542 128.020 1.00 98.91 C ANISOU 1494 CB THR A 252 12943 14684 9955 -1136 -1343 -44 C ATOM 1495 OG1 THR A 252 124.875 -20.125 128.409 1.00101.63 O ANISOU 1495 OG1 THR A 252 13152 15056 10405 -1189 -1444 80 O ATOM 1496 CG2 THR A 252 126.822 -19.488 127.120 1.00 95.84 C ANISOU 1496 CG2 THR A 252 12604 14449 9362 -1087 -1295 12 C ATOM 1497 N ILE A 253 128.355 -22.829 127.630 1.00 92.43 N ANISOU 1497 N ILE A 253 12378 13683 9059 -1025 -1229 -480 N ATOM 1498 CA ILE A 253 129.675 -23.325 127.215 1.00 92.29 C ANISOU 1498 CA ILE A 253 12441 13686 8937 -905 -1134 -673 C ATOM 1499 C ILE A 253 129.512 -24.521 126.278 1.00 98.50 C ANISOU 1499 C ILE A 253 13367 14423 9637 -921 -1250 -914 C ATOM 1500 O ILE A 253 130.103 -24.523 125.196 1.00100.20 O ANISOU 1500 O ILE A 253 13637 14795 9639 -866 -1209 -1069 O ATOM 1501 CB ILE A 253 130.656 -23.601 128.395 1.00 93.54 C ANISOU 1501 CB ILE A 253 12575 13717 9248 -779 -1025 -686 C ATOM 1502 CG1 ILE A 253 130.807 -22.364 129.308 1.00 91.13 C ANISOU 1502 CG1 ILE A 253 12141 13461 9022 -774 -927 -464 C ATOM 1503 CG2 ILE A 253 132.028 -24.030 127.853 1.00 95.64 C ANISOU 1503 CG2 ILE A 253 12877 14070 9394 -631 -925 -902 C ATOM 1504 CD1 ILE A 253 131.432 -22.633 130.699 1.00 90.54 C ANISOU 1504 CD1 ILE A 253 12039 13234 9127 -682 -872 -435 C ATOM 1505 N LYS A 254 128.651 -25.487 126.659 1.00 94.83 N ANISOU 1505 N LYS A 254 12958 13750 9322 -1016 -1395 -944 N ATOM 1506 CA LYS A 254 128.342 -26.666 125.853 1.00 96.96 C ANISOU 1506 CA LYS A 254 13379 13921 9541 -1061 -1541 -1174 C ATOM 1507 C LYS A 254 127.845 -26.264 124.463 1.00102.04 C ANISOU 1507 C LYS A 254 14033 14794 9945 -1133 -1622 -1229 C ATOM 1508 O LYS A 254 128.216 -26.909 123.479 1.00103.60 O ANISOU 1508 O LYS A 254 14358 15029 9978 -1086 -1665 -1473 O ATOM 1509 CB LYS A 254 127.287 -27.535 126.547 1.00100.01 C ANISOU 1509 CB LYS A 254 13804 14055 10142 -1222 -1687 -1134 C ATOM 1510 CG LYS A 254 127.849 -28.496 127.581 1.00112.68 C ANISOU 1510 CG LYS A 254 15519 15364 11929 -1148 -1671 -1178 C ATOM 1511 CD LYS A 254 127.057 -29.807 127.607 1.00126.91 C ANISOU 1511 CD LYS A 254 17478 16885 13856 -1313 -1857 -1270 C ATOM 1512 CE LYS A 254 125.894 -29.796 128.572 1.00138.65 C ANISOU 1512 CE LYS A 254 18868 18293 15519 -1544 -1899 -1038 C ATOM 1513 NZ LYS A 254 125.128 -31.068 128.515 1.00150.64 N ANISOU 1513 NZ LYS A 254 20540 19547 17148 -1756 -2081 -1125 N ATOM 1514 N ALA A 255 127.025 -25.183 124.389 1.00 98.03 N ANISOU 1514 N ALA A 255 13398 14443 9405 -1225 -1650 -1011 N ATOM 1515 CA ALA A 255 126.447 -24.664 123.140 1.00 99.42 C ANISOU 1515 CA ALA A 255 13583 14843 9348 -1288 -1753 -1012 C ATOM 1516 C ALA A 255 127.458 -23.914 122.281 1.00104.24 C ANISOU 1516 C ALA A 255 14236 15685 9686 -1187 -1614 -1027 C ATOM 1517 O ALA A 255 127.383 -24.015 121.061 1.00106.34 O ANISOU 1517 O ALA A 255 14593 16116 9696 -1209 -1684 -1140 O ATOM 1518 CB ALA A 255 125.241 -23.791 123.428 1.00 99.11 C ANISOU 1518 CB ALA A 255 13394 14874 9389 -1384 -1849 -775 C ATOM 1519 N LEU A 256 128.422 -23.197 122.906 1.00 99.37 N ANISOU 1519 N LEU A 256 13556 15092 9110 -1095 -1417 -918 N ATOM 1520 CA LEU A 256 129.488 -22.474 122.193 1.00 99.67 C ANISOU 1520 CA LEU A 256 13612 15356 8903 -1036 -1252 -919 C ATOM 1521 C LEU A 256 130.399 -23.459 121.454 1.00106.85 C ANISOU 1521 C LEU A 256 14618 16331 9648 -945 -1189 -1230 C ATOM 1522 O LEU A 256 130.899 -23.141 120.380 1.00108.01 O ANISOU 1522 O LEU A 256 14813 16727 9500 -942 -1111 -1292 O ATOM 1523 CB LEU A 256 130.315 -21.593 123.147 1.00 97.20 C ANISOU 1523 CB LEU A 256 13190 15031 8710 -983 -1070 -752 C ATOM 1524 CG LEU A 256 129.628 -20.339 123.687 1.00100.11 C ANISOU 1524 CG LEU A 256 13480 15392 9163 -1043 -1098 -454 C ATOM 1525 CD1 LEU A 256 130.248 -19.905 124.997 1.00 98.17 C ANISOU 1525 CD1 LEU A 256 13134 15037 9131 -985 -968 -350 C ATOM 1526 CD2 LEU A 256 129.670 -19.201 122.685 1.00103.41 C ANISOU 1526 CD2 LEU A 256 13954 16023 9317 -1101 -1079 -315 C ATOM 1527 N VAL A 257 130.590 -24.663 122.021 1.00104.68 N ANISOU 1527 N VAL A 257 14384 15834 9554 -866 -1227 -1426 N ATOM 1528 CA VAL A 257 131.388 -25.735 121.418 1.00107.12 C ANISOU 1528 CA VAL A 257 14795 16155 9749 -736 -1201 -1762 C ATOM 1529 C VAL A 257 130.593 -26.304 120.234 1.00114.45 C ANISOU 1529 C VAL A 257 15865 17136 10486 -815 -1380 -1931 C ATOM 1530 O VAL A 257 131.172 -26.567 119.184 1.00117.21 O ANISOU 1530 O VAL A 257 16290 17681 10563 -745 -1330 -2153 O ATOM 1531 CB VAL A 257 131.781 -26.824 122.464 1.00110.39 C ANISOU 1531 CB VAL A 257 15242 16260 10439 -610 -1223 -1896 C ATOM 1532 CG1 VAL A 257 132.576 -27.963 121.823 1.00113.22 C ANISOU 1532 CG1 VAL A 257 15723 16601 10694 -436 -1228 -2274 C ATOM 1533 CG2 VAL A 257 132.572 -26.216 123.618 1.00107.49 C ANISOU 1533 CG2 VAL A 257 14732 15874 10233 -526 -1062 -1736 C ATOM 1534 N SER A 258 129.263 -26.436 120.395 1.00111.08 N ANISOU 1534 N SER A 258 15453 16565 10186 -969 -1585 -1825 N ATOM 1535 CA SER A 258 128.349 -26.956 119.379 1.00113.71 C ANISOU 1535 CA SER A 258 15897 16931 10375 -1076 -1799 -1966 C ATOM 1536 C SER A 258 128.099 -26.010 118.206 1.00119.40 C ANISOU 1536 C SER A 258 16624 17984 10758 -1132 -1812 -1881 C ATOM 1537 O SER A 258 127.644 -26.474 117.160 1.00122.23 O ANISOU 1537 O SER A 258 17097 18431 10911 -1180 -1966 -2060 O ATOM 1538 CB SER A 258 127.025 -27.369 120.011 1.00117.37 C ANISOU 1538 CB SER A 258 16328 17167 11101 -1243 -2003 -1864 C ATOM 1539 OG SER A 258 127.108 -28.688 120.523 1.00129.59 O ANISOU 1539 OG SER A 258 17985 18400 12853 -1233 -2078 -2057 O ATOM 1540 N ARG A 259 128.404 -24.700 118.363 1.00114.52 N ANISOU 1540 N ARG A 259 15907 17537 10070 -1130 -1667 -1610 N ATOM 1541 CA ARG A 259 128.208 -23.671 117.333 1.00115.76 C ANISOU 1541 CA ARG A 259 16096 17982 9906 -1189 -1679 -1467 C ATOM 1542 C ARG A 259 128.689 -24.120 115.945 1.00125.26 C ANISOU 1542 C ARG A 259 17449 19421 10723 -1157 -1665 -1726 C ATOM 1543 O ARG A 259 129.743 -24.750 115.822 1.00125.99 O ANISOU 1543 O ARG A 259 17573 19544 10752 -1041 -1511 -1972 O ATOM 1544 CB ARG A 259 128.828 -22.313 117.751 1.00112.59 C ANISOU 1544 CB ARG A 259 15605 17682 9491 -1180 -1484 -1176 C ATOM 1545 CG ARG A 259 130.276 -22.086 117.311 1.00122.20 C ANISOU 1545 CG ARG A 259 16840 19111 10480 -1116 -1223 -1259 C ATOM 1546 CD ARG A 259 130.937 -20.897 117.973 1.00131.56 C ANISOU 1546 CD ARG A 259 17924 20329 11733 -1135 -1039 -990 C ATOM 1547 NE ARG A 259 132.336 -20.769 117.557 1.00142.11 N ANISOU 1547 NE ARG A 259 19240 21895 12860 -1104 -781 -1089 N ATOM 1548 CZ ARG A 259 133.373 -21.313 118.191 1.00155.27 C ANISOU 1548 CZ ARG A 259 20801 23526 14668 -989 -616 -1261 C ATOM 1549 NH1 ARG A 259 134.603 -21.142 117.730 1.00147.48 N ANISOU 1549 NH1 ARG A 259 19760 22804 13473 -970 -381 -1357 N ATOM 1550 NH2 ARG A 259 133.186 -22.030 119.292 1.00136.46 N ANISOU 1550 NH2 ARG A 259 18362 20859 12629 -895 -688 -1336 N ATOM 1551 N GLY A1000 127.880 -23.830 114.931 1.00112.47 N ANISOU 1551 N GLY A1000 14132 18820 9783 -650 -3279 1203 N ATOM 1552 CA GLY A1000 128.192 -24.155 113.547 1.00112.79 C ANISOU 1552 CA GLY A1000 14033 18915 9905 -351 -3132 1115 C ATOM 1553 C GLY A1000 129.038 -23.071 112.921 1.00118.26 C ANISOU 1553 C GLY A1000 14263 20067 10603 -548 -2972 1082 C ATOM 1554 O GLY A1000 129.727 -22.323 113.625 1.00118.87 O ANISOU 1554 O GLY A1000 14072 20452 10643 -824 -3074 1140 O ATOM 1555 N SER A1001 128.982 -22.976 111.589 1.00116.14 N ANISOU 1555 N SER A1001 13921 19855 10352 -463 -2748 1014 N ATOM 1556 CA SER A1001 129.698 -21.959 110.823 1.00118.27 C ANISOU 1556 CA SER A1001 13779 20577 10580 -740 -2578 1054 C ATOM 1557 C SER A1001 129.033 -20.592 111.038 1.00121.03 C ANISOU 1557 C SER A1001 14336 20677 10975 -1341 -2564 1097 C ATOM 1558 O SER A1001 127.873 -20.533 111.464 1.00117.78 O ANISOU 1558 O SER A1001 14353 19791 10610 -1408 -2596 1034 O ATOM 1559 CB SER A1001 129.706 -22.322 109.339 1.00123.31 C ANISOU 1559 CB SER A1001 14344 21353 11156 -448 -2346 976 C ATOM 1560 OG SER A1001 128.396 -22.474 108.818 1.00129.38 O ANISOU 1560 OG SER A1001 15610 21565 11985 -445 -2273 898 O ATOM 1561 N ASN A1002 129.764 -19.498 110.750 1.00120.43 N ANISOU 1561 N ASN A1002 13960 20937 10859 -1775 -2549 1209 N ATOM 1562 CA ASN A1002 129.236 -18.140 110.899 1.00119.45 C ANISOU 1562 CA ASN A1002 14114 20502 10769 -2320 -2631 1238 C ATOM 1563 C ASN A1002 128.023 -17.870 109.991 1.00120.78 C ANISOU 1563 C ASN A1002 14689 20221 10980 -2308 -2482 1169 C ATOM 1564 O ASN A1002 127.122 -17.154 110.422 1.00118.58 O ANISOU 1564 O ASN A1002 14799 19512 10743 -2486 -2592 1084 O ATOM 1565 CB ASN A1002 130.326 -17.086 110.724 1.00124.02 C ANISOU 1565 CB ASN A1002 14335 21498 11288 -2864 -2719 1433 C ATOM 1566 CG ASN A1002 131.499 -17.249 111.655 1.00145.79 C ANISOU 1566 CG ASN A1002 16663 24729 14003 -2949 -2923 1503 C ATOM 1567 OD1 ASN A1002 131.375 -17.177 112.884 1.00138.08 O ANISOU 1567 OD1 ASN A1002 15888 23533 13044 -2989 -3164 1418 O ATOM 1568 ND2 ASN A1002 132.671 -17.465 111.083 1.00141.96 N ANISOU 1568 ND2 ASN A1002 15537 24982 13418 -2968 -2834 1660 N ATOM 1569 N ILE A1003 127.970 -18.475 108.772 1.00117.87 N ANISOU 1569 N ILE A1003 14237 19977 10572 -2037 -2257 1172 N ATOM 1570 CA ILE A1003 126.824 -18.333 107.845 1.00115.39 C ANISOU 1570 CA ILE A1003 14283 19281 10279 -1989 -2139 1111 C ATOM 1571 C ILE A1003 125.597 -18.997 108.462 1.00116.07 C ANISOU 1571 C ILE A1003 14728 18922 10450 -1724 -2190 953 C ATOM 1572 O ILE A1003 124.526 -18.391 108.491 1.00113.63 O ANISOU 1572 O ILE A1003 14732 18260 10184 -1835 -2221 887 O ATOM 1573 CB ILE A1003 127.044 -18.889 106.401 1.00120.06 C ANISOU 1573 CB ILE A1003 14717 20152 10749 -1746 -1909 1128 C ATOM 1574 CG1 ILE A1003 128.442 -19.500 106.199 1.00125.24 C ANISOU 1574 CG1 ILE A1003 14832 21483 11270 -1500 -1820 1165 C ATOM 1575 CG2 ILE A1003 126.722 -17.846 105.325 1.00121.08 C ANISOU 1575 CG2 ILE A1003 14965 20241 10800 -2114 -1834 1261 C ATOM 1576 CD1 ILE A1003 128.391 -20.955 105.791 1.00137.16 C ANISOU 1576 CD1 ILE A1003 16378 23016 12721 -833 -1743 973 C ATOM 1577 N PHE A1004 125.765 -20.247 108.951 1.00113.05 N ANISOU 1577 N PHE A1004 14291 18592 10071 -1379 -2226 912 N ATOM 1578 CA PHE A1004 124.727 -21.069 109.573 1.00111.13 C ANISOU 1578 CA PHE A1004 14347 18011 9865 -1213 -2300 850 C ATOM 1579 C PHE A1004 124.020 -20.334 110.718 1.00112.85 C ANISOU 1579 C PHE A1004 14722 18082 10075 -1461 -2396 824 C ATOM 1580 O PHE A1004 122.791 -20.207 110.688 1.00111.33 O ANISOU 1580 O PHE A1004 14751 17664 9884 -1485 -2365 761 O ATOM 1581 CB PHE A1004 125.323 -22.415 110.032 1.00115.19 C ANISOU 1581 CB PHE A1004 14809 18595 10361 -861 -2417 873 C ATOM 1582 CG PHE A1004 124.401 -23.324 110.810 1.00116.30 C ANISOU 1582 CG PHE A1004 15274 18409 10507 -808 -2558 908 C ATOM 1583 CD1 PHE A1004 123.456 -24.108 110.156 1.00119.10 C ANISOU 1583 CD1 PHE A1004 15921 18444 10888 -706 -2567 884 C ATOM 1584 CD2 PHE A1004 124.501 -23.424 112.193 1.00119.20 C ANISOU 1584 CD2 PHE A1004 15656 18820 10815 -912 -2711 997 C ATOM 1585 CE1 PHE A1004 122.614 -24.962 110.876 1.00120.40 C ANISOU 1585 CE1 PHE A1004 16369 18347 11031 -784 -2730 993 C ATOM 1586 CE2 PHE A1004 123.656 -24.273 112.911 1.00122.43 C ANISOU 1586 CE2 PHE A1004 16349 18999 11169 -951 -2839 1103 C ATOM 1587 CZ PHE A1004 122.717 -25.037 112.248 1.00120.17 C ANISOU 1587 CZ PHE A1004 16333 18407 10921 -922 -2850 1123 C ATOM 1588 N GLU A1005 124.800 -19.820 111.693 1.00108.67 N ANISOU 1588 N GLU A1005 14051 17737 9503 -1624 -2522 849 N ATOM 1589 CA GLU A1005 124.285 -19.085 112.848 1.00107.38 C ANISOU 1589 CA GLU A1005 14048 17488 9263 -1799 -2640 766 C ATOM 1590 C GLU A1005 123.604 -17.767 112.447 1.00110.58 C ANISOU 1590 C GLU A1005 14659 17672 9685 -1971 -2641 642 C ATOM 1591 O GLU A1005 122.603 -17.394 113.064 1.00109.89 O ANISOU 1591 O GLU A1005 14774 17464 9517 -1925 -2672 495 O ATOM 1592 CB GLU A1005 125.381 -18.864 113.910 1.00110.86 C ANISOU 1592 CB GLU A1005 14318 18171 9632 -1929 -2831 805 C ATOM 1593 CG GLU A1005 126.032 -20.137 114.450 1.00116.39 C ANISOU 1593 CG GLU A1005 14855 19070 10299 -1695 -2905 925 C ATOM 1594 CD GLU A1005 125.174 -21.115 115.238 1.00122.32 C ANISOU 1594 CD GLU A1005 15834 19691 10953 -1547 -2941 970 C ATOM 1595 OE1 GLU A1005 124.048 -20.748 115.649 1.00114.47 O ANISOU 1595 OE1 GLU A1005 15042 18594 9856 -1656 -2892 894 O ATOM 1596 OE2 GLU A1005 125.641 -22.256 115.457 1.00104.69 O ANISOU 1596 OE2 GLU A1005 13573 17488 8716 -1319 -3044 1094 O ATOM 1597 N MET A1006 124.123 -17.088 111.396 1.00107.56 N ANISOU 1597 N MET A1006 14226 17270 9372 -2142 -2620 710 N ATOM 1598 CA MET A1006 123.577 -15.836 110.851 1.00107.71 C ANISOU 1598 CA MET A1006 14515 16997 9413 -2313 -2694 645 C ATOM 1599 C MET A1006 122.134 -16.056 110.383 1.00109.53 C ANISOU 1599 C MET A1006 14948 17011 9659 -2056 -2585 526 C ATOM 1600 O MET A1006 121.246 -15.297 110.770 1.00110.50 O ANISOU 1600 O MET A1006 15318 16925 9744 -1990 -2694 348 O ATOM 1601 CB MET A1006 124.452 -15.322 109.684 1.00111.70 C ANISOU 1601 CB MET A1006 14895 17603 9944 -2596 -2669 846 C ATOM 1602 CG MET A1006 123.969 -14.031 109.051 1.00116.12 C ANISOU 1602 CG MET A1006 15812 17793 10515 -2835 -2822 853 C ATOM 1603 SD MET A1006 124.625 -13.854 107.380 1.00121.56 S ANISOU 1603 SD MET A1006 16351 18678 11156 -3098 -2676 1150 S ATOM 1604 CE MET A1006 125.250 -12.212 107.454 1.00122.79 C ANISOU 1604 CE MET A1006 16803 18558 11292 -3734 -3048 1323 C ATOM 1605 N LEU A1007 121.901 -17.109 109.582 1.00103.50 N ANISOU 1605 N LEU A1007 14074 16321 8929 -1880 -2404 598 N ATOM 1606 CA LEU A1007 120.571 -17.427 109.076 1.00101.33 C ANISOU 1606 CA LEU A1007 13937 15897 8667 -1697 -2330 519 C ATOM 1607 C LEU A1007 119.676 -18.085 110.128 1.00105.12 C ANISOU 1607 C LEU A1007 14403 16459 9078 -1575 -2323 447 C ATOM 1608 O LEU A1007 118.455 -18.060 109.972 1.00104.55 O ANISOU 1608 O LEU A1007 14390 16355 8981 -1477 -2295 365 O ATOM 1609 CB LEU A1007 120.642 -18.235 107.784 1.00100.41 C ANISOU 1609 CB LEU A1007 13777 15794 8582 -1600 -2201 607 C ATOM 1610 CG LEU A1007 120.824 -17.344 106.572 1.00105.49 C ANISOU 1610 CG LEU A1007 14511 16355 9216 -1720 -2190 664 C ATOM 1611 CD1 LEU A1007 122.119 -17.627 105.862 1.00107.08 C ANISOU 1611 CD1 LEU A1007 14493 16836 9355 -1784 -2080 808 C ATOM 1612 CD2 LEU A1007 119.637 -17.406 105.671 1.00106.62 C ANISOU 1612 CD2 LEU A1007 14828 16320 9362 -1585 -2174 604 C ATOM 1613 N ARG A1008 120.263 -18.613 111.224 1.00101.85 N ANISOU 1613 N ARG A1008 13886 16211 8600 -1605 -2362 499 N ATOM 1614 CA ARG A1008 119.479 -19.182 112.320 1.00101.81 C ANISOU 1614 CA ARG A1008 13868 16358 8458 -1573 -2361 495 C ATOM 1615 C ARG A1008 118.769 -18.034 113.066 1.00106.66 C ANISOU 1615 C ARG A1008 14550 17048 8927 -1527 -2402 273 C ATOM 1616 O ARG A1008 117.580 -18.152 113.371 1.00106.77 O ANISOU 1616 O ARG A1008 14519 17238 8812 -1438 -2333 206 O ATOM 1617 CB ARG A1008 120.357 -20.002 113.280 1.00102.47 C ANISOU 1617 CB ARG A1008 13875 16583 8477 -1612 -2437 635 C ATOM 1618 CG ARG A1008 119.535 -20.860 114.226 1.00109.11 C ANISOU 1618 CG ARG A1008 14731 17580 9145 -1655 -2439 744 C ATOM 1619 CD ARG A1008 120.374 -21.541 115.269 1.00117.48 C ANISOU 1619 CD ARG A1008 15781 18754 10102 -1691 -2572 899 C ATOM 1620 NE ARG A1008 119.531 -22.273 116.214 1.00126.42 N ANISOU 1620 NE ARG A1008 16957 20073 11005 -1823 -2583 1059 N ATOM 1621 CZ ARG A1008 119.988 -22.952 117.259 1.00139.35 C ANISOU 1621 CZ ARG A1008 18643 21827 12477 -1895 -2723 1248 C ATOM 1622 NH1 ARG A1008 121.291 -23.000 117.512 1.00120.38 N ANISOU 1622 NH1 ARG A1008 16221 19382 10136 -1789 -2877 1262 N ATOM 1623 NH2 ARG A1008 119.148 -23.590 118.061 1.00133.12 N ANISOU 1623 NH2 ARG A1008 17897 21252 11432 -2098 -2726 1453 N ATOM 1624 N ILE A1009 119.496 -16.919 113.324 1.00103.35 N ANISOU 1624 N ILE A1009 14240 16517 8509 -1580 -2544 151 N ATOM 1625 CA ILE A1009 118.974 -15.716 113.978 1.00104.78 C ANISOU 1625 CA ILE A1009 14606 16660 8547 -1460 -2676 -131 C ATOM 1626 C ILE A1009 117.828 -15.093 113.136 1.00108.88 C ANISOU 1626 C ILE A1009 15245 17020 9106 -1245 -2664 -287 C ATOM 1627 O ILE A1009 116.778 -14.737 113.685 1.00109.14 O ANISOU 1627 O ILE A1009 15284 17227 8956 -972 -2663 -523 O ATOM 1628 CB ILE A1009 120.139 -14.718 114.276 1.00109.59 C ANISOU 1628 CB ILE A1009 15391 17067 9183 -1657 -2927 -185 C ATOM 1629 CG1 ILE A1009 121.050 -15.259 115.418 1.00110.82 C ANISOU 1629 CG1 ILE A1009 15394 17481 9233 -1797 -2979 -88 C ATOM 1630 CG2 ILE A1009 119.621 -13.303 114.607 1.00112.93 C ANISOU 1630 CG2 ILE A1009 16171 17247 9493 -1496 -3170 -522 C ATOM 1631 CD1 ILE A1009 122.510 -14.798 115.423 1.00116.55 C ANISOU 1631 CD1 ILE A1009 16102 18132 10050 -2117 -3190 18 C ATOM 1632 N ASP A1010 118.023 -15.020 111.806 1.00105.59 N ANISOU 1632 N ASP A1010 14884 16350 8885 -1333 -2652 -153 N ATOM 1633 CA ASP A1010 117.074 -14.421 110.870 1.00106.71 C ANISOU 1633 CA ASP A1010 15170 16300 9076 -1145 -2694 -256 C ATOM 1634 C ASP A1010 115.861 -15.287 110.500 1.00111.90 C ANISOU 1634 C ASP A1010 15603 17206 9709 -989 -2518 -232 C ATOM 1635 O ASP A1010 114.748 -14.760 110.485 1.00113.33 O ANISOU 1635 O ASP A1010 15787 17467 9807 -706 -2562 -432 O ATOM 1636 CB ASP A1010 117.794 -13.959 109.597 1.00108.25 C ANISOU 1636 CB ASP A1010 15538 16164 9426 -1356 -2773 -85 C ATOM 1637 CG ASP A1010 118.750 -12.795 109.787 1.00119.61 C ANISOU 1637 CG ASP A1010 17251 17316 10880 -1597 -3033 -82 C ATOM 1638 OD1 ASP A1010 118.570 -12.025 110.758 1.00122.34 O ANISOU 1638 OD1 ASP A1010 17807 17548 11128 -1476 -3244 -325 O ATOM 1639 OD2 ASP A1010 119.636 -12.615 108.931 1.00125.69 O ANISOU 1639 OD2 ASP A1010 18038 17993 11725 -1917 -3050 161 O ATOM 1640 N GLU A1011 116.064 -16.587 110.189 1.00108.26 N ANISOU 1640 N GLU A1011 14963 16861 9309 -1158 -2367 -2 N ATOM 1641 CA GLU A1011 114.989 -17.494 109.757 1.00108.18 C ANISOU 1641 CA GLU A1011 14791 17025 9289 -1134 -2272 71 C ATOM 1642 C GLU A1011 114.520 -18.530 110.805 1.00113.89 C ANISOU 1642 C GLU A1011 15294 18120 9861 -1245 -2186 174 C ATOM 1643 O GLU A1011 113.328 -18.838 110.849 1.00115.46 O ANISOU 1643 O GLU A1011 15300 18616 9956 -1231 -2141 172 O ATOM 1644 CB GLU A1011 115.380 -18.201 108.456 1.00107.94 C ANISOU 1644 CB GLU A1011 14831 16776 9405 -1241 -2249 239 C ATOM 1645 CG GLU A1011 115.174 -17.331 107.227 1.00119.51 C ANISOU 1645 CG GLU A1011 16460 18010 10937 -1146 -2317 181 C ATOM 1646 CD GLU A1011 115.667 -17.883 105.903 1.00136.66 C ANISOU 1646 CD GLU A1011 18720 20031 13174 -1221 -2281 315 C ATOM 1647 OE1 GLU A1011 115.500 -19.099 105.653 1.00129.29 O ANISOU 1647 OE1 GLU A1011 17735 19142 12247 -1255 -2243 390 O ATOM 1648 OE2 GLU A1011 116.178 -17.081 105.090 1.00130.34 O ANISOU 1648 OE2 GLU A1011 18072 19066 12383 -1249 -2318 347 O ATOM 1649 N GLY A1012 115.444 -19.078 111.592 1.00110.04 N ANISOU 1649 N GLY A1012 14817 17649 9342 -1387 -2186 300 N ATOM 1650 CA GLY A1012 115.122 -20.071 112.615 1.00111.33 C ANISOU 1650 CA GLY A1012 14848 18118 9333 -1554 -2151 470 C ATOM 1651 C GLY A1012 115.489 -21.495 112.254 1.00115.02 C ANISOU 1651 C GLY A1012 15407 18394 9903 -1748 -2214 744 C ATOM 1652 O GLY A1012 115.577 -21.837 111.071 1.00114.08 O ANISOU 1652 O GLY A1012 15400 17988 9958 -1717 -2249 762 O ATOM 1653 N LEU A1013 115.691 -22.340 113.280 1.00112.88 N ANISOU 1653 N LEU A1013 15137 18262 9489 -1925 -2266 950 N ATOM 1654 CA LEU A1013 116.045 -23.748 113.103 1.00113.30 C ANISOU 1654 CA LEU A1013 15382 18052 9614 -2077 -2423 1213 C ATOM 1655 C LEU A1013 115.002 -24.680 113.718 1.00119.18 C ANISOU 1655 C LEU A1013 16099 19019 10165 -2445 -2485 1497 C ATOM 1656 O LEU A1013 114.702 -24.576 114.910 1.00120.18 O ANISOU 1656 O LEU A1013 16073 19568 10021 -2591 -2422 1590 O ATOM 1657 CB LEU A1013 117.450 -24.044 113.672 1.00113.66 C ANISOU 1657 CB LEU A1013 15538 17967 9681 -1968 -2534 1270 C ATOM 1658 CG LEU A1013 118.006 -25.462 113.462 1.00119.90 C ANISOU 1658 CG LEU A1013 16601 18402 10555 -1958 -2770 1478 C ATOM 1659 CD1 LEU A1013 118.557 -25.641 112.054 1.00118.86 C ANISOU 1659 CD1 LEU A1013 16575 17946 10639 -1677 -2792 1327 C ATOM 1660 CD2 LEU A1013 119.089 -25.768 114.473 1.00124.20 C ANISOU 1660 CD2 LEU A1013 17186 18986 11018 -1880 -2908 1585 C ATOM 1661 N ARG A1014 114.456 -25.588 112.887 1.00116.19 N ANISOU 1661 N ARG A1014 15876 18380 9890 -2631 -2629 1645 N ATOM 1662 CA ARG A1014 113.475 -26.595 113.288 1.00119.37 C ANISOU 1662 CA ARG A1014 16299 18925 10132 -3118 -2766 1992 C ATOM 1663 C ARG A1014 114.003 -27.971 112.899 1.00124.31 C ANISOU 1663 C ARG A1014 17419 18919 10894 -3230 -3125 2206 C ATOM 1664 O ARG A1014 114.266 -28.218 111.721 1.00122.75 O ANISOU 1664 O ARG A1014 17448 18281 10912 -3019 -3236 2046 O ATOM 1665 CB ARG A1014 112.096 -26.326 112.661 1.00120.25 C ANISOU 1665 CB ARG A1014 16126 19355 10210 -3298 -2679 1958 C ATOM 1666 CG ARG A1014 111.343 -25.172 113.307 1.00130.50 C ANISOU 1666 CG ARG A1014 16933 21374 11278 -3176 -2386 1780 C ATOM 1667 CD ARG A1014 109.864 -25.471 113.424 1.00144.87 C ANISOU 1667 CD ARG A1014 18370 23797 12879 -3575 -2351 1977 C ATOM 1668 NE ARG A1014 109.057 -24.516 112.666 1.00156.70 N ANISOU 1668 NE ARG A1014 19549 25563 14427 -3275 -2223 1671 N ATOM 1669 CZ ARG A1014 107.728 -24.517 112.630 1.00176.50 C ANISOU 1669 CZ ARG A1014 21597 28711 16754 -3489 -2171 1752 C ATOM 1670 NH1 ARG A1014 107.077 -23.613 111.909 1.00162.48 N ANISOU 1670 NH1 ARG A1014 19564 27132 15039 -3114 -2103 1445 N ATOM 1671 NH2 ARG A1014 107.038 -25.425 113.312 1.00168.69 N ANISOU 1671 NH2 ARG A1014 20389 28204 15503 -4101 -2213 2168 N ATOM 1672 N LEU A1015 114.196 -28.846 113.896 1.00123.74 N ANISOU 1672 N LEU A1015 17559 18789 10667 -3512 -3335 2547 N ATOM 1673 CA LEU A1015 114.740 -30.192 113.698 1.00126.09 C ANISOU 1673 CA LEU A1015 18432 18408 11069 -3562 -3772 2755 C ATOM 1674 C LEU A1015 113.668 -31.264 113.436 1.00134.53 C ANISOU 1674 C LEU A1015 19774 19249 12093 -4167 -4095 3099 C ATOM 1675 O LEU A1015 114.009 -32.421 113.170 1.00137.22 O ANISOU 1675 O LEU A1015 20709 18901 12526 -4213 -4551 3248 O ATOM 1676 CB LEU A1015 115.657 -30.586 114.873 1.00127.94 C ANISOU 1676 CB LEU A1015 18852 18588 11171 -3509 -3929 2960 C ATOM 1677 CG LEU A1015 116.853 -29.668 115.149 1.00128.83 C ANISOU 1677 CG LEU A1015 18734 18885 11332 -2972 -3712 2655 C ATOM 1678 CD1 LEU A1015 117.442 -29.955 116.497 1.00131.50 C ANISOU 1678 CD1 LEU A1015 19157 19355 11453 -3053 -3851 2908 C ATOM 1679 CD2 LEU A1015 117.923 -29.791 114.071 1.00128.96 C ANISOU 1679 CD2 LEU A1015 18921 18454 11625 -2397 -3801 2350 C ATOM 1680 N LYS A1016 112.381 -30.873 113.481 1.00132.23 N ANISOU 1680 N LYS A1016 19053 19537 11650 -4610 -3900 3209 N ATOM 1681 CA LYS A1016 111.240 -31.755 113.213 1.00136.98 C ANISOU 1681 CA LYS A1016 19773 20088 12184 -5304 -4185 3564 C ATOM 1682 C LYS A1016 110.537 -31.306 111.919 1.00139.17 C ANISOU 1682 C LYS A1016 19846 20400 12632 -5195 -4097 3269 C ATOM 1683 O LYS A1016 110.468 -30.102 111.651 1.00134.74 O ANISOU 1683 O LYS A1016 18830 20262 12103 -4773 -3703 2914 O ATOM 1684 CB LYS A1016 110.264 -31.745 114.403 1.00143.49 C ANISOU 1684 CB LYS A1016 20152 21751 12617 -5969 -4038 3992 C ATOM 1685 CG LYS A1016 109.273 -32.904 114.415 1.00160.55 C ANISOU 1685 CG LYS A1016 22513 23843 14646 -6889 -4439 4544 C ATOM 1686 CD LYS A1016 108.266 -32.758 115.546 1.00171.26 C ANISOU 1686 CD LYS A1016 23242 26287 15543 -7545 -4190 4956 C ATOM 1687 CE LYS A1016 107.178 -33.800 115.474 1.00181.09 C ANISOU 1687 CE LYS A1016 24581 27587 16638 -8584 -4580 5551 C ATOM 1688 NZ LYS A1016 106.125 -33.571 116.499 1.00182.12 N ANISOU 1688 NZ LYS A1016 23957 28780 16461 -8847 -4111 5749 N ATOM 1689 N ILE A1017 110.038 -32.269 111.113 1.00139.29 N ANISOU 1689 N ILE A1017 20259 19920 12745 -5576 -4520 3418 N ATOM 1690 CA ILE A1017 109.326 -31.986 109.859 1.00138.22 C ANISOU 1690 CA ILE A1017 19990 19787 12741 -5537 -4523 3178 C ATOM 1691 C ILE A1017 108.090 -31.123 110.139 1.00143.81 C ANISOU 1691 C ILE A1017 19887 21492 13263 -5820 -4174 3236 C ATOM 1692 O ILE A1017 107.293 -31.456 111.019 1.00148.23 O ANISOU 1692 O ILE A1017 20150 22606 13564 -6479 -4194 3660 O ATOM 1693 CB ILE A1017 109.014 -33.286 109.050 1.00145.86 C ANISOU 1693 CB ILE A1017 21624 19987 13810 -5950 -5138 3338 C ATOM 1694 CG1 ILE A1017 110.270 -33.759 108.282 1.00144.70 C ANISOU 1694 CG1 ILE A1017 22187 18925 13867 -5264 -5386 2987 C ATOM 1695 CG2 ILE A1017 107.818 -33.107 108.098 1.00147.74 C ANISOU 1695 CG2 ILE A1017 21575 20495 14064 -6275 -5197 3291 C ATOM 1696 CD1 ILE A1017 110.140 -35.065 107.454 1.00157.67 C ANISOU 1696 CD1 ILE A1017 24657 19657 15592 -5487 -6068 3026 C ATOM 1697 N TYR A1018 107.971 -29.994 109.424 1.00137.03 N ANISOU 1697 N TYR A1018 18664 20903 12499 -5287 -3862 2816 N ATOM 1698 CA TYR A1018 106.855 -29.063 109.574 1.00137.88 C ANISOU 1698 CA TYR A1018 18018 21926 12443 -5330 -3557 2759 C ATOM 1699 C TYR A1018 106.379 -28.539 108.229 1.00139.32 C ANISOU 1699 C TYR A1018 18107 22040 12789 -5049 -3583 2449 C ATOM 1700 O TYR A1018 107.154 -28.501 107.276 1.00135.38 O ANISOU 1700 O TYR A1018 18055 20878 12503 -4630 -3673 2179 O ATOM 1701 CB TYR A1018 107.235 -27.898 110.509 1.00136.99 C ANISOU 1701 CB TYR A1018 17515 22345 12190 -4847 -3115 2544 C ATOM 1702 CG TYR A1018 108.215 -26.909 109.914 1.00134.10 C ANISOU 1702 CG TYR A1018 17324 21588 12041 -4087 -2946 2084 C ATOM 1703 CD1 TYR A1018 109.586 -27.141 109.962 1.00133.68 C ANISOU 1703 CD1 TYR A1018 17744 20917 12131 -3815 -3002 2012 C ATOM 1704 CD2 TYR A1018 107.774 -25.721 109.338 1.00133.40 C ANISOU 1704 CD2 TYR A1018 16909 21790 11986 -3657 -2756 1748 C ATOM 1705 CE1 TYR A1018 110.493 -26.236 109.415 1.00130.90 C ANISOU 1705 CE1 TYR A1018 17490 20306 11940 -3232 -2849 1655 C ATOM 1706 CE2 TYR A1018 108.672 -24.802 108.799 1.00130.26 C ANISOU 1706 CE2 TYR A1018 16712 21021 11759 -3078 -2644 1404 C ATOM 1707 CZ TYR A1018 110.032 -25.060 108.846 1.00137.16 C ANISOU 1707 CZ TYR A1018 18006 21351 12759 -2916 -2675 1378 C ATOM 1708 OH TYR A1018 110.929 -24.161 108.324 1.00137.74 O ANISOU 1708 OH TYR A1018 18215 21156 12964 -2456 -2566 1104 O ATOM 1709 N LYS A1019 105.114 -28.109 108.164 1.00138.58 N ANISOU 1709 N LYS A1019 17391 22711 12554 -5244 -3498 2487 N ATOM 1710 CA LYS A1019 104.532 -27.526 106.960 1.00137.28 C ANISOU 1710 CA LYS A1019 17064 22593 12503 -4967 -3542 2215 C ATOM 1711 C LYS A1019 104.710 -26.007 107.005 1.00138.55 C ANISOU 1711 C LYS A1019 16900 23083 12659 -4201 -3176 1812 C ATOM 1712 O LYS A1019 104.688 -25.415 108.092 1.00138.98 O ANISOU 1712 O LYS A1019 16569 23714 12523 -4045 -2893 1786 O ATOM 1713 CB LYS A1019 103.047 -27.890 106.830 1.00145.07 C ANISOU 1713 CB LYS A1019 17522 24261 13335 -5579 -3716 2478 C ATOM 1714 CG LYS A1019 102.800 -29.308 106.324 1.00158.35 C ANISOU 1714 CG LYS A1019 19672 25408 15087 -6336 -4232 2810 C ATOM 1715 CD LYS A1019 101.315 -29.568 106.094 1.00170.99 C ANISOU 1715 CD LYS A1019 20682 27746 16542 -6980 -4431 3066 C ATOM 1716 CE LYS A1019 101.055 -30.943 105.527 1.00182.49 C ANISOU 1716 CE LYS A1019 22687 28580 18072 -7787 -5037 3383 C ATOM 1717 NZ LYS A1019 99.637 -31.110 105.106 1.00192.38 N ANISOU 1717 NZ LYS A1019 23339 30511 19246 -8349 -5240 3568 N ATOM 1718 N ASP A1020 104.920 -25.385 105.830 1.00132.19 N ANISOU 1718 N ASP A1020 16316 21878 12033 -3731 -3219 1503 N ATOM 1719 CA ASP A1020 105.070 -23.933 105.703 1.00129.45 C ANISOU 1719 CA ASP A1020 15799 21686 11701 -3045 -2986 1149 C ATOM 1720 C ASP A1020 103.704 -23.275 105.424 1.00137.75 C ANISOU 1720 C ASP A1020 16256 23447 12635 -2907 -3002 1050 C ATOM 1721 O ASP A1020 102.678 -23.958 105.508 1.00142.01 O ANISOU 1721 O ASP A1020 16394 24513 13051 -3404 -3126 1290 O ATOM 1722 CB ASP A1020 106.137 -23.562 104.644 1.00126.79 C ANISOU 1722 CB ASP A1020 16020 20588 11565 -2645 -3026 929 C ATOM 1723 CG ASP A1020 105.956 -24.160 103.252 1.00137.41 C ANISOU 1723 CG ASP A1020 17687 21519 13005 -2780 -3311 933 C ATOM 1724 OD1 ASP A1020 104.802 -24.191 102.755 1.00139.80 O ANISOU 1724 OD1 ASP A1020 17701 22159 13258 -2940 -3481 966 O ATOM 1725 OD2 ASP A1020 106.976 -24.521 102.627 1.00142.10 O ANISOU 1725 OD2 ASP A1020 18795 21506 13690 -2669 -3365 871 O ATOM 1726 N THR A1021 103.690 -21.963 105.086 1.00133.33 N ANISOU 1726 N THR A1021 15644 22912 12103 -2249 -2920 719 N ATOM 1727 CA THR A1021 102.463 -21.206 104.790 1.00136.80 C ANISOU 1727 CA THR A1021 15555 23988 12434 -1929 -2974 558 C ATOM 1728 C THR A1021 101.682 -21.785 103.606 1.00142.46 C ANISOU 1728 C THR A1021 16215 24698 13213 -2229 -3281 674 C ATOM 1729 O THR A1021 100.454 -21.727 103.618 1.00147.16 O ANISOU 1729 O THR A1021 16183 26065 13666 -2281 -3358 702 O ATOM 1730 CB THR A1021 102.743 -19.703 104.615 1.00144.73 C ANISOU 1730 CB THR A1021 16713 24805 13474 -1138 -2926 184 C ATOM 1731 OG1 THR A1021 103.533 -19.493 103.444 1.00140.73 O ANISOU 1731 OG1 THR A1021 16834 23462 13175 -1029 -3066 138 O ATOM 1732 CG2 THR A1021 103.414 -19.075 105.842 1.00143.60 C ANISOU 1732 CG2 THR A1021 16597 24736 13228 -844 -2684 30 C ATOM 1733 N GLU A1022 102.384 -22.351 102.600 1.00135.60 N ANISOU 1733 N GLU A1022 15970 23032 12521 -2408 -3467 723 N ATOM 1734 CA GLU A1022 101.761 -22.958 101.414 1.00137.17 C ANISOU 1734 CA GLU A1022 16251 23107 12759 -2697 -3809 800 C ATOM 1735 C GLU A1022 101.329 -24.417 101.642 1.00143.32 C ANISOU 1735 C GLU A1022 16981 23972 13500 -3527 -4022 1140 C ATOM 1736 O GLU A1022 100.546 -24.957 100.854 1.00145.91 O ANISOU 1736 O GLU A1022 17249 24371 13819 -3881 -4357 1233 O ATOM 1737 CB GLU A1022 102.677 -22.838 100.192 1.00134.84 C ANISOU 1737 CB GLU A1022 16661 21982 12589 -2438 -3918 652 C ATOM 1738 CG GLU A1022 102.715 -21.434 99.618 1.00145.70 C ANISOU 1738 CG GLU A1022 18081 23307 13971 -1773 -3869 405 C ATOM 1739 CD GLU A1022 103.813 -21.167 98.608 1.00164.92 C ANISOU 1739 CD GLU A1022 21176 25026 16460 -1550 -3887 315 C ATOM 1740 OE1 GLU A1022 104.984 -21.515 98.885 1.00165.25 O ANISOU 1740 OE1 GLU A1022 21572 24665 16550 -1607 -3715 339 O ATOM 1741 OE2 GLU A1022 103.510 -20.551 97.561 1.00154.94 O ANISOU 1741 OE2 GLU A1022 20040 23673 15156 -1298 -4070 230 O ATOM 1742 N GLY A1023 101.828 -25.018 102.726 1.00138.78 N ANISOU 1742 N GLY A1023 16468 23373 12890 -3854 -3878 1339 N ATOM 1743 CA GLY A1023 101.525 -26.392 103.115 1.00141.84 C ANISOU 1743 CA GLY A1023 16913 23755 13226 -4692 -4116 1723 C ATOM 1744 C GLY A1023 102.546 -27.413 102.653 1.00141.87 C ANISOU 1744 C GLY A1023 17785 22743 13377 -4878 -4365 1765 C ATOM 1745 O GLY A1023 102.238 -28.607 102.592 1.00145.18 O ANISOU 1745 O GLY A1023 18452 22925 13785 -5555 -4740 2041 O ATOM 1746 N TYR A1024 103.768 -26.949 102.326 1.00131.99 N ANISOU 1746 N TYR A1024 17004 20906 12241 -4274 -4191 1490 N ATOM 1747 CA TYR A1024 104.869 -27.792 101.860 1.00129.81 C ANISOU 1747 CA TYR A1024 17501 19756 12065 -4238 -4375 1438 C ATOM 1748 C TYR A1024 105.764 -28.247 103.016 1.00132.52 C ANISOU 1748 C TYR A1024 18030 19907 12414 -4310 -4247 1590 C ATOM 1749 O TYR A1024 106.024 -27.469 103.940 1.00129.92 O ANISOU 1749 O TYR A1024 17346 19978 12039 -4083 -3891 1575 O ATOM 1750 CB TYR A1024 105.718 -27.049 100.816 1.00126.58 C ANISOU 1750 CB TYR A1024 17410 18967 11717 -3566 -4245 1085 C ATOM 1751 CG TYR A1024 105.017 -26.689 99.522 1.00129.31 C ANISOU 1751 CG TYR A1024 17734 19366 12032 -3451 -4428 933 C ATOM 1752 CD1 TYR A1024 104.375 -27.661 98.759 1.00135.10 C ANISOU 1752 CD1 TYR A1024 18716 19882 12734 -3866 -4874 993 C ATOM 1753 CD2 TYR A1024 105.090 -25.400 99.004 1.00127.50 C ANISOU 1753 CD2 TYR A1024 17343 19310 11791 -2925 -4214 728 C ATOM 1754 CE1 TYR A1024 103.771 -27.344 97.544 1.00136.57 C ANISOU 1754 CE1 TYR A1024 18912 20116 12864 -3748 -5073 846 C ATOM 1755 CE2 TYR A1024 104.492 -25.072 97.788 1.00129.58 C ANISOU 1755 CE2 TYR A1024 17641 19594 11999 -2799 -4417 611 C ATOM 1756 CZ TYR A1024 103.836 -26.049 97.060 1.00140.94 C ANISOU 1756 CZ TYR A1024 19265 20892 13393 -3198 -4831 662 C ATOM 1757 OH TYR A1024 103.247 -25.734 95.858 1.00145.46 O ANISOU 1757 OH TYR A1024 19880 21506 13883 -3072 -5059 543 O ATOM 1758 N TYR A1025 106.258 -29.500 102.945 1.00130.65 N ANISOU 1758 N TYR A1025 18405 19019 12218 -4576 -4586 1710 N ATOM 1759 CA TYR A1025 107.134 -30.081 103.962 1.00129.92 C ANISOU 1759 CA TYR A1025 18583 18652 12127 -4631 -4571 1873 C ATOM 1760 C TYR A1025 108.511 -29.432 103.975 1.00128.06 C ANISOU 1760 C TYR A1025 18490 18206 11961 -3912 -4253 1585 C ATOM 1761 O TYR A1025 109.178 -29.352 102.940 1.00125.70 O ANISOU 1761 O TYR A1025 18526 17515 11717 -3463 -4280 1297 O ATOM 1762 CB TYR A1025 107.211 -31.608 103.843 1.00135.84 C ANISOU 1762 CB TYR A1025 20017 18700 12894 -5084 -5126 2079 C ATOM 1763 CG TYR A1025 105.903 -32.299 104.163 1.00143.84 C ANISOU 1763 CG TYR A1025 20852 19989 13811 -6002 -5461 2502 C ATOM 1764 CD1 TYR A1025 105.439 -32.388 105.472 1.00148.52 C ANISOU 1764 CD1 TYR A1025 21024 21152 14254 -6554 -5347 2927 C ATOM 1765 CD2 TYR A1025 105.132 -32.874 103.157 1.00148.60 C ANISOU 1765 CD2 TYR A1025 21692 20340 14430 -6368 -5909 2499 C ATOM 1766 CE1 TYR A1025 104.230 -33.013 105.771 1.00156.04 C ANISOU 1766 CE1 TYR A1025 21727 22494 15067 -7490 -5638 3378 C ATOM 1767 CE2 TYR A1025 103.927 -33.513 103.446 1.00156.01 C ANISOU 1767 CE2 TYR A1025 22419 21590 15269 -7319 -6254 2935 C ATOM 1768 CZ TYR A1025 103.481 -33.585 104.755 1.00166.60 C ANISOU 1768 CZ TYR A1025 23281 23567 16454 -7903 -6105 3397 C ATOM 1769 OH TYR A1025 102.295 -34.215 105.044 1.00174.92 O ANISOU 1769 OH TYR A1025 24050 25050 17360 -8927 -6430 3887 O ATOM 1770 N THR A1026 108.902 -28.929 105.158 1.00122.51 N ANISOU 1770 N THR A1026 17486 17850 11214 -3836 -3950 1674 N ATOM 1771 CA THR A1026 110.139 -28.192 105.413 1.00118.05 C ANISOU 1771 CA THR A1026 16931 17226 10695 -3276 -3648 1462 C ATOM 1772 C THR A1026 110.830 -28.691 106.712 1.00123.49 C ANISOU 1772 C THR A1026 17721 17863 11338 -3383 -3652 1672 C ATOM 1773 O THR A1026 110.171 -29.251 107.595 1.00126.98 O ANISOU 1773 O THR A1026 18058 18528 11661 -3900 -3762 2000 O ATOM 1774 CB THR A1026 109.811 -26.673 105.433 1.00119.99 C ANISOU 1774 CB THR A1026 16671 18005 10915 -2993 -3287 1279 C ATOM 1775 OG1 THR A1026 108.915 -26.360 104.359 1.00120.61 O ANISOU 1775 OG1 THR A1026 16634 18190 11004 -2996 -3368 1174 O ATOM 1776 CG2 THR A1026 111.043 -25.787 105.332 1.00112.75 C ANISOU 1776 CG2 THR A1026 15820 16958 10061 -2477 -3048 1047 C ATOM 1777 N ILE A1027 112.164 -28.497 106.800 1.00116.91 N ANISOU 1777 N ILE A1027 17068 16786 10568 -2919 -3546 1508 N ATOM 1778 CA ILE A1027 113.032 -28.856 107.928 1.00116.85 C ANISOU 1778 CA ILE A1027 17163 16713 10523 -2887 -3562 1652 C ATOM 1779 C ILE A1027 114.283 -27.947 107.915 1.00116.97 C ANISOU 1779 C ILE A1027 17048 16804 10592 -2351 -3288 1398 C ATOM 1780 O ILE A1027 114.559 -27.315 106.891 1.00114.36 O ANISOU 1780 O ILE A1027 16692 16432 10326 -2033 -3163 1150 O ATOM 1781 CB ILE A1027 113.364 -30.385 107.940 1.00123.77 C ANISOU 1781 CB ILE A1027 18641 16966 11419 -3025 -4028 1831 C ATOM 1782 CG1 ILE A1027 113.882 -30.853 109.327 1.00125.71 C ANISOU 1782 CG1 ILE A1027 18972 17219 11573 -3174 -4120 2115 C ATOM 1783 CG2 ILE A1027 114.311 -30.789 106.795 1.00124.16 C ANISOU 1783 CG2 ILE A1027 19110 16495 11570 -2466 -4181 1517 C ATOM 1784 CD1 ILE A1027 113.359 -32.174 109.792 1.00135.49 C ANISOU 1784 CD1 ILE A1027 20664 18074 12740 -3722 -4595 2513 C ATOM 1785 N GLY A1028 114.997 -27.886 109.046 1.00113.15 N ANISOU 1785 N GLY A1028 16474 16467 10050 -2318 -3220 1497 N ATOM 1786 CA GLY A1028 116.210 -27.091 109.226 1.00110.71 C ANISOU 1786 CA GLY A1028 16009 16279 9775 -1930 -3019 1318 C ATOM 1787 C GLY A1028 115.980 -25.614 109.000 1.00112.33 C ANISOU 1787 C GLY A1028 15871 16826 9982 -1847 -2724 1131 C ATOM 1788 O GLY A1028 114.949 -25.077 109.419 1.00112.32 O ANISOU 1788 O GLY A1028 15647 17137 9893 -2050 -2627 1159 O ATOM 1789 N ILE A1029 116.922 -24.951 108.314 1.00107.32 N ANISOU 1789 N ILE A1029 15199 16158 9420 -1543 -2604 945 N ATOM 1790 CA ILE A1029 116.763 -23.536 107.977 1.00105.51 C ANISOU 1790 CA ILE A1029 14770 16121 9200 -1489 -2413 796 C ATOM 1791 C ILE A1029 116.087 -23.473 106.603 1.00110.27 C ANISOU 1791 C ILE A1029 15465 16593 9839 -1444 -2421 708 C ATOM 1792 O ILE A1029 116.756 -23.605 105.568 1.00109.76 O ANISOU 1792 O ILE A1029 15512 16400 9790 -1255 -2405 630 O ATOM 1793 CB ILE A1029 118.078 -22.707 108.080 1.00107.72 C ANISOU 1793 CB ILE A1029 14941 16491 9498 -1341 -2312 724 C ATOM 1794 CG1 ILE A1029 118.658 -22.774 109.507 1.00108.66 C ANISOU 1794 CG1 ILE A1029 14971 16757 9559 -1400 -2352 804 C ATOM 1795 CG2 ILE A1029 117.854 -21.240 107.642 1.00107.06 C ANISOU 1795 CG2 ILE A1029 14783 16475 9422 -1354 -2213 607 C ATOM 1796 CD1 ILE A1029 120.138 -22.604 109.579 1.00118.07 C ANISOU 1796 CD1 ILE A1029 16058 18030 10773 -1268 -2348 794 C ATOM 1797 N GLY A1030 114.754 -23.367 106.641 1.00108.11 N ANISOU 1797 N GLY A1030 15115 16426 9537 -1615 -2457 731 N ATOM 1798 CA GLY A1030 113.848 -23.267 105.497 1.00108.19 C ANISOU 1798 CA GLY A1030 15171 16376 9561 -1613 -2513 665 C ATOM 1799 C GLY A1030 114.130 -24.155 104.306 1.00112.75 C ANISOU 1799 C GLY A1030 16044 16640 10157 -1534 -2647 632 C ATOM 1800 O GLY A1030 114.021 -23.693 103.172 1.00113.04 O ANISOU 1800 O GLY A1030 16147 16627 10175 -1402 -2628 525 O ATOM 1801 N HIS A1031 114.501 -25.427 104.542 1.00110.74 N ANISOU 1801 N HIS A1031 16019 16150 9907 -1580 -2821 712 N ATOM 1802 CA HIS A1031 114.799 -26.369 103.462 1.00112.19 C ANISOU 1802 CA HIS A1031 16567 15988 10072 -1413 -3010 612 C ATOM 1803 C HIS A1031 113.554 -27.143 103.066 1.00118.51 C ANISOU 1803 C HIS A1031 17555 16606 10868 -1725 -3296 682 C ATOM 1804 O HIS A1031 113.088 -27.991 103.826 1.00120.11 O ANISOU 1804 O HIS A1031 17856 16699 11083 -2060 -3510 882 O ATOM 1805 CB HIS A1031 115.960 -27.316 103.837 1.00114.56 C ANISOU 1805 CB HIS A1031 17097 16060 10369 -1173 -3125 603 C ATOM 1806 CG HIS A1031 116.274 -28.348 102.794 1.00120.75 C ANISOU 1806 CG HIS A1031 18316 16470 11093 -885 -3370 429 C ATOM 1807 ND1 HIS A1031 117.304 -28.170 101.891 1.00122.85 N ANISOU 1807 ND1 HIS A1031 18585 16842 11249 -411 -3223 195 N ATOM 1808 CD2 HIS A1031 115.690 -29.547 102.557 1.00125.89 C ANISOU 1808 CD2 HIS A1031 19423 16665 11744 -1014 -3773 450 C ATOM 1809 CE1 HIS A1031 117.306 -29.251 101.129 1.00125.89 C ANISOU 1809 CE1 HIS A1031 19430 16851 11554 -171 -3522 22 C ATOM 1810 NE2 HIS A1031 116.353 -30.108 101.493 1.00128.14 N ANISOU 1810 NE2 HIS A1031 20047 16719 11920 -532 -3895 163 N ATOM 1811 N LEU A1032 113.029 -26.860 101.865 1.00115.97 N ANISOU 1811 N LEU A1032 17290 16268 10505 -1665 -3330 549 N ATOM 1812 CA LEU A1032 111.850 -27.528 101.312 1.00118.60 C ANISOU 1812 CA LEU A1032 17784 16455 10822 -1976 -3641 593 C ATOM 1813 C LEU A1032 112.224 -28.959 100.909 1.00126.11 C ANISOU 1813 C LEU A1032 19309 16863 11746 -1933 -4013 532 C ATOM 1814 O LEU A1032 113.164 -29.155 100.138 1.00126.79 O ANISOU 1814 O LEU A1032 19667 16756 11753 -1468 -3999 293 O ATOM 1815 CB LEU A1032 111.285 -26.711 100.122 1.00117.97 C ANISOU 1815 CB LEU A1032 17612 16528 10681 -1860 -3588 450 C ATOM 1816 CG LEU A1032 110.359 -27.398 99.102 1.00126.16 C ANISOU 1816 CG LEU A1032 18899 17374 11660 -2061 -3947 407 C ATOM 1817 CD1 LEU A1032 109.062 -27.865 99.731 1.00128.99 C ANISOU 1817 CD1 LEU A1032 19045 17894 12071 -2631 -4174 648 C ATOM 1818 CD2 LEU A1032 110.031 -26.461 97.971 1.00128.22 C ANISOU 1818 CD2 LEU A1032 19072 17815 11832 -1859 -3866 270 C ATOM 1819 N LEU A1033 111.502 -29.949 101.458 1.00125.17 N ANISOU 1819 N LEU A1033 19378 16519 11661 -2413 -4367 755 N ATOM 1820 CA LEU A1033 111.751 -31.364 101.182 1.00129.13 C ANISOU 1820 CA LEU A1033 20549 16370 12146 -2427 -4850 721 C ATOM 1821 C LEU A1033 111.119 -31.805 99.863 1.00135.56 C ANISOU 1821 C LEU A1033 21723 16897 12885 -2474 -5185 536 C ATOM 1822 O LEU A1033 111.827 -32.321 98.994 1.00136.96 O ANISOU 1822 O LEU A1033 22384 16690 12966 -1987 -5346 220 O ATOM 1823 CB LEU A1033 111.278 -32.245 102.351 1.00132.47 C ANISOU 1823 CB LEU A1033 21102 16616 12613 -3026 -5157 1109 C ATOM 1824 CG LEU A1033 112.033 -32.057 103.672 1.00135.49 C ANISOU 1824 CG LEU A1033 21282 17179 13021 -2946 -4928 1283 C ATOM 1825 CD1 LEU A1033 111.150 -32.375 104.852 1.00138.06 C ANISOU 1825 CD1 LEU A1033 21429 17717 13311 -3686 -5047 1741 C ATOM 1826 CD2 LEU A1033 113.303 -32.883 103.706 1.00139.89 C ANISOU 1826 CD2 LEU A1033 22379 17188 13586 -2438 -5150 1133 C ATOM 1827 N THR A1034 109.795 -31.587 99.711 1.00132.64 N ANISOU 1827 N THR A1034 21089 16782 12525 -3022 -5295 711 N ATOM 1828 CA THR A1034 109.017 -31.938 98.516 1.00135.42 C ANISOU 1828 CA THR A1034 21715 16937 12800 -3177 -5656 577 C ATOM 1829 C THR A1034 107.752 -31.092 98.377 1.00137.53 C ANISOU 1829 C THR A1034 21365 17818 13071 -3547 -5534 719 C ATOM 1830 O THR A1034 107.177 -30.657 99.381 1.00136.06 O ANISOU 1830 O THR A1034 20622 18136 12940 -3890 -5334 996 O ATOM 1831 CB THR A1034 108.711 -33.464 98.448 1.00150.18 C ANISOU 1831 CB THR A1034 24302 18095 14666 -3597 -6345 663 C ATOM 1832 OG1 THR A1034 108.070 -33.763 97.204 1.00150.75 O ANISOU 1832 OG1 THR A1034 24697 17946 14637 -3679 -6719 463 O ATOM 1833 CG2 THR A1034 107.847 -33.966 99.617 1.00151.66 C ANISOU 1833 CG2 THR A1034 24300 18393 14930 -4466 -6564 1170 C ATOM 1834 N LYS A1035 107.300 -30.904 97.126 1.00134.48 N ANISOU 1834 N LYS A1035 21086 17420 12589 -3440 -5685 513 N ATOM 1835 CA LYS A1035 106.071 -30.171 96.826 1.00134.12 C ANISOU 1835 CA LYS A1035 20500 17928 12531 -3710 -5665 610 C ATOM 1836 C LYS A1035 104.841 -31.085 96.893 1.00144.17 C ANISOU 1836 C LYS A1035 21779 19189 13811 -4509 -6188 867 C ATOM 1837 O LYS A1035 103.710 -30.597 96.854 1.00145.60 O ANISOU 1837 O LYS A1035 21381 19960 13979 -4823 -6199 1011 O ATOM 1838 CB LYS A1035 106.168 -29.408 95.496 1.00134.48 C ANISOU 1838 CB LYS A1035 20617 18034 12446 -3227 -5581 315 C ATOM 1839 CG LYS A1035 107.022 -28.152 95.598 1.00138.80 C ANISOU 1839 CG LYS A1035 20907 18845 12984 -2653 -5036 210 C ATOM 1840 CD LYS A1035 106.625 -27.104 94.575 1.00148.01 C ANISOU 1840 CD LYS A1035 21903 20297 14038 -2400 -4960 102 C ATOM 1841 CE LYS A1035 107.533 -25.899 94.603 1.00155.80 C ANISOU 1841 CE LYS A1035 22739 21456 15002 -1933 -4505 49 C ATOM 1842 NZ LYS A1035 107.324 -25.061 95.815 1.00162.23 N ANISOU 1842 NZ LYS A1035 23033 22626 15979 -1984 -4239 209 N ATOM 1843 N SER A1036 105.069 -32.408 97.040 1.00144.62 N ANISOU 1843 N SER A1036 22483 18589 13878 -4847 -6652 942 N ATOM 1844 CA SER A1036 104.027 -33.428 97.160 1.00150.86 C ANISOU 1844 CA SER A1036 23419 19233 14669 -5742 -7247 1250 C ATOM 1845 C SER A1036 103.360 -33.346 98.551 1.00155.34 C ANISOU 1845 C SER A1036 23315 20431 15277 -6398 -7081 1745 C ATOM 1846 O SER A1036 104.067 -33.143 99.545 1.00151.80 O ANISOU 1846 O SER A1036 22753 20056 14868 -6189 -6721 1836 O ATOM 1847 CB SER A1036 104.622 -34.815 96.937 1.00158.97 C ANISOU 1847 CB SER A1036 25475 19241 15685 -5823 -7833 1164 C ATOM 1848 OG SER A1036 103.622 -35.821 96.884 1.00175.16 O ANISOU 1848 OG SER A1036 27802 21025 17724 -6757 -8524 1460 O ATOM 1849 N PRO A1037 102.014 -33.498 98.652 1.00156.48 N ANISOU 1849 N PRO A1037 22971 21113 15372 -7198 -7336 2075 N ATOM 1850 CA PRO A1037 101.362 -33.411 99.974 1.00158.03 C ANISOU 1850 CA PRO A1037 22445 22080 15517 -7813 -7129 2552 C ATOM 1851 C PRO A1037 101.571 -34.627 100.887 1.00165.45 C ANISOU 1851 C PRO A1037 23877 22541 16444 -8532 -7494 2981 C ATOM 1852 O PRO A1037 101.186 -34.582 102.059 1.00167.20 O ANISOU 1852 O PRO A1037 23549 23414 16567 -9033 -7288 3402 O ATOM 1853 CB PRO A1037 99.886 -33.206 99.625 1.00164.58 C ANISOU 1853 CB PRO A1037 22548 23729 16256 -8383 -7300 2736 C ATOM 1854 CG PRO A1037 99.717 -33.875 98.309 1.00172.54 C ANISOU 1854 CG PRO A1037 24227 24044 17286 -8523 -7916 2541 C ATOM 1855 CD PRO A1037 101.024 -33.728 97.576 1.00162.78 C ANISOU 1855 CD PRO A1037 23782 21954 16114 -7578 -7811 2032 C ATOM 1856 N SER A1038 102.173 -35.707 100.352 1.00163.14 N ANISOU 1856 N SER A1038 24648 21123 16216 -8551 -8059 2867 N ATOM 1857 CA SER A1038 102.447 -36.948 101.076 1.00167.48 C ANISOU 1857 CA SER A1038 25888 20984 16764 -9172 -8555 3250 C ATOM 1858 C SER A1038 103.582 -36.781 102.095 1.00167.01 C ANISOU 1858 C SER A1038 25923 20800 16732 -8652 -8149 3258 C ATOM 1859 O SER A1038 104.644 -36.245 101.759 1.00160.96 O ANISOU 1859 O SER A1038 25323 19796 16040 -7654 -7799 2789 O ATOM 1860 CB SER A1038 102.769 -38.069 100.091 1.00172.10 C ANISOU 1860 CB SER A1038 27501 20405 17483 -8976 -9163 2909 C ATOM 1861 OG SER A1038 103.067 -39.292 100.745 1.00177.38 O ANISOU 1861 OG SER A1038 28135 20655 18605 -8540 -8793 2725 O ATOM 1862 N LEU A1039 103.346 -37.239 103.342 1.00166.76 N ANISOU 1862 N LEU A1039 25762 20988 16610 -9383 -8213 3824 N ATOM 1863 CA LEU A1039 104.323 -37.205 104.434 1.00163.46 C ANISOU 1863 CA LEU A1039 25453 20474 16181 -9045 -7925 3925 C ATOM 1864 C LEU A1039 105.379 -38.295 104.203 1.00169.97 C ANISOU 1864 C LEU A1039 27487 19983 17109 -8710 -8497 3772 C ATOM 1865 O LEU A1039 106.554 -38.083 104.508 1.00165.28 O ANISOU 1865 O LEU A1039 27081 19145 16572 -7894 -8223 3510 O ATOM 1866 CB LEU A1039 103.613 -37.393 105.792 1.00167.84 C ANISOU 1866 CB LEU A1039 25493 21752 16528 -10015 -7862 4622 C ATOM 1867 CG LEU A1039 104.478 -37.429 107.060 1.00170.07 C ANISOU 1867 CG LEU A1039 25847 22023 16749 -9794 -7594 4810 C ATOM 1868 CD1 LEU A1039 104.818 -36.033 107.550 1.00162.77 C ANISOU 1868 CD1 LEU A1039 24104 21976 15767 -9057 -6772 4523 C ATOM 1869 CD2 LEU A1039 103.781 -38.193 108.163 1.00171.78 C ANISOU 1869 CD2 LEU A1039 25561 22553 17155 -9977 -7191 5041 C ATOM 1870 N ASN A1040 104.954 -39.451 103.647 1.00170.27 N ANISOU 1870 N ASN A1040 27950 19363 17382 -8807 -8863 3641 N ATOM 1871 CA ASN A1040 105.820 -40.588 103.317 1.00170.71 C ANISOU 1871 CA ASN A1040 28816 18352 17695 -8084 -9084 3243 C ATOM 1872 C ASN A1040 106.866 -40.175 102.273 1.00172.89 C ANISOU 1872 C ASN A1040 29763 18086 17841 -7250 -9321 2710 C ATOM 1873 O ASN A1040 108.043 -40.511 102.424 1.00172.82 O ANISOU 1873 O ASN A1040 30383 17434 17846 -6561 -9468 2484 O ATOM 1874 CB ASN A1040 104.990 -41.776 102.806 1.00172.91 C ANISOU 1874 CB ASN A1040 28885 18411 18401 -8037 -8939 2966 C ATOM 1875 CG ASN A1040 105.801 -43.031 102.581 1.00188.08 C ANISOU 1875 CG ASN A1040 30600 19931 20930 -6629 -8143 2201 C ATOM 1876 OD1 ASN A1040 106.395 -43.596 103.509 1.00185.62 O ANISOU 1876 OD1 ASN A1040 30616 19258 20652 -6608 -8217 2460 O ATOM 1877 ND2 ASN A1040 105.847 -43.491 101.339 1.00183.41 N ANISOU 1877 ND2 ASN A1040 30626 18759 20302 -6525 -8645 1840 N ATOM 1878 N ALA A1041 106.432 -39.414 101.242 1.00170.04 N ANISOU 1878 N ALA A1041 29376 17958 17274 -7383 -9481 2564 N ATOM 1879 CA ALA A1041 107.279 -38.890 100.169 1.00165.57 C ANISOU 1879 CA ALA A1041 28935 17268 16705 -6244 -9196 1869 C ATOM 1880 C ALA A1041 108.321 -37.919 100.716 1.00162.90 C ANISOU 1880 C ALA A1041 28036 17462 16397 -5429 -8413 1698 C ATOM 1881 O ALA A1041 109.433 -37.878 100.195 1.00161.04 O ANISOU 1881 O ALA A1041 28135 16912 16142 -4486 -8304 1230 O ATOM 1882 CB ALA A1041 106.426 -38.198 99.120 1.00164.58 C ANISOU 1882 CB ALA A1041 28340 17663 16531 -6321 -9042 1668 C ATOM 1883 N ALA A1042 107.964 -37.161 101.778 1.00156.15 N ANISOU 1883 N ALA A1042 26325 17448 15556 -5803 -7897 2074 N ATOM 1884 CA ALA A1042 108.837 -36.195 102.446 1.00149.17 C ANISOU 1884 CA ALA A1042 24885 17097 14694 -5191 -7205 1975 C ATOM 1885 C ALA A1042 109.877 -36.878 103.318 1.00155.02 C ANISOU 1885 C ALA A1042 26121 17324 15457 -4938 -7381 2073 C ATOM 1886 O ALA A1042 111.027 -36.436 103.330 1.00151.23 O ANISOU 1886 O ALA A1042 25573 16890 14998 -4116 -7035 1760 O ATOM 1887 CB ALA A1042 108.012 -35.227 103.279 1.00146.96 C ANISOU 1887 CB ALA A1042 23639 17824 14375 -5671 -6709 2308 C ATOM 1888 N LYS A1043 109.477 -37.939 104.061 1.00157.60 N ANISOU 1888 N LYS A1043 26929 17191 15760 -5678 -7943 2543 N ATOM 1889 CA LYS A1043 110.366 -38.704 104.948 1.00159.94 C ANISOU 1889 CA LYS A1043 27796 16912 16060 -5516 -8242 2714 C ATOM 1890 C LYS A1043 111.419 -39.472 104.147 1.00166.39 C ANISOU 1890 C LYS A1043 29520 16781 16919 -4630 -8685 2213 C ATOM 1891 O LYS A1043 112.551 -39.610 104.611 1.00165.23 O ANISOU 1891 O LYS A1043 29555 16439 16785 -3946 -8631 2074 O ATOM 1892 CB LYS A1043 109.575 -39.660 105.856 1.00168.91 C ANISOU 1892 CB LYS A1043 29283 17774 17121 -6639 -8802 3408 C ATOM 1893 CG LYS A1043 108.883 -38.971 107.022 1.00167.47 C ANISOU 1893 CG LYS A1043 28181 18643 16807 -7334 -8297 3921 C ATOM 1894 CD LYS A1043 108.221 -39.979 107.939 1.00173.58 C ANISOU 1894 CD LYS A1043 28904 19391 17659 -7964 -8368 4396 C ATOM 1895 CE LYS A1043 107.506 -39.308 109.082 1.00176.30 C ANISOU 1895 CE LYS A1043 28233 20891 17864 -8408 -7720 4768 C ATOM 1896 NZ LYS A1043 106.937 -40.300 110.031 1.00183.01 N ANISOU 1896 NZ LYS A1043 28540 21881 19115 -8125 -7062 4765 N ATOM 1897 N SER A1044 111.042 -39.953 102.941 1.00166.14 N ANISOU 1897 N SER A1044 30023 16227 16877 -4593 -9123 1912 N ATOM 1898 CA SER A1044 111.926 -40.665 102.017 1.00169.39 C ANISOU 1898 CA SER A1044 31298 15807 17254 -3674 -9552 1339 C ATOM 1899 C SER A1044 112.879 -39.692 101.307 1.00167.84 C ANISOU 1899 C SER A1044 30571 16194 17006 -2581 -8854 761 C ATOM 1900 O SER A1044 113.972 -40.102 100.909 1.00169.75 O ANISOU 1900 O SER A1044 31265 16052 17180 -1622 -8988 316 O ATOM 1901 CB SER A1044 111.115 -41.465 101.006 1.00174.50 C ANISOU 1901 CB SER A1044 32131 16148 18023 -3860 -9771 1105 C ATOM 1902 OG SER A1044 110.415 -42.512 101.659 1.00180.61 O ANISOU 1902 OG SER A1044 32117 17222 19283 -4231 -9216 1323 O ATOM 1903 N GLU A1045 112.467 -38.407 101.160 1.00157.79 N ANISOU 1903 N GLU A1045 28341 15873 15739 -2730 -8137 786 N ATOM 1904 CA GLU A1045 113.274 -37.333 100.566 1.00151.76 C ANISOU 1904 CA GLU A1045 26997 15752 14913 -1910 -7451 371 C ATOM 1905 C GLU A1045 114.384 -36.923 101.549 1.00152.27 C ANISOU 1905 C GLU A1045 26681 16153 15023 -1470 -7048 434 C ATOM 1906 O GLU A1045 115.523 -36.700 101.132 1.00150.47 O ANISOU 1906 O GLU A1045 26376 16081 14714 -604 -6795 46 O ATOM 1907 CB GLU A1045 112.397 -36.117 100.220 1.00147.81 C ANISOU 1907 CB GLU A1045 25700 16043 14418 -2300 -6937 457 C ATOM 1908 CG GLU A1045 111.833 -36.134 98.809 1.00162.08 C ANISOU 1908 CG GLU A1045 27736 17738 16111 -2236 -7117 144 C ATOM 1909 CD GLU A1045 112.766 -35.710 97.691 1.00184.54 C ANISOU 1909 CD GLU A1045 30602 20741 18773 -1302 -6823 -392 C ATOM 1910 OE1 GLU A1045 113.599 -34.800 97.912 1.00176.31 O ANISOU 1910 OE1 GLU A1045 29001 20268 17719 -864 -6229 -452 O ATOM 1911 OE2 GLU A1045 112.620 -36.248 96.569 1.00183.92 O ANISOU 1911 OE2 GLU A1045 31078 20273 18529 -1063 -7191 -736 O ATOM 1912 N LEU A1046 114.038 -36.832 102.852 1.00148.22 N ANISOU 1912 N LEU A1046 25898 15821 14599 -2091 -6998 934 N ATOM 1913 CA LEU A1046 114.950 -36.495 103.947 1.00145.85 C ANISOU 1913 CA LEU A1046 25265 15823 14327 -1818 -6696 1062 C ATOM 1914 C LEU A1046 115.950 -37.642 104.172 1.00155.46 C ANISOU 1914 C LEU A1046 27234 16304 15532 -1254 -7223 944 C ATOM 1915 O LEU A1046 117.137 -37.379 104.367 1.00153.93 O ANISOU 1915 O LEU A1046 26824 16342 15318 -528 -6976 731 O ATOM 1916 CB LEU A1046 114.146 -36.189 105.234 1.00144.69 C ANISOU 1916 CB LEU A1046 24687 16086 14201 -2682 -6553 1625 C ATOM 1917 CG LEU A1046 114.906 -35.722 106.494 1.00146.89 C ANISOU 1917 CG LEU A1046 24558 16781 14471 -2534 -6220 1800 C ATOM 1918 CD1 LEU A1046 115.657 -34.414 106.259 1.00140.88 C ANISOU 1918 CD1 LEU A1046 23122 16683 13725 -1946 -5568 1469 C ATOM 1919 CD2 LEU A1046 113.952 -35.538 107.655 1.00149.29 C ANISOU 1919 CD2 LEU A1046 24499 17519 14707 -3403 -6121 2327 C ATOM 1920 N ASP A1047 115.472 -38.906 104.110 1.00158.70 N ANISOU 1920 N ASP A1047 28537 15820 15942 -1575 -7995 1074 N ATOM 1921 CA ASP A1047 116.296 -40.107 104.271 1.00165.20 C ANISOU 1921 CA ASP A1047 30257 15763 16747 -1019 -8660 949 C ATOM 1922 C ASP A1047 117.328 -40.258 103.151 1.00171.45 C ANISOU 1922 C ASP A1047 31292 16415 17435 191 -8667 236 C ATOM 1923 O ASP A1047 118.416 -40.768 103.399 1.00174.59 O ANISOU 1923 O ASP A1047 32013 16528 17795 1003 -8899 20 O ATOM 1924 CB ASP A1047 115.420 -41.368 104.386 1.00174.49 C ANISOU 1924 CB ASP A1047 32411 15947 17940 -1771 -9557 1287 C ATOM 1925 CG ASP A1047 114.745 -41.566 105.736 1.00178.28 C ANISOU 1925 CG ASP A1047 32550 16661 18527 -2760 -9461 2011 C ATOM 1926 OD1 ASP A1047 114.885 -40.684 106.610 1.00175.68 O ANISOU 1926 OD1 ASP A1047 31669 16973 18106 -2994 -9085 2295 O ATOM 1927 OD2 ASP A1047 114.067 -42.599 105.914 1.00182.97 O ANISOU 1927 OD2 ASP A1047 32618 17390 19511 -3006 -9013 2132 O ATOM 1928 N LYS A1048 116.994 -39.802 101.930 1.00166.72 N ANISOU 1928 N LYS A1048 30503 16093 16749 340 -8409 -128 N ATOM 1929 CA LYS A1048 117.889 -39.845 100.772 1.00168.80 C ANISOU 1929 CA LYS A1048 30893 16421 16821 1445 -8323 -805 C ATOM 1930 C LYS A1048 118.994 -38.784 100.908 1.00168.44 C ANISOU 1930 C LYS A1048 29914 17366 16720 2069 -7537 -959 C ATOM 1931 O LYS A1048 120.150 -39.061 100.582 1.00171.53 O ANISOU 1931 O LYS A1048 30378 17838 16957 3082 -7542 -1385 O ATOM 1932 CB LYS A1048 117.094 -39.629 99.472 1.00170.98 C ANISOU 1932 CB LYS A1048 31253 16735 16976 1277 -8301 -1067 C ATOM 1933 CG LYS A1048 117.815 -40.123 98.225 1.00186.04 C ANISOU 1933 CG LYS A1048 33583 18475 18628 2336 -8439 -1769 C ATOM 1934 CD LYS A1048 117.315 -39.424 96.969 1.00188.72 C ANISOU 1934 CD LYS A1048 33668 19267 18771 2297 -8121 -2029 C ATOM 1935 CE LYS A1048 118.141 -39.774 95.753 1.00192.99 C ANISOU 1935 CE LYS A1048 33778 20312 19238 3102 -7587 -2602 C ATOM 1936 NZ LYS A1048 119.506 -39.179 95.807 1.00196.64 N ANISOU 1936 NZ LYS A1048 33625 21558 19531 3920 -7022 -2804 N ATOM 1937 N ALA A1049 118.629 -37.575 101.389 1.00157.95 N ANISOU 1937 N ALA A1049 27715 16805 15495 1464 -6902 -618 N ATOM 1938 CA ALA A1049 119.535 -36.442 101.582 1.00152.60 C ANISOU 1938 CA ALA A1049 26153 17044 14785 1822 -6195 -674 C ATOM 1939 C ALA A1049 120.518 -36.671 102.724 1.00158.24 C ANISOU 1939 C ALA A1049 26754 17806 15563 2134 -6245 -534 C ATOM 1940 O ALA A1049 121.663 -36.223 102.635 1.00157.71 O ANISOU 1940 O ALA A1049 26197 18325 15401 2783 -5890 -755 O ATOM 1941 CB ALA A1049 118.735 -35.174 101.835 1.00146.13 C ANISOU 1941 CB ALA A1049 24620 16841 14063 1063 -5659 -358 C ATOM 1942 N ILE A1050 120.071 -37.354 103.796 1.00156.78 N ANISOU 1942 N ILE A1050 26995 17064 15511 1628 -6697 -134 N ATOM 1943 CA ILE A1050 120.874 -37.634 104.989 1.00157.92 C ANISOU 1943 CA ILE A1050 27113 17186 15703 1834 -6830 68 C ATOM 1944 C ILE A1050 121.608 -38.981 104.874 1.00169.70 C ANISOU 1944 C ILE A1050 29449 17900 17131 2648 -7534 -200 C ATOM 1945 O ILE A1050 122.823 -39.033 105.074 1.00171.72 O ANISOU 1945 O ILE A1050 29489 18439 17319 3491 -7474 -438 O ATOM 1946 CB ILE A1050 120.012 -37.505 106.289 1.00158.95 C ANISOU 1946 CB ILE A1050 27161 17291 15942 821 -6870 696 C ATOM 1947 CG1 ILE A1050 119.389 -36.081 106.451 1.00151.77 C ANISOU 1947 CG1 ILE A1050 25375 17228 15064 217 -6164 867 C ATOM 1948 CG2 ILE A1050 120.772 -37.943 107.555 1.00162.25 C ANISOU 1948 CG2 ILE A1050 27700 17581 16368 993 -7125 946 C ATOM 1949 CD1 ILE A1050 120.372 -34.839 106.565 1.00154.90 C ANISOU 1949 CD1 ILE A1050 24928 18486 15441 629 -5521 695 C ATOM 1950 N GLY A1051 120.865 -40.041 104.561 1.00170.73 N ANISOU 1950 N GLY A1051 30528 17069 17273 2396 -8227 -163 N ATOM 1951 CA GLY A1051 121.398 -41.393 104.429 1.00179.11 C ANISOU 1951 CA GLY A1051 32595 17184 18275 3133 -9044 -424 C ATOM 1952 C GLY A1051 120.625 -42.395 105.259 1.00182.12 C ANISOU 1952 C GLY A1051 33132 17080 18988 2221 -9211 166 C ATOM 1953 O GLY A1051 120.075 -43.362 104.721 1.00182.62 O ANISOU 1953 O GLY A1051 33175 16884 19329 1981 -9085 143 O ATOM 1954 N ARG A1052 120.574 -42.156 106.580 1.00179.12 N ANISOU 1954 N ARG A1052 33002 16546 18509 1722 -9570 689 N ATOM 1955 CA ARG A1052 119.878 -43.010 107.546 1.00179.34 C ANISOU 1955 CA ARG A1052 32991 16356 18794 847 -9574 1323 C ATOM 1956 C ARG A1052 118.363 -42.746 107.587 1.00180.25 C ANISOU 1956 C ARG A1052 33008 16560 18918 -409 -9495 1754 C ATOM 1957 O ARG A1052 117.884 -41.786 106.973 1.00177.88 O ANISOU 1957 O ARG A1052 32825 16385 18378 -714 -9604 1654 O ATOM 1958 CB ARG A1052 120.516 -42.895 108.951 1.00179.64 C ANISOU 1958 CB ARG A1052 32938 16546 18771 861 -9663 1716 C ATOM 1959 CG ARG A1052 120.534 -41.484 109.553 1.00182.74 C ANISOU 1959 CG ARG A1052 32872 17619 18942 514 -9399 1889 C ATOM 1960 CD ARG A1052 119.556 -41.339 110.704 1.00184.63 C ANISOU 1960 CD ARG A1052 32972 18047 19133 -733 -9351 2625 C ATOM 1961 NE ARG A1052 119.561 -39.982 111.253 1.00174.88 N ANISOU 1961 NE ARG A1052 30630 17951 17866 -974 -8495 2703 N ATOM 1962 CZ ARG A1052 118.707 -39.540 112.171 1.00179.88 C ANISOU 1962 CZ ARG A1052 30885 19065 18396 -1931 -8241 3223 C ATOM 1963 NH1 ARG A1052 117.763 -40.340 112.651 1.00171.70 N ANISOU 1963 NH1 ARG A1052 30402 17568 17266 -2839 -8732 3783 N ATOM 1964 NH2 ARG A1052 118.783 -38.291 112.608 1.00155.19 N ANISOU 1964 NH2 ARG A1052 26833 16907 15226 -1997 -7516 3186 N ATOM 1965 N ASN A1053 117.616 -43.613 108.307 1.00178.57 N ANISOU 1965 N ASN A1053 32779 16170 18901 -1128 -9487 2249 N ATOM 1966 CA ASN A1053 116.173 -43.471 108.489 1.00177.35 C ANISOU 1966 CA ASN A1053 32487 16173 18724 -2317 -9450 2700 C ATOM 1967 C ASN A1053 115.964 -42.466 109.627 1.00177.98 C ANISOU 1967 C ASN A1053 32271 16820 18535 -3025 -9372 3221 C ATOM 1968 O ASN A1053 116.194 -42.788 110.799 1.00178.36 O ANISOU 1968 O ASN A1053 32162 17016 18590 -3154 -9262 3611 O ATOM 1969 CB ASN A1053 115.510 -44.826 108.791 1.00178.73 C ANISOU 1969 CB ASN A1053 32404 16230 19277 -2602 -9127 2924 C ATOM 1970 CG ASN A1053 114.182 -45.044 108.100 1.00191.76 C ANISOU 1970 CG ASN A1053 32933 18595 21334 -2899 -8113 2728 C ATOM 1971 OD1 ASN A1053 113.957 -46.076 107.458 1.00189.60 O ANISOU 1971 OD1 ASN A1053 32909 17839 21293 -2798 -8211 2525 O ATOM 1972 ND2 ASN A1053 113.261 -44.091 108.224 1.00184.81 N ANISOU 1972 ND2 ASN A1053 32250 17862 20108 -3885 -8527 3103 N ATOM 1973 N THR A1054 115.608 -41.223 109.257 1.00171.48 N ANISOU 1973 N THR A1054 31281 16403 17471 -3410 -9334 3193 N ATOM 1974 CA THR A1054 115.416 -40.100 110.180 1.00164.97 C ANISOU 1974 CA THR A1054 29447 16670 16566 -3780 -8588 3458 C ATOM 1975 C THR A1054 114.038 -40.091 110.828 1.00170.28 C ANISOU 1975 C THR A1054 29870 17734 17096 -5059 -8574 4100 C ATOM 1976 O THR A1054 113.930 -39.794 112.021 1.00169.36 O ANISOU 1976 O THR A1054 29365 18170 16812 -5489 -8339 4527 O ATOM 1977 CB THR A1054 115.719 -38.766 109.485 1.00165.76 C ANISOU 1977 CB THR A1054 28664 17584 16735 -3184 -7785 2931 C ATOM 1978 OG1 THR A1054 114.845 -38.619 108.367 1.00166.32 O ANISOU 1978 OG1 THR A1054 28688 17654 16852 -3423 -7748 2740 O ATOM 1979 CG2 THR A1054 117.174 -38.651 109.037 1.00163.52 C ANISOU 1979 CG2 THR A1054 28412 17201 16518 -1992 -7687 2385 C ATOM 1980 N ASN A1055 112.990 -40.411 110.035 1.00169.27 N ANISOU 1980 N ASN A1055 29921 17400 16995 -5654 -8823 4157 N ATOM 1981 CA ASN A1055 111.577 -40.445 110.428 1.00171.49 C ANISOU 1981 CA ASN A1055 29856 18163 17139 -6871 -8805 4725 C ATOM 1982 C ASN A1055 111.087 -39.087 110.979 1.00170.08 C ANISOU 1982 C ASN A1055 28488 19316 16820 -7075 -7948 4789 C ATOM 1983 O ASN A1055 110.383 -39.029 111.992 1.00172.25 O ANISOU 1983 O ASN A1055 28372 20220 16854 -7910 -7828 5346 O ATOM 1984 CB ASN A1055 111.277 -41.620 111.378 1.00172.29 C ANISOU 1984 CB ASN A1055 29819 18185 17460 -6920 -8568 5005 C ATOM 1985 CG ASN A1055 111.297 -42.962 110.688 1.00186.31 C ANISOU 1985 CG ASN A1055 31157 19649 19983 -5678 -7789 4287 C ATOM 1986 OD1 ASN A1055 110.594 -43.194 109.691 1.00182.75 O ANISOU 1986 OD1 ASN A1055 30869 18945 19623 -5986 -8025 4148 O ATOM 1987 ND2 ASN A1055 112.093 -43.883 111.213 1.00181.20 N ANISOU 1987 ND2 ASN A1055 31142 18345 19359 -5409 -8171 4443 N ATOM 1988 N GLY A1056 111.472 -38.016 110.284 1.00159.54 N ANISOU 1988 N GLY A1056 26598 18407 15611 -6274 -7366 4198 N ATOM 1989 CA GLY A1056 111.082 -36.649 110.608 1.00153.48 C ANISOU 1989 CA GLY A1056 24793 18766 14756 -6252 -6592 4108 C ATOM 1990 C GLY A1056 111.981 -35.875 111.549 1.00153.34 C ANISOU 1990 C GLY A1056 24375 19218 14670 -5742 -6129 4012 C ATOM 1991 O GLY A1056 111.886 -34.647 111.606 1.00147.40 O ANISOU 1991 O GLY A1056 22893 19219 13895 -5469 -5530 3760 O ATOM 1992 N VAL A1057 112.839 -36.574 112.310 1.00153.12 N ANISOU 1992 N VAL A1057 24852 18727 14598 -5615 -6455 4215 N ATOM 1993 CA VAL A1057 113.723 -35.935 113.286 1.00150.02 C ANISOU 1993 CA VAL A1057 24123 18761 14115 -5190 -6103 4163 C ATOM 1994 C VAL A1057 115.197 -35.999 112.847 1.00152.25 C ANISOU 1994 C VAL A1057 24717 18533 14599 -4194 -6195 3713 C ATOM 1995 O VAL A1057 115.687 -37.073 112.493 1.00156.89 O ANISOU 1995 O VAL A1057 26065 18268 15277 -3953 -6773 3705 O ATOM 1996 CB VAL A1057 113.511 -36.482 114.734 1.00158.95 C ANISOU 1996 CB VAL A1057 25386 20061 14948 -5850 -6306 4795 C ATOM 1997 CG1 VAL A1057 114.173 -35.575 115.769 1.00155.02 C ANISOU 1997 CG1 VAL A1057 24375 20232 14293 -5500 -5847 4714 C ATOM 1998 CG2 VAL A1057 112.027 -36.657 115.059 1.00162.89 C ANISOU 1998 CG2 VAL A1057 25609 21083 15198 -6916 -6296 5303 C ATOM 1999 N ILE A1058 115.894 -34.841 112.880 1.00142.13 N ANISOU 1999 N ILE A1058 22841 17802 13360 -3619 -5654 3342 N ATOM 2000 CA ILE A1058 117.318 -34.707 112.532 1.00139.57 C ANISOU 2000 CA ILE A1058 22577 17276 13176 -2720 -5632 2936 C ATOM 2001 C ILE A1058 118.120 -33.983 113.646 1.00140.83 C ANISOU 2001 C ILE A1058 22306 17972 13232 -2519 -5344 2964 C ATOM 2002 O ILE A1058 117.541 -33.529 114.639 1.00140.19 O ANISOU 2002 O ILE A1058 21890 18420 12955 -3019 -5122 3234 O ATOM 2003 CB ILE A1058 117.550 -34.071 111.122 1.00138.39 C ANISOU 2003 CB ILE A1058 22199 17190 13192 -2193 -5343 2413 C ATOM 2004 CG1 ILE A1058 116.886 -32.679 110.990 1.00133.15 C ANISOU 2004 CG1 ILE A1058 20814 17268 12508 -2407 -4752 2302 C ATOM 2005 CG2 ILE A1058 117.131 -35.022 109.996 1.00142.08 C ANISOU 2005 CG2 ILE A1058 23265 16977 13740 -2187 -5767 2306 C ATOM 2006 CD1 ILE A1058 117.567 -31.737 110.035 1.00133.43 C ANISOU 2006 CD1 ILE A1058 20521 17524 12654 -1831 -4395 1851 C ATOM 2007 N THR A1059 119.452 -33.897 113.476 1.00135.87 N ANISOU 2007 N THR A1059 21667 17259 12699 -1777 -5365 2672 N ATOM 2008 CA THR A1059 120.357 -33.224 114.412 1.00133.52 C ANISOU 2008 CA THR A1059 20969 17440 12324 -1544 -5159 2654 C ATOM 2009 C THR A1059 120.839 -31.900 113.800 1.00131.49 C ANISOU 2009 C THR A1059 20085 17713 12163 -1207 -4641 2247 C ATOM 2010 O THR A1059 120.719 -31.713 112.589 1.00129.45 O ANISOU 2010 O THR A1059 19781 17375 12028 -1016 -4501 1974 O ATOM 2011 CB THR A1059 121.533 -34.147 114.797 1.00145.53 C ANISOU 2011 CB THR A1059 22890 18551 13852 -1011 -5629 2689 C ATOM 2012 OG1 THR A1059 122.388 -34.346 113.671 1.00144.82 O ANISOU 2012 OG1 THR A1059 22892 18211 13923 -261 -5710 2271 O ATOM 2013 CG2 THR A1059 121.078 -35.491 115.362 1.00150.47 C ANISOU 2013 CG2 THR A1059 24254 18548 14370 -1390 -6231 3150 C ATOM 2014 N LYS A1060 121.385 -30.989 114.631 1.00125.98 N ANISOU 2014 N LYS A1060 18950 17534 11383 -1179 -4401 2227 N ATOM 2015 CA LYS A1060 121.927 -29.685 114.217 1.00121.68 C ANISOU 2015 CA LYS A1060 17865 17458 10908 -968 -3994 1913 C ATOM 2016 C LYS A1060 123.005 -29.868 113.132 1.00126.78 C ANISOU 2016 C LYS A1060 18456 18018 11697 -348 -4016 1619 C ATOM 2017 O LYS A1060 123.032 -29.103 112.166 1.00123.60 O ANISOU 2017 O LYS A1060 17776 17821 11366 -264 -3717 1386 O ATOM 2018 CB LYS A1060 122.499 -28.941 115.444 1.00123.51 C ANISOU 2018 CB LYS A1060 17786 18140 11002 -1053 -3907 1976 C ATOM 2019 CG LYS A1060 123.003 -27.516 115.192 1.00124.71 C ANISOU 2019 CG LYS A1060 17452 18728 11202 -994 -3565 1710 C ATOM 2020 CD LYS A1060 123.644 -26.945 116.463 1.00127.71 C ANISOU 2020 CD LYS A1060 17624 19465 11436 -1057 -3606 1761 C ATOM 2021 CE LYS A1060 124.551 -25.767 116.195 1.00128.12 C ANISOU 2021 CE LYS A1060 17268 19847 11563 -961 -3431 1530 C ATOM 2022 NZ LYS A1060 123.841 -24.467 116.306 1.00129.20 N ANISOU 2022 NZ LYS A1060 17286 20159 11644 -1272 -3188 1398 N ATOM 2023 N ASP A1061 123.861 -30.903 113.287 1.00128.32 N ANISOU 2023 N ASP A1061 18924 17937 11893 105 -4390 1637 N ATOM 2024 CA ASP A1061 124.933 -31.262 112.355 1.00130.67 C ANISOU 2024 CA ASP A1061 19154 18241 12252 819 -4451 1337 C ATOM 2025 C ASP A1061 124.357 -31.666 110.978 1.00134.07 C ANISOU 2025 C ASP A1061 19880 18323 12737 964 -4447 1129 C ATOM 2026 O ASP A1061 124.892 -31.249 109.947 1.00132.87 O ANISOU 2026 O ASP A1061 19435 18466 12585 1334 -4205 839 O ATOM 2027 CB ASP A1061 125.813 -32.382 112.946 1.00138.46 C ANISOU 2027 CB ASP A1061 20444 18963 13200 1338 -4938 1397 C ATOM 2028 CG ASP A1061 126.290 -32.128 114.370 1.00154.95 C ANISOU 2028 CG ASP A1061 22340 21333 15200 1164 -5033 1645 C ATOM 2029 OD1 ASP A1061 126.976 -31.104 114.596 1.00154.63 O ANISOU 2029 OD1 ASP A1061 21693 21914 15144 1159 -4746 1554 O ATOM 2030 OD2 ASP A1061 125.998 -32.965 115.253 1.00165.36 O ANISOU 2030 OD2 ASP A1061 24146 22242 16441 1003 -5435 1948 O ATOM 2031 N GLU A1062 123.246 -32.441 110.975 1.00131.18 N ANISOU 2031 N GLU A1062 20078 17383 12383 611 -4723 1305 N ATOM 2032 CA GLU A1062 122.540 -32.892 109.768 1.00131.14 C ANISOU 2032 CA GLU A1062 20437 16975 12415 637 -4810 1140 C ATOM 2033 C GLU A1062 121.818 -31.718 109.088 1.00130.27 C ANISOU 2033 C GLU A1062 19908 17259 12327 280 -4329 1049 C ATOM 2034 O GLU A1062 121.764 -31.665 107.856 1.00129.00 O ANISOU 2034 O GLU A1062 19787 17060 12165 526 -4238 785 O ATOM 2035 CB GLU A1062 121.550 -34.018 110.102 1.00135.78 C ANISOU 2035 CB GLU A1062 21722 16867 12999 201 -5301 1434 C ATOM 2036 CG GLU A1062 122.215 -35.356 110.388 1.00151.18 C ANISOU 2036 CG GLU A1062 24333 18173 14935 680 -5924 1451 C ATOM 2037 CD GLU A1062 121.314 -36.478 110.872 1.00173.55 C ANISOU 2037 CD GLU A1062 27925 20268 17746 124 -6501 1851 C ATOM 2038 OE1 GLU A1062 120.224 -36.188 111.416 1.00164.66 O ANISOU 2038 OE1 GLU A1062 26675 19314 16575 -733 -6369 2223 O ATOM 2039 OE2 GLU A1062 121.724 -37.655 110.748 1.00172.04 O ANISOU 2039 OE2 GLU A1062 28460 19351 17558 550 -7116 1807 O ATOM 2040 N ALA A1063 121.279 -30.776 109.900 1.00123.98 N ANISOU 2040 N ALA A1063 18742 16845 11519 -247 -4052 1248 N ATOM 2041 CA ALA A1063 120.605 -29.555 109.446 1.00119.54 C ANISOU 2041 CA ALA A1063 17800 16647 10974 -543 -3649 1170 C ATOM 2042 C ALA A1063 121.623 -28.629 108.781 1.00122.68 C ANISOU 2042 C ALA A1063 17784 17449 11380 -181 -3341 923 C ATOM 2043 O ALA A1063 121.316 -28.006 107.762 1.00121.14 O ANISOU 2043 O ALA A1063 17469 17367 11192 -197 -3124 779 O ATOM 2044 CB ALA A1063 119.949 -28.850 110.622 1.00118.28 C ANISOU 2044 CB ALA A1063 17394 16797 10750 -1042 -3499 1390 C ATOM 2045 N GLU A1064 122.844 -28.573 109.346 1.00120.79 N ANISOU 2045 N GLU A1064 17322 17456 11116 112 -3355 909 N ATOM 2046 CA GLU A1064 123.969 -27.797 108.833 1.00120.28 C ANISOU 2046 CA GLU A1064 16802 17875 11024 387 -3107 745 C ATOM 2047 C GLU A1064 124.420 -28.390 107.498 1.00126.28 C ANISOU 2047 C GLU A1064 17653 18606 11721 910 -3114 497 C ATOM 2048 O GLU A1064 124.768 -27.629 106.597 1.00125.68 O ANISOU 2048 O GLU A1064 17259 18915 11578 960 -2826 381 O ATOM 2049 CB GLU A1064 125.121 -27.795 109.846 1.00123.62 C ANISOU 2049 CB GLU A1064 16954 18595 11419 555 -3201 817 C ATOM 2050 CG GLU A1064 126.069 -26.617 109.691 1.00132.94 C ANISOU 2050 CG GLU A1064 17561 20381 12568 504 -2931 767 C ATOM 2051 CD GLU A1064 127.188 -26.506 110.711 1.00151.67 C ANISOU 2051 CD GLU A1064 19604 23115 14908 585 -3048 849 C ATOM 2052 OE1 GLU A1064 127.070 -27.093 111.812 1.00142.70 O ANISOU 2052 OE1 GLU A1064 18693 21758 13767 558 -3306 985 O ATOM 2053 OE2 GLU A1064 128.179 -25.799 110.412 1.00143.71 O ANISOU 2053 OE2 GLU A1064 18097 22653 13854 619 -2895 809 O ATOM 2054 N LYS A1065 124.377 -29.741 107.364 1.00125.73 N ANISOU 2054 N LYS A1065 18068 18064 11640 1287 -3474 420 N ATOM 2055 CA LYS A1065 124.724 -30.466 106.135 1.00128.97 C ANISOU 2055 CA LYS A1065 18692 18368 11943 1888 -3562 114 C ATOM 2056 C LYS A1065 123.728 -30.113 105.006 1.00129.65 C ANISOU 2056 C LYS A1065 18922 18335 12003 1630 -3400 25 C ATOM 2057 O LYS A1065 124.157 -29.872 103.876 1.00130.13 O ANISOU 2057 O LYS A1065 18817 18717 11909 1961 -3195 -205 O ATOM 2058 CB LYS A1065 124.781 -31.985 106.383 1.00136.66 C ANISOU 2058 CB LYS A1065 20308 18696 12921 2312 -4105 54 C ATOM 2059 CG LYS A1065 125.346 -32.779 105.207 1.00158.00 C ANISOU 2059 CG LYS A1065 23256 21313 15462 3128 -4253 -358 C ATOM 2060 CD LYS A1065 125.118 -34.277 105.358 1.00174.01 C ANISOU 2060 CD LYS A1065 26133 22471 17511 3474 -4905 -428 C ATOM 2061 CE LYS A1065 125.202 -35.011 104.037 1.00188.64 C ANISOU 2061 CE LYS A1065 28422 24061 19190 4148 -5097 -879 C ATOM 2062 NZ LYS A1065 126.597 -35.111 103.530 1.00202.23 N ANISOU 2062 NZ LYS A1065 29752 26401 20685 5145 -4964 -1273 N ATOM 2063 N LEU A1066 122.413 -30.054 105.327 1.00122.91 N ANISOU 2063 N LEU A1066 18326 17111 11262 1037 -3488 223 N ATOM 2064 CA LEU A1066 121.358 -29.673 104.385 1.00120.16 C ANISOU 2064 CA LEU A1066 18080 16671 10905 744 -3381 176 C ATOM 2065 C LEU A1066 121.480 -28.190 104.043 1.00120.77 C ANISOU 2065 C LEU A1066 17640 17294 10955 544 -2940 191 C ATOM 2066 O LEU A1066 121.217 -27.811 102.898 1.00120.75 O ANISOU 2066 O LEU A1066 17637 17385 10858 580 -2801 65 O ATOM 2067 CB LEU A1066 119.958 -29.967 104.953 1.00118.96 C ANISOU 2067 CB LEU A1066 18206 16134 10859 149 -3593 418 C ATOM 2068 CG LEU A1066 119.429 -31.390 104.786 1.00127.61 C ANISOU 2068 CG LEU A1066 19963 16564 11960 154 -4100 426 C ATOM 2069 CD1 LEU A1066 118.324 -31.673 105.780 1.00127.54 C ANISOU 2069 CD1 LEU A1066 20081 16359 12021 -531 -4294 796 C ATOM 2070 CD2 LEU A1066 118.912 -31.630 103.378 1.00131.50 C ANISOU 2070 CD2 LEU A1066 20744 16839 12380 267 -4192 185 C ATOM 2071 N PHE A1067 121.891 -27.355 105.030 1.00114.53 N ANISOU 2071 N PHE A1067 16469 16823 10225 321 -2773 352 N ATOM 2072 CA PHE A1067 122.100 -25.914 104.846 1.00111.43 C ANISOU 2072 CA PHE A1067 15671 16852 9815 87 -2453 394 C ATOM 2073 C PHE A1067 123.276 -25.664 103.889 1.00117.82 C ANISOU 2073 C PHE A1067 16198 18107 10460 423 -2257 269 C ATOM 2074 O PHE A1067 123.126 -24.892 102.941 1.00116.76 O ANISOU 2074 O PHE A1067 15963 18165 10234 292 -2060 262 O ATOM 2075 CB PHE A1067 122.305 -25.193 106.194 1.00111.12 C ANISOU 2075 CB PHE A1067 15387 16979 9854 -210 -2417 559 C ATOM 2076 CG PHE A1067 122.621 -23.717 106.089 1.00110.65 C ANISOU 2076 CG PHE A1067 15012 17249 9782 -464 -2196 600 C ATOM 2077 CD1 PHE A1067 121.613 -22.786 105.866 1.00111.01 C ANISOU 2077 CD1 PHE A1067 15131 17186 9862 -762 -2128 617 C ATOM 2078 CD2 PHE A1067 123.925 -23.257 106.231 1.00114.18 C ANISOU 2078 CD2 PHE A1067 15102 18108 10172 -414 -2109 632 C ATOM 2079 CE1 PHE A1067 121.907 -21.423 105.775 1.00111.34 C ANISOU 2079 CE1 PHE A1067 15009 17403 9891 -996 -2022 662 C ATOM 2080 CE2 PHE A1067 124.218 -21.895 106.140 1.00116.34 C ANISOU 2080 CE2 PHE A1067 15162 18611 10429 -755 -1986 715 C ATOM 2081 CZ PHE A1067 123.207 -20.988 105.917 1.00112.20 C ANISOU 2081 CZ PHE A1067 14830 17852 9950 -1040 -1966 729 C ATOM 2082 N ASN A1068 124.430 -26.339 104.123 1.00117.53 N ANISOU 2082 N ASN A1068 16019 18285 10351 870 -2325 186 N ATOM 2083 CA ASN A1068 125.624 -26.231 103.278 1.00120.38 C ANISOU 2083 CA ASN A1068 16002 19246 10492 1258 -2126 58 C ATOM 2084 C ASN A1068 125.285 -26.558 101.820 1.00124.38 C ANISOU 2084 C ASN A1068 16729 19733 10796 1539 -2056 -153 C ATOM 2085 O ASN A1068 125.795 -25.888 100.921 1.00126.04 O ANISOU 2085 O ASN A1068 16607 20504 10780 1556 -1775 -162 O ATOM 2086 CB ASN A1068 126.758 -27.119 103.803 1.00125.24 C ANISOU 2086 CB ASN A1068 16458 20069 11058 1821 -2284 -47 C ATOM 2087 CG ASN A1068 127.601 -26.513 104.914 1.00151.17 C ANISOU 2087 CG ASN A1068 19270 23752 14415 1600 -2250 147 C ATOM 2088 OD1 ASN A1068 127.117 -25.807 105.812 1.00142.88 O ANISOU 2088 OD1 ASN A1068 18238 22524 13526 1051 -2268 351 O ATOM 2089 ND2 ASN A1068 128.888 -26.830 104.908 1.00147.36 N ANISOU 2089 ND2 ASN A1068 18352 23849 13789 2078 -2235 57 N ATOM 2090 N GLN A1069 124.377 -27.541 101.595 1.00119.35 N ANISOU 2090 N GLN A1069 16670 18465 10215 1683 -2335 -290 N ATOM 2091 CA GLN A1069 123.894 -27.929 100.265 1.00120.19 C ANISOU 2091 CA GLN A1069 17099 18439 10129 1920 -2357 -517 C ATOM 2092 C GLN A1069 123.137 -26.764 99.633 1.00120.97 C ANISOU 2092 C GLN A1069 17108 18646 10209 1397 -2131 -365 C ATOM 2093 O GLN A1069 123.410 -26.426 98.483 1.00122.83 O ANISOU 2093 O GLN A1069 17247 19251 10171 1538 -1932 -459 O ATOM 2094 CB GLN A1069 123.001 -29.177 100.338 1.00122.29 C ANISOU 2094 CB GLN A1069 18045 17920 10498 2037 -2805 -642 C ATOM 2095 CG GLN A1069 123.785 -30.484 100.407 1.00139.85 C ANISOU 2095 CG GLN A1069 20551 19951 12636 2765 -3116 -903 C ATOM 2096 CD GLN A1069 122.923 -31.715 100.591 1.00159.62 C ANISOU 2096 CD GLN A1069 23831 21563 15253 2773 -3661 -966 C ATOM 2097 OE1 GLN A1069 121.687 -31.676 100.527 1.00153.00 O ANISOU 2097 OE1 GLN A1069 23284 20314 14533 2218 -3794 -824 O ATOM 2098 NE2 GLN A1069 123.567 -32.851 100.815 1.00155.73 N ANISOU 2098 NE2 GLN A1069 23698 20759 14715 3402 -4034 -1170 N ATOM 2099 N ASP A1070 122.231 -26.116 100.403 1.00113.66 N ANISOU 2099 N ASP A1070 16200 17452 9533 833 -2166 -131 N ATOM 2100 CA ASP A1070 121.456 -24.956 99.954 1.00111.03 C ANISOU 2100 CA ASP A1070 15817 17155 9216 391 -2026 9 C ATOM 2101 C ASP A1070 122.332 -23.745 99.646 1.00116.53 C ANISOU 2101 C ASP A1070 16101 18400 9777 229 -1732 152 C ATOM 2102 O ASP A1070 121.994 -22.976 98.746 1.00116.34 O ANISOU 2102 O ASP A1070 16106 18473 9624 40 -1627 220 O ATOM 2103 CB ASP A1070 120.356 -24.596 100.956 1.00109.26 C ANISOU 2103 CB ASP A1070 15668 16595 9250 -39 -2152 168 C ATOM 2104 CG ASP A1070 119.236 -25.611 101.034 1.00120.99 C ANISOU 2104 CG ASP A1070 17534 17611 10825 -83 -2441 118 C ATOM 2105 OD1 ASP A1070 118.911 -26.223 99.990 1.00124.62 O ANISOU 2105 OD1 ASP A1070 18280 17904 11164 90 -2561 -37 O ATOM 2106 OD2 ASP A1070 118.658 -25.767 102.123 1.00126.05 O ANISOU 2106 OD2 ASP A1070 18184 18086 11624 -339 -2560 250 O ATOM 2107 N VAL A1071 123.463 -23.595 100.374 1.00114.60 N ANISOU 2107 N VAL A1071 15486 18516 9542 265 -1641 227 N ATOM 2108 CA VAL A1071 124.459 -22.535 100.173 1.00116.26 C ANISOU 2108 CA VAL A1071 15257 19307 9609 23 -1408 410 C ATOM 2109 C VAL A1071 125.138 -22.749 98.806 1.00125.87 C ANISOU 2109 C VAL A1071 16310 21074 10443 328 -1197 320 C ATOM 2110 O VAL A1071 125.243 -21.798 98.030 1.00126.77 O ANISOU 2110 O VAL A1071 16310 21488 10368 -5 -1031 506 O ATOM 2111 CB VAL A1071 125.473 -22.448 101.353 1.00120.56 C ANISOU 2111 CB VAL A1071 15422 20130 10256 -27 -1421 505 C ATOM 2112 CG1 VAL A1071 126.652 -21.533 101.028 1.00123.74 C ANISOU 2112 CG1 VAL A1071 15307 21250 10457 -285 -1209 704 C ATOM 2113 CG2 VAL A1071 124.783 -21.974 102.620 1.00116.45 C ANISOU 2113 CG2 VAL A1071 15060 19164 10022 -398 -1591 610 C ATOM 2114 N ASP A1072 125.541 -24.007 98.498 1.00126.34 N ANISOU 2114 N ASP A1072 16413 21239 10353 978 -1237 28 N ATOM 2115 CA ASP A1072 126.174 -24.390 97.227 1.00131.52 C ANISOU 2115 CA ASP A1072 16928 22472 10572 1440 -1044 -162 C ATOM 2116 C ASP A1072 125.288 -24.045 96.041 1.00134.40 C ANISOU 2116 C ASP A1072 17639 22673 10755 1283 -1007 -169 C ATOM 2117 O ASP A1072 125.777 -23.481 95.062 1.00137.65 O ANISOU 2117 O ASP A1072 17803 23715 10781 1227 -744 -83 O ATOM 2118 CB ASP A1072 126.517 -25.896 97.207 1.00137.17 C ANISOU 2118 CB ASP A1072 17823 23093 11201 2274 -1225 -564 C ATOM 2119 CG ASP A1072 127.683 -26.328 98.086 1.00150.11 C ANISOU 2119 CG ASP A1072 19031 25126 12878 2633 -1242 -601 C ATOM 2120 OD1 ASP A1072 128.101 -25.533 98.961 1.00148.64 O ANISOU 2120 OD1 ASP A1072 18444 25169 12864 2152 -1162 -302 O ATOM 2121 OD2 ASP A1072 128.163 -27.468 97.912 1.00160.58 O ANISOU 2121 OD2 ASP A1072 20459 26499 14056 3425 -1387 -949 O ATOM 2122 N ALA A1073 123.980 -24.356 96.149 1.00127.01 N ANISOU 2122 N ALA A1073 17238 20951 10067 1168 -1278 -236 N ATOM 2123 CA ALA A1073 122.976 -24.090 95.118 1.00125.92 C ANISOU 2123 CA ALA A1073 17461 20578 9803 1018 -1329 -251 C ATOM 2124 C ALA A1073 122.707 -22.603 94.939 1.00127.51 C ANISOU 2124 C ALA A1073 17539 20893 10017 401 -1201 109 C ATOM 2125 O ALA A1073 122.527 -22.168 93.803 1.00129.19 O ANISOU 2125 O ALA A1073 17857 21298 9932 324 -1119 163 O ATOM 2126 CB ALA A1073 121.685 -24.821 95.437 1.00123.93 C ANISOU 2126 CB ALA A1073 17716 19538 9832 1012 -1688 -386 C ATOM 2127 N THR A1074 122.673 -21.820 96.044 1.00120.79 N ANISOU 2127 N THR A1074 16526 19888 9481 -20 -1231 345 N ATOM 2128 CA THR A1074 122.449 -20.372 95.953 1.00119.66 C ANISOU 2128 CA THR A1074 16365 19734 9365 -574 -1206 665 C ATOM 2129 C THR A1074 123.655 -19.689 95.306 1.00128.52 C ANISOU 2129 C THR A1074 17121 21580 10131 -787 -945 907 C ATOM 2130 O THR A1074 123.463 -18.765 94.515 1.00130.55 O ANISOU 2130 O THR A1074 17499 21902 10200 -1139 -926 1149 O ATOM 2131 CB THR A1074 122.015 -19.739 97.279 1.00121.23 C ANISOU 2131 CB THR A1074 16582 19525 9957 -891 -1367 776 C ATOM 2132 OG1 THR A1074 122.915 -20.135 98.301 1.00125.50 O ANISOU 2132 OG1 THR A1074 16816 20264 10606 -797 -1322 745 O ATOM 2133 CG2 THR A1074 120.583 -20.099 97.664 1.00113.96 C ANISOU 2133 CG2 THR A1074 15994 18015 9289 -826 -1600 633 C ATOM 2134 N VAL A1075 124.880 -20.198 95.565 1.00127.08 N ANISOU 2134 N VAL A1075 16482 21989 9813 -562 -762 855 N ATOM 2135 CA VAL A1075 126.114 -19.694 94.950 1.00132.18 C ANISOU 2135 CA VAL A1075 16629 23536 10057 -756 -478 1090 C ATOM 2136 C VAL A1075 126.068 -19.968 93.421 1.00140.45 C ANISOU 2136 C VAL A1075 17756 25015 10595 -502 -294 1010 C ATOM 2137 O VAL A1075 126.464 -19.098 92.638 1.00144.27 O ANISOU 2137 O VAL A1075 18077 26010 10728 -943 -128 1351 O ATOM 2138 CB VAL A1075 127.392 -20.229 95.665 1.00138.64 C ANISOU 2138 CB VAL A1075 16864 24959 10854 -484 -353 1011 C ATOM 2139 CG1 VAL A1075 128.664 -19.903 94.889 1.00145.43 C ANISOU 2139 CG1 VAL A1075 17089 26967 11203 -577 -16 1206 C ATOM 2140 CG2 VAL A1075 127.496 -19.674 97.083 1.00135.42 C ANISOU 2140 CG2 VAL A1075 16371 24217 10864 -896 -537 1180 C ATOM 2141 N ARG A1076 125.501 -21.134 93.005 1.00136.15 N ANISOU 2141 N ARG A1076 17534 24200 9996 146 -377 584 N ATOM 2142 CA ARG A1076 125.321 -21.517 91.592 1.00139.46 C ANISOU 2142 CA ARG A1076 18141 24924 9924 479 -270 410 C ATOM 2143 C ARG A1076 124.427 -20.516 90.851 1.00140.97 C ANISOU 2143 C ARG A1076 18700 24821 10043 -49 -358 702 C ATOM 2144 O ARG A1076 124.726 -20.161 89.712 1.00145.09 O ANISOU 2144 O ARG A1076 19159 25924 10045 -136 -164 844 O ATOM 2145 CB ARG A1076 124.724 -22.928 91.475 1.00139.97 C ANISOU 2145 CB ARG A1076 18633 24503 10045 1196 -492 -114 C ATOM 2146 CG ARG A1076 125.748 -24.023 91.243 1.00158.95 C ANISOU 2146 CG ARG A1076 20771 27506 12119 1987 -354 -499 C ATOM 2147 CD ARG A1076 125.127 -25.399 91.396 1.00172.46 C ANISOU 2147 CD ARG A1076 23043 28493 13989 2620 -716 -987 C ATOM 2148 NE ARG A1076 125.052 -25.811 92.799 1.00180.37 N ANISOU 2148 NE ARG A1076 24102 28897 15532 2594 -966 -984 N ATOM 2149 CZ ARG A1076 124.500 -26.943 93.225 1.00195.44 C ANISOU 2149 CZ ARG A1076 26527 30053 17678 2950 -1356 -1280 C ATOM 2150 NH1 ARG A1076 123.955 -27.791 92.361 1.00184.60 N ANISOU 2150 NH1 ARG A1076 25693 28365 16084 3366 -1581 -1641 N ATOM 2151 NH2 ARG A1076 124.485 -27.235 94.519 1.00181.32 N ANISOU 2151 NH2 ARG A1076 24758 27811 16324 2848 -1560 -1197 N ATOM 2152 N GLY A1077 123.356 -20.074 91.516 1.00131.35 N ANISOU 2152 N GLY A1077 17839 22761 9307 -363 -656 791 N ATOM 2153 CA GLY A1077 122.406 -19.097 90.995 1.00129.52 C ANISOU 2153 CA GLY A1077 17984 22137 9092 -788 -831 1043 C ATOM 2154 C GLY A1077 123.007 -17.714 90.855 1.00135.07 C ANISOU 2154 C GLY A1077 18523 23144 9652 -1447 -745 1554 C ATOM 2155 O GLY A1077 122.753 -17.027 89.861 1.00137.05 O ANISOU 2155 O GLY A1077 19008 23461 9603 -1729 -781 1812 O ATOM 2156 N ILE A1078 123.819 -17.303 91.856 1.00131.25 N ANISOU 2156 N ILE A1078 17676 22824 9370 -1734 -683 1725 N ATOM 2157 CA ILE A1078 124.519 -16.012 91.889 1.00134.09 C ANISOU 2157 CA ILE A1078 17880 23441 9625 -2461 -669 2236 C ATOM 2158 C ILE A1078 125.525 -15.951 90.725 1.00145.47 C ANISOU 2158 C ILE A1078 18947 25915 10411 -2618 -327 2486 C ATOM 2159 O ILE A1078 125.495 -14.994 89.946 1.00148.94 O ANISOU 2159 O ILE A1078 19568 26460 10561 -3174 -373 2922 O ATOM 2160 CB ILE A1078 125.172 -15.730 93.285 1.00135.33 C ANISOU 2160 CB ILE A1078 17738 23526 10154 -2709 -732 2303 C ATOM 2161 CG1 ILE A1078 124.098 -15.517 94.376 1.00129.48 C ANISOU 2161 CG1 ILE A1078 17412 21819 9967 -2651 -1077 2126 C ATOM 2162 CG2 ILE A1078 126.110 -14.520 93.230 1.00140.91 C ANISOU 2162 CG2 ILE A1078 18227 24631 10681 -3518 -730 2843 C ATOM 2163 CD1 ILE A1078 124.548 -15.814 95.820 1.00131.37 C ANISOU 2163 CD1 ILE A1078 17383 21975 10556 -2580 -1115 1981 C ATOM 2164 N LEU A1079 126.378 -16.995 90.591 1.00144.43 N ANISOU 2164 N LEU A1079 18313 26558 10006 -2090 -6 2204 N ATOM 2165 CA LEU A1079 127.389 -17.100 89.531 1.00151.53 C ANISOU 2165 CA LEU A1079 18725 28646 10205 -2083 385 2351 C ATOM 2166 C LEU A1079 126.789 -17.144 88.122 1.00157.12 C ANISOU 2166 C LEU A1079 19809 29470 10419 -1953 436 2341 C ATOM 2167 O LEU A1079 127.400 -16.610 87.196 1.00163.35 O ANISOU 2167 O LEU A1079 20347 31112 10608 -2335 680 2718 O ATOM 2168 CB LEU A1079 128.335 -18.291 89.769 1.00154.12 C ANISOU 2168 CB LEU A1079 18460 29729 10368 -1343 663 1935 C ATOM 2169 CG LEU A1079 129.292 -18.183 90.965 1.00158.93 C ANISOU 2169 CG LEU A1079 18491 30636 11260 -1525 691 2042 C ATOM 2170 CD1 LEU A1079 129.852 -19.536 91.327 1.00160.16 C ANISOU 2170 CD1 LEU A1079 18297 31157 11398 -580 807 1506 C ATOM 2171 CD2 LEU A1079 130.433 -17.210 90.690 1.00168.48 C ANISOU 2171 CD2 LEU A1079 19058 32889 12066 -2302 926 2621 C ATOM 2172 N ARG A1080 125.593 -17.752 87.966 1.00148.62 N ANISOU 2172 N ARG A1080 19319 27586 9563 -1473 190 1946 N ATOM 2173 CA ARG A1080 124.890 -17.830 86.681 1.00150.35 C ANISOU 2173 CA ARG A1080 19965 27806 9354 -1325 155 1893 C ATOM 2174 C ARG A1080 124.182 -16.521 86.307 1.00153.15 C ANISOU 2174 C ARG A1080 20771 27679 9740 -2045 -107 2408 C ATOM 2175 O ARG A1080 123.915 -16.297 85.124 1.00156.75 O ANISOU 2175 O ARG A1080 21466 28409 9683 -2131 -82 2566 O ATOM 2176 CB ARG A1080 123.931 -19.029 86.628 1.00147.59 C ANISOU 2176 CB ARG A1080 20046 26830 9201 -580 -60 1281 C ATOM 2177 CG ARG A1080 124.626 -20.317 86.207 1.00165.45 C ANISOU 2177 CG ARG A1080 22063 29751 11051 229 183 773 C ATOM 2178 CD ARG A1080 123.648 -21.435 85.899 1.00176.87 C ANISOU 2178 CD ARG A1080 24076 30548 12578 857 -112 220 C ATOM 2179 NE ARG A1080 123.414 -22.300 87.058 1.00183.02 N ANISOU 2179 NE ARG A1080 24939 30653 13948 1195 -343 -117 N ATOM 2180 CZ ARG A1080 124.070 -23.432 87.302 1.00200.00 C ANISOU 2180 CZ ARG A1080 26951 33019 16021 1891 -292 -558 C ATOM 2181 NH1 ARG A1080 125.016 -23.853 86.470 1.00195.62 N ANISOU 2181 NH1 ARG A1080 26110 33405 14813 2416 11 -782 N ATOM 2182 NH2 ARG A1080 123.782 -24.152 88.378 1.00181.01 N ANISOU 2182 NH2 ARG A1080 24701 29918 14157 2096 -562 -777 N ATOM 2183 N ASN A1081 123.894 -15.654 87.304 1.00145.15 N ANISOU 2183 N ASN A1081 19908 25954 9290 -2522 -389 2658 N ATOM 2184 CA ASN A1081 123.263 -14.350 87.080 1.00144.99 C ANISOU 2184 CA ASN A1081 20377 25363 9351 -3143 -729 3124 C ATOM 2185 C ASN A1081 124.333 -13.347 86.638 1.00155.65 C ANISOU 2185 C ASN A1081 21481 27408 10250 -3938 -576 3773 C ATOM 2186 O ASN A1081 125.349 -13.191 87.319 1.00156.98 O ANISOU 2186 O ASN A1081 21142 28029 10474 -4239 -404 3930 O ATOM 2187 CB ASN A1081 122.544 -13.860 88.343 1.00138.70 C ANISOU 2187 CB ASN A1081 19845 23578 9278 -3239 -1107 3061 C ATOM 2188 CG ASN A1081 121.647 -12.658 88.132 1.00154.39 C ANISOU 2188 CG ASN A1081 22455 24805 11402 -3605 -1558 3369 C ATOM 2189 OD1 ASN A1081 122.077 -11.578 87.707 1.00149.25 O ANISOU 2189 OD1 ASN A1081 21976 24212 10520 -4262 -1681 3911 O ATOM 2190 ND2 ASN A1081 120.383 -12.804 88.488 1.00141.53 N ANISOU 2190 ND2 ASN A1081 21176 22442 10156 -3194 -1857 3042 N ATOM 2191 N ALA A1082 124.092 -12.671 85.498 1.00156.48 N ANISOU 2191 N ALA A1082 21945 27621 9889 -4321 -670 4185 N ATOM 2192 CA ALA A1082 124.990 -11.685 84.886 1.00163.90 C ANISOU 2192 CA ALA A1082 22740 29233 10301 -5196 -570 4907 C ATOM 2193 C ALA A1082 125.273 -10.455 85.756 1.00167.98 C ANISOU 2193 C ALA A1082 23425 29193 11208 -6026 -925 5398 C ATOM 2194 O ALA A1082 126.353 -9.874 85.646 1.00174.38 O ANISOU 2194 O ALA A1082 23868 30707 11680 -6793 -783 5943 O ATOM 2195 CB ALA A1082 124.435 -11.247 83.544 1.00168.95 C ANISOU 2195 CB ALA A1082 23879 29920 10394 -5383 -692 5225 C ATOM 2196 N LYS A1083 124.306 -10.057 86.604 1.00157.81 N ANISOU 2196 N LYS A1083 22683 26691 10587 -5880 -1404 5202 N ATOM 2197 CA LYS A1083 124.409 -8.885 87.472 1.00157.99 C ANISOU 2197 CA LYS A1083 23028 25995 11004 -6534 -1846 5553 C ATOM 2198 C LYS A1083 124.997 -9.197 88.854 1.00157.62 C ANISOU 2198 C LYS A1083 22516 25950 11421 -6453 -1757 5276 C ATOM 2199 O LYS A1083 125.745 -8.377 89.388 1.00160.98 O ANISOU 2199 O LYS A1083 22894 26348 11923 -7185 -1935 5672 O ATOM 2200 CB LYS A1083 123.036 -8.212 87.613 1.00157.39 C ANISOU 2200 CB LYS A1083 23815 24665 11321 -6335 -2444 5462 C ATOM 2201 CG LYS A1083 123.102 -6.696 87.791 1.00175.19 C ANISOU 2201 CG LYS A1083 26697 26196 13670 -7139 -3021 6028 C ATOM 2202 CD LYS A1083 121.729 -6.077 88.084 1.00181.36 C ANISOU 2202 CD LYS A1083 28291 25737 14881 -6730 -3638 5808 C ATOM 2203 CE LYS A1083 120.876 -5.858 86.853 1.00192.51 C ANISOU 2203 CE LYS A1083 30233 26949 15964 -6592 -3862 5990 C ATOM 2204 NZ LYS A1083 119.538 -5.312 87.200 1.00197.53 N ANISOU 2204 NZ LYS A1083 31542 26482 17028 -6062 -4456 5707 N ATOM 2205 N LEU A1084 124.651 -10.363 89.434 1.00146.77 N ANISOU 2205 N LEU A1084 20850 24571 10343 -5613 -1537 4624 N ATOM 2206 CA LEU A1084 125.106 -10.771 90.766 1.00142.49 C ANISOU 2206 CA LEU A1084 19908 24001 10231 -5442 -1471 4328 C ATOM 2207 C LEU A1084 126.536 -11.339 90.800 1.00150.68 C ANISOU 2207 C LEU A1084 20092 26204 10957 -5562 -1010 4408 C ATOM 2208 O LEU A1084 127.200 -11.221 91.834 1.00149.62 O ANISOU 2208 O LEU A1084 19632 26128 11088 -5771 -1046 4413 O ATOM 2209 CB LEU A1084 124.114 -11.754 91.429 1.00134.42 C ANISOU 2209 CB LEU A1084 18985 22440 9648 -4570 -1495 3667 C ATOM 2210 CG LEU A1084 122.659 -11.285 91.650 1.00134.65 C ANISOU 2210 CG LEU A1084 19699 21424 10039 -4344 -1939 3501 C ATOM 2211 CD1 LEU A1084 121.803 -12.412 92.197 1.00128.03 C ANISOU 2211 CD1 LEU A1084 18800 20335 9510 -3576 -1878 2917 C ATOM 2212 CD2 LEU A1084 122.580 -10.085 92.585 1.00137.39 C ANISOU 2212 CD2 LEU A1084 20401 21061 10739 -4762 -2372 3670 C ATOM 2213 N LYS A1085 127.005 -11.951 89.687 1.00152.05 N ANISOU 2213 N LYS A1085 19885 27347 10542 -5380 -595 4442 N ATOM 2214 CA LYS A1085 128.349 -12.539 89.578 1.00157.10 C ANISOU 2214 CA LYS A1085 19636 29269 10787 -5352 -125 4473 C ATOM 2215 C LYS A1085 129.500 -11.520 89.820 1.00168.37 C ANISOU 2215 C LYS A1085 20652 31277 12044 -6396 -149 5129 C ATOM 2216 O LYS A1085 130.329 -11.814 90.688 1.00168.65 O ANISOU 2216 O LYS A1085 20076 31774 12230 -6374 -27 5034 O ATOM 2217 CB LYS A1085 128.539 -13.296 88.248 1.00164.04 C ANISOU 2217 CB LYS A1085 20254 31093 10982 -4892 300 4348 C ATOM 2218 CG LYS A1085 129.721 -14.259 88.253 1.00181.58 C ANISOU 2218 CG LYS A1085 21562 34570 12860 -4412 783 4096 C ATOM 2219 CD LYS A1085 130.196 -14.595 86.844 1.00192.93 C ANISOU 2219 CD LYS A1085 23085 36303 13919 -3870 1271 3944 C ATOM 2220 CE LYS A1085 131.401 -15.510 86.844 1.00200.17 C ANISOU 2220 CE LYS A1085 23879 36881 15294 -2892 1787 3343 C ATOM 2221 NZ LYS A1085 132.628 -14.839 87.358 1.00205.24 N ANISOU 2221 NZ LYS A1085 24529 36747 16705 -3071 2013 3457 N ATOM 2222 N PRO A1086 129.585 -10.338 89.130 1.00170.85 N ANISOU 2222 N PRO A1086 21293 31567 12055 -7349 -353 5814 N ATOM 2223 CA PRO A1086 130.699 -9.407 89.413 1.00174.94 C ANISOU 2223 CA PRO A1086 21585 32140 12745 -8010 -321 6246 C ATOM 2224 C PRO A1086 130.704 -8.825 90.828 1.00176.30 C ANISOU 2224 C PRO A1086 21938 31540 13507 -8421 -798 6260 C ATOM 2225 O PRO A1086 131.769 -8.472 91.335 1.00176.80 O ANISOU 2225 O PRO A1086 21654 31560 13961 -8469 -628 6266 O ATOM 2226 CB PRO A1086 130.523 -8.312 88.358 1.00177.75 C ANISOU 2226 CB PRO A1086 22694 31589 13254 -8037 -294 6529 C ATOM 2227 CG PRO A1086 129.083 -8.349 88.010 1.00179.85 C ANISOU 2227 CG PRO A1086 23661 31309 13365 -7983 -721 6493 C ATOM 2228 CD PRO A1086 128.711 -9.797 88.066 1.00173.56 C ANISOU 2228 CD PRO A1086 22386 31399 12161 -7525 -569 6066 C ATOM 2229 N VAL A1087 129.521 -8.735 91.463 1.00168.20 N ANISOU 2229 N VAL A1087 21580 29531 12799 -8318 -1295 6041 N ATOM 2230 CA VAL A1087 129.354 -8.217 92.823 1.00165.05 C ANISOU 2230 CA VAL A1087 21508 28208 12996 -8477 -1753 5906 C ATOM 2231 C VAL A1087 129.905 -9.239 93.830 1.00165.59 C ANISOU 2231 C VAL A1087 20866 28745 13308 -7902 -1471 5430 C ATOM 2232 O VAL A1087 130.681 -8.862 94.710 1.00167.66 O ANISOU 2232 O VAL A1087 20850 29121 13731 -8397 -1637 5582 O ATOM 2233 CB VAL A1087 127.882 -7.809 93.127 1.00163.36 C ANISOU 2233 CB VAL A1087 22279 26566 13225 -8065 -2226 5599 C ATOM 2234 CG1 VAL A1087 127.756 -7.160 94.505 1.00161.39 C ANISOU 2234 CG1 VAL A1087 22399 25431 13492 -8244 -2717 5464 C ATOM 2235 CG2 VAL A1087 127.333 -6.873 92.054 1.00167.62 C ANISOU 2235 CG2 VAL A1087 23529 26665 13494 -8520 -2531 6057 C ATOM 2236 N TYR A1088 129.527 -10.527 93.673 1.00156.98 N ANISOU 2236 N TYR A1088 19521 27909 12217 -6892 -1096 4878 N ATOM 2237 CA TYR A1088 129.948 -11.642 94.529 1.00153.22 C ANISOU 2237 CA TYR A1088 18468 27806 11943 -6214 -859 4402 C ATOM 2238 C TYR A1088 131.477 -11.788 94.590 1.00163.19 C ANISOU 2238 C TYR A1088 18768 30358 12878 -6560 -570 4662 C ATOM 2239 O TYR A1088 132.030 -11.930 95.684 1.00161.72 O ANISOU 2239 O TYR A1088 18229 30254 12962 -6551 -656 4543 O ATOM 2240 CB TYR A1088 129.284 -12.951 94.055 1.00149.96 C ANISOU 2240 CB TYR A1088 18077 27417 11483 -5165 -574 3852 C ATOM 2241 CG TYR A1088 129.516 -14.142 94.961 1.00148.11 C ANISOU 2241 CG TYR A1088 17464 27310 11502 -4405 -445 3345 C ATOM 2242 CD1 TYR A1088 128.710 -14.363 96.076 1.00143.26 C ANISOU 2242 CD1 TYR A1088 17251 25764 11419 -4086 -719 3007 C ATOM 2243 CD2 TYR A1088 130.514 -15.071 94.684 1.00152.87 C ANISOU 2243 CD2 TYR A1088 17325 28988 11769 -3956 -63 3197 C ATOM 2244 CE1 TYR A1088 128.920 -15.458 96.915 1.00140.92 C ANISOU 2244 CE1 TYR A1088 16670 25549 11325 -3446 -645 2607 C ATOM 2245 CE2 TYR A1088 130.737 -16.166 95.519 1.00151.14 C ANISOU 2245 CE2 TYR A1088 16843 28804 11780 -3225 -22 2748 C ATOM 2246 CZ TYR A1088 129.935 -16.358 96.631 1.00150.86 C ANISOU 2246 CZ TYR A1088 17266 27769 12283 -3015 -326 2483 C ATOM 2247 OH TYR A1088 130.150 -17.442 97.448 1.00148.60 O ANISOU 2247 OH TYR A1088 16780 27489 12192 -2352 -326 2104 O ATOM 2248 N ASP A1089 132.148 -11.730 93.421 1.00166.44 N ANISOU 2248 N ASP A1089 18726 31841 12674 -6865 -233 5025 N ATOM 2249 CA ASP A1089 133.602 -11.858 93.290 1.00173.31 C ANISOU 2249 CA ASP A1089 18609 34057 13186 -7118 117 5267 C ATOM 2250 C ASP A1089 134.364 -10.708 93.967 1.00176.36 C ANISOU 2250 C ASP A1089 19242 33475 14293 -7588 -56 5440 C ATOM 2251 O ASP A1089 135.392 -10.954 94.601 1.00176.82 O ANISOU 2251 O ASP A1089 18746 33791 14647 -7367 119 5269 O ATOM 2252 CB ASP A1089 134.005 -11.995 91.807 1.00176.56 C ANISOU 2252 CB ASP A1089 19128 34480 13476 -6542 694 5155 C ATOM 2253 CG ASP A1089 133.443 -13.209 91.071 1.00182.34 C ANISOU 2253 CG ASP A1089 19930 35398 13952 -5472 1000 4611 C ATOM 2254 OD1 ASP A1089 132.458 -13.806 91.564 1.00180.43 O ANISOU 2254 OD1 ASP A1089 19711 35329 13514 -5326 702 4431 O ATOM 2255 OD2 ASP A1089 133.965 -13.538 89.984 1.00187.51 O ANISOU 2255 OD2 ASP A1089 20745 35832 14667 -4776 1521 4331 O ATOM 2256 N SER A1090 133.846 -9.466 93.853 1.00173.75 N ANISOU 2256 N SER A1090 19624 32354 14041 -8427 -498 5878 N ATOM 2257 CA SER A1090 134.450 -8.260 94.436 1.00174.12 C ANISOU 2257 CA SER A1090 19940 31543 14673 -8924 -742 6057 C ATOM 2258 C SER A1090 134.334 -8.190 95.959 1.00174.86 C ANISOU 2258 C SER A1090 20085 31247 15106 -9138 -1236 5902 C ATOM 2259 O SER A1090 135.150 -7.520 96.596 1.00175.45 O ANISOU 2259 O SER A1090 20070 30932 15661 -9334 -1320 5892 O ATOM 2260 CB SER A1090 133.845 -7.005 93.815 1.00177.00 C ANISOU 2260 CB SER A1090 21256 30692 15305 -9151 -960 6275 C ATOM 2261 OG SER A1090 132.470 -6.877 94.138 1.00179.83 O ANISOU 2261 OG SER A1090 22375 30258 15693 -9100 -1446 6167 O ATOM 2262 N LEU A1091 133.314 -8.852 96.537 1.00170.41 N ANISOU 2262 N LEU A1091 19628 30970 14148 -9310 -1620 5874 N ATOM 2263 CA LEU A1091 133.060 -8.854 97.980 1.00165.36 C ANISOU 2263 CA LEU A1091 19261 29524 14046 -9068 -1974 5491 C ATOM 2264 C LEU A1091 133.857 -9.915 98.747 1.00168.10 C ANISOU 2264 C LEU A1091 18735 30684 14451 -8505 -1686 5157 C ATOM 2265 O LEU A1091 134.205 -10.958 98.188 1.00168.32 O ANISOU 2265 O LEU A1091 18124 31619 14210 -7855 -1191 4971 O ATOM 2266 CB LEU A1091 131.553 -9.014 98.280 1.00156.88 C ANISOU 2266 CB LEU A1091 19076 27171 13359 -8308 -2162 4982 C ATOM 2267 CG LEU A1091 130.613 -7.881 97.845 1.00162.21 C ANISOU 2267 CG LEU A1091 20750 26786 14098 -8710 -2606 5198 C ATOM 2268 CD1 LEU A1091 129.172 -8.338 97.875 1.00154.39 C ANISOU 2268 CD1 LEU A1091 20334 24967 13360 -7780 -2606 4672 C ATOM 2269 CD2 LEU A1091 130.790 -6.632 98.700 1.00168.27 C ANISOU 2269 CD2 LEU A1091 22058 26777 15102 -9486 -3257 5412 C ATOM 2270 N ASP A1092 134.121 -9.642 100.039 1.00163.22 N ANISOU 2270 N ASP A1092 18154 29692 14169 -8702 -2045 5054 N ATOM 2271 CA ASP A1092 134.819 -10.540 100.965 1.00161.71 C ANISOU 2271 CA ASP A1092 17260 30094 14088 -8197 -1908 4747 C ATOM 2272 C ASP A1092 133.851 -11.615 101.488 1.00157.28 C ANISOU 2272 C ASP A1092 17038 28889 13831 -7042 -1800 4096 C ATOM 2273 O ASP A1092 132.647 -11.509 101.247 1.00151.95 O ANISOU 2273 O ASP A1092 17125 27297 13314 -6757 -1883 3903 O ATOM 2274 CB ASP A1092 135.433 -9.741 102.134 1.00166.34 C ANISOU 2274 CB ASP A1092 17831 30494 14877 -8952 -2401 4928 C ATOM 2275 CG ASP A1092 134.460 -8.836 102.869 1.00167.61 C ANISOU 2275 CG ASP A1092 19076 29211 15398 -9184 -2964 4796 C ATOM 2276 OD1 ASP A1092 133.634 -9.358 103.645 1.00160.88 O ANISOU 2276 OD1 ASP A1092 18614 27672 14841 -8406 -3010 4276 O ATOM 2277 OD2 ASP A1092 134.549 -7.605 102.694 1.00173.99 O ANISOU 2277 OD2 ASP A1092 20349 29575 16186 -10106 -3372 5197 O ATOM 2278 N ALA A1093 134.371 -12.626 102.216 1.00152.95 N ANISOU 2278 N ALA A1093 15930 28830 13354 -6415 -1658 3790 N ATOM 2279 CA ALA A1093 133.594 -13.733 102.794 1.00145.82 C ANISOU 2279 CA ALA A1093 15296 27403 12705 -5409 -1594 3245 C ATOM 2280 C ALA A1093 132.453 -13.288 103.730 1.00143.81 C ANISOU 2280 C ALA A1093 15897 25913 12830 -5400 -1964 3023 C ATOM 2281 O ALA A1093 131.365 -13.869 103.665 1.00137.92 O ANISOU 2281 O ALA A1093 15600 24582 12221 -4776 -1888 2696 O ATOM 2282 CB ALA A1093 134.517 -14.703 103.517 1.00148.28 C ANISOU 2282 CB ALA A1093 14894 28434 13010 -4911 -1509 3062 C ATOM 2283 N VAL A1094 132.700 -12.259 104.583 1.00142.00 N ANISOU 2283 N VAL A1094 15881 25338 12733 -6090 -2379 3190 N ATOM 2284 CA VAL A1094 131.721 -11.696 105.529 1.00137.51 C ANISOU 2284 CA VAL A1094 16097 23701 12450 -6078 -2759 2953 C ATOM 2285 C VAL A1094 130.593 -10.985 104.761 1.00140.78 C ANISOU 2285 C VAL A1094 17253 23348 12888 -6167 -2852 2979 C ATOM 2286 O VAL A1094 129.418 -11.216 105.056 1.00135.78 O ANISOU 2286 O VAL A1094 17121 22042 12426 -5634 -2887 2636 O ATOM 2287 CB VAL A1094 132.363 -10.770 106.600 1.00144.93 C ANISOU 2287 CB VAL A1094 17098 24496 13472 -6752 -3230 3078 C ATOM 2288 CG1 VAL A1094 131.340 -10.358 107.657 1.00140.63 C ANISOU 2288 CG1 VAL A1094 17319 22958 13157 -6519 -3578 2715 C ATOM 2289 CG2 VAL A1094 133.575 -11.429 107.258 1.00147.54 C ANISOU 2289 CG2 VAL A1094 16605 25713 13742 -6717 -3161 3113 C ATOM 2290 N ARG A1095 130.951 -10.141 103.769 1.00142.18 N ANISOU 2290 N ARG A1095 17467 23690 12866 -6847 -2901 3412 N ATOM 2291 CA ARG A1095 129.983 -9.419 102.935 1.00141.36 C ANISOU 2291 CA ARG A1095 18069 22898 12744 -6964 -3038 3504 C ATOM 2292 C ARG A1095 129.209 -10.333 101.992 1.00141.15 C ANISOU 2292 C ARG A1095 18021 22977 12632 -6256 -2627 3313 C ATOM 2293 O ARG A1095 128.052 -10.035 101.691 1.00138.11 O ANISOU 2293 O ARG A1095 18261 21878 12336 -6026 -2759 3182 O ATOM 2294 CB ARG A1095 130.642 -8.266 102.178 1.00147.84 C ANISOU 2294 CB ARG A1095 18989 23842 13342 -7987 -3273 4095 C ATOM 2295 CG ARG A1095 130.825 -7.037 103.048 1.00156.25 C ANISOU 2295 CG ARG A1095 20582 24221 14563 -8686 -3913 4218 C ATOM 2296 CD ARG A1095 131.658 -5.998 102.345 1.00166.34 C ANISOU 2296 CD ARG A1095 21899 25703 15599 -9843 -4183 4889 C ATOM 2297 NE ARG A1095 131.723 -4.750 103.101 1.00171.28 N ANISOU 2297 NE ARG A1095 23238 25459 16381 -10527 -4918 4991 N ATOM 2298 CZ ARG A1095 132.669 -4.461 103.986 1.00180.08 C ANISOU 2298 CZ ARG A1095 23941 26515 17964 -10284 -4821 4686 C ATOM 2299 NH1 ARG A1095 133.643 -5.329 104.235 1.00172.68 N ANISOU 2299 NH1 ARG A1095 22066 26920 16625 -10837 -4689 5027 N ATOM 2300 NH2 ARG A1095 132.648 -3.304 104.632 1.00175.22 N ANISOU 2300 NH2 ARG A1095 24022 25037 17515 -10773 -5474 4680 N ATOM 2301 N ARG A1096 129.830 -11.454 101.548 1.00137.98 N ANISOU 2301 N ARG A1096 16921 23456 12048 -5866 -2175 3263 N ATOM 2302 CA ARG A1096 129.190 -12.459 100.685 1.00134.47 C ANISOU 2302 CA ARG A1096 16458 23137 11498 -5158 -1820 3029 C ATOM 2303 C ARG A1096 128.040 -13.130 101.437 1.00132.13 C ANISOU 2303 C ARG A1096 16547 22144 11512 -4461 -1888 2557 C ATOM 2304 O ARG A1096 127.010 -13.414 100.829 1.00128.73 O ANISOU 2304 O ARG A1096 16469 21352 11091 -4091 -1827 2398 O ATOM 2305 CB ARG A1096 130.194 -13.524 100.217 1.00136.63 C ANISOU 2305 CB ARG A1096 15935 24483 11495 -4814 -1402 3007 C ATOM 2306 CG ARG A1096 131.000 -13.134 98.989 1.00150.50 C ANISOU 2306 CG ARG A1096 17283 27104 12797 -5295 -1170 3429 C ATOM 2307 CD ARG A1096 132.025 -14.200 98.670 1.00158.90 C ANISOU 2307 CD ARG A1096 17495 29319 13559 -4813 -766 3320 C ATOM 2308 NE ARG A1096 132.916 -13.797 97.584 1.00172.53 N ANISOU 2308 NE ARG A1096 18690 32094 14771 -5314 -504 3749 N ATOM 2309 CZ ARG A1096 133.839 -14.584 97.042 1.00190.22 C ANISOU 2309 CZ ARG A1096 20132 35536 16608 -4901 -104 3685 C ATOM 2310 NH1 ARG A1096 133.999 -15.829 97.475 1.00176.01 N ANISOU 2310 NH1 ARG A1096 18057 33922 14896 -3940 22 3193 N ATOM 2311 NH2 ARG A1096 134.608 -14.134 96.059 1.00182.42 N ANISOU 2311 NH2 ARG A1096 18628 35595 15089 -5426 153 4116 N ATOM 2312 N ALA A1097 128.208 -13.352 102.765 1.00127.21 N ANISOU 2312 N ALA A1097 15841 21382 11110 -4338 -2032 2366 N ATOM 2313 CA ALA A1097 127.187 -13.940 103.634 1.00121.63 C ANISOU 2313 CA ALA A1097 15440 20126 10649 -3792 -2104 1983 C ATOM 2314 C ALA A1097 125.941 -13.049 103.683 1.00124.10 C ANISOU 2314 C ALA A1097 16423 19636 11093 -3853 -2367 1898 C ATOM 2315 O ALA A1097 124.825 -13.571 103.681 1.00119.90 O ANISOU 2315 O ALA A1097 16123 18777 10655 -3381 -2320 1643 O ATOM 2316 CB ALA A1097 127.741 -14.148 105.029 1.00122.19 C ANISOU 2316 CB ALA A1097 15296 20285 10846 -3785 -2241 1881 C ATOM 2317 N ALA A1098 126.135 -11.706 103.677 1.00124.20 N ANISOU 2317 N ALA A1098 16749 19347 11096 -4435 -2681 2120 N ATOM 2318 CA ALA A1098 125.053 -10.717 103.667 1.00123.65 C ANISOU 2318 CA ALA A1098 17364 18496 11121 -4452 -3013 2035 C ATOM 2319 C ALA A1098 124.277 -10.769 102.340 1.00126.64 C ANISOU 2319 C ALA A1098 17958 18762 11398 -4278 -2897 2105 C ATOM 2320 O ALA A1098 123.065 -10.547 102.339 1.00124.61 O ANISOU 2320 O ALA A1098 18121 17985 11241 -3925 -3046 1886 O ATOM 2321 CB ALA A1098 125.608 -9.324 103.906 1.00129.69 C ANISOU 2321 CB ALA A1098 18471 18932 11873 -5150 -3451 2289 C ATOM 2322 N LEU A1099 124.969 -11.092 101.220 1.00124.67 N ANISOU 2322 N LEU A1099 17379 19080 10911 -4486 -2629 2391 N ATOM 2323 CA LEU A1099 124.354 -11.244 99.896 1.00123.83 C ANISOU 2323 CA LEU A1099 17434 18984 10633 -4331 -2495 2469 C ATOM 2324 C LEU A1099 123.541 -12.544 99.865 1.00123.03 C ANISOU 2324 C LEU A1099 17202 18941 10603 -3607 -2244 2094 C ATOM 2325 O LEU A1099 122.374 -12.505 99.486 1.00121.03 O ANISOU 2325 O LEU A1099 17299 18290 10396 -3323 -2336 1956 O ATOM 2326 CB LEU A1099 125.415 -11.220 98.778 1.00128.47 C ANISOU 2326 CB LEU A1099 17664 20291 10859 -4775 -2263 2879 C ATOM 2327 CG LEU A1099 124.908 -11.124 97.332 1.00134.21 C ANISOU 2327 CG LEU A1099 18622 21058 11312 -4763 -2179 3047 C ATOM 2328 CD1 LEU A1099 124.546 -9.693 96.962 1.00137.98 C ANISOU 2328 CD1 LEU A1099 19733 20933 11759 -5314 -2609 3391 C ATOM 2329 CD2 LEU A1099 125.953 -11.635 96.364 1.00140.40 C ANISOU 2329 CD2 LEU A1099 18839 22831 11677 -4904 -1774 3280 C ATOM 2330 N ILE A1100 124.140 -13.679 100.316 1.00118.19 N ANISOU 2330 N ILE A1100 16114 18791 10002 -3324 -1989 1937 N ATOM 2331 CA ILE A1100 123.498 -15.005 100.409 1.00114.08 C ANISOU 2331 CA ILE A1100 15518 18273 9554 -2713 -1827 1612 C ATOM 2332 C ILE A1100 122.230 -14.912 101.287 1.00114.69 C ANISOU 2332 C ILE A1100 15926 17762 9890 -2488 -2036 1367 C ATOM 2333 O ILE A1100 121.212 -15.521 100.957 1.00111.16 O ANISOU 2333 O ILE A1100 15618 17144 9475 -2154 -2014 1195 O ATOM 2334 CB ILE A1100 124.509 -16.092 100.906 1.00117.32 C ANISOU 2334 CB ILE A1100 15435 19207 9934 -2477 -1626 1522 C ATOM 2335 CG1 ILE A1100 125.653 -16.294 99.889 1.00122.26 C ANISOU 2335 CG1 ILE A1100 15650 20577 10226 -2545 -1369 1702 C ATOM 2336 CG2 ILE A1100 123.821 -17.437 101.201 1.00113.94 C ANISOU 2336 CG2 ILE A1100 15065 18609 9620 -1914 -1585 1213 C ATOM 2337 CD1 ILE A1100 126.986 -16.779 100.488 1.00130.45 C ANISOU 2337 CD1 ILE A1100 16104 22256 11204 -2488 -1250 1720 C ATOM 2338 N ASN A1101 122.290 -14.110 102.375 1.00112.74 N ANISOU 2338 N ASN A1101 15792 17259 9785 -2686 -2253 1351 N ATOM 2339 CA ASN A1101 121.161 -13.877 103.277 1.00110.80 C ANISOU 2339 CA ASN A1101 15804 16590 9704 -2452 -2436 1102 C ATOM 2340 C ASN A1101 119.999 -13.258 102.504 1.00116.36 C ANISOU 2340 C ASN A1101 16888 16922 10402 -2332 -2592 1065 C ATOM 2341 O ASN A1101 118.873 -13.736 102.641 1.00114.72 O ANISOU 2341 O ASN A1101 16712 16618 10259 -1978 -2587 854 O ATOM 2342 CB ASN A1101 121.563 -12.993 104.460 1.00112.01 C ANISOU 2342 CB ASN A1101 16063 16565 9930 -2677 -2674 1071 C ATOM 2343 CG ASN A1101 120.583 -13.047 105.606 1.00129.06 C ANISOU 2343 CG ASN A1101 18338 18520 12180 -2344 -2774 764 C ATOM 2344 OD1 ASN A1101 119.455 -12.546 105.526 1.00125.00 O ANISOU 2344 OD1 ASN A1101 18109 17702 11685 -2113 -2922 601 O ATOM 2345 ND2 ASN A1101 120.996 -13.661 106.702 1.00116.69 N ANISOU 2345 ND2 ASN A1101 16524 17183 10630 -2289 -2699 683 N ATOM 2346 N MET A1102 120.282 -12.238 101.659 1.00116.24 N ANISOU 2346 N MET A1102 17138 16741 10286 -2654 -2747 1306 N ATOM 2347 CA MET A1102 119.284 -11.564 100.823 1.00117.53 C ANISOU 2347 CA MET A1102 17711 16530 10417 -2547 -2958 1321 C ATOM 2348 C MET A1102 118.658 -12.533 99.810 1.00120.74 C ANISOU 2348 C MET A1102 17993 17151 10731 -2268 -2747 1279 C ATOM 2349 O MET A1102 117.433 -12.562 99.688 1.00120.17 O ANISOU 2349 O MET A1102 18077 16866 10714 -1943 -2872 1107 O ATOM 2350 CB MET A1102 119.894 -10.347 100.109 1.00124.62 C ANISOU 2350 CB MET A1102 18957 17208 11185 -3055 -3201 1678 C ATOM 2351 CG MET A1102 119.609 -9.035 100.801 1.00131.13 C ANISOU 2351 CG MET A1102 20294 17408 12121 -3138 -3673 1618 C ATOM 2352 SD MET A1102 120.472 -7.634 100.049 1.00141.94 S ANISOU 2352 SD MET A1102 22156 18441 13336 -3911 -4055 2132 S ATOM 2353 CE MET A1102 119.374 -7.244 98.722 1.00140.12 C ANISOU 2353 CE MET A1102 22387 17861 12993 -3670 -4249 2227 C ATOM 2354 N VAL A1103 119.500 -13.340 99.113 1.00117.23 N ANISOU 2354 N VAL A1103 17253 17166 10125 -2362 -2453 1407 N ATOM 2355 CA VAL A1103 119.095 -14.349 98.118 1.00115.92 C ANISOU 2355 CA VAL A1103 17008 17214 9821 -2098 -2276 1335 C ATOM 2356 C VAL A1103 118.142 -15.382 98.757 1.00116.70 C ANISOU 2356 C VAL A1103 17009 17233 10098 -1711 -2261 1028 C ATOM 2357 O VAL A1103 117.164 -15.782 98.129 1.00115.79 O ANISOU 2357 O VAL A1103 17006 17034 9956 -1507 -2319 928 O ATOM 2358 CB VAL A1103 120.324 -14.999 97.416 1.00121.45 C ANISOU 2358 CB VAL A1103 17405 18479 10263 -2192 -1978 1470 C ATOM 2359 CG1 VAL A1103 119.905 -16.100 96.444 1.00120.77 C ANISOU 2359 CG1 VAL A1103 17315 18563 10008 -1838 -1845 1308 C ATOM 2360 CG2 VAL A1103 121.166 -13.951 96.692 1.00125.63 C ANISOU 2360 CG2 VAL A1103 17989 19198 10547 -2682 -1989 1852 C ATOM 2361 N PHE A1104 118.409 -15.767 100.017 1.00111.95 N ANISOU 2361 N PHE A1104 16209 16672 9657 -1670 -2218 915 N ATOM 2362 CA PHE A1104 117.578 -16.694 100.786 1.00109.39 C ANISOU 2362 CA PHE A1104 15784 16312 9468 -1427 -2220 708 C ATOM 2363 C PHE A1104 116.183 -16.081 101.052 1.00112.51 C ANISOU 2363 C PHE A1104 16320 16480 9951 -1297 -2418 587 C ATOM 2364 O PHE A1104 115.183 -16.799 101.014 1.00111.29 O ANISOU 2364 O PHE A1104 16097 16363 9825 -1145 -2441 478 O ATOM 2365 CB PHE A1104 118.273 -17.038 102.117 1.00110.52 C ANISOU 2365 CB PHE A1104 15716 16572 9705 -1466 -2158 675 C ATOM 2366 CG PHE A1104 119.038 -18.344 102.162 1.00112.04 C ANISOU 2366 CG PHE A1104 15717 16991 9862 -1356 -2012 666 C ATOM 2367 CD1 PHE A1104 120.285 -18.462 101.557 1.00116.77 C ANISOU 2367 CD1 PHE A1104 16164 17877 10324 -1388 -1874 766 C ATOM 2368 CD2 PHE A1104 118.545 -19.434 102.871 1.00112.87 C ANISOU 2368 CD2 PHE A1104 15790 17051 10046 -1216 -2043 570 C ATOM 2369 CE1 PHE A1104 121.000 -19.661 101.617 1.00118.16 C ANISOU 2369 CE1 PHE A1104 16176 18268 10452 -1150 -1782 699 C ATOM 2370 CE2 PHE A1104 119.267 -20.630 102.939 1.00116.15 C ANISOU 2370 CE2 PHE A1104 16132 17567 10432 -1058 -1999 551 C ATOM 2371 CZ PHE A1104 120.486 -20.736 102.306 1.00116.05 C ANISOU 2371 CZ PHE A1104 15984 17816 10293 -962 -1876 582 C ATOM 2372 N GLN A1105 116.124 -14.750 101.287 1.00109.47 N ANISOU 2372 N GLN A1105 16136 15873 9587 -1352 -2598 604 N ATOM 2373 CA GLN A1105 114.893 -14.015 101.590 1.00109.24 C ANISOU 2373 CA GLN A1105 16242 15657 9609 -1105 -2822 435 C ATOM 2374 C GLN A1105 114.038 -13.642 100.362 1.00114.92 C ANISOU 2374 C GLN A1105 17172 16231 10263 -968 -2992 466 C ATOM 2375 O GLN A1105 112.816 -13.798 100.420 1.00114.97 O ANISOU 2375 O GLN A1105 17077 16313 10295 -688 -3083 303 O ATOM 2376 CB GLN A1105 115.214 -12.759 102.423 1.00111.75 C ANISOU 2376 CB GLN A1105 16785 15713 9961 -1136 -3029 379 C ATOM 2377 CG GLN A1105 114.019 -12.200 103.197 1.00114.85 C ANISOU 2377 CG GLN A1105 17213 16048 10376 -728 -3213 81 C ATOM 2378 CD GLN A1105 114.323 -10.960 104.014 1.00134.14 C ANISOU 2378 CD GLN A1105 19999 18147 12821 -679 -3496 -47 C ATOM 2379 OE1 GLN A1105 115.480 -10.590 104.270 1.00128.94 O ANISOU 2379 OE1 GLN A1105 19495 17322 12173 -1043 -3546 99 O ATOM 2380 NE2 GLN A1105 113.274 -10.296 104.470 1.00129.13 N ANISOU 2380 NE2 GLN A1105 19479 17429 12155 -203 -3716 -349 N ATOM 2381 N MET A1106 114.663 -13.113 99.284 1.00112.78 N ANISOU 2381 N MET A1106 17165 15810 9875 -1182 -3050 697 N ATOM 2382 CA MET A1106 113.962 -12.613 98.092 1.00114.55 C ANISOU 2382 CA MET A1106 17668 15860 9995 -1083 -3262 777 C ATOM 2383 C MET A1106 114.096 -13.477 96.848 1.00118.14 C ANISOU 2383 C MET A1106 18067 16545 10274 -1162 -3102 892 C ATOM 2384 O MET A1106 113.197 -13.472 96.001 1.00119.03 O ANISOU 2384 O MET A1106 18288 16621 10317 -987 -3256 862 O ATOM 2385 CB MET A1106 114.464 -11.210 97.721 1.00120.52 C ANISOU 2385 CB MET A1106 18883 16228 10680 -1303 -3535 1003 C ATOM 2386 CG MET A1106 114.481 -10.231 98.848 1.00125.65 C ANISOU 2386 CG MET A1106 19737 16540 11466 -1233 -3785 872 C ATOM 2387 SD MET A1106 115.494 -8.830 98.360 1.00134.94 S ANISOU 2387 SD MET A1106 21488 17245 12540 -1749 -4111 1253 S ATOM 2388 CE MET A1106 115.955 -8.239 99.927 1.00132.42 C ANISOU 2388 CE MET A1106 21220 16720 12375 -1803 -4242 1062 C ATOM 2389 N GLY A1107 115.243 -14.131 96.707 1.00113.63 N ANISOU 2389 N GLY A1107 17347 16230 9599 -1390 -2828 1009 N ATOM 2390 CA GLY A1107 115.572 -14.932 95.538 1.00113.73 C ANISOU 2390 CA GLY A1107 17333 16509 9372 -1408 -2661 1073 C ATOM 2391 C GLY A1107 116.531 -14.177 94.646 1.00120.80 C ANISOU 2391 C GLY A1107 18386 17519 9992 -1726 -2615 1393 C ATOM 2392 O GLY A1107 116.711 -12.965 94.813 1.00122.28 O ANISOU 2392 O GLY A1107 18805 17452 10204 -1970 -2809 1596 O ATOM 2393 N GLU A1108 117.149 -14.892 93.688 1.00118.55 N ANISOU 2393 N GLU A1108 18001 17636 9408 -1733 -2382 1441 N ATOM 2394 CA GLU A1108 118.111 -14.349 92.729 1.00122.26 C ANISOU 2394 CA GLU A1108 18516 18433 9504 -2060 -2260 1773 C ATOM 2395 C GLU A1108 117.595 -13.098 92.003 1.00129.16 C ANISOU 2395 C GLU A1108 19837 18984 10252 -2292 -2571 2066 C ATOM 2396 O GLU A1108 118.335 -12.118 91.904 1.00132.28 O ANISOU 2396 O GLU A1108 20350 19392 10519 -2752 -2626 2432 O ATOM 2397 CB GLU A1108 118.541 -15.428 91.719 1.00125.06 C ANISOU 2397 CB GLU A1108 18715 19313 9490 -1853 -1984 1670 C ATOM 2398 CG GLU A1108 119.611 -16.382 92.230 1.00134.31 C ANISOU 2398 CG GLU A1108 19460 20927 10644 -1706 -1672 1516 C ATOM 2399 CD GLU A1108 119.177 -17.501 93.161 1.00151.56 C ANISOU 2399 CD GLU A1108 21549 22883 13156 -1332 -1704 1147 C ATOM 2400 OE1 GLU A1108 117.954 -17.703 93.343 1.00144.30 O ANISOU 2400 OE1 GLU A1108 20841 21539 12447 -1191 -1934 986 O ATOM 2401 OE2 GLU A1108 120.071 -18.188 93.705 1.00145.58 O ANISOU 2401 OE2 GLU A1108 20487 22408 12418 -1197 -1519 1044 O ATOM 2402 N THR A1109 116.324 -13.116 91.541 1.00124.99 N ANISOU 2402 N THR A1109 19570 18153 9767 -2003 -2825 1926 N ATOM 2403 CA THR A1109 115.713 -11.992 90.817 1.00128.22 C ANISOU 2403 CA THR A1109 20452 18207 10060 -2110 -3196 2174 C ATOM 2404 C THR A1109 115.425 -10.797 91.749 1.00132.31 C ANISOU 2404 C THR A1109 21234 18153 10885 -2177 -3550 2228 C ATOM 2405 O THR A1109 115.661 -9.654 91.355 1.00136.16 O ANISOU 2405 O THR A1109 22146 18344 11243 -2499 -3831 2579 O ATOM 2406 CB THR A1109 114.483 -12.443 90.001 1.00135.98 C ANISOU 2406 CB THR A1109 21573 19125 10967 -1739 -3379 1988 C ATOM 2407 OG1 THR A1109 114.777 -13.673 89.333 1.00133.92 O ANISOU 2407 OG1 THR A1109 21102 19334 10449 -1627 -3082 1839 O ATOM 2408 CG2 THR A1109 114.058 -11.407 88.960 1.00139.88 C ANISOU 2408 CG2 THR A1109 22565 19366 11215 -1847 -3742 2300 C ATOM 2409 N GLY A1110 114.946 -11.076 92.962 1.00125.12 N ANISOU 2409 N GLY A1110 20110 17094 10335 -1880 -3559 1888 N ATOM 2410 CA GLY A1110 114.642 -10.061 93.969 1.00125.60 C ANISOU 2410 CA GLY A1110 20396 16666 10659 -1808 -3879 1815 C ATOM 2411 C GLY A1110 115.822 -9.176 94.332 1.00131.54 C ANISOU 2411 C GLY A1110 21336 17257 11387 -2325 -3944 2110 C ATOM 2412 O GLY A1110 115.670 -7.956 94.427 1.00135.53 O ANISOU 2412 O GLY A1110 22346 17207 11942 -2415 -4383 2232 O ATOM 2413 N VAL A1111 117.013 -9.788 94.504 1.00125.32 N ANISOU 2413 N VAL A1111 20158 16950 10507 -2665 -3555 2227 N ATOM 2414 CA VAL A1111 118.279 -9.116 94.839 1.00127.08 C ANISOU 2414 CA VAL A1111 20409 17198 10676 -3257 -3571 2544 C ATOM 2415 C VAL A1111 118.795 -8.313 93.633 1.00135.46 C ANISOU 2415 C VAL A1111 21813 18273 11385 -3810 -3713 3075 C ATOM 2416 O VAL A1111 119.265 -7.189 93.809 1.00138.97 O ANISOU 2416 O VAL A1111 22636 18345 11821 -4317 -4050 3395 O ATOM 2417 CB VAL A1111 119.335 -10.126 95.366 1.00127.94 C ANISOU 2417 CB VAL A1111 19892 17939 10782 -3357 -3111 2474 C ATOM 2418 CG1 VAL A1111 120.634 -9.431 95.754 1.00131.29 C ANISOU 2418 CG1 VAL A1111 20259 18471 11154 -4001 -3156 2806 C ATOM 2419 CG2 VAL A1111 118.789 -10.925 96.543 1.00122.60 C ANISOU 2419 CG2 VAL A1111 18946 17222 10413 -2862 -3010 2015 C ATOM 2420 N ALA A1112 118.685 -8.886 92.415 1.00132.60 N ANISOU 2420 N ALA A1112 21360 18321 10701 -3738 -3497 3178 N ATOM 2421 CA ALA A1112 119.108 -8.267 91.148 1.00138.22 C ANISOU 2421 CA ALA A1112 22355 19189 10974 -4240 -3574 3701 C ATOM 2422 C ALA A1112 118.425 -6.917 90.849 1.00146.41 C ANISOU 2422 C ALA A1112 24183 19407 12038 -4391 -4207 3961 C ATOM 2423 O ALA A1112 119.021 -6.073 90.178 1.00152.56 O ANISOU 2423 O ALA A1112 25301 20152 12514 -5048 -4396 4518 O ATOM 2424 CB ALA A1112 118.895 -9.233 89.991 1.00138.23 C ANISOU 2424 CB ALA A1112 22147 19750 10625 -3955 -3253 3624 C ATOM 2425 N GLY A1113 117.208 -6.726 91.370 1.00139.85 N ANISOU 2425 N GLY A1113 23629 17963 11545 -3785 -4548 3571 N ATOM 2426 CA GLY A1113 116.424 -5.502 91.214 1.00143.55 C ANISOU 2426 CA GLY A1113 24862 17594 12085 -3696 -5214 3686 C ATOM 2427 C GLY A1113 116.998 -4.286 91.923 1.00150.70 C ANISOU 2427 C GLY A1113 26261 17876 13123 -4167 -5656 3917 C ATOM 2428 O GLY A1113 116.579 -3.158 91.649 1.00155.53 O ANISOU 2428 O GLY A1113 27645 17729 13722 -4221 -6286 4121 O ATOM 2429 N PHE A1114 117.968 -4.510 92.834 1.00144.99 N ANISOU 2429 N PHE A1114 25139 17432 12519 -4507 -5388 3882 N ATOM 2430 CA PHE A1114 118.662 -3.478 93.616 1.00148.83 C ANISOU 2430 CA PHE A1114 26019 17404 13127 -5045 -5788 4078 C ATOM 2431 C PHE A1114 119.934 -3.015 92.868 1.00158.42 C ANISOU 2431 C PHE A1114 27269 18953 13971 -6115 -5753 4815 C ATOM 2432 O PHE A1114 121.012 -2.917 93.463 1.00159.01 O ANISOU 2432 O PHE A1114 27035 19329 14052 -6701 -5622 4989 O ATOM 2433 CB PHE A1114 119.007 -4.021 95.022 1.00145.60 C ANISOU 2433 CB PHE A1114 25104 17203 13016 -4837 -5525 3640 C ATOM 2434 CG PHE A1114 117.844 -4.220 95.966 1.00142.89 C ANISOU 2434 CG PHE A1114 24782 16517 12993 -3928 -5639 2983 C ATOM 2435 CD1 PHE A1114 117.037 -5.349 95.875 1.00140.13 C ANISOU 2435 CD1 PHE A1114 23915 16630 12696 -3278 -5233 2609 C ATOM 2436 CD2 PHE A1114 117.603 -3.321 96.997 1.00147.85 C ANISOU 2436 CD2 PHE A1114 25914 16428 13833 -3748 -6150 2731 C ATOM 2437 CE1 PHE A1114 115.974 -5.543 96.763 1.00138.29 C ANISOU 2437 CE1 PHE A1114 23608 16231 12703 -2522 -5310 2059 C ATOM 2438 CE2 PHE A1114 116.545 -3.520 97.891 1.00147.77 C ANISOU 2438 CE2 PHE A1114 25835 16273 14039 -2878 -6203 2113 C ATOM 2439 CZ PHE A1114 115.737 -4.629 97.767 1.00140.27 C ANISOU 2439 CZ PHE A1114 24295 15883 13121 -2304 -5762 1811 C ATOM 2440 N THR A1115 119.786 -2.728 91.554 1.00159.35 N ANISOU 2440 N THR A1115 27732 19084 13729 -6382 -5880 5268 N ATOM 2441 CA THR A1115 120.841 -2.305 90.623 1.00166.01 C ANISOU 2441 CA THR A1115 28607 20367 14100 -7406 -5831 6041 C ATOM 2442 C THR A1115 121.766 -1.229 91.219 1.00174.51 C ANISOU 2442 C THR A1115 29859 21057 15391 -8027 -6075 6345 C ATOM 2443 O THR A1115 122.986 -1.404 91.194 1.00175.05 O ANISOU 2443 O THR A1115 29211 21896 15405 -8447 -5525 6584 O ATOM 2444 CB THR A1115 120.227 -1.877 89.272 1.00176.65 C ANISOU 2444 CB THR A1115 30487 21533 15100 -7412 -6069 6405 C ATOM 2445 OG1 THR A1115 119.201 -2.799 88.894 1.00170.43 O ANISOU 2445 OG1 THR A1115 29439 20982 14335 -6505 -5794 5908 O ATOM 2446 CG2 THR A1115 121.262 -1.784 88.156 1.00177.62 C ANISOU 2446 CG2 THR A1115 29989 22532 14967 -7675 -5362 6857 C ATOM 2447 N ASN A1116 121.179 -0.151 91.785 1.00172.63 N ANISOU 2447 N ASN A1116 30291 19719 15582 -7659 -6643 6121 N ATOM 2448 CA ASN A1116 121.903 0.974 92.389 1.00173.41 C ANISOU 2448 CA ASN A1116 30261 19431 16196 -7663 -6561 6089 C ATOM 2449 C ASN A1116 122.750 0.561 93.587 1.00175.03 C ANISOU 2449 C ASN A1116 29994 19956 16554 -7969 -6407 5884 C ATOM 2450 O ASN A1116 123.868 1.057 93.730 1.00175.96 O ANISOU 2450 O ASN A1116 29634 20310 16914 -8251 -6039 6028 O ATOM 2451 CB ASN A1116 120.950 2.110 92.758 1.00174.08 C ANISOU 2451 CB ASN A1116 30931 18453 16758 -6896 -7001 5711 C ATOM 2452 CG ASN A1116 120.172 2.639 91.580 1.00191.05 C ANISOU 2452 CG ASN A1116 32349 20864 19375 -5529 -6113 5453 C ATOM 2453 OD1 ASN A1116 120.640 3.503 90.829 1.00189.46 O ANISOU 2453 OD1 ASN A1116 32165 20588 19234 -5718 -5931 5853 O ATOM 2454 ND2 ASN A1116 118.978 2.103 91.373 1.00185.37 N ANISOU 2454 ND2 ASN A1116 32311 19821 18300 -5369 -6761 5378 N ATOM 2455 N SER A1117 122.231 -0.355 94.429 1.00170.73 N ANISOU 2455 N SER A1117 29836 19326 15709 -8193 -6922 5686 N ATOM 2456 CA SER A1117 122.930 -0.864 95.615 1.00167.92 C ANISOU 2456 CA SER A1117 28931 19357 15513 -8317 -6703 5421 C ATOM 2457 C SER A1117 124.121 -1.758 95.246 1.00170.89 C ANISOU 2457 C SER A1117 28272 21045 15615 -8841 -5975 5738 C ATOM 2458 O SER A1117 125.187 -1.621 95.850 1.00171.72 O ANISOU 2458 O SER A1117 28014 21480 15751 -9441 -5935 5905 O ATOM 2459 CB SER A1117 121.969 -1.620 96.528 1.00163.37 C ANISOU 2459 CB SER A1117 28108 18687 15278 -7153 -6487 4588 C ATOM 2460 OG SER A1117 120.969 -0.768 97.064 1.00176.23 O ANISOU 2460 OG SER A1117 30593 19232 17135 -6608 -7152 4226 O ATOM 2461 N LEU A1118 123.934 -2.663 94.255 1.00164.93 N ANISOU 2461 N LEU A1118 27017 21054 14596 -8519 -5402 5765 N ATOM 2462 CA LEU A1118 124.948 -3.608 93.764 1.00164.48 C ANISOU 2462 CA LEU A1118 25978 22307 14209 -8789 -4686 5972 C ATOM 2463 C LEU A1118 126.161 -2.897 93.158 1.00174.24 C ANISOU 2463 C LEU A1118 26962 23984 15257 -9584 -4534 6587 C ATOM 2464 O LEU A1118 127.295 -3.323 93.396 1.00174.03 O ANISOU 2464 O LEU A1118 26101 24853 15170 -9809 -4061 6656 O ATOM 2465 CB LEU A1118 124.340 -4.593 92.745 1.00160.72 C ANISOU 2465 CB LEU A1118 25199 22365 13501 -8111 -4189 5775 C ATOM 2466 CG LEU A1118 123.318 -5.606 93.275 1.00157.02 C ANISOU 2466 CG LEU A1118 24554 21734 13374 -6986 -3964 5011 C ATOM 2467 CD1 LEU A1118 122.450 -6.139 92.152 1.00155.58 C ANISOU 2467 CD1 LEU A1118 24476 21656 12983 -6461 -3801 4905 C ATOM 2468 CD2 LEU A1118 123.995 -6.761 94.000 1.00155.19 C ANISOU 2468 CD2 LEU A1118 23455 22278 13231 -6699 -3424 4678 C ATOM 2469 N ARG A1119 125.917 -1.809 92.391 1.00173.71 N ANISOU 2469 N ARG A1119 27410 23225 15367 -9450 -4661 6782 N ATOM 2470 CA ARG A1119 126.950 -0.985 91.754 1.00175.80 C ANISOU 2470 CA ARG A1119 27291 23616 15891 -9394 -4127 7008 C ATOM 2471 C ARG A1119 127.859 -0.344 92.816 1.00179.64 C ANISOU 2471 C ARG A1119 27454 23791 17009 -9330 -4007 6756 C ATOM 2472 O ARG A1119 129.074 -0.286 92.621 1.00180.84 O ANISOU 2472 O ARG A1119 26962 24473 17275 -9433 -3452 6870 O ATOM 2473 CB ARG A1119 126.309 0.092 90.858 1.00176.87 C ANISOU 2473 CB ARG A1119 28038 22967 16198 -9023 -4246 7145 C ATOM 2474 CG ARG A1119 127.307 0.827 89.962 1.00186.23 C ANISOU 2474 CG ARG A1119 28666 24287 17807 -8412 -3312 7171 C ATOM 2475 CD ARG A1119 126.649 1.804 89.000 1.00194.16 C ANISOU 2475 CD ARG A1119 29975 24645 19150 -7538 -3077 7110 C ATOM 2476 NE ARG A1119 126.126 2.993 89.677 1.00198.47 N ANISOU 2476 NE ARG A1119 30797 24212 20401 -7005 -3287 6758 N ATOM 2477 CZ ARG A1119 124.833 3.274 89.813 1.00206.39 C ANISOU 2477 CZ ARG A1119 31990 24701 21728 -6104 -3423 6311 C ATOM 2478 NH1 ARG A1119 124.451 4.376 90.445 1.00198.07 N ANISOU 2478 NH1 ARG A1119 31615 22772 20870 -6475 -4134 6387 N ATOM 2479 NH2 ARG A1119 123.911 2.461 89.310 1.00196.15 N ANISOU 2479 NH2 ARG A1119 31305 23538 19685 -6592 -4087 6621 N ATOM 2480 N MET A1120 127.269 0.107 93.942 1.00176.46 N ANISOU 2480 N MET A1120 27663 22554 16830 -9467 -4731 6538 N ATOM 2481 CA MET A1120 127.993 0.730 95.052 1.00176.75 C ANISOU 2481 CA MET A1120 27565 22254 17338 -9600 -4834 6329 C ATOM 2482 C MET A1120 128.826 -0.275 95.857 1.00178.03 C ANISOU 2482 C MET A1120 26961 23265 17416 -9801 -4573 6192 C ATOM 2483 O MET A1120 129.835 0.116 96.449 1.00178.59 O ANISOU 2483 O MET A1120 26631 23403 17824 -9961 -4420 6119 O ATOM 2484 CB MET A1120 127.037 1.522 95.957 1.00178.09 C ANISOU 2484 CB MET A1120 28492 21273 17901 -9168 -5447 5882 C ATOM 2485 CG MET A1120 126.608 2.845 95.354 1.00182.24 C ANISOU 2485 CG MET A1120 29353 21021 18869 -8565 -5352 5793 C ATOM 2486 SD MET A1120 125.299 3.664 96.291 1.00184.86 S ANISOU 2486 SD MET A1120 30389 20237 19611 -7790 -5917 5155 S ATOM 2487 CE MET A1120 125.134 5.160 95.352 1.00184.82 C ANISOU 2487 CE MET A1120 30660 19621 19942 -7530 -5795 5349 C ATOM 2488 N LEU A1121 128.417 -1.565 95.860 1.00173.51 N ANISOU 2488 N LEU A1121 26280 23418 16226 -10132 -4700 6320 N ATOM 2489 CA LEU A1121 129.113 -2.650 96.566 1.00172.12 C ANISOU 2489 CA LEU A1121 25335 24238 15823 -10414 -4491 6278 C ATOM 2490 C LEU A1121 130.446 -3.011 95.903 1.00175.81 C ANISOU 2490 C LEU A1121 24754 25718 16326 -10224 -3619 6367 C ATOM 2491 O LEU A1121 131.425 -3.271 96.606 1.00175.63 O ANISOU 2491 O LEU A1121 24099 26188 16445 -10353 -3442 6284 O ATOM 2492 CB LEU A1121 128.216 -3.893 96.707 1.00167.68 C ANISOU 2492 CB LEU A1121 24733 24044 14934 -10088 -4473 6035 C ATOM 2493 CG LEU A1121 127.023 -3.767 97.660 1.00166.69 C ANISOU 2493 CG LEU A1121 25263 22808 15266 -9260 -4827 5384 C ATOM 2494 CD1 LEU A1121 126.021 -4.878 97.426 1.00158.47 C ANISOU 2494 CD1 LEU A1121 24009 21900 14303 -8155 -4373 4854 C ATOM 2495 CD2 LEU A1121 127.467 -3.732 99.119 1.00167.99 C ANISOU 2495 CD2 LEU A1121 25271 22839 15720 -9270 -5002 5080 C ATOM 2496 N GLN A1122 130.480 -3.019 94.551 1.00174.24 N ANISOU 2496 N GLN A1122 24487 25898 15817 -10212 -3256 6677 N ATOM 2497 CA GLN A1122 131.688 -3.295 93.767 1.00175.36 C ANISOU 2497 CA GLN A1122 23822 26907 15900 -10058 -2486 6793 C ATOM 2498 C GLN A1122 132.617 -2.072 93.821 1.00179.28 C ANISOU 2498 C GLN A1122 24318 26699 17102 -9897 -2252 6729 C ATOM 2499 O GLN A1122 133.839 -2.227 93.821 1.00180.06 O ANISOU 2499 O GLN A1122 23738 27315 17360 -9862 -1764 6699 O ATOM 2500 CB GLN A1122 131.323 -3.665 92.317 1.00176.90 C ANISOU 2500 CB GLN A1122 24048 27482 15682 -9709 -2072 6931 C ATOM 2501 CG GLN A1122 132.475 -4.295 91.527 1.00187.71 C ANISOU 2501 CG GLN A1122 24658 29389 17273 -8722 -1012 6584 C ATOM 2502 CD GLN A1122 132.034 -5.077 90.312 1.00199.48 C ANISOU 2502 CD GLN A1122 26237 30847 18709 -7522 -388 6187 C ATOM 2503 OE1 GLN A1122 131.105 -4.700 89.585 1.00197.36 O ANISOU 2503 OE1 GLN A1122 26521 30312 18153 -7641 -633 6432 O ATOM 2504 NE2 GLN A1122 132.731 -6.168 90.035 1.00193.99 N ANISOU 2504 NE2 GLN A1122 24839 31388 17481 -7619 -19 6219 N ATOM 2505 N GLN A1123 132.024 -0.863 93.904 1.00177.10 N ANISOU 2505 N GLN A1123 24829 25378 17083 -10104 -2754 6838 N ATOM 2506 CA GLN A1123 132.730 0.418 94.006 1.00178.92 C ANISOU 2506 CA GLN A1123 25141 24926 17915 -10110 -2653 6822 C ATOM 2507 C GLN A1123 133.202 0.683 95.449 1.00181.04 C ANISOU 2507 C GLN A1123 25240 24856 18689 -10125 -2889 6425 C ATOM 2508 O GLN A1123 133.907 1.663 95.700 1.00182.25 O ANISOU 2508 O GLN A1123 25346 24546 19353 -10180 -2798 6348 O ATOM 2509 CB GLN A1123 131.847 1.563 93.480 1.00180.71 C ANISOU 2509 CB GLN A1123 26166 24123 18372 -9844 -2889 6867 C ATOM 2510 CG GLN A1123 131.790 1.635 91.950 1.00192.78 C ANISOU 2510 CG GLN A1123 27554 25655 20037 -8831 -2016 6791 C ATOM 2511 CD GLN A1123 130.705 2.539 91.403 1.00206.97 C ANISOU 2511 CD GLN A1123 29776 26469 22393 -7557 -1771 6372 C ATOM 2512 OE1 GLN A1123 130.093 3.347 92.114 1.00203.84 O ANISOU 2512 OE1 GLN A1123 29858 25377 22214 -7736 -2358 6299 O ATOM 2513 NE2 GLN A1123 130.453 2.429 90.107 1.00202.83 N ANISOU 2513 NE2 GLN A1123 29477 26236 21354 -7714 -1667 6840 N ATOM 2514 N LYS A1124 132.814 -0.216 96.384 1.00176.98 N ANISOU 2514 N LYS A1124 24692 24721 17832 -10434 -3346 6353 N ATOM 2515 CA LYS A1124 133.147 -0.244 97.815 1.00176.49 C ANISOU 2515 CA LYS A1124 24504 24541 18012 -10609 -3700 6063 C ATOM 2516 C LYS A1124 132.642 0.996 98.597 1.00180.09 C ANISOU 2516 C LYS A1124 25663 23733 19029 -10343 -4149 5680 C ATOM 2517 O LYS A1124 133.200 1.336 99.645 1.00180.39 O ANISOU 2517 O LYS A1124 25565 23573 19401 -10452 -4324 5418 O ATOM 2518 CB LYS A1124 134.655 -0.500 98.044 1.00179.35 C ANISOU 2518 CB LYS A1124 23922 25556 18666 -10543 -3144 5949 C ATOM 2519 CG LYS A1124 135.126 -1.864 97.539 1.00186.76 C ANISOU 2519 CG LYS A1124 24044 27407 19510 -9776 -2353 5721 C ATOM 2520 CD LYS A1124 136.428 -2.306 98.198 1.00193.06 C ANISOU 2520 CD LYS A1124 24038 28533 20783 -9326 -1912 5308 C ATOM 2521 CE LYS A1124 136.861 -3.690 97.766 1.00197.92 C ANISOU 2521 CE LYS A1124 24000 29996 21203 -8727 -1336 5143 C ATOM 2522 NZ LYS A1124 136.040 -4.761 98.395 1.00199.34 N ANISOU 2522 NZ LYS A1124 24183 30495 21060 -8491 -1576 4959 N ATOM 2523 N ARG A1125 131.544 1.620 98.118 1.00177.79 N ANISOU 2523 N ARG A1125 26210 22702 18641 -10291 -4540 5785 N ATOM 2524 CA ARG A1125 130.898 2.776 98.754 1.00178.15 C ANISOU 2524 CA ARG A1125 26990 21616 19081 -10060 -5038 5459 C ATOM 2525 C ARG A1125 129.876 2.240 99.780 1.00178.50 C ANISOU 2525 C ARG A1125 27495 21349 18980 -9786 -5574 5066 C ATOM 2526 O ARG A1125 128.663 2.336 99.568 1.00177.30 O ANISOU 2526 O ARG A1125 28040 20649 18675 -9492 -5943 4998 O ATOM 2527 CB ARG A1125 130.227 3.677 97.690 1.00179.68 C ANISOU 2527 CB ARG A1125 27667 21201 19402 -9715 -4954 5593 C ATOM 2528 CG ARG A1125 131.207 4.414 96.776 1.00189.80 C ANISOU 2528 CG ARG A1125 28263 22600 21250 -9176 -3953 5546 C ATOM 2529 CD ARG A1125 130.616 4.709 95.405 1.00198.69 C ANISOU 2529 CD ARG A1125 29410 23600 22481 -8364 -3371 5584 C ATOM 2530 NE ARG A1125 129.718 5.868 95.411 1.00205.71 N ANISOU 2530 NE ARG A1125 30625 23661 23873 -7556 -3325 5200 N ATOM 2531 CZ ARG A1125 129.156 6.393 94.324 1.00215.89 C ANISOU 2531 CZ ARG A1125 31818 24793 25416 -6645 -2722 5126 C ATOM 2532 NH1 ARG A1125 128.357 7.447 94.427 1.00208.25 N ANISOU 2532 NH1 ARG A1125 31614 23049 24464 -6894 -3361 5261 N ATOM 2533 NH2 ARG A1125 129.391 5.871 93.126 1.00206.65 N ANISOU 2533 NH2 ARG A1125 30859 24052 23608 -7314 -2794 5851 N ATOM 2534 N TRP A1126 130.390 1.647 100.881 1.00175.43 N ANISOU 2534 N TRP A1126 26867 21318 18472 -10183 -5820 4970 N ATOM 2535 CA TRP A1126 129.622 0.996 101.954 1.00173.78 C ANISOU 2535 CA TRP A1126 27087 20926 18014 -10122 -6365 4686 C ATOM 2536 C TRP A1126 128.553 1.872 102.612 1.00176.92 C ANISOU 2536 C TRP A1126 28307 20191 18723 -9426 -6805 4112 C ATOM 2537 O TRP A1126 127.437 1.392 102.829 1.00175.16 O ANISOU 2537 O TRP A1126 28698 19638 18215 -9168 -7221 3954 O ATOM 2538 CB TRP A1126 130.548 0.398 103.035 1.00172.63 C ANISOU 2538 CB TRP A1126 26360 21402 17829 -10476 -6369 4607 C ATOM 2539 CG TRP A1126 131.751 -0.344 102.518 1.00173.51 C ANISOU 2539 CG TRP A1126 25383 22701 17840 -10767 -5718 4939 C ATOM 2540 CD1 TRP A1126 133.055 -0.094 102.825 1.00176.81 C ANISOU 2540 CD1 TRP A1126 25052 23466 18662 -10739 -5325 4812 C ATOM 2541 CD2 TRP A1126 131.758 -1.455 101.607 1.00172.25 C ANISOU 2541 CD2 TRP A1126 24708 23532 17209 -10890 -5297 5308 C ATOM 2542 NE1 TRP A1126 133.876 -0.979 102.166 1.00176.46 N ANISOU 2542 NE1 TRP A1126 24126 24526 18393 -10878 -4762 5118 N ATOM 2543 CE2 TRP A1126 133.108 -1.823 101.408 1.00175.95 C ANISOU 2543 CE2 TRP A1126 24115 24881 17859 -10784 -4621 5328 C ATOM 2544 CE3 TRP A1126 130.755 -2.173 100.932 1.00171.59 C ANISOU 2544 CE3 TRP A1126 24892 23625 16679 -10801 -5301 5458 C ATOM 2545 CZ2 TRP A1126 133.479 -2.885 100.577 1.00175.01 C ANISOU 2545 CZ2 TRP A1126 23260 25901 17337 -10785 -4078 5597 C ATOM 2546 CZ3 TRP A1126 131.127 -3.205 100.085 1.00172.10 C ANISOU 2546 CZ3 TRP A1126 24165 24848 16376 -10795 -4699 5703 C ATOM 2547 CH2 TRP A1126 132.475 -3.545 99.905 1.00173.62 C ANISOU 2547 CH2 TRP A1126 23340 25958 16671 -10748 -4090 5758 C ATOM 2548 N ASP A1127 128.893 3.132 102.944 1.00176.46 N ANISOU 2548 N ASP A1127 28432 19525 19091 -9394 -6920 3917 N ATOM 2549 CA ASP A1127 127.975 4.077 103.583 1.00177.04 C ANISOU 2549 CA ASP A1127 29233 18622 19411 -8806 -7342 3381 C ATOM 2550 C ASP A1127 126.798 4.458 102.679 1.00179.23 C ANISOU 2550 C ASP A1127 29960 18428 19713 -8198 -7319 3356 C ATOM 2551 O ASP A1127 125.659 4.475 103.150 1.00178.53 O ANISOU 2551 O ASP A1127 30493 17793 19548 -7630 -7738 2951 O ATOM 2552 CB ASP A1127 128.729 5.325 104.077 1.00180.66 C ANISOU 2552 CB ASP A1127 29397 18795 20451 -8699 -7106 3049 C ATOM 2553 CG ASP A1127 129.541 5.104 105.343 1.00189.33 C ANISOU 2553 CG ASP A1127 29736 20347 21853 -8419 -6757 2496 C ATOM 2554 OD1 ASP A1127 130.374 4.170 105.361 1.00189.24 O ANISOU 2554 OD1 ASP A1127 29141 21081 21681 -8817 -6557 2760 O ATOM 2555 OD2 ASP A1127 129.367 5.885 106.303 1.00194.74 O ANISOU 2555 OD2 ASP A1127 30414 20681 22899 -7861 -6706 1827 O ATOM 2556 N GLU A1128 127.070 4.729 101.382 1.00176.94 N ANISOU 2556 N GLU A1128 29590 18268 19372 -8542 -7082 3912 N ATOM 2557 CA GLU A1128 126.054 5.101 100.392 1.00176.69 C ANISOU 2557 CA GLU A1128 30032 17813 19290 -8134 -7148 4030 C ATOM 2558 C GLU A1128 125.134 3.935 100.009 1.00176.59 C ANISOU 2558 C GLU A1128 30214 18058 18825 -7921 -7277 4095 C ATOM 2559 O GLU A1128 123.934 4.153 99.823 1.00175.89 O ANISOU 2559 O GLU A1128 30716 17414 18699 -7344 -7598 3890 O ATOM 2560 CB GLU A1128 126.691 5.743 99.149 1.00179.26 C ANISOU 2560 CB GLU A1128 29935 18352 19822 -8272 -6551 4461 C ATOM 2561 CG GLU A1128 127.135 7.181 99.369 1.00189.12 C ANISOU 2561 CG GLU A1128 30683 19304 21870 -7673 -5909 4026 C ATOM 2562 CD GLU A1128 127.543 7.943 98.121 1.00205.65 C ANISOU 2562 CD GLU A1128 31785 21756 24596 -6792 -4559 3968 C ATOM 2563 OE1 GLU A1128 128.482 7.494 97.426 1.00204.14 O ANISOU 2563 OE1 GLU A1128 31293 22045 24227 -7286 -4290 4426 O ATOM 2564 OE2 GLU A1128 126.951 9.016 97.864 1.00201.79 O ANISOU 2564 OE2 GLU A1128 31791 20617 24265 -6667 -4769 4005 O ATOM 2565 N ALA A1129 125.690 2.704 99.906 1.00172.58 N ANISOU 2565 N ALA A1129 29420 18311 17840 -8639 -7260 4491 N ATOM 2566 CA ALA A1129 124.951 1.476 99.575 1.00170.40 C ANISOU 2566 CA ALA A1129 29347 18354 17042 -8686 -7420 4625 C ATOM 2567 C ALA A1129 123.906 1.146 100.644 1.00171.32 C ANISOU 2567 C ALA A1129 30018 17931 17146 -8054 -7890 4024 C ATOM 2568 O ALA A1129 122.826 0.658 100.311 1.00169.08 O ANISOU 2568 O ALA A1129 30147 17458 16639 -7627 -8080 3904 O ATOM 2569 CB ALA A1129 125.912 0.308 99.409 1.00170.07 C ANISOU 2569 CB ALA A1129 28466 19502 16649 -9360 -6959 5012 C ATOM 2570 N ALA A1130 124.233 1.439 101.922 1.00169.68 N ANISOU 2570 N ALA A1130 29959 17414 17098 -8075 -8198 3679 N ATOM 2571 CA ALA A1130 123.380 1.241 103.098 1.00169.03 C ANISOU 2571 CA ALA A1130 30475 16788 16961 -7472 -8700 3074 C ATOM 2572 C ALA A1130 122.089 2.068 102.997 1.00172.22 C ANISOU 2572 C ALA A1130 31349 16446 17640 -6328 -8837 2524 C ATOM 2573 O ALA A1130 121.011 1.553 103.307 1.00170.65 O ANISOU 2573 O ALA A1130 31530 16021 17289 -5592 -9075 2096 O ATOM 2574 CB ALA A1130 124.146 1.620 104.358 1.00170.27 C ANISOU 2574 CB ALA A1130 30374 16969 17350 -7562 -8714 2753 C ATOM 2575 N VAL A1131 122.205 3.335 102.530 1.00171.76 N ANISOU 2575 N VAL A1131 31342 16001 17916 -6269 -8774 2595 N ATOM 2576 CA VAL A1131 121.098 4.282 102.347 1.00172.67 C ANISOU 2576 CA VAL A1131 31849 15484 18275 -5364 -8908 2198 C ATOM 2577 C VAL A1131 120.111 3.769 101.294 1.00174.67 C ANISOU 2577 C VAL A1131 32183 15838 18347 -4925 -8836 2332 C ATOM 2578 O VAL A1131 118.904 3.794 101.539 1.00174.35 O ANISOU 2578 O VAL A1131 32517 15444 18284 -4029 -9108 1852 O ATOM 2579 CB VAL A1131 121.600 5.717 102.018 1.00177.49 C ANISOU 2579 CB VAL A1131 32006 15997 19436 -5335 -8410 2226 C ATOM 2580 CG1 VAL A1131 120.438 6.704 101.908 1.00178.44 C ANISOU 2580 CG1 VAL A1131 32416 15575 19808 -4448 -8474 1828 C ATOM 2581 CG2 VAL A1131 122.613 6.200 103.053 1.00178.35 C ANISOU 2581 CG2 VAL A1131 31819 16152 19795 -5690 -8310 2017 C ATOM 2582 N ASN A1132 120.627 3.299 100.136 1.00171.87 N ANISOU 2582 N ASN A1132 31751 15834 17717 -5698 -8731 3039 N ATOM 2583 CA ASN A1132 119.821 2.781 99.024 1.00170.91 C ANISOU 2583 CA ASN A1132 31850 15776 17311 -5508 -8790 3275 C ATOM 2584 C ASN A1132 119.068 1.498 99.376 1.00171.79 C ANISOU 2584 C ASN A1132 32028 16115 17128 -5104 -8885 2963 C ATOM 2585 O ASN A1132 117.939 1.316 98.912 1.00170.05 O ANISOU 2585 O ASN A1132 31839 15857 16915 -4293 -8843 2706 O ATOM 2586 CB ASN A1132 120.659 2.616 97.757 1.00170.99 C ANISOU 2586 CB ASN A1132 31406 16406 17159 -6300 -8332 4009 C ATOM 2587 CG ASN A1132 121.077 3.934 97.151 1.00184.96 C ANISOU 2587 CG ASN A1132 32123 18481 19671 -5678 -7259 3924 C ATOM 2588 OD1 ASN A1132 120.287 4.627 96.500 1.00181.64 O ANISOU 2588 OD1 ASN A1132 32185 17555 19274 -5350 -7528 4001 O ATOM 2589 ND2 ASN A1132 122.326 4.319 97.365 1.00180.44 N ANISOU 2589 ND2 ASN A1132 31457 17961 19140 -6488 -7246 4244 N ATOM 2590 N LEU A1133 119.675 0.626 100.205 1.00162.55 N ANISOU 2590 N LEU A1133 30034 15700 16028 -5193 -8317 2769 N ATOM 2591 CA LEU A1133 119.042 -0.613 100.670 1.00153.72 C ANISOU 2591 CA LEU A1133 28057 15350 15000 -4369 -7625 2251 C ATOM 2592 C LEU A1133 117.934 -0.284 101.670 1.00157.71 C ANISOU 2592 C LEU A1133 28884 15398 15642 -3343 -7929 1517 C ATOM 2593 O LEU A1133 116.907 -0.960 101.674 1.00152.42 O ANISOU 2593 O LEU A1133 27780 15129 15004 -2531 -7578 1135 O ATOM 2594 CB LEU A1133 120.062 -1.573 101.311 1.00149.13 C ANISOU 2594 CB LEU A1133 26604 15625 14432 -4778 -7031 2294 C ATOM 2595 CG LEU A1133 121.045 -2.274 100.373 1.00152.41 C ANISOU 2595 CG LEU A1133 26371 16867 14671 -5484 -6498 2860 C ATOM 2596 CD1 LEU A1133 122.183 -2.891 101.156 1.00150.76 C ANISOU 2596 CD1 LEU A1133 25493 17313 14475 -5941 -6155 2920 C ATOM 2597 CD2 LEU A1133 120.353 -3.337 99.519 1.00149.56 C ANISOU 2597 CD2 LEU A1133 25477 17101 14247 -4926 -5928 2757 C ATOM 2598 N ALA A1134 118.141 0.765 102.506 1.00160.51 N ANISOU 2598 N ALA A1134 30000 14946 16042 -3389 -8607 1320 N ATOM 2599 CA ALA A1134 117.170 1.248 103.494 1.00162.17 C ANISOU 2599 CA ALA A1134 30617 14694 16304 -2378 -8983 582 C ATOM 2600 C ALA A1134 115.930 1.827 102.796 1.00169.36 C ANISOU 2600 C ALA A1134 32090 15064 17196 -1586 -9407 402 C ATOM 2601 O ALA A1134 114.822 1.709 103.324 1.00168.37 O ANISOU 2601 O ALA A1134 31837 15063 17072 -515 -9381 -225 O ATOM 2602 CB ALA A1134 117.806 2.299 104.385 1.00169.78 C ANISOU 2602 CB ALA A1134 32376 14854 17278 -2706 -9689 455 C ATOM 2603 N LYS A1135 116.120 2.426 101.599 1.00169.37 N ANISOU 2603 N LYS A1135 32666 14544 17142 -2117 -9792 975 N ATOM 2604 CA LYS A1135 115.044 2.990 100.782 1.00170.28 C ANISOU 2604 CA LYS A1135 32916 14426 17356 -1402 -9885 890 C ATOM 2605 C LYS A1135 114.437 1.855 99.941 1.00169.82 C ANISOU 2605 C LYS A1135 32419 14984 17123 -1182 -9537 1012 C ATOM 2606 O LYS A1135 114.633 1.796 98.724 1.00169.53 O ANISOU 2606 O LYS A1135 32463 14976 16977 -1675 -9511 1572 O ATOM 2607 CB LYS A1135 115.565 4.151 99.906 1.00173.21 C ANISOU 2607 CB LYS A1135 32952 14775 18084 -1895 -9480 1383 C ATOM 2608 CG LYS A1135 115.947 5.406 100.690 1.00183.65 C ANISOU 2608 CG LYS A1135 33382 16357 20040 -1710 -8687 1062 C ATOM 2609 CD LYS A1135 116.586 6.467 99.794 1.00191.06 C ANISOU 2609 CD LYS A1135 33635 17531 21428 -2077 -7939 1511 C ATOM 2610 CE LYS A1135 116.980 7.706 100.564 1.00198.96 C ANISOU 2610 CE LYS A1135 33969 18625 23002 -1951 -7284 1192 C ATOM 2611 NZ LYS A1135 117.668 8.700 99.699 1.00205.57 N ANISOU 2611 NZ LYS A1135 34212 19631 24266 -2224 -6575 1592 N ATOM 2612 N SER A1136 113.744 0.917 100.624 1.00160.83 N ANISOU 2612 N SER A1136 30434 14635 16041 -453 -8961 479 N ATOM 2613 CA SER A1136 113.103 -0.260 100.025 1.00154.24 C ANISOU 2613 CA SER A1136 28735 14687 15182 -172 -8307 484 C ATOM 2614 C SER A1136 111.892 -0.758 100.830 1.00155.83 C ANISOU 2614 C SER A1136 28391 15396 15422 892 -8081 -201 C ATOM 2615 O SER A1136 111.802 -0.529 102.040 1.00156.90 O ANISOU 2615 O SER A1136 28561 15479 15574 1309 -8179 -678 O ATOM 2616 CB SER A1136 114.112 -1.392 99.832 1.00151.32 C ANISOU 2616 CB SER A1136 27593 15109 14793 -976 -7568 864 C ATOM 2617 OG SER A1136 114.489 -1.992 101.061 1.00156.22 O ANISOU 2617 OG SER A1136 27698 16167 15491 -952 -7198 553 O ATOM 2618 N ARG A1137 110.985 -1.475 100.142 1.00149.28 N ANISOU 2618 N ARG A1137 27022 15134 14565 1275 -7769 -225 N ATOM 2619 CA ARG A1137 109.756 -2.067 100.682 1.00147.31 C ANISOU 2619 CA ARG A1137 26111 15549 14310 2161 -7511 -758 C ATOM 2620 C ARG A1137 110.107 -3.215 101.642 1.00146.50 C ANISOU 2620 C ARG A1137 25179 16251 14235 1942 -6824 -892 C ATOM 2621 O ARG A1137 109.389 -3.450 102.617 1.00146.08 O ANISOU 2621 O ARG A1137 24703 16662 14139 2565 -6677 -1370 O ATOM 2622 CB ARG A1137 108.841 -2.539 99.532 1.00145.14 C ANISOU 2622 CB ARG A1137 25517 15635 13994 2415 -7424 -630 C ATOM 2623 CG ARG A1137 108.850 -1.604 98.305 1.00153.48 C ANISOU 2623 CG ARG A1137 27396 15925 14993 2325 -8028 -272 C ATOM 2624 CD ARG A1137 107.884 -2.025 97.220 1.00155.43 C ANISOU 2624 CD ARG A1137 27332 16554 15172 2637 -7990 -189 C ATOM 2625 NE ARG A1137 106.517 -1.579 97.500 1.00160.93 N ANISOU 2625 NE ARG A1137 27994 17294 15859 3737 -8375 -696 N ATOM 2626 CZ ARG A1137 105.956 -0.488 96.985 1.00173.71 C ANISOU 2626 CZ ARG A1137 30363 18208 17431 4277 -9117 -731 C ATOM 2627 NH1 ARG A1137 106.636 0.284 96.147 1.00162.00 N ANISOU 2627 NH1 ARG A1137 29784 15867 15900 3722 -9573 -230 N ATOM 2628 NH2 ARG A1137 104.710 -0.163 97.302 1.00160.18 N ANISOU 2628 NH2 ARG A1137 28492 16679 15689 5379 -9428 -1249 N ATOM 2629 N TRP A1138 111.251 -3.883 101.375 1.00139.73 N ANISOU 2629 N TRP A1138 24105 15574 13410 1068 -6432 -458 N ATOM 2630 CA TRP A1138 111.855 -4.969 102.154 1.00134.27 C ANISOU 2630 CA TRP A1138 22745 15523 12748 736 -5846 -473 C ATOM 2631 C TRP A1138 112.232 -4.499 103.563 1.00140.63 C ANISOU 2631 C TRP A1138 23714 16169 13552 849 -5980 -798 C ATOM 2632 O TRP A1138 111.998 -5.226 104.531 1.00137.63 O ANISOU 2632 O TRP A1138 22779 16374 13141 1052 -5612 -1062 O ATOM 2633 CB TRP A1138 113.089 -5.509 101.396 1.00129.94 C ANISOU 2633 CB TRP A1138 22075 15093 12202 -139 -5541 66 C ATOM 2634 CG TRP A1138 114.131 -6.191 102.232 1.00127.60 C ANISOU 2634 CG TRP A1138 21386 15156 11939 -587 -5161 121 C ATOM 2635 CD1 TRP A1138 114.003 -7.374 102.898 1.00125.90 C ANISOU 2635 CD1 TRP A1138 20507 15584 11746 -480 -4684 -37 C ATOM 2636 CD2 TRP A1138 115.494 -5.777 102.408 1.00129.10 C ANISOU 2636 CD2 TRP A1138 21811 15110 12130 -1266 -5256 409 C ATOM 2637 NE1 TRP A1138 115.187 -7.698 103.522 1.00124.02 N ANISOU 2637 NE1 TRP A1138 20103 15491 11526 -956 -4494 96 N ATOM 2638 CE2 TRP A1138 116.122 -6.739 103.232 1.00129.23 C ANISOU 2638 CE2 TRP A1138 21257 15668 12175 -1446 -4823 362 C ATOM 2639 CE3 TRP A1138 116.248 -4.681 101.954 1.00135.53 C ANISOU 2639 CE3 TRP A1138 23267 15320 12910 -1789 -5705 737 C ATOM 2640 CZ2 TRP A1138 117.468 -6.638 103.612 1.00129.35 C ANISOU 2640 CZ2 TRP A1138 21255 15702 12190 -2067 -4810 595 C ATOM 2641 CZ3 TRP A1138 117.577 -4.575 102.342 1.00138.06 C ANISOU 2641 CZ3 TRP A1138 23558 15675 13224 -2494 -5685 996 C ATOM 2642 CH2 TRP A1138 118.171 -5.539 103.170 1.00134.48 C ANISOU 2642 CH2 TRP A1138 22465 15827 12806 -2596 -5236 904 C ATOM 2643 N TYR A1139 112.822 -3.289 103.668 1.00142.80 N ANISOU 2643 N TYR A1139 24790 15635 13831 677 -6546 -759 N ATOM 2644 CA TYR A1139 113.247 -2.668 104.929 1.00145.62 C ANISOU 2644 CA TYR A1139 25481 15687 14162 754 -6816 -1080 C ATOM 2645 C TYR A1139 112.047 -2.426 105.838 1.00151.54 C ANISOU 2645 C TYR A1139 26175 16606 14798 1803 -6941 -1756 C ATOM 2646 O TYR A1139 112.129 -2.704 107.027 1.00150.41 O ANISOU 2646 O TYR A1139 25781 16803 14563 1978 -6769 -2087 O ATOM 2647 CB TYR A1139 113.997 -1.350 104.646 1.00153.47 C ANISOU 2647 CB TYR A1139 27467 15665 15180 295 -7521 -848 C ATOM 2648 CG TYR A1139 114.636 -0.701 105.856 1.00159.30 C ANISOU 2648 CG TYR A1139 28634 16002 15890 195 -7872 -1118 C ATOM 2649 CD1 TYR A1139 115.906 -1.079 106.285 1.00159.00 C ANISOU 2649 CD1 TYR A1139 28340 16190 15882 -639 -7641 -831 C ATOM 2650 CD2 TYR A1139 114.007 0.344 106.526 1.00166.95 C ANISOU 2650 CD2 TYR A1139 30311 16342 16779 953 -8499 -1672 C ATOM 2651 CE1 TYR A1139 116.510 -0.469 107.385 1.00163.32 C ANISOU 2651 CE1 TYR A1139 29298 16366 16388 -776 -8015 -1074 C ATOM 2652 CE2 TYR A1139 114.600 0.960 107.628 1.00171.93 C ANISOU 2652 CE2 TYR A1139 31416 16560 17351 868 -8881 -1960 C ATOM 2653 CZ TYR A1139 115.854 0.552 108.051 1.00176.70 C ANISOU 2653 CZ TYR A1139 31744 17400 17994 -40 -8643 -1642 C ATOM 2654 OH TYR A1139 116.447 1.166 109.128 1.00183.06 O ANISOU 2654 OH TYR A1139 33026 17800 18727 -164 -9066 -1921 O ATOM 2655 N ASN A1140 110.931 -1.939 105.272 1.00151.59 N ANISOU 2655 N ASN A1140 26368 16461 14768 2522 -7232 -1960 N ATOM 2656 CA ASN A1140 109.702 -1.653 106.010 1.00155.51 C ANISOU 2656 CA ASN A1140 26736 17244 15106 3627 -7360 -2620 C ATOM 2657 C ASN A1140 108.958 -2.908 106.470 1.00155.26 C ANISOU 2657 C ASN A1140 25608 18406 14978 3883 -6660 -2773 C ATOM 2658 O ASN A1140 108.350 -2.890 107.542 1.00157.72 O ANISOU 2658 O ASN A1140 25629 19209 15087 4543 -6576 -3284 O ATOM 2659 CB ASN A1140 108.793 -0.734 105.198 1.00161.74 C ANISOU 2659 CB ASN A1140 28075 17496 15885 4334 -7956 -2767 C ATOM 2660 CG ASN A1140 109.363 0.652 104.990 1.00185.69 C ANISOU 2660 CG ASN A1140 32233 19323 18999 4172 -8703 -2684 C ATOM 2661 OD1 ASN A1140 110.553 0.836 104.693 1.00181.63 O ANISOU 2661 OD1 ASN A1140 32249 18209 18556 3240 -8910 -2201 O ATOM 2662 ND2 ASN A1140 108.518 1.664 105.126 1.00182.48 N ANISOU 2662 ND2 ASN A1140 31798 18815 18721 4793 -8757 -2994 N ATOM 2663 N GLN A1141 109.012 -3.992 105.673 1.00145.96 N ANISOU 2663 N GLN A1141 23852 17698 13906 3347 -6188 -2329 N ATOM 2664 CA GLN A1141 108.348 -5.262 105.979 1.00141.70 C ANISOU 2664 CA GLN A1141 22344 18201 13296 3411 -5588 -2364 C ATOM 2665 C GLN A1141 109.066 -6.017 107.109 1.00142.53 C ANISOU 2665 C GLN A1141 22075 18735 13346 2996 -5162 -2353 C ATOM 2666 O GLN A1141 108.413 -6.457 108.061 1.00143.21 O ANISOU 2666 O GLN A1141 21626 19548 13238 3375 -4900 -2654 O ATOM 2667 CB GLN A1141 108.207 -6.119 104.703 1.00138.62 C ANISOU 2667 CB GLN A1141 21624 18015 13030 2973 -5345 -1917 C ATOM 2668 CG GLN A1141 107.355 -7.389 104.854 1.00147.36 C ANISOU 2668 CG GLN A1141 21820 20100 14072 3013 -4859 -1924 C ATOM 2669 CD GLN A1141 105.872 -7.159 105.064 1.00166.72 C ANISOU 2669 CD GLN A1141 23867 23117 16361 3847 -4965 -2314 C ATOM 2670 OE1 GLN A1141 105.324 -6.074 104.821 1.00168.29 O ANISOU 2670 OE1 GLN A1141 24469 22953 16519 4515 -5437 -2578 O ATOM 2671 NE2 GLN A1141 105.179 -8.200 105.499 1.00154.18 N ANISOU 2671 NE2 GLN A1141 21455 22466 14659 3814 -4553 -2333 N ATOM 2672 N THR A1142 110.404 -6.151 107.008 1.00135.70 N ANISOU 2672 N THR A1142 21465 17480 12616 2222 -5108 -1991 N ATOM 2673 CA THR A1142 111.240 -6.822 108.011 1.00132.03 C ANISOU 2673 CA THR A1142 20714 17337 12115 1800 -4779 -1936 C ATOM 2674 C THR A1142 112.325 -5.841 108.522 1.00140.01 C ANISOU 2674 C THR A1142 22397 17660 13142 1544 -5174 -1981 C ATOM 2675 O THR A1142 113.472 -5.915 108.071 1.00137.65 O ANISOU 2675 O THR A1142 22269 17052 12981 827 -5181 -1573 O ATOM 2676 CB THR A1142 111.799 -8.150 107.463 1.00128.36 C ANISOU 2676 CB THR A1142 19763 17234 11773 1142 -4312 -1473 C ATOM 2677 OG1 THR A1142 112.508 -7.901 106.249 1.00124.19 O ANISOU 2677 OG1 THR A1142 19578 16216 11394 688 -4449 -1093 O ATOM 2678 CG2 THR A1142 110.719 -9.206 107.246 1.00123.30 C ANISOU 2678 CG2 THR A1142 18468 17298 11082 1335 -3964 -1472 C ATOM 2679 N PRO A1143 111.979 -4.901 109.446 1.00142.83 N ANISOU 2679 N PRO A1143 23140 17801 13330 2125 -5535 -2483 N ATOM 2680 CA PRO A1143 112.972 -3.909 109.903 1.00146.32 C ANISOU 2680 CA PRO A1143 24320 17492 13783 1845 -6021 -2539 C ATOM 2681 C PRO A1143 114.168 -4.461 110.660 1.00147.21 C ANISOU 2681 C PRO A1143 24213 17818 13902 1170 -5786 -2339 C ATOM 2682 O PRO A1143 115.272 -3.964 110.455 1.00148.51 O ANISOU 2682 O PRO A1143 24806 17438 14185 522 -6074 -2056 O ATOM 2683 CB PRO A1143 112.154 -2.944 110.772 1.00155.07 C ANISOU 2683 CB PRO A1143 25842 18424 14652 2784 -6437 -3224 C ATOM 2684 CG PRO A1143 110.734 -3.202 110.423 1.00160.48 C ANISOU 2684 CG PRO A1143 26066 19669 15239 3560 -6246 -3458 C ATOM 2685 CD PRO A1143 110.663 -4.650 110.067 1.00148.77 C ANISOU 2685 CD PRO A1143 23693 18994 13837 3087 -5562 -3043 C ATOM 2686 N ASN A1144 113.960 -5.467 111.528 1.00139.78 N ANISOU 2686 N ASN A1144 22607 17688 12816 1289 -5300 -2451 N ATOM 2687 CA ASN A1144 115.033 -6.060 112.326 1.00136.56 C ANISOU 2687 CA ASN A1144 21960 17541 12386 744 -5092 -2281 C ATOM 2688 C ASN A1144 116.023 -6.860 111.485 1.00134.21 C ANISOU 2688 C ASN A1144 21359 17312 12322 -34 -4817 -1689 C ATOM 2689 O ASN A1144 117.228 -6.701 111.671 1.00134.03 O ANISOU 2689 O ASN A1144 21464 17098 12363 -605 -4941 -1474 O ATOM 2690 CB ASN A1144 114.472 -6.881 113.487 1.00137.02 C ANISOU 2690 CB ASN A1144 21454 18430 12177 1100 -4697 -2533 C ATOM 2691 CG ASN A1144 113.564 -6.089 114.399 1.00163.45 C ANISOU 2691 CG ASN A1144 25030 21876 15199 1925 -4927 -3165 C ATOM 2692 OD1 ASN A1144 113.943 -5.049 114.953 1.00162.05 O ANISOU 2692 OD1 ASN A1144 25486 21168 14918 2079 -5406 -3492 O ATOM 2693 ND2 ASN A1144 112.335 -6.557 114.559 1.00154.79 N ANISOU 2693 ND2 ASN A1144 23416 21495 13902 2482 -4613 -3363 N ATOM 2694 N ARG A1145 115.521 -7.677 110.536 1.00126.78 N ANISOU 2694 N ARG A1145 20020 16666 11485 -36 -4478 -1447 N ATOM 2695 CA ARG A1145 116.352 -8.478 109.629 1.00122.07 C ANISOU 2695 CA ARG A1145 19141 16183 11056 -629 -4210 -955 C ATOM 2696 C ARG A1145 117.155 -7.598 108.661 1.00128.18 C ANISOU 2696 C ARG A1145 20384 16371 11946 -1102 -4537 -659 C ATOM 2697 O ARG A1145 118.360 -7.815 108.519 1.00127.68 O ANISOU 2697 O ARG A1145 20200 16376 11937 -1692 -4468 -334 O ATOM 2698 CB ARG A1145 115.524 -9.522 108.862 1.00116.36 C ANISOU 2698 CB ARG A1145 17970 15870 10371 -465 -3841 -836 C ATOM 2699 CG ARG A1145 116.408 -10.569 108.201 1.00116.94 C ANISOU 2699 CG ARG A1145 17714 16168 10550 -951 -3531 -434 C ATOM 2700 CD ARG A1145 115.638 -11.628 107.454 1.00116.75 C ANISOU 2700 CD ARG A1145 17351 16455 10553 -821 -3249 -339 C ATOM 2701 NE ARG A1145 116.551 -12.479 106.691 1.00110.91 N ANISOU 2701 NE ARG A1145 16422 15837 9882 -1197 -3031 -16 N ATOM 2702 CZ ARG A1145 116.200 -13.604 106.080 1.00113.70 C ANISOU 2702 CZ ARG A1145 16510 16441 10251 -1165 -2799 82 C ATOM 2703 NH1 ARG A1145 114.945 -14.032 106.130 1.00 95.92 N ANISOU 2703 NH1 ARG A1145 14106 14369 7970 -887 -2751 -56 N ATOM 2704 NH2 ARG A1145 117.103 -14.313 105.417 1.00 97.82 N ANISOU 2704 NH2 ARG A1145 14375 14533 8260 -1404 -2638 305 N ATOM 2705 N ALA A1146 116.496 -6.603 108.017 1.00126.78 N ANISOU 2705 N ALA A1146 20727 15664 11778 -848 -4914 -750 N ATOM 2706 CA ALA A1146 117.147 -5.673 107.091 1.00129.30 C ANISOU 2706 CA ALA A1146 21590 15375 12163 -1335 -5298 -421 C ATOM 2707 C ALA A1146 118.272 -4.873 107.768 1.00135.47 C ANISOU 2707 C ALA A1146 22772 15762 12938 -1856 -5686 -356 C ATOM 2708 O ALA A1146 119.332 -4.705 107.167 1.00136.28 O ANISOU 2708 O ALA A1146 22920 15780 13078 -2598 -5746 103 O ATOM 2709 CB ALA A1146 116.125 -4.737 106.470 1.00133.97 C ANISOU 2709 CB ALA A1146 22743 15416 12744 -856 -5717 -583 C ATOM 2710 N LYS A1147 118.056 -4.431 109.031 1.00133.15 N ANISOU 2710 N LYS A1147 22722 15312 12557 -1492 -5938 -811 N ATOM 2711 CA LYS A1147 119.035 -3.681 109.829 1.00136.59 C ANISOU 2711 CA LYS A1147 23577 15358 12964 -1944 -6372 -831 C ATOM 2712 C LYS A1147 120.297 -4.495 110.125 1.00136.20 C ANISOU 2712 C LYS A1147 22933 15870 12945 -2618 -6032 -487 C ATOM 2713 O LYS A1147 121.391 -3.940 110.058 1.00139.53 O ANISOU 2713 O LYS A1147 23573 16045 13398 -3355 -6340 -178 O ATOM 2714 CB LYS A1147 118.414 -3.151 111.129 1.00142.00 C ANISOU 2714 CB LYS A1147 24612 15859 13482 -1272 -6670 -1474 C ATOM 2715 CG LYS A1147 117.776 -1.775 110.988 1.00157.97 C ANISOU 2715 CG LYS A1147 27579 16978 15464 -834 -7377 -1799 C ATOM 2716 CD LYS A1147 117.317 -1.239 112.336 1.00170.55 C ANISOU 2716 CD LYS A1147 29548 18423 16832 -170 -7704 -2483 C ATOM 2717 CE LYS A1147 116.916 0.213 112.271 1.00187.26 C ANISOU 2717 CE LYS A1147 32754 19494 18902 237 -8548 -2830 C ATOM 2718 NZ LYS A1147 116.862 0.832 113.621 1.00194.79 N ANISOU 2718 NZ LYS A1147 33607 20630 19773 643 -8467 -3434 N ATOM 2719 N ARG A1148 120.148 -5.802 110.437 1.00125.86 N ANISOU 2719 N ARG A1148 20885 15318 11617 -2382 -5440 -517 N ATOM 2720 CA ARG A1148 121.276 -6.702 110.707 1.00122.66 C ANISOU 2720 CA ARG A1148 19885 15486 11234 -2858 -5115 -230 C ATOM 2721 C ARG A1148 122.088 -6.967 109.431 1.00126.43 C ANISOU 2721 C ARG A1148 20097 16140 11800 -3440 -4935 306 C ATOM 2722 O ARG A1148 123.315 -7.028 109.499 1.00127.82 O ANISOU 2722 O ARG A1148 20024 16564 11978 -4032 -4947 601 O ATOM 2723 CB ARG A1148 120.807 -8.030 111.331 1.00116.77 C ANISOU 2723 CB ARG A1148 18543 15394 10431 -2411 -4613 -393 C ATOM 2724 CG ARG A1148 120.344 -7.922 112.786 1.00124.69 C ANISOU 2724 CG ARG A1148 19653 16471 11252 -1982 -4720 -844 C ATOM 2725 CD ARG A1148 120.129 -9.277 113.450 1.00121.10 C ANISOU 2725 CD ARG A1148 18606 16699 10708 -1769 -4262 -859 C ATOM 2726 NE ARG A1148 119.036 -10.045 112.844 1.00117.94 N ANISOU 2726 NE ARG A1148 17914 16569 10328 -1404 -3901 -849 N ATOM 2727 CZ ARG A1148 117.772 -10.027 113.259 1.00123.51 C ANISOU 2727 CZ ARG A1148 18613 17438 10879 -860 -3834 -1171 C ATOM 2728 NH1 ARG A1148 117.413 -9.266 114.289 1.00105.53 N ANISOU 2728 NH1 ARG A1148 16625 15090 8382 -513 -4080 -1582 N ATOM 2729 NH2 ARG A1148 116.855 -10.764 112.646 1.00102.89 N ANISOU 2729 NH2 ARG A1148 15686 15111 8296 -651 -3537 -1099 N ATOM 2730 N VAL A1149 121.401 -7.113 108.276 1.00121.44 N ANISOU 2730 N VAL A1149 19488 15454 11201 -3256 -4775 422 N ATOM 2731 CA VAL A1149 122.007 -7.362 106.959 1.00121.07 C ANISOU 2731 CA VAL A1149 19214 15630 11156 -3708 -4575 891 C ATOM 2732 C VAL A1149 122.787 -6.126 106.471 1.00132.28 C ANISOU 2732 C VAL A1149 21106 16609 12544 -4436 -5038 1247 C ATOM 2733 O VAL A1149 123.950 -6.264 106.086 1.00133.76 O ANISOU 2733 O VAL A1149 20943 17204 12675 -5076 -4925 1656 O ATOM 2734 CB VAL A1149 120.965 -7.874 105.920 1.00121.32 C ANISOU 2734 CB VAL A1149 19183 15724 11190 -3272 -4314 873 C ATOM 2735 CG1 VAL A1149 121.540 -7.901 104.505 1.00122.20 C ANISOU 2735 CG1 VAL A1149 19200 16006 11225 -3723 -4184 1331 C ATOM 2736 CG2 VAL A1149 120.440 -9.255 106.302 1.00115.64 C ANISOU 2736 CG2 VAL A1149 17929 15519 10490 -2783 -3860 656 C ATOM 2737 N ILE A1150 122.148 -4.931 106.498 1.00133.37 N ANISOU 2737 N ILE A1150 22035 15944 12696 -4334 -5588 1096 N ATOM 2738 CA ILE A1150 122.741 -3.650 106.086 1.00140.39 C ANISOU 2738 CA ILE A1150 23571 16216 13555 -5044 -6174 1437 C ATOM 2739 C ILE A1150 124.046 -3.364 106.867 1.00147.96 C ANISOU 2739 C ILE A1150 24428 17292 14499 -5777 -6396 1610 C ATOM 2740 O ILE A1150 125.041 -2.961 106.260 1.00151.92 O ANISOU 2740 O ILE A1150 24904 17884 14934 -6662 -6539 2147 O ATOM 2741 CB ILE A1150 121.689 -2.496 106.165 1.00147.72 C ANISOU 2741 CB ILE A1150 25452 16168 14506 -4587 -6796 1121 C ATOM 2742 CG1 ILE A1150 120.656 -2.611 105.026 1.00146.16 C ANISOU 2742 CG1 ILE A1150 25355 15884 14297 -4158 -6668 1182 C ATOM 2743 CG2 ILE A1150 122.340 -1.101 106.166 1.00157.53 C ANISOU 2743 CG2 ILE A1150 27548 16577 15731 -5305 -7586 1363 C ATOM 2744 CD1 ILE A1150 119.332 -1.885 105.276 1.00154.31 C ANISOU 2744 CD1 ILE A1150 27024 16253 15352 -3287 -7085 681 C ATOM 2745 N THR A1151 124.044 -3.626 108.194 1.00143.06 N ANISOU 2745 N THR A1151 23684 16771 13902 -5437 -6403 1184 N ATOM 2746 CA THR A1151 125.192 -3.446 109.093 1.00145.80 C ANISOU 2746 CA THR A1151 23896 17275 14227 -6030 -6626 1269 C ATOM 2747 C THR A1151 126.360 -4.375 108.685 1.00147.65 C ANISOU 2747 C THR A1151 23198 18472 14429 -6559 -6133 1728 C ATOM 2748 O THR A1151 127.511 -3.939 108.725 1.00152.76 O ANISOU 2748 O THR A1151 23740 19270 15032 -7411 -6384 2106 O ATOM 2749 CB THR A1151 124.743 -3.581 110.566 1.00150.88 C ANISOU 2749 CB THR A1151 24634 17851 14845 -5412 -6712 669 C ATOM 2750 OG1 THR A1151 123.689 -2.646 110.813 1.00152.36 O ANISOU 2750 OG1 THR A1151 25664 17219 15007 -4858 -7174 227 O ATOM 2751 CG2 THR A1151 125.873 -3.339 111.565 1.00152.61 C ANISOU 2751 CG2 THR A1151 24796 18169 15019 -5996 -7032 710 C ATOM 2752 N THR A1152 126.058 -5.623 108.249 1.00137.11 N ANISOU 2752 N THR A1152 21210 17788 13099 -6051 -5476 1694 N ATOM 2753 CA THR A1152 127.055 -6.604 107.789 1.00135.21 C ANISOU 2753 CA THR A1152 20098 18477 12797 -6314 -4988 2031 C ATOM 2754 C THR A1152 127.727 -6.130 106.489 1.00142.75 C ANISOU 2754 C THR A1152 20978 19630 13630 -7047 -4995 2603 C ATOM 2755 O THR A1152 128.927 -6.341 106.319 1.00145.54 O ANISOU 2755 O THR A1152 20726 20696 13876 -7607 -4857 2963 O ATOM 2756 CB THR A1152 126.438 -8.013 107.658 1.00137.31 C ANISOU 2756 CB THR A1152 19881 19203 13090 -5525 -4400 1794 C ATOM 2757 OG1 THR A1152 125.657 -8.305 108.820 1.00136.01 O ANISOU 2757 OG1 THR A1152 19877 18815 12988 -4930 -4440 1324 O ATOM 2758 CG2 THR A1152 127.491 -9.106 107.471 1.00134.37 C ANISOU 2758 CG2 THR A1152 18661 19746 12649 -5604 -3973 2004 C ATOM 2759 N PHE A1153 126.960 -5.488 105.585 1.00139.54 N ANISOU 2759 N PHE A1153 21158 18659 13203 -7039 -5164 2699 N ATOM 2760 CA PHE A1153 127.475 -4.946 104.322 1.00143.76 C ANISOU 2760 CA PHE A1153 21738 19322 13564 -7767 -5216 3281 C ATOM 2761 C PHE A1153 128.326 -3.695 104.576 1.00154.98 C ANISOU 2761 C PHE A1153 23568 20375 14941 -8795 -5846 3665 C ATOM 2762 O PHE A1153 129.356 -3.506 103.927 1.00159.42 O ANISOU 2762 O PHE A1153 23749 21512 15313 -9651 -5796 4239 O ATOM 2763 CB PHE A1153 126.319 -4.583 103.368 1.00144.56 C ANISOU 2763 CB PHE A1153 22441 18837 13649 -7415 -5297 3260 C ATOM 2764 CG PHE A1153 125.801 -5.678 102.466 1.00140.61 C ANISOU 2764 CG PHE A1153 21480 18878 13068 -6836 -4692 3197 C ATOM 2765 CD1 PHE A1153 126.647 -6.328 101.574 1.00144.43 C ANISOU 2765 CD1 PHE A1153 21278 20279 13321 -7145 -4229 3562 C ATOM 2766 CD2 PHE A1153 124.450 -5.998 102.442 1.00137.87 C ANISOU 2766 CD2 PHE A1153 21411 18137 12835 -5998 -4628 2777 C ATOM 2767 CE1 PHE A1153 126.160 -7.318 100.716 1.00141.15 C ANISOU 2767 CE1 PHE A1153 20541 20291 12800 -6586 -3738 3458 C ATOM 2768 CE2 PHE A1153 123.962 -6.985 101.579 1.00136.35 C ANISOU 2768 CE2 PHE A1153 20859 18387 12562 -5538 -4149 2728 C ATOM 2769 CZ PHE A1153 124.820 -7.639 100.724 1.00135.12 C ANISOU 2769 CZ PHE A1153 20114 19043 12183 -5824 -3727 3051 C ATOM 2770 N ARG A1154 127.874 -2.840 105.512 1.00152.99 N ANISOU 2770 N ARG A1154 24105 19191 14835 -8712 -6461 3342 N ATOM 2771 CA ARG A1154 128.504 -1.574 105.867 1.00161.04 C ANISOU 2771 CA ARG A1154 25748 19599 15841 -9630 -7221 3613 C ATOM 2772 C ARG A1154 129.835 -1.752 106.607 1.00168.27 C ANISOU 2772 C ARG A1154 26020 21196 16719 -10315 -7236 3806 C ATOM 2773 O ARG A1154 130.842 -1.205 106.159 1.00170.05 O ANISOU 2773 O ARG A1154 25789 21707 17115 -10759 -7048 4098 O ATOM 2774 CB ARG A1154 127.517 -0.701 106.667 1.00161.62 C ANISOU 2774 CB ARG A1154 26900 18458 16051 -9113 -7880 3074 C ATOM 2775 CG ARG A1154 127.954 0.742 106.869 1.00172.58 C ANISOU 2775 CG ARG A1154 28574 19186 17811 -9214 -8151 2930 C ATOM 2776 CD ARG A1154 127.115 1.414 107.936 1.00177.74 C ANISOU 2776 CD ARG A1154 29708 19087 18736 -8209 -8348 2084 C ATOM 2777 NE ARG A1154 127.812 2.551 108.536 1.00185.29 N ANISOU 2777 NE ARG A1154 30113 19983 20305 -7819 -7945 1581 N ATOM 2778 CZ ARG A1154 127.700 3.808 108.118 1.00195.22 C ANISOU 2778 CZ ARG A1154 30967 21019 22190 -7100 -7309 1188 C ATOM 2779 NH1 ARG A1154 126.913 4.106 107.090 1.00186.56 N ANISOU 2779 NH1 ARG A1154 30714 19310 20862 -7300 -7767 1582 N ATOM 2780 NH2 ARG A1154 128.375 4.777 108.723 1.00185.97 N ANISOU 2780 NH2 ARG A1154 30221 19338 21101 -7696 -7852 1156 N ATOM 2781 N THR A1155 129.838 -2.501 107.730 1.00161.17 N ANISOU 2781 N THR A1155 24730 20593 15914 -9716 -7030 3320 N ATOM 2782 CA THR A1155 131.028 -2.705 108.567 1.00164.19 C ANISOU 2782 CA THR A1155 24520 21597 16268 -10234 -7096 3426 C ATOM 2783 C THR A1155 131.910 -3.889 108.164 1.00166.82 C ANISOU 2783 C THR A1155 23619 23270 16495 -10262 -6396 3700 C ATOM 2784 O THR A1155 133.103 -3.890 108.478 1.00171.20 O ANISOU 2784 O THR A1155 23590 24493 16966 -10967 -6486 4017 O ATOM 2785 CB THR A1155 130.646 -2.817 110.053 1.00170.34 C ANISOU 2785 CB THR A1155 25561 22016 17145 -9613 -7308 2789 C ATOM 2786 OG1 THR A1155 129.743 -3.908 110.236 1.00159.94 O ANISOU 2786 OG1 THR A1155 23956 20935 15879 -8501 -6724 2342 O ATOM 2787 CG2 THR A1155 130.068 -1.522 110.623 1.00174.65 C ANISOU 2787 CG2 THR A1155 27307 21320 17730 -9681 -8129 2493 C ATOM 2788 N GLY A1156 131.322 -4.890 107.517 1.00157.60 N ANISOU 2788 N GLY A1156 22070 22489 15320 -9463 -5753 3544 N ATOM 2789 CA GLY A1156 132.036 -6.101 107.127 1.00155.74 C ANISOU 2789 CA GLY A1156 20762 23440 14971 -9260 -5109 3685 C ATOM 2790 C GLY A1156 132.375 -6.969 108.322 1.00157.62 C ANISOU 2790 C GLY A1156 20506 24091 15292 -8765 -4978 3335 C ATOM 2791 O GLY A1156 133.424 -7.619 108.340 1.00159.04 O ANISOU 2791 O GLY A1156 19807 25253 15369 -8883 -4716 3520 O ATOM 2792 N THR A1157 131.488 -6.960 109.341 1.00150.96 N ANISOU 2792 N THR A1157 20221 22538 14598 -8190 -5181 2830 N ATOM 2793 CA THR A1157 131.623 -7.717 110.591 1.00148.07 C ANISOU 2793 CA THR A1157 19557 22421 14280 -7698 -5122 2481 C ATOM 2794 C THR A1157 130.343 -8.486 110.952 1.00145.10 C ANISOU 2794 C THR A1157 19441 21707 13984 -6701 -4842 2003 C ATOM 2795 O THR A1157 129.256 -8.181 110.446 1.00141.87 O ANISOU 2795 O THR A1157 19559 20729 13617 -6408 -4821 1866 O ATOM 2796 CB THR A1157 132.045 -6.800 111.756 1.00160.27 C ANISOU 2796 CB THR A1157 21495 23568 15832 -8202 -5761 2389 C ATOM 2797 OG1 THR A1157 131.161 -5.680 111.824 1.00160.85 O ANISOU 2797 OG1 THR A1157 22578 22588 15948 -8259 -6226 2194 O ATOM 2798 CG2 THR A1157 133.501 -6.345 111.665 1.00166.14 C ANISOU 2798 CG2 THR A1157 21739 24899 16487 -9212 -6022 2875 C ATOM 2799 N TRP A1158 130.486 -9.473 111.855 1.00139.56 N ANISOU 2799 N TRP A1158 18360 21385 13283 -6219 -4664 1780 N ATOM 2800 CA TRP A1158 129.389 -10.300 112.362 1.00133.65 C ANISOU 2800 CA TRP A1158 17774 20440 12566 -5394 -4420 1397 C ATOM 2801 C TRP A1158 128.709 -9.624 113.566 1.00138.66 C ANISOU 2801 C TRP A1158 19032 20489 13164 -5244 -4797 1015 C ATOM 2802 O TRP A1158 127.718 -10.148 114.076 1.00134.15 O ANISOU 2802 O TRP A1158 18608 19801 12563 -4628 -4625 706 O ATOM 2803 CB TRP A1158 129.904 -11.701 112.740 1.00129.80 C ANISOU 2803 CB TRP A1158 16637 20625 12058 -4984 -4096 1399 C ATOM 2804 CG TRP A1158 130.579 -12.422 111.613 1.00130.92 C ANISOU 2804 CG TRP A1158 16169 21394 12182 -4973 -3739 1678 C ATOM 2805 CD1 TRP A1158 131.921 -12.566 111.420 1.00138.17 C ANISOU 2805 CD1 TRP A1158 16431 23043 13024 -5316 -3729 1954 C ATOM 2806 CD2 TRP A1158 129.941 -13.048 110.493 1.00127.40 C ANISOU 2806 CD2 TRP A1158 15698 20963 11748 -4579 -3357 1680 C ATOM 2807 NE1 TRP A1158 132.160 -13.274 110.265 1.00137.33 N ANISOU 2807 NE1 TRP A1158 15883 23445 12853 -5083 -3333 2096 N ATOM 2808 CE2 TRP A1158 130.962 -13.577 109.672 1.00134.00 C ANISOU 2808 CE2 TRP A1158 15881 22549 12484 -4643 -3116 1926 C ATOM 2809 CE3 TRP A1158 128.600 -13.229 110.107 1.00124.06 C ANISOU 2809 CE3 TRP A1158 15711 20044 11381 -4160 -3209 1483 C ATOM 2810 CZ2 TRP A1158 130.685 -14.270 108.487 1.00131.64 C ANISOU 2810 CZ2 TRP A1158 15435 22457 12125 -4279 -2746 1947 C ATOM 2811 CZ3 TRP A1158 128.327 -13.932 108.944 1.00123.39 C ANISOU 2811 CZ3 TRP A1158 15471 20140 11272 -3868 -2870 1539 C ATOM 2812 CH2 TRP A1158 129.361 -14.454 108.156 1.00126.68 C ANISOU 2812 CH2 TRP A1158 15313 21246 11574 -3908 -2647 1750 C ATOM 2813 N ASP A1159 129.234 -8.444 113.988 1.00141.37 N ANISOU 2813 N ASP A1159 19750 20488 13475 -5828 -5331 1041 N ATOM 2814 CA ASP A1159 128.795 -7.597 115.106 1.00144.24 C ANISOU 2814 CA ASP A1159 20779 20274 13752 -5753 -5809 653 C ATOM 2815 C ASP A1159 127.275 -7.490 115.299 1.00145.35 C ANISOU 2815 C ASP A1159 21444 19934 13846 -5014 -5732 210 C ATOM 2816 O ASP A1159 126.817 -7.528 116.441 1.00145.51 O ANISOU 2816 O ASP A1159 21673 19902 13711 -4612 -5835 -178 O ATOM 2817 CB ASP A1159 129.411 -6.187 114.991 1.00153.58 C ANISOU 2817 CB ASP A1159 22471 20943 14941 -6555 -6450 806 C ATOM 2818 CG ASP A1159 130.863 -6.054 115.432 1.00169.24 C ANISOU 2818 CG ASP A1159 24034 23381 16891 -7324 -6731 1108 C ATOM 2819 OD1 ASP A1159 131.561 -7.092 115.514 1.00168.16 O ANISOU 2819 OD1 ASP A1159 23072 24074 16750 -7261 -6358 1296 O ATOM 2820 OD2 ASP A1159 131.309 -4.907 115.667 1.00180.99 O ANISOU 2820 OD2 ASP A1159 26026 24390 18352 -7992 -7366 1161 O ATOM 2821 N ALA A1160 126.503 -7.356 114.204 1.00139.77 N ANISOU 2821 N ALA A1160 20911 18962 13233 -4827 -5555 269 N ATOM 2822 CA ALA A1160 125.039 -7.256 114.245 1.00137.35 C ANISOU 2822 CA ALA A1160 20997 18306 12883 -4116 -5474 -121 C ATOM 2823 C ALA A1160 124.375 -8.544 114.769 1.00135.90 C ANISOU 2823 C ALA A1160 20355 18656 12624 -3504 -4974 -288 C ATOM 2824 O ALA A1160 123.340 -8.473 115.437 1.00134.53 O ANISOU 2824 O ALA A1160 20411 18398 12307 -2952 -4963 -677 O ATOM 2825 CB ALA A1160 124.502 -6.909 112.863 1.00137.50 C ANISOU 2825 CB ALA A1160 21227 17996 13020 -4126 -5420 55 C ATOM 2826 N TYR A1161 124.993 -9.708 114.484 1.00130.03 N ANISOU 2826 N TYR A1161 18976 18482 11947 -3610 -4594 15 N ATOM 2827 CA TYR A1161 124.530 -11.041 114.880 1.00126.14 C ANISOU 2827 CA TYR A1161 18083 18442 11401 -3162 -4184 -32 C ATOM 2828 C TYR A1161 125.168 -11.551 116.183 1.00134.82 C ANISOU 2828 C TYR A1161 18963 19904 12357 -3178 -4249 -74 C ATOM 2829 O TYR A1161 124.504 -12.250 116.950 1.00133.00 O ANISOU 2829 O TYR A1161 18662 19891 11979 -2797 -4074 -221 O ATOM 2830 CB TYR A1161 124.747 -12.039 113.731 1.00123.29 C ANISOU 2830 CB TYR A1161 17284 18379 11182 -3161 -3801 278 C ATOM 2831 CG TYR A1161 123.912 -11.720 112.509 1.00122.63 C ANISOU 2831 CG TYR A1161 17410 17999 11186 -3052 -3699 297 C ATOM 2832 CD1 TYR A1161 124.405 -10.903 111.497 1.00126.77 C ANISOU 2832 CD1 TYR A1161 18070 18314 11781 -3467 -3842 522 C ATOM 2833 CD2 TYR A1161 122.612 -12.200 112.385 1.00120.10 C ANISOU 2833 CD2 TYR A1161 17144 17641 10846 -2580 -3489 121 C ATOM 2834 CE1 TYR A1161 123.626 -10.569 110.392 1.00126.18 C ANISOU 2834 CE1 TYR A1161 18235 17953 11755 -3363 -3792 556 C ATOM 2835 CE2 TYR A1161 121.826 -11.876 111.282 1.00120.08 C ANISOU 2835 CE2 TYR A1161 17327 17384 10913 -2463 -3441 130 C ATOM 2836 CZ TYR A1161 122.341 -11.067 110.284 1.00128.78 C ANISOU 2836 CZ TYR A1161 18612 18235 12084 -2830 -3597 342 C ATOM 2837 OH TYR A1161 121.576 -10.750 109.191 1.00129.48 O ANISOU 2837 OH TYR A1161 18915 18071 12211 -2711 -3581 374 O ATOM 2838 N GLY A1162 126.432 -11.193 116.415 1.00137.09 N ANISOU 2838 N GLY A1162 19131 20293 12664 -3659 -4517 89 N ATOM 2839 CA GLY A1162 127.182 -11.582 117.605 1.00139.68 C ANISOU 2839 CA GLY A1162 19247 20971 12855 -3725 -4657 77 C ATOM 2840 C GLY A1162 128.679 -11.379 117.486 1.00150.32 C ANISOU 2840 C GLY A1162 20253 22588 14274 -4298 -4884 366 C ATOM 2841 O GLY A1162 129.146 -10.670 116.592 1.00151.86 O ANISOU 2841 O GLY A1162 20467 22645 14586 -4761 -5008 566 O ATOM 2842 N SER A1163 129.442 -11.995 118.403 1.00151.28 N ANISOU 2842 N SER A1163 20038 23147 14295 -4298 -4962 419 N ATOM 2843 CA SER A1163 130.905 -11.917 118.428 1.00156.57 C ANISOU 2843 CA SER A1163 20248 24242 15001 -4796 -5186 689 C ATOM 2844 C SER A1163 131.515 -12.955 117.464 1.00162.74 C ANISOU 2844 C SER A1163 20349 25576 15908 -4666 -4811 1000 C ATOM 2845 O SER A1163 131.913 -12.589 116.352 1.00164.22 O ANISOU 2845 O SER A1163 20325 25877 16195 -5005 -4728 1228 O ATOM 2846 CB SER A1163 131.424 -12.091 119.851 1.00162.32 C ANISOU 2846 CB SER A1163 20935 25202 15537 -4793 -5490 577 C ATOM 2847 OG SER A1163 130.927 -13.286 120.430 1.00167.61 O ANISOU 2847 OG SER A1163 21499 26082 16101 -4207 -5226 515 O ATOM 2848 N TRP A 273 131.550 -14.246 117.883 1.00147.08 N ANISOU 2848 N TRP A 273 20039 22496 13348 -1574 -796 475 N ATOM 2849 CA TRP A 273 132.031 -15.434 117.150 1.00149.37 C ANISOU 2849 CA TRP A 273 20324 22994 13438 -1547 -710 167 C ATOM 2850 C TRP A 273 133.541 -15.424 116.774 1.00153.70 C ANISOU 2850 C TRP A 273 20828 23795 13777 -1620 -405 68 C ATOM 2851 O TRP A 273 134.011 -16.380 116.147 1.00155.40 O ANISOU 2851 O TRP A 273 21028 24203 13814 -1569 -318 -215 O ATOM 2852 CB TRP A 273 131.170 -15.730 115.889 1.00151.38 C ANISOU 2852 CB TRP A 273 20743 23390 13386 -1564 -905 131 C ATOM 2853 CG TRP A 273 129.679 -15.711 116.095 1.00152.03 C ANISOU 2853 CG TRP A 273 20840 23291 13635 -1507 -1214 220 C ATOM 2854 CD1 TRP A 273 128.783 -14.881 115.488 1.00156.55 C ANISOU 2854 CD1 TRP A 273 21545 23881 14057 -1540 -1425 454 C ATOM 2855 CD2 TRP A 273 128.909 -16.583 116.942 1.00150.05 C ANISOU 2855 CD2 TRP A 273 20456 22835 13721 -1411 -1348 70 C ATOM 2856 NE1 TRP A 273 127.505 -15.172 115.908 1.00155.20 N ANISOU 2856 NE1 TRP A 273 21295 23555 14119 -1457 -1679 439 N ATOM 2857 CE2 TRP A 273 127.554 -16.204 116.810 1.00154.53 C ANISOU 2857 CE2 TRP A 273 21045 23336 14332 -1398 -1625 214 C ATOM 2858 CE3 TRP A 273 129.235 -17.636 117.817 1.00149.60 C ANISOU 2858 CE3 TRP A 273 20267 22643 13930 -1338 -1268 -160 C ATOM 2859 CZ2 TRP A 273 126.525 -16.841 117.520 1.00152.56 C ANISOU 2859 CZ2 TRP A 273 20661 22923 14381 -1345 -1796 130 C ATOM 2860 CZ3 TRP A 273 128.215 -18.268 118.517 1.00149.74 C ANISOU 2860 CZ3 TRP A 273 20196 22465 14232 -1296 -1444 -218 C ATOM 2861 CH2 TRP A 273 126.880 -17.872 118.365 1.00150.83 C ANISOU 2861 CH2 TRP A 273 20330 22573 14406 -1313 -1692 -78 C ATOM 2862 N GLY A 274 134.278 -14.387 117.171 1.00148.25 N ANISOU 2862 N GLY A 274 20103 23107 13117 -1735 -249 277 N ATOM 2863 CA GLY A 274 135.702 -14.277 116.872 1.00149.24 C ANISOU 2863 CA GLY A 274 20143 23499 13061 -1837 48 203 C ATOM 2864 C GLY A 274 136.551 -15.083 117.831 1.00150.28 C ANISOU 2864 C GLY A 274 20039 23599 13461 -1703 190 -57 C ATOM 2865 O GLY A 274 136.452 -16.312 117.874 1.00149.56 O ANISOU 2865 O GLY A 274 19895 23492 13438 -1530 146 -351 O ATOM 2866 N ARG A 275 137.399 -14.381 118.598 1.00144.94 N ANISOU 2866 N ARG A 275 19234 22901 12936 -1784 344 50 N ATOM 2867 CA ARG A 275 138.261 -14.943 119.638 1.00142.47 C ANISOU 2867 CA ARG A 275 18688 22552 12893 -1660 461 -154 C ATOM 2868 C ARG A 275 137.566 -14.719 120.980 1.00140.77 C ANISOU 2868 C ARG A 275 18451 21964 13071 -1572 293 -36 C ATOM 2869 O ARG A 275 138.027 -15.209 122.014 1.00138.78 O ANISOU 2869 O ARG A 275 18041 21612 13078 -1442 325 -178 O ATOM 2870 CB ARG A 275 139.638 -14.257 119.631 1.00144.74 C ANISOU 2870 CB ARG A 275 18825 23083 13088 -1826 728 -116 C ATOM 2871 N ILE A 276 136.441 -13.978 120.946 1.00134.70 N ANISOU 2871 N ILE A 276 17844 21006 12331 -1629 106 219 N ATOM 2872 CA ILE A 276 135.612 -13.642 122.105 1.00130.89 C ANISOU 2872 CA ILE A 276 17354 20202 12177 -1550 -59 348 C ATOM 2873 C ILE A 276 134.850 -14.894 122.592 1.00130.41 C ANISOU 2873 C ILE A 276 17250 19993 12306 -1362 -200 153 C ATOM 2874 O ILE A 276 134.495 -14.966 123.770 1.00127.82 O ANISOU 2874 O ILE A 276 16849 19448 12270 -1275 -267 173 O ATOM 2875 CB ILE A 276 134.685 -12.412 121.817 1.00134.52 C ANISOU 2875 CB ILE A 276 17991 20537 12583 -1648 -216 664 C ATOM 2876 CG1 ILE A 276 135.442 -11.278 121.082 1.00137.64 C ANISOU 2876 CG1 ILE A 276 18490 21078 12727 -1873 -85 869 C ATOM 2877 CG2 ILE A 276 134.041 -11.863 123.098 1.00132.57 C ANISOU 2877 CG2 ILE A 276 17707 19993 12669 -1566 -341 788 C ATOM 2878 CD1 ILE A 276 135.061 -11.087 119.621 1.00149.28 C ANISOU 2878 CD1 ILE A 276 20163 22736 13821 -1975 -133 967 C ATOM 2879 N THR A 277 134.651 -15.892 121.695 1.00125.79 N ANISOU 2879 N THR A 277 16719 19530 11545 -1315 -239 -42 N ATOM 2880 CA THR A 277 133.974 -17.162 121.990 1.00123.45 C ANISOU 2880 CA THR A 277 16414 19091 11399 -1177 -378 -240 C ATOM 2881 C THR A 277 134.720 -17.961 123.095 1.00123.48 C ANISOU 2881 C THR A 277 16280 18984 11652 -1041 -295 -423 C ATOM 2882 O THR A 277 134.063 -18.590 123.923 1.00121.61 O ANISOU 2882 O THR A 277 16032 18524 11651 -958 -418 -459 O ATOM 2883 CB THR A 277 133.699 -17.971 120.693 1.00131.33 C ANISOU 2883 CB THR A 277 17524 20249 12126 -1172 -439 -425 C ATOM 2884 OG1 THR A 277 132.850 -19.078 120.990 1.00128.31 O ANISOU 2884 OG1 THR A 277 17158 19681 11911 -1082 -612 -579 O ATOM 2885 CG2 THR A 277 134.969 -18.456 119.989 1.00131.85 C ANISOU 2885 CG2 THR A 277 17556 20584 11959 -1147 -233 -657 C ATOM 2886 N THR A 278 136.068 -17.906 123.124 1.00119.12 N ANISOU 2886 N THR A 278 15619 18599 11043 -1025 -93 -525 N ATOM 2887 CA THR A 278 136.882 -18.574 124.145 1.00117.32 C ANISOU 2887 CA THR A 278 15252 18294 11031 -876 -26 -694 C ATOM 2888 C THR A 278 137.001 -17.655 125.365 1.00118.42 C ANISOU 2888 C THR A 278 15306 18293 11396 -913 -10 -490 C ATOM 2889 O THR A 278 136.997 -18.150 126.493 1.00116.96 O ANISOU 2889 O THR A 278 15065 17921 11453 -793 -62 -538 O ATOM 2890 CB THR A 278 138.216 -19.086 123.563 1.00125.72 C ANISOU 2890 CB THR A 278 16210 19635 11924 -809 162 -946 C ATOM 2891 OG1 THR A 278 137.931 -20.007 122.509 1.00128.85 O ANISOU 2891 OG1 THR A 278 16714 20132 12112 -756 120 -1151 O ATOM 2892 CG2 THR A 278 139.078 -19.801 124.593 1.00122.55 C ANISOU 2892 CG2 THR A 278 15662 19159 11743 -614 200 -1138 C ATOM 2893 N GLU A 279 137.061 -16.318 125.140 1.00113.95 N ANISOU 2893 N GLU A 279 14755 17800 10739 -1081 46 -259 N ATOM 2894 CA GLU A 279 137.122 -15.308 126.204 1.00111.29 C ANISOU 2894 CA GLU A 279 14369 17323 10595 -1133 46 -66 C ATOM 2895 C GLU A 279 135.882 -15.409 127.105 1.00111.10 C ANISOU 2895 C GLU A 279 14396 17022 10794 -1054 -136 31 C ATOM 2896 O GLU A 279 136.026 -15.415 128.328 1.00109.50 O ANISOU 2896 O GLU A 279 14116 16680 10810 -984 -144 41 O ATOM 2897 CB GLU A 279 137.257 -13.888 125.623 1.00113.96 C ANISOU 2897 CB GLU A 279 14777 17750 10774 -1341 104 168 C ATOM 2898 CG GLU A 279 138.656 -13.534 125.148 1.00127.98 C ANISOU 2898 CG GLU A 279 16444 19790 12392 -1469 323 118 C ATOM 2899 CD GLU A 279 138.826 -12.092 124.711 1.00152.19 C ANISOU 2899 CD GLU A 279 19603 22893 15328 -1714 374 383 C ATOM 2900 OE1 GLU A 279 138.545 -11.789 123.529 1.00154.18 O ANISOU 2900 OE1 GLU A 279 20007 23260 15313 -1834 371 493 O ATOM 2901 OE2 GLU A 279 139.253 -11.264 125.548 1.00142.99 O ANISOU 2901 OE2 GLU A 279 18379 21630 14322 -1792 404 484 O ATOM 2902 N THR A 280 134.677 -15.548 126.497 1.00106.04 N ANISOU 2902 N THR A 280 13873 16331 10087 -1067 -281 89 N ATOM 2903 CA THR A 280 133.402 -15.704 127.212 1.00103.21 C ANISOU 2903 CA THR A 280 13532 15766 9916 -1009 -447 166 C ATOM 2904 C THR A 280 133.359 -17.029 127.968 1.00104.26 C ANISOU 2904 C THR A 280 13616 15782 10217 -891 -477 -10 C ATOM 2905 O THR A 280 132.921 -17.036 129.116 1.00102.77 O ANISOU 2905 O THR A 280 13381 15433 10232 -843 -524 51 O ATOM 2906 CB THR A 280 132.192 -15.544 126.282 1.00108.19 C ANISOU 2906 CB THR A 280 14270 16419 10419 -1060 -601 254 C ATOM 2907 OG1 THR A 280 132.409 -16.320 125.111 1.00111.98 O ANISOU 2907 OG1 THR A 280 14813 17054 10681 -1079 -590 94 O ATOM 2908 CG2 THR A 280 131.925 -14.099 125.906 1.00104.68 C ANISOU 2908 CG2 THR A 280 13903 15991 9881 -1145 -635 492 C ATOM 2909 N ALA A 281 133.852 -18.133 127.350 1.00 99.79 N ANISOU 2909 N ALA A 281 13070 15290 9555 -840 -449 -229 N ATOM 2910 CA ALA A 281 133.916 -19.463 127.971 1.00 98.46 C ANISOU 2910 CA ALA A 281 12900 14978 9533 -722 -494 -405 C ATOM 2911 C ALA A 281 134.736 -19.429 129.278 1.00100.53 C ANISOU 2911 C ALA A 281 13065 15156 9977 -627 -420 -409 C ATOM 2912 O ALA A 281 134.282 -19.964 130.291 1.00 99.33 O ANISOU 2912 O ALA A 281 12923 14812 10004 -571 -496 -396 O ATOM 2913 CB ALA A 281 134.504 -20.478 127.001 1.00101.02 C ANISOU 2913 CB ALA A 281 13276 15408 9702 -660 -469 -660 C ATOM 2914 N ILE A 282 135.906 -18.755 129.262 1.00 96.59 N ANISOU 2914 N ILE A 282 12470 14811 9419 -629 -278 -416 N ATOM 2915 CA ILE A 282 136.785 -18.596 130.427 1.00 95.35 C ANISOU 2915 CA ILE A 282 12200 14616 9412 -546 -217 -428 C ATOM 2916 C ILE A 282 136.131 -17.684 131.472 1.00 97.32 C ANISOU 2916 C ILE A 282 12443 14725 9807 -597 -266 -214 C ATOM 2917 O ILE A 282 136.248 -17.959 132.666 1.00 95.97 O ANISOU 2917 O ILE A 282 12240 14429 9796 -508 -295 -216 O ATOM 2918 CB ILE A 282 138.210 -18.123 130.005 1.00 99.68 C ANISOU 2918 CB ILE A 282 12617 15411 9846 -564 -51 -516 C ATOM 2919 CG1 ILE A 282 138.935 -19.174 129.098 1.00102.56 C ANISOU 2919 CG1 ILE A 282 12958 15937 10072 -458 8 -784 C ATOM 2920 CG2 ILE A 282 139.080 -17.694 131.197 1.00 98.74 C ANISOU 2920 CG2 ILE A 282 12360 15278 9877 -516 -4 -504 C ATOM 2921 CD1 ILE A 282 139.185 -20.641 129.686 1.00110.53 C ANISOU 2921 CD1 ILE A 282 13987 16792 11216 -224 -80 -1003 C ATOM 2922 N GLN A 283 135.417 -16.632 131.024 1.00 93.31 N ANISOU 2922 N GLN A 283 11981 14238 9234 -723 -287 -37 N ATOM 2923 CA GLN A 283 134.720 -15.713 131.925 1.00 91.51 C ANISOU 2923 CA GLN A 283 11753 13883 9133 -746 -342 143 C ATOM 2924 C GLN A 283 133.568 -16.420 132.656 1.00 94.83 C ANISOU 2924 C GLN A 283 12198 14147 9686 -686 -455 162 C ATOM 2925 O GLN A 283 133.426 -16.243 133.862 1.00 94.52 O ANISOU 2925 O GLN A 283 12120 14008 9786 -635 -464 213 O ATOM 2926 CB GLN A 283 134.218 -14.470 131.177 1.00 93.29 C ANISOU 2926 CB GLN A 283 12044 14150 9253 -864 -366 315 C ATOM 2927 CG GLN A 283 133.779 -13.350 132.113 1.00103.04 C ANISOU 2927 CG GLN A 283 13275 15259 10616 -862 -408 468 C ATOM 2928 CD GLN A 283 132.865 -12.360 131.450 1.00119.46 C ANISOU 2928 CD GLN A 283 15449 17313 12628 -919 -501 635 C ATOM 2929 OE1 GLN A 283 133.244 -11.213 131.194 1.00118.68 O ANISOU 2929 OE1 GLN A 283 15409 17207 12475 -1002 -481 751 O ATOM 2930 NE2 GLN A 283 131.626 -12.764 131.200 1.00105.46 N ANISOU 2930 NE2 GLN A 283 13693 15512 10865 -876 -620 655 N ATOM 2931 N LEU A 284 132.775 -17.240 131.941 1.00 91.39 N ANISOU 2931 N LEU A 284 11823 13703 9198 -707 -536 114 N ATOM 2932 CA LEU A 284 131.652 -17.985 132.525 1.00 90.33 C ANISOU 2932 CA LEU A 284 11702 13440 9181 -700 -637 131 C ATOM 2933 C LEU A 284 132.145 -19.049 133.515 1.00 94.36 C ANISOU 2933 C LEU A 284 12219 13828 9808 -616 -624 38 C ATOM 2934 O LEU A 284 131.477 -19.325 134.517 1.00 92.67 O ANISOU 2934 O LEU A 284 11996 13503 9713 -615 -663 108 O ATOM 2935 CB LEU A 284 130.783 -18.630 131.433 1.00 91.21 C ANISOU 2935 CB LEU A 284 11875 13579 9202 -769 -739 80 C ATOM 2936 CG LEU A 284 130.112 -17.696 130.430 1.00 95.47 C ANISOU 2936 CG LEU A 284 12427 14230 9619 -840 -800 188 C ATOM 2937 CD1 LEU A 284 129.836 -18.420 129.151 1.00 96.86 C ANISOU 2937 CD1 LEU A 284 12681 14484 9636 -891 -871 76 C ATOM 2938 CD2 LEU A 284 128.845 -17.099 130.990 1.00 97.55 C ANISOU 2938 CD2 LEU A 284 12622 14448 9994 -853 -892 327 C ATOM 2939 N MET A 285 133.319 -19.634 133.228 1.00 92.82 N ANISOU 2939 N MET A 285 12038 13665 9566 -537 -571 -119 N ATOM 2940 CA MET A 285 133.962 -20.641 134.063 1.00 93.49 C ANISOU 2940 CA MET A 285 12147 13629 9747 -418 -581 -221 C ATOM 2941 C MET A 285 134.400 -19.976 135.369 1.00 93.27 C ANISOU 2941 C MET A 285 12044 13579 9814 -364 -535 -129 C ATOM 2942 O MET A 285 134.130 -20.518 136.434 1.00 91.70 O ANISOU 2942 O MET A 285 11884 13240 9716 -317 -582 -94 O ATOM 2943 CB MET A 285 135.145 -21.286 133.310 1.00 98.37 C ANISOU 2943 CB MET A 285 12769 14329 10279 -312 -538 -438 C ATOM 2944 CG MET A 285 135.803 -22.444 134.053 1.00104.02 C ANISOU 2944 CG MET A 285 13534 14896 11095 -146 -587 -567 C ATOM 2945 SD MET A 285 134.768 -23.925 134.119 1.00110.33 S ANISOU 2945 SD MET A 285 14530 15421 11969 -169 -745 -600 S ATOM 2946 CE MET A 285 134.476 -24.019 135.871 1.00105.77 C ANISOU 2946 CE MET A 285 13982 14657 11548 -152 -787 -425 C ATOM 2947 N ALA A 286 135.004 -18.769 135.273 1.00 88.67 N ANISOU 2947 N ALA A 286 11370 13130 9188 -392 -453 -81 N ATOM 2948 CA ALA A 286 135.467 -17.948 136.392 1.00 87.13 C ANISOU 2948 CA ALA A 286 11103 12932 9069 -360 -417 -12 C ATOM 2949 C ALA A 286 134.323 -17.571 137.331 1.00 91.31 C ANISOU 2949 C ALA A 286 11654 13360 9680 -388 -465 138 C ATOM 2950 O ALA A 286 134.487 -17.713 138.542 1.00 91.59 O ANISOU 2950 O ALA A 286 11680 13331 9788 -319 -473 157 O ATOM 2951 CB ALA A 286 136.161 -16.696 135.881 1.00 87.80 C ANISOU 2951 CB ALA A 286 11113 13162 9085 -435 -333 13 C ATOM 2952 N ILE A 287 133.167 -17.123 136.785 1.00 87.64 N ANISOU 2952 N ILE A 287 11208 12902 9190 -477 -500 234 N ATOM 2953 CA ILE A 287 131.968 -16.762 137.552 1.00 86.66 C ANISOU 2953 CA ILE A 287 11066 12726 9134 -494 -538 353 C ATOM 2954 C ILE A 287 131.610 -17.916 138.492 1.00 90.18 C ANISOU 2954 C ILE A 287 11546 13072 9648 -470 -564 347 C ATOM 2955 O ILE A 287 131.528 -17.696 139.698 1.00 89.81 O ANISOU 2955 O ILE A 287 11479 12996 9650 -426 -545 400 O ATOM 2956 CB ILE A 287 130.769 -16.386 136.627 1.00 90.37 C ANISOU 2956 CB ILE A 287 11531 13240 9564 -573 -597 423 C ATOM 2957 CG1 ILE A 287 131.001 -15.044 135.918 1.00 91.28 C ANISOU 2957 CG1 ILE A 287 11650 13422 9611 -595 -587 480 C ATOM 2958 CG2 ILE A 287 129.431 -16.378 137.393 1.00 90.87 C ANISOU 2958 CG2 ILE A 287 11538 13284 9705 -581 -636 508 C ATOM 2959 CD1 ILE A 287 130.141 -14.813 134.649 1.00 99.28 C ANISOU 2959 CD1 ILE A 287 12694 14496 10532 -661 -666 526 C ATOM 2960 N MET A 288 131.447 -19.143 137.937 1.00 86.77 N ANISOU 2960 N MET A 288 11186 12578 9205 -503 -613 280 N ATOM 2961 CA MET A 288 131.085 -20.364 138.666 1.00 86.99 C ANISOU 2961 CA MET A 288 11293 12469 9291 -516 -657 287 C ATOM 2962 C MET A 288 132.055 -20.691 139.818 1.00 90.29 C ANISOU 2962 C MET A 288 11752 12813 9742 -395 -642 271 C ATOM 2963 O MET A 288 131.604 -21.105 140.884 1.00 90.80 O ANISOU 2963 O MET A 288 11859 12800 9841 -412 -653 359 O ATOM 2964 CB MET A 288 130.946 -21.563 137.711 1.00 90.70 C ANISOU 2964 CB MET A 288 11863 12856 9742 -563 -731 184 C ATOM 2965 CG MET A 288 129.769 -21.461 136.752 1.00 95.12 C ANISOU 2965 CG MET A 288 12393 13479 10271 -700 -781 207 C ATOM 2966 SD MET A 288 129.516 -22.955 135.748 1.00101.23 S ANISOU 2966 SD MET A 288 13307 14127 11030 -776 -892 67 S ATOM 2967 CE MET A 288 130.803 -22.750 134.550 1.00 98.04 C ANISOU 2967 CE MET A 288 12923 13829 10498 -654 -855 -109 C ATOM 2968 N CYS A 289 133.369 -20.486 139.610 1.00 86.16 N ANISOU 2968 N CYS A 289 11206 12337 9196 -281 -616 162 N ATOM 2969 CA CYS A 289 134.400 -20.732 140.617 1.00 86.62 C ANISOU 2969 CA CYS A 289 11277 12353 9280 -143 -625 125 C ATOM 2970 C CYS A 289 134.344 -19.697 141.749 1.00 89.02 C ANISOU 2970 C CYS A 289 11512 12716 9594 -132 -585 222 C ATOM 2971 O CYS A 289 134.350 -20.079 142.921 1.00 88.42 O ANISOU 2971 O CYS A 289 11492 12570 9532 -77 -614 274 O ATOM 2972 CB CYS A 289 135.785 -20.785 139.977 1.00 87.95 C ANISOU 2972 CB CYS A 289 11392 12603 9423 -29 -608 -43 C ATOM 2973 SG CYS A 289 136.094 -22.268 138.988 1.00 93.76 S ANISOU 2973 SG CYS A 289 12238 13241 10146 44 -676 -213 S ATOM 2974 N VAL A 290 134.297 -18.395 141.390 1.00 84.29 N ANISOU 2974 N VAL A 290 10814 12234 8979 -182 -528 244 N ATOM 2975 CA VAL A 290 134.261 -17.270 142.327 1.00 83.16 C ANISOU 2975 CA VAL A 290 10615 12136 8848 -167 -500 304 C ATOM 2976 C VAL A 290 132.987 -17.299 143.174 1.00 88.06 C ANISOU 2976 C VAL A 290 11258 12725 9476 -201 -500 419 C ATOM 2977 O VAL A 290 133.066 -17.204 144.396 1.00 87.77 O ANISOU 2977 O VAL A 290 11235 12682 9431 -143 -497 448 O ATOM 2978 CB VAL A 290 134.468 -15.902 141.615 1.00 86.08 C ANISOU 2978 CB VAL A 290 10912 12592 9204 -223 -460 303 C ATOM 2979 CG1 VAL A 290 134.308 -14.734 142.587 1.00 85.31 C ANISOU 2979 CG1 VAL A 290 10785 12499 9130 -202 -452 351 C ATOM 2980 CG2 VAL A 290 135.829 -15.837 140.921 1.00 86.30 C ANISOU 2980 CG2 VAL A 290 10887 12695 9207 -214 -431 192 C ATOM 2981 N LEU A 291 131.830 -17.462 142.527 1.00 86.14 N ANISOU 2981 N LEU A 291 11007 12487 9237 -296 -503 475 N ATOM 2982 CA LEU A 291 130.519 -17.480 143.173 1.00 86.86 C ANISOU 2982 CA LEU A 291 11070 12600 9334 -350 -487 573 C ATOM 2983 C LEU A 291 130.383 -18.619 144.193 1.00 93.58 C ANISOU 2983 C LEU A 291 12005 13377 10172 -367 -492 625 C ATOM 2984 O LEU A 291 129.924 -18.376 145.308 1.00 93.79 O ANISOU 2984 O LEU A 291 12012 13453 10171 -359 -449 692 O ATOM 2985 CB LEU A 291 129.410 -17.516 142.096 1.00 87.12 C ANISOU 2985 CB LEU A 291 11053 12670 9377 -454 -512 600 C ATOM 2986 CG LEU A 291 128.019 -16.990 142.449 1.00 91.88 C ANISOU 2986 CG LEU A 291 11544 13371 9994 -492 -493 673 C ATOM 2987 CD1 LEU A 291 128.043 -15.548 142.902 1.00 91.21 C ANISOU 2987 CD1 LEU A 291 11393 13350 9913 -383 -470 670 C ATOM 2988 CD2 LEU A 291 127.102 -17.103 141.268 1.00 95.04 C ANISOU 2988 CD2 LEU A 291 11892 13814 10406 -588 -550 681 C ATOM 2989 N SER A 292 130.863 -19.825 143.849 1.00 91.78 N ANISOU 2989 N SER A 292 11891 13027 9954 -378 -547 591 N ATOM 2990 CA SER A 292 130.794 -20.999 144.727 1.00 93.16 C ANISOU 2990 CA SER A 292 12201 13079 10118 -401 -579 659 C ATOM 2991 C SER A 292 131.706 -20.952 145.961 1.00 96.07 C ANISOU 2991 C SER A 292 12628 13429 10443 -268 -587 670 C ATOM 2992 O SER A 292 131.303 -21.459 147.001 1.00 96.28 O ANISOU 2992 O SER A 292 12734 13428 10422 -308 -578 782 O ATOM 2993 CB SER A 292 131.049 -22.279 143.940 1.00 98.71 C ANISOU 2993 CB SER A 292 13036 13616 10854 -427 -664 600 C ATOM 2994 OG SER A 292 132.298 -22.224 143.272 1.00109.06 O ANISOU 2994 OG SER A 292 14345 14921 12172 -282 -696 453 O ATOM 2995 N VAL A 293 132.924 -20.393 145.861 1.00 91.39 N ANISOU 2995 N VAL A 293 11999 12869 9858 -124 -609 559 N ATOM 2996 CA VAL A 293 133.837 -20.334 147.019 1.00 91.32 C ANISOU 2996 CA VAL A 293 12029 12861 9807 12 -644 549 C ATOM 2997 C VAL A 293 133.404 -19.229 147.997 1.00 94.86 C ANISOU 2997 C VAL A 293 12404 13439 10201 9 -577 600 C ATOM 2998 O VAL A 293 133.481 -19.411 149.213 1.00 94.55 O ANISOU 2998 O VAL A 293 12437 13403 10086 58 -592 659 O ATOM 2999 CB VAL A 293 135.330 -20.242 146.597 1.00 94.70 C ANISOU 2999 CB VAL A 293 12410 13305 10267 158 -698 394 C ATOM 3000 CG1 VAL A 293 136.239 -19.892 147.770 1.00 94.62 C ANISOU 3000 CG1 VAL A 293 12388 13345 10217 292 -743 366 C ATOM 3001 CG2 VAL A 293 135.786 -21.545 145.964 1.00 95.76 C ANISOU 3001 CG2 VAL A 293 12649 13299 10436 218 -780 329 C ATOM 3002 N CYS A 294 132.915 -18.106 147.455 1.00 90.81 N ANISOU 3002 N CYS A 294 11764 13024 9716 -41 -514 577 N ATOM 3003 CA CYS A 294 132.478 -16.951 148.227 1.00 89.89 C ANISOU 3003 CA CYS A 294 11576 13015 9563 -19 -460 588 C ATOM 3004 C CYS A 294 131.146 -17.145 148.938 1.00 94.31 C ANISOU 3004 C CYS A 294 12132 13636 10064 -90 -393 696 C ATOM 3005 O CYS A 294 131.023 -16.720 150.086 1.00 95.18 O ANISOU 3005 O CYS A 294 12245 13826 10093 -35 -359 708 O ATOM 3006 CB CYS A 294 132.458 -15.704 147.351 1.00 89.06 C ANISOU 3006 CB CYS A 294 11367 12955 9517 -29 -442 524 C ATOM 3007 SG CYS A 294 134.085 -15.210 146.734 1.00 92.50 S ANISOU 3007 SG CYS A 294 11772 13379 9993 20 -486 400 S ATOM 3008 N TRP A 295 130.151 -17.767 148.272 1.00 90.22 N ANISOU 3008 N TRP A 295 11595 13107 9578 -218 -370 763 N ATOM 3009 CA TRP A 295 128.797 -17.897 148.811 1.00 90.60 C ANISOU 3009 CA TRP A 295 11583 13260 9580 -317 -290 857 C ATOM 3010 C TRP A 295 128.411 -19.253 149.436 1.00 96.96 C ANISOU 3010 C TRP A 295 12508 14008 10323 -444 -278 986 C ATOM 3011 O TRP A 295 127.439 -19.274 150.187 1.00 98.19 O ANISOU 3011 O TRP A 295 12610 14294 10404 -527 -187 1069 O ATOM 3012 CB TRP A 295 127.774 -17.515 147.740 1.00 88.75 C ANISOU 3012 CB TRP A 295 11208 13094 9419 -395 -275 847 C ATOM 3013 CG TRP A 295 127.447 -16.054 147.747 1.00 88.99 C ANISOU 3013 CG TRP A 295 11110 13237 9464 -286 -249 781 C ATOM 3014 CD1 TRP A 295 127.997 -15.083 146.963 1.00 90.79 C ANISOU 3014 CD1 TRP A 295 11324 13421 9749 -204 -301 703 C ATOM 3015 CD2 TRP A 295 126.527 -15.392 148.622 1.00 89.65 C ANISOU 3015 CD2 TRP A 295 11077 13486 9498 -240 -168 781 C ATOM 3016 NE1 TRP A 295 127.452 -13.858 147.274 1.00 90.50 N ANISOU 3016 NE1 TRP A 295 11197 13472 9719 -105 -281 661 N ATOM 3017 CE2 TRP A 295 126.543 -14.019 148.287 1.00 93.04 C ANISOU 3017 CE2 TRP A 295 11442 13932 9977 -106 -199 691 C ATOM 3018 CE3 TRP A 295 125.662 -15.830 149.640 1.00 92.39 C ANISOU 3018 CE3 TRP A 295 11369 13978 9756 -304 -68 848 C ATOM 3019 CZ2 TRP A 295 125.728 -13.082 148.932 1.00 93.24 C ANISOU 3019 CZ2 TRP A 295 11350 14099 9979 4 -148 639 C ATOM 3020 CZ3 TRP A 295 124.852 -14.901 150.275 1.00 94.75 C ANISOU 3020 CZ3 TRP A 295 11522 14466 10014 -208 9 794 C ATOM 3021 CH2 TRP A 295 124.887 -13.546 149.919 1.00 94.78 C ANISOU 3021 CH2 TRP A 295 11463 14467 10082 -37 -39 679 C ATOM 3022 N SER A 296 129.123 -20.364 149.147 1.00 94.06 N ANISOU 3022 N SER A 296 12305 13454 9982 -461 -368 1003 N ATOM 3023 CA SER A 296 128.773 -21.670 149.735 1.00 95.69 C ANISOU 3023 CA SER A 296 12674 13550 10135 -592 -382 1144 C ATOM 3024 C SER A 296 128.963 -21.760 151.260 1.00100.98 C ANISOU 3024 C SER A 296 13448 14264 10655 -550 -351 1242 C ATOM 3025 O SER A 296 128.045 -22.267 151.907 1.00102.88 O ANISOU 3025 O SER A 296 13722 14557 10812 -719 -276 1387 O ATOM 3026 CB SER A 296 129.502 -22.822 149.049 1.00 99.45 C ANISOU 3026 CB SER A 296 13326 13779 10681 -584 -512 1119 C ATOM 3027 OG SER A 296 129.131 -22.929 147.686 1.00108.14 O ANISOU 3027 OG SER A 296 14354 14850 11884 -664 -534 1044 O ATOM 3028 N PRO A 297 130.093 -21.300 151.874 1.00 96.31 N ANISOU 3028 N PRO A 297 12906 13675 10013 -351 -406 1173 N ATOM 3029 CA PRO A 297 130.241 -21.446 153.333 1.00 97.35 C ANISOU 3029 CA PRO A 297 13157 13859 9973 -314 -393 1272 C ATOM 3030 C PRO A 297 129.114 -20.843 154.158 1.00101.13 C ANISOU 3030 C PRO A 297 13525 14575 10324 -407 -232 1337 C ATOM 3031 O PRO A 297 128.617 -21.536 155.034 1.00102.60 O ANISOU 3031 O PRO A 297 13828 14786 10369 -530 -182 1499 O ATOM 3032 CB PRO A 297 131.594 -20.798 153.628 1.00 98.22 C ANISOU 3032 CB PRO A 297 13267 13977 10077 -82 -485 1134 C ATOM 3033 CG PRO A 297 132.333 -20.890 152.352 1.00101.47 C ANISOU 3033 CG PRO A 297 13633 14267 10652 -21 -569 1009 C ATOM 3034 CD PRO A 297 131.301 -20.682 151.293 1.00 96.25 C ANISOU 3034 CD PRO A 297 12846 13636 10087 -170 -486 1007 C ATOM 3035 N LEU A 298 128.664 -19.605 153.846 1.00 95.59 N ANISOU 3035 N LEU A 298 12605 14046 9669 -354 -152 1214 N ATOM 3036 CA LEU A 298 127.558 -18.970 154.573 1.00 95.69 C ANISOU 3036 CA LEU A 298 12476 14310 9572 -398 3 1230 C ATOM 3037 C LEU A 298 126.307 -19.840 154.493 1.00 99.99 C ANISOU 3037 C LEU A 298 12977 14919 10097 -648 104 1380 C ATOM 3038 O LEU A 298 125.780 -20.227 155.534 1.00101.16 O ANISOU 3038 O LEU A 298 13155 15209 10071 -751 212 1498 O ATOM 3039 CB LEU A 298 127.270 -17.545 154.046 1.00 94.14 C ANISOU 3039 CB LEU A 298 12069 14230 9469 -273 32 1059 C ATOM 3040 CG LEU A 298 126.152 -16.752 154.750 1.00 99.69 C ANISOU 3040 CG LEU A 298 12601 15202 10075 -249 178 1019 C ATOM 3041 CD1 LEU A 298 126.640 -16.140 156.051 1.00100.53 C ANISOU 3041 CD1 LEU A 298 12775 15410 10011 -94 197 951 C ATOM 3042 CD2 LEU A 298 125.637 -15.652 153.862 1.00101.38 C ANISOU 3042 CD2 LEU A 298 12621 15466 10433 -164 175 887 C ATOM 3043 N LEU A 299 125.887 -20.197 153.258 1.00 95.71 N ANISOU 3043 N LEU A 299 12369 14277 9717 -763 64 1376 N ATOM 3044 CA LEU A 299 124.704 -21.015 152.975 1.00 96.95 C ANISOU 3044 CA LEU A 299 12461 14483 9892 -1030 133 1496 C ATOM 3045 C LEU A 299 124.748 -22.397 153.640 1.00104.36 C ANISOU 3045 C LEU A 299 13641 15280 10729 -1225 123 1697 C ATOM 3046 O LEU A 299 123.719 -22.854 154.145 1.00106.32 O ANISOU 3046 O LEU A 299 13836 15670 10891 -1459 245 1832 O ATOM 3047 CB LEU A 299 124.442 -21.125 151.464 1.00 95.55 C ANISOU 3047 CB LEU A 299 12190 14208 9905 -1090 53 1424 C ATOM 3048 CG LEU A 299 124.215 -19.819 150.672 1.00 98.24 C ANISOU 3048 CG LEU A 299 12305 14678 10342 -936 52 1263 C ATOM 3049 CD1 LEU A 299 124.051 -20.106 149.196 1.00 97.31 C ANISOU 3049 CD1 LEU A 299 12161 14438 10373 -999 -53 1213 C ATOM 3050 CD2 LEU A 299 122.998 -19.052 151.161 1.00102.39 C ANISOU 3050 CD2 LEU A 299 12573 15509 10821 -958 189 1248 C ATOM 3051 N ILE A 300 125.936 -23.036 153.692 1.00101.55 N ANISOU 3051 N ILE A 300 13550 14657 10378 -1127 -24 1721 N ATOM 3052 CA ILE A 300 126.091 -24.339 154.356 1.00104.10 C ANISOU 3052 CA ILE A 300 14160 14789 10604 -1273 -75 1921 C ATOM 3053 C ILE A 300 126.088 -24.158 155.885 1.00109.97 C ANISOU 3053 C ILE A 300 14983 15700 11099 -1253 18 2037 C ATOM 3054 O ILE A 300 125.442 -24.952 156.569 1.00112.52 O ANISOU 3054 O ILE A 300 15429 16034 11288 -1490 88 2246 O ATOM 3055 CB ILE A 300 127.297 -25.177 153.822 1.00106.69 C ANISOU 3055 CB ILE A 300 14741 14760 11035 -1148 -289 1890 C ATOM 3056 CG1 ILE A 300 127.255 -25.369 152.273 1.00105.72 C ANISOU 3056 CG1 ILE A 300 14540 14502 11126 -1175 -366 1759 C ATOM 3057 CG2 ILE A 300 127.455 -26.525 154.555 1.00110.02 C ANISOU 3057 CG2 ILE A 300 15504 14940 11359 -1270 -375 2107 C ATOM 3058 CD1 ILE A 300 125.955 -25.989 151.627 1.00115.93 C ANISOU 3058 CD1 ILE A 300 15771 15782 12493 -1496 -319 1837 C ATOM 3059 N MET A 301 126.762 -23.096 156.412 1.00105.48 N ANISOU 3059 N MET A 301 14345 15273 10459 -993 22 1902 N ATOM 3060 CA MET A 301 126.812 -22.772 157.852 1.00107.11 C ANISOU 3060 CA MET A 301 14616 15671 10408 -938 102 1968 C ATOM 3061 C MET A 301 125.406 -22.547 158.403 1.00113.01 C ANISOU 3061 C MET A 301 15180 16741 11018 -1139 336 2043 C ATOM 3062 O MET A 301 125.104 -23.016 159.502 1.00115.52 O ANISOU 3062 O MET A 301 15627 17169 11098 -1265 426 2216 O ATOM 3063 CB MET A 301 127.668 -21.517 158.139 1.00107.74 C ANISOU 3063 CB MET A 301 14616 15851 10471 -635 55 1759 C ATOM 3064 CG MET A 301 129.158 -21.768 158.187 1.00111.35 C ANISOU 3064 CG MET A 301 15275 16082 10950 -436 -155 1721 C ATOM 3065 SD MET A 301 129.687 -22.768 159.592 1.00119.97 S ANISOU 3065 SD MET A 301 16706 17115 11763 -437 -234 1936 S ATOM 3066 CE MET A 301 129.706 -21.530 160.912 1.00117.22 C ANISOU 3066 CE MET A 301 16255 17109 11173 -280 -136 1818 C ATOM 3067 N MET A 302 124.550 -21.838 157.633 1.00108.25 N ANISOU 3067 N MET A 302 14272 16303 10555 -1166 432 1913 N ATOM 3068 CA MET A 302 123.170 -21.532 158.012 1.00110.00 C ANISOU 3068 CA MET A 302 14245 16870 10680 -1325 653 1937 C ATOM 3069 C MET A 302 122.295 -22.783 158.111 1.00116.97 C ANISOU 3069 C MET A 302 15187 17746 11509 -1704 735 2177 C ATOM 3070 O MET A 302 121.549 -22.923 159.084 1.00119.51 O ANISOU 3070 O MET A 302 15465 18332 11612 -1868 919 2298 O ATOM 3071 CB MET A 302 122.561 -20.473 157.091 1.00110.63 C ANISOU 3071 CB MET A 302 13995 17098 10943 -1217 686 1730 C ATOM 3072 CG MET A 302 123.107 -19.087 157.351 1.00112.77 C ANISOU 3072 CG MET A 302 14181 17469 11196 -892 672 1514 C ATOM 3073 SD MET A 302 122.401 -17.844 156.253 1.00115.75 S ANISOU 3073 SD MET A 302 14227 17962 11790 -749 674 1295 S ATOM 3074 CE MET A 302 120.906 -17.454 157.141 1.00115.77 C ANISOU 3074 CE MET A 302 13937 18423 11626 -806 922 1272 C ATOM 3075 N LEU A 303 122.433 -23.715 157.148 1.00113.28 N ANISOU 3075 N LEU A 303 14840 16973 11227 -1851 598 2244 N ATOM 3076 CA LEU A 303 121.689 -24.977 157.145 1.00116.15 C ANISOU 3076 CA LEU A 303 15306 17250 11575 -2238 634 2469 C ATOM 3077 C LEU A 303 122.118 -25.875 158.306 1.00123.24 C ANISOU 3077 C LEU A 303 16562 18020 12243 -2350 623 2717 C ATOM 3078 O LEU A 303 121.284 -26.604 158.846 1.00126.27 O ANISOU 3078 O LEU A 303 16989 18495 12495 -2693 750 2933 O ATOM 3079 CB LEU A 303 121.837 -25.714 155.804 1.00115.09 C ANISOU 3079 CB LEU A 303 15252 16781 11697 -2326 454 2442 C ATOM 3080 CG LEU A 303 121.140 -25.086 154.593 1.00118.21 C ANISOU 3080 CG LEU A 303 15310 17307 12296 -2322 464 2258 C ATOM 3081 CD1 LEU A 303 121.761 -25.574 153.314 1.00116.62 C ANISOU 3081 CD1 LEU A 303 15244 16759 12309 -2272 252 2173 C ATOM 3082 CD2 LEU A 303 119.647 -25.385 154.584 1.00123.40 C ANISOU 3082 CD2 LEU A 303 15724 18218 12945 -2678 620 2347 C ATOM 3083 N LYS A 304 123.410 -25.797 158.703 1.00119.07 N ANISOU 3083 N LYS A 304 16286 17296 11660 -2070 467 2689 N ATOM 3084 CA LYS A 304 123.973 -26.555 159.823 1.00121.73 C ANISOU 3084 CA LYS A 304 16988 17498 11766 -2102 410 2911 C ATOM 3085 C LYS A 304 123.447 -26.005 161.147 1.00129.19 C ANISOU 3085 C LYS A 304 17851 18843 12392 -2139 628 2981 C ATOM 3086 O LYS A 304 123.120 -26.788 162.039 1.00132.59 O ANISOU 3086 O LYS A 304 18503 19287 12587 -2374 694 3245 O ATOM 3087 CB LYS A 304 125.509 -26.529 159.797 1.00122.13 C ANISOU 3087 CB LYS A 304 17268 17271 11866 -1752 164 2816 C ATOM 3088 N MET A 305 123.335 -24.662 161.257 1.00124.83 N ANISOU 3088 N MET A 305 16994 18613 11823 -1914 740 2743 N ATOM 3089 CA MET A 305 122.823 -23.967 162.444 1.00127.09 C ANISOU 3089 CA MET A 305 17158 19318 11813 -1893 955 2734 C ATOM 3090 C MET A 305 121.337 -24.262 162.693 1.00134.90 C ANISOU 3090 C MET A 305 17933 20630 12691 -2255 1223 2866 C ATOM 3091 O MET A 305 120.935 -24.390 163.850 1.00137.63 O ANISOU 3091 O MET A 305 18328 21247 12716 -2382 1399 3005 O ATOM 3092 CB MET A 305 123.087 -22.458 162.355 1.00126.81 C ANISOU 3092 CB MET A 305 16868 19481 11833 -1538 969 2413 C ATOM 3093 CG MET A 305 124.508 -22.087 162.706 1.00128.80 C ANISOU 3093 CG MET A 305 17335 19562 12043 -1221 771 2314 C ATOM 3094 SD MET A 305 124.861 -20.333 162.479 1.00130.08 S ANISOU 3094 SD MET A 305 17230 19878 12315 -849 756 1939 S ATOM 3095 CE MET A 305 126.520 -20.274 163.078 1.00125.87 C ANISOU 3095 CE MET A 305 16991 19137 11696 -587 515 1896 C ATOM 3096 N ILE A 306 120.538 -24.389 161.609 1.00131.39 N ANISOU 3096 N ILE A 306 17246 20177 12498 -2427 1252 2819 N ATOM 3097 CA ILE A 306 119.108 -24.724 161.653 1.00134.69 C ANISOU 3097 CA ILE A 306 17409 20899 12867 -2798 1484 2925 C ATOM 3098 C ILE A 306 118.945 -26.164 162.165 1.00143.49 C ANISOU 3098 C ILE A 306 18847 21838 13834 -3212 1496 3285 C ATOM 3099 O ILE A 306 118.061 -26.422 162.981 1.00147.10 O ANISOU 3099 O ILE A 306 19220 22619 14054 -3512 1734 3450 O ATOM 3100 CB ILE A 306 118.432 -24.475 160.267 1.00135.94 C ANISOU 3100 CB ILE A 306 17235 21060 13355 -2835 1451 2757 C ATOM 3101 CG1 ILE A 306 118.274 -22.964 160.000 1.00133.85 C ANISOU 3101 CG1 ILE A 306 16623 21063 13170 -2468 1495 2436 C ATOM 3102 CG2 ILE A 306 117.076 -25.193 160.132 1.00140.24 C ANISOU 3102 CG2 ILE A 306 17566 21817 13904 -3293 1622 2903 C ATOM 3103 CD1 ILE A 306 118.233 -22.576 158.539 1.00137.81 C ANISOU 3103 CD1 ILE A 306 16950 21407 14006 -2345 1340 2250 C ATOM 3104 N PHE A 307 119.829 -27.079 161.715 1.00140.40 N ANISOU 3104 N PHE A 307 18838 20936 13573 -3217 1237 3402 N ATOM 3105 CA PHE A 307 119.859 -28.491 162.108 1.00144.42 C ANISOU 3105 CA PHE A 307 19744 21151 13980 -3564 1174 3742 C ATOM 3106 C PHE A 307 120.194 -28.628 163.611 1.00150.87 C ANISOU 3106 C PHE A 307 20835 22086 14400 -3565 1251 3953 C ATOM 3107 O PHE A 307 121.346 -28.424 164.014 1.00149.03 O ANISOU 3107 O PHE A 307 20858 21675 14092 -3234 1075 3917 O ATOM 3108 CB PHE A 307 120.869 -29.264 161.230 1.00144.70 C ANISOU 3108 CB PHE A 307 20108 20602 14268 -3450 846 3741 C ATOM 3109 CG PHE A 307 120.760 -30.772 161.273 1.00150.28 C ANISOU 3109 CG PHE A 307 21208 20920 14970 -3820 738 4053 C ATOM 3110 CD1 PHE A 307 121.463 -31.511 162.219 1.00156.07 C ANISOU 3110 CD1 PHE A 307 22412 21398 15489 -3812 617 4303 C ATOM 3111 CD2 PHE A 307 119.992 -31.456 160.338 1.00153.98 C ANISOU 3111 CD2 PHE A 307 21599 21249 15657 -4167 727 4088 C ATOM 3112 CE1 PHE A 307 121.367 -32.907 162.255 1.00160.81 C ANISOU 3112 CE1 PHE A 307 23419 21590 16094 -4149 493 4602 C ATOM 3113 CE2 PHE A 307 119.901 -32.853 160.370 1.00160.63 C ANISOU 3113 CE2 PHE A 307 22837 21687 16509 -4522 607 4370 C ATOM 3114 CZ PHE A 307 120.588 -33.568 161.330 1.00161.24 C ANISOU 3114 CZ PHE A 307 23401 21490 16375 -4510 490 4630 C ATOM 3115 N ASN A 308 119.169 -28.935 164.437 1.00151.35 N ANISOU 3115 N ASN A 308 20820 22492 14195 -3938 1521 4162 N ATOM 3116 CA ASN A 308 119.311 -29.092 165.891 1.00182.37 C ANISOU 3116 CA ASN A 308 24996 26603 17693 -4001 1637 4387 C ATOM 3117 C ASN A 308 118.295 -30.066 166.500 1.00211.68 C ANISOU 3117 C ASN A 308 28795 30456 21179 -4577 1850 4748 C ATOM 3118 O ASN A 308 117.114 -30.041 166.161 1.00172.81 O ANISOU 3118 O ASN A 308 23506 25815 16338 -4892 2064 4728 O ATOM 3119 CB ASN A 308 119.287 -27.735 166.619 1.00181.55 C ANISOU 3119 CB ASN A 308 24608 26996 17374 -3674 1815 4141 C ATOM 3120 CG ASN A 308 118.151 -26.815 166.236 1.00200.18 C ANISOU 3120 CG ASN A 308 26397 29839 19822 -3700 2075 3897 C ATOM 3121 OD1 ASN A 308 116.973 -27.092 166.485 1.00198.22 O ANISOU 3121 OD1 ASN A 308 25931 29937 19448 -4079 2342 4022 O ATOM 3122 ND2 ASN A 308 118.489 -25.667 165.668 1.00186.09 N ANISOU 3122 ND2 ASN A 308 24355 28105 18245 -3289 2002 3541 N ATOM 3123 N GLU A 320 136.612 -22.032 175.028 1.00183.20 N ANISOU 3123 N GLU A 320 27038 26639 15931 1226 -1654 2341 N ATOM 3124 CA GLU A 320 135.310 -21.744 174.429 1.00181.46 C ANISOU 3124 CA GLU A 320 26626 26528 15792 963 -1267 2359 C ATOM 3125 C GLU A 320 134.596 -23.023 174.001 1.00185.55 C ANISOU 3125 C GLU A 320 27321 26814 16367 700 -1163 2730 C ATOM 3126 O GLU A 320 135.240 -23.955 173.510 1.00185.13 O ANISOU 3126 O GLU A 320 27425 26407 16510 756 -1395 2867 O ATOM 3127 CB GLU A 320 135.453 -20.788 173.235 1.00178.33 C ANISOU 3127 CB GLU A 320 25825 26098 15835 1019 -1191 2014 C ATOM 3128 N LYS A 321 133.263 -23.058 174.183 1.00182.34 N ANISOU 3128 N LYS A 321 26876 26611 15793 414 -818 2874 N ATOM 3129 CA LYS A 321 132.418 -24.202 173.840 1.00182.88 C ANISOU 3129 CA LYS A 321 27093 26507 15888 94 -677 3225 C ATOM 3130 C LYS A 321 132.323 -24.448 172.329 1.00181.34 C ANISOU 3130 C LYS A 321 26699 25997 16206 34 -682 3159 C ATOM 3131 O LYS A 321 132.399 -25.604 171.906 1.00181.90 O ANISOU 3131 O LYS A 321 26995 25723 16396 -73 -803 3405 O ATOM 3132 CB LYS A 321 131.022 -24.058 174.465 1.00187.88 C ANISOU 3132 CB LYS A 321 27664 27517 16206 -202 -287 3349 C ATOM 3133 N GLN A 322 132.168 -23.376 171.520 1.00172.50 N ANISOU 3133 N GLN A 322 25185 24981 15377 108 -565 2829 N ATOM 3134 CA GLN A 322 132.052 -23.494 170.062 1.00168.07 C ANISOU 3134 CA GLN A 322 24418 24166 15275 55 -558 2744 C ATOM 3135 C GLN A 322 132.870 -22.454 169.283 1.00165.94 C ANISOU 3135 C GLN A 322 23867 23860 15324 316 -679 2372 C ATOM 3136 O GLN A 322 132.898 -21.274 169.646 1.00164.90 O ANISOU 3136 O GLN A 322 23553 23983 15118 441 -616 2124 O ATOM 3137 CB GLN A 322 130.576 -23.495 169.602 1.00169.24 C ANISOU 3137 CB GLN A 322 24369 24454 15481 -257 -224 2818 C ATOM 3138 CG GLN A 322 129.765 -22.246 169.962 1.00183.41 C ANISOU 3138 CG GLN A 322 25864 26675 17149 -253 46 2600 C ATOM 3139 CD GLN A 322 128.358 -22.313 169.427 1.00202.54 C ANISOU 3139 CD GLN A 322 28061 29238 19659 -539 345 2664 C ATOM 3140 OE1 GLN A 322 128.111 -22.166 168.224 1.00194.43 O ANISOU 3140 OE1 GLN A 322 26811 28073 18992 -569 362 2552 O ATOM 3141 NE2 GLN A 322 127.397 -22.519 170.316 1.00198.99 N ANISOU 3141 NE2 GLN A 322 27647 29094 18866 -757 588 2837 N ATOM 3142 N LYS A 323 133.527 -22.914 168.200 1.00158.27 N ANISOU 3142 N LYS A 323 22872 22564 14699 385 -851 2335 N ATOM 3143 CA LYS A 323 134.343 -22.097 167.298 1.00153.50 C ANISOU 3143 CA LYS A 323 22012 21894 14417 585 -963 2022 C ATOM 3144 C LYS A 323 133.557 -21.756 166.014 1.00151.64 C ANISOU 3144 C LYS A 323 21500 21627 14490 440 -772 1925 C ATOM 3145 O LYS A 323 134.147 -21.349 165.007 1.00148.19 O ANISOU 3145 O LYS A 323 20877 21080 14348 548 -852 1722 O ATOM 3146 CB LYS A 323 135.667 -22.814 166.976 1.00156.01 C ANISOU 3146 CB LYS A 323 22467 21923 14885 782 -1281 2023 C ATOM 3147 N GLU A 324 132.215 -21.913 166.071 1.00147.02 N ANISOU 3147 N GLU A 324 20881 21162 13817 188 -520 2072 N ATOM 3148 CA GLU A 324 131.291 -21.620 164.974 1.00143.62 C ANISOU 3148 CA GLU A 324 20193 20743 13633 35 -336 2005 C ATOM 3149 C GLU A 324 131.167 -20.116 164.744 1.00143.07 C ANISOU 3149 C GLU A 324 19824 20883 13655 160 -241 1706 C ATOM 3150 O GLU A 324 130.994 -19.694 163.600 1.00140.36 O ANISOU 3150 O GLU A 324 19274 20464 13595 150 -210 1578 O ATOM 3151 CB GLU A 324 129.914 -22.250 165.231 1.00147.18 C ANISOU 3151 CB GLU A 324 20677 21307 13939 -274 -106 2244 C ATOM 3152 CG GLU A 324 129.863 -23.731 164.895 1.00158.71 C ANISOU 3152 CG GLU A 324 22389 22460 15455 -461 -195 2519 C ATOM 3153 CD GLU A 324 128.580 -24.437 165.286 1.00181.50 C ANISOU 3153 CD GLU A 324 25337 25452 18171 -814 19 2786 C ATOM 3154 OE1 GLU A 324 127.515 -24.103 164.718 1.00175.15 O ANISOU 3154 OE1 GLU A 324 24263 24802 17482 -986 224 2733 O ATOM 3155 OE2 GLU A 324 128.646 -25.350 166.139 1.00178.22 O ANISOU 3155 OE2 GLU A 324 25245 24964 17508 -929 -27 3059 O ATOM 3156 N CYS A 325 131.278 -19.314 165.827 1.00138.83 N ANISOU 3156 N CYS A 325 19289 20591 12870 283 -212 1595 N ATOM 3157 CA CYS A 325 131.217 -17.849 165.805 1.00136.36 C ANISOU 3157 CA CYS A 325 18746 20454 12613 424 -151 1300 C ATOM 3158 C CYS A 325 132.372 -17.241 165.004 1.00134.64 C ANISOU 3158 C CYS A 325 18437 20044 12674 593 -351 1086 C ATOM 3159 O CYS A 325 132.161 -16.270 164.271 1.00132.50 O ANISOU 3159 O CYS A 325 17956 19781 12608 627 -298 896 O ATOM 3160 CB CYS A 325 131.167 -17.288 167.223 1.00139.39 C ANISOU 3160 CB CYS A 325 19203 21121 12639 520 -103 1228 C ATOM 3161 SG CYS A 325 129.518 -17.310 167.973 1.00146.44 S ANISOU 3161 SG CYS A 325 20043 22372 13226 330 234 1358 S ATOM 3162 N ASN A 326 133.584 -17.819 165.142 1.00128.80 N ANISOU 3162 N ASN A 326 17856 19142 11940 696 -584 1121 N ATOM 3163 CA ASN A 326 134.785 -17.384 164.433 1.00125.35 C ANISOU 3163 CA ASN A 326 17323 18555 11749 837 -775 931 C ATOM 3164 C ASN A 326 134.681 -17.690 162.945 1.00123.62 C ANISOU 3164 C ASN A 326 16979 18138 11852 751 -750 942 C ATOM 3165 O ASN A 326 135.019 -16.823 162.142 1.00121.49 O ANISOU 3165 O ASN A 326 16526 17838 11796 791 -764 753 O ATOM 3166 CB ASN A 326 136.049 -18.014 165.035 1.00128.77 C ANISOU 3166 CB ASN A 326 17935 18908 12083 984 -1031 966 C ATOM 3167 CG ASN A 326 137.296 -17.822 164.195 1.00152.14 C ANISOU 3167 CG ASN A 326 20768 21727 15310 1106 -1219 793 C ATOM 3168 OD1 ASN A 326 137.787 -16.701 164.004 1.00145.07 O ANISOU 3168 OD1 ASN A 326 19700 20899 14523 1166 -1250 558 O ATOM 3169 ND2 ASN A 326 137.810 -18.913 163.642 1.00143.67 N ANISOU 3169 ND2 ASN A 326 19777 20457 14354 1136 -1344 901 N ATOM 3170 N PHE A 327 134.219 -18.911 162.575 1.00117.97 N ANISOU 3170 N PHE A 327 16379 17283 11160 621 -721 1164 N ATOM 3171 CA PHE A 327 134.069 -19.315 161.172 1.00114.39 C ANISOU 3171 CA PHE A 327 15834 16644 10984 534 -705 1175 C ATOM 3172 C PHE A 327 132.915 -18.598 160.476 1.00113.25 C ANISOU 3172 C PHE A 327 15482 16597 10951 405 -503 1122 C ATOM 3173 O PHE A 327 133.012 -18.348 159.278 1.00110.50 O ANISOU 3173 O PHE A 327 14998 16147 10839 390 -509 1034 O ATOM 3174 CB PHE A 327 133.972 -20.844 161.000 1.00117.48 C ANISOU 3174 CB PHE A 327 16440 16827 11371 440 -766 1406 C ATOM 3175 CG PHE A 327 134.080 -21.302 159.558 1.00117.33 C ANISOU 3175 CG PHE A 327 16350 16600 11629 397 -800 1373 C ATOM 3176 CD1 PHE A 327 135.314 -21.364 158.919 1.00119.25 C ANISOU 3176 CD1 PHE A 327 16559 16715 12035 567 -972 1231 C ATOM 3177 CD2 PHE A 327 132.944 -21.639 158.831 1.00119.03 C ANISOU 3177 CD2 PHE A 327 16515 16779 11934 186 -656 1464 C ATOM 3178 CE1 PHE A 327 135.408 -21.762 157.582 1.00118.82 C ANISOU 3178 CE1 PHE A 327 16439 16501 12207 535 -989 1181 C ATOM 3179 CE2 PHE A 327 133.040 -22.041 157.495 1.00120.41 C ANISOU 3179 CE2 PHE A 327 16635 16775 12341 151 -696 1416 C ATOM 3180 CZ PHE A 327 134.272 -22.102 156.880 1.00117.51 C ANISOU 3180 CZ PHE A 327 16252 16283 12112 330 -856 1273 C ATOM 3181 N PHE A 328 131.845 -18.246 161.215 1.00109.01 N ANISOU 3181 N PHE A 328 14912 16274 10234 328 -329 1166 N ATOM 3182 CA PHE A 328 130.708 -17.521 160.648 1.00107.08 C ANISOU 3182 CA PHE A 328 14450 16153 10084 244 -151 1099 C ATOM 3183 C PHE A 328 131.128 -16.137 160.152 1.00108.08 C ANISOU 3183 C PHE A 328 14409 16293 10364 390 -189 848 C ATOM 3184 O PHE A 328 130.601 -15.679 159.137 1.00107.06 O ANISOU 3184 O PHE A 328 14118 16143 10416 349 -127 788 O ATOM 3185 CB PHE A 328 129.531 -17.439 161.633 1.00110.99 C ANISOU 3185 CB PHE A 328 14922 16914 10333 153 48 1179 C ATOM 3186 CG PHE A 328 128.184 -17.227 160.980 1.00112.14 C ANISOU 3186 CG PHE A 328 14851 17179 10579 19 229 1184 C ATOM 3187 CD1 PHE A 328 127.628 -18.202 160.158 1.00115.23 C ANISOU 3187 CD1 PHE A 328 15235 17455 11091 -188 258 1346 C ATOM 3188 CD2 PHE A 328 127.455 -16.068 161.214 1.00114.37 C ANISOU 3188 CD2 PHE A 328 14935 17690 10829 109 355 1014 C ATOM 3189 CE1 PHE A 328 126.384 -18.004 159.550 1.00116.19 C ANISOU 3189 CE1 PHE A 328 15132 17710 11305 -313 406 1339 C ATOM 3190 CE2 PHE A 328 126.202 -15.880 160.619 1.00117.47 C ANISOU 3190 CE2 PHE A 328 15104 18215 11316 12 503 1008 C ATOM 3191 CZ PHE A 328 125.678 -16.846 159.788 1.00115.45 C ANISOU 3191 CZ PHE A 328 14820 17864 11180 -204 526 1173 C ATOM 3192 N LEU A 329 132.114 -15.503 160.827 1.00103.30 N ANISOU 3192 N LEU A 329 13856 15703 9689 549 -311 708 N ATOM 3193 CA LEU A 329 132.666 -14.207 160.428 1.00101.40 C ANISOU 3193 CA LEU A 329 13496 15439 9594 660 -376 478 C ATOM 3194 C LEU A 329 133.481 -14.387 159.152 1.00102.65 C ANISOU 3194 C LEU A 329 13603 15393 10006 637 -483 454 C ATOM 3195 O LEU A 329 133.365 -13.561 158.245 1.00101.40 O ANISOU 3195 O LEU A 329 13317 15184 10024 628 -466 348 O ATOM 3196 CB LEU A 329 133.518 -13.586 161.548 1.00102.92 C ANISOU 3196 CB LEU A 329 13766 15712 9627 803 -489 337 C ATOM 3197 CG LEU A 329 134.099 -12.188 161.286 1.00106.98 C ANISOU 3197 CG LEU A 329 14184 16191 10273 892 -569 91 C ATOM 3198 CD1 LEU A 329 133.012 -11.121 161.260 1.00107.37 C ANISOU 3198 CD1 LEU A 329 14138 16332 10324 922 -435 -24 C ATOM 3199 CD2 LEU A 329 135.140 -11.840 162.324 1.00111.06 C ANISOU 3199 CD2 LEU A 329 14788 16761 10648 1006 -728 -35 C ATOM 3200 N ILE A 330 134.259 -15.493 159.058 1.00 98.15 N ANISOU 3200 N ILE A 330 13139 14709 9444 634 -591 556 N ATOM 3201 CA ILE A 330 135.035 -15.835 157.858 1.00 95.90 C ANISOU 3201 CA ILE A 330 12803 14262 9374 624 -679 528 C ATOM 3202 C ILE A 330 134.056 -16.057 156.693 1.00 98.14 C ANISOU 3202 C ILE A 330 13010 14485 9795 487 -562 602 C ATOM 3203 O ILE A 330 134.289 -15.533 155.607 1.00 97.66 O ANISOU 3203 O ILE A 330 12835 14366 9907 468 -568 514 O ATOM 3204 CB ILE A 330 135.968 -17.074 158.065 1.00 99.79 C ANISOU 3204 CB ILE A 330 13435 14649 9832 690 -829 607 C ATOM 3205 CG1 ILE A 330 136.815 -16.995 159.369 1.00102.44 C ANISOU 3205 CG1 ILE A 330 13870 15069 9985 833 -964 565 C ATOM 3206 CG2 ILE A 330 136.851 -17.344 156.843 1.00 98.71 C ANISOU 3206 CG2 ILE A 330 13212 14386 9905 716 -914 526 C ATOM 3207 CD1 ILE A 330 137.819 -15.803 159.540 1.00111.66 C ANISOU 3207 CD1 ILE A 330 14910 16317 11199 931 -1064 334 C ATOM 3208 N ALA A 331 132.950 -16.796 156.937 1.00 93.95 N ANISOU 3208 N ALA A 331 12538 13984 9174 377 -459 765 N ATOM 3209 CA ALA A 331 131.920 -17.127 155.948 1.00 92.43 C ANISOU 3209 CA ALA A 331 12271 13756 9093 230 -361 842 C ATOM 3210 C ALA A 331 131.191 -15.908 155.373 1.00 95.08 C ANISOU 3210 C ALA A 331 12422 14184 9521 227 -272 735 C ATOM 3211 O ALA A 331 131.018 -15.832 154.154 1.00 93.41 O ANISOU 3211 O ALA A 331 12127 13897 9466 170 -274 718 O ATOM 3212 CB ALA A 331 130.929 -18.119 156.528 1.00 94.72 C ANISOU 3212 CB ALA A 331 12653 14090 9247 87 -270 1035 C ATOM 3213 N VAL A 332 130.771 -14.959 156.232 1.00 92.10 N ANISOU 3213 N VAL A 332 11993 13963 9038 304 -209 655 N ATOM 3214 CA VAL A 332 130.087 -13.749 155.765 1.00 91.22 C ANISOU 3214 CA VAL A 332 11729 13917 9014 345 -151 540 C ATOM 3215 C VAL A 332 131.076 -12.829 155.020 1.00 93.96 C ANISOU 3215 C VAL A 332 12055 14131 9516 414 -263 403 C ATOM 3216 O VAL A 332 130.685 -12.177 154.049 1.00 93.07 O ANISOU 3216 O VAL A 332 11853 13973 9538 399 -256 366 O ATOM 3217 CB VAL A 332 129.268 -13.022 156.873 1.00 96.59 C ANISOU 3217 CB VAL A 332 12359 14806 9535 426 -46 473 C ATOM 3218 CG1 VAL A 332 130.168 -12.386 157.936 1.00 96.80 C ANISOU 3218 CG1 VAL A 332 12479 14858 9443 566 -121 343 C ATOM 3219 CG2 VAL A 332 128.311 -11.990 156.273 1.00 96.24 C ANISOU 3219 CG2 VAL A 332 12149 14822 9596 477 13 378 C ATOM 3220 N ARG A 333 132.362 -12.813 155.455 1.00 90.06 N ANISOU 3220 N ARG A 333 11640 13581 8996 476 -372 338 N ATOM 3221 CA ARG A 333 133.418 -12.015 154.823 1.00 88.12 C ANISOU 3221 CA ARG A 333 11364 13233 8886 500 -471 215 C ATOM 3222 C ARG A 333 133.691 -12.496 153.411 1.00 89.99 C ANISOU 3222 C ARG A 333 11561 13362 9271 408 -486 268 C ATOM 3223 O ARG A 333 133.880 -11.663 152.521 1.00 89.47 O ANISOU 3223 O ARG A 333 11436 13235 9324 376 -500 210 O ATOM 3224 CB ARG A 333 134.698 -11.998 155.664 1.00 86.77 C ANISOU 3224 CB ARG A 333 11253 13070 8647 576 -587 128 C ATOM 3225 CG ARG A 333 134.676 -10.904 156.708 1.00 88.97 C ANISOU 3225 CG ARG A 333 11550 13424 8830 668 -606 -9 C ATOM 3226 CD ARG A 333 136.057 -10.623 157.234 1.00 90.54 C ANISOU 3226 CD ARG A 333 11773 13618 9009 718 -752 -130 C ATOM 3227 NE ARG A 333 136.020 -9.678 158.345 1.00 91.76 N ANISOU 3227 NE ARG A 333 11972 13845 9047 808 -786 -275 N ATOM 3228 CZ ARG A 333 136.802 -9.751 159.416 1.00101.74 C ANISOU 3228 CZ ARG A 333 13299 15188 10171 884 -895 -352 C ATOM 3229 NH1 ARG A 333 137.693 -10.730 159.531 1.00 84.25 N ANISOU 3229 NH1 ARG A 333 11105 12983 7925 897 -990 -288 N ATOM 3230 NH2 ARG A 333 136.707 -8.841 160.375 1.00 89.05 N ANISOU 3230 NH2 ARG A 333 11739 13647 8450 965 -927 -507 N ATOM 3231 N LEU A 334 133.651 -13.836 153.194 1.00 85.72 N ANISOU 3231 N LEU A 334 11069 12791 8711 360 -483 382 N ATOM 3232 CA LEU A 334 133.832 -14.440 151.871 1.00 84.11 C ANISOU 3232 CA LEU A 334 10841 12493 8623 283 -495 416 C ATOM 3233 C LEU A 334 132.657 -14.088 150.983 1.00 85.95 C ANISOU 3233 C LEU A 334 11002 12734 8922 200 -419 459 C ATOM 3234 O LEU A 334 132.886 -13.679 149.858 1.00 85.43 O ANISOU 3234 O LEU A 334 10887 12619 8954 160 -434 424 O ATOM 3235 CB LEU A 334 134.042 -15.957 151.940 1.00 84.81 C ANISOU 3235 CB LEU A 334 11032 12517 8676 270 -531 509 C ATOM 3236 CG LEU A 334 135.400 -16.418 152.480 1.00 90.36 C ANISOU 3236 CG LEU A 334 11796 13189 9347 383 -648 455 C ATOM 3237 CD1 LEU A 334 135.297 -17.796 153.086 1.00 92.04 C ANISOU 3237 CD1 LEU A 334 12170 13332 9470 399 -692 580 C ATOM 3238 CD2 LEU A 334 136.472 -16.395 151.397 1.00 91.99 C ANISOU 3238 CD2 LEU A 334 11922 13355 9675 403 -703 346 C ATOM 3239 N ALA A 335 131.411 -14.156 151.504 1.00 82.62 N ANISOU 3239 N ALA A 335 10559 12399 8435 178 -338 526 N ATOM 3240 CA ALA A 335 130.197 -13.777 150.760 1.00 82.40 C ANISOU 3240 CA ALA A 335 10428 12413 8466 123 -280 553 C ATOM 3241 C ALA A 335 130.233 -12.304 150.343 1.00 86.04 C ANISOU 3241 C ALA A 335 10832 12859 9001 197 -308 453 C ATOM 3242 O ALA A 335 129.770 -11.978 149.252 1.00 84.43 O ANISOU 3242 O ALA A 335 10575 12623 8881 159 -320 467 O ATOM 3243 CB ALA A 335 128.952 -14.063 151.584 1.00 84.41 C ANISOU 3243 CB ALA A 335 10635 12813 8624 96 -180 621 C ATOM 3244 N SER A 336 130.826 -11.430 151.195 1.00 83.51 N ANISOU 3244 N SER A 336 10544 12541 8644 297 -336 353 N ATOM 3245 CA SER A 336 130.985 -9.997 150.929 1.00 83.39 C ANISOU 3245 CA SER A 336 10520 12462 8702 359 -385 252 C ATOM 3246 C SER A 336 132.033 -9.762 149.840 1.00 87.96 C ANISOU 3246 C SER A 336 11125 12917 9379 278 -453 243 C ATOM 3247 O SER A 336 131.925 -8.782 149.105 1.00 88.49 O ANISOU 3247 O SER A 336 11196 12903 9524 268 -489 226 O ATOM 3248 CB SER A 336 131.382 -9.249 152.198 1.00 85.85 C ANISOU 3248 CB SER A 336 10876 12802 8940 471 -408 133 C ATOM 3249 OG SER A 336 130.374 -9.338 153.188 1.00 91.16 O ANISOU 3249 OG SER A 336 11517 13625 9495 550 -325 127 O ATOM 3250 N LEU A 337 133.046 -10.663 149.738 1.00 83.81 N ANISOU 3250 N LEU A 337 10619 12384 8841 226 -471 256 N ATOM 3251 CA LEU A 337 134.139 -10.592 148.750 1.00 82.15 C ANISOU 3251 CA LEU A 337 10399 12114 8700 145 -510 233 C ATOM 3252 C LEU A 337 133.618 -10.775 147.316 1.00 84.12 C ANISOU 3252 C LEU A 337 10629 12334 8998 58 -486 308 C ATOM 3253 O LEU A 337 134.159 -10.172 146.385 1.00 83.92 O ANISOU 3253 O LEU A 337 10601 12265 9018 -17 -504 297 O ATOM 3254 CB LEU A 337 135.240 -11.622 149.096 1.00 81.71 C ANISOU 3254 CB LEU A 337 10346 12089 8611 160 -539 205 C ATOM 3255 CG LEU A 337 136.479 -11.690 148.218 1.00 85.27 C ANISOU 3255 CG LEU A 337 10744 12537 9117 98 -564 148 C ATOM 3256 CD1 LEU A 337 137.379 -10.487 148.439 1.00 85.85 C ANISOU 3256 CD1 LEU A 337 10783 12609 9229 63 -607 51 C ATOM 3257 CD2 LEU A 337 137.244 -12.961 148.481 1.00 87.31 C ANISOU 3257 CD2 LEU A 337 11000 12827 9346 163 -599 124 C ATOM 3258 N ASN A 338 132.545 -11.565 147.145 1.00 79.29 N ANISOU 3258 N ASN A 338 10004 11756 8364 50 -449 386 N ATOM 3259 CA ASN A 338 131.934 -11.801 145.837 1.00 78.39 C ANISOU 3259 CA ASN A 338 9872 11631 8282 -28 -446 447 C ATOM 3260 C ASN A 338 131.466 -10.505 145.159 1.00 82.95 C ANISOU 3260 C ASN A 338 10446 12169 8902 -27 -477 459 C ATOM 3261 O ASN A 338 131.558 -10.393 143.933 1.00 83.66 O ANISOU 3261 O ASN A 338 10551 12233 9003 -104 -498 494 O ATOM 3262 CB ASN A 338 130.773 -12.779 145.942 1.00 77.40 C ANISOU 3262 CB ASN A 338 9720 11557 8133 -51 -414 518 C ATOM 3263 CG ASN A 338 130.207 -13.138 144.597 1.00 93.09 C ANISOU 3263 CG ASN A 338 11687 13538 10143 -138 -433 561 C ATOM 3264 OD1 ASN A 338 130.832 -13.860 143.810 1.00 83.48 O ANISOU 3264 OD1 ASN A 338 10509 12288 8922 -196 -447 548 O ATOM 3265 ND2 ASN A 338 129.071 -12.543 144.265 1.00 81.68 N ANISOU 3265 ND2 ASN A 338 10180 12135 8719 -128 -447 594 N ATOM 3266 N GLN A 339 130.964 -9.540 145.949 1.00 78.81 N ANISOU 3266 N GLN A 339 9918 11636 8389 70 -490 426 N ATOM 3267 CA GLN A 339 130.487 -8.249 145.443 1.00 78.77 C ANISOU 3267 CA GLN A 339 9941 11554 8435 110 -549 430 C ATOM 3268 C GLN A 339 131.649 -7.250 145.238 1.00 82.45 C ANISOU 3268 C GLN A 339 10497 11896 8935 54 -597 394 C ATOM 3269 O GLN A 339 131.437 -6.181 144.655 1.00 82.52 O ANISOU 3269 O GLN A 339 10576 11794 8985 52 -663 423 O ATOM 3270 CB GLN A 339 129.358 -7.681 146.324 1.00 80.64 C ANISOU 3270 CB GLN A 339 10132 11834 8674 265 -548 385 C ATOM 3271 CG GLN A 339 128.032 -8.453 146.243 1.00 80.71 C ANISOU 3271 CG GLN A 339 10019 11985 8663 285 -504 435 C ATOM 3272 CD GLN A 339 128.065 -9.818 146.899 1.00 92.76 C ANISOU 3272 CD GLN A 339 11504 13620 10122 214 -417 463 C ATOM 3273 OE1 GLN A 339 127.982 -10.856 146.236 1.00 83.85 O ANISOU 3273 OE1 GLN A 339 10363 12507 8990 99 -407 530 O ATOM 3274 NE2 GLN A 339 128.251 -9.853 148.206 1.00 85.86 N ANISOU 3274 NE2 GLN A 339 10633 12806 9184 279 -365 411 N ATOM 3275 N ILE A 340 132.876 -7.615 145.691 1.00 77.96 N ANISOU 3275 N ILE A 340 9926 11347 8349 0 -575 337 N ATOM 3276 CA ILE A 340 134.098 -6.830 145.476 1.00 78.67 C ANISOU 3276 CA ILE A 340 10060 11361 8471 -101 -608 297 C ATOM 3277 C ILE A 340 134.720 -7.309 144.144 1.00 82.84 C ANISOU 3277 C ILE A 340 10568 11927 8981 -249 -573 357 C ATOM 3278 O ILE A 340 135.206 -6.493 143.351 1.00 81.68 O ANISOU 3278 O ILE A 340 10472 11714 8848 -374 -590 393 O ATOM 3279 CB ILE A 340 135.099 -6.900 146.672 1.00 82.06 C ANISOU 3279 CB ILE A 340 10464 11826 8889 -73 -618 181 C ATOM 3280 CG1 ILE A 340 134.418 -6.488 148.004 1.00 83.38 C ANISOU 3280 CG1 ILE A 340 10661 11984 9037 84 -643 110 C ATOM 3281 CG2 ILE A 340 136.333 -6.027 146.405 1.00 83.77 C ANISOU 3281 CG2 ILE A 340 10695 11983 9152 -213 -656 132 C ATOM 3282 CD1 ILE A 340 135.197 -6.755 149.276 1.00 92.09 C ANISOU 3282 CD1 ILE A 340 11745 13164 10082 143 -656 11 C ATOM 3283 N LEU A 341 134.650 -8.641 143.890 1.00 79.89 N ANISOU 3283 N LEU A 341 10134 11656 8564 -239 -524 368 N ATOM 3284 CA LEU A 341 135.181 -9.271 142.680 1.00 79.13 C ANISOU 3284 CA LEU A 341 10013 11622 8430 -344 -483 390 C ATOM 3285 C LEU A 341 134.274 -9.092 141.468 1.00 83.56 C ANISOU 3285 C LEU A 341 10624 12164 8963 -393 -496 491 C ATOM 3286 O LEU A 341 134.793 -9.029 140.353 1.00 83.89 O ANISOU 3286 O LEU A 341 10679 12242 8953 -509 -470 517 O ATOM 3287 CB LEU A 341 135.539 -10.751 142.908 1.00 78.41 C ANISOU 3287 CB LEU A 341 9865 11615 8312 -293 -452 336 C ATOM 3288 CG LEU A 341 136.686 -11.027 143.913 1.00 82.84 C ANISOU 3288 CG LEU A 341 10373 12217 8886 -238 -461 233 C ATOM 3289 CD1 LEU A 341 136.627 -12.432 144.445 1.00 82.11 C ANISOU 3289 CD1 LEU A 341 10282 12146 8771 -136 -469 213 C ATOM 3290 CD2 LEU A 341 138.045 -10.781 143.288 1.00 86.06 C ANISOU 3290 CD2 LEU A 341 10702 12701 9293 -335 -435 162 C ATOM 3291 N ASP A 342 132.939 -8.967 141.676 1.00 80.46 N ANISOU 3291 N ASP A 342 10247 11737 8589 -305 -537 541 N ATOM 3292 CA ASP A 342 131.944 -8.777 140.600 1.00 81.15 C ANISOU 3292 CA ASP A 342 10366 11816 8651 -323 -583 631 C ATOM 3293 C ASP A 342 132.393 -7.785 139.488 1.00 88.60 C ANISOU 3293 C ASP A 342 11410 12697 9559 -435 -615 705 C ATOM 3294 O ASP A 342 132.451 -8.212 138.329 1.00 88.91 O ANISOU 3294 O ASP A 342 11466 12799 9515 -522 -604 750 O ATOM 3295 CB ASP A 342 130.554 -8.372 141.152 1.00 82.69 C ANISOU 3295 CB ASP A 342 10534 11992 8891 -189 -637 651 C ATOM 3296 CG ASP A 342 129.604 -9.471 141.586 1.00 90.06 C ANISOU 3296 CG ASP A 342 11367 13029 9822 -145 -608 641 C ATOM 3297 OD1 ASP A 342 129.903 -10.662 141.327 1.00 91.84 O ANISOU 3297 OD1 ASP A 342 11575 13305 10013 -217 -566 630 O ATOM 3298 OD2 ASP A 342 128.553 -9.144 142.169 1.00 92.32 O ANISOU 3298 OD2 ASP A 342 11591 13347 10140 -41 -627 640 O ATOM 3299 N PRO A 343 132.767 -6.500 139.776 1.00 86.58 N ANISOU 3299 N PRO A 343 11235 12314 9346 -453 -657 722 N ATOM 3300 CA PRO A 343 133.177 -5.605 138.674 1.00 88.06 C ANISOU 3300 CA PRO A 343 11547 12428 9483 -598 -688 827 C ATOM 3301 C PRO A 343 134.382 -6.109 137.878 1.00 91.89 C ANISOU 3301 C PRO A 343 11998 13038 9876 -782 -585 821 C ATOM 3302 O PRO A 343 134.467 -5.855 136.681 1.00 92.05 O ANISOU 3302 O PRO A 343 12099 13081 9795 -905 -583 921 O ATOM 3303 CB PRO A 343 133.468 -4.268 139.381 1.00 90.83 C ANISOU 3303 CB PRO A 343 11998 12594 9920 -595 -753 822 C ATOM 3304 CG PRO A 343 133.686 -4.613 140.805 1.00 93.87 C ANISOU 3304 CG PRO A 343 12281 13013 10372 -490 -719 680 C ATOM 3305 CD PRO A 343 132.794 -5.784 141.071 1.00 88.06 C ANISOU 3305 CD PRO A 343 11433 12408 9618 -356 -687 650 C ATOM 3306 N TRP A 344 135.297 -6.840 138.540 1.00 88.09 N ANISOU 3306 N TRP A 344 11395 12659 9418 -787 -503 698 N ATOM 3307 CA TRP A 344 136.496 -7.383 137.904 1.00 88.32 C ANISOU 3307 CA TRP A 344 11344 12844 9369 -921 -398 647 C ATOM 3308 C TRP A 344 136.168 -8.569 137.001 1.00 91.19 C ANISOU 3308 C TRP A 344 11676 13337 9636 -895 -360 632 C ATOM 3309 O TRP A 344 136.625 -8.603 135.861 1.00 90.83 O ANISOU 3309 O TRP A 344 11647 13395 9470 -1024 -301 661 O ATOM 3310 CB TRP A 344 137.571 -7.736 138.949 1.00 86.46 C ANISOU 3310 CB TRP A 344 10978 12674 9198 -893 -356 505 C ATOM 3311 CG TRP A 344 138.043 -6.541 139.723 1.00 88.33 C ANISOU 3311 CG TRP A 344 11247 12798 9517 -956 -399 498 C ATOM 3312 CD1 TRP A 344 137.563 -6.096 140.919 1.00 90.75 C ANISOU 3312 CD1 TRP A 344 11593 12977 9912 -831 -480 464 C ATOM 3313 CD2 TRP A 344 139.029 -5.588 139.308 1.00 89.94 C ANISOU 3313 CD2 TRP A 344 11460 13000 9711 -1179 -370 525 C ATOM 3314 NE1 TRP A 344 138.208 -4.940 141.289 1.00 91.41 N ANISOU 3314 NE1 TRP A 344 11721 12960 10052 -946 -518 449 N ATOM 3315 CE2 TRP A 344 139.114 -4.604 140.318 1.00 94.22 C ANISOU 3315 CE2 TRP A 344 12059 13382 10357 -1177 -454 496 C ATOM 3316 CE3 TRP A 344 139.866 -5.477 138.186 1.00 92.93 C ANISOU 3316 CE3 TRP A 344 11802 13514 9994 -1396 -272 566 C ATOM 3317 CZ2 TRP A 344 139.996 -3.522 140.238 1.00 95.50 C ANISOU 3317 CZ2 TRP A 344 12253 13482 10550 -1403 -460 512 C ATOM 3318 CZ3 TRP A 344 140.735 -4.399 138.106 1.00 96.51 C ANISOU 3318 CZ3 TRP A 344 12270 13933 10466 -1633 -257 599 C ATOM 3319 CH2 TRP A 344 140.799 -3.441 139.127 1.00 97.51 C ANISOU 3319 CH2 TRP A 344 12464 13869 10718 -1643 -358 574 C ATOM 3320 N VAL A 345 135.353 -9.517 137.501 1.00 86.82 N ANISOU 3320 N VAL A 345 11088 12777 9121 -746 -393 587 N ATOM 3321 CA VAL A 345 134.948 -10.727 136.784 1.00 86.19 C ANISOU 3321 CA VAL A 345 10993 12782 8972 -718 -382 552 C ATOM 3322 C VAL A 345 134.110 -10.385 135.553 1.00 91.47 C ANISOU 3322 C VAL A 345 11755 13455 9544 -779 -433 660 C ATOM 3323 O VAL A 345 134.422 -10.875 134.469 1.00 93.05 O ANISOU 3323 O VAL A 345 11967 13767 9620 -849 -393 636 O ATOM 3324 CB VAL A 345 134.242 -11.754 137.716 1.00 88.80 C ANISOU 3324 CB VAL A 345 11283 13075 9380 -582 -415 498 C ATOM 3325 CG1 VAL A 345 133.737 -12.961 136.935 1.00 89.18 C ANISOU 3325 CG1 VAL A 345 11342 13173 9371 -579 -425 459 C ATOM 3326 CG2 VAL A 345 135.167 -12.211 138.834 1.00 88.02 C ANISOU 3326 CG2 VAL A 345 11118 12982 9344 -513 -382 399 C ATOM 3327 N TYR A 346 133.079 -9.525 135.712 1.00 87.59 N ANISOU 3327 N TYR A 346 11328 12854 9098 -737 -529 768 N ATOM 3328 CA TYR A 346 132.160 -9.140 134.637 1.00 87.83 C ANISOU 3328 CA TYR A 346 11448 12880 9044 -760 -618 879 C ATOM 3329 C TYR A 346 132.665 -8.104 133.656 1.00 93.26 C ANISOU 3329 C TYR A 346 12265 13550 9619 -897 -623 998 C ATOM 3330 O TYR A 346 132.171 -8.102 132.528 1.00 94.53 O ANISOU 3330 O TYR A 346 12507 13758 9651 -938 -681 1077 O ATOM 3331 CB TYR A 346 130.816 -8.665 135.205 1.00 88.72 C ANISOU 3331 CB TYR A 346 11554 12900 9256 -623 -735 930 C ATOM 3332 CG TYR A 346 130.001 -9.790 135.797 1.00 89.61 C ANISOU 3332 CG TYR A 346 11547 13070 9429 -537 -737 852 C ATOM 3333 CD1 TYR A 346 129.184 -10.585 134.994 1.00 91.75 C ANISOU 3333 CD1 TYR A 346 11796 13423 9641 -555 -793 851 C ATOM 3334 CD2 TYR A 346 130.059 -10.079 137.157 1.00 88.77 C ANISOU 3334 CD2 TYR A 346 11361 12940 9428 -460 -688 783 C ATOM 3335 CE1 TYR A 346 128.459 -11.648 135.528 1.00 90.87 C ANISOU 3335 CE1 TYR A 346 11583 13354 9591 -523 -795 789 C ATOM 3336 CE2 TYR A 346 129.332 -11.133 137.703 1.00 89.06 C ANISOU 3336 CE2 TYR A 346 11307 13027 9504 -421 -681 738 C ATOM 3337 CZ TYR A 346 128.540 -11.921 136.883 1.00 96.89 C ANISOU 3337 CZ TYR A 346 12276 14084 10453 -465 -731 744 C ATOM 3338 OH TYR A 346 127.824 -12.958 137.427 1.00 99.21 O ANISOU 3338 OH TYR A 346 12488 14412 10793 -469 -725 710 O ATOM 3339 N LEU A 347 133.592 -7.199 134.049 1.00 89.62 N ANISOU 3339 N LEU A 347 11840 13019 9194 -986 -576 1024 N ATOM 3340 CA LEU A 347 133.989 -6.144 133.116 1.00 91.35 C ANISOU 3340 CA LEU A 347 12212 13195 9301 -1154 -587 1172 C ATOM 3341 C LEU A 347 135.468 -5.729 133.127 1.00 97.21 C ANISOU 3341 C LEU A 347 12931 13989 10015 -1353 -458 1157 C ATOM 3342 O LEU A 347 136.124 -5.842 132.093 1.00 97.59 O ANISOU 3342 O LEU A 347 12993 14190 9895 -1522 -363 1191 O ATOM 3343 CB LEU A 347 133.096 -4.908 133.364 1.00 92.15 C ANISOU 3343 CB LEU A 347 12464 13066 9484 -1073 -749 1301 C ATOM 3344 CG LEU A 347 133.184 -3.756 132.364 1.00 99.58 C ANISOU 3344 CG LEU A 347 13630 13897 10310 -1221 -820 1501 C ATOM 3345 CD1 LEU A 347 132.079 -3.842 131.331 1.00100.64 C ANISOU 3345 CD1 LEU A 347 13860 14054 10325 -1145 -950 1609 C ATOM 3346 CD2 LEU A 347 133.098 -2.428 133.078 1.00103.67 C ANISOU 3346 CD2 LEU A 347 14285 14141 10966 -1192 -928 1567 C ATOM 3347 N LEU A 348 135.959 -5.188 134.258 1.00 95.51 N ANISOU 3347 N LEU A 348 12678 13663 9950 -1345 -459 1104 N ATOM 3348 CA LEU A 348 137.285 -4.581 134.440 1.00 97.47 C ANISOU 3348 CA LEU A 348 12892 13930 10211 -1545 -371 1087 C ATOM 3349 C LEU A 348 138.509 -5.432 134.036 1.00103.39 C ANISOU 3349 C LEU A 348 13461 14959 10865 -1663 -198 971 C ATOM 3350 O LEU A 348 139.437 -4.854 133.470 1.00105.00 O ANISOU 3350 O LEU A 348 13671 15243 10981 -1906 -110 1031 O ATOM 3351 CB LEU A 348 137.472 -4.069 135.877 1.00 96.92 C ANISOU 3351 CB LEU A 348 12783 13714 10327 -1463 -425 997 C ATOM 3352 CG LEU A 348 136.441 -3.055 136.407 1.00101.83 C ANISOU 3352 CG LEU A 348 13576 14059 11055 -1344 -588 1073 C ATOM 3353 CD1 LEU A 348 136.677 -2.766 137.860 1.00101.38 C ANISOU 3353 CD1 LEU A 348 13456 13914 11149 -1241 -621 936 C ATOM 3354 CD2 LEU A 348 136.472 -1.760 135.632 1.00106.19 C ANISOU 3354 CD2 LEU A 348 14355 14424 11567 -1531 -657 1255 C ATOM 3355 N LEU A 349 138.545 -6.754 134.330 1.00 99.68 N ANISOU 3355 N LEU A 349 12830 14632 10411 -1499 -153 806 N ATOM 3356 CA LEU A 349 139.702 -7.593 133.969 1.00101.03 C ANISOU 3356 CA LEU A 349 12819 15064 10503 -1554 -6 662 C ATOM 3357 C LEU A 349 139.897 -7.749 132.461 1.00109.98 C ANISOU 3357 C LEU A 349 13990 16382 11415 -1699 91 715 C ATOM 3358 O LEU A 349 141.041 -7.758 132.001 1.00112.06 O ANISOU 3358 O LEU A 349 14132 16862 11585 -1857 235 658 O ATOM 3359 CB LEU A 349 139.681 -8.964 134.654 1.00 99.38 C ANISOU 3359 CB LEU A 349 12477 14916 10368 -1322 -12 479 C ATOM 3360 CG LEU A 349 140.386 -9.036 136.007 1.00103.68 C ANISOU 3360 CG LEU A 349 12887 15445 11063 -1240 -26 356 C ATOM 3361 CD1 LEU A 349 139.782 -10.116 136.874 1.00101.95 C ANISOU 3361 CD1 LEU A 349 12653 15153 10929 -997 -100 273 C ATOM 3362 CD2 LEU A 349 141.885 -9.244 135.844 1.00107.28 C ANISOU 3362 CD2 LEU A 349 13138 16140 11482 -1326 94 216 C ATOM 3363 N ARG A 350 138.788 -7.856 131.696 1.00107.39 N ANISOU 3363 N ARG A 350 13819 15994 10992 -1650 13 819 N ATOM 3364 CA ARG A 350 138.812 -7.972 130.240 1.00109.25 C ANISOU 3364 CA ARG A 350 14129 16396 10984 -1774 79 882 C ATOM 3365 C ARG A 350 139.233 -6.625 129.643 1.00116.28 C ANISOU 3365 C ARG A 350 15155 17263 11764 -2048 114 1087 C ATOM 3366 O ARG A 350 140.151 -6.588 128.826 1.00118.26 O ANISOU 3366 O ARG A 350 15361 17746 11827 -2245 269 1091 O ATOM 3367 CB ARG A 350 137.430 -8.384 129.721 1.00110.13 C ANISOU 3367 CB ARG A 350 14373 16431 11041 -1638 -55 936 C ATOM 3368 CG ARG A 350 137.453 -9.040 128.349 1.00128.99 C ANISOU 3368 CG ARG A 350 16796 19039 13175 -1694 7 906 C ATOM 3369 CD ARG A 350 136.120 -8.852 127.651 1.00148.47 C ANISOU 3369 CD ARG A 350 19449 21411 15553 -1651 -157 1048 C ATOM 3370 NE ARG A 350 135.694 -10.038 126.904 1.00162.75 N ANISOU 3370 NE ARG A 350 21241 23364 17231 -1564 -170 914 N ATOM 3371 CZ ARG A 350 134.971 -11.032 127.416 1.00176.90 C ANISOU 3371 CZ ARG A 350 22969 25088 19156 -1385 -258 784 C ATOM 3372 NH1 ARG A 350 134.616 -12.059 126.658 1.00165.43 N ANISOU 3372 NH1 ARG A 350 21527 23749 17579 -1337 -282 659 N ATOM 3373 NH2 ARG A 350 134.603 -11.008 128.692 1.00161.16 N ANISOU 3373 NH2 ARG A 350 20909 22914 17410 -1269 -322 775 N ATOM 3374 N LYS A 351 138.594 -5.522 130.096 1.00113.36 N ANISOU 3374 N LYS A 351 14952 16610 11510 -2063 -27 1252 N ATOM 3375 CA LYS A 351 138.860 -4.145 129.661 1.00115.98 C ANISOU 3375 CA LYS A 351 15473 16821 11772 -2316 -43 1474 C ATOM 3376 C LYS A 351 140.303 -3.684 129.931 1.00123.43 C ANISOU 3376 C LYS A 351 16288 17875 12734 -2573 112 1437 C ATOM 3377 O LYS A 351 140.821 -2.870 129.170 1.00125.80 O ANISOU 3377 O LYS A 351 16704 18206 12889 -2866 178 1606 O ATOM 3378 CB LYS A 351 137.845 -3.173 130.288 1.00117.53 C ANISOU 3378 CB LYS A 351 15869 16657 12130 -2205 -257 1606 C ATOM 3379 CG LYS A 351 137.320 -2.112 129.329 1.00131.25 C ANISOU 3379 CG LYS A 351 17909 18232 13728 -2335 -369 1877 C ATOM 3380 CD LYS A 351 136.042 -2.553 128.618 1.00139.50 C ANISOU 3380 CD LYS A 351 19051 19289 14663 -2145 -499 1934 C ATOM 3381 CE LYS A 351 135.575 -1.536 127.604 1.00153.94 C ANISOU 3381 CE LYS A 351 21192 20969 16329 -2258 -631 2211 C ATOM 3382 NZ LYS A 351 134.334 -1.976 126.910 1.00162.82 N ANISOU 3382 NZ LYS A 351 22388 22133 17344 -2066 -779 2251 N ATOM 3383 N ILE A 352 140.948 -4.204 130.994 1.00120.58 N ANISOU 3383 N ILE A 352 15689 17584 12543 -2476 162 1225 N ATOM 3384 CA ILE A 352 142.337 -3.868 131.325 1.00123.14 C ANISOU 3384 CA ILE A 352 15833 18051 12905 -2698 293 1150 C ATOM 3385 C ILE A 352 143.305 -4.863 130.658 1.00131.76 C ANISOU 3385 C ILE A 352 16669 19552 13843 -2742 502 983 C ATOM 3386 O ILE A 352 144.175 -4.433 129.899 1.00134.63 O ANISOU 3386 O ILE A 352 16978 20121 14053 -3038 658 1042 O ATOM 3387 CB ILE A 352 142.587 -3.694 132.859 1.00124.52 C ANISOU 3387 CB ILE A 352 15902 18070 13339 -2583 204 1018 C ATOM 3388 CG1 ILE A 352 141.787 -2.496 133.427 1.00124.81 C ANISOU 3388 CG1 ILE A 352 16201 17716 13507 -2576 15 1171 C ATOM 3389 CG2 ILE A 352 144.087 -3.539 133.173 1.00126.69 C ANISOU 3389 CG2 ILE A 352 15933 18552 13651 -2799 333 900 C ATOM 3390 CD1 ILE A 352 141.518 -2.538 134.957 1.00128.14 C ANISOU 3390 CD1 ILE A 352 16569 17967 14152 -2337 -108 1028 C ATOM 3391 N LEU A 353 143.144 -6.178 130.926 1.00128.79 N ANISOU 3391 N LEU A 353 16143 19292 13501 -2454 505 775 N ATOM 3392 CA LEU A 353 144.017 -7.231 130.395 1.00130.94 C ANISOU 3392 CA LEU A 353 16174 19928 13651 -2418 675 570 C ATOM 3393 C LEU A 353 143.552 -7.832 129.053 1.00139.34 C ANISOU 3393 C LEU A 353 17336 21146 14460 -2404 737 594 C ATOM 3394 O LEU A 353 143.600 -9.051 128.861 1.00138.10 O ANISOU 3394 O LEU A 353 17067 21145 14260 -2196 773 392 O ATOM 3395 CB LEU A 353 144.242 -8.330 131.445 1.00128.98 C ANISOU 3395 CB LEU A 353 15726 19701 13578 -2115 630 320 C ATOM 3396 CG LEU A 353 145.298 -8.024 132.492 1.00134.27 C ANISOU 3396 CG LEU A 353 16181 20421 14416 -2156 642 207 C ATOM 3397 CD1 LEU A 353 144.668 -7.525 133.782 1.00132.28 C ANISOU 3397 CD1 LEU A 353 16047 19837 14376 -2050 458 267 C ATOM 3398 CD2 LEU A 353 146.149 -9.244 132.763 1.00137.40 C ANISOU 3398 CD2 LEU A 353 16298 21067 14841 -1943 704 -72 C ATOM 3399 N GLY A2000 143.169 -6.958 128.124 1.00141.03 N ANISOU 3399 N GLY A2000 17772 21315 14499 -2629 741 835 N ATOM 3400 CA GLY A2000 142.747 -7.335 126.776 1.00143.79 C ANISOU 3400 CA GLY A2000 18247 21822 14566 -2658 789 888 C ATOM 3401 C GLY A2000 143.919 -7.584 125.843 1.00154.40 C ANISOU 3401 C GLY A2000 19411 23590 15664 -2844 1043 787 C ATOM 3402 O GLY A2000 143.798 -8.353 124.884 1.00155.05 O ANISOU 3402 O GLY A2000 19496 23891 15525 -2770 1113 688 O ATOM 3403 N ARG A2001 145.065 -6.921 126.121 1.00155.32 N ANISOU 3403 N ARG A2001 19359 23844 15813 -3093 1184 796 N ATOM 3404 CA ARG A2001 146.313 -7.046 125.363 1.00159.68 C ANISOU 3404 CA ARG A2001 19675 24847 16150 -3306 1453 691 C ATOM 3405 C ARG A2001 147.040 -8.389 125.622 1.00165.37 C ANISOU 3405 C ARG A2001 20054 25859 16919 -3029 1553 313 C ATOM 3406 O ARG A2001 147.334 -9.060 124.631 1.00166.89 O ANISOU 3406 O ARG A2001 20166 26384 16861 -3008 1708 180 O ATOM 3407 CB ARG A2001 147.242 -5.836 125.582 1.00163.27 C ANISOU 3407 CB ARG A2001 20053 25344 16638 -3699 1558 836 C ATOM 3408 CG ARG A2001 146.789 -4.568 124.866 1.00176.84 C ANISOU 3408 CG ARG A2001 22119 26880 18194 -4041 1526 1212 C ATOM 3409 N PRO A2002 147.298 -8.853 126.888 1.00161.64 N ANISOU 3409 N PRO A2002 19399 25273 16743 -2792 1454 127 N ATOM 3410 CA PRO A2002 147.974 -10.158 127.070 1.00162.36 C ANISOU 3410 CA PRO A2002 19199 25620 16870 -2503 1522 -225 C ATOM 3411 C PRO A2002 147.238 -11.365 126.478 1.00167.58 C ANISOU 3411 C PRO A2002 19975 26273 17425 -2208 1467 -366 C ATOM 3412 O PRO A2002 147.859 -12.414 126.291 1.00168.22 O ANISOU 3412 O PRO A2002 19847 26600 17468 -1994 1549 -660 O ATOM 3413 CB PRO A2002 148.123 -10.276 128.592 1.00161.60 C ANISOU 3413 CB PRO A2002 18985 25310 17105 -2317 1368 -317 C ATOM 3414 CG PRO A2002 148.049 -8.882 129.091 1.00165.60 C ANISOU 3414 CG PRO A2002 19611 25596 17714 -2602 1308 -63 C ATOM 3415 CD PRO A2002 147.042 -8.224 128.201 1.00161.07 C ANISOU 3415 CD PRO A2002 19382 24850 16969 -2766 1274 216 C ATOM 3416 N LEU A2003 145.928 -11.210 126.172 1.00164.24 N ANISOU 3416 N LEU A2003 19879 25568 16958 -2192 1318 -171 N ATOM 3417 CA LEU A2003 145.075 -12.227 125.547 1.00164.12 C ANISOU 3417 CA LEU A2003 20011 25513 16835 -1969 1239 -272 C ATOM 3418 C LEU A2003 145.601 -12.523 124.133 1.00172.58 C ANISOU 3418 C LEU A2003 21031 26987 17554 -2067 1444 -377 C ATOM 3419 O LEU A2003 145.707 -13.691 123.756 1.00172.86 O ANISOU 3419 O LEU A2003 21002 27161 17517 -1831 1464 -646 O ATOM 3420 CB LEU A2003 143.607 -11.728 125.490 1.00162.33 C ANISOU 3420 CB LEU A2003 20112 24936 16629 -1994 1037 -8 C ATOM 3421 CG LEU A2003 142.443 -12.753 125.359 1.00165.51 C ANISOU 3421 CG LEU A2003 20667 25163 17056 -1739 865 -93 C ATOM 3422 CD1 LEU A2003 142.278 -13.289 123.932 1.00167.88 C ANISOU 3422 CD1 LEU A2003 21057 25694 17036 -1754 930 -172 C ATOM 3423 CD2 LEU A2003 142.490 -13.851 126.432 1.00166.41 C ANISOU 3423 CD2 LEU A2003 20657 25146 17426 -1444 777 -320 C ATOM 3424 N GLU A2004 145.947 -11.462 123.370 1.00172.41 N ANISOU 3424 N GLU A2004 21051 27149 17308 -2418 1594 -168 N ATOM 3425 CA GLU A2004 146.500 -11.565 122.016 1.00176.32 C ANISOU 3425 CA GLU A2004 21501 28071 17422 -2570 1821 -230 C ATOM 3426 C GLU A2004 147.943 -12.086 122.055 1.00183.13 C ANISOU 3426 C GLU A2004 21961 29360 18259 -2529 2056 -538 C ATOM 3427 O GLU A2004 148.370 -12.768 121.120 1.00185.51 O ANISOU 3427 O GLU A2004 22161 30029 18296 -2468 2222 -753 O ATOM 3428 CB GLU A2004 146.436 -10.209 121.298 1.00179.94 C ANISOU 3428 CB GLU A2004 22153 28564 17653 -2987 1898 132 C ATOM 3429 N VAL A2005 148.680 -11.771 123.143 1.00179.16 N ANISOU 3429 N VAL A2005 21221 28823 18029 -2546 2061 -579 N ATOM 3430 CA VAL A2005 150.064 -12.196 123.366 1.00181.45 C ANISOU 3430 CA VAL A2005 21086 29508 18351 -2489 2248 -874 C ATOM 3431 C VAL A2005 150.145 -13.702 123.642 1.00184.75 C ANISOU 3431 C VAL A2005 21371 29946 18879 -2014 2170 -1254 C ATOM 3432 O VAL A2005 150.983 -14.383 123.047 1.00187.51 O ANISOU 3432 O VAL A2005 21460 30710 19077 -1898 2351 -1552 O ATOM 3433 CB VAL A2005 150.737 -11.373 124.487 1.00184.93 C ANISOU 3433 CB VAL A2005 21334 29879 19053 -2659 2233 -790 C ATOM 3434 N LEU A2006 149.264 -14.218 124.527 1.00177.46 N ANISOU 3434 N LEU A2006 20636 28578 18213 -1744 1901 -1245 N ATOM 3435 CA LEU A2006 149.198 -15.634 124.897 1.00206.48 C ANISOU 3435 CA LEU A2006 24265 32166 22023 -1308 1777 -1556 C ATOM 3436 C LEU A2006 148.593 -16.468 123.770 1.00239.15 C ANISOU 3436 C LEU A2006 28586 36362 25919 -1174 1783 -1685 C ATOM 3437 O LEU A2006 149.185 -17.458 123.346 1.00203.39 O ANISOU 3437 O LEU A2006 23908 32046 21325 -910 1842 -2026 O ATOM 3438 CB LEU A2006 148.380 -15.811 126.181 1.00202.41 C ANISOU 3438 CB LEU A2006 23919 31156 21833 -1134 1501 -1451 C TER 3439 LEU A2006 HETATM 3440 C01 J9P A2101 125.471 -11.713 153.693 1.00 79.89 C HETATM 3441 C02 J9P A2101 125.985 -11.098 152.400 1.00 81.54 C HETATM 3442 C03 J9P A2101 126.083 -9.576 152.453 1.00 83.17 C HETATM 3443 C04 J9P A2101 126.987 -9.075 151.320 1.00 84.74 C HETATM 3444 C05 J9P A2101 126.850 -7.623 150.827 1.00 86.06 C HETATM 3445 C06 J9P A2101 125.442 -7.371 150.307 1.00 85.95 C HETATM 3446 C07 J9P A2101 127.134 -6.541 151.880 1.00 87.54 C HETATM 3447 C08 J9P A2101 128.465 -6.717 152.613 1.00 89.65 C HETATM 3448 C09 J9P A2101 129.204 -5.656 152.853 1.00 91.43 C HETATM 3449 C10 J9P A2101 130.501 -5.766 153.576 1.00 91.60 C HETATM 3450 C11 J9P A2101 131.659 -4.895 152.739 1.00 91.86 C HETATM 3451 C12 J9P A2101 132.607 -4.536 153.685 1.00 93.67 C HETATM 3452 C13 J9P A2101 131.851 -4.551 155.066 1.00 94.50 C HETATM 3453 C15 J9P A2101 130.422 -5.107 154.822 1.00 93.56 C HETATM 3454 C16 J9P A2101 129.905 -6.024 155.987 1.00 93.62 C HETATM 3455 C17 J9P A2101 130.792 -7.234 156.286 1.00 94.68 C HETATM 3456 C18 J9P A2101 130.145 -8.236 157.242 1.00 96.40 C HETATM 3457 C19 J9P A2101 130.348 -7.882 158.715 1.00 97.49 C HETATM 3458 C20 J9P A2101 131.730 -8.225 159.263 1.00 99.28 C HETATM 3459 C21 J9P A2101 132.063 -7.351 160.469 1.00102.29 C HETATM 3460 C22 J9P A2101 133.553 -7.294 160.814 1.00105.28 C HETATM 3461 O14 J9P A2101 132.307 -4.199 156.109 1.00 94.35 O HETATM 3462 O23 J9P A2101 133.919 -7.460 162.009 1.00105.72 O HETATM 3463 O24 J9P A2101 134.416 -7.066 159.922 1.00107.18 O1- HETATM 3464 O25 J9P A2101 132.233 -5.696 151.788 1.00 93.13 O HETATM 3465 O26 J9P A2101 127.735 -7.454 149.753 1.00 86.46 O HETATM 3466 S SO4 A2102 115.614 -21.167 117.331 1.00130.88 S HETATM 3467 O1 SO4 A2102 114.691 -21.483 116.237 1.00132.17 O HETATM 3468 O2 SO4 A2102 116.862 -20.632 116.784 1.00130.31 O HETATM 3469 O3 SO4 A2102 115.904 -22.397 118.073 1.00131.11 O HETATM 3470 O4 SO4 A2102 114.993 -20.165 118.205 1.00129.50 O HETATM 3471 S SO4 A2103 111.393 -8.674 111.681 1.00175.38 S HETATM 3472 O1 SO4 A2103 111.074 -9.956 111.051 1.00175.29 O HETATM 3473 O2 SO4 A2103 112.496 -8.036 110.962 1.00175.03 O HETATM 3474 O3 SO4 A2103 111.782 -8.908 113.071 1.00175.57 O HETATM 3475 O4 SO4 A2103 110.219 -7.801 111.649 1.00175.35 O HETATM 3476 S SO4 A2104 131.672 -19.633 100.318 1.00219.52 S HETATM 3477 O1 SO4 A2104 130.980 -20.816 99.808 1.00219.30 O HETATM 3478 O2 SO4 A2104 132.081 -18.781 99.200 1.00219.50 O HETATM 3479 O3 SO4 A2104 132.854 -20.051 101.069 1.00219.75 O HETATM 3480 O4 SO4 A2104 130.778 -18.884 101.199 1.00219.35 O HETATM 3481 S SO4 A2105 123.423 2.515 135.986 1.00200.75 S HETATM 3482 O1 SO4 A2105 123.357 2.885 134.571 1.00200.63 O HETATM 3483 O2 SO4 A2105 122.415 1.493 136.274 1.00200.64 O HETATM 3484 O3 SO4 A2105 124.753 1.992 136.284 1.00200.88 O HETATM 3485 O4 SO4 A2105 123.171 3.691 136.818 1.00200.81 O HETATM 3486 C10 OLC A2106 142.037 -13.310 145.988 1.00131.64 C HETATM 3487 C9 OLC A2106 142.008 -13.376 144.651 1.00133.35 C HETATM 3488 C11 OLC A2106 141.902 -12.040 146.802 1.00130.45 C HETATM 3489 C8 OLC A2106 141.827 -12.195 143.715 1.00135.40 C HETATM 3490 C24 OLC A2106 137.751 -12.682 132.075 1.00148.44 C HETATM 3491 C12 OLC A2106 142.822 -12.113 148.017 1.00129.47 C HETATM 3492 C7 OLC A2106 141.912 -12.661 142.261 1.00137.27 C HETATM 3493 C13 OLC A2106 142.067 -12.549 149.267 1.00128.41 C HETATM 3494 C6 OLC A2106 140.562 -13.149 141.733 1.00138.89 C HETATM 3495 C14 OLC A2106 142.967 -12.481 150.493 1.00128.20 C HETATM 3496 C5 OLC A2106 140.565 -13.289 140.215 1.00140.41 C HETATM 3497 C4 OLC A2106 139.169 -13.610 139.685 1.00141.92 C HETATM 3498 C3 OLC A2106 139.221 -14.573 138.502 1.00143.72 C HETATM 3499 C2 OLC A2106 139.062 -13.829 137.176 1.00145.76 C HETATM 3500 C21 OLC A2106 139.052 -14.090 133.678 1.00148.58 C HETATM 3501 C1 OLC A2106 139.671 -14.582 136.007 1.00147.75 C HETATM 3502 C22 OLC A2106 138.022 -12.965 133.550 1.00148.65 C HETATM 3503 O19 OLC A2106 140.837 -14.965 136.028 1.00148.37 O HETATM 3504 O25 OLC A2106 136.796 -11.620 131.950 1.00148.29 O HETATM 3505 O23 OLC A2106 136.791 -13.302 134.202 1.00148.80 O HETATM 3506 O20 OLC A2106 138.898 -14.832 134.895 1.00148.36 O HETATM 3507 C1 OLA A2107 134.088 -25.496 161.892 1.00129.58 C HETATM 3508 O1 OLA A2107 134.810 -24.475 162.069 1.00129.87 O HETATM 3509 O2 OLA A2107 134.451 -26.612 162.353 1.00130.25 O HETATM 3510 C2 OLA A2107 132.773 -25.385 161.122 1.00127.98 C HETATM 3511 C3 OLA A2107 133.067 -25.288 159.626 1.00126.47 C HETATM 3512 C4 OLA A2107 132.136 -26.215 158.846 1.00124.97 C HETATM 3513 C5 OLA A2107 131.599 -25.477 157.622 1.00123.88 C HETATM 3514 C6 OLA A2107 132.228 -26.063 156.358 1.00123.79 C HETATM 3515 C7 OLA A2107 131.955 -25.156 155.155 1.00123.09 C HETATM 3516 C8 OLA A2107 131.196 -25.920 154.068 1.00122.01 C HETATM 3517 C9 OLA A2107 132.190 -26.580 153.108 1.00122.15 C HETATM 3518 C10 OLA A2107 131.938 -26.906 151.848 1.00123.12 C HETATM 3519 C11 OLA A2107 130.621 -26.667 151.099 1.00123.40 C HETATM 3520 C12 OLA A2107 130.801 -27.037 149.626 1.00123.39 C HETATM 3521 C13 OLA A2107 129.437 -27.245 148.966 1.00123.81 C HETATM 3522 C1 OLA A2108 148.123 -5.228 157.042 1.00171.50 C HETATM 3523 O1 OLA A2108 146.922 -5.599 157.137 1.00171.83 O HETATM 3524 O2 OLA A2108 148.780 -4.947 158.080 1.00172.03 O HETATM 3525 C2 OLA A2108 148.785 -5.123 155.668 1.00170.22 C HETATM 3526 C3 OLA A2108 148.414 -3.795 155.011 1.00168.74 C HETATM 3527 C4 OLA A2108 149.648 -3.192 154.344 1.00167.34 C HETATM 3528 C5 OLA A2108 149.624 -1.676 154.515 1.00166.17 C HETATM 3529 C6 OLA A2108 150.790 -1.245 155.399 1.00165.46 C HETATM 3530 C7 OLA A2108 150.257 -0.426 156.572 1.00165.07 C HETATM 3531 C1 OLA A2109 139.470 -20.224 137.285 1.00119.41 C HETATM 3532 O1 OLA A2109 140.348 -20.483 136.418 1.00118.73 O HETATM 3533 O2 OLA A2109 138.265 -20.125 136.930 1.00121.02 O HETATM 3534 C2 OLA A2109 139.857 -20.044 138.756 1.00118.08 C HETATM 3535 C3 OLA A2109 139.595 -18.611 139.228 1.00117.37 C HETATM 3536 C4 OLA A2109 140.255 -18.387 140.590 1.00116.98 C HETATM 3537 C5 OLA A2109 139.407 -17.439 141.442 1.00116.19 C HETATM 3538 C6 OLA A2109 139.898 -17.466 142.893 1.00114.75 C HETATM 3539 C7 OLA A2109 138.883 -16.779 143.807 1.00113.02 C HETATM 3540 C8 OLA A2109 139.513 -16.495 145.172 1.00111.94 C HETATM 3541 C9 OLA A2109 138.592 -17.024 146.279 1.00110.95 C HETATM 3542 C10 OLA A2109 138.869 -17.036 147.577 1.00110.27 C HETATM 3543 C11 OLA A2109 140.166 -16.521 148.209 1.00110.68 C HETATM 3544 C12 OLA A2109 140.167 -16.836 149.706 1.00110.63 C HETATM 3545 C13 OLA A2109 140.183 -15.540 150.518 1.00110.20 C HETATM 3546 C14 OLA A2109 141.194 -15.659 151.658 1.00109.97 C HETATM 3547 C1 OLA A2110 139.437 -13.512 157.302 1.00116.91 C HETATM 3548 O1 OLA A2110 140.554 -13.596 157.886 1.00117.75 O HETATM 3549 O2 OLA A2110 138.509 -12.844 157.846 1.00116.43 O HETATM 3550 C2 OLA A2110 139.229 -14.249 155.970 1.00115.71 C HETATM 3551 C3 OLA A2110 138.207 -13.564 155.055 1.00114.38 C HETATM 3552 C4 OLA A2110 138.880 -13.110 153.760 1.00112.61 C HETATM 3553 C5 OLA A2110 138.197 -11.844 153.246 1.00111.71 C HETATM 3554 C6 OLA A2110 139.124 -10.642 153.417 1.00111.43 C HETATM 3555 C7 OLA A2110 138.882 -9.641 152.288 1.00111.40 C HETATM 3556 C8 OLA A2110 140.216 -9.074 151.796 1.00111.20 C HETATM 3557 C9 OLA A2110 139.991 -7.678 151.203 1.00111.27 C HETATM 3558 C10 OLA A2110 140.127 -7.355 149.922 1.00111.21 C HETATM 3559 C11 OLA A2110 140.543 -8.314 148.802 1.00110.89 C HETATM 3560 C12 OLA A2110 140.238 -7.662 147.459 1.00111.66 C HETATM 3561 C13 OLA A2110 140.972 -8.402 146.342 1.00113.43 C HETATM 3562 C14 OLA A2110 141.008 -7.518 145.094 1.00114.60 C HETATM 3563 C15 OLA A2110 140.899 -8.362 143.824 1.00114.54 C HETATM 3564 C16 OLA A2110 141.348 -7.522 142.629 1.00114.83 C HETATM 3565 C17 OLA A2110 141.558 -8.421 141.411 1.00115.02 C HETATM 3566 C18 OLA A2110 142.927 -8.127 140.800 1.00114.64 C HETATM 3567 O HOH A2201 131.866 0.065 173.379 1.00113.65 O HETATM 3568 O HOH A2202 130.563 -6.500 149.651 1.00 60.59 O HETATM 3569 O HOH A2203 136.501 -4.095 143.345 1.00 66.69 O HETATM 3570 O HOH A2204 112.105 -20.440 116.795 1.00116.10 O HETATM 3571 O HOH A2205 140.920 -10.250 122.407 1.00119.00 O CONECT 625 1225 CONECT 1225 625 CONECT 3440 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3445 3446 3465 CONECT 3445 3444 CONECT 3446 3444 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 CONECT 3449 3448 3450 3453 CONECT 3450 3449 3451 3464 CONECT 3451 3450 3452 CONECT 3452 3451 3453 3461 CONECT 3453 3449 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3462 3463 CONECT 3461 3452 CONECT 3462 3460 CONECT 3463 3460 CONECT 3464 3450 CONECT 3465 3444 CONECT 3466 3467 3468 3469 3470 CONECT 3467 3466 CONECT 3468 3466 CONECT 3469 3466 CONECT 3470 3466 CONECT 3471 3472 3473 3474 3475 CONECT 3472 3471 CONECT 3473 3471 CONECT 3474 3471 CONECT 3475 3471 CONECT 3476 3477 3478 3479 3480 CONECT 3477 3476 CONECT 3478 3476 CONECT 3479 3476 CONECT 3480 3476 CONECT 3481 3482 3483 3484 3485 CONECT 3482 3481 CONECT 3483 3481 CONECT 3484 3481 CONECT 3485 3481 CONECT 3486 3487 3488 CONECT 3487 3486 3489 CONECT 3488 3486 3491 CONECT 3489 3487 3492 CONECT 3490 3502 3504 CONECT 3491 3488 3493 CONECT 3492 3489 3494 CONECT 3493 3491 3495 CONECT 3494 3492 3496 CONECT 3495 3493 CONECT 3496 3494 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3498 3501 CONECT 3500 3502 3506 CONECT 3501 3499 3503 3506 CONECT 3502 3490 3500 3505 CONECT 3503 3501 CONECT 3504 3490 CONECT 3505 3502 CONECT 3506 3500 3501 CONECT 3507 3508 3509 3510 CONECT 3508 3507 CONECT 3509 3507 CONECT 3510 3507 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 CONECT 3522 3523 3524 3525 CONECT 3523 3522 CONECT 3524 3522 CONECT 3525 3522 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 CONECT 3531 3532 3533 3534 CONECT 3532 3531 CONECT 3533 3531 CONECT 3534 3531 3535 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3538 CONECT 3538 3537 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 CONECT 3547 3548 3549 3550 CONECT 3548 3547 CONECT 3549 3547 CONECT 3550 3547 3551 CONECT 3551 3550 3552 CONECT 3552 3551 3553 CONECT 3553 3552 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 CONECT 3562 3561 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 MASTER 450 0 10 22 5 0 12 6 3548 1 129 42 END