HEADER SIGNALING PROTEIN 04-AUG-11 3VGA TITLE CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN ALLOSTERIC TITLE 2 INVERSE-AGONIST ANTIBODY AT 3.1 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 1-316; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN; COMPND 9 CHAIN: B; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN; COMPND 12 CHAIN: C SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A, ADORA2; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9K; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 16 ORGANISM_COMMON: MOUSE; SOURCE 17 ORGANISM_TAXID: 10090 KEYWDS 7 TRANSMEMBRANE RECEPTOR, SIGNAL TRANSDUCTION, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO,Y.NAKADA- AUTHOR 2 NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA,A.D.CAMERON, AUTHOR 3 T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA REVDAT 2 15-FEB-12 3VGA 1 JRNL REVDAT 1 01-FEB-12 3VGA 0 JRNL AUTH T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO, JRNL AUTH 2 Y.NAKADA-NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA, JRNL AUTH 3 A.D.CAMERON,T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA JRNL TITL G-PROTEIN-COUPLED RECEPTOR INACTIVATION BY AN ALLOSTERIC JRNL TITL 2 INVERSE-AGONIST ANTIBODY JRNL REF NATURE V. 482 237 2012 JRNL REFN ISSN 0028-0836 JRNL PMID 22286059 JRNL DOI 10.1038/NATURE10750 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4 REMARK 3 NUMBER OF REFLECTIONS : 17901 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130 REMARK 3 FREE R VALUE TEST SET COUNT : 968 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.9969 - 5.8866 0.85 2518 151 0.2252 0.2838 REMARK 3 2 5.8866 - 4.6922 0.90 2612 135 0.1722 0.2451 REMARK 3 3 4.6922 - 4.1049 0.86 2498 132 0.1564 0.2259 REMARK 3 4 4.1049 - 3.7323 0.90 2584 158 0.1779 0.2710 REMARK 3 5 3.7323 - 3.4662 0.88 2523 137 0.2033 0.2460 REMARK 3 6 3.4662 - 3.2628 0.89 2575 114 0.2224 0.2869 REMARK 3 7 3.2628 - 3.1000 0.90 2591 141 0.2614 0.3167 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 0.60 REMARK 3 SHRINKAGE RADIUS : 0.27 REMARK 3 K_SOL : 0.30 REMARK 3 B_SOL : 58.17 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.830 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -15.73960 REMARK 3 B22 (A**2) : 6.80060 REMARK 3 B33 (A**2) : 8.93910 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -9.55300 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 5768 REMARK 3 ANGLE : 1.278 7850 REMARK 3 CHIRALITY : 0.084 902 REMARK 3 PLANARITY : 0.006 980 REMARK 3 DIHEDRAL : 17.053 2007 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 62.7650 -8.8708 36.3356 REMARK 3 T TENSOR REMARK 3 T11: -0.4586 T22: 0.8223 REMARK 3 T33: -0.0638 T12: 0.0402 REMARK 3 T13: -0.2764 T23: -0.1037 REMARK 3 L TENSOR REMARK 3 L11: 0.9795 L22: 1.4776 REMARK 3 L33: 1.7749 L12: 0.0699 REMARK 3 L13: -0.6019 L23: 0.3411 REMARK 3 S TENSOR REMARK 3 S11: 0.0755 S12: -0.6853 S13: -0.0693 REMARK 3 S21: 0.5246 S22: 0.1228 S23: -0.6416 REMARK 3 S31: -0.0417 S32: 0.8520 S33: 0.0461 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 19.7508 1.4067 0.0609 REMARK 3 T TENSOR REMARK 3 T11: 0.3953 T22: 0.2013 REMARK 3 T33: 0.4645 T12: -0.0364 REMARK 3 T13: 0.0060 T23: 0.0775 REMARK 3 L TENSOR REMARK 3 L11: 4.9038 L22: 0.8705 REMARK 3 L33: 1.1396 L12: 0.7196 REMARK 3 L13: 1.6861 L23: 0.2871 REMARK 3 S TENSOR REMARK 3 S11: -0.2429 S12: 0.1178 S13: 0.6495 REMARK 3 S21: -0.0755 S22: -0.0260 S23: 0.0882 REMARK 3 S31: -0.2084 S32: 0.0898 S33: 0.2253 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'B' REMARK 3 ORIGIN FOR THE GROUP (A): 20.4190 -15.9471 -4.7868 REMARK 3 T TENSOR REMARK 3 T11: 0.3184 T22: 0.3262 REMARK 3 T33: 0.3417 T12: 0.0975 REMARK 3 T13: 0.0384 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 3.9493 L22: 1.3228 REMARK 3 L33: 2.8884 L12: 0.2629 REMARK 3 L13: 2.6339 L23: 0.5871 REMARK 3 S TENSOR REMARK 3 S11: 0.1956 S12: 0.7483 S13: -0.0005 REMARK 3 S21: -0.2767 S22: -0.0522 S23: 0.0071 REMARK 3 S31: 0.0717 S32: 0.4044 S33: -0.1589 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3VGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-11. REMARK 100 THE RCSB ID CODE IS RCSB095008. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18451 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 71.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.8 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.10900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : 0.63600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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 ENTRY 1VGA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1M MES, 0.2M MAGNESIUM REMARK 280 CHLORIDE, 0.5% OCTHYL THIOGLUCOSIDE , PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, 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 60.15650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.88300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.15650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.88300 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 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 231 LIES ON A SPECIAL POSITION. 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 MET A 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 MET A 4 REMARK 465 GLY A 5 REMARK 465 PRO A 149 REMARK 465 LYS A 150 REMARK 465 GLU A 151 REMARK 465 GLY A 152 REMARK 465 LYS A 153 REMARK 465 GLN A 154 REMARK 465 HIS A 155 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 HIS A 317 REMARK 465 HIS A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 CYS C 139 REMARK 465 GLY C 140 REMARK 465 ASP C 141 REMARK 465 THR C 142 REMARK 465 SER C 143 REMARK 465 PRO C 226 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 ARG A 220 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 212 O CG OD1 ND2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 GLY C 225 O REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 CB CYS A 259 SG CYS A 262 1.74 REMARK 500 O ILE B 29 O SER B 31 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -66.94 -107.33 REMARK 500 CYS A 146 -75.80 -91.82 REMARK 500 GLU A 161 66.70 39.13 REMARK 500 PHE A 182 -74.28 -97.37 REMARK 500 VAL A 186 -62.49 -128.54 REMARK 500 LEU A 216 149.82 72.33 REMARK 500 PRO A 260 43.66 -76.92 REMARK 500 ASP A 261 -61.07 -134.66 REMARK 500 PRO A 266 -172.50 -66.33 REMARK 500 SER A 305 -71.71 -117.90 REMARK 500 TYR B 30 -124.64 62.87 REMARK 500 SER B 32 9.31 98.46 REMARK 500 LEU B 47 -64.15 -108.49 REMARK 500 ALA B 51 -26.10 77.37 REMARK 500 SER B 67 166.32 179.98 REMARK 500 ARG B 77 73.91 45.00 REMARK 500 LYS B 169 -70.14 -99.03 REMARK 500 ASN B 190 -61.17 -90.48 REMARK 500 LYS C 43 -73.96 -130.27 REMARK 500 ALA C 92 -177.43 -173.36 REMARK 500 PRO C 137 -166.29 -68.26 REMARK 500 SER C 171 -70.30 -100.31 REMARK 500 SER C 183 -115.27 51.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMA A 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3VG9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN REMARK 900 ALLOSTERIC INVERSE-AGONIST ANTIBODY AT 2.7 A RESOLUTION DBREF 3VGA A 1 316 UNP P29274 AA2AR_HUMAN 1 316 DBREF 3VGA B 1 214 PDB 3VGA 3VGA 1 214 DBREF 3VGA C 1 226 PDB 3VGA 3VGA 1 226 SEQADV 3VGA GLN A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 3VGA HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 3VGA HIS A 326 UNP P29274 EXPRESSION TAG SEQRES 1 A 326 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU SEQRES 2 A 326 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU SEQRES 3 A 326 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN SEQRES 4 A 326 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP SEQRES 5 A 326 ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR SEQRES 6 A 326 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU SEQRES 7 A 326 PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER SEQRES 8 A 326 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE SEQRES 9 A 326 ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR SEQRES 10 A 326 GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL SEQRES 11 A 326 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP SEQRES 12 A 326 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS GLN HIS SER SEQRES 13 A 326 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU SEQRES 14 A 326 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE SEQRES 15 A 326 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY SEQRES 16 A 326 VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU SEQRES 17 A 326 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA SEQRES 18 A 326 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER SEQRES 19 A 326 LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU SEQRES 20 A 326 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO SEQRES 21 A 326 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA SEQRES 22 A 326 ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE SEQRES 23 A 326 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE SEQRES 24 A 326 ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU SEQRES 25 A 326 PRO PHE LYS ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 26 A 326 HIS SEQRES 1 B 214 ASP ILE VAL MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 214 GLU PHE ILE TYR SER SER LEU THR TRP TYR GLN GLN LYS SEQRES 4 B 214 GLN GLY GLY SER PRO GLN LEU LEU VAL TYR ALA ALA THR SEQRES 5 B 214 ASN LEU ALA ASP ALA VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN ARG LEU SEQRES 7 B 214 GLN PRO GLU ASP PHE GLY THR TYR TYR CYS GLN HIS PHE SEQRES 8 B 214 TYR GLY SER THR TRP ALA PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 B 214 PHE ASN ARG ASN GLU CYS SEQRES 1 C 226 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 C 226 PRO GLY SER SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 C 226 ASP SER PHE THR ALA TYR ASN MET ASN TRP VAL LYS GLN SEQRES 4 C 226 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASN ILE ASN SEQRES 5 C 226 PRO TYR TYR GLY SER THR ARG TYR ASN GLN LYS PHE LYS SEQRES 6 C 226 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 C 226 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 C 226 ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR TYR ASP SEQRES 9 C 226 GLY GLY SER VAL ARG TYR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 C 226 THR THR LEU THR VAL SER SER ALA LYS THR THR ALA PRO SEQRES 11 C 226 SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SER SEQRES 12 C 226 GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 13 C 226 PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER SEQRES 14 C 226 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 C 226 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR SEQRES 16 C 226 SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL SEQRES 17 C 226 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 C 226 GLU PRO ARG GLY PRO HET ZMA A 401 25 HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3, HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL FORMUL 4 ZMA C16 H15 N7 O2 FORMUL 5 HOH *14(H2 O) HELIX 1 1 SER A 6 ASN A 34 1 29 HELIX 2 2 SER A 35 GLN A 38 5 4 HELIX 3 3 ASN A 39 LEU A 58 1 20 HELIX 4 4 LEU A 58 ILE A 66 1 9 HELIX 5 5 ALA A 73 CYS A 82 1 10 HELIX 6 6 CYS A 82 ILE A 108 1 27 HELIX 7 7 ILE A 108 VAL A 116 1 9 HELIX 8 8 THR A 117 LEU A 137 1 21 HELIX 9 9 THR A 138 LEU A 141 5 4 HELIX 10 10 LEU A 167 VAL A 172 1 6 HELIX 11 11 PRO A 173 TYR A 179 1 7 HELIX 12 12 VAL A 186 SER A 213 1 28 HELIX 13 13 ALA A 221 PHE A 258 1 38 HELIX 14 14 PRO A 266 THR A 279 1 14 HELIX 15 15 VAL A 282 ILE A 292 1 11 HELIX 16 16 ILE A 292 VAL A 307 1 16 HELIX 17 17 GLN B 79 PHE B 83 5 5 HELIX 18 18 SER B 121 THR B 126 1 6 HELIX 19 19 LYS B 183 GLU B 187 1 5 HELIX 20 20 SER C 28 TYR C 32 5 5 HELIX 21 21 GLN C 62 LYS C 65 5 4 HELIX 22 22 THR C 87 SER C 91 5 5 HELIX 23 23 SER C 167 SER C 169 5 3 HELIX 24 24 PRO C 211 SER C 214 5 4 SHEET 1 A 2 CYS A 71 ALA A 72 0 SHEET 2 A 2 VAL A 164 ALA A 165 -1 O VAL A 164 N ALA A 72 SHEET 1 B 4 MET B 4 SER B 7 0 SHEET 2 B 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 B 4 GLN B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 4 B 4 PHE B 62 SER B 67 -1 N SER B 63 O LYS B 74 SHEET 1 C 6 SER B 10 ALA B 13 0 SHEET 2 C 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 C 6 GLY B 84 HIS B 90 -1 N TYR B 86 O THR B 102 SHEET 4 C 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 C 6 GLN B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 C 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49 SHEET 1 D 4 SER B 10 ALA B 13 0 SHEET 2 D 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 D 4 GLY B 84 HIS B 90 -1 N TYR B 86 O THR B 102 SHEET 4 D 4 ALA B 97 PHE B 98 -1 O ALA B 97 N HIS B 90 SHEET 1 E 4 THR B 114 PHE B 118 0 SHEET 2 E 4 GLY B 129 PHE B 139 -1 O ASN B 137 N THR B 114 SHEET 3 E 4 TYR B 173 THR B 182 -1 O TYR B 173 N PHE B 139 SHEET 4 E 4 VAL B 159 TRP B 163 -1 N SER B 162 O SER B 176 SHEET 1 F 4 SER B 153 ARG B 155 0 SHEET 2 F 4 ASN B 145 ILE B 150 -1 N ILE B 150 O SER B 153 SHEET 3 F 4 SER B 191 HIS B 198 -1 O THR B 193 N LYS B 149 SHEET 4 F 4 SER B 201 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 G 4 GLN C 3 GLN C 6 0 SHEET 2 G 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 G 4 THR C 78 LEU C 83 -1 O ILE C 81 N ILE C 20 SHEET 4 G 4 ALA C 68 ASP C 73 -1 N THR C 71 O TYR C 80 SHEET 1 H 6 GLU C 10 VAL C 12 0 SHEET 2 H 6 THR C 118 VAL C 122 1 O THR C 119 N GLU C 10 SHEET 3 H 6 ALA C 92 TYR C 103 -1 N ALA C 92 O LEU C 120 SHEET 4 H 6 MET C 34 SER C 40 -1 N GLN C 39 O VAL C 93 SHEET 5 H 6 SER C 44 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 6 H 6 THR C 58 TYR C 60 -1 O ARG C 59 N ASN C 50 SHEET 1 I 4 GLU C 10 VAL C 12 0 SHEET 2 I 4 THR C 118 VAL C 122 1 O THR C 119 N GLU C 10 SHEET 3 I 4 ALA C 92 TYR C 103 -1 N ALA C 92 O LEU C 120 SHEET 4 I 4 SER C 107 TRP C 114 -1 O TYR C 113 N ARG C 98 SHEET 1 J 4 SER C 131 LEU C 135 0 SHEET 2 J 4 SER C 146 TYR C 156 -1 O GLY C 150 N LEU C 135 SHEET 3 J 4 LEU C 185 THR C 195 -1 O LEU C 188 N VAL C 153 SHEET 4 J 4 VAL C 174 THR C 176 -1 N HIS C 175 O SER C 191 SHEET 1 K 4 SER C 131 LEU C 135 0 SHEET 2 K 4 SER C 146 TYR C 156 -1 O GLY C 150 N LEU C 135 SHEET 3 K 4 LEU C 185 THR C 195 -1 O LEU C 188 N VAL C 153 SHEET 4 K 4 VAL C 180 GLN C 182 -1 N GLN C 182 O LEU C 185 SHEET 1 L 3 THR C 162 TRP C 165 0 SHEET 2 L 3 THR C 205 HIS C 210 -1 O ASN C 207 N THR C 164 SHEET 3 L 3 THR C 215 LYS C 220 -1 O LYS C 219 N CYS C 206 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04 SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 6 CYS B 134 CYS B 194 1555 1555 2.04 SSBOND 7 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 8 CYS C 151 CYS C 206 1555 1555 2.03 CISPEP 1 GLY A 218 GLU A 219 0 3.64 CISPEP 2 SER B 7 PRO B 8 0 -6.28 CISPEP 3 TYR B 140 PRO B 141 0 1.62 CISPEP 4 PHE C 157 PRO C 158 0 -7.32 CISPEP 5 GLU C 159 PRO C 160 0 -9.31 CISPEP 6 TRP C 199 PRO C 200 0 0.22 SITE 1 AC1 7 LEU A 85 PHE A 168 GLU A 169 MET A 177 SITE 2 AC1 7 LEU A 249 HIS A 250 MET A 270 CRYST1 120.313 89.766 110.682 90.00 96.14 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 0.008312 0.000000 0.000894 0.00000 SCALE2 0.000000 0.011140 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009087 0.00000 ATOM 1 N SER A 6 82.462 -28.202 42.353 1.00156.68 N ANISOU 1 N SER A 6 15716 24838 18977 2647 -2564 238 N ATOM 2 CA SER A 6 81.737 -26.990 41.994 1.00152.01 C ANISOU 2 CA SER A 6 15234 24204 18319 2440 -2409 127 C ATOM 3 C SER A 6 81.812 -26.729 40.491 1.00152.28 C ANISOU 3 C SER A 6 15271 24132 18456 2349 -2254 47 C ATOM 4 O SER A 6 81.332 -25.700 40.008 1.00153.36 O ANISOU 4 O SER A 6 15487 24230 18553 2184 -2124 -51 O ATOM 5 CB SER A 6 82.272 -25.792 42.780 1.00151.91 C ANISOU 5 CB SER A 6 15106 24376 18236 2356 -2507 32 C ATOM 6 OG SER A 6 83.688 -25.819 42.847 1.00155.34 O ANISOU 6 OG SER A 6 15294 24973 18755 2435 -2666 2 O ATOM 7 N SER A 7 82.415 -27.669 39.761 1.00149.17 N ANISOU 7 N SER A 7 14792 23691 18193 2462 -2272 92 N ATOM 8 CA SER A 7 82.437 -27.630 38.299 1.00139.91 C ANISOU 8 CA SER A 7 13637 22399 17124 2394 -2129 35 C ATOM 9 C SER A 7 81.027 -27.795 37.758 1.00130.96 C ANISOU 9 C SER A 7 12753 21071 15933 2311 -1950 62 C ATOM 10 O SER A 7 80.777 -27.568 36.578 1.00127.44 O ANISOU 10 O SER A 7 12370 20516 15536 2219 -1815 7 O ATOM 11 CB SER A 7 83.326 -28.739 37.735 1.00139.15 C ANISOU 11 CB SER A 7 13399 22288 17184 2553 -2191 94 C ATOM 12 OG SER A 7 84.695 -28.490 37.989 1.00142.73 O ANISOU 12 OG SER A 7 13598 22920 17712 2614 -2338 50 O ATOM 13 N VAL A 8 80.119 -28.216 38.633 1.00129.77 N ANISOU 13 N VAL A 8 12741 20884 15683 2346 -1957 148 N ATOM 14 CA VAL A 8 78.701 -28.367 38.302 1.00125.11 C ANISOU 14 CA VAL A 8 12382 20127 15029 2268 -1797 178 C ATOM 15 C VAL A 8 77.966 -27.025 38.336 1.00119.75 C ANISOU 15 C VAL A 8 11806 19449 14245 2085 -1689 82 C ATOM 16 O VAL A 8 77.096 -26.764 37.506 1.00113.26 O ANISOU 16 O VAL A 8 11130 18496 13406 1978 -1531 51 O ATOM 17 CB VAL A 8 78.008 -29.362 39.257 1.00120.51 C ANISOU 17 CB VAL A 8 11900 19504 14385 2380 -1844 310 C ATOM 18 CG1 VAL A 8 76.532 -29.482 38.930 1.00103.72 C ANISOU 18 CG1 VAL A 8 9995 17217 12196 2289 -1676 333 C ATOM 19 CG2 VAL A 8 78.710 -30.728 39.201 1.00124.73 C ANISOU 19 CG2 VAL A 8 12344 20025 15024 2574 -1946 412 C ATOM 20 N TYR A 9 78.322 -26.182 39.302 1.00123.34 N ANISOU 20 N TYR A 9 12183 20052 14629 2056 -1779 37 N ATOM 21 CA TYR A 9 77.823 -24.816 39.335 1.00126.57 C ANISOU 21 CA TYR A 9 12658 20479 14953 1891 -1687 -65 C ATOM 22 C TYR A 9 78.173 -24.095 38.033 1.00130.16 C ANISOU 22 C TYR A 9 13089 20894 15473 1784 -1587 -173 C ATOM 23 O TYR A 9 77.508 -23.130 37.650 1.00135.80 O ANISOU 23 O TYR A 9 13913 21556 16128 1647 -1462 -245 O ATOM 24 CB TYR A 9 78.374 -24.042 40.539 1.00130.42 C ANISOU 24 CB TYR A 9 13031 21150 15373 1882 -1820 -104 C ATOM 25 CG TYR A 9 78.470 -22.556 40.280 1.00133.55 C ANISOU 25 CG TYR A 9 13410 21598 15735 1723 -1752 -240 C ATOM 26 CD1 TYR A 9 77.324 -21.791 40.079 1.00128.06 C ANISOU 26 CD1 TYR A 9 12887 20807 14961 1595 -1593 -278 C ATOM 27 CD2 TYR A 9 79.705 -21.919 40.215 1.00139.51 C ANISOU 27 CD2 TYR A 9 13972 22496 16540 1704 -1845 -330 C ATOM 28 CE1 TYR A 9 77.404 -20.438 39.824 1.00128.11 C ANISOU 28 CE1 TYR A 9 12884 20853 14938 1459 -1528 -398 C ATOM 29 CE2 TYR A 9 79.795 -20.559 39.966 1.00138.80 C ANISOU 29 CE2 TYR A 9 13869 22449 16420 1557 -1780 -456 C ATOM 30 CZ TYR A 9 78.641 -19.826 39.770 1.00133.18 C ANISOU 30 CZ TYR A 9 13340 21633 15627 1438 -1621 -487 C ATOM 31 OH TYR A 9 78.722 -18.477 39.520 1.00130.80 O ANISOU 31 OH TYR A 9 13033 21369 15297 1301 -1555 -608 O ATOM 32 N ILE A 10 79.217 -24.559 37.354 1.00124.96 N ANISOU 32 N ILE A 10 12286 20257 14935 1852 -1644 -182 N ATOM 33 CA ILE A 10 79.563 -24.010 36.050 1.00119.00 C ANISOU 33 CA ILE A 10 11511 19452 14252 1761 -1552 -275 C ATOM 34 C ILE A 10 78.626 -24.498 34.946 1.00122.48 C ANISOU 34 C ILE A 10 12131 19698 14710 1725 -1401 -244 C ATOM 35 O ILE A 10 78.120 -23.694 34.160 1.00125.18 O ANISOU 35 O ILE A 10 12578 19964 15019 1597 -1277 -316 O ATOM 36 CB ILE A 10 80.983 -24.370 35.646 1.00113.66 C ANISOU 36 CB ILE A 10 10610 18863 13713 1845 -1655 -295 C ATOM 37 CG1 ILE A 10 81.970 -23.931 36.727 1.00118.08 C ANISOU 37 CG1 ILE A 10 10975 19631 14261 1884 -1821 -326 C ATOM 38 CG2 ILE A 10 81.306 -23.741 34.303 1.00107.57 C ANISOU 38 CG2 ILE A 10 9823 18038 13012 1741 -1554 -395 C ATOM 39 CD1 ILE A 10 83.392 -24.425 36.487 1.00120.92 C ANISOU 39 CD1 ILE A 10 11088 20094 14762 1993 -1943 -331 C ATOM 40 N THR A 11 78.401 -25.811 34.896 1.00121.91 N ANISOU 40 N THR A 11 12091 19544 14684 1841 -1418 -136 N ATOM 41 CA THR A 11 77.585 -26.435 33.848 1.00122.69 C ANISOU 41 CA THR A 11 12342 19464 14811 1819 -1292 -101 C ATOM 42 C THR A 11 76.126 -25.977 33.868 1.00123.31 C ANISOU 42 C THR A 11 12640 19444 14768 1705 -1160 -103 C ATOM 43 O THR A 11 75.469 -25.898 32.822 1.00120.51 O ANISOU 43 O THR A 11 12413 18962 14414 1625 -1039 -125 O ATOM 44 CB THR A 11 77.609 -27.975 33.954 1.00120.88 C ANISOU 44 CB THR A 11 12101 19175 14652 1974 -1343 20 C ATOM 45 OG1 THR A 11 78.964 -28.427 33.995 1.00128.06 O ANISOU 45 OG1 THR A 11 12797 20181 15679 2096 -1470 29 O ATOM 46 CG2 THR A 11 76.909 -28.611 32.762 1.00113.06 C ANISOU 46 CG2 THR A 11 11243 18008 13707 1945 -1220 44 C ATOM 47 N VAL A 12 75.615 -25.693 35.062 1.00120.81 N ANISOU 47 N VAL A 12 12364 19189 14350 1702 -1187 -77 N ATOM 48 CA VAL A 12 74.240 -25.239 35.195 1.00113.12 C ANISOU 48 CA VAL A 12 11578 18135 13268 1603 -1064 -77 C ATOM 49 C VAL A 12 74.137 -23.766 34.806 1.00107.29 C ANISOU 49 C VAL A 12 10872 17417 12476 1460 -986 -193 C ATOM 50 O VAL A 12 73.164 -23.354 34.178 1.00105.07 O ANISOU 50 O VAL A 12 10746 17030 12146 1364 -855 -216 O ATOM 51 CB VAL A 12 73.691 -25.474 36.622 1.00111.20 C ANISOU 51 CB VAL A 12 11365 17945 12942 1652 -1115 -5 C ATOM 52 CG1 VAL A 12 74.485 -24.679 37.637 1.00111.25 C ANISOU 52 CG1 VAL A 12 11234 18122 12912 1658 -1232 -52 C ATOM 53 CG2 VAL A 12 72.219 -25.113 36.692 1.00107.93 C ANISOU 53 CG2 VAL A 12 11136 17439 12435 1556 -975 1 C ATOM 54 N GLU A 13 75.155 -22.986 35.160 1.00103.79 N ANISOU 54 N GLU A 13 10280 17111 12046 1449 -1070 -266 N ATOM 55 CA GLU A 13 75.186 -21.570 34.809 1.00104.53 C ANISOU 55 CA GLU A 13 10388 17231 12096 1320 -1005 -380 C ATOM 56 C GLU A 13 75.241 -21.353 33.293 1.00102.54 C ANISOU 56 C GLU A 13 10188 16875 11897 1254 -914 -436 C ATOM 57 O GLU A 13 74.561 -20.473 32.768 1.00 99.44 O ANISOU 57 O GLU A 13 9920 16419 11445 1147 -804 -493 O ATOM 58 CB GLU A 13 76.367 -20.869 35.480 1.00109.56 C ANISOU 58 CB GLU A 13 10834 18045 12747 1324 -1126 -449 C ATOM 59 CG GLU A 13 76.180 -19.359 35.651 1.00107.66 C ANISOU 59 CG GLU A 13 10621 17854 12430 1195 -1068 -553 C ATOM 60 CD GLU A 13 75.484 -18.986 36.953 1.00104.02 C ANISOU 60 CD GLU A 13 10210 17449 11865 1182 -1079 -528 C ATOM 61 OE1 GLU A 13 74.522 -19.676 37.337 1.00 98.13 O ANISOU 61 OE1 GLU A 13 9580 16628 11078 1221 -1043 -438 O ATOM 62 OE2 GLU A 13 75.909 -18.008 37.603 1.00106.20 O ANISOU 62 OE2 GLU A 13 10403 17847 12103 1129 -1126 -600 O ATOM 63 N LEU A 14 76.058 -22.142 32.598 1.00100.44 N ANISOU 63 N LEU A 14 9823 16594 11746 1324 -963 -419 N ATOM 64 CA LEU A 14 76.121 -22.078 31.139 1.00 98.89 C ANISOU 64 CA LEU A 14 9671 16292 11609 1272 -885 -463 C ATOM 65 C LEU A 14 74.845 -22.647 30.515 1.00103.28 C ANISOU 65 C LEU A 14 10431 16683 12128 1249 -776 -403 C ATOM 66 O LEU A 14 74.406 -22.197 29.454 1.00100.67 O ANISOU 66 O LEU A 14 10209 16257 11784 1163 -684 -449 O ATOM 67 CB LEU A 14 77.346 -22.833 30.598 1.00100.25 C ANISOU 67 CB LEU A 14 9668 16495 11928 1360 -965 -456 C ATOM 68 CG LEU A 14 78.682 -22.116 30.311 1.00 99.38 C ANISOU 68 CG LEU A 14 9363 16500 11896 1337 -1023 -554 C ATOM 69 CD1 LEU A 14 78.479 -20.652 29.913 1.00 96.05 C ANISOU 69 CD1 LEU A 14 9008 16082 11406 1192 -942 -667 C ATOM 70 CD2 LEU A 14 79.677 -22.231 31.474 1.00 98.13 C ANISOU 70 CD2 LEU A 14 9001 16517 11765 1425 -1172 -545 C ATOM 71 N ALA A 15 74.257 -23.644 31.172 1.00108.47 N ANISOU 71 N ALA A 15 11135 17309 12768 1325 -793 -302 N ATOM 72 CA ALA A 15 73.009 -24.243 30.697 1.00106.79 C ANISOU 72 CA ALA A 15 11104 16952 12520 1303 -695 -242 C ATOM 73 C ALA A 15 71.887 -23.215 30.772 1.00103.16 C ANISOU 73 C ALA A 15 10802 16456 11937 1187 -589 -282 C ATOM 74 O ALA A 15 70.982 -23.195 29.940 1.00102.00 O ANISOU 74 O ALA A 15 10805 16193 11759 1123 -493 -282 O ATOM 75 CB ALA A 15 72.662 -25.476 31.523 1.00105.84 C ANISOU 75 CB ALA A 15 10987 16821 12407 1410 -740 -129 C ATOM 76 N ILE A 16 71.969 -22.371 31.796 1.00 98.59 N ANISOU 76 N ILE A 16 10181 15984 11293 1165 -615 -315 N ATOM 77 CA ILE A 16 71.067 -21.244 31.992 1.00 87.06 C ANISOU 77 CA ILE A 16 8839 14513 9726 1064 -522 -362 C ATOM 78 C ILE A 16 71.463 -20.068 31.108 1.00 85.45 C ANISOU 78 C ILE A 16 8638 14309 9519 974 -483 -471 C ATOM 79 O ILE A 16 70.611 -19.371 30.589 1.00 86.91 O ANISOU 79 O ILE A 16 8963 14420 9638 892 -384 -503 O ATOM 80 CB ILE A 16 71.052 -20.802 33.472 1.00 85.07 C ANISOU 80 CB ILE A 16 8529 14380 9415 1079 -569 -356 C ATOM 81 CG1 ILE A 16 70.025 -21.620 34.261 1.00 84.35 C ANISOU 81 CG1 ILE A 16 8518 14248 9281 1123 -546 -256 C ATOM 82 CG2 ILE A 16 70.768 -19.310 33.600 1.00 78.05 C ANISOU 82 CG2 ILE A 16 7680 13527 8449 976 -505 -445 C ATOM 83 CD1 ILE A 16 70.104 -23.121 34.019 1.00 83.13 C ANISOU 83 CD1 ILE A 16 8354 14033 9198 1220 -587 -165 C ATOM 84 N ALA A 17 72.758 -19.845 30.936 1.00 93.01 N ANISOU 84 N ALA A 17 9437 15352 10551 992 -564 -526 N ATOM 85 CA ALA A 17 73.227 -18.783 30.049 1.00 94.86 C ANISOU 85 CA ALA A 17 9660 15587 10796 908 -531 -632 C ATOM 86 C ALA A 17 72.559 -18.898 28.686 1.00 98.27 C ANISOU 86 C ALA A 17 10242 15868 11227 861 -441 -633 C ATOM 87 O ALA A 17 71.837 -17.997 28.261 1.00 98.68 O ANISOU 87 O ALA A 17 10423 15866 11205 778 -357 -678 O ATOM 88 CB ALA A 17 74.739 -18.831 29.902 1.00 91.21 C ANISOU 88 CB ALA A 17 8992 15225 10441 946 -631 -679 C ATOM 89 N VAL A 18 72.815 -20.014 28.008 1.00 98.76 N ANISOU 89 N VAL A 18 10281 15866 11376 919 -466 -583 N ATOM 90 CA VAL A 18 72.308 -20.234 26.663 1.00 93.94 C ANISOU 90 CA VAL A 18 9792 15120 10780 880 -399 -584 C ATOM 91 C VAL A 18 70.799 -20.225 26.674 1.00 92.50 C ANISOU 91 C VAL A 18 9809 14843 10492 838 -311 -541 C ATOM 92 O VAL A 18 70.181 -19.515 25.881 1.00 96.92 O ANISOU 92 O VAL A 18 10496 15333 10998 761 -242 -584 O ATOM 93 CB VAL A 18 72.779 -21.577 26.078 1.00 96.58 C ANISOU 93 CB VAL A 18 10061 15405 11232 960 -441 -525 C ATOM 94 CG1 VAL A 18 72.333 -21.710 24.636 1.00 88.90 C ANISOU 94 CG1 VAL A 18 9200 14299 10277 910 -379 -538 C ATOM 95 CG2 VAL A 18 74.290 -21.700 26.169 1.00103.20 C ANISOU 95 CG2 VAL A 18 10679 16347 12187 1018 -533 -557 C ATOM 96 N LEU A 19 70.200 -21.000 27.575 1.00 90.77 N ANISOU 96 N LEU A 19 9615 14628 10248 890 -315 -456 N ATOM 97 CA LEU A 19 68.735 -21.085 27.625 1.00 95.45 C ANISOU 97 CA LEU A 19 10381 15134 10749 852 -228 -411 C ATOM 98 C LEU A 19 68.116 -19.690 27.569 1.00 95.44 C ANISOU 98 C LEU A 19 10481 15134 10650 761 -156 -479 C ATOM 99 O LEU A 19 67.213 -19.431 26.772 1.00 88.91 O ANISOU 99 O LEU A 19 9798 14212 9771 705 -85 -486 O ATOM 100 CB LEU A 19 68.253 -21.811 28.887 1.00 96.25 C ANISOU 100 CB LEU A 19 10471 15272 10828 911 -242 -326 C ATOM 101 CG LEU A 19 67.404 -23.068 28.692 1.00 94.93 C ANISOU 101 CG LEU A 19 10388 15007 10675 944 -213 -235 C ATOM 102 CD1 LEU A 19 66.508 -22.915 27.480 1.00 87.38 C ANISOU 102 CD1 LEU A 19 9586 13931 9684 868 -132 -252 C ATOM 103 CD2 LEU A 19 68.285 -24.299 28.542 1.00100.90 C ANISOU 103 CD2 LEU A 19 11030 15763 11546 1041 -296 -185 C ATOM 104 N ALA A 20 68.633 -18.792 28.404 1.00 99.44 N ANISOU 104 N ALA A 20 10901 15749 11132 751 -180 -529 N ATOM 105 CA ALA A 20 68.095 -17.441 28.535 1.00 94.87 C ANISOU 105 CA ALA A 20 10399 15182 10465 675 -113 -592 C ATOM 106 C ALA A 20 68.223 -16.629 27.256 1.00 94.31 C ANISOU 106 C ALA A 20 10390 15039 10402 607 -84 -665 C ATOM 107 O ALA A 20 67.314 -15.893 26.893 1.00102.43 O ANISOU 107 O ALA A 20 11564 15810 11543 517 -59 -623 O ATOM 108 CB ALA A 20 68.758 -16.712 29.690 1.00 91.21 C ANISOU 108 CB ALA A 20 9809 14855 9991 679 -157 -633 C ATOM 109 N ILE A 21 69.346 -16.748 26.568 1.00 88.86 N ANISOU 109 N ILE A 21 9596 14379 9787 619 -140 -711 N ATOM 110 CA ILE A 21 69.506 -15.989 25.343 1.00 90.55 C ANISOU 110 CA ILE A 21 9861 14538 10006 557 -114 -786 C ATOM 111 C ILE A 21 68.544 -16.514 24.270 1.00 87.70 C ANISOU 111 C ILE A 21 9660 13966 9695 530 -82 -718 C ATOM 112 O ILE A 21 67.899 -15.736 23.559 1.00 84.81 O ANISOU 112 O ILE A 21 9423 13369 9431 446 -63 -692 O ATOM 113 CB ILE A 21 70.957 -16.037 24.830 1.00 92.59 C ANISOU 113 CB ILE A 21 9956 14848 10375 569 -182 -842 C ATOM 114 CG1 ILE A 21 71.940 -16.065 26.000 1.00 89.90 C ANISOU 114 CG1 ILE A 21 9432 14651 10077 613 -255 -850 C ATOM 115 CG2 ILE A 21 71.236 -14.859 23.907 1.00 90.07 C ANISOU 115 CG2 ILE A 21 9662 14511 10051 490 -153 -941 C ATOM 116 CD1 ILE A 21 73.161 -16.933 25.723 1.00 88.78 C ANISOU 116 CD1 ILE A 21 9119 14548 10065 676 -337 -843 C ATOM 117 N LEU A 22 68.444 -17.833 24.156 1.00 86.00 N ANISOU 117 N LEU A 22 9435 13781 9461 597 -91 -667 N ATOM 118 CA LEU A 22 67.556 -18.420 23.159 1.00 89.47 C ANISOU 118 CA LEU A 22 10013 13988 9994 562 -76 -593 C ATOM 119 C LEU A 22 66.106 -17.972 23.326 1.00 86.56 C ANISOU 119 C LEU A 22 9819 13332 9739 479 -47 -502 C ATOM 120 O LEU A 22 65.582 -17.234 22.497 1.00 86.41 O ANISOU 120 O LEU A 22 9911 13111 9811 405 -34 -491 O ATOM 121 CB LEU A 22 67.645 -19.943 23.178 1.00 94.43 C ANISOU 121 CB LEU A 22 10594 14693 10591 649 -90 -545 C ATOM 122 CG LEU A 22 68.751 -20.555 22.312 1.00 95.01 C ANISOU 122 CG LEU A 22 10554 14752 10793 682 -145 -560 C ATOM 123 CD1 LEU A 22 68.771 -22.077 22.464 1.00 96.59 C ANISOU 123 CD1 LEU A 22 10710 14921 11070 759 -175 -471 C ATOM 124 CD2 LEU A 22 68.584 -20.157 20.847 1.00 84.21 C ANISOU 124 CD2 LEU A 22 9269 13297 9429 622 -121 -611 C ATOM 125 N GLY A 23 65.473 -18.412 24.408 1.00 82.38 N ANISOU 125 N GLY A 23 9304 12797 9198 500 -38 -440 N ATOM 126 CA GLY A 23 64.093 -18.073 24.691 1.00 73.56 C ANISOU 126 CA GLY A 23 8335 11432 8181 432 -13 -369 C ATOM 127 C GLY A 23 63.769 -16.598 24.546 1.00 74.45 C ANISOU 127 C GLY A 23 8524 11406 8357 358 0 -387 C ATOM 128 O GLY A 23 62.739 -16.241 23.986 1.00 76.12 O ANISOU 128 O GLY A 23 8502 11914 8507 398 -49 -423 O ATOM 129 N ASN A 24 64.647 -15.731 25.038 1.00 80.93 N ANISOU 129 N ASN A 24 9247 12390 9113 366 -9 -455 N ATOM 130 CA ASN A 24 64.362 -14.291 25.054 1.00 81.54 C ANISOU 130 CA ASN A 24 9385 12356 9240 304 5 -470 C ATOM 131 C ASN A 24 64.560 -13.584 23.720 1.00 71.92 C ANISOU 131 C ASN A 24 8219 11032 8075 260 5 -496 C ATOM 132 O ASN A 24 63.931 -12.571 23.440 1.00 63.35 O ANISOU 132 O ASN A 24 7220 9813 7038 205 -34 -480 O ATOM 133 CB ASN A 24 65.147 -13.585 26.163 1.00 83.94 C ANISOU 133 CB ASN A 24 9562 12876 9455 321 -2 -537 C ATOM 134 CG ASN A 24 64.530 -13.799 27.536 1.00 87.09 C ANISOU 134 CG ASN A 24 9957 13299 9833 339 6 -492 C ATOM 135 OD1 ASN A 24 63.816 -12.937 28.050 1.00 89.18 O ANISOU 135 OD1 ASN A 24 10291 13448 10146 297 23 -471 O ATOM 136 ND2 ASN A 24 64.792 -14.959 28.130 1.00 86.60 N ANISOU 136 ND2 ASN A 24 9811 13394 9698 408 -7 -477 N ATOM 137 N VAL A 25 65.441 -14.120 22.898 1.00 73.15 N ANISOU 137 N VAL A 25 8300 11300 8192 287 -11 -545 N ATOM 138 CA VAL A 25 65.611 -13.583 21.566 1.00 76.38 C ANISOU 138 CA VAL A 25 8755 11615 8653 248 -11 -568 C ATOM 139 C VAL A 25 64.393 -13.951 20.731 1.00 73.72 C ANISOU 139 C VAL A 25 8341 11037 8633 232 -41 -438 C ATOM 140 O VAL A 25 64.046 -13.246 19.789 1.00 67.89 O ANISOU 140 O VAL A 25 7862 10223 7712 182 -34 -484 O ATOM 141 CB VAL A 25 66.918 -14.098 20.918 1.00 78.47 C ANISOU 141 CB VAL A 25 8882 12088 8847 286 -32 -661 C ATOM 142 CG1 VAL A 25 66.760 -14.265 19.412 1.00 77.41 C ANISOU 142 CG1 VAL A 25 8818 11820 8776 260 -32 -649 C ATOM 143 CG2 VAL A 25 68.062 -13.163 21.253 1.00 71.91 C ANISOU 143 CG2 VAL A 25 7918 11457 7947 280 -39 -777 C ATOM 144 N LEU A 26 63.742 -15.053 21.104 1.00 76.38 N ANISOU 144 N LEU A 26 8932 11343 8747 238 -41 -424 N ATOM 145 CA LEU A 26 62.566 -15.552 20.398 1.00 73.88 C ANISOU 145 CA LEU A 26 8322 11389 8360 313 -47 -465 C ATOM 146 C LEU A 26 61.384 -14.644 20.696 1.00 75.55 C ANISOU 146 C LEU A 26 8708 11061 8938 221 -30 -318 C ATOM 147 O LEU A 26 60.609 -14.308 19.808 1.00 76.73 O ANISOU 147 O LEU A 26 8906 11123 9125 198 -27 -305 O ATOM 148 CB LEU A 26 62.266 -16.987 20.829 1.00 68.76 C ANISOU 148 CB LEU A 26 7818 10270 8038 288 -35 -301 C ATOM 149 CG LEU A 26 61.302 -17.851 20.010 1.00 70.08 C ANISOU 149 CG LEU A 26 8044 10340 8242 283 -32 -262 C ATOM 150 CD1 LEU A 26 61.803 -18.100 18.576 1.00 59.30 C ANISOU 150 CD1 LEU A 26 6883 8949 6698 253 -37 -310 C ATOM 151 CD2 LEU A 26 61.051 -19.169 20.741 1.00 70.52 C ANISOU 151 CD2 LEU A 26 8298 10417 8081 292 -33 -245 C ATOM 152 N VAL A 27 61.262 -14.236 21.954 1.00 81.81 N ANISOU 152 N VAL A 27 9684 11898 9504 206 -32 -345 N ATOM 153 CA VAL A 27 60.278 -13.230 22.353 1.00 82.03 C ANISOU 153 CA VAL A 27 9529 11879 9758 198 -26 -305 C ATOM 154 C VAL A 27 60.425 -11.943 21.536 1.00 79.04 C ANISOU 154 C VAL A 27 9357 11468 9205 150 -24 -365 C ATOM 155 O VAL A 27 59.438 -11.385 21.062 1.00 82.40 O ANISOU 155 O VAL A 27 9632 11817 9860 144 -23 -315 O ATOM 156 CB VAL A 27 60.386 -12.899 23.865 1.00 63.01 C ANISOU 156 CB VAL A 27 7079 9547 7316 207 -26 -310 C ATOM 157 CG1 VAL A 27 59.786 -11.537 24.170 1.00 63.25 C ANISOU 157 CG1 VAL A 27 7120 9550 7361 175 -25 -318 C ATOM 158 CG2 VAL A 27 59.724 -13.981 24.699 1.00 61.58 C ANISOU 158 CG2 VAL A 27 7116 9363 6919 214 -27 -291 C ATOM 159 N CYS A 28 61.661 -11.482 21.371 1.00 75.07 N ANISOU 159 N CYS A 28 8817 11037 8669 145 -25 -419 N ATOM 160 CA CYS A 28 61.931 -10.255 20.625 1.00 78.11 C ANISOU 160 CA CYS A 28 9201 11404 9072 113 -21 -456 C ATOM 161 C CYS A 28 61.730 -10.473 19.124 1.00 77.16 C ANISOU 161 C CYS A 28 9113 11209 8995 105 -20 -445 C ATOM 162 O CYS A 28 61.317 -9.573 18.389 1.00 71.15 O ANISOU 162 O CYS A 28 8373 10391 8267 82 -16 -446 O ATOM 163 CB CYS A 28 63.350 -9.749 20.924 1.00 75.11 C ANISOU 163 CB CYS A 28 8765 11133 8642 107 -22 -527 C ATOM 164 SG CYS A 28 63.638 -9.383 22.692 1.00100.04 S ANISOU 164 SG CYS A 28 11638 14402 11972 124 -25 -501 S ATOM 165 N TRP A 29 62.024 -11.686 18.679 1.00 79.73 N ANISOU 165 N TRP A 29 9441 11538 9317 127 -24 -435 N ATOM 166 CA TRP A 29 61.852 -12.057 17.287 1.00 79.57 C ANISOU 166 CA TRP A 29 9448 11452 9332 121 -23 -425 C ATOM 167 C TRP A 29 60.364 -12.162 17.013 1.00 77.59 C ANISOU 167 C TRP A 29 9071 11110 9301 128 -23 -339 C ATOM 168 O TRP A 29 59.871 -11.704 15.990 1.00 80.85 O ANISOU 168 O TRP A 29 9685 11454 9579 101 -19 -362 O ATOM 169 CB TRP A 29 62.530 -13.396 17.038 1.00 80.72 C ANISOU 169 CB TRP A 29 9386 11640 9645 162 -31 -394 C ATOM 170 CG TRP A 29 62.705 -13.753 15.619 1.00 81.87 C ANISOU 170 CG TRP A 29 9551 11745 9811 155 -31 -401 C ATOM 171 CD1 TRP A 29 62.142 -13.152 14.536 1.00 78.78 C ANISOU 171 CD1 TRP A 29 9198 11282 9453 129 -27 -394 C ATOM 172 CD2 TRP A 29 63.518 -14.810 15.116 1.00 94.16 C ANISOU 172 CD2 TRP A 29 11282 13330 11165 162 -33 -458 C ATOM 173 NE1 TRP A 29 62.550 -13.773 13.382 1.00 79.06 N ANISOU 173 NE1 TRP A 29 9417 11298 9324 120 -26 -443 N ATOM 174 CE2 TRP A 29 63.397 -14.797 13.713 1.00 92.46 C ANISOU 174 CE2 TRP A 29 11088 13058 10986 146 -31 -463 C ATOM 175 CE3 TRP A 29 64.344 -15.769 15.718 1.00101.00 C ANISOU 175 CE3 TRP A 29 11776 14729 11869 266 -53 -591 C ATOM 176 CZ2 TRP A 29 64.070 -15.708 12.902 1.00100.02 C ANISOU 176 CZ2 TRP A 29 12035 14031 11936 158 -35 -485 C ATOM 177 CZ3 TRP A 29 65.010 -16.671 14.913 1.00 98.00 C ANISOU 177 CZ3 TRP A 29 11696 13951 11588 220 -34 -507 C ATOM 178 CH2 TRP A 29 64.868 -16.637 13.519 1.00101.14 C ANISOU 178 CH2 TRP A 29 12141 14255 12033 193 -35 -505 C ATOM 179 N ALA A 30 59.634 -12.753 17.945 1.00 71.51 N ANISOU 179 N ALA A 30 8486 10328 8358 132 -22 -334 N ATOM 180 CA ALA A 30 58.192 -12.784 17.811 1.00 68.73 C ANISOU 180 CA ALA A 30 8013 9895 8206 137 -21 -267 C ATOM 181 C ALA A 30 57.637 -11.358 17.644 1.00 68.17 C ANISOU 181 C ALA A 30 7959 9789 8153 112 -18 -271 C ATOM 182 O ALA A 30 57.030 -11.039 16.628 1.00 66.60 O ANISOU 182 O ALA A 30 7796 9529 7981 100 -16 -260 O ATOM 183 CB ALA A 30 57.563 -13.488 19.015 1.00 60.82 C ANISOU 183 CB ALA A 30 7173 8900 7035 141 -21 -261 C ATOM 184 N VAL A 31 57.881 -10.483 18.615 1.00 65.72 N ANISOU 184 N VAL A 31 7513 9886 7570 132 -22 -392 N ATOM 185 CA VAL A 31 57.284 -9.151 18.563 1.00 62.89 C ANISOU 185 CA VAL A 31 7279 9132 7484 85 -14 -289 C ATOM 186 C VAL A 31 57.691 -8.374 17.314 1.00 70.80 C ANISOU 186 C VAL A 31 8445 10109 8348 60 -11 -337 C ATOM 187 O VAL A 31 56.895 -7.641 16.738 1.00 77.83 O ANISOU 187 O VAL A 31 9360 10942 9268 49 -9 -322 O ATOM 188 CB VAL A 31 57.553 -8.331 19.846 1.00 55.44 C ANISOU 188 CB VAL A 31 6300 8249 6518 79 -14 -310 C ATOM 189 CG1 VAL A 31 57.147 -6.866 19.657 1.00 44.49 C ANISOU 189 CG1 VAL A 31 5089 6829 4987 50 -9 -348 C ATOM 190 CG2 VAL A 31 56.805 -8.942 21.027 1.00 53.59 C ANISOU 190 CG2 VAL A 31 6068 8018 6275 96 -15 -283 C ATOM 191 N TRP A 32 58.927 -8.535 16.881 1.00 73.30 N ANISOU 191 N TRP A 32 8734 10474 8641 57 -11 -374 N ATOM 192 CA TRP A 32 59.347 -7.846 15.679 1.00 75.74 C ANISOU 192 CA TRP A 32 8882 10774 9122 42 -9 -364 C ATOM 193 C TRP A 32 58.451 -8.308 14.540 1.00 66.05 C ANISOU 193 C TRP A 32 7705 9468 7924 46 -9 -329 C ATOM 194 O TRP A 32 58.062 -7.528 13.680 1.00 63.26 O ANISOU 194 O TRP A 32 7374 9072 7589 32 -7 -325 O ATOM 195 CB TRP A 32 60.830 -8.120 15.375 1.00 80.39 C ANISOU 195 CB TRP A 32 9422 11434 9689 38 -9 -412 C ATOM 196 CG TRP A 32 61.348 -7.385 14.164 1.00 87.61 C ANISOU 196 CG TRP A 32 10508 12330 10449 11 -3 -482 C ATOM 197 CD1 TRP A 32 61.842 -6.110 14.124 1.00 89.25 C ANISOU 197 CD1 TRP A 32 10516 12574 10820 -20 5 -481 C ATOM 198 CD2 TRP A 32 61.423 -7.886 12.821 1.00 94.66 C ANISOU 198 CD2 TRP A 32 11417 13188 11363 10 -3 -477 C ATOM 199 NE1 TRP A 32 62.219 -5.786 12.840 1.00 94.65 N ANISOU 199 NE1 TRP A 32 11385 13229 11350 -37 10 -546 N ATOM 200 CE2 TRP A 32 61.971 -6.857 12.020 1.00 98.91 C ANISOU 200 CE2 TRP A 32 11769 13743 12069 -20 5 -474 C ATOM 201 CE3 TRP A 32 61.085 -9.106 12.216 1.00 96.09 C ANISOU 201 CE3 TRP A 32 11452 13343 11714 32 -8 -410 C ATOM 202 CZ2 TRP A 32 62.182 -7.008 10.642 1.00102.14 C ANISOU 202 CZ2 TRP A 32 12362 14115 12332 -28 8 -525 C ATOM 203 CZ3 TRP A 32 61.295 -9.255 10.842 1.00 99.81 C ANISOU 203 CZ3 TRP A 32 12097 13781 12045 21 -5 -456 C ATOM 204 CH2 TRP A 32 61.835 -8.211 10.073 1.00101.76 C ANISOU 204 CH2 TRP A 32 12332 14035 12296 -7 2 -493 C ATOM 205 N LEU A 33 58.091 -9.581 14.583 1.00 60.60 N ANISOU 205 N LEU A 33 7030 8761 7236 67 -13 -305 N ATOM 206 CA LEU A 33 57.541 -10.284 13.430 1.00 67.87 C ANISOU 206 CA LEU A 33 7985 9625 8177 71 -13 -283 C ATOM 207 C LEU A 33 56.011 -10.190 13.315 1.00 75.15 C ANISOU 207 C LEU A 33 8952 10478 9124 71 -13 -246 C ATOM 208 O LEU A 33 55.488 -9.663 12.335 1.00 79.38 O ANISOU 208 O LEU A 33 9638 10969 9556 57 -10 -260 O ATOM 209 CB LEU A 33 57.992 -11.742 13.487 1.00 72.49 C ANISOU 209 CB LEU A 33 8560 10233 8751 90 -17 -282 C ATOM 210 CG LEU A 33 58.055 -12.593 12.229 1.00 70.99 C ANISOU 210 CG LEU A 33 8385 10016 8573 93 -17 -279 C ATOM 211 CD1 LEU A 33 58.089 -14.061 12.639 1.00 68.76 C ANISOU 211 CD1 LEU A 33 8100 9745 8281 115 -20 -267 C ATOM 212 CD2 LEU A 33 56.861 -12.312 11.364 1.00 71.51 C ANISOU 212 CD2 LEU A 33 8624 10006 8539 76 -14 -277 C ATOM 213 N ASN A 34 55.301 -10.728 14.306 1.00 78.69 N ANISOU 213 N ASN A 34 9407 10920 9570 83 -13 -226 N ATOM 214 CA ASN A 34 53.845 -10.659 14.337 1.00 69.58 C ANISOU 214 CA ASN A 34 8410 9710 8317 76 -12 -216 C ATOM 215 C ASN A 34 53.395 -9.241 14.591 1.00 69.74 C ANISOU 215 C ASN A 34 8314 9723 8462 72 -11 -200 C ATOM 216 O ASN A 34 53.748 -8.632 15.605 1.00 71.89 O ANISOU 216 O ASN A 34 8689 10028 8597 64 -10 -232 O ATOM 217 CB ASN A 34 53.268 -11.574 15.418 1.00 67.12 C ANISOU 217 CB ASN A 34 8099 9403 7999 88 -12 -198 C ATOM 218 CG ASN A 34 51.749 -11.482 15.516 1.00 77.30 C ANISOU 218 CG ASN A 34 9297 10647 9426 94 -11 -159 C ATOM 219 OD1 ASN A 34 51.148 -10.458 15.195 1.00 73.85 O ANISOU 219 OD1 ASN A 34 8985 10184 8891 79 -10 -172 O ATOM 220 ND2 ASN A 34 51.124 -12.557 15.966 1.00 89.04 N ANISOU 220 ND2 ASN A 34 10792 12126 10915 103 -11 -144 N ATOM 221 N SER A 35 52.588 -8.734 13.672 1.00 69.45 N ANISOU 221 N SER A 35 8418 9637 8332 61 -9 -206 N ATOM 222 CA SER A 35 52.129 -7.360 13.714 1.00 68.71 C ANISOU 222 CA SER A 35 8217 9533 8357 58 -9 -190 C ATOM 223 C SER A 35 51.271 -7.068 14.929 1.00 74.22 C ANISOU 223 C SER A 35 8916 10230 9053 63 -9 -180 C ATOM 224 O SER A 35 51.300 -5.957 15.451 1.00 81.00 O ANISOU 224 O SER A 35 9767 11102 9908 56 -9 -190 O ATOM 225 CB SER A 35 51.338 -7.049 12.458 1.00 67.76 C ANISOU 225 CB SER A 35 8229 9366 8150 52 -8 -193 C ATOM 226 OG SER A 35 51.048 -5.675 12.412 1.00 70.44 O ANISOU 226 OG SER A 35 8571 9697 8494 45 -7 -196 O ATOM 227 N ASN A 36 50.502 -8.061 15.371 1.00 73.15 N ANISOU 227 N ASN A 36 8901 10081 8812 67 -9 -179 N ATOM 228 CA ASN A 36 49.598 -7.879 16.501 1.00 73.73 C ANISOU 228 CA ASN A 36 8866 10157 8992 77 -10 -155 C ATOM 229 C ASN A 36 50.374 -7.707 17.803 1.00 81.66 C ANISOU 229 C ASN A 36 9957 11211 9860 71 -9 -184 C ATOM 230 O ASN A 36 49.873 -7.116 18.755 1.00 90.34 O ANISOU 230 O ASN A 36 11052 12320 10954 71 -9 -184 O ATOM 231 CB ASN A 36 48.621 -9.054 16.644 1.00 75.14 C ANISOU 231 CB ASN A 36 8989 10559 9004 107 -13 -187 C ATOM 232 CG ASN A 36 47.965 -9.451 15.333 1.00 77.79 C ANISOU 232 CG ASN A 36 9416 10613 9527 85 -9 -128 C ATOM 233 OD1 ASN A 36 47.764 -10.639 15.072 1.00 79.99 O ANISOU 233 OD1 ASN A 36 9700 10883 9808 89 -9 -121 O ATOM 234 ND2 ASN A 36 47.625 -8.465 14.504 1.00 76.08 N ANISOU 234 ND2 ASN A 36 9309 10376 9222 74 -10 -141 N ATOM 235 N LEU A 37 51.598 -8.228 17.836 1.00 80.62 N ANISOU 235 N LEU A 37 9806 11116 9708 72 -10 -199 N ATOM 236 CA LEU A 37 52.414 -8.240 19.049 1.00 73.74 C ANISOU 236 CA LEU A 37 8908 10307 8803 75 -10 -215 C ATOM 237 C LEU A 37 53.006 -6.877 19.369 1.00 72.31 C ANISOU 237 C LEU A 37 8709 10157 8608 62 -9 -243 C ATOM 238 O LEU A 37 53.446 -6.629 20.492 1.00 71.68 O ANISOU 238 O LEU A 37 8462 10134 8639 67 -10 -237 O ATOM 239 CB LEU A 37 53.536 -9.275 18.928 1.00 68.23 C ANISOU 239 CB LEU A 37 8192 9648 8083 82 -12 -225 C ATOM 240 CG LEU A 37 53.080 -10.724 19.088 1.00 62.36 C ANISOU 240 CG LEU A 37 7325 8895 7475 105 -13 -183 C ATOM 241 CD1 LEU A 37 54.230 -11.706 18.891 1.00 61.77 C ANISOU 241 CD1 LEU A 37 7227 8861 7383 117 -14 -193 C ATOM 242 CD2 LEU A 37 52.430 -10.899 20.441 1.00 58.18 C ANISOU 242 CD2 LEU A 37 6788 8382 6936 112 -12 -171 C ATOM 243 N GLN A 38 52.987 -5.984 18.387 1.00 71.31 N ANISOU 243 N GLN A 38 8593 10001 8499 51 -8 -249 N ATOM 244 CA GLN A 38 53.637 -4.701 18.553 1.00 66.78 C ANISOU 244 CA GLN A 38 7865 9461 8046 39 -7 -256 C ATOM 245 C GLN A 38 52.636 -3.717 19.132 1.00 70.92 C ANISOU 245 C GLN A 38 8536 9961 8449 32 -6 -272 C ATOM 246 O GLN A 38 51.741 -3.224 18.446 1.00 74.65 O ANISOU 246 O GLN A 38 9033 10383 8949 33 -6 -254 O ATOM 247 CB GLN A 38 54.143 -4.202 17.197 1.00 56.63 C ANISOU 247 CB GLN A 38 6588 8158 6772 26 -5 -268 C ATOM 248 CG GLN A 38 55.055 -5.192 16.508 1.00 62.54 C ANISOU 248 CG GLN A 38 7463 8920 7382 27 -5 -301 C ATOM 249 CD GLN A 38 55.267 -4.877 15.041 1.00 73.13 C ANISOU 249 CD GLN A 38 8681 10235 8869 20 -4 -279 C ATOM 250 OE1 GLN A 38 54.637 -3.971 14.495 1.00 76.99 O ANISOU 250 OE1 GLN A 38 9192 10687 9375 13 -2 -270 O ATOM 251 NE2 GLN A 38 56.155 -5.630 14.390 1.00 71.48 N ANISOU 251 NE2 GLN A 38 8595 10041 8522 19 -4 -319 N ATOM 252 N ASN A 39 52.828 -3.425 20.410 1.00 71.04 N ANISOU 252 N ASN A 39 8529 10023 8438 30 -5 -287 N ATOM 253 CA ASN A 39 51.990 -2.500 21.143 1.00 74.69 C ANISOU 253 CA ASN A 39 8855 10482 9041 30 -5 -262 C ATOM 254 C ASN A 39 52.733 -2.059 22.396 1.00 70.92 C ANISOU 254 C ASN A 39 8482 10072 8390 17 -3 -319 C ATOM 255 O ASN A 39 53.677 -2.717 22.822 1.00 72.07 O ANISOU 255 O ASN A 39 8446 10279 8659 21 -4 -307 O ATOM 256 CB ASN A 39 50.637 -3.141 21.488 1.00 81.12 C ANISOU 256 CB ASN A 39 9830 11256 9736 43 -7 -251 C ATOM 257 CG ASN A 39 50.775 -4.445 22.273 1.00 83.43 C ANISOU 257 CG ASN A 39 10112 11578 10010 55 -8 -241 C ATOM 258 OD1 ASN A 39 51.303 -4.460 23.392 1.00 86.55 O ANISOU 258 OD1 ASN A 39 10337 12035 10515 59 -9 -235 O ATOM 259 ND2 ASN A 39 50.272 -5.540 21.700 1.00 76.74 N ANISOU 259 ND2 ASN A 39 9284 10695 9180 65 -9 -216 N ATOM 260 N VAL A 40 52.298 -0.961 22.995 1.00 68.63 N ANISOU 260 N VAL A 40 8038 9793 8246 8 -2 -303 N ATOM 261 CA VAL A 40 52.930 -0.465 24.204 1.00 69.81 C ANISOU 261 CA VAL A 40 8141 10016 8369 -6 1 -336 C ATOM 262 C VAL A 40 53.141 -1.548 25.256 1.00 69.85 C ANISOU 262 C VAL A 40 8287 10065 8186 9 -2 -360 C ATOM 263 O VAL A 40 54.260 -1.725 25.760 1.00 80.60 O ANISOU 263 O VAL A 40 9435 11507 9681 2 0 -359 O ATOM 264 CB VAL A 40 52.095 0.637 24.853 1.00 69.18 C ANISOU 264 CB VAL A 40 8065 9927 8294 -14 3 -340 C ATOM 265 CG1 VAL A 40 52.742 1.072 26.173 1.00 71.84 C ANISOU 265 CG1 VAL A 40 8522 10340 8433 -29 6 -411 C ATOM 266 CG2 VAL A 40 51.932 1.800 23.899 1.00 63.85 C ANISOU 266 CG2 VAL A 40 7566 9203 7490 -27 6 -380 C ATOM 267 N THR A 41 52.080 -2.278 25.583 1.00 58.95 N ANISOU 267 N THR A 41 6766 8657 6978 30 -5 -296 N ATOM 268 CA THR A 41 52.186 -3.299 26.616 1.00 69.13 C ANISOU 268 CA THR A 41 8198 9988 8080 41 -7 -314 C ATOM 269 C THR A 41 53.357 -4.226 26.338 1.00 77.90 C ANISOU 269 C THR A 41 9118 11144 9336 51 -8 -295 C ATOM 270 O THR A 41 53.990 -4.736 27.259 1.00 84.14 O ANISOU 270 O THR A 41 9867 12006 10095 59 -9 -304 O ATOM 271 CB THR A 41 50.931 -4.145 26.725 1.00 70.43 C ANISOU 271 CB THR A 41 8389 10105 8267 58 -8 -272 C ATOM 272 OG1 THR A 41 49.781 -3.299 26.632 1.00 80.51 O ANISOU 272 OG1 THR A 41 9533 11337 9721 59 -9 -243 O ATOM 273 CG2 THR A 41 50.921 -4.880 28.053 1.00 61.90 C ANISOU 273 CG2 THR A 41 7285 9080 7152 68 -9 -266 C ATOM 274 N ASN A 42 53.645 -4.437 25.061 1.00 71.93 N ANISOU 274 N ASN A 42 8553 10343 8435 46 -7 -317 N ATOM 275 CA ASN A 42 54.696 -5.354 24.677 1.00 62.83 C ANISOU 275 CA ASN A 42 7386 9225 7264 54 -9 -325 C ATOM 276 C ASN A 42 56.076 -4.752 24.500 1.00 70.74 C ANISOU 276 C ASN A 42 8353 10289 8236 38 -7 -374 C ATOM 277 O ASN A 42 57.052 -5.479 24.330 1.00 76.64 O ANISOU 277 O ASN A 42 9079 11081 8958 46 -8 -388 O ATOM 278 CB ASN A 42 54.283 -6.103 23.433 1.00 54.70 C ANISOU 278 CB ASN A 42 6227 8127 6429 68 -11 -271 C ATOM 279 CG ASN A 42 53.386 -7.255 23.751 1.00 60.43 C ANISOU 279 CG ASN A 42 7133 8821 7007 79 -11 -258 C ATOM 280 OD1 ASN A 42 53.276 -7.672 24.915 1.00 57.46 O ANISOU 280 OD1 ASN A 42 6740 8487 6606 88 -12 -252 O ATOM 281 ND2 ASN A 42 52.736 -7.794 22.726 1.00 64.67 N ANISOU 281 ND2 ASN A 42 7701 9292 7580 82 -11 -234 N ATOM 282 N TYR A 43 56.172 -3.433 24.545 1.00 71.67 N ANISOU 282 N TYR A 43 8278 10420 8532 17 -3 -370 N ATOM 283 CA TYR A 43 57.484 -2.811 24.532 1.00 78.09 C ANISOU 283 CA TYR A 43 9040 11307 9322 -6 1 -422 C ATOM 284 C TYR A 43 58.097 -3.015 25.906 1.00 78.13 C ANISOU 284 C TYR A 43 8987 11413 9287 -3 1 -446 C ATOM 285 O TYR A 43 59.306 -3.211 26.049 1.00 74.46 O ANISOU 285 O TYR A 43 8470 11031 8792 -7 2 -484 O ATOM 286 CB TYR A 43 57.383 -1.332 24.162 1.00 80.23 C ANISOU 286 CB TYR A 43 9511 11548 9422 -36 8 -488 C ATOM 287 CG TYR A 43 56.723 -1.148 22.825 1.00 86.49 C ANISOU 287 CG TYR A 43 10166 12258 10440 -37 8 -419 C ATOM 288 CD1 TYR A 43 56.736 -2.177 21.887 1.00 87.40 C ANISOU 288 CD1 TYR A 43 10307 12334 10566 -18 4 -394 C ATOM 289 CD2 TYR A 43 56.071 0.030 22.499 1.00 90.00 C ANISOU 289 CD2 TYR A 43 10811 12647 10737 -49 11 -457 C ATOM 290 CE1 TYR A 43 56.128 -2.036 20.661 1.00 90.09 C ANISOU 290 CE1 TYR A 43 10694 12598 10938 -17 4 -369 C ATOM 291 CE2 TYR A 43 55.451 0.182 21.268 1.00 94.08 C ANISOU 291 CE2 TYR A 43 11199 13095 11452 -49 11 -392 C ATOM 292 CZ TYR A 43 55.480 -0.858 20.351 1.00 91.67 C ANISOU 292 CZ TYR A 43 11077 12749 11004 -28 6 -401 C ATOM 293 OH TYR A 43 54.864 -0.729 19.119 1.00 86.06 O ANISOU 293 OH TYR A 43 10249 11976 10473 -26 6 -343 O ATOM 294 N PHE A 44 57.242 -3.000 26.919 1.00 76.21 N ANISOU 294 N PHE A 44 8750 11167 9040 5 -1 -425 N ATOM 295 CA PHE A 44 57.708 -3.214 28.272 1.00 81.66 C ANISOU 295 CA PHE A 44 9384 11954 9689 10 -2 -443 C ATOM 296 C PHE A 44 58.072 -4.675 28.465 1.00 87.46 C ANISOU 296 C PHE A 44 10330 12714 10187 40 -7 -460 C ATOM 297 O PHE A 44 58.849 -5.021 29.350 1.00 93.26 O ANISOU 297 O PHE A 44 10784 13554 11097 53 -9 -442 O ATOM 298 CB PHE A 44 56.647 -2.759 29.270 1.00 81.71 C ANISOU 298 CB PHE A 44 9401 11948 9698 8 -1 -428 C ATOM 299 CG PHE A 44 56.390 -1.286 29.230 1.00 83.32 C ANISOU 299 CG PHE A 44 9825 12127 9705 -24 5 -497 C ATOM 300 CD1 PHE A 44 55.106 -0.796 29.104 1.00 80.44 C ANISOU 300 CD1 PHE A 44 9498 11683 9382 -23 4 -467 C ATOM 301 CD2 PHE A 44 57.447 -0.385 29.308 1.00 89.01 C ANISOU 301 CD2 PHE A 44 10508 12916 10395 -56 12 -559 C ATOM 302 CE1 PHE A 44 54.872 0.563 29.058 1.00 81.64 C ANISOU 302 CE1 PHE A 44 9446 11830 9746 -53 11 -453 C ATOM 303 CE2 PHE A 44 57.224 0.982 29.263 1.00 89.41 C ANISOU 303 CE2 PHE A 44 10561 12952 10460 -88 20 -590 C ATOM 304 CZ PHE A 44 55.929 1.455 29.141 1.00 87.53 C ANISOU 304 CZ PHE A 44 10362 12630 10264 -83 19 -554 C ATOM 305 N VAL A 45 57.504 -5.532 27.626 1.00 83.67 N ANISOU 305 N VAL A 45 9678 12161 9953 63 -11 -381 N ATOM 306 CA VAL A 45 57.849 -6.945 27.641 1.00 79.17 C ANISOU 306 CA VAL A 45 9315 11608 9159 86 -13 -393 C ATOM 307 C VAL A 45 59.163 -7.184 26.897 1.00 74.67 C ANISOU 307 C VAL A 45 8721 11083 8567 87 -14 -428 C ATOM 308 O VAL A 45 59.960 -8.028 27.293 1.00 76.19 O ANISOU 308 O VAL A 45 8882 11350 8716 109 -18 -436 O ATOM 309 CB VAL A 45 56.690 -7.822 27.092 1.00 50.42 C ANISOU 309 CB VAL A 45 5723 7870 5566 100 -14 -337 C ATOM 310 CG1 VAL A 45 57.203 -9.086 26.384 1.00 49.57 C ANISOU 310 CG1 VAL A 45 5619 7759 5457 120 -16 -323 C ATOM 311 CG2 VAL A 45 55.730 -8.183 28.215 1.00 42.80 C ANISOU 311 CG2 VAL A 45 4562 6908 4792 121 -16 -280 C ATOM 312 N VAL A 46 59.393 -6.420 25.834 1.00 69.02 N ANISOU 312 N VAL A 46 7801 10335 8090 71 -13 -414 N ATOM 313 CA VAL A 46 60.648 -6.496 25.085 1.00 68.19 C ANISOU 313 CA VAL A 46 7887 10268 7754 60 -11 -494 C ATOM 314 C VAL A 46 61.830 -5.908 25.862 1.00 69.07 C ANISOU 314 C VAL A 46 7695 10509 8040 52 -10 -514 C ATOM 315 O VAL A 46 62.927 -6.466 25.853 1.00 52.29 O ANISOU 315 O VAL A 46 5520 8463 5883 66 -13 -545 O ATOM 316 CB VAL A 46 60.530 -5.797 23.717 1.00 61.58 C ANISOU 316 CB VAL A 46 6863 9365 7171 41 -8 -460 C ATOM 317 CG1 VAL A 46 61.906 -5.496 23.154 1.00 56.31 C ANISOU 317 CG1 VAL A 46 6147 8762 6486 24 -5 -518 C ATOM 318 CG2 VAL A 46 59.734 -6.668 22.758 1.00 59.70 C ANISOU 318 CG2 VAL A 46 6888 9024 6770 54 -10 -448 C ATOM 319 N SER A 47 61.597 -4.766 26.509 1.00 76.60 N ANISOU 319 N SER A 47 8634 11480 8991 23 -5 -536 N ATOM 320 CA SER A 47 62.555 -4.195 27.435 1.00 74.54 C ANISOU 320 CA SER A 47 8559 11329 8433 5 -1 -648 C ATOM 321 C SER A 47 62.877 -5.258 28.459 1.00 76.94 C ANISOU 321 C SER A 47 8558 11728 8948 45 -9 -583 C ATOM 322 O SER A 47 64.013 -5.375 28.908 1.00 80.72 O ANISOU 322 O SER A 47 8964 12324 9384 49 -10 -630 O ATOM 323 CB SER A 47 61.954 -2.977 28.140 1.00 79.45 C ANISOU 323 CB SER A 47 9181 11945 9060 -25 5 -661 C ATOM 324 OG SER A 47 62.587 -2.729 29.395 1.00 82.14 O ANISOU 324 OG SER A 47 9465 12407 9338 -33 7 -706 O ATOM 325 N LEU A 48 61.860 -6.033 28.821 1.00 76.10 N ANISOU 325 N LEU A 48 8759 11556 8599 67 -13 -569 N ATOM 326 CA LEU A 48 62.009 -7.118 29.785 1.00 82.01 C ANISOU 326 CA LEU A 48 9484 12375 9302 104 -18 -545 C ATOM 327 C LEU A 48 62.830 -8.300 29.245 1.00 87.20 C ANISOU 327 C LEU A 48 9854 13071 10207 149 -25 -498 C ATOM 328 O LEU A 48 63.537 -8.969 29.995 1.00 87.90 O ANISOU 328 O LEU A 48 10115 13296 9987 186 56 -561 O ATOM 329 CB LEU A 48 60.635 -7.615 30.231 1.00 83.20 C ANISOU 329 CB LEU A 48 9417 12456 9740 129 -20 -437 C ATOM 330 CG LEU A 48 60.672 -8.355 31.567 1.00 86.29 C ANISOU 330 CG LEU A 48 10036 12926 9825 148 -21 -459 C ATOM 331 CD1 LEU A 48 61.104 -7.389 32.660 1.00 89.42 C ANISOU 331 CD1 LEU A 48 10382 13423 10169 129 -20 -507 C ATOM 332 CD2 LEU A 48 59.333 -8.998 31.902 1.00 79.46 C ANISOU 332 CD2 LEU A 48 9211 11984 8995 161 -21 -394 C ATOM 333 N ALA A 49 62.719 -8.565 27.947 1.00 87.45 N ANISOU 333 N ALA A 49 10199 13011 10018 134 -23 -529 N ATOM 334 CA ALA A 49 63.419 -9.686 27.334 1.00 80.98 C ANISOU 334 CA ALA A 49 9373 12212 9185 163 -28 -527 C ATOM 335 C ALA A 49 64.867 -9.338 27.100 1.00 90.04 C ANISOU 335 C ALA A 49 10392 13533 10286 177 35 -621 C ATOM 336 O ALA A 49 65.738 -10.183 27.284 1.00 97.91 O ANISOU 336 O ALA A 49 11265 14738 11200 223 15 -667 O ATOM 337 CB ALA A 49 62.772 -10.069 26.022 1.00 76.00 C ANISOU 337 CB ALA A 49 8797 11459 8619 158 -27 -490 C ATOM 338 N ALA A 50 65.126 -8.100 26.674 1.00 88.47 N ANISOU 338 N ALA A 50 10203 13303 10108 133 43 -665 N ATOM 339 CA ALA A 50 66.488 -7.680 26.340 1.00 75.86 C ANISOU 339 CA ALA A 50 8469 11914 8440 123 31 -784 C ATOM 340 C ALA A 50 67.273 -7.526 27.614 1.00 79.96 C ANISOU 340 C ALA A 50 8826 12705 8852 137 22 -868 C ATOM 341 O ALA A 50 68.453 -7.858 27.663 1.00 87.04 O ANISOU 341 O ALA A 50 9565 13849 9656 160 3 -969 O ATOM 342 CB ALA A 50 66.499 -6.389 25.535 1.00 62.95 C ANISOU 342 CB ALA A 50 6890 10170 6859 66 45 -809 C ATOM 343 N ALA A 51 66.605 -7.048 28.658 1.00 80.22 N ANISOU 343 N ALA A 51 8886 12702 8889 126 34 -833 N ATOM 344 CA ALA A 51 67.212 -7.021 29.982 1.00 81.56 C ANISOU 344 CA ALA A 51 8903 13136 8951 144 23 -902 C ATOM 345 C ALA A 51 67.458 -8.435 30.524 1.00 87.13 C ANISOU 345 C ALA A 51 9526 13999 9581 222 0 -882 C ATOM 346 O ALA A 51 68.200 -8.601 31.480 1.00 94.35 O ANISOU 346 O ALA A 51 10281 15187 10381 256 -19 -951 O ATOM 347 CB ALA A 51 66.377 -6.195 30.953 1.00 77.21 C ANISOU 347 CB ALA A 51 8403 12506 8426 114 43 -866 C ATOM 348 N ASP A 52 66.819 -9.448 29.937 1.00 90.06 N ANISOU 348 N ASP A 52 10000 14209 10011 252 1 -791 N ATOM 349 CA ASP A 52 67.143 -10.847 30.251 1.00 96.04 C ANISOU 349 CA ASP A 52 10677 15118 10696 331 -21 -774 C ATOM 350 C ASP A 52 68.164 -11.465 29.288 1.00 97.51 C ANISOU 350 C ASP A 52 10782 15427 10840 367 -43 -835 C ATOM 351 O ASP A 52 68.679 -12.555 29.539 1.00102.49 O ANISOU 351 O ASP A 52 11314 16240 11389 447 -66 -842 O ATOM 352 CB ASP A 52 65.880 -11.725 30.291 1.00102.32 C ANISOU 352 CB ASP A 52 11611 15697 11569 344 -7 -648 C ATOM 353 CG ASP A 52 65.035 -11.497 31.540 1.00110.74 C ANISOU 353 CG ASP A 52 12704 16730 12641 337 7 -601 C ATOM 354 OD1 ASP A 52 65.610 -11.277 32.629 1.00114.71 O ANISOU 354 OD1 ASP A 52 13072 17470 13043 363 -6 -653 O ATOM 355 OD2 ASP A 52 63.788 -11.544 31.433 1.00109.57 O ANISOU 355 OD2 ASP A 52 12706 16330 12597 306 29 -518 O ATOM 356 N ILE A 53 68.442 -10.787 28.178 1.00 93.30 N ANISOU 356 N ILE A 53 10288 14801 10361 315 -36 -879 N ATOM 357 CA ILE A 53 69.465 -11.261 27.249 1.00 91.77 C ANISOU 357 CA ILE A 53 10004 14736 10128 342 -55 -957 C ATOM 358 C ILE A 53 70.834 -10.818 27.742 1.00101.72 C ANISOU 358 C ILE A 53 11059 16315 11277 355 -77 -1109 C ATOM 359 O ILE A 53 71.824 -11.534 27.593 1.00111.05 O ANISOU 359 O ILE A 53 12111 17538 12545 394 -152 -1106 O ATOM 360 CB ILE A 53 69.212 -10.790 25.798 1.00 78.95 C ANISOU 360 CB ILE A 53 8499 12890 8608 282 -40 -945 C ATOM 361 CG1 ILE A 53 67.816 -11.237 25.343 1.00 83.34 C ANISOU 361 CG1 ILE A 53 9250 13142 9275 269 -23 -802 C ATOM 362 CG2 ILE A 53 70.290 -11.321 24.857 1.00 58.24 C ANISOU 362 CG2 ILE A 53 5772 10414 5944 310 -60 -1036 C ATOM 363 CD1 ILE A 53 67.514 -10.982 23.877 1.00 82.79 C ANISOU 363 CD1 ILE A 53 9291 12868 9295 227 -14 -778 C ATOM 364 N ALA A 54 70.883 -9.633 28.344 1.00 96.99 N ANISOU 364 N ALA A 54 10434 15753 10663 297 -62 -1162 N ATOM 365 CA ALA A 54 72.130 -9.136 28.902 1.00 91.01 C ANISOU 365 CA ALA A 54 9487 15168 9927 278 -121 -1253 C ATOM 366 C ALA A 54 72.659 -10.146 29.917 1.00 93.47 C ANISOU 366 C ALA A 54 9663 15575 10277 354 -213 -1192 C ATOM 367 O ALA A 54 73.847 -10.469 29.916 1.00100.00 O ANISOU 367 O ALA A 54 10325 16485 11185 374 -300 -1221 O ATOM 368 CB ALA A 54 71.932 -7.761 29.533 1.00 79.48 C ANISOU 368 CB ALA A 54 8027 13766 8405 207 -76 -1326 C ATOM 369 N VAL A 55 71.758 -10.661 30.751 1.00 86.66 N ANISOU 369 N VAL A 55 8868 14698 9362 398 -196 -1106 N ATOM 370 CA VAL A 55 72.085 -11.642 31.789 1.00 87.82 C ANISOU 370 CA VAL A 55 8907 14925 9534 477 -284 -1035 C ATOM 371 C VAL A 55 72.771 -12.892 31.257 1.00 96.18 C ANISOU 371 C VAL A 55 9895 15967 10683 550 -357 -988 C ATOM 372 O VAL A 55 73.712 -13.399 31.868 1.00100.84 O ANISOU 372 O VAL A 55 10321 16664 11330 604 -464 -978 O ATOM 373 CB VAL A 55 70.826 -12.112 32.532 1.00 81.70 C ANISOU 373 CB VAL A 55 8246 14104 8693 511 -234 -942 C ATOM 374 CG1 VAL A 55 71.098 -13.413 33.259 1.00 83.25 C ANISOU 374 CG1 VAL A 55 8359 14343 8928 605 -324 -853 C ATOM 375 CG2 VAL A 55 70.355 -11.056 33.500 1.00 78.33 C ANISOU 375 CG2 VAL A 55 7825 13739 8196 461 -195 -976 C ATOM 376 N GLY A 56 72.269 -13.409 30.141 1.00 96.38 N ANISOU 376 N GLY A 56 10041 15859 10722 555 -303 -955 N ATOM 377 CA GLY A 56 72.877 -14.560 29.499 1.00 95.61 C ANISOU 377 CA GLY A 56 9881 15729 10716 618 -360 -913 C ATOM 378 C GLY A 56 74.192 -14.173 28.850 1.00 92.45 C ANISOU 378 C GLY A 56 9334 15387 10404 595 -410 -1001 C ATOM 379 O GLY A 56 75.172 -14.908 28.956 1.00 92.17 O ANISOU 379 O GLY A 56 9143 15418 10460 657 -500 -986 O ATOM 380 N VAL A 57 74.214 -13.014 28.191 1.00 88.84 N ANISOU 380 N VAL A 57 8921 14910 9924 506 -353 -1093 N ATOM 381 CA VAL A 57 75.413 -12.550 27.496 1.00 98.69 C ANISOU 381 CA VAL A 57 10033 16208 11256 467 -385 -1187 C ATOM 382 C VAL A 57 76.474 -11.987 28.438 1.00102.36 C ANISOU 382 C VAL A 57 10300 16845 11748 453 -462 -1254 C ATOM 383 O VAL A 57 77.665 -12.247 28.260 1.00101.06 O ANISOU 383 O VAL A 57 9955 16759 11683 472 -534 -1290 O ATOM 384 CB VAL A 57 75.102 -11.468 26.431 1.00 97.84 C ANISOU 384 CB VAL A 57 10038 16018 11119 373 -299 -1267 C ATOM 385 CG1 VAL A 57 76.400 -11.027 25.725 1.00 94.75 C ANISOU 385 CG1 VAL A 57 9490 15683 10827 329 -329 -1367 C ATOM 386 CG2 VAL A 57 74.080 -11.975 25.426 1.00 91.76 C ANISOU 386 CG2 VAL A 57 9458 15086 10321 382 -237 -1207 C ATOM 387 N LEU A 58 76.040 -11.217 29.433 1.00102.31 N ANISOU 387 N LEU A 58 10319 16900 11656 417 -447 -1272 N ATOM 388 CA LEU A 58 76.974 -10.498 30.298 1.00103.23 C ANISOU 388 CA LEU A 58 10257 17181 11784 382 -515 -1351 C ATOM 389 C LEU A 58 77.111 -11.061 31.718 1.00104.60 C ANISOU 389 C LEU A 58 10333 17470 11941 451 -612 -1290 C ATOM 390 O LEU A 58 78.162 -11.584 32.084 1.00108.17 O ANISOU 390 O LEU A 58 10600 18035 12466 502 -726 -1291 O ATOM 391 CB LEU A 58 76.621 -9.006 30.342 1.00 98.21 C ANISOU 391 CB LEU A 58 9686 16551 11077 272 -437 -1444 C ATOM 392 CG LEU A 58 76.742 -8.282 28.999 1.00 96.04 C ANISOU 392 CG LEU A 58 9471 16193 10828 195 -362 -1525 C ATOM 393 CD1 LEU A 58 76.223 -6.851 29.092 1.00 94.83 C ANISOU 393 CD1 LEU A 58 9405 16031 10597 97 -278 -1602 C ATOM 394 CD2 LEU A 58 78.185 -8.312 28.515 1.00 93.94 C ANISOU 394 CD2 LEU A 58 9005 16011 10676 176 -425 -1602 C ATOM 395 N ALA A 59 76.044 -10.963 32.505 1.00102.59 N ANISOU 395 N ALA A 59 10198 17188 11592 456 -571 -1236 N ATOM 396 CA ALA A 59 76.123 -11.189 33.951 1.00104.29 C ANISOU 396 CA ALA A 59 10326 17524 11777 499 -658 -1196 C ATOM 397 C ALA A 59 76.473 -12.608 34.422 1.00109.58 C ANISOU 397 C ALA A 59 10912 18227 12495 621 -767 -1096 C ATOM 398 O ALA A 59 76.960 -12.777 35.534 1.00117.27 O ANISOU 398 O ALA A 59 11760 19333 13465 661 -879 -1082 O ATOM 399 CB ALA A 59 74.854 -10.698 34.634 1.00100.10 C ANISOU 399 CB ALA A 59 9942 16950 11141 470 -576 -1165 C ATOM 400 N ILE A 60 76.179 -13.630 33.626 1.00109.03 N ANISOU 400 N ILE A 60 10919 18039 12469 682 -740 -1024 N ATOM 401 CA ILE A 60 76.627 -14.981 33.972 1.00114.29 C ANISOU 401 CA ILE A 60 11493 18735 13197 802 -845 -934 C ATOM 402 C ILE A 60 78.135 -15.156 33.790 1.00120.84 C ANISOU 402 C ILE A 60 12100 19681 14133 835 -960 -983 C ATOM 403 O ILE A 60 78.826 -15.599 34.715 1.00129.65 O ANISOU 403 O ILE A 60 13063 20925 15273 907 -1091 -955 O ATOM 404 CB ILE A 60 75.842 -16.078 33.231 1.00117.93 C ANISOU 404 CB ILE A 60 12095 19037 13675 857 -782 -840 C ATOM 405 CG1 ILE A 60 74.468 -16.269 33.893 1.00118.26 C ANISOU 405 CG1 ILE A 60 12301 19011 13622 862 -715 -763 C ATOM 406 CG2 ILE A 60 76.641 -17.374 33.226 1.00118.62 C ANISOU 406 CG2 ILE A 60 12055 19154 13863 975 -889 -773 C ATOM 407 CD1 ILE A 60 73.461 -17.058 33.067 1.00112.78 C ANISOU 407 CD1 ILE A 60 11777 18150 12924 877 -622 -691 C ATOM 408 N PRO A 61 78.657 -14.811 32.596 1.00110.70 N ANISOU 408 N PRO A 61 10788 18355 12916 784 -915 -1055 N ATOM 409 CA PRO A 61 80.121 -14.780 32.482 1.00104.69 C ANISOU 409 CA PRO A 61 9794 17723 12259 798 -1016 -1119 C ATOM 410 C PRO A 61 80.742 -13.923 33.597 1.00101.90 C ANISOU 410 C PRO A 61 9295 17552 11870 756 -1102 -1190 C ATOM 411 O PRO A 61 81.843 -14.216 34.045 1.00105.77 O ANISOU 411 O PRO A 61 9575 18184 12428 807 -1232 -1204 O ATOM 412 CB PRO A 61 80.348 -14.152 31.103 1.00 94.98 C ANISOU 412 CB PRO A 61 8593 16417 11078 712 -922 -1206 C ATOM 413 CG PRO A 61 79.136 -14.535 30.325 1.00 91.82 C ANISOU 413 CG PRO A 61 8425 15828 10635 711 -809 -1142 C ATOM 414 CD PRO A 61 77.994 -14.556 31.303 1.00 95.64 C ANISOU 414 CD PRO A 61 9048 16289 11003 723 -784 -1074 C ATOM 415 N PHE A 62 80.028 -12.887 34.038 1.00 93.72 N ANISOU 415 N PHE A 62 8367 16513 10730 665 -1035 -1234 N ATOM 416 CA PHE A 62 80.452 -12.054 35.157 1.00 90.16 C ANISOU 416 CA PHE A 62 7800 16224 10231 615 -1110 -1299 C ATOM 417 C PHE A 62 80.343 -12.822 36.474 1.00 98.10 C ANISOU 417 C PHE A 62 8761 17313 11199 714 -1229 -1205 C ATOM 418 O PHE A 62 81.202 -12.710 37.345 1.00109.74 O ANISOU 418 O PHE A 62 10057 18957 12683 729 -1366 -1235 O ATOM 419 CB PHE A 62 79.591 -10.786 35.256 1.00 87.80 C ANISOU 419 CB PHE A 62 7644 15882 9833 497 -993 -1360 C ATOM 420 CG PHE A 62 79.978 -9.680 34.293 1.00 94.03 C ANISOU 420 CG PHE A 62 8424 16655 10650 380 -911 -1486 C ATOM 421 CD1 PHE A 62 80.700 -9.942 33.139 1.00 98.33 C ANISOU 421 CD1 PHE A 62 8904 17164 11294 382 -902 -1520 C ATOM 422 CD2 PHE A 62 79.612 -8.362 34.559 1.00 95.02 C ANISOU 422 CD2 PHE A 62 8603 16797 10701 267 -841 -1569 C ATOM 423 CE1 PHE A 62 81.044 -8.908 32.270 1.00 99.03 C ANISOU 423 CE1 PHE A 62 8986 17235 11406 271 -826 -1637 C ATOM 424 CE2 PHE A 62 79.954 -7.328 33.699 1.00 93.81 C ANISOU 424 CE2 PHE A 62 8446 16627 10572 158 -765 -1685 C ATOM 425 CZ PHE A 62 80.669 -7.601 32.556 1.00 96.96 C ANISOU 425 CZ PHE A 62 8783 16990 11067 159 -758 -1719 C ATOM 426 N ALA A 63 79.267 -13.586 36.623 1.00 98.59 N ANISOU 426 N ALA A 63 8987 17256 11215 778 -1180 -1093 N ATOM 427 CA ALA A 63 78.974 -14.275 37.879 1.00 97.90 C ANISOU 427 CA ALA A 63 8890 17227 11079 865 -1277 -999 C ATOM 428 C ALA A 63 79.764 -15.562 38.044 1.00104.53 C ANISOU 428 C ALA A 63 9595 18120 12000 1004 -1415 -921 C ATOM 429 O ALA A 63 80.005 -15.995 39.164 1.00111.82 O ANISOU 429 O ALA A 63 10438 19151 12898 1078 -1547 -869 O ATOM 430 CB ALA A 63 77.478 -14.555 38.008 1.00 89.78 C ANISOU 430 CB ALA A 63 8083 16055 9973 871 -1162 -915 C ATOM 431 N ILE A 64 80.141 -16.192 36.935 1.00102.85 N ANISOU 431 N ILE A 64 9363 17829 11884 1043 -1387 -909 N ATOM 432 CA ILE A 64 80.911 -17.430 37.013 1.00107.26 C ANISOU 432 CA ILE A 64 9788 18432 12534 1183 -1511 -834 C ATOM 433 C ILE A 64 82.389 -17.102 37.275 1.00118.71 C ANISOU 433 C ILE A 64 10978 20071 14055 1191 -1652 -911 C ATOM 434 O ILE A 64 83.125 -17.870 37.914 1.00117.05 O ANISOU 434 O ILE A 64 10615 19970 13889 1308 -1806 -857 O ATOM 435 CB ILE A 64 80.731 -18.289 35.745 1.00 98.61 C ANISOU 435 CB ILE A 64 8766 17179 11524 1226 -1428 -786 C ATOM 436 CG1 ILE A 64 80.345 -19.716 36.128 1.00 99.45 C ANISOU 436 CG1 ILE A 64 8917 17228 11643 1366 -1478 -646 C ATOM 437 CG2 ILE A 64 81.987 -18.278 34.885 1.00 99.51 C ANISOU 437 CG2 ILE A 64 8696 17346 11767 1231 -1467 -853 C ATOM 438 CD1 ILE A 64 80.392 -20.678 34.969 1.00101.97 C ANISOU 438 CD1 ILE A 64 9262 17417 12063 1424 -1427 -599 C ATOM 439 N THR A 65 82.783 -15.925 36.791 1.00121.65 N ANISOU 439 N THR A 65 11303 20483 14434 1063 -1597 -1039 N ATOM 440 CA THR A 65 84.129 -15.372 36.926 1.00116.24 C ANISOU 440 CA THR A 65 10374 19978 13814 1031 -1703 -1141 C ATOM 441 C THR A 65 84.382 -14.828 38.332 1.00116.83 C ANISOU 441 C THR A 65 10354 20229 13807 1012 -1830 -1169 C ATOM 442 O THR A 65 85.501 -14.914 38.858 1.00113.64 O ANISOU 442 O THR A 65 9725 20003 13452 1052 -1986 -1199 O ATOM 443 CB THR A 65 84.347 -14.242 35.888 1.00103.11 C ANISOU 443 CB THR A 65 8716 18281 12179 886 -1582 -1273 C ATOM 444 OG1 THR A 65 84.831 -14.804 34.662 1.00100.49 O ANISOU 444 OG1 THR A 65 8338 17873 11969 920 -1541 -1272 O ATOM 445 CG2 THR A 65 85.334 -13.210 36.395 1.00101.42 C ANISOU 445 CG2 THR A 65 8305 18259 11969 796 -1663 -1401 C ATOM 446 N ILE A 66 83.339 -14.266 38.937 1.00114.13 N ANISOU 446 N ILE A 66 10179 19843 13344 950 -1764 -1161 N ATOM 447 CA ILE A 66 83.443 -13.775 40.302 1.00118.76 C ANISOU 447 CA ILE A 66 10700 20582 13843 929 -1880 -1180 C ATOM 448 C ILE A 66 83.629 -14.945 41.273 1.00129.39 C ANISOU 448 C ILE A 66 11981 22000 15181 1086 -2047 -1059 C ATOM 449 O ILE A 66 84.082 -14.755 42.401 1.00135.52 O ANISOU 449 O ILE A 66 12644 22941 15908 1098 -2199 -1070 O ATOM 450 CB ILE A 66 82.221 -12.919 40.705 1.00109.69 C ANISOU 450 CB ILE A 66 9747 19358 12572 829 -1760 -1193 C ATOM 451 CG1 ILE A 66 82.552 -12.043 41.914 1.00100.48 C ANISOU 451 CG1 ILE A 66 8481 18367 11329 760 -1867 -1262 C ATOM 452 CG2 ILE A 66 81.010 -13.794 40.986 1.00111.07 C ANISOU 452 CG2 ILE A 66 10114 19396 12692 913 -1708 -1057 C ATOM 453 CD1 ILE A 66 83.616 -11.009 41.643 1.00 92.55 C ANISOU 453 CD1 ILE A 66 7302 17493 10368 645 -1895 -1413 C ATOM 454 N SER A 67 83.303 -16.155 40.822 1.00129.97 N ANISOU 454 N SER A 67 12128 21951 15303 1205 -2024 -945 N ATOM 455 CA SER A 67 83.481 -17.354 41.643 1.00134.44 C ANISOU 455 CA SER A 67 12642 22569 15871 1368 -2177 -822 C ATOM 456 C SER A 67 84.957 -17.698 41.892 1.00144.90 C ANISOU 456 C SER A 67 13696 24078 17283 1453 -2368 -841 C ATOM 457 O SER A 67 85.274 -18.478 42.793 1.00152.06 O ANISOU 457 O SER A 67 14526 25075 18174 1583 -2533 -754 O ATOM 458 CB SER A 67 82.765 -18.555 41.017 1.00128.85 C ANISOU 458 CB SER A 67 12079 21677 15201 1467 -2093 -702 C ATOM 459 OG SER A 67 82.984 -19.734 41.779 1.00127.39 O ANISOU 459 OG SER A 67 11842 21538 15022 1632 -2241 -582 O ATOM 460 N THR A 68 85.851 -17.120 41.091 1.00142.47 N ANISOU 460 N THR A 68 13241 23825 17065 1382 -2348 -952 N ATOM 461 CA THR A 68 87.284 -17.384 41.214 1.00138.43 C ANISOU 461 CA THR A 68 12452 23492 16653 1453 -2516 -982 C ATOM 462 C THR A 68 87.920 -16.590 42.338 1.00137.31 C ANISOU 462 C THR A 68 12156 23571 16445 1398 -2671 -1059 C ATOM 463 O THR A 68 88.776 -17.096 43.052 1.00137.13 O ANISOU 463 O THR A 68 11947 23710 16446 1505 -2867 -1026 O ATOM 464 CB THR A 68 88.034 -17.008 39.935 1.00134.86 C ANISOU 464 CB THR A 68 11885 23026 16329 1385 -2432 -1083 C ATOM 465 OG1 THR A 68 87.280 -17.436 38.793 1.00129.73 O ANISOU 465 OG1 THR A 68 11416 22156 15717 1386 -2257 -1039 O ATOM 466 CG2 THR A 68 89.434 -17.637 39.929 1.00135.92 C ANISOU 466 CG2 THR A 68 11734 23314 16594 1499 -2594 -1081 C ATOM 467 N GLY A 69 87.486 -15.342 42.487 1.00139.01 N ANISOU 467 N GLY A 69 12449 23792 16576 1232 -2584 -1161 N ATOM 468 CA GLY A 69 88.110 -14.407 43.407 1.00144.01 C ANISOU 468 CA GLY A 69 12935 24632 17151 1144 -2709 -1262 C ATOM 469 C GLY A 69 89.403 -13.810 42.880 1.00146.13 C ANISOU 469 C GLY A 69 12956 25041 17524 1071 -2750 -1397 C ATOM 470 O GLY A 69 90.409 -13.747 43.596 1.00150.70 O ANISOU 470 O GLY A 69 13310 25833 18116 1093 -2938 -1437 O ATOM 471 N PHE A 70 89.369 -13.358 41.627 1.00142.07 N ANISOU 471 N PHE A 70 12484 24413 17083 980 -2577 -1470 N ATOM 472 CA PHE A 70 90.543 -12.786 40.971 1.00144.69 C ANISOU 472 CA PHE A 70 12592 24857 17525 900 -2586 -1603 C ATOM 473 C PHE A 70 90.892 -11.393 41.505 1.00148.89 C ANISOU 473 C PHE A 70 13039 25537 17994 724 -2608 -1756 C ATOM 474 O PHE A 70 90.255 -10.894 42.430 1.00153.29 O ANISOU 474 O PHE A 70 13704 26118 18423 672 -2629 -1755 O ATOM 475 CB PHE A 70 90.336 -12.729 39.454 1.00136.90 C ANISOU 475 CB PHE A 70 11698 23691 16628 854 -2389 -1631 C ATOM 476 CG PHE A 70 89.681 -11.462 38.974 1.00129.07 C ANISOU 476 CG PHE A 70 10865 22605 15571 673 -2212 -1734 C ATOM 477 CD1 PHE A 70 88.653 -10.871 39.697 1.00124.45 C ANISOU 477 CD1 PHE A 70 10466 21976 14843 609 -2166 -1724 C ATOM 478 CD2 PHE A 70 90.101 -10.859 37.798 1.00126.32 C ANISOU 478 CD2 PHE A 70 10475 22212 15308 570 -2091 -1841 C ATOM 479 CE1 PHE A 70 88.055 -9.704 39.256 1.00119.85 C ANISOU 479 CE1 PHE A 70 10025 21307 14206 454 -2003 -1815 C ATOM 480 CE2 PHE A 70 89.508 -9.694 37.352 1.00123.53 C ANISOU 480 CE2 PHE A 70 10271 21771 14894 412 -1932 -1932 C ATOM 481 CZ PHE A 70 88.482 -9.115 38.084 1.00120.83 C ANISOU 481 CZ PHE A 70 10112 21386 14411 357 -1889 -1918 C ATOM 482 N CYS A 71 91.909 -10.772 40.915 1.00146.31 N ANISOU 482 N CYS A 71 12517 25312 17763 628 -2602 -1890 N ATOM 483 CA CYS A 71 92.337 -9.439 41.325 1.00141.97 C ANISOU 483 CA CYS A 71 11868 24906 17168 449 -2616 -2050 C ATOM 484 C CYS A 71 91.973 -8.397 40.278 1.00133.91 C ANISOU 484 C CYS A 71 10968 23754 16158 284 -2397 -2159 C ATOM 485 O CYS A 71 92.002 -8.670 39.075 1.00135.87 O ANISOU 485 O CYS A 71 11251 23872 16500 299 -2277 -2152 O ATOM 486 CB CYS A 71 93.850 -9.412 41.568 1.00145.54 C ANISOU 486 CB CYS A 71 11979 25603 17716 446 -2788 -2139 C ATOM 487 SG CYS A 71 94.435 -10.627 42.772 1.00148.11 S ANISOU 487 SG CYS A 71 12131 26107 18037 652 -3071 -2015 S ATOM 488 N ALA A 72 91.655 -7.194 40.739 1.00124.46 N ANISOU 488 N ALA A 72 9831 22592 14864 126 -2351 -2259 N ATOM 489 CA ALA A 72 91.419 -6.082 39.835 1.00119.28 C ANISOU 489 CA ALA A 72 9267 21837 14215 -40 -2159 -2377 C ATOM 490 C ALA A 72 91.156 -4.797 40.603 1.00119.78 C ANISOU 490 C ALA A 72 9368 21974 14168 -205 -2144 -2484 C ATOM 491 O ALA A 72 90.811 -4.826 41.786 1.00111.60 O ANISOU 491 O ALA A 72 8358 21013 13030 -181 -2251 -2441 O ATOM 492 CB ALA A 72 90.260 -6.388 38.907 1.00114.56 C ANISOU 492 CB ALA A 72 8945 20978 13604 4 -1974 -2285 C ATOM 493 N ALA A 73 91.313 -3.674 39.908 1.00128.29 N ANISOU 493 N ALA A 73 10451 23025 15268 -373 -2007 -2624 N ATOM 494 CA ALA A 73 91.175 -2.351 40.505 1.00131.75 C ANISOU 494 CA ALA A 73 10908 23533 15619 -550 -1976 -2748 C ATOM 495 C ALA A 73 89.788 -2.181 41.094 1.00132.12 C ANISOU 495 C ALA A 73 11215 23454 15531 -534 -1910 -2661 C ATOM 496 O ALA A 73 88.792 -2.442 40.418 1.00129.77 O ANISOU 496 O ALA A 73 11140 22949 15219 -478 -1767 -2573 O ATOM 497 CB ALA A 73 91.444 -1.274 39.465 1.00129.68 C ANISOU 497 CB ALA A 73 10646 23216 15410 -719 -1810 -2895 C ATOM 498 N CYS A 74 89.729 -1.725 42.342 1.00134.77 N ANISOU 498 N CYS A 74 11517 23919 15769 -589 -2015 -2690 N ATOM 499 CA CYS A 74 88.468 -1.614 43.070 1.00136.76 C ANISOU 499 CA CYS A 74 11990 24078 15896 -569 -1975 -2605 C ATOM 500 C CYS A 74 87.347 -0.940 42.262 1.00141.77 C ANISOU 500 C CYS A 74 12873 24493 16501 -633 -1739 -2605 C ATOM 501 O CYS A 74 86.214 -1.432 42.240 1.00140.29 O ANISOU 501 O CYS A 74 12892 24149 16265 -537 -1666 -2477 O ATOM 502 CB CYS A 74 88.680 -0.884 44.403 1.00135.45 C ANISOU 502 CB CYS A 74 11740 24090 15635 -674 -2100 -2683 C ATOM 503 SG CYS A 74 87.146 -0.495 45.317 1.00157.32 S ANISOU 503 SG CYS A 74 14769 26751 18253 -686 -2032 -2607 S ATOM 504 N HIS A 75 87.661 0.169 41.592 1.00145.31 N ANISOU 504 N HIS A 75 13299 24930 16980 -793 -1622 -2748 N ATOM 505 CA HIS A 75 86.645 0.940 40.862 1.00143.51 C ANISOU 505 CA HIS A 75 13299 24509 16720 -862 -1408 -2759 C ATOM 506 C HIS A 75 86.244 0.370 39.493 1.00142.74 C ANISOU 506 C HIS A 75 13331 24217 16688 -775 -1278 -2687 C ATOM 507 O HIS A 75 85.151 0.652 38.995 1.00136.50 O ANISOU 507 O HIS A 75 12763 23247 15855 -774 -1126 -2642 O ATOM 508 CB HIS A 75 87.048 2.414 40.755 1.00142.47 C ANISOU 508 CB HIS A 75 13114 24435 16583 -1075 -1331 -2939 C ATOM 509 CG HIS A 75 86.839 3.184 42.023 1.00142.24 C ANISOU 509 CG HIS A 75 13077 24516 16454 -1176 -1390 -2993 C ATOM 510 ND1 HIS A 75 87.836 3.926 42.619 1.00147.32 N ANISOU 510 ND1 HIS A 75 13522 25356 17098 -1325 -1485 -3144 N ATOM 511 CD2 HIS A 75 85.745 3.320 42.811 1.00136.32 C ANISOU 511 CD2 HIS A 75 12488 23706 15600 -1155 -1369 -2917 C ATOM 512 CE1 HIS A 75 87.366 4.486 43.720 1.00146.06 C ANISOU 512 CE1 HIS A 75 13411 25251 16834 -1392 -1524 -3160 C ATOM 513 NE2 HIS A 75 86.100 4.135 43.859 1.00140.28 N ANISOU 513 NE2 HIS A 75 12895 24365 16040 -1289 -1453 -3022 N ATOM 514 N GLY A 76 87.123 -0.428 38.892 1.00146.99 N ANISOU 514 N GLY A 76 13727 24793 17330 -703 -1343 -2677 N ATOM 515 CA GLY A 76 86.762 -1.181 37.701 1.00143.76 C ANISOU 515 CA GLY A 76 13434 24209 16981 -602 -1250 -2591 C ATOM 516 C GLY A 76 86.173 -2.527 38.087 1.00136.95 C ANISOU 516 C GLY A 76 12650 23289 16097 -417 -1322 -2416 C ATOM 517 O GLY A 76 85.426 -3.141 37.328 1.00126.93 O ANISOU 517 O GLY A 76 11548 21843 14835 -331 -1231 -2319 O ATOM 518 N CYS A 77 86.513 -2.971 39.292 1.00142.71 N ANISOU 518 N CYS A 77 13257 24171 16794 -363 -1491 -2380 N ATOM 519 CA CYS A 77 86.055 -4.248 39.827 1.00146.86 C ANISOU 519 CA CYS A 77 13836 24667 17298 -191 -1579 -2219 C ATOM 520 C CYS A 77 84.583 -4.183 40.242 1.00141.58 C ANISOU 520 C CYS A 77 13415 23861 16520 -169 -1486 -2128 C ATOM 521 O CYS A 77 83.835 -5.152 40.073 1.00138.41 O ANISOU 521 O CYS A 77 13148 23333 16110 -44 -1459 -1994 O ATOM 522 CB CYS A 77 86.933 -4.656 41.021 1.00154.01 C ANISOU 522 CB CYS A 77 14525 25793 18199 -146 -1801 -2218 C ATOM 523 SG CYS A 77 86.621 -6.300 41.723 1.00158.45 S ANISOU 523 SG CYS A 77 15111 26346 18746 73 -1941 -2026 S ATOM 524 N LEU A 78 84.174 -3.039 40.784 1.00138.50 N ANISOU 524 N LEU A 78 13079 23497 16050 -294 -1435 -2203 N ATOM 525 CA LEU A 78 82.788 -2.846 41.203 1.00132.06 C ANISOU 525 CA LEU A 78 12481 22560 15137 -285 -1340 -2128 C ATOM 526 C LEU A 78 81.832 -2.936 40.019 1.00124.81 C ANISOU 526 C LEU A 78 11773 21419 14231 -258 -1155 -2075 C ATOM 527 O LEU A 78 80.646 -3.184 40.201 1.00122.16 O ANISOU 527 O LEU A 78 11618 20963 13836 -206 -1081 -1978 O ATOM 528 CB LEU A 78 82.601 -1.510 41.931 1.00131.19 C ANISOU 528 CB LEU A 78 12375 22522 14951 -436 -1313 -2232 C ATOM 529 CG LEU A 78 82.318 -1.547 43.440 1.00129.02 C ANISOU 529 CG LEU A 78 12082 22355 14584 -425 -1435 -2194 C ATOM 530 CD1 LEU A 78 81.805 -2.917 43.874 1.00124.35 C ANISOU 530 CD1 LEU A 78 11553 21719 13977 -252 -1508 -2028 C ATOM 531 CD2 LEU A 78 83.547 -1.157 44.254 1.00131.90 C ANISOU 531 CD2 LEU A 78 12214 22953 14947 -504 -1610 -2303 C ATOM 532 N PHE A 79 82.350 -2.743 38.810 1.00122.97 N ANISOU 532 N PHE A 79 11513 21134 14075 -296 -1086 -2140 N ATOM 533 CA PHE A 79 81.528 -2.844 37.609 1.00116.21 C ANISOU 533 CA PHE A 79 10851 20073 13230 -272 -929 -2096 C ATOM 534 C PHE A 79 81.112 -4.289 37.297 1.00110.29 C ANISOU 534 C PHE A 79 10178 19222 12506 -114 -949 -1949 C ATOM 535 O PHE A 79 79.977 -4.538 36.897 1.00104.02 O ANISOU 535 O PHE A 79 9584 18266 11672 -72 -842 -1868 O ATOM 536 CB PHE A 79 82.237 -2.206 36.405 1.00119.52 C ANISOU 536 CB PHE A 79 11219 20468 13724 -363 -857 -2212 C ATOM 537 CG PHE A 79 81.341 -2.018 35.202 1.00119.71 C ANISOU 537 CG PHE A 79 11456 20287 13740 -366 -694 -2187 C ATOM 538 CD1 PHE A 79 81.264 -0.788 34.565 1.00119.38 C ANISOU 538 CD1 PHE A 79 11471 20197 13691 -494 -578 -2296 C ATOM 539 CD2 PHE A 79 80.580 -3.074 34.705 1.00113.40 C ANISOU 539 CD2 PHE A 79 10800 19345 12941 -244 -664 -2057 C ATOM 540 CE1 PHE A 79 80.439 -0.618 33.467 1.00114.00 C ANISOU 540 CE1 PHE A 79 10985 19332 12997 -490 -444 -2271 C ATOM 541 CE2 PHE A 79 79.758 -2.909 33.611 1.00105.87 C ANISOU 541 CE2 PHE A 79 10039 18212 11974 -248 -530 -2036 C ATOM 542 CZ PHE A 79 79.685 -1.683 32.991 1.00107.11 C ANISOU 542 CZ PHE A 79 10251 18326 12120 -366 -426 -2141 C ATOM 543 N ILE A 80 82.026 -5.238 37.484 1.00114.94 N ANISOU 543 N ILE A 80 10602 19907 13161 -30 -1088 -1917 N ATOM 544 CA ILE A 80 81.782 -6.634 37.096 1.00113.67 C ANISOU 544 CA ILE A 80 10495 19654 13042 114 -1109 -1788 C ATOM 545 C ILE A 80 80.930 -7.435 38.090 1.00113.71 C ANISOU 545 C ILE A 80 10590 19639 12977 215 -1155 -1656 C ATOM 546 O ILE A 80 80.323 -8.439 37.718 1.00110.15 O ANISOU 546 O ILE A 80 10251 19065 12536 314 -1123 -1546 O ATOM 547 CB ILE A 80 83.103 -7.400 36.847 1.00108.85 C ANISOU 547 CB ILE A 80 9666 19149 12544 177 -1236 -1798 C ATOM 548 CG1 ILE A 80 84.166 -6.462 36.276 1.00109.40 C ANISOU 548 CG1 ILE A 80 9580 19307 12680 57 -1227 -1951 C ATOM 549 CG2 ILE A 80 82.869 -8.607 35.937 1.00 95.60 C ANISOU 549 CG2 ILE A 80 8064 17331 10930 291 -1205 -1695 C ATOM 550 CD1 ILE A 80 85.488 -6.500 37.030 1.00112.01 C ANISOU 550 CD1 ILE A 80 9635 19862 13061 54 -1399 -2013 C ATOM 551 N ALA A 81 80.927 -7.027 39.357 1.00117.14 N ANISOU 551 N ALA A 81 10967 20198 13344 188 -1237 -1671 N ATOM 552 CA ALA A 81 80.055 -7.643 40.364 1.00117.11 C ANISOU 552 CA ALA A 81 11056 20176 13266 267 -1272 -1555 C ATOM 553 C ALA A 81 78.619 -7.072 40.342 1.00119.25 C ANISOU 553 C ALA A 81 11547 20306 13457 220 -1111 -1530 C ATOM 554 O ALA A 81 77.624 -7.790 40.524 1.00114.00 O ANISOU 554 O ALA A 81 11019 19537 12758 296 -1068 -1417 O ATOM 555 CB ALA A 81 80.676 -7.511 41.755 1.00110.00 C ANISOU 555 CB ALA A 81 9997 19472 12325 264 -1445 -1577 C ATOM 556 N CYS A 82 78.544 -5.761 40.140 1.00118.49 N ANISOU 556 N CYS A 82 11472 20214 13335 91 -1024 -1638 N ATOM 557 CA CYS A 82 77.305 -4.997 40.220 1.00107.87 C ANISOU 557 CA CYS A 82 10302 18765 11918 33 -882 -1633 C ATOM 558 C CYS A 82 76.578 -4.716 38.912 1.00107.91 C ANISOU 558 C CYS A 82 10475 18590 11934 11 -710 -1635 C ATOM 559 O CYS A 82 75.691 -3.866 38.882 1.00116.42 O ANISOU 559 O CYS A 82 11677 19597 12961 -51 -592 -1655 O ATOM 560 CB CYS A 82 77.496 -3.722 41.035 1.00104.64 C ANISOU 560 CB CYS A 82 9826 18474 11460 -91 -898 -1738 C ATOM 561 SG CYS A 82 77.642 -4.070 42.809 1.00137.18 S ANISOU 561 SG CYS A 82 13845 22759 15519 -56 -1075 -1694 S ATOM 562 N PHE A 83 76.985 -5.338 37.814 1.00 99.85 N ANISOU 562 N PHE A 83 9455 17501 10981 56 -701 -1623 N ATOM 563 CA PHE A 83 76.194 -5.168 36.602 1.00 97.74 C ANISOU 563 CA PHE A 83 9366 17058 10712 44 -553 -1612 C ATOM 564 C PHE A 83 74.798 -5.832 36.694 1.00 93.11 C ANISOU 564 C PHE A 83 8964 16338 10074 118 -477 -1488 C ATOM 565 O PHE A 83 73.794 -5.271 36.231 1.00 79.55 O ANISOU 565 O PHE A 83 7406 14505 8314 83 -348 -1486 O ATOM 566 CB PHE A 83 76.945 -5.634 35.363 1.00103.13 C ANISOU 566 CB PHE A 83 10009 17696 11479 64 -561 -1634 C ATOM 567 CG PHE A 83 76.235 -5.302 34.091 1.00110.16 C ANISOU 567 CG PHE A 83 11074 18418 12362 36 -426 -1641 C ATOM 568 CD1 PHE A 83 76.122 -3.982 33.671 1.00114.36 C ANISOU 568 CD1 PHE A 83 11652 18929 12870 -73 -337 -1742 C ATOM 569 CD2 PHE A 83 75.651 -6.299 33.329 1.00111.88 C ANISOU 569 CD2 PHE A 83 11415 18502 12594 115 -391 -1548 C ATOM 570 CE1 PHE A 83 75.450 -3.659 32.499 1.00113.51 C ANISOU 570 CE1 PHE A 83 11710 18669 12750 -94 -225 -1746 C ATOM 571 CE2 PHE A 83 74.984 -5.989 32.157 1.00113.66 C ANISOU 571 CE2 PHE A 83 11802 18578 12805 88 -282 -1555 C ATOM 572 CZ PHE A 83 74.883 -4.664 31.739 1.00114.06 C ANISOU 572 CZ PHE A 83 11899 18610 12829 -13 -203 -1653 C ATOM 573 N VAL A 84 74.740 -7.014 37.302 1.00 98.18 N ANISOU 573 N VAL A 84 9579 17000 10723 218 -559 -1387 N ATOM 574 CA VAL A 84 73.466 -7.694 37.557 1.00 96.49 C ANISOU 574 CA VAL A 84 9517 16680 10465 282 -496 -1273 C ATOM 575 C VAL A 84 72.436 -6.799 38.268 1.00 93.94 C ANISOU 575 C VAL A 84 9280 16346 10066 225 -410 -1279 C ATOM 576 O VAL A 84 71.242 -6.873 37.982 1.00 93.07 O ANISOU 576 O VAL A 84 9328 16112 9923 237 -297 -1223 O ATOM 577 CB VAL A 84 73.671 -9.018 38.360 1.00107.03 C ANISOU 577 CB VAL A 84 10781 18068 11816 391 -616 -1172 C ATOM 578 CG1 VAL A 84 74.684 -8.825 39.474 1.00113.62 C ANISOU 578 CG1 VAL A 84 11427 19090 12653 386 -769 -1213 C ATOM 579 CG2 VAL A 84 72.345 -9.537 38.916 1.00100.47 C ANISOU 579 CG2 VAL A 84 10086 17155 10933 436 -553 -1067 C ATOM 580 N LEU A 85 72.902 -5.958 39.188 1.00 91.40 N ANISOU 580 N LEU A 85 8849 16157 9722 162 -468 -1348 N ATOM 581 CA LEU A 85 72.025 -5.030 39.896 1.00 90.32 C ANISOU 581 CA LEU A 85 8774 16021 9524 100 -394 -1364 C ATOM 582 C LEU A 85 71.328 -4.103 38.925 1.00 90.36 C ANISOU 582 C LEU A 85 8911 15905 9515 37 -238 -1409 C ATOM 583 O LEU A 85 70.168 -3.726 39.131 1.00 81.23 O ANISOU 583 O LEU A 85 7868 14676 8318 26 -136 -1376 O ATOM 584 CB LEU A 85 72.814 -4.180 40.890 1.00 90.34 C ANISOU 584 CB LEU A 85 8627 16191 9509 22 -490 -1452 C ATOM 585 CG LEU A 85 73.207 -4.842 42.207 1.00 88.54 C ANISOU 585 CG LEU A 85 8286 16092 9262 74 -649 -1404 C ATOM 586 CD1 LEU A 85 73.539 -3.768 43.218 1.00 87.87 C ANISOU 586 CD1 LEU A 85 8109 16145 9135 -27 -707 -1492 C ATOM 587 CD2 LEU A 85 72.086 -5.736 42.715 1.00 85.08 C ANISOU 587 CD2 LEU A 85 7956 15576 8796 160 -622 -1275 C ATOM 588 N VAL A 86 72.056 -3.725 37.876 1.00 95.21 N ANISOU 588 N VAL A 86 9505 16503 10168 -4 -226 -1487 N ATOM 589 CA VAL A 86 71.532 -2.814 36.863 1.00 95.80 C ANISOU 589 CA VAL A 86 9702 16468 10229 -63 -95 -1539 C ATOM 590 C VAL A 86 70.392 -3.468 36.065 1.00 95.78 C ANISOU 590 C VAL A 86 9882 16300 10211 4 -2 -1447 C ATOM 591 O VAL A 86 69.432 -2.793 35.668 1.00 89.12 O ANISOU 591 O VAL A 86 9208 15167 9485 -41 30 -1367 O ATOM 592 CB VAL A 86 72.659 -2.307 35.934 1.00 86.97 C ANISOU 592 CB VAL A 86 8508 15376 9161 -125 -116 -1647 C ATOM 593 CG1 VAL A 86 72.132 -1.274 34.950 1.00 73.20 C ANISOU 593 CG1 VAL A 86 6891 13524 7399 -191 9 -1706 C ATOM 594 CG2 VAL A 86 73.785 -1.714 36.774 1.00 93.60 C ANISOU 594 CG2 VAL A 86 9156 16392 10016 -198 -214 -1742 C ATOM 595 N LEU A 87 70.496 -4.784 35.864 1.00 94.69 N ANISOU 595 N LEU A 87 9747 16131 10100 91 -56 -1364 N ATOM 596 CA LEU A 87 69.495 -5.553 35.118 1.00 86.80 C ANISOU 596 CA LEU A 87 8926 14892 9163 139 -19 -1240 C ATOM 597 C LEU A 87 68.285 -5.904 35.977 1.00 92.00 C ANISOU 597 C LEU A 87 9678 15420 9856 165 -11 -1115 C ATOM 598 O LEU A 87 67.160 -5.510 35.666 1.00 94.30 O ANISOU 598 O LEU A 87 10145 15414 10271 131 17 -1023 O ATOM 599 CB LEU A 87 70.096 -6.817 34.486 1.00 74.44 C ANISOU 599 CB LEU A 87 7316 13391 7578 217 -55 -1229 C ATOM 600 CG LEU A 87 71.113 -6.594 33.361 1.00 74.00 C ANISOU 600 CG LEU A 87 7211 13328 7577 185 -83 -1307 C ATOM 601 CD1 LEU A 87 71.469 -7.895 32.657 1.00 71.85 C ANISOU 601 CD1 LEU A 87 6934 13004 7363 257 -135 -1247 C ATOM 602 CD2 LEU A 87 70.626 -5.556 32.358 1.00 70.18 C ANISOU 602 CD2 LEU A 87 6865 12652 7146 107 -15 -1326 C ATOM 603 N THR A 88 68.525 -6.649 37.050 1.00 91.19 N ANISOU 603 N THR A 88 9452 15554 9642 230 -38 -1119 N ATOM 604 CA THR A 88 67.466 -7.043 37.965 1.00 92.45 C ANISOU 604 CA THR A 88 9675 15632 9820 256 -32 -1014 C ATOM 605 C THR A 88 66.574 -5.832 38.257 1.00 94.99 C ANISOU 605 C THR A 88 10098 15767 10226 174 1 -995 C ATOM 606 O THR A 88 65.342 -5.944 38.333 1.00 95.48 O ANISOU 606 O THR A 88 10307 15582 10388 171 22 -889 O ATOM 607 CB THR A 88 68.071 -7.618 39.275 1.00 99.76 C ANISOU 607 CB THR A 88 10436 16797 10672 309 -120 -1017 C ATOM 608 OG1 THR A 88 68.675 -8.884 38.998 1.00104.53 O ANISOU 608 OG1 THR A 88 11001 17397 11318 388 -207 -961 O ATOM 609 CG2 THR A 88 67.017 -7.816 40.353 1.00 96.48 C ANISOU 609 CG2 THR A 88 10054 16380 10224 329 -90 -945 C ATOM 610 N GLN A 89 67.199 -4.669 38.387 1.00 95.19 N ANISOU 610 N GLN A 89 10042 15914 10213 105 7 -1105 N ATOM 611 CA GLN A 89 66.459 -3.446 38.650 1.00 97.42 C ANISOU 611 CA GLN A 89 10405 16045 10566 30 37 -1098 C ATOM 612 C GLN A 89 65.755 -2.914 37.400 1.00 93.19 C ANISOU 612 C GLN A 89 10064 15161 10185 -3 67 -1034 C ATOM 613 O GLN A 89 64.693 -2.314 37.506 1.00 97.54 O ANISOU 613 O GLN A 89 10738 15498 10825 -27 92 -969 O ATOM 614 CB GLN A 89 67.371 -2.376 39.260 1.00106.65 C ANISOU 614 CB GLN A 89 11411 17477 11633 -42 36 -1246 C ATOM 615 CG GLN A 89 66.627 -1.206 39.893 1.00109.86 C ANISOU 615 CG GLN A 89 11864 17798 12080 -114 64 -1245 C ATOM 616 CD GLN A 89 65.919 -1.578 41.191 1.00112.30 C ANISOU 616 CD GLN A 89 12145 18178 12345 -85 54 -1191 C ATOM 617 OE1 GLN A 89 66.428 -2.365 41.992 1.00113.52 O ANISOU 617 OE1 GLN A 89 12159 18599 12376 -35 22 -1216 O ATOM 618 NE2 GLN A 89 64.739 -1.005 41.404 1.00111.43 N ANISOU 618 NE2 GLN A 89 12163 17843 12332 -112 80 -1119 N ATOM 619 N SER A 90 66.329 -3.125 36.220 1.00 88.87 N ANISOU 619 N SER A 90 9538 14567 9662 2 64 -1054 N ATOM 620 CA SER A 90 65.656 -2.693 34.995 1.00 89.36 C ANISOU 620 CA SER A 90 9779 14314 9858 -20 87 -987 C ATOM 621 C SER A 90 64.442 -3.576 34.721 1.00 92.57 C ANISOU 621 C SER A 90 10345 14467 10360 28 91 -848 C ATOM 622 O SER A 90 63.434 -3.126 34.176 1.00 90.58 O ANISOU 622 O SER A 90 10251 13946 10220 14 112 -773 O ATOM 623 CB SER A 90 66.599 -2.706 33.799 1.00 85.59 C ANISOU 623 CB SER A 90 9273 13869 9378 -31 80 -1050 C ATOM 624 OG SER A 90 66.235 -1.682 32.886 1.00 83.96 O ANISOU 624 OG SER A 90 9183 13453 9265 -79 104 -1036 O ATOM 625 N SER A 91 64.555 -4.839 35.113 1.00 94.24 N ANISOU 625 N SER A 91 10505 14781 10519 86 71 -820 N ATOM 626 CA SER A 91 63.435 -5.765 35.095 1.00 87.04 C ANISOU 626 CA SER A 91 9717 13674 9682 122 78 -705 C ATOM 627 C SER A 91 62.249 -5.145 35.811 1.00 90.07 C ANISOU 627 C SER A 91 10185 13911 10128 99 100 -654 C ATOM 628 O SER A 91 61.139 -5.058 35.276 1.00 87.59 O ANISOU 628 O SER A 91 10063 13367 9850 69 -11 -594 O ATOM 629 CB SER A 91 63.821 -7.057 35.826 1.00 77.10 C ANISOU 629 CB SER A 91 8347 12620 8327 187 53 -699 C ATOM 630 OG SER A 91 64.418 -8.001 34.951 1.00 71.70 O ANISOU 630 OG SER A 91 7648 11966 7628 225 37 -698 O ATOM 631 N ILE A 92 62.509 -4.707 37.035 1.00 94.67 N ANISOU 631 N ILE A 92 10649 14695 10627 89 95 -705 N ATOM 632 CA ILE A 92 61.446 -4.329 37.958 1.00 97.10 C ANISOU 632 CA ILE A 92 11002 14921 10971 77 111 -663 C ATOM 633 C ILE A 92 60.621 -3.123 37.484 1.00 90.47 C ANISOU 633 C ILE A 92 10045 13856 10475 9 -2 -600 C ATOM 634 O ILE A 92 59.391 -3.119 37.599 1.00 81.91 O ANISOU 634 O ILE A 92 9018 12681 9423 13 -2 -556 O ATOM 635 CB ILE A 92 62.001 -4.196 39.400 1.00 80.67 C ANISOU 635 CB ILE A 92 8743 13150 8757 76 94 -730 C ATOM 636 CG1 ILE A 92 62.462 -5.577 39.871 1.00 90.83 C ANISOU 636 CG1 ILE A 92 9930 14631 9949 144 66 -716 C ATOM 637 CG2 ILE A 92 60.968 -3.631 40.351 1.00 72.82 C ANISOU 637 CG2 ILE A 92 7782 12090 7795 53 110 -700 C ATOM 638 CD1 ILE A 92 62.971 -5.620 41.273 1.00100.90 C ANISOU 638 CD1 ILE A 92 11027 16231 11080 160 42 -771 C ATOM 639 N PHE A 93 61.290 -2.127 36.913 1.00 88.75 N ANISOU 639 N PHE A 93 10054 13652 10016 -7 144 -703 N ATOM 640 CA PHE A 93 60.587 -0.973 36.372 1.00 89.94 C ANISOU 640 CA PHE A 93 10008 13706 10457 -77 15 -666 C ATOM 641 C PHE A 93 59.667 -1.377 35.224 1.00 90.72 C ANISOU 641 C PHE A 93 10498 13643 10327 -49 9 -664 C ATOM 642 O PHE A 93 58.591 -0.792 35.036 1.00 95.27 O ANISOU 642 O PHE A 93 11116 14128 10954 -59 12 -641 O ATOM 643 CB PHE A 93 61.576 0.097 35.926 1.00 89.91 C ANISOU 643 CB PHE A 93 10293 13739 10132 -119 25 -808 C ATOM 644 CG PHE A 93 62.384 0.660 37.048 1.00 93.31 C ANISOU 644 CG PHE A 93 10508 14407 10538 -133 168 -882 C ATOM 645 CD1 PHE A 93 63.770 0.759 36.947 1.00 96.68 C ANISOU 645 CD1 PHE A 93 10791 15077 10868 -164 156 -998 C ATOM 646 CD2 PHE A 93 61.762 1.077 38.216 1.00 88.07 C ANISOU 646 CD2 PHE A 93 9817 13786 9860 -149 176 -879 C ATOM 647 CE1 PHE A 93 64.517 1.264 37.988 1.00 95.81 C ANISOU 647 CE1 PHE A 93 10510 15249 10643 -216 153 -1112 C ATOM 648 CE2 PHE A 93 62.499 1.587 39.263 1.00 87.86 C ANISOU 648 CE2 PHE A 93 9624 14040 9719 -200 172 -987 C ATOM 649 CZ PHE A 93 63.880 1.681 39.154 1.00 93.50 C ANISOU 649 CZ PHE A 93 10194 14999 10333 -236 160 -1106 C ATOM 650 N SER A 94 60.074 -2.385 34.463 1.00 78.66 N ANISOU 650 N SER A 94 8688 12106 9092 -20 4 -587 N ATOM 651 CA SER A 94 59.224 -2.860 33.383 1.00 77.74 C ANISOU 651 CA SER A 94 8929 11847 8761 0 0 -583 C ATOM 652 C SER A 94 57.958 -3.602 33.894 1.00 91.92 C ANISOU 652 C SER A 94 10494 13593 10838 30 -5 -474 C ATOM 653 O SER A 94 56.826 -3.241 33.536 1.00 88.40 O ANISOU 653 O SER A 94 10358 13041 10188 22 -4 -488 O ATOM 654 CB SER A 94 60.039 -3.698 32.396 1.00 76.97 C ANISOU 654 CB SER A 94 8833 11746 8665 19 -4 -582 C ATOM 655 OG SER A 94 61.020 -2.903 31.738 1.00 73.53 O ANISOU 655 OG SER A 94 8093 11353 8492 -12 2 -590 O ATOM 656 N LEU A 95 58.145 -4.608 34.748 1.00 84.07 N ANISOU 656 N LEU A 95 9740 12660 9544 56 -9 -496 N ATOM 657 CA LEU A 95 57.022 -5.321 35.348 1.00 70.81 C ANISOU 657 CA LEU A 95 8085 10941 7879 78 -11 -440 C ATOM 658 C LEU A 95 56.039 -4.329 35.928 1.00 78.24 C ANISOU 658 C LEU A 95 8775 11859 9095 60 -9 -407 C ATOM 659 O LEU A 95 54.829 -4.499 35.819 1.00 85.78 O ANISOU 659 O LEU A 95 9783 12728 10082 68 -9 -371 O ATOM 660 CB LEU A 95 57.500 -6.237 36.475 1.00 65.66 C ANISOU 660 CB LEU A 95 7110 10401 7437 117 -15 -394 C ATOM 661 CG LEU A 95 58.538 -7.313 36.162 1.00 66.41 C ANISOU 661 CG LEU A 95 7176 10550 7505 151 -19 -390 C ATOM 662 CD1 LEU A 95 59.118 -7.872 37.441 1.00 70.57 C ANISOU 662 CD1 LEU A 95 7631 11210 7972 180 -21 -392 C ATOM 663 CD2 LEU A 95 57.933 -8.415 35.336 1.00 58.61 C ANISOU 663 CD2 LEU A 95 6251 9463 6553 176 -20 -340 C ATOM 664 N LEU A 96 56.570 -3.299 36.571 1.00 81.14 N ANISOU 664 N LEU A 96 9364 12299 9168 27 -4 -497 N ATOM 665 CA LEU A 96 55.737 -2.301 37.214 1.00 82.46 C ANISOU 665 CA LEU A 96 9263 12459 9610 3 0 -466 C ATOM 666 C LEU A 96 55.111 -1.395 36.173 1.00 81.12 C ANISOU 666 C LEU A 96 9151 12181 9489 -18 3 -468 C ATOM 667 O LEU A 96 54.006 -0.907 36.367 1.00 76.93 O ANISOU 667 O LEU A 96 8906 11588 8738 -21 4 -496 O ATOM 668 CB LEU A 96 56.554 -1.472 38.200 1.00 86.33 C ANISOU 668 CB LEU A 96 9675 13073 10053 -31 5 -523 C ATOM 669 CG LEU A 96 55.761 -0.499 39.077 1.00 84.97 C ANISOU 669 CG LEU A 96 9497 12908 9881 -61 10 -538 C ATOM 670 CD1 LEU A 96 54.903 -1.252 40.077 1.00 87.12 C ANISOU 670 CD1 LEU A 96 10062 13184 9856 -29 5 -541 C ATOM 671 CD2 LEU A 96 56.687 0.469 39.803 1.00 78.72 C ANISOU 671 CD2 LEU A 96 8629 12234 9047 -108 20 -605 C ATOM 672 N ALA A 97 55.824 -1.162 35.074 1.00 83.97 N ANISOU 672 N ALA A 97 9778 12511 9615 -26 5 -532 N ATOM 673 CA ALA A 97 55.275 -0.388 33.959 1.00 89.17 C ANISOU 673 CA ALA A 97 10480 13067 10333 -40 7 -528 C ATOM 674 C ALA A 97 54.057 -1.102 33.378 1.00 87.49 C ANISOU 674 C ALA A 97 10093 12755 10395 -12 2 -426 C ATOM 675 O ALA A 97 52.946 -0.551 33.300 1.00 82.59 O ANISOU 675 O ALA A 97 9511 12069 9802 -14 3 -412 O ATOM 676 CB ALA A 97 56.326 -0.198 32.887 1.00 87.93 C ANISOU 676 CB ALA A 97 10071 12920 10417 -58 11 -512 C ATOM 677 N ILE A 98 54.301 -2.346 32.984 1.00 80.04 N ANISOU 677 N ILE A 98 9160 11801 9451 16 -3 -398 N ATOM 678 CA ILE A 98 53.286 -3.251 32.480 1.00 67.01 C ANISOU 678 CA ILE A 98 7565 10064 7830 42 -6 -348 C ATOM 679 C ILE A 98 52.048 -3.268 33.372 1.00 64.63 C ANISOU 679 C ILE A 98 7277 9747 7533 49 -7 -326 C ATOM 680 O ILE A 98 50.937 -3.054 32.894 1.00 62.58 O ANISOU 680 O ILE A 98 7064 9407 7306 51 -7 -306 O ATOM 681 CB ILE A 98 53.879 -4.665 32.421 1.00 64.59 C ANISOU 681 CB ILE A 98 7247 9787 7508 69 -10 -328 C ATOM 682 CG1 ILE A 98 54.583 -4.887 31.093 1.00 65.30 C ANISOU 682 CG1 ILE A 98 7354 9843 7613 68 -10 -333 C ATOM 683 CG2 ILE A 98 52.825 -5.718 32.637 1.00 69.17 C ANISOU 683 CG2 ILE A 98 8068 10317 7895 84 -11 -308 C ATOM 684 CD1 ILE A 98 55.615 -5.976 31.147 1.00 69.26 C ANISOU 684 CD1 ILE A 98 8042 10403 7871 82 -12 -364 C ATOM 685 N ALA A 99 52.248 -3.497 34.668 1.00 65.02 N ANISOU 685 N ALA A 99 7279 9880 7545 53 -7 -332 N ATOM 686 CA ALA A 99 51.153 -3.574 35.630 1.00 68.76 C ANISOU 686 CA ALA A 99 7757 10353 8017 59 -8 -314 C ATOM 687 C ALA A 99 50.293 -2.331 35.561 1.00 73.56 C ANISOU 687 C ALA A 99 8386 10914 8647 40 -6 -327 C ATOM 688 O ALA A 99 49.070 -2.409 35.479 1.00 78.04 O ANISOU 688 O ALA A 99 9198 11417 9036 45 -6 -331 O ATOM 689 CB ALA A 99 51.700 -3.722 37.025 1.00 73.43 C ANISOU 689 CB ALA A 99 8519 11053 8329 54 -7 -358 C ATOM 690 N ILE A 100 50.944 -1.177 35.608 1.00 71.06 N ANISOU 690 N ILE A 100 8043 10634 8322 12 -2 -369 N ATOM 691 CA ILE A 100 50.237 0.081 35.535 1.00 68.36 C ANISOU 691 CA ILE A 100 7719 10255 8000 -8 1 -386 C ATOM 692 C ILE A 100 49.450 0.096 34.248 1.00 73.52 C ANISOU 692 C ILE A 100 8638 10795 8501 5 -1 -392 C ATOM 693 O ILE A 100 48.253 0.405 34.243 1.00 76.34 O ANISOU 693 O ILE A 100 9018 11102 8885 11 -2 -375 O ATOM 694 CB ILE A 100 51.203 1.253 35.553 1.00 69.75 C ANISOU 694 CB ILE A 100 7858 10482 8163 -45 8 -438 C ATOM 695 CG1 ILE A 100 51.621 1.570 36.991 1.00 71.10 C ANISOU 695 CG1 ILE A 100 7964 10762 8290 -67 12 -472 C ATOM 696 CG2 ILE A 100 50.560 2.465 34.939 1.00 68.55 C ANISOU 696 CG2 ILE A 100 7957 10257 7833 -57 11 -490 C ATOM 697 CD1 ILE A 100 53.113 1.953 37.121 1.00 71.18 C ANISOU 697 CD1 ILE A 100 8169 10855 8022 -90 18 -570 C ATOM 698 N ASP A 101 50.125 -0.265 33.161 1.00 71.15 N ANISOU 698 N ASP A 101 8351 10467 8217 7 -1 -386 N ATOM 699 CA ASP A 101 49.485 -0.343 31.859 1.00 67.42 C ANISOU 699 CA ASP A 101 7736 9906 7976 19 -3 -329 C ATOM 700 C ASP A 101 48.177 -1.152 31.888 1.00 71.28 C ANISOU 700 C ASP A 101 8437 10339 8306 39 -6 -315 C ATOM 701 O ASP A 101 47.132 -0.670 31.432 1.00 69.84 O ANISOU 701 O ASP A 101 8280 10099 8156 43 -7 -303 O ATOM 702 CB ASP A 101 50.438 -0.953 30.840 1.00 66.31 C ANISOU 702 CB ASP A 101 7601 9755 7839 22 -4 -326 C ATOM 703 CG ASP A 101 49.767 -1.200 29.506 1.00 75.91 C ANISOU 703 CG ASP A 101 9043 10875 8924 30 -5 -325 C ATOM 704 OD1 ASP A 101 49.735 -0.262 28.689 1.00 80.37 O ANISOU 704 OD1 ASP A 101 9454 11407 9674 21 -4 -308 O ATOM 705 OD2 ASP A 101 49.253 -2.319 29.274 1.00 76.64 O ANISOU 705 OD2 ASP A 101 8987 10940 9192 52 -8 -266 O ATOM 706 N ARG A 102 48.238 -2.379 32.412 1.00 65.89 N ANISOU 706 N ARG A 102 7746 9684 7605 53 -7 -294 N ATOM 707 CA ARG A 102 47.056 -3.234 32.495 1.00 59.88 C ANISOU 707 CA ARG A 102 7007 8884 6862 69 -9 -258 C ATOM 708 C ARG A 102 46.019 -2.591 33.381 1.00 69.71 C ANISOU 708 C ARG A 102 8247 10138 8102 68 -9 -262 C ATOM 709 O ARG A 102 44.821 -2.643 33.088 1.00 72.29 O ANISOU 709 O ARG A 102 8429 10417 8621 82 -10 -223 O ATOM 710 CB ARG A 102 47.393 -4.613 33.054 1.00 56.30 C ANISOU 710 CB ARG A 102 6360 8470 6559 90 -10 -217 C ATOM 711 CG ARG A 102 48.355 -5.424 32.210 1.00 65.62 C ANISOU 711 CG ARG A 102 7545 9645 7742 96 -11 -212 C ATOM 712 CD ARG A 102 47.771 -5.800 30.864 1.00 71.57 C ANISOU 712 CD ARG A 102 8349 10313 8530 99 -11 -192 C ATOM 713 NE ARG A 102 47.758 -4.680 29.931 1.00 70.70 N ANISOU 713 NE ARG A 102 8259 10161 8441 87 -10 -207 N ATOM 714 CZ ARG A 102 46.716 -4.362 29.175 1.00 70.05 C ANISOU 714 CZ ARG A 102 8215 10014 8387 87 -10 -196 C ATOM 715 NH1 ARG A 102 45.601 -5.086 29.238 1.00 59.04 N ANISOU 715 NH1 ARG A 102 6839 8590 7001 97 -10 -173 N ATOM 716 NH2 ARG A 102 46.792 -3.319 28.359 1.00 76.44 N ANISOU 716 NH2 ARG A 102 9040 10794 9212 78 -10 -208 N ATOM 717 N TYR A 103 46.482 -1.991 34.476 1.00 74.32 N ANISOU 717 N TYR A 103 8798 10792 8649 57 -8 -289 N ATOM 718 CA TYR A 103 45.583 -1.325 35.407 1.00 75.12 C ANISOU 718 CA TYR A 103 8702 10914 8925 59 -8 -274 C ATOM 719 C TYR A 103 44.834 -0.189 34.709 1.00 81.03 C ANISOU 719 C TYR A 103 9482 11606 9702 54 -8 -282 C ATOM 720 O TYR A 103 43.601 -0.107 34.754 1.00 79.72 O ANISOU 720 O TYR A 103 9511 11404 9374 59 -8 -293 O ATOM 721 CB TYR A 103 46.339 -0.805 36.623 1.00 71.11 C ANISOU 721 CB TYR A 103 8340 10495 8186 38 -5 -333 C ATOM 722 CG TYR A 103 45.446 -0.069 37.595 1.00 79.49 C ANISOU 722 CG TYR A 103 9389 11578 9235 32 -5 -347 C ATOM 723 CD1 TYR A 103 44.780 -0.750 38.606 1.00 84.59 C ANISOU 723 CD1 TYR A 103 9816 12261 10063 46 -6 -301 C ATOM 724 CD2 TYR A 103 45.253 1.307 37.491 1.00 76.94 C ANISOU 724 CD2 TYR A 103 9066 11243 8923 14 -2 -379 C ATOM 725 CE1 TYR A 103 43.954 -0.082 39.496 1.00 84.09 C ANISOU 725 CE1 TYR A 103 9948 12219 9784 36 -5 -343 C ATOM 726 CE2 TYR A 103 44.434 1.981 38.376 1.00 77.58 C ANISOU 726 CE2 TYR A 103 9137 11347 8994 9 -1 -395 C ATOM 727 CZ TYR A 103 43.786 1.280 39.377 1.00 82.80 C ANISOU 727 CZ TYR A 103 9574 12048 9838 21 -3 -346 C ATOM 728 OH TYR A 103 42.967 1.943 40.260 1.00 83.96 O ANISOU 728 OH TYR A 103 9704 12222 9976 14 -2 -362 O ATOM 729 N ILE A 104 45.581 0.682 34.048 1.00 82.51 N ANISOU 729 N ILE A 104 9669 11784 9897 38 -6 -304 N ATOM 730 CA ILE A 104 44.962 1.762 33.301 1.00 81.13 C ANISOU 730 CA ILE A 104 9697 11552 9579 32 -5 -339 C ATOM 731 C ILE A 104 44.024 1.224 32.236 1.00 80.58 C ANISOU 731 C ILE A 104 9500 11412 9705 56 -9 -276 C ATOM 732 O ILE A 104 42.893 1.670 32.114 1.00 80.67 O ANISOU 732 O ILE A 104 9529 11394 9729 66 -10 -269 O ATOM 733 CB ILE A 104 46.020 2.627 32.641 1.00 76.89 C ANISOU 733 CB ILE A 104 8979 11021 9215 13 -2 -337 C ATOM 734 CG1 ILE A 104 47.004 3.128 33.709 1.00 72.91 C ANISOU 734 CG1 ILE A 104 8421 10603 8680 -15 3 -378 C ATOM 735 CG2 ILE A 104 45.357 3.759 31.840 1.00 70.99 C ANISOU 735 CG2 ILE A 104 8429 10213 8331 11 -2 -371 C ATOM 736 CD1 ILE A 104 48.228 3.823 33.145 1.00 71.23 C ANISOU 736 CD1 ILE A 104 8191 10407 8465 -43 9 -411 C ATOM 737 N ALA A 105 44.510 0.250 31.478 1.00 81.15 N ANISOU 737 N ALA A 105 9747 11458 9627 57 -9 -282 N ATOM 738 CA ALA A 105 43.762 -0.340 30.376 1.00 75.44 C ANISOU 738 CA ALA A 105 9055 10672 8937 70 -10 -252 C ATOM 739 C ALA A 105 42.418 -0.940 30.793 1.00 69.37 C ANISOU 739 C ALA A 105 8294 9895 8171 84 -11 -230 C ATOM 740 O ALA A 105 41.413 -0.759 30.101 1.00 63.80 O ANISOU 740 O ALA A 105 7465 9150 7628 100 -13 -199 O ATOM 741 CB ALA A 105 44.618 -1.392 29.688 1.00 74.19 C ANISOU 741 CB ALA A 105 8654 10843 8691 97 -13 -299 C ATOM 742 N ILE A 106 42.427 -1.698 31.888 1.00 68.64 N ANISOU 742 N ILE A 106 8029 9848 8204 94 -12 -206 N ATOM 743 CA ILE A 106 41.225 -2.347 32.425 1.00 78.24 C ANISOU 743 CA ILE A 106 9400 11064 9264 96 -11 -207 C ATOM 744 C ILE A 106 40.338 -1.485 33.339 1.00 83.42 C ANISOU 744 C ILE A 106 10043 11746 9906 98 -12 -220 C ATOM 745 O ILE A 106 39.106 -1.512 33.242 1.00 83.10 O ANISOU 745 O ILE A 106 10012 11688 9873 108 -13 -210 O ATOM 746 CB ILE A 106 41.595 -3.625 33.191 1.00 78.80 C ANISOU 746 CB ILE A 106 9298 11173 9469 108 -10 -176 C ATOM 747 CG1 ILE A 106 42.462 -4.523 32.315 1.00 79.21 C ANISOU 747 CG1 ILE A 106 9519 11202 9375 99 -11 -180 C ATOM 748 CG2 ILE A 106 40.339 -4.354 33.666 1.00 74.80 C ANISOU 748 CG2 ILE A 106 8951 10667 8802 108 -11 -172 C ATOM 749 CD1 ILE A 106 43.180 -5.590 33.086 1.00 82.04 C ANISOU 749 CD1 ILE A 106 9858 11609 9706 103 -10 -170 C ATOM 750 N ARG A 107 40.960 -0.738 34.240 1.00 84.10 N ANISOU 750 N ARG A 107 9941 11882 10130 96 -12 -226 N ATOM 751 CA ARG A 107 40.199 0.063 35.185 1.00 92.06 C ANISOU 751 CA ARG A 107 10818 13304 10856 120 -16 -329 C ATOM 752 C ARG A 107 39.678 1.369 34.574 1.00 89.29 C ANISOU 752 C ARG A 107 10596 12539 10793 97 -14 -255 C ATOM 753 O ARG A 107 38.579 1.811 34.899 1.00 89.65 O ANISOU 753 O ARG A 107 10805 12583 10673 99 -14 -281 O ATOM 754 CB ARG A 107 41.016 0.324 36.449 1.00 96.86 C ANISOU 754 CB ARG A 107 11493 13603 11706 81 -11 -265 C ATOM 755 CG ARG A 107 40.497 -0.409 37.680 1.00105.53 C ANISOU 755 CG ARG A 107 12750 14749 12597 79 -10 -278 C ATOM 756 CD ARG A 107 39.560 0.476 38.485 1.00113.61 C ANISOU 756 CD ARG A 107 13761 15797 13609 78 -10 -298 C ATOM 757 NE ARG A 107 40.261 1.641 39.025 1.00121.27 N ANISOU 757 NE ARG A 107 14709 16808 14562 58 -9 -339 N ATOM 758 CZ ARG A 107 39.665 2.769 39.409 1.00124.39 C ANISOU 758 CZ ARG A 107 15096 17213 14955 52 -8 -366 C ATOM 759 NH1 ARG A 107 38.346 2.897 39.308 1.00127.24 N ANISOU 759 NH1 ARG A 107 15276 17553 15518 76 -12 -325 N ATOM 760 NH2 ARG A 107 40.390 3.775 39.886 1.00120.12 N ANISOU 760 NH2 ARG A 107 14532 16711 14397 27 -5 -408 N ATOM 761 N ILE A 108 40.447 1.964 33.666 1.00 85.94 N ANISOU 761 N ILE A 108 10184 12085 10382 88 -13 -264 N ATOM 762 CA ILE A 108 40.074 3.241 33.059 1.00 82.92 C ANISOU 762 CA ILE A 108 9816 11675 10016 89 -15 -276 C ATOM 763 C ILE A 108 40.049 3.123 31.543 1.00 81.00 C ANISOU 763 C ILE A 108 9510 11707 9559 122 -19 -351 C ATOM 764 O ILE A 108 40.725 3.874 30.850 1.00 81.48 O ANISOU 764 O ILE A 108 9826 11409 9722 80 -13 -293 O ATOM 765 CB ILE A 108 41.115 4.327 33.397 1.00 82.30 C ANISOU 765 CB ILE A 108 9713 11626 9931 64 -11 -312 C ATOM 766 CG1 ILE A 108 41.514 4.256 34.865 1.00 73.02 C ANISOU 766 CG1 ILE A 108 8668 10518 8558 45 -8 -364 C ATOM 767 CG2 ILE A 108 40.608 5.733 33.026 1.00 82.04 C ANISOU 767 CG2 ILE A 108 9851 11566 9754 59 -11 -358 C ATOM 768 CD1 ILE A 108 42.620 5.209 35.183 1.00 73.87 C ANISOU 768 CD1 ILE A 108 8572 10670 8825 16 -3 -373 C ATOM 769 N PRO A 109 39.223 2.216 31.018 1.00 77.06 N ANISOU 769 N PRO A 109 9034 11172 9071 142 -21 -315 N ATOM 770 CA PRO A 109 39.335 1.818 29.615 1.00 70.06 C ANISOU 770 CA PRO A 109 8414 9906 8299 107 -15 -233 C ATOM 771 C PRO A 109 39.158 2.969 28.622 1.00 79.57 C ANISOU 771 C PRO A 109 9496 11081 9656 121 -18 -218 C ATOM 772 O PRO A 109 39.781 2.936 27.559 1.00 76.79 O ANISOU 772 O PRO A 109 9293 10696 9188 106 -16 -232 O ATOM 773 CB PRO A 109 38.216 0.791 29.461 1.00 70.39 C ANISOU 773 CB PRO A 109 8237 10252 8257 164 -21 -262 C ATOM 774 CG PRO A 109 37.235 1.142 30.497 1.00 75.45 C ANISOU 774 CG PRO A 109 9090 10615 8964 129 -18 -217 C ATOM 775 CD PRO A 109 38.025 1.652 31.658 1.00 79.80 C ANISOU 775 CD PRO A 109 9472 11209 9642 128 -18 -220 C ATOM 776 N LEU A 110 38.346 3.972 28.963 1.00 90.94 N ANISOU 776 N LEU A 110 11067 12529 10957 121 -19 -249 N ATOM 777 CA LEU A 110 37.994 5.037 28.010 1.00 92.13 C ANISOU 777 CA LEU A 110 11230 12652 11123 130 -23 -249 C ATOM 778 C LEU A 110 39.110 6.072 27.802 1.00 95.33 C ANISOU 778 C LEU A 110 11499 13055 11667 123 -21 -248 C ATOM 779 O LEU A 110 39.279 6.606 26.697 1.00 90.78 O ANISOU 779 O LEU A 110 11071 12444 10977 114 -20 -265 O ATOM 780 CB LEU A 110 36.687 5.735 28.418 1.00 85.07 C ANISOU 780 CB LEU A 110 10195 11777 10352 166 -24 -231 C ATOM 781 CG LEU A 110 35.441 4.869 28.665 1.00 78.20 C ANISOU 781 CG LEU A 110 9321 10922 9471 185 -25 -216 C ATOM 782 CD1 LEU A 110 34.233 5.722 29.091 1.00 68.43 C ANISOU 782 CD1 LEU A 110 8211 9709 8079 193 -31 -243 C ATOM 783 CD2 LEU A 110 35.103 4.005 27.451 1.00 71.70 C ANISOU 783 CD2 LEU A 110 8651 10068 8522 175 -26 -210 C ATOM 784 N ARG A 111 39.866 6.348 28.864 1.00 97.98 N ANISOU 784 N ARG A 111 11808 13428 11992 102 -19 -273 N ATOM 785 CA ARG A 111 40.932 7.346 28.817 1.00103.66 C ANISOU 785 CA ARG A 111 12515 14155 12714 76 -15 -301 C ATOM 786 C ARG A 111 42.245 6.747 28.315 1.00104.96 C ANISOU 786 C ARG A 111 12822 14312 12745 52 -10 -329 C ATOM 787 O ARG A 111 43.213 7.468 28.055 1.00103.34 O ANISOU 787 O ARG A 111 12466 14118 12679 32 -7 -325 O ATOM 788 CB ARG A 111 41.138 7.967 30.201 1.00107.66 C ANISOU 788 CB ARG A 111 12986 14715 13206 58 -12 -335 C ATOM 789 CG ARG A 111 40.027 8.911 30.642 1.00113.20 C ANISOU 789 CG ARG A 111 13835 15415 13762 67 -14 -376 C ATOM 790 CD ARG A 111 40.349 10.361 30.298 1.00119.05 C ANISOU 790 CD ARG A 111 14573 16146 14514 51 -12 -405 C ATOM 791 NE ARG A 111 41.505 10.867 31.043 1.00123.89 N ANISOU 791 NE ARG A 111 15159 16799 15113 8 -2 -453 N ATOM 792 CZ ARG A 111 41.458 11.304 32.301 1.00121.14 C ANISOU 792 CZ ARG A 111 14785 16500 14745 -12 3 -490 C ATOM 793 NH1 ARG A 111 40.309 11.294 32.974 1.00121.61 N ANISOU 793 NH1 ARG A 111 14841 16572 14795 12 -3 -483 N ATOM 794 NH2 ARG A 111 42.563 11.745 32.892 1.00114.19 N ANISOU 794 NH2 ARG A 111 13878 15661 13848 -59 16 -539 N ATOM 795 N TYR A 112 42.268 5.426 28.170 1.00101.26 N ANISOU 795 N TYR A 112 12360 13838 12275 61 -11 -305 N ATOM 796 CA TYR A 112 43.506 4.711 27.890 1.00 95.83 C ANISOU 796 CA TYR A 112 11528 13164 11720 51 -10 -281 C ATOM 797 C TYR A 112 44.086 5.027 26.518 1.00100.49 C ANISOU 797 C TYR A 112 12138 13716 12326 45 -9 -278 C ATOM 798 O TYR A 112 45.239 5.440 26.412 1.00 98.73 O ANISOU 798 O TYR A 112 11899 13514 12100 22 -5 -301 O ATOM 799 CB TYR A 112 43.295 3.201 28.058 1.00 91.21 C ANISOU 799 CB TYR A 112 10948 12579 11129 64 -11 -257 C ATOM 800 CG TYR A 112 44.486 2.343 27.672 1.00 93.13 C ANISOU 800 CG TYR A 112 11327 12825 11232 51 -9 -279 C ATOM 801 CD1 TYR A 112 45.420 1.939 28.623 1.00 97.33 C ANISOU 801 CD1 TYR A 112 11685 13418 11879 44 -8 -272 C ATOM 802 CD2 TYR A 112 44.669 1.923 26.353 1.00 88.24 C ANISOU 802 CD2 TYR A 112 10593 12166 10766 60 -10 -240 C ATOM 803 CE1 TYR A 112 46.510 1.147 28.264 1.00 94.69 C ANISOU 803 CE1 TYR A 112 11343 13098 11538 40 -7 -272 C ATOM 804 CE2 TYR A 112 45.749 1.135 25.988 1.00 82.38 C ANISOU 804 CE2 TYR A 112 9846 11434 10020 53 -9 -240 C ATOM 805 CZ TYR A 112 46.663 0.751 26.944 1.00 86.65 C ANISOU 805 CZ TYR A 112 10496 12028 10398 41 -7 -280 C ATOM 806 OH TYR A 112 47.729 -0.032 26.577 1.00 84.06 O ANISOU 806 OH TYR A 112 10016 11719 10203 41 -7 -258 O ATOM 807 N ASN A 113 43.287 4.846 25.470 1.00109.60 N ANISOU 807 N ASN A 113 13324 14824 13497 64 -12 -252 N ATOM 808 CA ASN A 113 43.801 4.929 24.105 1.00119.61 C ANISOU 808 CA ASN A 113 14736 16054 14658 55 -10 -267 C ATOM 809 C ASN A 113 44.647 6.180 23.856 1.00119.72 C ANISOU 809 C ASN A 113 14615 16079 14795 38 -8 -270 C ATOM 810 O ASN A 113 45.677 6.126 23.169 1.00114.61 O ANISOU 810 O ASN A 113 14093 15424 14028 20 -4 -303 O ATOM 811 CB ASN A 113 42.659 4.843 23.087 1.00128.51 C ANISOU 811 CB ASN A 113 15886 17140 15803 76 -13 -238 C ATOM 812 CG ASN A 113 42.861 3.719 22.073 1.00133.24 C ANISOU 812 CG ASN A 113 16383 17717 16525 86 -14 -199 C ATOM 813 OD1 ASN A 113 43.377 2.649 22.408 1.00132.00 O ANISOU 813 OD1 ASN A 113 16220 17573 16362 81 -13 -197 O ATOM 814 ND2 ASN A 113 42.456 3.964 20.823 1.00132.82 N ANISOU 814 ND2 ASN A 113 16351 17633 16483 95 -15 -185 N ATOM 815 N GLY A 114 44.203 7.300 24.423 1.00120.53 N ANISOU 815 N GLY A 114 14837 16187 14773 32 -7 -313 N ATOM 816 CA GLY A 114 44.889 8.570 24.263 1.00116.90 C ANISOU 816 CA GLY A 114 14367 15733 14315 8 -2 -345 C ATOM 817 C GLY A 114 45.864 8.880 25.381 1.00111.43 C ANISOU 817 C GLY A 114 13644 15096 13598 -25 6 -391 C ATOM 818 O GLY A 114 46.756 9.705 25.212 1.00112.77 O ANISOU 818 O GLY A 114 13656 15289 13901 -62 16 -392 O ATOM 819 N LEU A 115 45.701 8.214 26.520 1.00106.57 N ANISOU 819 N LEU A 115 13013 14516 12961 -20 5 -393 N ATOM 820 CA LEU A 115 46.624 8.384 27.640 1.00102.97 C ANISOU 820 CA LEU A 115 12524 14125 12475 -50 12 -437 C ATOM 821 C LEU A 115 47.944 7.660 27.375 1.00 99.56 C ANISOU 821 C LEU A 115 11920 13730 12179 -71 18 -411 C ATOM 822 O LEU A 115 48.998 8.286 27.334 1.00 99.64 O ANISOU 822 O LEU A 115 12070 13764 12026 -100 26 -492 O ATOM 823 CB LEU A 115 46.006 7.920 28.967 1.00 98.58 C ANISOU 823 CB LEU A 115 11794 13612 12048 -42 10 -399 C ATOM 824 CG LEU A 115 46.775 8.368 30.219 1.00 88.35 C ANISOU 824 CG LEU A 115 10448 12392 10728 -80 20 -446 C ATOM 825 CD1 LEU A 115 47.036 9.871 30.175 1.00 86.65 C ANISOU 825 CD1 LEU A 115 10219 12183 10521 -120 33 -489 C ATOM 826 CD2 LEU A 115 46.062 7.978 31.512 1.00 76.34 C ANISOU 826 CD2 LEU A 115 8909 10907 9190 -67 16 -442 C ATOM 827 N VAL A 116 47.878 6.339 27.227 1.00 99.49 N ANISOU 827 N VAL A 116 12080 13704 12018 -41 9 -414 N ATOM 828 CA VAL A 116 49.046 5.532 26.871 1.00104.30 C ANISOU 828 CA VAL A 116 12519 14345 12766 -52 12 -384 C ATOM 829 C VAL A 116 49.305 5.575 25.365 1.00105.14 C ANISOU 829 C VAL A 116 12654 14401 12892 -51 12 -371 C ATOM 830 O VAL A 116 48.420 5.246 24.580 1.00109.72 O ANISOU 830 O VAL A 116 13273 14924 13491 -25 6 -335 O ATOM 831 CB VAL A 116 48.861 4.046 27.274 1.00 78.81 C ANISOU 831 CB VAL A 116 9293 11125 9527 -26 6 -356 C ATOM 832 CG1 VAL A 116 49.853 3.177 26.527 1.00 82.44 C ANISOU 832 CG1 VAL A 116 9911 11582 9832 -24 5 -384 C ATOM 833 CG2 VAL A 116 48.974 3.846 28.791 1.00 65.66 C ANISOU 833 CG2 VAL A 116 7588 9527 7834 -32 7 -373 C ATOM 834 N THR A 117 50.509 5.983 24.967 1.00103.94 N ANISOU 834 N THR A 117 12480 14278 12734 -81 20 -404 N ATOM 835 CA THR A 117 50.904 5.993 23.556 1.00108.90 C ANISOU 835 CA THR A 117 13131 14869 13379 -83 21 -396 C ATOM 836 C THR A 117 52.313 5.416 23.392 1.00112.78 C ANISOU 836 C THR A 117 13752 15399 13702 -93 23 -460 C ATOM 837 O THR A 117 53.047 5.260 24.372 1.00114.15 O ANISOU 837 O THR A 117 13720 15650 14001 -117 30 -453 O ATOM 838 CB THR A 117 50.853 7.412 22.940 1.00110.91 C ANISOU 838 CB THR A 117 13393 15100 13649 -108 29 -415 C ATOM 839 OG1 THR A 117 51.851 8.241 23.551 1.00118.58 O ANISOU 839 OG1 THR A 117 14483 16120 14453 -143 41 -516 O ATOM 840 CG2 THR A 117 49.479 8.045 23.132 1.00103.05 C ANISOU 840 CG2 THR A 117 12569 14056 12531 -80 21 -429 C ATOM 841 N GLY A 118 52.688 5.099 22.155 1.00111.43 N ANISOU 841 N GLY A 118 13594 15198 13546 -90 23 -448 N ATOM 842 CA GLY A 118 53.955 4.438 21.894 1.00111.53 C ANISOU 842 CA GLY A 118 13422 15264 13691 -110 28 -433 C ATOM 843 C GLY A 118 55.176 5.256 22.278 1.00112.50 C ANISOU 843 C GLY A 118 13670 15446 13630 -145 40 -542 C ATOM 844 O GLY A 118 56.167 4.721 22.789 1.00109.29 O ANISOU 844 O GLY A 118 13229 15107 13188 -154 42 -574 O ATOM 845 N THR A 119 55.108 6.559 22.024 1.00114.39 N ANISOU 845 N THR A 119 13734 15683 14045 -191 56 -521 N ATOM 846 CA THR A 119 56.223 7.453 22.318 1.00116.14 C ANISOU 846 CA THR A 119 13906 15969 14252 -250 78 -591 C ATOM 847 C THR A 119 56.300 7.830 23.808 1.00114.62 C ANISOU 847 C THR A 119 13672 15842 14037 -272 85 -626 C ATOM 848 O THR A 119 57.387 8.093 24.326 1.00122.34 O ANISOU 848 O THR A 119 14459 17315 14708 -396 128 -938 O ATOM 849 CB THR A 119 56.216 8.708 21.405 1.00103.88 C ANISOU 849 CB THR A 119 12558 14362 12550 -265 87 -671 C ATOM 850 OG1 THR A 119 55.026 9.473 21.634 1.00106.20 O ANISOU 850 OG1 THR A 119 12696 14623 13033 -279 92 -588 O ATOM 851 CG2 THR A 119 56.273 8.296 19.939 1.00100.39 C ANISOU 851 CG2 THR A 119 11961 13884 12297 -271 89 -584 C ATOM 852 N ARG A 120 55.158 7.848 24.494 1.00105.69 N ANISOU 852 N ARG A 120 12757 14668 12731 -222 67 -646 N ATOM 853 CA ARG A 120 55.161 7.989 25.947 1.00100.45 C ANISOU 853 CA ARG A 120 12064 14067 12034 -235 71 -674 C ATOM 854 C ARG A 120 55.790 6.742 26.567 1.00103.14 C ANISOU 854 C ARG A 120 12168 14485 12534 -235 68 -614 C ATOM 855 O ARG A 120 56.355 6.794 27.664 1.00104.22 O ANISOU 855 O ARG A 120 12476 14692 12433 -236 68 -713 O ATOM 856 CB ARG A 120 53.743 8.190 26.483 1.00 99.81 C ANISOU 856 CB ARG A 120 11687 14346 11889 -283 83 -790 C ATOM 857 CG ARG A 120 53.367 9.636 26.768 1.00104.18 C ANISOU 857 CG ARG A 120 12238 14889 12456 -332 103 -835 C ATOM 858 CD ARG A 120 52.098 9.695 27.601 1.00108.63 C ANISOU 858 CD ARG A 120 13135 15031 13109 -217 65 -638 C ATOM 859 NE ARG A 120 51.792 11.031 28.107 1.00117.02 N ANISOU 859 NE ARG A 120 14190 16097 14174 -255 81 -680 N ATOM 860 CZ ARG A 120 50.876 11.842 27.583 1.00120.86 C ANISOU 860 CZ ARG A 120 14705 16521 14697 -248 81 -663 C ATOM 861 NH1 ARG A 120 50.658 13.042 28.118 1.00126.90 N ANISOU 861 NH1 ARG A 120 15150 17675 15392 -394 135 -884 N ATOM 862 NH2 ARG A 120 50.174 11.456 26.526 1.00114.89 N ANISOU 862 NH2 ARG A 120 13808 15710 14134 -222 70 -552 N ATOM 863 N ALA A 121 55.693 5.625 25.844 1.00101.57 N ANISOU 863 N ALA A 121 12201 14235 12155 -177 49 -622 N ATOM 864 CA ALA A 121 56.244 4.346 26.282 1.00100.39 C ANISOU 864 CA ALA A 121 11689 14577 11876 -211 56 -766 C ATOM 865 C ALA A 121 57.764 4.345 26.194 1.00104.74 C ANISOU 865 C ALA A 121 12320 14783 12695 -202 55 -619 C ATOM 866 O ALA A 121 58.442 3.761 27.041 1.00107.39 O ANISOU 866 O ALA A 121 12838 15187 12779 -183 49 -698 O ATOM 867 CB ALA A 121 55.662 3.205 25.463 1.00 89.81 C ANISOU 867 CB ALA A 121 10536 12740 10850 -123 31 -503 C ATOM 868 N LYS A 122 58.294 4.997 25.163 1.00108.05 N ANISOU 868 N LYS A 122 12962 15168 12923 -213 61 -706 N ATOM 869 CA LYS A 122 59.742 5.157 25.010 1.00108.27 C ANISOU 869 CA LYS A 122 12946 15274 12916 -251 75 -779 C ATOM 870 C LYS A 122 60.335 5.940 26.176 1.00105.05 C ANISOU 870 C LYS A 122 12239 14980 12696 -323 100 -779 C ATOM 871 O LYS A 122 61.380 5.569 26.717 1.00 97.89 O ANISOU 871 O LYS A 122 11268 14171 11753 -336 104 -824 O ATOM 872 CB LYS A 122 60.070 5.863 23.693 1.00105.37 C ANISOU 872 CB LYS A 122 12363 14882 12793 -306 97 -733 C ATOM 873 CG LYS A 122 59.736 5.038 22.464 1.00107.09 C ANISOU 873 CG LYS A 122 12850 15007 12831 -242 75 -743 C ATOM 874 CD LYS A 122 59.676 5.886 21.199 1.00110.52 C ANISOU 874 CD LYS A 122 13097 15400 13498 -292 94 -686 C ATOM 875 CE LYS A 122 59.312 5.038 19.985 1.00111.13 C ANISOU 875 CE LYS A 122 13222 15409 13596 -251 79 -632 C ATOM 876 NZ LYS A 122 58.855 5.861 18.826 1.00111.83 N ANISOU 876 NZ LYS A 122 13350 15426 13713 -266 86 -620 N ATOM 877 N GLY A 123 59.658 7.023 26.553 1.00104.43 N ANISOU 877 N GLY A 123 12175 14875 12631 -351 111 -787 N ATOM 878 CA GLY A 123 60.116 7.879 27.630 1.00105.06 C ANISOU 878 CA GLY A 123 12461 15017 12441 -374 121 -932 C ATOM 879 C GLY A 123 60.406 7.079 28.882 1.00107.24 C ANISOU 879 C GLY A 123 12698 15385 12664 -355 110 -935 C ATOM 880 O GLY A 123 61.494 7.179 29.471 1.00103.83 O ANISOU 880 O GLY A 123 12212 15061 12179 -390 123 -1007 O ATOM 881 N ILE A 124 59.422 6.276 29.283 1.00105.86 N ANISOU 881 N ILE A 124 12286 15189 12749 -327 96 -787 N ATOM 882 CA ILE A 124 59.547 5.426 30.461 1.00104.35 C ANISOU 882 CA ILE A 124 12056 15075 12520 -300 84 -780 C ATOM 883 C ILE A 124 60.752 4.502 30.351 1.00 99.77 C ANISOU 883 C ILE A 124 11427 14573 11908 -288 80 -802 C ATOM 884 O ILE A 124 61.596 4.452 31.247 1.00 90.34 O ANISOU 884 O ILE A 124 10459 13476 10389 -282 78 -928 O ATOM 885 CB ILE A 124 58.300 4.536 30.653 1.00103.79 C ANISOU 885 CB ILE A 124 12297 14915 12222 -218 58 -765 C ATOM 886 CG1 ILE A 124 57.083 5.363 31.078 1.00101.22 C ANISOU 886 CG1 ILE A 124 11999 14537 11925 -224 60 -747 C ATOM 887 CG2 ILE A 124 58.587 3.448 31.686 1.00101.41 C ANISOU 887 CG2 ILE A 124 11699 14709 12124 -208 52 -689 C ATOM 888 CD1 ILE A 124 56.979 5.576 32.586 1.00100.21 C ANISOU 888 CD1 ILE A 124 11573 14504 11999 -261 68 -707 C ATOM 889 N ILE A 125 60.808 3.764 29.243 1.00104.59 N ANISOU 889 N ILE A 125 12076 15124 12541 -255 70 -767 N ATOM 890 CA ILE A 125 61.813 2.724 29.039 1.00106.44 C ANISOU 890 CA ILE A 125 12555 15401 12486 -213 58 -849 C ATOM 891 C ILE A 125 63.200 3.338 29.119 1.00109.85 C ANISOU 891 C ILE A 125 12927 15938 12872 -262 74 -948 C ATOM 892 O ILE A 125 64.105 2.755 29.706 1.00115.55 O ANISOU 892 O ILE A 125 13283 16788 13831 -278 78 -901 O ATOM 893 CB ILE A 125 61.591 1.956 27.690 1.00 75.17 C ANISOU 893 CB ILE A 125 8373 11365 8823 -197 52 -730 C ATOM 894 CG1 ILE A 125 60.173 1.345 27.638 1.00 74.54 C ANISOU 894 CG1 ILE A 125 8616 11170 8537 -138 35 -708 C ATOM 895 CG2 ILE A 125 62.639 0.875 27.491 1.00 60.40 C ANISOU 895 CG2 ILE A 125 6463 9559 6925 -173 46 -745 C ATOM 896 CD1 ILE A 125 59.823 0.640 26.339 1.00 63.24 C ANISOU 896 CD1 ILE A 125 7229 9648 7151 -112 28 -658 C ATOM 897 N ALA A 126 63.353 4.525 28.535 1.00108.95 N ANISOU 897 N ALA A 126 12819 15798 12781 -314 94 -995 N ATOM 898 CA ALA A 126 64.584 5.312 28.651 1.00105.64 C ANISOU 898 CA ALA A 126 12342 15475 12320 -377 119 -1102 C ATOM 899 C ALA A 126 64.927 5.640 30.109 1.00104.13 C ANISOU 899 C ALA A 126 11544 16093 11928 -552 172 -1442 C ATOM 900 O ALA A 126 65.922 5.163 30.659 1.00 91.54 O ANISOU 900 O ALA A 126 10349 13996 10436 -387 241 -1205 O ATOM 901 CB ALA A 126 64.459 6.592 27.841 1.00106.26 C ANISOU 901 CB ALA A 126 12128 15515 12730 -473 157 -1040 C ATOM 902 N ILE A 127 64.080 6.453 30.727 1.00102.03 N ANISOU 902 N ILE A 127 11848 15106 11814 -427 134 -1145 N ATOM 903 CA ILE A 127 64.251 6.850 32.120 1.00107.50 C ANISOU 903 CA ILE A 127 11923 16615 12305 -625 195 -1487 C ATOM 904 C ILE A 127 64.534 5.658 33.037 1.00104.14 C ANISOU 904 C ILE A 127 11940 15613 12016 -382 254 -1149 C ATOM 905 O ILE A 127 65.328 5.760 33.969 1.00108.81 O ANISOU 905 O ILE A 127 12376 16455 12511 -436 259 -1262 O ATOM 906 CB ILE A 127 63.002 7.602 32.622 1.00 96.27 C ANISOU 906 CB ILE A 127 10769 14436 11372 -511 159 -1057 C ATOM 907 CG1 ILE A 127 62.688 8.766 31.681 1.00 94.35 C ANISOU 907 CG1 ILE A 127 10573 14101 11175 -561 184 -1074 C ATOM 908 CG2 ILE A 127 63.176 8.057 34.077 1.00 93.29 C ANISOU 908 CG2 ILE A 127 10104 14870 10473 -693 215 -1508 C ATOM 909 CD1 ILE A 127 61.468 9.550 32.073 1.00102.18 C ANISOU 909 CD1 ILE A 127 11416 15638 11770 -714 235 -1431 C ATOM 910 N CYS A 128 63.880 4.532 32.767 1.00 99.63 N ANISOU 910 N CYS A 128 11500 14929 11426 -337 95 -1076 N ATOM 911 CA CYS A 128 64.050 3.334 33.582 1.00 97.51 C ANISOU 911 CA CYS A 128 11118 14771 11160 -261 207 -1029 C ATOM 912 C CYS A 128 65.396 2.672 33.371 1.00 98.64 C ANISOU 912 C CYS A 128 11123 15140 11215 -271 189 -1127 C ATOM 913 O CYS A 128 65.863 1.936 34.231 1.00105.67 O ANISOU 913 O CYS A 128 11895 16235 12019 -254 170 -1167 O ATOM 914 CB CYS A 128 62.934 2.329 33.312 1.00 96.69 C ANISOU 914 CB CYS A 128 10833 14541 11365 -243 62 -860 C ATOM 915 SG CYS A 128 61.362 2.786 34.057 1.00 99.86 S ANISOU 915 SG CYS A 128 11286 14866 11788 -240 59 -810 S ATOM 916 N TRP A 129 66.001 2.899 32.213 1.00 98.09 N ANISOU 916 N TRP A 129 11064 15040 11165 -292 192 -1166 N ATOM 917 CA TRP A 129 67.355 2.417 31.962 1.00105.26 C ANISOU 917 CA TRP A 129 11826 16179 11991 -310 179 -1283 C ATOM 918 C TRP A 129 68.403 3.369 32.544 1.00113.34 C ANISOU 918 C TRP A 129 12680 17457 12926 -405 199 -1454 C ATOM 919 O TRP A 129 69.471 2.952 33.004 1.00114.76 O ANISOU 919 O TRP A 129 12687 17914 13002 -420 185 -1573 O ATOM 920 CB TRP A 129 67.573 2.186 30.470 1.00 99.07 C ANISOU 920 CB TRP A 129 11113 15265 11263 -297 175 -1262 C ATOM 921 CG TRP A 129 67.047 0.861 30.023 1.00 97.87 C ANISOU 921 CG TRP A 129 11050 14988 11150 -215 149 -1147 C ATOM 922 CD1 TRP A 129 65.879 0.616 29.349 1.00 93.64 C ANISOU 922 CD1 TRP A 129 10693 14170 10714 -172 148 -1007 C ATOM 923 CD2 TRP A 129 67.664 -0.415 30.233 1.00 99.08 C ANISOU 923 CD2 TRP A 129 11106 15304 11235 -168 122 -1170 C ATOM 924 NE1 TRP A 129 65.739 -0.735 29.116 1.00 92.74 N ANISOU 924 NE1 TRP A 129 10604 14028 10604 -115 126 -946 N ATOM 925 CE2 TRP A 129 66.820 -1.389 29.650 1.00 99.84 C ANISOU 925 CE2 TRP A 129 11338 15196 11402 -107 110 -1040 C ATOM 926 CE3 TRP A 129 68.853 -0.828 30.846 1.00 95.85 C ANISOU 926 CE3 TRP A 129 10502 15208 10708 -171 105 -1295 C ATOM 927 CZ2 TRP A 129 67.130 -2.753 29.667 1.00100.32 C ANISOU 927 CZ2 TRP A 129 11350 15346 11421 -51 86 -1026 C ATOM 928 CZ3 TRP A 129 69.158 -2.181 30.864 1.00 95.26 C ANISOU 928 CZ3 TRP A 129 10376 15230 10589 -101 76 -1277 C ATOM 929 CH2 TRP A 129 68.299 -3.127 30.279 1.00 98.22 C ANISOU 929 CH2 TRP A 129 10894 15387 11038 -43 68 -1141 C ATOM 930 N VAL A 130 68.076 4.654 32.515 1.00113.77 N ANISOU 930 N VAL A 130 12781 17424 13021 -471 234 -1472 N ATOM 931 CA VAL A 130 68.899 5.676 33.136 1.00114.85 C ANISOU 931 CA VAL A 130 12774 17780 13085 -581 264 -1634 C ATOM 932 C VAL A 130 68.976 5.429 34.635 1.00111.29 C ANISOU 932 C VAL A 130 12200 17547 12538 -587 251 -1676 C ATOM 933 O VAL A 130 70.054 5.443 35.225 1.00112.09 O ANISOU 933 O VAL A 130 12115 17946 12527 -645 250 -1828 O ATOM 934 CB VAL A 130 68.304 7.082 32.893 1.00117.18 C ANISOU 934 CB VAL A 130 13165 17910 13450 -644 307 -1623 C ATOM 935 CG1 VAL A 130 68.754 8.059 33.982 1.00120.65 C ANISOU 935 CG1 VAL A 130 13472 18558 13812 -758 342 -1761 C ATOM 936 CG2 VAL A 130 68.650 7.588 31.488 1.00110.15 C ANISOU 936 CG2 VAL A 130 12332 16903 12616 -676 328 -1647 C ATOM 937 N LEU A 131 67.824 5.190 35.248 1.00109.31 N ANISOU 937 N LEU A 131 12047 17158 12328 -529 241 -1548 N ATOM 938 CA LEU A 131 67.762 5.020 36.692 1.00115.57 C ANISOU 938 CA LEU A 131 12733 18145 13034 -537 230 -1578 C ATOM 939 C LEU A 131 68.170 3.623 37.147 1.00112.66 C ANISOU 939 C LEU A 131 12272 17949 12584 -459 186 -1568 C ATOM 940 O LEU A 131 68.372 3.391 38.334 1.00114.44 O ANISOU 940 O LEU A 131 12372 18402 12709 -464 170 -1615 O ATOM 941 CB LEU A 131 66.369 5.366 37.219 1.00121.97 C ANISOU 941 CB LEU A 131 13671 18753 13918 -512 240 -1458 C ATOM 942 CG LEU A 131 65.936 6.812 36.964 1.00127.20 C ANISOU 942 CG LEU A 131 14404 19280 14645 -586 283 -1474 C ATOM 943 CD1 LEU A 131 64.552 7.095 37.569 1.00124.03 C ANISOU 943 CD1 LEU A 131 14109 18706 14311 -553 289 -1364 C ATOM 944 CD2 LEU A 131 66.995 7.796 37.484 1.00126.86 C ANISOU 944 CD2 LEU A 131 14196 19500 14506 -721 313 -1661 C ATOM 945 N SER A 132 68.285 2.691 36.212 1.00109.00 N ANISOU 945 N SER A 132 11867 17391 12159 -388 166 -1509 N ATOM 946 CA SER A 132 68.740 1.352 36.557 1.00112.47 C ANISOU 946 CA SER A 132 12213 18003 12518 -312 126 -1504 C ATOM 947 C SER A 132 70.259 1.265 36.674 1.00117.60 C ANISOU 947 C SER A 132 12647 18997 13040 -344 111 -1679 C ATOM 948 O SER A 132 70.773 0.527 37.510 1.00120.64 O ANISOU 948 O SER A 132 12885 19643 13308 -301 78 -1723 O ATOM 949 CB SER A 132 68.205 0.329 35.562 1.00116.55 C ANISOU 949 CB SER A 132 12874 18286 13122 -227 113 -1374 C ATOM 950 OG SER A 132 66.805 0.170 35.727 1.00119.50 O ANISOU 950 OG SER A 132 13413 18401 13590 -189 121 -1225 O ATOM 951 N PHE A 133 70.970 2.017 35.834 1.00117.31 N ANISOU 951 N PHE A 133 12584 18968 13022 -418 135 -1783 N ATOM 952 CA PHE A 133 72.431 2.090 35.896 1.00112.02 C ANISOU 952 CA PHE A 133 11708 18585 12270 -469 109 -1956 C ATOM 953 C PHE A 133 72.884 2.896 37.098 1.00109.53 C ANISOU 953 C PHE A 133 11261 18417 11940 -563 64 -2030 C ATOM 954 O PHE A 133 73.723 2.451 37.884 1.00106.62 O ANISOU 954 O PHE A 133 10744 18184 11584 -561 -61 -2041 O ATOM 955 CB PHE A 133 72.981 2.750 34.639 1.00106.05 C ANISOU 955 CB PHE A 133 10969 17776 11548 -536 158 -2052 C ATOM 956 CG PHE A 133 73.064 1.834 33.464 1.00102.95 C ANISOU 956 CG PHE A 133 10647 17261 11207 -460 140 -1991 C ATOM 957 CD1 PHE A 133 71.928 1.199 32.982 1.00 98.69 C ANISOU 957 CD1 PHE A 133 10305 16427 10767 -376 128 -1797 C ATOM 958 CD2 PHE A 133 74.276 1.616 32.830 1.00 98.64 C ANISOU 958 CD2 PHE A 133 9985 16783 10711 -484 88 -2069 C ATOM 959 CE1 PHE A 133 72.003 0.355 31.894 1.00 95.10 C ANISOU 959 CE1 PHE A 133 9911 15863 10358 -317 112 -1744 C ATOM 960 CE2 PHE A 133 74.358 0.779 31.739 1.00 96.02 C ANISOU 960 CE2 PHE A 133 9709 16357 10417 -418 79 -2024 C ATOM 961 CZ PHE A 133 73.222 0.147 31.267 1.00 94.65 C ANISOU 961 CZ PHE A 133 9720 15989 10253 -335 106 -1884 C ATOM 962 N ALA A 134 72.315 4.092 37.216 1.00106.66 N ANISOU 962 N ALA A 134 10953 18024 11547 -649 161 -2083 N ATOM 963 CA ALA A 134 72.594 5.005 38.316 1.00104.28 C ANISOU 963 CA ALA A 134 10550 17846 11227 -759 134 -2160 C ATOM 964 C ALA A 134 72.314 4.364 39.677 1.00103.69 C ANISOU 964 C ALA A 134 10422 17855 11121 -707 43 -2082 C ATOM 965 O ALA A 134 73.020 4.622 40.652 1.00111.79 O ANISOU 965 O ALA A 134 11313 19028 12136 -775 -58 -2141 O ATOM 966 CB ALA A 134 71.778 6.282 38.149 1.00 96.20 C ANISOU 966 CB ALA A 134 9631 16724 10198 -842 259 -2194 C ATOM 967 N ILE A 135 71.268 3.546 39.738 1.00 92.10 N ANISOU 967 N ILE A 135 9063 16295 9637 -593 77 -1954 N ATOM 968 CA ILE A 135 70.917 2.803 40.946 1.00 92.47 C ANISOU 968 CA ILE A 135 9074 16402 9657 -532 -5 -1867 C ATOM 969 C ILE A 135 71.748 1.530 41.125 1.00 97.00 C ANISOU 969 C ILE A 135 9555 17049 10250 -447 -146 -1820 C ATOM 970 O ILE A 135 72.038 1.117 42.252 1.00102.47 O ANISOU 970 O ILE A 135 10156 17855 10923 -431 -267 -1796 O ATOM 971 CB ILE A 135 69.415 2.414 40.956 1.00 99.27 C ANISOU 971 CB ILE A 135 10083 17135 10502 -450 96 -1750 C ATOM 972 CG1 ILE A 135 68.568 3.492 41.645 1.00 96.62 C ANISOU 972 CG1 ILE A 135 9795 16732 10185 -528 140 -1747 C ATOM 973 CG2 ILE A 135 69.202 1.061 41.632 1.00 95.77 C ANISOU 973 CG2 ILE A 135 9626 16711 10051 -341 11 -1635 C ATOM 974 CD1 ILE A 135 67.085 3.175 41.690 1.00 87.43 C ANISOU 974 CD1 ILE A 135 8818 15263 9139 -458 143 -1568 C ATOM 975 N GLY A 136 72.116 0.897 40.016 1.00 93.71 N ANISOU 975 N GLY A 136 9166 16566 9873 -390 -138 -1805 N ATOM 976 CA GLY A 136 72.766 -0.398 40.081 1.00 97.77 C ANISOU 976 CA GLY A 136 9607 17125 10416 -295 -258 -1744 C ATOM 977 C GLY A 136 74.225 -0.245 40.420 1.00107.07 C ANISOU 977 C GLY A 136 10592 18467 11622 -349 -394 -1837 C ATOM 978 O GLY A 136 74.821 -1.074 41.109 1.00104.13 O ANISOU 978 O GLY A 136 10110 18197 11257 -291 -534 -1799 O ATOM 979 N LEU A 137 74.793 0.837 39.902 1.00116.85 N ANISOU 979 N LEU A 137 11789 19730 12878 -463 -351 -1961 N ATOM 980 CA LEU A 137 76.217 1.138 40.019 1.00117.70 C ANISOU 980 CA LEU A 137 11709 19990 13023 -537 -459 -2073 C ATOM 981 C LEU A 137 76.627 2.116 41.151 1.00127.35 C ANISOU 981 C LEU A 137 12817 21363 14205 -659 -521 -2170 C ATOM 982 O LEU A 137 77.770 2.567 41.179 1.00132.78 O ANISOU 982 O LEU A 137 13352 22176 14922 -747 -592 -2285 O ATOM 983 CB LEU A 137 76.794 1.533 38.647 1.00108.87 C ANISOU 983 CB LEU A 137 10591 18813 11964 -586 -389 -2156 C ATOM 984 CG LEU A 137 76.564 0.469 37.558 1.00 99.56 C ANISOU 984 CG LEU A 137 9501 17501 10824 -470 -360 -2066 C ATOM 985 CD1 LEU A 137 77.293 0.810 36.260 1.00 98.69 C ANISOU 985 CD1 LEU A 137 9367 17352 10778 -522 -317 -2155 C ATOM 986 CD2 LEU A 137 76.971 -0.925 38.043 1.00 93.98 C ANISOU 986 CD2 LEU A 137 8709 16857 10143 -350 -495 -1973 C ATOM 987 N THR A 138 75.699 2.477 42.045 1.00122.54 N ANISOU 987 N THR A 138 12281 20743 13533 -675 -492 -2133 N ATOM 988 CA THR A 138 76.021 3.386 43.164 1.00123.67 C ANISOU 988 CA THR A 138 12331 21026 13633 -798 -557 -2223 C ATOM 989 C THR A 138 77.342 3.068 43.884 1.00125.50 C ANISOU 989 C THR A 138 12360 21455 13870 -819 -752 -2280 C ATOM 990 O THR A 138 78.092 3.984 44.213 1.00130.21 O ANISOU 990 O THR A 138 12846 22170 14459 -956 -793 -2412 O ATOM 991 CB THR A 138 74.896 3.482 44.232 1.00102.33 C ANISOU 991 CB THR A 138 9716 18301 10863 -785 -544 -2150 C ATOM 992 OG1 THR A 138 73.672 3.888 43.617 1.00100.92 O ANISOU 992 OG1 THR A 138 9706 17953 10685 -775 -366 -2107 O ATOM 993 CG2 THR A 138 75.265 4.508 45.307 1.00103.81 C ANISOU 993 CG2 THR A 138 9815 18627 11002 -930 -612 -2258 C ATOM 994 N PRO A 139 77.621 1.776 44.146 1.00120.20 N ANISOU 994 N PRO A 139 11637 20822 13211 -685 -875 -2184 N ATOM 995 CA PRO A 139 78.914 1.365 44.706 1.00124.05 C ANISOU 995 CA PRO A 139 11924 21497 13715 -683 -1069 -2228 C ATOM 996 C PRO A 139 80.107 1.921 43.912 1.00134.80 C ANISOU 996 C PRO A 139 13147 22926 15143 -779 -1069 -2365 C ATOM 997 O PRO A 139 81.228 1.986 44.422 1.00140.93 O ANISOU 997 O PRO A 139 13736 23881 15931 -828 -1217 -2446 O ATOM 998 CB PRO A 139 78.865 -0.156 44.584 1.00116.15 C ANISOU 998 CB PRO A 139 10931 20457 12742 -506 -1140 -2089 C ATOM 999 CG PRO A 139 77.440 -0.480 44.740 1.00112.12 C ANISOU 999 CG PRO A 139 10611 19800 12188 -436 -1038 -1970 C ATOM 1000 CD PRO A 139 76.669 0.651 44.109 1.00113.93 C ANISOU 1000 CD PRO A 139 10969 19909 12410 -533 -848 -2025 C ATOM 1001 N MET A 140 79.862 2.285 42.659 1.00132.92 N ANISOU 1001 N MET A 140 13002 22550 14952 -803 -911 -2391 N ATOM 1002 CA MET A 140 80.852 2.968 41.839 1.00128.73 C ANISOU 1002 CA MET A 140 12366 22062 14485 -912 -880 -2529 C ATOM 1003 C MET A 140 80.880 4.464 42.153 1.00126.83 C ANISOU 1003 C MET A 140 12116 21866 14206 -1098 -815 -2668 C ATOM 1004 O MET A 140 81.908 5.118 41.997 1.00130.69 O ANISOU 1004 O MET A 140 12462 22462 14732 -1222 -842 -2807 O ATOM 1005 CB MET A 140 80.515 2.753 40.373 1.00125.30 C ANISOU 1005 CB MET A 140 12052 21451 14106 -863 -741 -2497 C ATOM 1006 CG MET A 140 81.684 2.825 39.444 1.00127.33 C ANISOU 1006 CG MET A 140 12176 21751 14452 -910 -752 -2594 C ATOM 1007 SD MET A 140 81.145 2.162 37.871 1.00114.66 S ANISOU 1007 SD MET A 140 10733 19932 12900 -806 -628 -2510 S ATOM 1008 CE MET A 140 79.705 3.190 37.590 1.00198.01 C ANISOU 1008 CE MET A 140 21533 30320 23383 -862 -439 -2503 C ATOM 1009 N LEU A 141 79.734 4.993 42.583 1.00123.86 N ANISOU 1009 N LEU A 141 11893 21406 13764 -1120 -724 -2630 N ATOM 1010 CA LEU A 141 79.568 6.409 42.946 1.00127.78 C ANISOU 1010 CA LEU A 141 12407 21923 14220 -1292 -650 -2746 C ATOM 1011 C LEU A 141 80.352 6.865 44.191 1.00132.26 C ANISOU 1011 C LEU A 141 12813 22695 14744 -1407 -799 -2846 C ATOM 1012 O LEU A 141 80.295 8.039 44.569 1.00127.39 O ANISOU 1012 O LEU A 141 12202 22107 14092 -1566 -750 -2953 O ATOM 1013 CB LEU A 141 78.086 6.797 43.058 1.00126.61 C ANISOU 1013 CB LEU A 141 12459 21625 14021 -1274 -513 -2669 C ATOM 1014 CG LEU A 141 77.391 7.293 41.782 1.00127.75 C ANISOU 1014 CG LEU A 141 12760 21583 14196 -1277 -320 -2666 C ATOM 1015 CD1 LEU A 141 77.973 8.623 41.303 1.00126.19 C ANISOU 1015 CD1 LEU A 141 12524 21403 14020 -1458 -237 -2830 C ATOM 1016 CD2 LEU A 141 77.449 6.248 40.672 1.00128.98 C ANISOU 1016 CD2 LEU A 141 12958 21643 14405 -1139 -304 -2584 C ATOM 1017 N GLY A 142 81.071 5.939 44.825 1.00138.02 N ANISOU 1017 N GLY A 142 13402 23563 15474 -1329 -986 -2810 N ATOM 1018 CA GLY A 142 81.733 6.209 46.093 1.00143.52 C ANISOU 1018 CA GLY A 142 13956 24458 16115 -1415 -1156 -2885 C ATOM 1019 C GLY A 142 81.132 5.507 47.302 1.00146.60 C ANISOU 1019 C GLY A 142 14388 24886 16426 -1315 -1277 -2768 C ATOM 1020 O GLY A 142 81.479 5.812 48.445 1.00146.54 O ANISOU 1020 O GLY A 142 14298 25029 16351 -1390 -1415 -2824 O ATOM 1021 N TRP A 143 80.235 4.558 47.044 1.00148.36 N ANISOU 1021 N TRP A 143 14743 24972 16655 -1150 -1229 -2608 N ATOM 1022 CA TRP A 143 79.696 3.681 48.085 1.00148.75 C ANISOU 1022 CA TRP A 143 14832 25046 16641 -1034 -1345 -2482 C ATOM 1023 C TRP A 143 80.594 2.449 48.254 1.00152.07 C ANISOU 1023 C TRP A 143 15112 25577 17091 -907 -1528 -2425 C ATOM 1024 O TRP A 143 80.196 1.462 48.870 1.00154.74 O ANISOU 1024 O TRP A 143 15489 25912 17395 -776 -1618 -2298 O ATOM 1025 CB TRP A 143 78.237 3.276 47.821 1.00141.91 C ANISOU 1025 CB TRP A 143 14172 23982 15764 -930 -1201 -2342 C ATOM 1026 CG TRP A 143 77.504 2.867 49.083 1.00144.61 C ANISOU 1026 CG TRP A 143 14574 24348 16023 -876 -1288 -2250 C ATOM 1027 CD1 TRP A 143 77.908 1.941 50.001 1.00145.26 C ANISOU 1027 CD1 TRP A 143 14579 24547 16065 -787 -1484 -2187 C ATOM 1028 CD2 TRP A 143 76.247 3.374 49.560 1.00147.46 C ANISOU 1028 CD2 TRP A 143 15083 24613 16331 -908 -1187 -2212 C ATOM 1029 NE1 TRP A 143 76.988 1.839 51.016 1.00146.10 N ANISOU 1029 NE1 TRP A 143 14786 24634 16092 -766 -1510 -2115 N ATOM 1030 CE2 TRP A 143 75.959 2.707 50.769 1.00147.22 C ANISOU 1030 CE2 TRP A 143 15061 24647 16229 -840 -1328 -2130 C ATOM 1031 CE3 TRP A 143 75.339 4.324 49.081 1.00147.35 C ANISOU 1031 CE3 TRP A 143 15192 24466 16326 -984 -994 -2239 C ATOM 1032 CZ2 TRP A 143 74.801 2.958 51.504 1.00147.25 C ANISOU 1032 CZ2 TRP A 143 15190 24586 16173 -852 -1280 -2078 C ATOM 1033 CZ3 TRP A 143 74.189 4.571 49.816 1.00146.65 C ANISOU 1033 CZ3 TRP A 143 15218 24317 16185 -991 -948 -2184 C ATOM 1034 CH2 TRP A 143 73.932 3.891 51.013 1.00146.27 C ANISOU 1034 CH2 TRP A 143 15173 24335 16069 -929 -1088 -2107 C ATOM 1035 N ASN A 144 81.770 2.484 47.627 1.00150.75 N ANISOU 1035 N ASN A 144 14787 25495 16997 -941 -1573 -2514 N ATOM 1036 CA ASN A 144 82.779 1.430 47.785 1.00153.03 C ANISOU 1036 CA ASN A 144 14908 25911 17325 -835 -1758 -2478 C ATOM 1037 C ASN A 144 83.195 1.115 49.238 1.00152.86 C ANISOU 1037 C ASN A 144 14780 26077 17223 -817 -1990 -2467 C ATOM 1038 O ASN A 144 83.457 2.012 50.051 1.00154.37 O ANISOU 1038 O ASN A 144 14916 26392 17347 -956 -2056 -2575 O ATOM 1039 CB ASN A 144 84.027 1.728 46.931 1.00159.38 C ANISOU 1039 CB ASN A 144 15536 26796 18224 -906 -1765 -2602 C ATOM 1040 CG ASN A 144 84.970 2.753 47.578 1.00162.59 C ANISOU 1040 CG ASN A 144 15773 27400 18604 -1084 -1864 -2774 C ATOM 1041 OD1 ASN A 144 85.656 2.461 48.565 1.00161.68 O ANISOU 1041 OD1 ASN A 144 15510 27470 18450 -1075 -2071 -2789 O ATOM 1042 ND2 ASN A 144 85.022 3.949 47.002 1.00162.31 N ANISOU 1042 ND2 ASN A 144 15757 27327 18588 -1249 -1719 -2906 N ATOM 1043 N ASN A 145 83.265 -0.179 49.541 1.00144.87 N ANISOU 1043 N ASN A 145 13746 25083 16214 -646 -2116 -2337 N ATOM 1044 CA ASN A 145 83.635 -0.665 50.865 1.00135.70 C ANISOU 1044 CA ASN A 145 12498 24089 14973 -596 -2349 -2302 C ATOM 1045 C ASN A 145 85.126 -1.000 50.983 1.00140.22 C ANISOU 1045 C ASN A 145 12817 24868 15594 -582 -2549 -2366 C ATOM 1046 O ASN A 145 85.564 -1.517 52.011 1.00147.87 O ANISOU 1046 O ASN A 145 13694 25988 16502 -521 -2766 -2331 O ATOM 1047 CB ASN A 145 82.799 -1.906 51.205 1.00120.38 C ANISOU 1047 CB ASN A 145 10687 22049 13003 -413 -2377 -2116 C ATOM 1048 CG ASN A 145 82.330 -1.930 52.651 1.00110.69 C ANISOU 1048 CG ASN A 145 9516 20895 11645 -409 -2510 -2072 C ATOM 1049 OD1 ASN A 145 81.243 -1.442 52.976 1.00 95.72 O ANISOU 1049 OD1 ASN A 145 7785 18898 9687 -459 -2399 -2052 O ATOM 1050 ND2 ASN A 145 83.144 -2.516 53.526 1.00117.20 N ANISOU 1050 ND2 ASN A 145 10204 21899 12427 -346 -2754 -2054 N ATOM 1051 N CYS A 146 85.906 -0.720 49.941 1.00137.47 N ANISOU 1051 N CYS A 146 12351 24528 15351 -635 -2482 -2457 N ATOM 1052 CA CYS A 146 87.256 -1.294 49.851 1.00145.12 C ANISOU 1052 CA CYS A 146 13079 25666 16396 -582 -2655 -2488 C ATOM 1053 C CYS A 146 88.453 -0.497 50.429 1.00140.00 C ANISOU 1053 C CYS A 146 12200 25261 15735 -729 -2808 -2656 C ATOM 1054 O CYS A 146 88.953 -0.821 51.511 1.00134.83 O ANISOU 1054 O CYS A 146 11430 24784 15014 -694 -3034 -2647 O ATOM 1055 CB CYS A 146 87.553 -1.723 48.403 1.00150.79 C ANISOU 1055 CB CYS A 146 13772 26271 17251 -524 -2529 -2475 C ATOM 1056 SG CYS A 146 86.419 -1.068 47.127 1.00150.65 S ANISOU 1056 SG CYS A 146 13998 25982 17262 -590 -2211 -2479 S ATOM 1057 N GLY A 147 88.894 0.541 49.722 1.00136.92 N ANISOU 1057 N GLY A 147 11745 24877 15400 -896 -2689 -2811 N ATOM 1058 CA GLY A 147 90.127 1.232 50.072 1.00139.69 C ANISOU 1058 CA GLY A 147 11856 25456 15764 -1040 -2819 -2980 C ATOM 1059 C GLY A 147 90.097 1.964 51.400 1.00140.55 C ANISOU 1059 C GLY A 147 11953 25709 15740 -1163 -2945 -3057 C ATOM 1060 O GLY A 147 89.259 2.842 51.613 1.00136.35 O ANISOU 1060 O GLY A 147 11587 25084 15134 -1278 -2819 -3095 O ATOM 1061 N GLN A 148 91.033 1.620 52.282 1.00143.34 N ANISOU 1061 N GLN A 148 12105 26293 16063 -1141 -3200 -3084 N ATOM 1062 CA GLN A 148 91.090 2.196 53.628 1.00143.64 C ANISOU 1062 CA GLN A 148 12122 26491 15963 -1246 -3360 -3153 C ATOM 1063 C GLN A 148 92.507 2.153 54.196 1.00144.77 C ANISOU 1063 C GLN A 148 11971 26919 16115 -1286 -3612 -3257 C ATOM 1064 O GLN A 148 93.395 2.868 53.738 1.00120.74 O ANISOU 1064 O GLN A 148 8753 23977 13145 -1436 -3587 -3421 O ATOM 1065 CB GLN A 148 90.120 1.469 54.574 1.00142.60 C ANISOU 1065 CB GLN A 148 12170 26298 15711 -1104 -3444 -2986 C ATOM 1066 CG GLN A 148 88.641 1.689 54.259 1.00136.46 C ANISOU 1066 CG GLN A 148 11681 25266 14902 -1096 -3210 -2903 C ATOM 1067 CD GLN A 148 87.795 0.441 54.459 1.00134.50 C ANISOU 1067 CD GLN A 148 11583 24893 14626 -878 -3230 -2692 C ATOM 1068 OE1 GLN A 148 87.996 -0.316 55.412 1.00136.23 O ANISOU 1068 OE1 GLN A 148 11760 25226 14773 -769 -3446 -2612 O ATOM 1069 NE2 GLN A 148 86.848 0.219 53.555 1.00100.18 N ANISOU 1069 NE2 GLN A 148 7415 20314 10336 -815 -3008 -2603 N ATOM 1070 N SER A 156 92.552 -13.423 51.352 1.00151.22 N ANISOU 1070 N SER A 156 12807 27031 17617 1250 -4225 -1398 N ATOM 1071 CA SER A 156 93.702 -13.858 50.567 1.00152.90 C ANISOU 1071 CA SER A 156 12776 27323 17996 1322 -4272 -1426 C ATOM 1072 C SER A 156 94.552 -12.671 50.140 1.00155.67 C ANISOU 1072 C SER A 156 12930 27808 18409 1132 -4242 -1625 C ATOM 1073 O SER A 156 94.306 -12.078 49.089 1.00153.27 O ANISOU 1073 O SER A 156 12689 27373 18174 1011 -4022 -1706 O ATOM 1074 CB SER A 156 93.238 -14.599 49.310 1.00144.22 C ANISOU 1074 CB SER A 156 11793 25987 17015 1403 -4071 -1346 C ATOM 1075 OG SER A 156 92.774 -13.686 48.325 1.00136.25 O ANISOU 1075 OG SER A 156 10890 24839 16040 1229 -3824 -1453 O ATOM 1076 N GLN A 157 95.559 -12.312 50.924 1.00161.80 N ANISOU 1076 N GLN A 157 13469 28846 19162 1101 -4463 -1706 N ATOM 1077 CA GLN A 157 96.411 -11.234 50.460 1.00169.57 C ANISOU 1077 CA GLN A 157 14252 29957 20218 918 -4428 -1900 C ATOM 1078 C GLN A 157 97.725 -11.785 49.899 1.00180.64 C ANISOU 1078 C GLN A 157 15348 31495 21791 1012 -4530 -1921 C ATOM 1079 O GLN A 157 98.687 -12.051 50.634 1.00182.54 O ANISOU 1079 O GLN A 157 15350 31972 22034 1084 -4778 -1928 O ATOM 1080 CB GLN A 157 96.664 -10.258 51.625 1.00167.56 C ANISOU 1080 CB GLN A 157 13926 29909 19828 774 -4581 -2014 C ATOM 1081 CG GLN A 157 97.839 -9.302 51.461 1.00165.06 C ANISOU 1081 CG GLN A 157 13328 29805 19580 608 -4635 -2213 C ATOM 1082 CD GLN A 157 99.101 -9.799 52.147 1.00165.14 C ANISOU 1082 CD GLN A 157 13027 30095 19621 713 -4934 -2215 C ATOM 1083 OE1 GLN A 157 99.086 -10.815 52.842 1.00161.08 O ANISOU 1083 OE1 GLN A 157 12519 29623 19060 911 -5114 -2064 O ATOM 1084 NE2 GLN A 157 100.202 -9.083 51.951 1.00168.10 N ANISOU 1084 NE2 GLN A 157 13128 30666 20076 581 -4988 -2385 N ATOM 1085 N GLY A 158 97.739 -11.983 48.581 1.00183.24 N ANISOU 1085 N GLY A 158 15689 31671 22263 1018 -4337 -1927 N ATOM 1086 CA GLY A 158 98.937 -11.885 47.774 1.00188.42 C ANISOU 1086 CA GLY A 158 16062 32439 23090 993 -4343 -2029 C ATOM 1087 C GLY A 158 98.799 -10.773 46.748 1.00187.22 C ANISOU 1087 C GLY A 158 15961 32186 22987 776 -4100 -2182 C ATOM 1088 O GLY A 158 99.791 -10.331 46.164 1.00189.35 O ANISOU 1088 O GLY A 158 15996 32570 23377 690 -4090 -2312 O ATOM 1089 N CYS A 159 97.562 -10.307 46.553 1.00182.09 N ANISOU 1089 N CYS A 159 15617 31327 22242 689 -3907 -2166 N ATOM 1090 CA CYS A 159 97.198 -9.501 45.380 1.00178.87 C ANISOU 1090 CA CYS A 159 15323 30754 21885 530 -3646 -2265 C ATOM 1091 C CYS A 159 97.887 -8.136 45.256 1.00182.39 C ANISOU 1091 C CYS A 159 15613 31339 22347 299 -3612 -2477 C ATOM 1092 O CYS A 159 98.581 -7.886 44.270 1.00183.04 O ANISOU 1092 O CYS A 159 15553 31429 22563 235 -3523 -2571 O ATOM 1093 CB CYS A 159 95.677 -9.328 45.306 1.00174.63 C ANISOU 1093 CB CYS A 159 15146 29973 21232 502 -3464 -2191 C ATOM 1094 SG CYS A 159 94.771 -10.801 44.771 1.00214.69 S ANISOU 1094 SG CYS A 159 20437 34801 26336 722 -3384 -1975 S ATOM 1095 N GLY A 160 97.656 -7.248 46.224 1.00182.93 N ANISOU 1095 N GLY A 160 15720 31506 22280 168 -3672 -2554 N ATOM 1096 CA GLY A 160 98.474 -6.055 46.414 1.00183.62 C ANISOU 1096 CA GLY A 160 15613 31782 22371 -39 -3706 -2755 C ATOM 1097 C GLY A 160 98.533 -5.011 45.306 1.00179.18 C ANISOU 1097 C GLY A 160 15073 31128 21878 -235 -3475 -2905 C ATOM 1098 O GLY A 160 97.882 -5.142 44.267 1.00173.75 O ANISOU 1098 O GLY A 160 14570 30213 21235 -217 -3268 -2857 O ATOM 1099 N GLU A 161 99.319 -3.960 45.552 1.00178.71 N ANISOU 1099 N GLU A 161 14826 31252 21823 -427 -3515 -3091 N ATOM 1100 CA GLU A 161 99.751 -3.006 44.524 1.00172.32 C ANISOU 1100 CA GLU A 161 13952 30415 21107 -616 -3335 -3257 C ATOM 1101 C GLU A 161 98.665 -2.655 43.490 1.00164.88 C ANISOU 1101 C GLU A 161 13312 29182 20155 -663 -3056 -3230 C ATOM 1102 O GLU A 161 98.776 -3.008 42.315 1.00160.81 O ANISOU 1102 O GLU A 161 12803 28540 19756 -620 -2926 -3210 O ATOM 1103 CB GLU A 161 101.032 -3.504 43.833 1.00169.50 C ANISOU 1103 CB GLU A 161 13289 30182 20933 -565 -3393 -3302 C ATOM 1104 CG GLU A 161 102.180 -2.490 43.768 1.00168.61 C ANISOU 1104 CG GLU A 161 12900 30278 20886 -776 -3415 -3524 C ATOM 1105 CD GLU A 161 103.052 -2.478 45.020 1.00169.38 C ANISOU 1105 CD GLU A 161 12733 30679 20944 -784 -3692 -3580 C ATOM 1106 OE1 GLU A 161 104.105 -1.804 45.010 1.00164.81 O ANISOU 1106 OE1 GLU A 161 11888 30299 20434 -939 -3740 -3757 O ATOM 1107 OE2 GLU A 161 102.689 -3.139 46.014 1.00172.99 O ANISOU 1107 OE2 GLU A 161 13248 31180 21301 -639 -3866 -3451 O ATOM 1108 N GLY A 162 97.611 -1.978 43.935 1.00161.26 N ANISOU 1108 N GLY A 162 13100 28616 19555 -746 -2969 -3227 N ATOM 1109 CA GLY A 162 96.581 -1.490 43.031 1.00161.27 C ANISOU 1109 CA GLY A 162 13379 28361 19537 -807 -2712 -3216 C ATOM 1110 C GLY A 162 95.470 -2.494 42.757 1.00160.26 C ANISOU 1110 C GLY A 162 13501 28011 19379 -618 -2646 -3017 C ATOM 1111 O GLY A 162 94.346 -2.121 42.404 1.00148.50 O ANISOU 1111 O GLY A 162 12281 26320 17823 -651 -2471 -2981 O ATOM 1112 N GLN A 163 95.787 -3.775 42.935 1.00166.05 N ANISOU 1112 N GLN A 163 14142 28787 20163 -419 -2789 -2888 N ATOM 1113 CA GLN A 163 94.810 -4.846 42.783 1.00156.95 C ANISOU 1113 CA GLN A 163 13205 27445 18985 -234 -2749 -2697 C ATOM 1114 C GLN A 163 94.327 -5.280 44.161 1.00159.16 C ANISOU 1114 C GLN A 163 13546 27793 19136 -142 -2912 -2594 C ATOM 1115 O GLN A 163 95.126 -5.648 45.019 1.00165.10 O ANISOU 1115 O GLN A 163 14092 28753 19887 -85 -3132 -2593 O ATOM 1116 CB GLN A 163 95.424 -6.061 42.074 1.00149.59 C ANISOU 1116 CB GLN A 163 12145 26499 18194 -65 -2794 -2610 C ATOM 1117 CG GLN A 163 96.285 -5.749 40.866 1.00146.56 C ANISOU 1117 CG GLN A 163 11607 26121 17960 -146 -2695 -2723 C ATOM 1118 CD GLN A 163 95.480 -5.281 39.680 1.00142.92 C ANISOU 1118 CD GLN A 163 11381 25418 17505 -223 -2443 -2739 C ATOM 1119 OE1 GLN A 163 94.788 -4.266 39.747 1.00141.66 O ANISOU 1119 OE1 GLN A 163 11389 25186 17251 -363 -2325 -2804 O ATOM 1120 NE2 GLN A 163 95.564 -6.019 38.581 1.00141.00 N ANISOU 1120 NE2 GLN A 163 11151 25049 17373 -131 -2362 -2678 N ATOM 1121 N VAL A 164 93.022 -5.230 44.382 1.00156.22 N ANISOU 1121 N VAL A 164 13454 27249 18654 -128 -2808 -2508 N ATOM 1122 CA VAL A 164 92.447 -5.843 45.572 1.00155.36 C ANISOU 1122 CA VAL A 164 13431 27167 18431 -15 -2945 -2382 C ATOM 1123 C VAL A 164 91.401 -6.882 45.152 1.00151.26 C ANISOU 1123 C VAL A 164 13140 26423 17909 146 -2848 -2206 C ATOM 1124 O VAL A 164 90.522 -6.597 44.337 1.00140.58 O ANISOU 1124 O VAL A 164 11993 24866 16553 102 -2638 -2194 O ATOM 1125 CB VAL A 164 91.878 -4.795 46.561 1.00150.51 C ANISOU 1125 CB VAL A 164 12915 26600 17671 -156 -2948 -2449 C ATOM 1126 CG1 VAL A 164 92.977 -3.796 46.963 1.00150.57 C ANISOU 1126 CG1 VAL A 164 12686 26839 17686 -324 -3051 -2634 C ATOM 1127 CG2 VAL A 164 90.661 -4.083 45.975 1.00141.07 C ANISOU 1127 CG2 VAL A 164 11991 25181 16429 -248 -2699 -2455 C ATOM 1128 N ALA A 165 91.516 -8.089 45.703 1.00156.53 N ANISOU 1128 N ALA A 165 13765 27131 18576 329 -3004 -2070 N ATOM 1129 CA ALA A 165 90.720 -9.224 45.244 1.00153.98 C ANISOU 1129 CA ALA A 165 13619 26613 18275 489 -2929 -1906 C ATOM 1130 C ALA A 165 89.252 -8.861 45.274 1.00155.28 C ANISOU 1130 C ALA A 165 14082 26584 18334 440 -2757 -1859 C ATOM 1131 O ALA A 165 88.817 -8.097 46.136 1.00156.79 O ANISOU 1131 O ALA A 165 14337 26825 18413 347 -2773 -1900 O ATOM 1132 CB ALA A 165 90.983 -10.448 46.109 1.00153.89 C ANISOU 1132 CB ALA A 165 13533 26690 18248 681 -3139 -1770 C ATOM 1133 N CYS A 166 88.490 -9.397 44.323 1.00155.74 N ANISOU 1133 N CYS A 166 14316 26425 18432 500 -2592 -1777 N ATOM 1134 CA CYS A 166 87.083 -9.027 44.184 1.00148.38 C ANISOU 1134 CA CYS A 166 13659 25301 17415 449 -2411 -1739 C ATOM 1135 C CYS A 166 86.136 -10.085 44.745 1.00143.63 C ANISOU 1135 C CYS A 166 13220 24600 16752 593 -2434 -1571 C ATOM 1136 O CYS A 166 85.941 -11.146 44.148 1.00137.69 O ANISOU 1136 O CYS A 166 12523 23732 16062 717 -2402 -1467 O ATOM 1137 CB CYS A 166 86.741 -8.734 42.719 1.00141.40 C ANISOU 1137 CB CYS A 166 12887 24237 16602 392 -2196 -1776 C ATOM 1138 SG CYS A 166 85.308 -7.643 42.495 1.00161.85 S ANISOU 1138 SG CYS A 166 15752 26653 19092 260 -1971 -1806 S ATOM 1139 N LEU A 167 85.538 -9.757 45.890 1.00144.66 N ANISOU 1139 N LEU A 167 13429 24774 16761 567 -2486 -1551 N ATOM 1140 CA LEU A 167 84.559 -10.602 46.564 1.00144.48 C ANISOU 1140 CA LEU A 167 13567 24664 16664 679 -2503 -1403 C ATOM 1141 C LEU A 167 83.352 -9.732 46.884 1.00137.03 C ANISOU 1141 C LEU A 167 12820 23626 15620 570 -2362 -1421 C ATOM 1142 O LEU A 167 83.467 -8.509 46.927 1.00135.46 O ANISOU 1142 O LEU A 167 12595 23480 15392 420 -2315 -1546 O ATOM 1143 CB LEU A 167 85.136 -11.193 47.857 1.00153.78 C ANISOU 1143 CB LEU A 167 14619 26022 17789 778 -2753 -1347 C ATOM 1144 CG LEU A 167 86.161 -12.336 47.791 1.00157.41 C ANISOU 1144 CG LEU A 167 14900 26572 18335 936 -2922 -1281 C ATOM 1145 CD1 LEU A 167 85.660 -13.450 46.877 1.00155.38 C ANISOU 1145 CD1 LEU A 167 14760 26122 18155 1059 -2810 -1164 C ATOM 1146 CD2 LEU A 167 87.550 -11.860 47.360 1.00158.28 C ANISOU 1146 CD2 LEU A 167 14754 26843 18540 879 -2999 -1409 C ATOM 1147 N PHE A 168 82.201 -10.355 47.114 1.00133.36 N ANISOU 1147 N PHE A 168 12545 23022 15105 643 -2295 -1300 N ATOM 1148 CA PHE A 168 80.959 -9.599 47.264 1.00132.63 C ANISOU 1148 CA PHE A 168 12643 22816 14935 550 -2136 -1308 C ATOM 1149 C PHE A 168 80.736 -8.915 48.624 1.00138.35 C ANISOU 1149 C PHE A 168 13366 23656 15543 482 -2230 -1337 C ATOM 1150 O PHE A 168 80.358 -7.746 48.669 1.00135.55 O ANISOU 1150 O PHE A 168 13061 23294 15149 344 -2132 -1428 O ATOM 1151 CB PHE A 168 79.751 -10.460 46.894 1.00130.95 C ANISOU 1151 CB PHE A 168 12631 22403 14721 638 -2007 -1178 C ATOM 1152 CG PHE A 168 78.735 -9.736 46.056 1.00127.88 C ANISOU 1152 CG PHE A 168 12411 21847 14332 545 -1773 -1211 C ATOM 1153 CD1 PHE A 168 77.861 -8.831 46.636 1.00122.91 C ANISOU 1153 CD1 PHE A 168 11884 21196 13620 451 -1695 -1239 C ATOM 1154 CD2 PHE A 168 78.662 -9.948 44.685 1.00125.38 C ANISOU 1154 CD2 PHE A 168 12150 21395 14095 552 -1639 -1214 C ATOM 1155 CE1 PHE A 168 76.938 -8.156 45.870 1.00116.05 C ANISOU 1155 CE1 PHE A 168 11161 20179 12752 375 -1488 -1266 C ATOM 1156 CE2 PHE A 168 77.733 -9.275 43.912 1.00118.52 C ANISOU 1156 CE2 PHE A 168 11439 20378 13217 473 -1438 -1242 C ATOM 1157 CZ PHE A 168 76.874 -8.378 44.507 1.00114.60 C ANISOU 1157 CZ PHE A 168 11036 19866 12642 388 -1363 -1267 C ATOM 1158 N GLU A 169 80.972 -9.632 49.721 1.00146.35 N ANISOU 1158 N GLU A 169 14329 24777 16500 578 -2423 -1261 N ATOM 1159 CA GLU A 169 80.680 -9.110 51.062 1.00151.13 C ANISOU 1159 CA GLU A 169 14956 25483 16982 524 -2525 -1274 C ATOM 1160 C GLU A 169 81.820 -8.249 51.611 1.00156.66 C ANISOU 1160 C GLU A 169 15465 26403 17657 424 -2681 -1407 C ATOM 1161 O GLU A 169 81.789 -7.807 52.767 1.00155.43 O ANISOU 1161 O GLU A 169 15301 26362 17393 373 -2801 -1432 O ATOM 1162 CB GLU A 169 80.358 -10.241 52.043 1.00152.91 C ANISOU 1162 CB GLU A 169 15235 25724 17142 669 -2668 -1129 C ATOM 1163 CG GLU A 169 79.408 -11.294 51.502 1.00149.91 C ANISOU 1163 CG GLU A 169 15014 25147 16799 782 -2541 -994 C ATOM 1164 CD GLU A 169 80.119 -12.346 50.667 1.00151.03 C ANISOU 1164 CD GLU A 169 15070 25266 17050 906 -2576 -941 C ATOM 1165 OE1 GLU A 169 81.318 -12.161 50.368 1.00151.97 O ANISOU 1165 OE1 GLU A 169 15004 25511 17228 896 -2671 -1018 O ATOM 1166 OE2 GLU A 169 79.483 -13.362 50.314 1.00150.23 O ANISOU 1166 OE2 GLU A 169 15081 25022 16977 1012 -2508 -825 O ATOM 1167 N ASP A 170 82.837 -8.044 50.781 1.00159.25 N ANISOU 1167 N ASP A 170 15637 26790 18082 393 -2683 -1495 N ATOM 1168 CA ASP A 170 83.954 -7.175 51.126 1.00162.78 C ANISOU 1168 CA ASP A 170 15887 27440 18523 280 -2808 -1639 C ATOM 1169 C ASP A 170 83.869 -5.827 50.422 1.00156.67 C ANISOU 1169 C ASP A 170 15129 26623 17774 98 -2631 -1784 C ATOM 1170 O ASP A 170 83.843 -4.779 51.072 1.00153.84 O ANISOU 1170 O ASP A 170 14762 26350 17341 -40 -2650 -1883 O ATOM 1171 CB ASP A 170 85.282 -7.863 50.845 1.00168.67 C ANISOU 1171 CB ASP A 170 16411 28319 19359 369 -2965 -1645 C ATOM 1172 CG ASP A 170 85.575 -8.958 51.838 1.00172.33 C ANISOU 1172 CG ASP A 170 16820 28886 19773 529 -3194 -1527 C ATOM 1173 OD1 ASP A 170 85.169 -10.112 51.576 1.00169.81 O ANISOU 1173 OD1 ASP A 170 16585 28450 19487 683 -3175 -1387 O ATOM 1174 OD2 ASP A 170 86.190 -8.657 52.886 1.00175.72 O ANISOU 1174 OD2 ASP A 170 17129 29512 20124 497 -3395 -1574 O ATOM 1175 N VAL A 171 83.870 -5.859 49.093 1.00153.23 N ANISOU 1175 N VAL A 171 14719 26060 17443 97 -2468 -1799 N ATOM 1176 CA VAL A 171 83.789 -4.632 48.303 1.00151.09 C ANISOU 1176 CA VAL A 171 14475 25733 17200 -64 -2293 -1929 C ATOM 1177 C VAL A 171 82.371 -4.053 48.213 1.00141.90 C ANISOU 1177 C VAL A 171 13546 24393 15977 -121 -2097 -1903 C ATOM 1178 O VAL A 171 82.197 -2.834 48.138 1.00138.30 O ANISOU 1178 O VAL A 171 13118 23935 15496 -271 -1999 -2013 O ATOM 1179 CB VAL A 171 84.383 -4.815 46.878 1.00123.55 C ANISOU 1179 CB VAL A 171 10923 22179 13840 -52 -2200 -1965 C ATOM 1180 CG1 VAL A 171 85.872 -5.162 46.959 1.00128.75 C ANISOU 1180 CG1 VAL A 171 11317 23032 14568 -24 -2388 -2019 C ATOM 1181 CG2 VAL A 171 83.611 -5.868 46.093 1.00112.63 C ANISOU 1181 CG2 VAL A 171 9696 20598 12501 86 -2090 -1826 C ATOM 1182 N VAL A 172 81.365 -4.923 48.230 1.00137.63 N ANISOU 1182 N VAL A 172 13165 23709 15417 -1 -2040 -1759 N ATOM 1183 CA VAL A 172 79.974 -4.489 48.073 1.00134.52 C ANISOU 1183 CA VAL A 172 12986 23144 14981 -39 -1849 -1723 C ATOM 1184 C VAL A 172 79.224 -4.430 49.404 1.00127.68 C ANISOU 1184 C VAL A 172 12196 22310 14005 -39 -1915 -1670 C ATOM 1185 O VAL A 172 79.022 -5.456 50.057 1.00124.53 O ANISOU 1185 O VAL A 172 11819 21922 13574 84 -2023 -1555 O ATOM 1186 CB VAL A 172 79.204 -5.403 47.098 1.00133.91 C ANISOU 1186 CB VAL A 172 13052 22868 14958 74 -1712 -1608 C ATOM 1187 CG1 VAL A 172 77.847 -4.797 46.756 1.00124.34 C ANISOU 1187 CG1 VAL A 172 12040 21487 13716 19 -1503 -1592 C ATOM 1188 CG2 VAL A 172 80.026 -5.637 45.840 1.00136.55 C ANISOU 1188 CG2 VAL A 172 13306 23179 15400 90 -1678 -1648 C ATOM 1189 N PRO A 173 78.791 -3.224 49.802 1.00123.22 N ANISOU 1189 N PRO A 173 11679 21756 13382 -178 -1847 -1755 N ATOM 1190 CA PRO A 173 78.231 -3.078 51.152 1.00126.04 C ANISOU 1190 CA PRO A 173 12089 22170 13631 -195 -1934 -1724 C ATOM 1191 C PRO A 173 76.981 -3.934 51.376 1.00129.27 C ANISOU 1191 C PRO A 173 12667 22434 14014 -81 -1869 -1571 C ATOM 1192 O PRO A 173 76.053 -3.873 50.574 1.00132.87 O ANISOU 1192 O PRO A 173 13255 22718 14511 -75 -1673 -1535 O ATOM 1193 CB PRO A 173 77.894 -1.579 51.235 1.00121.23 C ANISOU 1193 CB PRO A 173 11518 21558 12987 -371 -1825 -1846 C ATOM 1194 CG PRO A 173 77.838 -1.101 49.809 1.00114.31 C ANISOU 1194 CG PRO A 173 10675 20558 12200 -415 -1629 -1898 C ATOM 1195 CD PRO A 173 78.778 -1.962 49.037 1.00115.46 C ANISOU 1195 CD PRO A 173 10712 20729 12429 -324 -1690 -1880 C ATOM 1196 N MET A 174 76.956 -4.718 52.450 1.00129.13 N ANISOU 1196 N MET A 174 12646 22489 13929 6 -2035 -1486 N ATOM 1197 CA MET A 174 75.738 -5.431 52.825 1.00126.99 C ANISOU 1197 CA MET A 174 12534 22093 13623 94 -1979 -1352 C ATOM 1198 C MET A 174 74.795 -4.404 53.426 1.00121.70 C ANISOU 1198 C MET A 174 11966 21390 12884 -21 -1893 -1393 C ATOM 1199 O MET A 174 73.606 -4.654 53.614 1.00116.55 O ANISOU 1199 O MET A 174 11454 20617 12214 12 -1795 -1309 O ATOM 1200 CB MET A 174 76.033 -6.555 53.820 1.00135.93 C ANISOU 1200 CB MET A 174 13637 23315 14696 220 -2192 -1250 C ATOM 1201 CG MET A 174 76.527 -7.848 53.176 1.00139.38 C ANISOU 1201 CG MET A 174 14027 23721 15211 369 -2235 -1161 C ATOM 1202 SD MET A 174 75.290 -8.677 52.144 1.00102.74 S ANISOU 1202 SD MET A 174 9561 18832 10645 456 -2009 -1044 S ATOM 1203 CE MET A 174 74.070 -9.155 53.364 1.00212.27 C ANISOU 1203 CE MET A 174 23581 32656 24416 504 -2037 -929 C ATOM 1204 N ASN A 175 75.374 -3.249 53.738 1.00124.53 N ANISOU 1204 N ASN A 175 12244 21865 13208 -161 -1936 -1527 N ATOM 1205 CA ASN A 175 74.654 -2.037 54.102 1.00125.12 C ANISOU 1205 CA ASN A 175 12395 21911 13234 -298 -1837 -1599 C ATOM 1206 C ASN A 175 73.674 -1.587 53.001 1.00122.93 C ANISOU 1206 C ASN A 175 12233 21444 13033 -324 -1576 -1593 C ATOM 1207 O ASN A 175 72.456 -1.569 53.188 1.00114.24 O ANISOU 1207 O ASN A 175 11262 20226 11916 -312 -1467 -1527 O ATOM 1208 CB ASN A 175 75.685 -0.938 54.381 1.00124.28 C ANISOU 1208 CB ASN A 175 12158 21965 13098 -447 -1926 -1760 C ATOM 1209 CG ASN A 175 75.070 0.313 54.966 1.00126.06 C ANISOU 1209 CG ASN A 175 12454 22187 13257 -598 -1862 -1842 C ATOM 1210 OD1 ASN A 175 73.974 0.731 54.581 1.00124.89 O ANISOU 1210 OD1 ASN A 175 12431 21887 13134 -622 -1674 -1818 O ATOM 1211 ND2 ASN A 175 75.778 0.924 55.908 1.00129.55 N ANISOU 1211 ND2 ASN A 175 12812 22798 13613 -702 -2024 -1943 N ATOM 1212 N TYR A 176 74.230 -1.213 51.856 1.00126.12 N ANISOU 1212 N TYR A 176 12584 21821 13516 -361 -1485 -1663 N ATOM 1213 CA TYR A 176 73.457 -0.750 50.710 1.00129.04 C ANISOU 1213 CA TYR A 176 13056 22022 13951 -385 -1254 -1667 C ATOM 1214 C TYR A 176 72.651 -1.891 50.059 1.00128.60 C ANISOU 1214 C TYR A 176 13107 21810 13943 -243 -1159 -1529 C ATOM 1215 O TYR A 176 71.620 -1.660 49.407 1.00122.75 O ANISOU 1215 O TYR A 176 12488 20919 13233 -244 -976 -1498 O ATOM 1216 CB TYR A 176 74.425 -0.088 49.719 1.00130.94 C ANISOU 1216 CB TYR A 176 13206 22294 14251 -463 -1213 -1786 C ATOM 1217 CG TYR A 176 74.044 -0.139 48.255 1.00129.68 C ANISOU 1217 CG TYR A 176 13130 21972 14170 -431 -1027 -1768 C ATOM 1218 CD1 TYR A 176 74.202 -1.305 47.507 1.00125.33 C ANISOU 1218 CD1 TYR A 176 12589 21356 13674 -303 -1029 -1684 C ATOM 1219 CD2 TYR A 176 73.575 0.993 47.607 1.00131.53 C ANISOU 1219 CD2 TYR A 176 13433 22120 14420 -532 -860 -1840 C ATOM 1220 CE1 TYR A 176 73.874 -1.343 46.166 1.00123.06 C ANISOU 1220 CE1 TYR A 176 12388 20924 13446 -280 -872 -1673 C ATOM 1221 CE2 TYR A 176 73.246 0.964 46.265 1.00129.61 C ANISOU 1221 CE2 TYR A 176 13275 21733 14236 -501 -705 -1825 C ATOM 1222 CZ TYR A 176 73.394 -0.202 45.550 1.00125.42 C ANISOU 1222 CZ TYR A 176 12761 21142 13751 -378 -714 -1744 C ATOM 1223 OH TYR A 176 73.055 -0.210 44.215 1.00123.15 O ANISOU 1223 OH TYR A 176 12571 20712 13511 -355 -571 -1735 O ATOM 1224 N MET A 177 73.118 -3.121 50.267 1.00125.78 N ANISOU 1224 N MET A 177 12704 21496 13591 -123 -1289 -1448 N ATOM 1225 CA MET A 177 72.529 -4.304 49.642 1.00114.29 C ANISOU 1225 CA MET A 177 11336 19906 12182 8 -1218 -1325 C ATOM 1226 C MET A 177 71.257 -4.797 50.304 1.00110.41 C ANISOU 1226 C MET A 177 10967 19330 11653 61 -1177 -1216 C ATOM 1227 O MET A 177 70.373 -5.332 49.636 1.00107.17 O ANISOU 1227 O MET A 177 10663 18772 11283 121 -1040 -1139 O ATOM 1228 CB MET A 177 73.547 -5.431 49.606 1.00111.80 C ANISOU 1228 CB MET A 177 10920 19667 11894 115 -1376 -1281 C ATOM 1229 CG MET A 177 74.412 -5.380 48.381 1.00112.42 C ANISOU 1229 CG MET A 177 10928 19735 12053 107 -1338 -1343 C ATOM 1230 SD MET A 177 73.435 -5.863 46.962 1.00126.86 S ANISOU 1230 SD MET A 177 12917 21336 13946 163 -1120 -1273 S ATOM 1231 CE MET A 177 72.818 -7.443 47.564 1.00 75.82 C ANISOU 1231 CE MET A 177 6517 14824 7467 315 -1187 -1108 C ATOM 1232 N VAL A 178 71.176 -4.644 51.621 1.00112.86 N ANISOU 1232 N VAL A 178 11262 19739 11882 38 -1302 -1211 N ATOM 1233 CA VAL A 178 69.967 -5.025 52.343 1.00108.82 C ANISOU 1233 CA VAL A 178 10862 19155 11328 76 -1271 -1117 C ATOM 1234 C VAL A 178 68.969 -3.866 52.371 1.00107.97 C ANISOU 1234 C VAL A 178 10831 18978 11215 -32 -1117 -1165 C ATOM 1235 O VAL A 178 67.873 -3.974 51.816 1.00103.20 O ANISOU 1235 O VAL A 178 10326 18229 10657 -9 -950 -1111 O ATOM 1236 CB VAL A 178 70.264 -5.566 53.756 1.00101.92 C ANISOU 1236 CB VAL A 178 9960 18406 10360 119 -1487 -1071 C ATOM 1237 CG1 VAL A 178 68.977 -6.042 54.413 1.00 98.18 C ANISOU 1237 CG1 VAL A 178 9612 17842 9849 163 -1446 -969 C ATOM 1238 CG2 VAL A 178 71.267 -6.714 53.676 1.00 95.26 C ANISOU 1238 CG2 VAL A 178 9033 17630 9531 236 -1641 -1018 C ATOM 1239 N TYR A 179 69.352 -2.761 53.005 1.00109.26 N ANISOU 1239 N TYR A 179 10944 19245 11323 -151 -1178 -1269 N ATOM 1240 CA TYR A 179 68.508 -1.563 53.017 1.00107.37 C ANISOU 1240 CA TYR A 179 10766 18946 11084 -261 -1039 -1326 C ATOM 1241 C TYR A 179 68.150 -1.003 51.640 1.00 96.29 C ANISOU 1241 C TYR A 179 9401 17417 9767 -290 -831 -1359 C ATOM 1242 O TYR A 179 66.981 -0.950 51.298 1.00 96.20 O ANISOU 1242 O TYR A 179 9485 17276 9792 -273 -680 -1307 O ATOM 1243 CB TYR A 179 69.088 -0.454 53.906 1.00116.24 C ANISOU 1243 CB TYR A 179 11829 20207 12130 -397 -1147 -1445 C ATOM 1244 CG TYR A 179 69.133 -0.813 55.371 1.00122.75 C ANISOU 1244 CG TYR A 179 12658 21139 12844 -385 -1338 -1413 C ATOM 1245 CD1 TYR A 179 70.343 -1.078 56.003 1.00130.14 C ANISOU 1245 CD1 TYR A 179 13491 22242 13715 -382 -1552 -1450 C ATOM 1246 CD2 TYR A 179 67.969 -0.900 56.121 1.00123.22 C ANISOU 1246 CD2 TYR A 179 12825 21133 12858 -376 -1311 -1347 C ATOM 1247 CE1 TYR A 179 70.396 -1.414 57.346 1.00133.67 C ANISOU 1247 CE1 TYR A 179 13956 22789 14044 -367 -1739 -1420 C ATOM 1248 CE2 TYR A 179 68.008 -1.236 57.463 1.00130.78 C ANISOU 1248 CE2 TYR A 179 13808 22184 13697 -365 -1492 -1319 C ATOM 1249 CZ TYR A 179 69.229 -1.494 58.072 1.00134.84 C ANISOU 1249 CZ TYR A 179 14231 22864 14137 -358 -1708 -1354 C ATOM 1250 OH TYR A 179 69.286 -1.832 59.408 1.00134.71 O ANISOU 1250 OH TYR A 179 14253 22944 13987 -343 -1900 -1324 O ATOM 1251 N PHE A 180 69.134 -0.551 50.867 1.00 95.38 N ANISOU 1251 N PHE A 180 9213 17343 9684 -335 -827 -1449 N ATOM 1252 CA PHE A 180 68.824 0.181 49.634 1.00104.67 C ANISOU 1252 CA PHE A 180 10437 18408 10923 -380 -640 -1495 C ATOM 1253 C PHE A 180 68.295 -0.660 48.462 1.00107.03 C ANISOU 1253 C PHE A 180 10820 18560 11286 -272 -515 -1409 C ATOM 1254 O PHE A 180 67.280 -0.319 47.851 1.00104.71 O ANISOU 1254 O PHE A 180 10624 18138 11023 -275 -350 -1387 O ATOM 1255 CB PHE A 180 69.997 1.058 49.163 1.00110.04 C ANISOU 1255 CB PHE A 180 11023 19173 11613 -481 -665 -1631 C ATOM 1256 CG PHE A 180 69.668 1.901 47.945 1.00109.80 C ANISOU 1256 CG PHE A 180 11055 19029 11636 -534 -480 -1683 C ATOM 1257 CD1 PHE A 180 68.829 3.007 48.051 1.00108.33 C ANISOU 1257 CD1 PHE A 180 10931 18784 11444 -623 -363 -1720 C ATOM 1258 CD2 PHE A 180 70.182 1.580 46.696 1.00105.95 C ANISOU 1258 CD2 PHE A 180 10568 18488 11200 -492 -430 -1693 C ATOM 1259 CE1 PHE A 180 68.514 3.781 46.935 1.00101.25 C ANISOU 1259 CE1 PHE A 180 10096 17782 10592 -664 -201 -1764 C ATOM 1260 CE2 PHE A 180 69.874 2.350 45.582 1.00101.63 C ANISOU 1260 CE2 PHE A 180 10092 17835 10689 -537 -272 -1740 C ATOM 1261 CZ PHE A 180 69.038 3.452 45.704 1.00 99.25 C ANISOU 1261 CZ PHE A 180 9853 17479 10380 -620 -158 -1774 C ATOM 1262 N ASN A 181 68.981 -1.736 48.113 1.00106.87 N ANISOU 1262 N ASN A 181 10762 18558 11284 -181 -595 -1365 N ATOM 1263 CA ASN A 181 68.541 -2.470 46.940 1.00101.33 C ANISOU 1263 CA ASN A 181 10148 17716 10636 -96 -479 -1298 C ATOM 1264 C ASN A 181 67.472 -3.520 47.199 1.00 98.67 C ANISOU 1264 C ASN A 181 9900 17289 10300 2 -444 -1169 C ATOM 1265 O ASN A 181 66.848 -4.003 46.262 1.00 98.95 O ANISOU 1265 O ASN A 181 10028 17195 10372 54 -325 -1116 O ATOM 1266 CB ASN A 181 69.712 -3.078 46.180 1.00108.06 C ANISOU 1266 CB ASN A 181 10932 18602 11524 -52 -553 -1317 C ATOM 1267 CG ASN A 181 69.267 -4.137 45.198 1.00113.74 C ANISOU 1267 CG ASN A 181 11744 19187 12285 49 -475 -1229 C ATOM 1268 OD1 ASN A 181 69.422 -5.331 45.450 1.00121.49 O ANISOU 1268 OD1 ASN A 181 12710 20177 13273 144 -561 -1146 O ATOM 1269 ND2 ASN A 181 68.679 -3.710 44.087 1.00110.13 N ANISOU 1269 ND2 ASN A 181 11391 18603 11851 28 -316 -1245 N ATOM 1270 N PHE A 182 67.255 -3.890 48.453 1.00101.76 N ANISOU 1270 N PHE A 182 10267 17748 10648 23 -550 -1120 N ATOM 1271 CA PHE A 182 66.147 -4.792 48.731 1.00106.54 C ANISOU 1271 CA PHE A 182 10958 18264 11257 101 -504 -1004 C ATOM 1272 C PHE A 182 64.939 -3.987 49.187 1.00101.68 C ANISOU 1272 C PHE A 182 10402 17599 10634 40 -399 -1006 C ATOM 1273 O PHE A 182 64.002 -3.767 48.427 1.00 92.38 O ANISOU 1273 O PHE A 182 9303 16300 9499 39 -233 -990 O ATOM 1274 CB PHE A 182 66.520 -5.846 49.778 1.00117.58 C ANISOU 1274 CB PHE A 182 12314 19747 12615 178 -683 -932 C ATOM 1275 CG PHE A 182 65.462 -6.911 49.970 1.00125.58 C ANISOU 1275 CG PHE A 182 13413 20663 13638 264 -638 -812 C ATOM 1276 CD1 PHE A 182 64.603 -7.254 48.930 1.00125.46 C ANISOU 1276 CD1 PHE A 182 13487 20501 13680 294 -468 -769 C ATOM 1277 CD2 PHE A 182 65.315 -7.556 51.193 1.00129.61 C ANISOU 1277 CD2 PHE A 182 13921 21233 14094 310 -772 -744 C ATOM 1278 CE1 PHE A 182 63.628 -8.227 49.103 1.00126.00 C ANISOU 1278 CE1 PHE A 182 13626 20486 13762 361 -425 -666 C ATOM 1279 CE2 PHE A 182 64.342 -8.528 51.376 1.00128.89 C ANISOU 1279 CE2 PHE A 182 13907 21052 14014 382 -731 -637 C ATOM 1280 CZ PHE A 182 63.497 -8.864 50.329 1.00128.81 C ANISOU 1280 CZ PHE A 182 13971 20900 14073 405 -553 -600 C ATOM 1281 N PHE A 183 64.999 -3.501 50.419 1.00110.87 N ANISOU 1281 N PHE A 183 11524 18862 11741 -14 -504 -1033 N ATOM 1282 CA PHE A 183 63.910 -2.724 50.996 1.00113.58 C ANISOU 1282 CA PHE A 183 11912 19170 12074 -78 -429 -1038 C ATOM 1283 C PHE A 183 63.383 -1.651 50.048 1.00105.95 C ANISOU 1283 C PHE A 183 10981 18115 11162 -144 -249 -1097 C ATOM 1284 O PHE A 183 62.214 -1.678 49.668 1.00102.62 O ANISOU 1284 O PHE A 183 10627 17579 10786 -121 -110 -1047 O ATOM 1285 CB PHE A 183 64.333 -2.094 52.327 1.00119.21 C ANISOU 1285 CB PHE A 183 12575 20016 12703 -157 -581 -1095 C ATOM 1286 CG PHE A 183 64.328 -3.057 53.477 1.00123.49 C ANISOU 1286 CG PHE A 183 13124 20619 13177 -91 -741 -1017 C ATOM 1287 CD1 PHE A 183 64.430 -4.423 53.256 1.00121.19 C ANISOU 1287 CD1 PHE A 183 12846 20298 12904 31 -779 -920 C ATOM 1288 CD2 PHE A 183 64.191 -2.598 54.782 1.00129.14 C ANISOU 1288 CD2 PHE A 183 13848 21416 13803 -153 -854 -1041 C ATOM 1289 CE1 PHE A 183 64.418 -5.316 54.318 1.00124.02 C ANISOU 1289 CE1 PHE A 183 13220 20708 13194 96 -930 -844 C ATOM 1290 CE2 PHE A 183 64.174 -3.483 55.853 1.00130.81 C ANISOU 1290 CE2 PHE A 183 14087 21682 13935 -89 -1009 -967 C ATOM 1291 CZ PHE A 183 64.289 -4.845 55.621 1.00128.54 C ANISOU 1291 CZ PHE A 183 13808 21365 13669 38 -1048 -866 C ATOM 1292 N ALA A 184 64.235 -0.701 49.685 1.00102.79 N ANISOU 1292 N ALA A 184 10530 17769 10755 -226 -256 -1203 N ATOM 1293 CA ALA A 184 63.797 0.423 48.872 1.00105.83 C ANISOU 1293 CA ALA A 184 10951 18078 11181 -296 -100 -1264 C ATOM 1294 C ALA A 184 63.527 0.063 47.409 1.00108.77 C ANISOU 1294 C ALA A 184 11395 18326 11607 -231 38 -1234 C ATOM 1295 O ALA A 184 62.505 0.471 46.845 1.00116.00 O ANISOU 1295 O ALA A 184 12482 18915 12676 -240 72 -1159 O ATOM 1296 CB ALA A 184 64.788 1.576 48.973 1.00110.47 C ANISOU 1296 CB ALA A 184 11468 18763 11743 -415 -152 -1393 C ATOM 1297 N CYS A 185 64.426 -0.692 46.785 1.00103.02 N ANISOU 1297 N CYS A 185 10651 17612 10880 -177 -16 -1229 N ATOM 1298 CA CYS A 185 64.300 -0.930 45.344 1.00100.00 C ANISOU 1298 CA CYS A 185 10395 17001 10599 -139 40 -1186 C ATOM 1299 C CYS A 185 63.504 -2.163 44.898 1.00 94.48 C ANISOU 1299 C CYS A 185 9831 16077 9991 -43 37 -1045 C ATOM 1300 O CYS A 185 63.175 -2.276 43.722 1.00 91.02 O ANISOU 1300 O CYS A 185 9543 15359 9680 -30 57 -986 O ATOM 1301 CB CYS A 185 65.673 -0.912 44.660 1.00103.23 C ANISOU 1301 CB CYS A 185 10704 17578 10942 -148 28 -1290 C ATOM 1302 SG CYS A 185 66.462 0.716 44.613 1.00107.11 S ANISOU 1302 SG CYS A 185 11123 18149 11424 -290 28 -1440 S ATOM 1303 N VAL A 186 63.184 -3.073 45.814 1.00 92.71 N ANISOU 1303 N VAL A 186 9552 15978 9698 17 15 -993 N ATOM 1304 CA VAL A 186 62.501 -4.313 45.422 1.00 85.62 C ANISOU 1304 CA VAL A 186 8766 14891 8876 99 15 -871 C ATOM 1305 C VAL A 186 61.239 -4.632 46.216 1.00 81.09 C ANISOU 1305 C VAL A 186 8253 14214 8342 114 23 -785 C ATOM 1306 O VAL A 186 60.161 -4.732 45.645 1.00 76.26 O ANISOU 1306 O VAL A 186 7813 13283 7880 113 51 -703 O ATOM 1307 CB VAL A 186 63.438 -5.543 45.430 1.00 79.64 C ANISOU 1307 CB VAL A 186 7893 14364 8003 189 -20 -874 C ATOM 1308 CG1 VAL A 186 62.682 -6.777 44.963 1.00 74.99 C ANISOU 1308 CG1 VAL A 186 7430 13561 7501 258 -13 -751 C ATOM 1309 CG2 VAL A 186 64.633 -5.295 44.537 1.00 75.24 C ANISOU 1309 CG2 VAL A 186 7286 13874 7427 176 -36 -957 C ATOM 1310 N LEU A 187 61.386 -4.838 47.519 1.00 84.13 N ANISOU 1310 N LEU A 187 8490 14887 8587 131 -4 -807 N ATOM 1311 CA LEU A 187 60.246 -5.088 48.388 1.00 91.39 C ANISOU 1311 CA LEU A 187 9444 15754 9525 141 0 -738 C ATOM 1312 C LEU A 187 59.147 -4.031 48.161 1.00 94.09 C ANISOU 1312 C LEU A 187 9927 15811 10014 67 37 -725 C ATOM 1313 O LEU A 187 57.955 -4.357 48.060 1.00 90.21 O ANISOU 1313 O LEU A 187 9563 15078 9637 82 56 -642 O ATOM 1314 CB LEU A 187 60.707 -5.107 49.853 1.00 98.23 C ANISOU 1314 CB LEU A 187 10183 16874 10267 136 -110 -763 C ATOM 1315 CG LEU A 187 59.887 -5.844 50.927 1.00101.74 C ANISOU 1315 CG LEU A 187 10648 17316 10694 176 -165 -677 C ATOM 1316 CD1 LEU A 187 58.607 -5.090 51.327 1.00 96.51 C ANISOU 1316 CD1 LEU A 187 10004 16605 10059 120 -70 -680 C ATOM 1317 CD2 LEU A 187 59.573 -7.277 50.495 1.00103.83 C ANISOU 1317 CD2 LEU A 187 10958 17506 10988 275 -141 -580 C ATOM 1318 N VAL A 188 59.552 -2.766 48.075 1.00 95.34 N ANISOU 1318 N VAL A 188 10055 16007 10165 -11 47 -812 N ATOM 1319 CA VAL A 188 58.598 -1.677 47.867 1.00 93.92 C ANISOU 1319 CA VAL A 188 9992 15585 10108 -72 80 -804 C ATOM 1320 C VAL A 188 57.874 -1.749 46.518 1.00 95.76 C ANISOU 1320 C VAL A 188 10429 15428 10528 -48 111 -724 C ATOM 1321 O VAL A 188 56.641 -1.789 46.487 1.00 98.85 O ANISOU 1321 O VAL A 188 10936 15595 11029 -37 129 -654 O ATOM 1322 CB VAL A 188 59.245 -0.287 48.072 1.00 92.79 C ANISOU 1322 CB VAL A 188 9763 15585 9907 -166 86 -921 C ATOM 1323 CG1 VAL A 188 58.373 0.807 47.487 1.00 91.81 C ANISOU 1323 CG1 VAL A 188 9780 15173 9930 -210 123 -903 C ATOM 1324 CG2 VAL A 188 59.491 -0.037 49.546 1.00 90.94 C ANISOU 1324 CG2 VAL A 188 9354 15693 9507 -212 63 -994 C ATOM 1325 N PRO A 189 58.627 -1.764 45.398 1.00 91.52 N ANISOU 1325 N PRO A 189 9929 14825 10019 -42 115 -740 N ATOM 1326 CA PRO A 189 57.957 -1.911 44.092 1.00 88.36 C ANISOU 1326 CA PRO A 189 9717 14078 9777 -20 140 -663 C ATOM 1327 C PRO A 189 57.161 -3.220 43.936 1.00 89.10 C ANISOU 1327 C PRO A 189 9899 14023 9932 39 141 -567 C ATOM 1328 O PRO A 189 56.149 -3.234 43.237 1.00 85.79 O ANISOU 1328 O PRO A 189 9427 13346 9823 23 -3 -481 O ATOM 1329 CB PRO A 189 59.114 -1.828 43.090 1.00 79.30 C ANISOU 1329 CB PRO A 189 8552 12970 8608 -25 135 -711 C ATOM 1330 CG PRO A 189 60.111 -0.969 43.790 1.00 83.42 C ANISOU 1330 CG PRO A 189 8909 13783 9004 -81 123 -828 C ATOM 1331 CD PRO A 189 60.040 -1.374 45.243 1.00 85.79 C ANISOU 1331 CD PRO A 189 9078 14331 9188 -72 101 -842 C ATOM 1332 N LEU A 190 57.596 -4.287 44.600 1.00 91.95 N ANISOU 1332 N LEU A 190 10156 14592 10190 82 115 -562 N ATOM 1333 CA LEU A 190 56.851 -5.544 44.594 1.00 92.74 C ANISOU 1333 CA LEU A 190 10321 14582 10334 131 117 -478 C ATOM 1334 C LEU A 190 55.539 -5.446 45.359 1.00 89.75 C ANISOU 1334 C LEU A 190 9986 14105 10010 121 130 -436 C ATOM 1335 O LEU A 190 54.509 -5.885 44.872 1.00 87.31 O ANISOU 1335 O LEU A 190 9808 13548 9818 130 151 -373 O ATOM 1336 CB LEU A 190 57.692 -6.693 45.156 1.00 98.49 C ANISOU 1336 CB LEU A 190 10912 15585 10925 190 85 -480 C ATOM 1337 CG LEU A 190 58.663 -7.369 44.185 1.00 96.79 C ANISOU 1337 CG LEU A 190 10690 15398 10689 225 74 -487 C ATOM 1338 CD1 LEU A 190 59.328 -8.577 44.849 1.00 95.70 C ANISOU 1338 CD1 LEU A 190 10414 15535 10412 303 41 -474 C ATOM 1339 CD2 LEU A 190 57.953 -7.764 42.882 1.00 87.69 C ANISOU 1339 CD2 LEU A 190 9722 13906 9689 219 100 -424 C ATOM 1340 N LEU A 191 55.568 -4.890 46.562 1.00 92.79 N ANISOU 1340 N LEU A 191 10254 14700 10303 101 116 -478 N ATOM 1341 CA LEU A 191 54.327 -4.734 47.311 1.00 99.65 C ANISOU 1341 CA LEU A 191 11152 15493 11216 89 124 -445 C ATOM 1342 C LEU A 191 53.396 -3.762 46.586 1.00 94.81 C ANISOU 1342 C LEU A 191 10684 14583 10756 54 157 -432 C ATOM 1343 O LEU A 191 52.183 -3.742 46.821 1.00 86.12 O ANISOU 1343 O LEU A 191 9481 13390 9851 37 -4 -384 O ATOM 1344 CB LEU A 191 54.600 -4.267 48.744 1.00109.88 C ANISOU 1344 CB LEU A 191 12283 17103 12364 65 99 -501 C ATOM 1345 CG LEU A 191 54.853 -5.356 49.794 1.00114.29 C ANISOU 1345 CG LEU A 191 12711 17933 12779 116 67 -480 C ATOM 1346 CD1 LEU A 191 55.969 -6.316 49.361 1.00114.18 C ANISOU 1346 CD1 LEU A 191 12643 18048 12693 175 49 -475 C ATOM 1347 CD2 LEU A 191 55.153 -4.729 51.156 1.00115.44 C ANISOU 1347 CD2 LEU A 191 12691 18405 12764 80 40 -546 C ATOM 1348 N LEU A 192 53.980 -2.960 45.701 1.00 93.91 N ANISOU 1348 N LEU A 192 10440 14411 10830 10 -1 -447 N ATOM 1349 CA LEU A 192 53.222 -1.989 44.927 1.00 95.20 C ANISOU 1349 CA LEU A 192 10986 14456 10731 -18 2 -503 C ATOM 1350 C LEU A 192 52.470 -2.694 43.787 1.00 96.11 C ANISOU 1350 C LEU A 192 11164 14433 10919 13 -2 -450 C ATOM 1351 O LEU A 192 51.311 -2.375 43.504 1.00 86.95 O ANISOU 1351 O LEU A 192 9756 13186 10096 10 -1 -397 O ATOM 1352 CB LEU A 192 54.158 -0.899 44.390 1.00 95.14 C ANISOU 1352 CB LEU A 192 10961 14470 10717 -57 8 -567 C ATOM 1353 CG LEU A 192 53.544 0.441 43.976 1.00 89.16 C ANISOU 1353 CG LEU A 192 10231 13638 10006 -96 16 -600 C ATOM 1354 CD1 LEU A 192 52.633 0.948 45.077 1.00 84.63 C ANISOU 1354 CD1 LEU A 192 9325 13096 9733 -126 20 -556 C ATOM 1355 CD2 LEU A 192 54.628 1.468 43.649 1.00 83.19 C ANISOU 1355 CD2 LEU A 192 9119 12941 9549 -154 27 -614 C ATOM 1356 N MET A 193 53.136 -3.665 43.154 1.00 96.88 N ANISOU 1356 N MET A 193 11266 14527 11016 41 -5 -426 N ATOM 1357 CA MET A 193 52.553 -4.472 42.071 1.00 90.26 C ANISOU 1357 CA MET A 193 10484 13572 10240 66 -7 -379 C ATOM 1358 C MET A 193 51.513 -5.498 42.542 1.00 93.90 C ANISOU 1358 C MET A 193 10963 14003 10712 93 -9 -323 C ATOM 1359 O MET A 193 50.568 -5.833 41.820 1.00 94.62 O ANISOU 1359 O MET A 193 10837 13990 11123 109 -10 -267 O ATOM 1360 CB MET A 193 53.655 -5.199 41.304 1.00 81.81 C ANISOU 1360 CB MET A 193 9408 12516 9160 85 -9 -376 C ATOM 1361 CG MET A 193 54.274 -4.381 40.193 1.00 83.77 C ANISOU 1361 CG MET A 193 9667 12725 9435 63 -8 -415 C ATOM 1362 SD MET A 193 55.657 -5.209 39.381 1.00144.72 S ANISOU 1362 SD MET A 193 17372 20481 17134 84 -10 -420 S ATOM 1363 CE MET A 193 56.825 -5.323 40.734 1.00 82.32 C ANISOU 1363 CE MET A 193 9389 12760 9130 91 -11 -455 C ATOM 1364 N LEU A 194 51.712 -6.016 43.745 1.00 92.44 N ANISOU 1364 N LEU A 194 10737 13919 10469 106 -10 -312 N ATOM 1365 CA LEU A 194 50.751 -6.909 44.360 1.00 93.52 C ANISOU 1365 CA LEU A 194 10401 14712 10419 174 -13 -329 C ATOM 1366 C LEU A 194 49.439 -6.160 44.508 1.00 84.98 C ANISOU 1366 C LEU A 194 9547 12898 9844 116 -9 -245 C ATOM 1367 O LEU A 194 48.361 -6.707 44.278 1.00 78.12 O ANISOU 1367 O LEU A 194 8723 11954 9004 128 -8 -212 O ATOM 1368 CB LEU A 194 51.261 -7.345 45.736 1.00 96.99 C ANISOU 1368 CB LEU A 194 11265 14618 10969 142 -11 -258 C ATOM 1369 CG LEU A 194 50.369 -8.276 46.562 1.00 99.08 C ANISOU 1369 CG LEU A 194 11529 14891 11224 164 -10 -207 C ATOM 1370 CD1 LEU A 194 50.089 -9.569 45.786 1.00 98.41 C ANISOU 1370 CD1 LEU A 194 11185 14731 11477 212 -9 -143 C ATOM 1371 CD2 LEU A 194 50.980 -8.563 47.947 1.00 89.98 C ANISOU 1371 CD2 LEU A 194 10103 13931 10156 200 142 -206 C ATOM 1372 N GLY A 195 49.545 -4.895 44.900 1.00 87.93 N ANISOU 1372 N GLY A 195 9895 13307 10207 82 -8 -288 N ATOM 1373 CA GLY A 195 48.380 -4.058 45.103 1.00 85.57 C ANISOU 1373 CA GLY A 195 9621 12960 9930 61 -6 -298 C ATOM 1374 C GLY A 195 47.706 -3.755 43.789 1.00 79.25 C ANISOU 1374 C GLY A 195 9157 12029 8924 55 -6 -319 C ATOM 1375 O GLY A 195 46.514 -3.987 43.626 1.00 76.24 O ANISOU 1375 O GLY A 195 8553 11583 8832 70 -7 -268 O ATOM 1376 N VAL A 196 48.481 -3.256 42.834 1.00 77.29 N ANISOU 1376 N VAL A 196 8918 11753 8694 46 -5 -343 N ATOM 1377 CA VAL A 196 47.910 -2.833 41.562 1.00 74.35 C ANISOU 1377 CA VAL A 196 8349 11271 8631 48 -6 -311 C ATOM 1378 C VAL A 196 47.167 -3.943 40.832 1.00 70.88 C ANISOU 1378 C VAL A 196 7961 10749 8221 75 -8 -265 C ATOM 1379 O VAL A 196 46.099 -3.711 40.287 1.00 69.32 O ANISOU 1379 O VAL A 196 7660 10986 7693 96 -10 -347 O ATOM 1380 CB VAL A 196 48.956 -2.189 40.641 1.00 68.85 C ANISOU 1380 CB VAL A 196 7653 10565 7943 31 -4 -341 C ATOM 1381 CG1 VAL A 196 48.506 -2.274 39.190 1.00 67.35 C ANISOU 1381 CG1 VAL A 196 7760 10257 7573 38 -5 -351 C ATOM 1382 CG2 VAL A 196 49.193 -0.742 41.063 1.00 59.34 C ANISOU 1382 CG2 VAL A 196 6671 9396 6478 -6 1 -426 C ATOM 1383 N TYR A 197 47.722 -5.147 40.812 1.00 76.25 N ANISOU 1383 N TYR A 197 8631 11451 8887 97 -9 -240 N ATOM 1384 CA TYR A 197 46.992 -6.262 40.217 1.00 85.66 C ANISOU 1384 CA TYR A 197 10095 12572 9880 107 -9 -218 C ATOM 1385 C TYR A 197 45.744 -6.628 41.028 1.00 84.88 C ANISOU 1385 C TYR A 197 9998 12472 9779 113 -9 -194 C ATOM 1386 O TYR A 197 44.632 -6.621 40.508 1.00 84.30 O ANISOU 1386 O TYR A 197 9957 12326 9747 113 -9 -181 O ATOM 1387 CB TYR A 197 47.892 -7.486 40.027 1.00 88.38 C ANISOU 1387 CB TYR A 197 10430 12944 10206 127 -10 -195 C ATOM 1388 CG TYR A 197 48.777 -7.388 38.817 1.00 90.94 C ANISOU 1388 CG TYR A 197 10392 13757 10404 170 -13 -260 C ATOM 1389 CD1 TYR A 197 48.287 -7.678 37.558 1.00 85.50 C ANISOU 1389 CD1 TYR A 197 9909 12447 10129 137 -9 -176 C ATOM 1390 CD2 TYR A 197 50.103 -6.998 38.931 1.00 94.13 C ANISOU 1390 CD2 TYR A 197 10902 13711 11152 131 -10 -220 C ATOM 1391 CE1 TYR A 197 49.097 -7.581 36.433 1.00 93.48 C ANISOU 1391 CE1 TYR A 197 10797 13912 10809 167 -14 -256 C ATOM 1392 CE2 TYR A 197 50.922 -6.903 37.812 1.00 97.19 C ANISOU 1392 CE2 TYR A 197 11304 14071 11553 128 -12 -234 C ATOM 1393 CZ TYR A 197 50.412 -7.191 36.563 1.00 93.17 C ANISOU 1393 CZ TYR A 197 11073 13458 10868 118 -12 -236 C ATOM 1394 OH TYR A 197 51.217 -7.089 35.446 1.00 90.51 O ANISOU 1394 OH TYR A 197 10530 13098 10763 125 -12 -229 O ATOM 1395 N LEU A 198 45.924 -6.920 42.308 1.00 81.73 N ANISOU 1395 N LEU A 198 9561 12162 9330 118 -9 -189 N ATOM 1396 CA LEU A 198 44.796 -7.297 43.141 1.00 83.54 C ANISOU 1396 CA LEU A 198 9390 12955 9395 167 -10 -208 C ATOM 1397 C LEU A 198 43.676 -6.278 43.007 1.00 80.04 C ANISOU 1397 C LEU A 198 8978 12447 8987 147 -10 -232 C ATOM 1398 O LEU A 198 42.502 -6.601 43.167 1.00 73.52 O ANISOU 1398 O LEU A 198 8553 11053 8329 112 -7 -166 O ATOM 1399 CB LEU A 198 45.219 -7.417 44.606 1.00 78.92 C ANISOU 1399 CB LEU A 198 8899 11931 9155 136 -7 -154 C ATOM 1400 CG LEU A 198 45.867 -8.749 44.975 1.00 75.44 C ANISOU 1400 CG LEU A 198 8691 11544 8428 150 -7 -132 C ATOM 1401 CD1 LEU A 198 45.735 -8.994 46.467 1.00 77.82 C ANISOU 1401 CD1 LEU A 198 8495 12581 8490 213 -8 -150 C ATOM 1402 CD2 LEU A 198 45.232 -9.893 44.173 1.00 67.63 C ANISOU 1402 CD2 LEU A 198 7741 10473 7483 166 -5 -90 C ATOM 1403 N ARG A 199 44.049 -5.043 42.710 1.00 74.60 N ANISOU 1403 N ARG A 199 8675 11213 8457 90 -7 -225 N ATOM 1404 CA ARG A 199 43.067 -3.995 42.551 1.00 73.67 C ANISOU 1404 CA ARG A 199 8347 11054 8592 87 -8 -225 C ATOM 1405 C ARG A 199 42.291 -4.253 41.257 1.00 76.67 C ANISOU 1405 C ARG A 199 8999 11329 8801 89 -8 -224 C ATOM 1406 O ARG A 199 41.073 -4.070 41.212 1.00 83.24 O ANISOU 1406 O ARG A 199 9500 12610 9518 126 -11 -273 O ATOM 1407 CB ARG A 199 43.748 -2.621 42.557 1.00 76.64 C ANISOU 1407 CB ARG A 199 8935 11451 8733 57 -6 -293 C ATOM 1408 CG ARG A 199 42.782 -1.472 42.741 1.00 88.00 C ANISOU 1408 CG ARG A 199 10380 12870 10187 46 -5 -317 C ATOM 1409 CD ARG A 199 43.461 -0.120 42.935 1.00 97.77 C ANISOU 1409 CD ARG A 199 11361 14147 11641 20 -3 -338 C ATOM 1410 NE ARG A 199 42.480 0.946 42.739 1.00108.30 N ANISOU 1410 NE ARG A 199 12715 15436 12997 14 -2 -355 N ATOM 1411 CZ ARG A 199 41.559 1.293 43.636 1.00109.81 C ANISOU 1411 CZ ARG A 199 13125 15652 12947 9 -1 -397 C ATOM 1412 NH1 ARG A 199 41.504 0.672 44.806 1.00110.33 N ANISOU 1412 NH1 ARG A 199 13161 15790 12970 8 -1 -389 N ATOM 1413 NH2 ARG A 199 40.693 2.263 43.364 1.00106.77 N ANISOU 1413 NH2 ARG A 199 12755 15227 12588 8 -1 -414 N ATOM 1414 N ILE A 200 42.998 -4.694 40.216 1.00 69.68 N ANISOU 1414 N ILE A 200 7924 10405 8145 102 -9 -197 N ATOM 1415 CA ILE A 200 42.384 -5.065 38.942 1.00 64.13 C ANISOU 1415 CA ILE A 200 7471 9613 7285 101 -9 -195 C ATOM 1416 C ILE A 200 41.532 -6.333 39.076 1.00 63.28 C ANISOU 1416 C ILE A 200 7371 9491 7181 113 -8 -158 C ATOM 1417 O ILE A 200 40.367 -6.364 38.700 1.00 58.34 O ANISOU 1417 O ILE A 200 6578 8820 6768 126 -8 -136 O ATOM 1418 CB ILE A 200 43.453 -5.357 37.887 1.00 65.43 C ANISOU 1418 CB ILE A 200 7454 9750 7657 111 -9 -178 C ATOM 1419 CG1 ILE A 200 44.341 -4.140 37.669 1.00 68.12 C ANISOU 1419 CG1 ILE A 200 7978 10104 7801 87 -9 -231 C ATOM 1420 CG2 ILE A 200 42.818 -5.776 36.588 1.00 61.28 C ANISOU 1420 CG2 ILE A 200 7159 9138 6986 107 -9 -174 C ATOM 1421 CD1 ILE A 200 45.624 -4.482 36.941 1.00 66.21 C ANISOU 1421 CD1 ILE A 200 7734 9864 7558 87 -9 -235 C ATOM 1422 N PHE A 201 42.127 -7.390 39.609 1.00 63.97 N ANISOU 1422 N PHE A 201 7242 9623 7442 132 -7 -126 N ATOM 1423 CA PHE A 201 41.417 -8.641 39.788 1.00 60.17 C ANISOU 1423 CA PHE A 201 6966 9134 6764 131 -6 -103 C ATOM 1424 C PHE A 201 40.163 -8.472 40.621 1.00 64.54 C ANISOU 1424 C PHE A 201 7511 9705 7306 129 -6 -99 C ATOM 1425 O PHE A 201 39.146 -9.118 40.355 1.00 72.52 O ANISOU 1425 O PHE A 201 8537 10681 8335 132 -5 -79 O ATOM 1426 CB PHE A 201 42.323 -9.653 40.456 1.00 66.05 C ANISOU 1426 CB PHE A 201 7479 9939 7679 156 -5 -75 C ATOM 1427 CG PHE A 201 43.584 -9.923 39.695 1.00 76.08 C ANISOU 1427 CG PHE A 201 8958 11203 8745 147 -6 -85 C ATOM 1428 CD1 PHE A 201 44.725 -10.388 40.350 1.00 78.37 C ANISOU 1428 CD1 PHE A 201 9216 11570 8991 159 -5 -80 C ATOM 1429 CD2 PHE A 201 43.630 -9.721 38.323 1.00 73.71 C ANISOU 1429 CD2 PHE A 201 8691 10827 8489 142 -6 -93 C ATOM 1430 CE1 PHE A 201 45.872 -10.646 39.646 1.00 77.75 C ANISOU 1430 CE1 PHE A 201 9137 11491 8912 165 -6 -85 C ATOM 1431 CE2 PHE A 201 44.782 -9.979 37.608 1.00 74.72 C ANISOU 1431 CE2 PHE A 201 8820 10952 8618 145 -7 -97 C ATOM 1432 CZ PHE A 201 45.905 -10.438 38.268 1.00 77.36 C ANISOU 1432 CZ PHE A 201 8917 11362 9114 171 -6 -86 C ATOM 1433 N LEU A 202 40.235 -7.635 41.651 1.00 65.43 N ANISOU 1433 N LEU A 202 7250 10360 7249 168 -8 -151 N ATOM 1434 CA LEU A 202 39.067 -7.427 42.507 1.00 67.86 C ANISOU 1434 CA LEU A 202 7893 10209 7680 121 -6 -121 C ATOM 1435 C LEU A 202 38.072 -6.428 41.926 1.00 68.56 C ANISOU 1435 C LEU A 202 7797 10248 8004 127 -7 -130 C ATOM 1436 O LEU A 202 36.885 -6.492 42.230 1.00 68.30 O ANISOU 1436 O LEU A 202 7970 10216 7765 118 -7 -136 O ATOM 1437 CB LEU A 202 39.448 -7.045 43.946 1.00 77.91 C ANISOU 1437 CB LEU A 202 8753 12095 8754 158 -8 -168 C ATOM 1438 CG LEU A 202 40.186 -8.045 44.849 1.00 80.44 C ANISOU 1438 CG LEU A 202 9415 11970 9179 125 -5 -109 C ATOM 1439 CD1 LEU A 202 40.019 -7.632 46.301 1.00 82.28 C ANISOU 1439 CD1 LEU A 202 9201 12862 9201 160 -7 -151 C ATOM 1440 CD2 LEU A 202 39.714 -9.483 44.655 1.00 81.75 C ANISOU 1440 CD2 LEU A 202 9364 12112 9587 151 -3 -60 C ATOM 1441 N ALA A 203 38.555 -5.503 41.100 1.00 75.95 N ANISOU 1441 N ALA A 203 8620 11612 8627 152 -10 -206 N ATOM 1442 CA ALA A 203 37.682 -4.519 40.457 1.00 82.56 C ANISOU 1442 CA ALA A 203 9486 12388 9496 151 -12 -227 C ATOM 1443 C ALA A 203 36.913 -5.184 39.314 1.00 84.52 C ANISOU 1443 C ALA A 203 9902 12119 10092 130 -8 -146 C ATOM 1444 O ALA A 203 35.699 -4.998 39.145 1.00 85.22 O ANISOU 1444 O ALA A 203 10000 12192 10187 135 -9 -145 O ATOM 1445 CB ALA A 203 38.499 -3.325 39.940 1.00 76.02 C ANISOU 1445 CB ALA A 203 8792 11094 8998 112 -10 -194 C ATOM 1446 N ALA A 204 37.646 -5.975 38.542 1.00 80.76 N ANISOU 1446 N ALA A 204 9445 11612 9628 131 -8 -131 N ATOM 1447 CA ALA A 204 37.096 -6.700 37.417 1.00 79.79 C ANISOU 1447 CA ALA A 204 9357 11431 9530 135 -7 -113 C ATOM 1448 C ALA A 204 36.006 -7.674 37.845 1.00 80.14 C ANISOU 1448 C ALA A 204 9394 11489 9566 138 -6 -94 C ATOM 1449 O ALA A 204 35.023 -7.851 37.136 1.00 86.77 O ANISOU 1449 O ALA A 204 10425 12296 10248 128 -7 -97 O ATOM 1450 CB ALA A 204 38.212 -7.437 36.677 1.00 82.91 C ANISOU 1450 CB ALA A 204 9936 11802 9763 123 -7 -113 C ATOM 1451 N ARG A 205 36.168 -8.316 38.993 1.00 79.69 N ANISOU 1451 N ARG A 205 9308 11486 9486 139 -5 -82 N ATOM 1452 CA ARG A 205 35.182 -9.305 39.398 1.00 90.06 C ANISOU 1452 CA ARG A 205 10614 12814 10792 140 -4 -61 C ATOM 1453 C ARG A 205 33.863 -8.664 39.834 1.00 94.79 C ANISOU 1453 C ARG A 205 11201 13432 11382 140 -5 -73 C ATOM 1454 O ARG A 205 32.799 -9.276 39.710 1.00 94.86 O ANISOU 1454 O ARG A 205 11212 13438 11393 139 -4 -61 O ATOM 1455 CB ARG A 205 35.724 -10.237 40.476 1.00101.31 C ANISOU 1455 CB ARG A 205 12007 14293 12191 143 -3 -41 C ATOM 1456 CG ARG A 205 35.257 -11.682 40.314 1.00110.68 C ANISOU 1456 CG ARG A 205 13201 15470 13383 144 -1 -12 C ATOM 1457 CD ARG A 205 35.167 -12.367 41.658 1.00127.40 C ANISOU 1457 CD ARG A 205 15281 17655 15471 147 1 9 C ATOM 1458 NE ARG A 205 36.269 -11.956 42.526 1.00146.05 N ANISOU 1458 NE ARG A 205 17611 20072 17809 152 0 3 N ATOM 1459 CZ ARG A 205 36.138 -11.637 43.812 1.00154.07 C ANISOU 1459 CZ ARG A 205 18802 21158 18578 139 0 1 C ATOM 1460 NH1 ARG A 205 34.945 -11.686 44.395 1.00153.59 N ANISOU 1460 NH1 ARG A 205 18732 21119 18506 134 0 6 N ATOM 1461 NH2 ARG A 205 37.204 -11.270 44.516 1.00157.14 N ANISOU 1461 NH2 ARG A 205 19167 21602 18936 143 0 -7 N ATOM 1462 N ARG A 206 33.923 -7.433 40.335 1.00 96.35 N ANISOU 1462 N ARG A 206 11384 13654 11571 139 -6 -97 N ATOM 1463 CA ARG A 206 32.697 -6.691 40.607 1.00 99.75 C ANISOU 1463 CA ARG A 206 11998 14100 11803 130 -7 -121 C ATOM 1464 C ARG A 206 32.030 -6.267 39.299 1.00108.13 C ANISOU 1464 C ARG A 206 12897 15106 13080 148 -8 -117 C ATOM 1465 O ARG A 206 30.814 -6.395 39.158 1.00117.82 O ANISOU 1465 O ARG A 206 14308 16340 14119 140 -9 -126 O ATOM 1466 CB ARG A 206 32.950 -5.478 41.506 1.00104.56 C ANISOU 1466 CB ARG A 206 12257 15211 12259 174 -11 -187 C ATOM 1467 CG ARG A 206 32.676 -5.726 42.994 1.00106.80 C ANISOU 1467 CG ARG A 206 12629 15110 12839 135 -7 -136 C ATOM 1468 CD ARG A 206 33.403 -4.711 43.900 1.00112.45 C ANISOU 1468 CD ARG A 206 13530 15874 13322 116 -9 -177 C ATOM 1469 NE ARG A 206 32.933 -3.329 43.754 1.00116.69 N ANISOU 1469 NE ARG A 206 14069 16403 13866 117 -11 -211 N ATOM 1470 CZ ARG A 206 33.501 -2.406 42.977 1.00121.44 C ANISOU 1470 CZ ARG A 206 14338 17448 14357 159 -15 -289 C ATOM 1471 NH1 ARG A 206 34.572 -2.703 42.252 1.00122.05 N ANISOU 1471 NH1 ARG A 206 14574 17008 14791 125 -10 -203 N ATOM 1472 NH2 ARG A 206 32.998 -1.178 42.922 1.00117.44 N ANISOU 1472 NH2 ARG A 206 14178 16455 13988 119 -12 -260 N ATOM 1473 N GLN A 207 32.815 -5.776 38.338 1.00101.05 N ANISOU 1473 N GLN A 207 12027 14163 12205 148 -9 -124 N ATOM 1474 CA GLN A 207 32.252 -5.412 37.036 1.00 94.22 C ANISOU 1474 CA GLN A 207 11076 13649 11073 193 -13 -172 C ATOM 1475 C GLN A 207 31.623 -6.624 36.353 1.00 89.02 C ANISOU 1475 C GLN A 207 10543 12570 10709 154 -8 -107 C ATOM 1476 O GLN A 207 30.588 -6.501 35.713 1.00 97.49 O ANISOU 1476 O GLN A 207 11622 13635 11786 160 -9 -109 O ATOM 1477 CB GLN A 207 33.292 -4.753 36.127 1.00 91.65 C ANISOU 1477 CB GLN A 207 11056 12880 10888 140 -11 -147 C ATOM 1478 CG GLN A 207 33.891 -3.464 36.688 1.00 99.70 C ANISOU 1478 CG GLN A 207 12065 13919 11898 138 -13 -173 C ATOM 1479 CD GLN A 207 35.200 -3.074 36.005 1.00105.58 C ANISOU 1479 CD GLN A 207 12546 15016 12553 180 -16 -225 C ATOM 1480 OE1 GLN A 207 35.293 -3.072 34.775 1.00103.54 O ANISOU 1480 OE1 GLN A 207 12426 14325 12590 146 -12 -159 O ATOM 1481 NE2 GLN A 207 36.221 -2.754 36.805 1.00102.59 N ANISOU 1481 NE2 GLN A 207 12142 14683 12154 168 -16 -242 N ATOM 1482 N LEU A 208 32.234 -7.795 36.508 1.00 85.38 N ANISOU 1482 N LEU A 208 9972 12501 9965 183 -9 -121 N ATOM 1483 CA LEU A 208 31.681 -9.033 35.950 1.00 85.58 C ANISOU 1483 CA LEU A 208 10287 12118 10112 131 -5 -77 C ATOM 1484 C LEU A 208 30.401 -9.530 36.651 1.00 96.15 C ANISOU 1484 C LEU A 208 11433 13500 11600 141 -4 -65 C ATOM 1485 O LEU A 208 29.481 -10.049 36.007 1.00 92.56 O ANISOU 1485 O LEU A 208 10870 13439 10861 174 -6 -83 O ATOM 1486 CB LEU A 208 32.749 -10.132 35.914 1.00 80.75 C ANISOU 1486 CB LEU A 208 9515 11493 9674 138 -4 -53 C ATOM 1487 CG LEU A 208 33.814 -9.888 34.833 1.00 84.47 C ANISOU 1487 CG LEU A 208 10014 11914 10166 138 -4 -58 C ATOM 1488 CD1 LEU A 208 35.010 -10.855 34.914 1.00 79.60 C ANISOU 1488 CD1 LEU A 208 9399 11295 9550 136 -3 -43 C ATOM 1489 CD2 LEU A 208 33.168 -9.936 33.446 1.00 88.92 C ANISOU 1489 CD2 LEU A 208 10602 12433 10748 137 -4 -60 C ATOM 1490 N LYS A 209 30.343 -9.364 37.967 1.00108.35 N ANISOU 1490 N LYS A 209 12949 15096 13123 141 -4 -66 N ATOM 1491 CA LYS A 209 29.171 -9.770 38.734 1.00110.89 C ANISOU 1491 CA LYS A 209 13429 15467 13236 126 -4 -67 C ATOM 1492 C LYS A 209 28.037 -8.750 38.599 1.00112.23 C ANISOU 1492 C LYS A 209 13402 15653 13585 146 -5 -83 C ATOM 1493 O LYS A 209 26.870 -9.084 38.818 1.00113.38 O ANISOU 1493 O LYS A 209 13528 15834 13716 144 -5 -83 O ATOM 1494 CB LYS A 209 29.544 -9.969 40.206 1.00112.92 C ANISOU 1494 CB LYS A 209 13663 15779 13464 123 -3 -59 C ATOM 1495 CG LYS A 209 28.686 -10.994 40.954 1.00117.13 C ANISOU 1495 CG LYS A 209 13978 16357 14171 125 -2 -37 C ATOM 1496 CD LYS A 209 27.372 -10.409 41.489 1.00115.68 C ANISOU 1496 CD LYS A 209 13971 16221 13761 114 -3 -58 C ATOM 1497 CE LYS A 209 26.597 -11.438 42.308 1.00108.20 C ANISOU 1497 CE LYS A 209 12789 15324 12997 111 -2 -36 C ATOM 1498 NZ LYS A 209 25.337 -10.892 42.876 1.00103.11 N ANISOU 1498 NZ LYS A 209 12113 14734 12329 108 -2 -54 N ATOM 1499 N GLN A 210 28.379 -7.514 38.235 1.00111.97 N ANISOU 1499 N GLN A 210 13567 15601 13375 143 -8 -110 N ATOM 1500 CA GLN A 210 27.378 -6.455 38.062 1.00112.49 C ANISOU 1500 CA GLN A 210 13626 15684 13432 155 -10 -132 C ATOM 1501 C GLN A 210 26.783 -6.399 36.657 1.00120.91 C ANISOU 1501 C GLN A 210 14707 16718 14516 162 -11 -133 C ATOM 1502 O GLN A 210 25.841 -5.647 36.406 1.00126.74 O ANISOU 1502 O GLN A 210 15126 17910 15118 240 -16 -185 O ATOM 1503 CB GLN A 210 27.939 -5.088 38.448 1.00104.70 C ANISOU 1503 CB GLN A 210 12448 14699 12634 177 -11 -141 C ATOM 1504 CG GLN A 210 27.965 -4.845 39.944 1.00105.21 C ANISOU 1504 CG GLN A 210 12479 14821 12675 172 -11 -149 C ATOM 1505 CD GLN A 210 28.618 -3.530 40.294 1.00107.13 C ANISOU 1505 CD GLN A 210 12917 15067 12721 161 -14 -188 C ATOM 1506 OE1 GLN A 210 29.211 -2.879 39.433 1.00108.94 O ANISOU 1506 OE1 GLN A 210 12973 15252 13168 180 -14 -179 O ATOM 1507 NE2 GLN A 210 28.514 -3.125 41.559 1.00104.28 N ANISOU 1507 NE2 GLN A 210 12325 14763 12535 172 -13 -186 N ATOM 1508 N MET A 211 27.360 -7.165 35.738 1.00122.67 N ANISOU 1508 N MET A 211 14772 16894 14944 169 -9 -109 N ATOM 1509 CA MET A 211 26.741 -7.396 34.439 1.00119.12 C ANISOU 1509 CA MET A 211 14335 16423 14503 173 -9 -108 C ATOM 1510 C MET A 211 25.704 -8.510 34.521 1.00118.32 C ANISOU 1510 C MET A 211 14214 16357 14387 164 -8 -101 C ATOM 1511 O MET A 211 24.715 -8.494 33.795 1.00121.91 O ANISOU 1511 O MET A 211 14659 16827 14835 170 -8 -108 O ATOM 1512 CB MET A 211 27.801 -7.694 33.384 1.00116.36 C ANISOU 1512 CB MET A 211 14188 16013 14012 153 -9 -109 C ATOM 1513 CG MET A 211 28.689 -6.499 33.125 1.00113.67 C ANISOU 1513 CG MET A 211 13860 15643 13688 160 -11 -120 C ATOM 1514 SD MET A 211 29.989 -6.772 31.921 1.00118.24 S ANISOU 1514 SD MET A 211 14311 16155 14459 167 -9 -103 S ATOM 1515 CE MET A 211 30.821 -5.191 32.036 1.00 61.30 C ANISOU 1515 CE MET A 211 7261 8932 7100 158 -12 -129 C ATOM 1516 N GLU A 212 25.963 -9.476 35.402 1.00116.05 N ANISOU 1516 N GLU A 212 13917 16085 14093 150 -6 -87 N ATOM 1517 CA GLU A 212 25.024 -10.547 35.757 1.00118.89 C ANISOU 1517 CA GLU A 212 14252 16485 14435 137 -5 -79 C ATOM 1518 C GLU A 212 23.679 -10.051 36.281 1.00124.80 C ANISOU 1518 C GLU A 212 14965 17299 15157 142 -6 -96 C ATOM 1519 O GLU A 212 22.625 -10.340 35.712 1.00122.37 O ANISOU 1519 O GLU A 212 14840 17018 14638 129 -7 -113 O ATOM 1520 CB GLU A 212 25.629 -11.434 36.839 1.00118.53 C ANISOU 1520 CB GLU A 212 14201 16453 14385 124 -3 -60 C ATOM 1521 CG GLU A 212 25.596 -12.891 36.502 1.00116.42 C ANISOU 1521 CG GLU A 212 14126 16175 13935 99 -2 -46 C ATOM 1522 CD GLU A 212 26.695 -13.246 35.550 1.00115.42 C ANISOU 1522 CD GLU A 212 14027 15985 13843 101 -2 -36 C ATOM 1523 OE1 GLU A 212 26.386 -13.567 34.379 1.00110.66 O ANISOU 1523 OE1 GLU A 212 13260 15356 13431 107 -2 -37 O ATOM 1524 OE2 GLU A 212 27.869 -13.185 35.984 1.00117.54 O ANISOU 1524 OE2 GLU A 212 14127 16235 14297 114 -1 -24 O ATOM 1525 N SER A 213 23.735 -9.338 37.403 1.00131.13 N ANISOU 1525 N SER A 213 15748 18132 15944 148 -6 -102 N ATOM 1526 CA SER A 213 22.551 -8.866 38.114 1.00136.62 C ANISOU 1526 CA SER A 213 16266 19379 16263 191 -10 -162 C ATOM 1527 C SER A 213 21.744 -7.892 37.260 1.00138.84 C ANISOU 1527 C SER A 213 16891 19186 16677 160 -11 -152 C ATOM 1528 O SER A 213 20.663 -7.454 37.658 1.00133.41 O ANISOU 1528 O SER A 213 15957 18558 16174 184 -11 -157 O ATOM 1529 CB SER A 213 22.960 -8.190 39.427 1.00130.86 C ANISOU 1529 CB SER A 213 15658 18192 15869 156 -8 -124 C ATOM 1530 OG SER A 213 24.102 -8.812 40.000 1.00126.05 O ANISOU 1530 OG SER A 213 15062 17563 15269 143 -6 -105 O ATOM 1531 N GLN A 214 22.291 -7.537 36.099 1.00149.67 N ANISOU 1531 N GLN A 214 18287 20503 18079 170 -11 -150 N ATOM 1532 CA GLN A 214 21.624 -6.628 35.171 1.00160.10 C ANISOU 1532 CA GLN A 214 19401 21831 19600 210 -13 -153 C ATOM 1533 C GLN A 214 21.452 -7.212 33.760 1.00167.36 C ANISOU 1533 C GLN A 214 20335 22725 20530 207 -13 -149 C ATOM 1534 O GLN A 214 22.334 -7.908 33.254 1.00163.71 O ANISOU 1534 O GLN A 214 20097 22210 19896 176 -12 -146 O ATOM 1535 CB GLN A 214 22.390 -5.308 35.091 1.00163.47 C ANISOU 1535 CB GLN A 214 19719 22685 19708 285 -21 -218 C ATOM 1536 CG GLN A 214 22.522 -4.589 36.416 1.00163.41 C ANISOU 1536 CG GLN A 214 20028 22245 19816 213 -18 -185 C ATOM 1537 CD GLN A 214 23.283 -3.290 36.283 1.00168.53 C ANISOU 1537 CD GLN A 214 20692 22860 20481 227 -20 -195 C ATOM 1538 OE1 GLN A 214 23.705 -2.916 35.187 1.00171.00 O ANISOU 1538 OE1 GLN A 214 21025 23127 20818 234 -21 -192 O ATOM 1539 NE2 GLN A 214 23.467 -2.593 37.398 1.00169.75 N ANISOU 1539 NE2 GLN A 214 20834 23040 20622 230 -21 -209 N ATOM 1540 N PRO A 215 20.306 -6.919 33.122 1.00180.09 N ANISOU 1540 N PRO A 215 21787 24863 21778 280 -20 -224 N ATOM 1541 CA PRO A 215 20.005 -7.353 31.751 1.00182.64 C ANISOU 1541 CA PRO A 215 22456 24698 22242 206 -16 -180 C ATOM 1542 C PRO A 215 20.718 -6.511 30.690 1.00186.67 C ANISOU 1542 C PRO A 215 22991 25155 22780 222 -18 -177 C ATOM 1543 O PRO A 215 21.045 -5.350 30.941 1.00185.53 O ANISOU 1543 O PRO A 215 22656 24998 22840 263 -18 -165 O ATOM 1544 CB PRO A 215 18.489 -7.158 31.652 1.00182.90 C ANISOU 1544 CB PRO A 215 22232 24817 22445 241 -17 -187 C ATOM 1545 CG PRO A 215 18.199 -6.046 32.595 1.00182.63 C ANISOU 1545 CG PRO A 215 22180 24817 22395 264 -20 -197 C ATOM 1546 CD PRO A 215 19.173 -6.202 33.734 1.00183.41 C ANISOU 1546 CD PRO A 215 22159 25380 22149 305 -24 -250 C ATOM 1547 N LEU A 216 20.954 -7.108 29.524 1.00191.65 N ANISOU 1547 N LEU A 216 23439 25754 23625 235 -16 -156 N ATOM 1548 CA LEU A 216 21.596 -6.433 28.394 1.00195.88 C ANISOU 1548 CA LEU A 216 24194 26244 23989 227 -18 -167 C ATOM 1549 C LEU A 216 23.093 -6.200 28.620 1.00198.45 C ANISOU 1549 C LEU A 216 24371 26495 24538 236 -15 -141 C ATOM 1550 O LEU A 216 23.539 -6.037 29.758 1.00198.25 O ANISOU 1550 O LEU A 216 24526 26466 24333 211 -16 -151 O ATOM 1551 CB LEU A 216 20.869 -5.113 28.079 1.00195.78 C ANISOU 1551 CB LEU A 216 24167 26271 23950 262 -22 -182 C ATOM 1552 CG LEU A 216 21.609 -3.895 27.509 1.00193.70 C ANISOU 1552 CG LEU A 216 23925 25963 23708 281 -24 -178 C ATOM 1553 CD1 LEU A 216 20.635 -2.979 26.779 1.00192.95 C ANISOU 1553 CD1 LEU A 216 23812 25921 23579 319 -28 -190 C ATOM 1554 CD2 LEU A 216 22.353 -3.123 28.599 1.00192.00 C ANISOU 1554 CD2 LEU A 216 23535 25721 23697 305 -22 -162 C ATOM 1555 N PRO A 217 23.874 -6.191 27.528 1.00202.37 N ANISOU 1555 N PRO A 217 24786 27337 24766 292 -21 -184 N ATOM 1556 CA PRO A 217 25.297 -5.839 27.579 1.00202.66 C ANISOU 1556 CA PRO A 217 24865 27292 24845 280 -20 -173 C ATOM 1557 C PRO A 217 25.512 -4.325 27.609 1.00198.26 C ANISOU 1557 C PRO A 217 24582 26351 24398 224 -18 -147 C ATOM 1558 O PRO A 217 24.662 -3.563 27.146 1.00196.20 O ANISOU 1558 O PRO A 217 24309 26123 24115 248 -21 -155 O ATOM 1559 CB PRO A 217 25.852 -6.443 26.284 1.00199.92 C ANISOU 1559 CB PRO A 217 24646 26523 24791 214 -14 -120 C ATOM 1560 CG PRO A 217 24.699 -6.425 25.347 1.00199.33 C ANISOU 1560 CG PRO A 217 24714 26492 24532 210 -16 -140 C ATOM 1561 CD PRO A 217 23.467 -6.655 26.188 1.00199.64 C ANISOU 1561 CD PRO A 217 24723 26599 24534 215 -17 -149 C ATOM 1562 N GLY A 218 26.648 -3.896 28.143 1.00195.96 N ANISOU 1562 N GLY A 218 24145 26021 24288 235 -16 -133 N ATOM 1563 CA GLY A 218 26.982 -2.487 28.158 1.00191.53 C ANISOU 1563 CA GLY A 218 23750 25453 23571 230 -20 -153 C ATOM 1564 C GLY A 218 26.869 -1.841 29.522 1.00188.38 C ANISOU 1564 C GLY A 218 23338 25083 23155 235 -22 -164 C ATOM 1565 O GLY A 218 26.083 -2.269 30.368 1.00188.57 O ANISOU 1565 O GLY A 218 23173 25150 23324 258 -20 -153 O ATOM 1566 N GLU A 219 27.646 -0.782 29.723 1.00185.35 N ANISOU 1566 N GLU A 219 22803 24676 22945 259 -21 -157 N ATOM 1567 CA GLU A 219 28.491 -0.233 28.662 1.00184.78 C ANISOU 1567 CA GLU A 219 22662 24909 22637 321 -30 -211 C ATOM 1568 C GLU A 219 29.612 -1.178 28.179 1.00178.70 C ANISOU 1568 C GLU A 219 22011 23741 22144 231 -19 -144 C ATOM 1569 O GLU A 219 29.850 -1.297 26.976 1.00180.55 O ANISOU 1569 O GLU A 219 22173 24276 22151 287 -25 -188 O ATOM 1570 CB GLU A 219 29.050 1.134 29.083 1.00183.48 C ANISOU 1570 CB GLU A 219 22597 24386 22732 264 -24 -167 C ATOM 1571 CG GLU A 219 27.960 2.160 29.401 1.00183.98 C ANISOU 1571 CG GLU A 219 22639 24492 22775 297 -28 -178 C ATOM 1572 CD GLU A 219 28.505 3.531 29.769 1.00182.19 C ANISOU 1572 CD GLU A 219 22416 24257 22551 304 -31 -191 C ATOM 1573 OE1 GLU A 219 27.703 4.490 29.821 1.00182.00 O ANISOU 1573 OE1 GLU A 219 22543 24265 22345 308 -38 -216 O ATOM 1574 OE2 GLU A 219 29.725 3.649 30.010 1.00179.43 O ANISOU 1574 OE2 GLU A 219 22079 23877 22218 279 -30 -196 O ATOM 1575 N ARG A 220 30.286 -1.849 29.109 1.00172.84 N ANISOU 1575 N ARG A 220 21267 22999 21404 212 -17 -142 N ATOM 1576 CA ARG A 220 31.362 -2.782 28.757 1.00163.25 C ANISOU 1576 CA ARG A 220 20072 21751 20206 192 -15 -133 C ATOM 1577 C ARG A 220 30.842 -4.138 28.247 1.00152.50 C ANISOU 1577 C ARG A 220 18854 20389 18701 171 -14 -131 C ATOM 1578 O ARG A 220 29.699 -4.516 28.525 1.00152.68 O ANISOU 1578 O ARG A 220 18862 20446 18703 178 -14 -131 O ATOM 1579 CB ARG A 220 32.316 -2.972 29.943 1.00162.07 C ANISOU 1579 CB ARG A 220 20059 21611 19909 164 -15 -148 C ATOM 1580 N ALA A 221 31.679 -4.853 27.489 1.00138.68 N ANISOU 1580 N ALA A 221 17119 18602 16972 160 -13 -122 N ATOM 1581 CA ALA A 221 31.356 -6.206 27.023 1.00123.90 C ANISOU 1581 CA ALA A 221 15112 16725 15240 168 -10 -102 C ATOM 1582 C ALA A 221 31.954 -7.253 27.959 1.00122.86 C ANISOU 1582 C ALA A 221 14889 16915 14878 194 -12 -127 C ATOM 1583 O ALA A 221 33.172 -7.343 28.101 1.00123.72 O ANISOU 1583 O ALA A 221 15097 16688 15224 148 -8 -91 O ATOM 1584 CB ALA A 221 31.851 -6.420 25.603 1.00115.45 C ANISOU 1584 CB ALA A 221 14195 15617 14054 150 -11 -108 C ATOM 1585 N ARG A 222 31.095 -8.044 28.596 1.00117.30 N ANISOU 1585 N ARG A 222 14255 15927 14388 154 -8 -88 N ATOM 1586 CA ARG A 222 31.540 -8.962 29.646 1.00110.37 C ANISOU 1586 CA ARG A 222 13276 15394 13266 182 -9 -107 C ATOM 1587 C ARG A 222 32.625 -9.905 29.144 1.00 96.35 C ANISOU 1587 C ARG A 222 11612 13254 11743 136 -6 -68 C ATOM 1588 O ARG A 222 33.699 -9.997 29.730 1.00 97.85 O ANISOU 1588 O ARG A 222 11801 13443 11932 134 -5 -65 O ATOM 1589 CB ARG A 222 30.362 -9.756 30.236 1.00104.76 C ANISOU 1589 CB ARG A 222 12783 14393 12627 131 -6 -79 C ATOM 1590 N SER A 223 32.345 -10.598 28.052 1.00 83.59 N ANISOU 1590 N SER A 223 10008 11616 10136 133 -5 -65 N ATOM 1591 CA SER A 223 33.258 -11.602 27.545 1.00 82.86 C ANISOU 1591 CA SER A 223 9932 11494 10057 125 -4 -56 C ATOM 1592 C SER A 223 34.641 -11.004 27.293 1.00 86.55 C ANISOU 1592 C SER A 223 10331 12234 10322 157 -7 -82 C ATOM 1593 O SER A 223 35.666 -11.695 27.378 1.00 85.31 O ANISOU 1593 O SER A 223 10262 11771 10382 123 -4 -53 O ATOM 1594 CB SER A 223 32.701 -12.181 26.248 1.00 86.49 C ANISOU 1594 CB SER A 223 10403 11935 10525 122 -4 -56 C ATOM 1595 OG SER A 223 32.694 -11.199 25.224 1.00 89.47 O ANISOU 1595 OG SER A 223 10917 12294 10783 117 -6 -72 O ATOM 1596 N THR A 224 34.655 -9.714 26.975 1.00 77.40 N ANISOU 1596 N THR A 224 9259 10770 9379 131 -6 -71 N ATOM 1597 CA THR A 224 35.864 -9.041 26.528 1.00 67.31 C ANISOU 1597 CA THR A 224 7994 9469 8112 129 -7 -77 C ATOM 1598 C THR A 224 36.643 -8.477 27.696 1.00 68.14 C ANISOU 1598 C THR A 224 8085 9600 8207 130 -7 -83 C ATOM 1599 O THR A 224 37.796 -8.111 27.565 1.00 69.23 O ANISOU 1599 O THR A 224 8226 9729 8349 127 -7 -88 O ATOM 1600 CB THR A 224 35.524 -7.933 25.519 1.00 70.28 C ANISOU 1600 CB THR A 224 8502 9826 8374 123 -9 -94 C ATOM 1601 OG1 THR A 224 36.436 -7.998 24.419 1.00 83.41 O ANISOU 1601 OG1 THR A 224 10062 11456 10175 129 -8 -86 O ATOM 1602 CG2 THR A 224 35.560 -6.544 26.162 1.00 59.65 C ANISOU 1602 CG2 THR A 224 7025 8495 7144 139 -9 -97 C ATOM 1603 N LEU A 225 35.998 -8.416 28.849 1.00 72.78 N ANISOU 1603 N LEU A 225 8652 10223 8779 133 -7 -82 N ATOM 1604 CA LEU A 225 36.670 -8.044 30.084 1.00 74.28 C ANISOU 1604 CA LEU A 225 8822 10448 8954 133 -7 -87 C ATOM 1605 C LEU A 225 37.445 -9.247 30.556 1.00 73.53 C ANISOU 1605 C LEU A 225 8719 10366 8852 130 -6 -75 C ATOM 1606 O LEU A 225 38.665 -9.234 30.569 1.00 79.59 O ANISOU 1606 O LEU A 225 9485 11138 9619 129 -6 -78 O ATOM 1607 CB LEU A 225 35.646 -7.680 31.153 1.00 75.06 C ANISOU 1607 CB LEU A 225 8900 10585 9036 137 -7 -90 C ATOM 1608 CG LEU A 225 36.000 -6.660 32.229 1.00 67.74 C ANISOU 1608 CG LEU A 225 7951 9693 8094 138 -8 -104 C ATOM 1609 CD1 LEU A 225 35.219 -6.992 33.476 1.00 63.22 C ANISOU 1609 CD1 LEU A 225 7504 9167 7347 129 -8 -109 C ATOM 1610 CD2 LEU A 225 37.475 -6.666 32.500 1.00 71.50 C ANISOU 1610 CD2 LEU A 225 8420 10179 8566 133 -8 -108 C ATOM 1611 N GLN A 226 36.725 -10.307 30.908 1.00 74.13 N ANISOU 1611 N GLN A 226 8789 10454 8922 131 -5 -60 N ATOM 1612 CA GLN A 226 37.353 -11.509 31.436 1.00 82.89 C ANISOU 1612 CA GLN A 226 10031 11582 9881 120 -4 -49 C ATOM 1613 C GLN A 226 38.450 -11.991 30.485 1.00 88.02 C ANISOU 1613 C GLN A 226 10466 12522 10455 162 -5 -59 C ATOM 1614 O GLN A 226 39.337 -12.741 30.879 1.00 88.77 O ANISOU 1614 O GLN A 226 10641 12315 10772 134 -3 -34 O ATOM 1615 CB GLN A 226 36.318 -12.611 31.676 1.00 85.00 C ANISOU 1615 CB GLN A 226 10296 11858 10144 119 -2 -32 C ATOM 1616 CG GLN A 226 35.771 -13.211 30.403 1.00 96.59 C ANISOU 1616 CG GLN A 226 11643 13285 11772 125 -2 -27 C ATOM 1617 CD GLN A 226 34.354 -13.762 30.548 1.00104.73 C ANISOU 1617 CD GLN A 226 12805 14331 12657 111 -2 -23 C ATOM 1618 OE1 GLN A 226 33.744 -14.202 29.564 1.00105.84 O ANISOU 1618 OE1 GLN A 226 12819 14449 12948 117 -2 -22 O ATOM 1619 NE2 GLN A 226 33.824 -13.736 31.772 1.00102.72 N ANISOU 1619 NE2 GLN A 226 12532 14119 12379 112 -1 -18 N ATOM 1620 N LYS A 227 38.410 -11.550 29.235 1.00 82.85 N ANISOU 1620 N LYS A 227 9925 11504 10050 127 -4 -52 N ATOM 1621 CA LYS A 227 39.518 -11.852 28.341 1.00 84.50 C ANISOU 1621 CA LYS A 227 10063 11989 10053 157 -6 -72 C ATOM 1622 C LYS A 227 40.730 -10.936 28.583 1.00 78.10 C ANISOU 1622 C LYS A 227 9328 10895 9453 126 -5 -66 C ATOM 1623 O LYS A 227 41.860 -11.398 28.529 1.00 81.96 O ANISOU 1623 O LYS A 227 9811 11395 9937 128 -5 -65 O ATOM 1624 CB LYS A 227 39.073 -11.885 26.870 1.00 92.25 C ANISOU 1624 CB LYS A 227 11279 12625 11148 111 -5 -60 C ATOM 1625 CG LYS A 227 38.794 -13.300 26.341 1.00 97.36 C ANISOU 1625 CG LYS A 227 11812 13256 11926 119 -4 -43 C ATOM 1626 CD LYS A 227 40.033 -14.190 26.531 1.00108.04 C ANISOU 1626 CD LYS A 227 13160 14617 13274 122 -3 -36 C ATOM 1627 CE LYS A 227 39.748 -15.674 26.273 1.00110.22 C ANISOU 1627 CE LYS A 227 13441 14884 13553 122 -2 -22 C ATOM 1628 NZ LYS A 227 40.852 -16.572 26.763 1.00103.91 N ANISOU 1628 NZ LYS A 227 12755 14108 12620 119 -1 -12 N ATOM 1629 N GLU A 228 40.497 -9.656 28.870 1.00 72.42 N ANISOU 1629 N GLU A 228 8602 10183 8731 125 -6 -79 N ATOM 1630 CA GLU A 228 41.568 -8.742 29.282 1.00 66.87 C ANISOU 1630 CA GLU A 228 7885 9506 8018 123 -7 -95 C ATOM 1631 C GLU A 228 42.200 -9.214 30.588 1.00 75.24 C ANISOU 1631 C GLU A 228 9056 10624 8908 117 -7 -100 C ATOM 1632 O GLU A 228 43.427 -9.152 30.757 1.00 78.32 O ANISOU 1632 O GLU A 228 9284 11043 9430 128 -7 -100 O ATOM 1633 CB GLU A 228 41.023 -7.331 29.529 1.00 61.45 C ANISOU 1633 CB GLU A 228 7194 8822 7331 121 -8 -109 C ATOM 1634 CG GLU A 228 40.814 -6.466 28.308 1.00 71.28 C ANISOU 1634 CG GLU A 228 8463 10023 8596 118 -9 -117 C ATOM 1635 CD GLU A 228 40.091 -5.149 28.629 1.00 86.65 C ANISOU 1635 CD GLU A 228 10406 11976 10542 120 -10 -129 C ATOM 1636 OE1 GLU A 228 38.992 -5.174 29.247 1.00 90.03 O ANISOU 1636 OE1 GLU A 228 10827 12419 10963 125 -10 -125 O ATOM 1637 OE2 GLU A 228 40.626 -4.082 28.252 1.00 88.43 O ANISOU 1637 OE2 GLU A 228 10766 12193 10641 106 -11 -155 O ATOM 1638 N VAL A 229 41.349 -9.662 31.514 1.00 73.20 N ANISOU 1638 N VAL A 229 8640 10388 8782 131 -6 -81 N ATOM 1639 CA VAL A 229 41.772 -9.996 32.876 1.00 73.97 C ANISOU 1639 CA VAL A 229 8859 10551 8697 125 -6 -83 C ATOM 1640 C VAL A 229 42.576 -11.290 32.964 1.00 73.12 C ANISOU 1640 C VAL A 229 8744 10462 8577 133 -5 -65 C ATOM 1641 O VAL A 229 43.412 -11.439 33.849 1.00 63.98 O ANISOU 1641 O VAL A 229 7561 9363 7386 139 -5 -65 O ATOM 1642 CB VAL A 229 40.571 -10.084 33.845 1.00 69.90 C ANISOU 1642 CB VAL A 229 8333 10057 8168 127 -5 -75 C ATOM 1643 CG1 VAL A 229 40.979 -10.739 35.168 1.00 60.69 C ANISOU 1643 CG1 VAL A 229 7138 8956 6963 133 -5 -62 C ATOM 1644 CG2 VAL A 229 39.973 -8.704 34.086 1.00 69.04 C ANISOU 1644 CG2 VAL A 229 8222 9950 8059 122 -7 -96 C ATOM 1645 N HIS A 230 42.315 -12.223 32.051 1.00 73.57 N ANISOU 1645 N HIS A 230 8668 10474 8811 145 -4 -46 N ATOM 1646 CA HIS A 230 43.053 -13.481 32.010 1.00 73.85 C ANISOU 1646 CA HIS A 230 8697 10523 8839 154 -3 -30 C ATOM 1647 C HIS A 230 44.490 -13.224 31.574 1.00 78.09 C ANISOU 1647 C HIS A 230 9226 11074 9370 158 -4 -42 C ATOM 1648 O HIS A 230 45.426 -13.926 31.976 1.00 80.58 O ANISOU 1648 O HIS A 230 9517 11433 9665 171 -3 -34 O ATOM 1649 CB HIS A 230 42.390 -14.470 31.046 1.00 75.35 C ANISOU 1649 CB HIS A 230 9063 10662 8904 139 -2 -18 C ATOM 1650 CG HIS A 230 43.068 -15.807 30.986 1.00 77.49 C ANISOU 1650 CG HIS A 230 9330 10945 9167 148 0 1 C ATOM 1651 ND1 HIS A 230 43.047 -16.702 32.039 1.00 74.21 N ANISOU 1651 ND1 HIS A 230 8895 10574 8726 159 2 25 N ATOM 1652 CD2 HIS A 230 43.790 -16.397 30.004 1.00 77.92 C ANISOU 1652 CD2 HIS A 230 9251 10974 9382 164 0 2 C ATOM 1653 CE1 HIS A 230 43.725 -17.784 31.702 1.00 77.84 C ANISOU 1653 CE1 HIS A 230 9201 11034 9340 185 4 37 C ATOM 1654 NE2 HIS A 230 44.190 -17.625 30.474 1.00 78.84 N ANISOU 1654 NE2 HIS A 230 9352 11120 9485 179 2 23 N ATOM 1655 N ALA A 231 44.665 -12.218 30.729 1.00 75.43 N ANISOU 1655 N ALA A 231 8906 10705 9049 148 -5 -62 N ATOM 1656 CA ALA A 231 45.997 -11.865 30.282 1.00 66.40 C ANISOU 1656 CA ALA A 231 7906 9578 7745 136 -7 -84 C ATOM 1657 C ALA A 231 46.707 -11.066 31.379 1.00 67.91 C ANISOU 1657 C ALA A 231 7904 9838 8061 150 -7 -93 C ATOM 1658 O ALA A 231 47.938 -11.093 31.467 1.00 59.97 O ANISOU 1658 O ALA A 231 7041 8879 6867 142 -9 -113 O ATOM 1659 CB ALA A 231 45.944 -11.093 28.961 1.00 50.91 C ANISOU 1659 CB ALA A 231 5821 7558 5963 137 -7 -91 C ATOM 1660 N ALA A 232 45.940 -10.364 32.217 1.00 69.95 N ANISOU 1660 N ALA A 232 8317 10111 8148 133 -8 -106 N ATOM 1661 CA ALA A 232 46.539 -9.632 33.331 1.00 72.93 C ANISOU 1661 CA ALA A 232 8664 10561 8487 132 -9 -125 C ATOM 1662 C ALA A 232 47.028 -10.627 34.377 1.00 83.05 C ANISOU 1662 C ALA A 232 9916 11913 9727 147 -8 -108 C ATOM 1663 O ALA A 232 48.175 -10.554 34.819 1.00 88.25 O ANISOU 1663 O ALA A 232 10545 12638 10347 153 -9 -121 O ATOM 1664 CB ALA A 232 45.560 -8.653 33.931 1.00 68.80 C ANISOU 1664 CB ALA A 232 7966 10035 8140 135 -8 -124 C ATOM 1665 N LYS A 233 46.164 -11.573 34.742 1.00 84.57 N ANISOU 1665 N LYS A 233 9934 12094 10106 169 -6 -72 N ATOM 1666 CA LYS A 233 46.541 -12.667 35.636 1.00 82.32 C ANISOU 1666 CA LYS A 233 9617 11870 9793 188 -4 -50 C ATOM 1667 C LYS A 233 47.826 -13.325 35.146 1.00 82.97 C ANISOU 1667 C LYS A 233 9686 11975 9863 203 -4 -48 C ATOM 1668 O LYS A 233 48.682 -13.710 35.932 1.00 84.62 O ANISOU 1668 O LYS A 233 9851 12263 10036 221 -4 -43 O ATOM 1669 CB LYS A 233 45.417 -13.713 35.734 1.00 80.93 C ANISOU 1669 CB LYS A 233 9460 11661 9630 192 -2 -20 C ATOM 1670 CG LYS A 233 44.193 -13.295 36.586 1.00 81.77 C ANISOU 1670 CG LYS A 233 9562 11773 9734 184 -1 -18 C ATOM 1671 CD LYS A 233 43.029 -14.296 36.425 1.00 82.25 C ANISOU 1671 CD LYS A 233 9826 11795 9630 169 1 8 C ATOM 1672 CE LYS A 233 41.741 -13.845 37.121 1.00 84.79 C ANISOU 1672 CE LYS A 233 9965 12120 10133 176 1 7 C ATOM 1673 NZ LYS A 233 41.699 -14.125 38.590 1.00 82.38 N ANISOU 1673 NZ LYS A 233 9617 11890 9794 186 2 22 N ATOM 1674 N SER A 234 47.960 -13.432 33.833 1.00 87.69 N ANISOU 1674 N SER A 234 10320 12509 10490 196 -5 -53 N ATOM 1675 CA SER A 234 49.122 -14.059 33.216 1.00 89.11 C ANISOU 1675 CA SER A 234 10491 12704 10661 209 -5 -53 C ATOM 1676 C SER A 234 50.385 -13.193 33.312 1.00 78.53 C ANISOU 1676 C SER A 234 9117 11424 9297 209 -7 -83 C ATOM 1677 O SER A 234 51.496 -13.708 33.354 1.00 79.48 O ANISOU 1677 O SER A 234 9206 11600 9391 227 -8 -85 O ATOM 1678 CB SER A 234 48.810 -14.373 31.749 1.00 96.12 C ANISOU 1678 CB SER A 234 11428 13507 11587 199 -5 -51 C ATOM 1679 OG SER A 234 49.268 -15.660 31.387 1.00 97.90 O ANISOU 1679 OG SER A 234 11654 13734 11809 216 -3 -32 O ATOM 1680 N LEU A 235 50.217 -11.878 33.322 1.00 70.56 N ANISOU 1680 N LEU A 235 8109 10406 8294 188 -9 -109 N ATOM 1681 CA LEU A 235 51.354 -10.976 33.441 1.00 68.77 C ANISOU 1681 CA LEU A 235 7846 10239 8044 182 -11 -143 C ATOM 1682 C LEU A 235 51.791 -10.846 34.900 1.00 78.58 C ANISOU 1682 C LEU A 235 9244 11585 9025 176 -12 -163 C ATOM 1683 O LEU A 235 52.956 -10.533 35.192 1.00 90.70 O ANISOU 1683 O LEU A 235 10370 13722 10369 245 -17 -239 O ATOM 1684 CB LEU A 235 51.032 -9.604 32.840 1.00 67.10 C ANISOU 1684 CB LEU A 235 7530 10429 7535 195 -15 -229 C ATOM 1685 CG LEU A 235 50.863 -9.580 31.316 1.00 61.33 C ANISOU 1685 CG LEU A 235 7160 9161 6981 135 -12 -181 C ATOM 1686 CD1 LEU A 235 50.551 -8.182 30.769 1.00 54.26 C ANISOU 1686 CD1 LEU A 235 5982 8635 5998 156 -15 -256 C ATOM 1687 CD2 LEU A 235 52.095 -10.171 30.661 1.00 56.04 C ANISOU 1687 CD2 LEU A 235 6479 8516 6296 144 -13 -189 C ATOM 1688 N ALA A 236 50.855 -11.085 35.815 1.00 70.59 N ANISOU 1688 N ALA A 236 8017 10579 8226 196 -10 -129 N ATOM 1689 CA ALA A 236 51.154 -11.041 37.245 1.00 66.97 C ANISOU 1689 CA ALA A 236 7502 10222 7723 207 -10 -132 C ATOM 1690 C ALA A 236 51.944 -12.270 37.703 1.00 71.29 C ANISOU 1690 C ALA A 236 8011 10841 8234 242 -9 -109 C ATOM 1691 O ALA A 236 52.717 -12.210 38.657 1.00 74.29 O ANISOU 1691 O ALA A 236 8332 11328 8569 257 -10 -119 O ATOM 1692 CB ALA A 236 49.875 -10.898 38.057 1.00 56.92 C ANISOU 1692 CB ALA A 236 6464 8934 6229 183 -9 -127 C ATOM 1693 N ILE A 237 51.729 -13.390 37.027 1.00 68.66 N ANISOU 1693 N ILE A 237 7941 10457 7689 235 -8 -87 N ATOM 1694 CA ILE A 237 52.404 -14.625 37.359 1.00 68.35 C ANISOU 1694 CA ILE A 237 7879 10478 7612 270 -6 -59 C ATOM 1695 C ILE A 237 53.898 -14.367 37.295 1.00 80.13 C ANISOU 1695 C ILE A 237 9085 12052 9308 309 -9 -83 C ATOM 1696 O ILE A 237 54.650 -14.700 38.208 1.00 88.78 O ANISOU 1696 O ILE A 237 10122 13255 10355 339 -9 -80 O ATOM 1697 CB ILE A 237 52.022 -15.705 36.353 1.00 68.41 C ANISOU 1697 CB ILE A 237 7925 10405 7664 276 -3 -29 C ATOM 1698 CG1 ILE A 237 50.867 -16.545 36.894 1.00 67.69 C ANISOU 1698 CG1 ILE A 237 7621 10283 7814 307 1 12 C ATOM 1699 CG2 ILE A 237 53.225 -16.568 35.989 1.00 70.54 C ANISOU 1699 CG2 ILE A 237 7942 10719 8141 333 -2 -21 C ATOM 1700 CD1 ILE A 237 50.208 -17.397 35.816 1.00 66.63 C ANISOU 1700 CD1 ILE A 237 7754 10058 7507 275 4 34 C ATOM 1701 N ILE A 238 54.319 -13.749 36.206 1.00 79.20 N ANISOU 1701 N ILE A 238 9234 11892 8966 264 -12 -122 N ATOM 1702 CA ILE A 238 55.702 -13.365 36.029 1.00 74.80 C ANISOU 1702 CA ILE A 238 8387 11409 8624 295 -14 -148 C ATOM 1703 C ILE A 238 56.204 -12.619 37.248 1.00 82.05 C ANISOU 1703 C ILE A 238 9509 12441 9224 270 -17 -190 C ATOM 1704 O ILE A 238 57.215 -12.988 37.829 1.00 95.12 O ANISOU 1704 O ILE A 238 11119 14209 10815 298 -19 -199 O ATOM 1705 CB ILE A 238 55.840 -12.472 34.804 1.00 72.43 C ANISOU 1705 CB ILE A 238 7962 11608 7950 327 -22 -244 C ATOM 1706 CG1 ILE A 238 55.720 -13.331 33.548 1.00 62.65 C ANISOU 1706 CG1 ILE A 238 7167 9719 6918 245 -16 -173 C ATOM 1707 CG2 ILE A 238 57.154 -11.729 34.844 1.00 73.55 C ANISOU 1707 CG2 ILE A 238 8467 11271 8207 236 -21 -248 C ATOM 1708 CD1 ILE A 238 55.884 -12.572 32.290 1.00 62.85 C ANISOU 1708 CD1 ILE A 238 6990 9679 7211 240 -16 -185 C ATOM 1709 N VAL A 239 55.491 -11.575 37.646 1.00 77.71 N ANISOU 1709 N VAL A 239 8700 11868 8959 262 -16 -189 N ATOM 1710 CA VAL A 239 55.850 -10.841 38.851 1.00 76.11 C ANISOU 1710 CA VAL A 239 8435 11772 8713 256 -16 -216 C ATOM 1711 C VAL A 239 56.109 -11.801 40.024 1.00 78.76 C ANISOU 1711 C VAL A 239 9012 12211 8704 273 -17 -206 C ATOM 1712 O VAL A 239 57.125 -11.710 40.709 1.00 70.48 O ANISOU 1712 O VAL A 239 7765 11359 7654 316 111 -243 O ATOM 1713 CB VAL A 239 54.741 -9.835 39.237 1.00 68.39 C ANISOU 1713 CB VAL A 239 7481 10744 7758 221 -15 -223 C ATOM 1714 CG1 VAL A 239 55.097 -9.098 40.524 1.00 65.84 C ANISOU 1714 CG1 VAL A 239 7090 10536 7389 211 -15 -252 C ATOM 1715 CG2 VAL A 239 54.494 -8.863 38.102 1.00 66.90 C ANISOU 1715 CG2 VAL A 239 7341 10463 7615 186 -15 -247 C ATOM 1716 N GLY A 240 55.186 -12.731 40.236 1.00 85.81 N ANISOU 1716 N GLY A 240 9642 13053 9909 316 -13 -140 N ATOM 1717 CA GLY A 240 55.273 -13.655 41.350 1.00 83.81 C ANISOU 1717 CA GLY A 240 9536 12893 9415 344 131 -128 C ATOM 1718 C GLY A 240 56.506 -14.519 41.274 1.00 83.81 C ANISOU 1718 C GLY A 240 9421 13123 9299 414 104 -128 C ATOM 1719 O GLY A 240 57.157 -14.770 42.289 1.00 88.32 O ANISOU 1719 O GLY A 240 9845 13975 9737 477 80 -130 O ATOM 1720 N LEU A 241 56.824 -14.978 40.068 1.00 81.64 N ANISOU 1720 N LEU A 241 9208 12746 9066 411 105 -125 N ATOM 1721 CA LEU A 241 58.026 -15.774 39.843 1.00 84.33 C ANISOU 1721 CA LEU A 241 9442 13298 9301 483 80 -128 C ATOM 1722 C LEU A 241 59.283 -14.989 40.211 1.00 86.50 C ANISOU 1722 C LEU A 241 9580 13827 9460 510 54 -196 C ATOM 1723 O LEU A 241 60.181 -15.520 40.865 1.00 92.50 O ANISOU 1723 O LEU A 241 10189 14878 10079 595 27 -202 O ATOM 1724 CB LEU A 241 58.108 -16.252 38.393 1.00 81.82 C ANISOU 1724 CB LEU A 241 9219 12812 9058 464 85 -122 C ATOM 1725 CG LEU A 241 56.909 -17.048 37.874 1.00 83.02 C ANISOU 1725 CG LEU A 241 9501 12720 9321 431 108 -69 C ATOM 1726 CD1 LEU A 241 57.271 -17.723 36.568 1.00 85.51 C ANISOU 1726 CD1 LEU A 241 9864 12960 9667 433 103 -65 C ATOM 1727 CD2 LEU A 241 56.459 -18.077 38.886 1.00 79.82 C ANISOU 1727 CD2 LEU A 241 9040 12417 8869 482 108 -16 C ATOM 1728 N PHE A 242 59.345 -13.727 39.797 1.00 78.60 N ANISOU 1728 N PHE A 242 8627 12728 8511 443 62 -248 N ATOM 1729 CA PHE A 242 60.478 -12.877 40.141 1.00 82.49 C ANISOU 1729 CA PHE A 242 8990 13455 8900 452 40 -326 C ATOM 1730 C PHE A 242 60.710 -12.925 41.658 1.00 85.46 C ANISOU 1730 C PHE A 242 9214 14113 9143 502 20 -335 C ATOM 1731 O PHE A 242 61.806 -13.249 42.125 1.00 86.08 O ANISOU 1731 O PHE A 242 9132 14501 9075 574 -12 -370 O ATOM 1732 CB PHE A 242 60.237 -11.444 39.649 1.00 84.92 C ANISOU 1732 CB PHE A 242 9382 13592 9294 368 59 -370 C ATOM 1733 CG PHE A 242 61.388 -10.504 39.902 1.00 96.09 C ANISOU 1733 CG PHE A 242 10665 15234 10609 361 40 -462 C ATOM 1734 CD1 PHE A 242 62.176 -10.050 38.856 1.00100.55 C ANISOU 1734 CD1 PHE A 242 11235 15783 11186 339 36 -516 C ATOM 1735 CD2 PHE A 242 61.683 -10.068 41.188 1.00101.77 C ANISOU 1735 CD2 PHE A 242 11250 16198 11220 371 24 -503 C ATOM 1736 CE1 PHE A 242 63.241 -9.171 39.088 1.00100.69 C ANISOU 1736 CE1 PHE A 242 11125 16021 11113 323 20 -615 C ATOM 1737 CE2 PHE A 242 62.748 -9.195 41.423 1.00103.89 C ANISOU 1737 CE2 PHE A 242 11389 16693 11393 354 7 -603 C ATOM 1738 CZ PHE A 242 63.524 -8.748 40.370 1.00100.66 C ANISOU 1738 CZ PHE A 242 10985 16259 11001 328 6 -662 C ATOM 1739 N ALA A 243 59.664 -12.624 42.420 1.00 85.75 N ANISOU 1739 N ALA A 243 9297 14058 9226 469 37 -303 N ATOM 1740 CA ALA A 243 59.709 -12.740 43.872 1.00 86.70 C ANISOU 1740 CA ALA A 243 9284 14435 9225 515 17 -300 C ATOM 1741 C ALA A 243 60.231 -14.105 44.318 1.00 85.86 C ANISOU 1741 C ALA A 243 9066 14559 8996 629 -8 -255 C ATOM 1742 O ALA A 243 60.998 -14.200 45.266 1.00 92.70 O ANISOU 1742 O ALA A 243 9788 15696 9739 690 -69 -271 O ATOM 1743 CB ALA A 243 58.329 -12.481 44.465 1.00 84.37 C ANISOU 1743 CB ALA A 243 9075 13966 9016 469 41 -258 C ATOM 1744 N LEU A 244 59.813 -15.158 43.629 1.00 78.46 N ANISOU 1744 N LEU A 244 8220 13462 8130 651 6 -190 N ATOM 1745 CA LEU A 244 60.198 -16.520 43.984 1.00 85.48 C ANISOU 1745 CA LEU A 244 9021 14544 8915 769 -12 -132 C ATOM 1746 C LEU A 244 61.677 -16.821 43.635 1.00 89.75 C ANISOU 1746 C LEU A 244 9484 15187 9431 824 -115 -157 C ATOM 1747 O LEU A 244 62.351 -17.600 44.313 1.00 84.14 O ANISOU 1747 O LEU A 244 8710 14536 8722 900 -256 -108 O ATOM 1748 CB LEU A 244 59.225 -17.497 43.305 1.00 89.88 C ANISOU 1748 CB LEU A 244 9719 14835 9597 752 17 -56 C ATOM 1749 CG LEU A 244 59.291 -19.018 43.479 1.00 89.67 C ANISOU 1749 CG LEU A 244 9649 14916 9507 862 12 24 C ATOM 1750 CD1 LEU A 244 59.402 -19.401 44.948 1.00 86.24 C ANISOU 1750 CD1 LEU A 244 9128 14621 9017 933 -84 75 C ATOM 1751 CD2 LEU A 244 58.070 -19.680 42.799 1.00 82.32 C ANISOU 1751 CD2 LEU A 244 8878 13671 8730 799 45 78 C ATOM 1752 N CYS A 245 62.171 -16.209 42.562 1.00 94.79 N ANISOU 1752 N CYS A 245 10139 15802 10074 782 -72 -228 N ATOM 1753 CA CYS A 245 63.582 -16.326 42.172 1.00 96.51 C ANISOU 1753 CA CYS A 245 10283 16076 10310 813 -187 -262 C ATOM 1754 C CYS A 245 64.537 -15.370 42.895 1.00 98.21 C ANISOU 1754 C CYS A 245 10386 16427 10504 791 -290 -332 C ATOM 1755 O CYS A 245 65.673 -15.740 43.201 1.00 99.16 O ANISOU 1755 O CYS A 245 10406 16633 10636 844 -435 -332 O ATOM 1756 CB CYS A 245 63.745 -16.177 40.658 1.00 94.29 C ANISOU 1756 CB CYS A 245 10069 15707 10048 780 -110 -307 C ATOM 1757 SG CYS A 245 63.333 -17.659 39.724 1.00127.87 S ANISOU 1757 SG CYS A 245 14410 19835 14341 830 -77 -225 S ATOM 1758 N TRP A 246 64.103 -14.130 43.118 1.00 96.91 N ANISOU 1758 N TRP A 246 10232 16282 10307 712 -216 -396 N ATOM 1759 CA TRP A 246 64.955 -13.151 43.799 1.00 98.16 C ANISOU 1759 CA TRP A 246 10286 16570 10442 675 -309 -470 C ATOM 1760 C TRP A 246 64.784 -13.004 45.308 1.00105.95 C ANISOU 1760 C TRP A 246 11215 17653 11389 681 -398 -446 C ATOM 1761 O TRP A 246 65.585 -12.333 45.947 1.00111.35 O ANISOU 1761 O TRP A 246 11806 18456 12046 654 -502 -502 O ATOM 1762 CB TRP A 246 64.864 -11.780 43.132 1.00 93.72 C ANISOU 1762 CB TRP A 246 9751 15990 9869 582 -204 -568 C ATOM 1763 CG TRP A 246 65.709 -11.718 41.924 1.00101.43 C ANISOU 1763 CG TRP A 246 10726 16941 10874 574 -205 -620 C ATOM 1764 CD1 TRP A 246 65.286 -11.675 40.637 1.00101.71 C ANISOU 1764 CD1 TRP A 246 10869 16857 10919 554 -91 -632 C ATOM 1765 CD2 TRP A 246 67.144 -11.741 41.878 1.00108.82 C ANISOU 1765 CD2 TRP A 246 11540 17974 11831 590 -339 -666 C ATOM 1766 NE1 TRP A 246 66.364 -11.648 39.787 1.00104.95 N ANISOU 1766 NE1 TRP A 246 11238 17280 11360 553 -144 -684 N ATOM 1767 CE2 TRP A 246 67.517 -11.691 40.524 1.00105.54 C ANISOU 1767 CE2 TRP A 246 11164 17489 11448 575 -291 -707 C ATOM 1768 CE3 TRP A 246 68.149 -11.791 42.852 1.00115.86 C ANISOU 1768 CE3 TRP A 246 12291 19011 12718 615 -503 -679 C ATOM 1769 CZ2 TRP A 246 68.849 -11.691 40.112 1.00106.01 C ANISOU 1769 CZ2 TRP A 246 11116 17616 11547 582 -390 -761 C ATOM 1770 CZ3 TRP A 246 69.474 -11.788 42.441 1.00115.62 C ANISOU 1770 CZ3 TRP A 246 12151 19055 12724 624 -603 -733 C ATOM 1771 CH2 TRP A 246 69.810 -11.739 41.082 1.00110.77 C ANISOU 1771 CH2 TRP A 246 11569 18366 12154 607 -542 -774 C ATOM 1772 N LEU A 247 63.746 -13.605 45.879 1.00108.37 N ANISOU 1772 N LEU A 247 11577 17910 11688 710 -362 -366 N ATOM 1773 CA LEU A 247 63.503 -13.457 47.314 1.00108.61 C ANISOU 1773 CA LEU A 247 11569 18023 11674 712 -450 -341 C ATOM 1774 C LEU A 247 64.513 -14.185 48.197 1.00107.06 C ANISOU 1774 C LEU A 247 11293 17937 11449 791 -659 -301 C ATOM 1775 O LEU A 247 65.100 -13.578 49.099 1.00103.58 O ANISOU 1775 O LEU A 247 10779 17617 10958 767 -781 -340 O ATOM 1776 CB LEU A 247 62.076 -13.860 47.689 1.00109.50 C ANISOU 1776 CB LEU A 247 11759 18053 11792 718 -356 -270 C ATOM 1777 CG LEU A 247 61.339 -12.784 48.484 1.00109.94 C ANISOU 1777 CG LEU A 247 11810 18140 11820 644 -313 -307 C ATOM 1778 CD1 LEU A 247 61.471 -11.436 47.785 1.00105.74 C ANISOU 1778 CD1 LEU A 247 11271 17607 11297 557 -215 -410 C ATOM 1779 CD2 LEU A 247 59.879 -13.163 48.683 1.00108.87 C ANISOU 1779 CD2 LEU A 247 11742 17915 11708 646 -204 -243 C ATOM 1780 N PRO A 248 64.717 -15.489 47.945 1.00108.29 N ANISOU 1780 N PRO A 248 11463 18052 11632 885 -709 -221 N ATOM 1781 CA PRO A 248 65.604 -16.255 48.827 1.00109.99 C ANISOU 1781 CA PRO A 248 11609 18367 11815 976 -914 -168 C ATOM 1782 C PRO A 248 66.956 -15.565 48.993 1.00115.77 C ANISOU 1782 C PRO A 248 12220 19238 12529 957 -1047 -249 C ATOM 1783 O PRO A 248 67.452 -15.455 50.114 1.00121.80 O ANISOU 1783 O PRO A 248 12924 20123 13230 976 -1208 -244 O ATOM 1784 CB PRO A 248 65.760 -17.589 48.094 1.00104.14 C ANISOU 1784 CB PRO A 248 10895 17545 11129 1069 -915 -93 C ATOM 1785 CG PRO A 248 64.509 -17.725 47.310 1.00104.43 C ANISOU 1785 CG PRO A 248 11043 17435 11202 1028 -718 -75 C ATOM 1786 CD PRO A 248 64.153 -16.326 46.871 1.00104.55 C ANISOU 1786 CD PRO A 248 11071 17441 11213 913 -589 -173 C ATOM 1787 N LEU A 249 67.534 -15.089 47.896 1.00110.33 N ANISOU 1787 N LEU A 249 11497 18535 11890 916 -984 -325 N ATOM 1788 CA LEU A 249 68.815 -14.402 47.964 1.00105.58 C ANISOU 1788 CA LEU A 249 10769 18064 11281 887 -1099 -411 C ATOM 1789 C LEU A 249 68.780 -13.292 49.007 1.00100.63 C ANISOU 1789 C LEU A 249 10105 17544 10584 808 -1151 -472 C ATOM 1790 O LEU A 249 69.737 -13.111 49.759 1.00106.01 O ANISOU 1790 O LEU A 249 10680 18371 11227 816 -1323 -501 O ATOM 1791 CB LEU A 249 69.198 -13.838 46.599 1.00107.80 C ANISOU 1791 CB LEU A 249 11043 18295 11620 830 -991 -495 C ATOM 1792 CG LEU A 249 70.668 -13.453 46.414 1.00111.85 C ANISOU 1792 CG LEU A 249 11410 18932 12155 820 -1114 -575 C ATOM 1793 CD1 LEU A 249 70.982 -13.232 44.940 1.00110.72 C ANISOU 1793 CD1 LEU A 249 11282 18711 12077 786 -1008 -633 C ATOM 1794 CD2 LEU A 249 71.039 -12.228 47.240 1.00111.16 C ANISOU 1794 CD2 LEU A 249 11246 18978 12012 731 -1178 -665 C ATOM 1795 N HIS A 250 67.681 -12.549 49.057 1.00 95.33 N ANISOU 1795 N HIS A 250 9517 16805 9897 729 -1007 -492 N ATOM 1796 CA HIS A 250 67.545 -11.490 50.053 1.00103.04 C ANISOU 1796 CA HIS A 250 10469 17872 10809 648 -1048 -548 C ATOM 1797 C HIS A 250 67.217 -12.043 51.455 1.00100.63 C ANISOU 1797 C HIS A 250 10182 17622 10430 699 -1181 -469 C ATOM 1798 O HIS A 250 67.804 -11.604 52.450 1.00 93.78 O ANISOU 1798 O HIS A 250 9252 16889 9491 675 -1335 -503 O ATOM 1799 CB HIS A 250 66.519 -10.437 49.614 1.00107.14 C ANISOU 1799 CB HIS A 250 11062 18303 11342 549 -853 -600 C ATOM 1800 CG HIS A 250 66.941 -9.626 48.422 1.00110.53 C ANISOU 1800 CG HIS A 250 11477 18704 11817 485 -749 -693 C ATOM 1801 ND1 HIS A 250 66.448 -9.854 47.152 1.00107.94 N ANISOU 1801 ND1 HIS A 250 11231 18239 11542 494 -594 -680 N ATOM 1802 CD2 HIS A 250 67.791 -8.579 48.309 1.00110.89 C ANISOU 1802 CD2 HIS A 250 11441 18837 11854 406 -784 -802 C ATOM 1803 CE1 HIS A 250 66.982 -8.989 46.308 1.00101.71 C ANISOU 1803 CE1 HIS A 250 10420 17452 10772 430 -541 -773 C ATOM 1804 NE2 HIS A 250 67.798 -8.201 46.986 1.00107.83 N ANISOU 1804 NE2 HIS A 250 11093 18362 11515 374 -649 -849 N ATOM 1805 N ILE A 251 66.297 -13.009 51.530 1.00100.58 N ANISOU 1805 N ILE A 251 10267 17514 10434 766 -1130 -366 N ATOM 1806 CA ILE A 251 65.999 -13.685 52.801 1.00103.27 C ANISOU 1806 CA ILE A 251 10641 17895 10700 827 -1263 -280 C ATOM 1807 C ILE A 251 67.303 -14.134 53.453 1.00107.27 C ANISOU 1807 C ILE A 251 11058 18543 11155 899 -1499 -266 C ATOM 1808 O ILE A 251 67.462 -14.059 54.673 1.00110.35 O ANISOU 1808 O ILE A 251 11446 19033 11448 906 -1655 -250 O ATOM 1809 CB ILE A 251 65.081 -14.939 52.629 1.00 84.02 C ANISOU 1809 CB ILE A 251 8300 15329 8293 911 -1196 -163 C ATOM 1810 CG1 ILE A 251 63.596 -14.585 52.764 1.00 90.33 C ANISOU 1810 CG1 ILE A 251 9190 16032 9100 851 -1039 -150 C ATOM 1811 CG2 ILE A 251 65.404 -15.990 53.686 1.00 82.13 C ANISOU 1811 CG2 ILE A 251 8073 15149 7983 1019 -1392 -64 C ATOM 1812 CD1 ILE A 251 62.917 -14.101 51.487 1.00 93.35 C ANISOU 1812 CD1 ILE A 251 9602 16298 9568 788 -813 -196 C ATOM 1813 N ILE A 252 68.225 -14.605 52.614 1.00107.66 N ANISOU 1813 N ILE A 252 11037 18602 11267 952 -1527 -274 N ATOM 1814 CA ILE A 252 69.526 -15.113 53.045 1.00111.31 C ANISOU 1814 CA ILE A 252 11393 19196 11704 1034 -1744 -259 C ATOM 1815 C ILE A 252 70.476 -13.979 53.455 1.00113.55 C ANISOU 1815 C ILE A 252 11560 19640 11945 950 -1852 -373 C ATOM 1816 O ILE A 252 71.181 -14.089 54.460 1.00109.99 O ANISOU 1816 O ILE A 252 11047 19328 11415 986 -2059 -363 O ATOM 1817 CB ILE A 252 70.160 -15.997 51.939 1.00 92.11 C ANISOU 1817 CB ILE A 252 8917 16714 9368 1117 -1729 -231 C ATOM 1818 CG1 ILE A 252 70.099 -17.479 52.324 1.00 89.24 C ANISOU 1818 CG1 ILE A 252 8595 16317 8994 1263 -1829 -95 C ATOM 1819 CG2 ILE A 252 71.583 -15.571 51.649 1.00 94.96 C ANISOU 1819 CG2 ILE A 252 9122 17204 9754 1107 -1842 -315 C ATOM 1820 CD1 ILE A 252 70.637 -18.416 51.250 1.00 83.44 C ANISOU 1820 CD1 ILE A 252 7826 15521 8356 1348 -1810 -60 C ATOM 1821 N ASN A 253 70.480 -12.892 52.683 1.00115.73 N ANISOU 1821 N ASN A 253 11811 19895 12267 837 -1715 -482 N ATOM 1822 CA ASN A 253 71.252 -11.699 53.027 1.00118.95 C ANISOU 1822 CA ASN A 253 12117 20441 12637 736 -1790 -602 C ATOM 1823 C ASN A 253 70.776 -11.043 54.308 1.00123.50 C ANISOU 1823 C ASN A 253 12733 21086 13104 671 -1858 -617 C ATOM 1824 O ASN A 253 71.574 -10.487 55.061 1.00127.36 O ANISOU 1824 O ASN A 253 13135 21730 13525 626 -2016 -681 O ATOM 1825 CB ASN A 253 71.204 -10.683 51.895 1.00118.44 C ANISOU 1825 CB ASN A 253 12044 20317 12641 629 -1610 -707 C ATOM 1826 CG ASN A 253 72.161 -11.022 50.789 1.00123.37 C ANISOU 1826 CG ASN A 253 12584 20940 13351 666 -1610 -735 C ATOM 1827 OD1 ASN A 253 72.527 -12.183 50.613 1.00124.09 O ANISOU 1827 OD1 ASN A 253 12655 21019 13475 782 -1684 -655 O ATOM 1828 ND2 ASN A 253 72.589 -10.011 50.041 1.00125.24 N ANISOU 1828 ND2 ASN A 253 12770 21190 13624 567 -1531 -849 N ATOM 1829 N CYS A 254 69.468 -11.093 54.538 1.00124.46 N ANISOU 1829 N CYS A 254 12985 21094 13210 659 -1738 -563 N ATOM 1830 CA CYS A 254 68.893 -10.643 55.800 1.00125.32 C ANISOU 1830 CA CYS A 254 13153 21250 13212 611 -1805 -559 C ATOM 1831 C CYS A 254 69.514 -11.418 56.950 1.00123.76 C ANISOU 1831 C CYS A 254 12938 21173 12913 700 -2054 -491 C ATOM 1832 O CYS A 254 70.059 -10.831 57.882 1.00126.83 O ANISOU 1832 O CYS A 254 13284 21702 13203 649 -2210 -546 O ATOM 1833 CB CYS A 254 67.382 -10.858 55.807 1.00124.61 C ANISOU 1833 CB CYS A 254 13200 21010 13135 611 -1645 -490 C ATOM 1834 SG CYS A 254 66.527 -10.109 54.433 1.00125.86 S ANISOU 1834 SG CYS A 254 13393 21018 13410 531 -1357 -545 S ATOM 1835 N PHE A 255 69.432 -12.743 56.874 1.00121.79 N ANISOU 1835 N PHE A 255 12727 20868 12681 833 -2093 -373 N ATOM 1836 CA PHE A 255 70.003 -13.593 57.913 1.00125.68 C ANISOU 1836 CA PHE A 255 13216 21463 13075 938 -2331 -291 C ATOM 1837 C PHE A 255 71.508 -13.395 58.088 1.00126.29 C ANISOU 1837 C PHE A 255 13135 21718 13131 950 -2527 -353 C ATOM 1838 O PHE A 255 72.019 -13.532 59.193 1.00128.69 O ANISOU 1838 O PHE A 255 13424 22154 13318 983 -2743 -331 O ATOM 1839 CB PHE A 255 69.642 -15.068 57.696 1.00124.39 C ANISOU 1839 CB PHE A 255 13124 21194 12946 1082 -2325 -151 C ATOM 1840 CG PHE A 255 68.377 -15.479 58.398 1.00126.36 C ANISOU 1840 CG PHE A 255 13534 21349 13129 1098 -2282 -61 C ATOM 1841 CD1 PHE A 255 68.378 -15.729 59.768 1.00128.77 C ANISOU 1841 CD1 PHE A 255 13908 21736 13284 1135 -2471 -2 C ATOM 1842 CD2 PHE A 255 67.180 -15.591 57.702 1.00123.39 C ANISOU 1842 CD2 PHE A 255 13243 20807 12834 1071 -2057 -38 C ATOM 1843 CE1 PHE A 255 67.211 -16.097 60.432 1.00126.95 C ANISOU 1843 CE1 PHE A 255 13835 21417 12985 1144 -2433 79 C ATOM 1844 CE2 PHE A 255 66.007 -15.964 58.359 1.00121.89 C ANISOU 1844 CE2 PHE A 255 13190 20534 12587 1081 -2020 40 C ATOM 1845 CZ PHE A 255 66.025 -16.216 59.727 1.00123.02 C ANISOU 1845 CZ PHE A 255 13406 20754 12580 1117 -2206 98 C ATOM 1846 N THR A 256 72.205 -13.075 57.000 1.00125.38 N ANISOU 1846 N THR A 256 12905 21609 13125 922 -2455 -430 N ATOM 1847 CA THR A 256 73.640 -12.770 57.049 1.00126.83 C ANISOU 1847 CA THR A 256 12918 21965 13308 916 -2622 -507 C ATOM 1848 C THR A 256 73.969 -11.336 57.483 1.00129.98 C ANISOU 1848 C THR A 256 13254 22482 13649 760 -2652 -648 C ATOM 1849 O THR A 256 74.942 -11.113 58.216 1.00132.08 O ANISOU 1849 O THR A 256 13414 22926 13843 752 -2861 -693 O ATOM 1850 CB THR A 256 74.338 -13.028 55.698 1.00118.35 C ANISOU 1850 CB THR A 256 11740 20854 12373 947 -2544 -537 C ATOM 1851 OG1 THR A 256 74.272 -14.423 55.373 1.00115.58 O ANISOU 1851 OG1 THR A 256 11425 20422 12070 1099 -2559 -411 O ATOM 1852 CG2 THR A 256 75.797 -12.581 55.766 1.00113.47 C ANISOU 1852 CG2 THR A 256 10931 20424 11760 923 -2710 -632 C ATOM 1853 N PHE A 257 73.186 -10.369 57.000 1.00125.58 N ANISOU 1853 N PHE A 257 12759 21830 13126 638 -2447 -719 N ATOM 1854 CA PHE A 257 73.459 -8.959 57.278 1.00124.89 C ANISOU 1854 CA PHE A 257 12618 21837 12998 482 -2449 -859 C ATOM 1855 C PHE A 257 73.031 -8.475 58.652 1.00129.38 C ANISOU 1855 C PHE A 257 13261 22478 13422 422 -2556 -868 C ATOM 1856 O PHE A 257 73.770 -7.748 59.309 1.00133.35 O ANISOU 1856 O PHE A 257 13683 23137 13848 340 -2699 -961 O ATOM 1857 CB PHE A 257 72.838 -8.034 56.235 1.00119.43 C ANISOU 1857 CB PHE A 257 11963 21021 12393 375 -2196 -935 C ATOM 1858 CG PHE A 257 72.913 -6.575 56.613 1.00116.86 C ANISOU 1858 CG PHE A 257 11613 20772 12019 211 -2182 -1069 C ATOM 1859 CD1 PHE A 257 71.774 -5.870 56.960 1.00111.92 C ANISOU 1859 CD1 PHE A 257 11105 20064 11354 129 -2060 -1080 C ATOM 1860 CD2 PHE A 257 74.133 -5.916 56.654 1.00114.25 C ANISOU 1860 CD2 PHE A 257 11133 20598 11679 136 -2297 -1187 C ATOM 1861 CE1 PHE A 257 71.857 -4.529 57.318 1.00107.04 C ANISOU 1861 CE1 PHE A 257 10466 19513 10689 -24 -2050 -1204 C ATOM 1862 CE2 PHE A 257 74.215 -4.577 57.010 1.00106.15 C ANISOU 1862 CE2 PHE A 257 10086 19642 10605 -24 -2285 -1316 C ATOM 1863 CZ PHE A 257 73.084 -3.887 57.340 1.00101.42 C ANISOU 1863 CZ PHE A 257 9614 18954 9966 -103 -2161 -1323 C ATOM 1864 N PHE A 258 71.832 -8.844 59.081 1.00130.96 N ANISOU 1864 N PHE A 258 13615 22565 13580 452 -2486 -778 N ATOM 1865 CA PHE A 258 71.319 -8.296 60.329 1.00139.05 C ANISOU 1865 CA PHE A 258 14729 23639 14464 382 -2566 -793 C ATOM 1866 C PHE A 258 72.090 -8.864 61.502 1.00144.18 C ANISOU 1866 C PHE A 258 15356 24447 14977 451 -2849 -751 C ATOM 1867 O PHE A 258 71.923 -8.446 62.648 1.00139.84 O ANISOU 1867 O PHE A 258 14875 23975 14284 395 -2968 -771 O ATOM 1868 CB PHE A 258 69.813 -8.505 60.447 1.00142.27 C ANISOU 1868 CB PHE A 258 15303 23884 14869 391 -2412 -713 C ATOM 1869 CG PHE A 258 69.023 -7.604 59.542 1.00145.54 C ANISOU 1869 CG PHE A 258 15739 24173 15385 291 -2158 -778 C ATOM 1870 CD1 PHE A 258 68.551 -8.063 58.321 1.00145.66 C ANISOU 1870 CD1 PHE A 258 15765 24043 15536 342 -1967 -734 C ATOM 1871 CD2 PHE A 258 68.789 -6.282 59.897 1.00146.28 C ANISOU 1871 CD2 PHE A 258 15844 24301 15436 144 -2117 -888 C ATOM 1872 CE1 PHE A 258 67.841 -7.226 57.480 1.00143.48 C ANISOU 1872 CE1 PHE A 258 15513 23659 15346 257 -1744 -790 C ATOM 1873 CE2 PHE A 258 68.082 -5.440 59.063 1.00143.80 C ANISOU 1873 CE2 PHE A 258 15548 23874 15214 60 -1891 -942 C ATOM 1874 CZ PHE A 258 67.606 -5.912 57.852 1.00143.10 C ANISOU 1874 CZ PHE A 258 15470 23643 15257 120 -1707 -891 C ATOM 1875 N CYS A 259 72.966 -9.807 61.181 1.00155.08 N ANISOU 1875 N CYS A 259 16643 25878 16403 573 -2959 -694 N ATOM 1876 CA CYS A 259 73.858 -10.401 62.161 1.00166.28 C ANISOU 1876 CA CYS A 259 18014 27458 17706 657 -3241 -651 C ATOM 1877 C CYS A 259 75.324 -10.319 61.726 1.00166.21 C ANISOU 1877 C CYS A 259 17795 27599 17758 668 -3363 -724 C ATOM 1878 O CYS A 259 75.957 -11.357 61.517 1.00159.21 O ANISOU 1878 O CYS A 259 16841 26741 16912 809 -3467 -642 O ATOM 1879 CB CYS A 259 73.485 -11.873 62.385 1.00171.47 C ANISOU 1879 CB CYS A 259 18768 28039 18345 831 -3296 -478 C ATOM 1880 SG CYS A 259 71.786 -12.335 61.910 1.00182.16 S ANISOU 1880 SG CYS A 259 20312 29141 19761 852 -3033 -382 S ATOM 1881 N PRO A 260 75.884 -9.098 61.594 1.00173.59 N ANISOU 1881 N PRO A 260 18623 28632 18701 520 -3354 -880 N ATOM 1882 CA PRO A 260 77.333 -9.176 61.396 1.00182.83 C ANISOU 1882 CA PRO A 260 19589 29969 19908 545 -3518 -937 C ATOM 1883 C PRO A 260 77.910 -9.466 62.774 1.00197.55 C ANISOU 1883 C PRO A 260 21438 32015 21608 590 -3814 -907 C ATOM 1884 O PRO A 260 78.914 -8.906 63.227 1.00201.30 O ANISOU 1884 O PRO A 260 21775 32682 22029 524 -3987 -1008 O ATOM 1885 CB PRO A 260 77.692 -7.766 60.923 1.00177.24 C ANISOU 1885 CB PRO A 260 18786 29312 19246 362 -3420 -1113 C ATOM 1886 CG PRO A 260 76.662 -6.887 61.555 1.00173.38 C ANISOU 1886 CG PRO A 260 18448 28765 18662 239 -3332 -1152 C ATOM 1887 CD PRO A 260 75.400 -7.709 61.693 1.00171.31 C ANISOU 1887 CD PRO A 260 18375 28332 18385 338 -3235 -1005 C ATOM 1888 N ASP A 261 77.211 -10.394 63.422 1.00203.68 N ANISOU 1888 N ASP A 261 22368 32721 22300 706 -3867 -762 N ATOM 1889 CA ASP A 261 77.553 -11.012 64.689 1.00210.69 C ANISOU 1889 CA ASP A 261 23294 33737 23022 796 -4139 -680 C ATOM 1890 C ASP A 261 77.322 -12.516 64.521 1.00212.29 C ANISOU 1890 C ASP A 261 23561 33840 23258 996 -4158 -501 C ATOM 1891 O ASP A 261 78.238 -13.323 64.681 1.00216.45 O ANISOU 1891 O ASP A 261 23987 34474 23780 1128 -4351 -437 O ATOM 1892 CB ASP A 261 76.696 -10.443 65.819 1.00210.44 C ANISOU 1892 CB ASP A 261 23443 33699 22815 705 -4166 -691 C ATOM 1893 CG ASP A 261 76.943 -11.137 67.142 1.00213.81 C ANISOU 1893 CG ASP A 261 23948 34241 23050 803 -4442 -593 C ATOM 1894 OD1 ASP A 261 76.227 -10.832 68.119 1.00214.94 O ANISOU 1894 OD1 ASP A 261 24263 34373 23032 747 -4478 -583 O ATOM 1895 OD2 ASP A 261 77.846 -11.995 67.203 1.00215.23 O ANISOU 1895 OD2 ASP A 261 24022 34520 23234 941 -4624 -522 O ATOM 1896 N CYS A 262 76.067 -12.871 64.233 1.00206.58 N ANISOU 1896 N CYS A 262 23011 32916 22566 1015 -3960 -421 N ATOM 1897 CA CYS A 262 75.639 -14.258 64.010 1.00201.15 C ANISOU 1897 CA CYS A 262 22411 32101 21915 1185 -3936 -255 C ATOM 1898 C CYS A 262 76.187 -14.897 62.727 1.00196.58 C ANISOU 1898 C CYS A 262 21703 31467 21522 1274 -3849 -236 C ATOM 1899 O CYS A 262 76.643 -14.205 61.814 1.00194.48 O ANISOU 1899 O CYS A 262 21306 31215 21374 1189 -3742 -352 O ATOM 1900 CB CYS A 262 74.108 -14.386 64.061 1.00195.60 C ANISOU 1900 CB CYS A 262 21921 31203 21195 1162 -3742 -189 C ATOM 1901 SG CYS A 262 73.198 -13.559 62.730 1.00180.27 S ANISOU 1901 SG CYS A 262 19987 29083 19425 1031 -3388 -283 S ATOM 1902 N SER A 263 76.112 -16.226 62.672 1.00194.04 N ANISOU 1902 N SER A 263 21432 31076 21216 1443 -3893 -87 N ATOM 1903 CA SER A 263 76.790 -17.034 61.656 1.00191.75 C ANISOU 1903 CA SER A 263 21022 30759 21076 1558 -3872 -49 C ATOM 1904 C SER A 263 76.322 -16.798 60.219 1.00186.50 C ANISOU 1904 C SER A 263 20347 29931 20583 1495 -3589 -105 C ATOM 1905 O SER A 263 75.243 -16.253 59.977 1.00185.34 O ANISOU 1905 O SER A 263 20318 29656 20446 1392 -3388 -137 O ATOM 1906 CB SER A 263 76.675 -18.519 62.002 1.00192.33 C ANISOU 1906 CB SER A 263 21183 30778 21116 1752 -3975 131 C ATOM 1907 OG SER A 263 77.267 -18.789 63.260 1.00197.07 O ANISOU 1907 OG SER A 263 21780 31541 21555 1827 -4257 189 O ATOM 1908 N HIS A 264 77.158 -17.222 59.274 1.00181.81 N ANISOU 1908 N HIS A 264 19613 29347 20120 1562 -3584 -114 N ATOM 1909 CA HIS A 264 77.014 -16.874 57.861 1.00172.11 C ANISOU 1909 CA HIS A 264 18346 28002 19046 1493 -3350 -190 C ATOM 1910 C HIS A 264 76.458 -18.031 57.024 1.00169.43 C ANISOU 1910 C HIS A 264 18094 27480 18803 1604 -3216 -79 C ATOM 1911 O HIS A 264 76.652 -19.202 57.359 1.00170.22 O ANISOU 1911 O HIS A 264 18213 27578 18886 1760 -3339 47 O ATOM 1912 CB HIS A 264 78.367 -16.422 57.303 1.00165.67 C ANISOU 1912 CB HIS A 264 17310 27325 18311 1467 -3427 -298 C ATOM 1913 CG HIS A 264 78.274 -15.648 56.025 1.00155.53 C ANISOU 1913 CG HIS A 264 15992 25954 17149 1348 -3202 -411 C ATOM 1914 ND1 HIS A 264 78.002 -16.244 54.810 1.00148.99 N ANISOU 1914 ND1 HIS A 264 15198 24968 16445 1395 -3033 -375 N ATOM 1915 CD2 HIS A 264 78.435 -14.329 55.768 1.00154.72 C ANISOU 1915 CD2 HIS A 264 15832 25900 17055 1185 -3124 -558 C ATOM 1916 CE1 HIS A 264 77.988 -15.323 53.865 1.00147.74 C ANISOU 1916 CE1 HIS A 264 15011 24764 16359 1268 -2864 -491 C ATOM 1917 NE2 HIS A 264 78.248 -14.152 54.418 1.00151.68 N ANISOU 1917 NE2 HIS A 264 15454 25385 16794 1141 -2912 -602 N ATOM 1918 N ALA A 265 75.742 -17.682 55.954 1.00163.39 N ANISOU 1918 N ALA A 265 17388 26561 18132 1520 -2966 -126 N ATOM 1919 CA ALA A 265 75.157 -18.655 55.029 1.00155.16 C ANISOU 1919 CA ALA A 265 16431 25339 17185 1597 -2815 -43 C ATOM 1920 C ALA A 265 76.204 -19.567 54.380 1.00152.76 C ANISOU 1920 C ALA A 265 16003 25063 16977 1726 -2902 -3 C ATOM 1921 O ALA A 265 77.195 -19.088 53.832 1.00147.31 O ANISOU 1921 O ALA A 265 15156 24462 16354 1692 -2934 -96 O ATOM 1922 CB ALA A 265 74.344 -17.935 53.960 1.00149.20 C ANISOU 1922 CB ALA A 265 15741 24442 16505 1469 -2547 -121 C ATOM 1923 N PRO A 266 75.960 -20.889 54.423 1.00156.60 N ANISOU 1923 N PRO A 266 16562 25465 17475 1873 -2934 135 N ATOM 1924 CA PRO A 266 76.856 -21.973 53.988 1.00158.18 C ANISOU 1924 CA PRO A 266 16665 25682 17756 2028 -3037 205 C ATOM 1925 C PRO A 266 77.129 -22.013 52.479 1.00155.37 C ANISOU 1925 C PRO A 266 16248 25234 17551 2002 -2881 147 C ATOM 1926 O PRO A 266 76.740 -21.099 51.755 1.00154.59 O ANISOU 1926 O PRO A 266 16171 25077 17488 1860 -2705 43 O ATOM 1927 CB PRO A 266 76.108 -23.242 54.422 1.00159.16 C ANISOU 1927 CB PRO A 266 16941 25693 17839 2159 -3051 366 C ATOM 1928 CG PRO A 266 75.142 -22.786 55.469 1.00159.20 C ANISOU 1928 CG PRO A 266 17086 25693 17709 2089 -3046 382 C ATOM 1929 CD PRO A 266 74.728 -21.418 55.032 1.00156.53 C ANISOU 1929 CD PRO A 266 16744 25343 17389 1899 -2881 238 C ATOM 1930 N LEU A 267 77.808 -23.068 52.027 1.00155.78 N ANISOU 1930 N LEU A 267 16228 25276 17685 2145 -2952 218 N ATOM 1931 CA LEU A 267 78.241 -23.207 50.632 1.00154.04 C ANISOU 1931 CA LEU A 267 15936 24985 17608 2138 -2839 170 C ATOM 1932 C LEU A 267 77.112 -23.610 49.678 1.00147.56 C ANISOU 1932 C LEU A 267 15281 23945 16838 2103 -2606 199 C ATOM 1933 O LEU A 267 76.750 -22.852 48.776 1.00141.17 O ANISOU 1933 O LEU A 267 14504 23062 16071 1971 -2430 104 O ATOM 1934 CB LEU A 267 79.397 -24.215 50.533 1.00157.34 C ANISOU 1934 CB LEU A 267 16208 25475 18101 2312 -3008 238 C ATOM 1935 CG LEU A 267 80.367 -24.159 49.342 1.00156.88 C ANISOU 1935 CG LEU A 267 15990 25432 18187 2310 -2977 164 C ATOM 1936 CD1 LEU A 267 81.584 -25.062 49.594 1.00161.61 C ANISOU 1936 CD1 LEU A 267 16417 26147 18841 2494 -3191 235 C ATOM 1937 CD2 LEU A 267 79.690 -24.507 48.016 1.00148.06 C ANISOU 1937 CD2 LEU A 267 14983 24110 17161 2273 -2753 164 C ATOM 1938 N TRP A 268 76.564 -24.807 49.880 1.00146.83 N ANISOU 1938 N TRP A 268 15298 23752 16738 2222 -2612 332 N ATOM 1939 CA TRP A 268 75.547 -25.350 48.977 1.00140.29 C ANISOU 1939 CA TRP A 268 14617 22724 15963 2201 -2410 369 C ATOM 1940 C TRP A 268 74.219 -24.604 49.090 1.00135.00 C ANISOU 1940 C TRP A 268 14098 21967 15227 2058 -2239 330 C ATOM 1941 O TRP A 268 73.265 -24.902 48.377 1.00134.82 O ANISOU 1941 O TRP A 268 14199 21788 15239 2019 -2063 348 O ATOM 1942 CB TRP A 268 75.363 -26.869 49.162 1.00141.82 C ANISOU 1942 CB TRP A 268 14879 22836 16171 2370 -2466 521 C ATOM 1943 CG TRP A 268 74.683 -27.306 50.441 1.00145.86 C ANISOU 1943 CG TRP A 268 15507 23350 16562 2431 -2548 627 C ATOM 1944 CD1 TRP A 268 75.281 -27.570 51.649 1.00148.30 C ANISOU 1944 CD1 TRP A 268 15769 23793 16785 2540 -2771 696 C ATOM 1945 CD2 TRP A 268 73.280 -27.560 50.628 1.00142.25 C ANISOU 1945 CD2 TRP A 268 15238 22756 16056 2388 -2412 680 C ATOM 1946 NE1 TRP A 268 74.335 -27.955 52.571 1.00149.05 N ANISOU 1946 NE1 TRP A 268 16022 23836 16773 2565 -2782 790 N ATOM 1947 CE2 TRP A 268 73.100 -27.957 51.969 1.00147.17 C ANISOU 1947 CE2 TRP A 268 15924 23433 16562 2472 -2561 780 C ATOM 1948 CE3 TRP A 268 72.159 -27.478 49.794 1.00131.09 C ANISOU 1948 CE3 TRP A 268 13942 21184 14683 2285 -2185 653 C ATOM 1949 CZ2 TRP A 268 71.841 -28.274 52.491 1.00141.91 C ANISOU 1949 CZ2 TRP A 268 15432 22663 15824 2454 -2483 850 C ATOM 1950 CZ3 TRP A 268 70.916 -27.794 50.316 1.00126.88 C ANISOU 1950 CZ3 TRP A 268 13566 20556 14086 2269 -2110 720 C ATOM 1951 CH2 TRP A 268 70.767 -28.188 51.648 1.00129.58 C ANISOU 1951 CH2 TRP A 268 13965 20951 14318 2352 -2256 816 C ATOM 1952 N LEU A 269 74.155 -23.652 50.013 1.00131.52 N ANISOU 1952 N LEU A 269 13644 21634 14694 1983 -2297 279 N ATOM 1953 CA LEU A 269 73.018 -22.748 50.086 1.00126.44 C ANISOU 1953 CA LEU A 269 13115 20928 14000 1839 -2136 224 C ATOM 1954 C LEU A 269 73.190 -21.598 49.098 1.00118.68 C ANISOU 1954 C LEU A 269 12084 19938 13072 1699 -2001 85 C ATOM 1955 O LEU A 269 72.368 -21.415 48.203 1.00112.62 O ANISOU 1955 O LEU A 269 11413 19035 12343 1623 -1805 59 O ATOM 1956 CB LEU A 269 72.814 -22.219 51.507 1.00132.98 C ANISOU 1956 CB LEU A 269 13961 21863 14702 1816 -2251 230 C ATOM 1957 CG LEU A 269 71.891 -23.036 52.418 1.00134.43 C ANISOU 1957 CG LEU A 269 14285 21984 14806 1888 -2281 356 C ATOM 1958 CD1 LEU A 269 70.689 -23.558 51.621 1.00130.47 C ANISOU 1958 CD1 LEU A 269 13920 21290 14362 1865 -2068 395 C ATOM 1959 CD2 LEU A 269 72.636 -24.179 53.117 1.00133.75 C ANISOU 1959 CD2 LEU A 269 14165 21967 14688 2065 -2498 475 C ATOM 1960 N MET A 270 74.255 -20.822 49.279 1.00118.44 N ANISOU 1960 N MET A 270 11906 20058 13037 1666 -2112 -2 N ATOM 1961 CA MET A 270 74.490 -19.606 48.498 1.00115.57 C ANISOU 1961 CA MET A 270 11495 19707 12709 1528 -2003 -138 C ATOM 1962 C MET A 270 74.456 -19.789 46.974 1.00116.58 C ANISOU 1962 C MET A 270 11649 19706 12941 1505 -1848 -167 C ATOM 1963 O MET A 270 73.616 -19.202 46.292 1.00114.44 O ANISOU 1963 O MET A 270 11484 19325 12673 1402 -1662 -213 O ATOM 1964 CB MET A 270 75.799 -18.942 48.917 1.00115.41 C ANISOU 1964 CB MET A 270 11290 19879 12680 1513 -2171 -221 C ATOM 1965 CG MET A 270 75.780 -17.430 48.786 1.00113.87 C ANISOU 1965 CG MET A 270 11073 19731 12462 1350 -2089 -358 C ATOM 1966 SD MET A 270 74.785 -16.641 50.065 1.00148.76 S ANISOU 1966 SD MET A 270 15594 24178 16751 1268 -2081 -362 S ATOM 1967 CE MET A 270 74.906 -14.925 49.568 1.00 70.24 C ANISOU 1967 CE MET A 270 5609 14268 6810 1085 -1964 -528 C ATOM 1968 N TYR A 271 75.380 -20.574 46.433 1.00120.87 N ANISOU 1968 N TYR A 271 12094 20266 13566 1601 -1928 -141 N ATOM 1969 CA TYR A 271 75.397 -20.809 44.991 1.00120.81 C ANISOU 1969 CA TYR A 271 12112 20137 13654 1583 -1797 -164 C ATOM 1970 C TYR A 271 74.025 -21.249 44.477 1.00116.10 C ANISOU 1970 C TYR A 271 11707 19354 13051 1560 -1617 -108 C ATOM 1971 O TYR A 271 73.654 -20.941 43.343 1.00109.22 O ANISOU 1971 O TYR A 271 10904 18374 12219 1482 -1464 -157 O ATOM 1972 CB TYR A 271 76.468 -21.833 44.610 1.00125.64 C ANISOU 1972 CB TYR A 271 12599 20781 14359 1716 -1917 -117 C ATOM 1973 CG TYR A 271 77.885 -21.352 44.837 1.00135.40 C ANISOU 1973 CG TYR A 271 13624 22197 15625 1728 -2076 -189 C ATOM 1974 CD1 TYR A 271 78.530 -20.551 43.900 1.00135.14 C ANISOU 1974 CD1 TYR A 271 13503 22186 15657 1637 -2019 -306 C ATOM 1975 CD2 TYR A 271 78.582 -21.707 45.990 1.00145.21 C ANISOU 1975 CD2 TYR A 271 14752 23592 16830 1830 -2287 -140 C ATOM 1976 CE1 TYR A 271 79.826 -20.115 44.106 1.00142.34 C ANISOU 1976 CE1 TYR A 271 14209 23270 16604 1641 -2162 -377 C ATOM 1977 CE2 TYR A 271 79.879 -21.280 46.205 1.00150.19 C ANISOU 1977 CE2 TYR A 271 15176 24400 17490 1839 -2439 -209 C ATOM 1978 CZ TYR A 271 80.498 -20.484 45.261 1.00151.17 C ANISOU 1978 CZ TYR A 271 15205 24546 17687 1742 -2373 -330 C ATOM 1979 OH TYR A 271 81.793 -20.063 45.479 1.00157.28 O ANISOU 1979 OH TYR A 271 15761 25503 18497 1745 -2523 -403 O ATOM 1980 N LEU A 272 73.287 -21.975 45.319 1.00117.37 N ANISOU 1980 N LEU A 272 11953 19483 13160 1626 -1644 -5 N ATOM 1981 CA LEU A 272 71.928 -22.424 45.007 1.00113.18 C ANISOU 1981 CA LEU A 272 11594 18791 12618 1603 -1486 52 C ATOM 1982 C LEU A 272 70.993 -21.221 44.832 1.00114.06 C ANISOU 1982 C LEU A 272 11796 18859 12684 1454 -1323 -28 C ATOM 1983 O LEU A 272 70.095 -21.238 43.988 1.00111.57 O ANISOU 1983 O LEU A 272 11596 18409 12387 1397 -1156 -31 O ATOM 1984 CB LEU A 272 71.417 -23.373 46.106 1.00109.73 C ANISOU 1984 CB LEU A 272 11213 18350 12128 1705 -1569 174 C ATOM 1985 CG LEU A 272 70.068 -24.103 46.030 1.00103.90 C ANISOU 1985 CG LEU A 272 10634 17463 11380 1710 -1443 255 C ATOM 1986 CD1 LEU A 272 69.958 -25.148 47.142 1.00102.07 C ANISOU 1986 CD1 LEU A 272 10427 17251 11102 1840 -1576 380 C ATOM 1987 CD2 LEU A 272 68.890 -23.137 46.103 1.00102.29 C ANISOU 1987 CD2 LEU A 272 10528 17211 11127 1575 -1286 202 C ATOM 1988 N ALA A 273 71.215 -20.175 45.624 1.00114.73 N ANISOU 1988 N ALA A 273 11824 19059 12708 1393 -1377 -92 N ATOM 1989 CA ALA A 273 70.432 -18.949 45.505 1.00111.48 C ANISOU 1989 CA ALA A 273 11482 18618 12258 1258 -1233 -171 C ATOM 1990 C ALA A 273 70.880 -18.091 44.323 1.00116.67 C ANISOU 1990 C ALA A 273 12114 19256 12960 1171 -1144 -279 C ATOM 1991 O ALA A 273 70.050 -17.439 43.691 1.00118.47 O ANISOU 1991 O ALA A 273 12444 19391 13180 1081 -979 -320 O ATOM 1992 CB ALA A 273 70.471 -18.145 46.801 1.00110.26 C ANISOU 1992 CB ALA A 273 11282 18590 12022 1222 -1323 -200 C ATOM 1993 N ILE A 274 72.182 -18.082 44.024 1.00120.66 N ANISOU 1993 N ILE A 274 12483 19850 13513 1200 -1255 -323 N ATOM 1994 CA ILE A 274 72.682 -17.344 42.858 1.00119.09 C ANISOU 1994 CA ILE A 274 12256 19631 13362 1123 -1180 -423 C ATOM 1995 C ILE A 274 72.163 -17.959 41.561 1.00123.27 C ANISOU 1995 C ILE A 274 12897 19995 13944 1128 -1050 -393 C ATOM 1996 O ILE A 274 71.731 -17.250 40.654 1.00123.20 O ANISOU 1996 O ILE A 274 12970 19905 13934 1039 -913 -454 O ATOM 1997 CB ILE A 274 74.214 -17.305 42.784 1.00113.31 C ANISOU 1997 CB ILE A 274 11338 19031 12683 1157 -1330 -475 C ATOM 1998 CG1 ILE A 274 74.811 -16.885 44.125 1.00112.93 C ANISOU 1998 CG1 ILE A 274 11169 19160 12580 1166 -1492 -494 C ATOM 1999 CG2 ILE A 274 74.654 -16.367 41.658 1.00107.70 C ANISOU 1999 CG2 ILE A 274 10605 18303 12015 1059 -1244 -589 C ATOM 2000 CD1 ILE A 274 76.328 -16.834 44.126 1.00114.24 C ANISOU 2000 CD1 ILE A 274 11133 19475 12799 1199 -1651 -548 C ATOM 2001 N VAL A 275 72.235 -19.285 41.479 1.00126.83 N ANISOU 2001 N VAL A 275 13350 20402 14439 1237 -1102 -298 N ATOM 2002 CA VAL A 275 71.597 -20.043 40.407 1.00119.45 C ANISOU 2002 CA VAL A 275 12531 19308 13545 1247 -988 -253 C ATOM 2003 C VAL A 275 70.116 -19.698 40.383 1.00110.26 C ANISOU 2003 C VAL A 275 11533 18039 12321 1172 -829 -240 C ATOM 2004 O VAL A 275 69.611 -19.140 39.413 1.00104.91 O ANISOU 2004 O VAL A 275 10949 17272 11641 1089 -698 -290 O ATOM 2005 CB VAL A 275 71.776 -21.569 40.607 1.00118.08 C ANISOU 2005 CB VAL A 275 12338 19110 13418 1383 -1076 -139 C ATOM 2006 CG1 VAL A 275 70.833 -22.349 39.703 1.00111.88 C ANISOU 2006 CG1 VAL A 275 11695 18157 12658 1381 -948 -85 C ATOM 2007 CG2 VAL A 275 73.225 -21.973 40.361 1.00120.09 C ANISOU 2007 CG2 VAL A 275 12426 19449 13752 1464 -1216 -150 C ATOM 2008 N LEU A 276 69.435 -20.014 41.476 1.00110.08 N ANISOU 2008 N LEU A 276 11543 18033 12249 1204 -849 -173 N ATOM 2009 CA LEU A 276 68.005 -19.771 41.597 1.00108.66 C ANISOU 2009 CA LEU A 276 11500 17765 12021 1143 -707 -153 C ATOM 2010 C LEU A 276 67.605 -18.375 41.115 1.00105.53 C ANISOU 2010 C LEU A 276 11154 17351 11592 1021 -584 -251 C ATOM 2011 O LEU A 276 66.560 -18.213 40.492 1.00106.46 O ANISOU 2011 O LEU A 276 11394 17358 11696 966 -439 -250 O ATOM 2012 CB LEU A 276 67.574 -19.972 43.048 1.00108.90 C ANISOU 2012 CB LEU A 276 11520 17859 12000 1183 -775 -93 C ATOM 2013 CG LEU A 276 66.351 -19.199 43.525 1.00105.58 C ANISOU 2013 CG LEU A 276 11182 17409 11524 1101 -657 -107 C ATOM 2014 CD1 LEU A 276 65.079 -19.976 43.228 1.00106.44 C ANISOU 2014 CD1 LEU A 276 11412 17387 11642 1106 -537 -34 C ATOM 2015 CD2 LEU A 276 66.478 -18.914 45.006 1.00103.58 C ANISOU 2015 CD2 LEU A 276 10866 17276 11215 1121 -774 -93 C ATOM 2016 N SER A 277 68.426 -17.370 41.401 1.00103.13 N ANISOU 2016 N SER A 277 10753 17158 11275 981 -645 -335 N ATOM 2017 CA SER A 277 68.138 -16.016 40.935 1.00104.41 C ANISOU 2017 CA SER A 277 10958 17305 11408 872 -536 -429 C ATOM 2018 C SER A 277 68.353 -15.907 39.427 1.00109.78 C ANISOU 2018 C SER A 277 11690 17895 12126 838 -462 -475 C ATOM 2019 O SER A 277 67.491 -15.415 38.705 1.00111.66 O ANISOU 2019 O SER A 277 12051 18034 12341 776 -326 -497 O ATOM 2020 CB SER A 277 68.988 -14.978 41.675 1.00105.12 C ANISOU 2020 CB SER A 277 10924 17542 11474 832 -628 -510 C ATOM 2021 OG SER A 277 70.299 -14.874 41.141 1.00100.81 O ANISOU 2021 OG SER A 277 10265 17062 10975 839 -715 -570 O ATOM 2022 N HIS A 278 69.503 -16.378 38.955 1.00112.56 N ANISOU 2022 N HIS A 278 11947 18284 12539 884 -560 -487 N ATOM 2023 CA HIS A 278 69.797 -16.394 37.525 1.00108.60 C ANISOU 2023 CA HIS A 278 11484 17698 12082 860 -509 -525 C ATOM 2024 C HIS A 278 68.776 -17.224 36.740 1.00104.58 C ANISOU 2024 C HIS A 278 11124 17035 11576 872 -408 -457 C ATOM 2025 O HIS A 278 68.648 -17.076 35.526 1.00 96.05 O ANISOU 2025 O HIS A 278 10121 15863 10511 832 -339 -488 O ATOM 2026 CB HIS A 278 71.217 -16.909 37.268 1.00109.44 C ANISOU 2026 CB HIS A 278 11439 17876 12267 921 -640 -539 C ATOM 2027 CG HIS A 278 72.292 -16.016 37.804 1.00113.41 C ANISOU 2027 CG HIS A 278 11787 18530 12772 892 -735 -624 C ATOM 2028 ND1 HIS A 278 73.629 -16.353 37.761 1.00122.68 N ANISOU 2028 ND1 HIS A 278 12795 19801 14017 944 -866 -645 N ATOM 2029 CD2 HIS A 278 72.231 -14.802 38.396 1.00114.75 C ANISOU 2029 CD2 HIS A 278 11938 18776 12886 815 -719 -696 C ATOM 2030 CE1 HIS A 278 74.343 -15.387 38.305 1.00126.31 C ANISOU 2030 CE1 HIS A 278 13137 20394 14461 895 -929 -729 C ATOM 2031 NE2 HIS A 278 73.521 -14.428 38.699 1.00121.28 N ANISOU 2031 NE2 HIS A 278 12590 19745 13746 814 -842 -762 N ATOM 2032 N THR A 279 68.060 -18.102 37.435 1.00110.03 N ANISOU 2032 N THR A 279 11852 17701 12254 925 -409 -364 N ATOM 2033 CA THR A 279 67.006 -18.888 36.810 1.00113.77 C ANISOU 2033 CA THR A 279 12461 18039 12727 928 -313 -300 C ATOM 2034 C THR A 279 65.936 -17.935 36.303 1.00118.55 C ANISOU 2034 C THR A 279 13200 18570 13274 833 -168 -343 C ATOM 2035 O THR A 279 65.243 -18.223 35.320 1.00119.31 O ANISOU 2035 O THR A 279 13414 18551 13367 807 -85 -328 O ATOM 2036 CB THR A 279 66.359 -19.881 37.806 1.00113.11 C ANISOU 2036 CB THR A 279 12387 17954 12636 995 -335 -198 C ATOM 2037 OG1 THR A 279 67.348 -20.793 38.294 1.00116.69 O ANISOU 2037 OG1 THR A 279 12722 18475 13138 1098 -480 -150 O ATOM 2038 CG2 THR A 279 65.236 -20.678 37.143 1.00108.28 C ANISOU 2038 CG2 THR A 279 11909 17206 12027 987 -232 -138 C ATOM 2039 N ASN A 280 65.819 -16.791 36.976 1.00118.39 N ANISOU 2039 N ASN A 280 13157 18620 13208 784 -147 -397 N ATOM 2040 CA ASN A 280 64.763 -15.824 36.688 1.00115.48 C ANISOU 2040 CA ASN A 280 12917 18112 12848 690 -46 -418 C ATOM 2041 C ASN A 280 64.688 -15.412 35.217 1.00115.85 C ANISOU 2041 C ASN A 280 13085 17925 13010 614 -32 -437 C ATOM 2042 O ASN A 280 63.616 -15.046 34.722 1.00116.96 O ANISOU 2042 O ASN A 280 13387 17767 13285 534 -3 -395 O ATOM 2043 CB ASN A 280 64.904 -14.594 37.586 1.00113.14 C ANISOU 2043 CB ASN A 280 12556 17922 12510 648 -49 -479 C ATOM 2044 CG ASN A 280 64.021 -13.443 37.144 1.00112.17 C ANISOU 2044 CG ASN A 280 12586 17504 12529 531 -17 -479 C ATOM 2045 OD1 ASN A 280 64.469 -12.547 36.430 1.00110.47 O ANISOU 2045 OD1 ASN A 280 12386 17245 12343 479 -15 -542 O ATOM 2046 ND2 ASN A 280 62.760 -13.463 37.564 1.00112.95 N ANISOU 2046 ND2 ASN A 280 12797 17407 12714 496 8 -409 N ATOM 2047 N SER A 281 65.821 -15.491 34.523 1.00111.42 N ANISOU 2047 N SER A 281 12436 17510 12387 649 -54 -504 N ATOM 2048 CA SER A 281 65.918 -15.038 33.135 1.00104.00 C ANISOU 2048 CA SER A 281 11585 16392 11538 585 -46 -534 C ATOM 2049 C SER A 281 65.613 -16.125 32.100 1.00100.58 C ANISOU 2049 C SER A 281 11235 15816 11163 603 -41 -475 C ATOM 2050 O SER A 281 65.783 -15.918 30.900 1.00102.98 O ANISOU 2050 O SER A 281 11596 16004 11526 564 -39 -499 O ATOM 2051 CB SER A 281 67.291 -14.423 32.880 1.00102.34 C ANISOU 2051 CB SER A 281 11234 16413 11240 598 -71 -655 C ATOM 2052 OG SER A 281 67.571 -13.449 33.867 1.00103.04 O ANISOU 2052 OG SER A 281 11234 16648 11267 577 -75 -716 O ATOM 2053 N VAL A 282 65.182 -17.287 32.569 1.00 94.66 N ANISOU 2053 N VAL A 282 10485 15088 10392 663 -40 -401 N ATOM 2054 CA VAL A 282 64.861 -18.391 31.674 1.00 93.64 C ANISOU 2054 CA VAL A 282 10426 14840 10313 681 -35 -345 C ATOM 2055 C VAL A 282 63.357 -18.662 31.536 1.00 96.30 C ANISOU 2055 C VAL A 282 10932 14878 10780 612 -4 -263 C ATOM 2056 O VAL A 282 62.832 -18.672 30.426 1.00 93.97 O ANISOU 2056 O VAL A 282 10756 14362 10587 552 8 -249 O ATOM 2057 CB VAL A 282 65.653 -19.665 32.003 1.00 94.24 C ANISOU 2057 CB VAL A 282 10371 15139 10297 807 -71 -321 C ATOM 2058 CG1 VAL A 282 64.976 -20.880 31.387 1.00 96.30 C ANISOU 2058 CG1 VAL A 282 10717 15289 10584 829 -43 -246 C ATOM 2059 CG2 VAL A 282 67.083 -19.534 31.491 1.00 86.95 C ANISOU 2059 CG2 VAL A 282 9328 14265 9442 828 -160 -377 C ATOM 2060 N VAL A 283 62.681 -18.935 32.651 1.00101.42 N ANISOU 2060 N VAL A 283 11580 15537 11418 626 7 -214 N ATOM 2061 CA VAL A 283 61.257 -19.307 32.635 1.00 99.07 C ANISOU 2061 CA VAL A 283 11422 14988 11233 569 34 -149 C ATOM 2062 C VAL A 283 60.304 -18.348 31.915 1.00 97.18 C ANISOU 2062 C VAL A 283 11341 14453 11131 460 55 -157 C ATOM 2063 O VAL A 283 59.222 -18.767 31.506 1.00 95.38 O ANISOU 2063 O VAL A 283 11229 14013 10996 416 72 -117 O ATOM 2064 CB VAL A 283 60.685 -19.525 34.060 1.00 71.14 C ANISOU 2064 CB VAL A 283 7848 11520 7660 596 42 -108 C ATOM 2065 CG1 VAL A 283 61.626 -20.371 34.896 1.00 74.08 C ANISOU 2065 CG1 VAL A 283 8056 12210 7881 723 19 -92 C ATOM 2066 CG2 VAL A 283 60.410 -18.193 34.730 1.00 71.33 C ANISOU 2066 CG2 VAL A 283 7886 11512 7704 541 49 -144 C ATOM 2067 N ASN A 284 60.672 -17.075 31.763 1.00 97.08 N ANISOU 2067 N ASN A 284 11330 14432 11126 422 53 -209 N ATOM 2068 CA ASN A 284 59.718 -16.102 31.205 1.00 93.65 C ANISOU 2068 CA ASN A 284 10788 13780 11013 368 -22 -183 C ATOM 2069 C ASN A 284 59.092 -16.446 29.839 1.00 88.61 C ANISOU 2069 C ASN A 284 10457 13022 10188 318 -22 -184 C ATOM 2070 O ASN A 284 57.877 -16.599 29.742 1.00 83.12 O ANISOU 2070 O ASN A 284 9573 12237 9770 329 -17 -139 O ATOM 2071 CB ASN A 284 60.265 -14.672 31.235 1.00 91.20 C ANISOU 2071 CB ASN A 284 10709 13511 10434 309 -28 -258 C ATOM 2072 CG ASN A 284 59.797 -13.903 32.459 1.00 96.66 C ANISOU 2072 CG ASN A 284 10947 14849 10932 405 -34 -327 C ATOM 2073 OD1 ASN A 284 59.629 -14.476 33.533 1.00 95.96 O ANISOU 2073 OD1 ASN A 284 11000 14207 11252 353 -23 -214 O ATOM 2074 ND2 ASN A 284 59.568 -12.605 32.299 1.00 92.18 N ANISOU 2074 ND2 ASN A 284 10558 13643 10821 282 -24 -270 N ATOM 2075 N PRO A 285 59.910 -16.587 28.785 1.00 90.23 N ANISOU 2075 N PRO A 285 10424 13223 10637 350 -23 -191 N ATOM 2076 CA PRO A 285 59.302 -17.039 27.531 1.00 87.91 C ANISOU 2076 CA PRO A 285 10416 12823 10164 306 -24 -190 C ATOM 2077 C PRO A 285 58.457 -18.295 27.709 1.00 86.76 C ANISOU 2077 C PRO A 285 10077 12632 10257 352 -17 -125 C ATOM 2078 O PRO A 285 57.455 -18.454 27.011 1.00 88.29 O ANISOU 2078 O PRO A 285 10325 12726 10494 327 -14 -108 O ATOM 2079 CB PRO A 285 60.516 -17.335 26.649 1.00 87.82 C ANISOU 2079 CB PRO A 285 10387 12849 10131 320 -28 -221 C ATOM 2080 CG PRO A 285 61.520 -16.342 27.096 1.00 95.34 C ANISOU 2080 CG PRO A 285 11294 13893 11037 317 -33 -273 C ATOM 2081 CD PRO A 285 61.316 -16.192 28.598 1.00 95.94 C ANISOU 2081 CD PRO A 285 11315 14041 11096 341 45 -268 C ATOM 2082 N PHE A 286 58.845 -19.169 28.633 1.00 84.01 N ANISOU 2082 N PHE A 286 9690 12361 9870 395 -15 -103 N ATOM 2083 CA PHE A 286 58.125 -20.427 28.820 1.00 82.34 C ANISOU 2083 CA PHE A 286 9502 12115 9668 414 -9 -56 C ATOM 2084 C PHE A 286 56.721 -20.221 29.350 1.00 79.85 C ANISOU 2084 C PHE A 286 9434 11742 9161 355 -5 -36 C ATOM 2085 O PHE A 286 55.788 -20.891 28.922 1.00 78.59 O ANISOU 2085 O PHE A 286 9308 11506 9045 345 -1 -8 O ATOM 2086 CB PHE A 286 58.920 -21.393 29.698 1.00 83.72 C ANISOU 2086 CB PHE A 286 9813 12434 9565 450 68 -49 C ATOM 2087 CG PHE A 286 60.076 -22.009 28.988 1.00 86.35 C ANISOU 2087 CG PHE A 286 10059 12923 9825 516 48 -63 C ATOM 2088 CD1 PHE A 286 61.359 -21.510 29.155 1.00 90.33 C ANISOU 2088 CD1 PHE A 286 10445 13642 10234 570 28 -112 C ATOM 2089 CD2 PHE A 286 59.874 -23.058 28.107 1.00 82.80 C ANISOU 2089 CD2 PHE A 286 9643 12414 9404 525 48 -36 C ATOM 2090 CE1 PHE A 286 62.431 -22.071 28.480 1.00 89.09 C ANISOU 2090 CE1 PHE A 286 10202 13642 10008 638 8 -135 C ATOM 2091 CE2 PHE A 286 60.931 -23.617 27.431 1.00 85.37 C ANISOU 2091 CE2 PHE A 286 9887 12888 9663 592 30 -51 C ATOM 2092 CZ PHE A 286 62.216 -23.123 27.618 1.00 88.52 C ANISOU 2092 CZ PHE A 286 10166 13504 9964 652 10 -101 C ATOM 2093 N ILE A 287 56.573 -19.276 30.269 1.00 82.57 N ANISOU 2093 N ILE A 287 9760 12124 9487 345 -7 -49 N ATOM 2094 CA ILE A 287 55.254 -18.893 30.755 1.00 83.13 C ANISOU 2094 CA ILE A 287 9640 12136 9808 349 -4 -31 C ATOM 2095 C ILE A 287 54.376 -18.364 29.611 1.00 85.97 C ANISOU 2095 C ILE A 287 10257 12388 10021 282 -6 -46 C ATOM 2096 O ILE A 287 53.227 -18.784 29.474 1.00 88.97 O ANISOU 2096 O ILE A 287 10477 12698 10630 295 -3 -20 O ATOM 2097 CB ILE A 287 55.351 -17.868 31.906 1.00 80.45 C ANISOU 2097 CB ILE A 287 9262 11863 9442 344 -6 -48 C ATOM 2098 CG1 ILE A 287 55.957 -18.522 33.161 1.00 81.32 C ANISOU 2098 CG1 ILE A 287 9548 12089 9259 357 -4 -32 C ATOM 2099 CG2 ILE A 287 53.990 -17.261 32.207 1.00 76.31 C ANISOU 2099 CG2 ILE A 287 8770 11274 8948 312 -5 -42 C ATOM 2100 CD1 ILE A 287 55.010 -19.440 33.941 1.00 78.64 C ANISOU 2100 CD1 ILE A 287 9216 11740 8924 371 3 18 C ATOM 2101 N TYR A 288 54.925 -17.471 28.783 1.00 81.32 N ANISOU 2101 N TYR A 288 9475 11782 9641 289 -9 -75 N ATOM 2102 CA TYR A 288 54.198 -16.926 27.630 1.00 77.88 C ANISOU 2102 CA TYR A 288 9091 11249 9250 256 -10 -84 C ATOM 2103 C TYR A 288 53.659 -18.007 26.715 1.00 79.20 C ANISOU 2103 C TYR A 288 9472 11352 9269 235 -8 -69 C ATOM 2104 O TYR A 288 52.536 -17.904 26.238 1.00 79.21 O ANISOU 2104 O TYR A 288 9504 11278 9314 215 -7 -61 O ATOM 2105 CB TYR A 288 55.088 -16.030 26.773 1.00 77.99 C ANISOU 2105 CB TYR A 288 9283 11270 9081 223 -14 -131 C ATOM 2106 CG TYR A 288 55.595 -14.811 27.463 1.00 74.11 C ANISOU 2106 CG TYR A 288 8764 10837 8559 215 -17 -162 C ATOM 2107 CD1 TYR A 288 55.028 -14.385 28.649 1.00 73.97 C ANISOU 2107 CD1 TYR A 288 8539 10843 8722 232 -14 -142 C ATOM 2108 CD2 TYR A 288 56.651 -14.085 26.933 1.00 76.83 C ANISOU 2108 CD2 TYR A 288 9090 11214 8889 208 -20 -201 C ATOM 2109 CE1 TYR A 288 55.494 -13.265 29.299 1.00 78.28 C ANISOU 2109 CE1 TYR A 288 9252 11447 9043 204 -17 -186 C ATOM 2110 CE2 TYR A 288 57.132 -12.958 27.575 1.00 84.77 C ANISOU 2110 CE2 TYR A 288 9862 12278 10070 216 -19 -215 C ATOM 2111 CZ TYR A 288 56.546 -12.553 28.761 1.00 82.05 C ANISOU 2111 CZ TYR A 288 9711 11958 9506 195 -20 -227 C ATOM 2112 OH TYR A 288 57.005 -11.436 29.412 1.00 81.73 O ANISOU 2112 OH TYR A 288 9283 12473 9297 250 -26 -329 O ATOM 2113 N ALA A 289 54.477 -19.017 26.429 1.00 78.87 N ANISOU 2113 N ALA A 289 9419 11342 9206 258 -8 -61 N ATOM 2114 CA ALA A 289 54.051 -20.100 25.558 1.00 74.06 C ANISOU 2114 CA ALA A 289 8837 10675 8628 259 -6 -42 C ATOM 2115 C ALA A 289 52.869 -20.839 26.193 1.00 80.76 C ANISOU 2115 C ALA A 289 9531 11493 9662 282 -1 -7 C ATOM 2116 O ALA A 289 51.828 -21.034 25.557 1.00 85.58 O ANISOU 2116 O ALA A 289 10338 12034 10145 239 0 -1 O ATOM 2117 CB ALA A 289 55.202 -21.043 25.282 1.00 66.53 C ANISOU 2117 CB ALA A 289 7865 9772 7642 289 -6 -40 C ATOM 2118 N TYR A 290 53.014 -21.226 27.454 1.00 76.90 N ANISOU 2118 N TYR A 290 9183 11072 8963 282 2 15 N ATOM 2119 CA TYR A 290 51.937 -21.932 28.133 1.00 84.72 C ANISOU 2119 CA TYR A 290 10009 12041 10141 308 7 44 C ATOM 2120 C TYR A 290 50.669 -21.066 28.268 1.00 81.40 C ANISOU 2120 C TYR A 290 9614 11568 9746 275 5 36 C ATOM 2121 O TYR A 290 49.566 -21.493 27.929 1.00 79.31 O ANISOU 2121 O TYR A 290 9539 11248 9347 237 7 51 O ATOM 2122 CB TYR A 290 52.415 -22.448 29.501 1.00 95.01 C ANISOU 2122 CB TYR A 290 11450 13438 11213 317 12 75 C ATOM 2123 CG TYR A 290 51.300 -22.900 30.427 1.00103.79 C ANISOU 2123 CG TYR A 290 12564 14543 12330 317 17 108 C ATOM 2124 CD1 TYR A 290 50.525 -21.968 31.111 1.00111.19 C ANISOU 2124 CD1 TYR A 290 13499 15474 13272 296 14 98 C ATOM 2125 CD2 TYR A 290 51.025 -24.252 30.626 1.00 99.15 C ANISOU 2125 CD2 TYR A 290 11792 13952 11931 368 23 136 C ATOM 2126 CE1 TYR A 290 49.497 -22.361 31.957 1.00113.40 C ANISOU 2126 CE1 TYR A 290 13595 15749 13742 322 17 115 C ATOM 2127 CE2 TYR A 290 49.996 -24.657 31.477 1.00105.47 C ANISOU 2127 CE2 TYR A 290 12479 15173 12421 458 37 222 C ATOM 2128 CZ TYR A 290 49.236 -23.702 32.139 1.00110.15 C ANISOU 2128 CZ TYR A 290 13183 15339 13331 343 23 151 C ATOM 2129 OH TYR A 290 48.210 -24.065 32.985 1.00109.29 O ANISOU 2129 OH TYR A 290 13071 15231 13224 341 27 175 O ATOM 2130 N ARG A 291 50.834 -19.848 28.767 1.00 80.34 N ANISOU 2130 N ARG A 291 9464 11461 9601 265 2 16 N ATOM 2131 CA ARG A 291 49.692 -19.013 29.140 1.00 73.48 C ANISOU 2131 CA ARG A 291 8775 10562 8581 222 2 12 C ATOM 2132 C ARG A 291 49.132 -18.015 28.101 1.00 66.32 C ANISOU 2132 C ARG A 291 7896 9585 7716 195 -1 -12 C ATOM 2133 O ARG A 291 48.084 -17.442 28.334 1.00 64.24 O ANISOU 2133 O ARG A 291 7644 9294 7470 181 -2 -14 O ATOM 2134 CB ARG A 291 49.997 -18.283 30.455 1.00 68.69 C ANISOU 2134 CB ARG A 291 7964 10025 8111 250 1 7 C ATOM 2135 CG ARG A 291 49.468 -18.992 31.688 1.00 67.84 C ANISOU 2135 CG ARG A 291 7835 9957 7985 266 4 36 C ATOM 2136 CD ARG A 291 48.378 -18.173 32.355 1.00 67.93 C ANISOU 2136 CD ARG A 291 7851 9955 8003 247 4 31 C ATOM 2137 NE ARG A 291 47.454 -18.991 33.129 1.00 72.01 N ANISOU 2137 NE ARG A 291 8544 10480 8338 232 8 66 N ATOM 2138 CZ ARG A 291 46.497 -18.484 33.898 1.00 86.58 C ANISOU 2138 CZ ARG A 291 10387 12328 10183 222 8 67 C ATOM 2139 NH1 ARG A 291 46.359 -17.163 33.987 1.00 86.76 N ANISOU 2139 NH1 ARG A 291 10410 12348 10208 207 4 38 N ATOM 2140 NH2 ARG A 291 45.685 -19.288 34.583 1.00 91.33 N ANISOU 2140 NH2 ARG A 291 10985 12938 10780 227 11 97 N ATOM 2141 N ILE A 292 49.806 -17.807 26.972 1.00 64.48 N ANISOU 2141 N ILE A 292 7520 9328 7652 208 -3 -28 N ATOM 2142 CA ILE A 292 49.366 -16.786 26.008 1.00 61.91 C ANISOU 2142 CA ILE A 292 7370 8947 7206 170 -5 -51 C ATOM 2143 C ILE A 292 49.337 -17.244 24.540 1.00 68.22 C ANISOU 2143 C ILE A 292 8192 9691 8037 163 -6 -54 C ATOM 2144 O ILE A 292 50.366 -17.459 23.909 1.00 74.55 O ANISOU 2144 O ILE A 292 8849 10504 8973 185 -6 -59 O ATOM 2145 CB ILE A 292 50.235 -15.509 26.128 1.00 62.16 C ANISOU 2145 CB ILE A 292 7235 9012 7371 181 -7 -72 C ATOM 2146 CG1 ILE A 292 49.948 -14.785 27.450 1.00 62.70 C ANISOU 2146 CG1 ILE A 292 7434 9124 7265 166 -8 -81 C ATOM 2147 CG2 ILE A 292 50.017 -14.599 24.945 1.00 58.28 C ANISOU 2147 CG2 ILE A 292 6916 8467 6763 148 -9 -96 C ATOM 2148 CD1 ILE A 292 50.940 -13.684 27.787 1.00 58.12 C ANISOU 2148 CD1 ILE A 292 6668 8596 6821 178 -9 -101 C ATOM 2149 N ARG A 293 48.143 -17.327 23.978 1.00 71.93 N ANISOU 2149 N ARG A 293 8686 10103 8540 151 -5 -48 N ATOM 2150 CA ARG A 293 47.980 -17.870 22.638 1.00 68.91 C ANISOU 2150 CA ARG A 293 8200 9672 8311 158 -5 -45 C ATOM 2151 C ARG A 293 48.806 -17.180 21.561 1.00 71.72 C ANISOU 2151 C ARG A 293 8561 10017 8673 152 -7 -64 C ATOM 2152 O ARG A 293 49.224 -17.827 20.612 1.00 76.33 O ANISOU 2152 O ARG A 293 9155 10585 9264 154 -7 -66 O ATOM 2153 CB ARG A 293 46.507 -17.871 22.230 1.00 62.69 C ANISOU 2153 CB ARG A 293 7557 8837 7426 132 -5 -44 C ATOM 2154 CG ARG A 293 46.250 -18.610 20.940 1.00 59.06 C ANISOU 2154 CG ARG A 293 7115 8337 6989 127 -5 -45 C ATOM 2155 CD ARG A 293 44.767 -18.768 20.694 1.00 66.12 C ANISOU 2155 CD ARG A 293 8021 9199 7902 117 -4 -40 C ATOM 2156 NE ARG A 293 44.138 -17.470 20.484 1.00 72.08 N ANISOU 2156 NE ARG A 293 8675 9939 8773 120 -4 -46 N ATOM 2157 CZ ARG A 293 42.892 -17.299 20.061 1.00 66.56 C ANISOU 2157 CZ ARG A 293 8091 9219 7980 103 -5 -51 C ATOM 2158 NH1 ARG A 293 42.128 -18.350 19.800 1.00 67.35 N ANISOU 2158 NH1 ARG A 293 8093 9308 8188 109 -4 -40 N ATOM 2159 NH2 ARG A 293 42.414 -16.073 19.894 1.00 61.28 N ANISOU 2159 NH2 ARG A 293 7323 8543 7419 108 -5 -54 N ATOM 2160 N GLU A 294 49.031 -15.875 21.694 1.00 73.44 N ANISOU 2160 N GLU A 294 8772 10243 8888 145 -8 -78 N ATOM 2161 CA GLU A 294 49.613 -15.100 20.589 1.00 73.14 C ANISOU 2161 CA GLU A 294 8864 10188 8736 126 -10 -104 C ATOM 2162 C GLU A 294 51.126 -15.258 20.460 1.00 76.01 C ANISOU 2162 C GLU A 294 9208 10597 9075 134 -11 -119 C ATOM 2163 O GLU A 294 51.661 -15.286 19.342 1.00 67.56 O ANISOU 2163 O GLU A 294 8144 9512 8015 131 -12 -130 O ATOM 2164 CB GLU A 294 49.247 -13.615 20.677 1.00 65.83 C ANISOU 2164 CB GLU A 294 7820 9253 7939 126 -9 -106 C ATOM 2165 CG GLU A 294 49.500 -12.849 19.377 1.00 64.46 C ANISOU 2165 CG GLU A 294 7585 9320 7588 144 -13 -160 C ATOM 2166 CD GLU A 294 48.432 -13.101 18.326 1.00 68.13 C ANISOU 2166 CD GLU A 294 8267 9462 8158 101 -10 -118 C ATOM 2167 OE1 GLU A 294 47.334 -13.540 18.716 1.00 76.20 O ANISOU 2167 OE1 GLU A 294 9296 10469 9186 101 -9 -105 O ATOM 2168 OE2 GLU A 294 48.679 -12.863 17.116 1.00 64.56 O ANISOU 2168 OE2 GLU A 294 7824 8988 7720 96 -10 -125 O ATOM 2169 N PHE A 295 51.810 -15.345 21.601 1.00 79.34 N ANISOU 2169 N PHE A 295 9604 11080 9461 146 -12 -121 N ATOM 2170 CA PHE A 295 53.241 -15.635 21.619 1.00 77.59 C ANISOU 2170 CA PHE A 295 9213 10916 9351 173 -13 -125 C ATOM 2171 C PHE A 295 53.448 -17.103 21.236 1.00 80.52 C ANISOU 2171 C PHE A 295 9496 11617 9481 236 -17 -152 C ATOM 2172 O PHE A 295 54.273 -17.434 20.376 1.00 75.75 O ANISOU 2172 O PHE A 295 8979 10687 9114 194 -14 -123 O ATOM 2173 CB PHE A 295 53.839 -15.358 23.003 1.00 70.18 C ANISOU 2173 CB PHE A 295 8232 10055 8379 185 -13 -131 C ATOM 2174 CG PHE A 295 54.222 -13.918 23.231 1.00 73.43 C ANISOU 2174 CG PHE A 295 8626 10491 8784 172 -14 -156 C ATOM 2175 CD1 PHE A 295 55.286 -13.353 22.550 1.00 77.55 C ANISOU 2175 CD1 PHE A 295 9292 11036 9137 152 -17 -202 C ATOM 2176 CD2 PHE A 295 53.533 -13.130 24.150 1.00 73.31 C ANISOU 2176 CD2 PHE A 295 8766 10479 8609 150 -15 -168 C ATOM 2177 CE1 PHE A 295 55.646 -12.016 22.770 1.00 77.03 C ANISOU 2177 CE1 PHE A 295 8937 11373 8957 188 -22 -288 C ATOM 2178 CE2 PHE A 295 53.884 -11.798 24.371 1.00 65.01 C ANISOU 2178 CE2 PHE A 295 7701 9452 7548 137 -15 -196 C ATOM 2179 CZ PHE A 295 54.936 -11.245 23.681 1.00 68.70 C ANISOU 2179 CZ PHE A 295 8156 9941 8006 130 -16 -226 C ATOM 2180 N ARG A 296 52.673 -17.973 21.877 1.00 71.21 N ANISOU 2180 N ARG A 296 8558 10099 8398 180 -11 -95 N ATOM 2181 CA ARG A 296 52.758 -19.399 21.643 1.00 63.85 C ANISOU 2181 CA ARG A 296 7488 9164 7609 212 -9 -71 C ATOM 2182 C ARG A 296 52.618 -19.706 20.160 1.00 63.98 C ANISOU 2182 C ARG A 296 7669 9127 7514 183 -10 -85 C ATOM 2183 O ARG A 296 53.293 -20.583 19.636 1.00 71.88 O ANISOU 2183 O ARG A 296 8530 10138 8645 214 -10 -78 O ATOM 2184 CB ARG A 296 51.684 -20.121 22.448 1.00 64.57 C ANISOU 2184 CB ARG A 296 7588 9242 7704 215 -6 -44 C ATOM 2185 CG ARG A 296 51.663 -21.626 22.254 1.00 63.50 C ANISOU 2185 CG ARG A 296 7596 9105 7425 211 -4 -27 C ATOM 2186 CD ARG A 296 50.605 -22.259 23.129 1.00 66.36 C ANISOU 2186 CD ARG A 296 7962 9459 7791 212 0 1 C ATOM 2187 NE ARG A 296 49.248 -21.863 22.760 1.00 71.19 N ANISOU 2187 NE ARG A 296 8467 10008 8573 204 0 -2 N ATOM 2188 CZ ARG A 296 48.372 -21.303 23.591 1.00 76.49 C ANISOU 2188 CZ ARG A 296 9137 10679 9245 196 0 2 C ATOM 2189 NH1 ARG A 296 47.162 -20.992 23.153 1.00 79.04 N ANISOU 2189 NH1 ARG A 296 9610 10956 9466 161 0 -2 N ATOM 2190 NH2 ARG A 296 48.694 -21.055 24.855 1.00 78.82 N ANISOU 2190 NH2 ARG A 296 9541 11032 9377 192 1 11 N ATOM 2191 N GLN A 297 51.746 -18.977 19.480 1.00 58.53 N ANISOU 2191 N GLN A 297 6873 8380 6986 178 -10 -83 N ATOM 2192 CA GLN A 297 51.560 -19.165 18.047 1.00 63.29 C ANISOU 2192 CA GLN A 297 7501 8936 7612 167 -10 -89 C ATOM 2193 C GLN A 297 52.683 -18.579 17.211 1.00 66.93 C ANISOU 2193 C GLN A 297 7873 9697 7862 207 -17 -152 C ATOM 2194 O GLN A 297 52.922 -19.037 16.100 1.00 64.65 O ANISOU 2194 O GLN A 297 7672 9103 7787 163 -13 -118 O ATOM 2195 CB GLN A 297 50.235 -18.565 17.588 1.00 69.64 C ANISOU 2195 CB GLN A 297 8449 9687 8325 135 -10 -94 C ATOM 2196 CG GLN A 297 49.049 -19.438 17.888 1.00 76.81 C ANISOU 2196 CG GLN A 297 9257 10570 9357 146 -8 -69 C ATOM 2197 CD GLN A 297 47.761 -18.805 17.463 1.00 80.01 C ANISOU 2197 CD GLN A 297 9789 10936 9674 120 -8 -76 C ATOM 2198 OE1 GLN A 297 47.525 -17.627 17.720 1.00 84.94 O ANISOU 2198 OE1 GLN A 297 10307 11559 10406 125 -7 -74 O ATOM 2199 NE2 GLN A 297 46.913 -19.578 16.805 1.00 77.72 N ANISOU 2199 NE2 GLN A 297 9409 10615 9503 125 -7 -65 N ATOM 2200 N THR A 298 53.340 -17.539 17.713 1.00 65.74 N ANISOU 2200 N THR A 298 7778 9298 7902 165 -13 -126 N ATOM 2201 CA THR A 298 54.455 -16.951 16.980 1.00 67.21 C ANISOU 2201 CA THR A 298 8081 9507 7949 148 -17 -164 C ATOM 2202 C THR A 298 55.720 -17.782 17.212 1.00 75.60 C ANISOU 2202 C THR A 298 8976 10632 9115 185 -18 -161 C ATOM 2203 O THR A 298 56.467 -18.098 16.278 1.00 73.40 O ANISOU 2203 O THR A 298 8835 10360 8693 172 -21 -193 O ATOM 2204 CB THR A 298 54.653 -15.475 17.347 1.00 64.44 C ANISOU 2204 CB THR A 298 7498 9480 7506 187 -21 -226 C ATOM 2205 OG1 THR A 298 53.447 -14.769 17.057 1.00 69.10 O ANISOU 2205 OG1 THR A 298 8125 9996 8134 167 -19 -212 O ATOM 2206 CG2 THR A 298 55.756 -14.857 16.528 1.00 57.85 C ANISOU 2206 CG2 THR A 298 6644 8676 6662 180 -23 -265 C ATOM 2207 N PHE A 299 55.931 -18.176 18.461 1.00 79.61 N ANISOU 2207 N PHE A 299 9459 11190 9599 204 -18 -152 N ATOM 2208 CA PHE A 299 56.985 -19.120 18.771 1.00 71.73 C ANISOU 2208 CA PHE A 299 8428 10257 8571 233 -19 -155 C ATOM 2209 C PHE A 299 56.840 -20.323 17.842 1.00 71.21 C ANISOU 2209 C PHE A 299 8384 10155 8519 240 -19 -145 C ATOM 2210 O PHE A 299 57.746 -20.628 17.076 1.00 70.71 O ANISOU 2210 O PHE A 299 8462 10115 8291 228 -24 -179 O ATOM 2211 CB PHE A 299 56.882 -19.555 20.229 1.00 64.59 C ANISOU 2211 CB PHE A 299 7662 9402 7477 233 -19 -147 C ATOM 2212 CG PHE A 299 57.071 -18.431 21.216 1.00 66.75 C ANISOU 2212 CG PHE A 299 7913 9719 7727 229 -20 -161 C ATOM 2213 CD1 PHE A 299 57.589 -17.214 20.814 1.00 71.95 C ANISOU 2213 CD1 PHE A 299 8564 10387 8387 212 -22 -195 C ATOM 2214 CD2 PHE A 299 56.747 -18.603 22.559 1.00 64.12 C ANISOU 2214 CD2 PHE A 299 7567 9424 7371 241 -18 -140 C ATOM 2215 CE1 PHE A 299 57.764 -16.187 21.735 1.00 73.45 C ANISOU 2215 CE1 PHE A 299 8558 10621 8730 225 -21 -193 C ATOM 2216 CE2 PHE A 299 56.924 -17.580 23.483 1.00 58.81 C ANISOU 2216 CE2 PHE A 299 6694 8795 6854 258 -17 -143 C ATOM 2217 CZ PHE A 299 57.426 -16.376 23.072 1.00 64.63 C ANISOU 2217 CZ PHE A 299 7422 9541 7594 239 -20 -176 C ATOM 2218 N ARG A 300 55.680 -20.974 17.864 1.00 72.04 N ANISOU 2218 N ARG A 300 8664 10208 8499 214 -18 -129 N ATOM 2219 CA ARG A 300 55.457 -22.145 17.016 1.00 73.21 C ANISOU 2219 CA ARG A 300 8828 10323 8664 218 -17 -120 C ATOM 2220 C ARG A 300 55.771 -21.857 15.545 1.00 76.74 C ANISOU 2220 C ARG A 300 9150 10740 9270 223 -18 -133 C ATOM 2221 O ARG A 300 56.563 -22.562 14.930 1.00 70.03 O ANISOU 2221 O ARG A 300 8289 9910 8410 237 -21 -144 O ATOM 2222 CB ARG A 300 54.029 -22.659 17.163 1.00 72.07 C ANISOU 2222 CB ARG A 300 8578 10122 8685 225 -12 -86 C ATOM 2223 CG ARG A 300 53.884 -24.158 16.998 1.00 79.36 C ANISOU 2223 CG ARG A 300 9508 11038 9608 240 -11 -69 C ATOM 2224 CD ARG A 300 52.419 -24.559 16.753 1.00 90.57 C ANISOU 2224 CD ARG A 300 10961 12397 11056 219 -8 -56 C ATOM 2225 NE ARG A 300 51.507 -24.041 17.777 1.00 98.04 N ANISOU 2225 NE ARG A 300 12031 13339 11880 193 -7 -47 N ATOM 2226 CZ ARG A 300 51.140 -24.711 18.871 1.00103.04 C ANISOU 2226 CZ ARG A 300 12658 13993 12500 204 -3 -21 C ATOM 2227 NH1 ARG A 300 51.596 -25.943 19.090 1.00105.15 N ANISOU 2227 NH1 ARG A 300 12789 14283 12880 247 0 -2 N ATOM 2228 NH2 ARG A 300 50.311 -24.149 19.747 1.00 99.53 N ANISOU 2228 NH2 ARG A 300 12213 13544 12059 195 -2 -13 N ATOM 2229 N LYS A 301 55.162 -20.814 14.987 1.00 83.53 N ANISOU 2229 N LYS A 301 10031 11556 10152 196 -18 -140 N ATOM 2230 CA LYS A 301 55.396 -20.467 13.588 1.00 81.87 C ANISOU 2230 CA LYS A 301 9831 11320 9957 182 -19 -159 C ATOM 2231 C LYS A 301 56.876 -20.271 13.303 1.00 83.37 C ANISOU 2231 C LYS A 301 10122 11564 9989 177 -25 -205 C ATOM 2232 O LYS A 301 57.408 -20.876 12.373 1.00 87.48 O ANISOU 2232 O LYS A 301 10504 12088 10645 198 -25 -201 O ATOM 2233 CB LYS A 301 54.623 -19.211 13.165 1.00 78.33 C ANISOU 2233 CB LYS A 301 9326 11107 9331 197 -24 -218 C ATOM 2234 CG LYS A 301 54.813 -18.869 11.679 1.00 75.06 C ANISOU 2234 CG LYS A 301 8923 10660 8936 181 -25 -239 C ATOM 2235 CD LYS A 301 54.502 -17.412 11.374 1.00 71.81 C ANISOU 2235 CD LYS A 301 8595 9962 8727 128 -17 -180 C ATOM 2236 CE LYS A 301 55.208 -16.938 10.100 1.00 71.87 C ANISOU 2236 CE LYS A 301 8598 9972 8738 119 -17 -201 C ATOM 2237 NZ LYS A 301 54.564 -17.427 8.854 1.00 73.43 N ANISOU 2237 NZ LYS A 301 8930 10127 8842 102 -17 -214 N ATOM 2238 N ILE A 302 57.524 -19.417 14.095 1.00 80.25 N ANISOU 2238 N ILE A 302 9705 11218 9569 179 -26 -218 N ATOM 2239 CA ILE A 302 58.959 -19.137 13.961 1.00 80.36 C ANISOU 2239 CA ILE A 302 9688 11298 9549 188 -30 -256 C ATOM 2240 C ILE A 302 59.797 -20.426 13.956 1.00 81.19 C ANISOU 2240 C ILE A 302 9617 11451 9782 238 -31 -241 C ATOM 2241 O ILE A 302 60.471 -20.751 12.972 1.00 71.84 O ANISOU 2241 O ILE A 302 8424 10274 8597 240 -34 -265 O ATOM 2242 CB ILE A 302 59.449 -18.213 15.097 1.00 78.95 C ANISOU 2242 CB ILE A 302 9482 11175 9339 191 -30 -270 C ATOM 2243 CG1 ILE A 302 58.666 -16.899 15.093 1.00 78.29 C ANISOU 2243 CG1 ILE A 302 9262 11050 9435 180 -24 -243 C ATOM 2244 CG2 ILE A 302 60.939 -17.946 14.972 1.00 80.33 C ANISOU 2244 CG2 ILE A 302 9619 11428 9475 199 -35 -318 C ATOM 2245 CD1 ILE A 302 59.062 -15.946 16.198 1.00 80.96 C ANISOU 2245 CD1 ILE A 302 9729 11439 9593 163 -26 -280 C ATOM 2246 N ILE A 303 59.737 -21.142 15.076 1.00 87.87 N ANISOU 2246 N ILE A 303 10349 12695 10342 329 -41 -299 N ATOM 2247 CA ILE A 303 60.408 -22.425 15.280 1.00 85.89 C ANISOU 2247 CA ILE A 303 10346 12128 10159 276 -35 -234 C ATOM 2248 C ILE A 303 60.175 -23.474 14.177 1.00 86.51 C ANISOU 2248 C ILE A 303 10283 12161 10427 303 -33 -210 C ATOM 2249 O ILE A 303 61.119 -24.126 13.745 1.00 84.26 O ANISOU 2249 O ILE A 303 10138 11926 9951 303 -32 -253 O ATOM 2250 CB ILE A 303 60.044 -22.992 16.684 1.00 72.73 C ANISOU 2250 CB ILE A 303 8674 10492 8469 299 -31 -196 C ATOM 2251 CG1 ILE A 303 60.585 -22.041 17.774 1.00 70.31 C ANISOU 2251 CG1 ILE A 303 8337 10253 8125 304 -33 -211 C ATOM 2252 CG2 ILE A 303 60.525 -24.446 16.850 1.00 65.13 C ANISOU 2252 CG2 ILE A 303 7694 9578 7474 344 -12 -181 C ATOM 2253 CD1 ILE A 303 60.159 -22.371 19.202 1.00 63.98 C ANISOU 2253 CD1 ILE A 303 7344 9479 7488 353 -26 -160 C ATOM 2254 N ARG A 304 58.941 -23.621 13.701 1.00 90.27 N ANISOU 2254 N ARG A 304 10956 12560 10785 254 -32 -206 N ATOM 2255 CA ARG A 304 58.639 -24.610 12.660 1.00 91.66 C ANISOU 2255 CA ARG A 304 11149 12695 10983 253 -33 -205 C ATOM 2256 C ARG A 304 59.000 -24.101 11.262 1.00 94.87 C ANISOU 2256 C ARG A 304 11412 13079 11553 255 -33 -221 C ATOM 2257 O ARG A 304 58.767 -24.779 10.266 1.00 92.70 O ANISOU 2257 O ARG A 304 11155 12773 11294 250 -34 -225 O ATOM 2258 CB ARG A 304 57.164 -25.022 12.691 1.00 91.87 C ANISOU 2258 CB ARG A 304 11070 12652 11186 258 -25 -158 C ATOM 2259 CG ARG A 304 56.303 -24.316 11.628 1.00 96.73 C ANISOU 2259 CG ARG A 304 11715 13202 11834 222 -24 -166 C ATOM 2260 CD ARG A 304 54.827 -24.755 11.668 1.00101.24 C ANISOU 2260 CD ARG A 304 12441 13719 12308 189 -22 -156 C ATOM 2261 NE ARG A 304 54.650 -26.184 11.404 1.00101.77 N ANISOU 2261 NE ARG A 304 12395 13777 12497 218 -21 -135 N ATOM 2262 CZ ARG A 304 54.251 -27.085 12.304 1.00 99.63 C ANISOU 2262 CZ ARG A 304 12126 13512 12220 232 -18 -110 C ATOM 2263 NH1 ARG A 304 54.131 -28.362 11.948 1.00103.26 N ANISOU 2263 NH1 ARG A 304 12592 13963 12681 243 -18 -104 N ATOM 2264 NH2 ARG A 304 53.963 -26.720 13.552 1.00 88.06 N ANISOU 2264 NH2 ARG A 304 10653 12062 10745 237 -15 -91 N ATOM 2265 N SER A 305 59.542 -22.892 11.183 1.00100.37 N ANISOU 2265 N SER A 305 12240 13797 12099 221 -37 -266 N ATOM 2266 CA SER A 305 59.981 -22.357 9.903 1.00108.65 C ANISOU 2266 CA SER A 305 13137 14836 13307 224 -36 -276 C ATOM 2267 C SER A 305 61.485 -22.091 9.896 1.00122.07 C ANISOU 2267 C SER A 305 14789 16612 14981 238 -41 -319 C ATOM 2268 O SER A 305 62.250 -22.823 9.255 1.00125.88 O ANISOU 2268 O SER A 305 15413 17122 15293 231 -54 -379 O ATOM 2269 CB SER A 305 59.202 -21.093 9.553 1.00107.57 C ANISOU 2269 CB SER A 305 13025 14652 13194 191 -31 -269 C ATOM 2270 OG SER A 305 57.811 -21.362 9.541 1.00110.57 O ANISOU 2270 OG SER A 305 13445 14970 13597 180 -28 -236 O ATOM 2271 N HIS A 306 61.907 -21.058 10.623 1.00129.98 N ANISOU 2271 N HIS A 306 15662 18013 15712 291 -55 -452 N ATOM 2272 CA HIS A 306 63.322 -20.663 10.668 1.00132.64 C ANISOU 2272 CA HIS A 306 16222 18071 16104 223 -49 -418 C ATOM 2273 C HIS A 306 64.271 -21.721 11.271 1.00133.14 C ANISOU 2273 C HIS A 306 16146 18360 16081 300 -61 -473 C ATOM 2274 O HIS A 306 65.457 -21.759 10.935 1.00131.65 O ANISOU 2274 O HIS A 306 15836 18349 15837 337 -74 -565 O ATOM 2275 CB HIS A 306 63.482 -19.317 11.386 1.00132.53 C ANISOU 2275 CB HIS A 306 16017 18082 16256 226 -47 -393 C ATOM 2276 CG HIS A 306 62.663 -18.215 10.787 1.00132.06 C ANISOU 2276 CG HIS A 306 16164 17949 16062 172 -36 -416 C ATOM 2277 ND1 HIS A 306 61.334 -18.370 10.462 1.00131.16 N ANISOU 2277 ND1 HIS A 306 16090 17756 15987 162 -32 -369 N ATOM 2278 CD2 HIS A 306 62.988 -16.943 10.455 1.00133.04 C ANISOU 2278 CD2 HIS A 306 16278 18079 16191 148 -33 -446 C ATOM 2279 CE1 HIS A 306 60.872 -17.238 9.956 1.00132.31 C ANISOU 2279 CE1 HIS A 306 16095 17869 16308 149 -31 -337 C ATOM 2280 NE2 HIS A 306 61.855 -16.357 9.943 1.00134.59 N ANISOU 2280 NE2 HIS A 306 16240 18556 16340 174 -38 -513 N ATOM 2281 N VAL A 307 63.753 -22.554 12.172 1.00133.35 N ANISOU 2281 N VAL A 307 16184 18389 16093 328 -58 -422 N ATOM 2282 CA VAL A 307 64.506 -23.695 12.710 1.00133.66 C ANISOU 2282 CA VAL A 307 16101 18640 16046 419 -70 -451 C ATOM 2283 C VAL A 307 64.231 -24.998 11.925 1.00129.94 C ANISOU 2283 C VAL A 307 15624 18168 15579 449 -75 -442 C ATOM 2284 O VAL A 307 64.882 -26.020 12.144 1.00128.76 O ANISOU 2284 O VAL A 307 15368 18164 15389 535 -85 -454 O ATOM 2285 CB VAL A 307 64.283 -23.868 14.248 1.00115.53 C ANISOU 2285 CB VAL A 307 13794 16391 13711 451 -64 -403 C ATOM 2286 CG1 VAL A 307 64.885 -25.182 14.766 1.00113.83 C ANISOU 2286 CG1 VAL A 307 13465 16384 13403 562 -74 -405 C ATOM 2287 CG2 VAL A 307 64.853 -22.665 15.016 1.00109.73 C ANISOU 2287 CG2 VAL A 307 13024 15721 12949 440 -64 -438 C ATOM 2288 N LEU A 308 63.267 -24.949 11.007 1.00128.76 N ANISOU 2288 N LEU A 308 15584 17825 15513 380 -67 -407 N ATOM 2289 CA LEU A 308 63.023 -26.060 10.086 1.00126.83 C ANISOU 2289 CA LEU A 308 15332 17580 15279 399 -72 -413 C ATOM 2290 C LEU A 308 63.586 -25.751 8.702 1.00126.71 C ANISOU 2290 C LEU A 308 15285 17581 15278 381 -80 -486 C ATOM 2291 O LEU A 308 64.189 -26.610 8.062 1.00127.33 O ANISOU 2291 O LEU A 308 15274 17775 15331 433 -91 -546 O ATOM 2292 CB LEU A 308 61.531 -26.371 9.973 1.00122.20 C ANISOU 2292 CB LEU A 308 14874 16788 14769 339 -59 -335 C ATOM 2293 CG LEU A 308 61.190 -27.431 8.920 1.00117.62 C ANISOU 2293 CG LEU A 308 14290 16196 14206 347 -64 -347 C ATOM 2294 CD1 LEU A 308 61.825 -28.749 9.320 1.00115.52 C ANISOU 2294 CD1 LEU A 308 13911 16123 13858 450 -72 -365 C ATOM 2295 CD2 LEU A 308 59.673 -27.588 8.692 1.00113.25 C ANISOU 2295 CD2 LEU A 308 13861 15438 13732 280 -54 -284 C TER 2296 LEU A 308 ATOM 2297 N ASP B 1 46.786 -7.103 -1.334 1.00118.46 N ANISOU 2297 N ASP B 1 11581 18622 14808 -1039 1523 892 N ATOM 2298 CA ASP B 1 47.267 -7.226 0.039 1.00112.82 C ANISOU 2298 CA ASP B 1 10838 17672 14355 -970 1457 753 C ATOM 2299 C ASP B 1 46.945 -8.607 0.585 1.00 99.71 C ANISOU 2299 C ASP B 1 9227 15932 12728 -590 1442 369 C ATOM 2300 O ASP B 1 47.246 -9.610 -0.060 1.00107.11 O ANISOU 2300 O ASP B 1 10098 17125 13473 -364 1477 114 O ATOM 2301 CB ASP B 1 46.680 -6.123 0.925 1.00113.45 C ANISOU 2301 CB ASP B 1 11070 17313 14724 -1193 1349 1026 C ATOM 2302 CG ASP B 1 47.141 -4.732 0.505 1.00119.98 C ANISOU 2302 CG ASP B 1 11877 18142 15569 -1562 1296 1384 C ATOM 2303 OD1 ASP B 1 48.259 -4.609 -0.053 1.00127.18 O ANISOU 2303 OD1 ASP B 1 12595 19404 16325 -1659 1347 1401 O ATOM 2304 OD2 ASP B 1 46.386 -3.763 0.729 1.00115.73 O ANISOU 2304 OD2 ASP B 1 11524 17243 15205 -1745 1181 1644 O ATOM 2305 N ILE B 2 46.326 -8.669 1.759 1.00 84.33 N ANISOU 2305 N ILE B 2 7471 13543 11025 -505 1341 316 N ATOM 2306 CA ILE B 2 45.920 -9.961 2.307 1.00 82.35 C ANISOU 2306 CA ILE B 2 7375 13094 10820 -154 1269 -26 C ATOM 2307 C ILE B 2 44.509 -10.323 1.860 1.00 79.55 C ANISOU 2307 C ILE B 2 7273 12544 10408 -49 1262 -19 C ATOM 2308 O ILE B 2 43.551 -9.723 2.317 1.00 78.10 O ANISOU 2308 O ILE B 2 7343 11966 10365 -141 1198 145 O ATOM 2309 CB ILE B 2 45.886 -9.942 3.828 1.00 73.73 C ANISOU 2309 CB ILE B 2 6479 11532 10002 -100 1122 -98 C ATOM 2310 CG1 ILE B 2 47.303 -9.837 4.398 1.00 64.94 C ANISOU 2310 CG1 ILE B 2 5126 10585 8962 -138 1100 -179 C ATOM 2311 CG2 ILE B 2 45.121 -11.169 4.335 1.00 66.20 C ANISOU 2311 CG2 ILE B 2 5753 10310 9089 200 1026 -355 C ATOM 2312 CD1 ILE B 2 47.346 -9.847 5.901 1.00 60.45 C ANISOU 2312 CD1 ILE B 2 4737 9591 8640 -80 946 -262 C ATOM 2313 N VAL B 3 44.400 -11.332 1.001 1.00 80.32 N ANISOU 2313 N VAL B 3 7288 12924 10305 161 1312 -228 N ATOM 2314 CA VAL B 3 43.151 -11.692 0.332 1.00 80.69 C ANISOU 2314 CA VAL B 3 7521 12880 10257 249 1316 -221 C ATOM 2315 C VAL B 3 42.376 -12.746 1.137 1.00 79.14 C ANISOU 2315 C VAL B 3 7584 12280 10204 506 1176 -452 C ATOM 2316 O VAL B 3 42.888 -13.826 1.435 1.00 81.79 O ANISOU 2316 O VAL B 3 7862 12657 10557 743 1099 -746 O ATOM 2317 CB VAL B 3 43.418 -12.203 -1.125 1.00 75.94 C ANISOU 2317 CB VAL B 3 6717 12791 9345 328 1419 -323 C ATOM 2318 CG1 VAL B 3 42.120 -12.396 -1.894 1.00 77.47 C ANISOU 2318 CG1 VAL B 3 7062 12946 9428 381 1438 -277 C ATOM 2319 CG2 VAL B 3 44.337 -11.252 -1.883 1.00 72.00 C ANISOU 2319 CG2 VAL B 3 6028 12638 8693 54 1509 -91 C ATOM 2320 N MET B 4 41.141 -12.418 1.501 1.00 74.96 N ANISOU 2320 N MET B 4 7334 11365 9785 449 1125 -311 N ATOM 2321 CA MET B 4 40.300 -13.336 2.255 1.00 74.13 C ANISOU 2321 CA MET B 4 7472 10897 9799 636 996 -473 C ATOM 2322 C MET B 4 39.328 -13.993 1.305 1.00 72.95 C ANISOU 2322 C MET B 4 7403 10801 9514 757 1001 -538 C ATOM 2323 O MET B 4 38.721 -13.317 0.483 1.00 77.71 O ANISOU 2323 O MET B 4 8020 11491 10015 628 1083 -348 O ATOM 2324 CB MET B 4 39.526 -12.599 3.348 1.00 69.12 C ANISOU 2324 CB MET B 4 7069 9835 9359 507 935 -307 C ATOM 2325 CG MET B 4 40.383 -12.019 4.459 1.00 63.77 C ANISOU 2325 CG MET B 4 6348 9044 8838 411 894 -275 C ATOM 2326 SD MET B 4 41.272 -13.273 5.391 1.00 72.96 S ANISOU 2326 SD MET B 4 7475 10172 10072 631 771 -568 S ATOM 2327 CE MET B 4 39.959 -13.931 6.414 1.00 69.09 C ANISOU 2327 CE MET B 4 7310 9250 9691 718 635 -608 C ATOM 2328 N THR B 5 39.200 -15.311 1.410 1.00 67.98 N ANISOU 2328 N THR B 5 6828 10107 8892 1001 889 -803 N ATOM 2329 CA THR B 5 38.314 -16.077 0.535 1.00 68.58 C ANISOU 2329 CA THR B 5 6980 10219 8857 1140 859 -907 C ATOM 2330 C THR B 5 37.553 -17.190 1.276 1.00 59.46 C ANISOU 2330 C THR B 5 6053 8692 7846 1298 671 -1055 C ATOM 2331 O THR B 5 38.162 -18.062 1.886 1.00 55.78 O ANISOU 2331 O THR B 5 5577 8145 7472 1451 533 -1256 O ATOM 2332 CB THR B 5 39.096 -16.630 -0.705 1.00 59.69 C ANISOU 2332 CB THR B 5 5592 9583 7507 1293 915 -1116 C ATOM 2333 OG1 THR B 5 38.909 -18.044 -0.824 1.00 55.13 O ANISOU 2333 OG1 THR B 5 5092 8909 6944 1553 741 -1409 O ATOM 2334 CG2 THR B 5 40.590 -16.307 -0.602 1.00 58.10 C ANISOU 2334 CG2 THR B 5 5118 9691 7266 1257 984 -1163 C ATOM 2335 N GLN B 6 36.225 -17.177 1.211 1.00 61.98 N ANISOU 2335 N GLN B 6 6573 8790 8187 1253 647 -948 N ATOM 2336 CA GLN B 6 35.442 -18.174 1.960 1.00 64.32 C ANISOU 2336 CA GLN B 6 7082 8741 8617 1347 466 -1038 C ATOM 2337 C GLN B 6 34.552 -19.101 1.146 1.00 67.46 C ANISOU 2337 C GLN B 6 7561 9118 8954 1482 375 -1157 C ATOM 2338 O GLN B 6 34.280 -18.865 -0.032 1.00 67.06 O ANISOU 2338 O GLN B 6 7433 9302 8745 1493 469 -1148 O ATOM 2339 CB GLN B 6 34.641 -17.555 3.101 1.00 54.37 C ANISOU 2339 CB GLN B 6 6006 7162 7490 1176 462 -837 C ATOM 2340 CG GLN B 6 33.565 -16.608 2.711 1.00 46.72 C ANISOU 2340 CG GLN B 6 5108 6158 6484 1030 569 -634 C ATOM 2341 CD GLN B 6 32.932 -15.991 3.934 1.00 53.36 C ANISOU 2341 CD GLN B 6 6088 6730 7455 893 556 -495 C ATOM 2342 OE1 GLN B 6 33.042 -14.787 4.158 1.00 58.35 O ANISOU 2342 OE1 GLN B 6 6688 7361 8121 756 642 -349 O ATOM 2343 NE2 GLN B 6 32.288 -16.820 4.756 1.00 54.36 N ANISOU 2343 NE2 GLN B 6 6362 6637 7656 926 430 -545 N ATOM 2344 N SER B 7 34.157 -20.198 1.783 1.00 70.89 N ANISOU 2344 N SER B 7 8147 9276 9514 1579 169 -1270 N ATOM 2345 CA SER B 7 33.374 -21.234 1.123 1.00 76.22 C ANISOU 2345 CA SER B 7 8908 9880 10173 1715 24 -1407 C ATOM 2346 C SER B 7 32.418 -21.881 2.102 1.00 77.15 C ANISOU 2346 C SER B 7 9256 9610 10448 1654 -155 -1335 C ATOM 2347 O SER B 7 32.667 -21.869 3.311 1.00 70.97 O ANISOU 2347 O SER B 7 8543 8643 9780 1574 -214 -1260 O ATOM 2348 CB SER B 7 34.270 -22.289 0.466 1.00 76.32 C ANISOU 2348 CB SER B 7 8820 10052 10127 1904 -116 -1670 C ATOM 2349 OG SER B 7 35.520 -22.396 1.128 1.00 84.97 O ANISOU 2349 OG SER B 7 9829 11179 11276 1926 -159 -1739 O ATOM 2350 N PRO B 8 31.295 -22.405 1.575 1.00 79.96 N ANISOU 2350 N PRO B 8 9720 9865 10794 1671 -237 -1340 N ATOM 2351 CA PRO B 8 30.985 -22.211 0.151 1.00 74.47 C ANISOU 2351 CA PRO B 8 8936 9421 9939 1744 -138 -1401 C ATOM 2352 C PRO B 8 30.360 -20.837 -0.038 1.00 71.00 C ANISOU 2352 C PRO B 8 8492 9068 9417 1547 93 -1145 C ATOM 2353 O PRO B 8 30.126 -20.177 0.974 1.00 71.27 O ANISOU 2353 O PRO B 8 8597 8944 9540 1385 148 -965 O ATOM 2354 CB PRO B 8 29.950 -23.294 -0.119 1.00 75.44 C ANISOU 2354 CB PRO B 8 9203 9337 10122 1812 -349 -1484 C ATOM 2355 CG PRO B 8 29.251 -23.446 1.183 1.00 78.74 C ANISOU 2355 CG PRO B 8 9797 9423 10697 1646 -444 -1308 C ATOM 2356 CD PRO B 8 30.285 -23.236 2.253 1.00 78.34 C ANISOU 2356 CD PRO B 8 9715 9333 10719 1614 -438 -1285 C ATOM 2357 N ALA B 9 30.085 -20.411 -1.270 1.00 68.21 N ANISOU 2357 N ALA B 9 8059 8956 8901 1563 205 -1132 N ATOM 2358 CA ALA B 9 29.485 -19.084 -1.480 1.00 66.73 C ANISOU 2358 CA ALA B 9 7877 8819 8657 1379 382 -879 C ATOM 2359 C ALA B 9 27.995 -19.085 -1.140 1.00 68.14 C ANISOU 2359 C ALA B 9 8228 8737 8923 1290 327 -762 C ATOM 2360 O ALA B 9 27.409 -18.047 -0.835 1.00 67.00 O ANISOU 2360 O ALA B 9 8121 8527 8809 1139 423 -567 O ATOM 2361 CB ALA B 9 29.724 -18.578 -2.893 1.00 60.95 C ANISOU 2361 CB ALA B 9 7003 8447 7709 1399 506 -867 C ATOM 2362 N SER B 10 27.387 -20.263 -1.185 1.00 73.30 N ANISOU 2362 N SER B 10 8976 9246 9629 1385 153 -894 N ATOM 2363 CA SER B 10 26.023 -20.438 -0.714 1.00 77.39 C ANISOU 2363 CA SER B 10 9639 9526 10240 1288 81 -794 C ATOM 2364 C SER B 10 25.873 -21.851 -0.184 1.00 73.88 C ANISOU 2364 C SER B 10 9295 8862 9914 1354 -156 -921 C ATOM 2365 O SER B 10 26.493 -22.795 -0.674 1.00 74.77 O ANISOU 2365 O SER B 10 9377 9010 10020 1528 -296 -1130 O ATOM 2366 CB SER B 10 25.021 -20.170 -1.831 1.00 83.98 C ANISOU 2366 CB SER B 10 10480 10452 10977 1291 117 -756 C ATOM 2367 OG SER B 10 25.408 -20.882 -2.994 1.00 95.33 O ANISOU 2367 OG SER B 10 11853 12072 12298 1467 53 -951 O ATOM 2368 N LEU B 11 25.062 -21.984 0.847 1.00 69.30 N ANISOU 2368 N LEU B 11 8826 8063 9442 1211 -217 -794 N ATOM 2369 CA LEU B 11 24.864 -23.265 1.482 1.00 65.47 C ANISOU 2369 CA LEU B 11 8450 7346 9078 1212 -463 -847 C ATOM 2370 C LEU B 11 23.402 -23.291 1.880 1.00 63.87 C ANISOU 2370 C LEU B 11 8336 7019 8914 1042 -489 -691 C ATOM 2371 O LEU B 11 22.906 -22.329 2.476 1.00 63.65 O ANISOU 2371 O LEU B 11 8291 7028 8865 900 -329 -537 O ATOM 2372 CB LEU B 11 25.765 -23.340 2.714 1.00 61.71 C ANISOU 2372 CB LEU B 11 7988 6780 8679 1169 -501 -817 C ATOM 2373 CG LEU B 11 26.099 -24.696 3.310 1.00 64.31 C ANISOU 2373 CG LEU B 11 8414 6886 9137 1212 -794 -898 C ATOM 2374 CD1 LEU B 11 24.921 -25.242 4.067 1.00 70.11 C ANISOU 2374 CD1 LEU B 11 9279 7415 9944 1021 -932 -733 C ATOM 2375 CD2 LEU B 11 26.532 -25.639 2.209 1.00 68.38 C ANISOU 2375 CD2 LEU B 11 8900 7422 9659 1439 -968 -1148 C ATOM 2376 N SER B 12 22.693 -24.361 1.551 1.00 57.51 N ANISOU 2376 N SER B 12 7608 6076 8167 1057 -699 -743 N ATOM 2377 CA SER B 12 21.304 -24.425 1.979 1.00 64.61 C ANISOU 2377 CA SER B 12 8566 6883 9098 872 -726 -586 C ATOM 2378 C SER B 12 21.094 -25.588 2.931 1.00 68.90 C ANISOU 2378 C SER B 12 9220 7195 9764 752 -982 -522 C ATOM 2379 O SER B 12 21.552 -26.701 2.685 1.00 74.36 O ANISOU 2379 O SER B 12 9975 7732 10547 858 -1236 -647 O ATOM 2380 CB SER B 12 20.323 -24.436 0.794 1.00 69.33 C ANISOU 2380 CB SER B 12 9151 7539 9650 918 -728 -629 C ATOM 2381 OG SER B 12 20.208 -25.707 0.190 1.00 71.93 O ANISOU 2381 OG SER B 12 9545 7734 10049 1016 -993 -770 O ATOM 2382 N ALA B 13 20.422 -25.312 4.039 1.00 66.83 N ANISOU 2382 N ALA B 13 8972 6919 9499 529 -929 -327 N ATOM 2383 CA ALA B 13 20.327 -26.280 5.116 1.00 66.69 C ANISOU 2383 CA ALA B 13 9050 6721 9566 365 -1153 -208 C ATOM 2384 C ALA B 13 18.961 -26.330 5.792 1.00 64.91 C ANISOU 2384 C ALA B 13 8828 6519 9317 100 -1151 -4 C ATOM 2385 O ALA B 13 18.244 -25.333 5.874 1.00 60.33 O ANISOU 2385 O ALA B 13 8154 6125 8644 34 -920 52 O ATOM 2386 CB ALA B 13 21.411 -26.017 6.143 1.00 63.91 C ANISOU 2386 CB ALA B 13 8700 6372 9210 354 -1113 -178 C ATOM 2387 N SER B 14 18.631 -27.516 6.286 1.00 64.81 N ANISOU 2387 N SER B 14 8914 6318 9393 -53 -1433 105 N ATOM 2388 CA SER B 14 17.416 -27.750 7.044 1.00 63.21 C ANISOU 2388 CA SER B 14 8702 6158 9159 -349 -1468 328 C ATOM 2389 C SER B 14 17.613 -27.316 8.489 1.00 66.65 C ANISOU 2389 C SER B 14 9107 6720 9496 -531 -1358 490 C ATOM 2390 O SER B 14 18.687 -27.479 9.057 1.00 70.52 O ANISOU 2390 O SER B 14 9657 7126 10012 -485 -1427 480 O ATOM 2391 CB SER B 14 17.069 -29.234 7.011 1.00 61.48 C ANISOU 2391 CB SER B 14 8607 5671 9081 -471 -1852 412 C ATOM 2392 OG SER B 14 17.094 -29.724 5.681 1.00 65.98 O ANISOU 2392 OG SER B 14 9215 6102 9752 -257 -1995 211 O ATOM 2393 N VAL B 15 16.576 -26.751 9.087 1.00 64.89 N ANISOU 2393 N VAL B 15 8780 6724 9153 -728 -1191 620 N ATOM 2394 CA VAL B 15 16.625 -26.432 10.504 1.00 59.45 C ANISOU 2394 CA VAL B 15 8048 6198 8341 -921 -1106 769 C ATOM 2395 C VAL B 15 17.001 -27.677 11.286 1.00 59.83 C ANISOU 2395 C VAL B 15 8232 6055 8447 -1106 -1417 950 C ATOM 2396 O VAL B 15 16.441 -28.751 11.066 1.00 61.53 O ANISOU 2396 O VAL B 15 8523 6103 8752 -1248 -1679 1066 O ATOM 2397 CB VAL B 15 15.277 -25.880 11.004 1.00 59.32 C ANISOU 2397 CB VAL B 15 7877 6483 8180 -1124 -931 872 C ATOM 2398 CG1 VAL B 15 15.106 -26.131 12.495 1.00 53.29 C ANISOU 2398 CG1 VAL B 15 7086 5884 7278 -1412 -960 1085 C ATOM 2399 CG2 VAL B 15 15.168 -24.404 10.677 1.00 64.23 C ANISOU 2399 CG2 VAL B 15 8364 7306 8734 -940 -623 697 C ATOM 2400 N GLY B 16 17.978 -27.537 12.173 1.00 68.29 N ANISOU 2400 N GLY B 16 9341 7126 9481 -1102 -1416 976 N ATOM 2401 CA GLY B 16 18.389 -28.622 13.047 1.00 73.28 C ANISOU 2401 CA GLY B 16 10105 7583 10155 -1287 -1720 1169 C ATOM 2402 C GLY B 16 19.643 -29.372 12.632 1.00 72.60 C ANISOU 2402 C GLY B 16 10167 7159 10260 -1076 -1986 1047 C ATOM 2403 O GLY B 16 20.312 -29.963 13.480 1.00 83.56 O ANISOU 2403 O GLY B 16 11639 8448 11661 -1152 -2183 1151 O ATOM 2404 N ASP B 17 19.976 -29.358 11.344 1.00 63.50 N ANISOU 2404 N ASP B 17 9017 5884 9227 -791 -1987 802 N ATOM 2405 CA ASP B 17 21.238 -29.947 10.906 1.00 68.04 C ANISOU 2405 CA ASP B 17 9660 6259 9932 -532 -2179 609 C ATOM 2406 C ASP B 17 22.428 -28.982 11.143 1.00 72.25 C ANISOU 2406 C ASP B 17 10146 6874 10431 -351 -1976 475 C ATOM 2407 O ASP B 17 22.230 -27.777 11.303 1.00 68.78 O ANISOU 2407 O ASP B 17 9586 6695 9851 -357 -1639 464 O ATOM 2408 CB ASP B 17 21.144 -30.567 9.488 1.00 59.47 C ANISOU 2408 CB ASP B 17 8569 5081 8947 -314 -2301 395 C ATOM 2409 CG ASP B 17 21.230 -29.548 8.365 1.00 77.14 C ANISOU 2409 CG ASP B 17 10731 7405 11173 -81 -2043 182 C ATOM 2410 OD1 ASP B 17 21.897 -28.506 8.537 1.00 89.27 O ANISOU 2410 OD1 ASP B 17 12188 9105 12627 17 -1783 115 O ATOM 2411 OD2 ASP B 17 20.651 -29.808 7.285 1.00 75.46 O ANISOU 2411 OD2 ASP B 17 10503 7174 10993 7 -2081 76 O ATOM 2412 N THR B 18 23.644 -29.514 11.239 1.00 73.69 N ANISOU 2412 N THR B 18 10362 6951 10687 -190 -2141 355 N ATOM 2413 CA THR B 18 24.809 -28.677 11.552 1.00 71.89 C ANISOU 2413 CA THR B 18 10089 6781 10443 -41 -1986 246 C ATOM 2414 C THR B 18 25.658 -28.267 10.324 1.00 69.14 C ANISOU 2414 C THR B 18 9642 6499 10131 286 -1861 -54 C ATOM 2415 O THR B 18 25.829 -29.039 9.382 1.00 70.67 O ANISOU 2415 O THR B 18 9818 6663 10372 436 -1999 -215 O ATOM 2416 CB THR B 18 25.680 -29.317 12.654 1.00 71.22 C ANISOU 2416 CB THR B 18 10064 6624 10373 -102 -2197 323 C ATOM 2417 OG1 THR B 18 27.050 -28.961 12.449 1.00 68.78 O ANISOU 2417 OG1 THR B 18 9692 6340 10103 146 -2141 108 O ATOM 2418 CG2 THR B 18 25.552 -30.819 12.613 1.00 74.82 C ANISOU 2418 CG2 THR B 18 10588 6936 10902 -151 -2555 358 C ATOM 2419 N VAL B 19 26.187 -27.046 10.350 1.00 60.62 N ANISOU 2419 N VAL B 19 8452 5615 8968 364 -1564 -121 N ATOM 2420 CA VAL B 19 26.826 -26.452 9.182 1.00 62.84 C ANISOU 2420 CA VAL B 19 8614 6024 9238 611 -1395 -348 C ATOM 2421 C VAL B 19 28.184 -25.861 9.539 1.00 68.60 C ANISOU 2421 C VAL B 19 9260 6843 9960 725 -1298 -444 C ATOM 2422 O VAL B 19 28.359 -25.298 10.617 1.00 72.74 O ANISOU 2422 O VAL B 19 9783 7419 10437 594 -1209 -323 O ATOM 2423 CB VAL B 19 25.931 -25.347 8.571 1.00 70.51 C ANISOU 2423 CB VAL B 19 9494 7203 10093 567 -1088 -313 C ATOM 2424 CG1 VAL B 19 26.728 -24.408 7.691 1.00 73.41 C ANISOU 2424 CG1 VAL B 19 9726 7754 10411 750 -868 -469 C ATOM 2425 CG2 VAL B 19 24.793 -25.966 7.788 1.00 77.09 C ANISOU 2425 CG2 VAL B 19 10375 7967 10947 539 -1188 -302 C ATOM 2426 N THR B 20 29.151 -26.017 8.640 1.00 67.45 N ANISOU 2426 N THR B 20 9032 6738 9856 968 -1324 -673 N ATOM 2427 CA THR B 20 30.436 -25.351 8.773 1.00 68.60 C ANISOU 2427 CA THR B 20 9057 7022 9985 1079 -1199 -777 C ATOM 2428 C THR B 20 30.718 -24.536 7.523 1.00 70.70 C ANISOU 2428 C THR B 20 9162 7537 10164 1213 -957 -909 C ATOM 2429 O THR B 20 30.566 -25.025 6.391 1.00 75.85 O ANISOU 2429 O THR B 20 9780 8249 10789 1336 -1001 -1041 O ATOM 2430 CB THR B 20 31.597 -26.352 8.950 1.00 75.99 C ANISOU 2430 CB THR B 20 9978 7921 10973 1187 -1431 -908 C ATOM 2431 OG1 THR B 20 31.464 -27.034 10.198 1.00 81.77 O ANISOU 2431 OG1 THR B 20 10850 8450 11767 1038 -1657 -755 O ATOM 2432 CG2 THR B 20 32.938 -25.628 8.928 1.00 75.03 C ANISOU 2432 CG2 THR B 20 9701 7975 10833 1310 -1289 -1036 C ATOM 2433 N ILE B 21 31.130 -23.291 7.723 1.00 62.81 N ANISOU 2433 N ILE B 21 8058 6713 9094 1156 -705 -851 N ATOM 2434 CA ILE B 21 31.648 -22.510 6.617 1.00 64.40 C ANISOU 2434 CA ILE B 21 8093 7164 9211 1258 -501 -947 C ATOM 2435 C ILE B 21 33.137 -22.214 6.855 1.00 65.95 C ANISOU 2435 C ILE B 21 8155 7480 9424 1345 -471 -1051 C ATOM 2436 O ILE B 21 33.563 -22.072 7.988 1.00 71.73 O ANISOU 2436 O ILE B 21 8922 8121 10213 1269 -512 -986 O ATOM 2437 CB ILE B 21 30.772 -21.260 6.337 1.00 67.82 C ANISOU 2437 CB ILE B 21 8505 7706 9557 1115 -253 -786 C ATOM 2438 CG1 ILE B 21 30.998 -20.157 7.363 1.00 64.24 C ANISOU 2438 CG1 ILE B 21 8034 7265 9112 972 -120 -655 C ATOM 2439 CG2 ILE B 21 29.278 -21.653 6.292 1.00 62.28 C ANISOU 2439 CG2 ILE B 21 7932 6879 8853 1024 -310 -691 C ATOM 2440 CD1 ILE B 21 29.830 -19.202 7.433 1.00 60.17 C ANISOU 2440 CD1 ILE B 21 7550 6757 8556 830 26 -506 C ATOM 2441 N THR B 22 33.938 -22.180 5.796 1.00 65.99 N ANISOU 2441 N THR B 22 7992 7711 9369 1505 -410 -1222 N ATOM 2442 CA THR B 22 35.383 -22.007 5.954 1.00 72.05 C ANISOU 2442 CA THR B 22 8598 8627 10150 1596 -395 -1343 C ATOM 2443 C THR B 22 35.867 -20.682 5.372 1.00 70.94 C ANISOU 2443 C THR B 22 8275 8781 9897 1519 -119 -1271 C ATOM 2444 O THR B 22 35.221 -20.115 4.496 1.00 77.23 O ANISOU 2444 O THR B 22 9049 9706 10591 1462 30 -1189 O ATOM 2445 CB THR B 22 36.212 -23.197 5.356 1.00 69.97 C ANISOU 2445 CB THR B 22 8273 8449 9862 1768 -580 -1570 C ATOM 2446 OG1 THR B 22 35.460 -23.865 4.339 1.00 67.38 O ANISOU 2446 OG1 THR B 22 7993 8141 9469 1827 -643 -1637 O ATOM 2447 CG2 THR B 22 36.559 -24.208 6.432 1.00 69.84 C ANISOU 2447 CG2 THR B 22 8384 8183 9969 1770 -856 -1591 C ATOM 2448 N CYS B 23 36.990 -20.188 5.891 1.00 63.76 N ANISOU 2448 N CYS B 23 7242 7965 9017 1500 -73 -1284 N ATOM 2449 CA CYS B 23 37.601 -18.931 5.445 1.00 60.81 C ANISOU 2449 CA CYS B 23 6687 7858 8561 1395 154 -1192 C ATOM 2450 C CYS B 23 39.131 -19.057 5.394 1.00 64.23 C ANISOU 2450 C CYS B 23 6895 8516 8993 1504 142 -1361 C ATOM 2451 O CYS B 23 39.755 -19.444 6.376 1.00 65.01 O ANISOU 2451 O CYS B 23 7018 8477 9208 1549 5 -1431 O ATOM 2452 CB CYS B 23 37.192 -17.784 6.377 1.00 49.74 C ANISOU 2452 CB CYS B 23 5376 6303 7219 1173 246 -958 C ATOM 2453 SG CYS B 23 37.491 -16.122 5.758 1.00113.82 S ANISOU 2453 SG CYS B 23 13337 14644 15267 989 479 -771 S ATOM 2454 N ARG B 24 39.728 -18.718 4.254 1.00 65.13 N ANISOU 2454 N ARG B 24 6779 9002 8963 1538 283 -1422 N ATOM 2455 CA ARG B 24 41.158 -18.924 4.020 1.00 67.74 C ANISOU 2455 CA ARG B 24 6857 9625 9257 1652 280 -1610 C ATOM 2456 C ARG B 24 41.902 -17.607 3.705 1.00 71.45 C ANISOU 2456 C ARG B 24 7099 10406 9643 1463 502 -1452 C ATOM 2457 O ARG B 24 41.674 -16.989 2.671 1.00 82.86 O ANISOU 2457 O ARG B 24 8446 12110 10929 1363 665 -1337 O ATOM 2458 CB ARG B 24 41.325 -19.916 2.862 1.00 75.69 C ANISOU 2458 CB ARG B 24 7832 10819 10107 1797 206 -1795 C ATOM 2459 CG ARG B 24 42.705 -20.513 2.712 1.00 93.82 C ANISOU 2459 CG ARG B 24 9970 13319 12358 1907 114 -2005 C ATOM 2460 CD ARG B 24 42.851 -21.233 1.382 1.00108.27 C ANISOU 2460 CD ARG B 24 11718 15420 14002 2031 80 -2193 C ATOM 2461 NE ARG B 24 42.858 -20.297 0.258 1.00120.55 N ANISOU 2461 NE ARG B 24 13092 17367 15343 1917 327 -2076 N ATOM 2462 CZ ARG B 24 43.964 -19.804 -0.297 1.00132.08 C ANISOU 2462 CZ ARG B 24 14298 19233 16653 1862 453 -2094 C ATOM 2463 NH1 ARG B 24 45.159 -20.158 0.164 1.00135.49 N ANISOU 2463 NH1 ARG B 24 14616 19733 17132 1935 362 -2253 N ATOM 2464 NH2 ARG B 24 43.877 -18.957 -1.314 1.00135.50 N ANISOU 2464 NH2 ARG B 24 14591 20010 16882 1719 658 -1941 N ATOM 2465 N ALA B 25 42.800 -17.183 4.586 1.00 61.76 N ANISOU 2465 N ALA B 25 5795 9149 8520 1392 487 -1426 N ATOM 2466 CA ALA B 25 43.583 -15.964 4.363 1.00 56.72 C ANISOU 2466 CA ALA B 25 4945 8776 7829 1185 658 -1260 C ATOM 2467 C ALA B 25 44.841 -16.201 3.504 1.00 58.57 C ANISOU 2467 C ALA B 25 4861 9483 7912 1265 720 -1424 C ATOM 2468 O ALA B 25 45.513 -17.215 3.637 1.00 61.45 O ANISOU 2468 O ALA B 25 5232 9835 8281 1447 569 -1651 O ATOM 2469 CB ALA B 25 43.955 -15.340 5.698 1.00 55.27 C ANISOU 2469 CB ALA B 25 4834 8338 7828 1052 603 -1148 C ATOM 2470 N SER B 26 45.164 -15.262 2.622 1.00 63.64 N ANISOU 2470 N SER B 26 5310 10474 8397 1071 905 -1248 N ATOM 2471 CA SER B 26 46.272 -15.458 1.681 1.00 73.29 C ANISOU 2471 CA SER B 26 6322 12105 9420 1084 952 -1340 C ATOM 2472 C SER B 26 47.648 -15.313 2.345 1.00 86.23 C ANISOU 2472 C SER B 26 7787 13837 11139 1060 916 -1405 C ATOM 2473 O SER B 26 48.693 -15.517 1.715 1.00 85.35 O ANISOU 2473 O SER B 26 7484 14068 10879 1085 939 -1516 O ATOM 2474 CB SER B 26 46.157 -14.480 0.511 1.00 71.95 C ANISOU 2474 CB SER B 26 6024 12273 9042 849 1142 -1091 C ATOM 2475 OG SER B 26 46.675 -13.207 0.860 1.00 71.20 O ANISOU 2475 OG SER B 26 5795 12245 9010 563 1237 -825 O ATOM 2476 N GLU B 27 47.630 -14.915 3.612 1.00 91.50 N ANISOU 2476 N GLU B 27 8514 14216 12036 1004 858 -1341 N ATOM 2477 CA GLU B 27 48.833 -14.754 4.414 1.00 90.99 C ANISOU 2477 CA GLU B 27 8310 14180 12083 982 801 -1398 C ATOM 2478 C GLU B 27 48.553 -15.236 5.824 1.00 86.72 C ANISOU 2478 C GLU B 27 7959 13211 11782 1112 616 -1507 C ATOM 2479 O GLU B 27 47.405 -15.495 6.179 1.00 90.17 O ANISOU 2479 O GLU B 27 8620 13341 12299 1169 558 -1492 O ATOM 2480 CB GLU B 27 49.282 -13.303 4.426 1.00 99.44 C ANISOU 2480 CB GLU B 27 9196 15413 13173 658 943 -1115 C ATOM 2481 CG GLU B 27 49.978 -12.885 3.149 1.00113.81 C ANISOU 2481 CG GLU B 27 10804 17686 14754 514 1086 -1013 C ATOM 2482 CD GLU B 27 50.649 -11.538 3.277 1.00123.43 C ANISOU 2482 CD GLU B 27 11851 19026 16022 179 1168 -730 C ATOM 2483 OE1 GLU B 27 50.675 -10.982 4.399 1.00124.72 O ANISOU 2483 OE1 GLU B 27 12040 18931 16415 79 1102 -651 O ATOM 2484 OE2 GLU B 27 51.148 -11.033 2.253 1.00128.32 O ANISOU 2484 OE2 GLU B 27 12315 19993 16448 7 1279 -588 O ATOM 2485 N PHE B 28 49.584 -15.344 6.647 1.00 79.60 N ANISOU 2485 N PHE B 28 6973 12280 10989 1148 514 -1607 N ATOM 2486 CA PHE B 28 49.380 -15.965 7.938 1.00 79.26 C ANISOU 2486 CA PHE B 28 7131 11839 11143 1286 304 -1720 C ATOM 2487 C PHE B 28 48.952 -14.881 8.916 1.00 74.68 C ANISOU 2487 C PHE B 28 6673 10984 10717 1062 324 -1486 C ATOM 2488 O PHE B 28 49.731 -13.999 9.267 1.00 83.63 O ANISOU 2488 O PHE B 28 7660 12206 11911 892 366 -1387 O ATOM 2489 CB PHE B 28 50.679 -16.631 8.388 1.00 81.83 C ANISOU 2489 CB PHE B 28 7364 12226 11500 1423 154 -1926 C ATOM 2490 CG PHE B 28 50.508 -17.625 9.499 1.00 74.89 C ANISOU 2490 CG PHE B 28 6724 10961 10770 1598 -109 -2064 C ATOM 2491 CD1 PHE B 28 50.412 -17.201 10.818 1.00 68.79 C ANISOU 2491 CD1 PHE B 28 6045 9905 10187 1530 -201 -1984 C ATOM 2492 CD2 PHE B 28 50.476 -18.983 9.227 1.00 70.51 C ANISOU 2492 CD2 PHE B 28 6296 10329 10166 1811 -288 -2268 C ATOM 2493 CE1 PHE B 28 50.270 -18.108 11.840 1.00 66.21 C ANISOU 2493 CE1 PHE B 28 5946 9241 9971 1662 -454 -2073 C ATOM 2494 CE2 PHE B 28 50.336 -19.902 10.248 1.00 68.46 C ANISOU 2494 CE2 PHE B 28 6262 9710 10040 1929 -556 -2354 C ATOM 2495 CZ PHE B 28 50.234 -19.464 11.559 1.00 66.67 C ANISOU 2495 CZ PHE B 28 6137 9219 9976 1849 -634 -2241 C ATOM 2496 N ILE B 29 47.684 -14.936 9.311 1.00 63.14 N ANISOU 2496 N ILE B 29 5532 9169 9290 1035 282 -1371 N ATOM 2497 CA ILE B 29 47.101 -13.963 10.230 1.00 64.38 C ANISOU 2497 CA ILE B 29 5889 9022 9550 829 281 -1149 C ATOM 2498 C ILE B 29 46.932 -14.378 11.699 1.00 63.23 C ANISOU 2498 C ILE B 29 5964 8527 9534 888 92 -1198 C ATOM 2499 O ILE B 29 46.353 -13.616 12.467 1.00 51.01 O ANISOU 2499 O ILE B 29 4580 6753 8049 741 90 -1048 O ATOM 2500 CB ILE B 29 45.765 -13.418 9.702 1.00 68.50 C ANISOU 2500 CB ILE B 29 6584 9433 10009 706 389 -952 C ATOM 2501 CG1 ILE B 29 44.725 -14.538 9.592 1.00 53.16 C ANISOU 2501 CG1 ILE B 29 4851 7328 8020 878 312 -1045 C ATOM 2502 CG2 ILE B 29 45.984 -12.724 8.358 1.00 77.93 C ANISOU 2502 CG2 ILE B 29 7565 10970 11075 576 570 -831 C ATOM 2503 CD1 ILE B 29 43.331 -14.046 9.633 1.00 40.37 C ANISOU 2503 CD1 ILE B 29 3457 5491 6391 765 361 -868 C ATOM 2504 N TYR B 30 47.396 -15.576 12.072 1.00 69.93 N ANISOU 2504 N TYR B 30 6817 9339 10416 1105 -81 -1410 N ATOM 2505 CA TYR B 30 47.265 -16.107 13.446 1.00 71.32 C ANISOU 2505 CA TYR B 30 7205 9204 10691 1157 -289 -1441 C ATOM 2506 C TYR B 30 45.787 -16.291 13.835 1.00 76.15 C ANISOU 2506 C TYR B 30 8123 9540 11271 1104 -313 -1311 C ATOM 2507 O TYR B 30 45.064 -17.029 13.162 1.00 75.64 O ANISOU 2507 O TYR B 30 8139 9458 11144 1195 -322 -1343 O ATOM 2508 CB TYR B 30 48.027 -15.220 14.443 1.00 67.73 C ANISOU 2508 CB TYR B 30 6692 8711 10333 1026 -312 -1386 C ATOM 2509 CG TYR B 30 49.411 -14.837 13.948 1.00 68.41 C ANISOU 2509 CG TYR B 30 6443 9109 10441 1023 -251 -1473 C ATOM 2510 CD1 TYR B 30 50.495 -15.703 14.097 1.00 72.39 C ANISOU 2510 CD1 TYR B 30 6789 9725 10991 1220 -398 -1703 C ATOM 2511 CD2 TYR B 30 49.632 -13.618 13.312 1.00 67.08 C ANISOU 2511 CD2 TYR B 30 6104 9134 10250 816 -63 -1321 C ATOM 2512 CE1 TYR B 30 51.763 -15.361 13.632 1.00 70.26 C ANISOU 2512 CE1 TYR B 30 6176 9792 10728 1215 -332 -1796 C ATOM 2513 CE2 TYR B 30 50.890 -13.275 12.838 1.00 68.96 C ANISOU 2513 CE2 TYR B 30 6012 9700 10489 779 -2 -1376 C ATOM 2514 CZ TYR B 30 51.948 -14.151 13.003 1.00 68.67 C ANISOU 2514 CZ TYR B 30 5799 9809 10482 981 -124 -1623 C ATOM 2515 OH TYR B 30 53.189 -13.806 12.537 1.00 67.61 O ANISOU 2515 OH TYR B 30 5306 10044 10337 940 -54 -1688 O ATOM 2516 N SER B 31 45.355 -15.688 14.941 1.00 79.60 N ANISOU 2516 N SER B 31 8717 9783 11746 968 -339 -1187 N ATOM 2517 CA SER B 31 43.951 -15.287 15.107 1.00 78.88 C ANISOU 2517 CA SER B 31 8829 9541 11602 851 -267 -1034 C ATOM 2518 C SER B 31 44.008 -13.836 14.660 1.00 85.65 C ANISOU 2518 C SER B 31 9569 10498 12475 689 -90 -918 C ATOM 2519 O SER B 31 45.067 -13.435 14.189 1.00 96.37 O ANISOU 2519 O SER B 31 10709 12042 13866 671 -40 -950 O ATOM 2520 CB SER B 31 43.507 -15.470 16.540 1.00 72.08 C ANISOU 2520 CB SER B 31 8167 8468 10750 809 -404 -995 C ATOM 2521 OG SER B 31 43.829 -16.790 16.951 1.00 69.01 O ANISOU 2521 OG SER B 31 7848 7996 10375 945 -614 -1090 O ATOM 2522 N SER B 32 42.986 -13.006 14.860 1.00 77.19 N ANISOU 2522 N SER B 32 8622 9311 11396 563 -19 -790 N ATOM 2523 CA SER B 32 42.865 -11.787 14.018 1.00 73.69 C ANISOU 2523 CA SER B 32 8080 8952 10969 427 128 -666 C ATOM 2524 C SER B 32 41.888 -11.968 12.869 1.00 64.56 C ANISOU 2524 C SER B 32 6965 7846 9717 439 233 -599 C ATOM 2525 O SER B 32 41.875 -11.198 11.927 1.00 64.60 O ANISOU 2525 O SER B 32 6872 7964 9708 343 342 -492 O ATOM 2526 CB SER B 32 44.213 -11.300 13.446 1.00 72.79 C ANISOU 2526 CB SER B 32 7708 9053 10896 373 175 -666 C ATOM 2527 OG SER B 32 44.995 -10.613 14.407 1.00 69.21 O ANISOU 2527 OG SER B 32 7203 8533 10560 292 98 -673 O ATOM 2528 N LEU B 33 41.172 -13.074 12.907 1.00 63.37 N ANISOU 2528 N LEU B 33 6950 7628 9499 556 180 -661 N ATOM 2529 CA LEU B 33 40.017 -13.314 12.052 1.00 57.09 C ANISOU 2529 CA LEU B 33 6240 6829 8620 571 250 -607 C ATOM 2530 C LEU B 33 38.698 -13.138 12.818 1.00 49.68 C ANISOU 2530 C LEU B 33 5502 5697 7678 516 226 -544 C ATOM 2531 O LEU B 33 38.514 -13.717 13.875 1.00 48.42 O ANISOU 2531 O LEU B 33 5455 5425 7518 541 118 -586 O ATOM 2532 CB LEU B 33 40.125 -14.742 11.524 1.00 56.84 C ANISOU 2532 CB LEU B 33 6209 6859 8529 742 179 -736 C ATOM 2533 CG LEU B 33 39.022 -15.293 10.659 1.00 54.04 C ANISOU 2533 CG LEU B 33 5944 6498 8091 790 209 -720 C ATOM 2534 CD1 LEU B 33 37.868 -15.683 11.541 1.00 52.10 C ANISOU 2534 CD1 LEU B 33 5915 6030 7849 758 126 -672 C ATOM 2535 CD2 LEU B 33 38.653 -14.243 9.640 1.00 53.56 C ANISOU 2535 CD2 LEU B 33 5809 6561 7982 686 375 -595 C ATOM 2536 N THR B 34 37.765 -12.358 12.284 1.00 55.37 N ANISOU 2536 N THR B 34 6257 6397 8385 440 319 -443 N ATOM 2537 CA THR B 34 36.432 -12.251 12.907 1.00 56.29 C ANISOU 2537 CA THR B 34 6530 6377 8480 409 305 -413 C ATOM 2538 C THR B 34 35.294 -12.655 11.965 1.00 58.72 C ANISOU 2538 C THR B 34 6900 6699 8711 437 359 -371 C ATOM 2539 O THR B 34 35.502 -12.839 10.764 1.00 59.76 O ANISOU 2539 O THR B 34 6958 6944 8805 473 416 -356 O ATOM 2540 CB THR B 34 36.144 -10.871 13.543 1.00 50.80 C ANISOU 2540 CB THR B 34 5843 5596 7865 311 316 -374 C ATOM 2541 OG1 THR B 34 35.567 -10.006 12.575 1.00 53.30 O ANISOU 2541 OG1 THR B 34 6136 5912 8205 259 389 -281 O ATOM 2542 CG2 THR B 34 37.411 -10.254 14.047 1.00 58.72 C ANISOU 2542 CG2 THR B 34 6744 6604 8963 268 274 -398 C ATOM 2543 N TRP B 35 34.112 -12.847 12.544 1.00 54.08 N ANISOU 2543 N TRP B 35 6436 6025 8087 419 336 -361 N ATOM 2544 CA TRP B 35 32.957 -13.374 11.829 1.00 49.52 C ANISOU 2544 CA TRP B 35 5926 5447 7441 442 362 -330 C ATOM 2545 C TRP B 35 31.754 -12.495 12.052 1.00 59.76 C ANISOU 2545 C TRP B 35 7266 6699 8743 381 408 -289 C ATOM 2546 O TRP B 35 31.450 -12.126 13.180 1.00 60.67 O ANISOU 2546 O TRP B 35 7412 6776 8863 342 380 -320 O ATOM 2547 CB TRP B 35 32.614 -14.761 12.338 1.00 45.08 C ANISOU 2547 CB TRP B 35 5465 4840 6824 477 254 -363 C ATOM 2548 CG TRP B 35 33.498 -15.789 11.825 1.00 49.84 C ANISOU 2548 CG TRP B 35 6038 5468 7431 579 176 -431 C ATOM 2549 CD1 TRP B 35 34.522 -16.374 12.478 1.00 52.79 C ANISOU 2549 CD1 TRP B 35 6400 5816 7840 625 62 -498 C ATOM 2550 CD2 TRP B 35 33.456 -16.376 10.519 1.00 54.39 C ANISOU 2550 CD2 TRP B 35 6579 6111 7975 672 186 -471 C ATOM 2551 NE1 TRP B 35 35.137 -17.295 11.662 1.00 60.20 N ANISOU 2551 NE1 TRP B 35 7292 6797 8785 756 -8 -593 N ATOM 2552 CE2 TRP B 35 34.494 -17.316 10.455 1.00 55.14 C ANISOU 2552 CE2 TRP B 35 6633 6223 8094 788 71 -586 C ATOM 2553 CE3 TRP B 35 32.639 -16.196 9.402 1.00 52.24 C ANISOU 2553 CE3 TRP B 35 6302 5893 7653 679 270 -434 C ATOM 2554 CZ2 TRP B 35 34.741 -18.069 9.326 1.00 56.51 C ANISOU 2554 CZ2 TRP B 35 6750 6483 8239 923 39 -691 C ATOM 2555 CZ3 TRP B 35 32.878 -16.948 8.291 1.00 56.48 C ANISOU 2555 CZ3 TRP B 35 6794 6517 8148 795 245 -516 C ATOM 2556 CH2 TRP B 35 33.922 -17.871 8.254 1.00 62.32 C ANISOU 2556 CH2 TRP B 35 7483 7290 8908 922 133 -655 C ATOM 2557 N TYR B 36 31.052 -12.172 10.974 1.00 64.98 N ANISOU 2557 N TYR B 36 7918 7379 9391 385 470 -235 N ATOM 2558 CA TYR B 36 29.857 -11.357 11.087 1.00 57.38 C ANISOU 2558 CA TYR B 36 6986 6369 8446 352 494 -216 C ATOM 2559 C TYR B 36 28.658 -12.067 10.489 1.00 55.99 C ANISOU 2559 C TYR B 36 6866 6214 8193 376 507 -199 C ATOM 2560 O TYR B 36 28.780 -12.802 9.520 1.00 57.07 O ANISOU 2560 O TYR B 36 7005 6395 8286 418 513 -179 O ATOM 2561 CB TYR B 36 30.063 -10.034 10.381 1.00 52.35 C ANISOU 2561 CB TYR B 36 6287 5703 7899 317 522 -149 C ATOM 2562 CG TYR B 36 31.248 -9.231 10.864 1.00 55.36 C ANISOU 2562 CG TYR B 36 6603 6053 8379 270 493 -147 C ATOM 2563 CD1 TYR B 36 31.219 -8.562 12.076 1.00 53.72 C ANISOU 2563 CD1 TYR B 36 6406 5763 8243 255 434 -225 C ATOM 2564 CD2 TYR B 36 32.378 -9.106 10.078 1.00 61.79 C ANISOU 2564 CD2 TYR B 36 7327 6944 9207 236 521 -74 C ATOM 2565 CE1 TYR B 36 32.288 -7.812 12.492 1.00 55.15 C ANISOU 2565 CE1 TYR B 36 6527 5898 8529 208 388 -227 C ATOM 2566 CE2 TYR B 36 33.459 -8.363 10.487 1.00 61.57 C ANISOU 2566 CE2 TYR B 36 7223 6893 9275 171 487 -59 C ATOM 2567 CZ TYR B 36 33.411 -7.720 11.691 1.00 62.11 C ANISOU 2567 CZ TYR B 36 7321 6839 9437 157 413 -133 C ATOM 2568 OH TYR B 36 34.505 -6.981 12.080 1.00 68.88 O ANISOU 2568 OH TYR B 36 8104 7662 10406 88 360 -121 O ATOM 2569 N GLN B 37 27.493 -11.846 11.074 1.00 58.09 N ANISOU 2569 N GLN B 37 7162 6468 8441 354 505 -224 N ATOM 2570 CA GLN B 37 26.257 -12.386 10.524 1.00 58.64 C ANISOU 2570 CA GLN B 37 7267 6563 8449 361 515 -204 C ATOM 2571 C GLN B 37 25.348 -11.257 10.053 1.00 51.33 C ANISOU 2571 C GLN B 37 6311 5617 7576 373 544 -200 C ATOM 2572 O GLN B 37 25.002 -10.359 10.819 1.00 47.80 O ANISOU 2572 O GLN B 37 5832 5152 7176 370 532 -264 O ATOM 2573 CB GLN B 37 25.537 -13.215 11.575 1.00 60.99 C ANISOU 2573 CB GLN B 37 7606 6905 8663 309 477 -227 C ATOM 2574 CG GLN B 37 24.281 -13.894 11.082 1.00 60.48 C ANISOU 2574 CG GLN B 37 7568 6873 8539 291 471 -196 C ATOM 2575 CD GLN B 37 23.361 -14.188 12.222 1.00 59.58 C ANISOU 2575 CD GLN B 37 7448 6853 8338 204 458 -208 C ATOM 2576 OE1 GLN B 37 23.198 -13.352 13.100 1.00 56.34 O ANISOU 2576 OE1 GLN B 37 6981 6509 7918 194 490 -277 O ATOM 2577 NE2 GLN B 37 22.772 -15.381 12.242 1.00 60.22 N ANISOU 2577 NE2 GLN B 37 7576 6955 8350 133 398 -144 N ATOM 2578 N GLN B 38 24.965 -11.292 8.787 1.00 52.93 N ANISOU 2578 N GLN B 38 6519 5822 7771 400 562 -140 N ATOM 2579 CA GLN B 38 24.094 -10.244 8.276 1.00 61.47 C ANISOU 2579 CA GLN B 38 7580 6864 8913 416 558 -125 C ATOM 2580 C GLN B 38 22.768 -10.786 7.745 1.00 60.72 C ANISOU 2580 C GLN B 38 7504 6810 8758 437 560 -128 C ATOM 2581 O GLN B 38 22.735 -11.521 6.748 1.00 60.20 O ANISOU 2581 O GLN B 38 7465 6776 8632 453 567 -77 O ATOM 2582 CB GLN B 38 24.802 -9.412 7.209 1.00 59.25 C ANISOU 2582 CB GLN B 38 7277 6544 8691 405 557 -19 C ATOM 2583 CG GLN B 38 23.876 -8.466 6.481 1.00 57.06 C ANISOU 2583 CG GLN B 38 7000 6204 8477 419 515 28 C ATOM 2584 CD GLN B 38 24.626 -7.501 5.617 1.00 64.95 C ANISOU 2584 CD GLN B 38 7980 7157 9541 365 485 170 C ATOM 2585 OE1 GLN B 38 25.236 -7.880 4.624 1.00 64.71 O ANISOU 2585 OE1 GLN B 38 7935 7231 9422 336 531 272 O ATOM 2586 NE2 GLN B 38 24.601 -6.237 5.997 1.00 76.88 N ANISOU 2586 NE2 GLN B 38 9482 8524 11204 346 392 175 N ATOM 2587 N LYS B 39 21.684 -10.432 8.438 1.00 56.20 N ANISOU 2587 N LYS B 39 6901 6258 8196 443 547 -208 N ATOM 2588 CA LYS B 39 20.333 -10.807 8.022 1.00 58.41 C ANISOU 2588 CA LYS B 39 7171 6591 8430 456 544 -221 C ATOM 2589 C LYS B 39 19.836 -9.868 6.923 1.00 70.48 C ANISOU 2589 C LYS B 39 8691 8051 10036 512 512 -185 C ATOM 2590 O LYS B 39 20.325 -8.738 6.798 1.00 73.47 O ANISOU 2590 O LYS B 39 9062 8333 10521 530 474 -166 O ATOM 2591 CB LYS B 39 19.378 -10.872 9.219 1.00 47.19 C ANISOU 2591 CB LYS B 39 5688 5281 6963 431 551 -329 C ATOM 2592 CG LYS B 39 19.390 -12.233 9.898 1.00 51.85 C ANISOU 2592 CG LYS B 39 6304 5963 7432 336 559 -297 C ATOM 2593 CD LYS B 39 19.468 -12.095 11.409 1.00 62.57 C ANISOU 2593 CD LYS B 39 7611 7432 8731 286 573 -373 C ATOM 2594 CE LYS B 39 19.742 -13.433 12.082 1.00 68.77 C ANISOU 2594 CE LYS B 39 8448 8277 9405 166 547 -292 C ATOM 2595 NZ LYS B 39 19.791 -13.288 13.573 1.00 75.45 N ANISOU 2595 NZ LYS B 39 9239 9271 10157 101 560 -350 N ATOM 2596 N GLN B 40 18.896 -10.344 6.109 1.00 73.31 N ANISOU 2596 N GLN B 40 9058 8447 10351 529 504 -162 N ATOM 2597 CA GLN B 40 18.495 -9.593 4.925 1.00 79.70 C ANISOU 2597 CA GLN B 40 9875 9195 11215 576 458 -99 C ATOM 2598 C GLN B 40 18.017 -8.202 5.303 1.00 76.64 C ANISOU 2598 C GLN B 40 9439 8718 10962 627 385 -167 C ATOM 2599 O GLN B 40 17.140 -8.042 6.156 1.00 71.40 O ANISOU 2599 O GLN B 40 8706 8107 10315 665 373 -310 O ATOM 2600 CB GLN B 40 17.426 -10.335 4.129 1.00 92.62 C ANISOU 2600 CB GLN B 40 11517 10891 12782 593 448 -91 C ATOM 2601 CG GLN B 40 17.284 -9.865 2.690 1.00101.95 C ANISOU 2601 CG GLN B 40 12730 12034 13972 629 402 10 C ATOM 2602 CD GLN B 40 17.022 -11.016 1.725 1.00114.05 C ANISOU 2602 CD GLN B 40 14300 13647 15389 634 410 41 C ATOM 2603 OE1 GLN B 40 16.546 -12.093 2.115 1.00111.80 O ANISOU 2603 OE1 GLN B 40 14013 13412 15054 615 417 -21 O ATOM 2604 NE2 GLN B 40 17.343 -10.794 0.454 1.00120.80 N ANISOU 2604 NE2 GLN B 40 15184 14519 16195 651 392 142 N ATOM 2605 N GLY B 41 18.625 -7.203 4.664 1.00 78.36 N ANISOU 2605 N GLY B 41 9686 8813 11276 626 320 -67 N ATOM 2606 CA GLY B 41 18.296 -5.805 4.883 1.00 72.56 C ANISOU 2606 CA GLY B 41 8927 7931 10711 679 191 -117 C ATOM 2607 C GLY B 41 18.746 -5.264 6.220 1.00 65.35 C ANISOU 2607 C GLY B 41 7974 6977 9881 694 170 -254 C ATOM 2608 O GLY B 41 18.407 -4.140 6.589 1.00 56.43 O ANISOU 2608 O GLY B 41 6812 5722 8907 766 38 -356 O ATOM 2609 N GLY B 42 19.492 -6.083 6.953 1.00 68.30 N ANISOU 2609 N GLY B 42 8346 7451 10152 639 277 -271 N ATOM 2610 CA GLY B 42 20.086 -5.665 8.206 1.00 70.11 C ANISOU 2610 CA GLY B 42 8543 7662 10433 642 263 -388 C ATOM 2611 C GLY B 42 21.552 -5.351 7.991 1.00 71.78 C ANISOU 2611 C GLY B 42 8796 7778 10700 564 252 -255 C ATOM 2612 O GLY B 42 22.108 -5.688 6.940 1.00 64.04 O ANISOU 2612 O GLY B 42 7853 6809 9671 503 290 -82 O ATOM 2613 N SER B 43 22.158 -4.691 8.981 1.00 74.40 N ANISOU 2613 N SER B 43 9104 8042 11124 569 197 -349 N ATOM 2614 CA SER B 43 23.589 -4.396 9.007 1.00 73.78 C ANISOU 2614 CA SER B 43 9041 7891 11102 485 184 -245 C ATOM 2615 C SER B 43 24.319 -5.531 9.718 1.00 68.55 C ANISOU 2615 C SER B 43 8374 7372 10298 448 302 -272 C ATOM 2616 O SER B 43 23.740 -6.180 10.575 1.00 78.41 O ANISOU 2616 O SER B 43 9609 8736 11447 483 349 -398 O ATOM 2617 CB SER B 43 23.821 -3.086 9.750 1.00 84.18 C ANISOU 2617 CB SER B 43 10335 9036 12613 515 29 -351 C ATOM 2618 OG SER B 43 23.103 -3.084 10.970 1.00 91.56 O ANISOU 2618 OG SER B 43 11220 10046 13521 618 20 -600 O ATOM 2619 N PRO B 44 25.593 -5.781 9.376 1.00 59.03 N ANISOU 2619 N PRO B 44 7173 6175 9079 372 338 -151 N ATOM 2620 CA PRO B 44 26.237 -6.963 9.953 1.00 58.84 C ANISOU 2620 CA PRO B 44 7152 6274 8930 358 421 -182 C ATOM 2621 C PRO B 44 26.363 -6.863 11.469 1.00 63.61 C ANISOU 2621 C PRO B 44 7740 6886 9541 376 392 -334 C ATOM 2622 O PRO B 44 26.517 -5.763 12.001 1.00 65.44 O ANISOU 2622 O PRO B 44 7946 7015 9901 389 305 -407 O ATOM 2623 CB PRO B 44 27.621 -6.954 9.306 1.00 48.86 C ANISOU 2623 CB PRO B 44 5861 5020 7682 290 441 -54 C ATOM 2624 CG PRO B 44 27.475 -6.108 8.114 1.00 49.46 C ANISOU 2624 CG PRO B 44 5930 5039 7823 248 405 89 C ATOM 2625 CD PRO B 44 26.511 -5.052 8.496 1.00 54.21 C ANISOU 2625 CD PRO B 44 6551 5489 8557 288 296 19 C ATOM 2626 N GLN B 45 26.274 -7.998 12.153 1.00 59.86 N ANISOU 2626 N GLN B 45 7284 6531 8930 373 443 -380 N ATOM 2627 CA GLN B 45 26.442 -8.029 13.593 1.00 65.31 C ANISOU 2627 CA GLN B 45 7958 7274 9581 372 419 -503 C ATOM 2628 C GLN B 45 27.630 -8.911 13.957 1.00 76.43 C ANISOU 2628 C GLN B 45 9390 8713 10936 330 426 -457 C ATOM 2629 O GLN B 45 27.965 -9.844 13.221 1.00 77.82 O ANISOU 2629 O GLN B 45 9596 8908 11064 319 456 -366 O ATOM 2630 CB GLN B 45 25.159 -8.503 14.275 1.00 74.88 C ANISOU 2630 CB GLN B 45 9158 8629 10662 383 445 -592 C ATOM 2631 CG GLN B 45 23.941 -7.610 14.006 1.00 88.88 C ANISOU 2631 CG GLN B 45 10882 10395 12494 452 424 -683 C ATOM 2632 CD GLN B 45 24.224 -6.118 14.240 1.00104.72 C ANISOU 2632 CD GLN B 45 12851 12261 14678 517 323 -791 C ATOM 2633 OE1 GLN B 45 25.362 -5.718 14.520 1.00114.20 O ANISOU 2633 OE1 GLN B 45 14062 13368 15962 491 276 -777 O ATOM 2634 NE2 GLN B 45 23.183 -5.292 14.128 1.00103.17 N ANISOU 2634 NE2 GLN B 45 12606 12040 14554 604 264 -909 N ATOM 2635 N LEU B 46 28.286 -8.595 15.074 1.00 77.01 N ANISOU 2635 N LEU B 46 9446 8789 11025 321 381 -540 N ATOM 2636 CA LEU B 46 29.470 -9.332 15.497 1.00 63.90 C ANISOU 2636 CA LEU B 46 7801 7145 9333 292 361 -510 C ATOM 2637 C LEU B 46 29.104 -10.745 15.984 1.00 64.57 C ANISOU 2637 C LEU B 46 7945 7329 9259 264 360 -483 C ATOM 2638 O LEU B 46 28.225 -10.928 16.833 1.00 62.33 O ANISOU 2638 O LEU B 46 7668 7149 8864 236 360 -530 O ATOM 2639 CB LEU B 46 30.239 -8.556 16.570 1.00 58.42 C ANISOU 2639 CB LEU B 46 7072 6423 8703 290 295 -609 C ATOM 2640 CG LEU B 46 31.503 -9.257 17.107 1.00 57.34 C ANISOU 2640 CG LEU B 46 6942 6301 8542 267 255 -592 C ATOM 2641 CD1 LEU B 46 32.627 -9.233 16.084 1.00 48.01 C ANISOU 2641 CD1 LEU B 46 5717 5063 7464 261 267 -505 C ATOM 2642 CD2 LEU B 46 31.975 -8.707 18.473 1.00 56.31 C ANISOU 2642 CD2 LEU B 46 6792 6185 8419 265 180 -713 C ATOM 2643 N LEU B 47 29.785 -11.743 15.432 1.00 67.17 N ANISOU 2643 N LEU B 47 8306 7636 9578 268 344 -409 N ATOM 2644 CA LEU B 47 29.492 -13.141 15.745 1.00 69.09 C ANISOU 2644 CA LEU B 47 8623 7917 9711 236 292 -362 C ATOM 2645 C LEU B 47 30.581 -13.795 16.604 1.00 66.94 C ANISOU 2645 C LEU B 47 8380 7630 9425 224 192 -366 C ATOM 2646 O LEU B 47 30.334 -14.191 17.744 1.00 63.95 O ANISOU 2646 O LEU B 47 8043 7312 8946 158 133 -358 O ATOM 2647 CB LEU B 47 29.260 -13.935 14.453 1.00 64.57 C ANISOU 2647 CB LEU B 47 8078 7310 9144 273 299 -301 C ATOM 2648 CG LEU B 47 27.884 -14.594 14.365 1.00 62.11 C ANISOU 2648 CG LEU B 47 7817 7038 8744 225 296 -255 C ATOM 2649 CD1 LEU B 47 28.045 -16.081 14.168 1.00 61.81 C ANISOU 2649 CD1 LEU B 47 7858 6947 8679 219 182 -202 C ATOM 2650 CD2 LEU B 47 27.063 -14.311 15.624 1.00 57.08 C ANISOU 2650 CD2 LEU B 47 7171 6509 8010 141 305 -274 C ATOM 2651 N VAL B 48 31.778 -13.900 16.031 1.00 64.97 N ANISOU 2651 N VAL B 48 8095 7325 9265 285 169 -378 N ATOM 2652 CA VAL B 48 32.962 -14.435 16.700 1.00 60.07 C ANISOU 2652 CA VAL B 48 7481 6681 8663 302 62 -403 C ATOM 2653 C VAL B 48 34.138 -13.487 16.468 1.00 63.85 C ANISOU 2653 C VAL B 48 7851 7154 9255 336 97 -455 C ATOM 2654 O VAL B 48 34.308 -12.974 15.371 1.00 68.54 O ANISOU 2654 O VAL B 48 8372 7760 9909 360 179 -440 O ATOM 2655 CB VAL B 48 33.302 -15.851 16.173 1.00 51.16 C ANISOU 2655 CB VAL B 48 6403 5501 7535 359 -46 -384 C ATOM 2656 CG1 VAL B 48 34.775 -16.158 16.312 1.00 41.87 C ANISOU 2656 CG1 VAL B 48 5176 4301 6432 433 -139 -449 C ATOM 2657 CG2 VAL B 48 32.474 -16.885 16.896 1.00 48.38 C ANISOU 2657 CG2 VAL B 48 6171 5124 7085 281 -159 -308 C ATOM 2658 N TYR B 49 34.926 -13.236 17.509 1.00 67.81 N ANISOU 2658 N TYR B 49 8337 7651 9778 320 29 -502 N ATOM 2659 CA TYR B 49 36.132 -12.414 17.391 1.00 68.18 C ANISOU 2659 CA TYR B 49 8272 7693 9942 332 37 -545 C ATOM 2660 C TYR B 49 37.328 -13.218 17.895 1.00 69.20 C ANISOU 2660 C TYR B 49 8387 7820 10088 377 -83 -588 C ATOM 2661 O TYR B 49 37.127 -14.152 18.668 1.00 84.52 O ANISOU 2661 O TYR B 49 10426 9738 11949 377 -191 -579 O ATOM 2662 CB TYR B 49 35.976 -11.094 18.161 1.00 64.76 C ANISOU 2662 CB TYR B 49 7814 7238 9553 280 48 -591 C ATOM 2663 CG TYR B 49 35.738 -11.214 19.660 1.00 71.09 C ANISOU 2663 CG TYR B 49 8680 8069 10262 257 -32 -652 C ATOM 2664 CD1 TYR B 49 34.484 -11.511 20.167 1.00 66.88 C ANISOU 2664 CD1 TYR B 49 8221 7602 9588 227 -15 -645 C ATOM 2665 CD2 TYR B 49 36.771 -10.992 20.571 1.00 83.57 C ANISOU 2665 CD2 TYR B 49 10230 9643 11881 255 -124 -717 C ATOM 2666 CE1 TYR B 49 34.270 -11.604 21.531 1.00 73.48 C ANISOU 2666 CE1 TYR B 49 9094 8527 10299 188 -78 -693 C ATOM 2667 CE2 TYR B 49 36.564 -11.081 21.941 1.00 82.89 C ANISOU 2667 CE2 TYR B 49 10196 9617 11680 229 -199 -772 C ATOM 2668 CZ TYR B 49 35.312 -11.386 22.413 1.00 80.40 C ANISOU 2668 CZ TYR B 49 9949 9398 11201 192 -171 -757 C ATOM 2669 OH TYR B 49 35.100 -11.469 23.770 1.00 81.72 O ANISOU 2669 OH TYR B 49 10149 9686 11216 152 -237 -805 O ATOM 2670 N ALA B 50 38.553 -12.900 17.459 1.00 57.98 N ANISOU 2670 N ALA B 50 6836 6429 8764 407 -79 -624 N ATOM 2671 CA ALA B 50 39.717 -13.687 17.902 1.00 62.41 C ANISOU 2671 CA ALA B 50 7364 6996 9354 474 -208 -691 C ATOM 2672 C ALA B 50 39.640 -15.092 17.318 1.00 65.99 C ANISOU 2672 C ALA B 50 7864 7441 9769 574 -283 -707 C ATOM 2673 O ALA B 50 40.348 -16.000 17.719 1.00 71.16 O ANISOU 2673 O ALA B 50 8532 8063 10445 651 -439 -766 O ATOM 2674 CB ALA B 50 39.851 -13.724 19.413 1.00 59.34 C ANISOU 2674 CB ALA B 50 7055 6559 8934 438 -330 -715 C ATOM 2675 N ALA B 51 38.644 -15.271 16.475 1.00 66.38 N ANISOU 2675 N ALA B 51 7959 7496 9768 573 -201 -656 N ATOM 2676 CA ALA B 51 38.464 -16.465 15.673 1.00 65.97 C ANISOU 2676 CA ALA B 51 7938 7432 9693 675 -265 -686 C ATOM 2677 C ALA B 51 37.900 -17.605 16.496 1.00 70.62 C ANISOU 2677 C ALA B 51 8699 7893 10239 665 -445 -648 C ATOM 2678 O ALA B 51 37.228 -18.488 15.954 1.00 63.85 O ANISOU 2678 O ALA B 51 7920 6982 9358 699 -504 -631 O ATOM 2679 CB ALA B 51 39.795 -16.877 15.077 1.00 56.53 C ANISOU 2679 CB ALA B 51 6592 6323 8562 806 -315 -812 C ATOM 2680 N THR B 52 38.148 -17.581 17.802 1.00 71.61 N ANISOU 2680 N THR B 52 8885 7973 10349 601 -545 -622 N ATOM 2681 CA THR B 52 37.505 -18.545 18.676 1.00 64.94 C ANISOU 2681 CA THR B 52 8208 7033 9433 535 -713 -532 C ATOM 2682 C THR B 52 36.441 -18.016 19.636 1.00 62.41 C ANISOU 2682 C THR B 52 7964 6765 8982 373 -645 -425 C ATOM 2683 O THR B 52 35.672 -18.805 20.188 1.00 64.23 O ANISOU 2683 O THR B 52 8319 6965 9121 280 -753 -314 O ATOM 2684 CB THR B 52 38.553 -19.351 19.440 1.00 59.16 C ANISOU 2684 CB THR B 52 7509 6216 8754 591 -951 -569 C ATOM 2685 OG1 THR B 52 39.266 -18.494 20.337 1.00 52.06 O ANISOU 2685 OG1 THR B 52 6548 5379 7855 554 -922 -600 O ATOM 2686 CG2 THR B 52 39.532 -19.959 18.453 1.00 60.07 C ANISOU 2686 CG2 THR B 52 7525 6307 8993 780 -1032 -716 C ATOM 2687 N ASN B 53 36.336 -16.697 19.784 1.00 60.49 N ANISOU 2687 N ASN B 53 7638 6613 8730 337 -478 -462 N ATOM 2688 CA ASN B 53 35.557 -16.130 20.898 1.00 64.22 C ANISOU 2688 CA ASN B 53 8152 7173 9077 220 -440 -425 C ATOM 2689 C ASN B 53 34.160 -15.631 20.520 1.00 63.67 C ANISOU 2689 C ASN B 53 8082 7175 8936 165 -290 -394 C ATOM 2690 O ASN B 53 34.005 -14.846 19.594 1.00 60.12 O ANISOU 2690 O ASN B 53 7559 6719 8565 213 -161 -437 O ATOM 2691 CB ASN B 53 36.345 -15.030 21.629 1.00 64.08 C ANISOU 2691 CB ASN B 53 8053 7197 9098 226 -416 -521 C ATOM 2692 CG ASN B 53 37.625 -15.555 22.285 1.00 77.17 C ANISOU 2692 CG ASN B 53 9715 8806 10798 263 -586 -549 C ATOM 2693 OD1 ASN B 53 37.730 -16.732 22.672 1.00 73.51 O ANISOU 2693 OD1 ASN B 53 9350 8292 10290 252 -754 -479 O ATOM 2694 ND2 ASN B 53 38.608 -14.674 22.413 1.00 82.39 N ANISOU 2694 ND2 ASN B 53 10271 9472 11562 302 -566 -646 N ATOM 2695 N LEU B 54 33.146 -16.098 21.241 1.00 60.21 N ANISOU 2695 N LEU B 54 7717 6820 8342 54 -319 -311 N ATOM 2696 CA LEU B 54 31.782 -15.691 20.944 1.00 56.80 C ANISOU 2696 CA LEU B 54 7265 6483 7834 6 -188 -296 C ATOM 2697 C LEU B 54 31.477 -14.296 21.498 1.00 59.27 C ANISOU 2697 C LEU B 54 7488 6913 8118 14 -77 -418 C ATOM 2698 O LEU B 54 32.005 -13.881 22.528 1.00 61.59 O ANISOU 2698 O LEU B 54 7763 7269 8370 3 -122 -484 O ATOM 2699 CB LEU B 54 30.782 -16.722 21.473 1.00 53.70 C ANISOU 2699 CB LEU B 54 6955 6172 7276 -135 -261 -156 C ATOM 2700 CG LEU B 54 30.876 -18.114 20.845 1.00 52.18 C ANISOU 2700 CG LEU B 54 6864 5823 7140 -143 -410 -40 C ATOM 2701 CD1 LEU B 54 29.822 -19.070 21.403 1.00 49.57 C ANISOU 2701 CD1 LEU B 54 6614 5566 6654 -327 -503 134 C ATOM 2702 CD2 LEU B 54 30.774 -18.034 19.331 1.00 45.93 C ANISOU 2702 CD2 LEU B 54 6040 4929 6482 -24 -330 -93 C ATOM 2703 N ALA B 55 30.639 -13.560 20.789 1.00 60.05 N ANISOU 2703 N ALA B 55 7533 7030 8254 47 44 -463 N ATOM 2704 CA ALA B 55 30.258 -12.229 21.216 1.00 64.17 C ANISOU 2704 CA ALA B 55 7970 7630 8781 81 112 -605 C ATOM 2705 C ALA B 55 29.262 -12.346 22.361 1.00 73.04 C ANISOU 2705 C ALA B 55 9075 8991 9684 0 122 -635 C ATOM 2706 O ALA B 55 28.704 -13.423 22.583 1.00 72.70 O ANISOU 2706 O ALA B 55 9085 9040 9496 -108 95 -503 O ATOM 2707 CB ALA B 55 29.675 -11.451 20.047 1.00 64.75 C ANISOU 2707 CB ALA B 55 7997 7627 8976 146 203 -635 C ATOM 2708 N ASP B 56 29.061 -11.251 23.097 1.00 79.72 N ANISOU 2708 N ASP B 56 9838 9949 10503 47 143 -811 N ATOM 2709 CA ASP B 56 28.058 -11.201 24.161 1.00 83.25 C ANISOU 2709 CA ASP B 56 10221 10694 10715 -9 173 -887 C ATOM 2710 C ASP B 56 26.726 -11.723 23.624 1.00 78.59 C ANISOU 2710 C ASP B 56 9613 10215 10032 -71 252 -802 C ATOM 2711 O ASP B 56 26.298 -11.328 22.534 1.00 73.02 O ANISOU 2711 O ASP B 56 8892 9380 9473 4 306 -820 O ATOM 2712 CB ASP B 56 27.862 -9.753 24.639 1.00 92.96 C ANISOU 2712 CB ASP B 56 11340 11995 11987 113 185 -1152 C ATOM 2713 CG ASP B 56 28.705 -9.397 25.864 1.00 99.20 C ANISOU 2713 CG ASP B 56 12114 12866 12711 125 100 -1271 C ATOM 2714 OD1 ASP B 56 28.295 -8.472 26.610 1.00100.01 O ANISOU 2714 OD1 ASP B 56 12114 13135 12749 205 94 -1509 O ATOM 2715 OD2 ASP B 56 29.768 -10.022 26.078 1.00 98.25 O ANISOU 2715 OD2 ASP B 56 12076 12648 12608 72 26 -1152 O ATOM 2716 N ALA B 57 26.091 -12.620 24.384 1.00 79.95 N ANISOU 2716 N ALA B 57 9786 10632 9959 -224 247 -693 N ATOM 2717 CA ALA B 57 24.746 -13.149 24.087 1.00 79.16 C ANISOU 2717 CA ALA B 57 9643 10699 9735 -320 315 -608 C ATOM 2718 C ALA B 57 24.562 -13.717 22.685 1.00 77.68 C ANISOU 2718 C ALA B 57 9534 10269 9714 -310 317 -473 C ATOM 2719 O ALA B 57 23.489 -13.583 22.091 1.00 72.87 O ANISOU 2719 O ALA B 57 8861 9724 9103 -301 392 -493 O ATOM 2720 CB ALA B 57 23.654 -12.107 24.384 1.00 77.72 C ANISOU 2720 CB ALA B 57 9287 10774 9468 -241 417 -837 C ATOM 2721 N VAL B 58 25.621 -14.331 22.164 1.00 77.23 N ANISOU 2721 N VAL B 58 9599 9948 9796 -295 228 -361 N ATOM 2722 CA VAL B 58 25.567 -15.115 20.933 1.00 67.45 C ANISOU 2722 CA VAL B 58 8441 8505 8680 -291 200 -234 C ATOM 2723 C VAL B 58 25.362 -16.558 21.366 1.00 70.86 C ANISOU 2723 C VAL B 58 8965 8973 8988 -470 77 -27 C ATOM 2724 O VAL B 58 26.065 -17.035 22.269 1.00 70.77 O ANISOU 2724 O VAL B 58 9011 8976 8904 -543 -34 42 O ATOM 2725 CB VAL B 58 26.883 -14.990 20.145 1.00 57.89 C ANISOU 2725 CB VAL B 58 7287 7030 7679 -163 157 -257 C ATOM 2726 CG1 VAL B 58 26.983 -16.042 19.057 1.00 50.27 C ANISOU 2726 CG1 VAL B 58 6407 5893 6801 -156 91 -143 C ATOM 2727 CG2 VAL B 58 27.017 -13.602 19.573 1.00 55.85 C ANISOU 2727 CG2 VAL B 58 6948 6714 7558 -27 253 -407 C ATOM 2728 N PRO B 59 24.395 -17.256 20.739 1.00 71.98 N ANISOU 2728 N PRO B 59 9122 9116 9111 -550 72 83 N ATOM 2729 CA PRO B 59 24.024 -18.595 21.210 1.00 76.29 C ANISOU 2729 CA PRO B 59 9749 9700 9539 -760 -72 304 C ATOM 2730 C PRO B 59 25.215 -19.571 21.159 1.00 81.41 C ANISOU 2730 C PRO B 59 10549 10082 10301 -750 -280 404 C ATOM 2731 O PRO B 59 25.985 -19.591 20.189 1.00 79.32 O ANISOU 2731 O PRO B 59 10328 9580 10230 -581 -308 327 O ATOM 2732 CB PRO B 59 22.915 -19.024 20.238 1.00 74.75 C ANISOU 2732 CB PRO B 59 9542 9480 9379 -799 -49 366 C ATOM 2733 CG PRO B 59 22.534 -17.795 19.479 1.00 73.56 C ANISOU 2733 CG PRO B 59 9283 9356 9312 -623 130 170 C ATOM 2734 CD PRO B 59 23.743 -16.928 19.460 1.00 71.08 C ANISOU 2734 CD PRO B 59 8973 8919 9115 -452 159 27 C ATOM 2735 N SER B 60 25.345 -20.381 22.206 1.00 81.91 N ANISOU 2735 N SER B 60 10681 10208 10232 -932 -435 574 N ATOM 2736 CA SER B 60 26.499 -21.247 22.383 1.00 79.25 C ANISOU 2736 CA SER B 60 10482 9632 9995 -918 -666 655 C ATOM 2737 C SER B 60 26.672 -22.192 21.210 1.00 75.63 C ANISOU 2737 C SER B 60 10125 8869 9741 -840 -819 689 C ATOM 2738 O SER B 60 27.727 -22.784 21.048 1.00 81.84 O ANISOU 2738 O SER B 60 11002 9425 10668 -743 -1002 674 O ATOM 2739 CB SER B 60 26.342 -22.075 23.649 1.00 87.56 C ANISOU 2739 CB SER B 60 11605 10807 10857 -1174 -842 887 C ATOM 2740 OG SER B 60 25.452 -23.154 23.408 1.00 97.55 O ANISOU 2740 OG SER B 60 12937 12026 12100 -1367 -980 1104 O ATOM 2741 N ARG B 61 25.642 -22.356 20.394 1.00 69.44 N ANISOU 2741 N ARG B 61 9318 8092 8975 -869 -760 713 N ATOM 2742 CA ARG B 61 25.745 -23.298 19.279 1.00 72.38 C ANISOU 2742 CA ARG B 61 9784 8187 9531 -790 -925 725 C ATOM 2743 C ARG B 61 26.753 -22.881 18.207 1.00 67.36 C ANISOU 2743 C ARG B 61 9124 7391 9077 -507 -871 508 C ATOM 2744 O ARG B 61 27.205 -23.718 17.430 1.00 67.13 O ANISOU 2744 O ARG B 61 9169 7139 9197 -400 -1045 473 O ATOM 2745 CB ARG B 61 24.375 -23.590 18.652 1.00 73.55 C ANISOU 2745 CB ARG B 61 9908 8386 9651 -895 -888 801 C ATOM 2746 CG ARG B 61 23.711 -22.396 17.996 1.00 67.00 C ANISOU 2746 CG ARG B 61 8937 7722 8798 -788 -602 647 C ATOM 2747 CD ARG B 61 22.307 -22.750 17.579 1.00 62.16 C ANISOU 2747 CD ARG B 61 8293 7190 8137 -922 -586 740 C ATOM 2748 NE ARG B 61 21.690 -21.663 16.835 1.00 60.51 N ANISOU 2748 NE ARG B 61 7959 7099 7934 -794 -351 584 N ATOM 2749 CZ ARG B 61 20.928 -20.732 17.392 1.00 62.02 C ANISOU 2749 CZ ARG B 61 8012 7568 7985 -844 -165 536 C ATOM 2750 NH1 ARG B 61 20.697 -20.771 18.704 1.00 68.36 N ANISOU 2750 NH1 ARG B 61 8770 8601 8601 -1025 -165 627 N ATOM 2751 NH2 ARG B 61 20.401 -19.768 16.642 1.00 47.88 N ANISOU 2751 NH2 ARG B 61 6123 5835 6236 -709 3 390 N ATOM 2752 N PHE B 62 27.096 -21.597 18.155 1.00 65.17 N ANISOU 2752 N PHE B 62 8736 7240 8787 -391 -644 359 N ATOM 2753 CA PHE B 62 28.146 -21.134 17.247 1.00 62.88 C ANISOU 2753 CA PHE B 62 8402 6846 8642 -164 -587 186 C ATOM 2754 C PHE B 62 29.546 -21.369 17.807 1.00 68.11 C ANISOU 2754 C PHE B 62 9094 7417 9367 -93 -721 143 C ATOM 2755 O PHE B 62 29.804 -21.214 19.005 1.00 72.88 O ANISOU 2755 O PHE B 62 9712 8096 9884 -189 -756 198 O ATOM 2756 CB PHE B 62 28.021 -19.651 16.982 1.00 57.04 C ANISOU 2756 CB PHE B 62 7537 6248 7887 -93 -333 72 C ATOM 2757 CG PHE B 62 26.769 -19.262 16.316 1.00 63.39 C ANISOU 2757 CG PHE B 62 8296 7134 8657 -118 -201 77 C ATOM 2758 CD1 PHE B 62 26.778 -18.863 14.993 1.00 61.64 C ANISOU 2758 CD1 PHE B 62 8032 6865 8525 17 -111 -5 C ATOM 2759 CD2 PHE B 62 25.584 -19.266 17.011 1.00 70.89 C ANISOU 2759 CD2 PHE B 62 9228 8238 9469 -278 -166 163 C ATOM 2760 CE1 PHE B 62 25.633 -18.488 14.370 1.00 58.37 C ANISOU 2760 CE1 PHE B 62 7577 6516 8084 2 -8 -1 C ATOM 2761 CE2 PHE B 62 24.432 -18.889 16.393 1.00 74.06 C ANISOU 2761 CE2 PHE B 62 9570 8722 9847 -287 -53 149 C ATOM 2762 CZ PHE B 62 24.457 -18.501 15.065 1.00 68.92 C ANISOU 2762 CZ PHE B 62 8896 7984 9307 -141 18 68 C ATOM 2763 N SER B 63 30.464 -21.741 16.936 1.00 60.50 N ANISOU 2763 N SER B 63 8125 6317 8545 85 -800 28 N ATOM 2764 CA SER B 63 31.826 -21.856 17.371 1.00 55.72 C ANISOU 2764 CA SER B 63 7513 5648 8010 178 -911 -46 C ATOM 2765 C SER B 63 32.770 -21.490 16.235 1.00 59.62 C ANISOU 2765 C SER B 63 7894 6141 8616 389 -830 -230 C ATOM 2766 O SER B 63 32.558 -21.901 15.083 1.00 58.54 O ANISOU 2766 O SER B 63 7745 5967 8530 489 -838 -295 O ATOM 2767 CB SER B 63 32.080 -23.270 17.826 1.00 48.43 C ANISOU 2767 CB SER B 63 6726 4537 7138 144 -1236 36 C ATOM 2768 OG SER B 63 32.381 -24.045 16.691 1.00 61.81 O ANISOU 2768 OG SER B 63 8429 6086 8969 314 -1365 -80 O ATOM 2769 N GLY B 64 33.787 -20.690 16.566 1.00 55.44 N ANISOU 2769 N GLY B 64 7271 5682 8111 444 -750 -310 N ATOM 2770 CA GLY B 64 34.907 -20.430 15.679 1.00 56.80 C ANISOU 2770 CA GLY B 64 7314 5892 8376 617 -702 -468 C ATOM 2771 C GLY B 64 36.108 -21.309 15.982 1.00 61.57 C ANISOU 2771 C GLY B 64 7922 6399 9073 735 -933 -561 C ATOM 2772 O GLY B 64 36.320 -21.735 17.117 1.00 66.19 O ANISOU 2772 O GLY B 64 8599 6897 9652 666 -1102 -492 O ATOM 2773 N SER B 65 36.911 -21.570 14.962 1.00 59.44 N ANISOU 2773 N SER B 65 7540 6167 8878 919 -948 -727 N ATOM 2774 CA SER B 65 38.105 -22.380 15.129 1.00 65.27 C ANISOU 2774 CA SER B 65 8247 6834 9720 1074 -1175 -867 C ATOM 2775 C SER B 65 39.068 -22.140 13.978 1.00 77.31 C ANISOU 2775 C SER B 65 9559 8535 11281 1261 -1076 -1073 C ATOM 2776 O SER B 65 38.668 -21.642 12.920 1.00 83.96 O ANISOU 2776 O SER B 65 10317 9522 12063 1271 -878 -1089 O ATOM 2777 CB SER B 65 37.755 -23.850 15.169 1.00 61.53 C ANISOU 2777 CB SER B 65 7929 6137 9314 1126 -1488 -867 C ATOM 2778 OG SER B 65 38.031 -24.407 13.900 1.00 72.17 O ANISOU 2778 OG SER B 65 9186 7537 10700 1316 -1523 -1056 O ATOM 2779 N GLY B 66 40.330 -22.512 14.178 1.00 75.12 N ANISOU 2779 N GLY B 66 9184 8269 11088 1406 -1220 -1229 N ATOM 2780 CA GLY B 66 41.348 -22.271 13.179 1.00 71.62 C ANISOU 2780 CA GLY B 66 8497 8059 10656 1573 -1121 -1433 C ATOM 2781 C GLY B 66 42.271 -21.139 13.564 1.00 73.15 C ANISOU 2781 C GLY B 66 8526 8422 10844 1502 -956 -1420 C ATOM 2782 O GLY B 66 42.065 -20.457 14.557 1.00 72.24 O ANISOU 2782 O GLY B 66 8493 8236 10719 1336 -908 -1267 O ATOM 2783 N SER B 67 43.292 -20.937 12.746 1.00 81.03 N ANISOU 2783 N SER B 67 9276 9668 11842 1628 -875 -1590 N ATOM 2784 CA SER B 67 44.389 -20.048 13.079 1.00 80.12 C ANISOU 2784 CA SER B 67 8974 9719 11750 1579 -774 -1606 C ATOM 2785 C SER B 67 45.360 -20.070 11.916 1.00 78.16 C ANISOU 2785 C SER B 67 8436 9801 11460 1721 -687 -1801 C ATOM 2786 O SER B 67 45.296 -20.957 11.062 1.00 79.45 O ANISOU 2786 O SER B 67 8616 10033 11537 1826 -749 -1913 O ATOM 2787 CB SER B 67 45.102 -20.570 14.309 1.00 78.94 C ANISOU 2787 CB SER B 67 8886 9400 11709 1631 -1019 -1659 C ATOM 2788 OG SER B 67 45.659 -21.840 14.018 1.00 79.57 O ANISOU 2788 OG SER B 67 8968 9468 11798 1799 -1240 -1836 O ATOM 2789 N GLY B 68 46.285 -19.124 11.891 1.00 74.13 N ANISOU 2789 N GLY B 68 7699 9516 10951 1648 -543 -1796 N ATOM 2790 CA GLY B 68 47.152 -19.019 10.740 1.00 75.93 C ANISOU 2790 CA GLY B 68 7652 10124 11072 1707 -416 -1922 C ATOM 2791 C GLY B 68 46.345 -18.584 9.541 1.00 76.01 C ANISOU 2791 C GLY B 68 7619 10308 10954 1648 -207 -1838 C ATOM 2792 O GLY B 68 45.798 -17.487 9.526 1.00 80.97 O ANISOU 2792 O GLY B 68 8282 10926 11558 1435 -34 -1612 O ATOM 2793 N THR B 69 46.331 -19.412 8.506 1.00 71.76 N ANISOU 2793 N THR B 69 7074 9912 10279 1767 -232 -1963 N ATOM 2794 CA THR B 69 45.570 -19.105 7.306 1.00 73.54 C ANISOU 2794 CA THR B 69 7267 10315 10360 1724 -55 -1894 C ATOM 2795 C THR B 69 44.189 -19.766 7.123 1.00 79.37 C ANISOU 2795 C THR B 69 8261 10799 11095 1770 -136 -1863 C ATOM 2796 O THR B 69 43.454 -19.396 6.208 1.00 76.93 O ANISOU 2796 O THR B 69 7937 10615 10679 1724 14 -1786 O ATOM 2797 CB THR B 69 46.397 -19.496 6.110 1.00 71.70 C ANISOU 2797 CB THR B 69 6838 10456 9950 1811 -11 -2054 C ATOM 2798 OG1 THR B 69 46.678 -20.892 6.203 1.00 72.79 O ANISOU 2798 OG1 THR B 69 7079 10466 10112 2006 -268 -2284 O ATOM 2799 CG2 THR B 69 47.701 -18.728 6.121 1.00 69.22 C ANISOU 2799 CG2 THR B 69 6246 10448 9606 1725 105 -2049 C ATOM 2800 N GLN B 70 43.816 -20.705 7.989 1.00 84.06 N ANISOU 2800 N GLN B 70 9087 11048 11802 1837 -377 -1899 N ATOM 2801 CA GLN B 70 42.591 -21.489 7.784 1.00 75.36 C ANISOU 2801 CA GLN B 70 8216 9722 10696 1864 -488 -1871 C ATOM 2802 C GLN B 70 41.643 -21.345 8.963 1.00 69.76 C ANISOU 2802 C GLN B 70 7736 8660 10108 1756 -558 -1695 C ATOM 2803 O GLN B 70 42.022 -21.649 10.091 1.00 77.08 O ANISOU 2803 O GLN B 70 8749 9400 11140 1747 -723 -1687 O ATOM 2804 CB GLN B 70 42.923 -22.969 7.595 1.00 76.54 C ANISOU 2804 CB GLN B 70 8435 9797 10849 2017 -759 -2069 C ATOM 2805 CG GLN B 70 43.806 -23.286 6.386 1.00 94.66 C ANISOU 2805 CG GLN B 70 10514 12444 13008 2146 -726 -2289 C ATOM 2806 CD GLN B 70 43.008 -23.635 5.121 1.00104.01 C ANISOU 2806 CD GLN B 70 11716 13739 14064 2193 -685 -2336 C ATOM 2807 OE1 GLN B 70 41.785 -23.795 5.166 1.00104.32 O ANISOU 2807 OE1 GLN B 70 11944 13557 14135 2141 -712 -2216 O ATOM 2808 NE2 GLN B 70 43.706 -23.749 3.989 1.00103.09 N ANISOU 2808 NE2 GLN B 70 11396 13982 13792 2288 -623 -2514 N ATOM 2809 N PHE B 71 40.417 -20.889 8.705 1.00 51.73 N ANISOU 2809 N PHE B 71 5555 6304 7796 1662 -439 -1551 N ATOM 2810 CA PHE B 71 39.440 -20.691 9.765 1.00 50.33 C ANISOU 2810 CA PHE B 71 5612 5852 7661 1484 -472 -1338 C ATOM 2811 C PHE B 71 38.087 -21.259 9.375 1.00 63.95 C ANISOU 2811 C PHE B 71 7507 7435 9355 1467 -522 -1278 C ATOM 2812 O PHE B 71 37.807 -21.411 8.195 1.00 74.59 O ANISOU 2812 O PHE B 71 8790 8919 10633 1552 -459 -1357 O ATOM 2813 CB PHE B 71 39.282 -19.208 10.077 1.00 47.68 C ANISOU 2813 CB PHE B 71 5242 5588 7287 1275 -243 -1145 C ATOM 2814 CG PHE B 71 40.565 -18.508 10.383 1.00 56.10 C ANISOU 2814 CG PHE B 71 6129 6801 8387 1256 -183 -1180 C ATOM 2815 CD1 PHE B 71 40.889 -18.172 11.679 1.00 57.15 C ANISOU 2815 CD1 PHE B 71 6323 6797 8594 1168 -247 -1118 C ATOM 2816 CD2 PHE B 71 41.447 -18.170 9.362 1.00 62.96 C ANISOU 2816 CD2 PHE B 71 6750 7975 9197 1314 -62 -1271 C ATOM 2817 CE1 PHE B 71 42.072 -17.516 11.946 1.00 65.46 C ANISOU 2817 CE1 PHE B 71 7203 7980 9690 1145 -204 -1152 C ATOM 2818 CE2 PHE B 71 42.630 -17.511 9.620 1.00 63.15 C ANISOU 2818 CE2 PHE B 71 6587 8155 9253 1271 -7 -1288 C ATOM 2819 CZ PHE B 71 42.943 -17.181 10.912 1.00 67.99 C ANISOU 2819 CZ PHE B 71 7272 8594 9967 1189 -84 -1231 C ATOM 2820 N SER B 72 37.248 -21.571 10.362 1.00 64.48 N ANISOU 2820 N SER B 72 7781 7255 9462 1349 -636 -1136 N ATOM 2821 CA SER B 72 35.894 -22.034 10.077 1.00 64.98 C ANISOU 2821 CA SER B 72 7997 7195 9498 1293 -675 -1050 C ATOM 2822 C SER B 72 34.898 -21.698 11.175 1.00 67.82 C ANISOU 2822 C SER B 72 8512 7418 9838 1077 -656 -832 C ATOM 2823 O SER B 72 35.206 -21.792 12.352 1.00 74.62 O ANISOU 2823 O SER B 72 9437 8184 10732 1006 -757 -772 O ATOM 2824 CB SER B 72 35.880 -23.546 9.847 1.00 71.39 C ANISOU 2824 CB SER B 72 8895 7848 10381 1434 -969 -1178 C ATOM 2825 OG SER B 72 35.969 -24.240 11.079 1.00 75.21 O ANISOU 2825 OG SER B 72 9523 8114 10939 1360 -1202 -1097 O ATOM 2826 N LEU B 73 33.686 -21.339 10.774 1.00 68.42 N ANISOU 2826 N LEU B 73 8638 7510 9850 980 -535 -727 N ATOM 2827 CA LEU B 73 32.583 -21.123 11.696 1.00 65.75 C ANISOU 2827 CA LEU B 73 8420 7090 9471 790 -518 -550 C ATOM 2828 C LEU B 73 31.668 -22.331 11.575 1.00 71.57 C ANISOU 2828 C LEU B 73 9294 7676 10225 767 -711 -508 C ATOM 2829 O LEU B 73 31.318 -22.745 10.466 1.00 77.23 O ANISOU 2829 O LEU B 73 9999 8396 10948 862 -729 -585 O ATOM 2830 CB LEU B 73 31.814 -19.861 11.303 1.00 64.87 C ANISOU 2830 CB LEU B 73 8252 7104 9290 706 -269 -475 C ATOM 2831 CG LEU B 73 31.069 -19.067 12.378 1.00 63.58 C ANISOU 2831 CG LEU B 73 8128 6951 9079 540 -182 -353 C ATOM 2832 CD1 LEU B 73 30.129 -18.126 11.708 1.00 54.75 C ANISOU 2832 CD1 LEU B 73 6968 5913 7921 503 -5 -314 C ATOM 2833 CD2 LEU B 73 30.297 -19.960 13.332 1.00 71.53 C ANISOU 2833 CD2 LEU B 73 9263 7865 10048 421 -333 -253 C ATOM 2834 N LYS B 74 31.283 -22.904 12.707 1.00 66.89 N ANISOU 2834 N LYS B 74 8825 6959 9633 629 -868 -380 N ATOM 2835 CA LYS B 74 30.430 -24.084 12.700 1.00 61.62 C ANISOU 2835 CA LYS B 74 8292 6129 8994 561 -1088 -300 C ATOM 2836 C LYS B 74 29.209 -23.796 13.552 1.00 63.44 C ANISOU 2836 C LYS B 74 8578 6409 9117 317 -1016 -93 C ATOM 2837 O LYS B 74 29.334 -23.340 14.677 1.00 72.44 O ANISOU 2837 O LYS B 74 9719 7617 10188 199 -969 -5 O ATOM 2838 CB LYS B 74 31.213 -25.282 13.250 1.00 63.47 C ANISOU 2838 CB LYS B 74 8621 6155 9337 612 -1423 -323 C ATOM 2839 CG LYS B 74 30.428 -26.554 13.447 1.00 66.94 C ANISOU 2839 CG LYS B 74 9222 6378 9834 502 -1720 -200 C ATOM 2840 CD LYS B 74 31.115 -27.489 14.446 1.00 73.87 C ANISOU 2840 CD LYS B 74 10205 7082 10782 461 -2038 -135 C ATOM 2841 CE LYS B 74 30.350 -28.821 14.588 1.00 83.02 C ANISOU 2841 CE LYS B 74 11482 8103 11957 310 -2327 6 C ATOM 2842 NZ LYS B 74 30.795 -29.709 15.725 1.00 82.70 N ANISOU 2842 NZ LYS B 74 11542 7942 11939 188 -2632 139 N ATOM 2843 N ILE B 75 28.027 -24.035 13.002 1.00 64.81 N ANISOU 2843 N ILE B 75 8780 6581 9265 247 -1000 -32 N ATOM 2844 CA ILE B 75 26.773 -23.865 13.738 1.00 63.30 C ANISOU 2844 CA ILE B 75 8613 6476 8961 13 -939 151 C ATOM 2845 C ILE B 75 26.204 -25.245 14.001 1.00 64.99 C ANISOU 2845 C ILE B 75 8960 6518 9216 -126 -1231 294 C ATOM 2846 O ILE B 75 25.906 -25.987 13.069 1.00 60.69 O ANISOU 2846 O ILE B 75 8459 5837 8763 -54 -1368 244 O ATOM 2847 CB ILE B 75 25.728 -23.068 12.935 1.00 57.57 C ANISOU 2847 CB ILE B 75 7805 5890 8181 14 -714 128 C ATOM 2848 CG1 ILE B 75 26.323 -21.768 12.420 1.00 57.82 C ANISOU 2848 CG1 ILE B 75 7718 6041 8208 159 -477 -3 C ATOM 2849 CG2 ILE B 75 24.531 -22.766 13.786 1.00 57.17 C ANISOU 2849 CG2 ILE B 75 7734 5986 8002 -205 -630 277 C ATOM 2850 CD1 ILE B 75 25.411 -21.046 11.475 1.00 59.69 C ANISOU 2850 CD1 ILE B 75 7889 6375 8417 186 -304 -29 C ATOM 2851 N ASN B 76 26.082 -25.609 15.269 1.00 70.93 N ANISOU 2851 N ASN B 76 9777 7275 9898 -332 -1349 477 N ATOM 2852 CA ASN B 76 25.592 -26.929 15.605 1.00 76.36 C ANISOU 2852 CA ASN B 76 10599 7784 10629 -509 -1664 661 C ATOM 2853 C ASN B 76 24.118 -26.878 15.593 1.00 84.39 C ANISOU 2853 C ASN B 76 11584 8942 11540 -718 -1572 808 C ATOM 2854 O ASN B 76 23.550 -25.893 16.040 1.00 97.56 O ANISOU 2854 O ASN B 76 13138 10880 13049 -804 -1305 831 O ATOM 2855 CB ASN B 76 26.050 -27.328 16.991 1.00 82.70 C ANISOU 2855 CB ASN B 76 11482 8565 11374 -679 -1837 836 C ATOM 2856 CG ASN B 76 27.320 -28.113 16.959 1.00 97.23 C ANISOU 2856 CG ASN B 76 13420 10134 13388 -515 -2130 749 C ATOM 2857 OD1 ASN B 76 27.311 -29.301 16.639 1.00110.96 O ANISOU 2857 OD1 ASN B 76 15253 11656 15251 -506 -2437 769 O ATOM 2858 ND2 ASN B 76 28.433 -27.460 17.267 1.00 96.17 N ANISOU 2858 ND2 ASN B 76 13226 10063 13251 -365 -2027 613 N ATOM 2859 N ARG B 77 23.475 -27.913 15.079 1.00 88.02 N ANISOU 2859 N ARG B 77 12128 9223 12093 -795 -1801 890 N ATOM 2860 CA ARG B 77 22.036 -27.992 15.260 1.00 89.23 C ANISOU 2860 CA ARG B 77 12242 9525 12136 -1052 -1748 1074 C ATOM 2861 C ARG B 77 21.407 -26.610 14.971 1.00 77.83 C ANISOU 2861 C ARG B 77 10625 8388 10561 -990 -1353 959 C ATOM 2862 O ARG B 77 21.015 -25.866 15.885 1.00 66.23 O ANISOU 2862 O ARG B 77 9058 7194 8913 -1125 -1162 1027 O ATOM 2863 CB ARG B 77 21.744 -28.439 16.685 1.00 91.48 C ANISOU 2863 CB ARG B 77 12570 9903 12284 -1380 -1876 1364 C ATOM 2864 CG ARG B 77 20.974 -29.731 16.865 1.00 98.63 C ANISOU 2864 CG ARG B 77 13570 10680 13225 -1646 -2190 1614 C ATOM 2865 CD ARG B 77 20.275 -29.626 18.217 1.00113.56 C ANISOU 2865 CD ARG B 77 15398 12888 14863 -2003 -2126 1892 C ATOM 2866 NE ARG B 77 20.920 -28.582 19.030 1.00123.47 N ANISOU 2866 NE ARG B 77 16583 14363 15966 -1949 -1891 1824 N ATOM 2867 CZ ARG B 77 20.615 -27.279 18.991 1.00120.53 C ANISOU 2867 CZ ARG B 77 16036 14300 15461 -1838 -1516 1648 C ATOM 2868 NH1 ARG B 77 19.657 -26.841 18.179 1.00121.17 N ANISOU 2868 NH1 ARG B 77 16006 14490 15541 -1793 -1336 1554 N ATOM 2869 NH2 ARG B 77 21.276 -26.409 19.756 1.00109.81 N ANISOU 2869 NH2 ARG B 77 14616 13121 13984 -1764 -1347 1556 N ATOM 2870 N LEU B 78 21.363 -26.285 13.683 1.00 68.04 N ANISOU 2870 N LEU B 78 9347 7094 9412 -771 -1257 769 N ATOM 2871 CA LEU B 78 20.910 -25.014 13.150 1.00 55.49 C ANISOU 2871 CA LEU B 78 7617 5715 7752 -663 -940 638 C ATOM 2872 C LEU B 78 19.518 -24.599 13.619 1.00 70.74 C ANISOU 2872 C LEU B 78 9440 7901 9537 -869 -796 751 C ATOM 2873 O LEU B 78 18.645 -25.431 13.845 1.00 72.08 O ANISOU 2873 O LEU B 78 9635 8071 9683 -1087 -940 921 O ATOM 2874 CB LEU B 78 20.856 -25.167 11.644 1.00 44.07 C ANISOU 2874 CB LEU B 78 6180 4141 6422 -463 -959 487 C ATOM 2875 CG LEU B 78 21.051 -23.926 10.810 1.00 44.42 C ANISOU 2875 CG LEU B 78 6121 4308 6451 -260 -697 314 C ATOM 2876 CD1 LEU B 78 22.144 -23.075 11.439 1.00 48.53 C ANISOU 2876 CD1 LEU B 78 6601 4896 6942 -183 -569 254 C ATOM 2877 CD2 LEU B 78 21.401 -24.336 9.394 1.00 42.51 C ANISOU 2877 CD2 LEU B 78 5909 3931 6310 -52 -778 166 C ATOM 2878 N GLN B 79 19.316 -23.292 13.750 1.00 77.99 N ANISOU 2878 N GLN B 79 10227 9040 10365 -798 -526 646 N ATOM 2879 CA GLN B 79 18.027 -22.733 14.136 1.00 78.94 C ANISOU 2879 CA GLN B 79 10206 9439 10348 -935 -370 683 C ATOM 2880 C GLN B 79 17.494 -21.825 13.039 1.00 86.75 C ANISOU 2880 C GLN B 79 11107 10467 11387 -758 -203 523 C ATOM 2881 O GLN B 79 18.261 -21.310 12.227 1.00 92.11 O ANISOU 2881 O GLN B 79 11814 11019 12163 -541 -151 390 O ATOM 2882 CB GLN B 79 18.172 -21.927 15.418 1.00 74.98 C ANISOU 2882 CB GLN B 79 9610 9188 9689 -1001 -230 674 C ATOM 2883 CG GLN B 79 18.432 -22.772 16.623 1.00 77.07 C ANISOU 2883 CG GLN B 79 9938 9493 9850 -1229 -384 869 C ATOM 2884 CD GLN B 79 17.295 -23.708 16.906 1.00 82.33 C ANISOU 2884 CD GLN B 79 10588 10266 10429 -1517 -501 1087 C ATOM 2885 OE1 GLN B 79 17.506 -24.874 17.240 1.00 85.55 O ANISOU 2885 OE1 GLN B 79 11123 10522 10861 -1694 -749 1291 O ATOM 2886 NE2 GLN B 79 16.070 -23.205 16.775 1.00 83.54 N ANISOU 2886 NE2 GLN B 79 10577 10677 10486 -1573 -342 1052 N ATOM 2887 N PRO B 80 16.173 -21.604 13.024 1.00 83.11 N ANISOU 2887 N PRO B 80 10527 10201 10850 -858 -123 544 N ATOM 2888 CA PRO B 80 15.551 -20.783 11.988 1.00 74.49 C ANISOU 2888 CA PRO B 80 9355 9138 9810 -700 2 406 C ATOM 2889 C PRO B 80 16.141 -19.384 11.971 1.00 67.87 C ANISOU 2889 C PRO B 80 8460 8338 8988 -505 169 243 C ATOM 2890 O PRO B 80 16.244 -18.799 10.891 1.00 65.11 O ANISOU 2890 O PRO B 80 8116 7892 8730 -332 217 147 O ATOM 2891 CB PRO B 80 14.098 -20.726 12.434 1.00 80.48 C ANISOU 2891 CB PRO B 80 9960 10167 10451 -870 61 453 C ATOM 2892 CG PRO B 80 14.176 -20.872 13.901 1.00 88.58 C ANISOU 2892 CG PRO B 80 10937 11401 11319 -1061 71 550 C ATOM 2893 CD PRO B 80 15.228 -21.903 14.107 1.00 87.99 C ANISOU 2893 CD PRO B 80 11046 11084 11302 -1123 -120 683 C ATOM 2894 N GLU B 81 16.531 -18.870 13.139 1.00 67.61 N ANISOU 2894 N GLU B 81 8378 8443 8868 -545 236 222 N ATOM 2895 CA GLU B 81 17.089 -17.517 13.257 1.00 62.99 C ANISOU 2895 CA GLU B 81 7737 7880 8314 -378 362 66 C ATOM 2896 C GLU B 81 18.481 -17.349 12.641 1.00 64.17 C ANISOU 2896 C GLU B 81 7996 7797 8588 -228 335 33 C ATOM 2897 O GLU B 81 18.949 -16.226 12.465 1.00 61.42 O ANISOU 2897 O GLU B 81 7612 7426 8301 -96 417 -73 O ATOM 2898 CB GLU B 81 17.121 -17.074 14.721 1.00 57.21 C ANISOU 2898 CB GLU B 81 6918 7374 7446 -460 420 32 C ATOM 2899 CG GLU B 81 18.325 -17.551 15.486 1.00 69.88 C ANISOU 2899 CG GLU B 81 8624 8898 9029 -511 344 103 C ATOM 2900 CD GLU B 81 18.179 -17.401 16.999 1.00 86.32 C ANISOU 2900 CD GLU B 81 10620 11252 10924 -643 377 108 C ATOM 2901 OE1 GLU B 81 17.886 -18.418 17.665 1.00 87.19 O ANISOU 2901 OE1 GLU B 81 10754 11467 10907 -859 290 281 O ATOM 2902 OE2 GLU B 81 18.371 -16.277 17.524 1.00 92.04 O ANISOU 2902 OE2 GLU B 81 11256 12089 11625 -538 472 -57 O ATOM 2903 N ASP B 82 19.127 -18.469 12.310 1.00 68.15 N ANISOU 2903 N ASP B 82 8620 8136 9136 -251 203 118 N ATOM 2904 CA ASP B 82 20.525 -18.487 11.868 1.00 62.95 C ANISOU 2904 CA ASP B 82 8038 7309 8569 -121 166 78 C ATOM 2905 C ASP B 82 20.699 -18.259 10.379 1.00 68.53 C ANISOU 2905 C ASP B 82 8756 7920 9363 33 190 16 C ATOM 2906 O ASP B 82 21.812 -18.054 9.903 1.00 72.21 O ANISOU 2906 O ASP B 82 9242 8311 9885 147 197 -33 O ATOM 2907 CB ASP B 82 21.185 -19.812 12.231 1.00 51.54 C ANISOU 2907 CB ASP B 82 6705 5740 7137 -189 -17 163 C ATOM 2908 CG ASP B 82 21.148 -20.084 13.705 1.00 55.21 C ANISOU 2908 CG ASP B 82 7172 6306 7498 -361 -61 257 C ATOM 2909 OD1 ASP B 82 21.000 -19.124 14.477 1.00 51.77 O ANISOU 2909 OD1 ASP B 82 6647 6041 6983 -379 70 209 O ATOM 2910 OD2 ASP B 82 21.271 -21.256 14.099 1.00 64.03 O ANISOU 2910 OD2 ASP B 82 8382 7334 8611 -478 -245 378 O ATOM 2911 N PHE B 83 19.606 -18.313 9.636 1.00 68.44 N ANISOU 2911 N PHE B 83 8720 7937 9347 30 201 22 N ATOM 2912 CA PHE B 83 19.707 -18.164 8.196 1.00 66.85 C ANISOU 2912 CA PHE B 83 8531 7671 9198 165 212 -25 C ATOM 2913 C PHE B 83 20.048 -16.720 7.861 1.00 74.04 C ANISOU 2913 C PHE B 83 9377 8618 10137 260 343 -77 C ATOM 2914 O PHE B 83 19.563 -15.783 8.507 1.00 88.13 O ANISOU 2914 O PHE B 83 11093 10477 11916 234 416 -100 O ATOM 2915 CB PHE B 83 18.436 -18.671 7.505 1.00 58.73 C ANISOU 2915 CB PHE B 83 7499 6656 8160 130 164 -2 C ATOM 2916 CG PHE B 83 18.234 -20.147 7.669 1.00 56.23 C ANISOU 2916 CG PHE B 83 7262 6254 7849 32 -12 61 C ATOM 2917 CD1 PHE B 83 18.802 -21.033 6.774 1.00 58.54 C ANISOU 2917 CD1 PHE B 83 7636 6411 8196 129 -145 18 C ATOM 2918 CD2 PHE B 83 17.532 -20.650 8.748 1.00 51.62 C ANISOU 2918 CD2 PHE B 83 6666 5735 7214 -162 -64 163 C ATOM 2919 CE1 PHE B 83 18.648 -22.393 6.930 1.00 61.24 C ANISOU 2919 CE1 PHE B 83 8064 6626 8579 47 -358 67 C ATOM 2920 CE2 PHE B 83 17.379 -22.004 8.910 1.00 57.04 C ANISOU 2920 CE2 PHE B 83 7437 6311 7924 -281 -264 256 C ATOM 2921 CZ PHE B 83 17.941 -22.880 7.999 1.00 63.09 C ANISOU 2921 CZ PHE B 83 8304 6884 8783 -170 -428 204 C ATOM 2922 N GLY B 84 20.926 -16.551 6.883 1.00 59.13 N ANISOU 2922 N GLY B 84 7504 6686 8277 367 354 -98 N ATOM 2923 CA GLY B 84 21.427 -15.244 6.522 1.00 54.33 C ANISOU 2923 CA GLY B 84 6844 6094 7703 424 446 -105 C ATOM 2924 C GLY B 84 22.813 -15.438 5.958 1.00 59.26 C ANISOU 2924 C GLY B 84 7474 6714 8329 491 444 -115 C ATOM 2925 O GLY B 84 23.285 -16.567 5.855 1.00 63.49 O ANISOU 2925 O GLY B 84 8050 7228 8847 521 365 -149 O ATOM 2926 N THR B 85 23.474 -14.354 5.582 1.00 59.67 N ANISOU 2926 N THR B 85 7476 6790 8407 512 513 -89 N ATOM 2927 CA THR B 85 24.802 -14.488 4.990 1.00 60.61 C ANISOU 2927 CA THR B 85 7561 6964 8505 562 527 -97 C ATOM 2928 C THR B 85 25.887 -14.123 6.005 1.00 53.12 C ANISOU 2928 C THR B 85 6584 5992 7608 530 539 -109 C ATOM 2929 O THR B 85 25.693 -13.205 6.817 1.00 44.45 O ANISOU 2929 O THR B 85 5476 4845 6570 475 560 -91 O ATOM 2930 CB THR B 85 24.928 -13.719 3.630 1.00 56.04 C ANISOU 2930 CB THR B 85 6931 6476 7885 583 584 -30 C ATOM 2931 OG1 THR B 85 26.133 -12.942 3.599 1.00 49.30 O ANISOU 2931 OG1 THR B 85 6005 5677 7049 552 634 18 O ATOM 2932 CG2 THR B 85 23.698 -12.818 3.376 1.00 54.46 C ANISOU 2932 CG2 THR B 85 6746 6225 7719 551 590 36 C ATOM 2933 N TYR B 86 26.997 -14.876 5.969 1.00 50.01 N ANISOU 2933 N TYR B 86 6170 5636 7195 581 506 -165 N ATOM 2934 CA TYR B 86 28.091 -14.763 6.952 1.00 47.18 C ANISOU 2934 CA TYR B 86 5785 5256 6884 562 492 -192 C ATOM 2935 C TYR B 86 29.426 -14.269 6.381 1.00 53.81 C ANISOU 2935 C TYR B 86 6514 6208 7722 584 546 -190 C ATOM 2936 O TYR B 86 29.912 -14.745 5.362 1.00 56.51 O ANISOU 2936 O TYR B 86 6797 6677 7996 657 557 -231 O ATOM 2937 CB TYR B 86 28.317 -16.095 7.651 1.00 43.47 C ANISOU 2937 CB TYR B 86 5379 4725 6414 593 373 -263 C ATOM 2938 CG TYR B 86 27.193 -16.506 8.548 1.00 48.71 C ANISOU 2938 CG TYR B 86 6131 5305 7071 515 316 -229 C ATOM 2939 CD1 TYR B 86 27.303 -16.391 9.923 1.00 52.80 C ANISOU 2939 CD1 TYR B 86 6673 5789 7600 438 288 -214 C ATOM 2940 CD2 TYR B 86 26.007 -17.001 8.025 1.00 51.95 C ANISOU 2940 CD2 TYR B 86 6588 5701 7448 505 289 -207 C ATOM 2941 CE1 TYR B 86 26.264 -16.773 10.757 1.00 51.85 C ANISOU 2941 CE1 TYR B 86 6609 5657 7437 342 246 -171 C ATOM 2942 CE2 TYR B 86 24.958 -17.372 8.856 1.00 51.34 C ANISOU 2942 CE2 TYR B 86 6565 5592 7350 405 243 -161 C ATOM 2943 CZ TYR B 86 25.100 -17.252 10.215 1.00 49.21 C ANISOU 2943 CZ TYR B 86 6305 5323 7070 319 228 -139 C ATOM 2944 OH TYR B 86 24.075 -17.605 11.033 1.00 53.13 O ANISOU 2944 OH TYR B 86 6827 5850 7509 199 195 -83 O ATOM 2945 N TYR B 87 30.022 -13.314 7.071 1.00 60.86 N ANISOU 2945 N TYR B 87 7365 7073 8684 515 574 -153 N ATOM 2946 CA TYR B 87 31.247 -12.686 6.611 1.00 61.77 C ANISOU 2946 CA TYR B 87 7360 7302 8808 491 624 -119 C ATOM 2947 C TYR B 87 32.368 -12.880 7.608 1.00 57.45 C ANISOU 2947 C TYR B 87 6774 6738 8315 496 582 -187 C ATOM 2948 O TYR B 87 32.153 -12.875 8.818 1.00 50.75 O ANISOU 2948 O TYR B 87 5996 5765 7522 472 528 -215 O ATOM 2949 CB TYR B 87 31.023 -11.188 6.428 1.00 61.86 C ANISOU 2949 CB TYR B 87 7346 7273 8884 383 664 12 C ATOM 2950 CG TYR B 87 30.035 -10.851 5.345 1.00 61.54 C ANISOU 2950 CG TYR B 87 7331 7255 8796 372 691 100 C ATOM 2951 CD1 TYR B 87 30.371 -10.993 3.996 1.00 60.92 C ANISOU 2951 CD1 TYR B 87 7179 7366 8603 380 743 156 C ATOM 2952 CD2 TYR B 87 28.775 -10.374 5.660 1.00 61.02 C ANISOU 2952 CD2 TYR B 87 7350 7050 8786 360 659 115 C ATOM 2953 CE1 TYR B 87 29.475 -10.676 2.994 1.00 60.48 C ANISOU 2953 CE1 TYR B 87 7151 7336 8491 366 754 246 C ATOM 2954 CE2 TYR B 87 27.866 -10.061 4.666 1.00 67.53 C ANISOU 2954 CE2 TYR B 87 8197 7885 9575 359 665 192 C ATOM 2955 CZ TYR B 87 28.218 -10.214 3.334 1.00 68.81 C ANISOU 2955 CZ TYR B 87 8304 8214 9626 357 708 267 C ATOM 2956 OH TYR B 87 27.306 -9.899 2.352 1.00 72.59 O ANISOU 2956 OH TYR B 87 8812 8708 10060 352 701 352 O ATOM 2957 N CYS B 88 33.575 -13.032 7.089 1.00 59.37 N ANISOU 2957 N CYS B 88 6891 7138 8531 527 605 -219 N ATOM 2958 CA CYS B 88 34.759 -13.019 7.938 1.00 58.53 C ANISOU 2958 CA CYS B 88 6717 7033 8487 523 567 -276 C ATOM 2959 C CYS B 88 35.631 -11.793 7.674 1.00 54.13 C ANISOU 2959 C CYS B 88 6023 6571 7972 407 632 -175 C ATOM 2960 O CYS B 88 35.699 -11.270 6.560 1.00 48.36 O ANISOU 2960 O CYS B 88 5205 5989 7181 349 709 -74 O ATOM 2961 CB CYS B 88 35.572 -14.305 7.781 1.00 52.19 C ANISOU 2961 CB CYS B 88 5859 6327 7642 666 501 -431 C ATOM 2962 SG CYS B 88 36.314 -14.509 6.174 1.00 62.25 S ANISOU 2962 SG CYS B 88 6941 7922 8790 739 585 -481 S ATOM 2963 N GLN B 89 36.295 -11.322 8.712 1.00 57.54 N ANISOU 2963 N GLN B 89 6436 6921 8505 355 587 -187 N ATOM 2964 CA GLN B 89 37.221 -10.231 8.511 1.00 68.47 C ANISOU 2964 CA GLN B 89 7681 8384 9949 229 620 -88 C ATOM 2965 C GLN B 89 38.546 -10.398 9.257 1.00 71.64 C ANISOU 2965 C GLN B 89 7978 8834 10407 240 575 -175 C ATOM 2966 O GLN B 89 38.565 -10.759 10.431 1.00 80.29 O ANISOU 2966 O GLN B 89 9159 9788 11559 291 489 -271 O ATOM 2967 CB GLN B 89 36.568 -8.919 8.901 1.00 67.62 C ANISOU 2967 CB GLN B 89 7650 8087 9958 107 590 28 C ATOM 2968 CG GLN B 89 37.509 -7.758 8.719 1.00 70.18 C ANISOU 2968 CG GLN B 89 7844 8448 10373 -51 581 155 C ATOM 2969 CD GLN B 89 37.030 -6.571 9.471 1.00 67.35 C ANISOU 2969 CD GLN B 89 7571 7840 10179 -133 485 201 C ATOM 2970 OE1 GLN B 89 35.881 -6.548 9.922 1.00 60.73 O ANISOU 2970 OE1 GLN B 89 6870 6847 9358 -67 451 142 O ATOM 2971 NE2 GLN B 89 37.900 -5.578 9.640 1.00 62.83 N ANISOU 2971 NE2 GLN B 89 6906 7234 9733 -272 425 289 N ATOM 2972 N HIS B 90 39.655 -10.128 8.577 1.00 64.77 N ANISOU 2972 N HIS B 90 6910 8189 9511 183 629 -137 N ATOM 2973 CA HIS B 90 40.940 -10.135 9.259 1.00 60.59 C ANISOU 2973 CA HIS B 90 6255 7717 9051 177 583 -212 C ATOM 2974 C HIS B 90 41.261 -8.737 9.727 1.00 62.48 C ANISOU 2974 C HIS B 90 6463 7845 9429 -11 552 -75 C ATOM 2975 O HIS B 90 41.013 -7.768 9.019 1.00 67.25 O ANISOU 2975 O HIS B 90 7038 8466 10049 -162 589 105 O ATOM 2976 CB HIS B 90 42.067 -10.674 8.378 1.00 50.09 C ANISOU 2976 CB HIS B 90 4688 6728 7616 228 646 -282 C ATOM 2977 CG HIS B 90 42.673 -9.651 7.471 1.00 51.84 C ANISOU 2977 CG HIS B 90 4713 7183 7802 33 742 -101 C ATOM 2978 ND1 HIS B 90 43.385 -8.571 7.939 1.00 58.25 N ANISOU 2978 ND1 HIS B 90 5439 7953 8741 -153 709 21 N ATOM 2979 CD2 HIS B 90 42.692 -9.559 6.119 1.00 53.40 C ANISOU 2979 CD2 HIS B 90 4777 7673 7840 -23 855 -7 C ATOM 2980 CE1 HIS B 90 43.812 -7.851 6.914 1.00 62.20 C ANISOU 2980 CE1 HIS B 90 5763 8700 9170 -336 793 208 C ATOM 2981 NE2 HIS B 90 43.406 -8.431 5.799 1.00 56.96 N ANISOU 2981 NE2 HIS B 90 5063 8261 8317 -262 891 197 N ATOM 2982 N PHE B 91 41.716 -8.642 10.969 1.00 59.22 N ANISOU 2982 N PHE B 91 6082 7291 9129 0 455 -161 N ATOM 2983 CA PHE B 91 42.311 -7.423 11.491 1.00 55.69 C ANISOU 2983 CA PHE B 91 5574 6753 8833 -160 392 -76 C ATOM 2984 C PHE B 91 43.804 -7.435 11.539 1.00 53.31 C ANISOU 2984 C PHE B 91 5055 6638 8561 -206 385 -104 C ATOM 2985 O PHE B 91 44.384 -6.531 12.124 1.00 58.57 O ANISOU 2985 O PHE B 91 5672 7213 9370 -333 306 -56 O ATOM 2986 CB PHE B 91 41.761 -7.056 12.849 1.00 55.01 C ANISOU 2986 CB PHE B 91 5656 6389 8856 -136 277 -152 C ATOM 2987 CG PHE B 91 40.299 -6.736 12.830 1.00 51.31 C ANISOU 2987 CG PHE B 91 5363 5753 8381 -120 277 -120 C ATOM 2988 CD1 PHE B 91 39.869 -5.420 12.790 1.00 45.49 C ANISOU 2988 CD1 PHE B 91 4657 4853 7773 -238 216 -18 C ATOM 2989 CD2 PHE B 91 39.356 -7.755 12.834 1.00 41.37 C ANISOU 2989 CD2 PHE B 91 4227 4494 6998 13 315 -194 C ATOM 2990 CE1 PHE B 91 38.533 -5.131 12.780 1.00 42.42 C ANISOU 2990 CE1 PHE B 91 4408 4323 7385 -199 202 -18 C ATOM 2991 CE2 PHE B 91 38.015 -7.460 12.827 1.00 42.85 C ANISOU 2991 CE2 PHE B 91 4548 4557 7175 25 318 -174 C ATOM 2992 CZ PHE B 91 37.605 -6.147 12.799 1.00 45.12 C ANISOU 2992 CZ PHE B 91 4853 4702 7587 -69 267 -99 C ATOM 2993 N TYR B 92 44.426 -8.483 11.004 1.00 51.87 N ANISOU 2993 N TYR B 92 4740 6709 8257 -87 445 -212 N ATOM 2994 CA TYR B 92 45.888 -8.533 10.957 1.00 49.00 C ANISOU 2994 CA TYR B 92 4125 6583 7909 -117 447 -262 C ATOM 2995 C TYR B 92 46.412 -7.429 10.053 1.00 55.72 C ANISOU 2995 C TYR B 92 4780 7629 8762 -363 523 -42 C ATOM 2996 O TYR B 92 45.989 -7.294 8.903 1.00 65.05 O ANISOU 2996 O TYR B 92 5922 8973 9820 -428 627 87 O ATOM 2997 CB TYR B 92 46.437 -9.898 10.489 1.00 47.16 C ANISOU 2997 CB TYR B 92 3765 6608 7544 93 478 -462 C ATOM 2998 CG TYR B 92 47.938 -9.943 10.611 1.00 61.81 C ANISOU 2998 CG TYR B 92 5350 8703 9430 85 460 -552 C ATOM 2999 CD1 TYR B 92 48.546 -10.420 11.763 1.00 70.41 C ANISOU 2999 CD1 TYR B 92 6463 9667 10624 200 321 -718 C ATOM 3000 CD2 TYR B 92 48.753 -9.432 9.608 1.00 63.38 C ANISOU 3000 CD2 TYR B 92 5259 9270 9552 -61 577 -453 C ATOM 3001 CE1 TYR B 92 49.927 -10.420 11.898 1.00 68.90 C ANISOU 3001 CE1 TYR B 92 6011 9696 10474 195 293 -809 C ATOM 3002 CE2 TYR B 92 50.118 -9.415 9.737 1.00 62.63 C ANISOU 3002 CE2 TYR B 92 4889 9423 9484 -86 565 -533 C ATOM 3003 CZ TYR B 92 50.708 -9.911 10.883 1.00 70.24 C ANISOU 3003 CZ TYR B 92 5877 10241 10569 53 421 -722 C ATOM 3004 OH TYR B 92 52.086 -9.904 11.003 1.00 79.85 O ANISOU 3004 OH TYR B 92 6802 11717 11821 38 401 -817 O ATOM 3005 N GLY B 93 47.333 -6.632 10.568 1.00 55.64 N ANISOU 3005 N GLY B 93 4647 7607 8888 -518 456 18 N ATOM 3006 CA GLY B 93 48.016 -5.686 9.717 1.00 67.89 C ANISOU 3006 CA GLY B 93 5974 9385 10436 -781 510 244 C ATOM 3007 C GLY B 93 47.345 -4.350 9.846 1.00 81.07 C ANISOU 3007 C GLY B 93 7793 10748 12262 -992 416 472 C ATOM 3008 O GLY B 93 46.545 -4.148 10.757 1.00 79.27 O ANISOU 3008 O GLY B 93 7804 10160 12156 -911 308 400 O ATOM 3009 N SER B 94 47.716 -3.430 8.961 1.00 89.21 N ANISOU 3009 N SER B 94 8670 11935 13290 -1267 440 742 N ATOM 3010 CA SER B 94 47.119 -2.101 8.895 1.00 88.06 C ANISOU 3010 CA SER B 94 8654 11495 13311 -1489 312 991 C ATOM 3011 C SER B 94 45.824 -2.053 8.079 1.00 94.51 C ANISOU 3011 C SER B 94 9642 12236 14032 -1464 358 1102 C ATOM 3012 O SER B 94 44.845 -1.411 8.489 1.00100.39 O ANISOU 3012 O SER B 94 10613 12605 14928 -1456 228 1132 O ATOM 3013 CB SER B 94 48.121 -1.150 8.285 1.00 85.39 C ANISOU 3013 CB SER B 94 8073 11355 13015 -1832 286 1274 C ATOM 3014 OG SER B 94 48.688 -1.765 7.141 1.00 90.65 O ANISOU 3014 OG SER B 94 8487 12542 13415 -1869 483 1328 O ATOM 3015 N THR B 95 45.831 -2.728 6.925 1.00 86.18 N ANISOU 3015 N THR B 95 8465 11554 12725 -1438 532 1141 N ATOM 3016 CA THR B 95 44.703 -2.695 5.986 1.00 74.29 C ANISOU 3016 CA THR B 95 7088 10037 11102 -1434 581 1266 C ATOM 3017 C THR B 95 43.893 -3.997 5.990 1.00 70.03 C ANISOU 3017 C THR B 95 6677 9516 10415 -1116 678 1008 C ATOM 3018 O THR B 95 44.452 -5.090 5.948 1.00 78.39 O ANISOU 3018 O THR B 95 7614 10834 11338 -946 775 803 O ATOM 3019 CB THR B 95 45.144 -2.338 4.546 1.00 69.76 C ANISOU 3019 CB THR B 95 6298 9869 10337 -1679 683 1550 C ATOM 3020 OG1 THR B 95 44.095 -2.693 3.641 1.00 79.48 O ANISOU 3020 OG1 THR B 95 7641 11159 11397 -1594 759 1588 O ATOM 3021 CG2 THR B 95 46.390 -3.094 4.150 1.00 61.61 C ANISOU 3021 CG2 THR B 95 4949 9351 9107 -1658 838 1444 C ATOM 3022 N TRP B 96 42.572 -3.875 6.041 1.00 60.48 N ANISOU 3022 N TRP B 96 5707 8025 9247 -1037 629 1014 N ATOM 3023 CA TRP B 96 41.715 -5.025 6.346 1.00 61.40 C ANISOU 3023 CA TRP B 96 5979 8068 9283 -757 674 772 C ATOM 3024 C TRP B 96 40.683 -5.372 5.268 1.00 66.80 C ANISOU 3024 C TRP B 96 6740 8837 9803 -702 751 830 C ATOM 3025 O TRP B 96 40.204 -4.513 4.534 1.00 77.49 O ANISOU 3025 O TRP B 96 8123 10158 11161 -863 726 1061 O ATOM 3026 CB TRP B 96 40.988 -4.792 7.659 1.00 59.50 C ANISOU 3026 CB TRP B 96 5955 7424 9229 -664 545 651 C ATOM 3027 CG TRP B 96 41.877 -4.441 8.799 1.00 60.04 C ANISOU 3027 CG TRP B 96 5975 7379 9457 -701 448 574 C ATOM 3028 CD1 TRP B 96 43.151 -4.868 9.016 1.00 55.31 C ANISOU 3028 CD1 TRP B 96 5194 6989 8834 -700 478 496 C ATOM 3029 CD2 TRP B 96 41.547 -3.584 9.896 1.00 59.72 C ANISOU 3029 CD2 TRP B 96 6065 6998 9627 -728 290 543 C ATOM 3030 NE1 TRP B 96 43.634 -4.322 10.179 1.00 56.73 N ANISOU 3030 NE1 TRP B 96 5392 6967 9198 -739 349 438 N ATOM 3031 CE2 TRP B 96 42.661 -3.535 10.736 1.00 60.10 C ANISOU 3031 CE2 TRP B 96 6012 7060 9765 -753 233 459 C ATOM 3032 CE3 TRP B 96 40.412 -2.848 10.245 1.00 59.20 C ANISOU 3032 CE3 TRP B 96 6180 6631 9681 -718 182 554 C ATOM 3033 CZ2 TRP B 96 42.671 -2.790 11.898 1.00 69.28 C ANISOU 3033 CZ2 TRP B 96 7255 7946 11122 -771 72 387 C ATOM 3034 CZ3 TRP B 96 40.430 -2.102 11.410 1.00 49.79 C ANISOU 3034 CZ3 TRP B 96 5057 5177 8684 -721 21 461 C ATOM 3035 CH2 TRP B 96 41.533 -2.090 12.219 1.00 59.35 C ANISOU 3035 CH2 TRP B 96 6174 6408 9968 -748 -31 380 C ATOM 3036 N ALA B 97 40.318 -6.641 5.194 1.00 60.30 N ANISOU 3036 N ALA B 97 5961 8103 8850 -473 819 620 N ATOM 3037 CA ALA B 97 39.542 -7.119 4.069 1.00 60.65 C ANISOU 3037 CA ALA B 97 6034 8296 8713 -410 898 647 C ATOM 3038 C ALA B 97 38.560 -8.181 4.508 1.00 66.72 C ANISOU 3038 C ALA B 97 6984 8896 9469 -176 878 436 C ATOM 3039 O ALA B 97 38.853 -8.976 5.413 1.00 66.23 O ANISOU 3039 O ALA B 97 6952 8760 9454 -35 839 238 O ATOM 3040 CB ALA B 97 40.459 -7.661 3.003 1.00 59.77 C ANISOU 3040 CB ALA B 97 5678 8652 8381 -409 1021 628 C ATOM 3041 N PHE B 98 37.392 -8.185 3.866 1.00 65.31 N ANISOU 3041 N PHE B 98 6926 8658 9230 -152 888 497 N ATOM 3042 CA PHE B 98 36.346 -9.142 4.196 1.00 59.14 C ANISOU 3042 CA PHE B 98 6312 7723 8434 33 862 333 C ATOM 3043 C PHE B 98 36.366 -10.367 3.298 1.00 58.05 C ANISOU 3043 C PHE B 98 6115 7833 8109 188 920 197 C ATOM 3044 O PHE B 98 37.179 -10.477 2.353 1.00 52.57 O ANISOU 3044 O PHE B 98 5233 7475 7267 170 999 209 O ATOM 3045 CB PHE B 98 34.966 -8.495 4.085 1.00 56.42 C ANISOU 3045 CB PHE B 98 6130 7157 8148 -8 820 443 C ATOM 3046 CG PHE B 98 34.658 -7.537 5.182 1.00 51.87 C ANISOU 3046 CG PHE B 98 5649 6286 7772 -78 724 477 C ATOM 3047 CD1 PHE B 98 33.863 -7.920 6.244 1.00 39.73 C ANISOU 3047 CD1 PHE B 98 4249 4544 6304 28 671 333 C ATOM 3048 CD2 PHE B 98 35.164 -6.246 5.151 1.00 52.84 C ANISOU 3048 CD2 PHE B 98 5715 6351 8011 -257 670 651 C ATOM 3049 CE1 PHE B 98 33.584 -7.042 7.239 1.00 39.29 C ANISOU 3049 CE1 PHE B 98 4257 4264 6408 -14 583 325 C ATOM 3050 CE2 PHE B 98 34.883 -5.356 6.156 1.00 47.20 C ANISOU 3050 CE2 PHE B 98 5084 5355 7494 -296 552 643 C ATOM 3051 CZ PHE B 98 34.092 -5.751 7.195 1.00 46.08 C ANISOU 3051 CZ PHE B 98 5065 5044 7400 -160 516 462 C ATOM 3052 N GLY B 99 35.445 -11.277 3.605 1.00 55.01 N ANISOU 3052 N GLY B 99 5881 7291 7728 337 870 62 N ATOM 3053 CA GLY B 99 35.185 -12.430 2.771 1.00 60.15 C ANISOU 3053 CA GLY B 99 6521 8099 8236 495 880 -77 C ATOM 3054 C GLY B 99 34.178 -12.087 1.687 1.00 69.90 C ANISOU 3054 C GLY B 99 7803 9385 9370 454 922 46 C ATOM 3055 O GLY B 99 33.701 -10.943 1.572 1.00 72.34 O ANISOU 3055 O GLY B 99 8155 9601 9731 302 933 247 O ATOM 3056 N GLY B 100 33.870 -13.080 0.864 1.00 73.67 N ANISOU 3056 N GLY B 100 8273 10006 9714 597 920 -86 N ATOM 3057 CA GLY B 100 32.846 -12.918 -0.142 1.00 76.04 C ANISOU 3057 CA GLY B 100 8630 10349 9912 583 942 3 C ATOM 3058 C GLY B 100 31.492 -13.104 0.501 1.00 70.45 C ANISOU 3058 C GLY B 100 8127 9315 9325 610 861 -4 C ATOM 3059 O GLY B 100 30.469 -12.791 -0.091 1.00 72.89 O ANISOU 3059 O GLY B 100 8508 9584 9601 581 861 87 O ATOM 3060 N GLY B 101 31.511 -13.598 1.734 1.00 68.18 N ANISOU 3060 N GLY B 101 7919 8817 9168 655 790 -105 N ATOM 3061 CA GLY B 101 30.321 -13.987 2.465 1.00 61.21 C ANISOU 3061 CA GLY B 101 7201 7681 8375 676 713 -133 C ATOM 3062 C GLY B 101 29.905 -15.371 2.024 1.00 61.90 C ANISOU 3062 C GLY B 101 7335 7783 8399 820 635 -286 C ATOM 3063 O GLY B 101 30.279 -15.807 0.939 1.00 65.02 O ANISOU 3063 O GLY B 101 7645 8390 8670 910 651 -364 O ATOM 3064 N THR B 102 29.166 -16.083 2.866 1.00 66.56 N ANISOU 3064 N THR B 102 8052 8166 9070 838 535 -335 N ATOM 3065 CA THR B 102 28.414 -17.245 2.383 1.00 71.69 C ANISOU 3065 CA THR B 102 8775 8775 9688 934 432 -434 C ATOM 3066 C THR B 102 26.946 -17.074 2.764 1.00 68.95 C ANISOU 3066 C THR B 102 8541 8269 9387 848 413 -342 C ATOM 3067 O THR B 102 26.643 -16.574 3.848 1.00 65.13 O ANISOU 3067 O THR B 102 8098 7671 8979 751 427 -271 O ATOM 3068 CB THR B 102 29.007 -18.634 2.814 1.00 65.90 C ANISOU 3068 CB THR B 102 8070 7969 9001 1053 271 -605 C ATOM 3069 OG1 THR B 102 28.122 -19.310 3.712 1.00 60.92 O ANISOU 3069 OG1 THR B 102 7580 7111 8456 999 144 -577 O ATOM 3070 CG2 THR B 102 30.368 -18.489 3.448 1.00 71.41 C ANISOU 3070 CG2 THR B 102 8682 8713 9736 1069 280 -651 C ATOM 3071 N LYS B 103 26.055 -17.451 1.843 1.00 71.59 N ANISOU 3071 N LYS B 103 8907 8629 9666 891 384 -359 N ATOM 3072 CA LYS B 103 24.608 -17.224 1.967 1.00 69.87 C ANISOU 3072 CA LYS B 103 8763 8309 9476 817 376 -279 C ATOM 3073 C LYS B 103 23.888 -18.496 2.420 1.00 66.39 C ANISOU 3073 C LYS B 103 8415 7730 9081 820 226 -338 C ATOM 3074 O LYS B 103 23.796 -19.479 1.668 1.00 69.52 O ANISOU 3074 O LYS B 103 8833 8130 9450 915 119 -437 O ATOM 3075 CB LYS B 103 24.055 -16.758 0.615 1.00 66.51 C ANISOU 3075 CB LYS B 103 8308 8003 8961 847 425 -241 C ATOM 3076 CG LYS B 103 22.643 -16.215 0.652 1.00 70.72 C ANISOU 3076 CG LYS B 103 8886 8456 9529 778 431 -155 C ATOM 3077 CD LYS B 103 22.324 -15.449 -0.635 1.00 79.87 C ANISOU 3077 CD LYS B 103 10009 9734 10603 793 480 -81 C ATOM 3078 CE LYS B 103 20.822 -15.214 -0.823 1.00 83.68 C ANISOU 3078 CE LYS B 103 10535 10143 11118 768 444 -41 C ATOM 3079 NZ LYS B 103 20.197 -14.579 0.381 1.00 85.64 N ANISOU 3079 NZ LYS B 103 10792 10265 11484 688 455 -4 N ATOM 3080 N LEU B 104 23.383 -18.489 3.646 1.00 53.21 N ANISOU 3080 N LEU B 104 6793 5950 7475 709 204 -275 N ATOM 3081 CA LEU B 104 22.793 -19.701 4.195 1.00 55.44 C ANISOU 3081 CA LEU B 104 7159 6109 7798 662 46 -285 C ATOM 3082 C LEU B 104 21.270 -19.745 3.985 1.00 61.81 C ANISOU 3082 C LEU B 104 7987 6903 8597 587 33 -228 C ATOM 3083 O LEU B 104 20.514 -19.020 4.628 1.00 62.16 O ANISOU 3083 O LEU B 104 8002 6976 8639 487 115 -154 O ATOM 3084 CB LEU B 104 23.129 -19.805 5.672 1.00 53.75 C ANISOU 3084 CB LEU B 104 6973 5826 7624 560 15 -234 C ATOM 3085 CG LEU B 104 23.006 -21.212 6.217 1.00 56.71 C ANISOU 3085 CG LEU B 104 7442 6062 8044 512 -197 -228 C ATOM 3086 CD1 LEU B 104 24.070 -22.048 5.559 1.00 58.78 C ANISOU 3086 CD1 LEU B 104 7719 6272 8344 675 -329 -366 C ATOM 3087 CD2 LEU B 104 23.152 -21.219 7.726 1.00 57.20 C ANISOU 3087 CD2 LEU B 104 7530 6092 8111 373 -220 -138 C ATOM 3088 N GLU B 105 20.826 -20.642 3.111 1.00 64.63 N ANISOU 3088 N GLU B 105 8382 7223 8952 645 -87 -285 N ATOM 3089 CA GLU B 105 19.445 -20.652 2.648 1.00 63.26 C ANISOU 3089 CA GLU B 105 8211 7057 8768 595 -100 -247 C ATOM 3090 C GLU B 105 18.670 -21.892 3.089 1.00 61.02 C ANISOU 3090 C GLU B 105 7996 6648 8539 490 -289 -216 C ATOM 3091 O GLU B 105 19.251 -22.934 3.328 1.00 63.73 O ANISOU 3091 O GLU B 105 8408 6869 8936 506 -460 -254 O ATOM 3092 CB GLU B 105 19.440 -20.530 1.133 1.00 70.71 C ANISOU 3092 CB GLU B 105 9132 8083 9652 734 -86 -325 C ATOM 3093 CG GLU B 105 20.176 -19.297 0.652 1.00 76.42 C ANISOU 3093 CG GLU B 105 9783 8943 10310 794 83 -307 C ATOM 3094 CD GLU B 105 20.065 -19.092 -0.843 1.00 88.43 C ANISOU 3094 CD GLU B 105 11273 10590 11734 898 104 -347 C ATOM 3095 OE1 GLU B 105 20.654 -19.903 -1.608 1.00 88.97 O ANISOU 3095 OE1 GLU B 105 11340 10716 11748 1020 25 -474 O ATOM 3096 OE2 GLU B 105 19.382 -18.116 -1.243 1.00 91.92 O ANISOU 3096 OE2 GLU B 105 11690 11084 12152 864 185 -259 O ATOM 3097 N ILE B 106 17.353 -21.776 3.205 1.00 60.65 N ANISOU 3097 N ILE B 106 7926 6631 8489 376 -278 -143 N ATOM 3098 CA ILE B 106 16.549 -22.862 3.765 1.00 61.07 C ANISOU 3098 CA ILE B 106 8025 6592 8588 217 -451 -67 C ATOM 3099 C ILE B 106 16.268 -23.928 2.729 1.00 66.39 C ANISOU 3099 C ILE B 106 8763 7147 9314 287 -653 -143 C ATOM 3100 O ILE B 106 15.798 -23.633 1.637 1.00 66.31 O ANISOU 3100 O ILE B 106 8723 7197 9275 387 -616 -211 O ATOM 3101 CB ILE B 106 15.190 -22.366 4.292 1.00 55.27 C ANISOU 3101 CB ILE B 106 7204 5980 7817 56 -363 30 C ATOM 3102 CG1 ILE B 106 15.322 -20.969 4.884 1.00 62.08 C ANISOU 3102 CG1 ILE B 106 7974 6988 8624 69 -144 31 C ATOM 3103 CG2 ILE B 106 14.631 -23.327 5.319 1.00 46.33 C ANISOU 3103 CG2 ILE B 106 6094 4812 6699 -174 -504 164 C ATOM 3104 CD1 ILE B 106 14.407 -19.967 4.246 1.00 63.20 C ANISOU 3104 CD1 ILE B 106 8026 7238 8748 126 -30 -5 C ATOM 3105 N LYS B 107 16.556 -25.176 3.065 1.00 74.43 N ANISOU 3105 N LYS B 107 9874 7987 10417 240 -894 -135 N ATOM 3106 CA LYS B 107 16.216 -26.268 2.171 1.00 76.24 C ANISOU 3106 CA LYS B 107 10171 8071 10725 301 -1138 -222 C ATOM 3107 C LYS B 107 14.717 -26.542 2.307 1.00 67.84 C ANISOU 3107 C LYS B 107 9087 7009 9682 97 -1199 -93 C ATOM 3108 O LYS B 107 14.159 -26.476 3.403 1.00 65.89 O ANISOU 3108 O LYS B 107 8807 6810 9417 -132 -1165 82 O ATOM 3109 CB LYS B 107 17.048 -27.523 2.499 1.00 80.29 C ANISOU 3109 CB LYS B 107 10798 8350 11357 328 -1428 -269 C ATOM 3110 CG LYS B 107 16.864 -28.696 1.525 1.00 82.75 C ANISOU 3110 CG LYS B 107 11187 8478 11777 441 -1731 -415 C ATOM 3111 CD LYS B 107 18.079 -28.892 0.638 1.00 89.87 C ANISOU 3111 CD LYS B 107 12088 9381 12675 748 -1783 -684 C ATOM 3112 CE LYS B 107 19.290 -29.330 1.466 1.00100.30 C ANISOU 3112 CE LYS B 107 13461 10579 14071 786 -1902 -708 C ATOM 3113 NZ LYS B 107 20.611 -29.170 0.769 1.00103.40 N ANISOU 3113 NZ LYS B 107 13767 11142 14377 1050 -1821 -942 N ATOM 3114 N ARG B 108 14.058 -26.817 1.189 1.00 62.19 N ANISOU 3114 N ARG B 108 8370 6274 8984 178 -1282 -183 N ATOM 3115 CA ARG B 108 12.694 -27.334 1.231 1.00 62.55 C ANISOU 3115 CA ARG B 108 8401 6288 9079 -14 -1406 -76 C ATOM 3116 C ARG B 108 12.479 -28.304 0.077 1.00 61.69 C ANISOU 3116 C ARG B 108 8364 6017 9060 104 -1667 -219 C ATOM 3117 O ARG B 108 13.362 -28.475 -0.759 1.00 57.14 O ANISOU 3117 O ARG B 108 7832 5400 8481 350 -1720 -418 O ATOM 3118 CB ARG B 108 11.668 -26.199 1.197 1.00 55.80 C ANISOU 3118 CB ARG B 108 7408 5665 8127 -74 -1159 -19 C ATOM 3119 CG ARG B 108 11.908 -25.174 0.106 1.00 49.92 C ANISOU 3119 CG ARG B 108 6620 5047 7301 161 -978 -158 C ATOM 3120 CD ARG B 108 10.617 -24.674 -0.434 1.00 53.99 C ANISOU 3120 CD ARG B 108 7045 5680 7790 131 -917 -145 C ATOM 3121 NE ARG B 108 9.866 -25.778 -1.025 1.00 64.34 N ANISOU 3121 NE ARG B 108 8398 6868 9182 82 -1162 -168 N ATOM 3122 CZ ARG B 108 8.542 -25.891 -1.001 1.00 56.52 C ANISOU 3122 CZ ARG B 108 7329 5931 8217 -69 -1204 -96 C ATOM 3123 NH1 ARG B 108 7.802 -24.965 -0.409 1.00 44.52 N ANISOU 3123 NH1 ARG B 108 5671 4605 6638 -168 -1011 -16 N ATOM 3124 NH2 ARG B 108 7.967 -26.939 -1.569 1.00 58.82 N ANISOU 3124 NH2 ARG B 108 7668 6084 8598 -112 -1455 -122 N ATOM 3125 N ALA B 109 11.311 -28.934 0.018 1.00 61.49 N ANISOU 3125 N ALA B 109 8336 5922 9107 -68 -1833 -133 N ATOM 3126 CA ALA B 109 11.079 -29.918 -1.027 1.00 61.08 C ANISOU 3126 CA ALA B 109 8358 5688 9159 38 -2122 -280 C ATOM 3127 C ALA B 109 11.100 -29.219 -2.381 1.00 58.19 C ANISOU 3127 C ALA B 109 7942 5483 8685 302 -1975 -480 C ATOM 3128 O ALA B 109 10.797 -28.041 -2.465 1.00 50.56 O ANISOU 3128 O ALA B 109 6876 4740 7594 314 -1691 -437 O ATOM 3129 CB ALA B 109 9.784 -30.604 -0.805 1.00 64.64 C ANISOU 3129 CB ALA B 109 8798 6055 9706 -224 -2313 -127 C ATOM 3130 N ASP B 110 11.477 -29.927 -3.440 1.00 63.99 N ANISOU 3130 N ASP B 110 8742 6111 9460 518 -2184 -705 N ATOM 3131 CA ASP B 110 11.519 -29.297 -4.755 1.00 62.83 C ANISOU 3131 CA ASP B 110 8542 6157 9172 755 -2052 -884 C ATOM 3132 C ASP B 110 10.103 -28.907 -5.079 1.00 62.37 C ANISOU 3132 C ASP B 110 8416 6187 9096 633 -1999 -788 C ATOM 3133 O ASP B 110 9.162 -29.445 -4.508 1.00 65.13 O ANISOU 3133 O ASP B 110 8765 6420 9560 402 -2138 -647 O ATOM 3134 CB ASP B 110 12.023 -30.237 -5.852 1.00 72.34 C ANISOU 3134 CB ASP B 110 9811 7266 10409 1006 -2316 -1171 C ATOM 3135 CG ASP B 110 13.485 -30.596 -5.709 1.00 86.93 C ANISOU 3135 CG ASP B 110 11697 9069 12263 1187 -2374 -1330 C ATOM 3136 OD1 ASP B 110 14.238 -29.922 -4.972 1.00 88.12 O ANISOU 3136 OD1 ASP B 110 11816 9312 12356 1155 -2156 -1231 O ATOM 3137 OD2 ASP B 110 13.883 -31.575 -6.368 1.00 99.51 O ANISOU 3137 OD2 ASP B 110 13328 10572 13910 1365 -2640 -1563 O ATOM 3138 N ALA B 111 9.956 -27.940 -5.970 1.00 58.09 N ANISOU 3138 N ALA B 111 7806 5863 8403 773 -1800 -848 N ATOM 3139 CA ALA B 111 8.655 -27.407 -6.284 1.00 48.91 C ANISOU 3139 CA ALA B 111 6566 4802 7217 683 -1734 -766 C ATOM 3140 C ALA B 111 8.604 -26.967 -7.741 1.00 61.29 C ANISOU 3140 C ALA B 111 8117 6524 8648 904 -1698 -919 C ATOM 3141 O ALA B 111 9.495 -26.273 -8.212 1.00 67.65 O ANISOU 3141 O ALA B 111 8911 7485 9308 1064 -1535 -978 O ATOM 3142 CB ALA B 111 8.367 -26.251 -5.359 1.00 40.26 C ANISOU 3142 CB ALA B 111 5375 3845 6076 543 -1461 -582 C ATOM 3143 N ALA B 112 7.543 -27.335 -8.449 1.00 67.91 N ANISOU 3143 N ALA B 112 8943 7339 9519 894 -1851 -965 N ATOM 3144 CA ALA B 112 7.428 -26.972 -9.855 1.00 61.96 C ANISOU 3144 CA ALA B 112 8178 6745 8620 1095 -1842 -1105 C ATOM 3145 C ALA B 112 6.859 -25.566 -10.004 1.00 65.93 C ANISOU 3145 C ALA B 112 8593 7441 9018 1070 -1600 -969 C ATOM 3146 O ALA B 112 5.897 -25.195 -9.314 1.00 67.10 O ANISOU 3146 O ALA B 112 8670 7574 9251 897 -1547 -826 O ATOM 3147 CB ALA B 112 6.587 -27.986 -10.599 1.00 53.48 C ANISOU 3147 CB ALA B 112 7135 5555 7629 1116 -2136 -1235 C ATOM 3148 N PRO B 113 7.471 -24.767 -10.896 1.00 66.78 N ANISOU 3148 N PRO B 113 8695 7743 8937 1239 -1466 -1014 N ATOM 3149 CA PRO B 113 7.041 -23.382 -11.138 1.00 64.71 C ANISOU 3149 CA PRO B 113 8369 7635 8584 1230 -1280 -880 C ATOM 3150 C PRO B 113 5.696 -23.296 -11.845 1.00 66.07 C ANISOU 3150 C PRO B 113 8504 7831 8769 1225 -1388 -885 C ATOM 3151 O PRO B 113 5.403 -24.104 -12.724 1.00 63.37 O ANISOU 3151 O PRO B 113 8197 7479 8403 1311 -1577 -1030 O ATOM 3152 CB PRO B 113 8.132 -22.831 -12.060 1.00 57.46 C ANISOU 3152 CB PRO B 113 7467 6915 7449 1397 -1175 -925 C ATOM 3153 CG PRO B 113 8.730 -24.036 -12.716 1.00 52.13 C ANISOU 3153 CG PRO B 113 6840 6243 6722 1541 -1347 -1153 C ATOM 3154 CD PRO B 113 8.667 -25.123 -11.684 1.00 57.69 C ANISOU 3154 CD PRO B 113 7585 6691 7644 1440 -1494 -1189 C ATOM 3155 N THR B 114 4.881 -22.326 -11.454 1.00 68.07 N ANISOU 3155 N THR B 114 8680 8114 9068 1138 -1285 -750 N ATOM 3156 CA THR B 114 3.717 -21.971 -12.245 1.00 71.79 C ANISOU 3156 CA THR B 114 9105 8644 9526 1167 -1365 -753 C ATOM 3157 C THR B 114 4.186 -20.932 -13.260 1.00 67.02 C ANISOU 3157 C THR B 114 8528 8203 8733 1306 -1280 -712 C ATOM 3158 O THR B 114 4.801 -19.937 -12.887 1.00 66.22 O ANISOU 3158 O THR B 114 8420 8144 8597 1296 -1116 -596 O ATOM 3159 CB THR B 114 2.586 -21.395 -11.370 1.00 75.08 C ANISOU 3159 CB THR B 114 9403 9039 10085 1029 -1316 -654 C ATOM 3160 OG1 THR B 114 2.019 -22.436 -10.564 1.00 69.35 O ANISOU 3160 OG1 THR B 114 8636 8209 9504 866 -1418 -667 O ATOM 3161 CG2 THR B 114 1.497 -20.774 -12.245 1.00 76.96 C ANISOU 3161 CG2 THR B 114 9586 9355 10302 1094 -1388 -656 C ATOM 3162 N VAL B 115 3.921 -21.179 -14.541 1.00 60.74 N ANISOU 3162 N VAL B 115 7764 7504 7812 1421 -1407 -800 N ATOM 3163 CA VAL B 115 4.410 -20.305 -15.603 1.00 58.04 C ANISOU 3163 CA VAL B 115 7449 7353 7249 1530 -1348 -741 C ATOM 3164 C VAL B 115 3.265 -19.670 -16.362 1.00 62.77 C ANISOU 3164 C VAL B 115 8022 7998 7830 1555 -1442 -686 C ATOM 3165 O VAL B 115 2.346 -20.351 -16.809 1.00 72.18 O ANISOU 3165 O VAL B 115 9201 9159 9067 1577 -1611 -796 O ATOM 3166 CB VAL B 115 5.291 -21.064 -16.609 1.00 60.66 C ANISOU 3166 CB VAL B 115 7834 7843 7372 1670 -1408 -900 C ATOM 3167 CG1 VAL B 115 5.539 -20.215 -17.855 1.00 53.45 C ANISOU 3167 CG1 VAL B 115 6930 7185 6193 1755 -1375 -822 C ATOM 3168 CG2 VAL B 115 6.612 -21.498 -15.956 1.00 65.36 C ANISOU 3168 CG2 VAL B 115 8446 8427 7961 1676 -1307 -953 C ATOM 3169 N SER B 116 3.330 -18.357 -16.511 1.00 59.30 N ANISOU 3169 N SER B 116 7577 7617 7337 1551 -1356 -514 N ATOM 3170 CA SER B 116 2.287 -17.603 -17.180 1.00 60.36 C ANISOU 3170 CA SER B 116 7690 7773 7471 1580 -1462 -442 C ATOM 3171 C SER B 116 2.937 -16.588 -18.104 1.00 67.44 C ANISOU 3171 C SER B 116 8645 8830 8150 1622 -1429 -278 C ATOM 3172 O SER B 116 3.843 -15.864 -17.702 1.00 74.00 O ANISOU 3172 O SER B 116 9491 9671 8954 1573 -1294 -143 O ATOM 3173 CB SER B 116 1.434 -16.861 -16.152 1.00 58.38 C ANISOU 3173 CB SER B 116 7353 7371 7457 1507 -1438 -375 C ATOM 3174 OG SER B 116 1.404 -17.557 -14.920 1.00 66.53 O ANISOU 3174 OG SER B 116 8329 8298 8652 1413 -1371 -450 O ATOM 3175 N ILE B 117 2.471 -16.518 -19.341 1.00 65.96 N ANISOU 3175 N ILE B 117 8485 8775 7802 1694 -1565 -274 N ATOM 3176 CA ILE B 117 2.975 -15.506 -20.252 1.00 63.13 C ANISOU 3176 CA ILE B 117 8177 8586 7222 1698 -1559 -73 C ATOM 3177 C ILE B 117 1.913 -14.419 -20.503 1.00 66.46 C ANISOU 3177 C ILE B 117 8598 8905 7749 1694 -1699 76 C ATOM 3178 O ILE B 117 0.707 -14.682 -20.415 1.00 74.52 O ANISOU 3178 O ILE B 117 9569 9814 8929 1731 -1827 -32 O ATOM 3179 CB ILE B 117 3.484 -16.147 -21.548 1.00 58.18 C ANISOU 3179 CB ILE B 117 7584 8254 6266 1782 -1602 -156 C ATOM 3180 CG1 ILE B 117 3.845 -15.065 -22.567 1.00 60.36 C ANISOU 3180 CG1 ILE B 117 7904 8746 6286 1751 -1619 95 C ATOM 3181 CG2 ILE B 117 2.460 -17.136 -22.078 1.00 52.53 C ANISOU 3181 CG2 ILE B 117 6858 7526 5575 1875 -1783 -374 C ATOM 3182 CD1 ILE B 117 4.590 -15.571 -23.776 1.00 62.17 C ANISOU 3182 CD1 ILE B 117 8138 9357 6127 1816 -1610 31 C ATOM 3183 N PHE B 118 2.365 -13.190 -20.755 1.00 59.29 N ANISOU 3183 N PHE B 118 7735 8020 6773 1641 -1691 325 N ATOM 3184 CA PHE B 118 1.461 -12.079 -21.024 1.00 58.39 C ANISOU 3184 CA PHE B 118 7634 7781 6769 1648 -1865 478 C ATOM 3185 C PHE B 118 1.962 -11.269 -22.223 1.00 67.42 C ANISOU 3185 C PHE B 118 8866 9108 7642 1605 -1944 741 C ATOM 3186 O PHE B 118 3.129 -10.903 -22.277 1.00 80.78 O ANISOU 3186 O PHE B 118 10590 10919 9181 1514 -1823 903 O ATOM 3187 CB PHE B 118 1.433 -11.144 -19.809 1.00 53.15 C ANISOU 3187 CB PHE B 118 6936 6867 6391 1601 -1822 549 C ATOM 3188 CG PHE B 118 1.024 -11.809 -18.521 1.00 54.74 C ANISOU 3188 CG PHE B 118 7036 6932 6830 1610 -1725 329 C ATOM 3189 CD1 PHE B 118 -0.241 -11.616 -17.997 1.00 55.11 C ANISOU 3189 CD1 PHE B 118 6986 6834 7119 1659 -1830 220 C ATOM 3190 CD2 PHE B 118 1.920 -12.604 -17.816 1.00 59.97 C ANISOU 3190 CD2 PHE B 118 7688 7631 7466 1561 -1534 240 C ATOM 3191 CE1 PHE B 118 -0.613 -12.213 -16.805 1.00 55.44 C ANISOU 3191 CE1 PHE B 118 6916 6806 7344 1635 -1732 44 C ATOM 3192 CE2 PHE B 118 1.562 -13.216 -16.626 1.00 55.43 C ANISOU 3192 CE2 PHE B 118 7025 6946 7089 1539 -1457 76 C ATOM 3193 CZ PHE B 118 0.293 -13.014 -16.118 1.00 59.94 C ANISOU 3193 CZ PHE B 118 7494 7407 7874 1564 -1548 -12 C ATOM 3194 N PRO B 119 1.063 -10.916 -23.148 1.00 63.58 N ANISOU 3194 N PRO B 119 8411 8644 7103 1653 -2159 809 N ATOM 3195 CA PRO B 119 1.346 -10.043 -24.294 1.00 68.28 C ANISOU 3195 CA PRO B 119 9095 9396 7452 1591 -2284 1104 C ATOM 3196 C PRO B 119 1.483 -8.575 -23.889 1.00 77.00 C ANISOU 3196 C PRO B 119 10248 10271 8737 1497 -2374 1386 C ATOM 3197 O PRO B 119 1.105 -8.207 -22.775 1.00 81.17 O ANISOU 3197 O PRO B 119 10730 10508 9601 1525 -2372 1305 O ATOM 3198 CB PRO B 119 0.098 -10.200 -25.167 1.00 69.46 C ANISOU 3198 CB PRO B 119 9253 9563 7577 1692 -2519 1039 C ATOM 3199 CG PRO B 119 -0.510 -11.466 -24.753 1.00 70.44 C ANISOU 3199 CG PRO B 119 9292 9657 7814 1796 -2471 693 C ATOM 3200 CD PRO B 119 -0.227 -11.603 -23.297 1.00 67.24 C ANISOU 3200 CD PRO B 119 8822 9047 7681 1764 -2295 587 C ATOM 3201 N PRO B 120 2.041 -7.740 -24.781 1.00 79.00 N ANISOU 3201 N PRO B 120 10589 10665 8764 1378 -2465 1718 N ATOM 3202 CA PRO B 120 2.040 -6.290 -24.562 1.00 78.61 C ANISOU 3202 CA PRO B 120 10608 10354 8905 1285 -2640 2013 C ATOM 3203 C PRO B 120 0.649 -5.735 -24.233 1.00 79.91 C ANISOU 3203 C PRO B 120 10763 10175 9422 1416 -2897 1926 C ATOM 3204 O PRO B 120 -0.332 -6.060 -24.905 1.00 80.04 O ANISOU 3204 O PRO B 120 10774 10239 9399 1519 -3051 1832 O ATOM 3205 CB PRO B 120 2.522 -5.755 -25.912 1.00 78.49 C ANISOU 3205 CB PRO B 120 10686 10609 8527 1142 -2759 2372 C ATOM 3206 CG PRO B 120 3.503 -6.797 -26.352 1.00 80.20 C ANISOU 3206 CG PRO B 120 10850 11262 8362 1109 -2495 2276 C ATOM 3207 CD PRO B 120 2.902 -8.117 -25.918 1.00 79.11 C ANISOU 3207 CD PRO B 120 10627 11109 8321 1301 -2386 1838 C ATOM 3208 N SER B 121 0.567 -4.900 -23.201 1.00 81.97 N ANISOU 3208 N SER B 121 11009 10106 10028 1423 -2951 1934 N ATOM 3209 CA SER B 121 -0.688 -4.224 -22.893 1.00 79.55 C ANISOU 3209 CA SER B 121 10676 9491 10060 1561 -3219 1844 C ATOM 3210 C SER B 121 -0.982 -3.134 -23.928 1.00 80.64 C ANISOU 3210 C SER B 121 10933 9548 10157 1506 -3536 2157 C ATOM 3211 O SER B 121 -0.108 -2.363 -24.311 1.00 84.00 O ANISOU 3211 O SER B 121 11456 9994 10466 1324 -3548 2472 O ATOM 3212 CB SER B 121 -0.681 -3.652 -21.472 1.00 75.33 C ANISOU 3212 CB SER B 121 10071 8657 9893 1608 -3188 1713 C ATOM 3213 OG SER B 121 0.041 -2.443 -21.418 1.00 79.60 O ANISOU 3213 OG SER B 121 10712 9020 10511 1485 -3306 2002 O ATOM 3214 N SER B 122 -2.223 -3.087 -24.387 1.00 81.88 N ANISOU 3214 N SER B 122 11053 9652 10404 1622 -3698 2027 N ATOM 3215 CA SER B 122 -2.636 -2.129 -25.405 1.00 84.22 C ANISOU 3215 CA SER B 122 11439 9899 10663 1559 -3919 2251 C ATOM 3216 C SER B 122 -2.420 -0.697 -24.943 1.00 84.82 C ANISOU 3216 C SER B 122 11565 9657 11006 1474 -4027 2388 C ATOM 3217 O SER B 122 -2.414 0.232 -25.748 1.00 74.43 O ANISOU 3217 O SER B 122 10354 8280 9648 1365 -4209 2644 O ATOM 3218 CB SER B 122 -4.113 -2.333 -25.727 1.00 87.94 C ANISOU 3218 CB SER B 122 11833 10319 11260 1725 -4073 2022 C ATOM 3219 OG SER B 122 -4.889 -2.223 -24.545 1.00 93.05 O ANISOU 3219 OG SER B 122 12342 10731 12281 1865 -4056 1701 O ATOM 3220 N GLU B 123 -2.274 -0.522 -23.634 1.00 95.10 N ANISOU 3220 N GLU B 123 12789 10756 12588 1527 -3929 2197 N ATOM 3221 CA GLU B 123 -2.002 0.793 -23.079 1.00100.02 C ANISOU 3221 CA GLU B 123 13454 11075 13472 1455 -4034 2276 C ATOM 3222 C GLU B 123 -0.596 1.155 -23.508 1.00 96.40 C ANISOU 3222 C GLU B 123 13119 10718 12791 1212 -3972 2652 C ATOM 3223 O GLU B 123 -0.298 2.317 -23.801 1.00100.77 O ANISOU 3223 O GLU B 123 13766 11100 13422 1069 -4138 2879 O ATOM 3224 CB GLU B 123 -2.111 0.792 -21.547 1.00103.63 C ANISOU 3224 CB GLU B 123 13786 11356 14234 1571 -3917 1956 C ATOM 3225 CG GLU B 123 -3.536 0.746 -20.980 1.00108.80 C ANISOU 3225 CG GLU B 123 14291 11900 15148 1785 -3991 1573 C ATOM 3226 CD GLU B 123 -4.140 -0.656 -20.970 1.00111.38 C ANISOU 3226 CD GLU B 123 14496 12463 15361 1904 -3844 1348 C ATOM 3227 OE1 GLU B 123 -5.373 -0.780 -20.789 1.00110.58 O ANISOU 3227 OE1 GLU B 123 14270 12337 15411 2050 -3915 1078 O ATOM 3228 OE2 GLU B 123 -3.381 -1.634 -21.143 1.00111.03 O ANISOU 3228 OE2 GLU B 123 14477 12635 15076 1847 -3671 1433 O ATOM 3229 N GLN B 124 0.265 0.138 -23.543 1.00 85.48 N ANISOU 3229 N GLN B 124 11724 9625 11127 1157 -3740 2706 N ATOM 3230 CA GLN B 124 1.668 0.315 -23.900 1.00 76.21 C ANISOU 3230 CA GLN B 124 10630 8629 9697 918 -3626 3034 C ATOM 3231 C GLN B 124 1.938 0.367 -25.405 1.00 77.75 C ANISOU 3231 C GLN B 124 10914 9123 9505 760 -3687 3348 C ATOM 3232 O GLN B 124 2.753 1.169 -25.866 1.00 79.02 O ANISOU 3232 O GLN B 124 11149 9315 9559 531 -3716 3661 O ATOM 3233 CB GLN B 124 2.531 -0.765 -23.268 1.00 64.54 C ANISOU 3233 CB GLN B 124 9089 7358 8075 920 -3353 2945 C ATOM 3234 CG GLN B 124 3.989 -0.494 -23.493 1.00 71.92 C ANISOU 3234 CG GLN B 124 10072 8477 8779 668 -3217 3253 C ATOM 3235 CD GLN B 124 4.849 -1.687 -23.214 1.00 72.49 C ANISOU 3235 CD GLN B 124 10076 8864 8604 657 -2942 3186 C ATOM 3236 OE1 GLN B 124 4.462 -2.820 -23.488 1.00 71.22 O ANISOU 3236 OE1 GLN B 124 9849 8938 8274 785 -2789 2924 O ATOM 3237 NE2 GLN B 124 6.026 -1.446 -22.655 1.00 70.01 N ANISOU 3237 NE2 GLN B 124 9745 8570 8284 506 -2779 3301 N ATOM 3238 N LEU B 125 1.274 -0.502 -26.160 1.00 73.38 N ANISOU 3238 N LEU B 125 10342 8807 8732 875 -3703 3252 N ATOM 3239 CA LEU B 125 1.416 -0.513 -27.607 1.00 77.84 C ANISOU 3239 CA LEU B 125 10978 9692 8905 754 -3758 3503 C ATOM 3240 C LEU B 125 1.094 0.856 -28.198 1.00 89.68 C ANISOU 3240 C LEU B 125 12574 10966 10535 637 -4014 3747 C ATOM 3241 O LEU B 125 1.801 1.323 -29.087 1.00 97.21 O ANISOU 3241 O LEU B 125 13599 12112 11223 413 -4026 4071 O ATOM 3242 CB LEU B 125 0.510 -1.572 -28.226 1.00 85.43 C ANISOU 3242 CB LEU B 125 11899 10872 9690 936 -3790 3296 C ATOM 3243 CG LEU B 125 0.896 -3.039 -28.066 1.00 89.96 C ANISOU 3243 CG LEU B 125 12398 11768 10015 1015 -3583 3095 C ATOM 3244 CD1 LEU B 125 -0.341 -3.919 -28.072 1.00 86.48 C ANISOU 3244 CD1 LEU B 125 11896 11296 9667 1251 -3673 2757 C ATOM 3245 CD2 LEU B 125 1.837 -3.430 -29.178 1.00 96.38 C ANISOU 3245 CD2 LEU B 125 13237 13086 10297 857 -3457 3299 C ATOM 3246 N THR B 126 0.030 1.501 -27.710 1.00 97.04 N ANISOU 3246 N THR B 126 13497 11502 11871 779 -4224 3580 N ATOM 3247 CA THR B 126 -0.341 2.847 -28.182 1.00102.56 C ANISOU 3247 CA THR B 126 14290 11931 12747 680 -4514 3781 C ATOM 3248 C THR B 126 0.654 3.907 -27.680 1.00 97.03 C ANISOU 3248 C THR B 126 13641 11020 12204 463 -4537 3991 C ATOM 3249 O THR B 126 0.584 5.076 -28.044 1.00 94.07 O ANISOU 3249 O THR B 126 13352 10418 11971 327 -4787 4197 O ATOM 3250 CB THR B 126 -1.834 3.237 -27.868 1.00 95.35 C ANISOU 3250 CB THR B 126 13338 10679 12209 906 -4753 3506 C ATOM 3251 OG1 THR B 126 -2.049 3.338 -26.453 1.00 95.65 O ANISOU 3251 OG1 THR B 126 13282 10441 12619 1046 -4700 3195 O ATOM 3252 CG2 THR B 126 -2.802 2.214 -28.461 1.00 88.93 C ANISOU 3252 CG2 THR B 126 12466 10089 11233 1089 -4745 3320 C ATOM 3253 N SER B 127 1.573 3.486 -26.824 1.00 96.81 N ANISOU 3253 N SER B 127 13558 11059 12166 427 -4292 3931 N ATOM 3254 CA SER B 127 2.770 4.268 -26.570 1.00100.14 C ANISOU 3254 CA SER B 127 14018 11416 12613 173 -4260 4180 C ATOM 3255 C SER B 127 3.794 4.024 -27.678 1.00106.82 C ANISOU 3255 C SER B 127 14896 12703 12987 -83 -4126 4525 C ATOM 3256 O SER B 127 4.463 4.955 -28.124 1.00114.29 O ANISOU 3256 O SER B 127 15898 13626 13901 -351 -4228 4843 O ATOM 3257 CB SER B 127 3.380 3.918 -25.216 1.00 91.40 C ANISOU 3257 CB SER B 127 12831 10223 11674 232 -4047 3977 C ATOM 3258 OG SER B 127 4.674 4.476 -25.114 1.00 90.58 O ANISOU 3258 OG SER B 127 12749 10155 11511 -34 -3975 4236 O ATOM 3259 N GLY B 128 3.866 2.782 -28.159 1.00101.79 N ANISOU 3259 N GLY B 128 14211 12484 11981 -5 -3917 4446 N ATOM 3260 CA GLY B 128 4.903 2.368 -29.092 1.00100.26 C ANISOU 3260 CA GLY B 128 14004 12788 11301 -217 -3729 4684 C ATOM 3261 C GLY B 128 5.997 1.463 -28.543 1.00 99.81 C ANISOU 3261 C GLY B 128 13850 13028 11047 -248 -3395 4597 C ATOM 3262 O GLY B 128 7.056 1.307 -29.154 1.00 97.46 O ANISOU 3262 O GLY B 128 13509 13130 10390 -457 -3221 4787 O ATOM 3263 N GLY B 129 5.759 0.889 -27.368 1.00103.92 N ANISOU 3263 N GLY B 129 14317 13359 11809 -45 -3307 4300 N ATOM 3264 CA GLY B 129 6.566 -0.222 -26.886 1.00 98.56 C ANISOU 3264 CA GLY B 129 13541 12979 10929 -15 -3008 4160 C ATOM 3265 C GLY B 129 5.824 -1.546 -26.981 1.00 95.48 C ANISOU 3265 C GLY B 129 13100 12778 10400 233 -2955 3867 C ATOM 3266 O GLY B 129 4.620 -1.587 -27.225 1.00 98.40 O ANISOU 3266 O GLY B 129 13503 12988 10897 401 -3147 3740 O ATOM 3267 N ALA B 130 6.553 -2.642 -26.819 1.00 91.09 N ANISOU 3267 N ALA B 130 12447 12583 9580 253 -2701 3747 N ATOM 3268 CA ALA B 130 5.945 -3.954 -26.642 1.00 76.67 C ANISOU 3268 CA ALA B 130 10544 10863 7726 500 -2581 3335 C ATOM 3269 C ALA B 130 6.798 -4.709 -25.655 1.00 69.09 C ANISOU 3269 C ALA B 130 9478 9956 6816 539 -2255 3073 C ATOM 3270 O ALA B 130 7.992 -4.832 -25.868 1.00 73.79 O ANISOU 3270 O ALA B 130 10020 10879 7138 395 -2066 3193 O ATOM 3271 CB ALA B 130 5.889 -4.690 -27.955 1.00 76.32 C ANISOU 3271 CB ALA B 130 10478 11304 7216 519 -2555 3318 C ATOM 3272 N SER B 131 6.205 -5.209 -24.577 1.00 65.05 N ANISOU 3272 N SER B 131 8926 9147 6643 723 -2193 2724 N ATOM 3273 CA SER B 131 6.963 -6.017 -23.630 1.00 68.65 C ANISOU 3273 CA SER B 131 9290 9647 7146 764 -1903 2469 C ATOM 3274 C SER B 131 6.199 -7.268 -23.305 1.00 75.15 C ANISOU 3274 C SER B 131 10054 10450 8049 978 -1827 2052 C ATOM 3275 O SER B 131 5.148 -7.211 -22.687 1.00 86.27 O ANISOU 3275 O SER B 131 11461 11547 9770 1093 -1936 1896 O ATOM 3276 CB SER B 131 7.208 -5.264 -22.330 1.00 60.41 C ANISOU 3276 CB SER B 131 8251 8225 6476 721 -1896 2501 C ATOM 3277 OG SER B 131 7.493 -3.917 -22.589 1.00 61.77 O ANISOU 3277 OG SER B 131 8506 8265 6698 542 -2088 2891 O ATOM 3278 N VAL B 132 6.737 -8.406 -23.698 1.00 68.33 N ANISOU 3278 N VAL B 132 9129 9925 6910 1030 -1651 1862 N ATOM 3279 CA VAL B 132 6.109 -9.651 -23.340 1.00 62.08 C ANISOU 3279 CA VAL B 132 8287 9086 6213 1209 -1600 1478 C ATOM 3280 C VAL B 132 6.736 -10.043 -22.030 1.00 62.78 C ANISOU 3280 C VAL B 132 8323 9025 6506 1211 -1405 1319 C ATOM 3281 O VAL B 132 7.936 -10.296 -21.949 1.00 77.54 O ANISOU 3281 O VAL B 132 10153 11098 8211 1152 -1229 1330 O ATOM 3282 CB VAL B 132 6.367 -10.747 -24.392 1.00 65.04 C ANISOU 3282 CB VAL B 132 8626 9868 6217 1290 -1551 1310 C ATOM 3283 CG1 VAL B 132 5.740 -12.050 -23.956 1.00 64.52 C ANISOU 3283 CG1 VAL B 132 8520 9699 6296 1458 -1536 922 C ATOM 3284 CG2 VAL B 132 5.832 -10.326 -25.753 1.00 65.30 C ANISOU 3284 CG2 VAL B 132 8712 10106 5995 1273 -1741 1490 C ATOM 3285 N VAL B 133 5.932 -10.085 -20.989 1.00 54.82 N ANISOU 3285 N VAL B 133 7299 7685 5844 1275 -1438 1170 N ATOM 3286 CA VAL B 133 6.432 -10.501 -19.687 1.00 60.19 C ANISOU 3286 CA VAL B 133 7930 8225 6716 1274 -1267 1016 C ATOM 3287 C VAL B 133 6.073 -11.962 -19.438 1.00 61.39 C ANISOU 3287 C VAL B 133 8034 8406 6885 1386 -1214 693 C ATOM 3288 O VAL B 133 5.079 -12.461 -19.968 1.00 60.41 O ANISOU 3288 O VAL B 133 7909 8289 6756 1471 -1343 573 O ATOM 3289 CB VAL B 133 5.888 -9.608 -18.559 1.00 57.29 C ANISOU 3289 CB VAL B 133 7556 7508 6705 1257 -1323 1053 C ATOM 3290 CG1 VAL B 133 6.131 -10.237 -17.206 1.00 51.84 C ANISOU 3290 CG1 VAL B 133 6804 6695 6198 1273 -1163 849 C ATOM 3291 CG2 VAL B 133 6.514 -8.232 -18.641 1.00 57.30 C ANISOU 3291 CG2 VAL B 133 7610 7439 6720 1133 -1379 1362 C ATOM 3292 N CYS B 134 6.921 -12.664 -18.692 1.00 58.03 N ANISOU 3292 N CYS B 134 7573 7998 6476 1380 -1049 562 N ATOM 3293 CA CYS B 134 6.664 -14.060 -18.353 1.00 53.57 C ANISOU 3293 CA CYS B 134 6976 7414 5963 1466 -1033 276 C ATOM 3294 C CYS B 134 6.950 -14.290 -16.881 1.00 59.06 C ANISOU 3294 C CYS B 134 7640 7906 6895 1422 -918 199 C ATOM 3295 O CYS B 134 8.009 -13.919 -16.384 1.00 60.14 O ANISOU 3295 O CYS B 134 7774 8062 7017 1361 -786 283 O ATOM 3296 CB CYS B 134 7.525 -14.976 -19.214 1.00 44.86 C ANISOU 3296 CB CYS B 134 5867 6610 4568 1533 -990 152 C ATOM 3297 SG CYS B 134 7.336 -16.712 -18.879 1.00 94.20 S ANISOU 3297 SG CYS B 134 12097 12799 10897 1644 -1032 -200 S ATOM 3298 N PHE B 135 5.996 -14.880 -16.171 1.00 60.70 N ANISOU 3298 N PHE B 135 7815 7937 7312 1439 -971 51 N ATOM 3299 CA PHE B 135 6.179 -15.142 -14.748 1.00 59.34 C ANISOU 3299 CA PHE B 135 7605 7601 7341 1381 -872 -12 C ATOM 3300 C PHE B 135 6.469 -16.611 -14.501 1.00 58.22 C ANISOU 3300 C PHE B 135 7464 7467 7191 1404 -869 -207 C ATOM 3301 O PHE B 135 5.831 -17.491 -15.096 1.00 57.13 O ANISOU 3301 O PHE B 135 7330 7353 7024 1461 -997 -340 O ATOM 3302 CB PHE B 135 4.949 -14.718 -13.956 1.00 59.49 C ANISOU 3302 CB PHE B 135 7561 7444 7598 1354 -928 -24 C ATOM 3303 CG PHE B 135 4.801 -13.232 -13.827 1.00 69.60 C ANISOU 3303 CG PHE B 135 8837 8648 8961 1342 -944 135 C ATOM 3304 CD1 PHE B 135 5.918 -12.427 -13.642 1.00 72.91 C ANISOU 3304 CD1 PHE B 135 9295 9069 9339 1294 -852 283 C ATOM 3305 CD2 PHE B 135 3.548 -12.636 -13.900 1.00 67.92 C ANISOU 3305 CD2 PHE B 135 8574 8352 8881 1382 -1078 130 C ATOM 3306 CE1 PHE B 135 5.783 -11.060 -13.525 1.00 72.37 C ANISOU 3306 CE1 PHE B 135 9233 8887 9375 1279 -913 431 C ATOM 3307 CE2 PHE B 135 3.410 -11.275 -13.787 1.00 66.49 C ANISOU 3307 CE2 PHE B 135 8394 8065 8803 1392 -1140 255 C ATOM 3308 CZ PHE B 135 4.523 -10.486 -13.594 1.00 70.71 C ANISOU 3308 CZ PHE B 135 8985 8569 9312 1338 -1069 409 C ATOM 3309 N LEU B 136 7.461 -16.871 -13.653 1.00 45.91 N ANISOU 3309 N LEU B 136 5904 5875 5663 1364 -749 -225 N ATOM 3310 CA LEU B 136 7.723 -18.222 -13.189 1.00 43.03 C ANISOU 3310 CA LEU B 136 5548 5454 5348 1373 -778 -396 C ATOM 3311 C LEU B 136 7.594 -18.186 -11.691 1.00 49.94 C ANISOU 3311 C LEU B 136 6389 6157 6428 1263 -710 -367 C ATOM 3312 O LEU B 136 8.427 -17.591 -11.023 1.00 63.18 O ANISOU 3312 O LEU B 136 8063 7823 8119 1222 -580 -286 O ATOM 3313 CB LEU B 136 9.116 -18.678 -13.621 1.00 47.90 C ANISOU 3313 CB LEU B 136 6188 6224 5790 1446 -722 -467 C ATOM 3314 CG LEU B 136 9.286 -18.685 -15.154 1.00 55.26 C ANISOU 3314 CG LEU B 136 7127 7406 6462 1557 -776 -506 C ATOM 3315 CD1 LEU B 136 9.782 -17.344 -15.644 1.00 67.93 C ANISOU 3315 CD1 LEU B 136 8722 9174 7916 1513 -668 -286 C ATOM 3316 CD2 LEU B 136 10.209 -19.767 -15.652 1.00 42.86 C ANISOU 3316 CD2 LEU B 136 5554 5986 4746 1680 -810 -720 C ATOM 3317 N ASN B 137 6.546 -18.806 -11.157 1.00 46.41 N ANISOU 3317 N ASN B 137 5907 5597 6129 1201 -799 -426 N ATOM 3318 CA ASN B 137 6.226 -18.617 -9.751 1.00 45.52 C ANISOU 3318 CA ASN B 137 5734 5383 6179 1080 -728 -381 C ATOM 3319 C ASN B 137 6.343 -19.870 -8.903 1.00 56.50 C ANISOU 3319 C ASN B 137 7135 6677 7657 987 -778 -447 C ATOM 3320 O ASN B 137 5.965 -20.956 -9.330 1.00 64.69 O ANISOU 3320 O ASN B 137 8200 7670 8711 991 -934 -537 O ATOM 3321 CB ASN B 137 4.843 -18.004 -9.604 1.00 47.37 C ANISOU 3321 CB ASN B 137 5874 5610 6512 1047 -767 -356 C ATOM 3322 CG ASN B 137 4.811 -16.524 -9.964 1.00 51.78 C ANISOU 3322 CG ASN B 137 6421 6203 7050 1112 -720 -261 C ATOM 3323 OD1 ASN B 137 5.812 -15.953 -10.361 1.00 53.16 O ANISOU 3323 OD1 ASN B 137 6660 6413 7125 1154 -656 -184 O ATOM 3324 ND2 ASN B 137 3.650 -15.903 -9.816 1.00 49.39 N ANISOU 3324 ND2 ASN B 137 6028 5890 6850 1115 -771 -265 N ATOM 3325 N ASN B 138 6.922 -19.690 -7.716 1.00 58.03 N ANISOU 3325 N ASN B 138 7313 6828 7907 904 -665 -394 N ATOM 3326 CA ASN B 138 6.985 -20.692 -6.640 1.00 57.21 C ANISOU 3326 CA ASN B 138 7211 6629 7896 773 -708 -402 C ATOM 3327 C ASN B 138 7.628 -22.034 -6.921 1.00 61.78 C ANISOU 3327 C ASN B 138 7885 7115 8475 801 -854 -493 C ATOM 3328 O ASN B 138 7.007 -23.074 -6.698 1.00 69.49 O ANISOU 3328 O ASN B 138 8868 7992 9543 704 -1017 -514 O ATOM 3329 CB ASN B 138 5.597 -20.910 -6.049 1.00 53.99 C ANISOU 3329 CB ASN B 138 6702 6223 7590 630 -763 -374 C ATOM 3330 CG ASN B 138 4.987 -19.628 -5.570 1.00 53.95 C ANISOU 3330 CG ASN B 138 6579 6313 7604 620 -633 -329 C ATOM 3331 OD1 ASN B 138 4.544 -18.808 -6.376 1.00 49.26 O ANISOU 3331 OD1 ASN B 138 5963 5768 6987 727 -636 -341 O ATOM 3332 ND2 ASN B 138 4.999 -19.414 -4.252 1.00 56.88 N ANISOU 3332 ND2 ASN B 138 6877 6718 8018 503 -534 -287 N ATOM 3333 N PHE B 139 8.871 -22.002 -7.389 1.00 59.59 N ANISOU 3333 N PHE B 139 7668 6872 8102 930 -813 -549 N ATOM 3334 CA PHE B 139 9.637 -23.215 -7.669 1.00 58.81 C ANISOU 3334 CA PHE B 139 7646 6696 8003 1005 -962 -683 C ATOM 3335 C PHE B 139 10.798 -23.324 -6.706 1.00 57.69 C ANISOU 3335 C PHE B 139 7530 6501 7890 977 -892 -661 C ATOM 3336 O PHE B 139 11.265 -22.326 -6.159 1.00 58.91 O ANISOU 3336 O PHE B 139 7647 6724 8012 947 -703 -563 O ATOM 3337 CB PHE B 139 10.204 -23.177 -9.082 1.00 58.22 C ANISOU 3337 CB PHE B 139 7591 6766 7763 1206 -982 -813 C ATOM 3338 CG PHE B 139 11.030 -21.961 -9.355 1.00 58.20 C ANISOU 3338 CG PHE B 139 7555 6944 7617 1263 -771 -736 C ATOM 3339 CD1 PHE B 139 10.433 -20.760 -9.673 1.00 65.88 C ANISOU 3339 CD1 PHE B 139 8486 8004 8540 1235 -667 -605 C ATOM 3340 CD2 PHE B 139 12.396 -22.007 -9.271 1.00 54.28 C ANISOU 3340 CD2 PHE B 139 7060 6516 7046 1335 -698 -786 C ATOM 3341 CE1 PHE B 139 11.198 -19.638 -9.906 1.00 62.63 C ANISOU 3341 CE1 PHE B 139 8052 7728 8017 1257 -510 -503 C ATOM 3342 CE2 PHE B 139 13.156 -20.886 -9.506 1.00 49.35 C ANISOU 3342 CE2 PHE B 139 6394 6062 6295 1352 -516 -688 C ATOM 3343 CZ PHE B 139 12.561 -19.712 -9.821 1.00 53.57 C ANISOU 3343 CZ PHE B 139 6903 6661 6789 1302 -429 -535 C ATOM 3344 N TYR B 140 11.248 -24.550 -6.487 1.00 52.24 N ANISOU 3344 N TYR B 140 6906 5668 7276 990 -1074 -757 N ATOM 3345 CA TYR B 140 12.471 -24.786 -5.758 1.00 51.83 C ANISOU 3345 CA TYR B 140 6885 5563 7246 1005 -1049 -773 C ATOM 3346 C TYR B 140 13.107 -25.980 -6.413 1.00 58.93 C ANISOU 3346 C TYR B 140 7846 6382 8162 1166 -1276 -987 C ATOM 3347 O TYR B 140 12.401 -26.887 -6.816 1.00 67.43 O ANISOU 3347 O TYR B 140 8966 7336 9319 1167 -1504 -1065 O ATOM 3348 CB TYR B 140 12.152 -25.082 -4.301 1.00 55.21 C ANISOU 3348 CB TYR B 140 7325 5845 7806 788 -1077 -626 C ATOM 3349 CG TYR B 140 13.369 -25.089 -3.405 1.00 57.92 C ANISOU 3349 CG TYR B 140 7693 6148 8164 785 -1022 -608 C ATOM 3350 CD1 TYR B 140 14.181 -26.208 -3.323 1.00 51.37 C ANISOU 3350 CD1 TYR B 140 6942 5168 7409 856 -1228 -722 C ATOM 3351 CD2 TYR B 140 13.703 -23.975 -2.640 1.00 57.79 C ANISOU 3351 CD2 TYR B 140 7621 6234 8103 723 -789 -492 C ATOM 3352 CE1 TYR B 140 15.282 -26.223 -2.518 1.00 51.43 C ANISOU 3352 CE1 TYR B 140 6967 5138 7436 861 -1194 -711 C ATOM 3353 CE2 TYR B 140 14.805 -23.983 -1.826 1.00 56.81 C ANISOU 3353 CE2 TYR B 140 7516 6075 7993 719 -748 -480 C ATOM 3354 CZ TYR B 140 15.595 -25.118 -1.764 1.00 58.63 C ANISOU 3354 CZ TYR B 140 7822 6165 8290 786 -947 -584 C ATOM 3355 OH TYR B 140 16.712 -25.151 -0.952 1.00 63.13 O ANISOU 3355 OH TYR B 140 8408 6697 8882 792 -924 -579 O ATOM 3356 N PRO B 141 14.443 -26.008 -6.519 1.00 63.19 N ANISOU 3356 N PRO B 141 8380 6992 8636 1312 -1234 -1101 N ATOM 3357 CA PRO B 141 15.461 -25.054 -6.065 1.00 62.52 C ANISOU 3357 CA PRO B 141 8243 7044 8469 1317 -997 -1026 C ATOM 3358 C PRO B 141 15.646 -23.859 -6.999 1.00 69.40 C ANISOU 3358 C PRO B 141 9035 8188 9146 1392 -780 -996 C ATOM 3359 O PRO B 141 15.085 -23.863 -8.093 1.00 74.44 O ANISOU 3359 O PRO B 141 9662 8930 9691 1471 -823 -1061 O ATOM 3360 CB PRO B 141 16.730 -25.896 -6.107 1.00 64.64 C ANISOU 3360 CB PRO B 141 8526 7284 8750 1478 -1122 -1223 C ATOM 3361 CG PRO B 141 16.493 -26.850 -7.243 1.00 60.87 C ANISOU 3361 CG PRO B 141 8069 6804 8253 1652 -1348 -1459 C ATOM 3362 CD PRO B 141 15.048 -27.197 -7.156 1.00 60.88 C ANISOU 3362 CD PRO B 141 8129 6634 8369 1505 -1481 -1360 C ATOM 3363 N LYS B 142 16.498 -22.907 -6.606 1.00 70.36 N ANISOU 3363 N LYS B 142 9105 8422 9207 1367 -578 -901 N ATOM 3364 CA LYS B 142 16.616 -21.600 -7.270 1.00 67.02 C ANISOU 3364 CA LYS B 142 8615 8218 8630 1369 -382 -791 C ATOM 3365 C LYS B 142 17.001 -21.660 -8.747 1.00 65.01 C ANISOU 3365 C LYS B 142 8312 8222 8168 1528 -387 -916 C ATOM 3366 O LYS B 142 16.914 -20.668 -9.447 1.00 76.06 O ANISOU 3366 O LYS B 142 9667 9802 9428 1509 -268 -801 O ATOM 3367 CB LYS B 142 17.609 -20.695 -6.515 1.00 69.82 C ANISOU 3367 CB LYS B 142 8926 8620 8982 1304 -205 -676 C ATOM 3368 CG LYS B 142 17.652 -19.205 -6.966 1.00 93.05 C ANISOU 3368 CG LYS B 142 11814 11720 11820 1249 -33 -502 C ATOM 3369 CD LYS B 142 18.812 -18.418 -6.292 1.00 77.42 C ANISOU 3369 CD LYS B 142 9786 9785 9845 1192 110 -411 C ATOM 3370 CE LYS B 142 19.026 -17.006 -6.894 1.00 74.58 C ANISOU 3370 CE LYS B 142 9375 9581 9381 1130 235 -231 C ATOM 3371 NZ LYS B 142 18.664 -15.848 -5.988 1.00 64.72 N ANISOU 3371 NZ LYS B 142 8142 8177 8272 1001 295 -62 N ATOM 3372 N ASP B 143 17.419 -22.812 -9.237 1.00 61.37 N ANISOU 3372 N ASP B 143 7852 7786 7678 1686 -543 -1156 N ATOM 3373 CA ASP B 143 18.006 -22.864 -10.573 1.00 66.17 C ANISOU 3373 CA ASP B 143 8380 8715 8049 1856 -527 -1311 C ATOM 3374 C ASP B 143 16.980 -23.188 -11.638 1.00 62.91 C ANISOU 3374 C ASP B 143 7994 8351 7559 1923 -650 -1390 C ATOM 3375 O ASP B 143 16.421 -24.275 -11.673 1.00 66.66 O ANISOU 3375 O ASP B 143 8531 8643 8152 1989 -872 -1553 O ATOM 3376 CB ASP B 143 19.207 -23.831 -10.612 1.00 79.56 C ANISOU 3376 CB ASP B 143 10024 10482 9721 2038 -621 -1582 C ATOM 3377 CG ASP B 143 20.269 -23.479 -9.567 1.00 93.53 C ANISOU 3377 CG ASP B 143 11759 12216 11563 1973 -502 -1504 C ATOM 3378 OD1 ASP B 143 21.169 -22.664 -9.881 1.00 93.55 O ANISOU 3378 OD1 ASP B 143 11648 12502 11394 1970 -312 -1445 O ATOM 3379 OD2 ASP B 143 20.188 -23.994 -8.422 1.00 97.33 O ANISOU 3379 OD2 ASP B 143 12323 12394 12264 1907 -604 -1483 O ATOM 3380 N ILE B 144 16.754 -22.221 -12.515 1.00 63.79 N ANISOU 3380 N ILE B 144 8058 8703 7476 1896 -524 -1261 N ATOM 3381 CA ILE B 144 15.740 -22.315 -13.554 1.00 66.39 C ANISOU 3381 CA ILE B 144 8410 9105 7712 1943 -622 -1295 C ATOM 3382 C ILE B 144 16.246 -21.653 -14.832 1.00 65.94 C ANISOU 3382 C ILE B 144 8260 9467 7327 2005 -509 -1274 C ATOM 3383 O ILE B 144 17.159 -20.831 -14.790 1.00 63.92 O ANISOU 3383 O ILE B 144 7930 9409 6950 1942 -330 -1138 O ATOM 3384 CB ILE B 144 14.439 -21.618 -13.097 1.00 72.64 C ANISOU 3384 CB ILE B 144 9266 9682 8654 1773 -610 -1064 C ATOM 3385 CG1 ILE B 144 13.197 -22.377 -13.594 1.00 73.93 C ANISOU 3385 CG1 ILE B 144 9481 9727 8882 1817 -816 -1175 C ATOM 3386 CG2 ILE B 144 14.439 -20.152 -13.521 1.00 69.36 C ANISOU 3386 CG2 ILE B 144 8813 9443 8098 1681 -442 -816 C ATOM 3387 CD1 ILE B 144 11.916 -22.076 -12.791 1.00 63.81 C ANISOU 3387 CD1 ILE B 144 8242 8186 7817 1653 -842 -1011 C ATOM 3388 N ASN B 145 15.637 -21.999 -15.962 1.00 73.03 N ANISOU 3388 N ASN B 145 9158 10512 8077 2109 -622 -1394 N ATOM 3389 CA ASN B 145 16.114 -21.564 -17.275 1.00 74.39 C ANISOU 3389 CA ASN B 145 9233 11141 7892 2179 -542 -1405 C ATOM 3390 C ASN B 145 14.995 -21.107 -18.204 1.00 78.50 C ANISOU 3390 C ASN B 145 9795 11733 8300 2147 -601 -1290 C ATOM 3391 O ASN B 145 14.007 -21.813 -18.395 1.00 80.96 O ANISOU 3391 O ASN B 145 10174 11867 8719 2215 -786 -1426 O ATOM 3392 CB ASN B 145 16.882 -22.697 -17.941 1.00 75.03 C ANISOU 3392 CB ASN B 145 9228 11468 7812 2423 -642 -1787 C ATOM 3393 CG ASN B 145 18.168 -22.227 -18.582 1.00 89.26 C ANISOU 3393 CG ASN B 145 10863 13769 9281 2461 -460 -1797 C ATOM 3394 OD1 ASN B 145 18.261 -22.116 -19.815 1.00 95.10 O ANISOU 3394 OD1 ASN B 145 11513 14931 9689 2537 -442 -1862 O ATOM 3395 ND2 ASN B 145 19.178 -21.946 -17.749 1.00 86.56 N ANISOU 3395 ND2 ASN B 145 10465 13413 9012 2396 -325 -1729 N ATOM 3396 N VAL B 146 15.156 -19.930 -18.795 1.00 77.83 N ANISOU 3396 N VAL B 146 9668 11901 8001 2034 -465 -1030 N ATOM 3397 CA VAL B 146 14.137 -19.409 -19.698 1.00 74.88 C ANISOU 3397 CA VAL B 146 9338 11600 7513 1998 -536 -894 C ATOM 3398 C VAL B 146 14.663 -19.105 -21.094 1.00 77.40 C ANISOU 3398 C VAL B 146 9562 12443 7405 2039 -485 -879 C ATOM 3399 O VAL B 146 15.495 -18.226 -21.280 1.00 82.82 O ANISOU 3399 O VAL B 146 10174 13391 7905 1918 -328 -660 O ATOM 3400 CB VAL B 146 13.488 -18.137 -19.131 1.00 70.26 C ANISOU 3400 CB VAL B 146 8822 10772 7101 1795 -485 -538 C ATOM 3401 CG1 VAL B 146 12.579 -18.482 -17.980 1.00 71.32 C ANISOU 3401 CG1 VAL B 146 9037 10454 7608 1766 -567 -576 C ATOM 3402 CG2 VAL B 146 14.548 -17.171 -18.671 1.00 67.95 C ANISOU 3402 CG2 VAL B 146 8479 10569 6772 1653 -303 -309 C ATOM 3403 N LYS B 147 14.176 -19.838 -22.081 1.00 79.23 N ANISOU 3403 N LYS B 147 9787 12845 7472 2199 -628 -1107 N ATOM 3404 CA LYS B 147 14.394 -19.446 -23.464 1.00 86.24 C ANISOU 3404 CA LYS B 147 10595 14241 7933 2215 -599 -1053 C ATOM 3405 C LYS B 147 13.153 -18.733 -24.022 1.00 84.08 C ANISOU 3405 C LYS B 147 10420 13875 7651 2118 -702 -814 C ATOM 3406 O LYS B 147 12.007 -19.116 -23.757 1.00 74.94 O ANISOU 3406 O LYS B 147 9362 12365 6745 2159 -861 -888 O ATOM 3407 CB LYS B 147 14.753 -20.653 -24.325 1.00 93.37 C ANISOU 3407 CB LYS B 147 11404 15476 8596 2477 -695 -1486 C ATOM 3408 CG LYS B 147 15.956 -21.419 -23.834 1.00108.41 C ANISOU 3408 CG LYS B 147 13201 17471 10518 2612 -635 -1770 C ATOM 3409 CD LYS B 147 16.054 -22.784 -24.520 1.00123.95 C ANISOU 3409 CD LYS B 147 15108 19620 12369 2919 -816 -2273 C ATOM 3410 CE LYS B 147 16.894 -22.741 -25.800 1.00132.80 C ANISOU 3410 CE LYS B 147 16000 21308 13149 2959 -713 -2324 C ATOM 3411 NZ LYS B 147 18.362 -22.594 -25.526 1.00132.15 N ANISOU 3411 NZ LYS B 147 15730 21472 13009 2922 -526 -2314 N ATOM 3412 N TRP B 148 13.393 -17.676 -24.782 1.00 83.94 N ANISOU 3412 N TRP B 148 10369 14180 7347 1976 -623 -509 N ATOM 3413 CA TRP B 148 12.328 -17.024 -25.508 1.00 78.68 C ANISOU 3413 CA TRP B 148 9785 13496 6614 1904 -747 -294 C ATOM 3414 C TRP B 148 12.379 -17.476 -26.952 1.00 88.63 C ANISOU 3414 C TRP B 148 10972 15267 7437 2030 -810 -455 C ATOM 3415 O TRP B 148 13.453 -17.583 -27.541 1.00 93.32 O ANISOU 3415 O TRP B 148 11425 16361 7670 2055 -687 -520 O ATOM 3416 CB TRP B 148 12.482 -15.512 -25.443 1.00 71.24 C ANISOU 3416 CB TRP B 148 8872 12545 5650 1648 -675 182 C ATOM 3417 CG TRP B 148 12.066 -14.918 -24.141 1.00 72.18 C ANISOU 3417 CG TRP B 148 9083 12131 6212 1540 -674 342 C ATOM 3418 CD1 TRP B 148 12.861 -14.680 -23.047 1.00 73.88 C ANISOU 3418 CD1 TRP B 148 9273 12181 6618 1459 -533 395 C ATOM 3419 CD2 TRP B 148 10.753 -14.467 -23.786 1.00 68.94 C ANISOU 3419 CD2 TRP B 148 8788 11310 6098 1511 -824 450 C ATOM 3420 NE1 TRP B 148 12.117 -14.112 -22.036 1.00 71.90 N ANISOU 3420 NE1 TRP B 148 9115 11453 6750 1386 -586 521 N ATOM 3421 CE2 TRP B 148 10.820 -13.972 -22.464 1.00 69.85 C ANISOU 3421 CE2 TRP B 148 8933 11045 6563 1420 -761 549 C ATOM 3422 CE3 TRP B 148 9.526 -14.436 -24.456 1.00 66.96 C ANISOU 3422 CE3 TRP B 148 8601 10993 5846 1563 -1012 455 C ATOM 3423 CZ2 TRP B 148 9.708 -13.450 -21.803 1.00 69.59 C ANISOU 3423 CZ2 TRP B 148 8977 10602 6862 1389 -873 634 C ATOM 3424 CZ3 TRP B 148 8.422 -13.918 -23.796 1.00 69.27 C ANISOU 3424 CZ3 TRP B 148 8971 10860 6487 1527 -1125 549 C ATOM 3425 CH2 TRP B 148 8.521 -13.430 -22.486 1.00 69.83 C ANISOU 3425 CH2 TRP B 148 9055 10588 6888 1446 -1052 629 C ATOM 3426 N LYS B 149 11.213 -17.758 -27.515 1.00 88.12 N ANISOU 3426 N LYS B 149 10987 15101 7394 2115 -1002 -536 N ATOM 3427 CA LYS B 149 11.115 -18.000 -28.937 1.00 89.09 C ANISOU 3427 CA LYS B 149 11056 15708 7088 2213 -1082 -639 C ATOM 3428 C LYS B 149 10.187 -16.980 -29.529 1.00 85.49 C ANISOU 3428 C LYS B 149 10696 15216 6572 2065 -1191 -280 C ATOM 3429 O LYS B 149 9.150 -16.679 -28.963 1.00 80.76 O ANISOU 3429 O LYS B 149 10214 14143 6330 2020 -1307 -173 O ATOM 3430 CB LYS B 149 10.591 -19.405 -29.225 1.00 93.03 C ANISOU 3430 CB LYS B 149 11556 16155 7636 2483 -1261 -1120 C ATOM 3431 CG LYS B 149 11.635 -20.486 -29.042 1.00 94.14 C ANISOU 3431 CG LYS B 149 11575 16452 7743 2667 -1195 -1518 C ATOM 3432 CD LYS B 149 11.166 -21.810 -29.604 1.00 95.11 C ANISOU 3432 CD LYS B 149 11675 16498 7963 2898 -1378 -1950 C ATOM 3433 CE LYS B 149 12.244 -22.854 -29.423 1.00 99.85 C ANISOU 3433 CE LYS B 149 12134 17168 8637 3069 -1327 -2309 C ATOM 3434 NZ LYS B 149 12.834 -22.768 -28.052 1.00 98.61 N ANISOU 3434 NZ LYS B 149 12014 16761 8690 3017 -1242 -2266 N ATOM 3435 N ILE B 150 10.577 -16.432 -30.665 1.00 91.63 N ANISOU 3435 N ILE B 150 11412 16510 6895 1981 -1160 -90 N ATOM 3436 CA ILE B 150 9.673 -15.617 -31.445 1.00 98.87 C ANISOU 3436 CA ILE B 150 12421 17418 7728 1861 -1306 211 C ATOM 3437 C ILE B 150 9.523 -16.294 -32.794 1.00105.74 C ANISOU 3437 C ILE B 150 13221 18615 8341 1963 -1350 -29 C ATOM 3438 O ILE B 150 10.474 -16.354 -33.573 1.00105.43 O ANISOU 3438 O ILE B 150 13036 19011 8010 1912 -1195 -53 O ATOM 3439 CB ILE B 150 10.206 -14.187 -31.608 1.00102.01 C ANISOU 3439 CB ILE B 150 12826 17931 8002 1554 -1218 737 C ATOM 3440 CG1 ILE B 150 10.623 -13.632 -30.240 1.00 98.64 C ANISOU 3440 CG1 ILE B 150 12430 17142 7906 1444 -1119 912 C ATOM 3441 CG2 ILE B 150 9.166 -13.308 -32.304 1.00 99.05 C ANISOU 3441 CG2 ILE B 150 12577 17445 7611 1435 -1425 1059 C ATOM 3442 CD1 ILE B 150 11.091 -12.194 -30.266 1.00 99.62 C ANISOU 3442 CD1 ILE B 150 12579 17308 7962 1142 -1086 1442 C ATOM 3443 N ASP B 151 8.325 -16.816 -33.049 1.00112.84 N ANISOU 3443 N ASP B 151 14206 19305 9363 2111 -1566 -216 N ATOM 3444 CA ASP B 151 8.043 -17.605 -34.250 1.00117.77 C ANISOU 3444 CA ASP B 151 14773 20179 9794 2247 -1640 -498 C ATOM 3445 C ASP B 151 9.002 -18.776 -34.438 1.00120.73 C ANISOU 3445 C ASP B 151 14981 20807 10085 2432 -1516 -930 C ATOM 3446 O ASP B 151 9.457 -19.048 -35.553 1.00120.27 O ANISOU 3446 O ASP B 151 14795 21170 9733 2469 -1458 -1044 O ATOM 3447 CB ASP B 151 8.040 -16.719 -35.488 1.00122.59 C ANISOU 3447 CB ASP B 151 15379 21133 10065 2063 -1638 -173 C ATOM 3448 CG ASP B 151 6.794 -15.885 -35.583 1.00126.73 C ANISOU 3448 CG ASP B 151 16073 21372 10706 1964 -1858 133 C ATOM 3449 OD1 ASP B 151 5.753 -16.342 -35.069 1.00126.28 O ANISOU 3449 OD1 ASP B 151 16099 20939 10944 2109 -2036 -43 O ATOM 3450 OD2 ASP B 151 6.850 -14.781 -36.162 1.00131.52 O ANISOU 3450 OD2 ASP B 151 16725 22111 11134 1740 -1870 546 O ATOM 3451 N GLY B 152 9.307 -19.452 -33.333 1.00118.53 N ANISOU 3451 N GLY B 152 14697 20260 10079 2552 -1493 -1167 N ATOM 3452 CA GLY B 152 10.162 -20.625 -33.328 1.00112.26 C ANISOU 3452 CA GLY B 152 13755 19595 9302 2754 -1427 -1595 C ATOM 3453 C GLY B 152 11.635 -20.304 -33.151 1.00107.17 C ANISOU 3453 C GLY B 152 12950 19272 8497 2667 -1175 -1510 C ATOM 3454 O GLY B 152 12.396 -21.121 -32.636 1.00106.66 O ANISOU 3454 O GLY B 152 12787 19177 8561 2814 -1124 -1808 O ATOM 3455 N SER B 153 12.033 -19.096 -33.534 1.00102.77 N ANISOU 3455 N SER B 153 12368 18988 7691 2414 -1038 -1087 N ATOM 3456 CA SER B 153 13.434 -18.709 -33.477 1.00103.11 C ANISOU 3456 CA SER B 153 12237 19370 7572 2292 -802 -971 C ATOM 3457 C SER B 153 13.746 -18.274 -32.066 1.00100.96 C ANISOU 3457 C SER B 153 12042 18772 7546 2196 -726 -807 C ATOM 3458 O SER B 153 12.925 -17.632 -31.424 1.00110.96 O ANISOU 3458 O SER B 153 13493 19682 8986 2098 -819 -554 O ATOM 3459 CB SER B 153 13.707 -17.562 -34.447 1.00109.44 C ANISOU 3459 CB SER B 153 12987 20559 8037 2021 -711 -550 C ATOM 3460 OG SER B 153 13.188 -17.849 -35.737 1.00114.17 O ANISOU 3460 OG SER B 153 13556 21419 8404 2093 -810 -655 O ATOM 3461 N GLU B 154 14.918 -18.622 -31.560 1.00 94.72 N ANISOU 3461 N GLU B 154 11103 18097 6788 2237 -572 -957 N ATOM 3462 CA GLU B 154 15.250 -18.200 -30.209 1.00 91.34 C ANISOU 3462 CA GLU B 154 10749 17371 6585 2144 -493 -802 C ATOM 3463 C GLU B 154 15.486 -16.688 -30.222 1.00 95.76 C ANISOU 3463 C GLU B 154 11338 18023 7022 1809 -386 -247 C ATOM 3464 O GLU B 154 15.711 -16.098 -31.289 1.00 99.33 O ANISOU 3464 O GLU B 154 11709 18833 7201 1650 -342 -28 O ATOM 3465 CB GLU B 154 16.454 -18.971 -29.651 1.00 88.35 C ANISOU 3465 CB GLU B 154 10206 17070 6295 2274 -375 -1107 C ATOM 3466 CG GLU B 154 16.831 -18.567 -28.227 1.00 89.95 C ANISOU 3466 CG GLU B 154 10484 16967 6725 2182 -289 -962 C ATOM 3467 CD GLU B 154 17.825 -19.513 -27.562 1.00100.43 C ANISOU 3467 CD GLU B 154 11686 18259 8212 2353 -235 -1318 C ATOM 3468 OE1 GLU B 154 18.250 -20.493 -28.217 1.00110.79 O ANISOU 3468 OE1 GLU B 154 12840 19782 9472 2552 -283 -1677 O ATOM 3469 OE2 GLU B 154 18.176 -19.278 -26.378 1.00 95.92 O ANISOU 3469 OE2 GLU B 154 11173 17440 7833 2294 -162 -1237 O ATOM 3470 N ARG B 155 15.365 -16.062 -29.051 1.00 90.57 N ANISOU 3470 N ARG B 155 10805 17018 6588 1701 -375 -12 N ATOM 3471 CA ARG B 155 15.660 -14.642 -28.881 1.00 89.30 C ANISOU 3471 CA ARG B 155 10677 16852 6402 1384 -301 514 C ATOM 3472 C ARG B 155 16.330 -14.369 -27.533 1.00 91.16 C ANISOU 3472 C ARG B 155 10916 16845 6874 1317 -183 595 C ATOM 3473 O ARG B 155 15.796 -14.730 -26.481 1.00 77.87 O ANISOU 3473 O ARG B 155 9344 14609 5633 1410 -241 447 O ATOM 3474 CB ARG B 155 14.386 -13.815 -29.011 1.00 92.06 C ANISOU 3474 CB ARG B 155 11223 16919 6837 1283 -499 841 C ATOM 3475 CG ARG B 155 14.571 -12.341 -28.735 1.00 92.37 C ANISOU 3475 CG ARG B 155 11325 16824 6949 966 -490 1382 C ATOM 3476 CD ARG B 155 15.174 -11.605 -29.918 1.00 97.98 C ANISOU 3476 CD ARG B 155 11941 17912 7376 716 -431 1661 C ATOM 3477 NE ARG B 155 15.166 -10.163 -29.682 1.00100.92 N ANISOU 3477 NE ARG B 155 12412 18047 7885 409 -497 2181 N ATOM 3478 CZ ARG B 155 14.833 -9.248 -30.591 1.00105.91 C ANISOU 3478 CZ ARG B 155 13109 18719 8414 201 -621 2524 C ATOM 3479 NH1 ARG B 155 14.481 -9.609 -31.827 1.00100.97 N ANISOU 3479 NH1 ARG B 155 12452 18406 7506 257 -669 2424 N ATOM 3480 NH2 ARG B 155 14.856 -7.961 -30.262 1.00108.16 N ANISOU 3480 NH2 ARG B 155 13493 18707 8895 -61 -714 2959 N ATOM 3481 N GLN B 156 17.483 -13.697 -27.591 1.00103.80 N ANISOU 3481 N GLN B 156 12382 18703 8355 1100 -15 828 N ATOM 3482 CA GLN B 156 18.375 -13.437 -26.449 1.00 96.28 C ANISOU 3482 CA GLN B 156 11387 17623 7571 1019 125 898 C ATOM 3483 C GLN B 156 18.438 -11.943 -26.069 1.00 94.63 C ANISOU 3483 C GLN B 156 11262 17200 7494 687 118 1442 C ATOM 3484 O GLN B 156 18.259 -11.584 -24.909 1.00 85.61 O ANISOU 3484 O GLN B 156 10226 15523 6780 642 98 1511 O ATOM 3485 CB GLN B 156 19.778 -13.995 -26.708 1.00101.20 C ANISOU 3485 CB GLN B 156 11755 18642 8055 1056 303 655 C ATOM 3486 CG GLN B 156 19.822 -15.473 -27.128 1.00105.68 C ANISOU 3486 CG GLN B 156 12219 19370 8563 1389 269 102 C ATOM 3487 CD GLN B 156 21.245 -16.046 -27.156 1.00106.46 C ANISOU 3487 CD GLN B 156 12059 19789 8604 1458 406 -152 C ATOM 3488 OE1 GLN B 156 21.754 -16.432 -28.222 1.00108.47 O ANISOU 3488 OE1 GLN B 156 12112 20478 8624 1513 427 -310 O ATOM 3489 NE2 GLN B 156 21.889 -16.109 -25.980 1.00 93.64 N ANISOU 3489 NE2 GLN B 156 10428 17956 7195 1464 486 -199 N ATOM 3490 N ASN B 157 18.806 -11.096 -27.032 1.00107.70 N ANISOU 3490 N ASN B 157 12848 19127 8947 434 128 1759 N ATOM 3491 CA ASN B 157 18.737 -9.633 -26.885 1.00110.93 C ANISOU 3491 CA ASN B 157 13359 19298 9493 110 47 2283 C ATOM 3492 C ASN B 157 17.370 -9.098 -26.451 1.00110.78 C ANISOU 3492 C ASN B 157 13584 18775 9732 125 -182 2481 C ATOM 3493 O ASN B 157 16.335 -9.436 -27.037 1.00114.09 O ANISOU 3493 O ASN B 157 14091 19171 10086 264 -325 2384 O ATOM 3494 CB ASN B 157 19.119 -8.929 -28.197 1.00112.14 C ANISOU 3494 CB ASN B 157 13420 19806 9383 -136 37 2551 C ATOM 3495 CG ASN B 157 20.591 -9.030 -28.506 1.00116.98 C ANISOU 3495 CG ASN B 157 13767 20879 9802 -244 237 2498 C ATOM 3496 OD1 ASN B 157 21.375 -9.515 -27.685 1.00117.60 O ANISOU 3496 OD1 ASN B 157 13741 20967 9974 -154 376 2287 O ATOM 3497 ND2 ASN B 157 20.983 -8.570 -29.694 1.00121.44 N ANISOU 3497 ND2 ASN B 157 14209 21838 10094 -437 242 2689 N ATOM 3498 N GLY B 158 17.375 -8.230 -25.445 1.00102.04 N ANISOU 3498 N GLY B 158 12573 17209 8988 -16 -233 2719 N ATOM 3499 CA GLY B 158 16.169 -7.535 -25.046 1.00 94.57 C ANISOU 3499 CA GLY B 158 11829 15682 8421 -23 -464 2866 C ATOM 3500 C GLY B 158 15.491 -8.205 -23.877 1.00 94.69 C ANISOU 3500 C GLY B 158 11915 15198 8865 219 -466 2493 C ATOM 3501 O GLY B 158 14.419 -7.772 -23.445 1.00104.82 O ANISOU 3501 O GLY B 158 13335 16015 10475 259 -642 2530 O ATOM 3502 N VAL B 159 16.107 -9.268 -23.365 1.00 83.96 N ANISOU 3502 N VAL B 159 10452 13950 7498 378 -284 2133 N ATOM 3503 CA VAL B 159 15.545 -9.989 -22.229 1.00 77.60 C ANISOU 3503 CA VAL B 159 9704 12710 7072 578 -283 1798 C ATOM 3504 C VAL B 159 16.143 -9.463 -20.943 1.00 75.24 C ANISOU 3504 C VAL B 159 9407 12100 7080 481 -208 1875 C ATOM 3505 O VAL B 159 17.309 -9.098 -20.898 1.00 79.72 O ANISOU 3505 O VAL B 159 9879 12893 7519 333 -86 2023 O ATOM 3506 CB VAL B 159 15.735 -11.527 -22.337 1.00 64.53 C ANISOU 3506 CB VAL B 159 7962 11269 5288 824 -189 1345 C ATOM 3507 CG1 VAL B 159 15.317 -12.229 -21.033 1.00 54.71 C ANISOU 3507 CG1 VAL B 159 6772 9571 4442 971 -190 1061 C ATOM 3508 CG2 VAL B 159 14.933 -12.079 -23.522 1.00 62.57 C ANISOU 3508 CG2 VAL B 159 7731 11249 4794 952 -305 1222 C ATOM 3509 N LEU B 160 15.311 -9.372 -19.916 1.00 75.37 N ANISOU 3509 N LEU B 160 9524 11621 7493 554 -290 1782 N ATOM 3510 CA LEU B 160 15.760 -9.000 -18.586 1.00 72.98 C ANISOU 3510 CA LEU B 160 9226 11008 7496 501 -228 1788 C ATOM 3511 C LEU B 160 15.055 -9.838 -17.543 1.00 65.19 C ANISOU 3511 C LEU B 160 8275 9699 6796 684 -225 1461 C ATOM 3512 O LEU B 160 13.828 -9.824 -17.448 1.00 78.34 O ANISOU 3512 O LEU B 160 10015 11120 8632 762 -359 1403 O ATOM 3513 CB LEU B 160 15.485 -7.524 -18.320 1.00 79.53 C ANISOU 3513 CB LEU B 160 10141 11538 8537 328 -377 2127 C ATOM 3514 CG LEU B 160 16.443 -6.555 -18.998 1.00 90.05 C ANISOU 3514 CG LEU B 160 11435 13122 9656 74 -379 2513 C ATOM 3515 CD1 LEU B 160 16.271 -5.190 -18.384 1.00 91.88 C ANISOU 3515 CD1 LEU B 160 11760 12945 10204 -76 -549 2787 C ATOM 3516 CD2 LEU B 160 17.882 -7.031 -18.833 1.00 94.98 C ANISOU 3516 CD2 LEU B 160 11912 14084 10093 21 -150 2447 C ATOM 3517 N ASN B 161 15.830 -10.529 -16.728 1.00 48.05 N ANISOU 3517 N ASN B 161 6043 7532 4683 735 -84 1266 N ATOM 3518 CA ASN B 161 15.277 -11.369 -15.681 1.00 51.83 C ANISOU 3518 CA ASN B 161 6550 7731 5413 871 -83 989 C ATOM 3519 C ASN B 161 15.383 -10.707 -14.292 1.00 59.90 C ANISOU 3519 C ASN B 161 7596 8417 6745 799 -61 1045 C ATOM 3520 O ASN B 161 16.251 -9.863 -14.066 1.00 68.63 O ANISOU 3520 O ASN B 161 8677 9541 7858 665 -12 1237 O ATOM 3521 CB ASN B 161 15.959 -12.735 -15.723 1.00 56.55 C ANISOU 3521 CB ASN B 161 7076 8538 5873 1001 12 702 C ATOM 3522 CG ASN B 161 15.979 -13.319 -17.126 1.00 66.03 C ANISOU 3522 CG ASN B 161 8232 10116 6741 1086 -13 619 C ATOM 3523 OD1 ASN B 161 15.081 -13.044 -17.922 1.00 68.26 O ANISOU 3523 OD1 ASN B 161 8565 10420 6950 1089 -127 704 O ATOM 3524 ND2 ASN B 161 17.011 -14.110 -17.446 1.00 63.53 N ANISOU 3524 ND2 ASN B 161 7810 10117 6214 1168 82 438 N ATOM 3525 N SER B 162 14.448 -11.021 -13.397 1.00 53.70 N ANISOU 3525 N SER B 162 6851 7344 6209 876 -112 891 N ATOM 3526 CA SER B 162 14.550 -10.605 -12.008 1.00 54.27 C ANISOU 3526 CA SER B 162 6927 7151 6544 837 -79 877 C ATOM 3527 C SER B 162 14.058 -11.716 -11.111 1.00 56.71 C ANISOU 3527 C SER B 162 7231 7335 6981 932 -56 620 C ATOM 3528 O SER B 162 13.014 -12.273 -11.357 1.00 66.43 O ANISOU 3528 O SER B 162 8478 8527 8234 1005 -137 511 O ATOM 3529 CB SER B 162 13.736 -9.342 -11.752 1.00 63.28 C ANISOU 3529 CB SER B 162 8112 8045 7885 790 -210 1026 C ATOM 3530 OG SER B 162 13.810 -8.974 -10.379 1.00 65.25 O ANISOU 3530 OG SER B 162 8351 8066 8376 776 -182 968 O ATOM 3531 N TRP B 163 14.804 -12.008 -10.053 1.00 65.13 N ANISOU 3531 N TRP B 163 8273 8339 8137 913 40 544 N ATOM 3532 CA TRP B 163 14.538 -13.137 -9.146 1.00 62.30 C ANISOU 3532 CA TRP B 163 7911 7879 7879 969 55 335 C ATOM 3533 C TRP B 163 14.132 -12.613 -7.778 1.00 58.11 C ANISOU 3533 C TRP B 163 7376 7127 7577 921 64 333 C ATOM 3534 O TRP B 163 14.670 -11.603 -7.332 1.00 54.37 O ANISOU 3534 O TRP B 163 6894 6591 7172 858 96 445 O ATOM 3535 CB TRP B 163 15.813 -13.969 -9.009 1.00 55.29 C ANISOU 3535 CB TRP B 163 6995 7121 6892 994 141 238 C ATOM 3536 CG TRP B 163 16.359 -14.318 -10.338 1.00 63.30 C ANISOU 3536 CG TRP B 163 7980 8415 7657 1051 146 222 C ATOM 3537 CD1 TRP B 163 16.685 -13.453 -11.344 1.00 69.08 C ANISOU 3537 CD1 TRP B 163 8687 9341 8218 996 165 403 C ATOM 3538 CD2 TRP B 163 16.615 -15.630 -10.839 1.00 73.42 C ANISOU 3538 CD2 TRP B 163 9244 9833 8817 1174 114 9 C ATOM 3539 NE1 TRP B 163 17.132 -14.143 -12.444 1.00 75.44 N ANISOU 3539 NE1 TRP B 163 9445 10448 8770 1077 173 308 N ATOM 3540 CE2 TRP B 163 17.099 -15.483 -12.164 1.00 78.21 C ANISOU 3540 CE2 TRP B 163 9799 10760 9156 1206 136 43 C ATOM 3541 CE3 TRP B 163 16.499 -16.915 -10.296 1.00 69.43 C ANISOU 3541 CE3 TRP B 163 8762 9213 8405 1256 47 -207 C ATOM 3542 CZ2 TRP B 163 17.465 -16.573 -12.952 1.00 78.22 C ANISOU 3542 CZ2 TRP B 163 9757 10985 8977 1350 101 -177 C ATOM 3543 CZ3 TRP B 163 16.860 -17.989 -11.076 1.00 77.51 C ANISOU 3543 CZ3 TRP B 163 9763 10401 9286 1394 -17 -410 C ATOM 3544 CH2 TRP B 163 17.341 -17.814 -12.396 1.00 80.64 C ANISOU 3544 CH2 TRP B 163 10094 11134 9411 1456 15 -417 C ATOM 3545 N THR B 164 13.171 -13.253 -7.117 1.00 54.16 N ANISOU 3545 N THR B 164 6869 6524 7185 942 24 207 N ATOM 3546 CA THR B 164 12.898 -12.864 -5.733 1.00 51.88 C ANISOU 3546 CA THR B 164 6549 6096 7069 897 53 177 C ATOM 3547 C THR B 164 13.869 -13.636 -4.867 1.00 54.55 C ANISOU 3547 C THR B 164 6889 6436 7403 866 132 112 C ATOM 3548 O THR B 164 14.641 -14.445 -5.386 1.00 62.44 O ANISOU 3548 O THR B 164 7910 7527 8289 898 145 74 O ATOM 3549 CB THR B 164 11.419 -13.103 -5.272 1.00 60.23 C ANISOU 3549 CB THR B 164 7563 7091 8231 904 -12 86 C ATOM 3550 OG1 THR B 164 10.980 -14.408 -5.642 1.00 56.53 O ANISOU 3550 OG1 THR B 164 7108 6668 7703 916 -60 -1 O ATOM 3551 CG2 THR B 164 10.464 -12.082 -5.886 1.00 63.75 C ANISOU 3551 CG2 THR B 164 7992 7502 8729 948 -105 138 C ATOM 3552 N ASP B 165 13.861 -13.383 -3.564 1.00 60.56 N ANISOU 3552 N ASP B 165 7621 7109 8279 817 173 85 N ATOM 3553 CA ASP B 165 14.634 -14.208 -2.641 1.00 70.70 C ANISOU 3553 CA ASP B 165 8913 8383 9567 779 221 25 C ATOM 3554 C ASP B 165 13.622 -15.180 -2.106 1.00 71.55 C ANISOU 3554 C ASP B 165 9009 8465 9713 744 166 -54 C ATOM 3555 O ASP B 165 12.456 -15.115 -2.486 1.00 70.74 O ANISOU 3555 O ASP B 165 8879 8370 9629 754 110 -67 O ATOM 3556 CB ASP B 165 15.248 -13.393 -1.507 1.00 79.34 C ANISOU 3556 CB ASP B 165 9982 9420 10745 732 289 49 C ATOM 3557 CG ASP B 165 15.042 -11.902 -1.685 1.00101.35 C ANISOU 3557 CG ASP B 165 12747 12158 13605 742 275 125 C ATOM 3558 OD1 ASP B 165 15.914 -11.244 -2.299 1.00105.00 O ANISOU 3558 OD1 ASP B 165 13228 12634 14034 734 287 231 O ATOM 3559 OD2 ASP B 165 14.001 -11.388 -1.215 1.00110.33 O ANISOU 3559 OD2 ASP B 165 13839 13246 14834 755 235 76 O ATOM 3560 N GLN B 166 14.043 -16.091 -1.242 1.00 73.04 N ANISOU 3560 N GLN B 166 9215 8625 9913 689 164 -93 N ATOM 3561 CA GLN B 166 13.108 -17.079 -0.736 1.00 67.85 C ANISOU 3561 CA GLN B 166 8547 7947 9285 612 89 -128 C ATOM 3562 C GLN B 166 11.889 -16.348 -0.207 1.00 65.10 C ANISOU 3562 C GLN B 166 8104 7641 8988 567 115 -127 C ATOM 3563 O GLN B 166 12.014 -15.289 0.434 1.00 53.76 O ANISOU 3563 O GLN B 166 6617 6219 7590 573 190 -126 O ATOM 3564 CB GLN B 166 13.740 -17.960 0.336 1.00 58.75 C ANISOU 3564 CB GLN B 166 7426 6747 8150 529 70 -130 C ATOM 3565 CG GLN B 166 14.694 -18.973 -0.229 1.00 62.33 C ANISOU 3565 CG GLN B 166 7961 7148 8574 593 -14 -177 C ATOM 3566 CD GLN B 166 15.245 -19.908 0.823 1.00 72.20 C ANISOU 3566 CD GLN B 166 9255 8316 9864 511 -83 -173 C ATOM 3567 OE1 GLN B 166 15.954 -19.490 1.736 1.00 69.31 O ANISOU 3567 OE1 GLN B 166 8878 7953 9506 476 -7 -144 O ATOM 3568 NE2 GLN B 166 14.919 -21.186 0.701 1.00 80.35 N ANISOU 3568 NE2 GLN B 166 10343 9257 10930 476 -255 -196 N ATOM 3569 N ASP B 167 10.720 -16.908 -0.522 1.00 57.29 N ANISOU 3569 N ASP B 167 7082 6679 8007 533 37 -147 N ATOM 3570 CA ASP B 167 9.442 -16.328 -0.161 1.00 55.77 C ANISOU 3570 CA ASP B 167 6769 6565 7854 505 47 -175 C ATOM 3571 C ASP B 167 9.223 -16.468 1.339 1.00 56.30 C ANISOU 3571 C ASP B 167 6750 6716 7924 377 102 -182 C ATOM 3572 O ASP B 167 9.717 -17.412 1.953 1.00 57.82 O ANISOU 3572 O ASP B 167 6991 6887 8090 270 83 -137 O ATOM 3573 CB ASP B 167 8.336 -17.027 -0.958 1.00 66.80 C ANISOU 3573 CB ASP B 167 8148 7982 9251 492 -61 -191 C ATOM 3574 CG ASP B 167 6.944 -16.569 -0.566 1.00 76.21 C ANISOU 3574 CG ASP B 167 9184 9290 10482 457 -59 -237 C ATOM 3575 OD1 ASP B 167 6.221 -17.366 0.069 1.00 80.32 O ANISOU 3575 OD1 ASP B 167 9628 9894 10997 313 -87 -229 O ATOM 3576 OD2 ASP B 167 6.565 -15.423 -0.894 1.00 74.68 O ANISOU 3576 OD2 ASP B 167 8937 9112 10326 568 -45 -279 O ATOM 3577 N SER B 168 8.492 -15.532 1.939 1.00 55.62 N ANISOU 3577 N SER B 168 6532 6739 7864 392 156 -246 N ATOM 3578 CA SER B 168 8.263 -15.578 3.383 1.00 54.77 C ANISOU 3578 CA SER B 168 6313 6777 7720 276 222 -272 C ATOM 3579 C SER B 168 7.104 -16.493 3.809 1.00 62.32 C ANISOU 3579 C SER B 168 7156 7895 8629 109 187 -251 C ATOM 3580 O SER B 168 6.828 -16.643 4.998 1.00 72.14 O ANISOU 3580 O SER B 168 8289 9317 9804 -22 242 -251 O ATOM 3581 CB SER B 168 8.052 -14.175 3.929 1.00 48.37 C ANISOU 3581 CB SER B 168 5388 6041 6949 381 285 -391 C ATOM 3582 OG SER B 168 6.964 -13.553 3.277 1.00 50.02 O ANISOU 3582 OG SER B 168 5503 6288 7215 481 235 -473 O ATOM 3583 N LYS B 169 6.423 -17.097 2.844 1.00 60.32 N ANISOU 3583 N LYS B 169 6921 7599 8400 101 91 -227 N ATOM 3584 CA LYS B 169 5.382 -18.076 3.146 1.00 70.05 C ANISOU 3584 CA LYS B 169 8055 8959 9600 -87 30 -177 C ATOM 3585 C LYS B 169 5.946 -19.497 2.999 1.00 74.48 C ANISOU 3585 C LYS B 169 8772 9363 10165 -216 -92 -51 C ATOM 3586 O LYS B 169 6.104 -20.217 3.994 1.00 71.27 O ANISOU 3586 O LYS B 169 8360 9008 9713 -408 -109 47 O ATOM 3587 CB LYS B 169 4.169 -17.874 2.222 1.00 70.52 C ANISOU 3587 CB LYS B 169 8022 9068 9705 -23 -32 -241 C ATOM 3588 CG LYS B 169 2.962 -18.753 2.501 1.00 70.11 C ANISOU 3588 CG LYS B 169 7830 9180 9629 -226 -95 -195 C ATOM 3589 CD LYS B 169 2.327 -18.425 3.837 1.00 81.97 C ANISOU 3589 CD LYS B 169 9105 10996 11046 -354 17 -227 C ATOM 3590 CE LYS B 169 0.995 -19.170 4.030 1.00 91.38 C ANISOU 3590 CE LYS B 169 10109 12410 12201 -569 -38 -178 C ATOM 3591 NZ LYS B 169 1.144 -20.480 4.733 1.00 91.89 N ANISOU 3591 NZ LYS B 169 10215 12495 12207 -874 -107 26 N ATOM 3592 N ASP B 170 6.218 -19.895 1.753 1.00 73.21 N ANISOU 3592 N ASP B 170 8744 9019 10054 -108 -198 -62 N ATOM 3593 CA ASP B 170 6.747 -21.223 1.442 1.00 75.18 C ANISOU 3593 CA ASP B 170 9141 9092 10333 -175 -358 2 C ATOM 3594 C ASP B 170 8.258 -21.276 1.219 1.00 71.45 C ANISOU 3594 C ASP B 170 8825 8463 9861 -47 -354 -19 C ATOM 3595 O ASP B 170 8.821 -22.350 1.011 1.00 66.44 O ANISOU 3595 O ASP B 170 8310 7675 9261 -68 -502 -2 O ATOM 3596 CB ASP B 170 6.003 -21.850 0.245 1.00 88.82 C ANISOU 3596 CB ASP B 170 10895 10744 12109 -144 -514 -29 C ATOM 3597 CG ASP B 170 5.888 -20.908 -0.954 1.00 97.07 C ANISOU 3597 CG ASP B 170 11941 11797 13145 79 -466 -130 C ATOM 3598 OD1 ASP B 170 4.961 -21.098 -1.779 1.00 92.15 O ANISOU 3598 OD1 ASP B 170 11281 11185 12545 100 -559 -165 O ATOM 3599 OD2 ASP B 170 6.721 -19.984 -1.072 1.00103.49 O ANISOU 3599 OD2 ASP B 170 12791 12604 13928 219 -350 -160 O ATOM 3600 N SER B 171 8.903 -20.115 1.276 1.00 77.68 N ANISOU 3600 N SER B 171 9603 9291 10622 83 -204 -63 N ATOM 3601 CA SER B 171 10.336 -19.968 0.978 1.00 73.94 C ANISOU 3601 CA SER B 171 9242 8715 10138 210 -175 -87 C ATOM 3602 C SER B 171 10.774 -20.661 -0.303 1.00 68.28 C ANISOU 3602 C SER B 171 8629 7893 9420 330 -295 -142 C ATOM 3603 O SER B 171 11.721 -21.444 -0.300 1.00 65.13 O ANISOU 3603 O SER B 171 8322 7395 9031 355 -375 -164 O ATOM 3604 CB SER B 171 11.226 -20.366 2.165 1.00 67.84 C ANISOU 3604 CB SER B 171 8508 7907 9359 114 -164 -36 C ATOM 3605 OG SER B 171 10.886 -21.632 2.683 1.00 61.02 O ANISOU 3605 OG SER B 171 7676 6989 8520 -56 -313 37 O ATOM 3606 N THR B 172 10.055 -20.369 -1.387 1.00 66.30 N ANISOU 3606 N THR B 172 8356 7678 9156 414 -319 -183 N ATOM 3607 CA THR B 172 10.415 -20.828 -2.724 1.00 60.50 C ANISOU 3607 CA THR B 172 7699 6904 8384 554 -414 -259 C ATOM 3608 C THR B 172 10.813 -19.601 -3.527 1.00 57.67 C ANISOU 3608 C THR B 172 7327 6635 7951 689 -294 -261 C ATOM 3609 O THR B 172 10.715 -18.476 -3.045 1.00 59.10 O ANISOU 3609 O THR B 172 7449 6860 8145 673 -175 -206 O ATOM 3610 CB THR B 172 9.240 -21.550 -3.463 1.00 64.10 C ANISOU 3610 CB THR B 172 8149 7339 8869 535 -572 -296 C ATOM 3611 OG1 THR B 172 8.126 -20.665 -3.607 1.00 57.09 O ANISOU 3611 OG1 THR B 172 7160 6549 7984 521 -508 -269 O ATOM 3612 CG2 THR B 172 8.782 -22.793 -2.724 1.00 67.17 C ANISOU 3612 CG2 THR B 172 8552 7624 9345 363 -729 -260 C ATOM 3613 N TYR B 173 11.237 -19.825 -4.762 1.00 55.87 N ANISOU 3613 N TYR B 173 7147 6441 7641 818 -345 -323 N ATOM 3614 CA TYR B 173 11.780 -18.770 -5.595 1.00 57.15 C ANISOU 3614 CA TYR B 173 7302 6712 7702 917 -248 -290 C ATOM 3615 C TYR B 173 10.832 -18.463 -6.718 1.00 64.28 C ANISOU 3615 C TYR B 173 8192 7675 8555 973 -308 -289 C ATOM 3616 O TYR B 173 10.037 -19.302 -7.118 1.00 74.52 O ANISOU 3616 O TYR B 173 9499 8944 9871 978 -438 -360 O ATOM 3617 CB TYR B 173 13.118 -19.207 -6.175 1.00 63.54 C ANISOU 3617 CB TYR B 173 8149 7588 8405 1017 -243 -359 C ATOM 3618 CG TYR B 173 14.190 -19.339 -5.123 1.00 61.62 C ANISOU 3618 CG TYR B 173 7911 7293 8207 978 -180 -354 C ATOM 3619 CD1 TYR B 173 14.907 -18.235 -4.695 1.00 55.40 C ANISOU 3619 CD1 TYR B 173 7092 6549 7410 950 -35 -261 C ATOM 3620 CD2 TYR B 173 14.463 -20.560 -4.545 1.00 62.62 C ANISOU 3620 CD2 TYR B 173 8082 7309 8403 962 -293 -437 C ATOM 3621 CE1 TYR B 173 15.862 -18.352 -3.734 1.00 58.29 C ANISOU 3621 CE1 TYR B 173 7459 6870 7817 916 14 -263 C ATOM 3622 CE2 TYR B 173 15.419 -20.684 -3.581 1.00 66.63 C ANISOU 3622 CE2 TYR B 173 8599 7765 8952 928 -254 -428 C ATOM 3623 CZ TYR B 173 16.122 -19.578 -3.176 1.00 64.34 C ANISOU 3623 CZ TYR B 173 8268 7541 8638 909 -91 -347 C ATOM 3624 OH TYR B 173 17.093 -19.714 -2.204 1.00 64.44 O ANISOU 3624 OH TYR B 173 8286 7505 8692 878 -61 -347 O ATOM 3625 N SER B 174 10.891 -17.239 -7.209 1.00 63.18 N ANISOU 3625 N SER B 174 8035 7607 8365 1005 -237 -199 N ATOM 3626 CA SER B 174 10.069 -16.853 -8.339 1.00 61.98 C ANISOU 3626 CA SER B 174 7880 7517 8154 1062 -309 -178 C ATOM 3627 C SER B 174 10.870 -15.870 -9.168 1.00 59.92 C ANISOU 3627 C SER B 174 7634 7371 7760 1103 -248 -69 C ATOM 3628 O SER B 174 11.825 -15.243 -8.683 1.00 52.26 O ANISOU 3628 O SER B 174 6659 6404 6793 1065 -146 9 O ATOM 3629 CB SER B 174 8.731 -16.242 -7.892 1.00 57.30 C ANISOU 3629 CB SER B 174 7225 6857 7690 1018 -342 -150 C ATOM 3630 OG SER B 174 8.228 -16.868 -6.721 1.00 56.24 O ANISOU 3630 OG SER B 174 7042 6653 7671 926 -342 -203 O ATOM 3631 N MET B 175 10.514 -15.770 -10.436 1.00 60.57 N ANISOU 3631 N MET B 175 7733 7564 7715 1165 -320 -51 N ATOM 3632 CA MET B 175 11.217 -14.849 -11.295 1.00 64.85 C ANISOU 3632 CA MET B 175 8285 8250 8105 1169 -278 92 C ATOM 3633 C MET B 175 10.380 -14.333 -12.466 1.00 62.07 C ANISOU 3633 C MET B 175 7950 7970 7665 1201 -385 172 C ATOM 3634 O MET B 175 9.623 -15.073 -13.092 1.00 62.16 O ANISOU 3634 O MET B 175 7969 8018 7632 1267 -486 61 O ATOM 3635 CB MET B 175 12.514 -15.497 -11.783 1.00 68.08 C ANISOU 3635 CB MET B 175 8687 8854 8325 1213 -213 27 C ATOM 3636 CG MET B 175 12.424 -16.044 -13.183 1.00 69.46 C ANISOU 3636 CG MET B 175 8865 9247 8281 1308 -287 -49 C ATOM 3637 SD MET B 175 14.028 -16.048 -13.964 1.00 96.84 S ANISOU 3637 SD MET B 175 12275 13055 11463 1338 -176 -43 S ATOM 3638 CE MET B 175 13.503 -15.985 -15.665 1.00 56.70 C ANISOU 3638 CE MET B 175 7192 8245 6108 1402 -268 -23 C ATOM 3639 N SER B 176 10.553 -13.057 -12.776 1.00 61.84 N ANISOU 3639 N SER B 176 7931 7951 7614 1149 -385 373 N ATOM 3640 CA SER B 176 9.906 -12.471 -13.933 1.00 68.14 C ANISOU 3640 CA SER B 176 8757 8823 8312 1165 -504 490 C ATOM 3641 C SER B 176 10.936 -12.399 -15.025 1.00 62.73 C ANISOU 3641 C SER B 176 8076 8421 7337 1143 -458 599 C ATOM 3642 O SER B 176 12.117 -12.279 -14.758 1.00 61.41 O ANISOU 3642 O SER B 176 7883 8347 7104 1086 -337 650 O ATOM 3643 CB SER B 176 9.379 -11.074 -13.624 1.00 78.15 C ANISOU 3643 CB SER B 176 10038 9903 9752 1115 -586 659 C ATOM 3644 OG SER B 176 10.444 -10.192 -13.317 1.00 87.26 O ANISOU 3644 OG SER B 176 11201 11045 10910 1018 -518 831 O ATOM 3645 N SER B 177 10.488 -12.540 -16.258 1.00 64.42 N ANISOU 3645 N SER B 177 8307 8808 7361 1189 -552 617 N ATOM 3646 CA SER B 177 11.365 -12.421 -17.406 1.00 62.21 C ANISOU 3646 CA SER B 177 8011 8870 6756 1159 -513 729 C ATOM 3647 C SER B 177 10.611 -11.651 -18.468 1.00 64.67 C ANISOU 3647 C SER B 177 8369 9241 6963 1130 -664 922 C ATOM 3648 O SER B 177 9.504 -12.022 -18.849 1.00 64.64 O ANISOU 3648 O SER B 177 8390 9176 6994 1220 -791 816 O ATOM 3649 CB SER B 177 11.773 -13.798 -17.922 1.00 57.23 C ANISOU 3649 CB SER B 177 7335 8484 5925 1285 -473 466 C ATOM 3650 OG SER B 177 12.692 -13.670 -18.986 1.00 66.00 O ANISOU 3650 OG SER B 177 8394 9993 6690 1262 -413 549 O ATOM 3651 N THR B 178 11.191 -10.560 -18.931 1.00 64.89 N ANISOU 3651 N THR B 178 8408 9375 6870 990 -669 1221 N ATOM 3652 CA THR B 178 10.472 -9.733 -19.869 1.00 68.06 C ANISOU 3652 CA THR B 178 8871 9792 7197 942 -847 1445 C ATOM 3653 C THR B 178 11.313 -9.400 -21.091 1.00 71.78 C ANISOU 3653 C THR B 178 9319 10675 7278 825 -823 1676 C ATOM 3654 O THR B 178 12.393 -8.816 -21.001 1.00 74.37 O ANISOU 3654 O THR B 178 9611 11126 7519 671 -729 1880 O ATOM 3655 CB THR B 178 9.895 -8.480 -19.182 1.00 65.71 C ANISOU 3655 CB THR B 178 8634 9110 7222 873 -985 1629 C ATOM 3656 OG1 THR B 178 9.673 -7.454 -20.154 1.00 72.08 O ANISOU 3656 OG1 THR B 178 9505 9963 7918 768 -1163 1944 O ATOM 3657 CG2 THR B 178 10.849 -7.982 -18.113 1.00 65.77 C ANISOU 3657 CG2 THR B 178 8619 8982 7388 774 -868 1696 C ATOM 3658 N LEU B 179 10.805 -9.823 -22.236 1.00 65.99 N ANISOU 3658 N LEU B 179 8592 10185 6295 894 -907 1635 N ATOM 3659 CA LEU B 179 11.430 -9.540 -23.501 1.00 70.29 C ANISOU 3659 CA LEU B 179 9105 11179 6423 785 -900 1850 C ATOM 3660 C LEU B 179 10.800 -8.261 -24.042 1.00 81.23 C ANISOU 3660 C LEU B 179 10592 12434 7839 642 -1121 2227 C ATOM 3661 O LEU B 179 9.586 -8.200 -24.283 1.00 82.69 O ANISOU 3661 O LEU B 179 10850 12419 8149 736 -1308 2187 O ATOM 3662 CB LEU B 179 11.184 -10.711 -24.440 1.00 70.77 C ANISOU 3662 CB LEU B 179 9118 11578 6192 955 -897 1573 C ATOM 3663 CG LEU B 179 11.411 -10.514 -25.932 1.00 76.09 C ANISOU 3663 CG LEU B 179 9762 12750 6399 885 -940 1749 C ATOM 3664 CD1 LEU B 179 12.890 -10.440 -26.220 1.00 81.19 C ANISOU 3664 CD1 LEU B 179 10277 13855 6715 758 -743 1854 C ATOM 3665 CD2 LEU B 179 10.756 -11.638 -26.712 1.00 74.78 C ANISOU 3665 CD2 LEU B 179 9580 12778 6055 1101 -1008 1421 C ATOM 3666 N THR B 180 11.625 -7.234 -24.222 1.00 80.93 N ANISOU 3666 N THR B 180 10555 12495 7701 409 -1120 2599 N ATOM 3667 CA THR B 180 11.130 -5.929 -24.640 1.00 80.90 C ANISOU 3667 CA THR B 180 10662 12307 7771 248 -1370 2995 C ATOM 3668 C THR B 180 11.571 -5.572 -26.049 1.00 81.10 C ANISOU 3668 C THR B 180 10672 12812 7331 64 -1418 3323 C ATOM 3669 O THR B 180 12.754 -5.533 -26.328 1.00 89.41 O ANISOU 3669 O THR B 180 11624 14251 8098 -98 -1254 3467 O ATOM 3670 CB THR B 180 11.619 -4.821 -23.693 1.00 83.80 C ANISOU 3670 CB THR B 180 11067 12325 8449 82 -1413 3232 C ATOM 3671 OG1 THR B 180 11.317 -5.172 -22.331 1.00 80.99 O ANISOU 3671 OG1 THR B 180 10703 11586 8482 245 -1341 2919 O ATOM 3672 CG2 THR B 180 10.951 -3.503 -24.055 1.00 82.84 C ANISOU 3672 CG2 THR B 180 11079 11916 8481 -47 -1741 3601 C ATOM 3673 N LEU B 181 10.616 -5.282 -26.927 1.00 85.77 N ANISOU 3673 N LEU B 181 11352 13398 7839 78 -1649 3452 N ATOM 3674 CA LEU B 181 10.912 -4.887 -28.304 1.00 86.86 C ANISOU 3674 CA LEU B 181 11490 13923 7590 -103 -1692 3709 C ATOM 3675 C LEU B 181 10.295 -3.533 -28.607 1.00 90.46 C ANISOU 3675 C LEU B 181 12096 13994 8280 -255 -1972 4029 C ATOM 3676 O LEU B 181 9.778 -2.848 -27.725 1.00 89.90 O ANISOU 3676 O LEU B 181 12114 13405 8637 -229 -2139 4081 O ATOM 3677 CB LEU B 181 10.344 -5.877 -29.325 1.00 86.88 C ANISOU 3677 CB LEU B 181 11461 14290 7260 74 -1693 3471 C ATOM 3678 CG LEU B 181 10.112 -7.351 -29.029 1.00 90.66 C ANISOU 3678 CG LEU B 181 11852 14913 7679 372 -1560 2992 C ATOM 3679 CD1 LEU B 181 9.003 -7.504 -28.011 1.00 92.47 C ANISOU 3679 CD1 LEU B 181 12164 14544 8427 558 -1666 2749 C ATOM 3680 CD2 LEU B 181 9.733 -8.054 -30.314 1.00 93.56 C ANISOU 3680 CD2 LEU B 181 12191 15701 7656 477 -1599 2841 C ATOM 3681 N THR B 182 10.372 -3.144 -29.870 1.00 94.89 N ANISOU 3681 N THR B 182 12672 14819 8561 -403 -2026 4219 N ATOM 3682 CA THR B 182 9.676 -1.967 -30.338 1.00100.78 C ANISOU 3682 CA THR B 182 13559 15247 9487 -515 -2315 4494 C ATOM 3683 C THR B 182 8.352 -2.422 -30.908 1.00102.93 C ANISOU 3683 C THR B 182 13908 15477 9723 -294 -2497 4337 C ATOM 3684 O THR B 182 8.270 -3.492 -31.507 1.00108.30 O ANISOU 3684 O THR B 182 14522 16553 10074 -163 -2386 4117 O ATOM 3685 CB THR B 182 10.465 -1.266 -31.436 1.00107.31 C ANISOU 3685 CB THR B 182 14351 16398 10025 -817 -2293 4819 C ATOM 3686 OG1 THR B 182 10.152 -1.857 -32.708 1.00113.28 O ANISOU 3686 OG1 THR B 182 15084 17582 10374 -766 -2282 4760 O ATOM 3687 CG2 THR B 182 11.959 -1.386 -31.148 1.00101.30 C ANISOU 3687 CG2 THR B 182 13426 15951 9111 -997 -2012 4861 C ATOM 3688 N LYS B 183 7.313 -1.617 -30.726 1.00 99.32 N ANISOU 3688 N LYS B 183 13577 14543 9617 -239 -2785 4417 N ATOM 3689 CA LYS B 183 6.032 -1.944 -31.311 1.00 98.01 C ANISOU 3689 CA LYS B 183 13474 14329 9437 -40 -2981 4284 C ATOM 3690 C LYS B 183 6.312 -2.370 -32.741 1.00107.13 C ANISOU 3690 C LYS B 183 14603 16025 10077 -118 -2910 4345 C ATOM 3691 O LYS B 183 5.739 -3.338 -33.228 1.00108.39 O ANISOU 3691 O LYS B 183 14740 16409 10034 71 -2908 4100 O ATOM 3692 CB LYS B 183 5.105 -0.723 -31.311 1.00100.26 C ANISOU 3692 CB LYS B 183 13878 14127 10088 -51 -3302 4448 C ATOM 3693 CG LYS B 183 3.684 -1.023 -31.813 1.00 99.45 C ANISOU 3693 CG LYS B 183 13821 13935 10029 177 -3517 4285 C ATOM 3694 CD LYS B 183 2.860 0.235 -32.070 1.00 98.08 C ANISOU 3694 CD LYS B 183 13749 13367 10148 140 -3832 4468 C ATOM 3695 CE LYS B 183 1.483 -0.111 -32.637 1.00 96.55 C ANISOU 3695 CE LYS B 183 13577 13138 9971 363 -4029 4300 C ATOM 3696 NZ LYS B 183 0.693 1.096 -33.045 1.00100.78 N ANISOU 3696 NZ LYS B 183 14203 13340 10748 321 -4343 4481 N ATOM 3697 N ASP B 184 7.226 -1.665 -33.403 1.00115.33 N ANISOU 3697 N ASP B 184 15626 17287 10909 -402 -2851 4655 N ATOM 3698 CA ASP B 184 7.536 -1.944 -34.803 1.00119.09 C ANISOU 3698 CA ASP B 184 16058 18294 10897 -504 -2785 4735 C ATOM 3699 C ASP B 184 7.924 -3.404 -35.071 1.00110.17 C ANISOU 3699 C ASP B 184 14790 17670 9400 -347 -2527 4380 C ATOM 3700 O ASP B 184 7.369 -4.030 -35.982 1.00106.84 O ANISOU 3700 O ASP B 184 14373 17506 8714 -222 -2575 4228 O ATOM 3701 CB ASP B 184 8.597 -0.978 -35.345 1.00127.70 C ANISOU 3701 CB ASP B 184 17105 19577 11840 -865 -2738 5127 C ATOM 3702 CG ASP B 184 8.177 -0.338 -36.667 1.00138.55 C ANISOU 3702 CG ASP B 184 18553 21083 13008 -1006 -2939 5402 C ATOM 3703 OD1 ASP B 184 9.060 0.059 -37.461 1.00146.18 O ANISOU 3703 OD1 ASP B 184 19433 22429 13681 -1286 -2854 5664 O ATOM 3704 OD2 ASP B 184 6.953 -0.231 -36.913 1.00136.55 O ANISOU 3704 OD2 ASP B 184 18430 20567 12886 -840 -3188 5355 O ATOM 3705 N GLU B 185 8.873 -3.944 -34.302 1.00 99.50 N ANISOU 3705 N GLU B 185 13308 16455 8040 -343 -2266 4227 N ATOM 3706 CA GLU B 185 9.260 -5.347 -34.482 1.00 95.73 C ANISOU 3706 CA GLU B 185 12683 16429 7262 -165 -2031 3838 C ATOM 3707 C GLU B 185 8.335 -6.367 -33.801 1.00 91.59 C ANISOU 3707 C GLU B 185 12179 15700 6920 159 -2086 3449 C ATOM 3708 O GLU B 185 8.191 -7.488 -34.280 1.00 87.70 O ANISOU 3708 O GLU B 185 11608 15519 6193 345 -2011 3111 O ATOM 3709 CB GLU B 185 10.732 -5.591 -34.139 1.00 99.17 C ANISOU 3709 CB GLU B 185 12936 17188 7557 -283 -1723 3803 C ATOM 3710 CG GLU B 185 11.134 -5.188 -32.742 1.00104.69 C ANISOU 3710 CG GLU B 185 13647 17506 8624 -328 -1675 3870 C ATOM 3711 CD GLU B 185 12.530 -5.675 -32.368 1.00108.74 C ANISOU 3711 CD GLU B 185 13964 18364 8989 -382 -1364 3746 C ATOM 3712 OE1 GLU B 185 13.014 -6.659 -32.965 1.00110.58 O ANISOU 3712 OE1 GLU B 185 14041 19087 8889 -274 -1181 3466 O ATOM 3713 OE2 GLU B 185 13.147 -5.072 -31.470 1.00109.79 O ANISOU 3713 OE2 GLU B 185 14090 18268 9358 -518 -1314 3905 O ATOM 3714 N TYR B 186 7.700 -5.984 -32.698 1.00 95.19 N ANISOU 3714 N TYR B 186 12723 15635 7809 229 -2227 3481 N ATOM 3715 CA TYR B 186 6.672 -6.837 -32.100 1.00 92.19 C ANISOU 3715 CA TYR B 186 12347 15050 7632 518 -2321 3154 C ATOM 3716 C TYR B 186 5.614 -7.237 -33.127 1.00 97.14 C ANISOU 3716 C TYR B 186 13025 15777 8107 653 -2508 3026 C ATOM 3717 O TYR B 186 5.084 -8.344 -33.087 1.00 95.27 O ANISOU 3717 O TYR B 186 12730 15626 7842 890 -2502 2661 O ATOM 3718 CB TYR B 186 5.970 -6.145 -30.931 1.00 82.43 C ANISOU 3718 CB TYR B 186 11189 13222 6908 553 -2499 3252 C ATOM 3719 CG TYR B 186 4.797 -6.951 -30.391 1.00 82.26 C ANISOU 3719 CG TYR B 186 11159 12910 7186 831 -2567 2850 C ATOM 3720 CD1 TYR B 186 5.001 -8.037 -29.541 1.00 80.13 C ANISOU 3720 CD1 TYR B 186 10797 12591 7060 988 -2338 2435 C ATOM 3721 CD2 TYR B 186 3.487 -6.639 -30.740 1.00 85.29 C ANISOU 3721 CD2 TYR B 186 11623 13050 7732 924 -2856 2865 C ATOM 3722 CE1 TYR B 186 3.934 -8.780 -29.048 1.00 77.76 C ANISOU 3722 CE1 TYR B 186 10482 12016 7048 1201 -2392 2075 C ATOM 3723 CE2 TYR B 186 2.412 -7.376 -30.250 1.00 82.69 C ANISOU 3723 CE2 TYR B 186 11264 12462 7693 1154 -2898 2479 C ATOM 3724 CZ TYR B 186 2.644 -8.441 -29.407 1.00 82.33 C ANISOU 3724 CZ TYR B 186 11123 12384 7775 1276 -2663 2100 C ATOM 3725 OH TYR B 186 1.586 -9.171 -28.922 1.00 82.75 O ANISOU 3725 OH TYR B 186 11137 12199 8104 1462 -2713 1757 O ATOM 3726 N GLU B 187 5.300 -6.322 -34.037 1.00104.53 N ANISOU 3726 N GLU B 187 14070 16683 8963 507 -2684 3319 N ATOM 3727 CA GLU B 187 4.213 -6.524 -34.992 1.00112.11 C ANISOU 3727 CA GLU B 187 15101 17679 9816 624 -2904 3243 C ATOM 3728 C GLU B 187 4.706 -7.184 -36.265 1.00115.00 C ANISOU 3728 C GLU B 187 15399 18611 9685 597 -2775 3136 C ATOM 3729 O GLU B 187 3.940 -7.394 -37.208 1.00115.21 O ANISOU 3729 O GLU B 187 15479 18740 9557 673 -2937 3073 O ATOM 3730 CB GLU B 187 3.533 -5.193 -35.320 1.00115.97 C ANISOU 3730 CB GLU B 187 15740 17825 10497 518 -3182 3590 C ATOM 3731 CG GLU B 187 3.114 -4.434 -34.080 1.00115.57 C ANISOU 3731 CG GLU B 187 15732 17209 10972 544 -3301 3670 C ATOM 3732 CD GLU B 187 1.900 -3.575 -34.304 1.00120.49 C ANISOU 3732 CD GLU B 187 16458 17452 11872 607 -3618 3784 C ATOM 3733 OE1 GLU B 187 1.840 -2.910 -35.358 1.00131.06 O ANISOU 3733 OE1 GLU B 187 17873 18901 13024 481 -3737 4032 O ATOM 3734 OE2 GLU B 187 1.008 -3.568 -33.430 1.00115.74 O ANISOU 3734 OE2 GLU B 187 15839 16457 11680 779 -3741 3614 O ATOM 3735 N ARG B 188 5.997 -7.492 -36.283 1.00114.89 N ANISOU 3735 N ARG B 188 15252 18968 9432 495 -2485 3103 N ATOM 3736 CA ARG B 188 6.600 -8.170 -37.411 1.00116.73 C ANISOU 3736 CA ARG B 188 15368 19773 9210 489 -2326 2950 C ATOM 3737 C ARG B 188 6.466 -9.666 -37.174 1.00115.92 C ANISOU 3737 C ARG B 188 15155 19812 9078 777 -2221 2421 C ATOM 3738 O ARG B 188 6.901 -10.475 -37.990 1.00115.62 O ANISOU 3738 O ARG B 188 14995 20219 8718 851 -2093 2170 O ATOM 3739 CB ARG B 188 8.071 -7.777 -37.530 1.00118.26 C ANISOU 3739 CB ARG B 188 15431 20307 9194 253 -2069 3142 C ATOM 3740 CG ARG B 188 8.510 -7.416 -38.935 1.00128.93 C ANISOU 3740 CG ARG B 188 16731 22124 10134 69 -2042 3343 C ATOM 3741 CD ARG B 188 8.829 -5.929 -39.057 1.00135.62 C ANISOU 3741 CD ARG B 188 17655 22825 11050 -258 -2130 3880 C ATOM 3742 NE ARG B 188 9.902 -5.520 -38.152 1.00131.65 N ANISOU 3742 NE ARG B 188 17061 22259 10699 -419 -1949 4012 N ATOM 3743 CZ ARG B 188 10.518 -4.340 -38.196 1.00126.50 C ANISOU 3743 CZ ARG B 188 16414 21555 10097 -731 -1970 4438 C ATOM 3744 NH1 ARG B 188 10.178 -3.439 -39.114 1.00127.24 N ANISOU 3744 NH1 ARG B 188 16597 21656 10092 -922 -2163 4788 N ATOM 3745 NH2 ARG B 188 11.481 -4.067 -37.323 1.00120.20 N ANISOU 3745 NH2 ARG B 188 15525 20694 9453 -858 -1810 4512 N ATOM 3746 N HIS B 189 5.847 -10.024 -36.050 1.00115.77 N ANISOU 3746 N HIS B 189 15166 19398 9421 949 -2290 2241 N ATOM 3747 CA HIS B 189 5.807 -11.417 -35.603 1.00113.01 C ANISOU 3747 CA HIS B 189 14714 19105 9121 1218 -2191 1739 C ATOM 3748 C HIS B 189 4.473 -11.880 -35.012 1.00114.40 C ANISOU 3748 C HIS B 189 14955 18874 9638 1439 -2402 1518 C ATOM 3749 O HIS B 189 3.800 -11.149 -34.280 1.00118.22 O ANISOU 3749 O HIS B 189 15523 18949 10445 1416 -2554 1721 O ATOM 3750 CB HIS B 189 6.945 -11.691 -34.615 1.00105.16 C ANISOU 3750 CB HIS B 189 13612 18154 8191 1214 -1937 1647 C ATOM 3751 CG HIS B 189 8.297 -11.691 -35.253 1.00103.08 C ANISOU 3751 CG HIS B 189 13211 18377 7579 1075 -1695 1688 C ATOM 3752 ND1 HIS B 189 8.523 -12.216 -36.507 1.00101.24 N ANISOU 3752 ND1 HIS B 189 12885 18594 6988 1113 -1649 1524 N ATOM 3753 CD2 HIS B 189 9.487 -11.216 -34.822 1.00104.33 C ANISOU 3753 CD2 HIS B 189 13285 18653 7702 900 -1492 1870 C ATOM 3754 CE1 HIS B 189 9.798 -12.071 -36.819 1.00102.16 C ANISOU 3754 CE1 HIS B 189 12849 19105 6863 975 -1424 1597 C ATOM 3755 NE2 HIS B 189 10.405 -11.465 -35.815 1.00106.09 N ANISOU 3755 NE2 HIS B 189 13350 19406 7553 837 -1326 1810 N ATOM 3756 N ASN B 190 4.131 -13.126 -35.327 1.00110.40 N ANISOU 3756 N ASN B 190 14388 18477 9080 1659 -2410 1078 N ATOM 3757 CA ASN B 190 2.883 -13.752 -34.921 1.00104.16 C ANISOU 3757 CA ASN B 190 13636 17341 8598 1865 -2602 809 C ATOM 3758 C ASN B 190 2.988 -14.489 -33.579 1.00100.42 C ANISOU 3758 C ASN B 190 13121 16595 8438 2018 -2524 526 C ATOM 3759 O ASN B 190 2.277 -14.162 -32.634 1.00 99.41 O ANISOU 3759 O ASN B 190 13039 15972 8758 1995 -2580 575 O ATOM 3760 CB ASN B 190 2.405 -14.698 -36.023 1.00110.34 C ANISOU 3760 CB ASN B 190 14388 18340 9194 1999 -2686 493 C ATOM 3761 CG ASN B 190 0.895 -14.855 -36.047 1.00118.12 C ANISOU 3761 CG ASN B 190 15440 18994 10448 2109 -2953 394 C ATOM 3762 OD1 ASN B 190 0.343 -15.748 -35.400 1.00113.37 O ANISOU 3762 OD1 ASN B 190 14812 18133 10131 2274 -3005 63 O ATOM 3763 ND2 ASN B 190 0.218 -13.990 -36.805 1.00125.17 N ANISOU 3763 ND2 ASN B 190 16413 19880 11264 2002 -3137 684 N ATOM 3764 N SER B 191 3.858 -15.499 -33.519 1.00 98.68 N ANISOU 3764 N SER B 191 12807 16591 8098 2113 -2350 206 N ATOM 3765 CA SER B 191 4.045 -16.327 -32.324 1.00 92.69 C ANISOU 3765 CA SER B 191 12015 15532 7672 2216 -2262 -85 C ATOM 3766 C SER B 191 5.133 -15.838 -31.360 1.00 91.74 C ANISOU 3766 C SER B 191 11862 15336 7658 2078 -2023 85 C ATOM 3767 O SER B 191 6.196 -15.368 -31.775 1.00 97.26 O ANISOU 3767 O SER B 191 12508 16425 8023 1974 -1879 268 O ATOM 3768 CB SER B 191 4.362 -17.768 -32.722 1.00 96.89 C ANISOU 3768 CB SER B 191 12469 16280 8066 2426 -2261 -560 C ATOM 3769 OG SER B 191 5.306 -18.331 -31.821 1.00101.13 O ANISOU 3769 OG SER B 191 12947 16764 8714 2469 -2096 -740 O ATOM 3770 N TYR B 192 4.844 -15.966 -30.068 1.00 82.47 N ANISOU 3770 N TYR B 192 10710 13683 6943 2069 -1986 23 N ATOM 3771 CA TYR B 192 5.781 -15.649 -29.000 1.00 77.62 C ANISOU 3771 CA TYR B 192 10068 12936 6489 1963 -1778 123 C ATOM 3772 C TYR B 192 5.731 -16.748 -27.939 1.00 88.62 C ANISOU 3772 C TYR B 192 11438 14024 8210 2073 -1741 -214 C ATOM 3773 O TYR B 192 4.691 -16.968 -27.324 1.00 94.62 O ANISOU 3773 O TYR B 192 12234 14402 9314 2096 -1853 -290 O ATOM 3774 CB TYR B 192 5.445 -14.286 -28.380 1.00 66.02 C ANISOU 3774 CB TYR B 192 8666 11149 5268 1781 -1792 508 C ATOM 3775 CG TYR B 192 5.737 -13.130 -29.296 1.00 67.39 C ANISOU 3775 CG TYR B 192 8872 11595 5137 1625 -1832 902 C ATOM 3776 CD1 TYR B 192 6.899 -12.373 -29.142 1.00 75.32 C ANISOU 3776 CD1 TYR B 192 9849 12764 6006 1448 -1673 1177 C ATOM 3777 CD2 TYR B 192 4.871 -12.809 -30.336 1.00 65.81 C ANISOU 3777 CD2 TYR B 192 8728 11498 4777 1638 -2044 1015 C ATOM 3778 CE1 TYR B 192 7.181 -11.314 -29.997 1.00 83.39 C ANISOU 3778 CE1 TYR B 192 10900 14041 6742 1263 -1733 1582 C ATOM 3779 CE2 TYR B 192 5.137 -11.755 -31.198 1.00 74.44 C ANISOU 3779 CE2 TYR B 192 9861 12844 5580 1469 -2109 1413 C ATOM 3780 CZ TYR B 192 6.292 -11.011 -31.025 1.00 86.23 C ANISOU 3780 CZ TYR B 192 11328 14493 6942 1271 -1956 1707 C ATOM 3781 OH TYR B 192 6.561 -9.965 -31.878 1.00 90.87 O ANISOU 3781 OH TYR B 192 11955 15330 7240 1064 -2043 2142 O ATOM 3782 N THR B 193 6.856 -17.427 -27.720 1.00 92.10 N ANISOU 3782 N THR B 193 11807 14646 8540 2133 -1595 -405 N ATOM 3783 CA THR B 193 6.922 -18.549 -26.790 1.00 82.99 C ANISOU 3783 CA THR B 193 10639 13225 7670 2235 -1591 -721 C ATOM 3784 C THR B 193 7.923 -18.259 -25.705 1.00 78.59 C ANISOU 3784 C THR B 193 10053 12559 7249 2138 -1388 -624 C ATOM 3785 O THR B 193 9.030 -17.818 -25.976 1.00 81.87 O ANISOU 3785 O THR B 193 10407 13291 7408 2084 -1234 -508 O ATOM 3786 CB THR B 193 7.420 -19.834 -27.472 1.00 92.70 C ANISOU 3786 CB THR B 193 11806 14741 8674 2446 -1650 -1123 C ATOM 3787 OG1 THR B 193 6.991 -19.878 -28.839 1.00105.10 O ANISOU 3787 OG1 THR B 193 13370 16648 9915 2533 -1782 -1178 O ATOM 3788 CG2 THR B 193 6.905 -21.042 -26.740 1.00 91.76 C ANISOU 3788 CG2 THR B 193 11715 14246 8902 2551 -1788 -1433 C ATOM 3789 N CYS B 194 7.533 -18.531 -24.473 1.00 78.89 N ANISOU 3789 N CYS B 194 10122 12172 7680 2106 -1391 -672 N ATOM 3790 CA CYS B 194 8.417 -18.406 -23.320 1.00 77.69 C ANISOU 3790 CA CYS B 194 9948 11878 7692 2029 -1220 -622 C ATOM 3791 C CYS B 194 8.511 -19.776 -22.632 1.00 79.86 C ANISOU 3791 C CYS B 194 10217 11957 8168 2140 -1277 -951 C ATOM 3792 O CYS B 194 7.527 -20.303 -22.104 1.00 75.37 O ANISOU 3792 O CYS B 194 9689 11071 7876 2140 -1409 -1040 O ATOM 3793 CB CYS B 194 7.909 -17.290 -22.391 1.00 74.84 C ANISOU 3793 CB CYS B 194 9630 11198 7606 1862 -1174 -330 C ATOM 3794 SG CYS B 194 8.045 -17.539 -20.600 1.00 74.63 S ANISOU 3794 SG CYS B 194 9604 10775 7977 1795 -1081 -373 S ATOM 3795 N GLU B 195 9.705 -20.357 -22.665 1.00 81.89 N ANISOU 3795 N GLU B 195 10414 12417 8282 2229 -1197 -1127 N ATOM 3796 CA GLU B 195 9.880 -21.768 -22.356 1.00 76.23 C ANISOU 3796 CA GLU B 195 9695 11576 7694 2379 -1317 -1481 C ATOM 3797 C GLU B 195 10.792 -22.006 -21.161 1.00 76.85 C ANISOU 3797 C GLU B 195 9759 11485 7957 2340 -1206 -1503 C ATOM 3798 O GLU B 195 11.921 -21.527 -21.140 1.00 87.13 O ANISOU 3798 O GLU B 195 10992 13021 9093 2319 -1029 -1429 O ATOM 3799 CB GLU B 195 10.467 -22.439 -23.580 1.00 77.91 C ANISOU 3799 CB GLU B 195 9836 12203 7563 2584 -1382 -1767 C ATOM 3800 CG GLU B 195 10.879 -23.849 -23.369 1.00 89.57 C ANISOU 3800 CG GLU B 195 11299 13586 9146 2773 -1530 -2163 C ATOM 3801 CD GLU B 195 11.410 -24.458 -24.640 1.00106.64 C ANISOU 3801 CD GLU B 195 13370 16196 10951 3007 -1609 -2488 C ATOM 3802 OE1 GLU B 195 11.822 -25.634 -24.608 1.00118.62 O ANISOU 3802 OE1 GLU B 195 14864 17670 12535 3207 -1766 -2866 O ATOM 3803 OE2 GLU B 195 11.413 -23.758 -25.677 1.00107.39 O ANISOU 3803 OE2 GLU B 195 13414 16697 10694 2995 -1530 -2370 O ATOM 3804 N ALA B 196 10.318 -22.759 -20.172 1.00 72.20 N ANISOU 3804 N ALA B 196 9226 10505 7701 2319 -1317 -1596 N ATOM 3805 CA ALA B 196 11.087 -22.966 -18.933 1.00 64.88 C ANISOU 3805 CA ALA B 196 8299 9384 6969 2262 -1230 -1587 C ATOM 3806 C ALA B 196 11.524 -24.404 -18.719 1.00 68.47 C ANISOU 3806 C ALA B 196 8763 9720 7531 2413 -1407 -1919 C ATOM 3807 O ALA B 196 10.767 -25.330 -18.978 1.00 79.09 O ANISOU 3807 O ALA B 196 10155 10907 8988 2486 -1644 -2104 O ATOM 3808 CB ALA B 196 10.293 -22.513 -17.743 1.00 53.74 C ANISOU 3808 CB ALA B 196 6939 7622 5857 2070 -1197 -1365 C ATOM 3809 N THR B 197 12.752 -24.590 -18.248 1.00 66.57 N ANISOU 3809 N THR B 197 8478 9543 7273 2461 -1318 -1997 N ATOM 3810 CA THR B 197 13.198 -25.901 -17.780 1.00 64.65 C ANISOU 3810 CA THR B 197 8259 9102 7205 2587 -1511 -2282 C ATOM 3811 C THR B 197 13.597 -25.819 -16.315 1.00 63.73 C ANISOU 3811 C THR B 197 8177 8703 7335 2440 -1431 -2130 C ATOM 3812 O THR B 197 14.021 -24.779 -15.832 1.00 62.53 O ANISOU 3812 O THR B 197 7992 8629 7139 2310 -1193 -1888 O ATOM 3813 CB THR B 197 14.338 -26.466 -18.614 1.00 66.54 C ANISOU 3813 CB THR B 197 8397 9682 7202 2841 -1545 -2612 C ATOM 3814 OG1 THR B 197 15.318 -25.448 -18.819 1.00 63.35 O ANISOU 3814 OG1 THR B 197 7881 9650 6538 2802 -1261 -2464 O ATOM 3815 CG2 THR B 197 13.814 -26.925 -19.960 1.00 75.49 C ANISOU 3815 CG2 THR B 197 9511 11033 8139 3017 -1711 -2849 C ATOM 3816 N HIS B 198 13.397 -26.907 -15.591 1.00 69.45 N ANISOU 3816 N HIS B 198 8976 9084 8328 2443 -1654 -2254 N ATOM 3817 CA HIS B 198 13.638 -26.911 -14.158 1.00 68.74 C ANISOU 3817 CA HIS B 198 8931 8717 8471 2283 -1609 -2094 C ATOM 3818 C HIS B 198 13.809 -28.359 -13.788 1.00 75.56 C ANISOU 3818 C HIS B 198 9861 9300 9549 2374 -1920 -2332 C ATOM 3819 O HIS B 198 13.389 -29.239 -14.545 1.00 81.69 O ANISOU 3819 O HIS B 198 10665 10030 10344 2512 -2177 -2568 O ATOM 3820 CB HIS B 198 12.448 -26.312 -13.424 1.00 61.24 C ANISOU 3820 CB HIS B 198 8025 7566 7677 2035 -1545 -1799 C ATOM 3821 CG HIS B 198 12.691 -26.046 -11.977 1.00 63.02 C ANISOU 3821 CG HIS B 198 8271 7600 8075 1856 -1440 -1605 C ATOM 3822 ND1 HIS B 198 12.285 -26.909 -10.986 1.00 67.60 N ANISOU 3822 ND1 HIS B 198 8919 7862 8902 1735 -1618 -1582 N ATOM 3823 CD2 HIS B 198 13.267 -24.993 -11.347 1.00 67.75 C ANISOU 3823 CD2 HIS B 198 8830 8286 8628 1764 -1187 -1416 C ATOM 3824 CE1 HIS B 198 12.615 -26.409 -9.807 1.00 70.44 C ANISOU 3824 CE1 HIS B 198 9276 8151 9338 1586 -1466 -1396 C ATOM 3825 NE2 HIS B 198 13.209 -25.244 -9.998 1.00 65.31 N ANISOU 3825 NE2 HIS B 198 8561 7731 8523 1611 -1207 -1307 N ATOM 3826 N LYS B 199 14.412 -28.614 -12.635 1.00 71.11 N ANISOU 3826 N LYS B 199 9331 8533 9156 2296 -1927 -2270 N ATOM 3827 CA LYS B 199 14.728 -29.978 -12.257 1.00 74.31 C ANISOU 3827 CA LYS B 199 9804 8661 9771 2378 -2251 -2475 C ATOM 3828 C LYS B 199 13.488 -30.848 -12.043 1.00 81.73 C ANISOU 3828 C LYS B 199 10845 9261 10947 2245 -2546 -2433 C ATOM 3829 O LYS B 199 13.553 -32.066 -12.201 1.00 89.58 O ANISOU 3829 O LYS B 199 11850 10127 12061 2286 -2848 -2556 O ATOM 3830 CB LYS B 199 15.656 -29.994 -11.044 1.00 73.82 C ANISOU 3830 CB LYS B 199 9746 8487 9817 2279 -2183 -2356 C ATOM 3831 CG LYS B 199 15.013 -29.771 -9.715 1.00 76.90 C ANISOU 3831 CG LYS B 199 10221 8588 10410 2014 -2153 -2070 C ATOM 3832 CD LYS B 199 15.395 -30.927 -8.799 1.00 87.63 C ANISOU 3832 CD LYS B 199 11644 9671 11982 1926 -2413 -2060 C ATOM 3833 CE LYS B 199 16.907 -31.191 -8.801 1.00 88.51 C ANISOU 3833 CE LYS B 199 11679 9938 12012 2073 -2397 -2204 C ATOM 3834 NZ LYS B 199 17.290 -32.343 -7.934 1.00 84.20 N ANISOU 3834 NZ LYS B 199 11189 9138 11666 1993 -2675 -2181 N ATOM 3835 N THR B 200 12.358 -30.213 -11.727 1.00 78.50 N ANISOU 3835 N THR B 200 10451 8800 10575 2025 -2431 -2174 N ATOM 3836 CA THR B 200 11.102 -30.906 -11.412 1.00 75.67 C ANISOU 3836 CA THR B 200 10164 8153 10436 1845 -2675 -2085 C ATOM 3837 C THR B 200 10.347 -31.412 -12.644 1.00 88.40 C ANISOU 3837 C THR B 200 11781 9791 12015 1977 -2889 -2289 C ATOM 3838 O THR B 200 9.636 -32.421 -12.592 1.00 86.29 O ANISOU 3838 O THR B 200 11584 9245 11957 1911 -3217 -2342 O ATOM 3839 CB THR B 200 10.149 -29.987 -10.615 1.00 67.80 C ANISOU 3839 CB THR B 200 9131 7165 9465 1557 -2449 -1738 C ATOM 3840 OG1 THR B 200 9.798 -28.851 -11.416 1.00 70.81 O ANISOU 3840 OG1 THR B 200 9433 7836 9634 1611 -2207 -1690 O ATOM 3841 CG2 THR B 200 10.804 -29.505 -9.328 1.00 57.97 C ANISOU 3841 CG2 THR B 200 7880 5890 8256 1417 -2256 -1542 C ATOM 3842 N SER B 201 10.484 -30.685 -13.746 1.00103.56 N ANISOU 3842 N SER B 201 13628 12053 13669 2144 -2713 -2385 N ATOM 3843 CA SER B 201 9.804 -31.030 -14.992 1.00107.90 C ANISOU 3843 CA SER B 201 14172 12690 14135 2285 -2886 -2582 C ATOM 3844 C SER B 201 10.788 -31.641 -15.978 1.00 98.74 C ANISOU 3844 C SER B 201 12970 11723 12824 2600 -3007 -2938 C ATOM 3845 O SER B 201 11.792 -31.022 -16.336 1.00100.06 O ANISOU 3845 O SER B 201 13057 12215 12748 2736 -2780 -3001 O ATOM 3846 CB SER B 201 9.119 -29.790 -15.599 1.00112.43 C ANISOU 3846 CB SER B 201 14678 13542 14499 2228 -2624 -2404 C ATOM 3847 OG SER B 201 9.871 -28.596 -15.384 1.00106.64 O ANISOU 3847 OG SER B 201 13881 13054 13582 2206 -2275 -2235 O ATOM 3848 N THR B 202 10.508 -32.862 -16.401 1.00 90.40 N ANISOU 3848 N THR B 202 11908 10526 11916 2675 -3328 -3070 N ATOM 3849 CA THR B 202 11.386 -33.554 -17.334 1.00 90.67 C ANISOU 3849 CA THR B 202 11832 10778 11840 2953 -3436 -3331 C ATOM 3850 C THR B 202 11.013 -33.204 -18.782 1.00 86.92 C ANISOU 3850 C THR B 202 11287 10632 11105 3133 -3384 -3493 C ATOM 3851 O THR B 202 11.593 -33.713 -19.737 1.00 86.94 O ANISOU 3851 O THR B 202 11177 10866 10991 3376 -3461 -3726 O ATOM 3852 CB THR B 202 11.402 -35.083 -17.077 1.00109.84 C ANISOU 3852 CB THR B 202 14277 12889 14569 2991 -3825 -3408 C ATOM 3853 OG1 THR B 202 12.058 -35.752 -18.162 1.00113.99 O ANISOU 3853 OG1 THR B 202 14680 13636 14996 3298 -3962 -3704 O ATOM 3854 CG2 THR B 202 9.979 -35.632 -16.923 1.00110.82 C ANISOU 3854 CG2 THR B 202 14500 12668 14940 2829 -4061 -3292 C ATOM 3855 N SER B 203 10.026 -32.331 -18.927 1.00 83.79 N ANISOU 3855 N SER B 203 10952 10266 10617 3008 -3263 -3368 N ATOM 3856 CA SER B 203 9.705 -31.749 -20.221 1.00 91.19 C ANISOU 3856 CA SER B 203 11832 11566 11250 3137 -3167 -3462 C ATOM 3857 C SER B 203 9.759 -30.245 -20.048 1.00 88.89 C ANISOU 3857 C SER B 203 11555 11517 10702 3025 -2844 -3273 C ATOM 3858 O SER B 203 9.395 -29.732 -18.988 1.00 87.73 O ANISOU 3858 O SER B 203 11441 11155 10736 2776 -2709 -2953 O ATOM 3859 CB SER B 203 8.309 -32.177 -20.701 1.00 98.14 C ANISOU 3859 CB SER B 203 12767 12261 12260 3091 -3392 -3474 C ATOM 3860 OG SER B 203 8.335 -33.426 -21.379 1.00104.62 O ANISOU 3860 OG SER B 203 13543 13002 13207 3281 -3656 -3695 O ATOM 3861 N PRO B 204 10.209 -29.523 -21.084 1.00 86.14 N ANISOU 3861 N PRO B 204 11115 11637 9977 3151 -2657 -3314 N ATOM 3862 CA PRO B 204 10.266 -28.069 -20.945 1.00 82.94 C ANISOU 3862 CA PRO B 204 10668 11441 9406 2976 -2306 -2944 C ATOM 3863 C PRO B 204 8.859 -27.546 -20.720 1.00 79.78 C ANISOU 3863 C PRO B 204 10325 10833 9156 2767 -2314 -2670 C ATOM 3864 O PRO B 204 7.961 -27.918 -21.476 1.00 81.62 O ANISOU 3864 O PRO B 204 10578 11057 9375 2825 -2507 -2783 O ATOM 3865 CB PRO B 204 10.769 -27.600 -22.315 1.00 82.58 C ANISOU 3865 CB PRO B 204 10522 11931 8924 3141 -2200 -3055 C ATOM 3866 CG PRO B 204 11.208 -28.821 -23.033 1.00 83.01 C ANISOU 3866 CG PRO B 204 10507 12065 8968 3394 -2408 -3435 C ATOM 3867 CD PRO B 204 10.440 -29.954 -22.468 1.00 84.16 C ANISOU 3867 CD PRO B 204 10748 11706 9522 3373 -2715 -3528 C ATOM 3868 N ILE B 205 8.667 -26.705 -19.708 1.00 75.26 N ANISOU 3868 N ILE B 205 9764 10109 8723 2544 -2119 -2341 N ATOM 3869 CA ILE B 205 7.361 -26.094 -19.462 1.00 77.31 C ANISOU 3869 CA ILE B 205 10044 10216 9113 2362 -2107 -2097 C ATOM 3870 C ILE B 205 7.150 -24.953 -20.465 1.00 77.99 C ANISOU 3870 C ILE B 205 10093 10623 8916 2379 -1971 -1953 C ATOM 3871 O ILE B 205 7.901 -23.969 -20.466 1.00 78.80 O ANISOU 3871 O ILE B 205 10160 10931 8848 2343 -1741 -1779 O ATOM 3872 CB ILE B 205 7.285 -25.547 -18.016 1.00 69.44 C ANISOU 3872 CB ILE B 205 9054 8989 8343 2141 -1947 -1830 C ATOM 3873 CG1 ILE B 205 7.565 -26.672 -17.011 1.00 73.25 C ANISOU 3873 CG1 ILE B 205 9579 9172 9081 2100 -2091 -1937 C ATOM 3874 CG2 ILE B 205 5.956 -24.852 -17.760 1.00 55.62 C ANISOU 3874 CG2 ILE B 205 7290 7131 6712 1978 -1927 -1613 C ATOM 3875 CD1 ILE B 205 7.554 -26.223 -15.557 1.00 70.24 C ANISOU 3875 CD1 ILE B 205 9195 8601 8890 1885 -1939 -1693 C ATOM 3876 N VAL B 206 6.127 -25.076 -21.312 1.00 72.44 N ANISOU 3876 N VAL B 206 9402 9953 8170 2422 -2133 -2009 N ATOM 3877 CA VAL B 206 5.970 -24.157 -22.444 1.00 74.21 C ANISOU 3877 CA VAL B 206 9601 10503 8092 2463 -2062 -1904 C ATOM 3878 C VAL B 206 4.702 -23.315 -22.343 1.00 77.56 C ANISOU 3878 C VAL B 206 10036 10799 8636 2323 -2069 -1660 C ATOM 3879 O VAL B 206 3.596 -23.850 -22.367 1.00 81.10 O ANISOU 3879 O VAL B 206 10496 11060 9257 2309 -2262 -1739 O ATOM 3880 CB VAL B 206 5.959 -24.909 -23.813 1.00 64.21 C ANISOU 3880 CB VAL B 206 8324 9493 6579 2680 -2253 -2206 C ATOM 3881 CG1 VAL B 206 5.713 -23.954 -24.935 1.00 62.18 C ANISOU 3881 CG1 VAL B 206 8048 9575 6004 2691 -2193 -2058 C ATOM 3882 CG2 VAL B 206 7.269 -25.637 -24.064 1.00 70.89 C ANISOU 3882 CG2 VAL B 206 9128 10549 7258 2862 -2246 -2488 C ATOM 3883 N LYS B 207 4.863 -21.998 -22.229 1.00 77.63 N ANISOU 3883 N LYS B 207 10032 10899 8563 2222 -1881 -1373 N ATOM 3884 CA LYS B 207 3.723 -21.081 -22.331 1.00 76.05 C ANISOU 3884 CA LYS B 207 9835 10621 8440 2133 -1914 -1165 C ATOM 3885 C LYS B 207 3.865 -20.120 -23.524 1.00 75.60 C ANISOU 3885 C LYS B 207 9786 10877 8062 2166 -1889 -1010 C ATOM 3886 O LYS B 207 4.940 -19.600 -23.788 1.00 75.83 O ANISOU 3886 O LYS B 207 9805 11143 7862 2157 -1739 -906 O ATOM 3887 CB LYS B 207 3.508 -20.331 -21.020 1.00 73.18 C ANISOU 3887 CB LYS B 207 9453 10012 8340 1974 -1783 -957 C ATOM 3888 CG LYS B 207 3.074 -21.232 -19.865 1.00 73.24 C ANISOU 3888 CG LYS B 207 9441 9730 8655 1902 -1835 -1066 C ATOM 3889 CD LYS B 207 1.749 -21.936 -20.143 1.00 73.40 C ANISOU 3889 CD LYS B 207 9445 9632 8813 1906 -2060 -1188 C ATOM 3890 CE LYS B 207 1.046 -22.355 -18.856 1.00 74.66 C ANISOU 3890 CE LYS B 207 9554 9527 9289 1753 -2082 -1170 C ATOM 3891 NZ LYS B 207 -0.247 -23.063 -19.118 1.00 81.14 N ANISOU 3891 NZ LYS B 207 10337 10247 10247 1728 -2308 -1274 N ATOM 3892 N SER B 208 2.784 -19.903 -24.261 1.00 80.30 N ANISOU 3892 N SER B 208 10393 11486 8630 2191 -2049 -985 N ATOM 3893 CA SER B 208 2.897 -19.211 -25.541 1.00 90.85 C ANISOU 3893 CA SER B 208 11747 13147 9624 2230 -2075 -862 C ATOM 3894 C SER B 208 1.608 -18.517 -25.974 1.00 89.89 C ANISOU 3894 C SER B 208 11645 12938 9571 2202 -2232 -718 C ATOM 3895 O SER B 208 0.524 -18.822 -25.469 1.00 95.57 O ANISOU 3895 O SER B 208 12345 13389 10577 2191 -2347 -794 O ATOM 3896 CB SER B 208 3.354 -20.194 -26.631 1.00 99.51 C ANISOU 3896 CB SER B 208 12831 14561 10416 2397 -2161 -1141 C ATOM 3897 OG SER B 208 3.196 -19.643 -27.932 1.00104.13 O ANISOU 3897 OG SER B 208 13427 15477 10661 2432 -2229 -1039 O ATOM 3898 N PHE B 209 1.732 -17.577 -26.908 1.00 81.60 N ANISOU 3898 N PHE B 209 10625 12127 8252 2182 -2246 -499 N ATOM 3899 CA PHE B 209 0.560 -16.948 -27.501 1.00 82.38 C ANISOU 3899 CA PHE B 209 10751 12173 8378 2181 -2434 -374 C ATOM 3900 C PHE B 209 0.852 -16.530 -28.933 1.00 88.82 C ANISOU 3900 C PHE B 209 11603 13379 8765 2206 -2500 -250 C ATOM 3901 O PHE B 209 2.001 -16.489 -29.348 1.00 90.62 O ANISOU 3901 O PHE B 209 11821 13927 8683 2190 -2365 -203 O ATOM 3902 CB PHE B 209 0.044 -15.772 -26.643 1.00 79.54 C ANISOU 3902 CB PHE B 209 10394 11514 8312 2068 -2421 -122 C ATOM 3903 CG PHE B 209 0.852 -14.497 -26.766 1.00 79.29 C ANISOU 3903 CG PHE B 209 10408 11579 8138 1955 -2328 215 C ATOM 3904 CD1 PHE B 209 0.480 -13.508 -27.663 1.00 81.78 C ANISOU 3904 CD1 PHE B 209 10781 11985 8305 1920 -2480 470 C ATOM 3905 CD2 PHE B 209 1.957 -14.276 -25.965 1.00 82.11 C ANISOU 3905 CD2 PHE B 209 10754 11916 8527 1870 -2116 293 C ATOM 3906 CE1 PHE B 209 1.202 -12.335 -27.775 1.00 83.80 C ANISOU 3906 CE1 PHE B 209 11086 12303 8451 1785 -2434 812 C ATOM 3907 CE2 PHE B 209 2.684 -13.102 -26.068 1.00 85.03 C ANISOU 3907 CE2 PHE B 209 11161 12357 8787 1743 -2055 616 C ATOM 3908 CZ PHE B 209 2.305 -12.131 -26.975 1.00 87.81 C ANISOU 3908 CZ PHE B 209 11576 12791 8999 1692 -2220 885 C ATOM 3909 N ASN B 210 -0.196 -16.262 -29.698 1.00 96.95 N ANISOU 3909 N ASN B 210 12661 14413 9761 2244 -2713 -205 N ATOM 3910 CA ASN B 210 -0.030 -15.693 -31.025 1.00108.62 C ANISOU 3910 CA ASN B 210 14182 16253 10834 2237 -2798 -22 C ATOM 3911 C ASN B 210 -0.690 -14.317 -31.047 1.00116.33 C ANISOU 3911 C ASN B 210 15218 17047 11935 2130 -2922 334 C ATOM 3912 O ASN B 210 -1.880 -14.197 -30.745 1.00120.24 O ANISOU 3912 O ASN B 210 15709 17245 12733 2170 -3085 290 O ATOM 3913 CB ASN B 210 -0.654 -16.605 -32.086 1.00113.12 C ANISOU 3913 CB ASN B 210 14746 17026 11208 2393 -2989 -290 C ATOM 3914 CG ASN B 210 -0.184 -18.048 -31.974 1.00113.94 C ANISOU 3914 CG ASN B 210 14796 17214 11284 2529 -2938 -698 C ATOM 3915 OD1 ASN B 210 -0.792 -18.859 -31.276 1.00113.52 O ANISOU 3915 OD1 ASN B 210 14720 16849 11565 2579 -3005 -931 O ATOM 3916 ND2 ASN B 210 0.896 -18.374 -32.670 1.00115.57 N ANISOU 3916 ND2 ASN B 210 14971 17852 11088 2585 -2839 -787 N ATOM 3917 N ARG B 211 0.072 -13.274 -31.376 1.00117.52 N ANISOU 3917 N ARG B 211 15414 17365 11872 1991 -2865 683 N ATOM 3918 CA ARG B 211 -0.506 -11.931 -31.409 1.00114.87 C ANISOU 3918 CA ARG B 211 15151 16818 11677 1892 -3032 1031 C ATOM 3919 C ARG B 211 -1.644 -11.920 -32.446 1.00109.59 C ANISOU 3919 C ARG B 211 14520 16208 10912 1978 -3315 1021 C ATOM 3920 O ARG B 211 -1.463 -12.347 -33.585 1.00108.66 O ANISOU 3920 O ARG B 211 14412 16483 10392 2017 -3363 981 O ATOM 3921 CB ARG B 211 0.569 -10.834 -31.623 1.00 87.53 C ANISOU 3921 CB ARG B 211 11738 13521 7998 1695 -2953 1441 C ATOM 3922 CG ARG B 211 0.800 -10.369 -33.053 1.00 96.75 C ANISOU 3922 CG ARG B 211 12961 15105 8695 1608 -3075 1714 C ATOM 3923 CD ARG B 211 1.280 -8.915 -33.110 1.00 98.75 C ANISOU 3923 CD ARG B 211 13294 15305 8921 1378 -3141 2217 C ATOM 3924 NE ARG B 211 0.684 -8.180 -34.234 1.00106.87 N ANISOU 3924 NE ARG B 211 14426 16403 9776 1301 -3413 2494 N ATOM 3925 CZ ARG B 211 -0.346 -7.331 -34.133 1.00113.33 C ANISOU 3925 CZ ARG B 211 15331 16831 10899 1321 -3699 2649 C ATOM 3926 NH1 ARG B 211 -0.915 -7.081 -32.956 1.00113.51 N ANISOU 3926 NH1 ARG B 211 15331 16381 11417 1400 -3747 2550 N ATOM 3927 NH2 ARG B 211 -0.815 -6.719 -35.213 1.00112.90 N ANISOU 3927 NH2 ARG B 211 15381 16815 10702 1284 -3882 2821 N ATOM 3928 N ASN B 212 -2.829 -11.482 -32.034 1.00106.89 N ANISOU 3928 N ASN B 212 14182 15496 10934 2023 -3504 1023 N ATOM 3929 CA ASN B 212 -4.010 -11.629 -32.880 1.00117.41 C ANISOU 3929 CA ASN B 212 15529 16846 12236 2130 -3776 947 C ATOM 3930 C ASN B 212 -4.234 -13.091 -33.278 1.00116.69 C ANISOU 3930 C ASN B 212 15375 16942 12019 2266 -3756 554 C ATOM 3931 CB ASN B 212 -3.915 -10.739 -34.129 1.00121.28 C ANISOU 3931 CB ASN B 212 16111 17568 12404 2017 -3928 1299 C TER 3932 ASN B 212 ATOM 3933 N GLU C 1 23.168 0.786 26.505 1.00131.03 N ANISOU 3933 N GLU C 1 14980 20475 14330 -1009 288 -1638 N ATOM 3934 CA GLU C 1 22.654 1.141 25.184 1.00132.75 C ANISOU 3934 CA GLU C 1 15350 20172 14915 -867 300 -1681 C ATOM 3935 C GLU C 1 23.702 1.864 24.330 1.00130.58 C ANISOU 3935 C GLU C 1 15241 19358 15015 -753 216 -1724 C ATOM 3936 O GLU C 1 24.313 2.833 24.780 1.00137.93 O ANISOU 3936 O GLU C 1 16095 20305 16009 -700 147 -2028 O ATOM 3937 CB GLU C 1 21.409 2.017 25.326 1.00137.62 C ANISOU 3937 CB GLU C 1 15802 20944 15544 -765 338 -2127 C ATOM 3938 CG GLU C 1 20.823 2.477 24.005 1.00142.63 C ANISOU 3938 CG GLU C 1 16571 21058 16562 -621 331 -2184 C ATOM 3939 CD GLU C 1 19.590 3.339 24.182 1.00149.85 C ANISOU 3939 CD GLU C 1 17303 22118 17516 -514 350 -2635 C ATOM 3940 OE1 GLU C 1 19.750 4.530 24.530 1.00151.97 O ANISOU 3940 OE1 GLU C 1 17446 22374 17922 -407 275 -3077 O ATOM 3941 OE2 GLU C 1 18.466 2.825 23.970 1.00150.87 O ANISOU 3941 OE2 GLU C 1 17402 22362 17561 -535 429 -2557 O ATOM 3942 N VAL C 2 23.930 1.387 23.110 1.00117.66 N ANISOU 3942 N VAL C 2 13817 17267 13622 -726 215 -1421 N ATOM 3943 CA VAL C 2 24.814 2.098 22.185 1.00109.25 C ANISOU 3943 CA VAL C 2 12893 15712 12905 -631 143 -1446 C ATOM 3944 C VAL C 2 24.236 2.105 20.770 1.00 96.56 C ANISOU 3944 C VAL C 2 11432 13684 11572 -550 161 -1341 C ATOM 3945 O VAL C 2 23.972 1.055 20.188 1.00 91.40 O ANISOU 3945 O VAL C 2 10882 12957 10889 -596 214 -1028 O ATOM 3946 CB VAL C 2 26.270 1.531 22.189 1.00 87.37 C ANISOU 3946 CB VAL C 2 10224 12839 10133 -702 100 -1154 C ATOM 3947 CG1 VAL C 2 27.158 2.291 21.206 1.00 79.37 C ANISOU 3947 CG1 VAL C 2 9335 11356 9465 -617 32 -1173 C ATOM 3948 CG2 VAL C 2 26.870 1.597 23.590 1.00 86.00 C ANISOU 3948 CG2 VAL C 2 9899 13086 9690 -785 66 -1259 C ATOM 3949 N GLN C 3 24.039 3.295 20.219 1.00 89.46 N ANISOU 3949 N GLN C 3 10528 12510 10953 -435 101 -1605 N ATOM 3950 CA GLN C 3 23.515 3.415 18.868 1.00 83.48 C ANISOU 3950 CA GLN C 3 9895 11369 10455 -367 101 -1505 C ATOM 3951 C GLN C 3 24.496 4.174 17.994 1.00 75.40 C ANISOU 3951 C GLN C 3 8974 9932 9743 -323 7 -1464 C ATOM 3952 O GLN C 3 25.078 5.165 18.426 1.00 73.58 O ANISOU 3952 O GLN C 3 8667 9658 9633 -291 -86 -1694 O ATOM 3953 CB GLN C 3 22.158 4.132 18.863 1.00 89.75 C ANISOU 3953 CB GLN C 3 10574 12196 11331 -278 98 -1814 C ATOM 3954 CG GLN C 3 21.055 3.408 19.626 1.00 99.35 C ANISOU 3954 CG GLN C 3 11671 13839 12239 -328 200 -1852 C ATOM 3955 CD GLN C 3 20.593 4.169 20.872 1.00110.60 C ANISOU 3955 CD GLN C 3 12852 15648 13523 -298 187 -2293 C ATOM 3956 OE1 GLN C 3 21.358 4.926 21.488 1.00109.80 O ANISOU 3956 OE1 GLN C 3 12670 15593 13458 -276 112 -2523 O ATOM 3957 NE2 GLN C 3 19.330 3.972 21.243 1.00114.04 N ANISOU 3957 NE2 GLN C 3 13154 16378 13798 -296 260 -2432 N ATOM 3958 N LEU C 4 24.696 3.684 16.774 1.00 68.76 N ANISOU 3958 N LEU C 4 8291 8810 9023 -331 27 -1170 N ATOM 3959 CA LEU C 4 25.380 4.448 15.746 1.00 64.71 C ANISOU 3959 CA LEU C 4 7860 7921 8807 -300 -58 -1110 C ATOM 3960 C LEU C 4 24.321 4.882 14.757 1.00 70.15 C ANISOU 3960 C LEU C 4 8574 8391 9688 -237 -78 -1137 C ATOM 3961 O LEU C 4 23.805 4.046 14.017 1.00 76.65 O ANISOU 3961 O LEU C 4 9487 9185 10453 -251 -3 -930 O ATOM 3962 CB LEU C 4 26.429 3.589 15.027 1.00 60.89 C ANISOU 3962 CB LEU C 4 7512 7323 8301 -362 -21 -766 C ATOM 3963 CG LEU C 4 27.676 3.104 15.781 1.00 54.79 C ANISOU 3963 CG LEU C 4 6732 6696 7388 -427 -20 -676 C ATOM 3964 CD1 LEU C 4 28.712 2.553 14.809 1.00 58.21 C ANISOU 3964 CD1 LEU C 4 7281 6939 7898 -460 -8 -393 C ATOM 3965 CD2 LEU C 4 28.287 4.209 16.606 1.00 44.45 C ANISOU 3965 CD2 LEU C 4 5320 5419 6150 -414 -115 -928 C ATOM 3966 N GLN C 5 23.999 6.176 14.734 1.00 75.35 N ANISOU 3966 N GLN C 5 9145 8886 10598 -167 -195 -1393 N ATOM 3967 CA GLN C 5 22.922 6.684 13.882 1.00 77.91 C ANISOU 3967 CA GLN C 5 9467 9001 11132 -103 -241 -1437 C ATOM 3968 C GLN C 5 23.439 7.375 12.619 1.00 78.22 C ANISOU 3968 C GLN C 5 9586 8659 11475 -114 -353 -1253 C ATOM 3969 O GLN C 5 23.938 8.493 12.696 1.00 85.29 O ANISOU 3969 O GLN C 5 10415 9365 12627 -97 -499 -1381 O ATOM 3970 CB GLN C 5 22.050 7.660 14.678 1.00 84.51 C ANISOU 3970 CB GLN C 5 10121 9905 12083 -12 -320 -1858 C ATOM 3971 CG GLN C 5 20.602 7.195 14.867 1.00 93.30 C ANISOU 3971 CG GLN C 5 11174 11221 13055 28 -231 -1969 C ATOM 3972 CD GLN C 5 19.815 7.114 13.556 1.00 94.01 C ANISOU 3972 CD GLN C 5 11358 11056 13306 50 -241 -1781 C ATOM 3973 OE1 GLN C 5 19.754 8.085 12.799 1.00 94.87 O ANISOU 3973 OE1 GLN C 5 11463 10836 13749 94 -383 -1803 O ATOM 3974 NE2 GLN C 5 19.206 5.953 13.289 1.00 89.27 N ANISOU 3974 NE2 GLN C 5 10832 10607 12479 12 -107 -1587 N ATOM 3975 N GLN C 6 23.284 6.726 11.461 1.00 72.17 N ANISOU 3975 N GLN C 6 8944 7794 10683 -148 -296 -958 N ATOM 3976 CA GLN C 6 23.767 7.267 10.177 1.00 70.50 C ANISOU 3976 CA GLN C 6 8797 7288 10700 -186 -388 -735 C ATOM 3977 C GLN C 6 22.770 8.161 9.437 1.00 75.13 C ANISOU 3977 C GLN C 6 9341 7640 11563 -139 -512 -781 C ATOM 3978 O GLN C 6 21.564 7.931 9.481 1.00 78.96 O ANISOU 3978 O GLN C 6 9802 8191 12008 -81 -473 -888 O ATOM 3979 CB GLN C 6 24.227 6.150 9.240 1.00 66.78 C ANISOU 3979 CB GLN C 6 8458 6859 10055 -253 -274 -407 C ATOM 3980 CG GLN C 6 25.272 5.248 9.850 1.00 73.55 C ANISOU 3980 CG GLN C 6 9351 7903 10691 -298 -178 -333 C ATOM 3981 CD GLN C 6 25.813 4.236 8.878 1.00 68.78 C ANISOU 3981 CD GLN C 6 8848 7312 9973 -351 -90 -54 C ATOM 3982 OE1 GLN C 6 26.067 4.541 7.720 1.00 62.59 O ANISOU 3982 OE1 GLN C 6 8098 6385 9298 -385 -127 110 O ATOM 3983 NE2 GLN C 6 25.986 3.018 9.345 1.00 68.91 N ANISOU 3983 NE2 GLN C 6 8895 7513 9774 -362 16 -3 N ATOM 3984 N SER C 7 23.293 9.165 8.738 1.00 76.01 N ANISOU 3984 N SER C 7 9437 7478 11965 -174 -672 -675 N ATOM 3985 CA SER C 7 22.487 10.043 7.900 1.00 72.78 C ANISOU 3985 CA SER C 7 8987 6809 11858 -153 -825 -645 C ATOM 3986 C SER C 7 21.786 9.228 6.796 1.00 74.88 C ANISOU 3986 C SER C 7 9353 7120 11979 -178 -729 -402 C ATOM 3987 O SER C 7 22.221 8.117 6.455 1.00 78.66 O ANISOU 3987 O SER C 7 9936 7771 12180 -230 -573 -212 O ATOM 3988 CB SER C 7 23.372 11.141 7.294 1.00 68.20 C ANISOU 3988 CB SER C 7 8374 5946 11595 -228 -1021 -483 C ATOM 3989 OG SER C 7 23.368 11.108 5.871 1.00 69.24 O ANISOU 3989 OG SER C 7 8571 5969 11767 -316 -1054 -126 O ATOM 3990 N GLY C 8 20.690 9.766 6.263 1.00 65.83 N ANISOU 3990 N GLY C 8 8163 5817 11034 -135 -833 -430 N ATOM 3991 CA GLY C 8 19.852 9.030 5.333 1.00 61.27 C ANISOU 3991 CA GLY C 8 7661 5297 10322 -145 -749 -256 C ATOM 3992 C GLY C 8 20.294 8.999 3.880 1.00 62.41 C ANISOU 3992 C GLY C 8 7878 5356 10478 -254 -786 118 C ATOM 3993 O GLY C 8 21.247 9.674 3.499 1.00 64.43 O ANISOU 3993 O GLY C 8 8117 5485 10880 -337 -897 280 O ATOM 3994 N ALA C 9 19.539 8.261 3.066 1.00 63.63 N ANISOU 3994 N ALA C 9 8096 5597 10486 -260 -704 248 N ATOM 3995 CA ALA C 9 19.903 7.894 1.697 1.00 58.36 C ANISOU 3995 CA ALA C 9 7494 4966 9713 -364 -685 577 C ATOM 3996 C ALA C 9 20.280 9.109 0.916 1.00 64.19 C ANISOU 3996 C ALA C 9 8169 5539 10683 -445 -881 772 C ATOM 3997 O ALA C 9 19.820 10.199 1.209 1.00 71.56 O ANISOU 3997 O ALA C 9 9004 6327 11861 -394 -1040 651 O ATOM 3998 CB ALA C 9 18.742 7.236 1.016 1.00 58.35 C ANISOU 3998 CB ALA C 9 7531 5038 9602 -337 -624 618 C ATOM 3999 N GLU C 10 21.160 8.936 -0.057 1.00 69.33 N ANISOU 3999 N GLU C 10 8846 6311 11185 -560 -853 1045 N ATOM 4000 CA GLU C 10 21.577 10.066 -0.875 1.00 81.80 C ANISOU 4000 CA GLU C 10 10340 7855 12887 -645 -1018 1245 C ATOM 4001 C GLU C 10 21.417 9.750 -2.355 1.00 84.97 C ANISOU 4001 C GLU C 10 10754 8414 13117 -740 -1000 1520 C ATOM 4002 O GLU C 10 21.766 8.653 -2.815 1.00 87.88 O ANISOU 4002 O GLU C 10 11194 8971 13225 -783 -840 1608 O ATOM 4003 CB GLU C 10 23.019 10.460 -0.558 1.00 88.86 C ANISOU 4003 CB GLU C 10 11205 8757 13802 -713 -1040 1303 C ATOM 4004 CG GLU C 10 23.267 10.700 0.920 1.00 93.56 C ANISOU 4004 CG GLU C 10 11783 9222 14544 -628 -1054 1021 C ATOM 4005 CD GLU C 10 23.482 12.159 1.243 1.00103.02 C ANISOU 4005 CD GLU C 10 12854 10243 16048 -620 -1270 966 C ATOM 4006 OE1 GLU C 10 23.827 12.932 0.321 1.00103.82 O ANISOU 4006 OE1 GLU C 10 12885 10334 16228 -711 -1400 1206 O ATOM 4007 OE2 GLU C 10 23.310 12.527 2.424 1.00108.22 O ANISOU 4007 OE2 GLU C 10 13465 10782 16870 -524 -1317 674 O ATOM 4008 N LEU C 11 20.857 10.703 -3.091 1.00 77.80 N ANISOU 4008 N LEU C 11 9758 7436 12365 -773 -1175 1644 N ATOM 4009 CA LEU C 11 20.719 10.547 -4.524 1.00 80.33 C ANISOU 4009 CA LEU C 11 10065 7922 12535 -880 -1189 1916 C ATOM 4010 C LEU C 11 21.479 11.684 -5.177 1.00 81.06 C ANISOU 4010 C LEU C 11 10038 8014 12746 -1003 -1367 2151 C ATOM 4011 O LEU C 11 21.224 12.861 -4.913 1.00 84.34 O ANISOU 4011 O LEU C 11 10353 8232 13462 -983 -1569 2129 O ATOM 4012 CB LEU C 11 19.252 10.546 -4.948 1.00 84.44 C ANISOU 4012 CB LEU C 11 10580 8388 13117 -827 -1245 1892 C ATOM 4013 CG LEU C 11 18.926 9.672 -6.162 1.00 87.84 C ANISOU 4013 CG LEU C 11 11054 9042 13282 -900 -1154 2074 C ATOM 4014 CD1 LEU C 11 17.706 10.204 -6.869 1.00 90.85 C ANISOU 4014 CD1 LEU C 11 11374 9358 13788 -899 -1303 2154 C ATOM 4015 CD2 LEU C 11 20.083 9.621 -7.130 1.00 92.68 C ANISOU 4015 CD2 LEU C 11 11628 9887 13698 -1055 -1134 2334 C ATOM 4016 N VAL C 12 22.424 11.323 -6.031 1.00 74.89 N ANISOU 4016 N VAL C 12 9250 7468 11737 -1131 -1299 2372 N ATOM 4017 CA VAL C 12 23.391 12.285 -6.500 1.00 70.03 C ANISOU 4017 CA VAL C 12 8518 6884 11207 -1257 -1443 2590 C ATOM 4018 C VAL C 12 23.687 12.123 -7.992 1.00 73.80 C ANISOU 4018 C VAL C 12 8934 7653 11456 -1418 -1446 2897 C ATOM 4019 O VAL C 12 23.493 11.045 -8.557 1.00 72.74 O ANISOU 4019 O VAL C 12 8861 7738 11038 -1432 -1283 2911 O ATOM 4020 CB VAL C 12 24.659 12.165 -5.658 1.00 59.88 C ANISOU 4020 CB VAL C 12 7256 5595 9902 -1254 -1361 2502 C ATOM 4021 CG1 VAL C 12 25.824 12.748 -6.374 1.00 66.04 C ANISOU 4021 CG1 VAL C 12 7930 6514 10649 -1410 -1443 2764 C ATOM 4022 CG2 VAL C 12 24.459 12.849 -4.320 1.00 54.70 C ANISOU 4022 CG2 VAL C 12 6591 4647 9546 -1134 -1455 2253 C ATOM 4023 N LYS C 13 24.112 13.213 -8.630 1.00 76.11 N ANISOU 4023 N LYS C 13 9085 7954 11878 -1543 -1648 3142 N ATOM 4024 CA LYS C 13 24.587 13.167 -10.008 1.00 79.31 C ANISOU 4024 CA LYS C 13 9397 8680 12056 -1721 -1665 3448 C ATOM 4025 C LYS C 13 26.091 12.899 -10.023 1.00 83.25 C ANISOU 4025 C LYS C 13 9872 9383 12375 -1806 -1559 3516 C ATOM 4026 O LYS C 13 26.828 13.407 -9.185 1.00 82.71 O ANISOU 4026 O LYS C 13 9794 9150 12480 -1780 -1603 3447 O ATOM 4027 CB LYS C 13 24.263 14.467 -10.749 1.00 81.36 C ANISOU 4027 CB LYS C 13 9494 8873 12548 -1833 -1955 3711 C ATOM 4028 CG LYS C 13 22.868 14.505 -11.354 1.00 89.28 C ANISOU 4028 CG LYS C 13 10486 9842 13595 -1818 -2041 3753 C ATOM 4029 CD LYS C 13 22.463 15.928 -11.740 1.00 99.23 C ANISOU 4029 CD LYS C 13 11577 10926 15199 -1898 -2367 3959 C ATOM 4030 CE LYS C 13 20.945 16.077 -11.862 1.00 95.62 C ANISOU 4030 CE LYS C 13 11122 10304 14904 -1822 -2466 3895 C ATOM 4031 NZ LYS C 13 20.239 15.465 -10.682 1.00 85.89 N ANISOU 4031 NZ LYS C 13 10043 8863 13730 -1605 -2315 3512 N ATOM 4032 N PRO C 14 26.553 12.077 -10.970 1.00 84.35 N ANISOU 4032 N PRO C 14 9990 9898 12161 -1906 -1417 3634 N ATOM 4033 CA PRO C 14 27.979 11.772 -11.005 1.00 74.03 C ANISOU 4033 CA PRO C 14 8643 8810 10674 -1984 -1308 3680 C ATOM 4034 C PRO C 14 28.836 13.024 -11.173 1.00 72.65 C ANISOU 4034 C PRO C 14 8324 8602 10679 -2109 -1513 3905 C ATOM 4035 O PRO C 14 28.536 13.919 -11.960 1.00 68.45 O ANISOU 4035 O PRO C 14 7664 8093 10249 -2221 -1723 4152 O ATOM 4036 CB PRO C 14 28.105 10.857 -12.228 1.00 78.02 C ANISOU 4036 CB PRO C 14 9098 9762 10784 -2084 -1169 3784 C ATOM 4037 CG PRO C 14 26.899 11.133 -13.056 1.00 82.62 C ANISOU 4037 CG PRO C 14 9646 10364 11383 -2119 -1291 3908 C ATOM 4038 CD PRO C 14 25.823 11.420 -12.067 1.00 87.30 C ANISOU 4038 CD PRO C 14 10354 10533 12284 -1957 -1358 3722 C ATOM 4039 N GLY C 15 29.927 13.070 -10.425 1.00 79.03 N ANISOU 4039 N GLY C 15 9141 9357 11529 -2095 -1462 3831 N ATOM 4040 CA GLY C 15 30.836 14.193 -10.481 1.00 79.93 C ANISOU 4040 CA GLY C 15 9121 9430 11818 -2208 -1649 4032 C ATOM 4041 C GLY C 15 30.734 15.054 -9.250 1.00 76.43 C ANISOU 4041 C GLY C 15 8709 8565 11768 -2100 -1791 3885 C ATOM 4042 O GLY C 15 31.420 16.054 -9.135 1.00 85.74 O ANISOU 4042 O GLY C 15 9779 9646 13153 -2173 -1970 4023 O ATOM 4043 N SER C 16 29.887 14.666 -8.314 1.00 70.83 N ANISOU 4043 N SER C 16 8134 7618 11161 -1928 -1718 3597 N ATOM 4044 CA SER C 16 29.693 15.494 -7.141 1.00 77.84 C ANISOU 4044 CA SER C 16 9029 8134 12415 -1819 -1858 3421 C ATOM 4045 C SER C 16 30.186 14.809 -5.891 1.00 76.95 C ANISOU 4045 C SER C 16 9035 7938 12264 -1702 -1680 3134 C ATOM 4046 O SER C 16 30.711 13.702 -5.946 1.00 73.43 O ANISOU 4046 O SER C 16 8662 7708 11529 -1708 -1458 3088 O ATOM 4047 CB SER C 16 28.235 15.922 -6.990 1.00 81.96 C ANISOU 4047 CB SER C 16 9559 8420 13162 -1720 -1986 3319 C ATOM 4048 OG SER C 16 27.392 14.801 -6.906 1.00 81.64 O ANISOU 4048 OG SER C 16 9654 8446 12920 -1621 -1788 3143 O ATOM 4049 N SER C 17 29.994 15.478 -4.762 1.00 80.59 N ANISOU 4049 N SER C 17 9498 8094 13030 -1596 -1792 2934 N ATOM 4050 CA SER C 17 30.602 15.082 -3.502 1.00 78.27 C ANISOU 4050 CA SER C 17 9280 7712 12748 -1507 -1678 2684 C ATOM 4051 C SER C 17 29.476 14.759 -2.564 1.00 73.28 C ANISOU 4051 C SER C 17 8740 6898 12205 -1340 -1632 2374 C ATOM 4052 O SER C 17 28.325 15.066 -2.842 1.00 81.38 O ANISOU 4052 O SER C 17 9750 7831 13341 -1294 -1722 2357 O ATOM 4053 CB SER C 17 31.447 16.224 -2.925 1.00 82.84 C ANISOU 4053 CB SER C 17 9753 8111 13613 -1535 -1867 2700 C ATOM 4054 OG SER C 17 31.861 17.122 -3.951 1.00 88.04 O ANISOU 4054 OG SER C 17 10267 8830 14355 -1683 -2054 3027 O ATOM 4055 N VAL C 18 29.787 14.067 -1.486 1.00 65.69 N ANISOU 4055 N VAL C 18 7868 5913 11178 -1257 -1487 2137 N ATOM 4056 CA VAL C 18 28.777 13.757 -0.491 1.00 64.87 C ANISOU 4056 CA VAL C 18 7835 5662 11152 -1105 -1446 1831 C ATOM 4057 C VAL C 18 29.428 13.595 0.857 1.00 68.82 C ANISOU 4057 C VAL C 18 8363 6082 11705 -1043 -1397 1593 C ATOM 4058 O VAL C 18 30.531 13.069 0.953 1.00 74.99 O ANISOU 4058 O VAL C 18 9171 6989 12333 -1104 -1290 1656 O ATOM 4059 CB VAL C 18 28.051 12.458 -0.820 1.00 62.62 C ANISOU 4059 CB VAL C 18 7667 5531 10595 -1067 -1246 1801 C ATOM 4060 CG1 VAL C 18 28.030 11.548 0.392 1.00 59.88 C ANISOU 4060 CG1 VAL C 18 7415 5164 10172 -968 -1095 1535 C ATOM 4061 CG2 VAL C 18 26.651 12.741 -1.334 1.00 62.17 C ANISOU 4061 CG2 VAL C 18 7596 5402 10623 -1021 -1329 1803 C ATOM 4062 N LYS C 19 28.741 14.038 1.898 1.00 67.89 N ANISOU 4062 N LYS C 19 8223 5773 11801 -922 -1479 1308 N ATOM 4063 CA LYS C 19 29.202 13.811 3.256 1.00 67.78 C ANISOU 4063 CA LYS C 19 8228 5704 11820 -856 -1431 1038 C ATOM 4064 C LYS C 19 28.148 12.958 3.931 1.00 66.72 C ANISOU 4064 C LYS C 19 8173 5582 11595 -743 -1309 787 C ATOM 4065 O LYS C 19 27.011 13.391 4.104 1.00 70.22 O ANISOU 4065 O LYS C 19 8574 5920 12185 -652 -1391 627 O ATOM 4066 CB LYS C 19 29.359 15.130 4.012 1.00 64.79 C ANISOU 4066 CB LYS C 19 7719 5116 11782 -809 -1649 866 C ATOM 4067 CG LYS C 19 30.659 15.302 4.793 1.00 67.09 C ANISOU 4067 CG LYS C 19 7983 5393 12115 -844 -1662 802 C ATOM 4068 CD LYS C 19 30.675 16.718 5.405 1.00 77.50 C ANISOU 4068 CD LYS C 19 9149 6495 13805 -786 -1907 631 C ATOM 4069 CE LYS C 19 32.075 17.227 5.755 1.00 81.80 C ANISOU 4069 CE LYS C 19 9632 7004 14443 -856 -1984 683 C ATOM 4070 NZ LYS C 19 32.474 17.067 7.197 1.00 77.47 N ANISOU 4070 NZ LYS C 19 9078 6436 13921 -783 -1955 333 N ATOM 4071 N ILE C 20 28.525 11.738 4.293 1.00 59.23 N ANISOU 4071 N ILE C 20 7323 4768 10413 -751 -1121 760 N ATOM 4072 CA ILE C 20 27.674 10.863 5.084 1.00 56.83 C ANISOU 4072 CA ILE C 20 7079 4517 9995 -647 -998 515 C ATOM 4073 C ILE C 20 28.065 10.965 6.559 1.00 64.55 C ANISOU 4073 C ILE C 20 8015 5539 10973 -573 -991 201 C ATOM 4074 O ILE C 20 29.240 10.950 6.889 1.00 71.67 O ANISOU 4074 O ILE C 20 8908 6488 11834 -626 -980 240 O ATOM 4075 CB ILE C 20 27.769 9.422 4.565 1.00 50.70 C ANISOU 4075 CB ILE C 20 6409 4012 8841 -662 -771 655 C ATOM 4076 CG1 ILE C 20 27.350 9.388 3.090 1.00 44.61 C ANISOU 4076 CG1 ILE C 20 5659 3230 8061 -738 -788 937 C ATOM 4077 CG2 ILE C 20 26.924 8.504 5.404 1.00 52.46 C ANISOU 4077 CG2 ILE C 20 6677 4394 8863 -545 -630 418 C ATOM 4078 CD1 ILE C 20 27.179 8.032 2.514 1.00 43.13 C ANISOU 4078 CD1 ILE C 20 5555 3284 7550 -730 -591 1017 C ATOM 4079 N SER C 21 27.086 11.099 7.446 1.00 68.24 N ANISOU 4079 N SER C 21 8437 6013 11479 -455 -1002 -118 N ATOM 4080 CA SER C 21 27.383 11.337 8.860 1.00 69.99 C ANISOU 4080 CA SER C 21 8585 6306 11703 -390 -1018 -446 C ATOM 4081 C SER C 21 27.064 10.112 9.705 1.00 65.26 C ANISOU 4081 C SER C 21 8034 6035 10727 -334 -809 -582 C ATOM 4082 O SER C 21 26.191 9.328 9.357 1.00 61.80 O ANISOU 4082 O SER C 21 7655 5706 10119 -307 -694 -528 O ATOM 4083 CB SER C 21 26.594 12.534 9.398 1.00 70.59 C ANISOU 4083 CB SER C 21 8521 6177 12122 -300 -1211 -765 C ATOM 4084 OG SER C 21 25.343 12.109 9.926 1.00 69.52 O ANISOU 4084 OG SER C 21 8364 6200 11852 -193 -1121 -1012 O ATOM 4085 N CYS C 22 27.802 9.935 10.797 1.00 62.67 N ANISOU 4085 N CYS C 22 7673 5867 10272 -330 -772 -735 N ATOM 4086 CA CYS C 22 27.481 8.910 11.778 1.00 60.42 C ANISOU 4086 CA CYS C 22 7398 5904 9655 -291 -614 -870 C ATOM 4087 C CYS C 22 27.549 9.507 13.172 1.00 66.15 C ANISOU 4087 C CYS C 22 7990 6743 10401 -240 -679 -1235 C ATOM 4088 O CYS C 22 28.608 9.910 13.636 1.00 63.35 O ANISOU 4088 O CYS C 22 7598 6369 10104 -274 -745 -1276 O ATOM 4089 CB CYS C 22 28.442 7.728 11.659 1.00 60.20 C ANISOU 4089 CB CYS C 22 7470 6041 9363 -362 -475 -621 C ATOM 4090 SG CYS C 22 27.972 6.273 12.633 1.00 88.60 S ANISOU 4090 SG CYS C 22 11088 10005 12570 -345 -299 -668 S ATOM 4091 N LYS C 23 26.405 9.563 13.837 1.00 80.02 N ANISOU 4091 N LYS C 23 9660 8642 12102 -160 -660 -1514 N ATOM 4092 CA LYS C 23 26.325 10.115 15.183 1.00 80.86 C ANISOU 4092 CA LYS C 23 9607 8922 12193 -105 -713 -1915 C ATOM 4093 C LYS C 23 26.334 8.945 16.149 1.00 79.68 C ANISOU 4093 C LYS C 23 9463 9201 11612 -137 -542 -1918 C ATOM 4094 O LYS C 23 25.641 7.954 15.930 1.00 79.69 O ANISOU 4094 O LYS C 23 9531 9352 11396 -151 -409 -1766 O ATOM 4095 CB LYS C 23 25.053 10.961 15.349 1.00 71.94 C ANISOU 4095 CB LYS C 23 8339 7720 11277 4 -807 -2258 C ATOM 4096 CG LYS C 23 25.005 11.739 16.646 1.00 77.81 C ANISOU 4096 CG LYS C 23 8880 8617 12068 75 -895 -2737 C ATOM 4097 CD LYS C 23 24.034 12.915 16.566 1.00 86.57 C ANISOU 4097 CD LYS C 23 9832 9502 13560 193 -1065 -3085 C ATOM 4098 CE LYS C 23 24.509 14.068 17.457 1.00 93.17 C ANISOU 4098 CE LYS C 23 10474 10280 14644 254 -1248 -3511 C ATOM 4099 NZ LYS C 23 23.885 15.393 17.152 1.00 92.03 N ANISOU 4099 NZ LYS C 23 10178 9798 14990 365 -1471 -3741 N ATOM 4100 N THR C 24 27.141 9.027 17.196 1.00 76.29 N ANISOU 4100 N THR C 24 8959 8966 11062 -162 -558 -2062 N ATOM 4101 CA THR C 24 27.148 7.944 18.169 1.00 74.06 C ANISOU 4101 CA THR C 24 8661 9111 10369 -212 -420 -2037 C ATOM 4102 C THR C 24 26.699 8.429 19.540 1.00 74.98 C ANISOU 4102 C THR C 24 8572 9558 10357 -170 -445 -2470 C ATOM 4103 O THR C 24 27.248 9.377 20.098 1.00 65.67 O ANISOU 4103 O THR C 24 7281 8344 9328 -140 -567 -2746 O ATOM 4104 CB THR C 24 28.512 7.166 18.238 1.00 70.11 C ANISOU 4104 CB THR C 24 8258 8663 9716 -308 -378 -1739 C ATOM 4105 OG1 THR C 24 29.253 7.535 19.411 1.00 70.39 O ANISOU 4105 OG1 THR C 24 8179 8907 9661 -327 -434 -1952 O ATOM 4106 CG2 THR C 24 29.355 7.409 16.995 1.00 67.69 C ANISOU 4106 CG2 THR C 24 8077 7977 9666 -332 -432 -1474 C ATOM 4107 N SER C 25 25.673 7.766 20.061 1.00 84.37 N ANISOU 4107 N SER C 25 9700 11089 11269 -173 -332 -2534 N ATOM 4108 CA SER C 25 25.147 8.053 21.381 1.00 92.17 C ANISOU 4108 CA SER C 25 10470 12500 12050 -151 -324 -2934 C ATOM 4109 C SER C 25 25.246 6.813 22.261 1.00 88.69 C ANISOU 4109 C SER C 25 10015 12541 11143 -269 -193 -2747 C ATOM 4110 O SER C 25 25.078 5.684 21.786 1.00 83.86 O ANISOU 4110 O SER C 25 9534 11937 10390 -338 -94 -2368 O ATOM 4111 CB SER C 25 23.679 8.486 21.276 1.00 98.21 C ANISOU 4111 CB SER C 25 11120 13291 12903 -54 -319 -3214 C ATOM 4112 OG SER C 25 22.857 7.418 20.825 1.00 95.48 O ANISOU 4112 OG SER C 25 10867 13042 12370 -98 -183 -2931 O ATOM 4113 N GLY C 26 25.494 7.031 23.547 1.00 89.52 N ANISOU 4113 N GLY C 26 9942 13053 11018 -298 -207 -3017 N ATOM 4114 CA GLY C 26 25.389 5.966 24.526 1.00 94.57 C ANISOU 4114 CA GLY C 26 10511 14225 11194 -423 -102 -2875 C ATOM 4115 C GLY C 26 26.714 5.446 25.022 1.00106.64 C ANISOU 4115 C GLY C 26 12090 15863 12564 -530 -124 -2637 C ATOM 4116 O GLY C 26 26.753 4.444 25.739 1.00107.54 O ANISOU 4116 O GLY C 26 12166 16375 12318 -656 -58 -2418 O ATOM 4117 N ASP C 27 27.795 6.123 24.634 1.00115.42 N ANISOU 4117 N ASP C 27 13277 16621 13957 -488 -228 -2660 N ATOM 4118 CA ASP C 27 29.129 5.845 25.170 1.00121.87 C ANISOU 4118 CA ASP C 27 14112 17532 14660 -573 -271 -2509 C ATOM 4119 C ASP C 27 30.044 7.051 24.957 1.00118.96 C ANISOU 4119 C ASP C 27 13738 16828 14632 -500 -409 -2733 C ATOM 4120 O ASP C 27 29.578 8.122 24.556 1.00119.99 O ANISOU 4120 O ASP C 27 13819 16702 15068 -389 -485 -3033 O ATOM 4121 CB ASP C 27 29.739 4.596 24.520 1.00124.44 C ANISOU 4121 CB ASP C 27 14634 17702 14946 -660 -218 -1972 C ATOM 4122 CG ASP C 27 30.679 3.844 25.457 1.00125.85 C ANISOU 4122 CG ASP C 27 14776 18201 14842 -785 -230 -1776 C ATOM 4123 OD1 ASP C 27 30.214 3.412 26.535 1.00127.37 O ANISOU 4123 OD1 ASP C 27 14822 18897 14677 -869 -194 -1820 O ATOM 4124 OD2 ASP C 27 31.877 3.690 25.117 1.00122.59 O ANISOU 4124 OD2 ASP C 27 14465 17554 14560 -806 -281 -1570 O ATOM 4125 N SER C 28 31.335 6.885 25.245 1.00113.50 N ANISOU 4125 N SER C 28 13083 16134 13906 -566 -459 -2584 N ATOM 4126 CA SER C 28 32.317 7.894 24.864 1.00105.00 C ANISOU 4126 CA SER C 28 12030 14685 13181 -517 -591 -2697 C ATOM 4127 C SER C 28 32.802 7.686 23.441 1.00 99.91 C ANISOU 4127 C SER C 28 11592 13552 12817 -515 -587 -2327 C ATOM 4128 O SER C 28 33.306 6.622 23.076 1.00 89.92 O ANISOU 4128 O SER C 28 10455 12277 11434 -586 -515 -1936 O ATOM 4129 CB SER C 28 33.524 7.930 25.780 1.00 96.86 C ANISOU 4129 CB SER C 28 10929 13859 12016 -585 -657 -2732 C ATOM 4130 OG SER C 28 34.555 8.638 25.110 1.00 89.49 O ANISOU 4130 OG SER C 28 10068 12492 11442 -561 -766 -2689 O ATOM 4131 N PHE C 29 32.659 8.743 22.659 1.00100.69 N ANISOU 4131 N PHE C 29 11700 13257 13299 -435 -681 -2468 N ATOM 4132 CA PHE C 29 32.888 8.705 21.234 1.00 91.08 C ANISOU 4132 CA PHE C 29 10649 11612 12347 -434 -681 -2156 C ATOM 4133 C PHE C 29 34.387 8.728 20.930 1.00 86.03 C ANISOU 4133 C PHE C 29 10076 10792 11820 -497 -736 -1937 C ATOM 4134 O PHE C 29 34.849 8.101 19.969 1.00 79.73 O ANISOU 4134 O PHE C 29 9417 9820 11057 -538 -679 -1579 O ATOM 4135 CB PHE C 29 32.145 9.888 20.605 1.00 88.05 C ANISOU 4135 CB PHE C 29 10219 10905 12333 -343 -789 -2381 C ATOM 4136 CG PHE C 29 32.560 10.199 19.209 1.00 83.50 C ANISOU 4136 CG PHE C 29 9766 9887 12072 -359 -841 -2098 C ATOM 4137 CD1 PHE C 29 33.516 11.178 18.962 1.00 83.27 C ANISOU 4137 CD1 PHE C 29 9706 9573 12360 -377 -998 -2122 C ATOM 4138 CD2 PHE C 29 31.988 9.529 18.142 1.00 74.73 C ANISOU 4138 CD2 PHE C 29 8789 8666 10939 -367 -742 -1807 C ATOM 4139 CE1 PHE C 29 33.903 11.469 17.680 1.00 79.15 C ANISOU 4139 CE1 PHE C 29 9277 8695 12102 -416 -1049 -1833 C ATOM 4140 CE2 PHE C 29 32.373 9.818 16.855 1.00 75.38 C ANISOU 4140 CE2 PHE C 29 8965 8403 11274 -396 -789 -1546 C ATOM 4141 CZ PHE C 29 33.333 10.790 16.622 1.00 77.44 C ANISOU 4141 CZ PHE C 29 9186 8411 11826 -428 -941 -1546 C ATOM 4142 N THR C 30 35.145 9.416 21.779 1.00 84.61 N ANISOU 4142 N THR C 30 9781 10685 11681 -504 -845 -2170 N ATOM 4143 CA THR C 30 36.573 9.616 21.543 1.00 81.62 C ANISOU 4143 CA THR C 30 9440 10127 11446 -561 -918 -2006 C ATOM 4144 C THR C 30 37.449 8.456 22.020 1.00 79.91 C ANISOU 4144 C THR C 30 9270 10165 10926 -643 -836 -1752 C ATOM 4145 O THR C 30 38.675 8.529 21.934 1.00 77.12 O ANISOU 4145 O THR C 30 8933 9710 10659 -691 -889 -1625 O ATOM 4146 CB THR C 30 37.071 10.898 22.222 1.00 78.66 C ANISOU 4146 CB THR C 30 8912 9685 11289 -536 -1094 -2369 C ATOM 4147 OG1 THR C 30 36.405 11.052 23.479 1.00 81.30 O ANISOU 4147 OG1 THR C 30 9089 10390 11409 -494 -1098 -2761 O ATOM 4148 CG2 THR C 30 36.786 12.113 21.359 1.00 75.17 C ANISOU 4148 CG2 THR C 30 8450 8805 11307 -485 -1235 -2471 C ATOM 4149 N ALA C 31 36.831 7.400 22.538 1.00 76.48 N ANISOU 4149 N ALA C 31 8844 10058 10158 -664 -722 -1671 N ATOM 4150 CA ALA C 31 37.594 6.280 23.061 1.00 71.24 C ANISOU 4150 CA ALA C 31 8205 9632 9232 -746 -674 -1420 C ATOM 4151 C ALA C 31 37.891 5.218 22.022 1.00 73.91 C ANISOU 4151 C ALA C 31 8693 9792 9596 -772 -590 -1012 C ATOM 4152 O ALA C 31 38.722 4.335 22.262 1.00 73.26 O ANISOU 4152 O ALA C 31 8633 9809 9392 -831 -579 -782 O ATOM 4153 CB ALA C 31 36.878 5.658 24.240 1.00 70.57 C ANISOU 4153 CB ALA C 31 8022 10017 8774 -783 -624 -1507 C ATOM 4154 N TYR C 32 37.232 5.308 20.867 1.00 74.80 N ANISOU 4154 N TYR C 32 8896 9646 9879 -725 -543 -936 N ATOM 4155 CA TYR C 32 37.260 4.216 19.894 1.00 71.30 C ANISOU 4155 CA TYR C 32 8576 9088 9427 -738 -451 -601 C ATOM 4156 C TYR C 32 37.473 4.692 18.483 1.00 71.15 C ANISOU 4156 C TYR C 32 8637 8716 9682 -713 -454 -498 C ATOM 4157 O TYR C 32 36.917 5.703 18.094 1.00 78.04 O ANISOU 4157 O TYR C 32 9493 9422 10736 -674 -501 -655 O ATOM 4158 CB TYR C 32 35.953 3.427 19.958 1.00 69.31 C ANISOU 4158 CB TYR C 32 8346 8993 8994 -726 -359 -561 C ATOM 4159 CG TYR C 32 35.853 2.620 21.207 1.00 80.79 C ANISOU 4159 CG TYR C 32 9726 10826 10144 -788 -348 -532 C ATOM 4160 CD1 TYR C 32 36.826 1.667 21.507 1.00 94.30 C ANISOU 4160 CD1 TYR C 32 11447 12618 11763 -853 -363 -285 C ATOM 4161 CD2 TYR C 32 34.817 2.816 22.106 1.00 82.13 C ANISOU 4161 CD2 TYR C 32 9794 11293 10118 -789 -332 -745 C ATOM 4162 CE1 TYR C 32 36.761 0.915 22.669 1.00 98.46 C ANISOU 4162 CE1 TYR C 32 11894 13503 12014 -932 -376 -210 C ATOM 4163 CE2 TYR C 32 34.738 2.071 23.275 1.00 89.69 C ANISOU 4163 CE2 TYR C 32 10663 12654 10762 -874 -327 -685 C ATOM 4164 CZ TYR C 32 35.715 1.120 23.549 1.00 98.97 C ANISOU 4164 CZ TYR C 32 11858 13891 11855 -952 -356 -396 C ATOM 4165 OH TYR C 32 35.665 0.368 24.702 1.00104.65 O ANISOU 4165 OH TYR C 32 12478 15011 12271 -1057 -374 -285 O ATOM 4166 N ASN C 33 38.257 3.944 17.711 1.00 68.81 N ANISOU 4166 N ASN C 33 8409 8321 9415 -740 -411 -233 N ATOM 4167 CA ASN C 33 38.367 4.175 16.270 1.00 67.34 C ANISOU 4167 CA ASN C 33 8288 7874 9423 -732 -388 -95 C ATOM 4168 C ASN C 33 37.058 3.964 15.496 1.00 59.51 C ANISOU 4168 C ASN C 33 7361 6818 8433 -690 -319 -70 C ATOM 4169 O ASN C 33 36.391 2.942 15.634 1.00 52.57 O ANISOU 4169 O ASN C 33 6516 6068 7390 -675 -242 -3 O ATOM 4170 CB ASN C 33 39.438 3.270 15.684 1.00 67.96 C ANISOU 4170 CB ASN C 33 8398 7932 9493 -763 -344 144 C ATOM 4171 CG ASN C 33 40.815 3.782 15.937 1.00 74.99 C ANISOU 4171 CG ASN C 33 9228 8789 10475 -807 -419 147 C ATOM 4172 OD1 ASN C 33 41.006 4.769 16.652 1.00 73.75 O ANISOU 4172 OD1 ASN C 33 9008 8631 10382 -819 -513 -31 O ATOM 4173 ND2 ASN C 33 41.798 3.120 15.344 1.00 81.22 N ANISOU 4173 ND2 ASN C 33 10022 9554 11285 -829 -385 329 N ATOM 4174 N MET C 34 36.685 4.928 14.671 1.00 63.88 N ANISOU 4174 N MET C 34 7921 7164 9184 -677 -361 -108 N ATOM 4175 CA MET C 34 35.514 4.743 13.824 1.00 67.92 C ANISOU 4175 CA MET C 34 8492 7604 9710 -642 -304 -63 C ATOM 4176 C MET C 34 35.969 4.288 12.459 1.00 69.19 C ANISOU 4176 C MET C 34 8713 7658 9919 -670 -249 180 C ATOM 4177 O MET C 34 36.891 4.875 11.889 1.00 71.46 O ANISOU 4177 O MET C 34 8975 7832 10342 -720 -299 267 O ATOM 4178 CB MET C 34 34.699 6.027 13.725 1.00 63.81 C ANISOU 4178 CB MET C 34 7931 6929 9384 -610 -398 -246 C ATOM 4179 CG MET C 34 33.877 6.297 14.963 1.00 61.96 C ANISOU 4179 CG MET C 34 7624 6854 9065 -559 -422 -534 C ATOM 4180 SD MET C 34 32.704 4.954 15.225 1.00110.94 S ANISOU 4180 SD MET C 34 13872 13297 14983 -533 -280 -488 S ATOM 4181 CE MET C 34 31.936 4.858 13.611 1.00107.66 C ANISOU 4181 CE MET C 34 13551 12658 14697 -513 -239 -314 C ATOM 4182 N ASN C 35 35.344 3.226 11.953 1.00 62.69 N ANISOU 4182 N ASN C 35 7950 6894 8977 -645 -150 283 N ATOM 4183 CA ASN C 35 35.700 2.690 10.645 1.00 63.23 C ANISOU 4183 CA ASN C 35 8055 6908 9063 -664 -90 472 C ATOM 4184 C ASN C 35 34.510 2.829 9.735 1.00 63.39 C ANISOU 4184 C ASN C 35 8119 6852 9115 -640 -64 492 C ATOM 4185 O ASN C 35 33.384 2.939 10.199 1.00 68.09 O ANISOU 4185 O ASN C 35 8727 7460 9685 -598 -67 374 O ATOM 4186 CB ASN C 35 36.090 1.211 10.712 1.00 64.14 C ANISOU 4186 CB ASN C 35 8185 7144 9043 -649 -12 567 C ATOM 4187 CG ASN C 35 37.233 0.940 11.659 1.00 61.52 C ANISOU 4187 CG ASN C 35 7804 6896 8675 -671 -47 566 C ATOM 4188 OD1 ASN C 35 38.274 0.424 11.260 1.00 69.91 O ANISOU 4188 OD1 ASN C 35 8840 7966 9755 -686 -31 664 O ATOM 4189 ND2 ASN C 35 37.042 1.272 12.925 1.00 54.47 N ANISOU 4189 ND2 ASN C 35 6884 6089 7724 -674 -98 444 N ATOM 4190 N TRP C 36 34.767 2.835 8.436 1.00 59.96 N ANISOU 4190 N TRP C 36 7694 6363 8726 -673 -40 638 N ATOM 4191 CA TRP C 36 33.706 2.836 7.444 1.00 56.94 C ANISOU 4191 CA TRP C 36 7350 5933 8353 -660 -13 686 C ATOM 4192 C TRP C 36 33.887 1.658 6.497 1.00 53.40 C ANISOU 4192 C TRP C 36 6919 5579 7792 -654 88 797 C ATOM 4193 O TRP C 36 34.983 1.388 6.036 1.00 55.52 O ANISOU 4193 O TRP C 36 7145 5905 8045 -690 113 878 O ATOM 4194 CB TRP C 36 33.711 4.132 6.638 1.00 55.88 C ANISOU 4194 CB TRP C 36 7185 5657 8391 -721 -107 762 C ATOM 4195 CG TRP C 36 33.165 5.337 7.340 1.00 60.18 C ANISOU 4195 CG TRP C 36 7700 6057 9109 -705 -231 621 C ATOM 4196 CD1 TRP C 36 33.875 6.277 8.027 1.00 61.00 C ANISOU 4196 CD1 TRP C 36 7743 6075 9358 -733 -341 545 C ATOM 4197 CD2 TRP C 36 31.793 5.763 7.377 1.00 68.44 C ANISOU 4197 CD2 TRP C 36 8758 7017 10229 -653 -273 514 C ATOM 4198 NE1 TRP C 36 33.030 7.257 8.505 1.00 67.42 N ANISOU 4198 NE1 TRP C 36 8522 6752 10345 -694 -454 374 N ATOM 4199 CE2 TRP C 36 31.747 6.964 8.120 1.00 70.14 C ANISOU 4199 CE2 TRP C 36 8907 7095 10647 -642 -413 352 C ATOM 4200 CE3 TRP C 36 30.595 5.239 6.863 1.00 68.00 C ANISOU 4200 CE3 TRP C 36 8751 6986 10099 -609 -212 523 C ATOM 4201 CZ2 TRP C 36 30.549 7.649 8.364 1.00 68.21 C ANISOU 4201 CZ2 TRP C 36 8633 6741 10541 -581 -493 184 C ATOM 4202 CZ3 TRP C 36 29.410 5.920 7.106 1.00 67.22 C ANISOU 4202 CZ3 TRP C 36 8633 6784 10122 -557 -284 382 C ATOM 4203 CH2 TRP C 36 29.397 7.112 7.850 1.00 66.59 C ANISOU 4203 CH2 TRP C 36 8478 6572 10252 -540 -423 208 C ATOM 4204 N VAL C 37 32.798 0.961 6.214 1.00 46.93 N ANISOU 4204 N VAL C 37 6146 4782 6903 -606 142 778 N ATOM 4205 CA VAL C 37 32.812 -0.132 5.273 1.00 43.51 C ANISOU 4205 CA VAL C 37 5717 4426 6389 -590 222 841 C ATOM 4206 C VAL C 37 31.806 0.175 4.196 1.00 50.34 C ANISOU 4206 C VAL C 37 6606 5261 7260 -596 229 883 C ATOM 4207 O VAL C 37 30.797 0.824 4.465 1.00 50.20 O ANISOU 4207 O VAL C 37 6618 5158 7296 -581 184 837 O ATOM 4208 CB VAL C 37 32.339 -1.402 5.933 1.00 50.49 C ANISOU 4208 CB VAL C 37 6627 5357 7199 -529 264 787 C ATOM 4209 CG1 VAL C 37 32.250 -2.524 4.892 1.00 55.13 C ANISOU 4209 CG1 VAL C 37 7206 5995 7747 -500 326 817 C ATOM 4210 CG2 VAL C 37 33.243 -1.763 7.130 1.00 46.90 C ANISOU 4210 CG2 VAL C 37 6144 4945 6732 -531 239 768 C ATOM 4211 N LYS C 38 32.078 -0.299 2.982 1.00 54.21 N ANISOU 4211 N LYS C 38 7068 5839 7692 -616 280 955 N ATOM 4212 CA LYS C 38 31.152 -0.166 1.857 1.00 48.71 C ANISOU 4212 CA LYS C 38 6383 5156 6967 -628 290 1007 C ATOM 4213 C LYS C 38 30.653 -1.516 1.381 1.00 57.74 C ANISOU 4213 C LYS C 38 7537 6382 8020 -566 367 948 C ATOM 4214 O LYS C 38 31.441 -2.423 1.142 1.00 68.34 O ANISOU 4214 O LYS C 38 8830 7820 9317 -546 416 915 O ATOM 4215 CB LYS C 38 31.834 0.524 0.696 1.00 42.80 C ANISOU 4215 CB LYS C 38 5566 4490 6208 -726 273 1149 C ATOM 4216 CG LYS C 38 31.389 0.019 -0.647 1.00 41.03 C ANISOU 4216 CG LYS C 38 5314 4407 5868 -740 327 1191 C ATOM 4217 CD LYS C 38 32.256 0.616 -1.737 1.00 42.31 C ANISOU 4217 CD LYS C 38 5376 4726 5973 -860 319 1348 C ATOM 4218 CE LYS C 38 31.475 0.815 -3.016 1.00 41.82 C ANISOU 4218 CE LYS C 38 5291 4773 5827 -917 312 1453 C ATOM 4219 NZ LYS C 38 32.297 1.462 -4.061 1.00 43.40 N ANISOU 4219 NZ LYS C 38 5372 5169 5947 -1064 294 1645 N ATOM 4220 N GLN C 39 29.337 -1.652 1.245 1.00 62.48 N ANISOU 4220 N GLN C 39 8189 6936 8616 -530 366 919 N ATOM 4221 CA GLN C 39 28.753 -2.891 0.740 1.00 55.51 C ANISOU 4221 CA GLN C 39 7310 6110 7671 -475 422 860 C ATOM 4222 C GLN C 39 28.141 -2.650 -0.602 1.00 53.62 C ANISOU 4222 C GLN C 39 7057 5940 7377 -505 429 909 C ATOM 4223 O GLN C 39 27.233 -1.842 -0.734 1.00 48.83 O ANISOU 4223 O GLN C 39 6486 5260 6805 -525 383 958 O ATOM 4224 CB GLN C 39 27.697 -3.459 1.679 1.00 49.22 C ANISOU 4224 CB GLN C 39 6570 5233 6899 -417 418 792 C ATOM 4225 CG GLN C 39 27.245 -4.848 1.261 1.00 55.55 C ANISOU 4225 CG GLN C 39 7362 6066 7678 -365 454 738 C ATOM 4226 CD GLN C 39 26.422 -5.553 2.327 1.00 60.37 C ANISOU 4226 CD GLN C 39 8006 6615 8316 -330 441 709 C ATOM 4227 OE1 GLN C 39 25.434 -5.013 2.844 1.00 57.46 O ANISOU 4227 OE1 GLN C 39 7677 6212 7945 -334 427 706 O ATOM 4228 NE2 GLN C 39 26.819 -6.774 2.650 1.00 58.23 N ANISOU 4228 NE2 GLN C 39 7702 6339 8083 -302 435 693 N ATOM 4229 N SER C 40 28.651 -3.357 -1.598 1.00 71.05 N ANISOU 4229 N SER C 40 9195 8301 9498 -508 480 885 N ATOM 4230 CA SER C 40 28.209 -3.187 -2.973 1.00 83.54 C ANISOU 4230 CA SER C 40 10738 10019 10985 -551 492 933 C ATOM 4231 C SER C 40 27.243 -4.302 -3.351 1.00 88.57 C ANISOU 4231 C SER C 40 11389 10671 11594 -476 522 814 C ATOM 4232 O SER C 40 27.513 -5.475 -3.092 1.00 82.87 O ANISOU 4232 O SER C 40 10640 9947 10899 -405 551 685 O ATOM 4233 CB SER C 40 29.420 -3.186 -3.896 1.00 85.16 C ANISOU 4233 CB SER C 40 10824 10449 11082 -614 531 961 C ATOM 4234 OG SER C 40 30.563 -2.776 -3.165 1.00 89.95 O ANISOU 4234 OG SER C 40 11412 11018 11747 -641 519 998 O ATOM 4235 N HIS C 41 26.118 -3.915 -3.956 1.00 99.57 N ANISOU 4235 N HIS C 41 12813 12060 12959 -495 497 863 N ATOM 4236 CA HIS C 41 25.040 -4.836 -4.340 1.00104.25 C ANISOU 4236 CA HIS C 41 13422 12654 13536 -433 513 762 C ATOM 4237 C HIS C 41 24.651 -5.810 -3.227 1.00104.35 C ANISOU 4237 C HIS C 41 13482 12512 13654 -347 515 659 C ATOM 4238 O HIS C 41 24.457 -7.010 -3.468 1.00102.74 O ANISOU 4238 O HIS C 41 13245 12324 13467 -289 530 541 O ATOM 4239 CB HIS C 41 25.347 -5.578 -5.658 1.00102.06 C ANISOU 4239 CB HIS C 41 13040 12608 13130 -434 558 672 C ATOM 4240 CG HIS C 41 26.779 -5.997 -5.811 1.00105.45 C ANISOU 4240 CG HIS C 41 13368 13178 13521 -434 601 600 C ATOM 4241 ND1 HIS C 41 27.665 -5.332 -6.635 1.00101.61 N ANISOU 4241 ND1 HIS C 41 12786 12918 12901 -528 623 684 N ATOM 4242 CD2 HIS C 41 27.476 -7.017 -5.256 1.00110.19 C ANISOU 4242 CD2 HIS C 41 13929 13731 14206 -357 618 456 C ATOM 4243 CE1 HIS C 41 28.847 -5.920 -6.573 1.00105.35 C ANISOU 4243 CE1 HIS C 41 13167 13490 13372 -500 665 571 C ATOM 4244 NE2 HIS C 41 28.760 -6.944 -5.744 1.00112.13 N ANISOU 4244 NE2 HIS C 41 14059 14171 14375 -391 657 429 N ATOM 4245 N GLY C 42 24.561 -5.293 -2.005 1.00 99.03 N ANISOU 4245 N GLY C 42 12869 11701 13057 -348 488 704 N ATOM 4246 CA GLY C 42 24.146 -6.107 -0.879 1.00100.84 C ANISOU 4246 CA GLY C 42 13130 11826 13359 -297 482 652 C ATOM 4247 C GLY C 42 24.862 -7.451 -0.782 1.00104.29 C ANISOU 4247 C GLY C 42 13512 12274 13839 -253 491 575 C ATOM 4248 O GLY C 42 24.287 -8.423 -0.297 1.00 99.47 O ANISOU 4248 O GLY C 42 12906 11589 13299 -218 469 543 O ATOM 4249 N LYS C 43 26.107 -7.523 -1.248 1.00108.61 N ANISOU 4249 N LYS C 43 13991 12910 14364 -259 510 547 N ATOM 4250 CA LYS C 43 26.873 -8.758 -1.130 1.00103.67 C ANISOU 4250 CA LYS C 43 13292 12276 13823 -206 499 452 C ATOM 4251 C LYS C 43 28.271 -8.560 -0.544 1.00104.85 C ANISOU 4251 C LYS C 43 13403 12439 13995 -221 496 476 C ATOM 4252 O LYS C 43 28.503 -8.876 0.618 1.00109.27 O ANISOU 4252 O LYS C 43 13982 12900 14636 -214 455 518 O ATOM 4253 CB LYS C 43 26.979 -9.439 -2.494 1.00102.11 C ANISOU 4253 CB LYS C 43 12999 12204 13593 -170 522 311 C ATOM 4254 N SER C 44 29.183 -8.000 -1.340 1.00 99.06 N ANISOU 4254 N SER C 44 12606 11852 13180 -253 535 466 N ATOM 4255 CA SER C 44 30.606 -7.945 -0.997 1.00 83.10 C ANISOU 4255 CA SER C 44 10519 9870 11184 -262 537 464 C ATOM 4256 C SER C 44 30.907 -6.788 -0.078 1.00 79.68 C ANISOU 4256 C SER C 44 10155 9380 10741 -325 519 597 C ATOM 4257 O SER C 44 30.343 -5.713 -0.217 1.00 83.76 O ANISOU 4257 O SER C 44 10729 9891 11204 -380 517 683 O ATOM 4258 CB SER C 44 31.443 -7.752 -2.252 1.00 79.26 C ANISOU 4258 CB SER C 44 9915 9606 10593 -289 590 405 C ATOM 4259 OG SER C 44 31.473 -6.375 -2.610 1.00 77.23 O ANISOU 4259 OG SER C 44 9686 9432 10225 -390 606 553 O ATOM 4260 N LEU C 45 31.837 -6.992 0.838 1.00 78.96 N ANISOU 4260 N LEU C 45 10041 9242 10717 -317 491 605 N ATOM 4261 CA LEU C 45 32.217 -5.935 1.769 1.00 70.02 C ANISOU 4261 CA LEU C 45 8958 8065 9583 -373 466 700 C ATOM 4262 C LEU C 45 33.658 -5.471 1.575 1.00 61.82 C ANISOU 4262 C LEU C 45 7839 7114 8534 -413 476 719 C ATOM 4263 O LEU C 45 34.571 -6.277 1.350 1.00 65.91 O ANISOU 4263 O LEU C 45 8264 7693 9087 -377 487 646 O ATOM 4264 CB LEU C 45 32.019 -6.406 3.206 1.00 67.06 C ANISOU 4264 CB LEU C 45 8625 7585 9269 -351 415 717 C ATOM 4265 CG LEU C 45 30.562 -6.539 3.609 1.00 59.94 C ANISOU 4265 CG LEU C 45 7798 6621 8355 -340 404 727 C ATOM 4266 CD1 LEU C 45 30.446 -6.954 5.058 1.00 56.50 C ANISOU 4266 CD1 LEU C 45 7378 6147 7943 -346 354 769 C ATOM 4267 CD2 LEU C 45 29.888 -5.210 3.368 1.00 57.38 C ANISOU 4267 CD2 LEU C 45 7529 6296 7978 -379 415 751 C ATOM 4268 N GLU C 46 33.846 -4.163 1.661 1.00 50.04 N ANISOU 4268 N GLU C 46 6372 5622 7019 -489 461 810 N ATOM 4269 CA GLU C 46 35.167 -3.572 1.557 1.00 53.29 C ANISOU 4269 CA GLU C 46 6709 6109 7431 -547 459 856 C ATOM 4270 C GLU C 46 35.406 -2.640 2.721 1.00 60.60 C ANISOU 4270 C GLU C 46 7683 6924 8418 -584 395 908 C ATOM 4271 O GLU C 46 34.515 -1.902 3.137 1.00 61.39 O ANISOU 4271 O GLU C 46 7858 6927 8542 -597 356 928 O ATOM 4272 CB GLU C 46 35.342 -2.815 0.239 1.00 49.69 C ANISOU 4272 CB GLU C 46 6190 5796 6893 -632 487 937 C ATOM 4273 CG GLU C 46 35.795 -3.687 -0.919 1.00 57.58 C ANISOU 4273 CG GLU C 46 7070 7004 7803 -612 559 853 C ATOM 4274 CD GLU C 46 35.509 -3.062 -2.276 1.00 76.68 C ANISOU 4274 CD GLU C 46 9436 9606 10093 -702 587 943 C ATOM 4275 OE1 GLU C 46 36.384 -3.143 -3.167 1.00 77.30 O ANISOU 4275 OE1 GLU C 46 9374 9928 10069 -752 638 936 O ATOM 4276 OE2 GLU C 46 34.402 -2.499 -2.457 1.00 86.35 O ANISOU 4276 OE2 GLU C 46 10744 10751 11313 -729 554 1024 O ATOM 4277 N TRP C 47 36.621 -2.689 3.251 1.00 62.57 N ANISOU 4277 N TRP C 47 7877 7196 8703 -596 380 907 N ATOM 4278 CA TRP C 47 37.031 -1.761 4.283 1.00 57.20 C ANISOU 4278 CA TRP C 47 7219 6437 8078 -638 314 938 C ATOM 4279 C TRP C 47 37.568 -0.467 3.626 1.00 57.23 C ANISOU 4279 C TRP C 47 7176 6460 8108 -739 287 1039 C ATOM 4280 O TRP C 47 38.494 -0.482 2.823 1.00 58.04 O ANISOU 4280 O TRP C 47 7184 6689 8179 -788 320 1090 O ATOM 4281 CB TRP C 47 38.024 -2.430 5.241 1.00 52.82 C ANISOU 4281 CB TRP C 47 6624 5891 7555 -608 292 901 C ATOM 4282 CG TRP C 47 38.485 -1.535 6.356 1.00 64.13 C ANISOU 4282 CG TRP C 47 8068 7268 9030 -649 221 910 C ATOM 4283 CD1 TRP C 47 37.801 -1.217 7.499 1.00 66.91 C ANISOU 4283 CD1 TRP C 47 8481 7562 9379 -638 171 864 C ATOM 4284 CD2 TRP C 47 39.738 -0.841 6.431 1.00 63.00 C ANISOU 4284 CD2 TRP C 47 7855 7146 8935 -711 188 948 C ATOM 4285 NE1 TRP C 47 38.545 -0.360 8.267 1.00 66.78 N ANISOU 4285 NE1 TRP C 47 8437 7527 9409 -682 106 851 N ATOM 4286 CE2 TRP C 47 39.735 -0.112 7.634 1.00 60.45 C ANISOU 4286 CE2 TRP C 47 7563 6756 8651 -728 111 912 C ATOM 4287 CE3 TRP C 47 40.861 -0.767 5.594 1.00 57.19 C ANISOU 4287 CE3 TRP C 47 7019 6503 8207 -756 217 1000 C ATOM 4288 CZ2 TRP C 47 40.803 0.677 8.019 1.00 58.74 C ANISOU 4288 CZ2 TRP C 47 7289 6528 8501 -787 52 929 C ATOM 4289 CZ3 TRP C 47 41.911 0.012 5.974 1.00 55.60 C ANISOU 4289 CZ3 TRP C 47 6761 6297 8065 -822 165 1039 C ATOM 4290 CH2 TRP C 47 41.883 0.723 7.178 1.00 60.96 C ANISOU 4290 CH2 TRP C 47 7483 6876 8803 -835 79 1005 C ATOM 4291 N ILE C 48 36.904 0.640 3.924 1.00 57.16 N ANISOU 4291 N ILE C 48 7220 6333 8167 -775 217 1069 N ATOM 4292 CA ILE C 48 37.228 1.945 3.361 1.00 56.81 C ANISOU 4292 CA ILE C 48 7131 6255 8201 -881 151 1192 C ATOM 4293 C ILE C 48 38.341 2.636 4.118 1.00 54.41 C ANISOU 4293 C ILE C 48 6779 5903 7993 -930 81 1203 C ATOM 4294 O ILE C 48 39.197 3.273 3.517 1.00 52.56 O ANISOU 4294 O ILE C 48 6462 5713 7797 -1031 53 1329 O ATOM 4295 CB ILE C 48 35.977 2.879 3.338 1.00 62.69 C ANISOU 4295 CB ILE C 48 7933 6847 9037 -889 72 1206 C ATOM 4296 CG1 ILE C 48 34.779 2.161 2.693 1.00 59.65 C ANISOU 4296 CG1 ILE C 48 7602 6504 8558 -833 138 1183 C ATOM 4297 CG2 ILE C 48 36.294 4.209 2.636 1.00 57.46 C ANISOU 4297 CG2 ILE C 48 7208 6124 8498 -1014 -29 1376 C ATOM 4298 CD1 ILE C 48 33.520 2.977 2.640 1.00 55.68 C ANISOU 4298 CD1 ILE C 48 7147 5860 8150 -830 62 1186 C ATOM 4299 N GLY C 49 38.304 2.528 5.443 1.00 56.10 N ANISOU 4299 N GLY C 49 7033 6045 8238 -871 48 1077 N ATOM 4300 CA GLY C 49 39.268 3.196 6.295 1.00 62.10 C ANISOU 4300 CA GLY C 49 7749 6757 9090 -909 -30 1056 C ATOM 4301 C GLY C 49 38.742 3.466 7.685 1.00 65.09 C ANISOU 4301 C GLY C 49 8171 7056 9504 -855 -93 899 C ATOM 4302 O GLY C 49 37.623 3.087 8.018 1.00 68.04 O ANISOU 4302 O GLY C 49 8606 7426 9820 -790 -68 814 O ATOM 4303 N ASN C 50 39.556 4.106 8.513 1.00 64.13 N ANISOU 4303 N ASN C 50 8003 6898 9464 -886 -174 849 N ATOM 4304 CA ASN C 50 39.085 4.526 9.825 1.00 63.68 C ANISOU 4304 CA ASN C 50 7959 6803 9432 -844 -244 669 C ATOM 4305 C ASN C 50 39.855 5.701 10.395 1.00 63.22 C ANISOU 4305 C ASN C 50 7831 6651 9537 -896 -372 609 C ATOM 4306 O ASN C 50 40.904 6.107 9.883 1.00 54.64 O ANISOU 4306 O ASN C 50 6688 5533 8541 -974 -406 732 O ATOM 4307 CB ASN C 50 39.157 3.374 10.820 1.00 59.11 C ANISOU 4307 CB ASN C 50 7399 6374 8686 -789 -188 603 C ATOM 4308 CG ASN C 50 40.567 2.973 11.105 1.00 56.12 C ANISOU 4308 CG ASN C 50 6967 6066 8292 -819 -191 661 C ATOM 4309 OD1 ASN C 50 41.459 3.312 10.342 1.00 60.53 O ANISOU 4309 OD1 ASN C 50 7478 6591 8929 -875 -197 763 O ATOM 4310 ND2 ASN C 50 40.789 2.258 12.197 1.00 51.36 N ANISOU 4310 ND2 ASN C 50 6357 5574 7583 -793 -194 610 N ATOM 4311 N ILE C 51 39.355 6.184 11.520 1.00 63.51 N ANISOU 4311 N ILE C 51 7857 6671 9601 -854 -443 403 N ATOM 4312 CA ILE C 51 39.778 7.459 12.029 1.00 60.19 C ANISOU 4312 CA ILE C 51 7363 6123 9384 -888 -591 289 C ATOM 4313 C ILE C 51 39.795 7.435 13.547 1.00 63.71 C ANISOU 4313 C ILE C 51 7773 6692 9743 -842 -626 49 C ATOM 4314 O ILE C 51 38.912 6.870 14.192 1.00 58.04 O ANISOU 4314 O ILE C 51 7081 6113 8859 -780 -568 -72 O ATOM 4315 CB ILE C 51 38.822 8.514 11.529 1.00 58.05 C ANISOU 4315 CB ILE C 51 7081 5651 9325 -885 -689 242 C ATOM 4316 CG1 ILE C 51 39.218 9.902 12.026 1.00 64.60 C ANISOU 4316 CG1 ILE C 51 7813 6298 10435 -915 -879 105 C ATOM 4317 CG2 ILE C 51 37.405 8.143 11.926 1.00 54.58 C ANISOU 4317 CG2 ILE C 51 6686 5277 8776 -791 -636 80 C ATOM 4318 CD1 ILE C 51 38.572 11.010 11.225 1.00 41.23 C ANISOU 4318 CD1 ILE C 51 4821 3077 7767 -943 -1016 153 C ATOM 4319 N ASN C 52 40.833 8.026 14.114 1.00 68.37 N ANISOU 4319 N ASN C 52 8290 7258 10430 -884 -722 -9 N ATOM 4320 CA ASN C 52 40.952 8.104 15.552 1.00 71.16 C ANISOU 4320 CA ASN C 52 8586 7756 10694 -853 -770 -246 C ATOM 4321 C ASN C 52 40.217 9.364 15.970 1.00 71.03 C ANISOU 4321 C ASN C 52 8500 7608 10879 -817 -905 -519 C ATOM 4322 O ASN C 52 40.612 10.472 15.604 1.00 67.11 O ANISOU 4322 O ASN C 52 7946 6880 10674 -856 -1043 -530 O ATOM 4323 CB ASN C 52 42.423 8.162 15.950 1.00 72.15 C ANISOU 4323 CB ASN C 52 8656 7915 10841 -913 -820 -197 C ATOM 4324 CG ASN C 52 42.637 7.876 17.412 1.00 73.16 C ANISOU 4324 CG ASN C 52 8734 8273 10792 -892 -841 -385 C ATOM 4325 OD1 ASN C 52 41.971 8.442 18.274 1.00 74.01 O ANISOU 4325 OD1 ASN C 52 8784 8445 10891 -852 -905 -657 O ATOM 4326 ND2 ASN C 52 43.560 6.976 17.702 1.00 74.86 N ANISOU 4326 ND2 ASN C 52 8952 8634 10858 -921 -794 -247 N ATOM 4327 N PRO C 53A 39.123 9.208 16.719 1.00 68.54 N ANISOU 4327 N PRO C 53A 8172 7439 10430 -744 -876 -742 N ATOM 4328 CA PRO C 53A 38.253 10.367 16.928 1.00 69.85 C ANISOU 4328 CA PRO C 53A 8260 7463 10818 -690 -1000 -1022 C ATOM 4329 C PRO C 53A 38.895 11.371 17.856 1.00 72.65 C ANISOU 4329 C PRO C 53A 8484 7785 11334 -691 -1161 -1295 C ATOM 4330 O PRO C 53A 38.449 12.515 17.928 1.00 76.00 O ANISOU 4330 O PRO C 53A 8817 8014 12047 -652 -1314 -1531 O ATOM 4331 CB PRO C 53A 36.996 9.773 17.581 1.00 64.03 C ANISOU 4331 CB PRO C 53A 7523 6970 9835 -617 -903 -1198 C ATOM 4332 CG PRO C 53A 37.311 8.370 17.872 1.00 69.12 C ANISOU 4332 CG PRO C 53A 8237 7882 10143 -648 -756 -1006 C ATOM 4333 CD PRO C 53A 38.755 8.084 17.581 1.00 64.94 C ANISOU 4333 CD PRO C 53A 7736 7302 9636 -719 -761 -777 C ATOM 4334 N TYR C 54 39.918 10.947 18.581 1.00 72.17 N ANISOU 4334 N TYR C 54 8403 7910 11109 -732 -1143 -1279 N ATOM 4335 CA TYR C 54 40.561 11.856 19.512 1.00 88.73 C ANISOU 4335 CA TYR C 54 10369 10003 13341 -736 -1298 -1555 C ATOM 4336 C TYR C 54 41.408 12.867 18.741 1.00 91.56 C ANISOU 4336 C TYR C 54 10697 10004 14089 -798 -1451 -1439 C ATOM 4337 O TYR C 54 41.244 14.077 18.895 1.00 90.33 O ANISOU 4337 O TYR C 54 10433 9630 14259 -775 -1635 -1676 O ATOM 4338 CB TYR C 54 41.386 11.071 20.539 1.00 98.41 C ANISOU 4338 CB TYR C 54 11575 11556 14258 -769 -1241 -1555 C ATOM 4339 CG TYR C 54 41.675 11.810 21.830 1.00106.98 C ANISOU 4339 CG TYR C 54 12508 12785 15355 -751 -1371 -1936 C ATOM 4340 CD1 TYR C 54 41.863 13.188 21.841 1.00113.85 C ANISOU 4340 CD1 TYR C 54 13268 13388 16604 -734 -1565 -2181 C ATOM 4341 CD2 TYR C 54 41.760 11.125 23.039 1.00109.04 C ANISOU 4341 CD2 TYR C 54 12718 13458 15255 -759 -1314 -2049 C ATOM 4342 CE1 TYR C 54 42.133 13.868 23.023 1.00121.57 C ANISOU 4342 CE1 TYR C 54 14087 14502 17602 -710 -1694 -2573 C ATOM 4343 CE2 TYR C 54 42.032 11.792 24.227 1.00115.85 C ANISOU 4343 CE2 TYR C 54 13423 14500 16094 -747 -1431 -2419 C ATOM 4344 CZ TYR C 54 42.218 13.166 24.215 1.00120.54 C ANISOU 4344 CZ TYR C 54 13907 14822 17070 -715 -1618 -2703 C ATOM 4345 OH TYR C 54 42.491 13.843 25.390 1.00117.13 O ANISOU 4345 OH TYR C 54 13302 14571 16630 -695 -1745 -3113 O ATOM 4346 N TYR C 55 42.316 12.353 17.916 1.00 94.07 N ANISOU 4346 N TYR C 55 11091 10270 14382 -881 -1385 -1076 N ATOM 4347 CA TYR C 55 43.222 13.189 17.132 1.00 90.00 C ANISOU 4347 CA TYR C 55 10537 9470 14190 -972 -1513 -898 C ATOM 4348 C TYR C 55 42.894 13.397 15.649 1.00 81.59 C ANISOU 4348 C TYR C 55 9526 8176 13298 -1025 -1509 -599 C ATOM 4349 O TYR C 55 43.591 14.144 14.965 1.00 71.66 O ANISOU 4349 O TYR C 55 8219 6701 12310 -1123 -1628 -420 O ATOM 4350 CB TYR C 55 44.657 12.730 17.353 1.00 93.07 C ANISOU 4350 CB TYR C 55 10916 9978 14468 -1046 -1482 -745 C ATOM 4351 CG TYR C 55 45.088 13.044 18.758 1.00105.88 C ANISOU 4351 CG TYR C 55 12439 11738 16052 -1019 -1575 -1060 C ATOM 4352 CD1 TYR C 55 45.306 14.365 19.149 1.00116.41 C ANISOU 4352 CD1 TYR C 55 13646 12864 17720 -1026 -1791 -1303 C ATOM 4353 CD2 TYR C 55 45.233 12.040 19.708 1.00110.44 C ANISOU 4353 CD2 TYR C 55 13035 12657 16270 -991 -1465 -1122 C ATOM 4354 CE1 TYR C 55 45.684 14.681 20.441 1.00125.33 C ANISOU 4354 CE1 TYR C 55 14668 14144 18808 -998 -1882 -1630 C ATOM 4355 CE2 TYR C 55 45.612 12.342 21.009 1.00122.14 C ANISOU 4355 CE2 TYR C 55 14412 14312 17685 -977 -1555 -1410 C ATOM 4356 CZ TYR C 55 45.839 13.671 21.372 1.00129.35 C ANISOU 4356 CZ TYR C 55 15197 15035 18915 -977 -1757 -1683 C ATOM 4357 OH TYR C 55 46.219 14.000 22.663 1.00131.20 O ANISOU 4357 OH TYR C 55 15310 15460 19079 -961 -1853 -2007 O ATOM 4358 N GLY C 56 41.835 12.750 15.167 1.00 81.79 N ANISOU 4358 N GLY C 56 9643 8270 13165 -972 -1380 -536 N ATOM 4359 CA GLY C 56 41.375 12.916 13.795 1.00 78.72 C ANISOU 4359 CA GLY C 56 9300 7704 12904 -1018 -1375 -273 C ATOM 4360 C GLY C 56 42.230 12.195 12.772 1.00 76.23 C ANISOU 4360 C GLY C 56 9038 7470 12457 -1112 -1254 94 C ATOM 4361 O GLY C 56 42.025 12.324 11.566 1.00 73.34 O ANISOU 4361 O GLY C 56 8691 7008 12166 -1176 -1248 342 O ATOM 4362 N SER C 57 43.196 11.438 13.273 1.00 77.90 N ANISOU 4362 N SER C 57 9254 7878 12466 -1122 -1165 117 N ATOM 4363 CA SER C 57 44.136 10.686 12.455 1.00 72.71 C ANISOU 4363 CA SER C 57 8617 7332 11679 -1195 -1050 402 C ATOM 4364 C SER C 57 43.456 9.519 11.752 1.00 71.29 C ANISOU 4364 C SER C 57 8535 7295 11259 -1149 -869 523 C ATOM 4365 O SER C 57 42.636 8.826 12.349 1.00 78.61 O ANISOU 4365 O SER C 57 9524 8333 12012 -1055 -792 381 O ATOM 4366 CB SER C 57 45.280 10.189 13.341 1.00 66.69 C ANISOU 4366 CB SER C 57 7819 6727 10793 -1198 -1027 346 C ATOM 4367 OG SER C 57 44.844 10.071 14.686 1.00 63.57 O ANISOU 4367 OG SER C 57 7426 6431 10296 -1112 -1049 64 O ATOM 4368 N THR C 58 43.813 9.299 10.489 1.00 64.92 N ANISOU 4368 N THR C 58 7724 6506 10438 -1224 -806 783 N ATOM 4369 CA THR C 58 43.151 8.295 9.666 1.00 64.93 C ANISOU 4369 CA THR C 58 7799 6626 10244 -1186 -653 885 C ATOM 4370 C THR C 58 44.081 7.287 9.012 1.00 72.03 C ANISOU 4370 C THR C 58 8676 7713 10979 -1214 -521 1042 C ATOM 4371 O THR C 58 45.202 7.608 8.600 1.00 72.11 O ANISOU 4371 O THR C 58 8597 7749 11051 -1310 -547 1174 O ATOM 4372 CB THR C 58 42.388 8.943 8.518 1.00 67.49 C ANISOU 4372 CB THR C 58 8126 6828 10688 -1240 -695 1032 C ATOM 4373 OG1 THR C 58 43.248 9.875 7.857 1.00 66.06 O ANISOU 4373 OG1 THR C 58 7846 6560 10692 -1382 -802 1229 O ATOM 4374 CG2 THR C 58 41.163 9.666 9.030 1.00 76.49 C ANISOU 4374 CG2 THR C 58 9295 7793 11975 -1175 -800 852 C ATOM 4375 N ARG C 59 43.587 6.058 8.910 1.00 71.76 N ANISOU 4375 N ARG C 59 8707 7810 10747 -1130 -388 1014 N ATOM 4376 CA ARG C 59 44.162 5.081 8.011 1.00 66.50 C ANISOU 4376 CA ARG C 59 8009 7306 9950 -1139 -265 1134 C ATOM 4377 C ARG C 59 43.119 4.823 6.965 1.00 60.84 C ANISOU 4377 C ARG C 59 7341 6608 9168 -1126 -197 1199 C ATOM 4378 O ARG C 59 41.945 4.760 7.285 1.00 62.67 O ANISOU 4378 O ARG C 59 7657 6769 9385 -1059 -200 1108 O ATOM 4379 CB ARG C 59 44.474 3.785 8.732 1.00 71.95 C ANISOU 4379 CB ARG C 59 8718 8112 10508 -1049 -194 1043 C ATOM 4380 CG ARG C 59 45.790 3.797 9.463 1.00 86.80 C ANISOU 4380 CG ARG C 59 10523 10031 12425 -1074 -240 1026 C ATOM 4381 CD ARG C 59 46.308 2.383 9.626 1.00 94.44 C ANISOU 4381 CD ARG C 59 11469 11126 13287 -1004 -165 1011 C ATOM 4382 NE ARG C 59 45.309 1.490 10.213 1.00 93.25 N ANISOU 4382 NE ARG C 59 11407 10982 13043 -913 -139 937 N ATOM 4383 CZ ARG C 59 44.808 1.634 11.440 1.00 92.46 C ANISOU 4383 CZ ARG C 59 11355 10862 12913 -890 -200 846 C ATOM 4384 NH1 ARG C 59 45.188 2.652 12.212 1.00 90.80 N ANISOU 4384 NH1 ARG C 59 11118 10612 12769 -935 -295 781 N ATOM 4385 NH2 ARG C 59 43.917 0.764 11.896 1.00 88.84 N ANISOU 4385 NH2 ARG C 59 10957 10442 12355 -828 -172 814 N ATOM 4386 N TYR C 60 43.547 4.706 5.713 1.00 61.78 N ANISOU 4386 N TYR C 60 7391 6845 9238 -1197 -137 1351 N ATOM 4387 CA TYR C 60 42.660 4.348 4.610 1.00 57.48 C ANISOU 4387 CA TYR C 60 6874 6370 8597 -1191 -63 1414 C ATOM 4388 C TYR C 60 43.133 3.062 3.920 1.00 56.73 C ANISOU 4388 C TYR C 60 6723 6495 8335 -1150 74 1398 C ATOM 4389 O TYR C 60 44.317 2.825 3.771 1.00 58.32 O ANISOU 4389 O TYR C 60 6821 6823 8516 -1184 104 1420 O ATOM 4390 CB TYR C 60 42.589 5.455 3.542 1.00 48.25 C ANISOU 4390 CB TYR C 60 5643 5184 7505 -1333 -130 1621 C ATOM 4391 CG TYR C 60 42.114 6.825 3.981 1.00 55.87 C ANISOU 4391 CG TYR C 60 6630 5899 8699 -1383 -300 1653 C ATOM 4392 CD1 TYR C 60 40.786 7.076 4.236 1.00 65.35 C ANISOU 4392 CD1 TYR C 60 7922 6946 9964 -1314 -346 1565 C ATOM 4393 CD2 TYR C 60 42.990 7.888 4.071 1.00 69.18 C ANISOU 4393 CD2 TYR C 60 8226 7498 10562 -1503 -425 1767 C ATOM 4394 CE1 TYR C 60 40.350 8.345 4.619 1.00 63.99 C ANISOU 4394 CE1 TYR C 60 7743 6529 10040 -1347 -520 1557 C ATOM 4395 CE2 TYR C 60 42.561 9.150 4.443 1.00 70.70 C ANISOU 4395 CE2 TYR C 60 8417 7431 11016 -1543 -608 1776 C ATOM 4396 CZ TYR C 60 41.243 9.362 4.720 1.00 63.46 C ANISOU 4396 CZ TYR C 60 7585 6358 10171 -1458 -655 1656 C ATOM 4397 OH TYR C 60 40.816 10.605 5.088 1.00 67.14 O ANISOU 4397 OH TYR C 60 8026 6553 10929 -1483 -851 1627 O ATOM 4398 N ASN C 61 42.189 2.233 3.507 1.00 56.90 N ANISOU 4398 N ASN C 61 6803 6558 8258 -1071 149 1338 N ATOM 4399 CA ASN C 61 42.427 1.246 2.470 1.00 56.11 C ANISOU 4399 CA ASN C 61 6627 6668 8023 -1050 261 1323 C ATOM 4400 C ASN C 61 42.927 1.979 1.219 1.00 60.40 C ANISOU 4400 C ASN C 61 7051 7384 8516 -1195 272 1496 C ATOM 4401 O ASN C 61 42.399 3.015 0.859 1.00 57.83 O ANISOU 4401 O ASN C 61 6747 6984 8241 -1289 201 1642 O ATOM 4402 CB ASN C 61 41.117 0.518 2.185 1.00 55.18 C ANISOU 4402 CB ASN C 61 6599 6530 7839 -961 309 1246 C ATOM 4403 CG ASN C 61 41.228 -0.454 1.051 1.00 58.84 C ANISOU 4403 CG ASN C 61 6974 7207 8176 -933 412 1195 C ATOM 4404 OD1 ASN C 61 42.008 -0.252 0.131 1.00 61.79 O ANISOU 4404 OD1 ASN C 61 7215 7787 8475 -1017 452 1261 O ATOM 4405 ND2 ASN C 61 40.441 -1.522 1.104 1.00 56.90 N ANISOU 4405 ND2 ASN C 61 6782 6931 7905 -821 450 1069 N ATOM 4406 N GLN C 62 43.955 1.458 0.561 1.00 70.52 N ANISOU 4406 N GLN C 62 8187 8907 9702 -1221 351 1485 N ATOM 4407 CA GLN C 62 44.573 2.179 -0.557 1.00 73.35 C ANISOU 4407 CA GLN C 62 8398 9488 9983 -1386 362 1672 C ATOM 4408 C GLN C 62 43.586 2.429 -1.697 1.00 72.46 C ANISOU 4408 C GLN C 62 8290 9483 9759 -1451 379 1785 C ATOM 4409 O GLN C 62 43.627 3.455 -2.374 1.00 69.12 O ANISOU 4409 O GLN C 62 7804 9125 9333 -1617 319 2022 O ATOM 4410 CB GLN C 62 45.805 1.432 -1.081 1.00 76.12 C ANISOU 4410 CB GLN C 62 8565 10136 10223 -1387 463 1591 C ATOM 4411 CG GLN C 62 46.605 2.215 -2.130 1.00 90.24 C ANISOU 4411 CG GLN C 62 10170 12207 11910 -1583 476 1800 C ATOM 4412 CD GLN C 62 47.192 3.535 -1.595 1.00 98.71 C ANISOU 4412 CD GLN C 62 11237 13120 13147 -1725 347 2013 C ATOM 4413 OE1 GLN C 62 47.307 3.740 -0.380 1.00 95.64 O ANISOU 4413 OE1 GLN C 62 10951 12454 12934 -1660 266 1946 O ATOM 4414 NE2 GLN C 62 47.559 4.435 -2.513 1.00100.39 N ANISOU 4414 NE2 GLN C 62 11317 13522 13306 -1930 316 2276 N ATOM 4415 N LYS C 63 42.691 1.478 -1.901 1.00 74.29 N ANISOU 4415 N LYS C 63 8589 9728 9911 -1329 446 1631 N ATOM 4416 CA LYS C 63 41.776 1.538 -3.017 1.00 70.12 C ANISOU 4416 CA LYS C 63 8053 9335 9254 -1377 473 1708 C ATOM 4417 C LYS C 63 40.976 2.810 -2.884 1.00 72.77 C ANISOU 4417 C LYS C 63 8484 9449 9717 -1468 342 1914 C ATOM 4418 O LYS C 63 40.709 3.491 -3.873 1.00 78.82 O ANISOU 4418 O LYS C 63 9187 10343 10418 -1608 306 2124 O ATOM 4419 CB LYS C 63 40.895 0.292 -3.016 1.00 71.74 C ANISOU 4419 CB LYS C 63 8332 9520 9404 -1211 544 1483 C ATOM 4420 CG LYS C 63 41.745 -0.969 -2.990 1.00 81.70 C ANISOU 4420 CG LYS C 63 9488 10932 10622 -1103 634 1257 C ATOM 4421 CD LYS C 63 40.967 -2.274 -2.956 1.00 87.08 C ANISOU 4421 CD LYS C 63 10222 11564 11301 -941 678 1032 C ATOM 4422 CE LYS C 63 41.936 -3.454 -2.708 1.00 91.54 C ANISOU 4422 CE LYS C 63 10672 12198 11912 -827 721 811 C ATOM 4423 NZ LYS C 63 43.184 -3.433 -3.560 1.00 89.20 N ANISOU 4423 NZ LYS C 63 10152 12241 11500 -897 789 781 N ATOM 4424 N PHE C 64 40.639 3.151 -1.643 1.00 72.90 N ANISOU 4424 N PHE C 64 8631 9144 9923 -1395 257 1851 N ATOM 4425 CA PHE C 64 39.797 4.315 -1.354 1.00 68.62 C ANISOU 4425 CA PHE C 64 8174 8346 9554 -1446 117 1974 C ATOM 4426 C PHE C 64 40.529 5.638 -1.066 1.00 63.79 C ANISOU 4426 C PHE C 64 7501 7606 9128 -1582 -25 2153 C ATOM 4427 O PHE C 64 39.899 6.687 -0.998 1.00 60.00 O ANISOU 4427 O PHE C 64 7054 6913 8828 -1639 -168 2269 O ATOM 4428 CB PHE C 64 38.808 3.979 -0.240 1.00 65.76 C ANISOU 4428 CB PHE C 64 7966 7737 9282 -1289 99 1776 C ATOM 4429 CG PHE C 64 37.870 2.861 -0.593 1.00 70.78 C ANISOU 4429 CG PHE C 64 8661 8451 9779 -1179 201 1648 C ATOM 4430 CD1 PHE C 64 36.808 3.079 -1.451 1.00 68.43 C ANISOU 4430 CD1 PHE C 64 8388 8173 9441 -1208 186 1732 C ATOM 4431 CD2 PHE C 64 38.056 1.587 -0.075 1.00 75.43 C ANISOU 4431 CD2 PHE C 64 9274 9086 10301 -1052 292 1455 C ATOM 4432 CE1 PHE C 64 35.949 2.055 -1.775 1.00 67.95 C ANISOU 4432 CE1 PHE C 64 8375 8178 9264 -1109 271 1607 C ATOM 4433 CE2 PHE C 64 37.193 0.553 -0.405 1.00 68.85 C ANISOU 4433 CE2 PHE C 64 8484 8300 9375 -957 365 1341 C ATOM 4434 CZ PHE C 64 36.145 0.791 -1.252 1.00 66.50 C ANISOU 4434 CZ PHE C 64 8212 8026 9028 -984 359 1409 C ATOM 4435 N LYS C 65 41.854 5.595 -0.930 1.00 64.43 N ANISOU 4435 N LYS C 65 7480 7808 9191 -1636 2 2173 N ATOM 4436 CA LYS C 65 42.625 6.814 -0.737 1.00 60.61 C ANISOU 4436 CA LYS C 65 6920 7218 8891 -1780 -137 2356 C ATOM 4437 C LYS C 65 42.296 7.744 -1.901 1.00 77.71 C ANISOU 4437 C LYS C 65 9025 9459 11042 -1907 -230 2593 C ATOM 4438 O LYS C 65 42.470 7.393 -3.074 1.00 81.73 O ANISOU 4438 O LYS C 65 9437 10287 11329 -1981 -145 2700 O ATOM 4439 CB LYS C 65 44.124 6.493 -0.716 1.00 54.32 C ANISOU 4439 CB LYS C 65 5994 6627 8018 -1829 -68 2357 C ATOM 4440 CG LYS C 65 45.052 7.650 -0.340 1.00 72.65 C ANISOU 4440 CG LYS C 65 8234 8827 10542 -1966 -211 2515 C ATOM 4441 CD LYS C 65 46.440 7.512 -1.013 1.00 84.87 C ANISOU 4441 CD LYS C 65 9598 10700 11950 -2081 -138 2625 C ATOM 4442 CE LYS C 65 47.010 8.854 -1.571 1.00110.94 C ANISOU 4442 CE LYS C 65 12815 14016 15320 -2208 -290 2836 C ATOM 4443 NZ LYS C 65 46.389 9.355 -2.863 1.00110.51 N ANISOU 4443 NZ LYS C 65 12729 14110 15151 -2280 -337 3020 N ATOM 4444 N GLY C 66 41.807 8.930 -1.562 1.00 83.74 N ANISOU 4444 N GLY C 66 9838 9952 12029 -1898 -415 2625 N ATOM 4445 CA GLY C 66 41.570 9.988 -2.525 1.00 89.30 C ANISOU 4445 CA GLY C 66 10477 10687 12768 -1989 -555 2833 C ATOM 4446 C GLY C 66 40.135 10.112 -2.992 1.00 89.37 C ANISOU 4446 C GLY C 66 10559 10615 12783 -1939 -600 2839 C ATOM 4447 O GLY C 66 39.709 11.194 -3.396 1.00 94.32 O ANISOU 4447 O GLY C 66 11152 11134 13553 -1981 -776 2974 O ATOM 4448 N LYS C 67 39.388 9.013 -2.956 1.00 83.46 N ANISOU 4448 N LYS C 67 9898 9918 11895 -1851 -454 2703 N ATOM 4449 CA LYS C 67 37.935 9.071 -3.134 1.00 79.77 C ANISOU 4449 CA LYS C 67 9520 9321 11466 -1778 -495 2661 C ATOM 4450 C LYS C 67 37.209 9.355 -1.811 1.00 78.83 C ANISOU 4450 C LYS C 67 9515 8849 11586 -1647 -571 2452 C ATOM 4451 O LYS C 67 36.288 10.160 -1.747 1.00 80.76 O ANISOU 4451 O LYS C 67 9784 8897 12004 -1609 -710 2440 O ATOM 4452 CB LYS C 67 37.411 7.802 -3.810 1.00 70.61 C ANISOU 4452 CB LYS C 67 8387 8397 10046 -1753 -317 2624 C ATOM 4453 CG LYS C 67 35.903 7.663 -3.789 1.00 66.75 C ANISOU 4453 CG LYS C 67 8008 7756 9600 -1658 -337 2542 C ATOM 4454 CD LYS C 67 35.362 7.272 -5.149 1.00 66.29 C ANISOU 4454 CD LYS C 67 7904 7963 9319 -1715 -282 2661 C ATOM 4455 CE LYS C 67 35.640 8.358 -6.156 1.00 78.93 C ANISOU 4455 CE LYS C 67 9385 9680 10923 -1849 -425 2905 C ATOM 4456 NZ LYS C 67 35.131 8.006 -7.504 1.00 87.59 N ANISOU 4456 NZ LYS C 67 10422 11073 11784 -1917 -383 3024 N ATOM 4457 N ALA C 68 37.650 8.683 -0.754 1.00 73.79 N ANISOU 4457 N ALA C 68 8926 8153 10956 -1583 -485 2283 N ATOM 4458 CA ALA C 68 37.130 8.899 0.591 1.00 60.92 C ANISOU 4458 CA ALA C 68 7380 6243 9525 -1472 -550 2067 C ATOM 4459 C ALA C 68 38.091 9.759 1.409 1.00 70.94 C ANISOU 4459 C ALA C 68 8591 7374 10987 -1503 -669 2036 C ATOM 4460 O ALA C 68 39.320 9.650 1.282 1.00 75.68 O ANISOU 4460 O ALA C 68 9119 8111 11527 -1584 -632 2128 O ATOM 4461 CB ALA C 68 36.902 7.571 1.285 1.00 39.06 C ANISOU 4461 CB ALA C 68 4700 3536 6607 -1352 -387 1865 C ATOM 4462 N THR C 69 37.526 10.638 2.225 1.00 68.88 N ANISOU 4462 N THR C 69 8347 6854 10970 -1438 -819 1894 N ATOM 4463 CA THR C 69 38.307 11.370 3.210 1.00 66.92 C ANISOU 4463 CA THR C 69 8049 6452 10924 -1444 -936 1796 C ATOM 4464 C THR C 69 37.474 11.407 4.480 1.00 57.12 C ANISOU 4464 C THR C 69 6868 5007 9829 -1322 -981 1501 C ATOM 4465 O THR C 69 36.293 11.745 4.444 1.00 54.32 O ANISOU 4465 O THR C 69 6538 4539 9561 -1250 -1041 1414 O ATOM 4466 CB THR C 69 38.782 12.787 2.706 1.00 58.38 C ANISOU 4466 CB THR C 69 6851 5289 10040 -1528 -1133 1961 C ATOM 4467 OG1 THR C 69 38.424 13.802 3.650 1.00 53.12 O ANISOU 4467 OG1 THR C 69 6158 4351 9676 -1458 -1316 1772 O ATOM 4468 CG2 THR C 69 38.188 13.127 1.335 1.00 61.78 C ANISOU 4468 CG2 THR C 69 7248 5809 10415 -1585 -1173 2189 C ATOM 4469 N LEU C 70 38.075 10.992 5.590 1.00 55.81 N ANISOU 4469 N LEU C 70 6713 4843 9648 -1288 -940 1327 N ATOM 4470 CA LEU C 70 37.348 10.873 6.847 1.00 56.18 C ANISOU 4470 CA LEU C 70 6804 4842 9699 -1141 -939 993 C ATOM 4471 C LEU C 70 37.653 12.034 7.770 1.00 64.80 C ANISOU 4471 C LEU C 70 7812 5722 11088 -1140 -1135 816 C ATOM 4472 O LEU C 70 38.757 12.590 7.755 1.00 68.64 O ANISOU 4472 O LEU C 70 8224 6148 11709 -1238 -1225 922 O ATOM 4473 CB LEU C 70 37.662 9.559 7.540 1.00 52.66 C ANISOU 4473 CB LEU C 70 6422 4641 8946 -1060 -752 869 C ATOM 4474 CG LEU C 70 37.565 8.319 6.654 1.00 56.79 C ANISOU 4474 CG LEU C 70 7007 5368 9202 -1057 -570 1018 C ATOM 4475 CD1 LEU C 70 37.770 7.061 7.475 1.00 60.48 C ANISOU 4475 CD1 LEU C 70 7524 6021 9435 -970 -431 884 C ATOM 4476 CD2 LEU C 70 36.241 8.257 5.925 1.00 47.59 C ANISOU 4476 CD2 LEU C 70 5891 4164 8028 -1026 -555 1054 C ATOM 4477 N THR C 71 36.647 12.414 8.549 1.00 63.82 N ANISOU 4477 N THR C 71 7682 5491 11075 -1029 -1205 533 N ATOM 4478 CA THR C 71 36.737 13.554 9.450 1.00 63.46 C ANISOU 4478 CA THR C 71 7535 5239 11340 -1002 -1407 288 C ATOM 4479 C THR C 71 35.802 13.292 10.609 1.00 64.48 C ANISOU 4479 C THR C 71 7670 5464 11366 -850 -1360 -97 C ATOM 4480 O THR C 71 34.937 12.429 10.510 1.00 58.12 O ANISOU 4480 O THR C 71 6944 4816 10324 -784 -1209 -116 O ATOM 4481 CB THR C 71 36.331 14.871 8.762 1.00 57.88 C ANISOU 4481 CB THR C 71 6744 4317 10932 -1010 -1605 382 C ATOM 4482 OG1 THR C 71 35.301 14.615 7.797 1.00 60.50 O ANISOU 4482 OG1 THR C 71 7130 4677 11179 -993 -1549 531 O ATOM 4483 CG2 THR C 71 37.505 15.479 8.067 1.00 53.20 C ANISOU 4483 CG2 THR C 71 6088 3721 10404 -1125 -1681 672 C ATOM 4484 N VAL C 72 35.972 14.034 11.702 1.00 66.34 N ANISOU 4484 N VAL C 72 7806 5626 11775 -800 -1493 -410 N ATOM 4485 CA VAL C 72 35.130 13.853 12.880 1.00 66.01 C ANISOU 4485 CA VAL C 72 7733 5737 11613 -667 -1453 -806 C ATOM 4486 C VAL C 72 34.718 15.174 13.527 1.00 80.25 C ANISOU 4486 C VAL C 72 9382 7313 13795 -599 -1686 -1163 C ATOM 4487 O VAL C 72 35.355 16.197 13.322 1.00 91.77 O ANISOU 4487 O VAL C 72 10758 8517 15594 -653 -1883 -1118 O ATOM 4488 CB VAL C 72 35.846 13.006 13.911 1.00 67.51 C ANISOU 4488 CB VAL C 72 7942 6238 11472 -656 -1317 -907 C ATOM 4489 CG1 VAL C 72 35.185 13.152 15.238 1.00 72.02 C ANISOU 4489 CG1 VAL C 72 8423 6972 11968 -549 -1332 -1336 C ATOM 4490 CG2 VAL C 72 35.854 11.545 13.469 1.00 73.24 C ANISOU 4490 CG2 VAL C 72 8802 7203 11824 -676 -1086 -653 C ATOM 4491 N ASP C 73 33.622 15.165 14.274 1.00 84.08 N ANISOU 4491 N ASP C 73 9815 7909 14223 -475 -1667 -1517 N ATOM 4492 CA ASP C 73 33.333 16.272 15.172 1.00 81.42 C ANISOU 4492 CA ASP C 73 9302 7446 14187 -388 -1866 -1963 C ATOM 4493 C ASP C 73 33.025 15.739 16.572 1.00 82.89 C ANISOU 4493 C ASP C 73 9429 8030 14034 -298 -1742 -2350 C ATOM 4494 O ASP C 73 31.962 15.152 16.799 1.00 86.08 O ANISOU 4494 O ASP C 73 9848 8650 14207 -227 -1610 -2468 O ATOM 4495 CB ASP C 73 32.163 17.085 14.639 1.00 82.47 C ANISOU 4495 CB ASP C 73 9365 7407 14561 -285 -1968 -1996 C ATOM 4496 CG ASP C 73 31.821 18.256 15.527 1.00 96.67 C ANISOU 4496 CG ASP C 73 10958 9181 16593 -142 -2129 -2398 C ATOM 4497 OD1 ASP C 73 32.640 18.586 16.413 1.00101.11 O ANISOU 4497 OD1 ASP C 73 11435 9808 17172 -136 -2186 -2605 O ATOM 4498 OD2 ASP C 73 30.741 18.859 15.328 1.00101.29 O ANISOU 4498 OD2 ASP C 73 11449 9683 17352 -33 -2206 -2505 O ATOM 4499 N LYS C 74 33.943 15.982 17.508 1.00 79.78 N ANISOU 4499 N LYS C 74 8954 7744 13614 -312 -1796 -2542 N ATOM 4500 CA LYS C 74 33.830 15.506 18.888 1.00 82.26 C ANISOU 4500 CA LYS C 74 9193 8485 13577 -256 -1692 -2883 C ATOM 4501 C LYS C 74 32.592 16.027 19.637 1.00 93.48 C ANISOU 4501 C LYS C 74 10447 10013 15059 -122 -1748 -3387 C ATOM 4502 O LYS C 74 31.885 15.257 20.292 1.00 96.38 O ANISOU 4502 O LYS C 74 10801 10777 15043 -84 -1581 -3523 O ATOM 4503 CB LYS C 74 35.089 15.880 19.666 1.00 82.46 C ANISOU 4503 CB LYS C 74 9140 8557 13634 -300 -1786 -3006 C ATOM 4504 CG LYS C 74 36.301 15.045 19.306 1.00 93.43 C ANISOU 4504 CG LYS C 74 10673 10018 14809 -421 -1671 -2577 C ATOM 4505 CD LYS C 74 37.605 15.636 19.853 1.00102.48 C ANISOU 4505 CD LYS C 74 11735 11107 16097 -473 -1808 -2663 C ATOM 4506 CE LYS C 74 38.192 16.676 18.902 1.00106.63 C ANISOU 4506 CE LYS C 74 12242 11157 17116 -536 -2013 -2485 C ATOM 4507 NZ LYS C 74 38.327 16.149 17.506 1.00104.06 N ANISOU 4507 NZ LYS C 74 12075 10690 16774 -625 -1916 -1970 N ATOM 4508 N SER C 75 32.350 17.334 19.538 1.00 95.96 N ANISOU 4508 N SER C 75 10622 10032 15807 -34 -1954 -3581 N ATOM 4509 CA SER C 75 31.246 18.011 20.221 1.00 92.59 C ANISOU 4509 CA SER C 75 10001 9734 15444 137 -1990 -3988 C ATOM 4510 C SER C 75 29.924 17.278 20.038 1.00 89.41 C ANISOU 4510 C SER C 75 9639 9503 14831 173 -1846 -4037 C ATOM 4511 O SER C 75 29.294 16.827 21.001 1.00 90.44 O ANISOU 4511 O SER C 75 9673 10044 14644 223 -1731 -4365 O ATOM 4512 CB SER C 75 31.113 19.442 19.694 1.00 94.12 C ANISOU 4512 CB SER C 75 10075 9546 16142 231 -2207 -3950 C ATOM 4513 OG SER C 75 32.375 20.097 19.668 1.00 94.88 O ANISOU 4513 OG SER C 75 10152 9442 16454 178 -2346 -3828 O ATOM 4514 N SER C 76 29.508 17.182 18.784 1.00 81.80 N ANISOU 4514 N SER C 76 8803 8247 14029 143 -1853 -3691 N ATOM 4515 CA SER C 76 28.274 16.516 18.424 1.00 81.77 C ANISOU 4515 CA SER C 76 8855 8343 13873 173 -1729 -3683 C ATOM 4516 C SER C 76 28.534 15.017 18.396 1.00 75.36 C ANISOU 4516 C SER C 76 8224 7836 12574 67 -1484 -3400 C ATOM 4517 O SER C 76 27.625 14.211 18.135 1.00 60.88 O ANISOU 4517 O SER C 76 6461 6172 10499 79 -1326 -3287 O ATOM 4518 CB SER C 76 27.827 16.990 17.043 1.00 88.80 C ANISOU 4518 CB SER C 76 9813 8848 15080 176 -1820 -3333 C ATOM 4519 OG SER C 76 28.726 16.544 16.042 1.00 90.59 O ANISOU 4519 OG SER C 76 10229 8876 15315 29 -1801 -2867 O ATOM 4520 N SER C 77 29.796 14.674 18.660 1.00 77.29 N ANISOU 4520 N SER C 77 8533 8170 12664 -24 -1448 -3224 N ATOM 4521 CA SER C 77 30.298 13.295 18.704 1.00 73.85 C ANISOU 4521 CA SER C 77 8252 8036 11773 -116 -1228 -2884 C ATOM 4522 C SER C 77 29.885 12.447 17.486 1.00 67.48 C ANISOU 4522 C SER C 77 7628 7132 10878 -158 -1099 -2454 C ATOM 4523 O SER C 77 29.317 11.358 17.611 1.00 56.89 O ANISOU 4523 O SER C 77 6353 6069 9195 -166 -920 -2350 O ATOM 4524 CB SER C 77 30.017 12.624 20.071 1.00 71.33 C ANISOU 4524 CB SER C 77 7841 8242 11020 -101 -1097 -3138 C ATOM 4525 OG SER C 77 28.817 11.879 20.086 1.00 67.46 O ANISOU 4525 OG SER C 77 7366 7986 10281 -73 -949 -3132 O ATOM 4526 N THR C 78 30.185 12.968 16.300 1.00 72.74 N ANISOU 4526 N THR C 78 8363 7411 11863 -195 -1204 -2200 N ATOM 4527 CA THR C 78 29.826 12.282 15.063 1.00 76.95 C ANISOU 4527 CA THR C 78 9050 7853 12335 -237 -1102 -1815 C ATOM 4528 C THR C 78 31.016 12.175 14.097 1.00 73.63 C ANISOU 4528 C THR C 78 8735 7256 11984 -350 -1115 -1414 C ATOM 4529 O THR C 78 31.862 13.061 14.016 1.00 73.80 O ANISOU 4529 O THR C 78 8700 7064 12277 -393 -1272 -1407 O ATOM 4530 CB THR C 78 28.588 12.940 14.354 1.00 76.95 C ANISOU 4530 CB THR C 78 9012 7609 12616 -170 -1201 -1884 C ATOM 4531 OG1 THR C 78 29.020 13.815 13.307 1.00 80.29 O ANISOU 4531 OG1 THR C 78 9444 7642 13421 -227 -1378 -1665 O ATOM 4532 CG2 THR C 78 27.715 13.727 15.345 1.00 71.96 C ANISOU 4532 CG2 THR C 78 8193 7022 12128 -48 -1304 -2392 C ATOM 4533 N ALA C 79 31.068 11.070 13.369 1.00 69.71 N ANISOU 4533 N ALA C 79 8376 6866 11244 -400 -950 -1094 N ATOM 4534 CA ALA C 79 32.100 10.849 12.372 1.00 71.68 C ANISOU 4534 CA ALA C 79 8709 7011 11515 -503 -935 -729 C ATOM 4535 C ALA C 79 31.526 11.040 10.956 1.00 75.17 C ANISOU 4535 C ALA C 79 9202 7253 12105 -534 -965 -481 C ATOM 4536 O ALA C 79 30.343 10.805 10.716 1.00 75.35 O ANISOU 4536 O ALA C 79 9248 7292 12089 -475 -922 -530 O ATOM 4537 CB ALA C 79 32.688 9.451 12.536 1.00 65.46 C ANISOU 4537 CB ALA C 79 8013 6495 10366 -535 -745 -565 C ATOM 4538 N TYR C 80 32.363 11.481 10.024 1.00 70.85 N ANISOU 4538 N TYR C 80 8660 6540 11718 -637 -1043 -209 N ATOM 4539 CA TYR C 80 31.929 11.683 8.652 1.00 64.57 C ANISOU 4539 CA TYR C 80 7898 5600 11037 -695 -1082 62 C ATOM 4540 C TYR C 80 32.745 10.877 7.647 1.00 64.64 C ANISOU 4540 C TYR C 80 7980 5741 10839 -797 -955 406 C ATOM 4541 O TYR C 80 33.796 10.338 7.967 1.00 67.19 O ANISOU 4541 O TYR C 80 8316 6209 11005 -829 -870 445 O ATOM 4542 CB TYR C 80 31.992 13.165 8.305 1.00 65.67 C ANISOU 4542 CB TYR C 80 7931 5406 11614 -745 -1341 93 C ATOM 4543 CG TYR C 80 31.122 14.029 9.199 1.00 68.92 C ANISOU 4543 CG TYR C 80 8240 5673 12273 -624 -1487 -286 C ATOM 4544 CD1 TYR C 80 29.750 14.108 8.996 1.00 70.00 C ANISOU 4544 CD1 TYR C 80 8369 5781 12447 -533 -1495 -391 C ATOM 4545 CD2 TYR C 80 31.666 14.761 10.244 1.00 60.48 C ANISOU 4545 CD2 TYR C 80 7064 4549 11368 -587 -1607 -557 C ATOM 4546 CE1 TYR C 80 28.950 14.890 9.808 1.00 65.08 C ANISOU 4546 CE1 TYR C 80 7623 5090 12015 -405 -1612 -758 C ATOM 4547 CE2 TYR C 80 30.872 15.543 11.055 1.00 55.55 C ANISOU 4547 CE2 TYR C 80 6316 3867 10923 -456 -1723 -935 C ATOM 4548 CZ TYR C 80 29.515 15.614 10.835 1.00 58.07 C ANISOU 4548 CZ TYR C 80 6617 4170 11276 -363 -1724 -1036 C ATOM 4549 OH TYR C 80 28.707 16.405 11.644 1.00 56.75 O ANISOU 4549 OH TYR C 80 6298 3977 11286 -223 -1836 -1429 O ATOM 4550 N ILE C 81 32.203 10.754 6.443 1.00 65.46 N ANISOU 4550 N ILE C 81 8119 5818 10933 -840 -939 630 N ATOM 4551 CA ILE C 81 32.921 10.239 5.286 1.00 62.52 C ANISOU 4551 CA ILE C 81 7774 5568 10411 -951 -855 949 C ATOM 4552 C ILE C 81 32.485 11.063 4.101 1.00 63.54 C ANISOU 4552 C ILE C 81 7861 5596 10684 -1019 -977 1166 C ATOM 4553 O ILE C 81 31.304 11.190 3.825 1.00 62.49 O ANISOU 4553 O ILE C 81 7744 5408 10590 -958 -1005 1119 O ATOM 4554 CB ILE C 81 32.587 8.758 5.006 1.00 63.82 C ANISOU 4554 CB ILE C 81 8032 5983 10232 -898 -635 963 C ATOM 4555 CG1 ILE C 81 33.355 8.241 3.782 1.00 63.45 C ANISOU 4555 CG1 ILE C 81 7983 6093 10033 -1004 -551 1240 C ATOM 4556 CG2 ILE C 81 31.090 8.561 4.820 1.00 59.96 C ANISOU 4556 CG2 ILE C 81 7588 5465 9729 -818 -617 880 C ATOM 4557 CD1 ILE C 81 33.446 6.698 3.710 1.00 52.00 C ANISOU 4557 CD1 ILE C 81 6597 4885 8277 -945 -346 1204 C ATOM 4558 N GLN C 82 33.433 11.637 3.392 1.00 69.71 N ANISOU 4558 N GLN C 82 8575 6429 11484 -1123 -1039 1385 N ATOM 4559 CA GLN C 82 33.069 12.447 2.249 1.00 69.47 C ANISOU 4559 CA GLN C 82 8482 6393 11522 -1176 -1154 1590 C ATOM 4560 C GLN C 82 33.530 11.742 0.994 1.00 77.99 C ANISOU 4560 C GLN C 82 9570 7732 12331 -1280 -1027 1853 C ATOM 4561 O GLN C 82 34.643 11.225 0.953 1.00 89.52 O ANISOU 4561 O GLN C 82 11021 9342 13651 -1345 -929 1927 O ATOM 4562 CB GLN C 82 33.717 13.809 2.347 1.00 63.31 C ANISOU 4562 CB GLN C 82 7581 5470 11004 -1225 -1364 1648 C ATOM 4563 CG GLN C 82 33.118 14.796 1.426 1.00 72.05 C ANISOU 4563 CG GLN C 82 8604 6506 12266 -1259 -1537 1818 C ATOM 4564 CD GLN C 82 33.933 16.049 1.366 1.00 82.05 C ANISOU 4564 CD GLN C 82 9738 7660 13779 -1331 -1747 1941 C ATOM 4565 OE1 GLN C 82 35.156 15.990 1.253 1.00 85.90 O ANISOU 4565 OE1 GLN C 82 10196 8253 14190 -1425 -1715 2073 O ATOM 4566 NE2 GLN C 82 33.269 17.201 1.452 1.00 83.01 N ANISOU 4566 NE2 GLN C 82 9762 7562 14216 -1285 -1973 1897 N ATOM 4567 N LEU C 83 32.682 11.691 -0.026 1.00 69.31 N ANISOU 4567 N LEU C 83 8476 6705 11156 -1294 -1029 1978 N ATOM 4568 CA LEU C 83 33.077 11.012 -1.252 1.00 61.64 C ANISOU 4568 CA LEU C 83 7492 6014 9915 -1393 -911 2198 C ATOM 4569 C LEU C 83 33.137 11.983 -2.415 1.00 68.69 C ANISOU 4569 C LEU C 83 8274 6965 10862 -1508 -1063 2462 C ATOM 4570 O LEU C 83 32.270 12.830 -2.584 1.00 77.90 O ANISOU 4570 O LEU C 83 9407 7973 12221 -1486 -1225 2483 O ATOM 4571 CB LEU C 83 32.182 9.809 -1.519 1.00 52.66 C ANISOU 4571 CB LEU C 83 6450 4986 8573 -1330 -749 2128 C ATOM 4572 CG LEU C 83 32.119 8.901 -0.275 1.00 57.30 C ANISOU 4572 CG LEU C 83 7131 5502 9139 -1223 -629 1886 C ATOM 4573 CD1 LEU C 83 30.722 8.376 -0.076 1.00 68.99 C ANISOU 4573 CD1 LEU C 83 8695 6911 10606 -1117 -586 1747 C ATOM 4574 CD2 LEU C 83 33.096 7.750 -0.300 1.00 47.34 C ANISOU 4574 CD2 LEU C 83 5879 4446 7663 -1257 -456 1911 C ATOM 4575 N ASN C 84A 34.196 11.870 -3.200 1.00 70.39 N ANISOU 4575 N ASN C 84A 8412 7418 10915 -1636 -1020 2665 N ATOM 4576 CA ASN C 84A 34.521 12.880 -4.190 1.00 77.04 C ANISOU 4576 CA ASN C 84A 9121 8332 11818 -1769 -1187 2941 C ATOM 4577 C ASN C 84A 34.508 12.313 -5.600 1.00 79.05 C ANISOU 4577 C ASN C 84A 9328 8933 11776 -1875 -1097 3143 C ATOM 4578 O ASN C 84A 34.699 11.117 -5.804 1.00 73.73 O ANISOU 4578 O ASN C 84A 8699 8481 10835 -1863 -889 3075 O ATOM 4579 CB ASN C 84A 35.881 13.493 -3.864 1.00 83.66 C ANISOU 4579 CB ASN C 84A 9872 9161 12754 -1848 -1258 3021 C ATOM 4580 CG ASN C 84A 36.030 13.806 -2.381 1.00 92.92 C ANISOU 4580 CG ASN C 84A 11094 10044 14167 -1740 -1306 2777 C ATOM 4581 OD1 ASN C 84A 37.072 13.541 -1.767 1.00 91.41 O ANISOU 4581 OD1 ASN C 84A 10902 9883 13948 -1752 -1238 2715 O ATOM 4582 ND2 ASN C 84A 34.970 14.356 -1.792 1.00 96.93 N ANISOU 4582 ND2 ASN C 84A 11633 10285 14910 -1633 -1426 2620 N ATOM 4583 N SER C 85B 34.253 13.178 -6.571 1.00 83.24 N ANISOU 4583 N SER C 85B 9750 9514 12362 -1979 -1268 3386 N ATOM 4584 CA SER C 85B 34.221 12.759 -7.960 1.00 81.83 C ANISOU 4584 CA SER C 85B 9499 9694 11897 -2095 -1210 3588 C ATOM 4585 C SER C 85B 33.383 11.509 -8.164 1.00 85.74 C ANISOU 4585 C SER C 85B 10100 10312 12164 -2012 -1016 3435 C ATOM 4586 O SER C 85B 33.781 10.618 -8.911 1.00 98.79 O ANISOU 4586 O SER C 85B 11717 12312 13507 -2071 -857 3471 O ATOM 4587 CB SER C 85B 35.637 12.490 -8.448 1.00 71.63 C ANISOU 4587 CB SER C 85B 8104 8726 10387 -2221 -1122 3716 C ATOM 4588 OG SER C 85B 36.308 13.699 -8.724 1.00 72.53 O ANISOU 4588 OG SER C 85B 8081 8813 10664 -2346 -1331 3955 O ATOM 4589 N LEU C 86C 32.226 11.451 -7.512 1.00 70.06 N ANISOU 4589 N LEU C 86C 8228 8058 10334 -1877 -1035 3258 N ATOM 4590 CA LEU C 86C 31.372 10.268 -7.536 1.00 62.10 C ANISOU 4590 CA LEU C 86C 7329 7116 9149 -1784 -863 3099 C ATOM 4591 C LEU C 86C 30.983 9.756 -8.944 1.00 70.99 C ANISOU 4591 C LEU C 86C 8398 8577 9998 -1873 -808 3251 C ATOM 4592 O LEU C 86C 30.733 10.541 -9.857 1.00 74.63 O ANISOU 4592 O LEU C 86C 8757 9117 10482 -1978 -963 3473 O ATOM 4593 CB LEU C 86C 30.119 10.545 -6.722 1.00 58.69 C ANISOU 4593 CB LEU C 86C 6996 6347 8956 -1644 -939 2923 C ATOM 4594 CG LEU C 86C 30.238 10.704 -5.214 1.00 53.44 C ANISOU 4594 CG LEU C 86C 6404 5394 8506 -1523 -945 2685 C ATOM 4595 CD1 LEU C 86C 29.002 11.378 -4.686 1.00 59.12 C ANISOU 4595 CD1 LEU C 86C 7151 5825 9487 -1420 -1084 2561 C ATOM 4596 CD2 LEU C 86C 30.420 9.356 -4.550 1.00 49.67 C ANISOU 4596 CD2 LEU C 86C 6033 4983 7857 -1441 -726 2490 C ATOM 4597 N THR C 87 30.938 8.426 -9.084 1.00 72.42 N ANISOU 4597 N THR C 87 8631 8961 9925 -1833 -597 3124 N ATOM 4598 CA THR C 87 30.561 7.707 -10.309 1.00 71.57 C ANISOU 4598 CA THR C 87 8469 9202 9521 -1896 -510 3197 C ATOM 4599 C THR C 87 29.606 6.584 -9.910 1.00 72.42 C ANISOU 4599 C THR C 87 8705 9237 9572 -1764 -372 2985 C ATOM 4600 O THR C 87 29.439 6.309 -8.729 1.00 71.42 O ANISOU 4600 O THR C 87 8692 8840 9603 -1643 -331 2801 O ATOM 4601 CB THR C 87 31.777 7.027 -10.991 1.00 63.38 C ANISOU 4601 CB THR C 87 7310 8596 8176 -1994 -362 3230 C ATOM 4602 OG1 THR C 87 32.270 5.973 -10.154 1.00 67.69 O ANISOU 4602 OG1 THR C 87 7919 9128 8672 -1901 -179 3008 O ATOM 4603 CG2 THR C 87 32.896 8.006 -11.257 1.00 56.11 C ANISOU 4603 CG2 THR C 87 6259 7761 7298 -2124 -478 3426 C ATOM 4604 N SER C 88 28.975 5.923 -10.877 1.00 78.35 N ANISOU 4604 N SER C 88 9430 10243 10098 -1793 -306 3008 N ATOM 4605 CA SER C 88 28.016 4.857 -10.539 1.00 72.89 C ANISOU 4605 CA SER C 88 8850 9482 9363 -1676 -189 2824 C ATOM 4606 C SER C 88 28.640 3.744 -9.695 1.00 77.08 C ANISOU 4606 C SER C 88 9430 10018 9839 -1567 -12 2574 C ATOM 4607 O SER C 88 27.955 3.118 -8.880 1.00 76.23 O ANISOU 4607 O SER C 88 9443 9700 9822 -1395 36 2327 O ATOM 4608 CB SER C 88 27.339 4.275 -11.791 1.00 65.16 C ANISOU 4608 CB SER C 88 7812 8827 8119 -1731 -142 2875 C ATOM 4609 OG SER C 88 28.281 3.897 -12.787 1.00 71.49 O ANISOU 4609 OG SER C 88 8456 10094 8614 -1844 -50 2924 O ATOM 4610 N GLU C 89 29.939 3.512 -9.885 1.00 76.85 N ANISOU 4610 N GLU C 89 9296 10234 9669 -1632 72 2580 N ATOM 4611 CA GLU C 89 30.636 2.427 -9.211 1.00 71.43 C ANISOU 4611 CA GLU C 89 8629 9578 8932 -1491 221 2280 C ATOM 4612 C GLU C 89 30.676 2.680 -7.707 1.00 71.77 C ANISOU 4612 C GLU C 89 8799 9228 9242 -1381 178 2173 C ATOM 4613 O GLU C 89 31.017 1.797 -6.924 1.00 71.57 O ANISOU 4613 O GLU C 89 8819 9150 9225 -1250 272 1934 O ATOM 4614 CB GLU C 89 32.044 2.244 -9.791 1.00 74.47 C ANISOU 4614 CB GLU C 89 8848 10323 9123 -1594 304 2320 C ATOM 4615 CG GLU C 89 32.072 1.483 -11.119 1.00 89.36 C ANISOU 4615 CG GLU C 89 10591 12673 10687 -1639 408 2261 C ATOM 4616 CD GLU C 89 32.511 2.341 -12.316 1.00105.76 C ANISOU 4616 CD GLU C 89 12495 15116 12574 -1886 354 2599 C ATOM 4617 OE1 GLU C 89 33.694 2.763 -12.359 1.00109.25 O ANISOU 4617 OE1 GLU C 89 12827 15694 12988 -1979 351 2693 O ATOM 4618 OE2 GLU C 89 31.675 2.578 -13.223 1.00108.25 O ANISOU 4618 OE2 GLU C 89 12785 15565 12779 -1954 292 2724 O ATOM 4619 N ASP C 90 30.309 3.893 -7.309 1.00 70.34 N ANISOU 4619 N ASP C 90 8659 8778 9290 -1439 21 2345 N ATOM 4620 CA ASP C 90 30.281 4.267 -5.900 1.00 62.37 C ANISOU 4620 CA ASP C 90 7745 7424 8528 -1343 -35 2226 C ATOM 4621 C ASP C 90 28.920 4.041 -5.254 1.00 59.85 C ANISOU 4621 C ASP C 90 7547 6872 8319 -1201 -52 2056 C ATOM 4622 O ASP C 90 28.783 4.174 -4.044 1.00 61.64 O ANISOU 4622 O ASP C 90 7843 6870 8705 -1106 -75 1907 O ATOM 4623 CB ASP C 90 30.722 5.723 -5.728 1.00 63.27 C ANISOU 4623 CB ASP C 90 7812 7371 8856 -1449 -208 2419 C ATOM 4624 CG ASP C 90 32.202 5.910 -5.991 1.00 71.96 C ANISOU 4624 CG ASP C 90 8802 8667 9874 -1557 -185 2524 C ATOM 4625 OD1 ASP C 90 32.975 5.053 -5.526 1.00 81.74 O ANISOU 4625 OD1 ASP C 90 10038 9997 11023 -1519 -52 2401 O ATOM 4626 OD2 ASP C 90 32.598 6.892 -6.659 1.00 68.72 O ANISOU 4626 OD2 ASP C 90 8296 8328 9485 -1664 -304 2707 O ATOM 4627 N SER C 91 27.920 3.683 -6.057 1.00 61.80 N ANISOU 4627 N SER C 91 7806 7210 8467 -1191 -38 2071 N ATOM 4628 CA SER C 91 26.578 3.430 -5.541 1.00 56.48 C ANISOU 4628 CA SER C 91 7230 6346 7883 -1065 -49 1918 C ATOM 4629 C SER C 91 26.604 2.155 -4.723 1.00 56.42 C ANISOU 4629 C SER C 91 7287 6352 7799 -922 91 1652 C ATOM 4630 O SER C 91 26.941 1.076 -5.222 1.00 61.68 O ANISOU 4630 O SER C 91 7925 7228 8283 -898 205 1570 O ATOM 4631 CB SER C 91 25.602 3.271 -6.692 1.00 59.49 C ANISOU 4631 CB SER C 91 7595 6854 8156 -1099 -64 2007 C ATOM 4632 OG SER C 91 25.907 4.180 -7.736 1.00 75.06 O ANISOU 4632 OG SER C 91 9469 8943 10108 -1272 -171 2305 O ATOM 4633 N ALA C 92 26.261 2.288 -3.451 1.00 51.11 N ANISOU 4633 N ALA C 92 6683 5461 7276 -831 68 1514 N ATOM 4634 CA ALA C 92 26.378 1.184 -2.517 1.00 48.65 C ANISOU 4634 CA ALA C 92 6420 5153 6913 -721 173 1311 C ATOM 4635 C ALA C 92 25.762 1.603 -1.211 1.00 51.04 C ANISOU 4635 C ALA C 92 6776 5252 7366 -650 123 1194 C ATOM 4636 O ALA C 92 25.213 2.698 -1.092 1.00 57.10 O ANISOU 4636 O ALA C 92 7537 5867 8290 -668 10 1232 O ATOM 4637 CB ALA C 92 27.830 0.801 -2.315 1.00 49.26 C ANISOU 4637 CB ALA C 92 6452 5339 6926 -744 232 1302 C ATOM 4638 N VAL C 93 25.836 0.719 -0.231 1.00 46.67 N ANISOU 4638 N VAL C 93 6256 4708 6769 -572 196 1046 N ATOM 4639 CA VAL C 93 25.489 1.089 1.125 1.00 53.34 C ANISOU 4639 CA VAL C 93 7123 5435 7710 -521 162 923 C ATOM 4640 C VAL C 93 26.777 1.218 1.939 1.00 59.27 C ANISOU 4640 C VAL C 93 7851 6196 8474 -539 161 904 C ATOM 4641 O VAL C 93 27.572 0.279 2.004 1.00 66.30 O ANISOU 4641 O VAL C 93 8736 7190 9267 -533 235 901 O ATOM 4642 CB VAL C 93 24.546 0.043 1.752 1.00 50.94 C ANISOU 4642 CB VAL C 93 6857 5163 7335 -442 229 800 C ATOM 4643 CG1 VAL C 93 24.293 0.342 3.234 1.00 40.63 C ANISOU 4643 CG1 VAL C 93 5546 3816 6074 -403 208 666 C ATOM 4644 CG2 VAL C 93 23.243 -0.013 0.967 1.00 54.73 C ANISOU 4644 CG2 VAL C 93 7354 5625 7817 -423 221 812 C ATOM 4645 N TYR C 94 26.983 2.380 2.552 1.00 49.81 N ANISOU 4645 N TYR C 94 6628 4881 7419 -558 66 878 N ATOM 4646 CA TYR C 94 28.135 2.602 3.417 1.00 46.62 C ANISOU 4646 CA TYR C 94 6196 4478 7039 -575 51 842 C ATOM 4647 C TYR C 94 27.740 2.483 4.877 1.00 50.52 C ANISOU 4647 C TYR C 94 6696 4973 7527 -510 54 657 C ATOM 4648 O TYR C 94 26.781 3.106 5.309 1.00 54.42 O ANISOU 4648 O TYR C 94 7177 5393 8106 -472 -1 542 O ATOM 4649 CB TYR C 94 28.732 3.976 3.121 1.00 51.04 C ANISOU 4649 CB TYR C 94 6704 4917 7773 -652 -73 934 C ATOM 4650 CG TYR C 94 29.193 4.070 1.690 1.00 58.18 C ANISOU 4650 CG TYR C 94 7579 5884 8641 -745 -74 1151 C ATOM 4651 CD1 TYR C 94 30.531 3.954 1.366 1.00 58.81 C ANISOU 4651 CD1 TYR C 94 7613 6070 8663 -817 -45 1255 C ATOM 4652 CD2 TYR C 94 28.280 4.209 0.656 1.00 65.35 C ANISOU 4652 CD2 TYR C 94 8493 6788 9549 -767 -98 1249 C ATOM 4653 CE1 TYR C 94 30.949 4.011 0.056 1.00 67.08 C ANISOU 4653 CE1 TYR C 94 8608 7242 9638 -914 -34 1445 C ATOM 4654 CE2 TYR C 94 28.690 4.261 -0.664 1.00 68.70 C ANISOU 4654 CE2 TYR C 94 8871 7333 9897 -868 -95 1453 C ATOM 4655 CZ TYR C 94 30.025 4.162 -0.958 1.00 70.09 C ANISOU 4655 CZ TYR C 94 8990 7643 9999 -944 -59 1548 C ATOM 4656 OH TYR C 94 30.450 4.209 -2.266 1.00 73.29 O ANISOU 4656 OH TYR C 94 9324 8231 10293 -1057 -47 1743 O ATOM 4657 N TYR C 95 28.469 1.663 5.628 1.00 58.20 N ANISOU 4657 N TYR C 95 7670 6051 8392 -501 114 628 N ATOM 4658 CA TYR C 95 28.230 1.502 7.066 1.00 62.79 C ANISOU 4658 CA TYR C 95 8237 6696 8925 -464 116 480 C ATOM 4659 C TYR C 95 29.316 2.153 7.882 1.00 59.18 C ANISOU 4659 C TYR C 95 7734 6233 8518 -492 58 429 C ATOM 4660 O TYR C 95 30.463 2.186 7.469 1.00 63.12 O ANISOU 4660 O TYR C 95 8224 6719 9041 -536 52 533 O ATOM 4661 CB TYR C 95 28.244 0.034 7.467 1.00 65.82 C ANISOU 4661 CB TYR C 95 8641 7212 9156 -449 200 511 C ATOM 4662 CG TYR C 95 27.152 -0.802 6.883 1.00 63.74 C ANISOU 4662 CG TYR C 95 8413 6965 8840 -419 254 541 C ATOM 4663 CD1 TYR C 95 25.974 -1.030 7.586 1.00 63.95 C ANISOU 4663 CD1 TYR C 95 8434 7052 8813 -393 268 457 C ATOM 4664 CD2 TYR C 95 27.306 -1.381 5.640 1.00 56.90 C ANISOU 4664 CD2 TYR C 95 7569 6080 7970 -423 291 640 C ATOM 4665 CE1 TYR C 95 24.979 -1.810 7.056 1.00 66.79 C ANISOU 4665 CE1 TYR C 95 8820 7420 9136 -372 310 491 C ATOM 4666 CE2 TYR C 95 26.319 -2.153 5.095 1.00 62.88 C ANISOU 4666 CE2 TYR C 95 8352 6849 8690 -395 330 651 C ATOM 4667 CZ TYR C 95 25.155 -2.375 5.803 1.00 69.12 C ANISOU 4667 CZ TYR C 95 9148 7668 9448 -370 336 586 C ATOM 4668 OH TYR C 95 24.167 -3.162 5.247 1.00 69.20 O ANISOU 4668 OH TYR C 95 9177 7681 9433 -348 369 604 O ATOM 4669 N CYS C 96 28.965 2.662 9.051 1.00 56.55 N ANISOU 4669 N CYS C 96 7358 5934 8194 -466 15 254 N ATOM 4670 CA CYS C 96 29.990 2.923 10.048 1.00 57.87 C ANISOU 4670 CA CYS C 96 7479 6160 8350 -488 -23 187 C ATOM 4671 C CYS C 96 29.976 1.793 11.064 1.00 60.15 C ANISOU 4671 C CYS C 96 7763 6655 8438 -485 43 174 C ATOM 4672 O CYS C 96 28.931 1.275 11.434 1.00 63.34 O ANISOU 4672 O CYS C 96 8166 7162 8738 -462 87 127 O ATOM 4673 CB CYS C 96 29.841 4.291 10.730 1.00 49.95 C ANISOU 4673 CB CYS C 96 6401 5081 7497 -471 -135 -19 C ATOM 4674 SG CYS C 96 28.259 4.583 11.539 1.00113.98 S ANISOU 4674 SG CYS C 96 14453 13275 15579 -399 -142 -278 S ATOM 4675 N ALA C 97 31.161 1.395 11.482 1.00 61.41 N ANISOU 4675 N ALA C 97 7909 6875 8549 -519 41 240 N ATOM 4676 CA ALA C 97 31.305 0.395 12.509 1.00 63.26 C ANISOU 4676 CA ALA C 97 8122 7299 8615 -536 70 264 C ATOM 4677 C ALA C 97 32.260 0.958 13.535 1.00 59.11 C ANISOU 4677 C ALA C 97 7533 6850 8076 -565 6 176 C ATOM 4678 O ALA C 97 33.217 1.677 13.185 1.00 51.91 O ANISOU 4678 O ALA C 97 6612 5818 7293 -579 -42 180 O ATOM 4679 CB ALA C 97 31.863 -0.881 11.916 1.00 66.85 C ANISOU 4679 CB ALA C 97 8614 7741 9044 -546 115 456 C ATOM 4680 N ARG C 98 31.990 0.655 14.799 1.00 54.89 N ANISOU 4680 N ARG C 98 6941 6536 7378 -584 2 101 N ATOM 4681 CA ARG C 98 32.911 1.036 15.855 1.00 58.94 C ANISOU 4681 CA ARG C 98 7384 7171 7841 -618 -59 21 C ATOM 4682 C ARG C 98 33.895 -0.077 16.164 1.00 55.26 C ANISOU 4682 C ARG C 98 6921 6786 7291 -666 -59 220 C ATOM 4683 O ARG C 98 33.495 -1.189 16.482 1.00 58.69 O ANISOU 4683 O ARG C 98 7355 7345 7602 -691 -32 350 O ATOM 4684 CB ARG C 98 32.176 1.421 17.127 1.00 63.05 C ANISOU 4684 CB ARG C 98 7808 7942 8207 -623 -76 -193 C ATOM 4685 CG ARG C 98 33.107 2.056 18.134 1.00 69.53 C ANISOU 4685 CG ARG C 98 8543 8880 8995 -651 -152 -331 C ATOM 4686 CD ARG C 98 32.407 2.347 19.432 1.00 74.92 C ANISOU 4686 CD ARG C 98 9104 9883 9481 -662 -163 -564 C ATOM 4687 NE ARG C 98 32.076 1.129 20.154 1.00 76.49 N ANISOU 4687 NE ARG C 98 9274 10378 9412 -733 -116 -399 N ATOM 4688 CZ ARG C 98 31.742 1.109 21.438 1.00 81.22 C ANISOU 4688 CZ ARG C 98 9744 11355 9760 -785 -123 -525 C ATOM 4689 NH1 ARG C 98 31.702 2.239 22.129 1.00 84.51 N ANISOU 4689 NH1 ARG C 98 10049 11897 10166 -754 -171 -865 N ATOM 4690 NH2 ARG C 98 31.453 -0.035 22.031 1.00 81.69 N ANISOU 4690 NH2 ARG C 98 9772 11681 9587 -873 -95 -313 N ATOM 4691 N GLU C 99 35.183 0.228 16.073 1.00 50.96 N ANISOU 4691 N GLU C 99 6366 6160 6838 -681 -104 252 N ATOM 4692 CA GLU C 99 36.223 -0.753 16.342 1.00 55.23 C ANISOU 4692 CA GLU C 99 6893 6752 7339 -717 -122 426 C ATOM 4693 C GLU C 99 36.370 -0.911 17.856 1.00 66.85 C ANISOU 4693 C GLU C 99 8283 8491 8626 -773 -176 390 C ATOM 4694 O GLU C 99 35.995 -0.016 18.600 1.00 76.22 O ANISOU 4694 O GLU C 99 9414 9805 9742 -777 -200 185 O ATOM 4695 CB GLU C 99 37.529 -0.313 15.675 1.00 53.43 C ANISOU 4695 CB GLU C 99 6667 6362 7271 -717 -148 461 C ATOM 4696 CG GLU C 99 38.653 -1.327 15.731 1.00 65.55 C ANISOU 4696 CG GLU C 99 8179 7913 8815 -736 -168 626 C ATOM 4697 CD GLU C 99 39.989 -0.769 15.237 1.00 74.84 C ANISOU 4697 CD GLU C 99 9328 8979 10127 -745 -195 633 C ATOM 4698 OE1 GLU C 99 41.041 -1.172 15.781 1.00 76.82 O ANISOU 4698 OE1 GLU C 99 9527 9287 10373 -770 -245 696 O ATOM 4699 OE2 GLU C 99 39.989 0.065 14.306 1.00 75.92 O ANISOU 4699 OE2 GLU C 99 9486 8981 10378 -737 -173 594 O ATOM 4700 N GLY C 100 36.921 -2.032 18.315 1.00 68.22 N ANISOU 4700 N GLY C 100 8432 8758 8730 -818 -206 582 N ATOM 4701 CA GLY C 100 37.053 -2.288 19.740 1.00 64.42 C ANISOU 4701 CA GLY C 100 7861 8567 8047 -894 -267 601 C ATOM 4702 C GLY C 100 38.337 -3.056 19.966 1.00 72.99 C ANISOU 4702 C GLY C 100 8919 9634 9178 -931 -340 793 C ATOM 4703 O GLY C 100 38.804 -3.782 19.095 1.00 76.54 O ANISOU 4703 O GLY C 100 9410 9883 9789 -897 -335 936 O ATOM 4704 N ASN C 101 38.893 -2.909 21.162 1.00 76.64 N ANISOU 4704 N ASN C 101 9295 10327 9497 -998 -416 780 N ATOM 4705 CA ASN C 101 40.305 -3.171 21.406 1.00 68.34 C ANISOU 4705 CA ASN C 101 8207 9243 8517 -1023 -499 887 C ATOM 4706 C ASN C 101 40.531 -3.761 22.760 1.00 72.02 C ANISOU 4706 C ASN C 101 8573 10012 8778 -1127 -594 1022 C ATOM 4707 O ASN C 101 39.979 -3.273 23.733 1.00 76.85 O ANISOU 4707 O ASN C 101 9119 10920 9163 -1181 -599 897 O ATOM 4708 CB ASN C 101 41.066 -1.855 21.413 1.00 68.15 C ANISOU 4708 CB ASN C 101 8167 9162 8564 -999 -514 668 C ATOM 4709 CG ASN C 101 41.666 -1.522 20.077 1.00 81.25 C ANISOU 4709 CG ASN C 101 9892 10507 10474 -931 -473 661 C ATOM 4710 OD1 ASN C 101 42.889 -1.364 19.954 1.00 86.80 O ANISOU 4710 OD1 ASN C 101 10566 11128 11286 -935 -518 689 O ATOM 4711 ND2 ASN C 101 40.810 -1.403 19.054 1.00 79.70 N ANISOU 4711 ND2 ASN C 101 9770 10156 10357 -877 -389 630 N ATOM 4712 N TYR C 102 41.364 -4.790 22.844 1.00 68.54 N ANISOU 4712 N TYR C 102 8104 9517 8420 -1159 -680 1269 N ATOM 4713 CA TYR C 102 41.928 -5.163 24.128 1.00 62.52 C ANISOU 4713 CA TYR C 102 7235 9028 7493 -1267 -801 1406 C ATOM 4714 C TYR C 102 43.180 -5.979 23.918 1.00 66.36 C ANISOU 4714 C TYR C 102 7697 9336 8182 -1261 -904 1613 C ATOM 4715 O TYR C 102 43.435 -6.417 22.800 1.00 66.60 O ANISOU 4715 O TYR C 102 7782 9062 8459 -1176 -873 1651 O ATOM 4716 CB TYR C 102 40.908 -5.883 24.988 1.00 65.56 C ANISOU 4716 CB TYR C 102 7558 9712 7640 -1375 -831 1575 C ATOM 4717 CG TYR C 102 40.624 -7.299 24.589 1.00 69.77 C ANISOU 4717 CG TYR C 102 8103 10096 8310 -1396 -883 1887 C ATOM 4718 CD1 TYR C 102 39.627 -7.603 23.681 1.00 66.57 C ANISOU 4718 CD1 TYR C 102 7776 9515 8003 -1336 -794 1878 C ATOM 4719 CD2 TYR C 102 41.337 -8.341 25.157 1.00 80.11 C ANISOU 4719 CD2 TYR C 102 9331 11439 9669 -1480 -1043 2194 C ATOM 4720 CE1 TYR C 102 39.359 -8.916 23.335 1.00 73.19 C ANISOU 4720 CE1 TYR C 102 8610 10204 8995 -1355 -862 2147 C ATOM 4721 CE2 TYR C 102 41.081 -9.642 24.821 1.00 82.57 C ANISOU 4721 CE2 TYR C 102 9633 11584 10155 -1499 -1124 2475 C ATOM 4722 CZ TYR C 102 40.093 -9.933 23.912 1.00 77.24 C ANISOU 4722 CZ TYR C 102 9035 10728 9585 -1435 -1033 2442 C ATOM 4723 OH TYR C 102 39.859 -11.253 23.597 1.00 75.71 O ANISOU 4723 OH TYR C 102 8818 10352 9597 -1454 -1135 2709 O ATOM 4724 N TYR C 103 43.965 -6.143 24.987 1.00 66.11 N ANISOU 4724 N TYR C 103 7568 9510 8042 -1350 -1028 1723 N ATOM 4725 CA TYR C 103 45.233 -6.881 24.980 1.00 54.23 C ANISOU 4725 CA TYR C 103 6011 7866 6727 -1352 -1154 1916 C ATOM 4726 C TYR C 103 45.073 -8.326 25.461 1.00 67.62 C ANISOU 4726 C TYR C 103 7638 9609 8445 -1438 -1295 2275 C ATOM 4727 O TYR C 103 44.684 -8.572 26.597 1.00 78.93 O ANISOU 4727 O TYR C 103 8991 11371 9629 -1572 -1375 2429 O ATOM 4728 CB TYR C 103 46.219 -6.146 25.866 1.00 59.28 C ANISOU 4728 CB TYR C 103 6577 8694 7253 -1402 -1225 1826 C ATOM 4729 CG TYR C 103 47.594 -6.766 25.998 1.00 66.72 C ANISOU 4729 CG TYR C 103 7449 9528 8373 -1410 -1365 2002 C ATOM 4730 CD1 TYR C 103 47.930 -7.578 27.100 1.00 62.16 C ANISOU 4730 CD1 TYR C 103 6761 9166 7693 -1531 -1539 2280 C ATOM 4731 CD2 TYR C 103 48.575 -6.503 25.050 1.00 65.82 C ANISOU 4731 CD2 TYR C 103 7361 9125 8524 -1306 -1333 1897 C ATOM 4732 CE1 TYR C 103 49.193 -8.131 27.217 1.00 56.70 C ANISOU 4732 CE1 TYR C 103 5994 8358 7191 -1531 -1683 2437 C ATOM 4733 CE2 TYR C 103 49.837 -7.048 25.162 1.00 65.89 C ANISOU 4733 CE2 TYR C 103 7287 9041 8706 -1304 -1459 2032 C ATOM 4734 CZ TYR C 103 50.145 -7.859 26.241 1.00 63.24 C ANISOU 4734 CZ TYR C 103 6849 8881 8296 -1409 -1638 2295 C ATOM 4735 OH TYR C 103 51.421 -8.379 26.313 1.00 65.16 O ANISOU 4735 OH TYR C 103 7004 9008 8746 -1397 -1775 2419 O ATOM 4736 N ASP C 104 45.319 -9.267 24.553 1.00 76.06 N ANISOU 4736 N ASP C 104 8725 10355 9820 -1363 -1330 2399 N ATOM 4737 CA ASP C 104 45.313 -10.704 24.812 1.00 81.99 C ANISOU 4737 CA ASP C 104 9400 11039 10715 -1422 -1499 2739 C ATOM 4738 C ASP C 104 46.741 -11.183 24.995 1.00 86.63 C ANISOU 4738 C ASP C 104 9896 11504 11517 -1413 -1660 2861 C ATOM 4739 O ASP C 104 46.994 -12.372 25.155 1.00 93.28 O ANISOU 4739 O ASP C 104 10653 12226 12562 -1445 -1838 3136 O ATOM 4740 CB ASP C 104 44.730 -11.425 23.600 1.00 93.03 C ANISOU 4740 CB ASP C 104 10855 12118 12373 -1320 -1449 2737 C ATOM 4741 CG ASP C 104 43.502 -12.239 23.935 1.00110.69 C ANISOU 4741 CG ASP C 104 13077 14442 14537 -1413 -1498 2962 C ATOM 4742 OD1 ASP C 104 43.363 -12.656 25.109 1.00123.29 O ANISOU 4742 OD1 ASP C 104 14581 16301 15964 -1570 -1633 3227 O ATOM 4743 OD2 ASP C 104 42.680 -12.470 23.017 1.00108.54 O ANISOU 4743 OD2 ASP C 104 12875 13992 14372 -1339 -1406 2886 O ATOM 4744 N GLY C 105 47.660 -10.224 24.953 1.00 84.59 N ANISOU 4744 N GLY C 105 9645 11263 11233 -1366 -1605 2650 N ATOM 4745 CA GLY C 105 49.081 -10.410 24.691 1.00 76.71 C ANISOU 4745 CA GLY C 105 8581 10081 10484 -1304 -1692 2648 C ATOM 4746 C GLY C 105 49.301 -9.995 23.238 1.00 77.31 C ANISOU 4746 C GLY C 105 8729 9884 10763 -1150 -1533 2389 C ATOM 4747 O GLY C 105 50.342 -9.447 22.870 1.00 72.01 O ANISOU 4747 O GLY C 105 8033 9136 10189 -1093 -1504 2244 O ATOM 4748 N GLY C 106 48.262 -10.183 22.425 1.00 78.52 N ANISOU 4748 N GLY C 106 8962 9926 10946 -1097 -1422 2330 N ATOM 4749 CA GLY C 106 48.171 -9.585 21.104 1.00 69.51 C ANISOU 4749 CA GLY C 106 7899 8616 9896 -981 -1246 2082 C ATOM 4750 C GLY C 106 47.129 -8.490 21.150 1.00 68.85 C ANISOU 4750 C GLY C 106 7923 8680 9558 -1009 -1099 1926 C ATOM 4751 O GLY C 106 46.334 -8.443 22.079 1.00 70.93 O ANISOU 4751 O GLY C 106 8193 9159 9600 -1100 -1125 2004 O ATOM 4752 N SER C 107 47.074 -7.648 20.127 1.00 66.25 N ANISOU 4752 N SER C 107 7662 8245 9266 -935 -952 1713 N ATOM 4753 CA SER C 107 46.107 -6.568 20.129 1.00 62.31 C ANISOU 4753 CA SER C 107 7251 7846 8577 -952 -835 1556 C ATOM 4754 C SER C 107 44.879 -7.101 19.451 1.00 68.32 C ANISOU 4754 C SER C 107 8078 8525 9354 -915 -763 1577 C ATOM 4755 O SER C 107 44.865 -7.235 18.233 1.00 84.88 O ANISOU 4755 O SER C 107 10207 10440 11605 -833 -685 1510 O ATOM 4756 CB SER C 107 46.633 -5.403 19.293 1.00 66.25 C ANISOU 4756 CB SER C 107 7781 8247 9145 -904 -737 1356 C ATOM 4757 OG SER C 107 47.849 -4.896 19.815 1.00 75.65 O ANISOU 4757 OG SER C 107 8903 9488 10353 -935 -806 1329 O ATOM 4758 N VAL C 108 43.827 -7.366 20.218 1.00 62.93 N ANISOU 4758 N VAL C 108 7408 8006 8498 -981 -783 1662 N ATOM 4759 CA VAL C 108 42.583 -7.879 19.645 1.00 57.36 C ANISOU 4759 CA VAL C 108 6760 7233 7801 -956 -721 1691 C ATOM 4760 C VAL C 108 41.702 -6.724 19.116 1.00 61.31 C ANISOU 4760 C VAL C 108 7350 7744 8201 -921 -575 1471 C ATOM 4761 O VAL C 108 41.499 -5.705 19.796 1.00 59.61 O ANISOU 4761 O VAL C 108 7134 7699 7815 -960 -555 1340 O ATOM 4762 CB VAL C 108 41.830 -8.744 20.673 1.00 55.07 C ANISOU 4762 CB VAL C 108 6423 7123 7380 -1059 -815 1911 C ATOM 4763 CG1 VAL C 108 40.593 -9.372 20.060 1.00 52.09 C ANISOU 4763 CG1 VAL C 108 6094 6656 7043 -1036 -765 1959 C ATOM 4764 CG2 VAL C 108 42.751 -9.810 21.221 1.00 54.18 C ANISOU 4764 CG2 VAL C 108 6209 6980 7398 -1104 -992 2154 C ATOM 4765 N ARG C 109 41.222 -6.866 17.881 1.00 63.64 N ANISOU 4765 N ARG C 109 7706 7854 8619 -844 -488 1415 N ATOM 4766 CA ARG C 109 40.334 -5.870 17.277 1.00 56.44 C ANISOU 4766 CA ARG C 109 6874 6924 7648 -811 -371 1241 C ATOM 4767 C ARG C 109 39.121 -6.571 16.687 1.00 58.68 C ANISOU 4767 C ARG C 109 7205 7145 7948 -784 -323 1289 C ATOM 4768 O ARG C 109 39.205 -7.723 16.262 1.00 55.46 O ANISOU 4768 O ARG C 109 6776 6624 7674 -759 -362 1409 O ATOM 4769 CB ARG C 109 41.042 -5.069 16.186 1.00 43.99 C ANISOU 4769 CB ARG C 109 5320 5194 6199 -755 -308 1117 C ATOM 4770 CG ARG C 109 42.464 -4.682 16.506 1.00 52.79 C ANISOU 4770 CG ARG C 109 6372 6317 7368 -773 -365 1107 C ATOM 4771 CD ARG C 109 43.052 -3.721 15.476 1.00 63.09 C ANISOU 4771 CD ARG C 109 7687 7508 8775 -746 -303 1001 C ATOM 4772 NE ARG C 109 44.438 -3.367 15.767 1.00 75.58 N ANISOU 4772 NE ARG C 109 9198 9100 10418 -771 -359 999 N ATOM 4773 CZ ARG C 109 44.797 -2.335 16.528 1.00 99.41 C ANISOU 4773 CZ ARG C 109 12198 12188 13385 -819 -405 915 C ATOM 4774 NH1 ARG C 109 43.868 -1.551 17.066 1.00106.44 N ANISOU 4774 NH1 ARG C 109 13126 13147 14169 -838 -401 803 N ATOM 4775 NH2 ARG C 109 46.082 -2.076 16.752 1.00108.28 N ANISOU 4775 NH2 ARG C 109 13251 13314 14575 -843 -460 921 N ATOM 4776 N TYR C 110 37.991 -5.874 16.702 1.00 64.43 N ANISOU 4776 N TYR C 110 7983 7942 8557 -787 -252 1180 N ATOM 4777 CA TYR C 110 36.730 -6.357 16.139 1.00 61.26 C ANISOU 4777 CA TYR C 110 7628 7493 8156 -764 -197 1200 C ATOM 4778 C TYR C 110 35.807 -5.169 15.844 1.00 63.22 C ANISOU 4778 C TYR C 110 7930 7759 8331 -739 -112 1015 C ATOM 4779 O TYR C 110 36.077 -4.050 16.272 1.00 62.11 O ANISOU 4779 O TYR C 110 7776 7682 8139 -749 -114 876 O ATOM 4780 CB TYR C 110 36.069 -7.336 17.096 1.00 53.73 C ANISOU 4780 CB TYR C 110 6627 6691 7097 -839 -262 1372 C ATOM 4781 CG TYR C 110 36.115 -6.882 18.518 1.00 52.88 C ANISOU 4781 CG TYR C 110 6453 6863 6773 -929 -307 1371 C ATOM 4782 CD1 TYR C 110 37.167 -7.229 19.343 1.00 60.88 C ANISOU 4782 CD1 TYR C 110 7395 7966 7771 -988 -412 1494 C ATOM 4783 CD2 TYR C 110 35.114 -6.091 19.034 1.00 54.38 C ANISOU 4783 CD2 TYR C 110 6638 7249 6775 -953 -250 1226 C ATOM 4784 CE1 TYR C 110 37.207 -6.800 20.655 1.00 69.28 C ANISOU 4784 CE1 TYR C 110 8385 9331 8607 -1078 -455 1480 C ATOM 4785 CE2 TYR C 110 35.146 -5.660 20.337 1.00 59.09 C ANISOU 4785 CE2 TYR C 110 7150 8151 7152 -1033 -287 1182 C ATOM 4786 CZ TYR C 110 36.187 -6.012 21.143 1.00 66.53 C ANISOU 4786 CZ TYR C 110 8023 9201 8052 -1100 -387 1312 C ATOM 4787 OH TYR C 110 36.195 -5.570 22.439 1.00 70.93 O ANISOU 4787 OH TYR C 110 8483 10106 8362 -1186 -424 1254 O ATOM 4788 N PHE C 111 34.742 -5.373 15.082 1.00 65.69 N ANISOU 4788 N PHE C 111 8294 7997 8668 -703 -51 1000 N ATOM 4789 CA PHE C 111 33.791 -4.280 14.947 1.00 65.64 C ANISOU 4789 CA PHE C 111 8321 8015 8605 -683 7 833 C ATOM 4790 C PHE C 111 32.580 -4.534 15.821 1.00 67.87 C ANISOU 4790 C PHE C 111 8572 8494 8723 -726 13 833 C ATOM 4791 O PHE C 111 31.678 -5.289 15.480 1.00 68.69 O ANISOU 4791 O PHE C 111 8695 8578 8825 -723 39 914 O ATOM 4792 CB PHE C 111 33.399 -4.055 13.492 1.00 63.12 C ANISOU 4792 CB PHE C 111 8069 7504 8410 -620 69 794 C ATOM 4793 CG PHE C 111 34.485 -3.440 12.671 1.00 63.13 C ANISOU 4793 CG PHE C 111 8078 7376 8532 -599 72 768 C ATOM 4794 CD1 PHE C 111 35.696 -3.099 13.249 1.00 66.77 C ANISOU 4794 CD1 PHE C 111 8493 7872 9005 -628 21 765 C ATOM 4795 CD2 PHE C 111 34.300 -3.191 11.330 1.00 65.10 C ANISOU 4795 CD2 PHE C 111 8367 7498 8869 -564 121 756 C ATOM 4796 CE1 PHE C 111 36.700 -2.521 12.501 1.00 66.54 C ANISOU 4796 CE1 PHE C 111 8455 7743 9083 -623 22 755 C ATOM 4797 CE2 PHE C 111 35.306 -2.614 10.574 1.00 71.93 C ANISOU 4797 CE2 PHE C 111 9217 8290 9822 -569 122 758 C ATOM 4798 CZ PHE C 111 36.507 -2.277 11.159 1.00 66.80 C ANISOU 4798 CZ PHE C 111 8519 7668 9193 -599 75 759 C ATOM 4799 N ASP C 112 32.572 -3.807 16.928 1.00 67.68 N ANISOU 4799 N ASP C 112 8486 8674 8557 -765 -10 716 N ATOM 4800 CA ASP C 112 31.645 -3.953 18.025 1.00 60.25 C ANISOU 4800 CA ASP C 112 7469 8020 7403 -827 -9 696 C ATOM 4801 C ASP C 112 30.216 -3.666 17.573 1.00 66.94 C ANISOU 4801 C ASP C 112 8338 8858 8238 -787 62 584 C ATOM 4802 O ASP C 112 29.330 -4.524 17.632 1.00 69.70 O ANISOU 4802 O ASP C 112 8676 9287 8518 -823 82 707 O ATOM 4803 CB ASP C 112 32.051 -2.908 19.053 1.00 57.03 C ANISOU 4803 CB ASP C 112 6981 7810 6878 -849 -41 497 C ATOM 4804 CG ASP C 112 32.130 -3.451 20.434 1.00 74.63 C ANISOU 4804 CG ASP C 112 9101 10388 8868 -957 -89 591 C ATOM 4805 OD1 ASP C 112 32.071 -4.679 20.597 1.00 89.09 O ANISOU 4805 OD1 ASP C 112 10922 12270 10657 -1025 -118 859 O ATOM 4806 OD2 ASP C 112 32.267 -2.646 21.371 1.00 79.89 O ANISOU 4806 OD2 ASP C 112 9677 11285 9392 -980 -110 397 O ATOM 4807 N TYR C 113 30.019 -2.446 17.091 1.00 66.08 N ANISOU 4807 N TYR C 113 8254 8631 8225 -716 84 362 N ATOM 4808 CA TYR C 113 28.707 -1.925 16.761 1.00 66.26 C ANISOU 4808 CA TYR C 113 8277 8646 8254 -669 131 210 C ATOM 4809 C TYR C 113 28.707 -1.350 15.347 1.00 68.01 C ANISOU 4809 C TYR C 113 8590 8549 8700 -592 144 179 C ATOM 4810 O TYR C 113 29.675 -0.715 14.919 1.00 72.27 O ANISOU 4810 O TYR C 113 9156 8931 9372 -574 108 157 O ATOM 4811 CB TYR C 113 28.324 -0.816 17.746 1.00 61.86 C ANISOU 4811 CB TYR C 113 7610 8294 7599 -661 114 -77 C ATOM 4812 CG TYR C 113 27.933 -1.275 19.130 1.00 62.34 C ANISOU 4812 CG TYR C 113 7547 8759 7379 -746 119 -86 C ATOM 4813 CD1 TYR C 113 28.840 -1.246 20.174 1.00 64.66 C ANISOU 4813 CD1 TYR C 113 7764 9266 7537 -810 68 -90 C ATOM 4814 CD2 TYR C 113 26.646 -1.716 19.397 1.00 68.33 C ANISOU 4814 CD2 TYR C 113 8250 9717 7994 -773 173 -85 C ATOM 4815 CE1 TYR C 113 28.481 -1.653 21.451 1.00 67.72 C ANISOU 4815 CE1 TYR C 113 8018 10079 7632 -908 68 -81 C ATOM 4816 CE2 TYR C 113 26.280 -2.127 20.667 1.00 75.21 C ANISOU 4816 CE2 TYR C 113 8985 11014 8579 -874 178 -71 C ATOM 4817 CZ TYR C 113 27.202 -2.093 21.687 1.00 75.66 C ANISOU 4817 CZ TYR C 113 8963 11300 8486 -945 125 -64 C ATOM 4818 OH TYR C 113 26.837 -2.502 22.945 1.00 80.79 O ANISOU 4818 OH TYR C 113 9458 12420 8818 -1064 126 -30 O ATOM 4819 N TRP C 114 27.610 -1.546 14.630 1.00 61.52 N ANISOU 4819 N TRP C 114 7808 7654 7914 -558 189 187 N ATOM 4820 CA TRP C 114 27.493 -0.986 13.298 1.00 63.29 C ANISOU 4820 CA TRP C 114 8104 7618 8324 -501 193 174 C ATOM 4821 C TRP C 114 26.305 -0.040 13.161 1.00 70.24 C ANISOU 4821 C TRP C 114 8958 8470 9262 -450 189 -18 C ATOM 4822 O TRP C 114 25.287 -0.184 13.838 1.00 76.74 O ANISOU 4822 O TRP C 114 9719 9473 9966 -451 216 -112 O ATOM 4823 CB TRP C 114 27.325 -2.090 12.277 1.00 60.73 C ANISOU 4823 CB TRP C 114 7853 7189 8033 -497 236 362 C ATOM 4824 CG TRP C 114 28.442 -3.065 12.136 1.00 55.43 C ANISOU 4824 CG TRP C 114 7199 6491 7372 -524 227 532 C ATOM 4825 CD1 TRP C 114 28.920 -3.924 13.078 1.00 53.61 C ANISOU 4825 CD1 TRP C 114 6925 6396 7049 -576 200 635 C ATOM 4826 CD2 TRP C 114 29.160 -3.341 10.939 1.00 52.54 C ANISOU 4826 CD2 TRP C 114 6880 5961 7123 -501 236 617 C ATOM 4827 NE1 TRP C 114 29.918 -4.710 12.544 1.00 49.02 N ANISOU 4827 NE1 TRP C 114 6362 5707 6557 -573 182 766 N ATOM 4828 CE2 TRP C 114 30.076 -4.374 11.228 1.00 52.50 C ANISOU 4828 CE2 TRP C 114 6852 5981 7115 -524 213 739 C ATOM 4829 CE3 TRP C 114 29.117 -2.812 9.645 1.00 54.90 C ANISOU 4829 CE3 TRP C 114 7220 6118 7523 -470 255 605 C ATOM 4830 CZ2 TRP C 114 30.943 -4.883 10.278 1.00 62.72 C ANISOU 4830 CZ2 TRP C 114 8155 7166 8509 -501 218 803 C ATOM 4831 CZ3 TRP C 114 29.980 -3.309 8.703 1.00 65.15 C ANISOU 4831 CZ3 TRP C 114 8527 7348 8880 -464 269 688 C ATOM 4832 CH2 TRP C 114 30.889 -4.336 9.021 1.00 69.72 C ANISOU 4832 CH2 TRP C 114 9074 7957 9460 -472 255 765 C ATOM 4833 N GLY C 115 26.437 0.926 12.265 1.00 69.10 N ANISOU 4833 N GLY C 115 8844 8104 9308 -412 146 -64 N ATOM 4834 CA GLY C 115 25.325 1.788 11.933 1.00 72.33 C ANISOU 4834 CA GLY C 115 9227 8426 9828 -359 118 -215 C ATOM 4835 C GLY C 115 24.307 1.038 11.091 1.00 73.52 C ANISOU 4835 C GLY C 115 9435 8545 9955 -345 179 -105 C ATOM 4836 O GLY C 115 24.494 -0.142 10.748 1.00 66.19 O ANISOU 4836 O GLY C 115 8561 7649 8938 -374 236 76 O ATOM 4837 N GLN C 116 23.231 1.733 10.741 1.00 75.18 N ANISOU 4837 N GLN C 116 9621 8676 10269 -296 151 -226 N ATOM 4838 CA GLN C 116 22.103 1.110 10.059 1.00 69.78 C ANISOU 4838 CA GLN C 116 8974 7982 9559 -278 202 -156 C ATOM 4839 C GLN C 116 22.314 1.019 8.546 1.00 69.85 C ANISOU 4839 C GLN C 116 9072 7793 9676 -283 193 23 C ATOM 4840 O GLN C 116 21.576 0.331 7.837 1.00 63.84 O ANISOU 4840 O GLN C 116 8351 7022 8882 -276 236 108 O ATOM 4841 CB GLN C 116 20.836 1.879 10.392 1.00 57.35 C ANISOU 4841 CB GLN C 116 7314 6430 8047 -221 172 -378 C ATOM 4842 CG GLN C 116 21.116 3.226 11.009 1.00 62.35 C ANISOU 4842 CG GLN C 116 7854 7012 8822 -184 73 -612 C ATOM 4843 CD GLN C 116 20.893 4.354 10.028 1.00 65.35 C ANISOU 4843 CD GLN C 116 8239 7103 9488 -144 -42 -634 C ATOM 4844 OE1 GLN C 116 20.738 4.120 8.829 1.00 63.97 O ANISOU 4844 OE1 GLN C 116 8148 6788 9372 -159 -40 -436 O ATOM 4845 NE2 GLN C 116 20.850 5.585 10.533 1.00 62.71 N ANISOU 4845 NE2 GLN C 116 7799 6684 9345 -95 -158 -876 N ATOM 4846 N GLY C 117 23.355 1.688 8.068 1.00 68.28 N ANISOU 4846 N GLY C 117 8889 7464 9589 -304 135 82 N ATOM 4847 CA GLY C 117 23.646 1.727 6.653 1.00 63.44 C ANISOU 4847 CA GLY C 117 8332 6720 9052 -328 122 252 C ATOM 4848 C GLY C 117 23.031 2.969 6.052 1.00 59.60 C ANISOU 4848 C GLY C 117 7818 6064 8763 -313 17 217 C ATOM 4849 O GLY C 117 22.005 3.456 6.525 1.00 55.45 O ANISOU 4849 O GLY C 117 7244 5520 8306 -261 -21 53 O ATOM 4850 N THR C 118 23.661 3.498 5.014 1.00 57.20 N ANISOU 4850 N THR C 118 7529 5645 8561 -364 -43 374 N ATOM 4851 CA THR C 118 23.099 4.642 4.325 1.00 64.20 C ANISOU 4851 CA THR C 118 8381 6352 9659 -370 -171 401 C ATOM 4852 C THR C 118 23.341 4.425 2.862 1.00 63.92 C ANISOU 4852 C THR C 118 8383 6316 9588 -439 -164 644 C ATOM 4853 O THR C 118 24.412 3.989 2.472 1.00 54.08 O ANISOU 4853 O THR C 118 7153 5155 8239 -496 -112 769 O ATOM 4854 CB THR C 118 23.721 5.958 4.794 1.00 68.25 C ANISOU 4854 CB THR C 118 8824 6711 10398 -386 -314 334 C ATOM 4855 OG1 THR C 118 23.905 6.834 3.677 1.00 66.33 O ANISOU 4855 OG1 THR C 118 8561 6302 10340 -457 -442 531 O ATOM 4856 CG2 THR C 118 25.051 5.688 5.432 1.00 67.91 C ANISOU 4856 CG2 THR C 118 8784 6756 10263 -420 -269 337 C ATOM 4857 N THR C 119 22.323 4.711 2.060 1.00 76.36 N ANISOU 4857 N THR C 119 9956 7820 11236 -434 -218 699 N ATOM 4858 CA THR C 119 22.304 4.296 0.663 1.00 76.23 C ANISOU 4858 CA THR C 119 9967 7874 11124 -496 -192 907 C ATOM 4859 C THR C 119 22.704 5.432 -0.248 1.00 68.87 C ANISOU 4859 C THR C 119 8985 6832 10352 -595 -338 1114 C ATOM 4860 O THR C 119 22.037 6.467 -0.306 1.00 72.64 O ANISOU 4860 O THR C 119 9416 7122 11060 -592 -490 1119 O ATOM 4861 CB THR C 119 20.899 3.809 0.233 1.00 76.31 C ANISOU 4861 CB THR C 119 10001 7904 11091 -445 -163 871 C ATOM 4862 OG1 THR C 119 20.280 3.080 1.297 1.00 72.15 O ANISOU 4862 OG1 THR C 119 9492 7436 10486 -358 -74 671 O ATOM 4863 CG2 THR C 119 20.993 2.927 -0.984 1.00 78.24 C ANISOU 4863 CG2 THR C 119 10274 8300 11151 -491 -86 1017 C ATOM 4864 N LEU C 120 23.787 5.231 -0.978 1.00 61.41 N ANISOU 4864 N LEU C 120 8030 6009 9293 -691 -303 1294 N ATOM 4865 CA LEU C 120 24.242 6.250 -1.909 1.00 64.72 C ANISOU 4865 CA LEU C 120 8385 6374 9833 -819 -442 1546 C ATOM 4866 C LEU C 120 24.047 5.758 -3.341 1.00 63.92 C ANISOU 4866 C LEU C 120 8275 6469 9543 -897 -399 1740 C ATOM 4867 O LEU C 120 24.550 4.699 -3.726 1.00 61.76 O ANISOU 4867 O LEU C 120 8016 6427 9024 -900 -250 1726 O ATOM 4868 CB LEU C 120 25.690 6.654 -1.600 1.00 55.76 C ANISOU 4868 CB LEU C 120 7210 5246 8733 -893 -463 1614 C ATOM 4869 CG LEU C 120 26.566 7.435 -2.576 1.00 56.62 C ANISOU 4869 CG LEU C 120 7232 5452 8830 -1024 -548 1849 C ATOM 4870 CD1 LEU C 120 27.339 6.479 -3.448 1.00 59.80 C ANISOU 4870 CD1 LEU C 120 7624 6135 8963 -1109 -407 1988 C ATOM 4871 CD2 LEU C 120 25.807 8.437 -3.423 1.00 54.55 C ANISOU 4871 CD2 LEU C 120 6907 5136 8683 -1060 -710 1978 C ATOM 4872 N THR C 121 23.274 6.523 -4.104 1.00 58.84 N ANISOU 4872 N THR C 121 7591 5772 8992 -932 -529 1859 N ATOM 4873 CA THR C 121 22.959 6.183 -5.484 1.00 61.50 C ANISOU 4873 CA THR C 121 7905 6311 9152 -1013 -512 2043 C ATOM 4874 C THR C 121 23.477 7.263 -6.399 1.00 64.80 C ANISOU 4874 C THR C 121 8216 6805 9602 -1138 -653 2273 C ATOM 4875 O THR C 121 23.054 8.413 -6.323 1.00 69.46 O ANISOU 4875 O THR C 121 8753 7219 10420 -1132 -830 2302 O ATOM 4876 CB THR C 121 21.432 6.058 -5.724 1.00 56.71 C ANISOU 4876 CB THR C 121 7330 5623 8595 -946 -549 1992 C ATOM 4877 OG1 THR C 121 20.947 4.825 -5.174 1.00 65.37 O ANISOU 4877 OG1 THR C 121 8506 6767 9565 -831 -389 1773 O ATOM 4878 CG2 THR C 121 21.123 6.092 -7.212 1.00 40.32 C ANISOU 4878 CG2 THR C 121 5200 3746 6376 -1052 -591 2214 C ATOM 4879 N VAL C 122 24.391 6.902 -7.277 1.00 63.83 N ANISOU 4879 N VAL C 122 8039 6958 9254 -1256 -585 2436 N ATOM 4880 CA VAL C 122 24.874 7.878 -8.227 1.00 68.29 C ANISOU 4880 CA VAL C 122 8484 7640 9825 -1392 -722 2680 C ATOM 4881 C VAL C 122 24.331 7.520 -9.599 1.00 77.39 C ANISOU 4881 C VAL C 122 9588 9055 10762 -1478 -714 2842 C ATOM 4882 O VAL C 122 24.448 6.376 -10.038 1.00 82.85 O ANISOU 4882 O VAL C 122 10297 9994 11188 -1492 -549 2810 O ATOM 4883 CB VAL C 122 26.413 7.968 -8.217 1.00 60.67 C ANISOU 4883 CB VAL C 122 7453 6823 8774 -1481 -680 2758 C ATOM 4884 CG1 VAL C 122 26.868 9.268 -8.873 1.00 60.06 C ANISOU 4884 CG1 VAL C 122 7244 6770 8805 -1608 -874 2998 C ATOM 4885 CG2 VAL C 122 26.930 7.892 -6.780 1.00 55.49 C ANISOU 4885 CG2 VAL C 122 6868 5951 8265 -1382 -633 2553 C ATOM 4886 N SER C 123 23.673 8.481 -10.242 1.00 80.19 N ANISOU 4886 N SER C 123 9870 9355 11241 -1532 -900 3001 N ATOM 4887 CA SER C 123 23.203 8.301 -11.614 1.00 80.53 C ANISOU 4887 CA SER C 123 9843 9674 11082 -1638 -925 3187 C ATOM 4888 C SER C 123 22.992 9.636 -12.322 1.00 76.20 C ANISOU 4888 C SER C 123 9163 9091 10699 -1748 -1172 3435 C ATOM 4889 O SER C 123 22.754 10.659 -11.680 1.00 73.54 O ANISOU 4889 O SER C 123 8811 8442 10689 -1702 -1338 3417 O ATOM 4890 CB SER C 123 21.898 7.514 -11.632 1.00 82.30 C ANISOU 4890 CB SER C 123 10160 9850 11262 -1541 -859 3061 C ATOM 4891 OG SER C 123 20.806 8.377 -11.899 1.00 85.93 O ANISOU 4891 OG SER C 123 10585 10133 11929 -1535 -1050 3142 O ATOM 4892 N SER C 124 23.059 9.620 -13.648 1.00 76.11 N ANISOU 4892 N SER C 124 9040 9415 10465 -1898 -1206 3661 N ATOM 4893 CA SER C 124 22.817 10.831 -14.421 1.00 92.19 C ANISOU 4893 CA SER C 124 10931 11447 12650 -2026 -1457 3934 C ATOM 4894 C SER C 124 21.365 10.930 -14.900 1.00 98.35 C ANISOU 4894 C SER C 124 11715 12150 13503 -2005 -1560 3972 C ATOM 4895 O SER C 124 21.016 11.829 -15.664 1.00107.06 O ANISOU 4895 O SER C 124 12687 13275 14716 -2122 -1774 4213 O ATOM 4896 CB SER C 124 23.810 10.969 -15.581 1.00 98.56 C ANISOU 4896 CB SER C 124 11574 12677 13198 -2230 -1477 4195 C ATOM 4897 OG SER C 124 23.831 9.797 -16.370 1.00102.58 O ANISOU 4897 OG SER C 124 12079 13590 13308 -2267 -1289 4155 O ATOM 4898 N ALA C 125 20.528 9.996 -14.457 1.00 92.59 N ANISOU 4898 N ALA C 125 11125 11334 12720 -1863 -1417 3745 N ATOM 4899 CA ALA C 125 19.103 10.016 -14.782 1.00 87.62 C ANISOU 4899 CA ALA C 125 10514 10604 12174 -1820 -1502 3746 C ATOM 4900 C ALA C 125 18.395 11.218 -14.163 1.00 88.87 C ANISOU 4900 C ALA C 125 10642 10359 12764 -1752 -1726 3728 C ATOM 4901 O ALA C 125 18.717 11.634 -13.041 1.00 81.30 O ANISOU 4901 O ALA C 125 9722 9129 12038 -1653 -1740 3565 O ATOM 4902 CB ALA C 125 18.440 8.726 -14.323 1.00 82.34 C ANISOU 4902 CB ALA C 125 9997 9918 11370 -1679 -1299 3497 C ATOM 4903 N LYS C 126 17.441 11.776 -14.909 1.00 97.14 N ANISOU 4903 N LYS C 126 11603 11386 13918 -1811 -1907 3888 N ATOM 4904 CA LYS C 126 16.547 12.808 -14.384 1.00102.08 C ANISOU 4904 CA LYS C 126 12186 11638 14960 -1733 -2122 3839 C ATOM 4905 C LYS C 126 15.263 12.126 -13.905 1.00 99.68 C ANISOU 4905 C LYS C 126 12000 11182 14690 -1567 -2034 3595 C ATOM 4906 O LYS C 126 14.807 11.161 -14.517 1.00 99.23 O ANISOU 4906 O LYS C 126 12002 11337 14364 -1579 -1911 3607 O ATOM 4907 CB LYS C 126 16.262 13.916 -15.421 1.00104.98 C ANISOU 4907 CB LYS C 126 12365 12041 15481 -1902 -2405 4165 C ATOM 4908 CG LYS C 126 15.370 13.510 -16.606 1.00105.78 C ANISOU 4908 CG LYS C 126 12430 12372 15389 -1992 -2428 4329 C ATOM 4909 CD LYS C 126 14.768 14.725 -17.353 1.00106.73 C ANISOU 4909 CD LYS C 126 12363 12407 15781 -2124 -2748 4605 C ATOM 4910 CE LYS C 126 13.609 14.299 -18.284 1.00104.38 C ANISOU 4910 CE LYS C 126 12053 12258 15349 -2168 -2771 4698 C ATOM 4911 NZ LYS C 126 12.798 15.419 -18.886 1.00102.10 N ANISOU 4911 NZ LYS C 126 11593 11831 15371 -2274 -3086 4929 N ATOM 4912 N THR C 127 14.696 12.611 -12.802 1.00 98.48 N ANISOU 4912 N THR C 127 11871 10683 14862 -1413 -2099 3362 N ATOM 4913 CA THR C 127 13.566 11.933 -12.161 1.00 93.28 C ANISOU 4913 CA THR C 127 11319 9886 14239 -1243 -1997 3093 C ATOM 4914 C THR C 127 12.382 11.729 -13.092 1.00 82.55 C ANISOU 4914 C THR C 127 9934 8599 12831 -1274 -2065 3206 C ATOM 4915 O THR C 127 11.836 12.682 -13.627 1.00 80.17 O ANISOU 4915 O THR C 127 9505 8209 12747 -1339 -2296 3363 O ATOM 4916 CB THR C 127 13.062 12.692 -10.927 1.00 96.90 C ANISOU 4916 CB THR C 127 11750 9995 15074 -1089 -2096 2832 C ATOM 4917 OG1 THR C 127 11.690 12.349 -10.707 1.00 98.41 O ANISOU 4917 OG1 THR C 127 11973 10076 15342 -968 -2085 2658 O ATOM 4918 CG2 THR C 127 13.168 14.199 -11.139 1.00 99.02 C ANISOU 4918 CG2 THR C 127 11841 10100 15681 -1166 -2389 2987 C ATOM 4919 N THR C 128 11.954 10.482 -13.235 1.00 78.73 N ANISOU 4919 N THR C 128 9566 8260 12088 -1226 -1876 3117 N ATOM 4920 CA THR C 128 10.959 10.139 -14.243 1.00 77.02 C ANISOU 4920 CA THR C 128 9330 8174 11760 -1276 -1923 3247 C ATOM 4921 C THR C 128 9.839 9.296 -13.657 1.00 72.49 C ANISOU 4921 C THR C 128 8862 7478 11204 -1112 -1813 2995 C ATOM 4922 O THR C 128 10.080 8.294 -13.005 1.00 79.05 O ANISOU 4922 O THR C 128 9811 8336 11890 -1027 -1608 2807 O ATOM 4923 CB THR C 128 11.613 9.428 -15.450 1.00 78.54 C ANISOU 4923 CB THR C 128 9512 8785 11544 -1440 -1829 3474 C ATOM 4924 OG1 THR C 128 12.391 10.377 -16.189 1.00 82.76 O ANISOU 4924 OG1 THR C 128 9902 9449 12094 -1615 -1983 3751 O ATOM 4925 CG2 THR C 128 10.563 8.828 -16.365 1.00 77.10 C ANISOU 4925 CG2 THR C 128 9331 8766 11199 -1471 -1837 3554 C ATOM 4926 N ALA C 129 8.607 9.730 -13.869 1.00 73.32 N ANISOU 4926 N ALA C 129 8909 7441 11507 -1073 -1962 2994 N ATOM 4927 CA ALA C 129 7.456 8.992 -13.396 1.00 72.21 C ANISOU 4927 CA ALA C 129 8845 7195 11397 -926 -1879 2770 C ATOM 4928 C ALA C 129 7.241 7.776 -14.298 1.00 71.00 C ANISOU 4928 C ALA C 129 8763 7320 10895 -988 -1758 2878 C ATOM 4929 O ALA C 129 7.502 7.816 -15.504 1.00 75.70 O ANISOU 4929 O ALA C 129 9301 8174 11289 -1147 -1817 3147 O ATOM 4930 CB ALA C 129 6.234 9.890 -13.379 1.00 78.43 C ANISOU 4930 CB ALA C 129 9527 7755 12516 -870 -2088 2734 C ATOM 4931 N PRO C 130 6.785 6.672 -13.710 1.00 65.83 N ANISOU 4931 N PRO C 130 8218 6636 10159 -871 -1590 2664 N ATOM 4932 CA PRO C 130 6.702 5.415 -14.453 1.00 66.12 C ANISOU 4932 CA PRO C 130 8313 6964 9846 -915 -1451 2697 C ATOM 4933 C PRO C 130 5.498 5.354 -15.356 1.00 72.63 C ANISOU 4933 C PRO C 130 9092 7854 10652 -937 -1563 2794 C ATOM 4934 O PRO C 130 4.540 6.092 -15.144 1.00 84.95 O ANISOU 4934 O PRO C 130 10605 9152 12521 -880 -1731 2800 O ATOM 4935 CB PRO C 130 6.571 4.373 -13.343 1.00 57.50 C ANISOU 4935 CB PRO C 130 7312 5837 8700 -747 -1220 2305 C ATOM 4936 CG PRO C 130 5.911 5.090 -12.245 1.00 51.25 C ANISOU 4936 CG PRO C 130 6506 4696 8273 -623 -1306 2154 C ATOM 4937 CD PRO C 130 6.399 6.508 -12.299 1.00 60.14 C ANISOU 4937 CD PRO C 130 7548 5666 9637 -693 -1505 2337 C ATOM 4938 N SER C 131 5.562 4.499 -16.367 1.00 69.10 N ANISOU 4938 N SER C 131 8641 7772 9844 -1015 -1473 2838 N ATOM 4939 CA SER C 131 4.366 4.082 -17.071 1.00 73.01 C ANISOU 4939 CA SER C 131 9110 8362 10268 -1001 -1517 2824 C ATOM 4940 C SER C 131 3.921 2.795 -16.403 1.00 75.27 C ANISOU 4940 C SER C 131 9478 8660 10461 -841 -1296 2435 C ATOM 4941 O SER C 131 4.739 1.901 -16.186 1.00 84.58 O ANISOU 4941 O SER C 131 10705 10005 11426 -822 -1104 2273 O ATOM 4942 CB SER C 131 4.677 3.828 -18.535 1.00 71.87 C ANISOU 4942 CB SER C 131 8896 8642 9769 -1175 -1545 3057 C ATOM 4943 OG SER C 131 5.477 4.872 -19.044 1.00 79.24 O ANISOU 4943 OG SER C 131 9753 9629 10726 -1352 -1705 3431 O ATOM 4944 N VAL C 132 2.643 2.705 -16.046 1.00 61.65 N ANISOU 4944 N VAL C 132 7754 6752 8916 -730 -1334 2293 N ATOM 4945 CA VAL C 132 2.119 1.477 -15.461 1.00 58.64 C ANISOU 4945 CA VAL C 132 7432 6391 8458 -602 -1146 1966 C ATOM 4946 C VAL C 132 1.265 0.764 -16.485 1.00 61.46 C ANISOU 4946 C VAL C 132 7759 6956 8637 -627 -1160 1959 C ATOM 4947 O VAL C 132 0.348 1.350 -17.036 1.00 68.49 O ANISOU 4947 O VAL C 132 8591 7792 9641 -654 -1330 2102 O ATOM 4948 CB VAL C 132 1.253 1.739 -14.210 1.00 50.88 C ANISOU 4948 CB VAL C 132 6457 5094 7780 -455 -1149 1766 C ATOM 4949 CG1 VAL C 132 0.907 0.425 -13.524 1.00 38.53 C ANISOU 4949 CG1 VAL C 132 4946 3578 6114 -354 -948 1471 C ATOM 4950 CG2 VAL C 132 1.962 2.664 -13.251 1.00 50.66 C ANISOU 4950 CG2 VAL C 132 6431 4847 7969 -431 -1184 1771 C ATOM 4951 N TYR C 133 1.539 -0.502 -16.745 1.00 58.56 N ANISOU 4951 N TYR C 133 7420 6818 8012 -615 -997 1783 N ATOM 4952 CA TYR C 133 0.701 -1.199 -17.695 1.00 59.69 C ANISOU 4952 CA TYR C 133 7523 7155 8000 -633 -1018 1741 C ATOM 4953 C TYR C 133 0.122 -2.397 -17.002 1.00 64.06 C ANISOU 4953 C TYR C 133 8121 7633 8584 -508 -876 1431 C ATOM 4954 O TYR C 133 0.842 -3.101 -16.311 1.00 71.27 O ANISOU 4954 O TYR C 133 9085 8535 9459 -459 -727 1266 O ATOM 4955 CB TYR C 133 1.560 -1.680 -18.851 1.00 59.87 C ANISOU 4955 CB TYR C 133 7501 7573 7674 -748 -979 1800 C ATOM 4956 CG TYR C 133 2.305 -0.577 -19.543 1.00 60.22 C ANISOU 4956 CG TYR C 133 7485 7753 7642 -904 -1106 2138 C ATOM 4957 CD1 TYR C 133 3.673 -0.661 -19.752 1.00 68.74 C ANISOU 4957 CD1 TYR C 133 8549 9054 8515 -984 -1020 2181 C ATOM 4958 CD2 TYR C 133 1.647 0.544 -19.997 1.00 56.64 C ANISOU 4958 CD2 TYR C 133 6976 7207 7337 -981 -1325 2430 C ATOM 4959 CE1 TYR C 133 4.366 0.358 -20.394 1.00 66.82 C ANISOU 4959 CE1 TYR C 133 8236 8956 8198 -1150 -1143 2525 C ATOM 4960 CE2 TYR C 133 2.322 1.554 -20.640 1.00 63.06 C ANISOU 4960 CE2 TYR C 133 7720 8138 8102 -1147 -1467 2785 C ATOM 4961 CZ TYR C 133 3.679 1.457 -20.834 1.00 67.42 C ANISOU 4961 CZ TYR C 133 8257 8928 8430 -1237 -1371 2839 C ATOM 4962 OH TYR C 133 4.347 2.466 -21.474 1.00 74.66 O ANISOU 4962 OH TYR C 133 9091 9980 9297 -1423 -1518 3221 O ATOM 4963 N PRO C 134 -1.184 -2.640 -17.185 1.00 67.38 N ANISOU 4963 N PRO C 134 8515 8000 9086 -464 -934 1369 N ATOM 4964 CA PRO C 134 -1.864 -3.836 -16.684 1.00 65.33 C ANISOU 4964 CA PRO C 134 8275 7694 8852 -370 -823 1108 C ATOM 4965 C PRO C 134 -1.626 -5.024 -17.598 1.00 63.40 C ANISOU 4965 C PRO C 134 8008 7722 8358 -402 -763 981 C ATOM 4966 O PRO C 134 -1.694 -4.869 -18.827 1.00 56.46 O ANISOU 4966 O PRO C 134 7069 7082 7300 -487 -851 1089 O ATOM 4967 CB PRO C 134 -3.319 -3.432 -16.730 1.00 71.63 C ANISOU 4967 CB PRO C 134 9029 8360 9828 -334 -942 1134 C ATOM 4968 CG PRO C 134 -3.384 -2.581 -17.955 1.00 80.82 C ANISOU 4968 CG PRO C 134 10135 9661 10912 -440 -1114 1390 C ATOM 4969 CD PRO C 134 -2.090 -1.807 -17.989 1.00 79.47 C ANISOU 4969 CD PRO C 134 9979 9531 10686 -518 -1128 1571 C ATOM 4970 N LEU C 135 -1.396 -6.193 -17.006 1.00 61.60 N ANISOU 4970 N LEU C 135 7810 7463 8131 -337 -631 752 N ATOM 4971 CA LEU C 135 -1.155 -7.396 -17.782 1.00 64.09 C ANISOU 4971 CA LEU C 135 8086 7998 8267 -345 -585 574 C ATOM 4972 C LEU C 135 -2.211 -8.441 -17.468 1.00 65.49 C ANISOU 4972 C LEU C 135 8252 8059 8572 -276 -571 383 C ATOM 4973 O LEU C 135 -2.193 -9.045 -16.399 1.00 67.01 O ANISOU 4973 O LEU C 135 8480 8069 8912 -216 -490 275 O ATOM 4974 CB LEU C 135 0.223 -7.969 -17.461 1.00 61.02 C ANISOU 4974 CB LEU C 135 7718 7671 7795 -336 -468 466 C ATOM 4975 CG LEU C 135 1.446 -7.051 -17.496 1.00 64.65 C ANISOU 4975 CG LEU C 135 8193 8215 8157 -400 -454 637 C ATOM 4976 CD1 LEU C 135 2.687 -7.844 -17.098 1.00 67.60 C ANISOU 4976 CD1 LEU C 135 8578 8631 8477 -370 -332 478 C ATOM 4977 CD2 LEU C 135 1.640 -6.381 -18.855 1.00 64.68 C ANISOU 4977 CD2 LEU C 135 8122 8524 7930 -517 -547 814 C ATOM 4978 N ALA C 136 -3.111 -8.676 -18.416 1.00 65.51 N ANISOU 4978 N ALA C 136 8193 8186 8511 -296 -657 355 N ATOM 4979 CA ALA C 136 -4.129 -9.697 -18.251 1.00 57.93 C ANISOU 4979 CA ALA C 136 7207 7133 7672 -244 -660 177 C ATOM 4980 C ALA C 136 -3.647 -10.954 -18.947 1.00 63.05 C ANISOU 4980 C ALA C 136 7800 7959 8197 -239 -633 -57 C ATOM 4981 O ALA C 136 -2.632 -10.930 -19.640 1.00 67.10 O ANISOU 4981 O ALA C 136 8284 8706 8505 -278 -613 -82 O ATOM 4982 CB ALA C 136 -5.433 -9.242 -18.869 1.00 51.59 C ANISOU 4982 CB ALA C 136 6357 6349 6895 -262 -782 262 C ATOM 4983 N PRO C 137 -4.406 -12.044 -18.796 1.00 62.82 N ANISOU 4983 N PRO C 137 7737 7829 8303 -195 -644 -240 N ATOM 4984 CA PRO C 137 -4.195 -13.331 -19.468 1.00 63.30 C ANISOU 4984 CA PRO C 137 7719 8012 8320 -175 -655 -510 C ATOM 4985 C PRO C 137 -4.467 -13.201 -20.970 1.00 66.29 C ANISOU 4985 C PRO C 137 8009 8718 8459 -225 -741 -557 C ATOM 4986 O PRO C 137 -4.466 -12.085 -21.460 1.00 67.94 O ANISOU 4986 O PRO C 137 8228 9077 8510 -289 -780 -339 O ATOM 4987 CB PRO C 137 -5.216 -14.246 -18.791 1.00 57.83 C ANISOU 4987 CB PRO C 137 7013 7069 7889 -133 -678 -610 C ATOM 4988 CG PRO C 137 -5.426 -13.642 -17.434 1.00 51.78 C ANISOU 4988 CG PRO C 137 6328 6064 7283 -124 -619 -423 C ATOM 4989 CD PRO C 137 -5.308 -12.168 -17.634 1.00 57.55 C ANISOU 4989 CD PRO C 137 7102 6879 7886 -156 -628 -207 C ATOM 4990 N VAL C 138 -4.597 -14.306 -21.695 1.00 73.79 N ANISOU 4990 N VAL C 138 8861 9796 9379 -203 -781 -834 N ATOM 4991 CA VAL C 138 -4.766 -14.253 -23.146 1.00 86.09 C ANISOU 4991 CA VAL C 138 10313 11731 10667 -255 -857 -914 C ATOM 4992 C VAL C 138 -6.164 -14.711 -23.615 1.00 91.16 C ANISOU 4992 C VAL C 138 10897 12349 11390 -247 -965 -1004 C ATOM 4993 O VAL C 138 -6.722 -14.225 -24.617 1.00 87.16 O ANISOU 4993 O VAL C 138 10333 12096 10689 -309 -1052 -930 O ATOM 4994 CB VAL C 138 -3.684 -15.104 -23.839 1.00 93.92 C ANISOU 4994 CB VAL C 138 11196 12991 11499 -236 -823 -1222 C ATOM 4995 CG1 VAL C 138 -3.601 -14.736 -25.319 1.00 97.07 C ANISOU 4995 CG1 VAL C 138 11476 13885 11522 -321 -878 -1244 C ATOM 4996 CG2 VAL C 138 -2.307 -14.950 -23.115 1.00 45.06 C ANISOU 4996 CG2 VAL C 138 5063 6736 5320 -219 -709 -1184 C ATOM 4997 N GLY C 144 -7.585 -22.900 -16.568 1.00 97.57 N ANISOU 4997 N GLY C 144 11568 10764 14738 -58 -1157 -1530 N ATOM 4998 CA GLY C 144 -7.167 -23.513 -15.318 1.00100.30 C ANISOU 4998 CA GLY C 144 11915 10856 15338 -93 -1166 -1386 C ATOM 4999 C GLY C 144 -8.057 -23.122 -14.151 1.00 99.34 C ANISOU 4999 C GLY C 144 11834 10645 15264 -181 -1111 -1064 C ATOM 5000 O GLY C 144 -9.044 -22.406 -14.335 1.00101.44 O ANISOU 5000 O GLY C 144 12121 11022 15398 -200 -1074 -981 O ATOM 5001 N SER C 145 -7.723 -23.604 -12.955 1.00 95.59 N ANISOU 5001 N SER C 145 11352 9990 14978 -238 -1114 -888 N ATOM 5002 CA SER C 145 -8.468 -23.242 -11.747 1.00 95.81 C ANISOU 5002 CA SER C 145 11395 9993 15017 -333 -1049 -588 C ATOM 5003 C SER C 145 -7.854 -22.027 -11.032 1.00 88.31 C ANISOU 5003 C SER C 145 10560 9184 13811 -325 -878 -427 C ATOM 5004 O SER C 145 -8.456 -21.461 -10.113 1.00 78.38 O ANISOU 5004 O SER C 145 9311 7979 12492 -385 -798 -224 O ATOM 5005 CB SER C 145 -8.554 -24.427 -10.786 1.00 99.10 C ANISOU 5005 CB SER C 145 11714 10174 15764 -429 -1160 -442 C ATOM 5006 OG SER C 145 -7.336 -24.569 -10.079 1.00104.37 O ANISOU 5006 OG SER C 145 12418 10776 16463 -431 -1134 -365 O ATOM 5007 N SER C 146 -6.659 -21.630 -11.462 1.00 84.24 N ANISOU 5007 N SER C 146 10115 8743 13149 -252 -826 -536 N ATOM 5008 CA SER C 146 -6.054 -20.390 -10.997 1.00 79.06 C ANISOU 5008 CA SER C 146 9566 8222 12250 -236 -679 -417 C ATOM 5009 C SER C 146 -5.729 -19.525 -12.200 1.00 73.42 C ANISOU 5009 C SER C 146 8908 7693 11296 -163 -644 -555 C ATOM 5010 O SER C 146 -5.424 -20.049 -13.269 1.00 73.90 O ANISOU 5010 O SER C 146 8926 7794 11359 -119 -715 -768 O ATOM 5011 CB SER C 146 -4.780 -20.667 -10.190 1.00 82.96 C ANISOU 5011 CB SER C 146 10088 8639 12793 -242 -649 -354 C ATOM 5012 OG SER C 146 -4.949 -20.369 -8.813 1.00 81.64 O ANISOU 5012 OG SER C 146 9934 8461 12626 -316 -579 -116 O ATOM 5013 N VAL C 147 -5.831 -18.207 -12.024 1.00 73.01 N ANISOU 5013 N VAL C 147 8930 7764 11045 -158 -548 -434 N ATOM 5014 CA VAL C 147 -5.336 -17.230 -12.998 1.00 72.96 C ANISOU 5014 CA VAL C 147 8979 7937 10805 -114 -517 -486 C ATOM 5015 C VAL C 147 -4.335 -16.321 -12.316 1.00 69.62 C ANISOU 5015 C VAL C 147 8641 7546 10266 -109 -414 -365 C ATOM 5016 O VAL C 147 -4.593 -15.800 -11.226 1.00 64.07 O ANISOU 5016 O VAL C 147 7963 6791 9590 -132 -354 -219 O ATOM 5017 CB VAL C 147 -6.458 -16.315 -13.594 1.00 67.46 C ANISOU 5017 CB VAL C 147 8282 7344 10007 -115 -538 -437 C ATOM 5018 CG1 VAL C 147 -7.401 -17.110 -14.480 1.00 79.51 C ANISOU 5018 CG1 VAL C 147 9724 8878 11610 -118 -645 -575 C ATOM 5019 CG2 VAL C 147 -7.231 -15.589 -12.494 1.00 57.68 C ANISOU 5019 CG2 VAL C 147 7054 6045 8816 -137 -483 -267 C ATOM 5020 N THR C 148 -3.188 -16.122 -12.944 1.00 68.94 N ANISOU 5020 N THR C 148 8583 7564 10045 -82 -394 -439 N ATOM 5021 CA THR C 148 -2.295 -15.090 -12.447 1.00 66.78 C ANISOU 5021 CA THR C 148 8388 7335 9650 -82 -308 -317 C ATOM 5022 C THR C 148 -2.382 -13.836 -13.332 1.00 61.33 C ANISOU 5022 C THR C 148 7727 6811 8766 -84 -313 -255 C ATOM 5023 O THR C 148 -2.349 -13.920 -14.564 1.00 58.39 O ANISOU 5023 O THR C 148 7317 6596 8273 -85 -363 -348 O ATOM 5024 CB THR C 148 -0.836 -15.602 -12.264 1.00 68.04 C ANISOU 5024 CB THR C 148 8558 7486 9810 -65 -274 -385 C ATOM 5025 OG1 THR C 148 -0.011 -15.149 -13.343 1.00 65.67 O ANISOU 5025 OG1 THR C 148 8259 7381 9313 -52 -265 -459 O ATOM 5026 CG2 THR C 148 -0.802 -17.140 -12.186 1.00 70.59 C ANISOU 5026 CG2 THR C 148 8803 7676 10342 -55 -345 -529 C ATOM 5027 N LEU C 149 -2.532 -12.685 -12.683 1.00 58.61 N ANISOU 5027 N LEU C 149 7431 6434 8404 -91 -275 -99 N ATOM 5028 CA LEU C 149 -2.555 -11.392 -13.352 1.00 60.33 C ANISOU 5028 CA LEU C 149 7670 6757 8494 -102 -305 6 C ATOM 5029 C LEU C 149 -1.204 -10.714 -13.242 1.00 61.03 C ANISOU 5029 C LEU C 149 7811 6900 8479 -113 -256 78 C ATOM 5030 O LEU C 149 -0.321 -11.211 -12.564 1.00 69.34 O ANISOU 5030 O LEU C 149 8886 7902 9560 -103 -190 37 O ATOM 5031 CB LEU C 149 -3.610 -10.522 -12.691 1.00 61.23 C ANISOU 5031 CB LEU C 149 7781 6771 8712 -92 -322 107 C ATOM 5032 CG LEU C 149 -5.020 -11.096 -12.833 1.00 58.93 C ANISOU 5032 CG LEU C 149 7427 6442 8520 -88 -373 50 C ATOM 5033 CD1 LEU C 149 -5.974 -10.343 -11.943 1.00 55.80 C ANISOU 5033 CD1 LEU C 149 7006 5955 8242 -69 -368 113 C ATOM 5034 CD2 LEU C 149 -5.463 -11.044 -14.293 1.00 55.74 C ANISOU 5034 CD2 LEU C 149 6990 6173 8016 -102 -470 28 C ATOM 5035 N GLY C 150 -1.040 -9.558 -13.865 1.00 56.59 N ANISOU 5035 N GLY C 150 7259 6430 7814 -142 -300 204 N ATOM 5036 CA GLY C 150 0.263 -8.910 -13.838 1.00 58.60 C ANISOU 5036 CA GLY C 150 7548 6745 7970 -168 -264 287 C ATOM 5037 C GLY C 150 0.235 -7.405 -13.977 1.00 61.79 C ANISOU 5037 C GLY C 150 7966 7139 8372 -202 -330 483 C ATOM 5038 O GLY C 150 -0.698 -6.837 -14.533 1.00 62.36 O ANISOU 5038 O GLY C 150 8007 7219 8469 -217 -427 564 O ATOM 5039 N CYS C 151 1.271 -6.754 -13.467 1.00 65.55 N ANISOU 5039 N CYS C 151 8479 7582 8843 -215 -294 564 N ATOM 5040 CA CYS C 151 1.364 -5.295 -13.533 1.00 63.51 C ANISOU 5040 CA CYS C 151 8224 7276 8632 -251 -379 756 C ATOM 5041 C CYS C 151 2.787 -4.892 -13.852 1.00 53.80 C ANISOU 5041 C CYS C 151 7004 6165 7271 -314 -359 854 C ATOM 5042 O CYS C 151 3.703 -5.304 -13.182 1.00 60.15 O ANISOU 5042 O CYS C 151 7843 6949 8064 -293 -261 778 O ATOM 5043 CB CYS C 151 0.938 -4.667 -12.215 1.00 61.42 C ANISOU 5043 CB CYS C 151 7976 6780 8580 -192 -372 743 C ATOM 5044 SG CYS C 151 0.553 -2.941 -12.357 1.00 80.82 S ANISOU 5044 SG CYS C 151 10398 9111 11198 -210 -533 927 S ATOM 5045 N LEU C 152 2.972 -4.092 -14.882 1.00 49.24 N ANISOU 5045 N LEU C 152 6387 5726 6595 -402 -459 1041 N ATOM 5046 CA LEU C 152 4.311 -3.772 -15.353 1.00 57.56 C ANISOU 5046 CA LEU C 152 7426 6955 7489 -485 -442 1152 C ATOM 5047 C LEU C 152 4.628 -2.290 -15.148 1.00 58.08 C ANISOU 5047 C LEU C 152 7491 6895 7682 -543 -551 1395 C ATOM 5048 O LEU C 152 4.085 -1.418 -15.846 1.00 54.49 O ANISOU 5048 O LEU C 152 6988 6450 7264 -612 -703 1601 O ATOM 5049 CB LEU C 152 4.415 -4.110 -16.836 1.00 64.45 C ANISOU 5049 CB LEU C 152 8221 8171 8098 -574 -474 1191 C ATOM 5050 CG LEU C 152 5.783 -4.451 -17.420 1.00 71.12 C ANISOU 5050 CG LEU C 152 9018 9308 8698 -641 -397 1172 C ATOM 5051 CD1 LEU C 152 5.697 -4.312 -18.923 1.00 71.80 C ANISOU 5051 CD1 LEU C 152 8997 9763 8522 -760 -473 1289 C ATOM 5052 CD2 LEU C 152 6.909 -3.590 -16.864 1.00 70.85 C ANISOU 5052 CD2 LEU C 152 9009 9201 8711 -686 -386 1328 C ATOM 5053 N VAL C 153 5.530 -2.009 -14.214 1.00 48.55 N ANISOU 5053 N VAL C 153 6326 5566 6556 -521 -491 1380 N ATOM 5054 CA VAL C 153 5.902 -0.630 -13.938 1.00 51.04 C ANISOU 5054 CA VAL C 153 6631 5730 7030 -570 -604 1583 C ATOM 5055 C VAL C 153 7.201 -0.318 -14.618 1.00 51.47 C ANISOU 5055 C VAL C 153 6651 5996 6907 -693 -606 1756 C ATOM 5056 O VAL C 153 8.237 -0.806 -14.206 1.00 59.27 O ANISOU 5056 O VAL C 153 7665 7048 7806 -680 -483 1657 O ATOM 5057 CB VAL C 153 6.157 -0.399 -12.459 1.00 49.47 C ANISOU 5057 CB VAL C 153 6484 5282 7030 -479 -547 1457 C ATOM 5058 CG1 VAL C 153 6.474 1.059 -12.228 1.00 50.02 C ANISOU 5058 CG1 VAL C 153 6526 5176 7305 -524 -693 1640 C ATOM 5059 CG2 VAL C 153 4.982 -0.846 -11.636 1.00 49.64 C ANISOU 5059 CG2 VAL C 153 6523 5150 7189 -364 -510 1259 C ATOM 5060 N LYS C 154 7.178 0.514 -15.641 1.00 52.11 N ANISOU 5060 N LYS C 154 6662 6197 6940 -822 -754 2032 N ATOM 5061 CA LYS C 154 8.389 0.649 -16.425 1.00 56.49 C ANISOU 5061 CA LYS C 154 7159 7045 7262 -961 -740 2198 C ATOM 5062 C LYS C 154 8.836 2.087 -16.632 1.00 64.24 C ANISOU 5062 C LYS C 154 8087 7946 8375 -1094 -918 2546 C ATOM 5063 O LYS C 154 8.015 2.981 -16.758 1.00 69.84 O ANISOU 5063 O LYS C 154 8769 8467 9300 -1118 -1104 2722 O ATOM 5064 CB LYS C 154 8.246 -0.096 -17.749 1.00 49.09 C ANISOU 5064 CB LYS C 154 6145 6508 5997 -1035 -712 2193 C ATOM 5065 CG LYS C 154 8.494 0.761 -18.951 1.00 59.30 C ANISOU 5065 CG LYS C 154 7328 8066 7138 -1232 -859 2549 C ATOM 5066 CD LYS C 154 8.661 -0.100 -20.185 1.00 66.78 C ANISOU 5066 CD LYS C 154 8179 9503 7692 -1307 -788 2482 C ATOM 5067 CE LYS C 154 9.258 -1.453 -19.820 1.00 67.00 C ANISOU 5067 CE LYS C 154 8234 9633 7590 -1186 -573 2095 C ATOM 5068 NZ LYS C 154 9.911 -2.119 -20.989 1.00 67.89 N ANISOU 5068 NZ LYS C 154 8212 10270 7312 -1277 -499 2021 N ATOM 5069 N GLY C 155 10.150 2.291 -16.630 1.00 68.70 N ANISOU 5069 N GLY C 155 8628 8638 8838 -1178 -871 2638 N ATOM 5070 CA GLY C 155 10.751 3.561 -17.004 1.00 66.77 C ANISOU 5070 CA GLY C 155 8309 8384 8677 -1342 -1042 3005 C ATOM 5071 C GLY C 155 10.756 4.658 -15.954 1.00 63.22 C ANISOU 5071 C GLY C 155 7893 7496 8633 -1296 -1171 3066 C ATOM 5072 O GLY C 155 10.620 5.828 -16.298 1.00 65.15 O ANISOU 5072 O GLY C 155 8051 7642 9062 -1376 -1372 3280 O ATOM 5073 N TYR C 156 10.934 4.297 -14.684 1.00 58.38 N ANISOU 5073 N TYR C 156 7369 6663 8152 -1140 -1044 2774 N ATOM 5074 CA TYR C 156 11.011 5.302 -13.626 1.00 58.67 C ANISOU 5074 CA TYR C 156 7419 6317 8555 -1087 -1155 2773 C ATOM 5075 C TYR C 156 12.383 5.483 -13.006 1.00 69.92 C ANISOU 5075 C TYR C 156 8854 7742 9972 -1106 -1079 2742 C ATOM 5076 O TYR C 156 13.231 4.586 -12.999 1.00 74.99 O ANISOU 5076 O TYR C 156 9527 8605 10359 -1112 -898 2648 O ATOM 5077 CB TYR C 156 10.027 5.015 -12.514 1.00 59.04 C ANISOU 5077 CB TYR C 156 7531 6101 8802 -894 -1105 2457 C ATOM 5078 CG TYR C 156 10.348 3.778 -11.735 1.00 68.00 C ANISOU 5078 CG TYR C 156 8749 7325 9764 -780 -861 2146 C ATOM 5079 CD1 TYR C 156 10.121 2.528 -12.267 1.00 77.63 C ANISOU 5079 CD1 TYR C 156 9993 8793 10709 -761 -718 2030 C ATOM 5080 CD2 TYR C 156 10.864 3.857 -10.458 1.00 64.40 C ANISOU 5080 CD2 TYR C 156 8333 6700 9434 -695 -792 1969 C ATOM 5081 CE1 TYR C 156 10.412 1.389 -11.546 1.00 78.12 C ANISOU 5081 CE1 TYR C 156 10117 8902 10662 -664 -527 1768 C ATOM 5082 CE2 TYR C 156 11.155 2.726 -9.737 1.00 60.29 C ANISOU 5082 CE2 TYR C 156 7878 6260 8769 -607 -592 1725 C ATOM 5083 CZ TYR C 156 10.926 1.499 -10.283 1.00 67.60 C ANISOU 5083 CZ TYR C 156 8826 7402 9456 -593 -468 1637 C ATOM 5084 OH TYR C 156 11.211 0.366 -9.568 1.00 68.82 O ANISOU 5084 OH TYR C 156 9032 7604 9511 -513 -301 1417 O ATOM 5085 N PHE C 157 12.606 6.693 -12.525 1.00 72.91 N ANISOU 5085 N PHE C 157 9174 7912 10615 -1090 -1216 2745 N ATOM 5086 CA PHE C 157 13.752 6.995 -11.701 1.00 73.12 C ANISOU 5086 CA PHE C 157 9211 7869 10702 -1076 -1167 2669 C ATOM 5087 C PHE C 157 13.263 8.047 -10.721 1.00 70.88 C ANISOU 5087 C PHE C 157 8894 7250 10787 -968 -1303 2519 C ATOM 5088 O PHE C 157 12.485 8.925 -11.090 1.00 71.43 O ANISOU 5088 O PHE C 157 8878 7207 11056 -978 -1490 2597 O ATOM 5089 CB PHE C 157 14.887 7.535 -12.571 1.00 77.31 C ANISOU 5089 CB PHE C 157 9645 8627 11104 -1245 -1225 2923 C ATOM 5090 CG PHE C 157 16.192 7.677 -11.840 1.00 81.13 C ANISOU 5090 CG PHE C 157 10141 9088 11599 -1246 -1154 2863 C ATOM 5091 CD1 PHE C 157 16.549 8.880 -11.273 1.00 83.63 C ANISOU 5091 CD1 PHE C 157 10395 9189 12194 -1238 -1302 2866 C ATOM 5092 CD2 PHE C 157 17.056 6.596 -11.702 1.00 81.28 C ANISOU 5092 CD2 PHE C 157 10221 9299 11364 -1256 -949 2797 C ATOM 5093 CE1 PHE C 157 17.743 9.007 -10.588 1.00 83.66 C ANISOU 5093 CE1 PHE C 157 10407 9170 12208 -1239 -1243 2810 C ATOM 5094 CE2 PHE C 157 18.253 6.718 -11.022 1.00 73.41 C ANISOU 5094 CE2 PHE C 157 9230 8279 10385 -1257 -889 2743 C ATOM 5095 CZ PHE C 157 18.591 7.920 -10.459 1.00 77.14 C ANISOU 5095 CZ PHE C 157 9651 8536 11122 -1248 -1034 2751 C ATOM 5096 N PRO C 158 13.718 7.982 -9.468 1.00 66.50 N ANISOU 5096 N PRO C 158 8390 6550 10328 -868 -1219 2297 N ATOM 5097 CA PRO C 158 14.530 6.934 -8.852 1.00 67.68 C ANISOU 5097 CA PRO C 158 8636 6791 10290 -841 -1010 2177 C ATOM 5098 C PRO C 158 13.678 5.942 -8.076 1.00 68.16 C ANISOU 5098 C PRO C 158 8784 6771 10344 -710 -882 1939 C ATOM 5099 O PRO C 158 12.466 6.108 -7.984 1.00 72.35 O ANISOU 5099 O PRO C 158 9299 7179 11013 -634 -949 1852 O ATOM 5100 CB PRO C 158 15.378 7.723 -7.864 1.00 74.91 C ANISOU 5100 CB PRO C 158 9524 7557 11380 -811 -1050 2080 C ATOM 5101 CG PRO C 158 14.403 8.820 -7.384 1.00 73.80 C ANISOU 5101 CG PRO C 158 9307 7163 11569 -726 -1231 1967 C ATOM 5102 CD PRO C 158 13.481 9.105 -8.544 1.00 67.78 C ANISOU 5102 CD PRO C 158 8488 6443 10824 -784 -1359 2150 C ATOM 5103 N GLU C 159 14.317 4.940 -7.483 1.00 68.00 N ANISOU 5103 N GLU C 159 8830 6865 10143 -667 -691 1786 N ATOM 5104 CA GLU C 159 13.640 4.039 -6.560 1.00 69.47 C ANISOU 5104 CA GLU C 159 9070 7043 10283 -528 -552 1498 C ATOM 5105 C GLU C 159 13.233 4.838 -5.327 1.00 73.47 C ANISOU 5105 C GLU C 159 9548 7305 11064 -435 -629 1321 C ATOM 5106 O GLU C 159 13.699 5.949 -5.126 1.00 79.42 O ANISOU 5106 O GLU C 159 10251 7890 12034 -469 -770 1392 O ATOM 5107 CB GLU C 159 14.580 2.904 -6.148 1.00 72.70 C ANISOU 5107 CB GLU C 159 9533 7627 10463 -512 -361 1389 C ATOM 5108 CG GLU C 159 14.831 1.844 -7.218 1.00 83.43 C ANISOU 5108 CG GLU C 159 10902 9245 11551 -562 -260 1449 C ATOM 5109 CD GLU C 159 13.948 0.612 -7.044 1.00101.00 C ANISOU 5109 CD GLU C 159 13166 11528 13679 -471 -151 1265 C ATOM 5110 OE1 GLU C 159 14.492 -0.518 -7.085 1.00101.99 O ANISOU 5110 OE1 GLU C 159 13311 11801 13640 -457 -27 1179 O ATOM 5111 OE2 GLU C 159 12.711 0.775 -6.874 1.00107.64 O ANISOU 5111 OE2 GLU C 159 14005 12261 14631 -417 -201 1206 O ATOM 5112 N PRO C 160 12.326 4.287 -4.513 1.00 75.98 N ANISOU 5112 N PRO C 160 9879 7612 11379 -322 -545 1083 N ATOM 5113 CA PRO C 160 11.568 3.076 -4.830 1.00 73.39 C ANISOU 5113 CA PRO C 160 9591 7437 10855 -290 -422 1023 C ATOM 5114 C PRO C 160 10.228 3.451 -5.440 1.00 73.24 C ANISOU 5114 C PRO C 160 9530 7339 10959 -269 -534 1053 C ATOM 5115 O PRO C 160 9.888 4.632 -5.506 1.00 70.67 O ANISOU 5115 O PRO C 160 9139 6825 10888 -269 -710 1104 O ATOM 5116 CB PRO C 160 11.316 2.487 -3.450 1.00 62.53 C ANISOU 5116 CB PRO C 160 8226 6079 9454 -196 -302 773 C ATOM 5117 CG PRO C 160 11.113 3.709 -2.586 1.00 60.11 C ANISOU 5117 CG PRO C 160 7846 5588 9405 -144 -419 651 C ATOM 5118 CD PRO C 160 11.978 4.807 -3.179 1.00 69.20 C ANISOU 5118 CD PRO C 160 8975 6613 10706 -223 -569 843 C ATOM 5119 N VAL C 161 9.467 2.452 -5.861 1.00 74.43 N ANISOU 5119 N VAL C 161 9708 7615 10958 -249 -450 1016 N ATOM 5120 CA VAL C 161 8.035 2.626 -6.065 1.00 69.67 C ANISOU 5120 CA VAL C 161 9061 6938 10471 -197 -524 966 C ATOM 5121 C VAL C 161 7.410 1.715 -5.036 1.00 69.84 C ANISOU 5121 C VAL C 161 9091 7017 10426 -110 -382 732 C ATOM 5122 O VAL C 161 8.044 0.752 -4.580 1.00 70.78 O ANISOU 5122 O VAL C 161 9262 7257 10374 -115 -240 678 O ATOM 5123 CB VAL C 161 7.536 2.188 -7.462 1.00 56.41 C ANISOU 5123 CB VAL C 161 7390 5379 8665 -258 -554 1124 C ATOM 5124 CG1 VAL C 161 8.173 3.026 -8.573 1.00 48.08 C ANISOU 5124 CG1 VAL C 161 6308 4336 7624 -378 -695 1405 C ATOM 5125 CG2 VAL C 161 7.770 0.683 -7.673 1.00 52.43 C ANISOU 5125 CG2 VAL C 161 6945 5086 7890 -261 -381 1058 C ATOM 5126 N THR C 162 6.185 2.031 -4.652 1.00 62.99 N ANISOU 5126 N THR C 162 8159 6067 9706 -38 -432 603 N ATOM 5127 CA THR C 162 5.457 1.199 -3.723 1.00 62.25 C ANISOU 5127 CA THR C 162 8049 6063 9542 25 -307 407 C ATOM 5128 C THR C 162 4.266 0.600 -4.488 1.00 59.77 C ANISOU 5128 C THR C 162 7725 5793 9190 31 -313 430 C ATOM 5129 O THR C 162 3.474 1.322 -5.091 1.00 63.36 O ANISOU 5129 O THR C 162 8129 6146 9800 47 -446 472 O ATOM 5130 CB THR C 162 5.106 2.001 -2.421 1.00 47.52 C ANISOU 5130 CB THR C 162 6085 4123 7846 106 -333 184 C ATOM 5131 OG1 THR C 162 4.036 1.370 -1.710 1.00 59.05 O ANISOU 5131 OG1 THR C 162 7488 5695 9255 157 -244 13 O ATOM 5132 CG2 THR C 162 4.719 3.435 -2.738 1.00 40.77 C ANISOU 5132 CG2 THR C 162 5146 3054 7289 141 -534 182 C ATOM 5133 N LEU C 163 4.167 -0.722 -4.524 1.00 54.70 N ANISOU 5133 N LEU C 163 7128 5291 8363 14 -188 417 N ATOM 5134 CA LEU C 163 3.115 -1.336 -5.350 1.00 63.30 C ANISOU 5134 CA LEU C 163 8209 6424 9417 11 -202 443 C ATOM 5135 C LEU C 163 2.131 -2.242 -4.592 1.00 61.95 C ANISOU 5135 C LEU C 163 7998 6326 9215 46 -110 305 C ATOM 5136 O LEU C 163 2.512 -3.219 -3.941 1.00 58.27 O ANISOU 5136 O LEU C 163 7556 5950 8635 27 2 270 O ATOM 5137 CB LEU C 163 3.725 -2.068 -6.549 1.00 65.28 C ANISOU 5137 CB LEU C 163 8527 6774 9503 -56 -186 578 C ATOM 5138 CG LEU C 163 2.802 -2.818 -7.504 1.00 65.78 C ANISOU 5138 CG LEU C 163 8583 6908 9503 -66 -201 593 C ATOM 5139 CD1 LEU C 163 3.495 -3.072 -8.824 1.00 65.66 C ANISOU 5139 CD1 LEU C 163 8599 7010 9339 -134 -226 718 C ATOM 5140 CD2 LEU C 163 2.366 -4.126 -6.900 1.00 63.41 C ANISOU 5140 CD2 LEU C 163 8282 6666 9144 -45 -91 475 C ATOM 5141 N THR C 164 0.854 -1.906 -4.677 1.00 65.40 N ANISOU 5141 N THR C 164 8360 6724 9765 88 -170 242 N ATOM 5142 CA THR C 164 -0.163 -2.729 -4.037 1.00 71.95 C ANISOU 5142 CA THR C 164 9131 7644 10563 105 -91 131 C ATOM 5143 C THR C 164 -1.229 -3.183 -5.031 1.00 69.77 C ANISOU 5143 C THR C 164 8842 7371 10298 100 -141 172 C ATOM 5144 O THR C 164 -1.373 -2.618 -6.123 1.00 69.17 O ANISOU 5144 O THR C 164 8779 7226 10277 96 -254 266 O ATOM 5145 CB THR C 164 -0.823 -2.029 -2.812 1.00 85.18 C ANISOU 5145 CB THR C 164 10684 9332 12348 168 -82 -55 C ATOM 5146 OG1 THR C 164 -1.524 -0.846 -3.230 1.00 82.48 O ANISOU 5146 OG1 THR C 164 10269 8855 12214 229 -223 -101 O ATOM 5147 CG2 THR C 164 0.230 -1.683 -1.751 1.00 82.30 C ANISOU 5147 CG2 THR C 164 10322 8999 11948 169 -27 -118 C ATOM 5148 N TRP C 165 -1.948 -4.228 -4.645 1.00 59.79 N ANISOU 5148 N TRP C 165 7544 6198 8976 88 -63 119 N ATOM 5149 CA TRP C 165 -3.065 -4.718 -5.415 1.00 56.29 C ANISOU 5149 CA TRP C 165 7070 5763 8554 85 -106 130 C ATOM 5150 C TRP C 165 -4.335 -4.554 -4.622 1.00 64.89 C ANISOU 5150 C TRP C 165 8033 6892 9732 123 -92 3 C ATOM 5151 O TRP C 165 -4.430 -5.038 -3.504 1.00 69.82 O ANISOU 5151 O TRP C 165 8602 7623 10302 106 7 -64 O ATOM 5152 CB TRP C 165 -2.862 -6.175 -5.693 1.00 56.79 C ANISOU 5152 CB TRP C 165 7182 5892 8503 29 -44 174 C ATOM 5153 CG TRP C 165 -1.803 -6.411 -6.673 1.00 64.78 C ANISOU 5153 CG TRP C 165 8287 6899 9427 0 -65 259 C ATOM 5154 CD1 TRP C 165 -0.492 -6.642 -6.420 1.00 62.89 C ANISOU 5154 CD1 TRP C 165 8110 6675 9111 -22 -11 288 C ATOM 5155 CD2 TRP C 165 -1.958 -6.450 -8.091 1.00 69.97 C ANISOU 5155 CD2 TRP C 165 8967 7572 10048 -14 -146 315 C ATOM 5156 NE1 TRP C 165 0.186 -6.833 -7.595 1.00 67.92 N ANISOU 5156 NE1 TRP C 165 8799 7344 9665 -46 -46 345 N ATOM 5157 CE2 TRP C 165 -0.694 -6.720 -8.638 1.00 71.12 C ANISOU 5157 CE2 TRP C 165 9178 7766 10079 -47 -128 363 C ATOM 5158 CE3 TRP C 165 -3.046 -6.286 -8.951 1.00 69.10 C ANISOU 5158 CE3 TRP C 165 8815 7461 9980 -7 -235 325 C ATOM 5159 CZ2 TRP C 165 -0.484 -6.827 -10.000 1.00 73.36 C ANISOU 5159 CZ2 TRP C 165 9475 8133 10267 -77 -186 411 C ATOM 5160 CZ3 TRP C 165 -2.838 -6.395 -10.291 1.00 74.74 C ANISOU 5160 CZ3 TRP C 165 9553 8242 10602 -40 -301 390 C ATOM 5161 CH2 TRP C 165 -1.566 -6.662 -10.811 1.00 76.48 C ANISOU 5161 CH2 TRP C 165 9828 8545 10685 -77 -273 427 C ATOM 5162 N ASN C 166 -5.313 -3.868 -5.196 1.00 67.71 N ANISOU 5162 N ASN C 166 8326 7182 10220 169 -196 -24 N ATOM 5163 CA ASN C 166 -6.568 -3.635 -4.500 1.00 63.54 C ANISOU 5163 CA ASN C 166 7651 6700 9789 216 -189 -172 C ATOM 5164 C ASN C 166 -6.354 -2.970 -3.147 1.00 63.87 C ANISOU 5164 C ASN C 166 7604 6802 9864 259 -132 -331 C ATOM 5165 O ASN C 166 -7.082 -3.248 -2.190 1.00 58.57 O ANISOU 5165 O ASN C 166 6807 6283 9164 261 -51 -460 O ATOM 5166 CB ASN C 166 -7.361 -4.937 -4.360 1.00 56.09 C ANISOU 5166 CB ASN C 166 6673 5880 8760 163 -111 -166 C ATOM 5167 CG ASN C 166 -8.069 -5.318 -5.648 1.00 63.47 C ANISOU 5167 CG ASN C 166 7631 6759 9725 152 -199 -90 C ATOM 5168 OD1 ASN C 166 -7.942 -4.634 -6.671 1.00 60.36 O ANISOU 5168 OD1 ASN C 166 7283 6263 9390 175 -315 -22 O ATOM 5169 ND2 ASN C 166 -8.820 -6.408 -5.608 1.00 70.01 N ANISOU 5169 ND2 ASN C 166 8419 7667 10516 106 -156 -88 N ATOM 5170 N SER C 167 -5.345 -2.097 -3.093 1.00 65.67 N ANISOU 5170 N SER C 167 7881 6929 10141 283 -178 -323 N ATOM 5171 CA SER C 167 -5.067 -1.234 -1.941 1.00 66.32 C ANISOU 5171 CA SER C 167 7870 7036 10291 338 -160 -503 C ATOM 5172 C SER C 167 -4.721 -2.059 -0.709 1.00 69.38 C ANISOU 5172 C SER C 167 8234 7646 10482 285 4 -556 C ATOM 5173 O SER C 167 -5.116 -1.723 0.424 1.00 64.26 O ANISOU 5173 O SER C 167 7438 7147 9832 319 57 -755 O ATOM 5174 CB SER C 167 -6.248 -0.298 -1.650 1.00 67.65 C ANISOU 5174 CB SER C 167 7858 7173 10671 437 -244 -714 C ATOM 5175 OG SER C 167 -7.028 -0.045 -2.814 1.00 70.38 O ANISOU 5175 OG SER C 167 8205 7374 11162 459 -379 -629 O ATOM 5176 N GLY C 168 -3.985 -3.146 -0.947 1.00 69.59 N ANISOU 5176 N GLY C 168 8387 7708 10345 199 73 -381 N ATOM 5177 CA GLY C 168 -3.541 -4.028 0.116 1.00 68.30 C ANISOU 5177 CA GLY C 168 8213 7732 10008 128 201 -365 C ATOM 5178 C GLY C 168 -4.623 -5.020 0.477 1.00 72.36 C ANISOU 5178 C GLY C 168 8631 8410 10452 72 265 -357 C ATOM 5179 O GLY C 168 -4.397 -5.987 1.188 1.00 77.55 O ANISOU 5179 O GLY C 168 9276 9216 10975 -17 349 -277 O ATOM 5180 N SER C 169 -5.827 -4.784 -0.011 1.00 77.78 N ANISOU 5180 N SER C 169 9239 9070 11245 114 213 -423 N ATOM 5181 CA SER C 169 -6.904 -5.700 0.309 1.00 82.53 C ANISOU 5181 CA SER C 169 9735 9831 11790 53 268 -409 C ATOM 5182 C SER C 169 -6.634 -7.022 -0.404 1.00 83.32 C ANISOU 5182 C SER C 169 9955 9862 11841 -32 264 -203 C ATOM 5183 O SER C 169 -7.269 -8.030 -0.094 1.00 93.42 O ANISOU 5183 O SER C 169 11166 11254 13074 -114 303 -134 O ATOM 5184 CB SER C 169 -8.280 -5.108 -0.048 1.00 79.29 C ANISOU 5184 CB SER C 169 9200 9408 11519 126 206 -543 C ATOM 5185 OG SER C 169 -8.708 -5.507 -1.340 1.00 79.76 O ANISOU 5185 OG SER C 169 9341 9310 11652 123 123 -429 O ATOM 5186 N LEU C 170 -5.707 -7.005 -1.370 1.00 71.90 N ANISOU 5186 N LEU C 170 8666 8238 10416 -15 208 -114 N ATOM 5187 CA LEU C 170 -5.271 -8.228 -2.041 1.00 66.42 C ANISOU 5187 CA LEU C 170 8070 7479 9685 -79 198 30 C ATOM 5188 C LEU C 170 -3.923 -8.565 -1.452 1.00 80.66 C ANISOU 5188 C LEU C 170 9946 9299 11403 -120 250 98 C ATOM 5189 O LEU C 170 -2.886 -8.004 -1.836 1.00 78.34 O ANISOU 5189 O LEU C 170 9749 8918 11101 -83 230 104 O ATOM 5190 CB LEU C 170 -5.118 -8.014 -3.549 1.00 58.61 C ANISOU 5190 CB LEU C 170 7181 6338 8749 -37 104 61 C ATOM 5191 CG LEU C 170 -5.854 -8.936 -4.532 1.00 60.89 C ANISOU 5191 CG LEU C 170 7473 6591 9071 -63 51 99 C ATOM 5192 CD1 LEU C 170 -5.239 -8.845 -5.917 1.00 60.56 C ANISOU 5192 CD1 LEU C 170 7536 6463 9012 -43 -23 137 C ATOM 5193 CD2 LEU C 170 -5.840 -10.371 -4.077 1.00 58.78 C ANISOU 5193 CD2 LEU C 170 7185 6361 8788 -146 89 163 C ATOM 5194 N SER C 171 -3.937 -9.548 -0.566 1.00 90.62 N ANISOU 5194 N SER C 171 11152 10672 12607 -208 303 173 N ATOM 5195 CA SER C 171 -2.798 -9.804 0.282 1.00 88.08 C ANISOU 5195 CA SER C 171 10860 10403 12203 -255 351 238 C ATOM 5196 C SER C 171 -2.043 -10.968 -0.321 1.00 83.04 C ANISOU 5196 C SER C 171 10313 9638 11601 -297 310 359 C ATOM 5197 O SER C 171 -0.966 -10.798 -0.887 1.00 85.13 O ANISOU 5197 O SER C 171 10683 9799 11864 -259 292 358 O ATOM 5198 CB SER C 171 -3.254 -10.118 1.718 1.00 90.08 C ANISOU 5198 CB SER C 171 10971 10892 12364 -342 421 266 C ATOM 5199 OG SER C 171 -4.674 -10.105 1.877 1.00 83.37 O ANISOU 5199 OG SER C 171 9986 10162 11529 -356 432 212 O ATOM 5200 N SER C 172 -2.638 -12.148 -0.239 1.00 75.30 N ANISOU 5200 N SER C 172 9273 8664 10672 -376 284 452 N ATOM 5201 CA SER C 172 -1.973 -13.353 -0.704 1.00 71.80 C ANISOU 5201 CA SER C 172 8883 8086 10313 -414 223 541 C ATOM 5202 C SER C 172 -1.917 -13.443 -2.229 1.00 63.68 C ANISOU 5202 C SER C 172 7933 6907 9354 -341 158 456 C ATOM 5203 O SER C 172 -2.676 -12.782 -2.927 1.00 52.08 O ANISOU 5203 O SER C 172 6465 5442 7882 -287 146 375 O ATOM 5204 CB SER C 172 -2.623 -14.590 -0.089 1.00 72.97 C ANISOU 5204 CB SER C 172 8923 8268 10534 -533 187 683 C ATOM 5205 OG SER C 172 -4.018 -14.411 0.046 1.00 76.50 O ANISOU 5205 OG SER C 172 9268 8824 10975 -556 203 662 O ATOM 5206 N GLY C 173 -0.977 -14.241 -2.727 1.00 64.10 N ANISOU 5206 N GLY C 173 8039 6849 9467 -339 110 467 N ATOM 5207 CA GLY C 173 -0.845 -14.488 -4.148 1.00 64.84 C ANISOU 5207 CA GLY C 173 8179 6852 9603 -281 49 366 C ATOM 5208 C GLY C 173 0.152 -13.610 -4.874 1.00 66.00 C ANISOU 5208 C GLY C 173 8415 7013 9648 -213 73 297 C ATOM 5209 O GLY C 173 0.493 -13.874 -6.025 1.00 71.94 O ANISOU 5209 O GLY C 173 9193 7742 10399 -177 29 214 O ATOM 5210 N VAL C 174 0.645 -12.578 -4.205 1.00 60.46 N ANISOU 5210 N VAL C 174 7748 6369 8857 -201 136 328 N ATOM 5211 CA VAL C 174 1.393 -11.543 -4.907 1.00 59.14 C ANISOU 5211 CA VAL C 174 7650 6217 8604 -151 144 292 C ATOM 5212 C VAL C 174 2.873 -11.848 -4.908 1.00 58.59 C ANISOU 5212 C VAL C 174 7626 6131 8504 -150 161 296 C ATOM 5213 O VAL C 174 3.379 -12.459 -3.973 1.00 63.84 O ANISOU 5213 O VAL C 174 8276 6774 9205 -183 180 345 O ATOM 5214 CB VAL C 174 1.145 -10.133 -4.306 1.00 57.26 C ANISOU 5214 CB VAL C 174 7412 6020 8326 -129 178 300 C ATOM 5215 CG1 VAL C 174 1.716 -9.063 -5.201 1.00 52.87 C ANISOU 5215 CG1 VAL C 174 6911 5456 7722 -94 148 298 C ATOM 5216 CG2 VAL C 174 -0.327 -9.897 -4.100 1.00 59.76 C ANISOU 5216 CG2 VAL C 174 7654 6362 8689 -126 165 274 C ATOM 5217 N HIS C 175 3.540 -11.478 -5.998 1.00 57.33 N ANISOU 5217 N HIS C 175 7505 5999 8277 -121 145 254 N ATOM 5218 CA HIS C 175 5.000 -11.446 -6.068 1.00 54.02 C ANISOU 5218 CA HIS C 175 7122 5598 7806 -115 170 251 C ATOM 5219 C HIS C 175 5.429 -10.145 -6.667 1.00 55.77 C ANISOU 5219 C HIS C 175 7382 5885 7924 -107 174 283 C ATOM 5220 O HIS C 175 5.186 -9.880 -7.832 1.00 63.66 O ANISOU 5220 O HIS C 175 8375 6951 8863 -106 135 268 O ATOM 5221 CB HIS C 175 5.561 -12.569 -6.946 1.00 56.89 C ANISOU 5221 CB HIS C 175 7456 5967 8194 -101 135 149 C ATOM 5222 CG HIS C 175 5.388 -13.927 -6.358 1.00 62.98 C ANISOU 5222 CG HIS C 175 8178 6630 9122 -113 98 130 C ATOM 5223 ND1 HIS C 175 5.783 -14.233 -5.073 1.00 65.34 N ANISOU 5223 ND1 HIS C 175 8474 6866 9488 -147 115 225 N ATOM 5224 CD2 HIS C 175 4.831 -15.051 -6.862 1.00 73.16 C ANISOU 5224 CD2 HIS C 175 9406 7858 10533 -108 27 44 C ATOM 5225 CE1 HIS C 175 5.490 -15.494 -4.816 1.00 77.76 C ANISOU 5225 CE1 HIS C 175 9985 8337 11225 -170 47 227 C ATOM 5226 NE2 HIS C 175 4.907 -16.011 -5.881 1.00 82.22 N ANISOU 5226 NE2 HIS C 175 10514 8885 11842 -143 -10 108 N ATOM 5227 N THR C 176 6.097 -9.332 -5.880 1.00 62.24 N ANISOU 5227 N THR C 176 8231 6692 8726 -112 209 339 N ATOM 5228 CA THR C 176 6.674 -8.125 -6.424 1.00 64.60 C ANISOU 5228 CA THR C 176 8557 7029 8958 -118 193 394 C ATOM 5229 C THR C 176 8.168 -8.353 -6.596 1.00 67.30 C ANISOU 5229 C THR C 176 8915 7422 9234 -131 225 394 C ATOM 5230 O THR C 176 8.881 -8.693 -5.651 1.00 77.95 O ANISOU 5230 O THR C 176 10274 8733 10611 -129 265 390 O ATOM 5231 CB THR C 176 6.381 -6.918 -5.529 1.00 70.21 C ANISOU 5231 CB THR C 176 9272 7679 9726 -110 187 433 C ATOM 5232 OG1 THR C 176 4.955 -6.749 -5.398 1.00 72.33 O ANISOU 5232 OG1 THR C 176 9502 7916 10063 -90 157 404 O ATOM 5233 CG2 THR C 176 7.018 -5.668 -6.113 1.00 65.73 C ANISOU 5233 CG2 THR C 176 8722 7115 9138 -127 138 514 C ATOM 5234 N PHE C 177 8.628 -8.204 -7.827 1.00 61.63 N ANISOU 5234 N PHE C 177 8184 6816 8417 -149 203 399 N ATOM 5235 CA PHE C 177 10.009 -8.476 -8.171 1.00 51.78 C ANISOU 5235 CA PHE C 177 6923 5661 7089 -162 236 375 C ATOM 5236 C PHE C 177 10.921 -7.261 -8.005 1.00 57.89 C ANISOU 5236 C PHE C 177 7721 6455 7821 -200 239 493 C ATOM 5237 O PHE C 177 10.491 -6.118 -8.130 1.00 53.05 O ANISOU 5237 O PHE C 177 7120 5813 7224 -226 188 600 O ATOM 5238 CB PHE C 177 10.084 -8.994 -9.601 1.00 46.05 C ANISOU 5238 CB PHE C 177 6139 5108 6248 -171 218 297 C ATOM 5239 CG PHE C 177 9.295 -10.246 -9.826 1.00 55.95 C ANISOU 5239 CG PHE C 177 7356 6331 7570 -131 199 153 C ATOM 5240 CD1 PHE C 177 9.914 -11.489 -9.802 1.00 53.73 C ANISOU 5240 CD1 PHE C 177 7026 6042 7347 -93 209 1 C ATOM 5241 CD2 PHE C 177 7.920 -10.182 -10.065 1.00 57.67 C ANISOU 5241 CD2 PHE C 177 7575 6512 7824 -129 153 167 C ATOM 5242 CE1 PHE C 177 9.174 -12.642 -10.013 1.00 52.63 C ANISOU 5242 CE1 PHE C 177 6839 5842 7315 -59 165 -132 C ATOM 5243 CE2 PHE C 177 7.170 -11.341 -10.273 1.00 53.91 C ANISOU 5243 CE2 PHE C 177 7058 5997 7430 -99 124 39 C ATOM 5244 CZ PHE C 177 7.793 -12.565 -10.245 1.00 51.09 C ANISOU 5244 CZ PHE C 177 6651 5615 7144 -66 124 -108 C ATOM 5245 N PRO C 178 12.199 -7.522 -7.710 1.00 63.66 N ANISOU 5245 N PRO C 178 8448 7218 8524 -203 285 472 N ATOM 5246 CA PRO C 178 13.263 -6.526 -7.686 1.00 49.81 C ANISOU 5246 CA PRO C 178 6700 5505 6722 -248 287 575 C ATOM 5247 C PRO C 178 13.311 -5.810 -9.015 1.00 55.72 C ANISOU 5247 C PRO C 178 7408 6415 7347 -315 242 676 C ATOM 5248 O PRO C 178 13.091 -6.437 -10.062 1.00 48.81 O ANISOU 5248 O PRO C 178 6482 5699 6365 -322 242 609 O ATOM 5249 CB PRO C 178 14.505 -7.376 -7.561 1.00 50.31 C ANISOU 5249 CB PRO C 178 6734 5630 6753 -233 343 488 C ATOM 5250 CG PRO C 178 14.045 -8.602 -6.899 1.00 58.09 C ANISOU 5250 CG PRO C 178 7721 6508 7842 -175 355 375 C ATOM 5251 CD PRO C 178 12.705 -8.869 -7.404 1.00 64.58 C ANISOU 5251 CD PRO C 178 8538 7320 8680 -163 320 345 C ATOM 5252 N ALA C 179 13.601 -4.509 -8.956 1.00 61.53 N ANISOU 5252 N ALA C 179 8155 7118 8107 -371 191 837 N ATOM 5253 CA ALA C 179 13.669 -3.649 -10.126 1.00 58.19 C ANISOU 5253 CA ALA C 179 7683 6839 7586 -465 119 1004 C ATOM 5254 C ALA C 179 14.982 -3.841 -10.861 1.00 61.30 C ANISOU 5254 C ALA C 179 8010 7479 7804 -531 166 1026 C ATOM 5255 O ALA C 179 15.992 -4.222 -10.263 1.00 56.87 O ANISOU 5255 O ALA C 179 7452 6908 7248 -505 235 949 O ATOM 5256 CB ALA C 179 13.528 -2.217 -9.705 1.00 60.23 C ANISOU 5256 CB ALA C 179 7961 6933 7993 -503 20 1173 C ATOM 5257 N VAL C 180 14.959 -3.572 -12.164 1.00 67.61 N ANISOU 5257 N VAL C 180 8733 8520 8434 -621 125 1133 N ATOM 5258 CA VAL C 180 16.137 -3.698 -13.012 1.00 70.31 C ANISOU 5258 CA VAL C 180 8976 9174 8565 -702 171 1156 C ATOM 5259 C VAL C 180 16.348 -2.432 -13.841 1.00 75.37 C ANISOU 5259 C VAL C 180 9555 9965 9118 -860 72 1460 C ATOM 5260 O VAL C 180 15.378 -1.805 -14.265 1.00 78.90 O ANISOU 5260 O VAL C 180 10007 10365 9605 -905 -37 1613 O ATOM 5261 CB VAL C 180 15.994 -4.904 -13.939 1.00 75.16 C ANISOU 5261 CB VAL C 180 9508 10050 9000 -671 229 943 C ATOM 5262 CG1 VAL C 180 16.924 -4.773 -15.129 1.00 80.87 C ANISOU 5262 CG1 VAL C 180 10089 11188 9451 -787 252 999 C ATOM 5263 CG2 VAL C 180 16.260 -6.191 -13.159 1.00 72.67 C ANISOU 5263 CG2 VAL C 180 9217 9607 8788 -538 314 664 C ATOM 5264 N LEU C 181 17.604 -2.046 -14.070 1.00 75.49 N ANISOU 5264 N LEU C 181 9501 10156 9027 -953 95 1567 N ATOM 5265 CA LEU C 181 17.877 -0.845 -14.862 1.00 74.62 C ANISOU 5265 CA LEU C 181 9312 10200 8839 -1132 -16 1902 C ATOM 5266 C LEU C 181 17.891 -1.118 -16.360 1.00 79.85 C ANISOU 5266 C LEU C 181 9835 11324 9182 -1246 -10 1957 C ATOM 5267 O LEU C 181 18.730 -1.845 -16.868 1.00 82.47 O ANISOU 5267 O LEU C 181 10063 11985 9286 -1259 100 1806 O ATOM 5268 CB LEU C 181 19.183 -0.170 -14.432 1.00 68.49 C ANISOU 5268 CB LEU C 181 8510 9410 8103 -1207 -13 2037 C ATOM 5269 CG LEU C 181 19.038 0.746 -13.217 1.00 73.99 C ANISOU 5269 CG LEU C 181 9310 9677 9125 -1165 -102 2121 C ATOM 5270 CD1 LEU C 181 20.357 1.363 -12.828 1.00 75.95 C ANISOU 5270 CD1 LEU C 181 9524 9921 9413 -1242 -104 2240 C ATOM 5271 CD2 LEU C 181 18.040 1.840 -13.518 1.00 84.81 C ANISOU 5271 CD2 LEU C 181 10685 10887 10653 -1234 -286 2367 C ATOM 5272 N GLN C 182 16.948 -0.513 -17.065 1.00 89.30 N ANISOU 5272 N GLN C 182 11011 12559 10362 -1331 -138 2167 N ATOM 5273 CA GLN C 182 16.871 -0.663 -18.505 1.00103.02 C ANISOU 5273 CA GLN C 182 12604 14765 11775 -1462 -153 2255 C ATOM 5274 C GLN C 182 17.446 0.630 -19.046 1.00108.17 C ANISOU 5274 C GLN C 182 13162 15564 12373 -1683 -281 2685 C ATOM 5275 O GLN C 182 16.793 1.675 -19.013 1.00108.14 O ANISOU 5275 O GLN C 182 13191 15332 12566 -1755 -458 2979 O ATOM 5276 CB GLN C 182 15.403 -0.858 -18.924 1.00111.11 C ANISOU 5276 CB GLN C 182 13660 15733 12822 -1421 -229 2229 C ATOM 5277 CG GLN C 182 15.118 -0.861 -20.425 1.00123.25 C ANISOU 5277 CG GLN C 182 15048 17750 14032 -1571 -281 2361 C ATOM 5278 CD GLN C 182 15.547 -2.143 -21.126 1.00131.46 C ANISOU 5278 CD GLN C 182 15972 19222 14756 -1529 -127 2020 C ATOM 5279 OE1 GLN C 182 16.580 -2.729 -20.795 1.00136.66 O ANISOU 5279 OE1 GLN C 182 16599 19961 15365 -1472 4 1806 O ATOM 5280 NE2 GLN C 182 14.753 -2.580 -22.108 1.00130.37 N ANISOU 5280 NE2 GLN C 182 15756 19363 14416 -1555 -155 1952 N ATOM 5281 N SER C 183 18.670 0.553 -19.559 1.00111.81 N ANISOU 5281 N SER C 183 13490 16411 12583 -1797 -202 2726 N ATOM 5282 CA SER C 183 19.435 1.760 -19.850 1.00111.49 C ANISOU 5282 CA SER C 183 13360 16472 12530 -2011 -315 3141 C ATOM 5283 C SER C 183 19.464 2.668 -18.620 1.00114.40 C ANISOU 5283 C SER C 183 13862 16277 13327 -1951 -419 3246 C ATOM 5284 O SER C 183 20.035 2.304 -17.593 1.00120.61 O ANISOU 5284 O SER C 183 14733 16848 14243 -1827 -313 3036 O ATOM 5285 CB SER C 183 18.901 2.482 -21.082 1.00105.86 C ANISOU 5285 CB SER C 183 12516 15986 11721 -2159 -488 3391 C ATOM 5286 OG SER C 183 19.319 1.805 -22.254 1.00102.76 O ANISOU 5286 OG SER C 183 11943 16193 10908 -2244 -391 3290 O ATOM 5287 N ASP C 184 18.862 3.848 -18.722 1.00108.11 N ANISOU 5287 N ASP C 184 13061 15228 12787 -1992 -638 3466 N ATOM 5288 CA ASP C 184 18.921 4.821 -17.633 1.00103.65 C ANISOU 5288 CA ASP C 184 12581 14167 12634 -1924 -755 3506 C ATOM 5289 C ASP C 184 17.933 4.579 -16.474 1.00 92.50 C ANISOU 5289 C ASP C 184 11344 12301 11500 -1745 -746 3329 C ATOM 5290 O ASP C 184 18.183 4.982 -15.334 1.00 82.89 O ANISOU 5290 O ASP C 184 10205 10733 10558 -1651 -761 3235 O ATOM 5291 CB ASP C 184 18.732 6.228 -18.197 1.00113.43 C ANISOU 5291 CB ASP C 184 13707 15334 14057 -2040 -1005 3783 C ATOM 5292 CG ASP C 184 19.525 7.269 -17.438 1.00120.86 C ANISOU 5292 CG ASP C 184 14637 15996 15287 -2040 -1107 3843 C ATOM 5293 OD1 ASP C 184 20.369 6.872 -16.596 1.00124.55 O ANISOU 5293 OD1 ASP C 184 15174 16393 15758 -1969 -970 3684 O ATOM 5294 OD2 ASP C 184 19.306 8.476 -17.693 1.00118.61 O ANISOU 5294 OD2 ASP C 184 14264 15573 15230 -2117 -1331 4049 O ATOM 5295 N LEU C 185 16.821 3.912 -16.774 1.00 89.79 N ANISOU 5295 N LEU C 185 11048 11993 11076 -1701 -723 3271 N ATOM 5296 CA LEU C 185 15.648 3.925 -15.906 1.00 78.88 C ANISOU 5296 CA LEU C 185 9786 10196 9988 -1531 -768 3101 C ATOM 5297 C LEU C 185 15.207 2.553 -15.440 1.00 76.64 C ANISOU 5297 C LEU C 185 9589 9917 9613 -1342 -578 2697 C ATOM 5298 O LEU C 185 15.365 1.572 -16.157 1.00 78.16 O ANISOU 5298 O LEU C 185 9736 10449 9513 -1347 -457 2566 O ATOM 5299 CB LEU C 185 14.499 4.558 -16.664 1.00 78.77 C ANISOU 5299 CB LEU C 185 9726 10149 10055 -1594 -958 3309 C ATOM 5300 CG LEU C 185 14.867 5.934 -17.200 1.00 83.36 C ANISOU 5300 CG LEU C 185 10174 10732 10766 -1716 -1157 3548 C ATOM 5301 CD1 LEU C 185 13.721 6.477 -18.019 1.00 87.38 C ANISOU 5301 CD1 LEU C 185 10613 11239 11349 -1771 -1342 3713 C ATOM 5302 CD2 LEU C 185 15.199 6.848 -16.030 1.00 81.77 C ANISOU 5302 CD2 LEU C 185 10008 10125 10935 -1630 -1236 3475 C ATOM 5303 N TYR C 186 14.624 2.505 -14.245 1.00 74.93 N ANISOU 5303 N TYR C 186 9479 9331 9659 -1182 -566 2499 N ATOM 5304 CA TYR C 186 14.134 1.260 -13.654 1.00 73.41 C ANISOU 5304 CA TYR C 186 9365 9096 9431 -1014 -411 2153 C ATOM 5305 C TYR C 186 12.830 0.731 -14.236 1.00 73.61 C ANISOU 5305 C TYR C 186 9393 9173 9404 -971 -430 2080 C ATOM 5306 O TYR C 186 11.902 1.481 -14.553 1.00 72.68 O ANISOU 5306 O TYR C 186 9258 8941 9416 -1005 -582 2239 O ATOM 5307 CB TYR C 186 13.883 1.455 -12.172 1.00 76.32 C ANISOU 5307 CB TYR C 186 9824 9097 10076 -882 -401 1995 C ATOM 5308 CG TYR C 186 15.094 1.824 -11.383 1.00 82.21 C ANISOU 5308 CG TYR C 186 10582 9763 10892 -893 -369 2000 C ATOM 5309 CD1 TYR C 186 15.966 0.845 -10.943 1.00 86.20 C ANISOU 5309 CD1 TYR C 186 11112 10376 11266 -839 -206 1813 C ATOM 5310 CD2 TYR C 186 15.357 3.150 -11.052 1.00 79.06 C ANISOU 5310 CD2 TYR C 186 10160 9158 10721 -953 -519 2184 C ATOM 5311 CE1 TYR C 186 17.075 1.169 -10.203 1.00 89.98 C ANISOU 5311 CE1 TYR C 186 11597 10784 11806 -848 -179 1816 C ATOM 5312 CE2 TYR C 186 16.454 3.486 -10.306 1.00 79.70 C ANISOU 5312 CE2 TYR C 186 10248 9161 10874 -962 -495 2175 C ATOM 5313 CZ TYR C 186 17.318 2.489 -9.882 1.00 86.92 C ANISOU 5313 CZ TYR C 186 11193 10209 11624 -911 -318 1994 C ATOM 5314 OH TYR C 186 18.436 2.795 -9.136 1.00 85.19 O ANISOU 5314 OH TYR C 186 10977 9923 11469 -921 -294 1984 O ATOM 5315 N THR C 187 12.741 -0.582 -14.328 1.00 69.71 N ANISOU 5315 N THR C 187 8913 8825 8751 -890 -289 1826 N ATOM 5316 CA THR C 187 11.489 -1.199 -14.690 1.00 70.34 C ANISOU 5316 CA THR C 187 9002 8913 8813 -829 -298 1712 C ATOM 5317 C THR C 187 11.226 -2.364 -13.759 1.00 66.19 C ANISOU 5317 C THR C 187 8546 8248 8355 -678 -171 1406 C ATOM 5318 O THR C 187 12.124 -3.140 -13.442 1.00 67.88 O ANISOU 5318 O THR C 187 8763 8534 8497 -641 -56 1255 O ATOM 5319 CB THR C 187 11.444 -1.624 -16.169 1.00 80.93 C ANISOU 5319 CB THR C 187 10242 10647 9861 -923 -303 1754 C ATOM 5320 OG1 THR C 187 10.214 -2.304 -16.421 1.00 90.12 O ANISOU 5320 OG1 THR C 187 11419 11792 11030 -850 -310 1609 O ATOM 5321 CG2 THR C 187 12.574 -2.555 -16.510 1.00 81.80 C ANISOU 5321 CG2 THR C 187 10292 11052 9737 -928 -163 1583 C ATOM 5322 N LEU C 188 9.983 -2.461 -13.309 1.00 68.15 N ANISOU 5322 N LEU C 188 8838 8296 8759 -598 -205 1332 N ATOM 5323 CA LEU C 188 9.581 -3.426 -12.291 1.00 70.13 C ANISOU 5323 CA LEU C 188 9147 8389 9109 -475 -111 1098 C ATOM 5324 C LEU C 188 8.234 -4.070 -12.646 1.00 69.37 C ANISOU 5324 C LEU C 188 9044 8288 9025 -428 -132 999 C ATOM 5325 O LEU C 188 7.503 -3.576 -13.507 1.00 74.75 O ANISOU 5325 O LEU C 188 9689 9036 9678 -477 -231 1116 O ATOM 5326 CB LEU C 188 9.532 -2.736 -10.922 1.00 67.71 C ANISOU 5326 CB LEU C 188 8895 7810 9022 -423 -122 1101 C ATOM 5327 CG LEU C 188 8.782 -3.404 -9.775 1.00 67.63 C ANISOU 5327 CG LEU C 188 8925 7637 9134 -320 -61 921 C ATOM 5328 CD1 LEU C 188 9.637 -3.375 -8.546 1.00 68.38 C ANISOU 5328 CD1 LEU C 188 9053 7636 9291 -290 6 866 C ATOM 5329 CD2 LEU C 188 7.440 -2.730 -9.496 1.00 69.10 C ANISOU 5329 CD2 LEU C 188 9102 7668 9486 -285 -148 936 C ATOM 5330 N SER C 189 7.919 -5.185 -11.996 1.00 62.50 N ANISOU 5330 N SER C 189 8201 7343 8205 -343 -51 800 N ATOM 5331 CA SER C 189 6.711 -5.944 -12.307 1.00 53.46 C ANISOU 5331 CA SER C 189 7040 6194 7080 -303 -67 693 C ATOM 5332 C SER C 189 6.207 -6.702 -11.090 1.00 49.89 C ANISOU 5332 C SER C 189 6623 5557 6777 -224 -9 559 C ATOM 5333 O SER C 189 6.980 -7.159 -10.276 1.00 53.36 O ANISOU 5333 O SER C 189 7086 5945 7245 -201 61 499 O ATOM 5334 CB SER C 189 6.988 -6.928 -13.441 1.00 51.94 C ANISOU 5334 CB SER C 189 6785 6242 6706 -321 -45 577 C ATOM 5335 OG SER C 189 7.952 -7.891 -13.042 1.00 52.55 O ANISOU 5335 OG SER C 189 6857 6335 6773 -282 43 422 O ATOM 5336 N SER C 190 4.900 -6.853 -10.974 1.00 56.35 N ANISOU 5336 N SER C 190 7433 6293 7686 -194 -45 526 N ATOM 5337 CA SER C 190 4.329 -7.644 -9.894 1.00 60.29 C ANISOU 5337 CA SER C 190 7940 6662 8304 -143 4 423 C ATOM 5338 C SER C 190 3.271 -8.563 -10.461 1.00 59.21 C ANISOU 5338 C SER C 190 7765 6550 8181 -130 -25 333 C ATOM 5339 O SER C 190 2.656 -8.257 -11.474 1.00 68.33 O ANISOU 5339 O SER C 190 8893 7785 9283 -148 -93 363 O ATOM 5340 CB SER C 190 3.720 -6.749 -8.820 1.00 59.37 C ANISOU 5340 CB SER C 190 7832 6409 8316 -120 -5 465 C ATOM 5341 OG SER C 190 3.278 -7.532 -7.730 1.00 57.24 O ANISOU 5341 OG SER C 190 7553 6076 8121 -94 53 386 O ATOM 5342 N SER C 191 3.060 -9.693 -9.811 1.00 49.22 N ANISOU 5342 N SER C 191 6489 5216 6998 -107 12 238 N ATOM 5343 CA SER C 191 2.052 -10.625 -10.271 1.00 48.01 C ANISOU 5343 CA SER C 191 6290 5059 6893 -98 -27 151 C ATOM 5344 C SER C 191 1.189 -11.070 -9.117 1.00 47.77 C ANISOU 5344 C SER C 191 6242 4905 7002 -93 -9 154 C ATOM 5345 O SER C 191 1.677 -11.266 -8.018 1.00 44.66 O ANISOU 5345 O SER C 191 5861 4454 6655 -99 42 181 O ATOM 5346 CB SER C 191 2.709 -11.838 -10.910 1.00 46.88 C ANISOU 5346 CB SER C 191 6111 4975 6727 -90 -31 13 C ATOM 5347 OG SER C 191 3.209 -12.710 -9.921 1.00 51.04 O ANISOU 5347 OG SER C 191 6636 5385 7370 -80 1 -19 O ATOM 5348 N VAL C 192 -0.105 -11.214 -9.370 1.00 56.91 N ANISOU 5348 N VAL C 192 7359 6048 8216 -91 -54 137 N ATOM 5349 CA VAL C 192 -1.009 -11.835 -8.413 1.00 51.28 C ANISOU 5349 CA VAL C 192 6601 5259 7624 -104 -42 139 C ATOM 5350 C VAL C 192 -1.554 -13.018 -9.115 1.00 52.77 C ANISOU 5350 C VAL C 192 6741 5430 7877 -111 -101 54 C ATOM 5351 O VAL C 192 -1.814 -12.965 -10.304 1.00 60.55 O ANISOU 5351 O VAL C 192 7717 6482 8806 -98 -156 -6 O ATOM 5352 CB VAL C 192 -2.231 -10.968 -8.089 1.00 49.51 C ANISOU 5352 CB VAL C 192 6343 5033 7436 -95 -52 173 C ATOM 5353 CG1 VAL C 192 -2.469 -10.937 -6.601 1.00 45.81 C ANISOU 5353 CG1 VAL C 192 5837 4551 7017 -112 13 205 C ATOM 5354 CG2 VAL C 192 -2.074 -9.560 -8.662 1.00 53.27 C ANISOU 5354 CG2 VAL C 192 6850 5536 7854 -69 -85 215 C ATOM 5355 N THR C 193 -1.724 -14.100 -8.386 1.00 55.59 N ANISOU 5355 N THR C 193 7057 5706 8360 -141 -105 56 N ATOM 5356 CA THR C 193 -2.492 -15.210 -8.906 1.00 52.42 C ANISOU 5356 CA THR C 193 6589 5252 8076 -154 -184 -19 C ATOM 5357 C THR C 193 -3.640 -15.448 -7.943 1.00 53.29 C ANISOU 5357 C THR C 193 6637 5322 8289 -205 -181 73 C ATOM 5358 O THR C 193 -3.478 -15.361 -6.720 1.00 50.83 O ANISOU 5358 O THR C 193 6315 5011 7986 -244 -124 178 O ATOM 5359 CB THR C 193 -1.627 -16.466 -9.094 1.00 48.66 C ANISOU 5359 CB THR C 193 6086 4696 7707 -152 -233 -108 C ATOM 5360 OG1 THR C 193 -2.174 -17.564 -8.354 1.00 47.74 O ANISOU 5360 OG1 THR C 193 5898 4450 7792 -206 -288 -55 O ATOM 5361 CG2 THR C 193 -0.199 -16.190 -8.656 1.00 45.38 C ANISOU 5361 CG2 THR C 193 5726 4292 7226 -138 -173 -81 C ATOM 5362 N VAL C 194 -4.815 -15.707 -8.499 1.00 51.74 N ANISOU 5362 N VAL C 194 6386 5123 8151 -210 -239 33 N ATOM 5363 CA VAL C 194 -5.992 -15.906 -7.677 1.00 52.93 C ANISOU 5363 CA VAL C 194 6456 5268 8387 -266 -236 116 C ATOM 5364 C VAL C 194 -6.783 -17.064 -8.236 1.00 61.78 C ANISOU 5364 C VAL C 194 7501 6309 9663 -296 -339 64 C ATOM 5365 O VAL C 194 -6.555 -17.462 -9.376 1.00 65.72 O ANISOU 5365 O VAL C 194 8013 6783 10177 -256 -409 -69 O ATOM 5366 CB VAL C 194 -6.849 -14.625 -7.623 1.00 45.32 C ANISOU 5366 CB VAL C 194 5484 4397 7337 -235 -196 126 C ATOM 5367 CG1 VAL C 194 -6.131 -13.564 -6.812 1.00 40.37 C ANISOU 5367 CG1 VAL C 194 4905 3825 6610 -213 -108 171 C ATOM 5368 CG2 VAL C 194 -7.118 -14.099 -9.025 1.00 42.09 C ANISOU 5368 CG2 VAL C 194 5108 4013 6872 -178 -258 42 C ATOM 5369 N THR C 195 -7.691 -17.613 -7.431 1.00 68.30 N ANISOU 5369 N THR C 195 8234 7114 10602 -375 -352 164 N ATOM 5370 CA THR C 195 -8.624 -18.641 -7.899 1.00 71.07 C ANISOU 5370 CA THR C 195 8496 7381 11126 -416 -461 133 C ATOM 5371 C THR C 195 -9.412 -18.049 -9.051 1.00 67.29 C ANISOU 5371 C THR C 195 8026 6962 10578 -352 -490 11 C ATOM 5372 O THR C 195 -9.860 -16.908 -8.952 1.00 74.70 O ANISOU 5372 O THR C 195 8982 8005 11395 -321 -427 33 O ATOM 5373 CB THR C 195 -9.616 -19.066 -6.792 1.00 78.92 C ANISOU 5373 CB THR C 195 9374 8399 12215 -528 -456 298 C ATOM 5374 OG1 THR C 195 -10.289 -17.914 -6.279 1.00 86.42 O ANISOU 5374 OG1 THR C 195 10306 9513 13017 -516 -353 329 O ATOM 5375 CG2 THR C 195 -8.904 -19.743 -5.642 1.00 80.24 C ANISOU 5375 CG2 THR C 195 9511 8526 12452 -619 -452 462 C ATOM 5376 N SER C 196 -9.582 -18.792 -10.142 1.00 60.60 N ANISOU 5376 N SER C 196 7155 6052 9818 -332 -598 -126 N ATOM 5377 CA SER C 196 -10.266 -18.226 -11.313 1.00 71.98 C ANISOU 5377 CA SER C 196 8601 7580 11167 -279 -637 -233 C ATOM 5378 C SER C 196 -11.715 -17.800 -11.034 1.00 73.12 C ANISOU 5378 C SER C 196 8675 7767 11339 -307 -634 -162 C ATOM 5379 O SER C 196 -12.324 -17.061 -11.811 1.00 75.33 O ANISOU 5379 O SER C 196 8961 8126 11535 -264 -658 -208 O ATOM 5380 CB SER C 196 -10.183 -19.158 -12.524 1.00 77.02 C ANISOU 5380 CB SER C 196 9205 8180 11879 -255 -756 -425 C ATOM 5381 OG SER C 196 -10.275 -20.513 -12.134 1.00 81.65 O ANISOU 5381 OG SER C 196 9709 8599 12717 -308 -842 -438 O ATOM 5382 N SER C 197 -12.252 -18.252 -9.908 1.00 75.18 N ANISOU 5382 N SER C 197 8858 7994 11714 -386 -610 -40 N ATOM 5383 CA SER C 197 -13.577 -17.831 -9.481 1.00 75.95 C ANISOU 5383 CA SER C 197 8865 8166 11827 -416 -588 22 C ATOM 5384 C SER C 197 -13.593 -16.347 -9.169 1.00 74.06 C ANISOU 5384 C SER C 197 8663 8044 11433 -354 -493 34 C ATOM 5385 O SER C 197 -14.655 -15.726 -9.203 1.00 81.01 O ANISOU 5385 O SER C 197 9475 8989 12315 -335 -495 21 O ATOM 5386 CB SER C 197 -14.027 -18.616 -8.247 1.00 78.25 C ANISOU 5386 CB SER C 197 9043 8450 12238 -536 -571 172 C ATOM 5387 OG SER C 197 -13.410 -18.135 -7.061 1.00 80.18 O ANISOU 5387 OG SER C 197 9301 8782 12380 -561 -456 278 O ATOM 5388 N THR C 198 -12.430 -15.797 -8.811 1.00 65.89 N ANISOU 5388 N THR C 198 7721 7024 10291 -321 -422 54 N ATOM 5389 CA THR C 198 -12.330 -14.375 -8.466 1.00 69.28 C ANISOU 5389 CA THR C 198 8178 7534 10611 -259 -351 55 C ATOM 5390 C THR C 198 -11.885 -13.398 -9.564 1.00 67.57 C ANISOU 5390 C THR C 198 8054 7316 10304 -177 -393 2 C ATOM 5391 O THR C 198 -11.996 -12.194 -9.402 1.00 69.30 O ANISOU 5391 O THR C 198 8275 7566 10489 -126 -376 6 O ATOM 5392 CB THR C 198 -11.493 -14.127 -7.184 1.00 57.77 C ANISOU 5392 CB THR C 198 6735 6121 9092 -283 -244 122 C ATOM 5393 OG1 THR C 198 -10.338 -13.341 -7.503 1.00 58.82 O ANISOU 5393 OG1 THR C 198 6986 6236 9127 -219 -223 100 O ATOM 5394 CG2 THR C 198 -11.095 -15.431 -6.528 1.00 48.43 C ANISOU 5394 CG2 THR C 198 5525 4900 7976 -378 -241 211 C ATOM 5395 N TRP C 199 -11.403 -13.894 -10.686 1.00 63.85 N ANISOU 5395 N TRP C 199 7639 6819 9801 -169 -462 -48 N ATOM 5396 CA TRP C 199 -11.150 -12.994 -11.787 1.00 63.38 C ANISOU 5396 CA TRP C 199 7636 6808 9635 -119 -516 -65 C ATOM 5397 C TRP C 199 -11.548 -13.716 -13.048 1.00 72.26 C ANISOU 5397 C TRP C 199 8738 7961 10755 -128 -617 -149 C ATOM 5398 O TRP C 199 -11.314 -14.916 -13.165 1.00 72.58 O ANISOU 5398 O TRP C 199 8761 7963 10853 -155 -636 -225 O ATOM 5399 CB TRP C 199 -9.675 -12.576 -11.844 1.00 57.98 C ANISOU 5399 CB TRP C 199 7053 6145 8833 -103 -470 -41 C ATOM 5400 CG TRP C 199 -9.437 -11.440 -12.791 1.00 55.50 C ANISOU 5400 CG TRP C 199 6778 5898 8410 -75 -527 2 C ATOM 5401 CD1 TRP C 199 -9.574 -10.110 -12.516 1.00 63.42 C ANISOU 5401 CD1 TRP C 199 7785 6883 9429 -46 -537 81 C ATOM 5402 CD2 TRP C 199 -9.060 -11.525 -14.173 1.00 50.64 C ANISOU 5402 CD2 TRP C 199 6184 5392 7666 -86 -600 -24 C ATOM 5403 NE1 TRP C 199 -9.298 -9.358 -13.639 1.00 63.47 N ANISOU 5403 NE1 TRP C 199 7817 6956 9341 -49 -625 148 N ATOM 5404 CE2 TRP C 199 -8.978 -10.203 -14.670 1.00 57.79 C ANISOU 5404 CE2 TRP C 199 7108 6346 8505 -80 -656 91 C ATOM 5405 CE3 TRP C 199 -8.780 -12.585 -15.037 1.00 46.75 C ANISOU 5405 CE3 TRP C 199 5676 4975 7112 -102 -634 -143 C ATOM 5406 CZ2 TRP C 199 -8.622 -9.913 -15.994 1.00 52.17 C ANISOU 5406 CZ2 TRP C 199 6401 5789 7631 -111 -736 131 C ATOM 5407 CZ3 TRP C 199 -8.428 -12.297 -16.358 1.00 48.06 C ANISOU 5407 CZ3 TRP C 199 5841 5316 7103 -117 -700 -154 C ATOM 5408 CH2 TRP C 199 -8.355 -10.970 -16.820 1.00 50.19 C ANISOU 5408 CH2 TRP C 199 6132 5665 7274 -131 -747 2 C ATOM 5409 N PRO C 200 -12.136 -12.992 -14.012 1.00 79.76 N ANISOU 5409 N PRO C 200 9674 8979 11650 -106 -699 -142 N ATOM 5410 CA PRO C 200 -12.477 -11.561 -14.074 1.00 75.75 C ANISOU 5410 CA PRO C 200 9169 8489 11125 -73 -728 -50 C ATOM 5411 C PRO C 200 -13.590 -11.156 -13.111 1.00 71.48 C ANISOU 5411 C PRO C 200 8542 7888 10730 -54 -706 -37 C ATOM 5412 O PRO C 200 -13.880 -9.970 -12.981 1.00 64.95 O ANISOU 5412 O PRO C 200 7695 7043 9941 -12 -735 9 O ATOM 5413 CB PRO C 200 -12.908 -11.363 -15.522 1.00 78.66 C ANISOU 5413 CB PRO C 200 9518 8955 11413 -79 -855 -50 C ATOM 5414 CG PRO C 200 -13.487 -12.687 -15.895 1.00 89.42 C ANISOU 5414 CG PRO C 200 10826 10325 12823 -104 -888 -174 C ATOM 5415 CD PRO C 200 -12.648 -13.719 -15.186 1.00 87.37 C ANISOU 5415 CD PRO C 200 10595 10001 12599 -120 -801 -239 C ATOM 5416 N SER C 201 -14.231 -12.143 -12.494 1.00 75.13 N ANISOU 5416 N SER C 201 8936 8326 11285 -88 -669 -81 N ATOM 5417 CA SER C 201 -15.413 -11.927 -11.662 1.00 74.66 C ANISOU 5417 CA SER C 201 8760 8264 11343 -86 -646 -85 C ATOM 5418 C SER C 201 -15.305 -10.707 -10.757 1.00 78.87 C ANISOU 5418 C SER C 201 9272 8804 11892 -35 -587 -73 C ATOM 5419 O SER C 201 -16.075 -9.750 -10.907 1.00 78.51 O ANISOU 5419 O SER C 201 9159 8750 11921 19 -647 -92 O ATOM 5420 CB SER C 201 -15.657 -13.151 -10.782 1.00 68.51 C ANISOU 5420 CB SER C 201 7918 7481 10632 -159 -582 -84 C ATOM 5421 OG SER C 201 -16.853 -13.800 -11.136 1.00 62.60 O ANISOU 5421 OG SER C 201 7071 6733 9983 -193 -650 -111 O ATOM 5422 N GLN C 202 -14.390 -10.756 -9.791 1.00 78.57 N ANISOU 5422 N GLN C 202 9275 8775 11804 -49 -481 -55 N ATOM 5423 CA GLN C 202 -14.133 -9.601 -8.926 1.00 78.65 C ANISOU 5423 CA GLN C 202 9262 8797 11823 3 -428 -76 C ATOM 5424 C GLN C 202 -13.200 -8.555 -9.559 1.00 72.69 C ANISOU 5424 C GLN C 202 8611 7979 11030 53 -485 -36 C ATOM 5425 O GLN C 202 -12.369 -8.882 -10.406 1.00 66.00 O ANISOU 5425 O GLN C 202 7869 7121 10088 29 -515 19 O ATOM 5426 CB GLN C 202 -13.582 -10.050 -7.575 1.00 80.91 C ANISOU 5426 CB GLN C 202 9532 9151 12061 -43 -296 -70 C ATOM 5427 CG GLN C 202 -14.581 -10.748 -6.679 1.00 83.64 C ANISOU 5427 CG GLN C 202 9732 9603 12444 -105 -238 -83 C ATOM 5428 CD GLN C 202 -14.025 -10.960 -5.287 1.00 90.20 C ANISOU 5428 CD GLN C 202 10525 10547 13199 -159 -117 -57 C ATOM 5429 OE1 GLN C 202 -13.045 -10.321 -4.898 1.00 92.21 O ANISOU 5429 OE1 GLN C 202 10848 10797 13393 -123 -74 -70 O ATOM 5430 NE2 GLN C 202 -14.636 -11.868 -4.531 1.00 92.77 N ANISOU 5430 NE2 GLN C 202 10735 10988 13526 -259 -69 -2 N ATOM 5431 N SER C 203 -13.335 -7.298 -9.142 1.00 75.60 N ANISOU 5431 N SER C 203 8930 8313 11482 120 -509 -72 N ATOM 5432 CA SER C 203 -12.446 -6.245 -9.629 1.00 78.82 C ANISOU 5432 CA SER C 203 9417 8642 11887 153 -580 -7 C ATOM 5433 C SER C 203 -11.055 -6.315 -8.993 1.00 79.01 C ANISOU 5433 C SER C 203 9534 8676 11809 132 -480 15 C ATOM 5434 O SER C 203 -10.926 -6.329 -7.767 1.00 80.98 O ANISOU 5434 O SER C 203 9738 8967 12062 139 -377 -59 O ATOM 5435 CB SER C 203 -13.053 -4.874 -9.369 1.00 80.03 C ANISOU 5435 CB SER C 203 9469 8715 12225 235 -669 -64 C ATOM 5436 OG SER C 203 -12.218 -3.867 -9.902 1.00 83.30 O ANISOU 5436 OG SER C 203 9950 9030 12670 250 -768 35 O ATOM 5437 N ILE C 204 -10.019 -6.355 -9.829 1.00 73.06 N ANISOU 5437 N ILE C 204 8895 7913 10951 101 -511 114 N ATOM 5438 CA ILE C 204 -8.637 -6.402 -9.342 1.00 66.63 C ANISOU 5438 CA ILE C 204 8169 7106 10043 82 -427 141 C ATOM 5439 C ILE C 204 -7.756 -5.335 -9.977 1.00 60.93 C ANISOU 5439 C ILE C 204 7508 6334 9310 86 -510 243 C ATOM 5440 O ILE C 204 -7.559 -5.322 -11.186 1.00 63.06 O ANISOU 5440 O ILE C 204 7816 6640 9505 51 -592 340 O ATOM 5441 CB ILE C 204 -8.006 -7.785 -9.583 1.00 62.12 C ANISOU 5441 CB ILE C 204 7664 6595 9343 24 -359 149 C ATOM 5442 CG1 ILE C 204 -8.672 -8.817 -8.670 1.00 61.11 C ANISOU 5442 CG1 ILE C 204 7469 6496 9252 -1 -280 87 C ATOM 5443 CG2 ILE C 204 -6.486 -7.732 -9.380 1.00 50.89 C ANISOU 5443 CG2 ILE C 204 6334 5178 7824 8 -301 190 C ATOM 5444 CD1 ILE C 204 -8.185 -10.217 -8.858 1.00 61.01 C ANISOU 5444 CD1 ILE C 204 7496 6498 9189 -55 -250 91 C ATOM 5445 N THR C 205 -7.218 -4.438 -9.163 1.00 60.51 N ANISOU 5445 N THR C 205 7449 6217 9327 120 -494 225 N ATOM 5446 CA THR C 205 -6.455 -3.320 -9.718 1.00 68.96 C ANISOU 5446 CA THR C 205 8556 7214 10431 115 -598 344 C ATOM 5447 C THR C 205 -5.050 -3.168 -9.113 1.00 63.93 C ANISOU 5447 C THR C 205 7991 6575 9724 98 -519 360 C ATOM 5448 O THR C 205 -4.814 -3.523 -7.970 1.00 64.84 O ANISOU 5448 O THR C 205 8100 6713 9823 117 -402 254 O ATOM 5449 CB THR C 205 -7.261 -1.963 -9.665 1.00 75.74 C ANISOU 5449 CB THR C 205 9313 7930 11534 178 -748 333 C ATOM 5450 OG1 THR C 205 -6.868 -1.193 -8.523 1.00 83.63 O ANISOU 5450 OG1 THR C 205 10273 8849 12655 232 -722 227 O ATOM 5451 CG2 THR C 205 -8.783 -2.206 -9.620 1.00 62.12 C ANISOU 5451 CG2 THR C 205 7482 6211 9911 222 -775 229 C ATOM 5452 N CYS C 206 -4.131 -2.644 -9.914 1.00 64.48 N ANISOU 5452 N CYS C 206 8117 6640 9741 52 -589 509 N ATOM 5453 CA CYS C 206 -2.755 -2.338 -9.506 1.00 67.01 C ANISOU 5453 CA CYS C 206 8499 6953 10009 30 -540 550 C ATOM 5454 C CYS C 206 -2.655 -0.929 -8.907 1.00 64.55 C ANISOU 5454 C CYS C 206 8136 6482 9910 73 -634 547 C ATOM 5455 O CYS C 206 -3.177 0.017 -9.483 1.00 68.71 O ANISOU 5455 O CYS C 206 8607 6904 10597 79 -798 633 O ATOM 5456 CB CYS C 206 -1.861 -2.400 -10.750 1.00 63.44 C ANISOU 5456 CB CYS C 206 8104 6603 9397 -54 -583 721 C ATOM 5457 SG CYS C 206 -0.106 -2.550 -10.474 1.00122.42 S ANISOU 5457 SG CYS C 206 15652 14136 16728 -98 -485 760 S ATOM 5458 N ASN C 207 -1.996 -0.774 -7.764 1.00 56.33 N ANISOU 5458 N ASN C 207 7101 5413 8888 102 -549 445 N ATOM 5459 CA ASN C 207 -1.720 0.573 -7.259 1.00 55.66 C ANISOU 5459 CA ASN C 207 6962 5171 9014 142 -652 424 C ATOM 5460 C ASN C 207 -0.229 0.853 -7.238 1.00 62.06 C ANISOU 5460 C ASN C 207 7847 5978 9756 88 -636 529 C ATOM 5461 O ASN C 207 0.557 0.088 -6.672 1.00 70.51 O ANISOU 5461 O ASN C 207 8978 7150 10662 71 -488 481 O ATOM 5462 CB ASN C 207 -2.316 0.802 -5.873 1.00 54.77 C ANISOU 5462 CB ASN C 207 6752 5035 9023 233 -597 175 C ATOM 5463 CG ASN C 207 -3.707 0.221 -5.736 1.00 63.45 C ANISOU 5463 CG ASN C 207 7774 6204 10129 272 -561 57 C ATOM 5464 OD1 ASN C 207 -3.859 -0.919 -5.299 1.00 72.22 O ANISOU 5464 OD1 ASN C 207 8905 7465 11069 249 -414 5 O ATOM 5465 ND2 ASN C 207 -4.735 0.998 -6.108 1.00 53.20 N ANISOU 5465 ND2 ASN C 207 6375 4790 9047 326 -708 25 N ATOM 5466 N VAL C 208 0.161 1.950 -7.872 1.00 58.49 N ANISOU 5466 N VAL C 208 7379 5404 9442 52 -801 691 N ATOM 5467 CA VAL C 208 1.573 2.295 -7.997 1.00 60.07 C ANISOU 5467 CA VAL C 208 7635 5605 9582 -17 -805 827 C ATOM 5468 C VAL C 208 1.874 3.714 -7.541 1.00 65.32 C ANISOU 5468 C VAL C 208 8233 6052 10535 7 -961 832 C ATOM 5469 O VAL C 208 1.478 4.675 -8.185 1.00 64.28 O ANISOU 5469 O VAL C 208 8036 5770 10618 -11 -1165 970 O ATOM 5470 CB VAL C 208 2.047 2.155 -9.456 1.00 56.41 C ANISOU 5470 CB VAL C 208 7214 5262 8959 -134 -863 1091 C ATOM 5471 CG1 VAL C 208 3.462 2.696 -9.619 1.00 43.83 C ANISOU 5471 CG1 VAL C 208 5649 3673 7331 -217 -891 1252 C ATOM 5472 CG2 VAL C 208 1.954 0.704 -9.904 1.00 55.44 C ANISOU 5472 CG2 VAL C 208 7149 5358 8558 -153 -711 1045 C ATOM 5473 N ALA C 209 2.608 3.843 -6.444 1.00 72.23 N ANISOU 5473 N ALA C 209 9114 6902 11428 43 -881 689 N ATOM 5474 CA ALA C 209 3.044 5.154 -5.983 1.00 71.83 C ANISOU 5474 CA ALA C 209 8995 6641 11658 65 -1032 671 C ATOM 5475 C ALA C 209 4.549 5.285 -6.149 1.00 75.59 C ANISOU 5475 C ALA C 209 9540 7146 12033 -28 -1014 837 C ATOM 5476 O ALA C 209 5.314 4.359 -5.881 1.00 77.83 O ANISOU 5476 O ALA C 209 9909 7606 12059 -55 -833 815 O ATOM 5477 CB ALA C 209 2.642 5.385 -4.544 1.00 70.99 C ANISOU 5477 CB ALA C 209 8804 6488 11682 186 -981 338 C ATOM 5478 N HIS C 210 4.953 6.440 -6.644 1.00 75.97 N ANISOU 5478 N HIS C 210 9541 7017 12306 -85 -1220 1024 N ATOM 5479 CA HIS C 210 6.348 6.763 -6.837 1.00 74.77 C ANISOU 5479 CA HIS C 210 9423 6919 12068 -184 -1222 1187 C ATOM 5480 C HIS C 210 6.457 8.229 -6.433 1.00 80.02 C ANISOU 5480 C HIS C 210 9964 7425 13016 -160 -1402 1126 C ATOM 5481 O HIS C 210 6.332 9.128 -7.271 1.00 86.46 O ANISOU 5481 O HIS C 210 10699 8195 13958 -230 -1590 1316 O ATOM 5482 CB HIS C 210 6.738 6.510 -8.296 1.00 73.52 C ANISOU 5482 CB HIS C 210 9304 6917 11714 -330 -1254 1520 C ATOM 5483 CG HIS C 210 7.961 7.249 -8.745 1.00 76.79 C ANISOU 5483 CG HIS C 210 9690 7385 12100 -449 -1329 1727 C ATOM 5484 ND1 HIS C 210 9.227 6.954 -8.283 1.00 74.52 N ANISOU 5484 ND1 HIS C 210 9461 7168 11686 -480 -1210 1716 N ATOM 5485 CD2 HIS C 210 8.113 8.259 -9.630 1.00 77.61 C ANISOU 5485 CD2 HIS C 210 9703 7493 12293 -552 -1517 1960 C ATOM 5486 CE1 HIS C 210 10.101 7.755 -8.856 1.00 75.47 C ANISOU 5486 CE1 HIS C 210 9526 7335 11813 -592 -1315 1923 C ATOM 5487 NE2 HIS C 210 9.451 8.562 -9.677 1.00 80.27 N ANISOU 5487 NE2 HIS C 210 10039 7905 12553 -643 -1505 2080 N ATOM 5488 N PRO C 211 6.619 8.470 -5.124 1.00 76.65 N ANISOU 5488 N PRO C 211 9502 6915 12706 -61 -1359 848 N ATOM 5489 CA PRO C 211 6.576 9.800 -4.502 1.00 85.03 C ANISOU 5489 CA PRO C 211 10422 7815 14070 -7 -1527 699 C ATOM 5490 C PRO C 211 7.543 10.823 -5.122 1.00 79.93 C ANISOU 5490 C PRO C 211 9728 7123 13519 -122 -1691 942 C ATOM 5491 O PRO C 211 7.233 12.023 -5.149 1.00 74.50 O ANISOU 5491 O PRO C 211 8896 6285 13126 -111 -1905 924 O ATOM 5492 CB PRO C 211 6.941 9.516 -3.033 1.00 84.37 C ANISOU 5492 CB PRO C 211 10345 7738 13975 88 -1392 386 C ATOM 5493 CG PRO C 211 7.545 8.149 -3.027 1.00 75.21 C ANISOU 5493 CG PRO C 211 9342 6730 12506 45 -1173 461 C ATOM 5494 CD PRO C 211 6.861 7.414 -4.130 1.00 70.69 C ANISOU 5494 CD PRO C 211 8830 6234 11797 -1 -1147 650 C ATOM 5495 N ALA C 212 8.682 10.342 -5.617 1.00 71.30 N ANISOU 5495 N ALA C 212 8736 6162 12191 -235 -1600 1162 N ATOM 5496 CA ALA C 212 9.679 11.192 -6.250 1.00 67.02 C ANISOU 5496 CA ALA C 212 8145 5620 11699 -360 -1734 1412 C ATOM 5497 C ALA C 212 9.033 12.101 -7.282 1.00 75.03 C ANISOU 5497 C ALA C 212 9040 6568 12899 -430 -1970 1619 C ATOM 5498 O ALA C 212 9.235 13.312 -7.257 1.00 79.68 O ANISOU 5498 O ALA C 212 9497 7017 13761 -458 -2178 1663 O ATOM 5499 CB ALA C 212 10.743 10.341 -6.897 1.00 62.78 C ANISOU 5499 CB ALA C 212 7723 5296 10834 -478 -1587 1633 C ATOM 5500 N SER C 213 8.249 11.522 -8.184 1.00 78.83 N ANISOU 5500 N SER C 213 9556 7146 13248 -463 -1952 1750 N ATOM 5501 CA SER C 213 7.544 12.316 -9.185 1.00 85.06 C ANISOU 5501 CA SER C 213 10228 7884 14208 -536 -2181 1955 C ATOM 5502 C SER C 213 6.185 12.739 -8.656 1.00 83.07 C ANISOU 5502 C SER C 213 9881 7442 14238 -401 -2284 1713 C ATOM 5503 O SER C 213 5.403 13.361 -9.370 1.00 84.38 O ANISOU 5503 O SER C 213 9942 7537 14583 -441 -2479 1839 O ATOM 5504 CB SER C 213 7.396 11.563 -10.515 1.00 90.01 C ANISOU 5504 CB SER C 213 10917 8734 14550 -657 -2135 2235 C ATOM 5505 OG SER C 213 6.624 10.386 -10.372 1.00 92.81 O ANISOU 5505 OG SER C 213 11377 9155 14733 -569 -1963 2091 O ATOM 5506 N SER C 214 5.919 12.404 -7.397 1.00 79.37 N ANISOU 5506 N SER C 214 9437 6909 13810 -249 -2156 1363 N ATOM 5507 CA SER C 214 4.615 12.647 -6.792 1.00 80.25 C ANISOU 5507 CA SER C 214 9451 6892 14147 -109 -2214 1083 C ATOM 5508 C SER C 214 3.484 12.093 -7.664 1.00 87.14 C ANISOU 5508 C SER C 214 10345 7819 14945 -118 -2219 1187 C ATOM 5509 O SER C 214 2.634 12.854 -8.147 1.00 80.39 O ANISOU 5509 O SER C 214 9362 6851 14331 -124 -2425 1236 O ATOM 5510 CB SER C 214 4.399 14.144 -6.530 1.00 72.84 C ANISOU 5510 CB SER C 214 8312 5742 13623 -86 -2483 1003 C ATOM 5511 OG SER C 214 4.728 14.491 -5.195 1.00 68.56 O ANISOU 5511 OG SER C 214 7712 5125 13211 24 -2449 677 O ATOM 5512 N THR C 215 3.470 10.770 -7.854 1.00 92.71 N ANISOU 5512 N THR C 215 11201 8690 15334 -120 -2006 1217 N ATOM 5513 CA THR C 215 2.371 10.124 -8.586 1.00 93.94 C ANISOU 5513 CA THR C 215 11379 8903 15410 -116 -1997 1283 C ATOM 5514 C THR C 215 1.825 8.833 -7.954 1.00 87.39 C ANISOU 5514 C THR C 215 10643 8151 14411 -11 -1773 1062 C ATOM 5515 O THR C 215 2.576 8.000 -7.431 1.00 82.73 O ANISOU 5515 O THR C 215 10163 7655 13617 -7 -1581 1001 O ATOM 5516 CB THR C 215 2.704 9.863 -10.090 1.00 73.69 C ANISOU 5516 CB THR C 215 8869 6493 12638 -283 -2045 1675 C ATOM 5517 OG1 THR C 215 3.164 8.516 -10.272 1.00 70.83 O ANISOU 5517 OG1 THR C 215 8659 6322 11931 -312 -1826 1722 O ATOM 5518 CG2 THR C 215 3.733 10.864 -10.617 1.00 69.15 C ANISOU 5518 CG2 THR C 215 8229 5917 12127 -421 -2197 1923 C ATOM 5519 N LYS C 216 0.497 8.710 -8.002 1.00 86.24 N ANISOU 5519 N LYS C 216 10436 7960 14374 68 -1813 945 N ATOM 5520 CA LYS C 216 -0.225 7.471 -7.701 1.00 85.01 C ANISOU 5520 CA LYS C 216 10345 7885 14070 143 -1637 796 C ATOM 5521 C LYS C 216 -1.059 7.105 -8.929 1.00 79.45 C ANISOU 5521 C LYS C 216 9653 7226 13310 90 -1714 1004 C ATOM 5522 O LYS C 216 -1.868 7.901 -9.410 1.00 80.34 O ANISOU 5522 O LYS C 216 9652 7246 13627 93 -1903 1051 O ATOM 5523 CB LYS C 216 -1.144 7.611 -6.469 1.00 89.13 C ANISOU 5523 CB LYS C 216 10753 8337 14775 303 -1599 409 C ATOM 5524 CG LYS C 216 -0.447 7.887 -5.124 1.00 95.53 C ANISOU 5524 CG LYS C 216 11532 9137 15627 368 -1514 151 C ATOM 5525 CD LYS C 216 -1.408 8.506 -4.083 1.00 99.20 C ANISOU 5525 CD LYS C 216 11813 9547 16331 511 -1558 -226 C ATOM 5526 CE LYS C 216 -0.690 8.891 -2.779 1.00 93.08 C ANISOU 5526 CE LYS C 216 10983 8787 15596 568 -1497 -491 C ATOM 5527 NZ LYS C 216 -1.456 9.821 -1.889 1.00 87.08 N ANISOU 5527 NZ LYS C 216 10005 7983 15098 686 -1596 -848 N ATOM 5528 N VAL C 217 -0.842 5.906 -9.449 1.00 76.51 N ANISOU 5528 N VAL C 217 9400 7055 12616 29 -1557 1107 N ATOM 5529 CA VAL C 217 -1.639 5.396 -10.551 1.00 76.77 C ANISOU 5529 CA VAL C 217 9440 7208 12523 -20 -1592 1250 C ATOM 5530 C VAL C 217 -2.291 4.103 -10.114 1.00 77.86 C ANISOU 5530 C VAL C 217 9616 7522 12444 45 -1372 1020 C ATOM 5531 O VAL C 217 -1.662 3.285 -9.455 1.00 82.43 O ANISOU 5531 O VAL C 217 10270 8231 12821 53 -1169 896 O ATOM 5532 CB VAL C 217 -0.793 5.140 -11.821 1.00 73.56 C ANISOU 5532 CB VAL C 217 9105 6992 11854 -183 -1610 1575 C ATOM 5533 CG1 VAL C 217 -1.539 4.215 -12.790 1.00 75.44 C ANISOU 5533 CG1 VAL C 217 9363 7444 11858 -221 -1566 1628 C ATOM 5534 CG2 VAL C 217 -0.436 6.458 -12.495 1.00 65.30 C ANISOU 5534 CG2 VAL C 217 7987 5792 11032 -280 -1877 1879 C ATOM 5535 N ASP C 218 -3.564 3.941 -10.453 1.00 78.81 N ANISOU 5535 N ASP C 218 9677 7635 12634 86 -1428 975 N ATOM 5536 CA ASP C 218 -4.283 2.712 -10.184 1.00 75.99 C ANISOU 5536 CA ASP C 218 9341 7441 12091 127 -1249 799 C ATOM 5537 C ASP C 218 -4.754 2.198 -11.516 1.00 71.92 C ANISOU 5537 C ASP C 218 8849 7054 11425 51 -1304 976 C ATOM 5538 O ASP C 218 -5.613 2.825 -12.130 1.00 75.88 O ANISOU 5538 O ASP C 218 9270 7458 12102 55 -1488 1069 O ATOM 5539 CB ASP C 218 -5.498 2.984 -9.294 1.00 79.63 C ANISOU 5539 CB ASP C 218 9678 7798 12779 253 -1264 544 C ATOM 5540 CG ASP C 218 -5.151 3.808 -8.057 1.00 92.61 C ANISOU 5540 CG ASP C 218 11250 9307 14628 336 -1268 347 C ATOM 5541 OD1 ASP C 218 -4.510 3.259 -7.135 1.00 99.08 O ANISOU 5541 OD1 ASP C 218 12117 10240 15288 343 -1085 216 O ATOM 5542 OD2 ASP C 218 -5.528 5.001 -7.998 1.00 93.09 O ANISOU 5542 OD2 ASP C 218 11196 9150 15025 396 -1467 314 O ATOM 5543 N LYS C 219 -4.201 1.080 -11.981 1.00 61.04 N ANISOU 5543 N LYS C 219 7563 5892 9736 -16 -1161 1012 N ATOM 5544 CA LYS C 219 -4.766 0.424 -13.159 1.00 59.50 C ANISOU 5544 CA LYS C 219 7373 5856 9379 -74 -1193 1105 C ATOM 5545 C LYS C 219 -5.551 -0.844 -12.835 1.00 64.99 C ANISOU 5545 C LYS C 219 8074 6643 9974 -25 -1048 902 C ATOM 5546 O LYS C 219 -5.065 -1.739 -12.156 1.00 69.74 O ANISOU 5546 O LYS C 219 8731 7313 10456 -10 -876 770 O ATOM 5547 CB LYS C 219 -3.718 0.164 -14.235 1.00 57.96 C ANISOU 5547 CB LYS C 219 7236 5865 8922 -197 -1191 1300 C ATOM 5548 CG LYS C 219 -3.229 1.437 -14.902 1.00 75.46 C ANISOU 5548 CG LYS C 219 9414 8024 11233 -285 -1389 1584 C ATOM 5549 CD LYS C 219 -3.649 1.538 -16.368 1.00 87.16 C ANISOU 5549 CD LYS C 219 10849 9673 12595 -393 -1540 1815 C ATOM 5550 CE LYS C 219 -2.975 2.749 -17.022 1.00 96.10 C ANISOU 5550 CE LYS C 219 11936 10783 13794 -517 -1738 2154 C ATOM 5551 NZ LYS C 219 -3.257 2.847 -18.481 1.00102.08 N ANISOU 5551 NZ LYS C 219 12635 11769 14383 -654 -1886 2423 N ATOM 5552 N LYS C 220 -6.785 -0.891 -13.319 1.00 71.65 N ANISOU 5552 N LYS C 220 8852 7477 10894 -5 -1138 894 N ATOM 5553 CA LYS C 220 -7.620 -2.074 -13.203 1.00 72.33 C ANISOU 5553 CA LYS C 220 8929 7652 10900 22 -1034 738 C ATOM 5554 C LYS C 220 -7.148 -3.074 -14.236 1.00 66.38 C ANISOU 5554 C LYS C 220 8235 7105 9879 -58 -991 791 C ATOM 5555 O LYS C 220 -6.877 -2.706 -15.374 1.00 68.32 O ANISOU 5555 O LYS C 220 8481 7453 10026 -132 -1103 964 O ATOM 5556 CB LYS C 220 -9.092 -1.726 -13.472 1.00 75.69 C ANISOU 5556 CB LYS C 220 9252 8004 11503 66 -1162 718 C ATOM 5557 CG LYS C 220 -10.043 -2.883 -13.185 1.00 75.07 C ANISOU 5557 CG LYS C 220 9144 7997 11382 94 -1058 551 C ATOM 5558 CD LYS C 220 -11.415 -2.676 -13.788 1.00 75.85 C ANISOU 5558 CD LYS C 220 9147 8068 11604 115 -1194 562 C ATOM 5559 CE LYS C 220 -12.366 -3.781 -13.358 1.00 74.18 C ANISOU 5559 CE LYS C 220 8892 7916 11378 139 -1089 394 C ATOM 5560 NZ LYS C 220 -13.408 -4.054 -14.396 1.00 74.55 N ANISOU 5560 NZ LYS C 220 8887 8014 11425 118 -1204 434 N ATOM 5561 N ILE C 221 -7.039 -4.340 -13.863 1.00 61.28 N ANISOU 5561 N ILE C 221 7625 6537 9123 -49 -842 641 N ATOM 5562 CA ILE C 221 -6.711 -5.333 -14.867 1.00 68.57 C ANISOU 5562 CA ILE C 221 8576 7647 9832 -107 -820 633 C ATOM 5563 C ILE C 221 -8.002 -5.907 -15.464 1.00 80.76 C ANISOU 5563 C ILE C 221 10058 9232 11394 -101 -882 573 C ATOM 5564 O ILE C 221 -8.847 -6.463 -14.749 1.00 78.48 O ANISOU 5564 O ILE C 221 9736 8863 11220 -54 -830 447 O ATOM 5565 CB ILE C 221 -5.789 -6.424 -14.324 1.00 68.63 C ANISOU 5565 CB ILE C 221 8640 7699 9738 -105 -665 509 C ATOM 5566 CG1 ILE C 221 -4.383 -5.865 -14.119 1.00 75.80 C ANISOU 5566 CG1 ILE C 221 9604 8621 10575 -130 -626 592 C ATOM 5567 CG2 ILE C 221 -5.703 -7.553 -15.305 1.00 71.55 C ANISOU 5567 CG2 ILE C 221 9001 8238 9946 -140 -659 427 C ATOM 5568 CD1 ILE C 221 -4.259 -4.818 -13.026 1.00 78.58 C ANISOU 5568 CD1 ILE C 221 9960 8800 11094 -90 -624 629 C ATOM 5569 N GLU C 222 -8.151 -5.738 -16.778 1.00 85.09 N ANISOU 5569 N GLU C 222 10580 9928 11821 -160 -998 676 N ATOM 5570 CA GLU C 222 -9.347 -6.160 -17.496 1.00 83.58 C ANISOU 5570 CA GLU C 222 10324 9795 11636 -163 -1082 637 C ATOM 5571 C GLU C 222 -9.040 -7.169 -18.594 1.00 80.15 C ANISOU 5571 C GLU C 222 9885 9603 10967 -217 -1075 562 C ATOM 5572 O GLU C 222 -8.007 -7.064 -19.258 1.00 78.24 O ANISOU 5572 O GLU C 222 9661 9542 10526 -278 -1072 626 O ATOM 5573 CB GLU C 222 -10.012 -4.953 -18.142 1.00 86.11 C ANISOU 5573 CB GLU C 222 10587 10089 12043 -186 -1269 831 C ATOM 5574 CG GLU C 222 -10.633 -3.992 -17.180 1.00 92.95 C ANISOU 5574 CG GLU C 222 11414 10707 13194 -112 -1314 847 C ATOM 5575 CD GLU C 222 -11.328 -2.862 -17.897 1.00105.59 C ANISOU 5575 CD GLU C 222 12939 12254 14925 -132 -1534 1038 C ATOM 5576 OE1 GLU C 222 -12.415 -2.443 -17.442 1.00112.87 O ANISOU 5576 OE1 GLU C 222 13784 13014 16088 -59 -1602 982 O ATOM 5577 OE2 GLU C 222 -10.782 -2.399 -18.923 1.00107.49 O ANISOU 5577 OE2 GLU C 222 13183 12630 15028 -228 -1646 1249 O ATOM 5578 N PRO C 223 -9.965 -8.122 -18.821 1.00 78.13 N ANISOU 5578 N PRO C 223 9584 9367 10737 -198 -1083 414 N ATOM 5579 CA PRO C 223 -9.838 -9.124 -19.882 1.00 79.31 C ANISOU 5579 CA PRO C 223 9700 9740 10696 -237 -1097 287 C ATOM 5580 C PRO C 223 -9.534 -8.458 -21.207 1.00 92.41 C ANISOU 5580 C PRO C 223 11323 11663 12128 -322 -1210 440 C ATOM 5581 O PRO C 223 -9.989 -7.339 -21.443 1.00 94.78 O ANISOU 5581 O PRO C 223 11602 11930 12481 -351 -1330 656 O ATOM 5582 CB PRO C 223 -11.227 -9.750 -19.937 1.00 67.36 C ANISOU 5582 CB PRO C 223 8123 8159 9311 -208 -1150 178 C ATOM 5583 CG PRO C 223 -11.742 -9.601 -18.581 1.00 70.40 C ANISOU 5583 CG PRO C 223 8522 8292 9934 -150 -1084 175 C ATOM 5584 CD PRO C 223 -11.228 -8.279 -18.085 1.00 76.28 C ANISOU 5584 CD PRO C 223 9307 8954 10723 -142 -1087 346 C ATOM 5585 N ARG C 224 -8.755 -9.125 -22.049 1.00 96.60 N ANISOU 5585 N ARG C 224 11827 12462 12414 -366 -1183 331 N ATOM 5586 CA ARG C 224 -8.437 -8.583 -23.357 1.00100.80 C ANISOU 5586 CA ARG C 224 12299 13326 12675 -470 -1283 477 C ATOM 5587 C ARG C 224 -9.604 -8.802 -24.335 1.00104.95 C ANISOU 5587 C ARG C 224 12736 14001 13141 -499 -1416 454 C ATOM 5588 O ARG C 224 -10.621 -9.404 -23.973 1.00103.59 O ANISOU 5588 O ARG C 224 12553 13653 13152 -433 -1423 312 O ATOM 5589 CB ARG C 224 -7.153 -9.225 -23.876 1.00 93.98 C ANISOU 5589 CB ARG C 224 11412 12746 11551 -504 -1193 331 C ATOM 5590 CG ARG C 224 -5.982 -9.058 -22.942 1.00 84.25 C ANISOU 5590 CG ARG C 224 10260 11375 10375 -476 -1067 348 C ATOM 5591 CD ARG C 224 -4.759 -9.782 -23.460 1.00 84.33 C ANISOU 5591 CD ARG C 224 10226 11666 10150 -497 -980 165 C ATOM 5592 NE ARG C 224 -3.599 -8.899 -23.548 1.00 86.88 N ANISOU 5592 NE ARG C 224 10563 12125 10321 -572 -954 370 N ATOM 5593 CZ ARG C 224 -2.612 -8.841 -22.659 1.00 84.65 C ANISOU 5593 CZ ARG C 224 10351 11693 10119 -537 -844 364 C ATOM 5594 NH1 ARG C 224 -2.615 -9.617 -21.585 1.00 78.51 N ANISOU 5594 NH1 ARG C 224 9635 10632 9562 -431 -752 176 N ATOM 5595 NH2 ARG C 224 -1.607 -8.002 -22.853 1.00 89.13 N ANISOU 5595 NH2 ARG C 224 10916 12407 10541 -621 -837 565 N ATOM 5596 N GLY C 225 -9.452 -8.307 -25.562 1.00103.18 N ANISOU 5596 N GLY C 225 12437 14116 12651 -611 -1526 610 N ATOM 5597 CA GLY C 225 -10.440 -8.508 -26.612 1.00106.76 C ANISOU 5597 CA GLY C 225 12794 14778 12993 -656 -1661 595 C ATOM 5598 C GLY C 225 -11.708 -9.246 -26.210 1.00103.38 C ANISOU 5598 C GLY C 225 12359 14118 12803 -563 -1675 401 C TER 5599 GLY C 225 HETATM 5600 C1 ZMA A 401 81.654 -15.454 49.157 1.00139.19 C ANISOU 5600 C1 ZMA A 401 13386 23707 15795 1283 -2724 -738 C HETATM 5601 C2 ZMA A 401 82.575 -15.576 50.188 1.00143.64 C ANISOU 5601 C2 ZMA A 401 13791 24472 16314 1340 -2967 -735 C HETATM 5602 C3 ZMA A 401 82.264 -16.320 51.318 1.00142.01 C ANISOU 5602 C3 ZMA A 401 13642 24300 16014 1450 -3109 -617 C HETATM 5603 O4 ZMA A 401 83.193 -16.434 52.336 1.00140.82 O ANISOU 5603 O4 ZMA A 401 13338 24356 15809 1511 -3363 -613 O HETATM 5604 C5 ZMA A 401 81.018 -16.940 51.406 1.00138.46 C ANISOU 5604 C5 ZMA A 401 13405 23679 15525 1497 -2998 -506 C HETATM 5605 C6 ZMA A 401 80.092 -16.820 50.375 1.00133.24 C ANISOU 5605 C6 ZMA A 401 12888 22820 14915 1435 -2752 -514 C HETATM 5606 C7 ZMA A 401 80.414 -16.073 49.248 1.00134.28 C ANISOU 5606 C7 ZMA A 401 12967 22920 15132 1330 -2619 -628 C HETATM 5607 C8 ZMA A 401 79.449 -15.921 48.126 1.00128.91 C ANISOU 5607 C8 ZMA A 401 12447 22036 14496 1266 -2370 -636 C HETATM 5608 C9 ZMA A 401 79.523 -14.663 47.331 1.00127.02 C ANISOU 5608 C9 ZMA A 401 12195 21781 14285 1110 -2231 -774 C HETATM 5609 N10 ZMA A 401 78.548 -14.461 46.299 1.00127.42 N ANISOU 5609 N10 ZMA A 401 12410 21641 14362 1050 -2002 -779 N HETATM 5610 C11 ZMA A 401 77.487 -13.528 46.507 1.00128.57 C ANISOU 5610 C11 ZMA A 401 12695 21721 14436 938 -1864 -815 C HETATM 5611 N12 ZMA A 401 76.707 -13.123 45.484 1.00123.83 N ANISOU 5611 N12 ZMA A 401 12226 20965 13860 868 -1658 -841 N HETATM 5612 N13 ZMA A 401 77.281 -13.045 47.756 1.00133.43 N ANISOU 5612 N13 ZMA A 401 13306 22436 14957 904 -1950 -822 N HETATM 5613 C14 ZMA A 401 76.295 -12.165 47.988 1.00130.40 C ANISOU 5613 C14 ZMA A 401 13041 21994 14512 802 -1824 -855 C HETATM 5614 N15 ZMA A 401 76.084 -11.663 49.314 1.00129.35 N ANISOU 5614 N15 ZMA A 401 12904 21965 14279 762 -1920 -863 N HETATM 5615 N16 ZMA A 401 75.491 -11.749 46.940 1.00128.25 N ANISOU 5615 N16 ZMA A 401 12894 21563 14272 737 -1608 -879 N HETATM 5616 N17 ZMA A 401 74.435 -10.873 46.921 1.00129.52 N ANISOU 5616 N17 ZMA A 401 13180 21641 14391 642 -1452 -909 N HETATM 5617 C18 ZMA A 401 75.688 -12.211 45.722 1.00125.53 C ANISOU 5617 C18 ZMA A 401 12563 21123 14010 769 -1531 -873 C HETATM 5618 N19 ZMA A 401 74.727 -11.620 44.878 1.00125.08 N ANISOU 5618 N19 ZMA A 401 12651 20918 13954 692 -1324 -899 N HETATM 5619 C20 ZMA A 401 73.966 -10.790 45.670 1.00129.49 C ANISOU 5619 C20 ZMA A 401 13272 21491 14439 618 -1280 -920 C HETATM 5620 C21 ZMA A 401 72.820 -9.930 45.241 1.00136.92 C ANISOU 5620 C21 ZMA A 401 14356 22312 15357 529 -1084 -949 C HETATM 5621 C22 ZMA A 401 72.764 -9.134 44.102 1.00138.45 C ANISOU 5621 C22 ZMA A 401 14595 22429 15582 451 -946 -1027 C HETATM 5622 C23 ZMA A 401 71.518 -8.502 44.100 1.00135.45 C ANISOU 5622 C23 ZMA A 401 14350 21952 15164 395 -794 -1022 C HETATM 5623 C24 ZMA A 401 70.845 -8.921 45.240 1.00136.19 C ANISOU 5623 C24 ZMA A 401 14471 22065 15211 435 -838 -945 C HETATM 5624 O25 ZMA A 401 71.657 -9.767 45.892 1.00139.10 O ANISOU 5624 O25 ZMA A 401 14737 22536 15580 513 -1014 -903 O HETATM 5625 O HOH A 327 46.395 -15.211 20.182 1.00 95.92 O HETATM 5626 O HOH A 328 40.349 3.821 24.841 1.00 67.15 O HETATM 5627 O HOH B 215 37.330 -18.295 13.231 1.00 66.70 O HETATM 5628 O HOH B 216 17.940 -22.772 -0.755 1.00 57.20 O HETATM 5629 O HOH B 217 38.781 -4.440 1.688 1.00 46.36 O HETATM 5630 O HOH B 218 46.440 -6.422 5.123 1.00 63.45 O HETATM 5631 O HOH B 219 6.970 1.461 -23.119 1.00 88.73 O HETATM 5632 O HOH C 227 -10.692 -6.473 -12.867 1.00 68.90 O HETATM 5633 O HOH C 228 -7.603 0.106 -5.520 1.00 60.57 O HETATM 5634 O HOH C 229 1.768 -14.358 -8.144 1.00 76.38 O HETATM 5635 O HOH C 230 -4.587 -13.913 -4.185 1.00 64.10 O HETATM 5636 O HOH C 231 0.000 -16.050 0.000 0.50 48.29 O HETATM 5637 O HOH C 232 10.905 -0.719 -5.532 1.00 66.94 O HETATM 5638 O HOH C 233 9.531 7.708 -5.177 1.00 72.96 O CONECT 487 1094 CONECT 503 1056 CONECT 523 1138 CONECT 1056 503 CONECT 1094 487 CONECT 1138 523 CONECT 1880 1901 CONECT 1901 1880 CONECT 2453 2962 CONECT 2962 2453 CONECT 3297 3794 CONECT 3794 3297 CONECT 4090 4674 CONECT 4674 4090 CONECT 5044 5457 CONECT 5457 5044 CONECT 5600 5601 5606 CONECT 5601 5600 5602 CONECT 5602 5601 5603 5604 CONECT 5603 5602 CONECT 5604 5602 5605 CONECT 5605 5604 5606 CONECT 5606 5600 5605 5607 CONECT 5607 5606 5608 CONECT 5608 5607 5609 CONECT 5609 5608 5610 CONECT 5610 5609 5611 5612 CONECT 5611 5610 5617 CONECT 5612 5610 5613 CONECT 5613 5612 5614 5615 CONECT 5614 5613 CONECT 5615 5613 5616 5617 CONECT 5616 5615 5619 CONECT 5617 5611 5615 5618 CONECT 5618 5617 5619 CONECT 5619 5616 5618 5620 CONECT 5620 5619 5621 5624 CONECT 5621 5620 5622 CONECT 5622 5621 5623 CONECT 5623 5622 5624 CONECT 5624 5620 5623 MASTER 371 0 1 24 49 0 2 6 5635 3 41 61 END