HEADER    MEMBRANE PROTEIN                        20-JUL-23   8PWN              
TITLE     STRUCTURE OF A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL, SOLVED AT        
TITLE    2 WAVELENGTH 2.75 A                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: ADORA2A, CYBC;                                                 
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    MEMBRANE PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.EL OMARI,R.DUMAN,V.MYKHAYLYK,C.ORR,M.ROMANO,I.MORAES,A.WAGNER       
REVDAT   1   25-OCT-23 8PWN    0                                                
JRNL        AUTH   K.EL OMARI,R.DUMAN,V.MYKHAYLYK,C.M.ORR,M.LATIMER-SMITH,      
JRNL        AUTH 2 G.WINTER,V.GRAMA,F.QU,K.BOUNTRA,H.S.KWONG,M.ROMANO,R.I.REIS, 
JRNL        AUTH 3 L.VOGELEY,L.VECCHIA,C.D.OWEN,S.WITTMANN,M.RENNER,M.SENDA,    
JRNL        AUTH 4 N.MATSUGAKI,Y.KAWANO,T.A.BOWDEN,I.MORAES,J.M.GRIMES,         
JRNL        AUTH 5 E.J.MANCINI,M.A.WALSH,C.R.GUZZO,R.J.OWENS,E.Y.JONES,         
JRNL        AUTH 6 D.G.BROWN,D.I.STUART,K.BEIS,A.WAGNER                         
JRNL        TITL   EXPERIMENTAL PHASING OPPORTUNITIES FOR MACROMOLECULAR        
JRNL        TITL 2 CRYSTALLOGRAPHY AT VERY LONG WAVELENGTHS.                    
JRNL        REF    COMMUN CHEM                   V.   6   219 2023              
JRNL        REFN                   ESSN 2399-3669                               
JRNL        PMID   37828292                                                     
JRNL        DOI    10.1038/S42004-023-01014-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0257                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18936                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1032                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1412                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3007                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 288                                     
REMARK   3   SOLVENT ATOMS            : 26                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.82000                                             
REMARK   3    B22 (A**2) : -1.36000                                             
REMARK   3    B33 (A**2) : 2.18000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.416         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.267         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.216         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.621         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3362 ; 0.008 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  3380 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4533 ; 1.206 ; 1.626       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7806 ; 1.406 ; 1.557       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   387 ; 5.143 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;33.280 ;21.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   499 ;15.288 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;14.934 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   441 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3572 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   693 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1554 ; 3.014 ; 5.868       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1553 ; 3.015 ; 5.863       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1939 ; 4.550 ; 8.787       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1940 ; 4.549 ; 8.793       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1807 ; 3.492 ; 6.395       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1808 ; 3.491 ; 6.394       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2595 ; 5.516 ; 9.358       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6876 ; 7.559 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6876 ; 7.559 ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 8PWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUL-23.                  
REMARK 100 THE DEPOSITION ID IS D_1292132080.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I23                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 2.7552                             
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 12M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18936                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 89.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 47.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL2MAP                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE PH 5.3-5.4,     
REMARK 280  0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2%(V/V) 2,5-HEXANEDIOL,   
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 293K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.77000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.77000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       19.65500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       89.82000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       19.65500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       89.82000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.77000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       19.65500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       89.82000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.77000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       19.65500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       89.82000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    17                                                      
REMARK 465     TYR A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     THR A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     PRO A   279                                                      
REMARK 465     LYS A   280                                                      
REMARK 465     LEU A   281                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     LYS A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     PRO A   286                                                      
REMARK 465     ASP A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     PRO A   289                                                      
REMARK 465     GLU A   290                                                      
REMARK 465     MET A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ARG A   430                                                      
REMARK 465     GLN A   431                                                      
REMARK 465     GLN A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     PRO A   434                                                      
REMARK 465     PHE A   435                                                      
REMARK 465     LYS A   436                                                      
REMARK 465     ALA A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     ALA A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     HIS A   442                                                      
REMARK 465     HIS A   443                                                      
REMARK 465     HIS A   444                                                      
REMARK 465     HIS A   445                                                      
REMARK 465     HIS A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     HIS A   449                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A   173     NE2  GLN A   173     3656     1.94            
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  83      -53.77   -126.54                                   
REMARK 500    TYR A 334      -53.36   -126.52                                   
REMARK 500    CYS A 380       74.86   -111.62                                   
REMARK 500    ALA A 386      133.21    -37.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A  501                                                       
REMARK 610     OLA A  502                                                       
REMARK 610     OLA A  503                                                       
REMARK 610     OLA A  504                                                       
REMARK 610     OLA A  505                                                       
REMARK 610     OLA A  506                                                       
REMARK 610     OLA A  507                                                       
REMARK 610     OLA A  508                                                       
REMARK 610     OLA A  509                                                       
REMARK 610     OLA A  510                                                       
REMARK 610     OLA A  511                                                       
DBREF  8PWN A   27   233  UNP    P29274   AA2AR_HUMAN      2    208             
DBREF  8PWN A  234   334  UNP    P0ABE7   C562_ECOLX      23    123             
DBREF  8PWN A  340   439  UNP    P29274   AA2AR_HUMAN    219    318             
SEQADV 8PWN ASP A   17  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN TYR A   18  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN LYS A   19  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN ASP A   20  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN ASP A   21  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN ASP A   22  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN ASP A   23  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN GLY A   24  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN ALA A   25  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN PRO A   26  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN LEU A   79  UNP  P29274    ALA    54 CONFLICT                       
SEQADV 8PWN ALA A  113  UNP  P29274    THR    88 CONFLICT                       
SEQADV 8PWN ALA A  132  UNP  P29274    ARG   107 CONFLICT                       
SEQADV 8PWN ALA A  147  UNP  P29274    LYS   122 CONFLICT                       
SEQADV 8PWN ALA A  179  UNP  P29274    ASN   154 CONFLICT                       
SEQADV 8PWN ALA A  227  UNP  P29274    LEU   202 CONFLICT                       
SEQADV 8PWN TRP A  240  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 8PWN ILE A  335  UNP  P0ABE7              LINKER                         
SEQADV 8PWN GLN A  336  UNP  P0ABE7              LINKER                         
SEQADV 8PWN LYS A  337  UNP  P0ABE7              LINKER                         
SEQADV 8PWN TYR A  338  UNP  P0ABE7              LINKER                         
SEQADV 8PWN LEU A  339  UNP  P0ABE7              LINKER                         
SEQADV 8PWN ALA A  356  UNP  P29274    LEU   235 CONFLICT                       
SEQADV 8PWN ALA A  360  UNP  P29274    VAL   239 CONFLICT                       
SEQADV 8PWN ALA A  398  UNP  P29274    SER   277 CONFLICT                       
SEQADV 8PWN ALA A  439  UNP  P29274    GLY   318 CONFLICT                       
SEQADV 8PWN HIS A  440  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  441  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  442  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  443  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  444  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  445  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  446  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  447  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  448  UNP  P29274              EXPRESSION TAG                 
SEQADV 8PWN HIS A  449  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  433  ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET          
SEQRES   2 A  433  GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA          
SEQRES   3 A  433  VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA          
SEQRES   4 A  433  VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR          
SEQRES   5 A  433  PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY          
SEQRES   6 A  433  VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY          
SEQRES   7 A  433  PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS          
SEQRES   8 A  433  PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU          
SEQRES   9 A  433  LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE          
SEQRES  10 A  433  PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA          
SEQRES  11 A  433  ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA          
SEQRES  12 A  433  ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY          
SEQRES  13 A  433  GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY          
SEQRES  14 A  433  GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO          
SEQRES  15 A  433  MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL          
SEQRES  16 A  433  LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG          
SEQRES  17 A  433  ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU          
SEQRES  18 A  433  ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE          
SEQRES  19 A  433  GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU          
SEQRES  20 A  433  THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA          
SEQRES  21 A  433  THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO          
SEQRES  22 A  433  GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL          
SEQRES  23 A  433  GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY          
SEQRES  24 A  433  LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS          
SEQRES  25 A  433  THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG          
SEQRES  26 A  433  ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS          
SEQRES  27 A  433  SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP          
SEQRES  28 A  433  LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS          
SEQRES  29 A  433  PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU          
SEQRES  30 A  433  ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO          
SEQRES  31 A  433  PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR          
SEQRES  32 A  433  PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN          
SEQRES  33 A  433  GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS          
SEQRES  34 A  433  HIS HIS HIS HIS                                              
HET    TEP  A 500      13                                                       
HET    OLA  A 501      17                                                       
HET    OLA  A 502      14                                                       
HET    OLA  A 503       9                                                       
HET    OLA  A 504      13                                                       
HET    OLA  A 505      17                                                       
HET    OLA  A 506      17                                                       
HET    OLA  A 507      15                                                       
HET    OLA  A 508      17                                                       
HET    OLA  A 509      17                                                       
HET    OLA  A 510      17                                                       
HET    OLA  A 511      18                                                       
HET    OLA  A 512      20                                                       
HET    CLR  A 513      28                                                       
HET    CLR  A 514      28                                                       
HET    CLR  A 515      28                                                       
HETNAM     TEP THEOPHYLLINE                                                     
HETNAM     OLA OLEIC ACID                                                       
HETNAM     CLR CHOLESTEROL                                                      
FORMUL   2  TEP    C7 H8 N4 O2                                                  
FORMUL   3  OLA    12(C18 H34 O2)                                               
FORMUL  15  CLR    3(C27 H46 O)                                                 
FORMUL  18  HOH   *26(H2 O)                                                     
HELIX    1 AA1 PRO A   26  ASN A   59  1                                  34    
HELIX    2 AA2 SER A   60  GLN A   63  5                                   4    
HELIX    3 AA3 ASN A   64  LEU A   83  1                                  20    
HELIX    4 AA4 LEU A   83  THR A   93  1                                  11    
HELIX    5 AA5 CYS A   99  ILE A  133  1                                  35    
HELIX    6 AA6 ILE A  133  VAL A  141  1                                   9    
HELIX    7 AA7 THR A  142  LEU A  162  1                                  21    
HELIX    8 AA8 THR A  163  GLY A  167  5                                   5    
HELIX    9 AA9 LYS A  175  GLN A  182  1                                   8    
HELIX   10 AB1 LEU A  192  VAL A  197  1                                   6    
HELIX   11 AB2 PRO A  198  PHE A  205  1                                   8    
HELIX   12 AB3 VAL A  211  ALA A  253  1                                  43    
HELIX   13 AB4 ASN A  255  ALA A  276  1                                  22    
HELIX   14 AB5 PHE A  294  GLU A  314  1                                  21    
HELIX   15 AB6 LYS A  316  GLU A  325  1                                  10    
HELIX   16 AB7 GLN A  326  TYR A  334  1                                   9    
HELIX   17 AB8 TYR A  334  CYS A  380  1                                  47    
HELIX   18 AB9 PRO A  387  ILE A  413  1                                  27    
HELIX   19 AC1 ILE A  413  LEU A  429  1                                  17    
SHEET    1 AA1 2 CYS A  96  ALA A  98  0                                        
SHEET    2 AA1 2 GLN A 188  ALA A 190 -1  O  VAL A 189   N  ALA A  97           
SSBOND   1 CYS A   96    CYS A  184                          1555   1555  2.05  
SSBOND   2 CYS A   99    CYS A  171                          1555   1555  2.02  
SSBOND   3 CYS A  102    CYS A  191                          1555   1555  2.06  
SSBOND   4 CYS A  380    CYS A  383                          1555   1555  2.04  
CRYST1   39.310  179.640  139.540  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025439  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005567  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007166        0.00000                         
ATOM      1  N   ALA A  25      17.178  21.743  70.154  1.00 88.71           N  
ATOM      2  CA  ALA A  25      15.991  20.959  69.738  1.00 89.24           C  
ATOM      3  C   ALA A  25      14.982  20.936  70.877  1.00 94.06           C  
ATOM      4  O   ALA A  25      15.357  20.746  72.037  1.00 97.03           O  
ATOM      5  CB  ALA A  25      16.403  19.562  69.348  1.00 89.21           C  
ATOM      6  N   PRO A  26      13.669  21.095  70.589  1.00 97.92           N  
ATOM      7  CA  PRO A  26      12.645  20.916  71.617  1.00 97.13           C  
ATOM      8  C   PRO A  26      12.850  19.590  72.337  1.00 97.49           C  
ATOM      9  O   PRO A  26      13.122  18.567  71.701  1.00 93.60           O  
ATOM     10  CB  PRO A  26      11.305  20.911  70.861  1.00 95.84           C  
ATOM     11  CG  PRO A  26      11.611  21.519  69.495  1.00 96.92           C  
ATOM     12  CD  PRO A  26      13.096  21.326  69.255  1.00 97.25           C  
ATOM     13  N   PRO A  27      12.719  19.540  73.676  1.00 98.90           N  
ATOM     14  CA  PRO A  27      12.993  18.297  74.385  1.00 95.75           C  
ATOM     15  C   PRO A  27      12.077  17.139  73.980  1.00 88.62           C  
ATOM     16  O   PRO A  27      12.484  15.982  74.002  1.00 85.48           O  
ATOM     17  CB  PRO A  27      12.754  18.648  75.864  1.00 99.64           C  
ATOM     18  CG  PRO A  27      12.846  20.165  75.917  1.00102.64           C  
ATOM     19  CD  PRO A  27      12.340  20.642  74.571  1.00101.51           C  
ATOM     20  N   ILE A  28      10.862  17.463  73.568  1.00 81.13           N  
ATOM     21  CA  ILE A  28       9.845  16.444  73.227  1.00 78.82           C  
ATOM     22  C   ILE A  28      10.280  15.518  72.098  1.00 73.15           C  
ATOM     23  O   ILE A  28       9.758  14.413  72.007  1.00 62.83           O  
ATOM     24  CB  ILE A  28       8.477  17.091  72.926  1.00 81.07           C  
ATOM     25  CG1 ILE A  28       7.375  16.028  72.819  1.00 77.98           C  
ATOM     26  CG2 ILE A  28       8.550  17.969  71.683  1.00 82.01           C  
ATOM     27  CD1 ILE A  28       5.975  16.563  72.985  1.00 81.72           C  
ATOM     28  N   MET A  29      11.250  15.907  71.304  1.00 72.99           N  
ATOM     29  CA  MET A  29      11.710  15.054  70.198  1.00 69.57           C  
ATOM     30  C   MET A  29      12.661  13.969  70.689  1.00 64.85           C  
ATOM     31  O   MET A  29      12.413  12.789  70.429  1.00 58.37           O  
ATOM     32  CB  MET A  29      12.395  15.896  69.125  1.00 74.61           C  
ATOM     33  CG  MET A  29      11.443  16.865  68.459  1.00 75.85           C  
ATOM     34  SD  MET A  29      12.262  17.878  67.225  1.00 82.29           S  
ATOM     35  CE  MET A  29      12.889  16.610  66.121  1.00 74.71           C  
ATOM     36  N   GLY A  30      13.705  14.345  71.394  1.00 61.48           N  
ATOM     37  CA  GLY A  30      14.619  13.359  71.974  1.00 61.92           C  
ATOM     38  C   GLY A  30      13.880  12.430  72.927  1.00 61.99           C  
ATOM     39  O   GLY A  30      14.165  11.213  72.964  1.00 58.52           O  
ATOM     40  N   SER A  31      12.929  12.974  73.681  1.00 56.35           N  
ATOM     41  CA  SER A  31      12.131  12.202  74.665  1.00 59.61           C  
ATOM     42  C   SER A  31      11.184  11.253  73.913  1.00 58.76           C  
ATOM     43  O   SER A  31      10.814  10.213  74.448  1.00 62.45           O  
ATOM     44  CB  SER A  31      11.404  13.122  75.632  1.00 60.37           C  
ATOM     45  OG  SER A  31      10.214  13.644  75.065  1.00 62.97           O  
ATOM     46  N   SER A  32      10.760  11.607  72.710  1.00 59.28           N  
ATOM     47  CA  SER A  32       9.897  10.708  71.907  1.00 57.45           C  
ATOM     48  C   SER A  32      10.676   9.464  71.510  1.00 52.84           C  
ATOM     49  O   SER A  32      10.106   8.375  71.519  1.00 48.61           O  
ATOM     50  CB  SER A  32       9.294  11.404  70.717  1.00 57.49           C  
ATOM     51  OG  SER A  32      10.310  11.919  69.880  1.00 69.47           O  
ATOM     52  N   VAL A  33      11.954   9.615  71.199  1.00 46.59           N  
ATOM     53  CA  VAL A  33      12.808   8.446  70.891  1.00 45.42           C  
ATOM     54  C   VAL A  33      12.959   7.592  72.139  1.00 47.24           C  
ATOM     55  O   VAL A  33      12.742   6.359  72.088  1.00 46.97           O  
ATOM     56  CB  VAL A  33      14.181   8.877  70.346  1.00 52.37           C  
ATOM     57  CG1 VAL A  33      15.108   7.689  70.119  1.00 49.23           C  
ATOM     58  CG2 VAL A  33      14.036   9.698  69.075  1.00 54.48           C  
ATOM     59  N   TYR A  34      13.313   8.217  73.251  1.00 47.33           N  
ATOM     60  CA  TYR A  34      13.510   7.487  74.522  1.00 43.88           C  
ATOM     61  C   TYR A  34      12.257   6.686  74.868  1.00 40.70           C  
ATOM     62  O   TYR A  34      12.319   5.489  75.110  1.00 37.10           O  
ATOM     63  CB  TYR A  34      13.870   8.459  75.650  1.00 46.70           C  
ATOM     64  CG  TYR A  34      13.817   7.874  77.041  1.00 45.13           C  
ATOM     65  CD1 TYR A  34      14.739   6.928  77.458  1.00 43.78           C  
ATOM     66  CD2 TYR A  34      12.847   8.272  77.944  1.00 44.10           C  
ATOM     67  CE1 TYR A  34      14.685   6.382  78.728  1.00 43.42           C  
ATOM     68  CE2 TYR A  34      12.793   7.751  79.226  1.00 43.88           C  
ATOM     69  CZ  TYR A  34      13.713   6.801  79.617  1.00 44.01           C  
ATOM     70  OH  TYR A  34      13.652   6.269  80.868  1.00 49.13           O  
ATOM     71  N   ILE A  35      11.115   7.341  74.887  1.00 41.50           N  
ATOM     72  CA  ILE A  35       9.834   6.691  75.281  1.00 44.07           C  
ATOM     73  C   ILE A  35       9.526   5.542  74.333  1.00 43.38           C  
ATOM     74  O   ILE A  35       9.103   4.480  74.780  1.00 43.25           O  
ATOM     75  CB  ILE A  35       8.714   7.761  75.282  1.00 42.67           C  
ATOM     76  CG1 ILE A  35       8.936   8.773  76.407  1.00 42.45           C  
ATOM     77  CG2 ILE A  35       7.330   7.129  75.350  1.00 42.98           C  
ATOM     78  CD1 ILE A  35       8.021   9.970  76.361  1.00 43.75           C  
ATOM     79  N   THR A  36       9.702   5.745  73.038  1.00 44.55           N  
ATOM     80  CA  THR A  36       9.386   4.690  72.051  1.00 42.07           C  
ATOM     81  C   THR A  36      10.246   3.457  72.301  1.00 44.03           C  
ATOM     82  O   THR A  36       9.732   2.337  72.261  1.00 41.60           O  
ATOM     83  CB  THR A  36       9.524   5.170  70.602  1.00 42.64           C  
ATOM     84  OG1 THR A  36       8.712   6.330  70.430  1.00 41.75           O  
ATOM     85  CG2 THR A  36       9.088   4.122  69.602  1.00 42.18           C  
ATOM     86  N   VAL A  37      11.525   3.646  72.569  1.00 44.97           N  
ATOM     87  CA  VAL A  37      12.427   2.506  72.850  1.00 45.08           C  
ATOM     88  C   VAL A  37      12.012   1.831  74.158  1.00 42.57           C  
ATOM     89  O   VAL A  37      11.965   0.600  74.231  1.00 44.45           O  
ATOM     90  CB  VAL A  37      13.902   2.957  72.873  1.00 44.61           C  
ATOM     91  CG1 VAL A  37      14.823   1.835  73.324  1.00 44.57           C  
ATOM     92  CG2 VAL A  37      14.344   3.505  71.520  1.00 43.47           C  
ATOM     93  N   GLU A  38      11.716   2.609  75.176  1.00 40.56           N  
ATOM     94  CA  GLU A  38      11.274   2.058  76.476  1.00 43.82           C  
ATOM     95  C   GLU A  38      10.033   1.175  76.281  1.00 41.85           C  
ATOM     96  O   GLU A  38       9.974   0.068  76.812  1.00 38.53           O  
ATOM     97  CB  GLU A  38      11.047   3.269  77.393  1.00 49.52           C  
ATOM     98  CG  GLU A  38      11.297   3.020  78.863  1.00 59.04           C  
ATOM     99  CD  GLU A  38      12.745   2.977  79.311  1.00 56.55           C  
ATOM    100  OE1 GLU A  38      13.428   2.016  78.944  1.00 60.44           O  
ATOM    101  OE2 GLU A  38      13.155   3.862  80.095  1.00 55.75           O  
ATOM    102  N   LEU A  39       9.056   1.647  75.528  1.00 40.59           N  
ATOM    103  CA  LEU A  39       7.823   0.864  75.296  1.00 41.71           C  
ATOM    104  C   LEU A  39       8.145  -0.395  74.495  1.00 41.47           C  
ATOM    105  O   LEU A  39       7.624  -1.465  74.807  1.00 38.37           O  
ATOM    106  CB  LEU A  39       6.812   1.731  74.542  1.00 43.02           C  
ATOM    107  CG  LEU A  39       6.211   2.886  75.341  1.00 44.65           C  
ATOM    108  CD1 LEU A  39       5.298   3.726  74.461  1.00 44.57           C  
ATOM    109  CD2 LEU A  39       5.458   2.367  76.561  1.00 45.19           C  
ATOM    110  N   ALA A  40       8.982  -0.282  73.479  1.00 41.41           N  
ATOM    111  CA  ALA A  40       9.429  -1.466  72.726  1.00 42.82           C  
ATOM    112  C   ALA A  40      10.047  -2.495  73.676  1.00 42.73           C  
ATOM    113  O   ALA A  40       9.740  -3.685  73.592  1.00 40.56           O  
ATOM    114  CB  ALA A  40      10.421  -1.045  71.666  1.00 44.85           C  
ATOM    115  N   ILE A  41      10.904  -2.045  74.573  1.00 43.37           N  
ATOM    116  CA  ILE A  41      11.552  -2.958  75.544  1.00 42.89           C  
ATOM    117  C   ILE A  41      10.489  -3.568  76.458  1.00 40.76           C  
ATOM    118  O   ILE A  41      10.523  -4.769  76.737  1.00 37.93           O  
ATOM    119  CB  ILE A  41      12.652  -2.220  76.336  1.00 43.64           C  
ATOM    120  CG1 ILE A  41      13.848  -1.912  75.435  1.00 46.61           C  
ATOM    121  CG2 ILE A  41      13.071  -3.007  77.568  1.00 41.30           C  
ATOM    122  CD1 ILE A  41      14.714  -0.780  75.931  1.00 50.25           C  
ATOM    123  N   ALA A  42       9.564  -2.756  76.939  1.00 40.31           N  
ATOM    124  CA  ALA A  42       8.507  -3.239  77.845  1.00 41.82           C  
ATOM    125  C   ALA A  42       7.729  -4.389  77.208  1.00 43.78           C  
ATOM    126  O   ALA A  42       7.470  -5.397  77.858  1.00 44.49           O  
ATOM    127  CB  ALA A  42       7.595  -2.091  78.199  1.00 40.02           C  
ATOM    128  N   VAL A  43       7.372  -4.248  75.944  1.00 44.53           N  
ATOM    129  CA  VAL A  43       6.588  -5.284  75.230  1.00 43.85           C  
ATOM    130  C   VAL A  43       7.392  -6.581  75.172  1.00 40.35           C  
ATOM    131  O   VAL A  43       6.847  -7.661  75.438  1.00 36.60           O  
ATOM    132  CB  VAL A  43       6.182  -4.809  73.813  1.00 47.54           C  
ATOM    133  CG1 VAL A  43       5.655  -5.952  72.946  1.00 45.96           C  
ATOM    134  CG2 VAL A  43       5.161  -3.677  73.866  1.00 46.52           C  
ATOM    135  N   LEU A  44       8.658  -6.489  74.797  1.00 40.76           N  
ATOM    136  CA  LEU A  44       9.510  -7.686  74.681  1.00 42.97           C  
ATOM    137  C   LEU A  44       9.717  -8.315  76.053  1.00 44.87           C  
ATOM    138  O   LEU A  44       9.698  -9.551  76.176  1.00 43.33           O  
ATOM    139  CB  LEU A  44      10.850  -7.289  74.052  1.00 46.30           C  
ATOM    140  CG  LEU A  44      10.782  -6.875  72.582  1.00 49.89           C  
ATOM    141  CD1 LEU A  44      12.148  -6.442  72.071  1.00 52.59           C  
ATOM    142  CD2 LEU A  44      10.231  -8.003  71.724  1.00 50.41           C  
ATOM    143  N   ALA A  45       9.926  -7.493  77.073  1.00 45.23           N  
ATOM    144  CA  ALA A  45      10.130  -8.007  78.446  1.00 45.01           C  
ATOM    145  C   ALA A  45       8.910  -8.802  78.889  1.00 45.97           C  
ATOM    146  O   ALA A  45       9.050  -9.885  79.459  1.00 46.29           O  
ATOM    147  CB  ALA A  45      10.396  -6.870  79.407  1.00 42.25           C  
ATOM    148  N   ILE A  46       7.725  -8.268  78.655  1.00 44.37           N  
ATOM    149  CA  ILE A  46       6.479  -8.936  79.101  1.00 47.45           C  
ATOM    150  C   ILE A  46       6.300 -10.252  78.360  1.00 47.64           C  
ATOM    151  O   ILE A  46       6.124 -11.298  79.006  1.00 48.44           O  
ATOM    152  CB  ILE A  46       5.269  -7.998  78.946  1.00 47.21           C  
ATOM    153  CG1 ILE A  46       5.395  -6.786  79.874  1.00 45.00           C  
ATOM    154  CG2 ILE A  46       3.973  -8.757  79.181  1.00 48.39           C  
ATOM    155  CD1 ILE A  46       4.499  -5.629  79.502  1.00 48.17           C  
ATOM    156  N   LEU A  47       6.379 -10.223  77.039  1.00 47.28           N  
ATOM    157  CA  LEU A  47       6.054 -11.409  76.211  1.00 47.40           C  
ATOM    158  C   LEU A  47       7.033 -12.533  76.514  1.00 46.81           C  
ATOM    159  O   LEU A  47       6.604 -13.694  76.726  1.00 48.70           O  
ATOM    160  CB  LEU A  47       6.180 -11.047  74.726  1.00 49.40           C  
ATOM    161  CG  LEU A  47       5.092 -10.158  74.133  1.00 48.83           C  
ATOM    162  CD1 LEU A  47       5.536  -9.636  72.784  1.00 50.11           C  
ATOM    163  CD2 LEU A  47       3.774 -10.907  74.007  1.00 49.43           C  
ATOM    164  N   GLY A  48       8.327 -12.231  76.467  1.00 41.63           N  
ATOM    165  CA  GLY A  48       9.345 -13.271  76.655  1.00 40.80           C  
ATOM    166  C   GLY A  48       9.244 -13.921  78.012  1.00 40.78           C  
ATOM    167  O   GLY A  48       9.396 -15.146  78.131  1.00 42.06           O  
ATOM    168  N   ASN A  49       9.000 -13.129  79.038  1.00 40.87           N  
ATOM    169  CA  ASN A  49       9.022 -13.658  80.420  1.00 46.04           C  
ATOM    170  C   ASN A  49       7.697 -14.301  80.782  1.00 45.93           C  
ATOM    171  O   ASN A  49       7.701 -15.222  81.609  1.00 45.55           O  
ATOM    172  CB  ASN A  49       9.466 -12.572  81.402  1.00 44.88           C  
ATOM    173  CG  ASN A  49      10.959 -12.342  81.329  1.00 43.73           C  
ATOM    174  OD1 ASN A  49      11.735 -13.239  81.641  1.00 45.51           O  
ATOM    175  ND2 ASN A  49      11.371 -11.170  80.873  1.00 43.23           N  
ATOM    176  N   VAL A  50       6.606 -13.863  80.172  1.00 44.18           N  
ATOM    177  CA  VAL A  50       5.333 -14.612  80.288  1.00 45.45           C  
ATOM    178  C   VAL A  50       5.535 -16.021  79.735  1.00 47.93           C  
ATOM    179  O   VAL A  50       5.072 -16.994  80.342  1.00 49.01           O  
ATOM    180  CB  VAL A  50       4.181 -13.847  79.597  1.00 48.34           C  
ATOM    181  CG1 VAL A  50       2.929 -14.701  79.419  1.00 47.57           C  
ATOM    182  CG2 VAL A  50       3.845 -12.557  80.338  1.00 46.09           C  
ATOM    183  N   LEU A  51       6.258 -16.133  78.632  1.00 50.48           N  
ATOM    184  CA  LEU A  51       6.517 -17.451  78.021  1.00 50.82           C  
ATOM    185  C   LEU A  51       7.306 -18.332  78.977  1.00 48.10           C  
ATOM    186  O   LEU A  51       7.040 -19.541  79.054  1.00 46.81           O  
ATOM    187  CB  LEU A  51       7.259 -17.225  76.699  1.00 55.55           C  
ATOM    188  CG  LEU A  51       7.166 -18.355  75.677  1.00 61.71           C  
ATOM    189  CD1 LEU A  51       5.726 -18.564  75.235  1.00 65.77           C  
ATOM    190  CD2 LEU A  51       8.064 -18.070  74.478  1.00 62.75           C  
ATOM    191  N   VAL A  52       8.245 -17.751  79.709  1.00 48.21           N  
ATOM    192  CA  VAL A  52       9.049 -18.541  80.680  1.00 47.78           C  
ATOM    193  C   VAL A  52       8.125 -19.106  81.749  1.00 44.94           C  
ATOM    194  O   VAL A  52       8.203 -20.307  82.057  1.00 46.03           O  
ATOM    195  CB  VAL A  52      10.207 -17.727  81.307  1.00 45.03           C  
ATOM    196  CG1 VAL A  52      10.802 -18.415  82.532  1.00 45.31           C  
ATOM    197  CG2 VAL A  52      11.306 -17.435  80.306  1.00 44.29           C  
ATOM    198  N   CYS A  53       7.263 -18.271  82.309  1.00 45.52           N  
ATOM    199  CA  CYS A  53       6.340 -18.708  83.378  1.00 49.97           C  
ATOM    200  C   CYS A  53       5.374 -19.747  82.827  1.00 50.27           C  
ATOM    201  O   CYS A  53       5.130 -20.773  83.496  1.00 49.51           O  
ATOM    202  CB  CYS A  53       5.557 -17.521  83.929  1.00 49.16           C  
ATOM    203  SG  CYS A  53       6.601 -16.218  84.632  1.00 51.96           S  
ATOM    204  N   TRP A  54       4.811 -19.473  81.653  1.00 54.05           N  
ATOM    205  CA  TRP A  54       3.916 -20.432  80.975  1.00 56.07           C  
ATOM    206  C   TRP A  54       4.627 -21.769  80.820  1.00 55.38           C  
ATOM    207  O   TRP A  54       4.012 -22.830  81.069  1.00 51.54           O  
ATOM    208  CB  TRP A  54       3.405 -19.910  79.619  1.00 65.27           C  
ATOM    209  CG  TRP A  54       1.930 -19.633  79.569  1.00 79.58           C  
ATOM    210  CD1 TRP A  54       1.322 -18.509  79.086  1.00 88.72           C  
ATOM    211  CD2 TRP A  54       0.864 -20.495  80.016  1.00 90.20           C  
ATOM    212  NE1 TRP A  54      -0.039 -18.609  79.207  1.00 97.21           N  
ATOM    213  CE2 TRP A  54      -0.350 -19.816  79.777  1.00 96.52           C  
ATOM    214  CE3 TRP A  54       0.814 -21.763  80.608  1.00 97.91           C  
ATOM    215  CZ2 TRP A  54      -1.591 -20.367  80.105  1.00 97.54           C  
ATOM    216  CZ3 TRP A  54      -0.412 -22.305  80.934  1.00 98.54           C  
ATOM    217  CH2 TRP A  54      -1.597 -21.617  80.681  1.00 95.78           C  
ATOM    218  N   ALA A  55       5.889 -21.742  80.414  1.00 54.82           N  
ATOM    219  CA  ALA A  55       6.631 -22.991  80.140  1.00 55.56           C  
ATOM    220  C   ALA A  55       6.783 -23.813  81.414  1.00 56.42           C  
ATOM    221  O   ALA A  55       6.560 -25.031  81.389  1.00 57.64           O  
ATOM    222  CB  ALA A  55       7.970 -22.672  79.520  1.00 55.23           C  
ATOM    223  N   VAL A  56       7.156 -23.170  82.506  1.00 56.47           N  
ATOM    224  CA  VAL A  56       7.372 -23.886  83.785  1.00 55.89           C  
ATOM    225  C   VAL A  56       6.039 -24.417  84.292  1.00 57.10           C  
ATOM    226  O   VAL A  56       6.003 -25.519  84.870  1.00 51.72           O  
ATOM    227  CB  VAL A  56       8.051 -22.953  84.802  1.00 53.19           C  
ATOM    228  CG1 VAL A  56       7.985 -23.500  86.219  1.00 53.25           C  
ATOM    229  CG2 VAL A  56       9.485 -22.663  84.387  1.00 52.37           C  
ATOM    230  N   TRP A  57       4.962 -23.674  84.075  1.00 58.52           N  
ATOM    231  CA  TRP A  57       3.634 -24.098  84.563  1.00 64.65           C  
ATOM    232  C   TRP A  57       3.203 -25.398  83.883  1.00 65.26           C  
ATOM    233  O   TRP A  57       2.700 -26.309  84.569  1.00 69.04           O  
ATOM    234  CB  TRP A  57       2.621 -22.963  84.352  1.00 68.52           C  
ATOM    235  CG  TRP A  57       1.201 -23.293  84.705  1.00 77.60           C  
ATOM    236  CD1 TRP A  57       0.332 -24.065  83.988  1.00 79.10           C  
ATOM    237  CD2 TRP A  57       0.452 -22.799  85.832  1.00 84.38           C  
ATOM    238  NE1 TRP A  57      -0.891 -24.104  84.601  1.00 79.67           N  
ATOM    239  CE2 TRP A  57      -0.849 -23.336  85.732  1.00 81.81           C  
ATOM    240  CE3 TRP A  57       0.754 -21.969  86.920  1.00 89.15           C  
ATOM    241  CZ2 TRP A  57      -1.836 -23.076  86.683  1.00 85.50           C  
ATOM    242  CZ3 TRP A  57      -0.225 -21.705  87.856  1.00 87.12           C  
ATOM    243  CH2 TRP A  57      -1.502 -22.253  87.736  1.00 85.01           C  
ATOM    244  N   LEU A  58       3.416 -25.508  82.582  1.00 62.51           N  
ATOM    245  CA  LEU A  58       2.846 -26.628  81.811  1.00 63.87           C  
ATOM    246  C   LEU A  58       3.744 -27.864  81.901  1.00 66.28           C  
ATOM    247  O   LEU A  58       3.222 -28.994  82.005  1.00 74.89           O  
ATOM    248  CB  LEU A  58       2.642 -26.193  80.355  1.00 63.00           C  
ATOM    249  CG  LEU A  58       1.515 -25.180  80.123  1.00 66.12           C  
ATOM    250  CD1 LEU A  58       1.530 -24.655  78.693  1.00 65.93           C  
ATOM    251  CD2 LEU A  58       0.154 -25.774  80.454  1.00 66.73           C  
ATOM    252  N   ASN A  59       5.050 -27.675  81.848  1.00 60.16           N  
ATOM    253  CA  ASN A  59       5.996 -28.795  81.680  1.00 62.08           C  
ATOM    254  C   ASN A  59       6.514 -29.228  83.041  1.00 65.54           C  
ATOM    255  O   ASN A  59       7.282 -28.478  83.678  1.00 62.02           O  
ATOM    256  CB  ASN A  59       7.132 -28.428  80.723  1.00 62.18           C  
ATOM    257  CG  ASN A  59       8.068 -29.588  80.453  1.00 64.73           C  
ATOM    258  OD1 ASN A  59       7.871 -30.685  80.978  1.00 65.85           O  
ATOM    259  ND2 ASN A  59       9.098 -29.351  79.654  1.00 64.51           N  
ATOM    260  N   SER A  60       6.161 -30.436  83.449  1.00 68.89           N  
ATOM    261  CA  SER A  60       6.584 -30.965  84.764  1.00 67.87           C  
ATOM    262  C   SER A  60       8.096 -31.162  84.832  1.00 64.27           C  
ATOM    263  O   SER A  60       8.635 -31.095  85.940  1.00 57.53           O  
ATOM    264  CB  SER A  60       5.817 -32.222  85.153  1.00 68.04           C  
ATOM    265  OG  SER A  60       5.393 -32.950  84.010  1.00 76.29           O  
ATOM    266  N   ASN A  61       8.754 -31.353  83.695  1.00 59.44           N  
ATOM    267  CA  ASN A  61      10.217 -31.532  83.659  1.00 62.76           C  
ATOM    268  C   ASN A  61      10.943 -30.221  83.952  1.00 64.83           C  
ATOM    269  O   ASN A  61      12.153 -30.267  84.244  1.00 62.26           O  
ATOM    270  CB  ASN A  61      10.699 -32.086  82.312  1.00 70.35           C  
ATOM    271  CG  ASN A  61      10.333 -33.540  82.086  1.00 75.43           C  
ATOM    272  OD1 ASN A  61      10.131 -34.291  83.037  1.00 82.81           O  
ATOM    273  ND2 ASN A  61      10.258 -33.947  80.830  1.00 70.55           N  
ATOM    274  N   LEU A  62      10.250 -29.095  83.855  1.00 59.78           N  
ATOM    275  CA  LEU A  62      10.837 -27.785  84.193  1.00 61.07           C  
ATOM    276  C   LEU A  62      10.514 -27.391  85.630  1.00 60.74           C  
ATOM    277  O   LEU A  62      11.023 -26.346  86.066  1.00 57.24           O  
ATOM    278  CB  LEU A  62      10.316 -26.716  83.221  1.00 59.13           C  
ATOM    279  CG  LEU A  62      10.816 -26.811  81.779  1.00 57.58           C  
ATOM    280  CD1 LEU A  62      10.068 -25.831  80.882  1.00 57.85           C  
ATOM    281  CD2 LEU A  62      12.315 -26.567  81.694  1.00 53.20           C  
ATOM    282  N   GLN A  63       9.703 -28.172  86.330  1.00 62.17           N  
ATOM    283  CA  GLN A  63       9.261 -27.828  87.698  1.00 64.06           C  
ATOM    284  C   GLN A  63      10.245 -28.421  88.690  1.00 61.71           C  
ATOM    285  O   GLN A  63       9.986 -29.479  89.267  1.00 68.15           O  
ATOM    286  CB  GLN A  63       7.835 -28.322  87.941  1.00 62.59           C  
ATOM    287  CG  GLN A  63       6.791 -27.549  87.151  1.00 67.37           C  
ATOM    288  CD  GLN A  63       5.440 -28.218  87.168  1.00 67.51           C  
ATOM    289  OE1 GLN A  63       5.176 -29.106  87.975  1.00 69.20           O  
ATOM    290  NE2 GLN A  63       4.575 -27.801  86.257  1.00 64.34           N  
ATOM    291  N   ASN A  64      11.314 -27.676  88.930  1.00 62.63           N  
ATOM    292  CA  ASN A  64      12.323 -27.989  89.960  1.00 58.32           C  
ATOM    293  C   ASN A  64      12.613 -26.725  90.750  1.00 59.46           C  
ATOM    294  O   ASN A  64      12.194 -25.611  90.348  1.00 54.60           O  
ATOM    295  CB  ASN A  64      13.584 -28.583  89.333  1.00 53.94           C  
ATOM    296  CG  ASN A  64      14.050 -27.791  88.134  1.00 57.18           C  
ATOM    297  OD1 ASN A  64      14.513 -26.661  88.275  1.00 62.01           O  
ATOM    298  ND2 ASN A  64      13.887 -28.352  86.949  1.00 57.38           N  
ATOM    299  N   VAL A  65      13.353 -26.865  91.827  1.00 62.91           N  
ATOM    300  CA  VAL A  65      13.648 -25.706  92.704  1.00 61.24           C  
ATOM    301  C   VAL A  65      14.409 -24.654  91.914  1.00 57.79           C  
ATOM    302  O   VAL A  65      14.125 -23.452  92.066  1.00 51.95           O  
ATOM    303  CB  VAL A  65      14.401 -26.120  93.980  1.00 62.88           C  
ATOM    304  CG1 VAL A  65      14.988 -24.911  94.702  1.00 63.93           C  
ATOM    305  CG2 VAL A  65      13.495 -26.915  94.909  1.00 66.08           C  
ATOM    306  N   THR A  66      15.352 -25.077  91.090  1.00 55.32           N  
ATOM    307  CA  THR A  66      16.148 -24.136  90.273  1.00 56.59           C  
ATOM    308  C   THR A  66      15.220 -23.208  89.488  1.00 57.66           C  
ATOM    309  O   THR A  66      15.425 -21.990  89.471  1.00 59.99           O  
ATOM    310  CB  THR A  66      17.096 -24.871  89.316  1.00 59.06           C  
ATOM    311  OG1 THR A  66      17.832 -25.856  90.046  1.00 60.15           O  
ATOM    312  CG2 THR A  66      18.053 -23.929  88.617  1.00 57.28           C  
ATOM    313  N   ASN A  67      14.227 -23.776  88.840  1.00 54.00           N  
ATOM    314  CA  ASN A  67      13.360 -23.007  87.931  1.00 51.86           C  
ATOM    315  C   ASN A  67      12.323 -22.191  88.690  1.00 50.97           C  
ATOM    316  O   ASN A  67      11.720 -21.306  88.069  1.00 47.43           O  
ATOM    317  CB  ASN A  67      12.701 -23.916  86.888  1.00 51.85           C  
ATOM    318  CG  ASN A  67      13.633 -24.292  85.754  1.00 54.01           C  
ATOM    319  OD1 ASN A  67      14.629 -23.612  85.503  1.00 54.04           O  
ATOM    320  ND2 ASN A  67      13.311 -25.364  85.050  1.00 55.28           N  
ATOM    321  N   TYR A  68      12.108 -22.441  89.975  1.00 51.43           N  
ATOM    322  CA  TYR A  68      11.229 -21.551  90.759  1.00 50.67           C  
ATOM    323  C   TYR A  68      11.900 -20.192  90.952  1.00 49.01           C  
ATOM    324  O   TYR A  68      11.205 -19.163  90.975  1.00 47.90           O  
ATOM    325  CB  TYR A  68      10.832 -22.182  92.097  1.00 55.63           C  
ATOM    326  CG  TYR A  68      10.098 -23.498  91.988  1.00 66.73           C  
ATOM    327  CD1 TYR A  68       9.253 -23.775  90.918  1.00 70.86           C  
ATOM    328  CD2 TYR A  68      10.236 -24.469  92.967  1.00 68.01           C  
ATOM    329  CE1 TYR A  68       8.582 -24.985  90.821  1.00 75.22           C  
ATOM    330  CE2 TYR A  68       9.573 -25.683  92.883  1.00 73.14           C  
ATOM    331  CZ  TYR A  68       8.742 -25.944  91.808  1.00 76.32           C  
ATOM    332  OH  TYR A  68       8.089 -27.142  91.730  1.00 76.92           O  
ATOM    333  N   PHE A  69      13.223 -20.171  91.054  1.00 46.52           N  
ATOM    334  CA  PHE A  69      13.964 -18.895  91.089  1.00 45.02           C  
ATOM    335  C   PHE A  69      13.957 -18.243  89.713  1.00 44.35           C  
ATOM    336  O   PHE A  69      13.885 -17.016  89.617  1.00 44.47           O  
ATOM    337  CB  PHE A  69      15.377 -19.109  91.635  1.00 49.30           C  
ATOM    338  CG  PHE A  69      15.406 -19.501  93.091  1.00 48.08           C  
ATOM    339  CD1 PHE A  69      15.221 -18.553  94.084  1.00 49.26           C  
ATOM    340  CD2 PHE A  69      15.571 -20.823  93.466  1.00 47.26           C  
ATOM    341  CE1 PHE A  69      15.201 -18.921  95.420  1.00 52.12           C  
ATOM    342  CE2 PHE A  69      15.576 -21.184  94.803  1.00 47.60           C  
ATOM    343  CZ  PHE A  69      15.378 -20.238  95.776  1.00 47.40           C  
ATOM    344  N   VAL A  70      14.025 -19.046  88.664  1.00 41.45           N  
ATOM    345  CA  VAL A  70      13.902 -18.541  87.278  1.00 40.34           C  
ATOM    346  C   VAL A  70      12.568 -17.826  87.114  1.00 39.86           C  
ATOM    347  O   VAL A  70      12.512 -16.740  86.510  1.00 41.96           O  
ATOM    348  CB  VAL A  70      14.051 -19.690  86.264  1.00 38.35           C  
ATOM    349  CG1 VAL A  70      13.592 -19.297  84.868  1.00 39.54           C  
ATOM    350  CG2 VAL A  70      15.474 -20.212  86.233  1.00 40.58           C  
ATOM    351  N   VAL A  71      11.509 -18.421  87.655  1.00 40.98           N  
ATOM    352  CA  VAL A  71      10.153 -17.828  87.546  1.00 40.13           C  
ATOM    353  C   VAL A  71      10.101 -16.543  88.352  1.00 41.23           C  
ATOM    354  O   VAL A  71       9.513 -15.553  87.895  1.00 45.55           O  
ATOM    355  CB  VAL A  71       9.062 -18.813  88.009  1.00 42.91           C  
ATOM    356  CG1 VAL A  71       7.751 -18.104  88.323  1.00 44.07           C  
ATOM    357  CG2 VAL A  71       8.837 -19.911  86.985  1.00 45.52           C  
ATOM    358  N   SER A  72      10.653 -16.552  89.552  1.00 41.82           N  
ATOM    359  CA  SER A  72      10.711 -15.319  90.369  1.00 42.82           C  
ATOM    360  C   SER A  72      11.458 -14.232  89.602  1.00 42.43           C  
ATOM    361  O   SER A  72      11.043 -13.076  89.617  1.00 41.66           O  
ATOM    362  CB  SER A  72      11.355 -15.586  91.722  1.00 43.81           C  
ATOM    363  OG  SER A  72      11.528 -14.371  92.443  1.00 44.43           O  
ATOM    364  N   LEU A  73      12.539 -14.606  88.940  1.00 42.98           N  
ATOM    365  CA  LEU A  73      13.303 -13.675  88.091  1.00 39.77           C  
ATOM    366  C   LEU A  73      12.442 -13.194  86.921  1.00 37.31           C  
ATOM    367  O   LEU A  73      12.447 -11.994  86.607  1.00 35.92           O  
ATOM    368  CB  LEU A  73      14.552 -14.421  87.614  1.00 41.88           C  
ATOM    369  CG  LEU A  73      15.589 -13.613  86.841  1.00 42.12           C  
ATOM    370  CD1 LEU A  73      16.105 -12.451  87.666  1.00 42.37           C  
ATOM    371  CD2 LEU A  73      16.739 -14.515  86.424  1.00 44.04           C  
ATOM    372  N   ALA A  74      11.707 -14.096  86.293  1.00 37.49           N  
ATOM    373  CA  ALA A  74      10.837 -13.708  85.171  1.00 39.13           C  
ATOM    374  C   ALA A  74       9.743 -12.758  85.660  1.00 41.94           C  
ATOM    375  O   ALA A  74       9.380 -11.814  84.944  1.00 39.90           O  
ATOM    376  CB  ALA A  74      10.260 -14.928  84.498  1.00 39.94           C  
ATOM    377  N   ALA A  75       9.217 -13.002  86.855  1.00 41.20           N  
ATOM    378  CA  ALA A  75       8.172 -12.134  87.418  1.00 40.65           C  
ATOM    379  C   ALA A  75       8.707 -10.724  87.618  1.00 42.65           C  
ATOM    380  O   ALA A  75       7.991  -9.747  87.321  1.00 40.05           O  
ATOM    381  CB  ALA A  75       7.661 -12.709  88.716  1.00 42.22           C  
ATOM    382  N   ALA A  76       9.928 -10.599  88.120  1.00 41.03           N  
ATOM    383  CA  ALA A  76      10.548  -9.269  88.278  1.00 42.14           C  
ATOM    384  C   ALA A  76      10.655  -8.585  86.928  1.00 43.03           C  
ATOM    385  O   ALA A  76      10.411  -7.362  86.835  1.00 42.62           O  
ATOM    386  CB  ALA A  76      11.899  -9.405  88.928  1.00 42.51           C  
ATOM    387  N   ASP A  77      11.000  -9.337  85.891  1.00 43.56           N  
ATOM    388  CA  ASP A  77      11.206  -8.747  84.550  1.00 44.48           C  
ATOM    389  C   ASP A  77       9.878  -8.369  83.915  1.00 43.35           C  
ATOM    390  O   ASP A  77       9.820  -7.346  83.230  1.00 41.29           O  
ATOM    391  CB  ASP A  77      12.024  -9.708  83.673  1.00 47.69           C  
ATOM    392  CG  ASP A  77      13.479  -9.841  84.114  1.00 51.13           C  
ATOM    393  OD1 ASP A  77      13.997  -8.862  84.683  1.00 52.95           O  
ATOM    394  OD2 ASP A  77      14.090 -10.929  83.885  1.00 57.01           O  
ATOM    395  N   ILE A  78       8.839  -9.158  84.134  1.00 41.35           N  
ATOM    396  CA  ILE A  78       7.470  -8.744  83.750  1.00 42.33           C  
ATOM    397  C   ILE A  78       7.146  -7.419  84.447  1.00 42.02           C  
ATOM    398  O   ILE A  78       6.628  -6.492  83.802  1.00 40.87           O  
ATOM    399  CB  ILE A  78       6.434  -9.854  84.068  1.00 42.13           C  
ATOM    400  CG1 ILE A  78       6.618 -11.087  83.180  1.00 43.07           C  
ATOM    401  CG2 ILE A  78       5.008  -9.332  83.968  1.00 43.77           C  
ATOM    402  CD1 ILE A  78       5.985 -12.360  83.737  1.00 43.26           C  
ATOM    403  N   LEU A  79       7.459  -7.321  85.733  1.00 43.58           N  
ATOM    404  CA  LEU A  79       7.107  -6.104  86.489  1.00 42.94           C  
ATOM    405  C   LEU A  79       7.882  -4.898  85.960  1.00 43.15           C  
ATOM    406  O   LEU A  79       7.404  -3.753  86.089  1.00 40.76           O  
ATOM    407  CB  LEU A  79       7.304  -6.334  87.992  1.00 46.03           C  
ATOM    408  CG  LEU A  79       6.223  -7.187  88.662  1.00 45.20           C  
ATOM    409  CD1 LEU A  79       6.525  -7.411  90.133  1.00 47.38           C  
ATOM    410  CD2 LEU A  79       4.844  -6.559  88.505  1.00 45.70           C  
ATOM    411  N   VAL A  80       9.052  -5.123  85.391  1.00 44.58           N  
ATOM    412  CA  VAL A  80       9.815  -4.010  84.768  1.00 44.40           C  
ATOM    413  C   VAL A  80       9.028  -3.471  83.578  1.00 42.33           C  
ATOM    414  O   VAL A  80       8.998  -2.270  83.357  1.00 42.54           O  
ATOM    415  CB  VAL A  80      11.235  -4.470  84.354  1.00 44.78           C  
ATOM    416  CG1 VAL A  80      11.941  -3.472  83.442  1.00 44.33           C  
ATOM    417  CG2 VAL A  80      12.098  -4.770  85.565  1.00 42.05           C  
ATOM    418  N   GLY A  81       8.410  -4.339  82.809  1.00 40.33           N  
ATOM    419  CA  GLY A  81       7.641  -3.879  81.654  1.00 42.55           C  
ATOM    420  C   GLY A  81       6.337  -3.243  82.018  1.00 41.95           C  
ATOM    421  O   GLY A  81       5.970  -2.207  81.417  1.00 40.93           O  
ATOM    422  N   VAL A  82       5.667  -3.790  83.025  1.00 41.50           N  
ATOM    423  CA  VAL A  82       4.296  -3.351  83.387  1.00 41.94           C  
ATOM    424  C   VAL A  82       4.365  -2.106  84.263  1.00 41.71           C  
ATOM    425  O   VAL A  82       3.452  -1.251  84.172  1.00 41.60           O  
ATOM    426  CB  VAL A  82       3.523  -4.503  84.058  1.00 44.63           C  
ATOM    427  CG1 VAL A  82       2.221  -4.034  84.686  1.00 48.96           C  
ATOM    428  CG2 VAL A  82       3.262  -5.638  83.076  1.00 42.50           C  
ATOM    429  N   LEU A  83       5.423  -1.959  85.065  1.00 43.32           N  
ATOM    430  CA  LEU A  83       5.443  -0.866  86.064  1.00 41.04           C  
ATOM    431  C   LEU A  83       6.689   0.004  85.956  1.00 41.16           C  
ATOM    432  O   LEU A  83       6.571   1.241  85.912  1.00 39.49           O  
ATOM    433  CB  LEU A  83       5.299  -1.461  87.466  1.00 43.85           C  
ATOM    434  CG  LEU A  83       3.910  -1.995  87.821  1.00 44.77           C  
ATOM    435  CD1 LEU A  83       3.882  -2.518  89.250  1.00 43.70           C  
ATOM    436  CD2 LEU A  83       2.843  -0.929  87.624  1.00 43.49           C  
ATOM    437  N   ALA A  84       7.868  -0.609  85.997  1.00 39.14           N  
ATOM    438  CA  ALA A  84       9.120   0.178  86.088  1.00 39.30           C  
ATOM    439  C   ALA A  84       9.303   1.053  84.851  1.00 37.28           C  
ATOM    440  O   ALA A  84       9.762   2.183  84.961  1.00 41.27           O  
ATOM    441  CB  ALA A  84      10.322  -0.727  86.279  1.00 41.49           C  
ATOM    442  N   ILE A  85       8.995   0.537  83.680  1.00 37.35           N  
ATOM    443  CA  ILE A  85       9.250   1.285  82.430  1.00 39.37           C  
ATOM    444  C   ILE A  85       8.239   2.419  82.354  1.00 36.20           C  
ATOM    445  O   ILE A  85       8.628   3.567  82.129  1.00 36.79           O  
ATOM    446  CB  ILE A  85       9.283   0.386  81.176  1.00 39.68           C  
ATOM    447  CG1 ILE A  85      10.682  -0.212  80.978  1.00 40.90           C  
ATOM    448  CG2 ILE A  85       8.830   1.149  79.942  1.00 41.54           C  
ATOM    449  CD1 ILE A  85      10.729  -1.465  80.123  1.00 39.52           C  
ATOM    450  N   PRO A  86       6.934   2.182  82.567  1.00 37.31           N  
ATOM    451  CA  PRO A  86       6.015   3.319  82.681  1.00 37.90           C  
ATOM    452  C   PRO A  86       6.444   4.344  83.734  1.00 39.51           C  
ATOM    453  O   PRO A  86       6.380   5.544  83.472  1.00 39.77           O  
ATOM    454  CB  PRO A  86       4.684   2.655  83.038  1.00 36.25           C  
ATOM    455  CG  PRO A  86       4.791   1.273  82.426  1.00 37.62           C  
ATOM    456  CD  PRO A  86       6.247   0.884  82.576  1.00 38.62           C  
ATOM    457  N   PHE A  87       6.903   3.890  84.896  1.00 41.31           N  
ATOM    458  CA  PHE A  87       7.446   4.811  85.914  1.00 38.13           C  
ATOM    459  C   PHE A  87       8.625   5.592  85.345  1.00 39.53           C  
ATOM    460  O   PHE A  87       8.727   6.811  85.562  1.00 39.32           O  
ATOM    461  CB  PHE A  87       7.843   4.004  87.155  1.00 40.45           C  
ATOM    462  CG  PHE A  87       6.699   3.430  87.966  1.00 44.55           C  
ATOM    463  CD1 PHE A  87       5.379   3.501  87.523  1.00 49.35           C  
ATOM    464  CD2 PHE A  87       6.944   2.781  89.170  1.00 44.32           C  
ATOM    465  CE1 PHE A  87       4.343   2.963  88.276  1.00 49.78           C  
ATOM    466  CE2 PHE A  87       5.908   2.243  89.918  1.00 43.78           C  
ATOM    467  CZ  PHE A  87       4.610   2.332  89.471  1.00 47.26           C  
ATOM    468  N   ALA A  88       9.518   4.907  84.640  1.00 37.87           N  
ATOM    469  CA  ALA A  88      10.713   5.559  84.077  1.00 36.41           C  
ATOM    470  C   ALA A  88      10.300   6.637  83.084  1.00 36.50           C  
ATOM    471  O   ALA A  88      10.869   7.745  83.101  1.00 35.11           O  
ATOM    472  CB  ALA A  88      11.643   4.563  83.440  1.00 38.32           C  
ATOM    473  N   ILE A  89       9.337   6.340  82.234  1.00 38.79           N  
ATOM    474  CA  ILE A  89       8.829   7.346  81.271  1.00 41.13           C  
ATOM    475  C   ILE A  89       8.283   8.537  82.050  1.00 41.83           C  
ATOM    476  O   ILE A  89       8.571   9.697  81.702  1.00 40.49           O  
ATOM    477  CB  ILE A  89       7.791   6.699  80.329  1.00 43.42           C  
ATOM    478  CG1 ILE A  89       8.472   5.733  79.351  1.00 45.22           C  
ATOM    479  CG2 ILE A  89       6.968   7.755  79.603  1.00 43.63           C  
ATOM    480  CD1 ILE A  89       7.554   4.692  78.745  1.00 46.48           C  
ATOM    481  N   THR A  90       7.520   8.276  83.099  1.00 41.07           N  
ATOM    482  CA  THR A  90       6.870   9.369  83.857  1.00 41.79           C  
ATOM    483  C   THR A  90       7.918  10.266  84.499  1.00 39.09           C  
ATOM    484  O   THR A  90       7.824  11.478  84.372  1.00 40.90           O  
ATOM    485  CB  THR A  90       5.843   8.883  84.891  1.00 44.52           C  
ATOM    486  OG1 THR A  90       6.526   8.343  86.019  1.00 62.96           O  
ATOM    487  CG2 THR A  90       4.886   7.853  84.342  1.00 44.67           C  
ATOM    488  N   ILE A  91       8.906   9.689  85.156  1.00 41.60           N  
ATOM    489  CA  ILE A  91       9.899  10.484  85.912  1.00 45.10           C  
ATOM    490  C   ILE A  91      10.807  11.250  84.963  1.00 43.07           C  
ATOM    491  O   ILE A  91      11.410  12.252  85.422  1.00 44.08           O  
ATOM    492  CB  ILE A  91      10.702   9.600  86.897  1.00 45.77           C  
ATOM    493  CG1 ILE A  91      11.252  10.424  88.063  1.00 51.32           C  
ATOM    494  CG2 ILE A  91      11.808   8.826  86.199  1.00 43.45           C  
ATOM    495  CD1 ILE A  91      11.548   9.610  89.304  1.00 51.55           C  
ATOM    496  N   SER A  92      10.902  10.844  83.704  1.00 42.59           N  
ATOM    497  CA  SER A  92      11.727  11.596  82.740  1.00 40.92           C  
ATOM    498  C   SER A  92      11.098  12.953  82.419  1.00 42.75           C  
ATOM    499  O   SER A  92      11.815  13.837  81.931  1.00 42.63           O  
ATOM    500  CB  SER A  92      12.012  10.815  81.486  1.00 39.02           C  
ATOM    501  OG  SER A  92      10.836  10.608  80.716  1.00 43.91           O  
ATOM    502  N   THR A  93       9.813  13.124  82.679  1.00 44.46           N  
ATOM    503  CA  THR A  93       9.114  14.379  82.347  1.00 46.25           C  
ATOM    504  C   THR A  93       9.343  15.450  83.409  1.00 47.67           C  
ATOM    505  O   THR A  93       9.072  16.630  83.127  1.00 51.95           O  
ATOM    506  CB  THR A  93       7.604  14.138  82.190  1.00 44.44           C  
ATOM    507  OG1 THR A  93       7.070  13.797  83.471  1.00 43.68           O  
ATOM    508  CG2 THR A  93       7.278  13.043  81.199  1.00 42.97           C  
ATOM    509  N   GLY A  94       9.764  15.063  84.608  1.00 52.39           N  
ATOM    510  CA  GLY A  94       9.894  16.012  85.715  1.00 49.39           C  
ATOM    511  C   GLY A  94       8.569  16.579  86.172  1.00 49.63           C  
ATOM    512  O   GLY A  94       8.543  17.678  86.726  1.00 49.28           O  
ATOM    513  N   PHE A  95       7.498  15.820  85.993  1.00 49.84           N  
ATOM    514  CA  PHE A  95       6.139  16.245  86.378  1.00 50.44           C  
ATOM    515  C   PHE A  95       6.069  16.584  87.869  1.00 51.49           C  
ATOM    516  O   PHE A  95       6.876  16.150  88.657  1.00 49.40           O  
ATOM    517  CB  PHE A  95       5.108  15.168  86.008  1.00 48.57           C  
ATOM    518  CG  PHE A  95       4.997  14.031  86.995  1.00 48.97           C  
ATOM    519  CD1 PHE A  95       6.020  13.107  87.138  1.00 49.90           C  
ATOM    520  CD2 PHE A  95       3.879  13.903  87.809  1.00 50.42           C  
ATOM    521  CE1 PHE A  95       5.920  12.069  88.054  1.00 49.81           C  
ATOM    522  CE2 PHE A  95       3.786  12.873  88.735  1.00 48.37           C  
ATOM    523  CZ  PHE A  95       4.803  11.954  88.851  1.00 50.64           C  
ATOM    524  N   CYS A  96       5.129  17.414  88.243  1.00 52.30           N  
ATOM    525  CA  CYS A  96       4.957  17.869  89.634  1.00 54.14           C  
ATOM    526  C   CYS A  96       4.323  16.767  90.473  1.00 52.94           C  
ATOM    527  O   CYS A  96       3.313  16.199  90.036  1.00 52.50           O  
ATOM    528  CB  CYS A  96       4.087  19.125  89.695  1.00 54.17           C  
ATOM    529  SG  CYS A  96       4.827  20.575  88.895  1.00 57.99           S  
ATOM    530  N   ALA A  97       4.862  16.511  91.648  1.00 49.37           N  
ATOM    531  CA  ALA A  97       4.394  15.382  92.464  1.00 49.48           C  
ATOM    532  C   ALA A  97       4.809  15.569  93.905  1.00 48.49           C  
ATOM    533  O   ALA A  97       5.889  16.173  94.174  1.00 49.39           O  
ATOM    534  CB  ALA A  97       4.936  14.087  91.907  1.00 50.93           C  
ATOM    535  N   ALA A  98       3.983  15.079  94.821  1.00 46.80           N  
ATOM    536  CA  ALA A  98       4.405  14.876  96.210  1.00 46.49           C  
ATOM    537  C   ALA A  98       5.693  14.063  96.219  1.00 48.89           C  
ATOM    538  O   ALA A  98       5.803  13.053  95.511  1.00 48.50           O  
ATOM    539  CB  ALA A  98       3.304  14.208  96.993  1.00 45.95           C  
ATOM    540  N   CYS A  99       6.658  14.505  97.002  1.00 49.07           N  
ATOM    541  CA  CYS A  99       8.015  13.952  96.928  1.00 50.71           C  
ATOM    542  C   CYS A  99       8.020  12.456  97.256  1.00 48.76           C  
ATOM    543  O   CYS A  99       8.766  11.698  96.633  1.00 46.84           O  
ATOM    544  CB  CYS A  99       8.964  14.723  97.840  1.00 54.55           C  
ATOM    545  SG  CYS A  99      10.705  14.249  97.639  1.00 56.42           S  
ATOM    546  N   HIS A 100       7.209  12.032  98.204  1.00 49.00           N  
ATOM    547  CA  HIS A 100       7.160  10.612  98.597  1.00 50.62           C  
ATOM    548  C   HIS A 100       6.505   9.766  97.509  1.00 47.24           C  
ATOM    549  O   HIS A 100       6.855   8.578  97.362  1.00 48.65           O  
ATOM    550  CB  HIS A 100       6.516  10.468  99.983  1.00 48.06           C  
ATOM    551  CG  HIS A 100       7.364  11.084 101.043  1.00 53.83           C  
ATOM    552  ND1 HIS A 100       8.290  10.352 101.769  1.00 54.25           N  
ATOM    553  CD2 HIS A 100       7.519  12.377 101.417  1.00 55.45           C  
ATOM    554  CE1 HIS A 100       8.936  11.163 102.585  1.00 55.16           C  
ATOM    555  NE2 HIS A 100       8.486  12.416 102.380  1.00 51.19           N  
ATOM    556  N   GLY A 101       5.578  10.351  96.767  1.00 44.50           N  
ATOM    557  CA  GLY A 101       5.027   9.672  95.588  1.00 45.33           C  
ATOM    558  C   GLY A 101       6.057   9.546  94.492  1.00 42.93           C  
ATOM    559  O   GLY A 101       6.193   8.456  93.896  1.00 40.55           O  
ATOM    560  N   CYS A 102       6.752  10.633  94.199  1.00 38.92           N  
ATOM    561  CA  CYS A 102       7.902  10.604  93.279  1.00 43.54           C  
ATOM    562  C   CYS A 102       8.892   9.517  93.702  1.00 44.34           C  
ATOM    563  O   CYS A 102       9.282   8.678  92.884  1.00 43.53           O  
ATOM    564  CB  CYS A 102       8.589  11.960  93.314  1.00 46.80           C  
ATOM    565  SG  CYS A 102       9.867  12.130  92.053  1.00 57.02           S  
ATOM    566  N   LEU A 103       9.281   9.530  94.968  1.00 44.17           N  
ATOM    567  CA  LEU A 103      10.248   8.548  95.497  1.00 42.56           C  
ATOM    568  C   LEU A 103       9.800   7.143  95.112  1.00 41.60           C  
ATOM    569  O   LEU A 103      10.649   6.317  94.718  1.00 40.86           O  
ATOM    570  CB  LEU A 103      10.299   8.637  97.029  1.00 46.82           C  
ATOM    571  CG  LEU A 103      11.398   9.503  97.636  1.00 48.03           C  
ATOM    572  CD1 LEU A 103      11.240   9.564  99.151  1.00 47.23           C  
ATOM    573  CD2 LEU A 103      12.775   8.982  97.261  1.00 50.84           C  
ATOM    574  N   PHE A 104       8.517   6.833  95.287  1.00 40.47           N  
ATOM    575  CA  PHE A 104       8.058   5.467  94.978  1.00 38.57           C  
ATOM    576  C   PHE A 104       8.225   5.179  93.492  1.00 38.18           C  
ATOM    577  O   PHE A 104       8.642   4.065  93.117  1.00 38.75           O  
ATOM    578  CB  PHE A 104       6.627   5.176  95.432  1.00 38.97           C  
ATOM    579  CG  PHE A 104       6.178   3.768  95.115  1.00 37.91           C  
ATOM    580  CD1 PHE A 104       6.569   2.698  95.907  1.00 39.04           C  
ATOM    581  CD2 PHE A 104       5.433   3.496  93.978  1.00 37.42           C  
ATOM    582  CE1 PHE A 104       6.175   1.401  95.607  1.00 38.64           C  
ATOM    583  CE2 PHE A 104       5.040   2.196  93.679  1.00 38.20           C  
ATOM    584  CZ  PHE A 104       5.411   1.151  94.492  1.00 36.10           C  
ATOM    585  N   ILE A 105       7.913   6.157  92.657  1.00 37.80           N  
ATOM    586  CA  ILE A 105       8.090   6.027  91.190  1.00 40.64           C  
ATOM    587  C   ILE A 105       9.563   5.813  90.875  1.00 41.37           C  
ATOM    588  O   ILE A 105       9.889   4.972  90.010  1.00 41.43           O  
ATOM    589  CB  ILE A 105       7.506   7.276  90.495  1.00 42.50           C  
ATOM    590  CG1 ILE A 105       5.985   7.328  90.631  1.00 48.29           C  
ATOM    591  CG2 ILE A 105       7.929   7.370  89.046  1.00 47.19           C  
ATOM    592  CD1 ILE A 105       5.286   6.109  90.106  1.00 50.63           C  
ATOM    593  N   ALA A 106      10.440   6.522  91.568  1.00 37.57           N  
ATOM    594  CA  ALA A 106      11.882   6.498  91.265  1.00 41.45           C  
ATOM    595  C   ALA A 106      12.501   5.182  91.717  1.00 43.46           C  
ATOM    596  O   ALA A 106      13.423   4.672  91.027  1.00 43.94           O  
ATOM    597  CB  ALA A 106      12.553   7.663  91.946  1.00 39.19           C  
ATOM    598  N   CYS A 107      12.018   4.633  92.820  1.00 41.98           N  
ATOM    599  CA  CYS A 107      12.737   3.544  93.526  1.00 42.24           C  
ATOM    600  C   CYS A 107      12.148   2.176  93.244  1.00 42.28           C  
ATOM    601  O   CYS A 107      12.819   1.189  93.559  1.00 40.03           O  
ATOM    602  CB  CYS A 107      12.691   3.769  95.028  1.00 41.73           C  
ATOM    603  SG  CYS A 107      13.702   5.171  95.541  1.00 44.13           S  
ATOM    604  N   PHE A 108      10.927   2.080  92.729  1.00 40.04           N  
ATOM    605  CA  PHE A 108      10.312   0.751  92.554  1.00 37.18           C  
ATOM    606  C   PHE A 108      11.221  -0.156  91.730  1.00 38.30           C  
ATOM    607  O   PHE A 108      11.286  -1.363  91.994  1.00 34.12           O  
ATOM    608  CB  PHE A 108       8.914   0.805  91.941  1.00 38.32           C  
ATOM    609  CG  PHE A 108       8.273  -0.557  91.812  1.00 39.37           C  
ATOM    610  CD1 PHE A 108       8.037  -1.339  92.938  1.00 40.59           C  
ATOM    611  CD2 PHE A 108       7.933  -1.076  90.570  1.00 40.10           C  
ATOM    612  CE1 PHE A 108       7.458  -2.597  92.826  1.00 41.94           C  
ATOM    613  CE2 PHE A 108       7.353  -2.334  90.459  1.00 40.69           C  
ATOM    614  CZ  PHE A 108       7.116  -3.094  91.587  1.00 42.29           C  
ATOM    615  N   VAL A 109      11.896   0.387  90.730  1.00 39.20           N  
ATOM    616  CA  VAL A 109      12.772  -0.426  89.860  1.00 39.64           C  
ATOM    617  C   VAL A 109      13.889  -1.059  90.698  1.00 39.52           C  
ATOM    618  O   VAL A 109      14.347  -2.170  90.385  1.00 37.74           O  
ATOM    619  CB  VAL A 109      13.336   0.408  88.691  1.00 39.65           C  
ATOM    620  CG1 VAL A 109      14.233   1.540  89.167  1.00 38.14           C  
ATOM    621  CG2 VAL A 109      14.064  -0.468  87.680  1.00 40.35           C  
ATOM    622  N   LEU A 110      14.306  -0.373  91.750  1.00 38.74           N  
ATOM    623  CA  LEU A 110      15.372  -0.888  92.621  1.00 36.69           C  
ATOM    624  C   LEU A 110      14.904  -2.122  93.366  1.00 36.45           C  
ATOM    625  O   LEU A 110      15.728  -2.982  93.717  1.00 40.12           O  
ATOM    626  CB  LEU A 110      15.833   0.227  93.565  1.00 38.14           C  
ATOM    627  CG  LEU A 110      16.396   1.466  92.859  1.00 40.42           C  
ATOM    628  CD1 LEU A 110      16.669   2.589  93.842  1.00 40.93           C  
ATOM    629  CD2 LEU A 110      17.656   1.122  92.073  1.00 40.12           C  
ATOM    630  N   VAL A 111      13.619  -2.203  93.661  1.00 35.19           N  
ATOM    631  CA  VAL A 111      13.043  -3.418  94.288  1.00 34.84           C  
ATOM    632  C   VAL A 111      13.198  -4.583  93.322  1.00 34.94           C  
ATOM    633  O   VAL A 111      13.619  -5.676  93.726  1.00 34.96           O  
ATOM    634  CB  VAL A 111      11.555  -3.215  94.630  1.00 35.42           C  
ATOM    635  CG1 VAL A 111      10.939  -4.492  95.178  1.00 33.98           C  
ATOM    636  CG2 VAL A 111      11.344  -2.041  95.575  1.00 32.95           C  
ATOM    637  N   LEU A 112      12.861  -4.357  92.057  1.00 34.67           N  
ATOM    638  CA  LEU A 112      12.884  -5.432  91.049  1.00 34.20           C  
ATOM    639  C   LEU A 112      14.320  -5.861  90.785  1.00 33.79           C  
ATOM    640  O   LEU A 112      14.574  -7.073  90.634  1.00 33.25           O  
ATOM    641  CB  LEU A 112      12.177  -4.962  89.767  1.00 33.92           C  
ATOM    642  CG  LEU A 112      10.701  -4.562  89.913  1.00 34.56           C  
ATOM    643  CD1 LEU A 112      10.174  -3.969  88.611  1.00 35.01           C  
ATOM    644  CD2 LEU A 112       9.832  -5.742  90.341  1.00 33.65           C  
ATOM    645  N   ALA A 113      15.236  -4.910  90.681  1.00 32.32           N  
ATOM    646  CA  ALA A 113      16.661  -5.232  90.474  1.00 34.87           C  
ATOM    647  C   ALA A 113      17.191  -6.020  91.667  1.00 36.69           C  
ATOM    648  O   ALA A 113      17.970  -6.963  91.487  1.00 39.79           O  
ATOM    649  CB  ALA A 113      17.445  -3.948  90.303  1.00 36.64           C  
ATOM    650  N   GLN A 114      16.781  -5.651  92.873  1.00 36.24           N  
ATOM    651  CA  GLN A 114      17.254  -6.361  94.071  1.00 36.00           C  
ATOM    652  C   GLN A 114      16.695  -7.771  94.091  1.00 39.15           C  
ATOM    653  O   GLN A 114      17.437  -8.726  94.437  1.00 41.95           O  
ATOM    654  CB  GLN A 114      16.847  -5.625  95.344  1.00 38.14           C  
ATOM    655  CG  GLN A 114      17.707  -6.010  96.535  1.00 39.55           C  
ATOM    656  CD  GLN A 114      19.161  -5.699  96.265  1.00 40.45           C  
ATOM    657  OE1 GLN A 114      19.491  -4.619  95.786  1.00 40.35           O  
ATOM    658  NE2 GLN A 114      20.035  -6.658  96.540  1.00 37.28           N  
ATOM    659  N   SER A 115      15.416  -7.922  93.777  1.00 39.99           N  
ATOM    660  CA  SER A 115      14.811  -9.263  93.677  1.00 38.94           C  
ATOM    661  C   SER A 115      15.601 -10.105  92.675  1.00 37.54           C  
ATOM    662  O   SER A 115      15.908 -11.266  92.940  1.00 39.76           O  
ATOM    663  CB  SER A 115      13.340  -9.134  93.334  1.00 39.03           C  
ATOM    664  OG  SER A 115      12.729 -10.400  93.161  1.00 39.45           O  
ATOM    665  N   SER A 116      15.938  -9.535  91.538  1.00 40.99           N  
ATOM    666  CA  SER A 116      16.704 -10.280  90.511  1.00 41.53           C  
ATOM    667  C   SER A 116      18.042 -10.735  91.067  1.00 39.50           C  
ATOM    668  O   SER A 116      18.457 -11.850  90.797  1.00 42.78           O  
ATOM    669  CB  SER A 116      16.876  -9.442  89.275  1.00 41.19           C  
ATOM    670  OG  SER A 116      15.639  -8.866  88.908  1.00 43.15           O  
ATOM    671  N   ILE A 117      18.693  -9.909  91.859  1.00 38.36           N  
ATOM    672  CA  ILE A 117      20.020 -10.263  92.425  1.00 40.99           C  
ATOM    673  C   ILE A 117      19.862 -11.445  93.375  1.00 39.80           C  
ATOM    674  O   ILE A 117      20.666 -12.391  93.322  1.00 41.86           O  
ATOM    675  CB  ILE A 117      20.685  -9.040  93.099  1.00 42.07           C  
ATOM    676  CG1 ILE A 117      21.280  -8.089  92.061  1.00 43.56           C  
ATOM    677  CG2 ILE A 117      21.734  -9.454  94.121  1.00 44.35           C  
ATOM    678  CD1 ILE A 117      21.267  -6.637  92.492  1.00 46.89           C  
ATOM    679  N   PHE A 118      18.859 -11.403  94.237  1.00 40.71           N  
ATOM    680  CA  PHE A 118      18.611 -12.525  95.166  1.00 45.08           C  
ATOM    681  C   PHE A 118      18.326 -13.809  94.381  1.00 42.02           C  
ATOM    682  O   PHE A 118      18.833 -14.879  94.726  1.00 40.80           O  
ATOM    683  CB  PHE A 118      17.460 -12.205  96.131  1.00 46.21           C  
ATOM    684  CG  PHE A 118      17.787 -11.225  97.233  1.00 50.71           C  
ATOM    685  CD1 PHE A 118      18.921 -11.380  98.024  1.00 58.03           C  
ATOM    686  CD2 PHE A 118      16.929 -10.172  97.524  1.00 52.48           C  
ATOM    687  CE1 PHE A 118      19.202 -10.490  99.053  1.00 57.00           C  
ATOM    688  CE2 PHE A 118      17.215  -9.279  98.547  1.00 52.32           C  
ATOM    689  CZ  PHE A 118      18.349  -9.440  99.311  1.00 54.81           C  
ATOM    690  N   SER A 119      17.514 -13.715  93.341  1.00 40.54           N  
ATOM    691  CA  SER A 119      17.190 -14.899  92.512  1.00 42.32           C  
ATOM    692  C   SER A 119      18.453 -15.438  91.851  1.00 43.71           C  
ATOM    693  O   SER A 119      18.671 -16.653  91.849  1.00 45.14           O  
ATOM    694  CB  SER A 119      16.149 -14.585  91.463  1.00 42.87           C  
ATOM    695  OG  SER A 119      14.883 -14.313  92.043  1.00 41.90           O  
ATOM    696  N   LEU A 120      19.268 -14.567  91.285  1.00 41.82           N  
ATOM    697  CA  LEU A 120      20.520 -14.998  90.636  1.00 42.90           C  
ATOM    698  C   LEU A 120      21.428 -15.661  91.660  1.00 43.99           C  
ATOM    699  O   LEU A 120      22.006 -16.731  91.367  1.00 46.91           O  
ATOM    700  CB  LEU A 120      21.203 -13.793  89.992  1.00 42.52           C  
ATOM    701  CG  LEU A 120      20.488 -13.235  88.765  1.00 45.42           C  
ATOM    702  CD1 LEU A 120      21.051 -11.869  88.381  1.00 46.00           C  
ATOM    703  CD2 LEU A 120      20.581 -14.205  87.597  1.00 43.15           C  
ATOM    704  N   LEU A 121      21.556 -15.062  92.834  1.00 41.51           N  
ATOM    705  CA  LEU A 121      22.402 -15.651  93.896  1.00 43.64           C  
ATOM    706  C   LEU A 121      21.857 -17.011  94.311  1.00 43.80           C  
ATOM    707  O   LEU A 121      22.638 -17.940  94.543  1.00 46.74           O  
ATOM    708  CB  LEU A 121      22.458 -14.700  95.097  1.00 47.74           C  
ATOM    709  CG  LEU A 121      23.394 -15.121  96.231  1.00 49.31           C  
ATOM    710  CD1 LEU A 121      24.774 -15.494  95.700  1.00 50.11           C  
ATOM    711  CD2 LEU A 121      23.499 -14.028  97.281  1.00 49.46           C  
ATOM    712  N   ALA A 122      20.547 -17.140  94.426  1.00 42.56           N  
ATOM    713  CA  ALA A 122      19.930 -18.416  94.843  1.00 41.97           C  
ATOM    714  C   ALA A 122      20.187 -19.497  93.809  1.00 42.75           C  
ATOM    715  O   ALA A 122      20.419 -20.655  94.178  1.00 41.37           O  
ATOM    716  CB  ALA A 122      18.449 -18.228  95.032  1.00 44.78           C  
ATOM    717  N   ILE A 123      20.131 -19.143  92.532  1.00 44.59           N  
ATOM    718  CA  ILE A 123      20.356 -20.128  91.444  1.00 42.60           C  
ATOM    719  C   ILE A 123      21.788 -20.638  91.529  1.00 43.92           C  
ATOM    720  O   ILE A 123      22.026 -21.849  91.383  1.00 50.16           O  
ATOM    721  CB  ILE A 123      20.033 -19.523  90.059  1.00 42.46           C  
ATOM    722  CG1 ILE A 123      18.534 -19.285  89.875  1.00 43.62           C  
ATOM    723  CG2 ILE A 123      20.579 -20.390  88.940  1.00 44.55           C  
ATOM    724  CD1 ILE A 123      18.201 -18.146  88.931  1.00 42.36           C  
ATOM    725  N   ALA A 124      22.739 -19.738  91.735  1.00 44.01           N  
ATOM    726  CA  ALA A 124      24.163 -20.114  91.829  1.00 44.84           C  
ATOM    727  C   ALA A 124      24.375 -21.077  92.986  1.00 42.57           C  
ATOM    728  O   ALA A 124      25.024 -22.115  92.818  1.00 42.70           O  
ATOM    729  CB  ALA A 124      25.002 -18.865  91.989  1.00 42.97           C  
ATOM    730  N   ILE A 125      23.846 -20.740  94.152  1.00 45.50           N  
ATOM    731  CA  ILE A 125      23.989 -21.603  95.350  1.00 46.89           C  
ATOM    732  C   ILE A 125      23.297 -22.936  95.087  1.00 47.84           C  
ATOM    733  O   ILE A 125      23.829 -23.988  95.462  1.00 48.56           O  
ATOM    734  CB  ILE A 125      23.436 -20.864  96.591  1.00 48.76           C  
ATOM    735  CG1 ILE A 125      24.279 -19.624  96.908  1.00 50.12           C  
ATOM    736  CG2 ILE A 125      23.330 -21.786  97.795  1.00 47.13           C  
ATOM    737  CD1 ILE A 125      23.808 -18.839  98.104  1.00 51.33           C  
ATOM    738  N   ASP A 126      22.131 -22.901  94.462  1.00 47.23           N  
ATOM    739  CA  ASP A 126      21.402 -24.146  94.143  1.00 47.49           C  
ATOM    740  C   ASP A 126      22.300 -25.078  93.331  1.00 49.35           C  
ATOM    741  O   ASP A 126      22.441 -26.258  93.683  1.00 52.28           O  
ATOM    742  CB  ASP A 126      20.093 -23.801  93.424  1.00 50.62           C  
ATOM    743  CG  ASP A 126      19.263 -24.997  92.987  1.00 51.17           C  
ATOM    744  OD1 ASP A 126      18.636 -25.612  93.852  1.00 53.82           O  
ATOM    745  OD2 ASP A 126      19.235 -25.284  91.771  1.00 53.62           O  
ATOM    746  N   ARG A 127      22.893 -24.563  92.266  1.00 48.90           N  
ATOM    747  CA  ARG A 127      23.742 -25.385  91.380  1.00 50.70           C  
ATOM    748  C   ARG A 127      24.993 -25.832  92.126  1.00 54.50           C  
ATOM    749  O   ARG A 127      25.524 -26.927  91.829  1.00 56.00           O  
ATOM    750  CB  ARG A 127      24.128 -24.587  90.127  1.00 50.34           C  
ATOM    751  CG  ARG A 127      23.010 -24.403  89.109  1.00 51.83           C  
ATOM    752  CD  ARG A 127      22.433 -25.732  88.643  1.00 55.20           C  
ATOM    753  NE  ARG A 127      21.434 -26.244  89.583  1.00 59.72           N  
ATOM    754  CZ  ARG A 127      21.154 -27.529  89.795  1.00 57.44           C  
ATOM    755  NH1 ARG A 127      20.232 -27.865  90.688  1.00 60.14           N  
ATOM    756  NH2 ARG A 127      21.802 -28.473  89.137  1.00 59.80           N  
ATOM    757  N   TYR A 128      25.480 -25.021  93.056  1.00 54.08           N  
ATOM    758  CA  TYR A 128      26.669 -25.406  93.844  1.00 57.25           C  
ATOM    759  C   TYR A 128      26.343 -26.576  94.756  1.00 56.05           C  
ATOM    760  O   TYR A 128      27.138 -27.515  94.869  1.00 54.59           O  
ATOM    761  CB  TYR A 128      27.215 -24.258  94.690  1.00 57.20           C  
ATOM    762  CG  TYR A 128      28.386 -24.676  95.540  1.00 58.58           C  
ATOM    763  CD1 TYR A 128      29.546 -25.156  94.958  1.00 58.33           C  
ATOM    764  CD2 TYR A 128      28.309 -24.677  96.922  1.00 61.93           C  
ATOM    765  CE1 TYR A 128      30.621 -25.571  95.725  1.00 60.88           C  
ATOM    766  CE2 TYR A 128      29.372 -25.096  97.706  1.00 62.41           C  
ATOM    767  CZ  TYR A 128      30.535 -25.543  97.106  1.00 62.31           C  
ATOM    768  OH  TYR A 128      31.592 -25.952  97.873  1.00 62.28           O  
ATOM    769  N   ILE A 129      25.204 -26.519  95.429  1.00 56.47           N  
ATOM    770  CA  ILE A 129      24.773 -27.635  96.310  1.00 58.53           C  
ATOM    771  C   ILE A 129      24.574 -28.884  95.470  1.00 58.19           C  
ATOM    772  O   ILE A 129      24.916 -29.976  95.927  1.00 58.31           O  
ATOM    773  CB  ILE A 129      23.487 -27.289  97.083  1.00 59.04           C  
ATOM    774  CG1 ILE A 129      23.679 -26.115  98.045  1.00 56.35           C  
ATOM    775  CG2 ILE A 129      22.966 -28.519  97.812  1.00 63.66           C  
ATOM    776  CD1 ILE A 129      22.378 -25.493  98.504  1.00 56.13           C  
ATOM    777  N   ALA A 130      24.034 -28.737  94.266  1.00 56.62           N  
ATOM    778  CA  ALA A 130      23.721 -29.896  93.414  1.00 56.15           C  
ATOM    779  C   ALA A 130      24.985 -30.663  93.052  1.00 58.18           C  
ATOM    780  O   ALA A 130      24.962 -31.940  93.093  1.00 66.30           O  
ATOM    781  CB  ALA A 130      22.998 -29.433  92.175  1.00 53.83           C  
ATOM    782  N   ILE A 131      26.065 -29.940  92.788  1.00 56.48           N  
ATOM    783  CA  ILE A 131      27.334 -30.552  92.304  1.00 60.87           C  
ATOM    784  C   ILE A 131      28.201 -31.005  93.479  1.00 65.26           C  
ATOM    785  O   ILE A 131      29.061 -31.891  93.282  1.00 68.31           O  
ATOM    786  CB  ILE A 131      28.096 -29.549  91.404  1.00 60.78           C  
ATOM    787  CG1 ILE A 131      29.304 -30.180  90.707  1.00 63.04           C  
ATOM    788  CG2 ILE A 131      28.512 -28.310  92.183  1.00 62.44           C  
ATOM    789  CD1 ILE A 131      28.960 -31.002  89.499  1.00 66.59           C  
ATOM    790  N   ALA A 132      28.065 -30.393  94.646  1.00 67.44           N  
ATOM    791  CA  ALA A 132      28.972 -30.654  95.779  1.00 68.45           C  
ATOM    792  C   ALA A 132      28.433 -31.745  96.696  1.00 71.62           C  
ATOM    793  O   ALA A 132      29.223 -32.530  97.229  1.00 75.83           O  
ATOM    794  CB  ALA A 132      29.228 -29.372  96.534  1.00 65.59           C  
ATOM    795  N   ILE A 133      27.118 -31.803  96.893  1.00 74.86           N  
ATOM    796  CA  ILE A 133      26.496 -32.808  97.774  1.00 76.51           C  
ATOM    797  C   ILE A 133      25.233 -33.308  97.095  1.00 73.49           C  
ATOM    798  O   ILE A 133      24.113 -33.162  97.635  1.00 72.58           O  
ATOM    799  CB  ILE A 133      26.228 -32.196  99.165  1.00 86.90           C  
ATOM    800  CG1 ILE A 133      27.459 -31.464  99.711  1.00 92.71           C  
ATOM    801  CG2 ILE A 133      25.743 -33.260 100.134  1.00 91.38           C  
ATOM    802  CD1 ILE A 133      27.224 -30.747 101.024  1.00 99.93           C  
ATOM    803  N   PRO A 134      25.354 -33.929  95.897  1.00 74.98           N  
ATOM    804  CA  PRO A 134      24.188 -34.415  95.165  1.00 74.74           C  
ATOM    805  C   PRO A 134      23.296 -35.353  95.982  1.00 78.66           C  
ATOM    806  O   PRO A 134      22.068 -35.306  95.881  1.00 81.41           O  
ATOM    807  CB  PRO A 134      24.755 -35.212  93.972  1.00 72.55           C  
ATOM    808  CG  PRO A 134      26.239 -34.881  93.908  1.00 70.31           C  
ATOM    809  CD  PRO A 134      26.623 -34.294  95.249  1.00 74.11           C  
ATOM    810  N   LEU A 135      23.938 -36.204  96.776  1.00 87.42           N  
ATOM    811  CA  LEU A 135      23.280 -37.205  97.636  1.00 88.10           C  
ATOM    812  C   LEU A 135      22.302 -36.505  98.590  1.00 80.83           C  
ATOM    813  O   LEU A 135      21.222 -37.052  98.917  1.00 74.91           O  
ATOM    814  CB  LEU A 135      24.354 -37.958  98.437  1.00 94.16           C  
ATOM    815  CG  LEU A 135      25.575 -38.454  97.655  1.00 95.98           C  
ATOM    816  CD1 LEU A 135      26.713 -38.800  98.603  1.00 98.32           C  
ATOM    817  CD2 LEU A 135      25.224 -39.650  96.781  1.00 91.32           C  
ATOM    818  N   ARG A 136      22.676 -35.324  99.049  1.00 79.92           N  
ATOM    819  CA  ARG A 136      21.887 -34.579 100.042  1.00 84.85           C  
ATOM    820  C   ARG A 136      21.036 -33.504  99.399  1.00 79.10           C  
ATOM    821  O   ARG A 136      20.373 -32.761 100.143  1.00 69.72           O  
ATOM    822  CB  ARG A 136      22.782 -33.964 101.121  1.00 91.92           C  
ATOM    823  CG  ARG A 136      23.648 -34.972 101.859  1.00100.13           C  
ATOM    824  CD  ARG A 136      24.162 -34.422 103.175  1.00108.29           C  
ATOM    825  NE  ARG A 136      24.920 -35.422 103.914  1.00117.61           N  
ATOM    826  CZ  ARG A 136      25.340 -35.289 105.171  1.00124.53           C  
ATOM    827  NH1 ARG A 136      25.076 -34.188 105.856  1.00124.93           N  
ATOM    828  NH2 ARG A 136      26.023 -36.268 105.741  1.00127.92           N  
ATOM    829  N   TYR A 137      21.061 -33.358  98.076  1.00 77.50           N  
ATOM    830  CA  TYR A 137      20.411 -32.205  97.414  1.00 75.87           C  
ATOM    831  C   TYR A 137      18.905 -32.161  97.708  1.00 79.77           C  
ATOM    832  O   TYR A 137      18.427 -31.203  98.314  1.00 83.37           O  
ATOM    833  CB  TYR A 137      20.679 -32.178  95.900  1.00 70.36           C  
ATOM    834  CG  TYR A 137      19.968 -31.066  95.159  1.00 67.19           C  
ATOM    835  CD1 TYR A 137      20.448 -29.764  95.173  1.00 64.45           C  
ATOM    836  CD2 TYR A 137      18.789 -31.307  94.469  1.00 66.34           C  
ATOM    837  CE1 TYR A 137      19.782 -28.736  94.522  1.00 63.18           C  
ATOM    838  CE2 TYR A 137      18.108 -30.292  93.815  1.00 65.11           C  
ATOM    839  CZ  TYR A 137      18.607 -29.001  93.837  1.00 67.76           C  
ATOM    840  OH  TYR A 137      17.938 -28.003  93.181  1.00 65.36           O  
ATOM    841  N   ASN A 138      18.165 -33.175  97.267  1.00 80.68           N  
ATOM    842  CA  ASN A 138      16.692 -33.202  97.380  1.00 84.08           C  
ATOM    843  C   ASN A 138      16.248 -33.137  98.837  1.00 83.38           C  
ATOM    844  O   ASN A 138      15.089 -32.769  99.099  1.00 88.46           O  
ATOM    845  CB  ASN A 138      16.080 -34.480  96.795  1.00 83.06           C  
ATOM    846  CG  ASN A 138      16.638 -34.857  95.441  1.00 85.41           C  
ATOM    847  OD1 ASN A 138      16.657 -34.038  94.522  1.00 82.98           O  
ATOM    848  ND2 ASN A 138      17.082 -36.097  95.308  1.00 78.85           N  
ATOM    849  N   GLY A 139      17.114 -33.528  99.759  1.00 83.11           N  
ATOM    850  CA  GLY A 139      16.790 -33.432 101.183  1.00 81.31           C  
ATOM    851  C   GLY A 139      16.932 -32.036 101.716  1.00 78.95           C  
ATOM    852  O   GLY A 139      16.163 -31.661 102.625  1.00 82.84           O  
ATOM    853  N   LEU A 140      17.893 -31.283 101.186  1.00 73.90           N  
ATOM    854  CA  LEU A 140      18.154 -29.887 101.605  1.00 77.66           C  
ATOM    855  C   LEU A 140      17.175 -28.984 100.864  1.00 75.22           C  
ATOM    856  O   LEU A 140      16.425 -28.297 101.540  1.00 75.29           O  
ATOM    857  CB  LEU A 140      19.583 -29.482 101.214  1.00 82.05           C  
ATOM    858  CG  LEU A 140      20.726 -30.059 102.045  1.00 88.51           C  
ATOM    859  CD1 LEU A 140      22.052 -29.893 101.320  1.00 89.27           C  
ATOM    860  CD2 LEU A 140      20.790 -29.395 103.406  1.00 93.31           C  
ATOM    861  N   VAL A 141      17.202 -29.066  99.529  1.00 72.45           N  
ATOM    862  CA  VAL A 141      16.604 -28.092  98.603  1.00 68.42           C  
ATOM    863  C   VAL A 141      15.283 -28.661  98.129  1.00 67.78           C  
ATOM    864  O   VAL A 141      15.280 -29.505  97.234  1.00 69.47           O  
ATOM    865  CB  VAL A 141      17.578 -27.779  97.449  1.00 62.91           C  
ATOM    866  CG1 VAL A 141      17.031 -26.728  96.499  1.00 61.94           C  
ATOM    867  CG2 VAL A 141      18.936 -27.352  97.976  1.00 62.58           C  
ATOM    868  N   THR A 142      14.193 -28.156  98.672  1.00 66.27           N  
ATOM    869  CA  THR A 142      12.827 -28.616  98.363  1.00 66.20           C  
ATOM    870  C   THR A 142      12.003 -27.451  97.860  1.00 67.81           C  
ATOM    871  O   THR A 142      12.361 -26.291  98.106  1.00 70.06           O  
ATOM    872  CB  THR A 142      12.144 -29.255  99.583  1.00 66.37           C  
ATOM    873  OG1 THR A 142      12.057 -28.277 100.620  1.00 65.89           O  
ATOM    874  CG2 THR A 142      12.873 -30.478 100.097  1.00 67.30           C  
ATOM    875  N   GLY A 143      10.897 -27.767  97.204  1.00 67.27           N  
ATOM    876  CA  GLY A 143       9.962 -26.752  96.705  1.00 64.56           C  
ATOM    877  C   GLY A 143       9.440 -25.870  97.810  1.00 66.52           C  
ATOM    878  O   GLY A 143       9.295 -24.652  97.628  1.00 72.96           O  
ATOM    879  N   THR A 144       9.139 -26.476  98.948  1.00 69.08           N  
ATOM    880  CA  THR A 144       8.552 -25.755 100.101  1.00 72.74           C  
ATOM    881  C   THR A 144       9.554 -24.748 100.643  1.00 70.75           C  
ATOM    882  O   THR A 144       9.172 -23.592 100.939  1.00 66.55           O  
ATOM    883  CB  THR A 144       8.088 -26.720 101.200  1.00 73.82           C  
ATOM    884  OG1 THR A 144       6.949 -27.422 100.703  1.00 79.09           O  
ATOM    885  CG2 THR A 144       7.719 -26.022 102.491  1.00 72.99           C  
ATOM    886  N   ARG A 145      10.801 -25.169 100.804  1.00 71.95           N  
ATOM    887  CA  ARG A 145      11.847 -24.273 101.343  1.00 74.15           C  
ATOM    888  C   ARG A 145      12.150 -23.179 100.328  1.00 69.77           C  
ATOM    889  O   ARG A 145      12.352 -22.014 100.727  1.00 61.83           O  
ATOM    890  CB  ARG A 145      13.112 -25.059 101.702  1.00 76.20           C  
ATOM    891  CG  ARG A 145      13.031 -25.762 103.050  1.00 81.94           C  
ATOM    892  CD  ARG A 145      14.089 -26.834 103.225  1.00 81.88           C  
ATOM    893  NE  ARG A 145      13.784 -27.714 104.344  1.00 84.98           N  
ATOM    894  CZ  ARG A 145      14.489 -28.792 104.681  1.00 88.21           C  
ATOM    895  NH1 ARG A 145      15.557 -29.141 103.983  1.00 84.18           N  
ATOM    896  NH2 ARG A 145      14.118 -29.521 105.720  1.00 89.69           N  
ATOM    897  N   ALA A 146      12.192 -23.531  99.046  1.00 63.76           N  
ATOM    898  CA  ALA A 146      12.464 -22.544  97.987  1.00 58.45           C  
ATOM    899  C   ALA A 146      11.406 -21.449  98.010  1.00 57.14           C  
ATOM    900  O   ALA A 146      11.755 -20.249  97.942  1.00 56.29           O  
ATOM    901  CB  ALA A 146      12.512 -23.224  96.644  1.00 59.81           C  
ATOM    902  N   ALA A 147      10.138 -21.842  98.081  1.00 52.05           N  
ATOM    903  CA  ALA A 147       9.031 -20.864  98.103  1.00 52.48           C  
ATOM    904  C   ALA A 147       9.212 -19.909  99.277  1.00 52.64           C  
ATOM    905  O   ALA A 147       8.963 -18.698  99.128  1.00 48.12           O  
ATOM    906  CB  ALA A 147       7.699 -21.566  98.199  1.00 49.27           C  
ATOM    907  N   GLY A 148       9.616 -20.434 100.426  1.00 52.70           N  
ATOM    908  CA  GLY A 148       9.863 -19.573 101.586  1.00 49.27           C  
ATOM    909  C   GLY A 148      10.997 -18.618 101.342  1.00 48.27           C  
ATOM    910  O   GLY A 148      10.923 -17.450 101.778  1.00 44.60           O  
ATOM    911  N   ILE A 149      12.037 -19.089 100.664  1.00 50.90           N  
ATOM    912  CA  ILE A 149      13.218 -18.235 100.371  1.00 50.93           C  
ATOM    913  C   ILE A 149      12.794 -17.135  99.416  1.00 51.49           C  
ATOM    914  O   ILE A 149      13.248 -15.987  99.548  1.00 47.50           O  
ATOM    915  CB  ILE A 149      14.399 -19.046  99.804  1.00 55.56           C  
ATOM    916  CG1 ILE A 149      14.907 -20.103 100.789  1.00 58.38           C  
ATOM    917  CG2 ILE A 149      15.516 -18.108  99.364  1.00 55.83           C  
ATOM    918  CD1 ILE A 149      15.739 -19.544 101.920  1.00 62.27           C  
ATOM    919  N   ILE A 150      11.959 -17.470  98.446  1.00 51.92           N  
ATOM    920  CA  ILE A 150      11.518 -16.465  97.443  1.00 49.87           C  
ATOM    921  C   ILE A 150      10.692 -15.385  98.133  1.00 50.30           C  
ATOM    922  O   ILE A 150      10.873 -14.215  97.852  1.00 46.40           O  
ATOM    923  CB  ILE A 150      10.768 -17.140  96.276  1.00 49.93           C  
ATOM    924  CG1 ILE A 150      11.734 -17.941  95.397  1.00 51.26           C  
ATOM    925  CG2 ILE A 150       9.978 -16.119  95.468  1.00 47.27           C  
ATOM    926  CD1 ILE A 150      11.058 -18.845  94.386  1.00 51.66           C  
ATOM    927  N   ALA A 151       9.806 -15.768  99.034  1.00 49.73           N  
ATOM    928  CA  ALA A 151       8.980 -14.783  99.753  1.00 48.03           C  
ATOM    929  C   ALA A 151       9.865 -13.861 100.584  1.00 47.76           C  
ATOM    930  O   ALA A 151       9.652 -12.630 100.567  1.00 45.98           O  
ATOM    931  CB  ALA A 151       7.957 -15.504 100.597  1.00 48.86           C  
ATOM    932  N   ILE A 152      10.838 -14.421 101.295  1.00 46.87           N  
ATOM    933  CA  ILE A 152      11.721 -13.599 102.158  1.00 48.68           C  
ATOM    934  C   ILE A 152      12.516 -12.622 101.285  1.00 45.52           C  
ATOM    935  O   ILE A 152      12.710 -11.459 101.652  1.00 44.71           O  
ATOM    936  CB  ILE A 152      12.632 -14.486 103.035  1.00 52.87           C  
ATOM    937  CG1 ILE A 152      11.831 -15.154 104.159  1.00 56.07           C  
ATOM    938  CG2 ILE A 152      13.810 -13.693 103.591  1.00 51.87           C  
ATOM    939  CD1 ILE A 152      12.493 -16.386 104.756  1.00 56.07           C  
ATOM    940  N   CYS A 153      12.988 -13.085 100.147  1.00 46.43           N  
ATOM    941  CA  CYS A 153      13.832 -12.242  99.279  1.00 45.16           C  
ATOM    942  C   CYS A 153      13.025 -11.096  98.697  1.00 45.14           C  
ATOM    943  O   CYS A 153      13.531  -9.981  98.611  1.00 45.18           O  
ATOM    944  CB  CYS A 153      14.491 -13.090  98.208  1.00 45.71           C  
ATOM    945  SG  CYS A 153      15.664 -14.266  98.930  1.00 52.39           S  
ATOM    946  N   TRP A 154      11.782 -11.337  98.334  1.00 45.18           N  
ATOM    947  CA  TRP A 154      10.913 -10.242  97.845  1.00 42.71           C  
ATOM    948  C   TRP A 154      10.691  -9.216  98.941  1.00 43.24           C  
ATOM    949  O   TRP A 154      10.775  -8.016  98.672  1.00 38.70           O  
ATOM    950  CB  TRP A 154       9.578 -10.782  97.310  1.00 41.87           C  
ATOM    951  CG  TRP A 154       9.624 -11.168  95.862  1.00 42.56           C  
ATOM    952  CD1 TRP A 154       9.703 -12.428  95.345  1.00 42.04           C  
ATOM    953  CD2 TRP A 154       9.605 -10.277  94.732  1.00 40.97           C  
ATOM    954  NE1 TRP A 154       9.718 -12.383  93.976  1.00 40.98           N  
ATOM    955  CE2 TRP A 154       9.662 -11.078  93.572  1.00 41.26           C  
ATOM    956  CE3 TRP A 154       9.530  -8.886  94.587  1.00 39.91           C  
ATOM    957  CZ2 TRP A 154       9.662 -10.531  92.288  1.00 43.79           C  
ATOM    958  CZ3 TRP A 154       9.510  -8.348  93.318  1.00 41.99           C  
ATOM    959  CH2 TRP A 154       9.582  -9.161  92.185  1.00 42.74           C  
ATOM    960  N   VAL A 155      10.433  -9.659 100.163  1.00 43.99           N  
ATOM    961  CA  VAL A 155      10.248  -8.710 101.293  1.00 41.67           C  
ATOM    962  C   VAL A 155      11.525  -7.881 101.476  1.00 41.77           C  
ATOM    963  O   VAL A 155      11.458  -6.659 101.587  1.00 40.03           O  
ATOM    964  CB  VAL A 155       9.826  -9.421 102.601  1.00 46.60           C  
ATOM    965  CG1 VAL A 155       9.946  -8.518 103.826  1.00 43.68           C  
ATOM    966  CG2 VAL A 155       8.408  -9.978 102.504  1.00 46.47           C  
ATOM    967  N   LEU A 156      12.672  -8.540 101.520  1.00 40.68           N  
ATOM    968  CA  LEU A 156      13.947  -7.825 101.672  1.00 42.14           C  
ATOM    969  C   LEU A 156      14.179  -6.897 100.476  1.00 42.61           C  
ATOM    970  O   LEU A 156      14.758  -5.812 100.643  1.00 41.43           O  
ATOM    971  CB  LEU A 156      15.090  -8.833 101.803  1.00 43.85           C  
ATOM    972  CG  LEU A 156      15.143  -9.608 103.115  1.00 47.55           C  
ATOM    973  CD1 LEU A 156      16.137 -10.755 103.017  1.00 48.32           C  
ATOM    974  CD2 LEU A 156      15.494  -8.694 104.281  1.00 48.76           C  
ATOM    975  N   SER A 157      13.749  -7.299  99.289  1.00 41.20           N  
ATOM    976  CA  SER A 157      13.920  -6.447  98.100  1.00 40.17           C  
ATOM    977  C   SER A 157      13.112  -5.162  98.242  1.00 40.54           C  
ATOM    978  O   SER A 157      13.586  -4.092  97.848  1.00 37.44           O  
ATOM    979  CB  SER A 157      13.595  -7.186  96.830  1.00 41.73           C  
ATOM    980  OG  SER A 157      14.518  -8.254  96.614  1.00 41.11           O  
ATOM    981  N   PHE A 158      11.921  -5.249  98.801  1.00 39.42           N  
ATOM    982  CA  PHE A 158      11.122  -4.034  99.064  1.00 41.35           C  
ATOM    983  C   PHE A 158      11.831  -3.153 100.077  1.00 40.16           C  
ATOM    984  O   PHE A 158      11.950  -1.952  99.864  1.00 40.71           O  
ATOM    985  CB  PHE A 158       9.702  -4.401  99.507  1.00 41.83           C  
ATOM    986  CG  PHE A 158       8.720  -4.520  98.367  1.00 42.43           C  
ATOM    987  CD1 PHE A 158       8.106  -3.395  97.842  1.00 42.07           C  
ATOM    988  CD2 PHE A 158       8.431  -5.749  97.799  1.00 43.89           C  
ATOM    989  CE1 PHE A 158       7.210  -3.501  96.790  1.00 43.79           C  
ATOM    990  CE2 PHE A 158       7.545  -5.850  96.738  1.00 44.82           C  
ATOM    991  CZ  PHE A 158       6.933  -4.729  96.238  1.00 42.67           C  
ATOM    992  N   ALA A 159      12.340  -3.733 101.146  1.00 41.57           N  
ATOM    993  CA  ALA A 159      13.035  -2.951 102.195  1.00 41.13           C  
ATOM    994  C   ALA A 159      14.258  -2.249 101.616  1.00 40.51           C  
ATOM    995  O   ALA A 159      14.462  -1.070 101.856  1.00 41.91           O  
ATOM    996  CB  ALA A 159      13.428  -3.864 103.332  1.00 40.02           C  
ATOM    997  N   ILE A 160      15.069  -2.977 100.862  1.00 40.66           N  
ATOM    998  CA  ILE A 160      16.327  -2.412 100.316  1.00 39.45           C  
ATOM    999  C   ILE A 160      15.984  -1.345  99.274  1.00 37.38           C  
ATOM   1000  O   ILE A 160      16.557  -0.236  99.290  1.00 36.92           O  
ATOM   1001  CB  ILE A 160      17.238  -3.509  99.729  1.00 38.49           C  
ATOM   1002  CG1 ILE A 160      17.891  -4.353 100.824  1.00 40.41           C  
ATOM   1003  CG2 ILE A 160      18.288  -2.911  98.804  1.00 40.25           C  
ATOM   1004  CD1 ILE A 160      18.344  -5.735 100.357  1.00 40.96           C  
ATOM   1005  N   GLY A 161      15.091  -1.672  98.358  1.00 38.95           N  
ATOM   1006  CA  GLY A 161      14.809  -0.768  97.241  1.00 38.56           C  
ATOM   1007  C   GLY A 161      14.059   0.477  97.633  1.00 38.70           C  
ATOM   1008  O   GLY A 161      14.254   1.523  97.023  1.00 38.40           O  
ATOM   1009  N   LEU A 162      13.293   0.401  98.703  1.00 39.75           N  
ATOM   1010  CA  LEU A 162      12.463   1.565  99.121  1.00 40.01           C  
ATOM   1011  C   LEU A 162      13.022   2.173 100.378  1.00 38.18           C  
ATOM   1012  O   LEU A 162      12.256   2.872 101.095  1.00 40.22           O  
ATOM   1013  CB  LEU A 162      11.012   1.110  99.355  1.00 40.26           C  
ATOM   1014  CG  LEU A 162      10.307   0.440  98.176  1.00 40.95           C  
ATOM   1015  CD1 LEU A 162       8.873   0.078  98.546  1.00 42.92           C  
ATOM   1016  CD2 LEU A 162      10.336   1.328  96.934  1.00 40.29           C  
ATOM   1017  N   THR A 163      14.284   1.915 100.699  1.00 40.61           N  
ATOM   1018  CA  THR A 163      14.972   2.578 101.848  1.00 42.70           C  
ATOM   1019  C   THR A 163      14.875   4.087 101.797  1.00 39.71           C  
ATOM   1020  O   THR A 163      14.633   4.684 102.830  1.00 40.17           O  
ATOM   1021  CB  THR A 163      16.433   2.104 101.932  1.00 42.85           C  
ATOM   1022  OG1 THR A 163      16.452   0.813 102.543  1.00 43.40           O  
ATOM   1023  CG2 THR A 163      17.328   3.026 102.725  1.00 44.59           C  
ATOM   1024  N   PRO A 164      15.022   4.747 100.629  1.00 38.93           N  
ATOM   1025  CA  PRO A 164      14.810   6.198 100.566  1.00 40.80           C  
ATOM   1026  C   PRO A 164      13.486   6.686 101.154  1.00 41.89           C  
ATOM   1027  O   PRO A 164      13.441   7.764 101.728  1.00 43.27           O  
ATOM   1028  CB  PRO A 164      14.850   6.463  99.050  1.00 38.38           C  
ATOM   1029  CG  PRO A 164      15.780   5.394  98.529  1.00 36.60           C  
ATOM   1030  CD  PRO A 164      15.413   4.169  99.334  1.00 37.34           C  
ATOM   1031  N   MET A 165      12.456   5.855 101.064  1.00 42.19           N  
ATOM   1032  CA  MET A 165      11.125   6.192 101.602  1.00 46.13           C  
ATOM   1033  C   MET A 165      11.131   6.259 103.138  1.00 47.18           C  
ATOM   1034  O   MET A 165      10.327   6.997 103.702  1.00 49.29           O  
ATOM   1035  CB  MET A 165      10.058   5.227 101.066  1.00 47.15           C  
ATOM   1036  CG  MET A 165       9.864   5.372  99.547  1.00 47.86           C  
ATOM   1037  SD  MET A 165       8.459   4.453  98.860  1.00 53.50           S  
ATOM   1038  CE  MET A 165       7.157   5.669  99.061  1.00 55.32           C  
ATOM   1039  N   LEU A 166      12.089   5.615 103.777  1.00 45.13           N  
ATOM   1040  CA  LEU A 166      12.170   5.624 105.245  1.00 46.30           C  
ATOM   1041  C   LEU A 166      12.892   6.867 105.759  1.00 44.72           C  
ATOM   1042  O   LEU A 166      13.118   6.934 106.986  1.00 51.76           O  
ATOM   1043  CB  LEU A 166      12.852   4.334 105.737  1.00 45.72           C  
ATOM   1044  CG  LEU A 166      12.360   3.008 105.132  1.00 47.27           C  
ATOM   1045  CD1 LEU A 166      13.005   1.823 105.829  1.00 48.59           C  
ATOM   1046  CD2 LEU A 166      10.853   2.863 105.193  1.00 46.46           C  
ATOM   1047  N   GLY A 167      13.343   7.763 104.878  1.00 39.25           N  
ATOM   1048  CA  GLY A 167      13.927   9.035 105.319  1.00 40.46           C  
ATOM   1049  C   GLY A 167      15.258   9.378 104.687  1.00 40.34           C  
ATOM   1050  O   GLY A 167      15.701  10.535 104.815  1.00 43.43           O  
ATOM   1051  N   TRP A 168      15.858   8.442 103.975  1.00 41.77           N  
ATOM   1052  CA  TRP A 168      17.131   8.664 103.271  1.00 40.44           C  
ATOM   1053  C   TRP A 168      16.807   9.224 101.898  1.00 41.89           C  
ATOM   1054  O   TRP A 168      16.851   8.484 100.898  1.00 39.26           O  
ATOM   1055  CB  TRP A 168      17.966   7.379 103.175  1.00 39.68           C  
ATOM   1056  CG  TRP A 168      19.403   7.637 102.835  1.00 40.93           C  
ATOM   1057  CD1 TRP A 168      19.972   8.841 102.521  1.00 38.62           C  
ATOM   1058  CD2 TRP A 168      20.463   6.663 102.765  1.00 35.72           C  
ATOM   1059  NE1 TRP A 168      21.306   8.682 102.266  1.00 41.48           N  
ATOM   1060  CE2 TRP A 168      21.638   7.358 102.409  1.00 36.45           C  
ATOM   1061  CE3 TRP A 168      20.532   5.281 102.964  1.00 35.57           C  
ATOM   1062  CZ2 TRP A 168      22.864   6.720 102.260  1.00 34.67           C  
ATOM   1063  CZ3 TRP A 168      21.746   4.648 102.811  1.00 38.52           C  
ATOM   1064  CH2 TRP A 168      22.899   5.363 102.472  1.00 36.43           C  
ATOM   1065  N   ASN A 169      16.488  10.504 101.846  1.00 40.86           N  
ATOM   1066  CA  ASN A 169      15.996  11.131 100.612  1.00 40.26           C  
ATOM   1067  C   ASN A 169      16.298  12.608 100.683  1.00 39.69           C  
ATOM   1068  O   ASN A 169      16.645  13.116 101.788  1.00 41.52           O  
ATOM   1069  CB  ASN A 169      14.517  10.808 100.377  1.00 41.58           C  
ATOM   1070  CG  ASN A 169      13.606  11.292 101.484  1.00 42.88           C  
ATOM   1071  OD1 ASN A 169      13.475  12.491 101.702  1.00 44.75           O  
ATOM   1072  ND2 ASN A 169      12.953  10.368 102.170  1.00 40.39           N  
ATOM   1073  N   ASN A 170      16.063  13.291  99.572  1.00 41.54           N  
ATOM   1074  CA  ASN A 170      16.209  14.765  99.492  1.00 43.29           C  
ATOM   1075  C   ASN A 170      14.859  15.459  99.503  1.00 42.67           C  
ATOM   1076  O   ASN A 170      14.808  16.594  99.114  1.00 43.82           O  
ATOM   1077  CB  ASN A 170      16.953  15.177  98.217  1.00 45.24           C  
ATOM   1078  CG  ASN A 170      18.289  14.484  98.040  1.00 47.18           C  
ATOM   1079  OD1 ASN A 170      18.977  14.200  99.009  1.00 47.73           O  
ATOM   1080  ND2 ASN A 170      18.669  14.209  96.802  1.00 50.98           N  
ATOM   1081  N   CYS A 171      13.800  14.787  99.933  1.00 44.70           N  
ATOM   1082  CA  CYS A 171      12.482  15.428 100.087  1.00 46.43           C  
ATOM   1083  C   CYS A 171      12.554  16.609 101.041  1.00 48.29           C  
ATOM   1084  O   CYS A 171      11.740  17.535 100.882  1.00 51.20           O  
ATOM   1085  CB  CYS A 171      11.426  14.444 100.565  1.00 46.39           C  
ATOM   1086  SG  CYS A 171      11.037  13.186  99.321  1.00 53.49           S  
ATOM   1087  N   GLY A 172      13.484  16.560 101.988  1.00 54.91           N  
ATOM   1088  CA  GLY A 172      13.672  17.613 102.992  1.00 53.79           C  
ATOM   1089  C   GLY A 172      14.296  18.882 102.441  1.00 55.79           C  
ATOM   1090  O   GLY A 172      14.206  19.940 103.085  1.00 58.90           O  
ATOM   1091  N   GLN A 173      14.982  18.777 101.315  1.00 61.58           N  
ATOM   1092  CA  GLN A 173      15.692  19.922 100.708  1.00 61.25           C  
ATOM   1093  C   GLN A 173      15.215  20.081  99.276  1.00 56.56           C  
ATOM   1094  O   GLN A 173      15.968  19.866  98.334  1.00 52.84           O  
ATOM   1095  CB  GLN A 173      17.199  19.725 100.881  1.00 69.61           C  
ATOM   1096  CG  GLN A 173      17.615  19.717 102.353  1.00 80.25           C  
ATOM   1097  CD  GLN A 173      19.073  19.418 102.599  1.00 88.58           C  
ATOM   1098  OE1 GLN A 173      19.717  18.687 101.847  1.00102.74           O  
ATOM   1099  NE2 GLN A 173      19.599  19.962 103.687  1.00 92.48           N  
ATOM   1100  N   PRO A 174      13.929  20.442  99.074  1.00 58.51           N  
ATOM   1101  CA  PRO A 174      13.374  20.437  97.721  1.00 55.90           C  
ATOM   1102  C   PRO A 174      13.958  21.572  96.904  1.00 57.47           C  
ATOM   1103  O   PRO A 174      14.335  22.553  97.522  1.00 57.74           O  
ATOM   1104  CB  PRO A 174      11.861  20.628  97.935  1.00 54.93           C  
ATOM   1105  CG  PRO A 174      11.750  21.282  99.298  1.00 54.48           C  
ATOM   1106  CD  PRO A 174      12.914  20.734 100.100  1.00 57.27           C  
ATOM   1107  N   LYS A 175      14.040  21.421  95.589  1.00 62.36           N  
ATOM   1108  CA  LYS A 175      14.536  22.500  94.736  1.00 61.14           C  
ATOM   1109  C   LYS A 175      13.394  23.476  94.509  1.00 64.43           C  
ATOM   1110  O   LYS A 175      12.477  23.163  93.730  1.00 62.19           O  
ATOM   1111  CB  LYS A 175      15.101  21.919  93.439  1.00 61.52           C  
ATOM   1112  CG  LYS A 175      16.251  20.951  93.653  1.00 60.48           C  
ATOM   1113  CD  LYS A 175      17.281  20.963  92.564  1.00 61.79           C  
ATOM   1114  CE  LYS A 175      18.553  20.263  92.987  1.00 66.54           C  
ATOM   1115  NZ  LYS A 175      19.121  19.457  91.884  1.00 69.84           N  
ATOM   1116  N   GLU A 176      13.446  24.649  95.134  1.00 73.95           N  
ATOM   1117  CA  GLU A 176      12.248  25.519  95.136  1.00 73.13           C  
ATOM   1118  C   GLU A 176      12.180  26.263  93.813  1.00 68.04           C  
ATOM   1119  O   GLU A 176      11.086  26.503  93.315  1.00 68.53           O  
ATOM   1120  CB  GLU A 176      12.228  26.428  96.368  1.00 79.18           C  
ATOM   1121  CG  GLU A 176      11.829  25.696  97.640  1.00 77.86           C  
ATOM   1122  CD  GLU A 176      10.478  25.000  97.590  1.00 82.42           C  
ATOM   1123  OE1 GLU A 176       9.708  25.278  96.652  1.00 89.95           O  
ATOM   1124  OE2 GLU A 176      10.197  24.183  98.491  1.00 86.78           O  
ATOM   1125  N   GLY A 177      13.323  26.580  93.235  1.00 67.15           N  
ATOM   1126  CA  GLY A 177      13.371  27.239  91.923  1.00 68.34           C  
ATOM   1127  C   GLY A 177      12.695  26.428  90.844  1.00 68.05           C  
ATOM   1128  O   GLY A 177      11.861  26.956  90.093  1.00 73.35           O  
ATOM   1129  N   LYS A 178      13.038  25.155  90.771  1.00 64.41           N  
ATOM   1130  CA  LYS A 178      12.475  24.232  89.767  1.00 65.26           C  
ATOM   1131  C   LYS A 178      10.991  24.019  90.061  1.00 62.28           C  
ATOM   1132  O   LYS A 178      10.176  23.909  89.098  1.00 57.98           O  
ATOM   1133  CB  LYS A 178      13.250  22.911  89.817  1.00 67.65           C  
ATOM   1134  CG  LYS A 178      13.435  22.194  88.491  1.00 68.30           C  
ATOM   1135  CD  LYS A 178      14.292  20.955  88.628  1.00 76.32           C  
ATOM   1136  CE  LYS A 178      15.480  20.937  87.689  1.00 80.08           C  
ATOM   1137  NZ  LYS A 178      16.452  19.890  88.076  1.00 80.11           N  
ATOM   1138  N   ALA A 179      10.631  23.951  91.344  1.00 60.01           N  
ATOM   1139  CA  ALA A 179       9.245  23.645  91.740  1.00 59.38           C  
ATOM   1140  C   ALA A 179       8.292  24.734  91.248  1.00 62.26           C  
ATOM   1141  O   ALA A 179       7.241  24.423  90.608  1.00 54.62           O  
ATOM   1142  CB  ALA A 179       9.153  23.427  93.231  1.00 58.10           C  
ATOM   1143  N   HIS A 180       8.710  25.977  91.411  1.00 62.67           N  
ATOM   1144  CA  HIS A 180       7.902  27.168  91.083  1.00 66.52           C  
ATOM   1145  C   HIS A 180       8.032  27.476  89.602  1.00 66.93           C  
ATOM   1146  O   HIS A 180       7.033  27.938  89.005  1.00 71.07           O  
ATOM   1147  CB  HIS A 180       8.325  28.371  91.947  1.00 68.31           C  
ATOM   1148  CG  HIS A 180       8.035  28.207  93.402  1.00 71.07           C  
ATOM   1149  ND1 HIS A 180       8.964  28.505  94.378  1.00 75.47           N  
ATOM   1150  CD2 HIS A 180       6.934  27.769  94.051  1.00 74.97           C  
ATOM   1151  CE1 HIS A 180       8.447  28.257  95.565  1.00 78.90           C  
ATOM   1152  NE2 HIS A 180       7.203  27.804  95.391  1.00 75.57           N  
ATOM   1153  N   SER A 181       9.211  27.288  89.009  1.00 64.66           N  
ATOM   1154  CA  SER A 181       9.396  27.428  87.554  1.00 62.82           C  
ATOM   1155  C   SER A 181       8.421  26.497  86.828  1.00 62.36           C  
ATOM   1156  O   SER A 181       7.856  26.882  85.777  1.00 65.82           O  
ATOM   1157  CB  SER A 181      10.825  27.115  87.182  1.00 64.33           C  
ATOM   1158  OG  SER A 181      10.978  26.990  85.778  1.00 69.15           O  
ATOM   1159  N   GLN A 182       8.258  25.277  87.374  1.00 66.91           N  
ATOM   1160  CA  GLN A 182       7.338  24.310  86.755  1.00 67.12           C  
ATOM   1161  C   GLN A 182       5.899  24.530  87.193  1.00 68.24           C  
ATOM   1162  O   GLN A 182       5.037  23.750  86.782  1.00 69.46           O  
ATOM   1163  CB  GLN A 182       7.803  22.887  87.040  1.00 72.38           C  
ATOM   1164  CG  GLN A 182       9.094  22.538  86.321  1.00 78.92           C  
ATOM   1165  CD  GLN A 182       9.300  21.050  86.253  1.00 85.64           C  
ATOM   1166  OE1 GLN A 182       8.347  20.274  86.308  1.00 89.07           O  
ATOM   1167  NE2 GLN A 182      10.553  20.642  86.130  1.00 90.76           N  
ATOM   1168  N   GLY A 183       5.661  25.380  88.168  1.00 71.33           N  
ATOM   1169  CA  GLY A 183       4.316  25.668  88.660  1.00 64.67           C  
ATOM   1170  C   GLY A 183       3.698  24.613  89.543  1.00 66.59           C  
ATOM   1171  O   GLY A 183       2.482  24.650  89.701  1.00 69.67           O  
ATOM   1172  N   CYS A 184       4.470  23.729  90.132  1.00 63.70           N  
ATOM   1173  CA  CYS A 184       3.958  22.740  91.087  1.00 65.79           C  
ATOM   1174  C   CYS A 184       3.275  23.434  92.268  1.00 62.80           C  
ATOM   1175  O   CYS A 184       3.649  24.564  92.663  1.00 66.81           O  
ATOM   1176  CB  CYS A 184       5.108  21.879  91.607  1.00 62.93           C  
ATOM   1177  SG  CYS A 184       6.177  21.251  90.284  1.00 63.44           S  
ATOM   1178  N   GLY A 185       2.256  22.781  92.767  1.00 65.86           N  
ATOM   1179  CA  GLY A 185       1.673  23.080  94.079  1.00 68.22           C  
ATOM   1180  C   GLY A 185       2.706  23.048  95.170  1.00 70.60           C  
ATOM   1181  O   GLY A 185       3.810  22.526  94.981  1.00 73.30           O  
ATOM   1182  N   GLU A 186       2.337  23.540  96.327  1.00 77.52           N  
ATOM   1183  CA  GLU A 186       3.208  23.458  97.517  1.00 82.28           C  
ATOM   1184  C   GLU A 186       3.110  22.080  98.137  1.00 77.91           C  
ATOM   1185  O   GLU A 186       2.032  21.463  98.071  1.00 79.51           O  
ATOM   1186  CB  GLU A 186       2.826  24.575  98.490  1.00 88.88           C  
ATOM   1187  CG  GLU A 186       3.173  25.961  97.958  1.00 93.33           C  
ATOM   1188  CD  GLU A 186       2.244  27.087  98.384  1.00103.35           C  
ATOM   1189  OE1 GLU A 186       1.609  26.966  99.455  1.00111.88           O  
ATOM   1190  OE2 GLU A 186       2.160  28.088  97.642  1.00102.24           O  
ATOM   1191  N   GLY A 187       4.230  21.635  98.697  1.00 76.78           N  
ATOM   1192  CA  GLY A 187       4.430  20.251  99.103  1.00 69.41           C  
ATOM   1193  C   GLY A 187       4.901  19.379  97.970  1.00 67.43           C  
ATOM   1194  O   GLY A 187       5.153  18.178  98.234  1.00 71.61           O  
ATOM   1195  N   GLN A 188       5.037  19.928  96.766  1.00 60.45           N  
ATOM   1196  CA  GLN A 188       5.337  19.112  95.575  1.00 59.60           C  
ATOM   1197  C   GLN A 188       6.651  19.550  94.979  1.00 53.65           C  
ATOM   1198  O   GLN A 188       7.018  20.701  95.112  1.00 55.54           O  
ATOM   1199  CB  GLN A 188       4.311  19.334  94.464  1.00 58.06           C  
ATOM   1200  CG  GLN A 188       2.896  18.946  94.828  1.00 61.31           C  
ATOM   1201  CD  GLN A 188       2.031  18.937  93.596  1.00 60.89           C  
ATOM   1202  OE1 GLN A 188       2.244  19.708  92.660  1.00 60.05           O  
ATOM   1203  NE2 GLN A 188       1.059  18.044  93.581  1.00 58.77           N  
ATOM   1204  N   VAL A 189       7.293  18.620  94.273  1.00 47.06           N  
ATOM   1205  CA  VAL A 189       8.606  18.861  93.649  1.00 49.73           C  
ATOM   1206  C   VAL A 189       8.523  18.552  92.165  1.00 45.52           C  
ATOM   1207  O   VAL A 189       7.617  17.855  91.707  1.00 43.44           O  
ATOM   1208  CB  VAL A 189       9.752  18.077  94.315  1.00 48.80           C  
ATOM   1209  CG1 VAL A 189      10.027  18.594  95.713  1.00 48.14           C  
ATOM   1210  CG2 VAL A 189       9.503  16.576  94.319  1.00 51.03           C  
ATOM   1211  N   ALA A 190       9.453  19.054  91.410  1.00 47.29           N  
ATOM   1212  CA  ALA A 190       9.704  18.506  90.066  1.00 48.87           C  
ATOM   1213  C   ALA A 190      10.244  17.095  90.247  1.00 50.38           C  
ATOM   1214  O   ALA A 190      11.330  16.925  90.786  1.00 56.51           O  
ATOM   1215  CB  ALA A 190      10.662  19.393  89.311  1.00 50.66           C  
ATOM   1216  N   CYS A 191       9.483  16.115  89.814  1.00 49.01           N  
ATOM   1217  CA  CYS A 191       9.760  14.689  90.103  1.00 48.18           C  
ATOM   1218  C   CYS A 191      10.842  14.201  89.168  1.00 50.11           C  
ATOM   1219  O   CYS A 191      10.538  13.753  88.054  1.00 53.64           O  
ATOM   1220  CB  CYS A 191       8.499  13.855  89.948  1.00 49.65           C  
ATOM   1221  SG  CYS A 191       8.755  12.106  90.323  1.00 52.16           S  
ATOM   1222  N   LEU A 192      12.091  14.289  89.631  1.00 49.40           N  
ATOM   1223  CA  LEU A 192      13.262  13.812  88.880  1.00 47.74           C  
ATOM   1224  C   LEU A 192      14.053  12.864  89.758  1.00 46.76           C  
ATOM   1225  O   LEU A 192      14.306  13.181  90.914  1.00 47.45           O  
ATOM   1226  CB  LEU A 192      14.095  15.017  88.444  1.00 49.40           C  
ATOM   1227  CG  LEU A 192      13.452  15.890  87.371  1.00 49.61           C  
ATOM   1228  CD1 LEU A 192      14.190  17.214  87.234  1.00 51.44           C  
ATOM   1229  CD2 LEU A 192      13.405  15.162  86.041  1.00 46.73           C  
ATOM   1230  N   PHE A 193      14.538  11.790  89.189  1.00 46.40           N  
ATOM   1231  CA  PHE A 193      15.298  10.761  89.935  1.00 45.00           C  
ATOM   1232  C   PHE A 193      16.409  11.385  90.782  1.00 45.15           C  
ATOM   1233  O   PHE A 193      16.424  11.193  92.014  1.00 39.99           O  
ATOM   1234  CB  PHE A 193      15.878   9.712  88.988  1.00 43.60           C  
ATOM   1235  CG  PHE A 193      16.502   8.524  89.679  1.00 41.87           C  
ATOM   1236  CD1 PHE A 193      17.823   8.562  90.109  1.00 40.41           C  
ATOM   1237  CD2 PHE A 193      15.777   7.358  89.880  1.00 39.17           C  
ATOM   1238  CE1 PHE A 193      18.391   7.471  90.751  1.00 40.54           C  
ATOM   1239  CE2 PHE A 193      16.354   6.262  90.510  1.00 39.89           C  
ATOM   1240  CZ  PHE A 193      17.660   6.318  90.940  1.00 39.22           C  
ATOM   1241  N   GLU A 194      17.308  12.120  90.146  1.00 43.25           N  
ATOM   1242  CA  GLU A 194      18.519  12.627  90.816  1.00 46.38           C  
ATOM   1243  C   GLU A 194      18.204  13.754  91.793  1.00 44.57           C  
ATOM   1244  O   GLU A 194      19.098  14.112  92.572  1.00 50.79           O  
ATOM   1245  CB  GLU A 194      19.561  13.059  89.781  1.00 46.74           C  
ATOM   1246  CG  GLU A 194      20.129  11.887  88.999  1.00 52.87           C  
ATOM   1247  CD  GLU A 194      21.418  12.151  88.238  1.00 56.25           C  
ATOM   1248  OE1 GLU A 194      22.351  12.722  88.835  1.00 56.13           O  
ATOM   1249  OE2 GLU A 194      21.486  11.770  87.049  1.00 60.47           O  
ATOM   1250  N   ASP A 195      16.995  14.277  91.793  1.00 41.04           N  
ATOM   1251  CA  ASP A 195      16.610  15.318  92.758  1.00 45.48           C  
ATOM   1252  C   ASP A 195      16.122  14.712  94.068  1.00 42.73           C  
ATOM   1253  O   ASP A 195      16.262  15.348  95.124  1.00 49.82           O  
ATOM   1254  CB  ASP A 195      15.584  16.280  92.140  1.00 49.11           C  
ATOM   1255  CG  ASP A 195      16.155  17.191  91.055  1.00 52.92           C  
ATOM   1256  OD1 ASP A 195      17.389  17.172  90.850  1.00 53.41           O  
ATOM   1257  OD2 ASP A 195      15.357  17.912  90.410  1.00 59.72           O  
ATOM   1258  N   VAL A 196      15.559  13.513  94.028  1.00 41.35           N  
ATOM   1259  CA  VAL A 196      14.815  12.942  95.178  1.00 41.24           C  
ATOM   1260  C   VAL A 196      15.568  11.767  95.795  1.00 40.37           C  
ATOM   1261  O   VAL A 196      15.501  11.595  97.032  1.00 38.87           O  
ATOM   1262  CB  VAL A 196      13.360  12.573  94.813  1.00 43.22           C  
ATOM   1263  CG1 VAL A 196      12.605  13.769  94.265  1.00 48.13           C  
ATOM   1264  CG2 VAL A 196      13.251  11.395  93.857  1.00 43.05           C  
ATOM   1265  N   VAL A 197      16.274  10.966  94.999  1.00 36.26           N  
ATOM   1266  CA  VAL A 197      17.073   9.839  95.517  1.00 40.43           C  
ATOM   1267  C   VAL A 197      18.479  10.356  95.768  1.00 40.05           C  
ATOM   1268  O   VAL A 197      19.128  10.838  94.853  1.00 44.58           O  
ATOM   1269  CB  VAL A 197      17.071   8.644  94.548  1.00 39.85           C  
ATOM   1270  CG1 VAL A 197      17.914   7.504  95.069  1.00 39.56           C  
ATOM   1271  CG2 VAL A 197      15.662   8.162  94.246  1.00 41.96           C  
ATOM   1272  N   PRO A 198      19.013  10.247  97.003  1.00 42.58           N  
ATOM   1273  CA  PRO A 198      20.368  10.706  97.288  1.00 41.88           C  
ATOM   1274  C   PRO A 198      21.420   9.847  96.574  1.00 39.25           C  
ATOM   1275  O   PRO A 198      21.265   8.626  96.482  1.00 37.06           O  
ATOM   1276  CB  PRO A 198      20.487  10.568  98.818  1.00 42.25           C  
ATOM   1277  CG  PRO A 198      19.051  10.521  99.298  1.00 42.46           C  
ATOM   1278  CD  PRO A 198      18.316   9.769  98.210  1.00 41.01           C  
ATOM   1279  N   MET A 199      22.464  10.476  96.058  1.00 39.88           N  
ATOM   1280  CA  MET A 199      23.492   9.725  95.296  1.00 40.47           C  
ATOM   1281  C   MET A 199      24.344   8.883  96.265  1.00 39.90           C  
ATOM   1282  O   MET A 199      24.838   7.833  95.843  1.00 38.12           O  
ATOM   1283  CB  MET A 199      24.356  10.664  94.455  1.00 43.02           C  
ATOM   1284  CG  MET A 199      24.848  10.034  93.175  1.00 49.80           C  
ATOM   1285  SD  MET A 199      23.555   9.211  92.180  1.00 58.44           S  
ATOM   1286  CE  MET A 199      23.032  10.562  91.126  1.00 58.33           C  
ATOM   1287  N   ASN A 200      24.487   9.277  97.537  1.00 40.63           N  
ATOM   1288  CA  ASN A 200      25.234   8.450  98.524  1.00 40.61           C  
ATOM   1289  C   ASN A 200      24.505   7.128  98.727  1.00 40.01           C  
ATOM   1290  O   ASN A 200      25.155   6.080  98.827  1.00 40.04           O  
ATOM   1291  CB  ASN A 200      25.527   9.208  99.823  1.00 46.07           C  
ATOM   1292  CG  ASN A 200      24.318   9.860 100.456  1.00 49.25           C  
ATOM   1293  OD1 ASN A 200      23.179   9.517 100.148  1.00 53.26           O  
ATOM   1294  ND2 ASN A 200      24.564  10.789 101.363  1.00 49.69           N  
ATOM   1295  N   TYR A 201      23.181   7.164  98.751  1.00 38.24           N  
ATOM   1296  CA  TYR A 201      22.383   5.925  98.816  1.00 34.88           C  
ATOM   1297  C   TYR A 201      22.650   5.073  97.584  1.00 33.13           C  
ATOM   1298  O   TYR A 201      22.857   3.853  97.696  1.00 33.62           O  
ATOM   1299  CB  TYR A 201      20.870   6.196  98.912  1.00 37.80           C  
ATOM   1300  CG  TYR A 201      20.021   4.995  98.569  1.00 35.02           C  
ATOM   1301  CD1 TYR A 201      19.712   4.043  99.519  1.00 36.39           C  
ATOM   1302  CD2 TYR A 201      19.634   4.742  97.262  1.00 37.48           C  
ATOM   1303  CE1 TYR A 201      18.997   2.897  99.198  1.00 37.46           C  
ATOM   1304  CE2 TYR A 201      18.906   3.609  96.922  1.00 37.06           C  
ATOM   1305  CZ  TYR A 201      18.584   2.683  97.894  1.00 36.93           C  
ATOM   1306  OH  TYR A 201      17.890   1.559  97.568  1.00 37.49           O  
ATOM   1307  N   MET A 202      22.599   5.687  96.404  1.00 34.20           N  
ATOM   1308  CA  MET A 202      22.697   4.914  95.142  1.00 34.60           C  
ATOM   1309  C   MET A 202      24.072   4.265  95.024  1.00 34.95           C  
ATOM   1310  O   MET A 202      24.185   3.147  94.515  1.00 31.05           O  
ATOM   1311  CB  MET A 202      22.429   5.796  93.920  1.00 36.94           C  
ATOM   1312  CG  MET A 202      20.944   6.063  93.687  1.00 37.57           C  
ATOM   1313  SD  MET A 202      19.990   4.530  93.613  1.00 40.47           S  
ATOM   1314  CE  MET A 202      20.792   3.707  92.239  1.00 39.97           C  
ATOM   1315  N   VAL A 203      25.109   4.951  95.479  1.00 37.67           N  
ATOM   1316  CA  VAL A 203      26.503   4.483  95.270  1.00 38.46           C  
ATOM   1317  C   VAL A 203      26.916   3.546  96.391  1.00 36.77           C  
ATOM   1318  O   VAL A 203      27.275   2.395  96.124  1.00 33.57           O  
ATOM   1319  CB  VAL A 203      27.489   5.654  95.097  1.00 40.22           C  
ATOM   1320  CG1 VAL A 203      28.928   5.173  94.990  1.00 41.27           C  
ATOM   1321  CG2 VAL A 203      27.131   6.491  93.885  1.00 42.49           C  
ATOM   1322  N   TYR A 204      26.891   4.021  97.626  1.00 36.90           N  
ATOM   1323  CA  TYR A 204      27.396   3.222  98.766  1.00 37.41           C  
ATOM   1324  C   TYR A 204      26.437   2.097  99.108  1.00 39.34           C  
ATOM   1325  O   TYR A 204      26.870   0.940  99.254  1.00 39.13           O  
ATOM   1326  CB  TYR A 204      27.649   4.097  99.992  1.00 37.87           C  
ATOM   1327  CG  TYR A 204      28.814   5.044  99.849  1.00 40.44           C  
ATOM   1328  CD1 TYR A 204      30.011   4.630  99.290  1.00 41.18           C  
ATOM   1329  CD2 TYR A 204      28.728   6.355 100.284  1.00 44.05           C  
ATOM   1330  CE1 TYR A 204      31.087   5.495  99.156  1.00 43.35           C  
ATOM   1331  CE2 TYR A 204      29.795   7.231 100.161  1.00 46.13           C  
ATOM   1332  CZ  TYR A 204      30.981   6.797  99.599  1.00 43.37           C  
ATOM   1333  OH  TYR A 204      32.031   7.653  99.475  1.00 46.87           O  
ATOM   1334  N   PHE A 205      25.150   2.402  99.217  1.00 39.82           N  
ATOM   1335  CA  PHE A 205      24.180   1.415  99.733  1.00 39.29           C  
ATOM   1336  C   PHE A 205      23.702   0.508  98.615  1.00 39.34           C  
ATOM   1337  O   PHE A 205      23.853  -0.727  98.702  1.00 42.69           O  
ATOM   1338  CB  PHE A 205      23.020   2.102 100.450  1.00 43.10           C  
ATOM   1339  CG  PHE A 205      22.140   1.177 101.260  1.00 43.94           C  
ATOM   1340  CD1 PHE A 205      21.080   0.500 100.666  1.00 44.06           C  
ATOM   1341  CD2 PHE A 205      22.340   1.017 102.625  1.00 40.79           C  
ATOM   1342  CE1 PHE A 205      20.249  -0.325 101.416  1.00 44.78           C  
ATOM   1343  CE2 PHE A 205      21.504   0.198 103.372  1.00 41.79           C  
ATOM   1344  CZ  PHE A 205      20.461  -0.473 102.768  1.00 41.39           C  
ATOM   1345  N   ASN A 206      23.119   1.077  97.573  1.00 40.98           N  
ATOM   1346  CA  ASN A 206      22.525   0.231  96.515  1.00 41.87           C  
ATOM   1347  C   ASN A 206      23.629  -0.466  95.718  1.00 40.82           C  
ATOM   1348  O   ASN A 206      23.610  -1.694  95.580  1.00 43.39           O  
ATOM   1349  CB  ASN A 206      21.598   1.038  95.603  1.00 44.61           C  
ATOM   1350  CG  ASN A 206      20.741   0.155  94.723  1.00 46.77           C  
ATOM   1351  OD1 ASN A 206      19.690  -0.326  95.154  1.00 46.26           O  
ATOM   1352  ND2 ASN A 206      21.191  -0.071  93.498  1.00 43.87           N  
ATOM   1353  N   PHE A 207      24.568   0.292  95.174  1.00 37.73           N  
ATOM   1354  CA  PHE A 207      25.554  -0.289  94.234  1.00 41.14           C  
ATOM   1355  C   PHE A 207      26.577  -1.143  94.980  1.00 41.61           C  
ATOM   1356  O   PHE A 207      26.641  -2.359  94.771  1.00 40.25           O  
ATOM   1357  CB  PHE A 207      26.212   0.802  93.382  1.00 42.51           C  
ATOM   1358  CG  PHE A 207      27.222   0.329  92.363  1.00 44.09           C  
ATOM   1359  CD1 PHE A 207      27.034  -0.849  91.651  1.00 44.88           C  
ATOM   1360  CD2 PHE A 207      28.342   1.095  92.072  1.00 43.57           C  
ATOM   1361  CE1 PHE A 207      27.949  -1.253  90.689  1.00 41.85           C  
ATOM   1362  CE2 PHE A 207      29.253   0.689  91.109  1.00 41.62           C  
ATOM   1363  CZ  PHE A 207      29.054  -0.485  90.422  1.00 41.05           C  
ATOM   1364  N   PHE A 208      27.398  -0.523  95.820  1.00 43.94           N  
ATOM   1365  CA  PHE A 208      28.508  -1.256  96.465  1.00 41.36           C  
ATOM   1366  C   PHE A 208      27.955  -2.405  97.304  1.00 40.54           C  
ATOM   1367  O   PHE A 208      28.361  -3.543  97.131  1.00 35.47           O  
ATOM   1368  CB  PHE A 208      29.385  -0.288  97.270  1.00 41.83           C  
ATOM   1369  CG  PHE A 208      30.217   0.684  96.461  1.00 43.36           C  
ATOM   1370  CD1 PHE A 208      30.264   0.630  95.071  1.00 46.94           C  
ATOM   1371  CD2 PHE A 208      31.018   1.619  97.099  1.00 43.45           C  
ATOM   1372  CE1 PHE A 208      31.046   1.518  94.345  1.00 42.39           C  
ATOM   1373  CE2 PHE A 208      31.800   2.505  96.371  1.00 44.43           C  
ATOM   1374  CZ  PHE A 208      31.814   2.449  94.996  1.00 44.08           C  
ATOM   1375  N   ALA A 209      27.030  -2.120  98.215  1.00 38.66           N  
ATOM   1376  CA  ALA A 209      26.627  -3.111  99.231  1.00 40.26           C  
ATOM   1377  C   ALA A 209      25.629  -4.116  98.660  1.00 41.48           C  
ATOM   1378  O   ALA A 209      25.778  -5.338  98.886  1.00 45.14           O  
ATOM   1379  CB  ALA A 209      26.070  -2.399 100.437  1.00 40.15           C  
ATOM   1380  N   CYS A 210      24.617  -3.648  97.949  1.00 42.87           N  
ATOM   1381  CA  CYS A 210      23.475  -4.522  97.596  1.00 45.08           C  
ATOM   1382  C   CYS A 210      23.600  -5.121  96.205  1.00 43.85           C  
ATOM   1383  O   CYS A 210      22.883  -6.074  95.907  1.00 45.59           O  
ATOM   1384  CB  CYS A 210      22.150  -3.788  97.771  1.00 44.43           C  
ATOM   1385  SG  CYS A 210      21.854  -3.324  99.496  1.00 49.30           S  
ATOM   1386  N   VAL A 211      24.467  -4.584  95.354  1.00 43.06           N  
ATOM   1387  CA  VAL A 211      24.594  -5.094  93.971  1.00 44.46           C  
ATOM   1388  C   VAL A 211      25.982  -5.700  93.790  1.00 43.49           C  
ATOM   1389  O   VAL A 211      26.106  -6.894  93.476  1.00 39.31           O  
ATOM   1390  CB  VAL A 211      24.317  -3.999  92.918  1.00 44.49           C  
ATOM   1391  CG1 VAL A 211      24.670  -4.467  91.509  1.00 44.06           C  
ATOM   1392  CG2 VAL A 211      22.870  -3.516  92.966  1.00 47.06           C  
ATOM   1393  N   LEU A 212      27.018  -4.896  93.988  1.00 40.73           N  
ATOM   1394  CA  LEU A 212      28.391  -5.331  93.673  1.00 45.88           C  
ATOM   1395  C   LEU A 212      28.794  -6.506  94.559  1.00 43.40           C  
ATOM   1396  O   LEU A 212      29.340  -7.486  94.068  1.00 47.45           O  
ATOM   1397  CB  LEU A 212      29.342  -4.148  93.880  1.00 45.40           C  
ATOM   1398  CG  LEU A 212      30.553  -4.114  92.961  1.00 49.74           C  
ATOM   1399  CD1 LEU A 212      30.139  -4.308  91.512  1.00 49.96           C  
ATOM   1400  CD2 LEU A 212      31.318  -2.808  93.131  1.00 53.50           C  
ATOM   1401  N   VAL A 213      28.542  -6.417  95.850  1.00 43.99           N  
ATOM   1402  CA  VAL A 213      28.960  -7.488  96.784  1.00 43.23           C  
ATOM   1403  C   VAL A 213      28.269  -8.799  96.421  1.00 44.52           C  
ATOM   1404  O   VAL A 213      28.936  -9.835  96.353  1.00 46.94           O  
ATOM   1405  CB  VAL A 213      28.739  -7.087  98.255  1.00 44.46           C  
ATOM   1406  CG1 VAL A 213      28.660  -8.295  99.181  1.00 44.43           C  
ATOM   1407  CG2 VAL A 213      29.821  -6.126  98.717  1.00 44.62           C  
ATOM   1408  N   PRO A 214      26.937  -8.847  96.209  1.00 45.86           N  
ATOM   1409  CA  PRO A 214      26.325 -10.101  95.757  1.00 43.21           C  
ATOM   1410  C   PRO A 214      26.858 -10.602  94.410  1.00 40.57           C  
ATOM   1411  O   PRO A 214      27.039 -11.798  94.227  1.00 41.81           O  
ATOM   1412  CB  PRO A 214      24.832  -9.740  95.655  1.00 44.24           C  
ATOM   1413  CG  PRO A 214      24.657  -8.638  96.680  1.00 42.58           C  
ATOM   1414  CD  PRO A 214      25.937  -7.832  96.587  1.00 43.45           C  
ATOM   1415  N   LEU A 215      27.119  -9.705  93.475  1.00 38.51           N  
ATOM   1416  CA  LEU A 215      27.704 -10.150  92.191  1.00 40.76           C  
ATOM   1417  C   LEU A 215      29.068 -10.814  92.409  1.00 40.44           C  
ATOM   1418  O   LEU A 215      29.307 -11.876  91.875  1.00 38.92           O  
ATOM   1419  CB  LEU A 215      27.745  -8.989  91.198  1.00 42.46           C  
ATOM   1420  CG  LEU A 215      26.371  -8.597  90.639  1.00 44.49           C  
ATOM   1421  CD1 LEU A 215      26.441  -7.312  89.828  1.00 47.20           C  
ATOM   1422  CD2 LEU A 215      25.778  -9.717  89.799  1.00 43.51           C  
ATOM   1423  N   LEU A 216      29.922 -10.238  93.224  1.00 41.78           N  
ATOM   1424  CA  LEU A 216      31.222 -10.865  93.529  1.00 42.81           C  
ATOM   1425  C   LEU A 216      31.007 -12.200  94.248  1.00 43.96           C  
ATOM   1426  O   LEU A 216      31.723 -13.163  93.967  1.00 46.00           O  
ATOM   1427  CB  LEU A 216      32.053  -9.890  94.370  1.00 44.32           C  
ATOM   1428  CG  LEU A 216      32.342  -8.545  93.698  1.00 45.92           C  
ATOM   1429  CD1 LEU A 216      32.989  -7.569  94.669  1.00 45.33           C  
ATOM   1430  CD2 LEU A 216      33.209  -8.723  92.458  1.00 47.08           C  
ATOM   1431  N   LEU A 217      30.026 -12.272  95.133  1.00 44.01           N  
ATOM   1432  CA  LEU A 217      29.703 -13.541  95.797  1.00 42.77           C  
ATOM   1433  C   LEU A 217      29.367 -14.613  94.763  1.00 44.22           C  
ATOM   1434  O   LEU A 217      29.859 -15.753  94.862  1.00 45.10           O  
ATOM   1435  CB  LEU A 217      28.564 -13.333  96.803  1.00 47.67           C  
ATOM   1436  CG  LEU A 217      28.977 -12.745  98.154  1.00 51.60           C  
ATOM   1437  CD1 LEU A 217      27.758 -12.378  98.979  1.00 54.08           C  
ATOM   1438  CD2 LEU A 217      29.863 -13.712  98.933  1.00 54.96           C  
ATOM   1439  N   MET A 218      28.536 -14.268  93.793  1.00 46.97           N  
ATOM   1440  CA  MET A 218      28.101 -15.223  92.745  1.00 48.42           C  
ATOM   1441  C   MET A 218      29.296 -15.635  91.897  1.00 46.81           C  
ATOM   1442  O   MET A 218      29.389 -16.776  91.479  1.00 45.94           O  
ATOM   1443  CB  MET A 218      27.112 -14.571  91.773  1.00 51.37           C  
ATOM   1444  CG  MET A 218      25.738 -14.281  92.322  1.00 55.46           C  
ATOM   1445  SD  MET A 218      24.759 -13.366  91.081  1.00 55.79           S  
ATOM   1446  CE  MET A 218      23.792 -12.293  92.142  1.00 55.01           C  
ATOM   1447  N   LEU A 219      30.160 -14.699  91.576  1.00 43.64           N  
ATOM   1448  CA  LEU A 219      31.422 -15.018  90.893  1.00 47.36           C  
ATOM   1449  C   LEU A 219      32.173 -16.090  91.677  1.00 49.10           C  
ATOM   1450  O   LEU A 219      32.629 -17.076  91.087  1.00 47.92           O  
ATOM   1451  CB  LEU A 219      32.246 -13.734  90.761  1.00 48.69           C  
ATOM   1452  CG  LEU A 219      33.586 -13.870  90.040  1.00 51.27           C  
ATOM   1453  CD1 LEU A 219      33.376 -14.254  88.584  1.00 57.14           C  
ATOM   1454  CD2 LEU A 219      34.389 -12.583  90.138  1.00 47.55           C  
ATOM   1455  N   GLY A 220      32.264 -15.924  92.992  1.00 51.12           N  
ATOM   1456  CA  GLY A 220      32.963 -16.900  93.829  1.00 50.28           C  
ATOM   1457  C   GLY A 220      32.288 -18.257  93.806  1.00 50.76           C  
ATOM   1458  O   GLY A 220      32.970 -19.302  93.716  1.00 58.19           O  
ATOM   1459  N   VAL A 221      30.968 -18.260  93.907  1.00 49.25           N  
ATOM   1460  CA  VAL A 221      30.196 -19.529  93.917  1.00 48.03           C  
ATOM   1461  C   VAL A 221      30.397 -20.254  92.591  1.00 49.15           C  
ATOM   1462  O   VAL A 221      30.660 -21.461  92.574  1.00 49.81           O  
ATOM   1463  CB  VAL A 221      28.701 -19.268  94.181  1.00 47.76           C  
ATOM   1464  CG1 VAL A 221      27.837 -20.471  93.824  1.00 51.27           C  
ATOM   1465  CG2 VAL A 221      28.451 -18.834  95.617  1.00 47.06           C  
ATOM   1466  N   TYR A 222      30.263 -19.545  91.483  1.00 46.29           N  
ATOM   1467  CA  TYR A 222      30.416 -20.159  90.142  1.00 47.36           C  
ATOM   1468  C   TYR A 222      31.837 -20.662  89.960  1.00 51.06           C  
ATOM   1469  O   TYR A 222      32.030 -21.737  89.406  1.00 47.54           O  
ATOM   1470  CB  TYR A 222      30.059 -19.163  89.027  1.00 45.00           C  
ATOM   1471  CG  TYR A 222      28.580 -19.079  88.744  1.00 48.02           C  
ATOM   1472  CD1 TYR A 222      27.865 -20.211  88.377  1.00 45.44           C  
ATOM   1473  CD2 TYR A 222      27.881 -17.890  88.899  1.00 49.71           C  
ATOM   1474  CE1 TYR A 222      26.499 -20.163  88.161  1.00 48.74           C  
ATOM   1475  CE2 TYR A 222      26.511 -17.824  88.686  1.00 50.78           C  
ATOM   1476  CZ  TYR A 222      25.816 -18.968  88.326  1.00 54.46           C  
ATOM   1477  OH  TYR A 222      24.467 -18.917  88.114  1.00 56.15           O  
ATOM   1478  N   LEU A 223      32.825 -19.909  90.414  1.00 54.41           N  
ATOM   1479  CA  LEU A 223      34.216 -20.395  90.395  1.00 57.43           C  
ATOM   1480  C   LEU A 223      34.292 -21.736  91.119  1.00 59.87           C  
ATOM   1481  O   LEU A 223      34.910 -22.698  90.589  1.00 57.99           O  
ATOM   1482  CB  LEU A 223      35.136 -19.383  91.086  1.00 58.95           C  
ATOM   1483  CG  LEU A 223      35.574 -18.188  90.241  1.00 63.88           C  
ATOM   1484  CD1 LEU A 223      36.629 -17.374  90.983  1.00 63.44           C  
ATOM   1485  CD2 LEU A 223      36.090 -18.631  88.876  1.00 62.65           C  
ATOM   1486  N   ARG A 224      33.694 -21.803  92.308  1.00 57.26           N  
ATOM   1487  CA  ARG A 224      33.740 -23.040  93.109  1.00 56.68           C  
ATOM   1488  C   ARG A 224      32.967 -24.159  92.405  1.00 55.61           C  
ATOM   1489  O   ARG A 224      33.298 -25.341  92.588  1.00 57.98           O  
ATOM   1490  CB  ARG A 224      33.230 -22.773  94.525  1.00 61.87           C  
ATOM   1491  CG  ARG A 224      34.217 -21.985  95.377  1.00 71.12           C  
ATOM   1492  CD  ARG A 224      33.691 -21.649  96.760  1.00 77.48           C  
ATOM   1493  NE  ARG A 224      33.434 -22.841  97.559  1.00 88.91           N  
ATOM   1494  CZ  ARG A 224      32.971 -22.836  98.807  1.00 94.94           C  
ATOM   1495  NH1 ARG A 224      32.710 -21.689  99.415  1.00 95.45           N  
ATOM   1496  NH2 ARG A 224      32.773 -23.979  99.444  1.00 92.36           N  
ATOM   1497  N   ILE A 225      31.953 -23.812  91.636  1.00 49.02           N  
ATOM   1498  CA  ILE A 225      31.187 -24.829  90.878  1.00 50.16           C  
ATOM   1499  C   ILE A 225      32.079 -25.452  89.815  1.00 50.47           C  
ATOM   1500  O   ILE A 225      32.176 -26.675  89.741  1.00 48.47           O  
ATOM   1501  CB  ILE A 225      29.901 -24.220  90.278  1.00 47.45           C  
ATOM   1502  CG1 ILE A 225      28.843 -23.961  91.355  1.00 50.56           C  
ATOM   1503  CG2 ILE A 225      29.348 -25.096  89.169  1.00 47.45           C  
ATOM   1504  CD1 ILE A 225      27.671 -23.103  90.884  1.00 48.54           C  
ATOM   1505  N   PHE A 226      32.723 -24.640  89.006  1.00 50.42           N  
ATOM   1506  CA  PHE A 226      33.567 -25.150  87.904  1.00 53.20           C  
ATOM   1507  C   PHE A 226      34.757 -25.913  88.468  1.00 53.19           C  
ATOM   1508  O   PHE A 226      35.154 -26.940  87.890  1.00 56.34           O  
ATOM   1509  CB  PHE A 226      33.952 -24.013  86.951  1.00 52.79           C  
ATOM   1510  CG  PHE A 226      32.775 -23.404  86.222  1.00 52.61           C  
ATOM   1511  CD1 PHE A 226      31.911 -24.198  85.480  1.00 52.94           C  
ATOM   1512  CD2 PHE A 226      32.503 -22.046  86.312  1.00 53.19           C  
ATOM   1513  CE1 PHE A 226      30.814 -23.646  84.838  1.00 55.00           C  
ATOM   1514  CE2 PHE A 226      31.409 -21.495  85.665  1.00 52.95           C  
ATOM   1515  CZ  PHE A 226      30.565 -22.295  84.930  1.00 56.54           C  
ATOM   1516  N   ALA A 227      35.302 -25.456  89.593  1.00 53.45           N  
ATOM   1517  CA  ALA A 227      36.431 -26.170  90.226  1.00 54.84           C  
ATOM   1518  C   ALA A 227      35.958 -27.533  90.731  1.00 56.15           C  
ATOM   1519  O   ALA A 227      36.664 -28.544  90.553  1.00 59.18           O  
ATOM   1520  CB  ALA A 227      37.019 -25.333  91.340  1.00 51.79           C  
ATOM   1521  N   ALA A 228      34.808 -27.565  91.389  1.00 54.84           N  
ATOM   1522  CA  ALA A 228      34.249 -28.839  91.886  1.00 54.26           C  
ATOM   1523  C   ALA A 228      34.026 -29.810  90.731  1.00 57.82           C  
ATOM   1524  O   ALA A 228      34.379 -30.970  90.833  1.00 59.31           O  
ATOM   1525  CB  ALA A 228      32.977 -28.577  92.645  1.00 53.41           C  
ATOM   1526  N   ALA A 229      33.453 -29.335  89.639  1.00 60.78           N  
ATOM   1527  CA  ALA A 229      33.182 -30.194  88.472  1.00 62.00           C  
ATOM   1528  C   ALA A 229      34.487 -30.718  87.896  1.00 61.58           C  
ATOM   1529  O   ALA A 229      34.560 -31.902  87.526  1.00 60.44           O  
ATOM   1530  CB  ALA A 229      32.406 -29.421  87.433  1.00 60.98           C  
ATOM   1531  N   ARG A 230      35.502 -29.866  87.823  1.00 65.54           N  
ATOM   1532  CA  ARG A 230      36.807 -30.275  87.261  1.00 70.90           C  
ATOM   1533  C   ARG A 230      37.440 -31.343  88.149  1.00 68.62           C  
ATOM   1534  O   ARG A 230      37.971 -32.346  87.629  1.00 69.30           O  
ATOM   1535  CB  ARG A 230      37.729 -29.059  87.103  1.00 76.89           C  
ATOM   1536  CG  ARG A 230      38.867 -29.263  86.111  1.00 81.63           C  
ATOM   1537  CD  ARG A 230      39.803 -28.070  86.014  1.00 83.52           C  
ATOM   1538  NE  ARG A 230      40.446 -27.747  87.289  1.00 84.16           N  
ATOM   1539  CZ  ARG A 230      40.304 -26.602  87.965  1.00 84.32           C  
ATOM   1540  NH1 ARG A 230      39.539 -25.626  87.503  1.00 90.05           N  
ATOM   1541  NH2 ARG A 230      40.939 -26.434  89.111  1.00 84.77           N  
ATOM   1542  N   ARG A 231      37.400 -31.141  89.457  1.00 65.11           N  
ATOM   1543  CA  ARG A 231      38.018 -32.099  90.402  1.00 69.10           C  
ATOM   1544  C   ARG A 231      37.336 -33.460  90.301  1.00 67.77           C  
ATOM   1545  O   ARG A 231      38.016 -34.482  90.286  1.00 72.49           O  
ATOM   1546  CB  ARG A 231      37.930 -31.509  91.814  1.00 75.50           C  
ATOM   1547  CG  ARG A 231      38.751 -32.236  92.869  1.00 86.36           C  
ATOM   1548  CD  ARG A 231      40.254 -32.118  92.659  1.00 94.70           C  
ATOM   1549  NE  ARG A 231      40.992 -32.626  93.811  1.00 99.03           N  
ATOM   1550  CZ  ARG A 231      41.143 -33.915  94.113  1.00103.60           C  
ATOM   1551  NH1 ARG A 231      40.617 -34.852  93.342  1.00104.16           N  
ATOM   1552  NH2 ARG A 231      41.821 -34.264  95.193  1.00107.55           N  
ATOM   1553  N   GLN A 232      36.019 -33.487  90.248  1.00 65.72           N  
ATOM   1554  CA  GLN A 232      35.278 -34.763  90.201  1.00 65.97           C  
ATOM   1555  C   GLN A 232      35.510 -35.463  88.870  1.00 66.84           C  
ATOM   1556  O   GLN A 232      35.544 -36.703  88.845  1.00 65.49           O  
ATOM   1557  CB  GLN A 232      33.789 -34.498  90.433  1.00 63.71           C  
ATOM   1558  CG  GLN A 232      33.481 -33.994  91.837  1.00 63.08           C  
ATOM   1559  CD  GLN A 232      32.039 -33.584  91.997  1.00 64.89           C  
ATOM   1560  OE1 GLN A 232      31.159 -34.061  91.289  1.00 70.31           O  
ATOM   1561  NE2 GLN A 232      31.788 -32.683  92.932  1.00 64.42           N  
ATOM   1562  N   LEU A 233      35.651 -34.706  87.785  1.00 65.96           N  
ATOM   1563  CA  LEU A 233      35.988 -35.316  86.485  1.00 66.29           C  
ATOM   1564  C   LEU A 233      37.371 -35.955  86.565  1.00 68.64           C  
ATOM   1565  O   LEU A 233      37.558 -37.099  86.093  1.00 64.31           O  
ATOM   1566  CB  LEU A 233      35.939 -34.269  85.365  1.00 66.63           C  
ATOM   1567  CG  LEU A 233      34.547 -33.859  84.875  1.00 71.25           C  
ATOM   1568  CD1 LEU A 233      34.613 -32.596  84.020  1.00 71.68           C  
ATOM   1569  CD2 LEU A 233      33.877 -34.982  84.096  1.00 71.94           C  
ATOM   1570  N   ALA A 234      38.326 -35.242  87.153  1.00 72.82           N  
ATOM   1571  CA  ALA A 234      39.693 -35.774  87.322  1.00 73.01           C  
ATOM   1572  C   ALA A 234      39.661 -37.041  88.169  1.00 74.87           C  
ATOM   1573  O   ALA A 234      40.280 -38.046  87.810  1.00 81.13           O  
ATOM   1574  CB  ALA A 234      40.581 -34.718  87.941  1.00 70.34           C  
ATOM   1575  N   ASP A 235      38.962 -36.999  89.287  1.00 77.77           N  
ATOM   1576  CA  ASP A 235      38.854 -38.175  90.181  1.00 83.83           C  
ATOM   1577  C   ASP A 235      38.308 -39.368  89.410  1.00 84.32           C  
ATOM   1578  O   ASP A 235      38.832 -40.467  89.557  1.00 90.44           O  
ATOM   1579  CB  ASP A 235      37.941 -37.887  91.376  1.00 89.19           C  
ATOM   1580  CG  ASP A 235      38.672 -37.354  92.594  1.00 95.48           C  
ATOM   1581  OD1 ASP A 235      39.670 -36.630  92.404  1.00100.16           O  
ATOM   1582  OD2 ASP A 235      38.243 -37.677  93.721  1.00 99.75           O  
ATOM   1583  N   LEU A 236      37.278 -39.167  88.606  1.00 79.39           N  
ATOM   1584  CA  LEU A 236      36.725 -40.271  87.807  1.00 81.96           C  
ATOM   1585  C   LEU A 236      37.804 -40.844  86.898  1.00 84.71           C  
ATOM   1586  O   LEU A 236      38.007 -42.087  86.882  1.00 85.50           O  
ATOM   1587  CB  LEU A 236      35.523 -39.788  86.988  1.00 81.89           C  
ATOM   1588  CG  LEU A 236      34.190 -39.740  87.735  1.00 84.43           C  
ATOM   1589  CD1 LEU A 236      33.121 -39.089  86.874  1.00 88.95           C  
ATOM   1590  CD2 LEU A 236      33.746 -41.130  88.176  1.00 84.64           C  
ATOM   1591  N   GLU A 237      38.483 -39.977  86.152  1.00 86.25           N  
ATOM   1592  CA  GLU A 237      39.527 -40.440  85.214  1.00 87.37           C  
ATOM   1593  C   GLU A 237      40.643 -41.156  85.982  1.00 87.22           C  
ATOM   1594  O   GLU A 237      41.194 -42.148  85.496  1.00 82.58           O  
ATOM   1595  CB  GLU A 237      40.064 -39.279  84.375  1.00 89.68           C  
ATOM   1596  CG  GLU A 237      41.038 -39.709  83.283  1.00 95.08           C  
ATOM   1597  CD  GLU A 237      40.590 -40.877  82.412  1.00 97.15           C  
ATOM   1598  OE1 GLU A 237      39.655 -40.699  81.601  1.00 93.79           O  
ATOM   1599  OE2 GLU A 237      41.181 -41.964  82.545  1.00 99.57           O  
ATOM   1600  N   ASP A 238      40.990 -40.650  87.151  1.00 85.35           N  
ATOM   1601  CA  ASP A 238      42.063 -41.270  87.958  1.00 85.45           C  
ATOM   1602  C   ASP A 238      41.684 -42.695  88.342  1.00 88.84           C  
ATOM   1603  O   ASP A 238      42.497 -43.600  88.143  1.00 97.19           O  
ATOM   1604  CB  ASP A 238      42.398 -40.422  89.188  1.00 86.22           C  
ATOM   1605  CG  ASP A 238      43.254 -39.207  88.865  1.00 94.17           C  
ATOM   1606  OD1 ASP A 238      43.844 -39.182  87.765  1.00 92.87           O  
ATOM   1607  OD2 ASP A 238      43.319 -38.289  89.713  1.00 98.48           O  
ATOM   1608  N   ASN A 239      40.491 -42.880  88.858  1.00 86.78           N  
ATOM   1609  CA  ASN A 239      40.033 -44.230  89.263  1.00 85.79           C  
ATOM   1610  C   ASN A 239      40.068 -45.172  88.073  1.00 81.63           C  
ATOM   1611  O   ASN A 239      40.250 -46.346  88.311  1.00 77.30           O  
ATOM   1612  CB  ASN A 239      38.628 -44.183  89.879  1.00 82.63           C  
ATOM   1613  CG  ASN A 239      38.624 -43.677  91.306  1.00 83.84           C  
ATOM   1614  OD1 ASN A 239      39.679 -43.476  91.903  1.00 90.12           O  
ATOM   1615  ND2 ASN A 239      37.442 -43.488  91.869  1.00 84.45           N  
ATOM   1616  N   TRP A 240      39.712 -44.687  86.892  1.00 78.86           N  
ATOM   1617  CA  TRP A 240      39.647 -45.553  85.694  1.00 77.28           C  
ATOM   1618  C   TRP A 240      41.052 -45.959  85.257  1.00 84.30           C  
ATOM   1619  O   TRP A 240      41.283 -47.126  84.956  1.00 89.43           O  
ATOM   1620  CB  TRP A 240      38.888 -44.830  84.576  1.00 71.65           C  
ATOM   1621  CG  TRP A 240      38.927 -45.477  83.224  1.00 71.32           C  
ATOM   1622  CD1 TRP A 240      39.653 -45.065  82.144  1.00 71.54           C  
ATOM   1623  CD2 TRP A 240      38.130 -46.587  82.765  1.00 72.63           C  
ATOM   1624  NE1 TRP A 240      39.385 -45.854  81.058  1.00 73.66           N  
ATOM   1625  CE2 TRP A 240      38.457 -46.797  81.407  1.00 73.53           C  
ATOM   1626  CE3 TRP A 240      37.182 -47.427  83.364  1.00 73.24           C  
ATOM   1627  CZ2 TRP A 240      37.873 -47.811  80.649  1.00 75.01           C  
ATOM   1628  CZ3 TRP A 240      36.606 -48.429  82.613  1.00 72.22           C  
ATOM   1629  CH2 TRP A 240      36.947 -48.616  81.274  1.00 73.46           C  
ATOM   1630  N   GLU A 241      41.968 -45.003  85.194  1.00 87.97           N  
ATOM   1631  CA  GLU A 241      43.371 -45.294  84.837  1.00 89.78           C  
ATOM   1632  C   GLU A 241      43.996 -46.170  85.925  1.00 81.15           C  
ATOM   1633  O   GLU A 241      44.842 -47.037  85.612  1.00 75.87           O  
ATOM   1634  CB  GLU A 241      44.111 -43.961  84.669  1.00 96.14           C  
ATOM   1635  CG  GLU A 241      45.558 -44.091  84.226  1.00102.21           C  
ATOM   1636  CD  GLU A 241      46.263 -42.769  83.958  1.00101.81           C  
ATOM   1637  OE1 GLU A 241      45.593 -41.713  84.011  1.00 99.38           O  
ATOM   1638  OE2 GLU A 241      47.481 -42.796  83.701  1.00 97.22           O  
ATOM   1639  N   THR A 242      43.634 -45.925  87.176  1.00 76.97           N  
ATOM   1640  CA  THR A 242      44.235 -46.707  88.285  1.00 79.31           C  
ATOM   1641  C   THR A 242      43.790 -48.165  88.236  1.00 81.97           C  
ATOM   1642  O   THR A 242      44.555 -49.035  88.581  1.00 83.44           O  
ATOM   1643  CB  THR A 242      43.946 -46.070  89.655  1.00 78.69           C  
ATOM   1644  OG1 THR A 242      44.920 -46.540  90.587  1.00 83.12           O  
ATOM   1645  CG2 THR A 242      42.575 -46.395  90.204  1.00 84.74           C  
ATOM   1646  N   LEU A 243      42.573 -48.405  87.787  1.00 76.25           N  
ATOM   1647  CA  LEU A 243      42.023 -49.765  87.611  1.00 75.77           C  
ATOM   1648  C   LEU A 243      42.642 -50.414  86.380  1.00 78.21           C  
ATOM   1649  O   LEU A 243      42.809 -51.661  86.368  1.00 80.65           O  
ATOM   1650  CB  LEU A 243      40.504 -49.635  87.456  1.00 77.28           C  
ATOM   1651  CG  LEU A 243      39.742 -50.932  87.206  1.00 82.22           C  
ATOM   1652  CD1 LEU A 243      39.796 -51.828  88.432  1.00 89.30           C  
ATOM   1653  CD2 LEU A 243      38.300 -50.642  86.826  1.00 84.79           C  
ATOM   1654  N   ASN A 244      42.977 -49.618  85.368  1.00 72.98           N  
ATOM   1655  CA  ASN A 244      43.599 -50.176  84.148  1.00 74.83           C  
ATOM   1656  C   ASN A 244      45.100 -50.368  84.342  1.00 74.74           C  
ATOM   1657  O   ASN A 244      45.648 -51.384  83.914  1.00 71.17           O  
ATOM   1658  CB  ASN A 244      43.251 -49.336  82.915  1.00 76.01           C  
ATOM   1659  CG  ASN A 244      41.802 -49.489  82.495  1.00 75.96           C  
ATOM   1660  OD1 ASN A 244      41.140 -50.453  82.873  1.00 75.38           O  
ATOM   1661  ND2 ASN A 244      41.297 -48.543  81.720  1.00 79.23           N  
ATOM   1662  N   ASP A 245      45.766 -49.398  84.949  1.00 74.08           N  
ATOM   1663  CA  ASP A 245      47.219 -49.520  85.204  1.00 72.95           C  
ATOM   1664  C   ASP A 245      47.537 -50.751  86.035  1.00 69.93           C  
ATOM   1665  O   ASP A 245      48.404 -51.527  85.639  1.00 72.89           O  
ATOM   1666  CB  ASP A 245      47.786 -48.248  85.832  1.00 73.00           C  
ATOM   1667  CG  ASP A 245      47.886 -47.109  84.834  1.00 78.49           C  
ATOM   1668  OD1 ASP A 245      47.701 -47.372  83.623  1.00 81.03           O  
ATOM   1669  OD2 ASP A 245      48.121 -45.972  85.270  1.00 86.51           O  
ATOM   1670  N   ASN A 246      46.840 -50.952  87.131  1.00 69.88           N  
ATOM   1671  CA  ASN A 246      47.085 -52.068  88.062  1.00 69.78           C  
ATOM   1672  C   ASN A 246      46.771 -53.406  87.410  1.00 70.23           C  
ATOM   1673  O   ASN A 246      47.298 -54.434  87.864  1.00 67.60           O  
ATOM   1674  CB  ASN A 246      46.254 -51.914  89.339  1.00 71.00           C  
ATOM   1675  CG  ASN A 246      46.902 -51.019  90.372  1.00 71.77           C  
ATOM   1676  OD1 ASN A 246      46.255 -50.131  90.924  1.00 79.50           O  
ATOM   1677  ND2 ASN A 246      48.168 -51.262  90.662  1.00 70.11           N  
ATOM   1678  N   LEU A 247      45.895 -53.416  86.418  1.00 72.80           N  
ATOM   1679  CA  LEU A 247      45.627 -54.648  85.656  1.00 78.85           C  
ATOM   1680  C   LEU A 247      46.885 -55.077  84.908  1.00 84.98           C  
ATOM   1681  O   LEU A 247      47.333 -56.229  85.057  1.00 81.81           O  
ATOM   1682  CB  LEU A 247      44.461 -54.423  84.683  1.00 78.62           C  
ATOM   1683  CG  LEU A 247      43.078 -54.835  85.193  1.00 80.93           C  
ATOM   1684  CD1 LEU A 247      41.978 -54.218  84.345  1.00 79.74           C  
ATOM   1685  CD2 LEU A 247      42.930 -56.348  85.223  1.00 81.69           C  
ATOM   1686  N   LYS A 248      47.450 -54.167  84.126  1.00 90.62           N  
ATOM   1687  CA  LYS A 248      48.707 -54.437  83.391  1.00 86.92           C  
ATOM   1688  C   LYS A 248      49.790 -54.860  84.376  1.00 83.77           C  
ATOM   1689  O   LYS A 248      50.604 -55.748  84.055  1.00 91.55           O  
ATOM   1690  CB  LYS A 248      49.225 -53.181  82.680  1.00 86.99           C  
ATOM   1691  CG  LYS A 248      48.309 -52.554  81.638  1.00 94.18           C  
ATOM   1692  CD  LYS A 248      48.884 -51.266  81.058  1.00 96.84           C  
ATOM   1693  CE  LYS A 248      47.852 -50.389  80.380  1.00100.23           C  
ATOM   1694  NZ  LYS A 248      47.369 -50.985  79.112  1.00103.02           N  
ATOM   1695  N   VAL A 249      49.832 -54.220  85.534  1.00 72.52           N  
ATOM   1696  CA  VAL A 249      50.831 -54.559  86.569  1.00 72.36           C  
ATOM   1697  C   VAL A 249      50.681 -56.018  86.955  1.00 73.28           C  
ATOM   1698  O   VAL A 249      51.711 -56.740  87.059  1.00 70.59           O  
ATOM   1699  CB  VAL A 249      50.699 -53.630  87.794  1.00 71.57           C  
ATOM   1700  CG1 VAL A 249      51.386 -54.192  89.030  1.00 71.78           C  
ATOM   1701  CG2 VAL A 249      51.216 -52.234  87.490  1.00 74.92           C  
ATOM   1702  N   ILE A 250      49.448 -56.455  87.170  1.00 78.83           N  
ATOM   1703  CA  ILE A 250      49.179 -57.855  87.592  1.00 74.05           C  
ATOM   1704  C   ILE A 250      49.543 -58.798  86.460  1.00 76.05           C  
ATOM   1705  O   ILE A 250      50.083 -59.904  86.750  1.00 81.07           O  
ATOM   1706  CB  ILE A 250      47.710 -58.021  88.041  1.00 72.67           C  
ATOM   1707  CG1 ILE A 250      47.451 -57.315  89.373  1.00 71.49           C  
ATOM   1708  CG2 ILE A 250      47.313 -59.493  88.103  1.00 70.14           C  
ATOM   1709  CD1 ILE A 250      45.988 -57.133  89.698  1.00 73.44           C  
ATOM   1710  N   GLU A 251      49.325 -58.385  85.219  1.00 76.96           N  
ATOM   1711  CA  GLU A 251      49.548 -59.268  84.052  1.00 78.43           C  
ATOM   1712  C   GLU A 251      51.034 -59.502  83.815  1.00 82.79           C  
ATOM   1713  O   GLU A 251      51.401 -60.523  83.204  1.00 87.80           O  
ATOM   1714  CB  GLU A 251      48.946 -58.661  82.782  1.00 75.85           C  
ATOM   1715  CG  GLU A 251      47.460 -58.910  82.631  1.00 79.01           C  
ATOM   1716  CD  GLU A 251      46.757 -57.987  81.650  1.00 84.91           C  
ATOM   1717  OE1 GLU A 251      47.457 -57.320  80.858  1.00 89.38           O  
ATOM   1718  OE2 GLU A 251      45.507 -57.933  81.682  1.00 88.20           O  
ATOM   1719  N   LYS A 252      51.894 -58.619  84.321  1.00 84.00           N  
ATOM   1720  CA  LYS A 252      53.351 -58.712  84.102  1.00 87.51           C  
ATOM   1721  C   LYS A 252      54.118 -58.985  85.385  1.00 88.27           C  
ATOM   1722  O   LYS A 252      55.279 -59.165  85.295  1.00 91.60           O  
ATOM   1723  CB  LYS A 252      53.857 -57.403  83.487  1.00 92.40           C  
ATOM   1724  CG  LYS A 252      53.422 -57.150  82.050  1.00 93.73           C  
ATOM   1725  CD  LYS A 252      53.845 -55.795  81.537  1.00 98.99           C  
ATOM   1726  CE  LYS A 252      53.524 -55.585  80.073  1.00100.21           C  
ATOM   1727  NZ  LYS A 252      53.769 -54.182  79.662  1.00102.22           N  
ATOM   1728  N   ALA A 253      53.415 -59.143  86.488  1.00 92.66           N  
ATOM   1729  CA  ALA A 253      54.046 -59.416  87.799  1.00 96.08           C  
ATOM   1730  C   ALA A 253      54.387 -60.914  87.863  1.00103.51           C  
ATOM   1731  O   ALA A 253      53.543 -61.734  87.449  1.00106.28           O  
ATOM   1732  CB  ALA A 253      53.130 -58.998  88.926  1.00 88.73           C  
ATOM   1733  N   ASP A 254      55.585 -61.264  88.336  1.00107.08           N  
ATOM   1734  CA  ASP A 254      56.044 -62.677  88.435  1.00108.05           C  
ATOM   1735  C   ASP A 254      56.053 -63.107  89.912  1.00105.51           C  
ATOM   1736  O   ASP A 254      56.649 -64.160  90.203  1.00102.28           O  
ATOM   1737  CB  ASP A 254      57.410 -62.849  87.758  1.00111.74           C  
ATOM   1738  CG  ASP A 254      57.591 -64.171  87.025  1.00112.93           C  
ATOM   1739  OD1 ASP A 254      56.569 -64.794  86.670  1.00108.91           O  
ATOM   1740  OD2 ASP A 254      58.757 -64.563  86.805  1.00111.83           O  
ATOM   1741  N   ASN A 255      55.405 -62.336  90.796  1.00103.39           N  
ATOM   1742  CA  ASN A 255      55.417 -62.533  92.273  1.00 98.12           C  
ATOM   1743  C   ASN A 255      53.984 -62.417  92.809  1.00 93.21           C  
ATOM   1744  O   ASN A 255      53.233 -61.600  92.276  1.00 91.92           O  
ATOM   1745  CB  ASN A 255      56.346 -61.520  92.952  1.00 94.66           C  
ATOM   1746  CG  ASN A 255      56.432 -61.704  94.451  1.00 96.36           C  
ATOM   1747  OD1 ASN A 255      56.160 -62.785  94.968  1.00 99.28           O  
ATOM   1748  ND2 ASN A 255      56.811 -60.653  95.158  1.00103.73           N  
ATOM   1749  N   ALA A 256      53.638 -63.180  93.849  1.00 88.92           N  
ATOM   1750  CA  ALA A 256      52.292 -63.203  94.474  1.00 83.77           C  
ATOM   1751  C   ALA A 256      52.056 -61.923  95.299  1.00 85.73           C  
ATOM   1752  O   ALA A 256      50.891 -61.506  95.413  1.00 89.85           O  
ATOM   1753  CB  ALA A 256      52.134 -64.450  95.310  1.00 80.41           C  
ATOM   1754  N   ALA A 257      53.111 -61.320  95.856  1.00 84.89           N  
ATOM   1755  CA  ALA A 257      53.045 -60.073  96.666  1.00 86.78           C  
ATOM   1756  C   ALA A 257      52.796 -58.869  95.758  1.00 86.39           C  
ATOM   1757  O   ALA A 257      52.037 -57.954  96.117  1.00 96.25           O  
ATOM   1758  CB  ALA A 257      54.318 -59.917  97.466  1.00 89.75           C  
ATOM   1759  N   GLN A 258      53.356 -58.934  94.557  1.00 79.04           N  
ATOM   1760  CA  GLN A 258      53.085 -57.895  93.527  1.00 79.74           C  
ATOM   1761  C   GLN A 258      51.609 -57.921  93.158  1.00 83.59           C  
ATOM   1762  O   GLN A 258      50.971 -56.891  93.223  1.00 85.26           O  
ATOM   1763  CB  GLN A 258      53.990 -58.097  92.315  1.00 77.40           C  
ATOM   1764  CG  GLN A 258      55.449 -57.801  92.616  1.00 79.98           C  
ATOM   1765  CD  GLN A 258      56.344 -58.032  91.427  1.00 83.77           C  
ATOM   1766  OE1 GLN A 258      55.968 -58.680  90.453  1.00 90.04           O  
ATOM   1767  NE2 GLN A 258      57.551 -57.500  91.503  1.00 89.03           N  
ATOM   1768  N   VAL A 259      51.062 -59.094  92.917  1.00 86.98           N  
ATOM   1769  CA  VAL A 259      49.628 -59.227  92.572  1.00 87.54           C  
ATOM   1770  C   VAL A 259      48.782 -58.750  93.745  1.00 89.37           C  
ATOM   1771  O   VAL A 259      47.747 -58.093  93.539  1.00 96.58           O  
ATOM   1772  CB  VAL A 259      49.283 -60.672  92.163  1.00 84.07           C  
ATOM   1773  CG1 VAL A 259      47.780 -60.888  92.038  1.00 84.92           C  
ATOM   1774  CG2 VAL A 259      49.988 -61.062  90.872  1.00 82.39           C  
ATOM   1775  N   LYS A 260      49.182 -59.080  94.955  1.00 88.65           N  
ATOM   1776  CA  LYS A 260      48.395 -58.689  96.146  1.00 87.18           C  
ATOM   1777  C   LYS A 260      48.424 -57.174  96.310  1.00 87.97           C  
ATOM   1778  O   LYS A 260      47.365 -56.561  96.544  1.00 89.15           O  
ATOM   1779  CB  LYS A 260      48.977 -59.388  97.382  1.00 84.73           C  
ATOM   1780  CG  LYS A 260      48.316 -59.063  98.715  1.00 82.02           C  
ATOM   1781  CD  LYS A 260      49.105 -59.589  99.892  1.00 84.25           C  
ATOM   1782  CE  LYS A 260      48.332 -59.569 101.193  1.00 87.54           C  
ATOM   1783  NZ  LYS A 260      48.552 -58.308 101.935  1.00 92.12           N  
ATOM   1784  N   ASP A 261      49.610 -56.576  96.211  1.00 89.12           N  
ATOM   1785  CA  ASP A 261      49.745 -55.112  96.366  1.00 89.34           C  
ATOM   1786  C   ASP A 261      48.799 -54.397  95.394  1.00 79.83           C  
ATOM   1787  O   ASP A 261      48.051 -53.484  95.813  1.00 83.45           O  
ATOM   1788  CB  ASP A 261      51.200 -54.669  96.160  1.00 95.24           C  
ATOM   1789  CG  ASP A 261      51.488 -53.239  96.596  1.00101.97           C  
ATOM   1790  OD1 ASP A 261      50.908 -52.309  95.995  1.00104.35           O  
ATOM   1791  OD2 ASP A 261      52.298 -53.065  97.531  1.00110.86           O  
ATOM   1792  N   ALA A 262      48.831 -54.798  94.126  1.00 71.02           N  
ATOM   1793  CA  ALA A 262      48.031 -54.151  93.078  1.00 70.62           C  
ATOM   1794  C   ALA A 262      46.552 -54.356  93.337  1.00 69.94           C  
ATOM   1795  O   ALA A 262      45.833 -53.381  93.094  1.00 67.27           O  
ATOM   1796  CB  ALA A 262      48.419 -54.690  91.723  1.00 64.93           C  
ATOM   1797  N   LEU A 263      46.147 -55.585  93.615  1.00 68.69           N  
ATOM   1798  CA  LEU A 263      44.716 -55.903  93.826  1.00 73.10           C  
ATOM   1799  C   LEU A 263      44.149 -55.147  95.016  1.00 71.81           C  
ATOM   1800  O   LEU A 263      42.989 -54.714  94.927  1.00 66.06           O  
ATOM   1801  CB  LEU A 263      44.555 -57.415  94.025  1.00 73.12           C  
ATOM   1802  CG  LEU A 263      44.588 -58.260  92.753  1.00 70.30           C  
ATOM   1803  CD1 LEU A 263      44.543 -59.745  93.094  1.00 71.46           C  
ATOM   1804  CD2 LEU A 263      43.446 -57.885  91.820  1.00 67.74           C  
ATOM   1805  N   THR A 264      44.959 -54.925  96.063  1.00 75.99           N  
ATOM   1806  CA  THR A 264      44.497 -54.172  97.248  1.00 78.59           C  
ATOM   1807  C   THR A 264      44.242 -52.710  96.861  1.00 78.57           C  
ATOM   1808  O   THR A 264      43.359 -52.048  97.452  1.00 75.38           O  
ATOM   1809  CB  THR A 264      45.545 -54.207  98.370  1.00 81.16           C  
ATOM   1810  OG1 THR A 264      45.774 -55.564  98.749  1.00 81.15           O  
ATOM   1811  CG2 THR A 264      45.137 -53.411  99.590  1.00 84.38           C  
ATOM   1812  N   LYS A 265      45.033 -52.189  95.942  1.00 77.98           N  
ATOM   1813  CA  LYS A 265      44.878 -50.806  95.458  1.00 81.99           C  
ATOM   1814  C   LYS A 265      43.727 -50.687  94.472  1.00 83.60           C  
ATOM   1815  O   LYS A 265      43.187 -49.575  94.335  1.00 94.91           O  
ATOM   1816  CB  LYS A 265      46.197 -50.301  94.864  1.00 84.97           C  
ATOM   1817  CG  LYS A 265      47.195 -49.815  95.906  1.00 90.99           C  
ATOM   1818  CD  LYS A 265      48.601 -49.641  95.388  1.00 95.74           C  
ATOM   1819  CE  LYS A 265      49.598 -49.367  96.495  1.00 98.45           C  
ATOM   1820  NZ  LYS A 265      50.992 -49.592  96.047  1.00100.03           N  
ATOM   1821  N   MET A 266      43.333 -51.775  93.843  1.00 83.29           N  
ATOM   1822  CA  MET A 266      42.127 -51.766  92.981  1.00 82.71           C  
ATOM   1823  C   MET A 266      40.861 -51.831  93.808  1.00 80.12           C  
ATOM   1824  O   MET A 266      39.863 -51.249  93.408  1.00 79.13           O  
ATOM   1825  CB  MET A 266      42.139 -52.952  92.017  1.00 84.43           C  
ATOM   1826  CG  MET A 266      43.129 -52.797  90.895  1.00 85.24           C  
ATOM   1827  SD  MET A 266      43.440 -54.368  90.071  1.00 90.19           S  
ATOM   1828  CE  MET A 266      42.104 -54.392  88.878  1.00 84.26           C  
ATOM   1829  N   ARG A 267      40.898 -52.546  94.930  1.00 74.61           N  
ATOM   1830  CA  ARG A 267      39.704 -52.706  95.786  1.00 77.04           C  
ATOM   1831  C   ARG A 267      39.304 -51.353  96.378  1.00 77.83           C  
ATOM   1832  O   ARG A 267      38.112 -50.995  96.366  1.00 91.52           O  
ATOM   1833  CB  ARG A 267      40.009 -53.733  96.881  1.00 76.03           C  
ATOM   1834  CG  ARG A 267      38.777 -54.309  97.558  1.00 75.13           C  
ATOM   1835  CD  ARG A 267      39.132 -55.341  98.603  1.00 77.73           C  
ATOM   1836  NE  ARG A 267      37.938 -55.998  99.112  1.00 83.20           N  
ATOM   1837  CZ  ARG A 267      37.131 -55.505 100.050  1.00 86.80           C  
ATOM   1838  NH1 ARG A 267      37.386 -54.333 100.610  1.00 86.33           N  
ATOM   1839  NH2 ARG A 267      36.065 -56.192 100.424  1.00 88.88           N  
ATOM   1840  N   ALA A 268      40.276 -50.644  96.926  1.00 79.94           N  
ATOM   1841  CA  ALA A 268      40.101 -49.264  97.420  1.00 77.28           C  
ATOM   1842  C   ALA A 268      39.516 -48.355  96.344  1.00 75.93           C  
ATOM   1843  O   ALA A 268      38.531 -47.640  96.628  1.00 76.03           O  
ATOM   1844  CB  ALA A 268      41.422 -48.728  97.925  1.00 75.26           C  
ATOM   1845  N   ALA A 269      40.162 -48.354  95.185  1.00 78.29           N  
ATOM   1846  CA  ALA A 269      39.783 -47.546  94.014  1.00 77.61           C  
ATOM   1847  C   ALA A 269      38.400 -47.918  93.539  1.00 85.33           C  
ATOM   1848  O   ALA A 269      37.656 -47.022  93.123  1.00 89.64           O  
ATOM   1849  CB  ALA A 269      40.787 -47.736  92.903  1.00 75.68           C  
ATOM   1850  N   ALA A 270      38.011 -49.170  93.674  1.00 85.69           N  
ATOM   1851  CA  ALA A 270      36.652 -49.614  93.295  1.00 85.35           C  
ATOM   1852  C   ALA A 270      35.618 -49.153  94.330  1.00 87.37           C  
ATOM   1853  O   ALA A 270      34.472 -48.839  93.921  1.00 83.42           O  
ATOM   1854  CB  ALA A 270      36.631 -51.116  93.153  1.00 86.36           C  
ATOM   1855  N   LEU A 271      36.031 -49.050  95.591  1.00 91.37           N  
ATOM   1856  CA  LEU A 271      35.086 -48.739  96.679  1.00 91.88           C  
ATOM   1857  C   LEU A 271      34.827 -47.235  96.736  1.00 97.88           C  
ATOM   1858  O   LEU A 271      33.750 -46.814  97.071  1.00100.73           O  
ATOM   1859  CB  LEU A 271      35.633 -49.249  98.018  1.00 88.82           C  
ATOM   1860  CG  LEU A 271      35.537 -50.758  98.246  1.00 89.36           C  
ATOM   1861  CD1 LEU A 271      36.034 -51.129  99.636  1.00 86.37           C  
ATOM   1862  CD2 LEU A 271      34.117 -51.262  98.040  1.00 91.35           C  
ATOM   1863  N   ASP A 272      35.797 -46.473  96.271  1.00102.23           N  
ATOM   1864  CA  ASP A 272      35.635 -44.996  96.157  1.00103.01           C  
ATOM   1865  C   ASP A 272      34.660 -44.685  95.030  1.00102.54           C  
ATOM   1866  O   ASP A 272      33.928 -43.697  95.101  1.00107.72           O  
ATOM   1867  CB  ASP A 272      36.975 -44.291  95.924  1.00104.85           C  
ATOM   1868  CG  ASP A 272      37.689 -43.885  97.203  1.00105.00           C  
ATOM   1869  OD1 ASP A 272      37.066 -43.972  98.280  1.00103.52           O  
ATOM   1870  OD2 ASP A 272      38.862 -43.482  97.109  1.00109.30           O  
ATOM   1871  N   ALA A 273      34.861 -45.410  93.934  1.00105.16           N  
ATOM   1872  CA  ALA A 273      34.061 -45.299  92.701  1.00107.82           C  
ATOM   1873  C   ALA A 273      32.626 -45.668  93.004  1.00114.02           C  
ATOM   1874  O   ALA A 273      31.698 -45.008  92.436  1.00117.10           O  
ATOM   1875  CB  ALA A 273      34.635 -46.171  91.609  1.00102.88           C  
ATOM   1876  N   GLN A 274      32.444 -46.680  93.867  1.00114.82           N  
ATOM   1877  CA  GLN A 274      31.082 -47.160  94.228  1.00112.75           C  
ATOM   1878  C   GLN A 274      30.292 -46.026  94.877  1.00114.98           C  
ATOM   1879  O   GLN A 274      29.158 -45.704  94.456  1.00115.87           O  
ATOM   1880  CB  GLN A 274      31.207 -48.341  95.195  1.00107.54           C  
ATOM   1881  CG  GLN A 274      29.981 -49.238  95.252  1.00102.85           C  
ATOM   1882  CD  GLN A 274      30.318 -50.601  95.809  1.00103.29           C  
ATOM   1883  OE1 GLN A 274      31.237 -50.757  96.612  1.00103.52           O  
ATOM   1884  NE2 GLN A 274      29.577 -51.607  95.376  1.00103.19           N  
ATOM   1885  N   LYS A 275      30.898 -45.411  95.868  1.00115.10           N  
ATOM   1886  CA  LYS A 275      30.272 -44.264  96.569  1.00117.40           C  
ATOM   1887  C   LYS A 275      30.037 -43.144  95.567  1.00117.40           C  
ATOM   1888  O   LYS A 275      28.846 -42.740  95.379  1.00111.77           O  
ATOM   1889  CB  LYS A 275      31.130 -43.867  97.773  1.00113.11           C  
ATOM   1890  CG  LYS A 275      31.102 -44.883  98.907  1.00115.09           C  
ATOM   1891  CD  LYS A 275      32.276 -44.804  99.849  1.00116.49           C  
ATOM   1892  CE  LYS A 275      32.340 -45.988 100.789  1.00115.56           C  
ATOM   1893  NZ  LYS A 275      33.181 -45.697 101.973  1.00118.72           N  
ATOM   1894  N   ALA A 276      31.099 -42.701  94.910  1.00114.04           N  
ATOM   1895  CA  ALA A 276      31.045 -41.559  93.969  1.00111.88           C  
ATOM   1896  C   ALA A 276      29.808 -41.651  93.059  1.00105.99           C  
ATOM   1897  O   ALA A 276      29.944 -41.312  91.853  1.00 96.62           O  
ATOM   1898  CB  ALA A 276      32.318 -41.504  93.154  1.00114.04           C  
ATOM   1899  N   ASP A 293      21.852 -51.733  87.284  1.00114.24           N  
ATOM   1900  CA  ASP A 293      22.808 -52.769  86.795  1.00118.92           C  
ATOM   1901  C   ASP A 293      24.226 -52.379  87.214  1.00123.27           C  
ATOM   1902  O   ASP A 293      25.113 -53.273  87.318  1.00134.14           O  
ATOM   1903  CB  ASP A 293      22.744 -52.922  85.271  1.00117.37           C  
ATOM   1904  CG  ASP A 293      21.383 -53.333  84.732  1.00117.67           C  
ATOM   1905  OD1 ASP A 293      20.632 -53.999  85.472  1.00117.99           O  
ATOM   1906  OD2 ASP A 293      21.088 -52.990  83.568  1.00112.34           O  
ATOM   1907  N   PHE A 294      24.435 -51.077  87.377  1.00120.75           N  
ATOM   1908  CA  PHE A 294      25.723 -50.474  87.784  1.00117.49           C  
ATOM   1909  C   PHE A 294      26.065 -50.849  89.217  1.00113.90           C  
ATOM   1910  O   PHE A 294      27.272 -50.936  89.564  1.00114.81           O  
ATOM   1911  CB  PHE A 294      25.678 -48.954  87.595  1.00118.81           C  
ATOM   1912  CG  PHE A 294      25.528 -48.513  86.161  1.00119.26           C  
ATOM   1913  CD1 PHE A 294      26.560 -48.697  85.255  1.00116.86           C  
ATOM   1914  CD2 PHE A 294      24.352 -47.929  85.711  1.00120.97           C  
ATOM   1915  CE1 PHE A 294      26.424 -48.296  83.935  1.00116.85           C  
ATOM   1916  CE2 PHE A 294      24.219 -47.529  84.389  1.00120.46           C  
ATOM   1917  CZ  PHE A 294      25.255 -47.714  83.503  1.00117.57           C  
ATOM   1918  N   ARG A 295      25.034 -51.046  90.027  1.00108.93           N  
ATOM   1919  CA  ARG A 295      25.195 -51.444  91.439  1.00106.77           C  
ATOM   1920  C   ARG A 295      25.629 -52.899  91.521  1.00104.01           C  
ATOM   1921  O   ARG A 295      26.369 -53.255  92.427  1.00101.47           O  
ATOM   1922  CB  ARG A 295      23.894 -51.196  92.207  1.00111.32           C  
ATOM   1923  CG  ARG A 295      23.530 -49.725  92.333  1.00116.58           C  
ATOM   1924  CD  ARG A 295      22.261 -49.512  93.131  1.00123.31           C  
ATOM   1925  NE  ARG A 295      21.902 -48.102  93.200  1.00130.68           N  
ATOM   1926  CZ  ARG A 295      20.825 -47.621  93.814  1.00132.10           C  
ATOM   1927  NH1 ARG A 295      19.983 -48.438  94.425  1.00133.09           N  
ATOM   1928  NH2 ARG A 295      20.592 -46.320  93.813  1.00134.68           N  
ATOM   1929  N   HIS A 296      25.233 -53.681  90.527  1.00 94.53           N  
ATOM   1930  CA  HIS A 296      25.581 -55.103  90.396  1.00 91.18           C  
ATOM   1931  C   HIS A 296      27.014 -55.208  89.876  1.00 89.86           C  
ATOM   1932  O   HIS A 296      27.736 -56.123  90.292  1.00 91.77           O  
ATOM   1933  CB  HIS A 296      24.536 -55.781  89.486  1.00 86.19           C  
ATOM   1934  CG  HIS A 296      24.696 -57.257  89.310  1.00 83.95           C  
ATOM   1935  ND1 HIS A 296      24.490 -58.155  90.341  1.00 80.36           N  
ATOM   1936  CD2 HIS A 296      24.987 -57.998  88.216  1.00 81.79           C  
ATOM   1937  CE1 HIS A 296      24.681 -59.383  89.895  1.00 81.77           C  
ATOM   1938  NE2 HIS A 296      24.988 -59.313  88.594  1.00 76.25           N  
ATOM   1939  N   GLY A 297      27.280 -54.411  88.851  1.00 84.32           N  
ATOM   1940  CA  GLY A 297      28.600 -54.295  88.221  1.00 79.40           C  
ATOM   1941  C   GLY A 297      29.697 -54.091  89.238  1.00 75.27           C  
ATOM   1942  O   GLY A 297      30.800 -54.608  89.025  1.00 69.30           O  
ATOM   1943  N   PHE A 298      29.408 -53.389  90.314  1.00 75.51           N  
ATOM   1944  CA  PHE A 298      30.413 -53.095  91.344  1.00 76.78           C  
ATOM   1945  C   PHE A 298      30.625 -54.269  92.284  1.00 79.06           C  
ATOM   1946  O   PHE A 298      31.738 -54.376  92.764  1.00 79.09           O  
ATOM   1947  CB  PHE A 298      30.116 -51.761  92.037  1.00 75.91           C  
ATOM   1948  CG  PHE A 298      30.860 -50.610  91.409  1.00 79.26           C  
ATOM   1949  CD1 PHE A 298      32.226 -50.464  91.605  1.00 78.91           C  
ATOM   1950  CD2 PHE A 298      30.219 -49.720  90.560  1.00 79.13           C  
ATOM   1951  CE1 PHE A 298      32.923 -49.429  91.002  1.00 80.21           C  
ATOM   1952  CE2 PHE A 298      30.917 -48.682  89.963  1.00 79.17           C  
ATOM   1953  CZ  PHE A 298      32.268 -48.538  90.185  1.00 80.50           C  
ATOM   1954  N   ASP A 299      29.559 -54.961  92.642  1.00 81.73           N  
ATOM   1955  CA  ASP A 299      29.599 -56.168  93.462  1.00 83.95           C  
ATOM   1956  C   ASP A 299      30.369 -57.262  92.746  1.00 76.39           C  
ATOM   1957  O   ASP A 299      31.115 -58.003  93.445  1.00 81.27           O  
ATOM   1958  CB  ASP A 299      28.188 -56.671  93.792  1.00 89.51           C  
ATOM   1959  CG  ASP A 299      27.355 -55.722  94.640  1.00 92.98           C  
ATOM   1960  OD1 ASP A 299      27.914 -54.712  95.121  1.00 98.30           O  
ATOM   1961  OD2 ASP A 299      26.151 -56.004  94.815  1.00 94.82           O  
ATOM   1962  N   ILE A 300      30.173 -57.357  91.431  1.00 69.91           N  
ATOM   1963  CA  ILE A 300      30.949 -58.301  90.596  1.00 68.27           C  
ATOM   1964  C   ILE A 300      32.428 -57.909  90.653  1.00 72.37           C  
ATOM   1965  O   ILE A 300      33.295 -58.756  90.902  1.00 68.78           O  
ATOM   1966  CB  ILE A 300      30.406 -58.340  89.153  1.00 67.51           C  
ATOM   1967  CG1 ILE A 300      28.976 -58.889  89.101  1.00 71.62           C  
ATOM   1968  CG2 ILE A 300      31.343 -59.128  88.245  1.00 70.38           C  
ATOM   1969  CD1 ILE A 300      28.290 -58.727  87.755  1.00 73.00           C  
ATOM   1970  N   LEU A 301      32.705 -56.618  90.484  1.00 69.00           N  
ATOM   1971  CA  LEU A 301      34.108 -56.152  90.448  1.00 68.21           C  
ATOM   1972  C   LEU A 301      34.783 -56.439  91.778  1.00 68.61           C  
ATOM   1973  O   LEU A 301      35.857 -57.047  91.805  1.00 68.35           O  
ATOM   1974  CB  LEU A 301      34.158 -54.653  90.154  1.00 67.00           C  
ATOM   1975  CG  LEU A 301      35.558 -54.125  89.836  1.00 67.11           C  
ATOM   1976  CD1 LEU A 301      35.867 -54.289  88.357  1.00 69.20           C  
ATOM   1977  CD2 LEU A 301      35.714 -52.676  90.258  1.00 67.39           C  
ATOM   1978  N   VAL A 302      34.162 -56.022  92.867  1.00 67.97           N  
ATOM   1979  CA  VAL A 302      34.740 -56.238  94.215  1.00 66.63           C  
ATOM   1980  C   VAL A 302      34.863 -57.737  94.478  1.00 65.57           C  
ATOM   1981  O   VAL A 302      35.892 -58.176  95.021  1.00 69.11           O  
ATOM   1982  CB  VAL A 302      33.923 -55.518  95.303  1.00 69.32           C  
ATOM   1983  CG1 VAL A 302      34.391 -55.884  96.704  1.00 70.05           C  
ATOM   1984  CG2 VAL A 302      33.952 -54.010  95.112  1.00 70.88           C  
ATOM   1985  N   GLY A 303      33.865 -58.510  94.102  1.00 61.08           N  
ATOM   1986  CA  GLY A 303      33.930 -59.958  94.304  1.00 59.82           C  
ATOM   1987  C   GLY A 303      35.080 -60.582  93.537  1.00 60.69           C  
ATOM   1988  O   GLY A 303      35.827 -61.404  94.090  1.00 61.25           O  
ATOM   1989  N   GLN A 304      35.223 -60.212  92.271  1.00 58.94           N  
ATOM   1990  CA  GLN A 304      36.297 -60.781  91.437  1.00 61.26           C  
ATOM   1991  C   GLN A 304      37.663 -60.371  91.971  1.00 63.76           C  
ATOM   1992  O   GLN A 304      38.615 -61.152  91.864  1.00 62.85           O  
ATOM   1993  CB  GLN A 304      36.103 -60.363  89.986  1.00 61.83           C  
ATOM   1994  CG  GLN A 304      34.929 -61.064  89.333  1.00 64.25           C  
ATOM   1995  CD  GLN A 304      34.674 -60.500  87.965  1.00 65.61           C  
ATOM   1996  OE1 GLN A 304      34.488 -59.297  87.807  1.00 69.04           O  
ATOM   1997  NE2 GLN A 304      34.691 -61.365  86.965  1.00 63.14           N  
ATOM   1998  N   ILE A 305      37.765 -59.173  92.530  1.00 64.70           N  
ATOM   1999  CA  ILE A 305      39.034 -58.728  93.157  1.00 61.32           C  
ATOM   2000  C   ILE A 305      39.277 -59.548  94.417  1.00 60.52           C  
ATOM   2001  O   ILE A 305      40.395 -60.021  94.642  1.00 54.26           O  
ATOM   2002  CB  ILE A 305      38.988 -57.214  93.464  1.00 59.67           C  
ATOM   2003  CG1 ILE A 305      39.052 -56.371  92.191  1.00 60.04           C  
ATOM   2004  CG2 ILE A 305      40.083 -56.815  94.447  1.00 60.66           C  
ATOM   2005  CD1 ILE A 305      38.730 -54.905  92.412  1.00 59.78           C  
ATOM   2006  N   ASP A 306      38.251 -59.702  95.241  1.00 63.33           N  
ATOM   2007  CA  ASP A 306      38.371 -60.525  96.464  1.00 67.66           C  
ATOM   2008  C   ASP A 306      38.789 -61.950  96.109  1.00 69.74           C  
ATOM   2009  O   ASP A 306      39.605 -62.538  96.819  1.00 67.38           O  
ATOM   2010  CB  ASP A 306      37.064 -60.546  97.268  1.00 69.57           C  
ATOM   2011  CG  ASP A 306      36.868 -59.343  98.176  1.00 75.86           C  
ATOM   2012  OD1 ASP A 306      37.831 -58.562  98.342  1.00 73.27           O  
ATOM   2013  OD2 ASP A 306      35.752 -59.196  98.713  1.00 86.61           O  
ATOM   2014  N   ASP A 307      38.233 -62.497  95.035  1.00 70.79           N  
ATOM   2015  CA  ASP A 307      38.594 -63.856  94.584  1.00 65.78           C  
ATOM   2016  C   ASP A 307      40.081 -63.905  94.239  1.00 65.76           C  
ATOM   2017  O   ASP A 307      40.850 -64.697  94.845  1.00 66.48           O  
ATOM   2018  CB  ASP A 307      37.795 -64.267  93.338  1.00 63.93           C  
ATOM   2019  CG  ASP A 307      36.308 -64.490  93.561  1.00 66.35           C  
ATOM   2020  OD1 ASP A 307      35.878 -64.459  94.734  1.00 71.02           O  
ATOM   2021  OD2 ASP A 307      35.583 -64.690  92.549  1.00 58.70           O  
ATOM   2022  N   ALA A 308      40.491 -63.089  93.273  1.00 61.24           N  
ATOM   2023  CA  ALA A 308      41.899 -63.033  92.842  1.00 62.58           C  
ATOM   2024  C   ALA A 308      42.817 -62.722  94.024  1.00 64.01           C  
ATOM   2025  O   ALA A 308      44.017 -63.030  93.950  1.00 61.39           O  
ATOM   2026  CB  ALA A 308      42.049 -62.000  91.753  1.00 58.39           C  
ATOM   2027  N   LEU A 309      42.290 -62.104  95.069  1.00 65.10           N  
ATOM   2028  CA  LEU A 309      43.124 -61.702  96.220  1.00 67.28           C  
ATOM   2029  C   LEU A 309      43.395 -62.879  97.140  1.00 64.94           C  
ATOM   2030  O   LEU A 309      44.547 -63.075  97.541  1.00 68.24           O  
ATOM   2031  CB  LEU A 309      42.406 -60.568  96.965  1.00 70.47           C  
ATOM   2032  CG  LEU A 309      43.270 -59.686  97.865  1.00 71.80           C  
ATOM   2033  CD1 LEU A 309      44.315 -58.929  97.063  1.00 72.01           C  
ATOM   2034  CD2 LEU A 309      42.397 -58.710  98.634  1.00 73.67           C  
ATOM   2035  N   LYS A 310      42.370 -63.646  97.472  1.00 64.64           N  
ATOM   2036  CA  LYS A 310      42.527 -64.833  98.344  1.00 67.26           C  
ATOM   2037  C   LYS A 310      43.434 -65.854  97.669  1.00 73.47           C  
ATOM   2038  O   LYS A 310      44.160 -66.581  98.381  1.00 81.10           O  
ATOM   2039  CB  LYS A 310      41.146 -65.449  98.602  1.00 64.60           C  
ATOM   2040  CG  LYS A 310      41.152 -66.773  99.348  1.00 71.02           C  
ATOM   2041  CD  LYS A 310      39.896 -67.591  99.157  1.00 76.34           C  
ATOM   2042  CE  LYS A 310      40.115 -69.067  99.418  1.00 81.26           C  
ATOM   2043  NZ  LYS A 310      40.783 -69.734  98.274  1.00 87.19           N  
ATOM   2044  N   LEU A 311      43.390 -65.935  96.343  1.00 72.26           N  
ATOM   2045  CA  LEU A 311      44.305 -66.827  95.613  1.00 66.07           C  
ATOM   2046  C   LEU A 311      45.738 -66.338  95.796  1.00 66.43           C  
ATOM   2047  O   LEU A 311      46.648 -67.166  96.087  1.00 62.65           O  
ATOM   2048  CB  LEU A 311      43.903 -66.890  94.135  1.00 67.09           C  
ATOM   2049  CG  LEU A 311      42.625 -67.676  93.834  1.00 66.20           C  
ATOM   2050  CD1 LEU A 311      42.217 -67.507  92.382  1.00 67.13           C  
ATOM   2051  CD2 LEU A 311      42.786 -69.150  94.173  1.00 63.07           C  
ATOM   2052  N   ALA A 312      45.962 -65.041  95.621  1.00 68.91           N  
ATOM   2053  CA  ALA A 312      47.317 -64.468  95.741  1.00 72.89           C  
ATOM   2054  C   ALA A 312      47.886 -64.726  97.129  1.00 76.20           C  
ATOM   2055  O   ALA A 312      49.076 -65.055  97.254  1.00 81.27           O  
ATOM   2056  CB  ALA A 312      47.264 -62.991  95.440  1.00 67.11           C  
ATOM   2057  N   ASN A 313      47.064 -64.579  98.154  1.00 78.60           N  
ATOM   2058  CA  ASN A 313      47.525 -64.803  99.543  1.00 79.74           C  
ATOM   2059  C   ASN A 313      47.957 -66.256  99.719  1.00 81.21           C  
ATOM   2060  O   ASN A 313      48.839 -66.520 100.562  1.00 85.49           O  
ATOM   2061  CB  ASN A 313      46.470 -64.368 100.562  1.00 79.46           C  
ATOM   2062  CG  ASN A 313      46.294 -62.865 100.614  1.00 79.53           C  
ATOM   2063  OD1 ASN A 313      45.236 -62.371 100.995  1.00 82.26           O  
ATOM   2064  ND2 ASN A 313      47.319 -62.128 100.218  1.00 78.79           N  
ATOM   2065  N   GLU A 314      47.386 -67.161  98.942  1.00 82.21           N  
ATOM   2066  CA  GLU A 314      47.714 -68.593  99.034  1.00 83.17           C  
ATOM   2067  C   GLU A 314      48.875 -68.963  98.126  1.00 79.22           C  
ATOM   2068  O   GLU A 314      49.188 -70.163  98.041  1.00 78.62           O  
ATOM   2069  CB  GLU A 314      46.466 -69.426  98.721  1.00 83.05           C  
ATOM   2070  CG  GLU A 314      45.471 -69.457  99.867  1.00 84.70           C  
ATOM   2071  CD  GLU A 314      44.063 -69.904  99.506  1.00 88.45           C  
ATOM   2072  OE1 GLU A 314      43.769 -70.038  98.299  1.00 84.15           O  
ATOM   2073  OE2 GLU A 314      43.259 -70.111 100.439  1.00 89.75           O  
ATOM   2074  N   GLY A 315      49.512 -67.984  97.507  1.00 78.01           N  
ATOM   2075  CA  GLY A 315      50.654 -68.217  96.639  1.00 80.83           C  
ATOM   2076  C   GLY A 315      50.271 -68.586  95.228  1.00 77.53           C  
ATOM   2077  O   GLY A 315      51.192 -68.921  94.506  1.00 85.19           O  
ATOM   2078  N   LYS A 316      48.992 -68.619  94.872  1.00 75.82           N  
ATOM   2079  CA  LYS A 316      48.590 -69.199  93.591  1.00 74.67           C  
ATOM   2080  C   LYS A 316      48.512 -68.051  92.630  1.00 78.55           C  
ATOM   2081  O   LYS A 316      47.451 -67.550  92.430  1.00 85.74           O  
ATOM   2082  CB  LYS A 316      47.278 -69.970  93.748  1.00 75.77           C  
ATOM   2083  CG  LYS A 316      47.315 -71.099  94.767  1.00 76.67           C  
ATOM   2084  CD  LYS A 316      45.974 -71.763  94.961  1.00 78.62           C  
ATOM   2085  CE  LYS A 316      46.022 -72.947  95.898  1.00 79.25           C  
ATOM   2086  NZ  LYS A 316      44.671 -73.506  96.125  1.00 82.41           N  
ATOM   2087  N   VAL A 317      49.642 -67.710  92.013  1.00 72.21           N  
ATOM   2088  CA  VAL A 317      49.846 -66.471  91.209  1.00 73.58           C  
ATOM   2089  C   VAL A 317      49.202 -66.569  89.819  1.00 74.39           C  
ATOM   2090  O   VAL A 317      48.453 -65.665  89.391  1.00 81.46           O  
ATOM   2091  CB  VAL A 317      51.356 -66.152  91.105  1.00 71.81           C  
ATOM   2092  CG1 VAL A 317      52.160 -67.287  90.475  1.00 74.54           C  
ATOM   2093  CG2 VAL A 317      51.614 -64.852  90.359  1.00 70.46           C  
ATOM   2094  N   LYS A 318      49.516 -67.628  89.096  1.00 72.20           N  
ATOM   2095  CA  LYS A 318      48.951 -67.843  87.749  1.00 74.21           C  
ATOM   2096  C   LYS A 318      47.431 -67.868  87.808  1.00 68.99           C  
ATOM   2097  O   LYS A 318      46.774 -67.325  86.900  1.00 73.08           O  
ATOM   2098  CB  LYS A 318      49.455 -69.152  87.137  1.00 74.68           C  
ATOM   2099  CG  LYS A 318      50.934 -69.179  86.786  1.00 77.99           C  
ATOM   2100  CD  LYS A 318      51.326 -68.249  85.664  1.00 77.08           C  
ATOM   2101  CE  LYS A 318      52.795 -68.370  85.319  1.00 80.58           C  
ATOM   2102  NZ  LYS A 318      53.270 -67.230  84.505  1.00 87.65           N  
ATOM   2103  N   GLU A 319      46.903 -68.490  88.861  1.00 65.86           N  
ATOM   2104  CA  GLU A 319      45.464 -68.571  89.173  1.00 71.23           C  
ATOM   2105  C   GLU A 319      44.912 -67.219  89.605  1.00 67.00           C  
ATOM   2106  O   GLU A 319      43.724 -66.921  89.359  1.00 63.59           O  
ATOM   2107  CB  GLU A 319      45.246 -69.604  90.288  1.00 71.51           C  
ATOM   2108  CG  GLU A 319      44.247 -70.690  89.943  1.00 78.05           C  
ATOM   2109  CD  GLU A 319      44.390 -71.961  90.765  1.00 83.79           C  
ATOM   2110  OE1 GLU A 319      44.686 -73.022  90.168  1.00 86.54           O  
ATOM   2111  OE2 GLU A 319      44.194 -71.894  91.995  1.00 86.83           O  
ATOM   2112  N   ALA A 320      45.740 -66.446  90.298  1.00 69.82           N  
ATOM   2113  CA  ALA A 320      45.389 -65.065  90.684  1.00 72.00           C  
ATOM   2114  C   ALA A 320      45.307 -64.192  89.433  1.00 69.71           C  
ATOM   2115  O   ALA A 320      44.327 -63.426  89.297  1.00 64.40           O  
ATOM   2116  CB  ALA A 320      46.390 -64.516  91.675  1.00 71.85           C  
ATOM   2117  N   GLN A 321      46.304 -64.309  88.567  1.00 68.10           N  
ATOM   2118  CA  GLN A 321      46.317 -63.560  87.308  1.00 65.09           C  
ATOM   2119  C   GLN A 321      45.121 -63.964  86.455  1.00 67.57           C  
ATOM   2120  O   GLN A 321      44.627 -63.091  85.739  1.00 75.70           O  
ATOM   2121  CB  GLN A 321      47.641 -63.789  86.586  1.00 64.10           C  
ATOM   2122  CG  GLN A 321      48.798 -63.067  87.252  1.00 68.56           C  
ATOM   2123  CD  GLN A 321      50.143 -63.551  86.769  1.00 72.24           C  
ATOM   2124  OE1 GLN A 321      50.512 -64.712  86.949  1.00 70.58           O  
ATOM   2125  NE2 GLN A 321      50.896 -62.650  86.161  1.00 72.48           N  
ATOM   2126  N   ALA A 322      44.844 -65.264  86.384  1.00 61.16           N  
ATOM   2127  CA  ALA A 322      43.673 -65.755  85.631  1.00 60.70           C  
ATOM   2128  C   ALA A 322      42.392 -65.175  86.219  1.00 60.05           C  
ATOM   2129  O   ALA A 322      41.528 -64.722  85.463  1.00 62.06           O  
ATOM   2130  CB  ALA A 322      43.652 -67.268  85.611  1.00 59.05           C  
ATOM   2131  N   ALA A 323      42.272 -65.170  87.540  1.00 59.61           N  
ATOM   2132  CA  ALA A 323      41.085 -64.596  88.195  1.00 59.71           C  
ATOM   2133  C   ALA A 323      41.034 -63.086  87.975  1.00 65.50           C  
ATOM   2134  O   ALA A 323      39.927 -62.525  87.886  1.00 71.31           O  
ATOM   2135  CB  ALA A 323      41.079 -64.950  89.662  1.00 57.38           C  
ATOM   2136  N   ALA A 324      42.191 -62.436  87.906  1.00 65.72           N  
ATOM   2137  CA  ALA A 324      42.232 -60.973  87.737  1.00 70.07           C  
ATOM   2138  C   ALA A 324      41.834 -60.593  86.321  1.00 72.04           C  
ATOM   2139  O   ALA A 324      41.363 -59.468  86.096  1.00 74.14           O  
ATOM   2140  CB  ALA A 324      43.604 -60.442  88.074  1.00 70.02           C  
ATOM   2141  N   GLU A 325      42.101 -61.478  85.377  1.00 74.01           N  
ATOM   2142  CA  GLU A 325      41.823 -61.193  83.955  1.00 77.40           C  
ATOM   2143  C   GLU A 325      40.326 -61.202  83.666  1.00 77.93           C  
ATOM   2144  O   GLU A 325      39.976 -60.699  82.589  1.00 79.44           O  
ATOM   2145  CB  GLU A 325      42.539 -62.235  83.087  1.00 79.87           C  
ATOM   2146  CG  GLU A 325      42.923 -61.734  81.707  1.00 83.28           C  
ATOM   2147  CD  GLU A 325      44.025 -60.690  81.688  1.00 84.39           C  
ATOM   2148  OE1 GLU A 325      44.700 -60.520  82.719  1.00 90.65           O  
ATOM   2149  OE2 GLU A 325      44.204 -60.051  80.641  1.00 88.36           O  
ATOM   2150  N   GLN A 326      39.494 -61.793  84.525  1.00 76.09           N  
ATOM   2151  CA  GLN A 326      38.045 -61.727  84.267  1.00 81.26           C  
ATOM   2152  C   GLN A 326      37.493 -60.344  84.571  1.00 83.82           C  
ATOM   2153  O   GLN A 326      36.301 -60.178  84.263  1.00 79.82           O  
ATOM   2154  CB  GLN A 326      37.296 -62.711  85.177  1.00 81.03           C  
ATOM   2155  CG  GLN A 326      37.869 -64.122  85.192  1.00 81.27           C  
ATOM   2156  CD  GLN A 326      37.868 -64.729  83.813  1.00 81.32           C  
ATOM   2157  OE1 GLN A 326      36.848 -64.745  83.129  1.00 79.95           O  
ATOM   2158  NE2 GLN A 326      39.024 -65.215  83.385  1.00 80.02           N  
ATOM   2159  N   LEU A 327      38.233 -59.554  85.357  1.00 78.72           N  
ATOM   2160  CA  LEU A 327      37.840 -58.152  85.628  1.00 74.56           C  
ATOM   2161  C   LEU A 327      37.631 -57.393  84.322  1.00 77.32           C  
ATOM   2162  O   LEU A 327      36.785 -56.504  84.290  1.00 78.25           O  
ATOM   2163  CB  LEU A 327      38.913 -57.487  86.492  1.00 73.10           C  
ATOM   2164  CG  LEU A 327      38.960 -57.961  87.943  1.00 75.44           C  
ATOM   2165  CD1 LEU A 327      40.219 -57.464  88.638  1.00 75.16           C  
ATOM   2166  CD2 LEU A 327      37.722 -57.514  88.703  1.00 75.71           C  
ATOM   2167  N   LYS A 328      38.328 -57.770  83.257  1.00 76.54           N  
ATOM   2168  CA  LYS A 328      38.182 -57.074  81.959  1.00 77.11           C  
ATOM   2169  C   LYS A 328      36.744 -57.064  81.475  1.00 76.67           C  
ATOM   2170  O   LYS A 328      36.295 -56.046  80.933  1.00 81.39           O  
ATOM   2171  CB  LYS A 328      39.046 -57.744  80.889  1.00 79.74           C  
ATOM   2172  CG  LYS A 328      40.527 -57.415  80.961  1.00 86.84           C  
ATOM   2173  CD  LYS A 328      41.321 -57.989  79.811  1.00 89.97           C  
ATOM   2174  CE  LYS A 328      42.785 -57.621  79.873  1.00 92.02           C  
ATOM   2175  NZ  LYS A 328      42.995 -56.172  79.654  1.00 98.10           N  
ATOM   2176  N   THR A 329      36.036 -58.173  81.667  1.00 75.43           N  
ATOM   2177  CA  THR A 329      34.642 -58.356  81.239  1.00 73.43           C  
ATOM   2178  C   THR A 329      33.699 -57.498  82.077  1.00 71.99           C  
ATOM   2179  O   THR A 329      32.722 -56.914  81.551  1.00 74.60           O  
ATOM   2180  CB  THR A 329      34.229 -59.833  81.319  1.00 73.24           C  
ATOM   2181  OG1 THR A 329      34.854 -60.497  80.222  1.00 79.94           O  
ATOM   2182  CG2 THR A 329      32.732 -60.056  81.259  1.00 71.43           C  
ATOM   2183  N   THR A 330      33.935 -57.504  83.381  1.00 72.73           N  
ATOM   2184  CA  THR A 330      33.175 -56.650  84.317  1.00 73.31           C  
ATOM   2185  C   THR A 330      33.403 -55.184  83.970  1.00 75.79           C  
ATOM   2186  O   THR A 330      32.434 -54.395  83.959  1.00 82.02           O  
ATOM   2187  CB  THR A 330      33.554 -56.955  85.768  1.00 70.14           C  
ATOM   2188  OG1 THR A 330      33.488 -58.371  85.910  1.00 73.64           O  
ATOM   2189  CG2 THR A 330      32.644 -56.285  86.774  1.00 70.91           C  
ATOM   2190  N   ARG A 331      34.644 -54.843  83.653  1.00 72.98           N  
ATOM   2191  CA  ARG A 331      34.995 -53.465  83.247  1.00 72.73           C  
ATOM   2192  C   ARG A 331      34.279 -53.094  81.951  1.00 71.78           C  
ATOM   2193  O   ARG A 331      33.599 -52.061  81.914  1.00 71.57           O  
ATOM   2194  CB  ARG A 331      36.514 -53.358  83.095  1.00 70.77           C  
ATOM   2195  CG  ARG A 331      37.028 -51.946  82.862  1.00 72.25           C  
ATOM   2196  CD  ARG A 331      38.425 -51.966  82.289  1.00 74.75           C  
ATOM   2197  NE  ARG A 331      38.505 -52.791  81.088  1.00 75.25           N  
ATOM   2198  CZ  ARG A 331      39.634 -53.199  80.522  1.00 73.57           C  
ATOM   2199  NH1 ARG A 331      40.803 -52.871  81.048  1.00 73.12           N  
ATOM   2200  NH2 ARG A 331      39.589 -53.942  79.431  1.00 74.70           N  
ATOM   2201  N   ASN A 332      34.397 -53.935  80.939  1.00 73.88           N  
ATOM   2202  CA  ASN A 332      33.818 -53.630  79.614  1.00 73.76           C  
ATOM   2203  C   ASN A 332      32.299 -53.536  79.745  1.00 77.09           C  
ATOM   2204  O   ASN A 332      31.710 -52.534  79.290  1.00 87.56           O  
ATOM   2205  CB  ASN A 332      34.287 -54.629  78.554  1.00 67.94           C  
ATOM   2206  CG  ASN A 332      35.775 -54.525  78.279  1.00 70.47           C  
ATOM   2207  OD1 ASN A 332      36.439 -53.608  78.756  1.00 71.14           O  
ATOM   2208  ND2 ASN A 332      36.315 -55.464  77.524  1.00 72.76           N  
ATOM   2209  N   ALA A 333      31.716 -54.484  80.444  1.00 77.11           N  
ATOM   2210  CA  ALA A 333      30.269 -54.647  80.620  1.00 77.05           C  
ATOM   2211  C   ALA A 333      29.611 -53.579  81.492  1.00 83.40           C  
ATOM   2212  O   ALA A 333      28.426 -53.249  81.165  1.00 85.99           O  
ATOM   2213  CB  ALA A 333      29.976 -56.034  81.144  1.00 76.28           C  
ATOM   2214  N   TYR A 334      30.231 -53.126  82.588  1.00 84.11           N  
ATOM   2215  CA  TYR A 334      29.521 -52.312  83.602  1.00 84.46           C  
ATOM   2216  C   TYR A 334      30.242 -50.997  83.896  1.00 78.57           C  
ATOM   2217  O   TYR A 334      29.651 -49.946  83.810  1.00 74.90           O  
ATOM   2218  CB  TYR A 334      29.310 -53.141  84.873  1.00 87.95           C  
ATOM   2219  CG  TYR A 334      28.449 -54.368  84.686  1.00 94.14           C  
ATOM   2220  CD1 TYR A 334      29.000 -55.573  84.279  1.00 95.08           C  
ATOM   2221  CD2 TYR A 334      27.081 -54.330  84.914  1.00 95.96           C  
ATOM   2222  CE1 TYR A 334      28.220 -56.704  84.097  1.00 91.98           C  
ATOM   2223  CE2 TYR A 334      26.286 -55.453  84.741  1.00 95.71           C  
ATOM   2224  CZ  TYR A 334      26.858 -56.645  84.331  1.00 93.54           C  
ATOM   2225  OH  TYR A 334      26.091 -57.760  84.156  1.00 91.98           O  
ATOM   2226  N   ILE A 335      31.499 -51.096  84.226  1.00 76.33           N  
ATOM   2227  CA  ILE A 335      32.318 -49.974  84.732  1.00 77.53           C  
ATOM   2228  C   ILE A 335      32.451 -48.866  83.699  1.00 76.77           C  
ATOM   2229  O   ILE A 335      32.205 -47.715  84.069  1.00 82.31           O  
ATOM   2230  CB  ILE A 335      33.690 -50.480  85.216  1.00 79.20           C  
ATOM   2231  CG1 ILE A 335      33.545 -51.666  86.177  1.00 84.39           C  
ATOM   2232  CG2 ILE A 335      34.488 -49.344  85.838  1.00 77.39           C  
ATOM   2233  CD1 ILE A 335      32.505 -51.466  87.262  1.00 83.14           C  
ATOM   2234  N   GLN A 336      32.747 -49.226  82.453  1.00 78.54           N  
ATOM   2235  CA  GLN A 336      32.904 -48.267  81.357  1.00 79.79           C  
ATOM   2236  C   GLN A 336      31.609 -47.504  81.127  1.00 77.23           C  
ATOM   2237  O   GLN A 336      31.704 -46.373  80.687  1.00 73.65           O  
ATOM   2238  CB  GLN A 336      33.354 -48.950  80.061  1.00 82.94           C  
ATOM   2239  CG  GLN A 336      33.455 -47.987  78.880  1.00 87.21           C  
ATOM   2240  CD  GLN A 336      34.476 -48.397  77.847  1.00 89.38           C  
ATOM   2241  OE1 GLN A 336      34.561 -49.556  77.451  1.00100.10           O  
ATOM   2242  NE2 GLN A 336      35.251 -47.432  77.384  1.00 89.77           N  
ATOM   2243  N   LYS A 337      30.474 -48.136  81.353  1.00 75.30           N  
ATOM   2244  CA  LYS A 337      29.166 -47.475  81.192  1.00 80.63           C  
ATOM   2245  C   LYS A 337      28.892 -46.505  82.332  1.00 77.91           C  
ATOM   2246  O   LYS A 337      28.378 -45.408  82.056  1.00 76.33           O  
ATOM   2247  CB  LYS A 337      28.081 -48.540  81.017  1.00 86.73           C  
ATOM   2248  CG  LYS A 337      28.180 -49.301  79.701  1.00 95.59           C  
ATOM   2249  CD  LYS A 337      27.155 -50.396  79.529  1.00103.05           C  
ATOM   2250  CE  LYS A 337      27.259 -51.075  78.178  1.00105.80           C  
ATOM   2251  NZ  LYS A 337      26.150 -52.031  77.952  1.00110.78           N  
ATOM   2252  N   TYR A 338      29.269 -46.866  83.559  1.00 77.95           N  
ATOM   2253  CA  TYR A 338      29.070 -45.988  84.732  1.00 81.17           C  
ATOM   2254  C   TYR A 338      30.001 -44.786  84.660  1.00 79.54           C  
ATOM   2255  O   TYR A 338      29.599 -43.673  85.055  1.00 81.53           O  
ATOM   2256  CB  TYR A 338      29.348 -46.711  86.058  1.00 84.93           C  
ATOM   2257  CG  TYR A 338      29.388 -45.791  87.258  1.00 97.25           C  
ATOM   2258  CD1 TYR A 338      30.547 -45.106  87.604  1.00100.86           C  
ATOM   2259  CD2 TYR A 338      28.254 -45.561  88.023  1.00104.78           C  
ATOM   2260  CE1 TYR A 338      30.581 -44.232  88.681  1.00100.81           C  
ATOM   2261  CE2 TYR A 338      28.273 -44.695  89.107  1.00104.13           C  
ATOM   2262  CZ  TYR A 338      29.439 -44.026  89.436  1.00102.33           C  
ATOM   2263  OH  TYR A 338      29.462 -43.171  90.499  1.00 99.62           O  
ATOM   2264  N   LEU A 339      31.242 -45.009  84.243  1.00 77.29           N  
ATOM   2265  CA  LEU A 339      32.205 -43.911  84.024  1.00 75.72           C  
ATOM   2266  C   LEU A 339      31.625 -42.873  83.047  1.00 76.17           C  
ATOM   2267  O   LEU A 339      31.919 -41.653  83.216  1.00 74.56           O  
ATOM   2268  CB  LEU A 339      33.529 -44.458  83.466  1.00 78.87           C  
ATOM   2269  CG  LEU A 339      34.450 -43.420  82.801  1.00 79.62           C  
ATOM   2270  CD1 LEU A 339      35.101 -42.520  83.843  1.00 82.18           C  
ATOM   2271  CD2 LEU A 339      35.516 -44.082  81.932  1.00 76.23           C  
ATOM   2272  N   GLU A 340      30.943 -43.337  81.995  1.00 74.47           N  
ATOM   2273  CA  GLU A 340      30.552 -42.498  80.834  1.00 75.87           C  
ATOM   2274  C   GLU A 340      29.254 -41.753  81.163  1.00 75.78           C  
ATOM   2275  O   GLU A 340      29.120 -40.595  80.721  1.00 71.30           O  
ATOM   2276  CB  GLU A 340      30.447 -43.347  79.566  1.00 80.00           C  
ATOM   2277  CG  GLU A 340      31.796 -43.576  78.903  1.00 87.60           C  
ATOM   2278  CD  GLU A 340      31.796 -44.461  77.666  1.00 92.47           C  
ATOM   2279  OE1 GLU A 340      30.849 -45.263  77.501  1.00 96.10           O  
ATOM   2280  OE2 GLU A 340      32.760 -44.357  76.877  1.00 97.55           O  
ATOM   2281  N   ARG A 341      28.358 -42.372  81.939  1.00 71.61           N  
ATOM   2282  CA  ARG A 341      27.083 -41.747  82.374  1.00 74.75           C  
ATOM   2283  C   ARG A 341      27.394 -40.642  83.394  1.00 73.48           C  
ATOM   2284  O   ARG A 341      26.815 -39.543  83.263  1.00 77.30           O  
ATOM   2285  CB  ARG A 341      26.122 -42.794  82.947  1.00 82.06           C  
ATOM   2286  CG  ARG A 341      24.669 -42.337  82.983  1.00 92.58           C  
ATOM   2287  CD  ARG A 341      23.771 -43.235  83.819  1.00105.54           C  
ATOM   2288  NE  ARG A 341      23.140 -44.304  83.048  1.00112.86           N  
ATOM   2289  CZ  ARG A 341      22.044 -44.168  82.300  1.00116.00           C  
ATOM   2290  NH1 ARG A 341      21.442 -42.993  82.194  1.00116.03           N  
ATOM   2291  NH2 ARG A 341      21.559 -45.213  81.652  1.00113.62           N  
ATOM   2292  N   ALA A 342      28.282 -40.920  84.356  1.00 63.75           N  
ATOM   2293  CA  ALA A 342      28.713 -39.978  85.415  1.00 65.21           C  
ATOM   2294  C   ALA A 342      29.433 -38.777  84.782  1.00 68.86           C  
ATOM   2295  O   ALA A 342      29.206 -37.639  85.246  1.00 67.86           O  
ATOM   2296  CB  ALA A 342      29.593 -40.684  86.418  1.00 62.37           C  
ATOM   2297  N   ARG A 343      30.267 -39.030  83.768  1.00 70.39           N  
ATOM   2298  CA  ARG A 343      30.983 -37.994  82.975  1.00 71.00           C  
ATOM   2299  C   ARG A 343      29.950 -37.112  82.266  1.00 70.75           C  
ATOM   2300  O   ARG A 343      30.113 -35.872  82.276  1.00 64.67           O  
ATOM   2301  CB  ARG A 343      31.922 -38.663  81.968  1.00 77.73           C  
ATOM   2302  CG  ARG A 343      32.959 -37.731  81.362  1.00 86.04           C  
ATOM   2303  CD  ARG A 343      34.117 -38.507  80.763  1.00 96.81           C  
ATOM   2304  NE  ARG A 343      34.791 -37.763  79.708  1.00108.50           N  
ATOM   2305  CZ  ARG A 343      35.765 -38.246  78.942  1.00112.84           C  
ATOM   2306  NH1 ARG A 343      36.195 -39.487  79.111  1.00111.57           N  
ATOM   2307  NH2 ARG A 343      36.304 -37.482  78.006  1.00115.13           N  
ATOM   2308  N   SER A 344      28.918 -37.743  81.697  1.00 67.08           N  
ATOM   2309  CA  SER A 344      27.803 -37.095  80.965  1.00 63.79           C  
ATOM   2310  C   SER A 344      27.017 -36.174  81.909  1.00 64.50           C  
ATOM   2311  O   SER A 344      26.667 -35.057  81.486  1.00 64.58           O  
ATOM   2312  CB  SER A 344      26.916 -38.132  80.336  1.00 65.45           C  
ATOM   2313  OG  SER A 344      25.843 -37.522  79.640  1.00 68.22           O  
ATOM   2314  N   THR A 345      26.749 -36.623  83.138  1.00 62.93           N  
ATOM   2315  CA  THR A 345      25.970 -35.865  84.156  1.00 65.51           C  
ATOM   2316  C   THR A 345      26.752 -34.612  84.572  1.00 62.34           C  
ATOM   2317  O   THR A 345      26.139 -33.529  84.592  1.00 62.92           O  
ATOM   2318  CB  THR A 345      25.605 -36.753  85.350  1.00 67.51           C  
ATOM   2319  OG1 THR A 345      24.807 -37.814  84.831  1.00 74.85           O  
ATOM   2320  CG2 THR A 345      24.843 -36.026  86.437  1.00 67.57           C  
ATOM   2321  N   LEU A 346      28.044 -34.762  84.883  1.00 59.42           N  
ATOM   2322  CA  LEU A 346      28.949 -33.645  85.270  1.00 62.22           C  
ATOM   2323  C   LEU A 346      28.986 -32.603  84.148  1.00 62.82           C  
ATOM   2324  O   LEU A 346      28.934 -31.399  84.460  1.00 67.14           O  
ATOM   2325  CB  LEU A 346      30.354 -34.187  85.553  1.00 59.94           C  
ATOM   2326  CG  LEU A 346      30.539 -34.877  86.905  1.00 63.75           C  
ATOM   2327  CD1 LEU A 346      31.985 -35.314  87.094  1.00 63.17           C  
ATOM   2328  CD2 LEU A 346      30.102 -33.978  88.055  1.00 61.78           C  
ATOM   2329  N   GLN A 347      29.072 -33.056  82.898  1.00 64.82           N  
ATOM   2330  CA  GLN A 347      29.193 -32.179  81.706  1.00 70.11           C  
ATOM   2331  C   GLN A 347      27.887 -31.391  81.543  1.00 67.48           C  
ATOM   2332  O   GLN A 347      27.969 -30.179  81.278  1.00 64.75           O  
ATOM   2333  CB  GLN A 347      29.539 -33.009  80.467  1.00 76.61           C  
ATOM   2334  CG  GLN A 347      30.070 -32.178  79.305  1.00 86.85           C  
ATOM   2335  CD  GLN A 347      30.732 -33.012  78.233  1.00 93.09           C  
ATOM   2336  OE1 GLN A 347      31.339 -34.048  78.507  1.00 97.65           O  
ATOM   2337  NE2 GLN A 347      30.626 -32.557  76.993  1.00 90.29           N  
ATOM   2338  N   LYS A 348      26.740 -32.060  81.726  1.00 67.60           N  
ATOM   2339  CA  LYS A 348      25.379 -31.452  81.735  1.00 65.44           C  
ATOM   2340  C   LYS A 348      25.302 -30.366  82.815  1.00 62.97           C  
ATOM   2341  O   LYS A 348      24.640 -29.332  82.573  1.00 66.93           O  
ATOM   2342  CB  LYS A 348      24.307 -32.512  82.009  1.00 67.73           C  
ATOM   2343  CG  LYS A 348      23.556 -33.028  80.792  1.00 71.32           C  
ATOM   2344  CD  LYS A 348      22.232 -33.673  81.153  1.00 79.35           C  
ATOM   2345  CE  LYS A 348      21.383 -34.029  79.949  1.00 87.35           C  
ATOM   2346  NZ  LYS A 348      21.785 -35.325  79.352  1.00 90.80           N  
ATOM   2347  N   GLU A 349      25.906 -30.622  83.978  1.00 57.66           N  
ATOM   2348  CA  GLU A 349      25.909 -29.703  85.145  1.00 57.95           C  
ATOM   2349  C   GLU A 349      26.809 -28.502  84.844  1.00 59.94           C  
ATOM   2350  O   GLU A 349      26.403 -27.371  85.169  1.00 59.93           O  
ATOM   2351  CB  GLU A 349      26.372 -30.427  86.407  1.00 58.83           C  
ATOM   2352  CG  GLU A 349      25.253 -31.129  87.146  1.00 57.85           C  
ATOM   2353  CD  GLU A 349      25.703 -31.795  88.431  1.00 61.12           C  
ATOM   2354  OE1 GLU A 349      26.280 -32.903  88.347  1.00 63.38           O  
ATOM   2355  OE2 GLU A 349      25.495 -31.196  89.515  1.00 61.60           O  
ATOM   2356  N   VAL A 350      27.976 -28.734  84.234  1.00 62.68           N  
ATOM   2357  CA  VAL A 350      28.895 -27.644  83.786  1.00 62.69           C  
ATOM   2358  C   VAL A 350      28.137 -26.748  82.792  1.00 60.20           C  
ATOM   2359  O   VAL A 350      28.245 -25.526  82.930  1.00 58.79           O  
ATOM   2360  CB  VAL A 350      30.212 -28.189  83.193  1.00 61.99           C  
ATOM   2361  CG1 VAL A 350      31.025 -27.098  82.513  1.00 60.71           C  
ATOM   2362  CG2 VAL A 350      31.056 -28.883  84.253  1.00 65.61           C  
ATOM   2363  N   HIS A 351      27.359 -27.336  81.872  1.00 57.94           N  
ATOM   2364  CA  HIS A 351      26.567 -26.609  80.840  1.00 62.47           C  
ATOM   2365  C   HIS A 351      25.499 -25.747  81.529  1.00 59.64           C  
ATOM   2366  O   HIS A 351      25.489 -24.523  81.292  1.00 58.20           O  
ATOM   2367  CB  HIS A 351      25.970 -27.587  79.810  1.00 68.26           C  
ATOM   2368  CG  HIS A 351      25.292 -26.926  78.648  1.00 77.61           C  
ATOM   2369  ND1 HIS A 351      25.940 -26.689  77.442  1.00 80.35           N  
ATOM   2370  CD2 HIS A 351      24.026 -26.469  78.490  1.00 81.24           C  
ATOM   2371  CE1 HIS A 351      25.106 -26.104  76.602  1.00 80.62           C  
ATOM   2372  NE2 HIS A 351      23.927 -25.957  77.219  1.00 83.56           N  
ATOM   2373  N   ALA A 352      24.661 -26.351  82.376  1.00 53.31           N  
ATOM   2374  CA  ALA A 352      23.587 -25.657  83.126  1.00 54.03           C  
ATOM   2375  C   ALA A 352      24.184 -24.488  83.928  1.00 55.72           C  
ATOM   2376  O   ALA A 352      23.576 -23.396  83.937  1.00 52.62           O  
ATOM   2377  CB  ALA A 352      22.861 -26.634  84.017  1.00 50.76           C  
ATOM   2378  N   ALA A 353      25.332 -24.705  84.577  1.00 56.65           N  
ATOM   2379  CA  ALA A 353      25.984 -23.714  85.465  1.00 57.21           C  
ATOM   2380  C   ALA A 353      26.547 -22.565  84.619  1.00 58.82           C  
ATOM   2381  O   ALA A 353      26.455 -21.405  85.066  1.00 62.61           O  
ATOM   2382  CB  ALA A 353      27.051 -24.372  86.302  1.00 55.85           C  
ATOM   2383  N   LYS A 354      27.087 -22.869  83.435  1.00 57.28           N  
ATOM   2384  CA  LYS A 354      27.584 -21.843  82.484  1.00 58.52           C  
ATOM   2385  C   LYS A 354      26.392 -21.008  82.003  1.00 52.30           C  
ATOM   2386  O   LYS A 354      26.504 -19.773  81.993  1.00 49.63           O  
ATOM   2387  CB  LYS A 354      28.340 -22.474  81.310  1.00 67.34           C  
ATOM   2388  CG  LYS A 354      29.017 -21.463  80.394  1.00 78.13           C  
ATOM   2389  CD  LYS A 354      29.700 -22.047  79.174  1.00 84.99           C  
ATOM   2390  CE  LYS A 354      30.041 -20.982  78.147  1.00 87.06           C  
ATOM   2391  NZ  LYS A 354      30.511 -21.568  76.870  1.00 88.38           N  
ATOM   2392  N   SER A 355      25.284 -21.665  81.655  1.00 50.30           N  
ATOM   2393  CA  SER A 355      24.008 -21.024  81.241  1.00 49.36           C  
ATOM   2394  C   SER A 355      23.565 -20.004  82.295  1.00 48.97           C  
ATOM   2395  O   SER A 355      23.261 -18.863  81.913  1.00 50.94           O  
ATOM   2396  CB  SER A 355      22.947 -22.050  81.002  1.00 48.62           C  
ATOM   2397  OG  SER A 355      23.226 -22.779  79.819  1.00 52.64           O  
ATOM   2398  N   ALA A 356      23.540 -20.414  83.569  1.00 47.21           N  
ATOM   2399  CA  ALA A 356      23.162 -19.584  84.732  1.00 45.01           C  
ATOM   2400  C   ALA A 356      24.158 -18.428  84.894  1.00 46.78           C  
ATOM   2401  O   ALA A 356      23.708 -17.300  85.179  1.00 48.97           O  
ATOM   2402  CB  ALA A 356      23.093 -20.440  85.970  1.00 46.43           C  
ATOM   2403  N   ALA A 357      25.455 -18.694  84.702  1.00 46.40           N  
ATOM   2404  CA  ALA A 357      26.558 -17.710  84.858  1.00 48.41           C  
ATOM   2405  C   ALA A 357      26.437 -16.607  83.803  1.00 45.53           C  
ATOM   2406  O   ALA A 357      26.726 -15.430  84.124  1.00 44.84           O  
ATOM   2407  CB  ALA A 357      27.898 -18.397  84.764  1.00 49.16           C  
ATOM   2408  N   ILE A 358      26.073 -16.977  82.578  1.00 45.41           N  
ATOM   2409  CA  ILE A 358      25.861 -16.017  81.458  1.00 47.43           C  
ATOM   2410  C   ILE A 358      24.763 -15.019  81.859  1.00 49.09           C  
ATOM   2411  O   ILE A 358      24.960 -13.812  81.657  1.00 51.23           O  
ATOM   2412  CB  ILE A 358      25.540 -16.769  80.156  1.00 49.00           C  
ATOM   2413  CG1 ILE A 358      26.798 -17.447  79.602  1.00 49.81           C  
ATOM   2414  CG2 ILE A 358      24.883 -15.841  79.136  1.00 49.83           C  
ATOM   2415  CD1 ILE A 358      26.525 -18.478  78.530  1.00 51.69           C  
ATOM   2416  N   ILE A 359      23.679 -15.504  82.462  1.00 48.75           N  
ATOM   2417  CA  ILE A 359      22.508 -14.680  82.879  1.00 48.22           C  
ATOM   2418  C   ILE A 359      22.928 -13.715  83.992  1.00 45.46           C  
ATOM   2419  O   ILE A 359      22.568 -12.515  83.897  1.00 47.34           O  
ATOM   2420  CB  ILE A 359      21.331 -15.591  83.269  1.00 53.51           C  
ATOM   2421  CG1 ILE A 359      20.628 -16.100  82.008  1.00 59.45           C  
ATOM   2422  CG2 ILE A 359      20.371 -14.886  84.213  1.00 52.72           C  
ATOM   2423  CD1 ILE A 359      19.672 -17.226  82.246  1.00 66.45           C  
ATOM   2424  N   ALA A 360      23.676 -14.194  84.988  1.00 43.07           N  
ATOM   2425  CA  ALA A 360      24.292 -13.348  86.040  1.00 44.96           C  
ATOM   2426  C   ALA A 360      25.223 -12.317  85.385  1.00 43.48           C  
ATOM   2427  O   ALA A 360      25.136 -11.129  85.742  1.00 45.48           O  
ATOM   2428  CB  ALA A 360      25.033 -14.202  87.038  1.00 46.77           C  
ATOM   2429  N   GLY A 361      26.072 -12.756  84.450  1.00 40.65           N  
ATOM   2430  CA  GLY A 361      27.009 -11.881  83.722  1.00 39.62           C  
ATOM   2431  C   GLY A 361      26.278 -10.808  82.939  1.00 38.23           C  
ATOM   2432  O   GLY A 361      26.746  -9.652  82.939  1.00 37.89           O  
ATOM   2433  N   LEU A 362      25.154 -11.163  82.313  1.00 41.11           N  
ATOM   2434  CA  LEU A 362      24.368 -10.242  81.447  1.00 43.30           C  
ATOM   2435  C   LEU A 362      23.701  -9.171  82.315  1.00 40.77           C  
ATOM   2436  O   LEU A 362      23.653  -8.019  81.884  1.00 41.95           O  
ATOM   2437  CB  LEU A 362      23.342 -11.037  80.635  1.00 45.57           C  
ATOM   2438  CG  LEU A 362      23.888 -11.754  79.396  1.00 50.79           C  
ATOM   2439  CD1 LEU A 362      22.756 -12.388  78.605  1.00 58.21           C  
ATOM   2440  CD2 LEU A 362      24.683 -10.816  78.504  1.00 50.34           C  
ATOM   2441  N   PHE A 363      23.255  -9.533  83.517  1.00 40.39           N  
ATOM   2442  CA  PHE A 363      22.706  -8.586  84.517  1.00 38.76           C  
ATOM   2443  C   PHE A 363      23.761  -7.521  84.828  1.00 38.68           C  
ATOM   2444  O   PHE A 363      23.439  -6.306  84.848  1.00 37.57           O  
ATOM   2445  CB  PHE A 363      22.284  -9.319  85.791  1.00 41.19           C  
ATOM   2446  CG  PHE A 363      21.613  -8.431  86.803  1.00 42.02           C  
ATOM   2447  CD1 PHE A 363      22.363  -7.726  87.733  1.00 42.11           C  
ATOM   2448  CD2 PHE A 363      20.238  -8.248  86.782  1.00 39.70           C  
ATOM   2449  CE1 PHE A 363      21.748  -6.875  88.641  1.00 42.90           C  
ATOM   2450  CE2 PHE A 363      19.623  -7.417  87.704  1.00 41.76           C  
ATOM   2451  CZ  PHE A 363      20.380  -6.723  88.627  1.00 43.56           C  
ATOM   2452  N   ALA A 364      24.987  -7.971  85.079  1.00 38.31           N  
ATOM   2453  CA  ALA A 364      26.158  -7.118  85.384  1.00 39.31           C  
ATOM   2454  C   ALA A 364      26.414  -6.161  84.216  1.00 39.48           C  
ATOM   2455  O   ALA A 364      26.452  -4.934  84.440  1.00 37.66           O  
ATOM   2456  CB  ALA A 364      27.359  -7.988  85.671  1.00 41.65           C  
ATOM   2457  N   LEU A 365      26.534  -6.695  83.001  1.00 44.10           N  
ATOM   2458  CA  LEU A 365      26.824  -5.882  81.792  1.00 45.54           C  
ATOM   2459  C   LEU A 365      25.744  -4.800  81.628  1.00 44.39           C  
ATOM   2460  O   LEU A 365      26.108  -3.632  81.390  1.00 43.61           O  
ATOM   2461  CB  LEU A 365      26.897  -6.802  80.570  1.00 54.24           C  
ATOM   2462  CG  LEU A 365      27.742  -6.277  79.411  1.00 59.58           C  
ATOM   2463  CD1 LEU A 365      29.227  -6.342  79.753  1.00 60.30           C  
ATOM   2464  CD2 LEU A 365      27.448  -7.053  78.131  1.00 60.06           C  
ATOM   2465  N   CYS A 366      24.470  -5.156  81.796  1.00 41.18           N  
ATOM   2466  CA  CYS A 366      23.315  -4.266  81.499  1.00 43.17           C  
ATOM   2467  C   CYS A 366      23.163  -3.169  82.566  1.00 40.44           C  
ATOM   2468  O   CYS A 366      22.720  -2.072  82.194  1.00 39.36           O  
ATOM   2469  CB  CYS A 366      22.027  -5.067  81.355  1.00 46.68           C  
ATOM   2470  SG  CYS A 366      21.977  -6.062  79.839  1.00 51.58           S  
ATOM   2471  N   TRP A 367      23.551  -3.430  83.822  1.00 41.12           N  
ATOM   2472  CA  TRP A 367      23.329  -2.510  84.980  1.00 39.12           C  
ATOM   2473  C   TRP A 367      24.574  -1.673  85.311  1.00 38.21           C  
ATOM   2474  O   TRP A 367      24.400  -0.568  85.844  1.00 37.73           O  
ATOM   2475  CB  TRP A 367      22.866  -3.293  86.208  1.00 38.67           C  
ATOM   2476  CG  TRP A 367      21.392  -3.510  86.223  1.00 39.06           C  
ATOM   2477  CD1 TRP A 367      20.718  -4.638  85.852  1.00 38.65           C  
ATOM   2478  CD2 TRP A 367      20.396  -2.543  86.580  1.00 39.84           C  
ATOM   2479  NE1 TRP A 367      19.370  -4.442  85.973  1.00 40.63           N  
ATOM   2480  CE2 TRP A 367      19.140  -3.167  86.415  1.00 38.77           C  
ATOM   2481  CE3 TRP A 367      20.440  -1.218  87.021  1.00 40.26           C  
ATOM   2482  CZ2 TRP A 367      17.947  -2.518  86.699  1.00 36.26           C  
ATOM   2483  CZ3 TRP A 367      19.254  -0.572  87.291  1.00 40.06           C  
ATOM   2484  CH2 TRP A 367      18.027  -1.216  87.131  1.00 39.08           C  
ATOM   2485  N   LEU A 368      25.781  -2.186  85.064  1.00 37.86           N  
ATOM   2486  CA  LEU A 368      27.040  -1.513  85.489  1.00 36.88           C  
ATOM   2487  C   LEU A 368      27.122  -0.104  84.905  1.00 37.69           C  
ATOM   2488  O   LEU A 368      27.483   0.826  85.621  1.00 43.64           O  
ATOM   2489  CB  LEU A 368      28.247  -2.354  85.080  1.00 39.22           C  
ATOM   2490  CG  LEU A 368      28.693  -3.372  86.123  1.00 43.21           C  
ATOM   2491  CD1 LEU A 368      29.728  -4.319  85.537  1.00 46.95           C  
ATOM   2492  CD2 LEU A 368      29.238  -2.681  87.361  1.00 45.13           C  
ATOM   2493  N   PRO A 369      26.816   0.113  83.604  1.00 34.80           N  
ATOM   2494  CA  PRO A 369      26.948   1.440  83.015  1.00 33.43           C  
ATOM   2495  C   PRO A 369      26.184   2.499  83.822  1.00 34.22           C  
ATOM   2496  O   PRO A 369      26.789   3.464  84.194  1.00 35.12           O  
ATOM   2497  CB  PRO A 369      26.411   1.261  81.582  1.00 35.58           C  
ATOM   2498  CG  PRO A 369      26.653  -0.210  81.293  1.00 37.23           C  
ATOM   2499  CD  PRO A 369      26.385  -0.896  82.619  1.00 36.56           C  
ATOM   2500  N   LEU A 370      24.898   2.273  84.112  1.00 37.81           N  
ATOM   2501  CA  LEU A 370      24.062   3.204  84.919  1.00 37.83           C  
ATOM   2502  C   LEU A 370      24.705   3.419  86.302  1.00 36.88           C  
ATOM   2503  O   LEU A 370      24.814   4.588  86.751  1.00 38.98           O  
ATOM   2504  CB  LEU A 370      22.645   2.637  85.050  1.00 37.76           C  
ATOM   2505  CG  LEU A 370      21.652   3.540  85.785  1.00 36.97           C  
ATOM   2506  CD1 LEU A 370      21.708   4.961  85.250  1.00 37.16           C  
ATOM   2507  CD2 LEU A 370      20.237   2.987  85.691  1.00 37.53           C  
ATOM   2508  N   HIS A 371      25.134   2.344  86.948  1.00 34.99           N  
ATOM   2509  CA  HIS A 371      25.806   2.393  88.272  1.00 38.61           C  
ATOM   2510  C   HIS A 371      27.112   3.187  88.186  1.00 38.63           C  
ATOM   2511  O   HIS A 371      27.417   3.944  89.152  1.00 38.24           O  
ATOM   2512  CB  HIS A 371      26.039   0.983  88.799  1.00 39.04           C  
ATOM   2513  CG  HIS A 371      24.817   0.391  89.404  1.00 38.45           C  
ATOM   2514  ND1 HIS A 371      24.095   1.050  90.371  1.00 37.15           N  
ATOM   2515  CD2 HIS A 371      24.198  -0.792  89.196  1.00 37.48           C  
ATOM   2516  CE1 HIS A 371      23.083   0.296  90.746  1.00 39.04           C  
ATOM   2517  NE2 HIS A 371      23.133  -0.849  90.051  1.00 36.91           N  
ATOM   2518  N   ILE A 372      27.865   3.011  87.098  1.00 36.90           N  
ATOM   2519  CA  ILE A 372      29.192   3.665  86.899  1.00 35.91           C  
ATOM   2520  C   ILE A 372      28.954   5.157  86.660  1.00 35.43           C  
ATOM   2521  O   ILE A 372      29.672   5.962  87.245  1.00 35.45           O  
ATOM   2522  CB  ILE A 372      29.985   2.976  85.768  1.00 37.27           C  
ATOM   2523  CG1 ILE A 372      30.430   1.571  86.190  1.00 37.69           C  
ATOM   2524  CG2 ILE A 372      31.169   3.823  85.320  1.00 38.01           C  
ATOM   2525  CD1 ILE A 372      30.929   0.705  85.056  1.00 39.01           C  
ATOM   2526  N   ILE A 373      27.936   5.517  85.877  1.00 37.58           N  
ATOM   2527  CA  ILE A 373      27.579   6.946  85.627  1.00 38.51           C  
ATOM   2528  C   ILE A 373      27.247   7.609  86.972  1.00 38.45           C  
ATOM   2529  O   ILE A 373      27.728   8.719  87.204  1.00 44.83           O  
ATOM   2530  CB  ILE A 373      26.435   7.080  84.602  1.00 39.10           C  
ATOM   2531  CG1 ILE A 373      26.853   6.595  83.215  1.00 38.28           C  
ATOM   2532  CG2 ILE A 373      25.931   8.512  84.548  1.00 39.28           C  
ATOM   2533  CD1 ILE A 373      25.711   6.544  82.231  1.00 40.52           C  
ATOM   2534  N   ASN A 374      26.483   6.936  87.834  1.00 38.64           N  
ATOM   2535  CA  ASN A 374      26.142   7.427  89.197  1.00 37.54           C  
ATOM   2536  C   ASN A 374      27.425   7.695  89.993  1.00 36.69           C  
ATOM   2537  O   ASN A 374      27.519   8.755  90.638  1.00 38.63           O  
ATOM   2538  CB  ASN A 374      25.218   6.453  89.927  1.00 38.49           C  
ATOM   2539  CG  ASN A 374      23.812   6.429  89.363  1.00 38.97           C  
ATOM   2540  OD1 ASN A 374      23.437   7.295  88.569  1.00 40.06           O  
ATOM   2541  ND2 ASN A 374      23.022   5.458  89.788  1.00 35.91           N  
ATOM   2542  N   CYS A 375      28.378   6.767  89.958  1.00 37.90           N  
ATOM   2543  CA  CYS A 375      29.705   6.906  90.616  1.00 37.60           C  
ATOM   2544  C   CYS A 375      30.409   8.178  90.130  1.00 35.83           C  
ATOM   2545  O   CYS A 375      30.940   8.900  90.974  1.00 39.59           O  
ATOM   2546  CB  CYS A 375      30.573   5.683  90.356  1.00 39.85           C  
ATOM   2547  SG  CYS A 375      30.004   4.216  91.249  1.00 42.60           S  
ATOM   2548  N   PHE A 376      30.397   8.453  88.824  1.00 35.12           N  
ATOM   2549  CA  PHE A 376      31.001   9.676  88.233  1.00 37.75           C  
ATOM   2550  C   PHE A 376      30.284  10.921  88.768  1.00 38.37           C  
ATOM   2551  O   PHE A 376      30.977  11.872  89.174  1.00 43.33           O  
ATOM   2552  CB  PHE A 376      30.998   9.618  86.701  1.00 38.53           C  
ATOM   2553  CG  PHE A 376      32.254   9.025  86.123  1.00 37.95           C  
ATOM   2554  CD1 PHE A 376      32.364   7.656  85.912  1.00 39.77           C  
ATOM   2555  CD2 PHE A 376      33.356   9.824  85.861  1.00 38.80           C  
ATOM   2556  CE1 PHE A 376      33.535   7.109  85.413  1.00 39.11           C  
ATOM   2557  CE2 PHE A 376      34.524   9.275  85.357  1.00 39.02           C  
ATOM   2558  CZ  PHE A 376      34.611   7.922  85.126  1.00 39.32           C  
ATOM   2559  N   THR A 377      28.948  10.917  88.768  1.00 39.03           N  
ATOM   2560  CA  THR A 377      28.096  12.023  89.288  1.00 40.54           C  
ATOM   2561  C   THR A 377      28.443  12.292  90.755  1.00 39.45           C  
ATOM   2562  O   THR A 377      28.593  13.462  91.119  1.00 39.96           O  
ATOM   2563  CB  THR A 377      26.606  11.691  89.161  1.00 44.47           C  
ATOM   2564  OG1 THR A 377      26.297  11.586  87.769  1.00 48.85           O  
ATOM   2565  CG2 THR A 377      25.722  12.727  89.823  1.00 44.70           C  
ATOM   2566  N   PHE A 378      28.534  11.237  91.561  1.00 37.64           N  
ATOM   2567  CA  PHE A 378      28.738  11.315  93.030  1.00 41.80           C  
ATOM   2568  C   PHE A 378      30.173  11.764  93.352  1.00 43.86           C  
ATOM   2569  O   PHE A 378      30.333  12.744  94.081  1.00 42.94           O  
ATOM   2570  CB  PHE A 378      28.446   9.959  93.670  1.00 42.75           C  
ATOM   2571  CG  PHE A 378      28.535   9.954  95.170  1.00 41.47           C  
ATOM   2572  CD1 PHE A 378      27.812  10.864  95.922  1.00 37.58           C  
ATOM   2573  CD2 PHE A 378      29.351   9.044  95.827  1.00 43.64           C  
ATOM   2574  CE1 PHE A 378      27.902  10.867  97.302  1.00 39.93           C  
ATOM   2575  CE2 PHE A 378      29.447   9.052  97.209  1.00 43.11           C  
ATOM   2576  CZ  PHE A 378      28.717   9.962  97.945  1.00 44.27           C  
ATOM   2577  N   PHE A 379      31.172  11.068  92.800  1.00 41.97           N  
ATOM   2578  CA  PHE A 379      32.589  11.104  93.241  1.00 43.00           C  
ATOM   2579  C   PHE A 379      33.349  12.249  92.559  1.00 46.58           C  
ATOM   2580  O   PHE A 379      34.272  12.773  93.186  1.00 47.73           O  
ATOM   2581  CB  PHE A 379      33.285   9.774  92.941  1.00 38.42           C  
ATOM   2582  CG  PHE A 379      32.980   8.658  93.906  1.00 36.57           C  
ATOM   2583  CD1 PHE A 379      33.078   8.857  95.279  1.00 36.28           C  
ATOM   2584  CD2 PHE A 379      32.668   7.387  93.442  1.00 34.33           C  
ATOM   2585  CE1 PHE A 379      32.839   7.816  96.164  1.00 36.61           C  
ATOM   2586  CE2 PHE A 379      32.403   6.355  94.328  1.00 34.33           C  
ATOM   2587  CZ  PHE A 379      32.492   6.569  95.687  1.00 36.19           C  
ATOM   2588  N   CYS A 380      33.011  12.580  91.307  1.00 50.72           N  
ATOM   2589  CA  CYS A 380      33.653  13.667  90.517  1.00 52.76           C  
ATOM   2590  C   CYS A 380      32.679  14.825  90.292  1.00 54.08           C  
ATOM   2591  O   CYS A 380      32.187  15.009  89.180  1.00 56.41           O  
ATOM   2592  CB  CYS A 380      34.179  13.164  89.176  1.00 52.83           C  
ATOM   2593  SG  CYS A 380      35.287  14.369  88.399  1.00 57.71           S  
ATOM   2594  N   PRO A 381      32.401  15.663  91.321  1.00 52.48           N  
ATOM   2595  CA  PRO A 381      31.567  16.853  91.146  1.00 54.60           C  
ATOM   2596  C   PRO A 381      32.219  17.968  90.310  1.00 57.04           C  
ATOM   2597  O   PRO A 381      31.544  18.942  90.037  1.00 60.93           O  
ATOM   2598  CB  PRO A 381      31.352  17.358  92.585  1.00 55.56           C  
ATOM   2599  CG  PRO A 381      32.566  16.853  93.335  1.00 53.87           C  
ATOM   2600  CD  PRO A 381      32.873  15.510  92.706  1.00 52.97           C  
ATOM   2601  N   ASP A 382      33.506  17.826  89.974  1.00 57.35           N  
ATOM   2602  CA  ASP A 382      34.239  18.722  89.036  1.00 60.84           C  
ATOM   2603  C   ASP A 382      34.073  18.224  87.592  1.00 59.13           C  
ATOM   2604  O   ASP A 382      34.403  18.983  86.671  1.00 54.39           O  
ATOM   2605  CB  ASP A 382      35.725  18.819  89.393  1.00 67.51           C  
ATOM   2606  CG  ASP A 382      36.009  19.635  90.643  1.00 75.54           C  
ATOM   2607  OD1 ASP A 382      35.278  20.630  90.876  1.00 81.03           O  
ATOM   2608  OD2 ASP A 382      36.967  19.276  91.372  1.00 81.06           O  
ATOM   2609  N   CYS A 383      33.628  16.980  87.404  1.00 58.92           N  
ATOM   2610  CA  CYS A 383      33.295  16.402  86.077  1.00 59.02           C  
ATOM   2611  C   CYS A 383      31.901  16.877  85.659  1.00 56.11           C  
ATOM   2612  O   CYS A 383      30.995  16.874  86.516  1.00 54.76           O  
ATOM   2613  CB  CYS A 383      33.342  14.879  86.096  1.00 60.66           C  
ATOM   2614  SG  CYS A 383      35.002  14.214  86.389  1.00 62.84           S  
ATOM   2615  N   SER A 384      31.760  17.303  84.401  1.00 54.67           N  
ATOM   2616  CA  SER A 384      30.463  17.592  83.741  1.00 53.47           C  
ATOM   2617  C   SER A 384      29.550  16.381  83.916  1.00 49.92           C  
ATOM   2618  O   SER A 384      30.035  15.248  83.749  1.00 47.33           O  
ATOM   2619  CB  SER A 384      30.644  17.921  82.283  1.00 54.52           C  
ATOM   2620  OG  SER A 384      31.089  19.258  82.121  1.00 59.16           O  
ATOM   2621  N   HIS A 385      28.285  16.612  84.250  1.00 44.56           N  
ATOM   2622  CA  HIS A 385      27.264  15.546  84.308  1.00 46.01           C  
ATOM   2623  C   HIS A 385      27.211  14.858  82.942  1.00 47.35           C  
ATOM   2624  O   HIS A 385      27.175  15.579  81.925  1.00 49.43           O  
ATOM   2625  CB  HIS A 385      25.904  16.101  84.731  1.00 46.31           C  
ATOM   2626  CG  HIS A 385      25.021  15.051  85.317  1.00 48.62           C  
ATOM   2627  ND1 HIS A 385      24.458  14.049  84.549  1.00 47.39           N  
ATOM   2628  CD2 HIS A 385      24.649  14.807  86.593  1.00 47.40           C  
ATOM   2629  CE1 HIS A 385      23.740  13.260  85.322  1.00 48.78           C  
ATOM   2630  NE2 HIS A 385      23.851  13.697  86.580  1.00 48.75           N  
ATOM   2631  N   ALA A 386      27.253  13.522  82.927  1.00 43.07           N  
ATOM   2632  CA  ALA A 386      26.906  12.691  81.759  1.00 42.03           C  
ATOM   2633  C   ALA A 386      25.720  13.337  81.055  1.00 43.40           C  
ATOM   2634  O   ALA A 386      24.754  13.745  81.712  1.00 38.51           O  
ATOM   2635  CB  ALA A 386      26.582  11.288  82.198  1.00 44.93           C  
ATOM   2636  N   PRO A 387      25.770  13.477  79.710  1.00 44.91           N  
ATOM   2637  CA  PRO A 387      24.699  14.140  78.969  1.00 45.94           C  
ATOM   2638  C   PRO A 387      23.385  13.339  79.037  1.00 43.00           C  
ATOM   2639  O   PRO A 387      23.414  12.173  79.365  1.00 41.62           O  
ATOM   2640  CB  PRO A 387      25.251  14.255  77.533  1.00 47.43           C  
ATOM   2641  CG  PRO A 387      26.315  13.176  77.431  1.00 49.31           C  
ATOM   2642  CD  PRO A 387      26.847  12.984  78.837  1.00 47.88           C  
ATOM   2643  N   LEU A 388      22.262  13.993  78.750  1.00 44.68           N  
ATOM   2644  CA  LEU A 388      20.910  13.384  78.838  1.00 45.55           C  
ATOM   2645  C   LEU A 388      20.841  12.127  77.949  1.00 43.49           C  
ATOM   2646  O   LEU A 388      20.298  11.109  78.410  1.00 45.08           O  
ATOM   2647  CB  LEU A 388      19.862  14.429  78.446  1.00 47.70           C  
ATOM   2648  CG  LEU A 388      18.404  13.979  78.557  1.00 52.17           C  
ATOM   2649  CD1 LEU A 388      18.141  13.298  79.894  1.00 52.59           C  
ATOM   2650  CD2 LEU A 388      17.458  15.155  78.360  1.00 50.96           C  
ATOM   2651  N   TRP A 389      21.408  12.163  76.746  1.00 42.37           N  
ATOM   2652  CA  TRP A 389      21.298  11.051  75.766  1.00 42.38           C  
ATOM   2653  C   TRP A 389      21.992   9.779  76.301  1.00 42.89           C  
ATOM   2654  O   TRP A 389      21.476   8.661  76.045  1.00 42.11           O  
ATOM   2655  CB  TRP A 389      21.820  11.483  74.391  1.00 41.63           C  
ATOM   2656  CG  TRP A 389      23.298  11.692  74.310  1.00 39.84           C  
ATOM   2657  CD1 TRP A 389      23.960  12.884  74.350  1.00 41.44           C  
ATOM   2658  CD2 TRP A 389      24.303  10.679  74.143  1.00 38.28           C  
ATOM   2659  NE1 TRP A 389      25.307  12.680  74.245  1.00 41.91           N  
ATOM   2660  CE2 TRP A 389      25.548  11.338  74.107  1.00 39.05           C  
ATOM   2661  CE3 TRP A 389      24.273   9.286  74.040  1.00 40.52           C  
ATOM   2662  CZ2 TRP A 389      26.749  10.651  73.963  1.00 40.83           C  
ATOM   2663  CZ3 TRP A 389      25.461   8.604  73.901  1.00 43.09           C  
ATOM   2664  CH2 TRP A 389      26.681   9.281  73.851  1.00 44.54           C  
ATOM   2665  N   LEU A 390      23.088   9.921  77.049  1.00 41.46           N  
ATOM   2666  CA  LEU A 390      23.844   8.765  77.612  1.00 41.30           C  
ATOM   2667  C   LEU A 390      23.112   8.232  78.855  1.00 38.46           C  
ATOM   2668  O   LEU A 390      23.063   6.989  79.035  1.00 37.70           O  
ATOM   2669  CB  LEU A 390      25.284   9.193  77.930  1.00 40.78           C  
ATOM   2670  CG  LEU A 390      26.178   8.111  78.535  1.00 41.35           C  
ATOM   2671  CD1 LEU A 390      26.310   6.930  77.596  1.00 42.72           C  
ATOM   2672  CD2 LEU A 390      27.552   8.667  78.884  1.00 44.19           C  
ATOM   2673  N   MET A 391      22.535   9.126  79.656  1.00 38.92           N  
ATOM   2674  CA  MET A 391      21.631   8.762  80.781  1.00 40.97           C  
ATOM   2675  C   MET A 391      20.514   7.885  80.227  1.00 43.43           C  
ATOM   2676  O   MET A 391      20.303   6.790  80.772  1.00 46.01           O  
ATOM   2677  CB  MET A 391      21.015   9.996  81.441  1.00 40.58           C  
ATOM   2678  CG  MET A 391      22.039  10.927  82.057  1.00 44.26           C  
ATOM   2679  SD  MET A 391      23.137  10.110  83.242  1.00 46.49           S  
ATOM   2680  CE  MET A 391      21.951   9.336  84.342  1.00 47.19           C  
ATOM   2681  N   TYR A 392      19.872   8.335  79.143  1.00 45.88           N  
ATOM   2682  CA  TYR A 392      18.779   7.608  78.449  1.00 46.27           C  
ATOM   2683  C   TYR A 392      19.289   6.232  77.992  1.00 44.14           C  
ATOM   2684  O   TYR A 392      18.576   5.233  78.203  1.00 40.58           O  
ATOM   2685  CB  TYR A 392      18.217   8.434  77.286  1.00 47.54           C  
ATOM   2686  CG  TYR A 392      17.279   9.556  77.662  1.00 51.08           C  
ATOM   2687  CD1 TYR A 392      16.519   9.520  78.825  1.00 56.13           C  
ATOM   2688  CD2 TYR A 392      17.110  10.647  76.821  1.00 56.59           C  
ATOM   2689  CE1 TYR A 392      15.636  10.542  79.149  1.00 56.18           C  
ATOM   2690  CE2 TYR A 392      16.231  11.677  77.130  1.00 56.59           C  
ATOM   2691  CZ  TYR A 392      15.496  11.630  78.302  1.00 58.34           C  
ATOM   2692  OH  TYR A 392      14.641  12.653  78.619  1.00 62.55           O  
ATOM   2693  N   LEU A 393      20.490   6.170  77.409  1.00 42.26           N  
ATOM   2694  CA  LEU A 393      21.071   4.905  76.881  1.00 42.01           C  
ATOM   2695  C   LEU A 393      21.336   3.943  78.043  1.00 40.69           C  
ATOM   2696  O   LEU A 393      20.993   2.756  77.917  1.00 40.90           O  
ATOM   2697  CB  LEU A 393      22.352   5.203  76.094  1.00 44.36           C  
ATOM   2698  CG  LEU A 393      23.052   3.975  75.502  1.00 45.94           C  
ATOM   2699  CD1 LEU A 393      22.110   3.199  74.598  1.00 46.59           C  
ATOM   2700  CD2 LEU A 393      24.313   4.370  74.744  1.00 45.29           C  
ATOM   2701  N   ALA A 394      21.913   4.438  79.138  1.00 42.29           N  
ATOM   2702  CA  ALA A 394      22.226   3.640  80.346  1.00 42.02           C  
ATOM   2703  C   ALA A 394      20.930   3.073  80.943  1.00 39.57           C  
ATOM   2704  O   ALA A 394      20.892   1.867  81.271  1.00 40.16           O  
ATOM   2705  CB  ALA A 394      22.983   4.482  81.343  1.00 43.45           C  
ATOM   2706  N   ILE A 395      19.894   3.902  81.059  1.00 40.73           N  
ATOM   2707  CA  ILE A 395      18.576   3.497  81.637  1.00 41.62           C  
ATOM   2708  C   ILE A 395      17.959   2.405  80.746  1.00 39.37           C  
ATOM   2709  O   ILE A 395      17.510   1.391  81.273  1.00 37.88           O  
ATOM   2710  CB  ILE A 395      17.649   4.721  81.808  1.00 41.24           C  
ATOM   2711  CG1 ILE A 395      18.179   5.688  82.872  1.00 38.97           C  
ATOM   2712  CG2 ILE A 395      16.224   4.277  82.115  1.00 42.25           C  
ATOM   2713  CD1 ILE A 395      17.617   7.097  82.773  1.00 39.16           C  
ATOM   2714  N   VAL A 396      17.964   2.617  79.434  1.00 41.15           N  
ATOM   2715  CA  VAL A 396      17.348   1.708  78.423  1.00 41.89           C  
ATOM   2716  C   VAL A 396      18.085   0.357  78.466  1.00 41.69           C  
ATOM   2717  O   VAL A 396      17.406  -0.704  78.451  1.00 37.61           O  
ATOM   2718  CB  VAL A 396      17.357   2.385  77.034  1.00 45.10           C  
ATOM   2719  CG1 VAL A 396      17.579   1.416  75.881  1.00 48.93           C  
ATOM   2720  CG2 VAL A 396      16.084   3.200  76.819  1.00 43.54           C  
ATOM   2721  N   LEU A 397      19.414   0.388  78.586  1.00 41.11           N  
ATOM   2722  CA  LEU A 397      20.255  -0.831  78.634  1.00 42.06           C  
ATOM   2723  C   LEU A 397      19.945  -1.611  79.919  1.00 38.67           C  
ATOM   2724  O   LEU A 397      19.794  -2.832  79.839  1.00 38.97           O  
ATOM   2725  CB  LEU A 397      21.731  -0.436  78.541  1.00 46.50           C  
ATOM   2726  CG  LEU A 397      22.710  -1.610  78.508  1.00 48.71           C  
ATOM   2727  CD1 LEU A 397      22.575  -2.400  77.215  1.00 47.56           C  
ATOM   2728  CD2 LEU A 397      24.139  -1.125  78.694  1.00 49.08           C  
ATOM   2729  N   ALA A 398      19.813  -0.936  81.059  1.00 38.34           N  
ATOM   2730  CA  ALA A 398      19.434  -1.584  82.336  1.00 38.73           C  
ATOM   2731  C   ALA A 398      18.079  -2.284  82.156  1.00 40.27           C  
ATOM   2732  O   ALA A 398      17.958  -3.453  82.583  1.00 42.12           O  
ATOM   2733  CB  ALA A 398      19.407  -0.580  83.465  1.00 38.78           C  
ATOM   2734  N   HIS A 399      17.114  -1.623  81.505  1.00 39.81           N  
ATOM   2735  CA  HIS A 399      15.754  -2.176  81.225  1.00 42.12           C  
ATOM   2736  C   HIS A 399      15.837  -3.371  80.260  1.00 41.44           C  
ATOM   2737  O   HIS A 399      15.100  -4.335  80.477  1.00 37.54           O  
ATOM   2738  CB  HIS A 399      14.824  -1.073  80.723  1.00 41.03           C  
ATOM   2739  CG  HIS A 399      14.532  -0.039  81.754  1.00 42.47           C  
ATOM   2740  ND1 HIS A 399      14.129   1.238  81.424  1.00 45.02           N  
ATOM   2741  CD2 HIS A 399      14.587  -0.087  83.107  1.00 44.63           C  
ATOM   2742  CE1 HIS A 399      13.928   1.931  82.532  1.00 48.88           C  
ATOM   2743  NE2 HIS A 399      14.199   1.135  83.582  1.00 43.68           N  
ATOM   2744  N   THR A 400      16.746  -3.319  79.276  1.00 43.49           N  
ATOM   2745  CA  THR A 400      16.983  -4.365  78.240  1.00 44.11           C  
ATOM   2746  C   THR A 400      17.313  -5.712  78.894  1.00 42.63           C  
ATOM   2747  O   THR A 400      17.058  -6.754  78.266  1.00 41.63           O  
ATOM   2748  CB  THR A 400      18.099  -3.935  77.271  1.00 48.07           C  
ATOM   2749  OG1 THR A 400      17.632  -2.802  76.539  1.00 48.39           O  
ATOM   2750  CG2 THR A 400      18.497  -5.013  76.287  1.00 48.34           C  
ATOM   2751  N   ASN A 401      17.887  -5.698  80.094  1.00 44.14           N  
ATOM   2752  CA  ASN A 401      18.220  -6.929  80.848  1.00 43.15           C  
ATOM   2753  C   ASN A 401      16.961  -7.789  81.047  1.00 40.92           C  
ATOM   2754  O   ASN A 401      17.084  -9.030  81.115  1.00 42.02           O  
ATOM   2755  CB  ASN A 401      18.857  -6.634  82.205  1.00 43.97           C  
ATOM   2756  CG  ASN A 401      19.288  -7.919  82.875  1.00 43.81           C  
ATOM   2757  OD1 ASN A 401      20.052  -8.691  82.302  1.00 47.90           O  
ATOM   2758  ND2 ASN A 401      18.719  -8.210  84.024  1.00 43.95           N  
ATOM   2759  N   SER A 402      15.800  -7.157  81.160  1.00 41.95           N  
ATOM   2760  CA  SER A 402      14.505  -7.832  81.417  1.00 45.58           C  
ATOM   2761  C   SER A 402      13.988  -8.501  80.138  1.00 46.04           C  
ATOM   2762  O   SER A 402      12.980  -9.229  80.224  1.00 49.83           O  
ATOM   2763  CB  SER A 402      13.515  -6.864  81.998  1.00 49.19           C  
ATOM   2764  OG  SER A 402      13.945  -6.434  83.290  1.00 48.97           O  
ATOM   2765  N   VAL A 403      14.695  -8.333  79.014  1.00 46.35           N  
ATOM   2766  CA  VAL A 403      14.375  -9.015  77.725  1.00 46.15           C  
ATOM   2767  C   VAL A 403      15.234 -10.278  77.558  1.00 46.62           C  
ATOM   2768  O   VAL A 403      14.732 -11.223  76.922  1.00 44.03           O  
ATOM   2769  CB  VAL A 403      14.553  -8.076  76.516  1.00 44.01           C  
ATOM   2770  CG1 VAL A 403      14.081  -8.746  75.240  1.00 44.92           C  
ATOM   2771  CG2 VAL A 403      13.845  -6.744  76.714  1.00 45.47           C  
ATOM   2772  N   VAL A 404      16.490 -10.278  78.030  1.00 45.30           N  
ATOM   2773  CA  VAL A 404      17.545 -11.197  77.501  1.00 49.67           C  
ATOM   2774  C   VAL A 404      17.373 -12.614  78.071  1.00 52.30           C  
ATOM   2775  O   VAL A 404      17.678 -13.566  77.327  1.00 62.21           O  
ATOM   2776  CB  VAL A 404      18.980 -10.674  77.726  1.00 52.68           C  
ATOM   2777  CG1 VAL A 404      19.258  -9.428  76.902  1.00 52.49           C  
ATOM   2778  CG2 VAL A 404      19.298 -10.432  79.194  1.00 52.92           C  
ATOM   2779  N   ASN A 405      16.931 -12.770  79.321  1.00 53.84           N  
ATOM   2780  CA  ASN A 405      16.874 -14.095  80.012  1.00 59.15           C  
ATOM   2781  C   ASN A 405      16.181 -15.140  79.119  1.00 57.28           C  
ATOM   2782  O   ASN A 405      16.761 -16.193  78.849  1.00 56.05           O  
ATOM   2783  CB  ASN A 405      16.267 -13.977  81.417  1.00 61.68           C  
ATOM   2784  CG  ASN A 405      17.146 -13.188  82.368  1.00 68.38           C  
ATOM   2785  OD1 ASN A 405      18.183 -12.653  81.975  1.00 64.18           O  
ATOM   2786  ND2 ASN A 405      16.745 -13.108  83.626  1.00 76.61           N  
ATOM   2787  N   PRO A 406      14.944 -14.901  78.611  1.00 52.67           N  
ATOM   2788  CA  PRO A 406      14.269 -15.863  77.728  1.00 57.92           C  
ATOM   2789  C   PRO A 406      15.062 -16.396  76.518  1.00 57.17           C  
ATOM   2790  O   PRO A 406      14.896 -17.551  76.185  1.00 52.43           O  
ATOM   2791  CB  PRO A 406      13.050 -15.072  77.224  1.00 58.29           C  
ATOM   2792  CG  PRO A 406      12.729 -14.138  78.369  1.00 56.04           C  
ATOM   2793  CD  PRO A 406      14.080 -13.759  78.946  1.00 53.05           C  
ATOM   2794  N   PHE A 407      15.883 -15.560  75.881  1.00 62.97           N  
ATOM   2795  CA  PHE A 407      16.730 -15.943  74.714  1.00 65.89           C  
ATOM   2796  C   PHE A 407      17.811 -16.939  75.152  1.00 63.44           C  
ATOM   2797  O   PHE A 407      18.042 -17.919  74.427  1.00 60.02           O  
ATOM   2798  CB  PHE A 407      17.316 -14.700  74.039  1.00 67.52           C  
ATOM   2799  CG  PHE A 407      16.289 -13.953  73.235  1.00 70.65           C  
ATOM   2800  CD1 PHE A 407      16.070 -14.276  71.904  1.00 72.29           C  
ATOM   2801  CD2 PHE A 407      15.462 -13.015  73.839  1.00 69.95           C  
ATOM   2802  CE1 PHE A 407      15.085 -13.629  71.178  1.00 72.60           C  
ATOM   2803  CE2 PHE A 407      14.473 -12.373  73.112  1.00 70.60           C  
ATOM   2804  CZ  PHE A 407      14.289 -12.681  71.783  1.00 74.71           C  
ATOM   2805  N   ILE A 408      18.404 -16.731  76.330  1.00 62.79           N  
ATOM   2806  CA  ILE A 408      19.497 -17.591  76.868  1.00 62.90           C  
ATOM   2807  C   ILE A 408      18.945 -18.998  77.152  1.00 64.76           C  
ATOM   2808  O   ILE A 408      19.590 -19.988  76.716  1.00 61.20           O  
ATOM   2809  CB  ILE A 408      20.138 -16.942  78.106  1.00 60.85           C  
ATOM   2810  CG1 ILE A 408      20.711 -15.559  77.783  1.00 57.19           C  
ATOM   2811  CG2 ILE A 408      21.189 -17.864  78.705  1.00 63.62           C  
ATOM   2812  CD1 ILE A 408      21.800 -15.567  76.734  1.00 54.45           C  
ATOM   2813  N   TYR A 409      17.785 -19.094  77.814  1.00 65.24           N  
ATOM   2814  CA  TYR A 409      17.105 -20.386  78.111  1.00 65.65           C  
ATOM   2815  C   TYR A 409      16.811 -21.109  76.792  1.00 62.44           C  
ATOM   2816  O   TYR A 409      17.137 -22.302  76.674  1.00 64.81           O  
ATOM   2817  CB  TYR A 409      15.808 -20.188  78.899  1.00 63.79           C  
ATOM   2818  CG  TYR A 409      15.931 -19.392  80.172  1.00 61.93           C  
ATOM   2819  CD1 TYR A 409      16.962 -19.605  81.074  1.00 65.22           C  
ATOM   2820  CD2 TYR A 409      14.985 -18.433  80.490  1.00 63.68           C  
ATOM   2821  CE1 TYR A 409      17.050 -18.878  82.254  1.00 65.40           C  
ATOM   2822  CE2 TYR A 409      15.064 -17.689  81.654  1.00 62.09           C  
ATOM   2823  CZ  TYR A 409      16.098 -17.910  82.543  1.00 64.58           C  
ATOM   2824  OH  TYR A 409      16.149 -17.168  83.690  1.00 67.06           O  
ATOM   2825  N   ALA A 410      16.240 -20.384  75.828  1.00 61.24           N  
ATOM   2826  CA  ALA A 410      15.904 -20.880  74.474  1.00 63.09           C  
ATOM   2827  C   ALA A 410      17.163 -21.431  73.785  1.00 67.64           C  
ATOM   2828  O   ALA A 410      17.098 -22.557  73.258  1.00 64.93           O  
ATOM   2829  CB  ALA A 410      15.264 -19.784  73.661  1.00 58.37           C  
ATOM   2830  N   TYR A 411      18.269 -20.683  73.800  1.00 69.51           N  
ATOM   2831  CA  TYR A 411      19.514 -21.036  73.063  1.00 74.07           C  
ATOM   2832  C   TYR A 411      20.256 -22.175  73.782  1.00 75.48           C  
ATOM   2833  O   TYR A 411      20.864 -23.014  73.076  1.00 73.83           O  
ATOM   2834  CB  TYR A 411      20.396 -19.799  72.848  1.00 78.15           C  
ATOM   2835  CG  TYR A 411      20.064 -19.026  71.597  1.00 84.34           C  
ATOM   2836  CD1 TYR A 411      19.101 -18.029  71.606  1.00 89.76           C  
ATOM   2837  CD2 TYR A 411      20.675 -19.325  70.388  1.00 89.52           C  
ATOM   2838  CE1 TYR A 411      18.765 -17.336  70.454  1.00 96.25           C  
ATOM   2839  CE2 TYR A 411      20.352 -18.642  69.227  1.00 92.19           C  
ATOM   2840  CZ  TYR A 411      19.392 -17.643  69.260  1.00 97.42           C  
ATOM   2841  OH  TYR A 411      19.067 -16.957  68.127  1.00102.64           O  
ATOM   2842  N   ARG A 412      20.199 -22.229  75.122  1.00 72.14           N  
ATOM   2843  CA  ARG A 412      21.161 -23.019  75.940  1.00 67.72           C  
ATOM   2844  C   ARG A 412      20.491 -24.199  76.666  1.00 63.04           C  
ATOM   2845  O   ARG A 412      21.246 -25.041  77.183  1.00 62.43           O  
ATOM   2846  CB  ARG A 412      21.875 -22.106  76.939  1.00 66.45           C  
ATOM   2847  CG  ARG A 412      22.767 -21.057  76.292  1.00 67.67           C  
ATOM   2848  CD  ARG A 412      23.815 -20.513  77.244  1.00 69.67           C  
ATOM   2849  NE  ARG A 412      25.169 -20.950  76.916  1.00 76.11           N  
ATOM   2850  CZ  ARG A 412      25.761 -22.058  77.371  1.00 81.69           C  
ATOM   2851  NH1 ARG A 412      25.125 -22.894  78.176  1.00 83.19           N  
ATOM   2852  NH2 ARG A 412      27.003 -22.328  77.011  1.00 86.37           N  
ATOM   2853  N   ILE A 413      19.155 -24.267  76.732  1.00 57.71           N  
ATOM   2854  CA  ILE A 413      18.428 -25.353  77.462  1.00 59.63           C  
ATOM   2855  C   ILE A 413      17.332 -25.928  76.557  1.00 62.84           C  
ATOM   2856  O   ILE A 413      16.330 -25.223  76.325  1.00 60.42           O  
ATOM   2857  CB  ILE A 413      17.852 -24.848  78.805  1.00 63.15           C  
ATOM   2858  CG1 ILE A 413      18.875 -24.058  79.629  1.00 63.51           C  
ATOM   2859  CG2 ILE A 413      17.274 -26.006  79.607  1.00 64.22           C  
ATOM   2860  CD1 ILE A 413      18.262 -23.189  80.703  1.00 59.92           C  
ATOM   2861  N   ARG A 414      17.497 -27.182  76.113  1.00 69.67           N  
ATOM   2862  CA  ARG A 414      16.583 -27.880  75.161  1.00 74.38           C  
ATOM   2863  C   ARG A 414      15.175 -27.995  75.755  1.00 70.77           C  
ATOM   2864  O   ARG A 414      14.202 -27.896  74.993  1.00 72.95           O  
ATOM   2865  CB  ARG A 414      17.111 -29.278  74.822  1.00 85.13           C  
ATOM   2866  CG  ARG A 414      18.262 -29.268  73.830  1.00 97.09           C  
ATOM   2867  CD  ARG A 414      18.439 -30.571  73.069  1.00100.01           C  
ATOM   2868  NE  ARG A 414      18.915 -31.651  73.919  1.00102.29           N  
ATOM   2869  CZ  ARG A 414      20.139 -31.733  74.438  1.00102.48           C  
ATOM   2870  NH1 ARG A 414      21.039 -30.789  74.207  1.00101.64           N  
ATOM   2871  NH2 ARG A 414      20.459 -32.767  75.195  1.00107.51           N  
ATOM   2872  N   GLU A 415      15.075 -28.236  77.058  1.00 69.89           N  
ATOM   2873  CA  GLU A 415      13.786 -28.491  77.745  1.00 68.68           C  
ATOM   2874  C   GLU A 415      12.881 -27.254  77.612  1.00 62.33           C  
ATOM   2875  O   GLU A 415      11.672 -27.436  77.405  1.00 56.36           O  
ATOM   2876  CB  GLU A 415      14.051 -28.895  79.196  1.00 71.81           C  
ATOM   2877  CG  GLU A 415      12.934 -29.724  79.804  1.00 79.18           C  
ATOM   2878  CD  GLU A 415      12.485 -30.908  78.964  1.00 79.95           C  
ATOM   2879  OE1 GLU A 415      13.353 -31.550  78.326  1.00 82.16           O  
ATOM   2880  OE2 GLU A 415      11.270 -31.178  78.942  1.00 77.55           O  
ATOM   2881  N   PHE A 416      13.452 -26.047  77.702  1.00 60.06           N  
ATOM   2882  CA  PHE A 416      12.728 -24.751  77.579  1.00 59.93           C  
ATOM   2883  C   PHE A 416      12.423 -24.478  76.103  1.00 62.21           C  
ATOM   2884  O   PHE A 416      11.273 -24.117  75.764  1.00 64.60           O  
ATOM   2885  CB  PHE A 416      13.548 -23.597  78.169  1.00 59.37           C  
ATOM   2886  CG  PHE A 416      13.237 -23.265  79.607  1.00 57.97           C  
ATOM   2887  CD1 PHE A 416      12.023 -22.693  79.955  1.00 54.00           C  
ATOM   2888  CD2 PHE A 416      14.166 -23.508  80.614  1.00 59.66           C  
ATOM   2889  CE1 PHE A 416      11.733 -22.397  81.278  1.00 53.33           C  
ATOM   2890  CE2 PHE A 416      13.880 -23.193  81.936  1.00 56.78           C  
ATOM   2891  CZ  PHE A 416      12.664 -22.638  82.264  1.00 55.00           C  
ATOM   2892  N   ARG A 417      13.449 -24.613  75.263  1.00 61.62           N  
ATOM   2893  CA  ARG A 417      13.375 -24.453  73.789  1.00 64.52           C  
ATOM   2894  C   ARG A 417      12.175 -25.252  73.259  1.00 62.81           C  
ATOM   2895  O   ARG A 417      11.315 -24.647  72.589  1.00 67.66           O  
ATOM   2896  CB  ARG A 417      14.706 -24.894  73.171  1.00 66.46           C  
ATOM   2897  CG  ARG A 417      14.713 -24.921  71.652  1.00 72.02           C  
ATOM   2898  CD  ARG A 417      16.089 -24.684  71.057  1.00 73.19           C  
ATOM   2899  NE  ARG A 417      16.980 -25.838  71.137  1.00 72.03           N  
ATOM   2900  CZ  ARG A 417      18.033 -25.952  71.946  1.00 72.71           C  
ATOM   2901  NH1 ARG A 417      18.352 -24.989  72.796  1.00 76.33           N  
ATOM   2902  NH2 ARG A 417      18.776 -27.041  71.895  1.00 77.05           N  
ATOM   2903  N   GLN A 418      12.096 -26.540  73.607  1.00 60.34           N  
ATOM   2904  CA  GLN A 418      11.047 -27.487  73.139  1.00 60.99           C  
ATOM   2905  C   GLN A 418       9.669 -26.997  73.589  1.00 58.90           C  
ATOM   2906  O   GLN A 418       8.729 -27.059  72.787  1.00 63.56           O  
ATOM   2907  CB  GLN A 418      11.327 -28.900  73.657  1.00 65.23           C  
ATOM   2908  CG  GLN A 418      12.328 -29.674  72.806  1.00 68.60           C  
ATOM   2909  CD  GLN A 418      13.012 -30.794  73.554  1.00 72.90           C  
ATOM   2910  OE1 GLN A 418      12.865 -30.943  74.766  1.00 79.59           O  
ATOM   2911  NE2 GLN A 418      13.788 -31.589  72.831  1.00 72.99           N  
ATOM   2912  N   THR A 419       9.544 -26.542  74.832  1.00 60.94           N  
ATOM   2913  CA  THR A 419       8.248 -26.100  75.408  1.00 57.20           C  
ATOM   2914  C   THR A 419       7.839 -24.770  74.783  1.00 58.29           C  
ATOM   2915  O   THR A 419       6.627 -24.550  74.643  1.00 60.23           O  
ATOM   2916  CB  THR A 419       8.310 -25.975  76.930  1.00 52.94           C  
ATOM   2917  OG1 THR A 419       9.051 -27.093  77.412  1.00 52.97           O  
ATOM   2918  CG2 THR A 419       6.937 -25.920  77.565  1.00 50.55           C  
ATOM   2919  N   PHE A 420       8.809 -23.904  74.470  1.00 58.79           N  
ATOM   2920  CA  PHE A 420       8.571 -22.623  73.757  1.00 62.23           C  
ATOM   2921  C   PHE A 420       7.956 -22.944  72.387  1.00 64.51           C  
ATOM   2922  O   PHE A 420       6.885 -22.391  72.071  1.00 66.24           O  
ATOM   2923  CB  PHE A 420       9.855 -21.791  73.642  1.00 61.00           C  
ATOM   2924  CG  PHE A 420      10.422 -21.232  74.930  1.00 58.18           C  
ATOM   2925  CD1 PHE A 420       9.716 -21.282  76.125  1.00 57.65           C  
ATOM   2926  CD2 PHE A 420      11.665 -20.612  74.934  1.00 56.65           C  
ATOM   2927  CE1 PHE A 420      10.247 -20.750  77.291  1.00 54.22           C  
ATOM   2928  CE2 PHE A 420      12.192 -20.075  76.098  1.00 54.12           C  
ATOM   2929  CZ  PHE A 420      11.483 -20.149  77.274  1.00 56.78           C  
ATOM   2930  N   ARG A 421       8.590 -23.838  71.619  1.00 70.06           N  
ATOM   2931  CA  ARG A 421       8.100 -24.287  70.283  1.00 76.44           C  
ATOM   2932  C   ARG A 421       6.627 -24.700  70.407  1.00 74.51           C  
ATOM   2933  O   ARG A 421       5.799 -24.171  69.639  1.00 68.65           O  
ATOM   2934  CB  ARG A 421       8.946 -25.445  69.734  1.00 83.30           C  
ATOM   2935  CG  ARG A 421      10.139 -25.016  68.889  1.00 85.74           C  
ATOM   2936  CD  ARG A 421      11.016 -26.192  68.494  1.00 90.77           C  
ATOM   2937  NE  ARG A 421      12.389 -25.791  68.189  1.00 97.64           N  
ATOM   2938  CZ  ARG A 421      13.439 -26.616  68.148  1.00101.43           C  
ATOM   2939  NH1 ARG A 421      13.290 -27.909  68.392  1.00100.24           N  
ATOM   2940  NH2 ARG A 421      14.641 -26.141  67.863  1.00102.35           N  
ATOM   2941  N   LYS A 422       6.319 -25.568  71.377  1.00 72.31           N  
ATOM   2942  CA  LYS A 422       4.991 -26.217  71.546  1.00 73.35           C  
ATOM   2943  C   LYS A 422       3.938 -25.188  71.983  1.00 69.11           C  
ATOM   2944  O   LYS A 422       2.802 -25.300  71.508  1.00 74.52           O  
ATOM   2945  CB  LYS A 422       5.093 -27.392  72.525  1.00 80.41           C  
ATOM   2946  CG  LYS A 422       5.785 -28.618  71.947  1.00 87.60           C  
ATOM   2947  CD  LYS A 422       5.881 -29.789  72.895  1.00 91.49           C  
ATOM   2948  CE  LYS A 422       6.636 -30.956  72.291  1.00 91.11           C  
ATOM   2949  NZ  LYS A 422       7.045 -31.934  73.325  1.00 96.85           N  
ATOM   2950  N   ILE A 423       4.286 -24.230  72.848  1.00 71.64           N  
ATOM   2951  CA  ILE A 423       3.354 -23.142  73.285  1.00 72.95           C  
ATOM   2952  C   ILE A 423       3.068 -22.221  72.088  1.00 75.59           C  
ATOM   2953  O   ILE A 423       1.916 -21.764  71.960  1.00 70.91           O  
ATOM   2954  CB  ILE A 423       3.904 -22.354  74.494  1.00 69.11           C  
ATOM   2955  CG1 ILE A 423       4.023 -23.231  75.742  1.00 70.80           C  
ATOM   2956  CG2 ILE A 423       3.055 -21.117  74.768  1.00 65.64           C  
ATOM   2957  CD1 ILE A 423       4.892 -22.637  76.829  1.00 69.91           C  
ATOM   2958  N   ILE A 424       4.081 -21.950  71.259  1.00 80.99           N  
ATOM   2959  CA  ILE A 424       3.972 -21.073  70.053  1.00 84.58           C  
ATOM   2960  C   ILE A 424       3.253 -21.843  68.930  1.00 86.39           C  
ATOM   2961  O   ILE A 424       2.291 -21.279  68.377  1.00 81.39           O  
ATOM   2962  CB  ILE A 424       5.360 -20.548  69.627  1.00 83.63           C  
ATOM   2963  CG1 ILE A 424       5.903 -19.527  70.631  1.00 84.11           C  
ATOM   2964  CG2 ILE A 424       5.320 -19.979  68.216  1.00 82.44           C  
ATOM   2965  CD1 ILE A 424       7.414 -19.493  70.721  1.00 82.96           C  
ATOM   2966  N   ARG A 425       3.685 -23.081  68.628  1.00 90.20           N  
ATOM   2967  CA  ARG A 425       3.137 -23.932  67.525  1.00 95.97           C  
ATOM   2968  C   ARG A 425       1.644 -24.220  67.762  1.00 97.38           C  
ATOM   2969  O   ARG A 425       0.883 -24.168  66.784  1.00110.26           O  
ATOM   2970  CB  ARG A 425       3.905 -25.253  67.376  1.00 96.03           C  
ATOM   2971  CG  ARG A 425       5.145 -25.172  66.491  1.00102.47           C  
ATOM   2972  CD  ARG A 425       5.441 -26.472  65.752  1.00107.83           C  
ATOM   2973  NE  ARG A 425       5.586 -27.625  66.642  1.00112.21           N  
ATOM   2974  CZ  ARG A 425       6.741 -28.209  66.979  1.00116.43           C  
ATOM   2975  NH1 ARG A 425       7.894 -27.758  66.508  1.00116.54           N  
ATOM   2976  NH2 ARG A 425       6.735 -29.250  67.797  1.00116.86           N  
ATOM   2977  N   SER A 426       1.242 -24.508  69.004  1.00 96.45           N  
ATOM   2978  CA  SER A 426      -0.147 -24.893  69.382  1.00101.15           C  
ATOM   2979  C   SER A 426      -1.012 -23.650  69.655  1.00102.92           C  
ATOM   2980  O   SER A 426      -2.153 -23.831  70.124  1.00100.00           O  
ATOM   2981  CB  SER A 426      -0.143 -25.830  70.567  1.00102.57           C  
ATOM   2982  OG  SER A 426       0.589 -27.013  70.275  1.00102.65           O  
ATOM   2983  N   HIS A 427      -0.488 -22.445  69.383  1.00112.99           N  
ATOM   2984  CA  HIS A 427      -1.232 -21.150  69.412  1.00118.89           C  
ATOM   2985  C   HIS A 427      -1.211 -20.485  68.026  1.00125.22           C  
ATOM   2986  O   HIS A 427      -2.144 -19.707  67.738  1.00125.46           O  
ATOM   2987  CB  HIS A 427      -0.677 -20.235  70.511  1.00114.43           C  
ATOM   2988  CG  HIS A 427      -1.252 -20.525  71.857  1.00118.14           C  
ATOM   2989  ND1 HIS A 427      -1.130 -21.766  72.464  1.00115.43           N  
ATOM   2990  CD2 HIS A 427      -1.970 -19.757  72.706  1.00116.64           C  
ATOM   2991  CE1 HIS A 427      -1.741 -21.745  73.630  1.00114.29           C  
ATOM   2992  NE2 HIS A 427      -2.265 -20.522  73.803  1.00118.22           N  
ATOM   2993  N   VAL A 428      -0.182 -20.768  67.217  1.00133.43           N  
ATOM   2994  CA  VAL A 428      -0.120 -20.442  65.759  1.00133.28           C  
ATOM   2995  C   VAL A 428      -0.975 -21.471  65.000  1.00139.24           C  
ATOM   2996  O   VAL A 428      -1.936 -21.046  64.329  1.00151.94           O  
ATOM   2997  CB  VAL A 428       1.339 -20.394  65.249  1.00128.84           C  
ATOM   2998  CG1 VAL A 428       1.436 -20.562  63.740  1.00128.76           C  
ATOM   2999  CG2 VAL A 428       2.042 -19.116  65.687  1.00122.65           C  
ATOM   3000  N   LEU A 429      -0.651 -22.767  65.122  1.00137.04           N  
ATOM   3001  CA  LEU A 429      -1.456 -23.901  64.576  1.00129.75           C  
ATOM   3002  C   LEU A 429      -2.515 -24.312  65.607  1.00128.18           C  
ATOM   3003  O   LEU A 429      -3.559 -23.680  65.755  1.00126.36           O  
ATOM   3004  CB  LEU A 429      -0.539 -25.086  64.246  1.00127.37           C  
ATOM   3005  CG  LEU A 429       0.601 -24.803  63.269  1.00128.29           C  
ATOM   3006  CD1 LEU A 429       1.567 -25.977  63.214  1.00128.30           C  
ATOM   3007  CD2 LEU A 429       0.063 -24.488  61.880  1.00126.32           C  
TER    3008      LEU A 429                                                      
HETATM 3009  C1  TEP A 500      17.999   3.219  88.485  1.00 41.46           C  
HETATM 3010  N1  TEP A 500      18.193   4.610  88.051  1.00 40.99           N  
HETATM 3011  C2  TEP A 500      17.124   5.181  87.354  1.00 42.02           C  
HETATM 3012  O2  TEP A 500      16.105   4.540  87.146  1.00 44.28           O  
HETATM 3013  N3  TEP A 500      17.268   6.485  86.926  1.00 44.19           N  
HETATM 3014  C3  TEP A 500      16.172   7.139  86.209  1.00 44.08           C  
HETATM 3015  C4  TEP A 500      18.436   7.157  87.193  1.00 46.32           C  
HETATM 3016  C5  TEP A 500      19.473   6.558  87.863  1.00 43.69           C  
HETATM 3017  C6  TEP A 500      19.425   5.222  88.336  1.00 42.06           C  
HETATM 3018  O6  TEP A 500      20.306   4.620  88.950  1.00 44.08           O  
HETATM 3019  N7  TEP A 500      20.458   7.517  87.932  1.00 45.48           N  
HETATM 3020  C8  TEP A 500      19.967   8.605  87.320  1.00 45.86           C  
HETATM 3021  N9  TEP A 500      18.728   8.438  86.845  1.00 45.30           N  
HETATM 3022  C1  OLA A 501       7.066   7.495 106.021  1.00 63.97           C  
HETATM 3023  O1  OLA A 501       7.752   8.516 105.785  1.00 68.17           O  
HETATM 3024  O2  OLA A 501       5.839   7.521 106.202  1.00 74.03           O  
HETATM 3025  C2  OLA A 501       7.772   6.157 106.107  1.00 60.87           C  
HETATM 3026  C3  OLA A 501       6.876   4.973 106.312  1.00 62.26           C  
HETATM 3027  C4  OLA A 501       7.571   3.839 107.052  1.00 66.32           C  
HETATM 3028  C5  OLA A 501       7.119   2.456 106.648  1.00 72.10           C  
HETATM 3029  C6  OLA A 501       7.418   1.366 107.664  1.00 71.11           C  
HETATM 3030  C7  OLA A 501       8.525   0.404 107.252  1.00 69.78           C  
HETATM 3031  C8  OLA A 501       8.884  -0.609 108.299  1.00 73.05           C  
HETATM 3032  C9  OLA A 501       8.679  -2.027 107.859  1.00 76.16           C  
HETATM 3033  C10 OLA A 501       9.456  -2.710 106.986  1.00 80.19           C  
HETATM 3034  C11 OLA A 501       9.245  -4.135 106.554  1.00 77.31           C  
HETATM 3035  C12 OLA A 501      10.432  -4.750 105.855  1.00 72.87           C  
HETATM 3036  C13 OLA A 501      11.491  -5.316 106.785  1.00 67.15           C  
HETATM 3037  C14 OLA A 501      12.197  -6.535 106.261  1.00 64.35           C  
HETATM 3038  C15 OLA A 501      13.421  -6.929 107.062  1.00 63.60           C  
HETATM 3039  C1  OLA A 502       2.741  15.407  83.071  1.00 79.69           C  
HETATM 3040  O1  OLA A 502       3.682  15.739  82.329  1.00 84.12           O  
HETATM 3041  O2  OLA A 502       2.202  16.182  83.880  1.00 88.97           O  
HETATM 3042  C2  OLA A 502       2.219  13.984  82.988  1.00 73.52           C  
HETATM 3043  C3  OLA A 502       3.109  13.020  82.267  1.00 70.86           C  
HETATM 3044  C4  OLA A 502       2.872  11.581  82.701  1.00 69.72           C  
HETATM 3045  C5  OLA A 502       3.388  10.541  81.740  1.00 66.31           C  
HETATM 3046  C6  OLA A 502       2.625   9.240  81.770  1.00 64.43           C  
HETATM 3047  C7  OLA A 502       3.359   8.082  81.106  1.00 63.47           C  
HETATM 3048  C8  OLA A 502       2.619   6.775  81.111  1.00 61.90           C  
HETATM 3049  C9  OLA A 502       3.400   5.664  80.477  1.00 60.99           C  
HETATM 3050  C10 OLA A 502       2.913   4.579  79.840  1.00 67.16           C  
HETATM 3051  C11 OLA A 502       1.472   4.225  79.626  1.00 68.56           C  
HETATM 3052  C12 OLA A 502       1.216   2.740  79.601  1.00 68.18           C  
HETATM 3053  C1  OLA A 503      18.997 -22.157  97.966  1.00 74.19           C  
HETATM 3054  O1  OLA A 503      18.292 -22.752  97.118  1.00 79.85           O  
HETATM 3055  O2  OLA A 503      19.810 -22.737  98.706  1.00 78.79           O  
HETATM 3056  C2  OLA A 503      18.847 -20.651  98.105  1.00 71.57           C  
HETATM 3057  C3  OLA A 503      19.945 -19.975  98.880  1.00 72.52           C  
HETATM 3058  C4  OLA A 503      19.517 -18.648  99.492  1.00 69.99           C  
HETATM 3059  C5  OLA A 503      19.772 -17.440  98.623  1.00 69.41           C  
HETATM 3060  C6  OLA A 503      19.470 -16.121  99.298  1.00 66.00           C  
HETATM 3061  C7  OLA A 503      19.435 -14.931  98.352  1.00 65.54           C  
HETATM 3062  C1  OLA A 504      30.907  14.110  77.073  1.00 82.94           C  
HETATM 3063  O1  OLA A 504      31.376  15.157  76.573  1.00 82.99           O  
HETATM 3064  O2  OLA A 504      29.982  14.102  77.900  1.00 89.31           O  
HETATM 3065  C2  OLA A 504      31.503  12.775  76.656  1.00 81.11           C  
HETATM 3066  C3  OLA A 504      30.528  11.630  76.596  1.00 80.63           C  
HETATM 3067  C4  OLA A 504      31.001  10.493  75.693  1.00 81.13           C  
HETATM 3068  C5  OLA A 504      30.689   9.099  76.203  1.00 79.44           C  
HETATM 3069  C6  OLA A 504      31.425   7.989  75.475  1.00 80.14           C  
HETATM 3070  C7  OLA A 504      30.708   6.641  75.462  1.00 79.64           C  
HETATM 3071  C8  OLA A 504      29.464   6.604  74.613  1.00 83.43           C  
HETATM 3072  C9  OLA A 504      29.120   5.245  74.070  1.00 81.64           C  
HETATM 3073  C10 OLA A 504      28.217   4.997  73.094  1.00 80.52           C  
HETATM 3074  C11 OLA A 504      27.848   3.655  72.534  1.00 74.80           C  
HETATM 3075  C1  OLA A 505      -3.536  16.470  82.985  1.00 85.62           C  
HETATM 3076  O1  OLA A 505      -4.474  17.148  82.495  1.00 79.26           O  
HETATM 3077  O2  OLA A 505      -2.567  16.971  83.615  1.00 88.69           O  
HETATM 3078  C2  OLA A 505      -3.583  14.958  82.807  1.00 78.36           C  
HETATM 3079  C3  OLA A 505      -2.398  14.191  83.331  1.00 69.29           C  
HETATM 3080  C4  OLA A 505      -2.320  12.786  82.752  1.00 67.99           C  
HETATM 3081  C5  OLA A 505      -1.980  11.700  83.747  1.00 65.52           C  
HETATM 3082  C6  OLA A 505      -1.305  10.492  83.139  1.00 64.44           C  
HETATM 3083  C7  OLA A 505      -2.019   9.168  83.375  1.00 67.28           C  
HETATM 3084  C8  OLA A 505      -1.564   8.059  82.468  1.00 69.21           C  
HETATM 3085  C9  OLA A 505      -1.664   6.689  83.071  1.00 67.02           C  
HETATM 3086  C10 OLA A 505      -2.313   5.634  82.534  1.00 66.39           C  
HETATM 3087  C11 OLA A 505      -2.393   4.264  83.142  1.00 66.71           C  
HETATM 3088  C12 OLA A 505      -3.771   3.657  83.172  1.00 58.74           C  
HETATM 3089  C13 OLA A 505      -3.808   2.163  82.836  1.00 59.05           C  
HETATM 3090  C14 OLA A 505      -4.411   1.281  83.913  1.00 58.96           C  
HETATM 3091  C15 OLA A 505      -4.286  -0.209  83.656  1.00 58.65           C  
HETATM 3092  C1  OLA A 506      -2.371  12.964  95.715  1.00 62.14           C  
HETATM 3093  O1  OLA A 506      -1.644  13.971  95.603  1.00 63.39           O  
HETATM 3094  O2  OLA A 506      -3.616  13.016  95.830  1.00 72.34           O  
HETATM 3095  C2  OLA A 506      -1.703  11.604  95.717  1.00 57.14           C  
HETATM 3096  C3  OLA A 506      -2.626  10.441  95.829  1.00 55.07           C  
HETATM 3097  C4  OLA A 506      -2.425   9.419  94.725  1.00 52.76           C  
HETATM 3098  C5  OLA A 506      -2.055   8.053  95.214  1.00 50.89           C  
HETATM 3099  C6  OLA A 506      -3.212   7.165  95.527  1.00 51.90           C  
HETATM 3100  C7  OLA A 506      -3.372   5.974  94.586  1.00 52.67           C  
HETATM 3101  C8  OLA A 506      -2.731   4.713  95.061  1.00 51.65           C  
HETATM 3102  C9  OLA A 506      -3.571   3.490  94.856  1.00 56.50           C  
HETATM 3103  C10 OLA A 506      -3.097   2.240  94.763  1.00 59.28           C  
HETATM 3104  C11 OLA A 506      -3.901   0.991  94.574  1.00 63.46           C  
HETATM 3105  C12 OLA A 506      -3.056  -0.216  94.288  1.00 67.30           C  
HETATM 3106  C13 OLA A 506      -3.745  -1.549  94.538  1.00 72.66           C  
HETATM 3107  C14 OLA A 506      -3.393  -2.637  93.536  1.00 76.72           C  
HETATM 3108  C15 OLA A 506      -3.419  -4.045  94.099  1.00 74.71           C  
HETATM 3109  C1  OLA A 507       7.068 -22.107  93.510  1.00 92.83           C  
HETATM 3110  O1  OLA A 507       5.975 -22.673  93.741  1.00 94.88           O  
HETATM 3111  O2  OLA A 507       8.137 -22.430  94.074  1.00103.43           O  
HETATM 3112  C2  OLA A 507       7.100 -20.976  92.484  1.00 82.04           C  
HETATM 3113  C3  OLA A 507       7.406 -19.611  93.046  1.00 75.45           C  
HETATM 3114  C4  OLA A 507       7.126 -18.478  92.069  1.00 67.79           C  
HETATM 3115  C5  OLA A 507       7.561 -17.120  92.565  1.00 63.46           C  
HETATM 3116  C6  OLA A 507       6.919 -15.944  91.857  1.00 64.51           C  
HETATM 3117  C7  OLA A 507       6.247 -14.937  92.787  1.00 67.36           C  
HETATM 3118  C8  OLA A 507       6.665 -13.503  92.603  1.00 65.97           C  
HETATM 3119  C9  OLA A 507       5.509 -12.587  92.346  1.00 65.11           C  
HETATM 3120  C10 OLA A 507       5.339 -11.325  92.795  1.00 66.75           C  
HETATM 3121  C11 OLA A 507       6.263 -10.527  93.664  1.00 64.77           C  
HETATM 3122  C12 OLA A 507       5.575  -9.410  94.409  1.00 65.53           C  
HETATM 3123  C13 OLA A 507       5.664  -8.046  93.742  1.00 59.58           C  
HETATM 3124  C1  OLA A 508       5.081 -22.928  88.974  1.00 85.39           C  
HETATM 3125  O1  OLA A 508       4.758 -24.087  89.325  1.00 80.58           O  
HETATM 3126  O2  OLA A 508       6.115 -22.354  89.368  1.00 93.65           O  
HETATM 3127  C2  OLA A 508       4.159 -22.181  88.020  1.00 82.88           C  
HETATM 3128  C3  OLA A 508       4.630 -20.820  87.567  1.00 74.21           C  
HETATM 3129  C4  OLA A 508       3.621 -19.724  87.873  1.00 71.02           C  
HETATM 3130  C5  OLA A 508       3.957 -18.374  87.277  1.00 69.09           C  
HETATM 3131  C6  OLA A 508       3.970 -17.233  88.276  1.00 66.33           C  
HETATM 3132  C7  OLA A 508       3.513 -15.894  87.711  1.00 66.30           C  
HETATM 3133  C8  OLA A 508       4.315 -14.721  88.174  1.00 66.09           C  
HETATM 3134  C9  OLA A 508       3.549 -13.435  88.167  1.00 69.97           C  
HETATM 3135  C10 OLA A 508       4.059 -12.210  87.965  1.00 73.54           C  
HETATM 3136  C11 OLA A 508       3.278 -10.931  87.974  1.00 80.85           C  
HETATM 3137  C12 OLA A 508       3.044 -10.382  89.362  1.00 87.40           C  
HETATM 3138  C13 OLA A 508       1.748  -9.587  89.525  1.00 90.44           C  
HETATM 3139  C14 OLA A 508       1.702  -8.688  90.752  1.00 86.61           C  
HETATM 3140  C15 OLA A 508       1.961  -9.398  92.060  1.00 82.86           C  
HETATM 3141  C1  OLA A 509      -4.080  10.409 100.161  1.00 93.41           C  
HETATM 3142  O1  OLA A 509      -4.709  10.633  99.101  1.00102.49           O  
HETATM 3143  O2  OLA A 509      -3.660  11.310 100.915  1.00 92.42           O  
HETATM 3144  C2  OLA A 509      -3.812   8.962 100.548  1.00 84.08           C  
HETATM 3145  C3  OLA A 509      -3.752   8.016  99.388  1.00 79.11           C  
HETATM 3146  C4  OLA A 509      -3.184   6.650  99.752  1.00 78.15           C  
HETATM 3147  C5  OLA A 509      -4.169   5.506  99.608  1.00 76.91           C  
HETATM 3148  C6  OLA A 509      -3.570   4.218  99.086  1.00 75.73           C  
HETATM 3149  C7  OLA A 509      -3.826   2.995  99.961  1.00 76.56           C  
HETATM 3150  C8  OLA A 509      -4.332   1.785  99.221  1.00 78.84           C  
HETATM 3151  C9  OLA A 509      -3.589   0.526  99.554  1.00 85.51           C  
HETATM 3152  C10 OLA A 509      -4.036  -0.742  99.424  1.00 89.92           C  
HETATM 3153  C11 OLA A 509      -5.380  -1.176  98.918  1.00 93.05           C  
HETATM 3154  C12 OLA A 509      -5.352  -1.668  97.501  1.00 90.52           C  
HETATM 3155  C13 OLA A 509      -6.380  -2.741  97.183  1.00 85.38           C  
HETATM 3156  C14 OLA A 509      -5.815  -4.139  97.105  1.00 87.63           C  
HETATM 3157  C15 OLA A 509      -5.438  -4.740  98.445  1.00 85.03           C  
HETATM 3158  C1  OLA A 510      23.332 -14.013  69.392  1.00 99.37           C  
HETATM 3159  O1  OLA A 510      23.265 -15.052  68.696  1.00 85.88           O  
HETATM 3160  O2  OLA A 510      23.675 -12.899  68.935  1.00 89.51           O  
HETATM 3161  C2  OLA A 510      23.014 -14.117  70.882  1.00105.79           C  
HETATM 3162  C3  OLA A 510      21.561 -13.938  71.259  1.00107.05           C  
HETATM 3163  C4  OLA A 510      21.352 -13.726  72.761  1.00 99.78           C  
HETATM 3164  C5  OLA A 510      21.486 -12.281  73.227  1.00 94.94           C  
HETATM 3165  C6  OLA A 510      20.210 -11.661  73.780  1.00 94.08           C  
HETATM 3166  C7  OLA A 510      19.146 -11.332  72.732  1.00 91.81           C  
HETATM 3167  C8  OLA A 510      18.300 -10.121  73.041  1.00 83.40           C  
HETATM 3168  C9  OLA A 510      19.041  -8.830  72.869  1.00 81.55           C  
HETATM 3169  C10 OLA A 510      18.515  -7.597  72.781  1.00 76.95           C  
HETATM 3170  C11 OLA A 510      17.062  -7.237  72.837  1.00 77.63           C  
HETATM 3171  C12 OLA A 510      16.801  -5.782  73.166  1.00 75.58           C  
HETATM 3172  C13 OLA A 510      16.070  -5.001  72.080  1.00 70.66           C  
HETATM 3173  C14 OLA A 510      15.715  -3.578  72.459  1.00 72.42           C  
HETATM 3174  C15 OLA A 510      14.525  -3.006  71.715  1.00 70.48           C  
HETATM 3175  C1  OLA A 511      18.062  12.232  72.783  1.00 94.63           C  
HETATM 3176  O1  OLA A 511      17.524  11.192  73.229  1.00 93.03           O  
HETATM 3177  O2  OLA A 511      18.239  13.265  73.465  1.00 86.77           O  
HETATM 3178  C2  OLA A 511      18.529  12.235  71.336  1.00 94.99           C  
HETATM 3179  C3  OLA A 511      18.482  10.892  70.664  1.00 96.59           C  
HETATM 3180  C4  OLA A 511      19.390   9.861  71.331  1.00 95.38           C  
HETATM 3181  C5  OLA A 511      18.715   8.548  71.671  1.00 88.49           C  
HETATM 3182  C6  OLA A 511      18.658   8.230  73.143  1.00 81.15           C  
HETATM 3183  C7  OLA A 511      17.661   7.135  73.507  1.00 80.69           C  
HETATM 3184  C8  OLA A 511      18.257   5.765  73.661  1.00 75.37           C  
HETATM 3185  C9  OLA A 511      18.238   4.953  72.403  1.00 73.80           C  
HETATM 3186  C10 OLA A 511      18.940   3.835  72.194  1.00 70.88           C  
HETATM 3187  C11 OLA A 511      18.936   3.023  70.941  1.00 75.00           C  
HETATM 3188  C12 OLA A 511      18.369   1.650  71.124  1.00 81.67           C  
HETATM 3189  C13 OLA A 511      19.017   0.853  72.243  1.00 84.16           C  
HETATM 3190  C14 OLA A 511      18.998  -0.647  72.045  1.00 84.35           C  
HETATM 3191  C15 OLA A 511      19.474  -1.440  73.245  1.00 80.85           C  
HETATM 3192  C16 OLA A 511      20.670  -0.848  73.955  1.00 74.24           C  
HETATM 3193  C1  OLA A 512       0.122  15.625  87.585  1.00 79.72           C  
HETATM 3194  O1  OLA A 512       1.003  16.305  88.148  1.00 83.59           O  
HETATM 3195  O2  OLA A 512      -0.666  16.083  86.732  1.00 92.73           O  
HETATM 3196  C2  OLA A 512       0.002  14.159  87.950  1.00 71.24           C  
HETATM 3197  C3  OLA A 512       0.340  13.219  86.844  1.00 65.28           C  
HETATM 3198  C4  OLA A 512       0.711  11.839  87.354  1.00 61.80           C  
HETATM 3199  C5  OLA A 512       0.957  10.823  86.272  1.00 57.69           C  
HETATM 3200  C6  OLA A 512       2.035   9.826  86.588  1.00 56.57           C  
HETATM 3201  C7  OLA A 512       1.528   8.485  87.094  1.00 56.44           C  
HETATM 3202  C8  OLA A 512       1.478   7.403  86.057  1.00 57.38           C  
HETATM 3203  C9  OLA A 512       2.468   6.316  86.303  1.00 55.85           C  
HETATM 3204  C10 OLA A 512       2.463   5.074  85.812  1.00 55.06           C  
HETATM 3205  C11 OLA A 512       1.466   4.431  84.913  1.00 55.92           C  
HETATM 3206  C12 OLA A 512       1.274   2.982  85.240  1.00 61.41           C  
HETATM 3207  C13 OLA A 512       0.488   2.196  84.206  1.00 66.06           C  
HETATM 3208  C14 OLA A 512       0.403   0.717  84.485  1.00 71.01           C  
HETATM 3209  C15 OLA A 512      -0.886   0.280  85.146  1.00 77.60           C  
HETATM 3210  C16 OLA A 512      -0.849  -1.110  85.756  1.00 82.44           C  
HETATM 3211  C17 OLA A 512      -1.048  -2.258  84.787  1.00 83.42           C  
HETATM 3212  C18 OLA A 512      -1.185  -3.604  85.468  1.00 80.64           C  
HETATM 3213  C1  CLR A 513       1.113  10.703  91.651  1.00 42.79           C  
HETATM 3214  C2  CLR A 513       1.460  12.167  91.934  1.00 41.75           C  
HETATM 3215  C3  CLR A 513       1.196  12.522  93.374  1.00 40.99           C  
HETATM 3216  C4  CLR A 513       1.950  11.593  94.299  1.00 40.89           C  
HETATM 3217  C5  CLR A 513       1.708  10.131  94.001  1.00 43.30           C  
HETATM 3218  C6  CLR A 513       1.386   9.293  94.978  1.00 44.46           C  
HETATM 3219  C7  CLR A 513       1.327   7.805  94.860  1.00 44.63           C  
HETATM 3220  C8  CLR A 513       1.662   7.283  93.461  1.00 47.51           C  
HETATM 3221  C9  CLR A 513       1.238   8.282  92.367  1.00 45.64           C  
HETATM 3222  C10 CLR A 513       1.867   9.695  92.549  1.00 44.46           C  
HETATM 3223  C11 CLR A 513       1.448   7.691  90.963  1.00 46.05           C  
HETATM 3224  C12 CLR A 513       0.793   6.316  90.778  1.00 46.42           C  
HETATM 3225  C13 CLR A 513       1.252   5.314  91.839  1.00 47.43           C  
HETATM 3226  C14 CLR A 513       0.953   5.960  93.208  1.00 49.25           C  
HETATM 3227  C15 CLR A 513       1.121   4.826  94.217  1.00 48.67           C  
HETATM 3228  C16 CLR A 513       0.654   3.574  93.441  1.00 49.10           C  
HETATM 3229  C17 CLR A 513       0.428   3.997  91.964  1.00 47.41           C  
HETATM 3230  C18 CLR A 513       2.738   4.973  91.656  1.00 47.73           C  
HETATM 3231  C19 CLR A 513       3.369   9.707  92.202  1.00 47.03           C  
HETATM 3232  C20 CLR A 513       0.691   2.837  90.990  1.00 50.47           C  
HETATM 3233  C21 CLR A 513       0.457   3.220  89.530  1.00 51.82           C  
HETATM 3234  C22 CLR A 513      -0.158   1.620  91.384  1.00 57.11           C  
HETATM 3235  C23 CLR A 513      -0.080   0.437  90.449  1.00 63.27           C  
HETATM 3236  C24 CLR A 513      -0.126  -0.894  91.166  1.00 69.56           C  
HETATM 3237  C25 CLR A 513      -1.014  -1.971  90.529  1.00 77.99           C  
HETATM 3238  C26 CLR A 513      -0.935  -1.948  89.008  1.00 76.56           C  
HETATM 3239  C27 CLR A 513      -0.656  -3.354  91.054  1.00 80.40           C  
HETATM 3240  O1  CLR A 513       1.619  13.864  93.639  1.00 45.30           O  
HETATM 3241  C1  CLR A 514      30.942  10.850  82.975  1.00 52.86           C  
HETATM 3242  C2  CLR A 514      30.848  12.376  83.002  1.00 51.52           C  
HETATM 3243  C3  CLR A 514      32.202  13.011  82.816  1.00 52.01           C  
HETATM 3244  C4  CLR A 514      32.862  12.518  81.538  1.00 49.37           C  
HETATM 3245  C5  CLR A 514      32.855  11.008  81.396  1.00 51.00           C  
HETATM 3246  C6  CLR A 514      33.944  10.356  81.012  1.00 51.85           C  
HETATM 3247  C7  CLR A 514      34.008   8.897  80.670  1.00 50.78           C  
HETATM 3248  C8  CLR A 514      32.641   8.220  80.650  1.00 52.20           C  
HETATM 3249  C9  CLR A 514      31.765   8.771  81.794  1.00 50.16           C  
HETATM 3250  C10 CLR A 514      31.529  10.302  81.659  1.00 53.11           C  
HETATM 3251  C11 CLR A 514      30.457   7.983  81.952  1.00 49.83           C  
HETATM 3252  C12 CLR A 514      30.631   6.461  81.999  1.00 48.16           C  
HETATM 3253  C13 CLR A 514      31.437   5.932  80.813  1.00 50.02           C  
HETATM 3254  C14 CLR A 514      32.773   6.707  80.796  1.00 53.99           C  
HETATM 3255  C15 CLR A 514      33.645   5.937  79.807  1.00 52.11           C  
HETATM 3256  C16 CLR A 514      33.184   4.471  79.966  1.00 52.14           C  
HETATM 3257  C17 CLR A 514      31.972   4.478  80.939  1.00 50.66           C  
HETATM 3258  C18 CLR A 514      30.643   6.087  79.506  1.00 52.38           C  
HETATM 3259  C19 CLR A 514      30.576  10.630  80.493  1.00 56.47           C  
HETATM 3260  C20 CLR A 514      31.014   3.293  80.711  1.00 50.50           C  
HETATM 3261  C21 CLR A 514      29.705   3.428  81.487  1.00 51.24           C  
HETATM 3262  C22 CLR A 514      31.703   1.971  81.078  1.00 49.53           C  
HETATM 3263  C23 CLR A 514      31.038   0.733  80.541  1.00 53.11           C  
HETATM 3264  C24 CLR A 514      31.631  -0.542  81.093  1.00 57.17           C  
HETATM 3265  C25 CLR A 514      30.697  -1.751  81.104  1.00 59.98           C  
HETATM 3266  C26 CLR A 514      30.971  -2.665  79.926  1.00 62.64           C  
HETATM 3267  C27 CLR A 514      30.805  -2.523  82.409  1.00 62.75           C  
HETATM 3268  O1  CLR A 514      32.046  14.437  82.772  1.00 55.12           O  
HETATM 3269  C1  CLR A 515      36.128   8.308  90.914  1.00 44.22           C  
HETATM 3270  C2  CLR A 515      36.305   9.826  90.870  1.00 43.96           C  
HETATM 3271  C3  CLR A 515      37.268  10.255  89.793  1.00 44.04           C  
HETATM 3272  C4  CLR A 515      36.870   9.684  88.443  1.00 45.54           C  
HETATM 3273  C5  CLR A 515      36.608   8.190  88.478  1.00 47.36           C  
HETATM 3274  C6  CLR A 515      37.164   7.386  87.581  1.00 47.54           C  
HETATM 3275  C7  CLR A 515      36.915   5.916  87.472  1.00 47.41           C  
HETATM 3276  C8  CLR A 515      35.726   5.455  88.305  1.00 47.02           C  
HETATM 3277  C9  CLR A 515      35.744   6.144  89.684  1.00 46.92           C  
HETATM 3278  C10 CLR A 515      35.666   7.694  89.574  1.00 45.70           C  
HETATM 3279  C11 CLR A 515      34.700   5.556  90.654  1.00 48.01           C  
HETATM 3280  C12 CLR A 515      34.673   4.020  90.705  1.00 48.49           C  
HETATM 3281  C13 CLR A 515      34.555   3.394  89.311  1.00 51.01           C  
HETATM 3282  C14 CLR A 515      35.745   3.945  88.496  1.00 47.89           C  
HETATM 3283  C15 CLR A 515      35.830   3.052  87.259  1.00 50.28           C  
HETATM 3284  C16 CLR A 515      35.254   1.698  87.714  1.00 53.18           C  
HETATM 3285  C17 CLR A 515      34.829   1.862  89.199  1.00 54.88           C  
HETATM 3286  C18 CLR A 515      33.188   3.736  88.682  1.00 50.08           C  
HETATM 3287  C19 CLR A 515      34.239   8.177  89.238  1.00 44.49           C  
HETATM 3288  C20 CLR A 515      33.754   0.834  89.606  1.00 55.53           C  
HETATM 3289  C21 CLR A 515      33.248   1.033  91.030  1.00 57.33           C  
HETATM 3290  C22 CLR A 515      34.301  -0.591  89.432  1.00 64.32           C  
HETATM 3291  C23 CLR A 515      33.318  -1.719  89.704  1.00 69.16           C  
HETATM 3292  C24 CLR A 515      33.440  -2.875  88.720  1.00 72.35           C  
HETATM 3293  C25 CLR A 515      33.789  -4.236  89.323  1.00 76.84           C  
HETATM 3294  C26 CLR A 515      33.824  -5.314  88.250  1.00 77.91           C  
HETATM 3295  C27 CLR A 515      35.114  -4.192  90.072  1.00 80.55           C  
HETATM 3296  O1  CLR A 515      37.279  11.688  89.735  1.00 47.19           O  
HETATM 3297  O   HOH A 601      24.934 -27.062  87.118  1.00 55.15           O  
HETATM 3298  O   HOH A 602      14.246   2.494  85.719  1.00 47.14           O  
HETATM 3299  O   HOH A 603      13.407 -12.114  91.419  1.00 40.29           O  
HETATM 3300  O   HOH A 604      24.321   3.359  91.449  1.00 41.90           O  
HETATM 3301  O   HOH A 605      15.829  -4.847  83.982  1.00 37.26           O  
HETATM 3302  O   HOH A 606      13.673   5.310  88.537  1.00 34.63           O  
HETATM 3303  O   HOH A 607      22.981   0.511  82.332  1.00 35.05           O  
HETATM 3304  O   HOH A 608      23.140 -16.812  88.876  1.00 38.35           O  
HETATM 3305  O   HOH A 609      13.811   7.453  83.186  1.00 44.40           O  
HETATM 3306  O   HOH A 610      11.405  20.516  92.366  1.00 41.12           O  
HETATM 3307  O   HOH A 611      19.910  -1.853  92.040  1.00 37.80           O  
HETATM 3308  O   HOH A 612      10.532   2.384  89.617  1.00 33.48           O  
HETATM 3309  O   HOH A 613      28.880  14.817  94.918  1.00 57.01           O  
HETATM 3310  O   HOH A 614      23.851   9.849  87.810  1.00 50.43           O  
HETATM 3311  O   HOH A 615      18.415  -2.622  94.284  1.00 47.53           O  
HETATM 3312  O   HOH A 616      27.791  12.164  85.506  1.00 55.29           O  
HETATM 3313  O   HOH A 617      24.325  12.063  98.040  1.00 40.20           O  
HETATM 3314  O   HOH A 618      30.239  14.043  86.784  1.00 46.80           O  
HETATM 3315  O   HOH A 619      17.386  12.725  87.258  1.00 41.56           O  
HETATM 3316  O   HOH A 620      21.050  -2.950  89.995  1.00 40.49           O  
HETATM 3317  O   HOH A 621      22.168  13.413  95.823  1.00 50.68           O  
HETATM 3318  O   HOH A 622      11.234   5.490  87.238  1.00 52.48           O  
HETATM 3319  O   HOH A 623      21.377  11.923 102.343  1.00 61.45           O  
HETATM 3320  O   HOH A 624      23.501 -40.120  86.770  1.00 74.43           O  
HETATM 3321  O   HOH A 625      27.860  10.650 101.765  1.00 55.61           O  
HETATM 3322  O   HOH A 626      19.049 -21.841  84.896  1.00 58.97           O  
CONECT  529 1177                                                                
CONECT  545 1086                                                                
CONECT  565 1221                                                                
CONECT 1086  545                                                                
CONECT 1177  529                                                                
CONECT 1221  565                                                                
CONECT 2593 2614                                                                
CONECT 2614 2593                                                                
CONECT 3009 3010                                                                
CONECT 3010 3009 3011 3017                                                      
CONECT 3011 3010 3012 3013                                                      
CONECT 3012 3011                                                                
CONECT 3013 3011 3014 3015                                                      
CONECT 3014 3013                                                                
CONECT 3015 3013 3016 3021                                                      
CONECT 3016 3015 3017 3019                                                      
CONECT 3017 3010 3016 3018                                                      
CONECT 3018 3017                                                                
CONECT 3019 3016 3020                                                           
CONECT 3020 3019 3021                                                           
CONECT 3021 3015 3020                                                           
CONECT 3022 3023 3024 3025                                                      
CONECT 3023 3022                                                                
CONECT 3024 3022                                                                
CONECT 3025 3022 3026                                                           
CONECT 3026 3025 3027                                                           
CONECT 3027 3026 3028                                                           
CONECT 3028 3027 3029                                                           
CONECT 3029 3028 3030                                                           
CONECT 3030 3029 3031                                                           
CONECT 3031 3030 3032                                                           
CONECT 3032 3031 3033                                                           
CONECT 3033 3032 3034                                                           
CONECT 3034 3033 3035                                                           
CONECT 3035 3034 3036                                                           
CONECT 3036 3035 3037                                                           
CONECT 3037 3036 3038                                                           
CONECT 3038 3037                                                                
CONECT 3039 3040 3041 3042                                                      
CONECT 3040 3039                                                                
CONECT 3041 3039                                                                
CONECT 3042 3039 3043                                                           
CONECT 3043 3042 3044                                                           
CONECT 3044 3043 3045                                                           
CONECT 3045 3044 3046                                                           
CONECT 3046 3045 3047                                                           
CONECT 3047 3046 3048                                                           
CONECT 3048 3047 3049                                                           
CONECT 3049 3048 3050                                                           
CONECT 3050 3049 3051                                                           
CONECT 3051 3050 3052                                                           
CONECT 3052 3051                                                                
CONECT 3053 3054 3055 3056                                                      
CONECT 3054 3053                                                                
CONECT 3055 3053                                                                
CONECT 3056 3053 3057                                                           
CONECT 3057 3056 3058                                                           
CONECT 3058 3057 3059                                                           
CONECT 3059 3058 3060                                                           
CONECT 3060 3059 3061                                                           
CONECT 3061 3060                                                                
CONECT 3062 3063 3064 3065                                                      
CONECT 3063 3062                                                                
CONECT 3064 3062                                                                
CONECT 3065 3062 3066                                                           
CONECT 3066 3065 3067                                                           
CONECT 3067 3066 3068                                                           
CONECT 3068 3067 3069                                                           
CONECT 3069 3068 3070                                                           
CONECT 3070 3069 3071                                                           
CONECT 3071 3070 3072                                                           
CONECT 3072 3071 3073                                                           
CONECT 3073 3072 3074                                                           
CONECT 3074 3073                                                                
CONECT 3075 3076 3077 3078                                                      
CONECT 3076 3075                                                                
CONECT 3077 3075                                                                
CONECT 3078 3075 3079                                                           
CONECT 3079 3078 3080                                                           
CONECT 3080 3079 3081                                                           
CONECT 3081 3080 3082                                                           
CONECT 3082 3081 3083                                                           
CONECT 3083 3082 3084                                                           
CONECT 3084 3083 3085                                                           
CONECT 3085 3084 3086                                                           
CONECT 3086 3085 3087                                                           
CONECT 3087 3086 3088                                                           
CONECT 3088 3087 3089                                                           
CONECT 3089 3088 3090                                                           
CONECT 3090 3089 3091                                                           
CONECT 3091 3090                                                                
CONECT 3092 3093 3094 3095                                                      
CONECT 3093 3092                                                                
CONECT 3094 3092                                                                
CONECT 3095 3092 3096                                                           
CONECT 3096 3095 3097                                                           
CONECT 3097 3096 3098                                                           
CONECT 3098 3097 3099                                                           
CONECT 3099 3098 3100                                                           
CONECT 3100 3099 3101                                                           
CONECT 3101 3100 3102                                                           
CONECT 3102 3101 3103                                                           
CONECT 3103 3102 3104                                                           
CONECT 3104 3103 3105                                                           
CONECT 3105 3104 3106                                                           
CONECT 3106 3105 3107                                                           
CONECT 3107 3106 3108                                                           
CONECT 3108 3107                                                                
CONECT 3109 3110 3111 3112                                                      
CONECT 3110 3109                                                                
CONECT 3111 3109                                                                
CONECT 3112 3109 3113                                                           
CONECT 3113 3112 3114                                                           
CONECT 3114 3113 3115                                                           
CONECT 3115 3114 3116                                                           
CONECT 3116 3115 3117                                                           
CONECT 3117 3116 3118                                                           
CONECT 3118 3117 3119                                                           
CONECT 3119 3118 3120                                                           
CONECT 3120 3119 3121                                                           
CONECT 3121 3120 3122                                                           
CONECT 3122 3121 3123                                                           
CONECT 3123 3122                                                                
CONECT 3124 3125 3126 3127                                                      
CONECT 3125 3124                                                                
CONECT 3126 3124                                                                
CONECT 3127 3124 3128                                                           
CONECT 3128 3127 3129                                                           
CONECT 3129 3128 3130                                                           
CONECT 3130 3129 3131                                                           
CONECT 3131 3130 3132                                                           
CONECT 3132 3131 3133                                                           
CONECT 3133 3132 3134                                                           
CONECT 3134 3133 3135                                                           
CONECT 3135 3134 3136                                                           
CONECT 3136 3135 3137                                                           
CONECT 3137 3136 3138                                                           
CONECT 3138 3137 3139                                                           
CONECT 3139 3138 3140                                                           
CONECT 3140 3139                                                                
CONECT 3141 3142 3143 3144                                                      
CONECT 3142 3141                                                                
CONECT 3143 3141                                                                
CONECT 3144 3141 3145                                                           
CONECT 3145 3144 3146                                                           
CONECT 3146 3145 3147                                                           
CONECT 3147 3146 3148                                                           
CONECT 3148 3147 3149                                                           
CONECT 3149 3148 3150                                                           
CONECT 3150 3149 3151                                                           
CONECT 3151 3150 3152                                                           
CONECT 3152 3151 3153                                                           
CONECT 3153 3152 3154                                                           
CONECT 3154 3153 3155                                                           
CONECT 3155 3154 3156                                                           
CONECT 3156 3155 3157                                                           
CONECT 3157 3156                                                                
CONECT 3158 3159 3160 3161                                                      
CONECT 3159 3158                                                                
CONECT 3160 3158                                                                
CONECT 3161 3158 3162                                                           
CONECT 3162 3161 3163                                                           
CONECT 3163 3162 3164                                                           
CONECT 3164 3163 3165                                                           
CONECT 3165 3164 3166                                                           
CONECT 3166 3165 3167                                                           
CONECT 3167 3166 3168                                                           
CONECT 3168 3167 3169                                                           
CONECT 3169 3168 3170                                                           
CONECT 3170 3169 3171                                                           
CONECT 3171 3170 3172                                                           
CONECT 3172 3171 3173                                                           
CONECT 3173 3172 3174                                                           
CONECT 3174 3173                                                                
CONECT 3175 3176 3177 3178                                                      
CONECT 3176 3175                                                                
CONECT 3177 3175                                                                
CONECT 3178 3175 3179                                                           
CONECT 3179 3178 3180                                                           
CONECT 3180 3179 3181                                                           
CONECT 3181 3180 3182                                                           
CONECT 3182 3181 3183                                                           
CONECT 3183 3182 3184                                                           
CONECT 3184 3183 3185                                                           
CONECT 3185 3184 3186                                                           
CONECT 3186 3185 3187                                                           
CONECT 3187 3186 3188                                                           
CONECT 3188 3187 3189                                                           
CONECT 3189 3188 3190                                                           
CONECT 3190 3189 3191                                                           
CONECT 3191 3190 3192                                                           
CONECT 3192 3191                                                                
CONECT 3193 3194 3195 3196                                                      
CONECT 3194 3193                                                                
CONECT 3195 3193                                                                
CONECT 3196 3193 3197                                                           
CONECT 3197 3196 3198                                                           
CONECT 3198 3197 3199                                                           
CONECT 3199 3198 3200                                                           
CONECT 3200 3199 3201                                                           
CONECT 3201 3200 3202                                                           
CONECT 3202 3201 3203                                                           
CONECT 3203 3202 3204                                                           
CONECT 3204 3203 3205                                                           
CONECT 3205 3204 3206                                                           
CONECT 3206 3205 3207                                                           
CONECT 3207 3206 3208                                                           
CONECT 3208 3207 3209                                                           
CONECT 3209 3208 3210                                                           
CONECT 3210 3209 3211                                                           
CONECT 3211 3210 3212                                                           
CONECT 3212 3211                                                                
CONECT 3213 3214 3222                                                           
CONECT 3214 3213 3215                                                           
CONECT 3215 3214 3216 3240                                                      
CONECT 3216 3215 3217                                                           
CONECT 3217 3216 3218 3222                                                      
CONECT 3218 3217 3219                                                           
CONECT 3219 3218 3220                                                           
CONECT 3220 3219 3221 3226                                                      
CONECT 3221 3220 3222 3223                                                      
CONECT 3222 3213 3217 3221 3231                                                 
CONECT 3223 3221 3224                                                           
CONECT 3224 3223 3225                                                           
CONECT 3225 3224 3226 3229 3230                                                 
CONECT 3226 3220 3225 3227                                                      
CONECT 3227 3226 3228                                                           
CONECT 3228 3227 3229                                                           
CONECT 3229 3225 3228 3232                                                      
CONECT 3230 3225                                                                
CONECT 3231 3222                                                                
CONECT 3232 3229 3233 3234                                                      
CONECT 3233 3232                                                                
CONECT 3234 3232 3235                                                           
CONECT 3235 3234 3236                                                           
CONECT 3236 3235 3237                                                           
CONECT 3237 3236 3238 3239                                                      
CONECT 3238 3237                                                                
CONECT 3239 3237                                                                
CONECT 3240 3215                                                                
CONECT 3241 3242 3250                                                           
CONECT 3242 3241 3243                                                           
CONECT 3243 3242 3244 3268                                                      
CONECT 3244 3243 3245                                                           
CONECT 3245 3244 3246 3250                                                      
CONECT 3246 3245 3247                                                           
CONECT 3247 3246 3248                                                           
CONECT 3248 3247 3249 3254                                                      
CONECT 3249 3248 3250 3251                                                      
CONECT 3250 3241 3245 3249 3259                                                 
CONECT 3251 3249 3252                                                           
CONECT 3252 3251 3253                                                           
CONECT 3253 3252 3254 3257 3258                                                 
CONECT 3254 3248 3253 3255                                                      
CONECT 3255 3254 3256                                                           
CONECT 3256 3255 3257                                                           
CONECT 3257 3253 3256 3260                                                      
CONECT 3258 3253                                                                
CONECT 3259 3250                                                                
CONECT 3260 3257 3261 3262                                                      
CONECT 3261 3260                                                                
CONECT 3262 3260 3263                                                           
CONECT 3263 3262 3264                                                           
CONECT 3264 3263 3265                                                           
CONECT 3265 3264 3266 3267                                                      
CONECT 3266 3265                                                                
CONECT 3267 3265                                                                
CONECT 3268 3243                                                                
CONECT 3269 3270 3278                                                           
CONECT 3270 3269 3271                                                           
CONECT 3271 3270 3272 3296                                                      
CONECT 3272 3271 3273                                                           
CONECT 3273 3272 3274 3278                                                      
CONECT 3274 3273 3275                                                           
CONECT 3275 3274 3276                                                           
CONECT 3276 3275 3277 3282                                                      
CONECT 3277 3276 3278 3279                                                      
CONECT 3278 3269 3273 3277 3287                                                 
CONECT 3279 3277 3280                                                           
CONECT 3280 3279 3281                                                           
CONECT 3281 3280 3282 3285 3286                                                 
CONECT 3282 3276 3281 3283                                                      
CONECT 3283 3282 3284                                                           
CONECT 3284 3283 3285                                                           
CONECT 3285 3281 3284 3288                                                      
CONECT 3286 3281                                                                
CONECT 3287 3278                                                                
CONECT 3288 3285 3289 3290                                                      
CONECT 3289 3288                                                                
CONECT 3290 3288 3291                                                           
CONECT 3291 3290 3292                                                           
CONECT 3292 3291 3293                                                           
CONECT 3293 3292 3294 3295                                                      
CONECT 3294 3293                                                                
CONECT 3295 3293                                                                
CONECT 3296 3271                                                                
MASTER      359    0   16   19    2    0    0    6 3321    1  296   34          
END