HEADER    MEMBRANE PROTEIN                        20-FEB-17   5UVI              
TITLE     SERIAL MILLISECOND CRYSTALLOGRAPHY OF MEMBRANE AND SOLUBLE PROTEIN    
TITLE    2 MICRO-CRYSTALS USING SYNCHROTRON RADIATION                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE   
COMPND   3 RECEPTOR A2A;                                                        
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CYTOCHROME B-562;                                           
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: ADORA2A, ADORA2, CYBC;                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, MEMBRANE PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.MARTIN-GARCIA,C.E.CONRAD,G.NELSON,N.STANDER,N.A.ZATSEPIN,J.ZOOK,  
AUTHOR   2 L.ZHU,J.GEIGER,E.CHUN,D.KISSICK,M.C.HILGART,C.OGATA,A.ISHCHENKO,     
AUTHOR   3 N.NAGARATNAM,S.ROY-CHOWDHURY,J.COE,G.SUBRAMANIAN,A.SCHAFFER,D.JAMES, 
AUTHOR   4 G.KETAWALA,N.VENUGOPALAN,S.XU,S.CORCORAN,D.FERGUSON,U.WEIERSTALL,    
AUTHOR   5 J.C.H.SPENCE,V.CHEREZOV,P.FROMME,R.F.FISCHETTI,W.LIU                 
REVDAT   6   13-APR-22 5UVI    1       REMARK                                   
REVDAT   5   04-DEC-19 5UVI    1       REMARK                                   
REVDAT   4   18-APR-18 5UVI    1       JRNL                                     
REVDAT   3   13-SEP-17 5UVI    1       REMARK                                   
REVDAT   2   12-JUL-17 5UVI    1       JRNL                                     
REVDAT   1   24-MAY-17 5UVI    0                                                
JRNL        AUTH   J.M.MARTIN-GARCIA,C.E.CONRAD,G.NELSON,N.STANDER,             
JRNL        AUTH 2 N.A.ZATSEPIN,J.ZOOK,L.ZHU,J.GEIGER,E.CHUN,D.KISSICK,         
JRNL        AUTH 3 M.C.HILGART,C.OGATA,A.ISHCHENKO,N.NAGARATNAM,                
JRNL        AUTH 4 S.ROY-CHOWDHURY,J.COE,G.SUBRAMANIAN,A.SCHAFFER,D.JAMES,      
JRNL        AUTH 5 G.KETWALA,N.VENUGOPALAN,S.XU,S.CORCORAN,D.FERGUSON,          
JRNL        AUTH 6 U.WEIERSTALL,J.C.H.SPENCE,V.CHEREZOV,P.FROMME,R.F.FISCHETTI, 
JRNL        AUTH 7 W.LIU                                                        
JRNL        TITL   SERIAL MILLISECOND CRYSTALLOGRAPHY OF MEMBRANE AND SOLUBLE   
JRNL        TITL 2 PROTEIN MICROCRYSTALS USING SYNCHROTRON RADIATION.           
JRNL        REF    IUCRJ                         V.   4   439 2017              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   28875031                                                     
JRNL        DOI    10.1107/S205225251700570X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 7702                           
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 14.500                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 555                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2978                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 152                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 107.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.46000                                              
REMARK   3    B22 (A**2) : -3.10000                                             
REMARK   3    B33 (A**2) : -0.36000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.619         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.683         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.863        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3216 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3195 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4388 ; 1.614 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7293 ; 1.068 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   387 ; 4.658 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   117 ;38.894 ;23.675       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   485 ;13.034 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;16.548 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   528 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3503 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   739 ; 0.003 ; 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):  1560 ; 4.728 ;10.786       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1559 ; 4.720 ;10.783       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1943 ; 7.718 ;16.171       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1944 ; 7.720 ;16.175       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1652 ; 4.266 ;11.117       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1653 ; 4.265 ;11.122       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2444 ; 7.173 ;16.565       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13130 ;12.834 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13130 ;12.826 ;  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 5UVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225536.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL 0.6.2                     
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL 0.6.2                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7702                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 142.6                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5K2B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.0, 32 % PEG    
REMARK 280  400, 75 MM SODIUM THOCYANATE, LIPIDIC CUBIC PHASE, TEMPERATURE      
REMARK 280  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       71.30000            
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       71.30000            
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       20.15000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       90.15000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       20.15000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       90.15000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.30000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       20.15000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       90.15000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.30000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       20.15000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       90.15000            
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     MET A   -24                                                      
REMARK 465     LYS A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ILE A   -21                                                      
REMARK 465     ILE A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     TYR A   -16                                                      
REMARK 465     ILE A   -15                                                      
REMARK 465     PHE A   -14                                                      
REMARK 465     CYS A   -13                                                      
REMARK 465     LEU A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     PHE A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     THR A  1044                                                      
REMARK 465     PRO A  1045                                                      
REMARK 465     PRO A  1046                                                      
REMARK 465     LYS A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     GLU A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     PRO A  1056                                                      
REMARK 465     GLU A  1057                                                      
REMARK 465     MET A  1058                                                      
REMARK 465     LYS A  1059                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     GLN A   310                                                      
REMARK 465     GLN A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     PHE A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 111    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 148    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 151    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 161    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 206    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A1015    CG   CD   CE   NZ                                   
REMARK 470     LYS A1019    CG   CD   CE   NZ                                   
REMARK 470     ASP A1021    CG   OD1  OD2                                       
REMARK 470     GLN A1025    CG   CD   OE1  NE2                                  
REMARK 470     ASP A1060    CG   OD1  OD2                                       
REMARK 470     ARG A1062    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1077    CG   CD   CE   NZ                                   
REMARK 470     ARG A 222    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 227    CG   CD   CE   NZ                                   
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS A    77     SG   CYS A   166              1.22            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A1106   C     GLU A 219   N       0.212                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  33   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ASN A  34   N   -  CA  -  CB  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    CYS A 166   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  58      -53.84   -124.00                                   
REMARK 500    ARG A 111       48.13   -110.00                                   
REMARK 500    ALA A 165      163.32    -47.74                                   
REMARK 500    CYS A 166       68.85   -114.02                                   
REMARK 500    TYR A1101      -60.69   -153.11                                   
REMARK 500    SER A 281       33.84    -99.99                                   
REMARK 500    VAL A 282      -20.30   -145.25                                   
REMARK 500    TYR A 288      -72.77    -58.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A 1205                                                       
REMARK 610     OLC A 1206                                                       
REMARK 610     OLA A 1207                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UVJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UVK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UVL   RELATED DB: PDB                                   
DBREF  5UVI A    2   208  UNP    P29274   AA2AR_HUMAN      2    208             
DBREF  5UVI A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  5UVI A  219   316  UNP    P29274   AA2AR_HUMAN    219    316             
SEQADV 5UVI MET A  -24  UNP  P29274              INITIATING METHIONINE          
SEQADV 5UVI LYS A  -23  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI THR A  -22  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ILE A  -21  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ILE A  -20  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ALA A  -19  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI LEU A  -18  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI SER A  -17  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI TYR A  -16  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ILE A  -15  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI PHE A  -14  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI CYS A  -13  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI LEU A  -12  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI VAL A  -11  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI PHE A  -10  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ALA A   -9  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ASP A   -8  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI TYR A   -7  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI LYS A   -6  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ASP A   -5  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ASP A   -4  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ASP A   -3  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ASP A   -2  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI GLY A   -1  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI ALA A    0  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI PRO A    1  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5UVI ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5UVI LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 5UVI HIS A  317  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 5UVI HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  447  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  447  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO          
SEQRES   3 A  447  PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU          
SEQRES   4 A  447  ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL          
SEQRES   5 A  447  CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL          
SEQRES   6 A  447  THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE          
SEQRES   7 A  447  ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE          
SEQRES   8 A  447  SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE          
SEQRES   9 A  447  ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER ILE          
SEQRES  10 A  447  PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA          
SEQRES  11 A  447  ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY          
SEQRES  12 A  447  THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL LEU          
SEQRES  13 A  447  SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN          
SEQRES  14 A  447  ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER GLN          
SEQRES  15 A  447  GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP          
SEQRES  16 A  447  VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE          
SEQRES  17 A  447  ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL          
SEQRES  18 A  447  TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU ALA          
SEQRES  19 A  447  ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU          
SEQRES  20 A  447  LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS          
SEQRES  21 A  447  ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA          
SEQRES  22 A  447  GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO          
SEQRES  23 A  447  ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP          
SEQRES  24 A  447  ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA          
SEQRES  25 A  447  ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU          
SEQRES  26 A  447  GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR          
SEQRES  27 A  447  LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS          
SEQRES  28 A  447  ALA ALA LYS SER LEU ALA ILE ILE VAL GLY LEU PHE ALA          
SEQRES  29 A  447  LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR          
SEQRES  30 A  447  PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU          
SEQRES  31 A  447  MET TYR LEU ALA ILE VAL LEU SER HIS THR ASN SER VAL          
SEQRES  32 A  447  VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE          
SEQRES  33 A  447  ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU          
SEQRES  34 A  447  ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS          
SEQRES  35 A  447  HIS HIS HIS HIS HIS                                          
HET    ZMA  A1201      25                                                       
HET    CLR  A1202      28                                                       
HET    CLR  A1203      28                                                       
HET    CLR  A1204      28                                                       
HET    OLC  A1205      16                                                       
HET    OLC  A1206      18                                                       
HET    OLA  A1207       9                                                       
HETNAM     ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,           
HETNAM   2 ZMA  5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL                               
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  ZMA    C16 H15 N7 O2                                                
FORMUL   3  CLR    3(C27 H46 O)                                                 
FORMUL   6  OLC    2(C21 H40 O4)                                                
FORMUL   8  OLA    C18 H34 O2                                                   
HELIX    1 AA1 PRO A    1  ASN A   34  1                                  34    
HELIX    2 AA2 SER A   35  GLN A   38  5                                   4    
HELIX    3 AA3 ASN A   39  LEU A   58  1                                  20    
HELIX    4 AA4 LEU A   58  THR A   68  1                                  11    
HELIX    5 AA5 ALA A   73  ILE A  108  1                                  36    
HELIX    6 AA6 THR A  117  LEU A  137  1                                  21    
HELIX    7 AA7 THR A  138  GLY A  142  5                                   5    
HELIX    8 AA8 LYS A  150  GLN A  157  1                                   8    
HELIX    9 AA9 LEU A  167  VAL A  172  1                                   6    
HELIX   10 AB1 PRO A  173  PHE A  180  1                                   8    
HELIX   11 AB2 VAL A  186  ALA A 1020  1                                  43    
HELIX   12 AB3 ASN A 1022  GLN A 1041  1                                  20    
HELIX   13 AB4 PHE A 1061  GLU A 1081  1                                  21    
HELIX   14 AB5 LYS A 1083  ALA A 1091  1                                   9    
HELIX   15 AB6 GLN A 1093  ASN A 1099  1                                   7    
HELIX   16 AB7 TYR A 1101  CYS A  259  1                                  47    
HELIX   17 AB8 PRO A  266  ASN A  280  1                                  15    
HELIX   18 AB9 VAL A  283  ILE A  292  1                                  10    
HELIX   19 AC1 ILE A  292  HIS A  306  1                                  15    
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  1.96  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  1.91  
SSBOND   3 CYS A  259    CYS A  262                          1555   1555  2.03  
CISPEP   1 HIS A  306    VAL A  307          0         1.30                     
SITE     1 AC1  9 PHE A 168  GLU A 169  MET A 177  TRP A 246                    
SITE     2 AC1  9 LEU A 249  HIS A 250  ASN A 253  LEU A 267                    
SITE     3 AC1  9 MET A 270                                                     
SITE     1 AC2  4 PHE A 255  PHE A 258  CYS A 259  CLR A1204                    
SITE     1 AC3  4 ILE A 251  CYS A 262  SER A 263  ALA A 265                    
SITE     1 AC4  6 LEU A  58  ALA A  72  ALA A  73  GLY A  76                    
SITE     2 AC4  6 ILE A  80  CLR A1202                                          
SITE     1 AC5  2 ILE A 125  TRP A 129                                          
SITE     1 AC6  2 SER A   6  TYR A 271                                          
SITE     1 AC7  2 SER A   7  THR A  11                                          
CRYST1   40.300  180.300  142.600  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      0.024814  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007013        0.00000                         
ATOM      1  N   ASP A  -2      20.950 -27.035   5.080  1.00136.42           N  
ATOM      2  CA  ASP A  -2      22.322 -27.042   4.476  1.00142.57           C  
ATOM      3  C   ASP A  -2      22.301 -26.523   3.013  1.00148.51           C  
ATOM      4  O   ASP A  -2      22.571 -27.265   2.051  1.00139.56           O  
ATOM      5  CB  ASP A  -2      22.950 -28.441   4.598  1.00137.91           C  
ATOM      6  CG  ASP A  -2      24.447 -28.430   4.373  1.00133.70           C  
ATOM      7  OD1 ASP A  -2      25.194 -28.091   5.312  1.00127.14           O  
ATOM      8  OD2 ASP A  -2      24.880 -28.768   3.258  1.00135.80           O  
ATOM      9  N   GLY A  -1      21.971 -25.229   2.891  1.00150.15           N  
ATOM     10  CA  GLY A  -1      21.760 -24.524   1.614  1.00144.98           C  
ATOM     11  C   GLY A  -1      22.903 -23.586   1.226  1.00142.78           C  
ATOM     12  O   GLY A  -1      24.060 -24.003   1.187  1.00142.66           O  
ATOM     13  N   ALA A   0      22.593 -22.317   0.940  1.00138.20           N  
ATOM     14  CA  ALA A   0      23.613 -21.350   0.484  1.00130.18           C  
ATOM     15  C   ALA A   0      24.730 -21.206   1.516  1.00131.88           C  
ATOM     16  O   ALA A   0      24.448 -21.182   2.711  1.00145.38           O  
ATOM     17  CB  ALA A   0      22.993 -19.988   0.209  1.00119.65           C  
ATOM     18  N   PRO A   1      25.999 -21.128   1.068  1.00131.46           N  
ATOM     19  CA  PRO A   1      27.079 -20.928   2.040  1.00128.09           C  
ATOM     20  C   PRO A   1      26.918 -19.594   2.766  1.00125.36           C  
ATOM     21  O   PRO A   1      26.649 -18.572   2.119  1.00118.79           O  
ATOM     22  CB  PRO A   1      28.354 -20.930   1.187  1.00129.20           C  
ATOM     23  CG  PRO A   1      27.963 -21.588  -0.087  1.00133.51           C  
ATOM     24  CD  PRO A   1      26.518 -21.238  -0.305  1.00134.95           C  
ATOM     25  N   PRO A   2      27.059 -19.596   4.102  1.00128.50           N  
ATOM     26  CA  PRO A   2      26.867 -18.342   4.834  1.00131.15           C  
ATOM     27  C   PRO A   2      27.827 -17.201   4.453  1.00126.23           C  
ATOM     28  O   PRO A   2      27.479 -16.037   4.660  1.00132.36           O  
ATOM     29  CB  PRO A   2      27.058 -18.758   6.301  1.00133.22           C  
ATOM     30  CG  PRO A   2      26.775 -20.219   6.324  1.00131.06           C  
ATOM     31  CD  PRO A   2      27.313 -20.721   5.021  1.00130.24           C  
ATOM     32  N   ILE A   3      29.000 -17.513   3.891  1.00115.40           N  
ATOM     33  CA  ILE A   3      29.944 -16.466   3.470  1.00110.69           C  
ATOM     34  C   ILE A   3      29.376 -15.524   2.388  1.00110.95           C  
ATOM     35  O   ILE A   3      29.827 -14.383   2.272  1.00118.75           O  
ATOM     36  CB  ILE A   3      31.297 -17.058   2.994  1.00108.03           C  
ATOM     37  CG1 ILE A   3      32.402 -15.984   2.952  1.00103.42           C  
ATOM     38  CG2 ILE A   3      31.148 -17.693   1.626  1.00112.37           C  
ATOM     39  CD1 ILE A   3      33.785 -16.531   2.672  1.00100.58           C  
ATOM     40  N   MET A   4      28.407 -15.990   1.599  1.00104.37           N  
ATOM     41  CA  MET A   4      27.853 -15.175   0.515  1.00 96.39           C  
ATOM     42  C   MET A   4      26.996 -14.063   1.090  1.00 89.15           C  
ATOM     43  O   MET A   4      27.196 -12.892   0.765  1.00 90.00           O  
ATOM     44  CB  MET A   4      27.079 -16.040  -0.478  1.00100.59           C  
ATOM     45  CG  MET A   4      27.974 -17.067  -1.168  1.00105.49           C  
ATOM     46  SD  MET A   4      27.238 -17.994  -2.536  1.00109.26           S  
ATOM     47  CE  MET A   4      27.049 -16.703  -3.764  1.00108.82           C  
ATOM     48  N   GLY A   5      26.068 -14.416   1.970  1.00 85.58           N  
ATOM     49  CA  GLY A   5      25.309 -13.406   2.712  1.00 91.80           C  
ATOM     50  C   GLY A   5      26.197 -12.459   3.519  1.00 93.25           C  
ATOM     51  O   GLY A   5      25.968 -11.239   3.555  1.00 89.33           O  
ATOM     52  N   SER A   6      27.211 -13.031   4.168  1.00 97.65           N  
ATOM     53  CA  SER A   6      28.160 -12.258   4.974  1.00100.54           C  
ATOM     54  C   SER A   6      28.880 -11.203   4.149  1.00 94.89           C  
ATOM     55  O   SER A   6      29.090 -10.088   4.623  1.00 96.92           O  
ATOM     56  CB  SER A   6      29.199 -13.166   5.645  1.00105.60           C  
ATOM     57  OG  SER A   6      28.590 -14.038   6.580  1.00118.90           O  
ATOM     58  N   SER A   7      29.249 -11.553   2.918  1.00 88.18           N  
ATOM     59  CA  SER A   7      29.987 -10.634   2.051  1.00 83.71           C  
ATOM     60  C   SER A   7      29.204  -9.370   1.753  1.00 77.96           C  
ATOM     61  O   SER A   7      29.761  -8.270   1.775  1.00 73.52           O  
ATOM     62  CB  SER A   7      30.378 -11.328   0.754  1.00 86.85           C  
ATOM     63  OG  SER A   7      31.205 -12.440   1.041  1.00 94.57           O  
ATOM     64  N   VAL A   8      27.905  -9.529   1.516  1.00 78.87           N  
ATOM     65  CA  VAL A   8      27.047  -8.380   1.238  1.00 80.22           C  
ATOM     66  C   VAL A   8      26.951  -7.517   2.481  1.00 75.75           C  
ATOM     67  O   VAL A   8      27.110  -6.308   2.402  1.00 69.85           O  
ATOM     68  CB  VAL A   8      25.614  -8.762   0.805  1.00 81.39           C  
ATOM     69  CG1 VAL A   8      24.843  -7.503   0.409  1.00 84.29           C  
ATOM     70  CG2 VAL A   8      25.634  -9.757  -0.348  1.00 81.70           C  
ATOM     71  N   TYR A   9      26.688  -8.152   3.617  1.00 78.47           N  
ATOM     72  CA  TYR A   9      26.521  -7.450   4.887  1.00 81.20           C  
ATOM     73  C   TYR A   9      27.777  -6.660   5.270  1.00 78.46           C  
ATOM     74  O   TYR A   9      27.681  -5.484   5.612  1.00 77.62           O  
ATOM     75  CB  TYR A   9      26.127  -8.439   6.003  1.00 85.34           C  
ATOM     76  CG  TYR A   9      26.269  -7.882   7.396  1.00 85.31           C  
ATOM     77  CD1 TYR A   9      25.424  -6.871   7.847  1.00 85.81           C  
ATOM     78  CD2 TYR A   9      27.265  -8.351   8.258  1.00 85.43           C  
ATOM     79  CE1 TYR A   9      25.560  -6.347   9.113  1.00 85.68           C  
ATOM     80  CE2 TYR A   9      27.407  -7.834   9.532  1.00 85.79           C  
ATOM     81  CZ  TYR A   9      26.555  -6.830   9.946  1.00 87.84           C  
ATOM     82  OH  TYR A   9      26.687  -6.305  11.200  1.00 99.77           O  
ATOM     83  N   ILE A  10      28.941  -7.301   5.193  1.00 76.01           N  
ATOM     84  CA  ILE A  10      30.197  -6.650   5.572  1.00 75.67           C  
ATOM     85  C   ILE A  10      30.512  -5.474   4.646  1.00 77.32           C  
ATOM     86  O   ILE A  10      30.895  -4.395   5.109  1.00 68.97           O  
ATOM     87  CB  ILE A  10      31.370  -7.653   5.613  1.00 76.93           C  
ATOM     88  CG1 ILE A  10      31.172  -8.622   6.780  1.00 82.34           C  
ATOM     89  CG2 ILE A  10      32.702  -6.934   5.791  1.00 77.50           C  
ATOM     90  CD1 ILE A  10      32.112  -9.811   6.789  1.00 82.90           C  
ATOM     91  N   THR A  11      30.334  -5.682   3.345  1.00 84.11           N  
ATOM     92  CA  THR A  11      30.577  -4.632   2.359  1.00 83.78           C  
ATOM     93  C   THR A  11      29.686  -3.416   2.608  1.00 81.56           C  
ATOM     94  O   THR A  11      30.166  -2.287   2.569  1.00 79.25           O  
ATOM     95  CB  THR A  11      30.362  -5.156   0.921  1.00 88.03           C  
ATOM     96  OG1 THR A  11      31.245  -6.260   0.678  1.00 86.81           O  
ATOM     97  CG2 THR A  11      30.601  -4.094  -0.105  1.00 91.02           C  
ATOM     98  N   VAL A  12      28.404  -3.655   2.880  1.00 82.93           N  
ATOM     99  CA  VAL A  12      27.459  -2.579   3.163  1.00 86.95           C  
ATOM    100  C   VAL A  12      27.852  -1.842   4.438  1.00 87.99           C  
ATOM    101  O   VAL A  12      27.828  -0.610   4.477  1.00 86.51           O  
ATOM    102  CB  VAL A  12      26.005  -3.110   3.292  1.00 90.26           C  
ATOM    103  CG1 VAL A  12      25.048  -2.025   3.774  1.00 89.68           C  
ATOM    104  CG2 VAL A  12      25.505  -3.647   1.958  1.00 95.68           C  
ATOM    105  N   GLU A  13      28.198  -2.597   5.479  1.00 86.99           N  
ATOM    106  CA  GLU A  13      28.574  -2.006   6.762  1.00 84.09           C  
ATOM    107  C   GLU A  13      29.777  -1.100   6.629  1.00 84.15           C  
ATOM    108  O   GLU A  13      29.805  -0.009   7.194  1.00 78.41           O  
ATOM    109  CB  GLU A  13      28.878  -3.094   7.778  1.00 83.88           C  
ATOM    110  CG  GLU A  13      27.647  -3.781   8.321  1.00 84.39           C  
ATOM    111  CD  GLU A  13      27.059  -3.057   9.502  1.00 87.69           C  
ATOM    112  OE1 GLU A  13      26.742  -1.856   9.383  1.00 87.27           O  
ATOM    113  OE2 GLU A  13      26.922  -3.693  10.563  1.00 95.48           O  
ATOM    114  N   LEU A  14      30.768  -1.556   5.876  1.00 86.06           N  
ATOM    115  CA  LEU A  14      31.965  -0.757   5.666  1.00 89.56           C  
ATOM    116  C   LEU A  14      31.679   0.484   4.815  1.00 86.28           C  
ATOM    117  O   LEU A  14      32.244   1.538   5.064  1.00 88.71           O  
ATOM    118  CB  LEU A  14      33.086  -1.613   5.076  1.00 90.93           C  
ATOM    119  CG  LEU A  14      33.555  -2.734   6.026  1.00 91.49           C  
ATOM    120  CD1 LEU A  14      34.669  -3.549   5.385  1.00 90.35           C  
ATOM    121  CD2 LEU A  14      33.999  -2.197   7.383  1.00 91.43           C  
ATOM    122  N   ALA A  15      30.784   0.374   3.842  1.00 82.90           N  
ATOM    123  CA  ALA A  15      30.359   1.541   3.074  1.00 82.31           C  
ATOM    124  C   ALA A  15      29.688   2.575   3.975  1.00 81.51           C  
ATOM    125  O   ALA A  15      29.883   3.781   3.801  1.00 82.98           O  
ATOM    126  CB  ALA A  15      29.422   1.127   1.953  1.00 83.95           C  
ATOM    127  N   ILE A  16      28.907   2.100   4.940  1.00 82.73           N  
ATOM    128  CA  ILE A  16      28.253   2.989   5.902  1.00 83.78           C  
ATOM    129  C   ILE A  16      29.282   3.648   6.807  1.00 84.61           C  
ATOM    130  O   ILE A  16      29.182   4.844   7.077  1.00 83.35           O  
ATOM    131  CB  ILE A  16      27.188   2.241   6.743  1.00 82.22           C  
ATOM    132  CG1 ILE A  16      26.011   1.875   5.847  1.00 83.96           C  
ATOM    133  CG2 ILE A  16      26.694   3.088   7.918  1.00 78.14           C  
ATOM    134  CD1 ILE A  16      25.092   0.819   6.425  1.00 85.33           C  
ATOM    135  N   ALA A  17      30.256   2.866   7.278  1.00 83.85           N  
ATOM    136  CA  ALA A  17      31.309   3.388   8.148  1.00 80.16           C  
ATOM    137  C   ALA A  17      32.070   4.529   7.479  1.00 80.93           C  
ATOM    138  O   ALA A  17      32.361   5.526   8.129  1.00 80.65           O  
ATOM    139  CB  ALA A  17      32.259   2.278   8.566  1.00 78.33           C  
ATOM    140  N   VAL A  18      32.356   4.396   6.182  1.00 81.86           N  
ATOM    141  CA  VAL A  18      33.077   5.430   5.435  1.00 83.24           C  
ATOM    142  C   VAL A  18      32.284   6.732   5.405  1.00 84.13           C  
ATOM    143  O   VAL A  18      32.839   7.809   5.657  1.00 81.44           O  
ATOM    144  CB  VAL A  18      33.414   4.970   3.998  1.00 86.36           C  
ATOM    145  CG1 VAL A  18      33.928   6.125   3.152  1.00 88.28           C  
ATOM    146  CG2 VAL A  18      34.461   3.866   4.021  1.00 87.53           C  
ATOM    147  N   LEU A  19      30.994   6.623   5.111  1.00 89.20           N  
ATOM    148  CA  LEU A  19      30.134   7.795   5.047  1.00 97.61           C  
ATOM    149  C   LEU A  19      29.886   8.424   6.436  1.00101.52           C  
ATOM    150  O   LEU A  19      29.831   9.646   6.558  1.00102.72           O  
ATOM    151  CB  LEU A  19      28.814   7.447   4.358  1.00 97.97           C  
ATOM    152  CG  LEU A  19      28.864   6.985   2.904  1.00 98.41           C  
ATOM    153  CD1 LEU A  19      27.503   6.461   2.467  1.00 98.39           C  
ATOM    154  CD2 LEU A  19      29.305   8.120   2.000  1.00 97.29           C  
ATOM    155  N   ALA A  20      29.751   7.602   7.478  1.00102.84           N  
ATOM    156  CA  ALA A  20      29.540   8.123   8.845  1.00 99.34           C  
ATOM    157  C   ALA A  20      30.752   8.892   9.339  1.00 95.79           C  
ATOM    158  O   ALA A  20      30.602   9.943   9.955  1.00 99.58           O  
ATOM    159  CB  ALA A  20      29.184   7.011   9.826  1.00 95.35           C  
ATOM    160  N   ILE A  21      31.947   8.391   9.042  1.00 94.73           N  
ATOM    161  CA  ILE A  21      33.177   9.067   9.460  1.00 99.33           C  
ATOM    162  C   ILE A  21      33.354  10.385   8.717  1.00 99.30           C  
ATOM    163  O   ILE A  21      33.564  11.436   9.340  1.00100.43           O  
ATOM    164  CB  ILE A  21      34.428   8.186   9.246  1.00100.85           C  
ATOM    165  CG1 ILE A  21      34.381   6.986  10.191  1.00102.71           C  
ATOM    166  CG2 ILE A  21      35.712   8.979   9.505  1.00101.18           C  
ATOM    167  CD1 ILE A  21      35.416   5.915   9.908  1.00103.55           C  
ATOM    168  N   LEU A  22      33.278  10.323   7.392  1.00 96.78           N  
ATOM    169  CA  LEU A  22      33.599  11.490   6.583  1.00 97.10           C  
ATOM    170  C   LEU A  22      32.619  12.627   6.831  1.00 95.86           C  
ATOM    171  O   LEU A  22      33.041  13.747   7.084  1.00 97.49           O  
ATOM    172  CB  LEU A  22      33.675  11.140   5.093  1.00 97.25           C  
ATOM    173  CG  LEU A  22      34.894  10.315   4.670  1.00 97.81           C  
ATOM    174  CD1 LEU A  22      34.833  10.023   3.184  1.00 98.21           C  
ATOM    175  CD2 LEU A  22      36.196  11.033   4.996  1.00100.44           C  
ATOM    176  N   GLY A  23      31.324  12.330   6.800  1.00 95.68           N  
ATOM    177  CA  GLY A  23      30.285  13.350   6.977  1.00 91.49           C  
ATOM    178  C   GLY A  23      30.347  14.049   8.314  1.00 88.00           C  
ATOM    179  O   GLY A  23      30.158  15.264   8.397  1.00 82.77           O  
ATOM    180  N   ASN A  24      30.627  13.278   9.360  1.00 90.97           N  
ATOM    181  CA  ASN A  24      30.649  13.816  10.717  1.00 92.01           C  
ATOM    182  C   ASN A  24      31.964  14.494  11.073  1.00 98.58           C  
ATOM    183  O   ASN A  24      31.964  15.414  11.888  1.00110.59           O  
ATOM    184  CB  ASN A  24      30.267  12.750  11.736  1.00 85.57           C  
ATOM    185  CG  ASN A  24      28.782  12.458  11.717  1.00 86.47           C  
ATOM    186  OD1 ASN A  24      27.979  13.258  12.191  1.00 85.03           O  
ATOM    187  ND2 ASN A  24      28.404  11.325  11.147  1.00 89.69           N  
ATOM    188  N   VAL A  25      33.069  14.069  10.466  1.00 93.21           N  
ATOM    189  CA  VAL A  25      34.304  14.839  10.555  1.00 86.84           C  
ATOM    190  C   VAL A  25      34.080  16.238   9.960  1.00 90.53           C  
ATOM    191  O   VAL A  25      34.574  17.223  10.501  1.00 97.82           O  
ATOM    192  CB  VAL A  25      35.468  14.118   9.853  1.00 85.02           C  
ATOM    193  CG1 VAL A  25      36.617  15.075   9.572  1.00 85.61           C  
ATOM    194  CG2 VAL A  25      35.964  12.955  10.701  1.00 84.54           C  
ATOM    195  N   LEU A  26      33.334  16.318   8.858  1.00 92.64           N  
ATOM    196  CA  LEU A  26      33.020  17.607   8.218  1.00 95.88           C  
ATOM    197  C   LEU A  26      32.241  18.545   9.141  1.00 92.51           C  
ATOM    198  O   LEU A  26      32.490  19.756   9.155  1.00 89.68           O  
ATOM    199  CB  LEU A  26      32.237  17.392   6.915  1.00101.70           C  
ATOM    200  CG  LEU A  26      31.946  18.587   6.001  1.00107.70           C  
ATOM    201  CD1 LEU A  26      33.230  19.249   5.525  1.00111.29           C  
ATOM    202  CD2 LEU A  26      31.090  18.142   4.824  1.00111.15           C  
ATOM    203  N   VAL A  27      31.314  17.981   9.913  1.00 92.32           N  
ATOM    204  CA  VAL A  27      30.525  18.764  10.868  1.00 95.27           C  
ATOM    205  C   VAL A  27      31.428  19.362  11.942  1.00 95.12           C  
ATOM    206  O   VAL A  27      31.353  20.554  12.225  1.00 99.45           O  
ATOM    207  CB  VAL A  27      29.414  17.921  11.521  1.00 95.99           C  
ATOM    208  CG1 VAL A  27      28.768  18.664  12.688  1.00 94.20           C  
ATOM    209  CG2 VAL A  27      28.369  17.551  10.478  1.00 96.56           C  
ATOM    210  N   CYS A  28      32.281  18.533  12.529  1.00 92.53           N  
ATOM    211  CA  CYS A  28      33.233  19.008  13.531  1.00 93.05           C  
ATOM    212  C   CYS A  28      34.181  20.064  12.976  1.00 93.18           C  
ATOM    213  O   CYS A  28      34.430  21.073  13.634  1.00100.08           O  
ATOM    214  CB  CYS A  28      34.039  17.845  14.104  1.00 92.26           C  
ATOM    215  SG  CYS A  28      32.995  16.574  14.837  1.00 91.32           S  
ATOM    216  N   TRP A  29      34.699  19.836  11.773  1.00 91.93           N  
ATOM    217  CA  TRP A  29      35.597  20.793  11.121  1.00 96.30           C  
ATOM    218  C   TRP A  29      34.883  22.140  10.934  1.00 93.44           C  
ATOM    219  O   TRP A  29      35.465  23.184  11.206  1.00 88.05           O  
ATOM    220  CB  TRP A  29      36.076  20.230   9.780  1.00103.09           C  
ATOM    221  CG  TRP A  29      37.237  20.932   9.122  1.00111.58           C  
ATOM    222  CD1 TRP A  29      37.750  22.167   9.414  1.00116.90           C  
ATOM    223  CD2 TRP A  29      38.000  20.437   8.012  1.00121.04           C  
ATOM    224  NE1 TRP A  29      38.791  22.464   8.568  1.00127.84           N  
ATOM    225  CE2 TRP A  29      38.969  21.419   7.697  1.00129.00           C  
ATOM    226  CE3 TRP A  29      37.964  19.253   7.256  1.00121.36           C  
ATOM    227  CZ2 TRP A  29      39.902  21.252   6.651  1.00128.65           C  
ATOM    228  CZ3 TRP A  29      38.889  19.086   6.221  1.00119.28           C  
ATOM    229  CH2 TRP A  29      39.843  20.085   5.928  1.00123.84           C  
ATOM    230  N   ALA A  30      33.623  22.106  10.501  1.00 93.30           N  
ATOM    231  CA  ALA A  30      32.846  23.329  10.282  1.00 94.05           C  
ATOM    232  C   ALA A  30      32.655  24.135  11.564  1.00 91.06           C  
ATOM    233  O   ALA A  30      32.820  25.352  11.566  1.00 89.40           O  
ATOM    234  CB  ALA A  30      31.492  23.007   9.655  1.00 96.88           C  
ATOM    235  N   VAL A  31      32.331  23.454  12.655  1.00 93.06           N  
ATOM    236  CA  VAL A  31      32.121  24.131  13.931  1.00 98.25           C  
ATOM    237  C   VAL A  31      33.448  24.693  14.463  1.00103.60           C  
ATOM    238  O   VAL A  31      33.476  25.790  15.029  1.00109.10           O  
ATOM    239  CB  VAL A  31      31.458  23.204  14.969  1.00 97.59           C  
ATOM    240  CG1 VAL A  31      31.334  23.900  16.316  1.00 99.15           C  
ATOM    241  CG2 VAL A  31      30.076  22.786  14.501  1.00 98.71           C  
ATOM    242  N   TRP A  32      34.539  23.955  14.269  1.00104.18           N  
ATOM    243  CA  TRP A  32      35.871  24.444  14.644  1.00108.60           C  
ATOM    244  C   TRP A  32      36.369  25.802  14.115  1.00114.42           C  
ATOM    245  O   TRP A  32      36.975  26.566  14.858  1.00113.28           O  
ATOM    246  CB  TRP A  32      36.922  23.340  14.439  1.00108.69           C  
ATOM    247  CG  TRP A  32      38.360  23.796  14.496  1.00114.19           C  
ATOM    248  CD1 TRP A  32      39.086  24.316  13.466  1.00120.72           C  
ATOM    249  CD2 TRP A  32      39.242  23.754  15.626  1.00117.89           C  
ATOM    250  NE1 TRP A  32      40.364  24.607  13.880  1.00121.10           N  
ATOM    251  CE2 TRP A  32      40.486  24.279  15.203  1.00118.73           C  
ATOM    252  CE3 TRP A  32      39.097  23.346  16.957  1.00120.94           C  
ATOM    253  CZ2 TRP A  32      41.580  24.400  16.061  1.00118.17           C  
ATOM    254  CZ3 TRP A  32      40.187  23.465  17.812  1.00119.33           C  
ATOM    255  CH2 TRP A  32      41.413  23.989  17.358  1.00119.81           C  
ATOM    256  N   LEU A  33      36.185  26.072  12.825  1.00117.12           N  
ATOM    257  CA  LEU A  33      36.612  27.356  12.251  1.00112.65           C  
ATOM    258  C   LEU A  33      35.595  28.488  11.722  1.00106.07           C  
ATOM    259  O   LEU A  33      35.868  29.480  11.045  1.00105.41           O  
ATOM    260  CB  LEU A  33      37.381  27.111  10.946  1.00118.83           C  
ATOM    261  CG  LEU A  33      36.604  26.430   9.819  1.00122.39           C  
ATOM    262  CD1 LEU A  33      35.722  27.433   9.090  1.00131.41           C  
ATOM    263  CD2 LEU A  33      37.554  25.742   8.849  1.00119.09           C  
ATOM    264  N   ASN A  34      34.374  28.260  12.181  1.00103.43           N  
ATOM    265  CA  ASN A  34      33.280  29.185  11.885  1.00105.21           C  
ATOM    266  C   ASN A  34      32.743  29.582  13.256  1.00108.55           C  
ATOM    267  O   ASN A  34      32.023  28.816  13.890  1.00116.07           O  
ATOM    268  CB  ASN A  34      32.134  28.795  10.938  1.00102.58           C  
ATOM    269  CG  ASN A  34      31.198  29.956  10.605  1.00103.06           C  
ATOM    270  OD1 ASN A  34      31.230  31.014  11.238  1.00100.81           O  
ATOM    271  ND2 ASN A  34      30.348  29.750   9.601  1.00107.74           N  
ATOM    272  N   SER A  35      33.092  30.786  13.700  1.00105.90           N  
ATOM    273  CA  SER A  35      32.655  31.285  14.998  1.00103.07           C  
ATOM    274  C   SER A  35      31.160  31.532  15.073  1.00103.98           C  
ATOM    275  O   SER A  35      30.619  31.555  16.168  1.00109.98           O  
ATOM    276  CB  SER A  35      33.394  32.566  15.368  1.00103.71           C  
ATOM    277  OG  SER A  35      34.728  32.271  15.716  1.00108.17           O  
ATOM    278  N   ASN A  36      30.490  31.714  13.936  1.00106.16           N  
ATOM    279  CA  ASN A  36      29.019  31.810  13.937  1.00111.29           C  
ATOM    280  C   ASN A  36      28.349  30.497  14.379  1.00109.73           C  
ATOM    281  O   ASN A  36      27.208  30.512  14.852  1.00108.23           O  
ATOM    282  CB  ASN A  36      28.470  32.250  12.560  1.00113.10           C  
ATOM    283  CG  ASN A  36      28.780  33.708  12.224  1.00114.31           C  
ATOM    284  OD1 ASN A  36      29.107  34.519  13.093  1.00122.12           O  
ATOM    285  ND2 ASN A  36      28.658  34.048  10.950  1.00114.53           N  
ATOM    286  N   LEU A  37      29.058  29.379  14.214  1.00108.61           N  
ATOM    287  CA  LEU A  37      28.574  28.060  14.623  1.00106.23           C  
ATOM    288  C   LEU A  37      29.027  27.652  16.029  1.00100.81           C  
ATOM    289  O   LEU A  37      28.657  26.584  16.503  1.00 97.93           O  
ATOM    290  CB  LEU A  37      29.043  26.997  13.617  1.00105.56           C  
ATOM    291  CG  LEU A  37      28.479  27.090  12.197  1.00102.39           C  
ATOM    292  CD1 LEU A  37      29.245  26.157  11.272  1.00106.56           C  
ATOM    293  CD2 LEU A  37      27.002  26.739  12.185  1.00100.70           C  
ATOM    294  N   GLN A  38      29.821  28.484  16.691  1.00 96.46           N  
ATOM    295  CA  GLN A  38      30.345  28.153  18.002  1.00 97.29           C  
ATOM    296  C   GLN A  38      29.410  28.720  19.054  1.00100.02           C  
ATOM    297  O   GLN A  38      29.658  29.769  19.638  1.00107.50           O  
ATOM    298  CB  GLN A  38      31.769  28.685  18.157  1.00100.57           C  
ATOM    299  CG  GLN A  38      32.750  28.043  17.194  1.00101.75           C  
ATOM    300  CD  GLN A  38      34.162  28.584  17.315  1.00104.63           C  
ATOM    301  OE1 GLN A  38      34.482  29.351  18.224  1.00102.00           O  
ATOM    302  NE2 GLN A  38      35.022  28.174  16.391  1.00107.41           N  
ATOM    303  N   ASN A  39      28.312  28.010  19.262  1.00105.21           N  
ATOM    304  CA  ASN A  39      27.341  28.325  20.312  1.00112.77           C  
ATOM    305  C   ASN A  39      27.042  27.045  21.069  1.00114.20           C  
ATOM    306  O   ASN A  39      27.467  25.961  20.670  1.00119.24           O  
ATOM    307  CB  ASN A  39      26.053  28.942  19.739  1.00116.26           C  
ATOM    308  CG  ASN A  39      25.538  28.204  18.510  1.00124.89           C  
ATOM    309  OD1 ASN A  39      25.154  27.040  18.587  1.00129.51           O  
ATOM    310  ND2 ASN A  39      25.532  28.881  17.364  1.00130.70           N  
ATOM    311  N   VAL A  40      26.316  27.180  22.169  1.00115.84           N  
ATOM    312  CA  VAL A  40      25.997  26.046  23.031  1.00109.31           C  
ATOM    313  C   VAL A  40      25.241  24.965  22.274  1.00104.31           C  
ATOM    314  O   VAL A  40      25.551  23.788  22.422  1.00110.29           O  
ATOM    315  CB  VAL A  40      25.195  26.498  24.273  1.00108.54           C  
ATOM    316  CG1 VAL A  40      24.436  25.341  24.907  1.00107.35           C  
ATOM    317  CG2 VAL A  40      26.126  27.154  25.282  1.00106.22           C  
ATOM    318  N   THR A  41      24.263  25.365  21.469  1.00 98.48           N  
ATOM    319  CA  THR A  41      23.458  24.406  20.719  1.00 95.28           C  
ATOM    320  C   THR A  41      24.329  23.481  19.857  1.00 98.34           C  
ATOM    321  O   THR A  41      24.111  22.274  19.814  1.00102.35           O  
ATOM    322  CB  THR A  41      22.420  25.123  19.835  1.00 88.78           C  
ATOM    323  OG1 THR A  41      21.868  26.230  20.557  1.00 83.98           O  
ATOM    324  CG2 THR A  41      21.304  24.169  19.418  1.00 86.31           C  
ATOM    325  N   ASN A  42      25.329  24.046  19.189  1.00 99.33           N  
ATOM    326  CA  ASN A  42      26.185  23.262  18.295  1.00102.47           C  
ATOM    327  C   ASN A  42      27.294  22.485  19.015  1.00102.15           C  
ATOM    328  O   ASN A  42      27.968  21.666  18.399  1.00105.98           O  
ATOM    329  CB  ASN A  42      26.782  24.148  17.197  1.00107.45           C  
ATOM    330  CG  ASN A  42      25.732  24.669  16.215  1.00109.84           C  
ATOM    331  OD1 ASN A  42      24.664  24.087  16.050  1.00103.74           O  
ATOM    332  ND2 ASN A  42      26.045  25.772  15.555  1.00118.54           N  
ATOM    333  N   TYR A  43      27.489  22.721  20.306  1.00103.62           N  
ATOM    334  CA  TYR A  43      28.369  21.851  21.089  1.00106.74           C  
ATOM    335  C   TYR A  43      27.722  20.500  21.300  1.00 97.50           C  
ATOM    336  O   TYR A  43      28.415  19.494  21.297  1.00 95.89           O  
ATOM    337  CB  TYR A  43      28.740  22.475  22.432  1.00121.04           C  
ATOM    338  CG  TYR A  43      29.444  23.811  22.330  1.00137.95           C  
ATOM    339  CD1 TYR A  43      30.059  24.227  21.138  1.00147.40           C  
ATOM    340  CD2 TYR A  43      29.525  24.658  23.437  1.00140.72           C  
ATOM    341  CE1 TYR A  43      30.703  25.447  21.056  1.00152.71           C  
ATOM    342  CE2 TYR A  43      30.173  25.878  23.356  1.00143.13           C  
ATOM    343  CZ  TYR A  43      30.752  26.267  22.165  1.00151.52           C  
ATOM    344  OH  TYR A  43      31.393  27.473  22.078  1.00171.46           O  
ATOM    345  N   PHE A  44      26.403  20.477  21.470  1.00 92.31           N  
ATOM    346  CA  PHE A  44      25.671  19.216  21.488  1.00 98.43           C  
ATOM    347  C   PHE A  44      25.628  18.565  20.098  1.00 98.43           C  
ATOM    348  O   PHE A  44      25.609  17.340  19.988  1.00 99.82           O  
ATOM    349  CB  PHE A  44      24.249  19.411  22.009  1.00104.05           C  
ATOM    350  CG  PHE A  44      24.176  19.902  23.432  1.00104.26           C  
ATOM    351  CD1 PHE A  44      24.549  19.079  24.496  1.00101.22           C  
ATOM    352  CD2 PHE A  44      23.699  21.175  23.714  1.00 99.19           C  
ATOM    353  CE1 PHE A  44      24.479  19.533  25.804  1.00 95.83           C  
ATOM    354  CE2 PHE A  44      23.604  21.624  25.021  1.00 93.43           C  
ATOM    355  CZ  PHE A  44      23.995  20.805  26.067  1.00 94.33           C  
ATOM    356  N   VAL A  45      25.596  19.379  19.045  1.00100.09           N  
ATOM    357  CA  VAL A  45      25.715  18.871  17.673  1.00100.41           C  
ATOM    358  C   VAL A  45      27.060  18.166  17.471  1.00102.26           C  
ATOM    359  O   VAL A  45      27.112  17.109  16.840  1.00111.30           O  
ATOM    360  CB  VAL A  45      25.522  19.995  16.627  1.00100.76           C  
ATOM    361  CG1 VAL A  45      25.912  19.539  15.224  1.00101.29           C  
ATOM    362  CG2 VAL A  45      24.077  20.474  16.635  1.00100.79           C  
ATOM    363  N   VAL A  46      28.129  18.743  18.018  1.00 97.16           N  
ATOM    364  CA  VAL A  46      29.459  18.136  17.939  1.00 93.77           C  
ATOM    365  C   VAL A  46      29.534  16.849  18.765  1.00 91.57           C  
ATOM    366  O   VAL A  46      30.107  15.857  18.319  1.00 92.36           O  
ATOM    367  CB  VAL A  46      30.566  19.117  18.369  1.00 95.33           C  
ATOM    368  CG1 VAL A  46      31.921  18.413  18.486  1.00 93.42           C  
ATOM    369  CG2 VAL A  46      30.662  20.259  17.368  1.00 98.52           C  
ATOM    370  N   SER A  47      28.956  16.856  19.958  1.00 89.56           N  
ATOM    371  CA  SER A  47      28.895  15.635  20.765  1.00 92.50           C  
ATOM    372  C   SER A  47      28.135  14.533  20.033  1.00 93.60           C  
ATOM    373  O   SER A  47      28.522  13.367  20.101  1.00 99.93           O  
ATOM    374  CB  SER A  47      28.248  15.906  22.127  1.00 95.27           C  
ATOM    375  OG  SER A  47      28.218  14.736  22.927  1.00 93.03           O  
ATOM    376  N   LEU A  48      27.062  14.908  19.336  1.00 92.44           N  
ATOM    377  CA  LEU A  48      26.279  13.962  18.542  1.00 89.08           C  
ATOM    378  C   LEU A  48      27.113  13.422  17.371  1.00 93.34           C  
ATOM    379  O   LEU A  48      27.073  12.224  17.077  1.00 95.68           O  
ATOM    380  CB  LEU A  48      24.987  14.627  18.049  1.00 84.27           C  
ATOM    381  CG  LEU A  48      23.971  13.788  17.268  1.00 84.75           C  
ATOM    382  CD1 LEU A  48      23.550  12.520  17.997  1.00 85.87           C  
ATOM    383  CD2 LEU A  48      22.751  14.635  16.961  1.00 82.30           C  
ATOM    384  N   ALA A  49      27.870  14.307  16.719  1.00 98.03           N  
ATOM    385  CA  ALA A  49      28.782  13.910  15.639  1.00 95.20           C  
ATOM    386  C   ALA A  49      29.889  12.981  16.144  1.00 92.03           C  
ATOM    387  O   ALA A  49      30.269  12.032  15.445  1.00 91.87           O  
ATOM    388  CB  ALA A  49      29.381  15.135  14.954  1.00 93.99           C  
ATOM    389  N   ALA A  50      30.390  13.234  17.355  1.00 84.30           N  
ATOM    390  CA  ALA A  50      31.426  12.385  17.940  1.00 86.02           C  
ATOM    391  C   ALA A  50      30.931  10.961  18.133  1.00 89.46           C  
ATOM    392  O   ALA A  50      31.664  10.001  17.872  1.00 92.81           O  
ATOM    393  CB  ALA A  50      31.909  12.950  19.259  1.00 87.89           C  
ATOM    394  N   ALA A  51      29.687  10.825  18.579  1.00 91.39           N  
ATOM    395  CA  ALA A  51      29.089   9.507  18.739  1.00 93.23           C  
ATOM    396  C   ALA A  51      28.938   8.792  17.392  1.00 96.49           C  
ATOM    397  O   ALA A  51      29.127   7.585  17.310  1.00 93.99           O  
ATOM    398  CB  ALA A  51      27.751   9.619  19.443  1.00 92.80           C  
ATOM    399  N   ASP A  52      28.612   9.541  16.342  1.00 98.23           N  
ATOM    400  CA  ASP A  52      28.444   8.966  15.011  1.00 93.95           C  
ATOM    401  C   ASP A  52      29.772   8.629  14.333  1.00 92.93           C  
ATOM    402  O   ASP A  52      29.837   7.687  13.539  1.00100.25           O  
ATOM    403  CB  ASP A  52      27.602   9.886  14.128  1.00 92.29           C  
ATOM    404  CG  ASP A  52      26.133   9.903  14.523  1.00 93.54           C  
ATOM    405  OD1 ASP A  52      25.650   8.930  15.154  1.00 91.32           O  
ATOM    406  OD2 ASP A  52      25.454  10.895  14.178  1.00 93.83           O  
ATOM    407  N   ILE A  53      30.828   9.380  14.632  1.00 88.03           N  
ATOM    408  CA  ILE A  53      32.168   8.997  14.165  1.00 90.32           C  
ATOM    409  C   ILE A  53      32.553   7.664  14.798  1.00 84.99           C  
ATOM    410  O   ILE A  53      33.059   6.772  14.116  1.00 84.26           O  
ATOM    411  CB  ILE A  53      33.245  10.068  14.472  1.00 94.44           C  
ATOM    412  CG1 ILE A  53      33.031  11.303  13.593  1.00 98.78           C  
ATOM    413  CG2 ILE A  53      34.651   9.533  14.208  1.00 89.43           C  
ATOM    414  CD1 ILE A  53      33.719  12.557  14.100  1.00 99.24           C  
ATOM    415  N   ALA A  54      32.295   7.539  16.097  1.00 81.64           N  
ATOM    416  CA  ALA A  54      32.605   6.319  16.831  1.00 81.85           C  
ATOM    417  C   ALA A  54      31.810   5.112  16.353  1.00 82.51           C  
ATOM    418  O   ALA A  54      32.258   3.984  16.516  1.00 82.18           O  
ATOM    419  CB  ALA A  54      32.386   6.528  18.315  1.00 85.14           C  
ATOM    420  N   VAL A  55      30.632   5.338  15.785  1.00 83.45           N  
ATOM    421  CA  VAL A  55      29.877   4.252  15.164  1.00 87.02           C  
ATOM    422  C   VAL A  55      30.663   3.657  13.986  1.00 86.71           C  
ATOM    423  O   VAL A  55      30.751   2.437  13.838  1.00 86.44           O  
ATOM    424  CB  VAL A  55      28.464   4.713  14.729  1.00 89.31           C  
ATOM    425  CG1 VAL A  55      27.811   3.719  13.775  1.00 88.78           C  
ATOM    426  CG2 VAL A  55      27.579   4.917  15.951  1.00 89.52           C  
ATOM    427  N   GLY A  56      31.229   4.525  13.156  1.00 85.97           N  
ATOM    428  CA  GLY A  56      32.014   4.081  12.011  1.00 83.87           C  
ATOM    429  C   GLY A  56      33.345   3.483  12.409  1.00 79.56           C  
ATOM    430  O   GLY A  56      33.763   2.478  11.844  1.00 85.11           O  
ATOM    431  N   VAL A  57      34.008   4.098  13.381  1.00 74.28           N  
ATOM    432  CA  VAL A  57      35.342   3.663  13.776  1.00 74.98           C  
ATOM    433  C   VAL A  57      35.316   2.425  14.675  1.00 80.06           C  
ATOM    434  O   VAL A  57      36.219   1.599  14.591  1.00 78.67           O  
ATOM    435  CB  VAL A  57      36.135   4.808  14.440  1.00 75.03           C  
ATOM    436  CG1 VAL A  57      37.475   4.314  14.974  1.00 74.22           C  
ATOM    437  CG2 VAL A  57      36.373   5.929  13.440  1.00 76.49           C  
ATOM    438  N   LEU A  58      34.294   2.289  15.522  1.00 90.04           N  
ATOM    439  CA  LEU A  58      34.262   1.216  16.542  1.00 89.90           C  
ATOM    440  C   LEU A  58      33.033   0.314  16.482  1.00 87.16           C  
ATOM    441  O   LEU A  58      33.179  -0.907  16.422  1.00 84.18           O  
ATOM    442  CB  LEU A  58      34.395   1.797  17.959  1.00 88.39           C  
ATOM    443  CG  LEU A  58      35.780   2.314  18.379  1.00 86.49           C  
ATOM    444  CD1 LEU A  58      35.640   3.061  19.698  1.00 90.10           C  
ATOM    445  CD2 LEU A  58      36.821   1.205  18.487  1.00 80.64           C  
ATOM    446  N   ALA A  59      31.837   0.897  16.516  1.00 86.57           N  
ATOM    447  CA  ALA A  59      30.600   0.097  16.612  1.00 94.54           C  
ATOM    448  C   ALA A  59      30.374  -0.848  15.428  1.00 92.90           C  
ATOM    449  O   ALA A  59      29.960  -1.994  15.620  1.00 84.13           O  
ATOM    450  CB  ALA A  59      29.383   0.992  16.793  1.00 96.58           C  
ATOM    451  N   ILE A  60      30.642  -0.351  14.221  1.00 95.15           N  
ATOM    452  CA  ILE A  60      30.481  -1.136  12.999  1.00 92.94           C  
ATOM    453  C   ILE A  60      31.516  -2.269  12.924  1.00 91.05           C  
ATOM    454  O   ILE A  60      31.141  -3.406  12.626  1.00 95.65           O  
ATOM    455  CB  ILE A  60      30.495  -0.243  11.734  1.00 93.78           C  
ATOM    456  CG1 ILE A  60      29.138   0.444  11.586  1.00 92.42           C  
ATOM    457  CG2 ILE A  60      30.814  -1.063  10.485  1.00 98.42           C  
ATOM    458  CD1 ILE A  60      29.069   1.488  10.491  1.00 94.08           C  
ATOM    459  N   PRO A  61      32.813  -1.972  13.179  1.00 82.88           N  
ATOM    460  CA  PRO A  61      33.753  -3.091  13.320  1.00 77.93           C  
ATOM    461  C   PRO A  61      33.368  -4.089  14.427  1.00 79.36           C  
ATOM    462  O   PRO A  61      33.567  -5.289  14.256  1.00 76.90           O  
ATOM    463  CB  PRO A  61      35.066  -2.395  13.663  1.00 77.31           C  
ATOM    464  CG  PRO A  61      34.960  -1.081  13.001  1.00 75.38           C  
ATOM    465  CD  PRO A  61      33.525  -0.679  13.135  1.00 78.25           C  
ATOM    466  N   PHE A  62      32.817  -3.601  15.538  1.00 80.62           N  
ATOM    467  CA  PHE A  62      32.293  -4.496  16.574  1.00 81.82           C  
ATOM    468  C   PHE A  62      31.119  -5.335  16.065  1.00 83.81           C  
ATOM    469  O   PHE A  62      31.067  -6.538  16.316  1.00 81.63           O  
ATOM    470  CB  PHE A  62      31.881  -3.703  17.816  1.00 82.63           C  
ATOM    471  CG  PHE A  62      33.037  -3.162  18.634  1.00 83.02           C  
ATOM    472  CD1 PHE A  62      34.375  -3.373  18.287  1.00 82.86           C  
ATOM    473  CD2 PHE A  62      32.772  -2.452  19.797  1.00 81.14           C  
ATOM    474  CE1 PHE A  62      35.398  -2.874  19.084  1.00 82.62           C  
ATOM    475  CE2 PHE A  62      33.793  -1.963  20.594  1.00 78.93           C  
ATOM    476  CZ  PHE A  62      35.107  -2.163  20.235  1.00 79.60           C  
ATOM    477  N   ALA A  63      30.196  -4.703  15.342  1.00 87.21           N  
ATOM    478  CA  ALA A  63      29.054  -5.410  14.753  1.00 86.57           C  
ATOM    479  C   ALA A  63      29.484  -6.527  13.797  1.00 85.02           C  
ATOM    480  O   ALA A  63      28.926  -7.620  13.833  1.00 82.31           O  
ATOM    481  CB  ALA A  63      28.133  -4.434  14.032  1.00 87.97           C  
ATOM    482  N   ILE A  64      30.467  -6.246  12.945  1.00 85.16           N  
ATOM    483  CA  ILE A  64      31.003  -7.254  12.022  1.00 83.88           C  
ATOM    484  C   ILE A  64      31.618  -8.408  12.821  1.00 79.76           C  
ATOM    485  O   ILE A  64      31.399  -9.566  12.503  1.00 75.49           O  
ATOM    486  CB  ILE A  64      32.055  -6.648  11.050  1.00 84.48           C  
ATOM    487  CG1 ILE A  64      31.400  -5.651  10.093  1.00 80.93           C  
ATOM    488  CG2 ILE A  64      32.756  -7.727  10.224  1.00 83.75           C  
ATOM    489  CD1 ILE A  64      32.396  -4.702   9.468  1.00 78.73           C  
ATOM    490  N   THR A  65      32.381  -8.084  13.859  1.00 81.88           N  
ATOM    491  CA  THR A  65      33.053  -9.096  14.665  1.00 83.44           C  
ATOM    492  C   THR A  65      32.057 -10.030  15.342  1.00 84.62           C  
ATOM    493  O   THR A  65      32.211 -11.246  15.290  1.00 87.41           O  
ATOM    494  CB  THR A  65      33.970  -8.433  15.704  1.00 84.94           C  
ATOM    495  OG1 THR A  65      34.999  -7.722  15.015  1.00 88.01           O  
ATOM    496  CG2 THR A  65      34.626  -9.454  16.610  1.00 90.04           C  
ATOM    497  N   ILE A  66      31.048  -9.453  15.987  1.00 88.33           N  
ATOM    498  CA  ILE A  66      30.038 -10.229  16.705  1.00 91.19           C  
ATOM    499  C   ILE A  66      29.180 -11.134  15.822  1.00 88.75           C  
ATOM    500  O   ILE A  66      28.649 -12.140  16.293  1.00 91.28           O  
ATOM    501  CB  ILE A  66      29.107  -9.311  17.522  1.00 98.18           C  
ATOM    502  CG1 ILE A  66      28.211 -10.144  18.442  1.00 99.78           C  
ATOM    503  CG2 ILE A  66      28.269  -8.442  16.597  1.00102.35           C  
ATOM    504  CD1 ILE A  66      27.736  -9.398  19.669  1.00102.15           C  
ATOM    505  N   SER A  67      29.042 -10.779  14.550  1.00 87.98           N  
ATOM    506  CA  SER A  67      28.229 -11.571  13.628  1.00 88.29           C  
ATOM    507  C   SER A  67      28.823 -12.944  13.331  1.00 83.16           C  
ATOM    508  O   SER A  67      28.092 -13.872  12.992  1.00 81.51           O  
ATOM    509  CB  SER A  67      27.987 -10.812  12.315  1.00 89.06           C  
ATOM    510  OG  SER A  67      29.186 -10.602  11.602  1.00 84.65           O  
ATOM    511  N   THR A  68      30.133 -13.079  13.494  1.00 82.97           N  
ATOM    512  CA  THR A  68      30.801 -14.336  13.206  1.00 87.57           C  
ATOM    513  C   THR A  68      30.548 -15.398  14.274  1.00 94.14           C  
ATOM    514  O   THR A  68      30.739 -16.584  14.018  1.00 93.83           O  
ATOM    515  CB  THR A  68      32.316 -14.141  13.062  1.00 87.22           C  
ATOM    516  OG1 THR A  68      32.868 -13.734  14.312  1.00 87.04           O  
ATOM    517  CG2 THR A  68      32.623 -13.086  12.018  1.00 88.67           C  
ATOM    518  N   GLY A  69      30.132 -14.980  15.468  1.00103.23           N  
ATOM    519  CA  GLY A  69      29.921 -15.911  16.575  1.00104.02           C  
ATOM    520  C   GLY A  69      31.221 -16.491  17.112  1.00104.67           C  
ATOM    521  O   GLY A  69      31.243 -17.619  17.610  1.00103.29           O  
ATOM    522  N   PHE A  70      32.304 -15.724  16.989  1.00104.17           N  
ATOM    523  CA  PHE A  70      33.632 -16.164  17.412  1.00107.44           C  
ATOM    524  C   PHE A  70      33.693 -16.496  18.897  1.00108.94           C  
ATOM    525  O   PHE A  70      32.926 -15.958  19.691  1.00105.17           O  
ATOM    526  CB  PHE A  70      34.698 -15.112  17.060  1.00107.74           C  
ATOM    527  CG  PHE A  70      34.738 -13.930  17.996  1.00107.54           C  
ATOM    528  CD1 PHE A  70      33.691 -13.014  18.037  1.00105.10           C  
ATOM    529  CD2 PHE A  70      35.835 -13.722  18.834  1.00110.70           C  
ATOM    530  CE1 PHE A  70      33.732 -11.920  18.890  1.00101.92           C  
ATOM    531  CE2 PHE A  70      35.884 -12.622  19.683  1.00108.68           C  
ATOM    532  CZ  PHE A  70      34.826 -11.724  19.715  1.00102.93           C  
ATOM    533  N   CYS A  71      34.610 -17.385  19.264  1.00105.71           N  
ATOM    534  CA  CYS A  71      34.771 -17.789  20.656  1.00102.95           C  
ATOM    535  C   CYS A  71      35.666 -16.814  21.413  1.00 97.61           C  
ATOM    536  O   CYS A  71      36.822 -16.603  21.044  1.00 97.56           O  
ATOM    537  CB  CYS A  71      35.347 -19.204  20.739  1.00110.59           C  
ATOM    538  SG  CYS A  71      34.428 -20.441  19.793  1.00120.75           S  
ATOM    539  N   ALA A  72      35.125 -16.222  22.473  1.00 95.91           N  
ATOM    540  CA  ALA A  72      35.873 -15.269  23.283  1.00100.39           C  
ATOM    541  C   ALA A  72      35.297 -15.170  24.691  1.00101.79           C  
ATOM    542  O   ALA A  72      34.292 -15.806  25.007  1.00 94.86           O  
ATOM    543  CB  ALA A  72      35.887 -13.902  22.616  1.00101.25           C  
ATOM    544  N   ALA A  73      35.941 -14.368  25.534  1.00107.80           N  
ATOM    545  CA  ALA A  73      35.494 -14.185  26.909  1.00111.23           C  
ATOM    546  C   ALA A  73      34.047 -13.704  26.960  1.00105.10           C  
ATOM    547  O   ALA A  73      33.607 -12.939  26.102  1.00 97.74           O  
ATOM    548  CB  ALA A  73      36.405 -13.209  27.637  1.00120.54           C  
ATOM    549  N   CYS A  74      33.314 -14.158  27.971  1.00 99.01           N  
ATOM    550  CA  CYS A  74      31.916 -13.775  28.136  1.00 99.55           C  
ATOM    551  C   CYS A  74      31.778 -12.272  28.356  1.00101.88           C  
ATOM    552  O   CYS A  74      30.850 -11.644  27.846  1.00104.59           O  
ATOM    553  CB  CYS A  74      31.286 -14.538  29.303  1.00100.45           C  
ATOM    554  SG  CYS A  74      29.482 -14.637  29.242  1.00 99.93           S  
ATOM    555  N   HIS A  75      32.706 -11.703  29.118  1.00108.56           N  
ATOM    556  CA  HIS A  75      32.689 -10.267  29.408  1.00109.71           C  
ATOM    557  C   HIS A  75      33.391  -9.462  28.329  1.00103.77           C  
ATOM    558  O   HIS A  75      33.058  -8.303  28.137  1.00100.62           O  
ATOM    559  CB  HIS A  75      33.279  -9.975  30.783  1.00115.18           C  
ATOM    560  CG  HIS A  75      32.371 -10.359  31.908  1.00121.38           C  
ATOM    561  ND1 HIS A  75      32.043 -11.669  32.189  1.00125.91           N  
ATOM    562  CD2 HIS A  75      31.714  -9.605  32.818  1.00124.06           C  
ATOM    563  CE1 HIS A  75      31.225 -11.705  33.224  1.00128.80           C  
ATOM    564  NE2 HIS A  75      31.012 -10.466  33.627  1.00130.08           N  
ATOM    565  N   GLY A  76      34.182 -10.158  27.531  1.00 99.86           N  
ATOM    566  CA  GLY A  76      34.797  -9.558  26.379  1.00 96.89           C  
ATOM    567  C   GLY A  76      33.679  -9.413  25.360  1.00 95.76           C  
ATOM    568  O   GLY A  76      33.505  -8.356  24.783  1.00 93.05           O  
ATOM    569  N   CYS A  77      32.901 -10.466  25.140  1.00 94.48           N  
ATOM    570  CA  CYS A  77      31.808 -10.387  24.175  1.00 91.95           C  
ATOM    571  C   CYS A  77      30.871  -9.279  24.569  1.00 89.40           C  
ATOM    572  O   CYS A  77      30.500  -8.457  23.754  1.00 90.46           O  
ATOM    573  CB  CYS A  77      31.033 -11.701  24.071  1.00 93.00           C  
ATOM    574  SG  CYS A  77      29.800 -11.787  22.752  1.00 93.77           S  
ATOM    575  N   LEU A  78      30.484  -9.250  25.829  1.00 89.27           N  
ATOM    576  CA  LEU A  78      29.571  -8.232  26.284  1.00 89.30           C  
ATOM    577  C   LEU A  78      30.023  -6.856  25.870  1.00 87.71           C  
ATOM    578  O   LEU A  78      29.247  -6.087  25.344  1.00 84.78           O  
ATOM    579  CB  LEU A  78      29.420  -8.291  27.792  1.00 94.19           C  
ATOM    580  CG  LEU A  78      28.368  -9.257  28.316  1.00 95.95           C  
ATOM    581  CD1 LEU A  78      27.969  -8.904  29.727  1.00100.64           C  
ATOM    582  CD2 LEU A  78      27.149  -9.247  27.434  1.00 93.32           C  
ATOM    583  N   PHE A  79      31.281  -6.540  26.103  1.00 90.28           N  
ATOM    584  CA  PHE A  79      31.779  -5.199  25.753  1.00 96.66           C  
ATOM    585  C   PHE A  79      31.645  -4.938  24.253  1.00101.05           C  
ATOM    586  O   PHE A  79      31.227  -3.854  23.831  1.00106.79           O  
ATOM    587  CB  PHE A  79      33.237  -4.994  26.188  1.00 92.21           C  
ATOM    588  CG  PHE A  79      33.749  -3.601  25.937  1.00 88.00           C  
ATOM    589  CD1 PHE A  79      33.532  -2.592  26.862  1.00 86.83           C  
ATOM    590  CD2 PHE A  79      34.426  -3.294  24.765  1.00 88.11           C  
ATOM    591  CE1 PHE A  79      33.990  -1.305  26.629  1.00 86.93           C  
ATOM    592  CE2 PHE A  79      34.885  -2.009  24.526  1.00 88.41           C  
ATOM    593  CZ  PHE A  79      34.670  -1.013  25.461  1.00 87.09           C  
ATOM    594  N   ILE A  80      32.006  -5.933  23.456  1.00 97.07           N  
ATOM    595  CA  ILE A  80      31.814  -5.848  22.020  1.00 95.62           C  
ATOM    596  C   ILE A  80      30.328  -5.670  21.689  1.00 85.68           C  
ATOM    597  O   ILE A  80      29.983  -4.852  20.848  1.00 89.39           O  
ATOM    598  CB  ILE A  80      32.419  -7.086  21.311  1.00102.60           C  
ATOM    599  CG1 ILE A  80      33.951  -7.054  21.405  1.00101.94           C  
ATOM    600  CG2 ILE A  80      31.980  -7.183  19.850  1.00104.50           C  
ATOM    601  CD1 ILE A  80      34.601  -5.893  20.675  1.00106.04           C  
ATOM    602  N   ALA A  81      29.461  -6.420  22.359  1.00 77.86           N  
ATOM    603  CA  ALA A  81      28.027  -6.391  22.061  1.00 76.82           C  
ATOM    604  C   ALA A  81      27.336  -5.097  22.483  1.00 80.67           C  
ATOM    605  O   ALA A  81      26.417  -4.634  21.802  1.00 76.87           O  
ATOM    606  CB  ALA A  81      27.331  -7.567  22.721  1.00 76.59           C  
ATOM    607  N   CYS A  82      27.780  -4.523  23.600  1.00 83.85           N  
ATOM    608  CA  CYS A  82      27.046  -3.448  24.262  1.00 82.62           C  
ATOM    609  C   CYS A  82      27.592  -2.056  24.007  1.00 77.78           C  
ATOM    610  O   CYS A  82      26.942  -1.081  24.363  1.00 78.37           O  
ATOM    611  CB  CYS A  82      27.022  -3.698  25.767  1.00 88.94           C  
ATOM    612  SG  CYS A  82      26.025  -5.121  26.275  1.00102.55           S  
ATOM    613  N   PHE A  83      28.766  -1.941  23.396  1.00 74.47           N  
ATOM    614  CA  PHE A  83      29.380  -0.633  23.218  1.00 72.23           C  
ATOM    615  C   PHE A  83      28.531   0.284  22.362  1.00 70.42           C  
ATOM    616  O   PHE A  83      28.514   1.488  22.589  1.00 70.28           O  
ATOM    617  CB  PHE A  83      30.779  -0.753  22.629  1.00 73.47           C  
ATOM    618  CG  PHE A  83      31.487   0.561  22.496  1.00 76.24           C  
ATOM    619  CD1 PHE A  83      31.900   1.262  23.625  1.00 80.52           C  
ATOM    620  CD2 PHE A  83      31.732   1.109  21.246  1.00 81.16           C  
ATOM    621  CE1 PHE A  83      32.556   2.481  23.512  1.00 82.56           C  
ATOM    622  CE2 PHE A  83      32.390   2.329  21.120  1.00 86.11           C  
ATOM    623  CZ  PHE A  83      32.807   3.015  22.256  1.00 85.99           C  
ATOM    624  N   VAL A  84      27.831  -0.288  21.387  1.00 75.21           N  
ATOM    625  CA  VAL A  84      26.973   0.491  20.505  1.00 77.86           C  
ATOM    626  C   VAL A  84      25.912   1.236  21.306  1.00 78.95           C  
ATOM    627  O   VAL A  84      25.514   2.345  20.951  1.00 82.59           O  
ATOM    628  CB  VAL A  84      26.281  -0.399  19.457  1.00 78.37           C  
ATOM    629  CG1 VAL A  84      25.293  -1.340  20.130  1.00 77.36           C  
ATOM    630  CG2 VAL A  84      25.584   0.457  18.411  1.00 77.34           C  
ATOM    631  N   LEU A  85      25.460   0.616  22.392  1.00 78.45           N  
ATOM    632  CA  LEU A  85      24.451   1.218  23.253  1.00 79.25           C  
ATOM    633  C   LEU A  85      24.980   2.507  23.870  1.00 76.71           C  
ATOM    634  O   LEU A  85      24.278   3.517  23.921  1.00 78.43           O  
ATOM    635  CB  LEU A  85      24.038   0.246  24.359  1.00 80.14           C  
ATOM    636  CG  LEU A  85      23.327  -1.031  23.906  1.00 82.07           C  
ATOM    637  CD1 LEU A  85      23.107  -1.970  25.082  1.00 81.42           C  
ATOM    638  CD2 LEU A  85      22.008  -0.700  23.225  1.00 85.49           C  
ATOM    639  N   VAL A  86      26.223   2.464  24.337  1.00 75.16           N  
ATOM    640  CA  VAL A  86      26.851   3.630  24.944  1.00 76.72           C  
ATOM    641  C   VAL A  86      26.768   4.804  23.977  1.00 72.37           C  
ATOM    642  O   VAL A  86      26.516   5.940  24.381  1.00 61.83           O  
ATOM    643  CB  VAL A  86      28.325   3.373  25.305  1.00 80.71           C  
ATOM    644  CG1 VAL A  86      28.970   4.644  25.837  1.00 81.14           C  
ATOM    645  CG2 VAL A  86      28.434   2.246  26.320  1.00 83.07           C  
ATOM    646  N   LEU A  87      26.979   4.520  22.696  1.00 74.92           N  
ATOM    647  CA  LEU A  87      26.922   5.540  21.671  1.00 78.52           C  
ATOM    648  C   LEU A  87      25.488   5.969  21.394  1.00 77.13           C  
ATOM    649  O   LEU A  87      25.226   7.160  21.195  1.00 78.76           O  
ATOM    650  CB  LEU A  87      27.602   5.034  20.395  1.00 82.10           C  
ATOM    651  CG  LEU A  87      29.091   4.702  20.536  1.00 83.09           C  
ATOM    652  CD1 LEU A  87      29.645   4.167  19.225  1.00 81.70           C  
ATOM    653  CD2 LEU A  87      29.874   5.923  21.018  1.00 83.78           C  
ATOM    654  N   THR A  88      24.566   5.010  21.395  1.00 75.12           N  
ATOM    655  CA  THR A  88      23.154   5.312  21.176  1.00 78.59           C  
ATOM    656  C   THR A  88      22.595   6.148  22.326  1.00 77.51           C  
ATOM    657  O   THR A  88      21.840   7.096  22.103  1.00 80.92           O  
ATOM    658  CB  THR A  88      22.314   4.025  21.004  1.00 83.60           C  
ATOM    659  OG1 THR A  88      22.905   3.188  20.001  1.00 81.61           O  
ATOM    660  CG2 THR A  88      20.887   4.355  20.583  1.00 88.42           C  
ATOM    661  N   GLN A  89      22.978   5.806  23.549  1.00 75.51           N  
ATOM    662  CA  GLN A  89      22.531   6.559  24.708  1.00 76.53           C  
ATOM    663  C   GLN A  89      23.083   7.985  24.705  1.00 79.19           C  
ATOM    664  O   GLN A  89      22.373   8.933  25.041  1.00 85.83           O  
ATOM    665  CB  GLN A  89      22.926   5.839  25.997  1.00 77.32           C  
ATOM    666  CG  GLN A  89      22.102   6.246  27.197  1.00 76.55           C  
ATOM    667  CD  GLN A  89      20.642   5.927  26.997  1.00 78.09           C  
ATOM    668  OE1 GLN A  89      20.301   4.852  26.506  1.00 78.84           O  
ATOM    669  NE2 GLN A  89      19.773   6.864  27.338  1.00 80.76           N  
ATOM    670  N   SER A  90      24.346   8.134  24.315  1.00 79.71           N  
ATOM    671  CA  SER A  90      24.958   9.456  24.181  1.00 81.31           C  
ATOM    672  C   SER A  90      24.197  10.311  23.172  1.00 80.97           C  
ATOM    673  O   SER A  90      24.002  11.506  23.400  1.00 81.22           O  
ATOM    674  CB  SER A  90      26.438   9.333  23.783  1.00 83.39           C  
ATOM    675  OG  SER A  90      27.044  10.603  23.603  1.00 87.16           O  
ATOM    676  N   SER A  91      23.764   9.693  22.075  1.00 81.07           N  
ATOM    677  CA  SER A  91      22.965  10.391  21.075  1.00 86.04           C  
ATOM    678  C   SER A  91      21.629  10.880  21.651  1.00 87.15           C  
ATOM    679  O   SER A  91      21.205  12.008  21.376  1.00 84.30           O  
ATOM    680  CB  SER A  91      22.728   9.498  19.854  1.00 91.06           C  
ATOM    681  OG  SER A  91      23.955   9.172  19.211  1.00 92.79           O  
ATOM    682  N   ILE A  92      20.983  10.039  22.458  1.00 87.63           N  
ATOM    683  CA  ILE A  92      19.730  10.416  23.121  1.00 86.70           C  
ATOM    684  C   ILE A  92      19.919  11.671  23.966  1.00 86.06           C  
ATOM    685  O   ILE A  92      19.140  12.623  23.855  1.00 81.97           O  
ATOM    686  CB  ILE A  92      19.170   9.261  24.001  1.00 87.85           C  
ATOM    687  CG1 ILE A  92      18.556   8.173  23.120  1.00 89.15           C  
ATOM    688  CG2 ILE A  92      18.143   9.755  25.023  1.00 85.64           C  
ATOM    689  CD1 ILE A  92      17.250   8.561  22.447  1.00 90.46           C  
ATOM    690  N   PHE A  93      20.949  11.665  24.805  1.00 87.33           N  
ATOM    691  CA  PHE A  93      21.192  12.791  25.694  1.00 89.07           C  
ATOM    692  C   PHE A  93      21.465  14.065  24.914  1.00 86.43           C  
ATOM    693  O   PHE A  93      20.964  15.124  25.292  1.00 88.33           O  
ATOM    694  CB  PHE A  93      22.326  12.510  26.696  1.00 91.06           C  
ATOM    695  CG  PHE A  93      21.973  11.503  27.765  1.00 90.93           C  
ATOM    696  CD1 PHE A  93      20.695  11.449  28.332  1.00 87.36           C  
ATOM    697  CD2 PHE A  93      22.931  10.603  28.215  1.00 95.86           C  
ATOM    698  CE1 PHE A  93      20.387  10.510  29.304  1.00 90.73           C  
ATOM    699  CE2 PHE A  93      22.623   9.664  29.192  1.00 97.44           C  
ATOM    700  CZ  PHE A  93      21.351   9.619  29.741  1.00 93.88           C  
ATOM    701  N   SER A  94      22.223  13.970  23.825  1.00 82.21           N  
ATOM    702  CA  SER A  94      22.518  15.148  23.000  1.00 81.03           C  
ATOM    703  C   SER A  94      21.255  15.718  22.365  1.00 80.65           C  
ATOM    704  O   SER A  94      21.049  16.934  22.354  1.00 74.59           O  
ATOM    705  CB  SER A  94      23.542  14.809  21.922  1.00 79.11           C  
ATOM    706  OG  SER A  94      24.806  14.576  22.498  1.00 76.78           O  
ATOM    707  N   LEU A  95      20.410  14.833  21.847  1.00 84.08           N  
ATOM    708  CA  LEU A  95      19.153  15.258  21.234  1.00 86.67           C  
ATOM    709  C   LEU A  95      18.221  15.903  22.246  1.00 84.09           C  
ATOM    710  O   LEU A  95      17.592  16.919  21.950  1.00 83.69           O  
ATOM    711  CB  LEU A  95      18.465  14.083  20.526  1.00 87.72           C  
ATOM    712  CG  LEU A  95      19.205  13.565  19.283  1.00 84.85           C  
ATOM    713  CD1 LEU A  95      18.625  12.247  18.816  1.00 86.02           C  
ATOM    714  CD2 LEU A  95      19.160  14.569  18.152  1.00 82.63           C  
ATOM    715  N   LEU A  96      18.158  15.325  23.441  1.00 84.10           N  
ATOM    716  CA  LEU A  96      17.332  15.874  24.512  1.00 85.21           C  
ATOM    717  C   LEU A  96      17.850  17.237  24.979  1.00 79.35           C  
ATOM    718  O   LEU A  96      17.082  18.159  25.214  1.00 79.21           O  
ATOM    719  CB  LEU A  96      17.239  14.887  25.682  1.00 86.92           C  
ATOM    720  CG  LEU A  96      16.279  15.200  26.847  1.00 88.66           C  
ATOM    721  CD1 LEU A  96      14.912  15.731  26.429  1.00 89.58           C  
ATOM    722  CD2 LEU A  96      16.075  13.953  27.694  1.00 85.28           C  
ATOM    723  N   ALA A  97      19.159  17.369  25.081  1.00 77.08           N  
ATOM    724  CA  ALA A  97      19.759  18.639  25.464  1.00 82.64           C  
ATOM    725  C   ALA A  97      19.517  19.748  24.431  1.00 83.33           C  
ATOM    726  O   ALA A  97      19.279  20.908  24.796  1.00 83.51           O  
ATOM    727  CB  ALA A  97      21.241  18.451  25.712  1.00 82.82           C  
ATOM    728  N   ILE A  98      19.567  19.395  23.150  1.00 83.06           N  
ATOM    729  CA  ILE A  98      19.295  20.365  22.085  1.00 85.19           C  
ATOM    730  C   ILE A  98      17.864  20.890  22.181  1.00 83.20           C  
ATOM    731  O   ILE A  98      17.630  22.097  22.031  1.00 79.27           O  
ATOM    732  CB  ILE A  98      19.588  19.778  20.680  1.00 88.25           C  
ATOM    733  CG1 ILE A  98      21.099  19.681  20.486  1.00 86.27           C  
ATOM    734  CG2 ILE A  98      19.016  20.661  19.571  1.00 87.17           C  
ATOM    735  CD1 ILE A  98      21.518  18.879  19.281  1.00 86.51           C  
ATOM    736  N   ALA A  99      16.924  19.982  22.436  1.00 82.64           N  
ATOM    737  CA  ALA A  99      15.515  20.354  22.590  1.00 82.55           C  
ATOM    738  C   ALA A  99      15.306  21.337  23.737  1.00 84.94           C  
ATOM    739  O   ALA A  99      14.676  22.383  23.562  1.00 85.82           O  
ATOM    740  CB  ALA A  99      14.656  19.117  22.796  1.00 81.73           C  
ATOM    741  N   ILE A 100      15.862  21.010  24.897  1.00 85.15           N  
ATOM    742  CA  ILE A 100      15.716  21.853  26.078  1.00 83.93           C  
ATOM    743  C   ILE A 100      16.394  23.204  25.851  1.00 82.94           C  
ATOM    744  O   ILE A 100      15.882  24.231  26.304  1.00 83.77           O  
ATOM    745  CB  ILE A 100      16.273  21.158  27.346  1.00 82.37           C  
ATOM    746  CG1 ILE A 100      15.489  19.870  27.630  1.00 84.69           C  
ATOM    747  CG2 ILE A 100      16.201  22.081  28.564  1.00 76.28           C  
ATOM    748  CD1 ILE A 100      16.239  18.886  28.501  1.00 88.26           C  
ATOM    749  N   ASP A 101      17.526  23.196  25.143  1.00 82.81           N  
ATOM    750  CA  ASP A 101      18.253  24.428  24.854  1.00 87.32           C  
ATOM    751  C   ASP A 101      17.388  25.384  24.023  1.00 90.88           C  
ATOM    752  O   ASP A 101      17.282  26.570  24.332  1.00 94.12           O  
ATOM    753  CB  ASP A 101      19.580  24.138  24.138  1.00 87.47           C  
ATOM    754  CG  ASP A 101      20.328  25.415  23.747  1.00 89.37           C  
ATOM    755  OD1 ASP A 101      20.971  26.033  24.618  1.00 88.67           O  
ATOM    756  OD2 ASP A 101      20.264  25.809  22.564  1.00 89.94           O  
ATOM    757  N   ARG A 102      16.767  24.861  22.977  1.00 91.03           N  
ATOM    758  CA  ARG A 102      15.898  25.677  22.148  1.00 92.41           C  
ATOM    759  C   ARG A 102      14.624  26.080  22.875  1.00 88.94           C  
ATOM    760  O   ARG A 102      14.079  27.138  22.600  1.00 86.41           O  
ATOM    761  CB  ARG A 102      15.572  24.952  20.839  1.00 99.88           C  
ATOM    762  CG  ARG A 102      16.776  24.737  19.925  1.00100.38           C  
ATOM    763  CD  ARG A 102      17.369  26.060  19.461  1.00 99.83           C  
ATOM    764  NE  ARG A 102      18.309  26.610  20.440  1.00 98.43           N  
ATOM    765  CZ  ARG A 102      18.690  27.885  20.511  1.00 99.01           C  
ATOM    766  NH1 ARG A 102      18.211  28.801  19.671  1.00102.94           N  
ATOM    767  NH2 ARG A 102      19.564  28.257  21.442  1.00 98.82           N  
ATOM    768  N   TYR A 103      14.151  25.250  23.797  1.00 91.97           N  
ATOM    769  CA  TYR A 103      12.981  25.608  24.602  1.00 95.45           C  
ATOM    770  C   TYR A 103      13.277  26.783  25.529  1.00 96.44           C  
ATOM    771  O   TYR A 103      12.493  27.734  25.603  1.00101.11           O  
ATOM    772  CB  TYR A 103      12.486  24.414  25.411  1.00 94.92           C  
ATOM    773  CG  TYR A 103      11.316  24.759  26.275  1.00 95.45           C  
ATOM    774  CD1 TYR A 103      10.060  24.931  25.723  1.00 98.59           C  
ATOM    775  CD2 TYR A 103      11.467  24.954  27.639  1.00 98.18           C  
ATOM    776  CE1 TYR A 103       8.974  25.271  26.508  1.00105.25           C  
ATOM    777  CE2 TYR A 103      10.382  25.287  28.436  1.00106.33           C  
ATOM    778  CZ  TYR A 103       9.134  25.441  27.861  1.00107.63           C  
ATOM    779  OH  TYR A 103       8.037  25.773  28.620  1.00113.71           O  
ATOM    780  N   ILE A 104      14.407  26.708  26.227  1.00 94.38           N  
ATOM    781  CA  ILE A 104      14.873  27.805  27.069  1.00 90.65           C  
ATOM    782  C   ILE A 104      15.049  29.078  26.232  1.00 97.50           C  
ATOM    783  O   ILE A 104      14.703  30.150  26.695  1.00102.78           O  
ATOM    784  CB  ILE A 104      16.193  27.440  27.790  1.00 88.35           C  
ATOM    785  CG1 ILE A 104      15.945  26.344  28.823  1.00 87.70           C  
ATOM    786  CG2 ILE A 104      16.813  28.638  28.506  1.00 89.30           C  
ATOM    787  CD1 ILE A 104      17.218  25.703  29.328  1.00 89.29           C  
ATOM    788  N   ALA A 105      15.581  28.955  25.015  1.00100.02           N  
ATOM    789  CA  ALA A 105      15.837  30.118  24.158  1.00 97.12           C  
ATOM    790  C   ALA A 105      14.574  30.847  23.698  1.00 96.55           C  
ATOM    791  O   ALA A 105      14.592  32.067  23.583  1.00 99.11           O  
ATOM    792  CB  ALA A 105      16.656  29.715  22.956  1.00 97.63           C  
ATOM    793  N   ILE A 106      13.489  30.121  23.438  1.00 94.68           N  
ATOM    794  CA  ILE A 106      12.241  30.765  22.988  1.00100.65           C  
ATOM    795  C   ILE A 106      11.288  31.279  24.084  1.00102.03           C  
ATOM    796  O   ILE A 106      10.496  32.189  23.824  1.00 96.51           O  
ATOM    797  CB  ILE A 106      11.451  29.859  22.012  1.00108.27           C  
ATOM    798  CG1 ILE A 106      10.556  30.719  21.102  1.00111.04           C  
ATOM    799  CG2 ILE A 106      10.635  28.797  22.753  1.00109.81           C  
ATOM    800  CD1 ILE A 106       9.784  29.962  20.043  1.00111.25           C  
ATOM    801  N   ARG A 107      11.336  30.695  25.278  1.00104.94           N  
ATOM    802  CA  ARG A 107      10.436  31.103  26.356  1.00107.31           C  
ATOM    803  C   ARG A 107      11.030  32.227  27.196  1.00106.06           C  
ATOM    804  O   ARG A 107      10.320  33.164  27.574  1.00116.47           O  
ATOM    805  CB  ARG A 107      10.094  29.912  27.243  1.00111.53           C  
ATOM    806  CG  ARG A 107       9.037  30.218  28.292  1.00121.67           C  
ATOM    807  CD  ARG A 107       8.675  28.970  29.085  1.00131.39           C  
ATOM    808  NE  ARG A 107       7.694  29.244  30.141  1.00135.34           N  
ATOM    809  CZ  ARG A 107       6.379  29.371  29.951  1.00135.58           C  
ATOM    810  NH1 ARG A 107       5.851  29.251  28.731  1.00136.54           N  
ATOM    811  NH2 ARG A 107       5.580  29.609  30.992  1.00133.21           N  
ATOM    812  N   ILE A 108      12.320  32.126  27.502  1.00100.96           N  
ATOM    813  CA  ILE A 108      13.026  33.159  28.280  1.00100.78           C  
ATOM    814  C   ILE A 108      14.314  33.572  27.564  1.00101.86           C  
ATOM    815  O   ILE A 108      15.422  33.358  28.064  1.00 92.13           O  
ATOM    816  CB  ILE A 108      13.297  32.746  29.748  1.00 99.83           C  
ATOM    817  CG1 ILE A 108      14.227  31.533  29.861  1.00101.68           C  
ATOM    818  CG2 ILE A 108      11.982  32.450  30.454  1.00101.37           C  
ATOM    819  CD1 ILE A 108      14.722  31.285  31.267  1.00105.13           C  
ATOM    820  N   PRO A 109      14.174  34.199  26.383  1.00107.78           N  
ATOM    821  CA  PRO A 109      15.352  34.662  25.646  1.00105.86           C  
ATOM    822  C   PRO A 109      16.064  35.710  26.481  1.00104.84           C  
ATOM    823  O   PRO A 109      17.274  35.889  26.383  1.00105.02           O  
ATOM    824  CB  PRO A 109      14.762  35.268  24.365  1.00105.01           C  
ATOM    825  CG  PRO A 109      13.366  35.626  24.723  1.00107.77           C  
ATOM    826  CD  PRO A 109      12.916  34.622  25.743  1.00108.97           C  
ATOM    827  N   LEU A 110      15.298  36.409  27.312  1.00103.41           N  
ATOM    828  CA  LEU A 110      15.850  37.448  28.173  1.00105.57           C  
ATOM    829  C   LEU A 110      16.986  36.905  29.033  1.00106.87           C  
ATOM    830  O   LEU A 110      18.086  37.458  29.047  1.00 99.72           O  
ATOM    831  CB  LEU A 110      14.757  38.044  29.062  1.00106.16           C  
ATOM    832  CG  LEU A 110      13.570  38.685  28.339  1.00106.07           C  
ATOM    833  CD1 LEU A 110      12.427  38.946  29.308  1.00108.55           C  
ATOM    834  CD2 LEU A 110      13.993  39.970  27.645  1.00104.66           C  
ATOM    835  N   ARG A 111      16.779  35.818  29.756  1.00112.82           N  
ATOM    836  CA  ARG A 111      17.863  35.302  30.593  1.00112.88           C  
ATOM    837  C   ARG A 111      18.442  33.993  30.087  1.00114.11           C  
ATOM    838  O   ARG A 111      18.624  33.051  30.835  1.00119.28           O  
ATOM    839  CB  ARG A 111      17.396  35.137  32.037  1.00108.02           C  
ATOM    840  CG  ARG A 111      15.896  35.006  32.208  1.00 99.45           C  
ATOM    841  N   TYR A 112      18.740  33.953  28.807  1.00110.25           N  
ATOM    842  CA  TYR A 112      19.256  32.769  28.130  1.00107.69           C  
ATOM    843  C   TYR A 112      20.779  32.722  28.187  1.00104.53           C  
ATOM    844  O   TYR A 112      21.367  31.689  28.507  1.00103.28           O  
ATOM    845  CB  TYR A 112      18.783  32.734  26.676  1.00109.21           C  
ATOM    846  CG  TYR A 112      19.450  31.665  25.840  1.00 99.53           C  
ATOM    847  CD1 TYR A 112      18.929  30.380  25.777  1.00 95.93           C  
ATOM    848  CD2 TYR A 112      20.600  31.942  25.113  1.00 93.72           C  
ATOM    849  CE1 TYR A 112      19.535  29.399  25.014  1.00 97.92           C  
ATOM    850  CE2 TYR A 112      21.213  30.968  24.348  1.00 93.96           C  
ATOM    851  CZ  TYR A 112      20.677  29.699  24.302  1.00 97.60           C  
ATOM    852  OH  TYR A 112      21.284  28.726  23.541  1.00 93.56           O  
ATOM    853  N   ASN A 113      21.413  33.848  27.875  1.00104.88           N  
ATOM    854  CA  ASN A 113      22.869  33.938  27.890  1.00109.16           C  
ATOM    855  C   ASN A 113      23.466  33.875  29.282  1.00110.75           C  
ATOM    856  O   ASN A 113      24.622  33.477  29.420  1.00115.13           O  
ATOM    857  CB  ASN A 113      23.354  35.203  27.175  1.00117.28           C  
ATOM    858  CG  ASN A 113      23.405  35.040  25.668  1.00127.60           C  
ATOM    859  OD1 ASN A 113      23.595  33.933  25.157  1.00127.13           O  
ATOM    860  ND2 ASN A 113      23.248  36.149  24.946  1.00138.74           N  
ATOM    861  N   GLY A 114      22.695  34.263  30.301  1.00110.84           N  
ATOM    862  CA  GLY A 114      23.147  34.187  31.703  1.00112.25           C  
ATOM    863  C   GLY A 114      22.984  32.812  32.342  1.00111.59           C  
ATOM    864  O   GLY A 114      23.686  32.473  33.308  1.00106.93           O  
ATOM    865  N   LEU A 115      22.049  32.030  31.797  1.00108.73           N  
ATOM    866  CA  LEU A 115      21.726  30.686  32.287  1.00106.14           C  
ATOM    867  C   LEU A 115      22.453  29.562  31.526  1.00105.68           C  
ATOM    868  O   LEU A 115      22.890  28.587  32.132  1.00 99.57           O  
ATOM    869  CB  LEU A 115      20.211  30.472  32.208  1.00106.23           C  
ATOM    870  CG  LEU A 115      19.652  29.072  32.470  1.00108.70           C  
ATOM    871  CD1 LEU A 115      19.984  28.589  33.867  1.00108.59           C  
ATOM    872  CD2 LEU A 115      18.146  29.078  32.272  1.00109.76           C  
ATOM    873  N   VAL A 116      22.551  29.687  30.205  1.00107.53           N  
ATOM    874  CA  VAL A 116      23.106  28.632  29.358  1.00103.35           C  
ATOM    875  C   VAL A 116      24.436  29.117  28.790  1.00 97.80           C  
ATOM    876  O   VAL A 116      24.469  29.849  27.807  1.00 99.67           O  
ATOM    877  CB  VAL A 116      22.125  28.250  28.220  1.00102.56           C  
ATOM    878  CG1 VAL A 116      22.617  27.016  27.489  1.00 98.29           C  
ATOM    879  CG2 VAL A 116      20.713  28.009  28.754  1.00103.11           C  
ATOM    880  N   THR A 117      25.529  28.721  29.429  1.00 96.03           N  
ATOM    881  CA  THR A 117      26.872  29.076  28.966  1.00 97.38           C  
ATOM    882  C   THR A 117      27.640  27.865  28.436  1.00 99.23           C  
ATOM    883  O   THR A 117      27.275  26.721  28.693  1.00 98.67           O  
ATOM    884  CB  THR A 117      27.683  29.730  30.096  1.00 96.45           C  
ATOM    885  OG1 THR A 117      27.749  28.843  31.227  1.00100.86           O  
ATOM    886  CG2 THR A 117      27.040  31.049  30.498  1.00 93.40           C  
ATOM    887  N   GLY A 118      28.705  28.138  27.684  1.00104.89           N  
ATOM    888  CA  GLY A 118      29.576  27.099  27.134  1.00103.17           C  
ATOM    889  C   GLY A 118      30.237  26.244  28.197  1.00107.49           C  
ATOM    890  O   GLY A 118      30.350  25.025  28.045  1.00114.65           O  
ATOM    891  N   THR A 119      30.666  26.892  29.279  1.00113.53           N  
ATOM    892  CA  THR A 119      31.267  26.209  30.427  1.00117.09           C  
ATOM    893  C   THR A 119      30.315  25.197  31.054  1.00114.04           C  
ATOM    894  O   THR A 119      30.718  24.080  31.378  1.00112.74           O  
ATOM    895  CB  THR A 119      31.686  27.219  31.516  1.00126.70           C  
ATOM    896  OG1 THR A 119      32.729  28.063  31.015  1.00145.45           O  
ATOM    897  CG2 THR A 119      32.181  26.507  32.767  1.00130.92           C  
ATOM    898  N   ARG A 120      29.062  25.600  31.239  1.00117.44           N  
ATOM    899  CA  ARG A 120      28.041  24.707  31.798  1.00120.23           C  
ATOM    900  C   ARG A 120      27.666  23.581  30.809  1.00117.31           C  
ATOM    901  O   ARG A 120      27.490  22.424  31.202  1.00116.20           O  
ATOM    902  CB  ARG A 120      26.815  25.513  32.246  1.00119.12           C  
ATOM    903  CG  ARG A 120      27.113  26.484  33.387  1.00117.45           C  
ATOM    904  CD  ARG A 120      25.912  27.359  33.696  1.00117.86           C  
ATOM    905  NE  ARG A 120      26.194  28.391  34.695  1.00119.76           N  
ATOM    906  CZ  ARG A 120      25.309  29.297  35.133  1.00119.77           C  
ATOM    907  NH1 ARG A 120      24.068  29.335  34.657  1.00117.90           N  
ATOM    908  NH2 ARG A 120      25.664  30.188  36.055  1.00120.12           N  
ATOM    909  N   ALA A 121      27.572  23.919  29.526  1.00116.72           N  
ATOM    910  CA  ALA A 121      27.333  22.921  28.483  1.00109.23           C  
ATOM    911  C   ALA A 121      28.417  21.849  28.485  1.00107.84           C  
ATOM    912  O   ALA A 121      28.098  20.665  28.421  1.00112.86           O  
ATOM    913  CB  ALA A 121      27.256  23.580  27.114  1.00110.27           C  
ATOM    914  N   LYS A 122      29.685  22.265  28.569  1.00106.89           N  
ATOM    915  CA  LYS A 122      30.819  21.319  28.623  1.00106.19           C  
ATOM    916  C   LYS A 122      30.694  20.336  29.787  1.00 98.33           C  
ATOM    917  O   LYS A 122      30.921  19.143  29.619  1.00 96.51           O  
ATOM    918  CB  LYS A 122      32.171  22.051  28.654  1.00111.07           C  
ATOM    919  CG  LYS A 122      32.581  22.579  27.280  1.00122.19           C  
ATOM    920  CD  LYS A 122      33.729  23.581  27.328  1.00132.38           C  
ATOM    921  CE  LYS A 122      34.197  23.970  25.927  1.00135.29           C  
ATOM    922  NZ  LYS A 122      33.112  24.577  25.102  1.00136.73           N  
ATOM    923  N   GLY A 123      30.299  20.839  30.949  1.00 94.12           N  
ATOM    924  CA  GLY A 123      30.040  19.980  32.103  1.00 94.21           C  
ATOM    925  C   GLY A 123      28.861  19.029  31.909  1.00 92.92           C  
ATOM    926  O   GLY A 123      28.911  17.865  32.334  1.00 93.13           O  
ATOM    927  N   ILE A 124      27.792  19.523  31.285  1.00 89.36           N  
ATOM    928  CA  ILE A 124      26.622  18.689  30.982  1.00 88.22           C  
ATOM    929  C   ILE A 124      27.005  17.541  30.033  1.00 89.93           C  
ATOM    930  O   ILE A 124      26.544  16.402  30.197  1.00 80.70           O  
ATOM    931  CB  ILE A 124      25.468  19.525  30.374  1.00 90.71           C  
ATOM    932  CG1 ILE A 124      24.830  20.408  31.445  1.00 93.58           C  
ATOM    933  CG2 ILE A 124      24.386  18.631  29.773  1.00 93.22           C  
ATOM    934  CD1 ILE A 124      23.837  21.424  30.905  1.00 98.97           C  
ATOM    935  N   ILE A 125      27.849  17.849  29.049  1.00 91.50           N  
ATOM    936  CA  ILE A 125      28.247  16.861  28.056  1.00 90.18           C  
ATOM    937  C   ILE A 125      29.096  15.767  28.705  1.00 93.26           C  
ATOM    938  O   ILE A 125      28.844  14.586  28.481  1.00102.38           O  
ATOM    939  CB  ILE A 125      28.956  17.518  26.847  1.00 88.01           C  
ATOM    940  CG1 ILE A 125      27.943  18.367  26.073  1.00 88.25           C  
ATOM    941  CG2 ILE A 125      29.536  16.470  25.897  1.00 88.83           C  
ATOM    942  CD1 ILE A 125      28.559  19.203  24.975  1.00 89.01           C  
ATOM    943  N   ALA A 126      30.076  16.158  29.517  1.00 93.61           N  
ATOM    944  CA  ALA A 126      30.929  15.191  30.222  1.00 91.74           C  
ATOM    945  C   ALA A 126      30.105  14.229  31.070  1.00 92.41           C  
ATOM    946  O   ALA A 126      30.324  13.018  31.028  1.00 86.61           O  
ATOM    947  CB  ALA A 126      31.949  15.908  31.094  1.00 91.00           C  
ATOM    948  N   ILE A 127      29.157  14.784  31.825  1.00 97.68           N  
ATOM    949  CA  ILE A 127      28.269  13.992  32.692  1.00 94.13           C  
ATOM    950  C   ILE A 127      27.428  13.014  31.883  1.00 93.42           C  
ATOM    951  O   ILE A 127      27.255  11.869  32.292  1.00 86.23           O  
ATOM    952  CB  ILE A 127      27.372  14.907  33.567  1.00 94.03           C  
ATOM    953  CG1 ILE A 127      28.244  15.558  34.652  1.00 98.03           C  
ATOM    954  CG2 ILE A 127      26.209  14.129  34.193  1.00 88.14           C  
ATOM    955  CD1 ILE A 127      27.587  16.665  35.444  1.00 99.71           C  
ATOM    956  N   CYS A 128      26.920  13.468  30.742  1.00 98.19           N  
ATOM    957  CA  CYS A 128      26.088  12.618  29.895  1.00102.22           C  
ATOM    958  C   CYS A 128      26.880  11.471  29.247  1.00101.83           C  
ATOM    959  O   CYS A 128      26.322  10.399  29.024  1.00 98.83           O  
ATOM    960  CB  CYS A 128      25.361  13.451  28.831  1.00103.28           C  
ATOM    961  SG  CYS A 128      24.066  14.517  29.505  1.00 93.33           S  
ATOM    962  N   TRP A 129      28.163  11.690  28.950  1.00 96.99           N  
ATOM    963  CA  TRP A 129      29.013  10.619  28.415  1.00 90.80           C  
ATOM    964  C   TRP A 129      29.281   9.569  29.475  1.00 91.03           C  
ATOM    965  O   TRP A 129      29.274   8.380  29.176  1.00 93.25           O  
ATOM    966  CB  TRP A 129      30.328  11.157  27.846  1.00 88.88           C  
ATOM    967  CG  TRP A 129      30.201  11.577  26.414  1.00 88.05           C  
ATOM    968  CD1 TRP A 129      30.017  12.842  25.940  1.00 85.77           C  
ATOM    969  CD2 TRP A 129      30.232  10.721  25.269  1.00 84.42           C  
ATOM    970  NE1 TRP A 129      29.934  12.827  24.572  1.00 84.49           N  
ATOM    971  CE2 TRP A 129      30.073  11.540  24.132  1.00 83.48           C  
ATOM    972  CE3 TRP A 129      30.390   9.344  25.092  1.00 84.01           C  
ATOM    973  CZ2 TRP A 129      30.065  11.027  22.833  1.00 83.73           C  
ATOM    974  CZ3 TRP A 129      30.381   8.830  23.796  1.00 86.15           C  
ATOM    975  CH2 TRP A 129      30.213   9.673  22.684  1.00 85.42           C  
ATOM    976  N   VAL A 130      29.489  10.004  30.714  1.00 90.57           N  
ATOM    977  CA  VAL A 130      29.732   9.059  31.805  1.00 88.31           C  
ATOM    978  C   VAL A 130      28.467   8.241  32.089  1.00 83.28           C  
ATOM    979  O   VAL A 130      28.540   7.021  32.196  1.00 83.22           O  
ATOM    980  CB  VAL A 130      30.264   9.749  33.074  1.00 86.06           C  
ATOM    981  CG1 VAL A 130      30.443   8.736  34.193  1.00 87.34           C  
ATOM    982  CG2 VAL A 130      31.608  10.413  32.796  1.00 86.93           C  
ATOM    983  N   LEU A 131      27.318   8.905  32.179  1.00 75.77           N  
ATOM    984  CA  LEU A 131      26.041   8.199  32.317  1.00 76.25           C  
ATOM    985  C   LEU A 131      25.752   7.221  31.164  1.00 84.03           C  
ATOM    986  O   LEU A 131      25.146   6.161  31.380  1.00 80.46           O  
ATOM    987  CB  LEU A 131      24.884   9.195  32.412  1.00 73.26           C  
ATOM    988  CG  LEU A 131      24.771  10.002  33.686  1.00 73.24           C  
ATOM    989  CD1 LEU A 131      23.762  11.131  33.536  1.00 72.94           C  
ATOM    990  CD2 LEU A 131      24.392   9.071  34.822  1.00 74.75           C  
ATOM    991  N   SER A 132      26.163   7.588  29.948  1.00 89.32           N  
ATOM    992  CA  SER A 132      25.967   6.731  28.777  1.00 87.67           C  
ATOM    993  C   SER A 132      26.778   5.436  28.868  1.00 87.94           C  
ATOM    994  O   SER A 132      26.277   4.365  28.490  1.00 84.35           O  
ATOM    995  CB  SER A 132      26.320   7.477  27.491  1.00 87.86           C  
ATOM    996  OG  SER A 132      25.476   8.599  27.313  1.00 88.36           O  
ATOM    997  N   PHE A 133      28.019   5.533  29.363  1.00 82.06           N  
ATOM    998  CA  PHE A 133      28.824   4.334  29.635  1.00 76.88           C  
ATOM    999  C   PHE A 133      28.167   3.444  30.689  1.00 78.09           C  
ATOM   1000  O   PHE A 133      28.113   2.222  30.517  1.00 76.88           O  
ATOM   1001  CB  PHE A 133      30.244   4.693  30.065  1.00 71.98           C  
ATOM   1002  CG  PHE A 133      31.183   4.890  28.924  1.00 69.70           C  
ATOM   1003  CD1 PHE A 133      31.346   6.138  28.355  1.00 70.71           C  
ATOM   1004  CD2 PHE A 133      31.911   3.826  28.419  1.00 70.83           C  
ATOM   1005  CE1 PHE A 133      32.222   6.335  27.296  1.00 71.54           C  
ATOM   1006  CE2 PHE A 133      32.791   4.008  27.360  1.00 73.51           C  
ATOM   1007  CZ  PHE A 133      32.946   5.270  26.796  1.00 72.46           C  
ATOM   1008  N   ALA A 134      27.664   4.053  31.764  1.00 76.26           N  
ATOM   1009  CA  ALA A 134      27.044   3.297  32.848  1.00 77.19           C  
ATOM   1010  C   ALA A 134      25.749   2.608  32.411  1.00 74.20           C  
ATOM   1011  O   ALA A 134      25.506   1.457  32.768  1.00 70.55           O  
ATOM   1012  CB  ALA A 134      26.792   4.202  34.040  1.00 81.51           C  
ATOM   1013  N   ILE A 135      24.928   3.303  31.632  1.00 71.84           N  
ATOM   1014  CA  ILE A 135      23.700   2.700  31.119  1.00 72.33           C  
ATOM   1015  C   ILE A 135      24.012   1.638  30.071  1.00 77.27           C  
ATOM   1016  O   ILE A 135      23.473   0.535  30.144  1.00 83.61           O  
ATOM   1017  CB  ILE A 135      22.721   3.747  30.547  1.00 69.46           C  
ATOM   1018  CG1 ILE A 135      22.166   4.595  31.691  1.00 68.48           C  
ATOM   1019  CG2 ILE A 135      21.566   3.078  29.797  1.00 63.85           C  
ATOM   1020  CD1 ILE A 135      21.308   5.763  31.255  1.00 69.12           C  
ATOM   1021  N   GLY A 136      24.856   1.972  29.095  1.00 77.78           N  
ATOM   1022  CA  GLY A 136      25.157   1.052  27.995  1.00 76.90           C  
ATOM   1023  C   GLY A 136      25.871  -0.231  28.382  1.00 76.01           C  
ATOM   1024  O   GLY A 136      25.653  -1.280  27.776  1.00 71.75           O  
ATOM   1025  N   LEU A 137      26.726  -0.144  29.396  1.00 76.93           N  
ATOM   1026  CA  LEU A 137      27.506  -1.289  29.861  1.00 80.45           C  
ATOM   1027  C   LEU A 137      26.974  -1.934  31.155  1.00 81.14           C  
ATOM   1028  O   LEU A 137      27.677  -2.723  31.798  1.00 78.20           O  
ATOM   1029  CB  LEU A 137      28.975  -0.874  30.016  1.00 80.07           C  
ATOM   1030  CG  LEU A 137      29.645  -0.314  28.754  1.00 79.34           C  
ATOM   1031  CD1 LEU A 137      31.036   0.196  29.074  1.00 80.52           C  
ATOM   1032  CD2 LEU A 137      29.700  -1.361  27.648  1.00 75.94           C  
ATOM   1033  N   THR A 138      25.729  -1.626  31.517  1.00 84.37           N  
ATOM   1034  CA  THR A 138      25.065  -2.261  32.666  1.00 87.90           C  
ATOM   1035  C   THR A 138      25.096  -3.801  32.640  1.00 90.58           C  
ATOM   1036  O   THR A 138      25.283  -4.419  33.694  1.00100.11           O  
ATOM   1037  CB  THR A 138      23.607  -1.748  32.832  1.00 88.27           C  
ATOM   1038  OG1 THR A 138      23.622  -0.444  33.421  1.00 85.94           O  
ATOM   1039  CG2 THR A 138      22.760  -2.668  33.712  1.00 87.45           C  
ATOM   1040  N   PRO A 139      24.915  -4.432  31.460  1.00 88.51           N  
ATOM   1041  CA  PRO A 139      25.025  -5.893  31.450  1.00 91.66           C  
ATOM   1042  C   PRO A 139      26.358  -6.452  31.974  1.00 93.66           C  
ATOM   1043  O   PRO A 139      26.377  -7.559  32.522  1.00 93.75           O  
ATOM   1044  CB  PRO A 139      24.825  -6.241  29.975  1.00 91.01           C  
ATOM   1045  CG  PRO A 139      23.910  -5.182  29.488  1.00 88.50           C  
ATOM   1046  CD  PRO A 139      24.368  -3.932  30.187  1.00 87.53           C  
ATOM   1047  N   MET A 140      27.443  -5.684  31.843  1.00 90.71           N  
ATOM   1048  CA  MET A 140      28.737  -6.098  32.393  1.00 88.14           C  
ATOM   1049  C   MET A 140      28.760  -6.080  33.920  1.00 83.39           C  
ATOM   1050  O   MET A 140      29.640  -6.689  34.518  1.00 90.49           O  
ATOM   1051  CB  MET A 140      29.873  -5.250  31.826  1.00 89.27           C  
ATOM   1052  CG  MET A 140      29.983  -5.377  30.317  1.00 94.12           C  
ATOM   1053  SD  MET A 140      31.396  -4.523  29.598  1.00 98.60           S  
ATOM   1054  CE  MET A 140      32.705  -5.658  30.044  1.00 98.60           C  
ATOM   1055  N   LEU A 141      27.798  -5.400  34.549  1.00 78.72           N  
ATOM   1056  CA  LEU A 141      27.651  -5.416  36.011  1.00 78.07           C  
ATOM   1057  C   LEU A 141      26.906  -6.628  36.573  1.00 78.71           C  
ATOM   1058  O   LEU A 141      26.637  -6.674  37.774  1.00 74.03           O  
ATOM   1059  CB  LEU A 141      26.956  -4.136  36.491  1.00 77.95           C  
ATOM   1060  CG  LEU A 141      27.632  -2.822  36.085  1.00 76.96           C  
ATOM   1061  CD1 LEU A 141      26.829  -1.636  36.604  1.00 79.76           C  
ATOM   1062  CD2 LEU A 141      29.070  -2.778  36.589  1.00 72.60           C  
ATOM   1063  N   GLY A 142      26.572  -7.605  35.732  1.00 81.82           N  
ATOM   1064  CA  GLY A 142      25.939  -8.841  36.211  1.00 85.52           C  
ATOM   1065  C   GLY A 142      24.598  -9.186  35.575  1.00 87.67           C  
ATOM   1066  O   GLY A 142      24.115 -10.319  35.734  1.00 82.14           O  
ATOM   1067  N   TRP A 143      23.986  -8.233  34.863  1.00 89.06           N  
ATOM   1068  CA  TRP A 143      22.726  -8.492  34.166  1.00 88.00           C  
ATOM   1069  C   TRP A 143      23.018  -9.068  32.779  1.00 92.64           C  
ATOM   1070  O   TRP A 143      22.919  -8.374  31.763  1.00102.96           O  
ATOM   1071  CB  TRP A 143      21.879  -7.219  34.071  1.00 80.78           C  
ATOM   1072  CG  TRP A 143      20.431  -7.480  33.732  1.00 78.68           C  
ATOM   1073  CD1 TRP A 143      19.844  -8.682  33.382  1.00 78.78           C  
ATOM   1074  CD2 TRP A 143      19.384  -6.511  33.699  1.00 76.80           C  
ATOM   1075  NE1 TRP A 143      18.503  -8.504  33.148  1.00 81.02           N  
ATOM   1076  CE2 TRP A 143      18.192  -7.182  33.333  1.00 78.05           C  
ATOM   1077  CE3 TRP A 143      19.334  -5.140  33.942  1.00 77.07           C  
ATOM   1078  CZ2 TRP A 143      16.966  -6.521  33.207  1.00 76.54           C  
ATOM   1079  CZ3 TRP A 143      18.112  -4.483  33.812  1.00 79.53           C  
ATOM   1080  CH2 TRP A 143      16.946  -5.177  33.448  1.00 77.35           C  
ATOM   1081  N   ASN A 144      23.388 -10.341  32.752  1.00 93.46           N  
ATOM   1082  CA  ASN A 144      23.745 -11.009  31.507  1.00 94.08           C  
ATOM   1083  C   ASN A 144      23.487 -12.499  31.602  1.00 96.83           C  
ATOM   1084  O   ASN A 144      23.136 -12.999  32.669  1.00102.48           O  
ATOM   1085  CB  ASN A 144      25.203 -10.719  31.134  1.00 91.66           C  
ATOM   1086  CG  ASN A 144      26.180 -11.224  32.167  1.00 91.80           C  
ATOM   1087  OD1 ASN A 144      26.262 -12.419  32.415  1.00 88.90           O  
ATOM   1088  ND2 ASN A 144      26.932 -10.313  32.776  1.00 97.86           N  
ATOM   1089  N   ASN A 145      23.675 -13.195  30.483  1.00 96.50           N  
ATOM   1090  CA  ASN A 145      23.482 -14.639  30.401  1.00 94.47           C  
ATOM   1091  C   ASN A 145      24.801 -15.399  30.422  1.00 94.04           C  
ATOM   1092  O   ASN A 145      24.826 -16.570  30.040  1.00 99.29           O  
ATOM   1093  CB  ASN A 145      22.727 -14.987  29.119  1.00 97.45           C  
ATOM   1094  CG  ASN A 145      21.376 -14.305  29.024  1.00104.93           C  
ATOM   1095  OD1 ASN A 145      20.647 -14.211  30.012  1.00106.73           O  
ATOM   1096  ND2 ASN A 145      21.024 -13.842  27.824  1.00109.63           N  
ATOM   1097  N   CYS A 146      25.886 -14.775  30.888  1.00 94.14           N  
ATOM   1098  CA  CYS A 146      27.168 -15.483  31.007  1.00 97.90           C  
ATOM   1099  C   CYS A 146      27.079 -16.666  31.966  1.00109.01           C  
ATOM   1100  O   CYS A 146      27.791 -17.649  31.798  1.00112.55           O  
ATOM   1101  CB  CYS A 146      28.293 -14.552  31.460  1.00 97.39           C  
ATOM   1102  SG  CYS A 146      28.688 -13.250  30.283  1.00 95.14           S  
ATOM   1103  N   GLY A 147      26.196 -16.567  32.959  1.00118.12           N  
ATOM   1104  CA  GLY A 147      25.911 -17.668  33.866  1.00122.00           C  
ATOM   1105  C   GLY A 147      25.088 -18.809  33.284  1.00120.03           C  
ATOM   1106  O   GLY A 147      24.963 -19.844  33.933  1.00128.77           O  
ATOM   1107  N   GLN A 148      24.536 -18.644  32.079  1.00111.12           N  
ATOM   1108  CA  GLN A 148      23.683 -19.660  31.455  1.00105.78           C  
ATOM   1109  C   GLN A 148      24.096 -19.954  30.002  1.00107.81           C  
ATOM   1110  O   GLN A 148      23.296 -19.733  29.079  1.00 96.00           O  
ATOM   1111  CB  GLN A 148      22.227 -19.191  31.522  1.00102.53           C  
ATOM   1112  N   PRO A 149      25.336 -20.479  29.799  1.00119.04           N  
ATOM   1113  CA  PRO A 149      25.849 -20.589  28.428  1.00123.91           C  
ATOM   1114  C   PRO A 149      25.196 -21.691  27.597  1.00124.02           C  
ATOM   1115  O   PRO A 149      24.706 -22.691  28.142  1.00118.15           O  
ATOM   1116  CB  PRO A 149      27.346 -20.882  28.627  1.00122.19           C  
ATOM   1117  CG  PRO A 149      27.409 -21.608  29.915  1.00121.42           C  
ATOM   1118  CD  PRO A 149      26.292 -21.053  30.773  1.00123.06           C  
ATOM   1119  N   LYS A 150      25.210 -21.490  26.282  1.00126.27           N  
ATOM   1120  CA  LYS A 150      24.650 -22.453  25.348  1.00122.90           C  
ATOM   1121  C   LYS A 150      25.647 -23.618  25.225  1.00120.02           C  
ATOM   1122  O   LYS A 150      26.684 -23.531  24.554  1.00121.62           O  
ATOM   1123  CB  LYS A 150      24.290 -21.772  24.003  1.00125.06           C  
ATOM   1124  CG  LYS A 150      23.360 -20.554  24.115  1.00128.24           C  
ATOM   1125  CD  LYS A 150      22.027 -20.894  24.784  1.00135.71           C  
ATOM   1126  CE  LYS A 150      21.187 -19.662  25.067  1.00140.41           C  
ATOM   1127  NZ  LYS A 150      20.609 -19.087  23.819  1.00142.76           N  
ATOM   1128  N   GLU A 151      25.336 -24.708  25.923  1.00121.50           N  
ATOM   1129  CA  GLU A 151      26.204 -25.899  25.947  1.00121.64           C  
ATOM   1130  C   GLU A 151      26.549 -26.373  24.503  1.00126.40           C  
ATOM   1131  O   GLU A 151      27.735 -26.441  24.111  1.00133.20           O  
ATOM   1132  CB  GLU A 151      25.554 -27.021  26.808  1.00119.26           C  
ATOM   1133  N   GLY A 152      25.513 -26.610  23.694  1.00124.52           N  
ATOM   1134  CA  GLY A 152      25.660 -26.958  22.275  1.00123.87           C  
ATOM   1135  C   GLY A 152      26.480 -26.080  21.330  1.00121.06           C  
ATOM   1136  O   GLY A 152      27.310 -26.601  20.583  1.00118.07           O  
ATOM   1137  N   LYS A 153      26.234 -24.771  21.335  1.00122.22           N  
ATOM   1138  CA  LYS A 153      26.972 -23.846  20.478  1.00126.63           C  
ATOM   1139  C   LYS A 153      28.444 -23.763  20.866  1.00127.52           C  
ATOM   1140  O   LYS A 153      29.304 -23.736  20.002  1.00131.59           O  
ATOM   1141  CB  LYS A 153      26.352 -22.446  20.515  1.00129.47           C  
ATOM   1142  CG  LYS A 153      24.934 -22.379  19.973  1.00133.69           C  
ATOM   1143  CD  LYS A 153      24.479 -20.942  19.774  1.00130.83           C  
ATOM   1144  CE  LYS A 153      22.993 -20.874  19.456  1.00125.71           C  
ATOM   1145  NZ  LYS A 153      22.498 -19.477  19.382  1.00123.10           N  
ATOM   1146  N   ASN A 154      28.734 -23.741  22.164  1.00129.30           N  
ATOM   1147  CA  ASN A 154      30.118 -23.579  22.629  1.00124.11           C  
ATOM   1148  C   ASN A 154      30.997 -24.782  22.323  1.00122.43           C  
ATOM   1149  O   ASN A 154      32.212 -24.634  22.193  1.00125.57           O  
ATOM   1150  CB  ASN A 154      30.160 -23.246  24.118  1.00123.91           C  
ATOM   1151  CG  ASN A 154      29.530 -21.900  24.426  1.00131.78           C  
ATOM   1152  OD1 ASN A 154      28.951 -21.250  23.553  1.00131.10           O  
ATOM   1153  ND2 ASN A 154      29.640 -21.470  25.674  1.00145.86           N  
ATOM   1154  N   HIS A 155      30.393 -25.962  22.196  1.00125.53           N  
ATOM   1155  CA  HIS A 155      31.126 -27.157  21.768  1.00133.91           C  
ATOM   1156  C   HIS A 155      31.187 -27.279  20.246  1.00137.50           C  
ATOM   1157  O   HIS A 155      32.195 -27.743  19.717  1.00144.27           O  
ATOM   1158  CB  HIS A 155      30.543 -28.425  22.397  1.00136.64           C  
ATOM   1159  CG  HIS A 155      30.690 -28.472  23.887  1.00141.10           C  
ATOM   1160  ND1 HIS A 155      29.673 -28.867  24.728  1.00141.22           N  
ATOM   1161  CD2 HIS A 155      31.730 -28.140  24.689  1.00148.24           C  
ATOM   1162  CE1 HIS A 155      30.084 -28.790  25.982  1.00144.67           C  
ATOM   1163  NE2 HIS A 155      31.328 -28.348  25.985  1.00148.95           N  
ATOM   1164  N   SER A 156      30.135 -26.851  19.547  1.00134.05           N  
ATOM   1165  CA  SER A 156      30.129 -26.859  18.077  1.00132.51           C  
ATOM   1166  C   SER A 156      31.257 -26.001  17.515  1.00126.51           C  
ATOM   1167  O   SER A 156      32.068 -26.474  16.716  1.00126.27           O  
ATOM   1168  CB  SER A 156      28.787 -26.366  17.532  1.00135.32           C  
ATOM   1169  OG  SER A 156      27.717 -27.101  18.087  1.00140.82           O  
ATOM   1170  N   GLN A 157      31.332 -24.761  17.989  1.00120.25           N  
ATOM   1171  CA  GLN A 157      32.351 -23.812  17.536  1.00114.73           C  
ATOM   1172  C   GLN A 157      33.719 -24.159  18.108  1.00109.72           C  
ATOM   1173  O   GLN A 157      34.720 -23.646  17.632  1.00104.74           O  
ATOM   1174  CB  GLN A 157      31.992 -22.371  17.920  1.00116.67           C  
ATOM   1175  CG  GLN A 157      30.534 -21.968  17.707  1.00119.60           C  
ATOM   1176  CD  GLN A 157      30.116 -21.902  16.255  1.00120.52           C  
ATOM   1177  OE1 GLN A 157      30.336 -20.890  15.594  1.00134.85           O  
ATOM   1178  NE2 GLN A 157      29.474 -22.958  15.760  1.00115.13           N  
ATOM   1179  N   GLY A 158      33.754 -25.006  19.138  1.00115.25           N  
ATOM   1180  CA  GLY A 158      35.002 -25.541  19.678  1.00122.96           C  
ATOM   1181  C   GLY A 158      35.728 -24.528  20.534  1.00127.60           C  
ATOM   1182  O   GLY A 158      36.955 -24.442  20.496  1.00137.72           O  
ATOM   1183  N   CYS A 159      34.969 -23.765  21.312  1.00125.15           N  
ATOM   1184  CA  CYS A 159      35.536 -22.764  22.196  1.00121.78           C  
ATOM   1185  C   CYS A 159      36.236 -23.448  23.354  1.00121.10           C  
ATOM   1186  O   CYS A 159      35.948 -24.602  23.667  1.00126.34           O  
ATOM   1187  CB  CYS A 159      34.429 -21.837  22.712  1.00124.46           C  
ATOM   1188  SG  CYS A 159      33.482 -20.962  21.429  1.00123.74           S  
ATOM   1189  N   GLY A 160      37.183 -22.736  23.936  1.00124.21           N  
ATOM   1190  CA  GLY A 160      37.939 -23.259  25.042  1.00124.95           C  
ATOM   1191  C   GLY A 160      37.017 -23.261  26.221  1.00125.80           C  
ATOM   1192  O   GLY A 160      35.844 -22.948  26.092  1.00123.51           O  
ATOM   1193  N   GLU A 161      37.549 -23.617  27.385  1.00128.04           N  
ATOM   1194  CA  GLU A 161      36.757 -23.660  28.609  1.00132.09           C  
ATOM   1195  C   GLU A 161      36.357 -22.258  29.057  1.00136.81           C  
ATOM   1196  O   GLU A 161      37.184 -21.348  29.092  1.00134.64           O  
ATOM   1197  CB  GLU A 161      37.531 -24.367  29.724  1.00129.59           C  
ATOM   1198  N   GLY A 162      35.083 -22.093  29.398  1.00137.56           N  
ATOM   1199  CA  GLY A 162      34.573 -20.809  29.842  1.00135.05           C  
ATOM   1200  C   GLY A 162      34.219 -19.894  28.686  1.00128.39           C  
ATOM   1201  O   GLY A 162      33.343 -19.038  28.805  1.00132.15           O  
ATOM   1202  N   GLN A 163      34.904 -20.077  27.562  1.00121.77           N  
ATOM   1203  CA  GLN A 163      34.662 -19.264  26.376  1.00119.17           C  
ATOM   1204  C   GLN A 163      33.272 -19.522  25.806  1.00112.19           C  
ATOM   1205  O   GLN A 163      32.644 -20.537  26.109  1.00112.68           O  
ATOM   1206  CB  GLN A 163      35.726 -19.538  25.312  1.00117.60           C  
ATOM   1207  CG  GLN A 163      36.942 -18.630  25.401  1.00109.87           C  
ATOM   1208  CD  GLN A 163      37.970 -18.925  24.327  1.00107.44           C  
ATOM   1209  OE1 GLN A 163      37.847 -19.900  23.585  1.00101.58           O  
ATOM   1210  NE2 GLN A 163      38.992 -18.082  24.238  1.00109.21           N  
ATOM   1211  N   VAL A 164      32.796 -18.598  24.978  1.00103.17           N  
ATOM   1212  CA  VAL A 164      31.479 -18.724  24.364  1.00 98.83           C  
ATOM   1213  C   VAL A 164      31.412 -17.967  23.042  1.00103.63           C  
ATOM   1214  O   VAL A 164      32.061 -16.934  22.874  1.00106.42           O  
ATOM   1215  CB  VAL A 164      30.369 -18.207  25.298  1.00 91.14           C  
ATOM   1216  CG1 VAL A 164      30.368 -18.987  26.603  1.00 91.37           C  
ATOM   1217  CG2 VAL A 164      30.546 -16.719  25.558  1.00 90.14           C  
ATOM   1218  N   ALA A 165      30.624 -18.487  22.107  1.00108.85           N  
ATOM   1219  CA  ALA A 165      30.471 -17.862  20.799  1.00110.80           C  
ATOM   1220  C   ALA A 165      30.210 -16.365  20.931  1.00107.56           C  
ATOM   1221  O   ALA A 165      29.902 -15.872  22.016  1.00108.38           O  
ATOM   1222  CB  ALA A 165      29.350 -18.531  20.019  1.00116.03           C  
ATOM   1223  N   CYS A 166      30.348 -15.519  19.937  1.00106.10           N  
ATOM   1224  CA  CYS A 166      29.975 -14.181  20.384  1.00100.80           C  
ATOM   1225  C   CYS A 166      28.771 -13.625  19.740  1.00 96.00           C  
ATOM   1226  O   CYS A 166      28.791 -12.694  18.963  1.00 91.08           O  
ATOM   1227  CB  CYS A 166      31.055 -13.159  20.697  1.00 99.52           C  
ATOM   1228  SG  CYS A 166      30.294 -11.806  21.641  1.00 96.95           S  
ATOM   1229  N   LEU A 167      27.712 -14.287  20.132  1.00 97.17           N  
ATOM   1230  CA  LEU A 167      26.315 -14.030  19.806  1.00 99.93           C  
ATOM   1231  C   LEU A 167      25.758 -12.878  20.636  1.00100.20           C  
ATOM   1232  O   LEU A 167      26.186 -12.652  21.768  1.00101.87           O  
ATOM   1233  CB  LEU A 167      25.474 -15.289  20.022  1.00 98.16           C  
ATOM   1234  CG  LEU A 167      25.564 -16.360  18.933  1.00 95.35           C  
ATOM   1235  CD1 LEU A 167      24.320 -17.235  18.935  1.00 96.54           C  
ATOM   1236  CD2 LEU A 167      25.774 -15.723  17.568  1.00 94.42           C  
ATOM   1237  N   PHE A 168      24.801 -12.153  20.066  1.00100.18           N  
ATOM   1238  CA  PHE A 168      24.184 -11.024  20.752  1.00 98.64           C  
ATOM   1239  C   PHE A 168      23.037 -11.483  21.647  1.00101.02           C  
ATOM   1240  O   PHE A 168      23.003 -11.170  22.837  1.00107.10           O  
ATOM   1241  CB  PHE A 168      23.681  -9.993  19.740  1.00 95.75           C  
ATOM   1242  CG  PHE A 168      23.129  -8.745  20.370  1.00 92.37           C  
ATOM   1243  CD1 PHE A 168      21.799  -8.674  20.747  1.00 91.96           C  
ATOM   1244  CD2 PHE A 168      23.942  -7.645  20.585  1.00 88.99           C  
ATOM   1245  CE1 PHE A 168      21.288  -7.528  21.326  1.00 88.96           C  
ATOM   1246  CE2 PHE A 168      23.438  -6.495  21.164  1.00 88.59           C  
ATOM   1247  CZ  PHE A 168      22.109  -6.437  21.535  1.00 87.98           C  
ATOM   1248  N   GLU A 169      22.100 -12.225  21.067  1.00 98.45           N  
ATOM   1249  CA  GLU A 169      20.949 -12.728  21.812  1.00 97.71           C  
ATOM   1250  C   GLU A 169      21.276 -13.878  22.765  1.00 96.71           C  
ATOM   1251  O   GLU A 169      20.395 -14.323  23.489  1.00103.13           O  
ATOM   1252  CB  GLU A 169      19.831 -13.154  20.862  1.00100.38           C  
ATOM   1253  CG  GLU A 169      19.210 -12.008  20.071  1.00102.53           C  
ATOM   1254  CD  GLU A 169      17.822 -12.332  19.543  1.00101.74           C  
ATOM   1255  OE1 GLU A 169      17.172 -11.454  18.929  1.00 98.10           O  
ATOM   1256  OE2 GLU A 169      17.364 -13.475  19.735  1.00103.89           O  
ATOM   1257  N   ASP A 170      22.514 -14.365  22.770  1.00 94.96           N  
ATOM   1258  CA  ASP A 170      22.933 -15.384  23.730  1.00 96.67           C  
ATOM   1259  C   ASP A 170      23.540 -14.829  25.025  1.00 97.35           C  
ATOM   1260  O   ASP A 170      23.450 -15.474  26.074  1.00 94.11           O  
ATOM   1261  CB  ASP A 170      23.914 -16.350  23.061  1.00 96.52           C  
ATOM   1262  CG  ASP A 170      23.254 -17.232  22.025  1.00 95.64           C  
ATOM   1263  OD1 ASP A 170      22.005 -17.242  21.920  1.00 95.86           O  
ATOM   1264  OD2 ASP A 170      23.996 -17.940  21.317  1.00 95.75           O  
ATOM   1265  N   VAL A 171      24.161 -13.655  24.948  1.00 97.22           N  
ATOM   1266  CA  VAL A 171      24.834 -13.058  26.111  1.00101.40           C  
ATOM   1267  C   VAL A 171      24.063 -11.895  26.726  1.00100.08           C  
ATOM   1268  O   VAL A 171      24.186 -11.654  27.929  1.00100.74           O  
ATOM   1269  CB  VAL A 171      26.285 -12.615  25.793  1.00104.09           C  
ATOM   1270  CG1 VAL A 171      27.122 -13.816  25.386  1.00105.65           C  
ATOM   1271  CG2 VAL A 171      26.335 -11.541  24.714  1.00105.46           C  
ATOM   1272  N   VAL A 172      23.286 -11.174  25.916  1.00 94.15           N  
ATOM   1273  CA  VAL A 172      22.542 -10.022  26.401  1.00 90.71           C  
ATOM   1274  C   VAL A 172      21.097 -10.433  26.614  1.00 96.81           C  
ATOM   1275  O   VAL A 172      20.423 -10.810  25.655  1.00104.47           O  
ATOM   1276  CB  VAL A 172      22.591  -8.841  25.419  1.00 84.39           C  
ATOM   1277  CG1 VAL A 172      21.979  -7.598  26.051  1.00 83.31           C  
ATOM   1278  CG2 VAL A 172      24.027  -8.564  24.997  1.00 86.15           C  
ATOM   1279  N   PRO A 173      20.609 -10.356  27.865  1.00 98.46           N  
ATOM   1280  CA  PRO A 173      19.227 -10.753  28.114  1.00 99.58           C  
ATOM   1281  C   PRO A 173      18.218  -9.797  27.456  1.00 98.40           C  
ATOM   1282  O   PRO A 173      18.441  -8.578  27.394  1.00 93.69           O  
ATOM   1283  CB  PRO A 173      19.124 -10.727  29.643  1.00 99.78           C  
ATOM   1284  CG  PRO A 173      20.150  -9.744  30.076  1.00 97.34           C  
ATOM   1285  CD  PRO A 173      21.269  -9.866  29.088  1.00 96.16           C  
ATOM   1286  N   MET A 174      17.131 -10.362  26.943  1.00 96.59           N  
ATOM   1287  CA  MET A 174      16.124  -9.568  26.242  1.00 97.49           C  
ATOM   1288  C   MET A 174      15.250  -8.714  27.166  1.00 97.51           C  
ATOM   1289  O   MET A 174      14.647  -7.760  26.693  1.00 93.64           O  
ATOM   1290  CB  MET A 174      15.238 -10.471  25.389  1.00 99.59           C  
ATOM   1291  CG  MET A 174      14.562  -9.769  24.221  1.00100.42           C  
ATOM   1292  SD  MET A 174      15.688  -9.064  22.988  1.00103.73           S  
ATOM   1293  CE  MET A 174      16.726 -10.455  22.572  1.00104.47           C  
ATOM   1294  N   ASN A 175      15.159  -9.054  28.455  1.00101.71           N  
ATOM   1295  CA  ASN A 175      14.410  -8.205  29.402  1.00 96.65           C  
ATOM   1296  C   ASN A 175      15.144  -6.891  29.677  1.00 91.96           C  
ATOM   1297  O   ASN A 175      14.492  -5.862  29.859  1.00 86.90           O  
ATOM   1298  CB  ASN A 175      14.056  -8.936  30.709  1.00 95.11           C  
ATOM   1299  CG  ASN A 175      15.249  -9.584  31.374  1.00 92.56           C  
ATOM   1300  OD1 ASN A 175      16.402  -9.253  31.093  1.00 96.44           O  
ATOM   1301  ND2 ASN A 175      14.976 -10.531  32.245  1.00 88.44           N  
ATOM   1302  N   TYR A 176      16.483  -6.928  29.698  1.00 87.19           N  
ATOM   1303  CA  TYR A 176      17.286  -5.695  29.735  1.00 83.00           C  
ATOM   1304  C   TYR A 176      17.017  -4.818  28.521  1.00 83.55           C  
ATOM   1305  O   TYR A 176      16.790  -3.619  28.657  1.00 85.89           O  
ATOM   1306  CB  TYR A 176      18.790  -5.975  29.829  1.00 79.98           C  
ATOM   1307  CG  TYR A 176      19.650  -4.761  29.541  1.00 81.67           C  
ATOM   1308  CD1 TYR A 176      20.010  -3.881  30.551  1.00 85.97           C  
ATOM   1309  CD2 TYR A 176      20.087  -4.479  28.250  1.00 85.44           C  
ATOM   1310  CE1 TYR A 176      20.799  -2.767  30.300  1.00 87.76           C  
ATOM   1311  CE2 TYR A 176      20.868  -3.358  27.984  1.00 87.46           C  
ATOM   1312  CZ  TYR A 176      21.226  -2.505  29.008  1.00 87.31           C  
ATOM   1313  OH  TYR A 176      22.012  -1.400  28.736  1.00 79.98           O  
ATOM   1314  N   MET A 177      17.051  -5.426  27.337  1.00 81.49           N  
ATOM   1315  CA  MET A 177      16.870  -4.684  26.095  1.00 75.83           C  
ATOM   1316  C   MET A 177      15.492  -4.063  25.920  1.00 74.99           C  
ATOM   1317  O   MET A 177      15.356  -2.992  25.343  1.00 71.40           O  
ATOM   1318  CB  MET A 177      17.150  -5.575  24.888  1.00 75.56           C  
ATOM   1319  CG  MET A 177      18.594  -5.990  24.806  1.00 77.54           C  
ATOM   1320  SD  MET A 177      19.612  -4.514  24.670  1.00 81.11           S  
ATOM   1321  CE  MET A 177      19.068  -4.000  23.058  1.00 84.80           C  
ATOM   1322  N   VAL A 178      14.473  -4.730  26.432  1.00 78.90           N  
ATOM   1323  CA  VAL A 178      13.104  -4.298  26.211  1.00 83.24           C  
ATOM   1324  C   VAL A 178      12.703  -3.328  27.311  1.00 83.23           C  
ATOM   1325  O   VAL A 178      12.277  -2.198  27.033  1.00 85.00           O  
ATOM   1326  CB  VAL A 178      12.102  -5.469  26.121  1.00 89.12           C  
ATOM   1327  CG1 VAL A 178      10.675  -4.953  26.040  1.00 90.36           C  
ATOM   1328  CG2 VAL A 178      12.392  -6.331  24.894  1.00 93.40           C  
ATOM   1329  N   TYR A 179      12.818  -3.774  28.558  1.00 82.68           N  
ATOM   1330  CA  TYR A 179      12.356  -2.960  29.677  1.00 82.59           C  
ATOM   1331  C   TYR A 179      13.312  -1.819  29.980  1.00 78.68           C  
ATOM   1332  O   TYR A 179      12.895  -0.665  30.038  1.00 82.30           O  
ATOM   1333  CB  TYR A 179      12.124  -3.802  30.933  1.00 85.51           C  
ATOM   1334  CG  TYR A 179      10.949  -4.768  30.854  1.00 86.74           C  
ATOM   1335  CD1 TYR A 179       9.690  -4.360  30.384  1.00 80.94           C  
ATOM   1336  CD2 TYR A 179      11.087  -6.091  31.292  1.00 93.64           C  
ATOM   1337  CE1 TYR A 179       8.627  -5.253  30.327  1.00 81.59           C  
ATOM   1338  CE2 TYR A 179      10.033  -6.987  31.243  1.00 90.90           C  
ATOM   1339  CZ  TYR A 179       8.812  -6.567  30.764  1.00 87.18           C  
ATOM   1340  OH  TYR A 179       7.803  -7.489  30.734  1.00 90.57           O  
ATOM   1341  N   PHE A 180      14.587  -2.134  30.145  1.00 79.48           N  
ATOM   1342  CA  PHE A 180      15.559  -1.145  30.585  1.00 84.74           C  
ATOM   1343  C   PHE A 180      15.982  -0.227  29.445  1.00 85.17           C  
ATOM   1344  O   PHE A 180      15.889   0.988  29.566  1.00 78.26           O  
ATOM   1345  CB  PHE A 180      16.778  -1.842  31.201  1.00 90.31           C  
ATOM   1346  CG  PHE A 180      17.672  -0.933  31.989  1.00 88.70           C  
ATOM   1347  CD1 PHE A 180      17.364  -0.604  33.304  1.00 89.41           C  
ATOM   1348  CD2 PHE A 180      18.825  -0.417  31.419  1.00 85.29           C  
ATOM   1349  CE1 PHE A 180      18.188   0.234  34.027  1.00 91.53           C  
ATOM   1350  CE2 PHE A 180      19.661   0.404  32.140  1.00 87.44           C  
ATOM   1351  CZ  PHE A 180      19.341   0.737  33.444  1.00 91.13           C  
ATOM   1352  N   ASN A 181      16.452  -0.805  28.346  1.00 90.11           N  
ATOM   1353  CA  ASN A 181      17.010  -0.002  27.254  1.00 92.57           C  
ATOM   1354  C   ASN A 181      15.919   0.672  26.414  1.00 91.64           C  
ATOM   1355  O   ASN A 181      15.946   1.883  26.228  1.00 87.93           O  
ATOM   1356  CB  ASN A 181      17.936  -0.846  26.376  1.00 91.48           C  
ATOM   1357  CG  ASN A 181      18.737  -0.015  25.420  1.00 88.38           C  
ATOM   1358  OD1 ASN A 181      18.350   0.167  24.274  1.00 87.97           O  
ATOM   1359  ND2 ASN A 181      19.839   0.530  25.898  1.00 91.88           N  
ATOM   1360  N   PHE A 182      14.956  -0.100  25.922  1.00 90.99           N  
ATOM   1361  CA  PHE A 182      13.931   0.465  25.043  1.00 93.26           C  
ATOM   1362  C   PHE A 182      12.949   1.383  25.777  1.00 96.85           C  
ATOM   1363  O   PHE A 182      12.918   2.587  25.512  1.00102.16           O  
ATOM   1364  CB  PHE A 182      13.175  -0.634  24.295  1.00 93.20           C  
ATOM   1365  CG  PHE A 182      12.116  -0.118  23.344  1.00 94.18           C  
ATOM   1366  CD1 PHE A 182      12.307   1.055  22.601  1.00 94.44           C  
ATOM   1367  CD2 PHE A 182      10.931  -0.829  23.163  1.00 94.82           C  
ATOM   1368  CE1 PHE A 182      11.336   1.510  21.729  1.00 92.72           C  
ATOM   1369  CE2 PHE A 182       9.962  -0.381  22.278  1.00 95.90           C  
ATOM   1370  CZ  PHE A 182      10.162   0.793  21.565  1.00 94.32           C  
ATOM   1371  N   PHE A 183      12.161   0.820  26.695  1.00 94.21           N  
ATOM   1372  CA  PHE A 183      11.118   1.595  27.389  1.00 84.88           C  
ATOM   1373  C   PHE A 183      11.680   2.749  28.210  1.00 76.69           C  
ATOM   1374  O   PHE A 183      11.279   3.883  28.011  1.00 74.08           O  
ATOM   1375  CB  PHE A 183      10.228   0.707  28.270  1.00 83.73           C  
ATOM   1376  CG  PHE A 183       9.352  -0.257  27.503  1.00 84.33           C  
ATOM   1377  CD1 PHE A 183       8.988  -0.033  26.180  1.00 85.05           C  
ATOM   1378  CD2 PHE A 183       8.865  -1.395  28.127  1.00 85.68           C  
ATOM   1379  CE1 PHE A 183       8.172  -0.927  25.503  1.00 84.89           C  
ATOM   1380  CE2 PHE A 183       8.049  -2.294  27.451  1.00 84.69           C  
ATOM   1381  CZ  PHE A 183       7.703  -2.061  26.136  1.00 82.29           C  
ATOM   1382  N   ALA A 184      12.640   2.474  29.079  1.00 70.32           N  
ATOM   1383  CA  ALA A 184      13.148   3.492  29.982  1.00 71.12           C  
ATOM   1384  C   ALA A 184      14.173   4.431  29.377  1.00 66.63           C  
ATOM   1385  O   ALA A 184      14.100   5.631  29.589  1.00 62.92           O  
ATOM   1386  CB  ALA A 184      13.732   2.836  31.211  1.00 77.70           C  
ATOM   1387  N   CYS A 185      15.139   3.889  28.650  1.00 69.34           N  
ATOM   1388  CA  CYS A 185      16.288   4.689  28.173  1.00 74.28           C  
ATOM   1389  C   CYS A 185      16.147   5.305  26.772  1.00 77.91           C  
ATOM   1390  O   CYS A 185      16.904   6.215  26.426  1.00 72.82           O  
ATOM   1391  CB  CYS A 185      17.567   3.858  28.196  1.00 75.35           C  
ATOM   1392  SG  CYS A 185      18.105   3.318  29.826  1.00 81.13           S  
ATOM   1393  N   VAL A 186      15.215   4.800  25.966  1.00 84.71           N  
ATOM   1394  CA  VAL A 186      15.023   5.297  24.601  1.00 85.36           C  
ATOM   1395  C   VAL A 186      13.642   5.909  24.416  1.00 83.83           C  
ATOM   1396  O   VAL A 186      13.525   7.065  24.031  1.00 81.40           O  
ATOM   1397  CB  VAL A 186      15.253   4.180  23.560  1.00 88.65           C  
ATOM   1398  CG1 VAL A 186      15.029   4.700  22.145  1.00 89.02           C  
ATOM   1399  CG2 VAL A 186      16.669   3.631  23.676  1.00 93.14           C  
ATOM   1400  N   LEU A 187      12.604   5.134  24.697  1.00 83.82           N  
ATOM   1401  CA  LEU A 187      11.242   5.560  24.406  1.00 84.04           C  
ATOM   1402  C   LEU A 187      10.813   6.736  25.277  1.00 82.70           C  
ATOM   1403  O   LEU A 187      10.219   7.691  24.775  1.00 81.06           O  
ATOM   1404  CB  LEU A 187      10.271   4.388  24.571  1.00 86.62           C  
ATOM   1405  CG  LEU A 187       8.864   4.565  24.006  1.00 87.21           C  
ATOM   1406  CD1 LEU A 187       8.906   4.960  22.541  1.00 89.86           C  
ATOM   1407  CD2 LEU A 187       8.064   3.285  24.182  1.00 88.79           C  
ATOM   1408  N   VAL A 188      11.121   6.674  26.569  1.00 81.37           N  
ATOM   1409  CA  VAL A 188      10.756   7.756  27.472  1.00 82.77           C  
ATOM   1410  C   VAL A 188      11.424   9.083  27.079  1.00 83.65           C  
ATOM   1411  O   VAL A 188      10.730  10.093  26.995  1.00 83.24           O  
ATOM   1412  CB  VAL A 188      11.010   7.390  28.954  1.00 82.79           C  
ATOM   1413  CG1 VAL A 188      10.969   8.624  29.850  1.00 83.56           C  
ATOM   1414  CG2 VAL A 188       9.975   6.380  29.428  1.00 83.20           C  
ATOM   1415  N   PRO A 189      12.755   9.094  26.833  1.00 77.91           N  
ATOM   1416  CA  PRO A 189      13.348  10.362  26.376  1.00 74.78           C  
ATOM   1417  C   PRO A 189      12.791  10.865  25.049  1.00 77.97           C  
ATOM   1418  O   PRO A 189      12.652  12.068  24.876  1.00 82.79           O  
ATOM   1419  CB  PRO A 189      14.826  10.031  26.233  1.00 74.00           C  
ATOM   1420  CG  PRO A 189      15.041   8.932  27.202  1.00 75.88           C  
ATOM   1421  CD  PRO A 189      13.795   8.105  27.166  1.00 75.36           C  
ATOM   1422  N   LEU A 190      12.472   9.955  24.129  1.00 81.14           N  
ATOM   1423  CA  LEU A 190      11.851  10.337  22.857  1.00 80.61           C  
ATOM   1424  C   LEU A 190      10.519  11.043  23.067  1.00 79.13           C  
ATOM   1425  O   LEU A 190      10.264  12.076  22.450  1.00 79.53           O  
ATOM   1426  CB  LEU A 190      11.654   9.126  21.939  1.00 80.83           C  
ATOM   1427  CG  LEU A 190      12.898   8.577  21.233  1.00 82.46           C  
ATOM   1428  CD1 LEU A 190      12.528   7.376  20.372  1.00 85.54           C  
ATOM   1429  CD2 LEU A 190      13.577   9.638  20.383  1.00 83.91           C  
ATOM   1430  N   LEU A 191       9.681  10.499  23.943  1.00 75.82           N  
ATOM   1431  CA  LEU A 191       8.413  11.149  24.251  1.00 77.18           C  
ATOM   1432  C   LEU A 191       8.608  12.503  24.932  1.00 77.29           C  
ATOM   1433  O   LEU A 191       7.822  13.423  24.708  1.00 74.41           O  
ATOM   1434  CB  LEU A 191       7.548  10.253  25.124  1.00 76.24           C  
ATOM   1435  CG  LEU A 191       7.100   8.963  24.471  1.00 76.96           C  
ATOM   1436  CD1 LEU A 191       6.351   8.161  25.524  1.00 77.46           C  
ATOM   1437  CD2 LEU A 191       6.251   9.229  23.233  1.00 74.45           C  
ATOM   1438  N   LEU A 192       9.652  12.629  25.749  1.00 77.30           N  
ATOM   1439  CA  LEU A 192       9.962  13.911  26.376  1.00 79.30           C  
ATOM   1440  C   LEU A 192      10.356  14.931  25.316  1.00 79.34           C  
ATOM   1441  O   LEU A 192       9.887  16.067  25.346  1.00 73.87           O  
ATOM   1442  CB  LEU A 192      11.058  13.764  27.443  1.00 80.38           C  
ATOM   1443  CG  LEU A 192      10.699  12.885  28.653  1.00 78.66           C  
ATOM   1444  CD1 LEU A 192      11.921  12.675  29.525  1.00 76.86           C  
ATOM   1445  CD2 LEU A 192       9.542  13.438  29.474  1.00 79.14           C  
ATOM   1446  N   MET A 193      11.186  14.511  24.361  1.00 86.11           N  
ATOM   1447  CA  MET A 193      11.577  15.385  23.245  1.00 86.21           C  
ATOM   1448  C   MET A 193      10.356  15.815  22.447  1.00 87.10           C  
ATOM   1449  O   MET A 193      10.271  16.974  22.043  1.00 85.07           O  
ATOM   1450  CB  MET A 193      12.582  14.701  22.321  1.00 84.13           C  
ATOM   1451  CG  MET A 193      13.943  14.499  22.939  1.00 86.18           C  
ATOM   1452  SD  MET A 193      15.031  13.633  21.807  1.00 97.84           S  
ATOM   1453  CE  MET A 193      15.704  12.313  22.823  1.00106.21           C  
ATOM   1454  N   LEU A 194       9.415  14.889  22.230  1.00 86.59           N  
ATOM   1455  CA  LEU A 194       8.156  15.211  21.552  1.00 86.21           C  
ATOM   1456  C   LEU A 194       7.439  16.301  22.320  1.00 80.63           C  
ATOM   1457  O   LEU A 194       6.953  17.244  21.724  1.00 82.28           O  
ATOM   1458  CB  LEU A 194       7.249  13.981  21.410  1.00 93.53           C  
ATOM   1459  CG  LEU A 194       5.782  14.241  21.010  1.00102.36           C  
ATOM   1460  CD1 LEU A 194       5.732  14.789  19.592  1.00102.23           C  
ATOM   1461  CD2 LEU A 194       4.909  13.003  21.170  1.00107.66           C  
ATOM   1462  N   GLY A 195       7.372  16.164  23.639  1.00 77.40           N  
ATOM   1463  CA  GLY A 195       6.708  17.153  24.479  1.00 79.97           C  
ATOM   1464  C   GLY A 195       7.358  18.522  24.442  1.00 75.36           C  
ATOM   1465  O   GLY A 195       6.673  19.539  24.372  1.00 74.92           O  
ATOM   1466  N   VAL A 196       8.684  18.544  24.476  1.00 71.97           N  
ATOM   1467  CA  VAL A 196       9.418  19.798  24.491  1.00 74.56           C  
ATOM   1468  C   VAL A 196       9.178  20.542  23.183  1.00 79.37           C  
ATOM   1469  O   VAL A 196       8.926  21.745  23.182  1.00 83.71           O  
ATOM   1470  CB  VAL A 196      10.936  19.589  24.679  1.00 76.84           C  
ATOM   1471  CG1 VAL A 196      11.661  20.921  24.552  1.00 77.53           C  
ATOM   1472  CG2 VAL A 196      11.264  18.950  26.027  1.00 75.15           C  
ATOM   1473  N   TYR A 197       9.260  19.821  22.071  1.00 85.95           N  
ATOM   1474  CA  TYR A 197       9.052  20.435  20.755  1.00 85.43           C  
ATOM   1475  C   TYR A 197       7.607  20.899  20.551  1.00 87.33           C  
ATOM   1476  O   TYR A 197       7.389  21.931  19.925  1.00 81.03           O  
ATOM   1477  CB  TYR A 197       9.508  19.507  19.623  1.00 80.95           C  
ATOM   1478  CG  TYR A 197      11.004  19.537  19.388  1.00 74.89           C  
ATOM   1479  CD1 TYR A 197      11.632  20.694  18.942  1.00 75.09           C  
ATOM   1480  CD2 TYR A 197      11.788  18.408  19.601  1.00 72.07           C  
ATOM   1481  CE1 TYR A 197      12.998  20.730  18.722  1.00 76.42           C  
ATOM   1482  CE2 TYR A 197      13.155  18.430  19.383  1.00 72.55           C  
ATOM   1483  CZ  TYR A 197      13.753  19.592  18.941  1.00 75.43           C  
ATOM   1484  OH  TYR A 197      15.108  19.616  18.710  1.00 82.02           O  
ATOM   1485  N   LEU A 198       6.635  20.161  21.098  1.00 93.07           N  
ATOM   1486  CA  LEU A 198       5.236  20.626  21.131  1.00 95.85           C  
ATOM   1487  C   LEU A 198       5.096  21.999  21.794  1.00 96.12           C  
ATOM   1488  O   LEU A 198       4.443  22.899  21.240  1.00106.50           O  
ATOM   1489  CB  LEU A 198       4.314  19.617  21.843  1.00 96.46           C  
ATOM   1490  CG  LEU A 198       3.979  18.318  21.112  1.00100.44           C  
ATOM   1491  CD1 LEU A 198       3.111  17.418  21.994  1.00101.52           C  
ATOM   1492  CD2 LEU A 198       3.314  18.600  19.775  1.00 98.44           C  
ATOM   1493  N   ARG A 199       5.731  22.160  22.949  1.00 94.91           N  
ATOM   1494  CA  ARG A 199       5.701  23.424  23.671  1.00 98.86           C  
ATOM   1495  C   ARG A 199       6.427  24.523  22.891  1.00100.31           C  
ATOM   1496  O   ARG A 199       6.033  25.689  22.933  1.00109.80           O  
ATOM   1497  CB  ARG A 199       6.289  23.252  25.072  1.00102.11           C  
ATOM   1498  CG  ARG A 199       5.517  22.286  25.956  1.00106.96           C  
ATOM   1499  CD  ARG A 199       4.130  22.818  26.276  1.00112.00           C  
ATOM   1500  NE  ARG A 199       3.383  21.912  27.144  1.00121.07           N  
ATOM   1501  CZ  ARG A 199       2.082  22.016  27.390  1.00122.35           C  
ATOM   1502  NH1 ARG A 199       1.485  21.146  28.194  1.00121.30           N  
ATOM   1503  NH2 ARG A 199       1.376  22.990  26.833  1.00123.42           N  
ATOM   1504  N   ILE A 200       7.485  24.146  22.176  1.00 95.02           N  
ATOM   1505  CA  ILE A 200       8.247  25.118  21.389  1.00 91.65           C  
ATOM   1506  C   ILE A 200       7.339  25.719  20.328  1.00 87.56           C  
ATOM   1507  O   ILE A 200       7.226  26.933  20.221  1.00 87.42           O  
ATOM   1508  CB  ILE A 200       9.549  24.540  20.756  1.00 90.29           C  
ATOM   1509  CG1 ILE A 200      10.620  24.300  21.836  1.00 88.72           C  
ATOM   1510  CG2 ILE A 200      10.108  25.513  19.714  1.00 91.70           C  
ATOM   1511  CD1 ILE A 200      11.932  23.714  21.345  1.00 84.99           C  
ATOM   1512  N   PHE A 201       6.669  24.863  19.573  1.00 85.04           N  
ATOM   1513  CA  PHE A 201       5.790  25.339  18.515  1.00 87.33           C  
ATOM   1514  C   PHE A 201       4.583  26.088  19.053  1.00 86.32           C  
ATOM   1515  O   PHE A 201       4.117  27.034  18.420  1.00 88.18           O  
ATOM   1516  CB  PHE A 201       5.342  24.188  17.612  1.00 90.26           C  
ATOM   1517  CG  PHE A 201       6.473  23.528  16.871  1.00 87.83           C  
ATOM   1518  CD1 PHE A 201       7.324  24.277  16.069  1.00 85.58           C  
ATOM   1519  CD2 PHE A 201       6.689  22.160  16.972  1.00 88.07           C  
ATOM   1520  CE1 PHE A 201       8.368  23.678  15.394  1.00 81.22           C  
ATOM   1521  CE2 PHE A 201       7.736  21.556  16.298  1.00 86.31           C  
ATOM   1522  CZ  PHE A 201       8.571  22.316  15.506  1.00 82.46           C  
ATOM   1523  N   LEU A 202       4.075  25.668  20.207  1.00 87.78           N  
ATOM   1524  CA  LEU A 202       2.933  26.364  20.809  1.00 93.24           C  
ATOM   1525  C   LEU A 202       3.323  27.718  21.368  1.00 93.05           C  
ATOM   1526  O   LEU A 202       2.560  28.668  21.248  1.00 86.23           O  
ATOM   1527  CB  LEU A 202       2.258  25.517  21.890  1.00 97.72           C  
ATOM   1528  CG  LEU A 202       1.336  24.447  21.304  1.00105.56           C  
ATOM   1529  CD1 LEU A 202       1.076  23.349  22.330  1.00111.52           C  
ATOM   1530  CD2 LEU A 202       0.030  25.067  20.795  1.00106.59           C  
ATOM   1531  N   ALA A 203       4.506  27.811  21.971  1.00 94.91           N  
ATOM   1532  CA  ALA A 203       4.999  29.086  22.491  1.00 98.00           C  
ATOM   1533  C   ALA A 203       5.198  30.095  21.361  1.00100.55           C  
ATOM   1534  O   ALA A 203       4.863  31.266  21.514  1.00103.53           O  
ATOM   1535  CB  ALA A 203       6.292  28.892  23.274  1.00 97.56           C  
ATOM   1536  N   ALA A 204       5.722  29.634  20.228  1.00101.28           N  
ATOM   1537  CA  ALA A 204       5.919  30.498  19.066  1.00101.46           C  
ATOM   1538  C   ALA A 204       4.581  30.972  18.505  1.00101.13           C  
ATOM   1539  O   ALA A 204       4.414  32.136  18.184  1.00 98.37           O  
ATOM   1540  CB  ALA A 204       6.720  29.774  17.997  1.00 98.70           C  
ATOM   1541  N   ARG A 205       3.633  30.058  18.395  1.00109.32           N  
ATOM   1542  CA  ARG A 205       2.290  30.394  17.946  1.00122.29           C  
ATOM   1543  C   ARG A 205       1.579  31.438  18.833  1.00126.61           C  
ATOM   1544  O   ARG A 205       0.919  32.339  18.308  1.00137.71           O  
ATOM   1545  CB  ARG A 205       1.467  29.111  17.834  1.00129.77           C  
ATOM   1546  CG  ARG A 205      -0.033  29.296  17.724  1.00138.80           C  
ATOM   1547  CD  ARG A 205      -0.693  27.986  17.337  1.00147.56           C  
ATOM   1548  NE  ARG A 205      -0.426  27.648  15.936  1.00159.62           N  
ATOM   1549  CZ  ARG A 205      -1.062  28.162  14.876  1.00167.58           C  
ATOM   1550  NH1 ARG A 205      -2.035  29.066  15.016  1.00167.69           N  
ATOM   1551  NH2 ARG A 205      -0.717  27.767  13.652  1.00171.69           N  
ATOM   1552  N   ARG A 206       1.708  31.317  20.155  1.00119.54           N  
ATOM   1553  CA  ARG A 206       1.089  32.280  21.081  1.00111.93           C  
ATOM   1554  C   ARG A 206       1.738  33.660  21.130  1.00111.05           C  
ATOM   1555  O   ARG A 206       1.050  34.660  21.343  1.00113.58           O  
ATOM   1556  CB  ARG A 206       1.033  31.731  22.507  1.00108.07           C  
ATOM   1557  CG  ARG A 206       0.471  32.706  23.534  1.00100.07           C  
ATOM   1558  N   GLN A 207       3.039  33.697  20.919  1.00109.55           N  
ATOM   1559  CA  GLN A 207       3.724  34.959  20.921  1.00113.53           C  
ATOM   1560  C   GLN A 207       3.336  35.718  19.688  1.00114.47           C  
ATOM   1561  O   GLN A 207       2.888  36.843  19.771  1.00121.53           O  
ATOM   1562  CB  GLN A 207       5.224  34.755  20.911  1.00114.66           C  
ATOM   1563  CG  GLN A 207       5.742  34.143  22.196  1.00122.16           C  
ATOM   1564  CD  GLN A 207       7.226  33.876  22.151  1.00122.85           C  
ATOM   1565  OE1 GLN A 207       7.798  33.705  21.086  1.00115.92           O  
ATOM   1566  NE2 GLN A 207       7.854  33.833  23.313  1.00127.14           N  
ATOM   1567  N   LEU A 208       3.476  35.085  18.536  1.00113.15           N  
ATOM   1568  CA  LEU A 208       3.110  35.733  17.292  1.00111.19           C  
ATOM   1569  C   LEU A 208       1.729  36.300  17.474  1.00103.18           C  
ATOM   1570  O   LEU A 208       1.491  37.468  17.215  1.00 94.26           O  
ATOM   1571  CB  LEU A 208       3.121  34.813  16.088  1.00120.10           C  
ATOM   1572  CG  LEU A 208       4.476  34.241  15.682  1.00129.00           C  
ATOM   1573  CD1 LEU A 208       4.307  33.232  14.563  1.00133.30           C  
ATOM   1574  CD2 LEU A 208       5.448  35.326  15.261  1.00129.29           C  
ATOM   1575  N   ALA A1001       0.813  35.467  17.930  1.00121.25           N  
ATOM   1576  CA  ALA A1001      -0.543  35.921  18.140  1.00124.23           C  
ATOM   1577  C   ALA A1001      -0.543  37.167  18.991  1.00121.44           C  
ATOM   1578  O   ALA A1001      -1.045  38.207  18.595  1.00118.72           O  
ATOM   1579  CB  ALA A1001      -1.362  34.837  18.802  1.00125.66           C  
ATOM   1580  N   ASP A1002       0.024  37.070  20.175  1.00124.96           N  
ATOM   1581  CA  ASP A1002       0.039  38.262  21.044  1.00129.15           C  
ATOM   1582  C   ASP A1002       0.381  39.563  20.329  1.00127.25           C  
ATOM   1583  O   ASP A1002      -0.349  40.550  20.472  1.00135.38           O  
ATOM   1584  CB  ASP A1002       0.987  38.072  22.237  1.00134.82           C  
ATOM   1585  CG  ASP A1002       0.443  37.101  23.275  1.00140.94           C  
ATOM   1586  OD1 ASP A1002      -0.613  36.476  23.035  1.00146.77           O  
ATOM   1587  OD2 ASP A1002       1.077  36.954  24.339  1.00143.71           O  
ATOM   1588  N   LEU A1003       1.478  39.565  19.572  1.00121.12           N  
ATOM   1589  CA  LEU A1003       1.870  40.732  18.758  1.00121.31           C  
ATOM   1590  C   LEU A1003       0.836  41.131  17.713  1.00127.80           C  
ATOM   1591  O   LEU A1003       0.654  42.327  17.441  1.00130.63           O  
ATOM   1592  CB  LEU A1003       3.185  40.477  18.014  1.00117.48           C  
ATOM   1593  CG  LEU A1003       4.494  40.780  18.739  1.00118.12           C  
ATOM   1594  CD1 LEU A1003       4.728  39.844  19.917  1.00124.49           C  
ATOM   1595  CD2 LEU A1003       5.671  40.717  17.766  1.00110.13           C  
ATOM   1596  N   GLU A1004       0.176  40.128  17.121  1.00130.40           N  
ATOM   1597  CA  GLU A1004      -0.867  40.395  16.127  1.00131.58           C  
ATOM   1598  C   GLU A1004      -2.025  41.061  16.836  1.00126.80           C  
ATOM   1599  O   GLU A1004      -2.582  42.014  16.302  1.00126.72           O  
ATOM   1600  CB  GLU A1004      -1.369  39.146  15.369  1.00136.40           C  
ATOM   1601  CG  GLU A1004      -2.272  39.476  14.170  1.00143.70           C  
ATOM   1602  CD  GLU A1004      -1.525  40.196  13.056  1.00147.59           C  
ATOM   1603  OE1 GLU A1004      -0.355  39.837  12.817  1.00155.27           O  
ATOM   1604  OE2 GLU A1004      -2.090  41.118  12.416  1.00141.68           O  
ATOM   1605  N   ASP A1005      -2.373  40.575  18.032  1.00124.74           N  
ATOM   1606  CA  ASP A1005      -3.459  41.174  18.808  1.00126.11           C  
ATOM   1607  C   ASP A1005      -3.123  42.581  19.236  1.00123.98           C  
ATOM   1608  O   ASP A1005      -3.970  43.465  19.140  1.00129.23           O  
ATOM   1609  CB  ASP A1005      -3.807  40.345  20.047  1.00133.82           C  
ATOM   1610  CG  ASP A1005      -4.523  39.065  19.709  1.00141.41           C  
ATOM   1611  OD1 ASP A1005      -5.179  39.000  18.649  1.00145.53           O  
ATOM   1612  OD2 ASP A1005      -4.432  38.121  20.516  1.00150.74           O  
ATOM   1613  N   ASN A1006      -1.902  42.787  19.717  1.00124.02           N  
ATOM   1614  CA  ASN A1006      -1.461  44.126  20.089  1.00134.07           C  
ATOM   1615  C   ASN A1006      -1.439  45.064  18.882  1.00138.02           C  
ATOM   1616  O   ASN A1006      -1.807  46.232  19.010  1.00150.85           O  
ATOM   1617  CB  ASN A1006      -0.089  44.089  20.770  1.00137.28           C  
ATOM   1618  CG  ASN A1006      -0.160  43.652  22.234  1.00139.19           C  
ATOM   1619  OD1 ASN A1006      -1.169  43.847  22.913  1.00133.05           O  
ATOM   1620  ND2 ASN A1006       0.928  43.072  22.730  1.00142.71           N  
ATOM   1621  N   TRP A1007      -1.030  44.553  17.720  1.00131.78           N  
ATOM   1622  CA  TRP A1007      -0.980  45.359  16.493  1.00128.99           C  
ATOM   1623  C   TRP A1007      -2.377  45.776  16.039  1.00130.76           C  
ATOM   1624  O   TRP A1007      -2.604  46.938  15.718  1.00125.64           O  
ATOM   1625  CB  TRP A1007      -0.260  44.594  15.382  1.00130.66           C  
ATOM   1626  CG  TRP A1007      -0.316  45.232  14.029  1.00135.32           C  
ATOM   1627  CD1 TRP A1007      -1.073  44.819  12.969  1.00139.78           C  
ATOM   1628  CD2 TRP A1007       0.418  46.382  13.577  1.00133.76           C  
ATOM   1629  NE1 TRP A1007      -0.857  45.640  11.885  1.00140.32           N  
ATOM   1630  CE2 TRP A1007       0.052  46.607  12.230  1.00135.15           C  
ATOM   1631  CE3 TRP A1007       1.344  47.247  14.179  1.00126.67           C  
ATOM   1632  CZ2 TRP A1007       0.576  47.668  11.474  1.00127.64           C  
ATOM   1633  CZ3 TRP A1007       1.870  48.305  13.420  1.00122.29           C  
ATOM   1634  CH2 TRP A1007       1.480  48.503  12.086  1.00122.61           C  
ATOM   1635  N   GLU A1008      -3.308  44.831  16.027  1.00146.60           N  
ATOM   1636  CA  GLU A1008      -4.692  45.137  15.669  1.00155.54           C  
ATOM   1637  C   GLU A1008      -5.355  46.036  16.719  1.00159.94           C  
ATOM   1638  O   GLU A1008      -6.090  46.952  16.358  1.00174.67           O  
ATOM   1639  CB  GLU A1008      -5.498  43.857  15.450  1.00157.49           C  
ATOM   1640  CG  GLU A1008      -5.057  43.061  14.226  1.00152.97           C  
ATOM   1641  CD  GLU A1008      -5.908  41.823  13.979  1.00155.45           C  
ATOM   1642  OE1 GLU A1008      -6.928  41.631  14.679  1.00156.30           O  
ATOM   1643  OE2 GLU A1008      -5.577  41.034  13.068  1.00151.60           O  
ATOM   1644  N   THR A1009      -5.074  45.793  18.000  1.00157.59           N  
ATOM   1645  CA  THR A1009      -5.536  46.680  19.075  1.00159.01           C  
ATOM   1646  C   THR A1009      -5.069  48.120  18.843  1.00157.04           C  
ATOM   1647  O   THR A1009      -5.822  49.057  19.095  1.00166.67           O  
ATOM   1648  CB  THR A1009      -5.059  46.195  20.464  1.00162.27           C  
ATOM   1649  OG1 THR A1009      -5.548  44.872  20.697  1.00170.26           O  
ATOM   1650  CG2 THR A1009      -5.559  47.102  21.588  1.00164.35           C  
ATOM   1651  N   LEU A1010      -3.838  48.289  18.362  1.00141.85           N  
ATOM   1652  CA  LEU A1010      -3.309  49.623  18.057  1.00131.01           C  
ATOM   1653  C   LEU A1010      -4.118  50.313  16.956  1.00132.36           C  
ATOM   1654  O   LEU A1010      -4.510  51.475  17.093  1.00135.28           O  
ATOM   1655  CB  LEU A1010      -1.830  49.544  17.653  1.00121.37           C  
ATOM   1656  CG  LEU A1010      -1.028  50.848  17.666  1.00119.96           C  
ATOM   1657  CD1 LEU A1010      -0.723  51.275  19.095  1.00116.67           C  
ATOM   1658  CD2 LEU A1010       0.260  50.710  16.855  1.00123.31           C  
ATOM   1659  N   ASN A1011      -4.391  49.583  15.881  1.00132.92           N  
ATOM   1660  CA  ASN A1011      -5.057  50.160  14.714  1.00133.12           C  
ATOM   1661  C   ASN A1011      -6.583  50.261  14.831  1.00132.83           C  
ATOM   1662  O   ASN A1011      -7.183  51.171  14.263  1.00132.07           O  
ATOM   1663  CB  ASN A1011      -4.667  49.384  13.454  1.00136.43           C  
ATOM   1664  CG  ASN A1011      -3.177  49.465  13.155  1.00137.81           C  
ATOM   1665  OD1 ASN A1011      -2.703  50.442  12.577  1.00132.07           O  
ATOM   1666  ND2 ASN A1011      -2.432  48.428  13.536  1.00149.02           N  
ATOM   1667  N   ASP A1012      -7.197  49.377  15.585  1.00138.31           N  
ATOM   1668  CA  ASP A1012      -8.618  49.501  15.728  1.00140.21           C  
ATOM   1669  C   ASP A1012      -8.840  50.714  16.610  1.00145.54           C  
ATOM   1670  O   ASP A1012      -9.450  51.685  16.186  1.00153.25           O  
ATOM   1671  CB  ASP A1012      -9.217  48.239  16.311  1.00140.89           C  
ATOM   1672  CG  ASP A1012      -9.111  47.070  15.364  1.00139.08           C  
ATOM   1673  OD1 ASP A1012      -9.077  47.308  14.144  1.00139.60           O  
ATOM   1674  OD2 ASP A1012      -9.051  45.917  15.829  1.00130.30           O  
ATOM   1675  N   ASN A1013      -8.323  50.686  17.828  1.00147.13           N  
ATOM   1676  CA  ASN A1013      -8.524  51.841  18.715  1.00157.31           C  
ATOM   1677  C   ASN A1013      -8.212  53.153  17.984  1.00162.73           C  
ATOM   1678  O   ASN A1013      -8.829  54.174  18.287  1.00179.02           O  
ATOM   1679  CB  ASN A1013      -7.715  51.756  20.018  1.00157.75           C  
ATOM   1680  CG  ASN A1013      -8.332  50.810  21.040  1.00161.89           C  
ATOM   1681  OD1 ASN A1013      -9.547  50.765  21.212  1.00175.02           O  
ATOM   1682  ND2 ASN A1013      -7.493  50.049  21.727  1.00163.12           N  
ATOM   1683  N   LEU A1014      -7.279  53.126  17.031  1.00157.41           N  
ATOM   1684  CA  LEU A1014      -6.981  54.308  16.205  1.00153.81           C  
ATOM   1685  C   LEU A1014      -8.185  54.724  15.335  1.00155.64           C  
ATOM   1686  O   LEU A1014      -8.563  55.899  15.319  1.00165.17           O  
ATOM   1687  CB  LEU A1014      -5.726  54.085  15.339  1.00144.50           C  
ATOM   1688  CG  LEU A1014      -5.339  55.220  14.369  1.00137.03           C  
ATOM   1689  CD1 LEU A1014      -4.997  56.482  15.141  1.00136.75           C  
ATOM   1690  CD2 LEU A1014      -4.203  54.824  13.444  1.00134.12           C  
ATOM   1691  N   LYS A1015      -8.789  53.766  14.628  1.00147.29           N  
ATOM   1692  CA  LYS A1015      -9.970  54.048  13.800  1.00137.93           C  
ATOM   1693  C   LYS A1015     -11.197  54.430  14.622  1.00136.64           C  
ATOM   1694  O   LYS A1015     -12.066  55.145  14.128  1.00141.21           O  
ATOM   1695  CB  LYS A1015     -10.317  52.855  12.908  1.00137.36           C  
ATOM   1696  N   VAL A1016     -11.273  53.944  15.862  1.00134.22           N  
ATOM   1697  CA  VAL A1016     -12.341  54.346  16.790  1.00135.26           C  
ATOM   1698  C   VAL A1016     -12.179  55.828  17.136  1.00140.52           C  
ATOM   1699  O   VAL A1016     -13.173  56.541  17.282  1.00144.54           O  
ATOM   1700  CB  VAL A1016     -12.384  53.469  18.077  1.00130.88           C  
ATOM   1701  CG1 VAL A1016     -13.288  54.071  19.154  1.00128.81           C  
ATOM   1702  CG2 VAL A1016     -12.858  52.062  17.742  1.00131.53           C  
ATOM   1703  N   ILE A1017     -10.933  56.288  17.244  1.00144.86           N  
ATOM   1704  CA  ILE A1017     -10.645  57.693  17.550  1.00150.14           C  
ATOM   1705  C   ILE A1017     -11.235  58.637  16.496  1.00156.62           C  
ATOM   1706  O   ILE A1017     -11.915  59.600  16.835  1.00170.80           O  
ATOM   1707  CB  ILE A1017      -9.119  57.942  17.725  1.00147.60           C  
ATOM   1708  CG1 ILE A1017      -8.540  57.037  18.822  1.00146.26           C  
ATOM   1709  CG2 ILE A1017      -8.812  59.403  18.049  1.00149.91           C  
ATOM   1710  CD1 ILE A1017      -9.162  57.204  20.191  1.00151.73           C  
ATOM   1711  N   GLU A1018     -11.037  58.311  15.226  1.00153.66           N  
ATOM   1712  CA  GLU A1018     -11.434  59.203  14.114  1.00145.71           C  
ATOM   1713  C   GLU A1018     -12.947  59.333  13.911  1.00144.53           C  
ATOM   1714  O   GLU A1018     -13.383  60.267  13.243  1.00154.90           O  
ATOM   1715  CB  GLU A1018     -10.806  58.777  12.778  1.00141.43           C  
ATOM   1716  CG  GLU A1018      -9.604  57.861  12.897  1.00145.26           C  
ATOM   1717  CD  GLU A1018      -8.755  57.819  11.653  1.00147.81           C  
ATOM   1718  OE1 GLU A1018      -9.304  57.939  10.537  1.00153.11           O  
ATOM   1719  OE2 GLU A1018      -7.527  57.652  11.806  1.00151.65           O  
ATOM   1720  N   LYS A1019     -13.732  58.400  14.454  1.00141.26           N  
ATOM   1721  CA  LYS A1019     -15.190  58.410  14.313  1.00143.74           C  
ATOM   1722  C   LYS A1019     -15.957  58.857  15.564  1.00159.11           C  
ATOM   1723  O   LYS A1019     -17.145  59.188  15.460  1.00172.88           O  
ATOM   1724  CB  LYS A1019     -15.681  57.018  13.919  1.00135.45           C  
ATOM   1725  N   ALA A1020     -15.300  58.860  16.731  1.00170.51           N  
ATOM   1726  CA  ALA A1020     -15.979  59.168  18.001  1.00178.20           C  
ATOM   1727  C   ALA A1020     -16.425  60.615  17.993  1.00184.94           C  
ATOM   1728  O   ALA A1020     -15.954  61.420  17.184  1.00187.19           O  
ATOM   1729  CB  ALA A1020     -15.095  58.889  19.222  1.00174.80           C  
ATOM   1730  N   ASP A1021     -17.374  60.912  18.874  1.00185.10           N  
ATOM   1731  CA  ASP A1021     -17.883  62.267  19.059  1.00183.50           C  
ATOM   1732  C   ASP A1021     -17.838  62.759  20.515  1.00178.79           C  
ATOM   1733  O   ASP A1021     -18.229  63.895  20.782  1.00185.42           O  
ATOM   1734  CB  ASP A1021     -19.311  62.339  18.520  1.00178.25           C  
ATOM   1735  N   ASN A1022     -17.342  61.930  21.434  1.00167.79           N  
ATOM   1736  CA  ASN A1022     -17.319  62.252  22.851  1.00165.07           C  
ATOM   1737  C   ASN A1022     -15.878  62.241  23.346  1.00165.28           C  
ATOM   1738  O   ASN A1022     -15.051  61.468  22.859  1.00167.39           O  
ATOM   1739  CB  ASN A1022     -18.177  61.246  23.621  1.00169.68           C  
ATOM   1740  CG  ASN A1022     -17.825  61.178  25.091  1.00180.38           C  
ATOM   1741  OD1 ASN A1022     -17.176  60.233  25.524  1.00186.47           O  
ATOM   1742  ND2 ASN A1022     -18.214  62.193  25.857  1.00186.85           N  
ATOM   1743  N   ALA A1023     -15.587  63.102  24.317  1.00169.34           N  
ATOM   1744  CA  ALA A1023     -14.243  63.214  24.877  1.00171.88           C  
ATOM   1745  C   ALA A1023     -13.801  61.917  25.563  1.00180.91           C  
ATOM   1746  O   ALA A1023     -12.680  61.457  25.339  1.00189.63           O  
ATOM   1747  CB  ALA A1023     -14.163  64.385  25.846  1.00166.80           C  
ATOM   1748  N   ALA A1024     -14.672  61.339  26.393  1.00181.81           N  
ATOM   1749  CA  ALA A1024     -14.361  60.077  27.085  1.00174.65           C  
ATOM   1750  C   ALA A1024     -14.332  58.879  26.116  1.00173.92           C  
ATOM   1751  O   ALA A1024     -13.599  57.916  26.344  1.00184.14           O  
ATOM   1752  CB  ALA A1024     -15.333  59.827  28.237  1.00168.13           C  
ATOM   1753  N   GLN A1025     -15.111  58.949  25.031  1.00158.72           N  
ATOM   1754  CA  GLN A1025     -15.087  57.918  23.985  1.00150.04           C  
ATOM   1755  C   GLN A1025     -13.683  57.815  23.376  1.00155.11           C  
ATOM   1756  O   GLN A1025     -13.164  56.720  23.163  1.00162.04           O  
ATOM   1757  CB  GLN A1025     -16.127  58.210  22.897  1.00139.25           C  
ATOM   1758  N   VAL A1026     -13.070  58.967  23.126  1.00157.39           N  
ATOM   1759  CA  VAL A1026     -11.681  59.034  22.672  1.00154.80           C  
ATOM   1760  C   VAL A1026     -10.681  58.590  23.755  1.00149.69           C  
ATOM   1761  O   VAL A1026      -9.720  57.874  23.449  1.00146.60           O  
ATOM   1762  CB  VAL A1026     -11.364  60.459  22.145  1.00157.08           C  
ATOM   1763  CG1 VAL A1026      -9.875  60.796  22.197  1.00156.18           C  
ATOM   1764  CG2 VAL A1026     -11.920  60.625  20.733  1.00156.83           C  
ATOM   1765  N   LYS A1027     -10.899  59.018  25.000  1.00147.22           N  
ATOM   1766  CA  LYS A1027      -9.986  58.667  26.099  1.00150.31           C  
ATOM   1767  C   LYS A1027      -9.992  57.167  26.399  1.00150.08           C  
ATOM   1768  O   LYS A1027      -8.998  56.635  26.896  1.00145.04           O  
ATOM   1769  CB  LYS A1027     -10.283  59.469  27.383  1.00154.47           C  
ATOM   1770  CG  LYS A1027     -11.155  58.760  28.422  1.00155.35           C  
ATOM   1771  CD  LYS A1027     -11.175  59.507  29.742  1.00150.98           C  
ATOM   1772  CE  LYS A1027      -9.923  59.210  30.559  1.00145.66           C  
ATOM   1773  NZ  LYS A1027      -9.894  59.960  31.842  1.00141.22           N  
ATOM   1774  N   ASP A1028     -11.113  56.497  26.127  1.00150.97           N  
ATOM   1775  CA  ASP A1028     -11.206  55.055  26.336  1.00153.07           C  
ATOM   1776  C   ASP A1028     -10.363  54.292  25.313  1.00154.65           C  
ATOM   1777  O   ASP A1028      -9.624  53.374  25.679  1.00163.56           O  
ATOM   1778  CB  ASP A1028     -12.660  54.588  26.283  1.00154.38           C  
ATOM   1779  CG  ASP A1028     -12.795  53.097  26.490  1.00159.47           C  
ATOM   1780  OD1 ASP A1028     -12.829  52.656  27.658  1.00158.00           O  
ATOM   1781  OD2 ASP A1028     -12.863  52.369  25.478  1.00166.94           O  
ATOM   1782  N   ALA A1029     -10.471  54.676  24.040  1.00153.27           N  
ATOM   1783  CA  ALA A1029      -9.656  54.062  22.971  1.00155.00           C  
ATOM   1784  C   ALA A1029      -8.148  54.327  23.030  1.00154.25           C  
ATOM   1785  O   ALA A1029      -7.390  53.617  22.384  1.00150.90           O  
ATOM   1786  CB  ALA A1029     -10.176  54.459  21.600  1.00156.76           C  
ATOM   1787  N   LEU A1030      -7.725  55.357  23.765  1.00154.09           N  
ATOM   1788  CA  LEU A1030      -6.295  55.645  23.986  1.00155.72           C  
ATOM   1789  C   LEU A1030      -5.680  54.931  25.192  1.00156.66           C  
ATOM   1790  O   LEU A1030      -4.492  54.588  25.175  1.00161.61           O  
ATOM   1791  CB  LEU A1030      -6.081  57.150  24.187  1.00156.44           C  
ATOM   1792  CG  LEU A1030      -6.353  58.077  23.001  1.00154.08           C  
ATOM   1793  CD1 LEU A1030      -6.231  59.553  23.380  1.00157.89           C  
ATOM   1794  CD2 LEU A1030      -5.427  57.728  21.848  1.00147.97           C  
ATOM   1795  N   THR A1031      -6.468  54.737  26.248  1.00152.29           N  
ATOM   1796  CA  THR A1031      -5.972  54.022  27.425  1.00148.14           C  
ATOM   1797  C   THR A1031      -5.796  52.560  27.043  1.00149.11           C  
ATOM   1798  O   THR A1031      -4.825  51.946  27.445  1.00144.97           O  
ATOM   1799  CB  THR A1031      -6.872  54.142  28.675  1.00147.34           C  
ATOM   1800  OG1 THR A1031      -8.216  53.781  28.347  1.00155.72           O  
ATOM   1801  CG2 THR A1031      -6.837  55.552  29.244  1.00142.34           C  
ATOM   1802  N   LYS A1032      -6.714  52.028  26.235  1.00156.31           N  
ATOM   1803  CA  LYS A1032      -6.589  50.667  25.692  1.00150.04           C  
ATOM   1804  C   LYS A1032      -5.474  50.566  24.652  1.00141.82           C  
ATOM   1805  O   LYS A1032      -4.831  49.532  24.529  1.00132.97           O  
ATOM   1806  CB  LYS A1032      -7.924  50.182  25.105  1.00143.81           C  
ATOM   1807  CG  LYS A1032      -8.999  50.032  26.166  1.00142.73           C  
ATOM   1808  CD  LYS A1032     -10.357  49.674  25.596  1.00143.03           C  
ATOM   1809  CE  LYS A1032     -11.402  49.697  26.705  1.00146.06           C  
ATOM   1810  NZ  LYS A1032     -12.776  49.356  26.241  1.00148.02           N  
ATOM   1811  N   MET A1033      -5.260  51.640  23.904  1.00141.31           N  
ATOM   1812  CA  MET A1033      -4.147  51.709  22.958  1.00146.22           C  
ATOM   1813  C   MET A1033      -2.808  51.853  23.676  1.00144.92           C  
ATOM   1814  O   MET A1033      -1.783  51.429  23.150  1.00137.19           O  
ATOM   1815  CB  MET A1033      -4.362  52.880  21.998  1.00152.91           C  
ATOM   1816  CG  MET A1033      -3.432  52.950  20.795  1.00153.80           C  
ATOM   1817  SD  MET A1033      -3.657  54.476  19.848  1.00149.41           S  
ATOM   1818  CE  MET A1033      -5.436  54.582  19.706  1.00148.85           C  
ATOM   1819  N   ARG A1034      -2.821  52.453  24.867  1.00147.59           N  
ATOM   1820  CA  ARG A1034      -1.601  52.666  25.652  1.00149.24           C  
ATOM   1821  C   ARG A1034      -1.103  51.375  26.309  1.00157.13           C  
ATOM   1822  O   ARG A1034       0.110  51.136  26.376  1.00158.17           O  
ATOM   1823  CB  ARG A1034      -1.844  53.730  26.725  1.00140.25           C  
ATOM   1824  CG  ARG A1034      -0.596  54.205  27.442  1.00133.71           C  
ATOM   1825  CD  ARG A1034      -0.967  55.128  28.588  1.00132.10           C  
ATOM   1826  NE  ARG A1034       0.178  55.904  29.056  1.00131.89           N  
ATOM   1827  CZ  ARG A1034       1.071  55.507  29.967  1.00134.25           C  
ATOM   1828  NH1 ARG A1034       1.003  54.303  30.545  1.00127.57           N  
ATOM   1829  NH2 ARG A1034       2.062  56.331  30.307  1.00141.56           N  
ATOM   1830  N   ALA A1035      -2.033  50.555  26.806  1.00158.66           N  
ATOM   1831  CA  ALA A1035      -1.683  49.261  27.405  1.00149.50           C  
ATOM   1832  C   ALA A1035      -1.065  48.354  26.354  1.00141.66           C  
ATOM   1833  O   ALA A1035       0.005  47.810  26.574  1.00136.41           O  
ATOM   1834  CB  ALA A1035      -2.898  48.598  28.049  1.00145.93           C  
ATOM   1835  N   ALA A1036      -1.718  48.236  25.199  1.00137.05           N  
ATOM   1836  CA  ALA A1036      -1.169  47.472  24.078  1.00133.36           C  
ATOM   1837  C   ALA A1036       0.157  48.033  23.579  1.00134.33           C  
ATOM   1838  O   ALA A1036       0.936  47.301  22.989  1.00141.98           O  
ATOM   1839  CB  ALA A1036      -2.164  47.399  22.931  1.00129.22           C  
ATOM   1840  N   ALA A1037       0.408  49.321  23.803  1.00139.48           N  
ATOM   1841  CA  ALA A1037       1.661  49.948  23.376  1.00152.36           C  
ATOM   1842  C   ALA A1037       2.861  49.421  24.173  1.00162.85           C  
ATOM   1843  O   ALA A1037       3.774  48.818  23.603  1.00176.16           O  
ATOM   1844  CB  ALA A1037       1.562  51.464  23.486  1.00152.56           C  
ATOM   1845  N   LEU A1038       2.830  49.612  25.489  1.00160.90           N  
ATOM   1846  CA  LEU A1038       3.902  49.112  26.371  1.00156.24           C  
ATOM   1847  C   LEU A1038       4.041  47.598  26.623  1.00149.63           C  
ATOM   1848  O   LEU A1038       5.085  47.137  27.087  1.00145.83           O  
ATOM   1849  CB  LEU A1038       3.899  49.831  27.726  1.00155.91           C  
ATOM   1850  CG  LEU A1038       2.679  49.719  28.649  1.00159.47           C  
ATOM   1851  CD1 LEU A1038       2.643  48.421  29.439  1.00161.16           C  
ATOM   1852  CD2 LEU A1038       2.679  50.902  29.607  1.00162.56           C  
ATOM   1853  N   ASP A1039       2.996  46.830  26.312  1.00139.94           N  
ATOM   1854  CA  ASP A1039       3.096  45.365  26.325  1.00130.96           C  
ATOM   1855  C   ASP A1039       3.774  44.753  25.088  1.00130.22           C  
ATOM   1856  O   ASP A1039       4.570  43.825  25.184  1.00131.33           O  
ATOM   1857  CB  ASP A1039       1.698  44.741  26.332  1.00126.86           C  
ATOM   1858  CG  ASP A1039       0.992  44.910  27.632  1.00126.33           C  
ATOM   1859  OD1 ASP A1039       1.649  45.254  28.644  1.00122.76           O  
ATOM   1860  OD2 ASP A1039      -0.241  44.748  27.612  1.00133.34           O  
ATOM   1861  N   ALA A1040       3.487  45.352  23.932  1.00134.22           N  
ATOM   1862  CA  ALA A1040       4.175  45.002  22.680  1.00138.33           C  
ATOM   1863  C   ALA A1040       5.636  45.430  22.830  1.00146.53           C  
ATOM   1864  O   ALA A1040       6.520  44.830  22.211  1.00149.21           O  
ATOM   1865  CB  ALA A1040       3.608  45.551  21.379  1.00132.35           C  
ATOM   1866  N   GLN A1041       5.890  46.451  23.650  1.00152.64           N  
ATOM   1867  CA  GLN A1041       7.254  46.881  23.947  1.00159.83           C  
ATOM   1868  C   GLN A1041       8.071  45.770  24.640  1.00158.28           C  
ATOM   1869  O   GLN A1041       9.291  45.739  24.514  1.00162.22           O  
ATOM   1870  CB  GLN A1041       7.236  48.163  24.789  1.00164.91           C  
ATOM   1871  CG  GLN A1041       8.557  48.923  24.824  1.00167.47           C  
ATOM   1872  CD  GLN A1041       8.484  50.206  25.633  1.00172.12           C  
ATOM   1873  OE1 GLN A1041       7.679  50.328  26.563  1.00174.53           O  
ATOM   1874  NE2 GLN A1041       9.330  51.175  25.283  1.00173.81           N  
ATOM   1875  N   LYS A1042       7.401  44.856  25.340  1.00154.65           N  
ATOM   1876  CA  LYS A1042       8.068  43.707  25.954  1.00154.01           C  
ATOM   1877  C   LYS A1042       7.921  42.455  25.068  1.00151.87           C  
ATOM   1878  O   LYS A1042       7.139  41.560  25.380  1.00155.62           O  
ATOM   1879  CB  LYS A1042       7.508  43.449  27.368  1.00154.61           C  
ATOM   1880  CG  LYS A1042       7.249  44.686  28.219  1.00157.33           C  
ATOM   1881  CD  LYS A1042       8.494  45.521  28.437  1.00161.96           C  
ATOM   1882  CE  LYS A1042       8.145  46.808  29.162  1.00164.80           C  
ATOM   1883  NZ  LYS A1042       7.463  47.786  28.265  1.00162.32           N  
ATOM   1884  N   ALA A1043       8.660  42.386  23.961  1.00149.82           N  
ATOM   1885  CA  ALA A1043       8.616  41.174  23.116  1.00145.56           C  
ATOM   1886  C   ALA A1043       9.848  40.955  22.243  1.00136.33           C  
ATOM   1887  O   ALA A1043      10.754  41.777  22.196  1.00124.55           O  
ATOM   1888  CB  ALA A1043       7.366  41.184  22.251  1.00146.57           C  
ATOM   1889  N   ASP A1060      17.477  52.374  20.566  1.00149.25           N  
ATOM   1890  CA  ASP A1060      17.518  52.162  19.132  1.00150.29           C  
ATOM   1891  C   ASP A1060      16.095  52.066  18.650  1.00150.36           C  
ATOM   1892  O   ASP A1060      15.686  52.770  17.738  1.00143.46           O  
ATOM   1893  CB  ASP A1060      18.326  50.908  18.793  1.00143.05           C  
ATOM   1894  N   PHE A1061      15.357  51.177  19.300  1.00158.48           N  
ATOM   1895  CA  PHE A1061      13.938  51.006  19.093  1.00169.11           C  
ATOM   1896  C   PHE A1061      13.185  51.568  20.311  1.00179.30           C  
ATOM   1897  O   PHE A1061      11.962  51.719  20.278  1.00194.04           O  
ATOM   1898  CB  PHE A1061      13.595  49.509  18.924  1.00167.64           C  
ATOM   1899  CG  PHE A1061      13.984  48.650  20.101  1.00167.22           C  
ATOM   1900  CD1 PHE A1061      13.111  48.462  21.179  1.00166.54           C  
ATOM   1901  CD2 PHE A1061      15.220  48.014  20.125  1.00165.38           C  
ATOM   1902  CE1 PHE A1061      13.467  47.658  22.250  1.00163.28           C  
ATOM   1903  CE2 PHE A1061      15.582  47.212  21.199  1.00162.35           C  
ATOM   1904  CZ  PHE A1061      14.703  47.035  22.262  1.00161.12           C  
ATOM   1905  N   ARG A1062      13.931  51.857  21.385  1.00175.54           N  
ATOM   1906  CA  ARG A1062      13.360  52.479  22.587  1.00165.34           C  
ATOM   1907  C   ARG A1062      12.790  53.849  22.178  1.00173.14           C  
ATOM   1908  O   ARG A1062      11.725  54.255  22.648  1.00172.83           O  
ATOM   1909  CB  ARG A1062      14.375  52.628  23.733  1.00150.50           C  
ATOM   1910  N   HIS A1063      13.497  54.532  21.279  1.00182.96           N  
ATOM   1911  CA  HIS A1063      13.048  55.796  20.694  1.00188.47           C  
ATOM   1912  C   HIS A1063      11.677  55.728  19.996  1.00185.31           C  
ATOM   1913  O   HIS A1063      10.848  56.633  20.161  1.00187.10           O  
ATOM   1914  CB  HIS A1063      14.103  56.286  19.697  1.00193.60           C  
ATOM   1915  CG  HIS A1063      13.824  57.642  19.133  1.00199.93           C  
ATOM   1916  ND1 HIS A1063      13.807  58.781  19.908  1.00204.66           N  
ATOM   1917  CD2 HIS A1063      13.557  58.043  17.868  1.00201.10           C  
ATOM   1918  CE1 HIS A1063      13.537  59.825  19.146  1.00201.35           C  
ATOM   1919  NE2 HIS A1063      13.383  59.405  17.904  1.00202.83           N  
ATOM   1920  N   GLY A1064      11.459  54.671  19.212  1.00178.40           N  
ATOM   1921  CA  GLY A1064      10.205  54.478  18.490  1.00170.24           C  
ATOM   1922  C   GLY A1064       9.010  54.353  19.410  1.00167.71           C  
ATOM   1923  O   GLY A1064       7.963  54.966  19.168  1.00175.08           O  
ATOM   1924  N   PHE A1065       9.177  53.575  20.478  1.00159.31           N  
ATOM   1925  CA  PHE A1065       8.098  53.356  21.448  1.00155.33           C  
ATOM   1926  C   PHE A1065       7.895  54.530  22.401  1.00159.06           C  
ATOM   1927  O   PHE A1065       6.792  54.703  22.911  1.00165.28           O  
ATOM   1928  CB  PHE A1065       8.312  52.057  22.242  1.00149.71           C  
ATOM   1929  CG  PHE A1065       7.783  50.837  21.546  1.00147.16           C  
ATOM   1930  CD1 PHE A1065       8.571  50.141  20.631  1.00147.07           C  
ATOM   1931  CD2 PHE A1065       6.488  50.388  21.792  1.00143.97           C  
ATOM   1932  CE1 PHE A1065       8.080  49.016  19.980  1.00147.06           C  
ATOM   1933  CE2 PHE A1065       5.992  49.262  21.145  1.00145.58           C  
ATOM   1934  CZ  PHE A1065       6.789  48.575  20.240  1.00147.39           C  
ATOM   1935  N   ASP A1066       8.938  55.320  22.651  1.00153.29           N  
ATOM   1936  CA  ASP A1066       8.796  56.507  23.500  1.00144.71           C  
ATOM   1937  C   ASP A1066       8.056  57.633  22.787  1.00138.14           C  
ATOM   1938  O   ASP A1066       7.247  58.316  23.405  1.00136.40           O  
ATOM   1939  CB  ASP A1066      10.153  56.980  24.030  1.00143.37           C  
ATOM   1940  CG  ASP A1066      10.713  56.056  25.096  1.00145.44           C  
ATOM   1941  OD1 ASP A1066       9.920  55.467  25.863  1.00137.67           O  
ATOM   1942  OD2 ASP A1066      11.951  55.920  25.173  1.00158.53           O  
ATOM   1943  N   ILE A1067       8.308  57.814  21.494  1.00132.01           N  
ATOM   1944  CA  ILE A1067       7.532  58.776  20.712  1.00127.85           C  
ATOM   1945  C   ILE A1067       6.056  58.353  20.684  1.00124.01           C  
ATOM   1946  O   ILE A1067       5.164  59.199  20.781  1.00123.86           O  
ATOM   1947  CB  ILE A1067       8.085  58.945  19.277  1.00131.38           C  
ATOM   1948  CG1 ILE A1067       9.496  59.548  19.320  1.00135.23           C  
ATOM   1949  CG2 ILE A1067       7.169  59.851  18.447  1.00131.42           C  
ATOM   1950  CD1 ILE A1067      10.157  59.674  17.965  1.00140.17           C  
ATOM   1951  N   LEU A1068       5.803  57.051  20.565  1.00121.28           N  
ATOM   1952  CA  LEU A1068       4.434  56.554  20.485  1.00122.46           C  
ATOM   1953  C   LEU A1068       3.676  56.743  21.796  1.00127.63           C  
ATOM   1954  O   LEU A1068       2.570  57.290  21.808  1.00134.89           O  
ATOM   1955  CB  LEU A1068       4.416  55.078  20.095  1.00123.35           C  
ATOM   1956  CG  LEU A1068       3.020  54.459  19.978  1.00123.27           C  
ATOM   1957  CD1 LEU A1068       2.288  55.039  18.783  1.00119.10           C  
ATOM   1958  CD2 LEU A1068       3.119  52.949  19.889  1.00130.12           C  
ATOM   1959  N   VAL A1069       4.269  56.291  22.896  1.00126.91           N  
ATOM   1960  CA  VAL A1069       3.602  56.367  24.197  1.00123.60           C  
ATOM   1961  C   VAL A1069       3.478  57.828  24.639  1.00125.37           C  
ATOM   1962  O   VAL A1069       2.477  58.208  25.238  1.00125.69           O  
ATOM   1963  CB  VAL A1069       4.320  55.523  25.273  1.00120.77           C  
ATOM   1964  CG1 VAL A1069       3.617  55.650  26.620  1.00124.57           C  
ATOM   1965  CG2 VAL A1069       4.365  54.059  24.864  1.00119.24           C  
ATOM   1966  N   GLY A1070       4.489  58.641  24.335  1.00126.04           N  
ATOM   1967  CA  GLY A1070       4.439  60.076  24.599  1.00130.34           C  
ATOM   1968  C   GLY A1070       3.336  60.776  23.827  1.00136.27           C  
ATOM   1969  O   GLY A1070       2.671  61.651  24.365  1.00149.78           O  
ATOM   1970  N   GLN A1071       3.147  60.398  22.564  1.00136.62           N  
ATOM   1971  CA  GLN A1071       2.062  60.956  21.745  1.00130.11           C  
ATOM   1972  C   GLN A1071       0.688  60.561  22.271  1.00128.33           C  
ATOM   1973  O   GLN A1071      -0.249  61.350  22.179  1.00133.27           O  
ATOM   1974  CB  GLN A1071       2.194  60.537  20.279  1.00124.93           C  
ATOM   1975  CG  GLN A1071       3.202  61.363  19.506  1.00122.05           C  
ATOM   1976  CD  GLN A1071       3.491  60.815  18.124  1.00117.73           C  
ATOM   1977  OE1 GLN A1071       3.375  59.617  17.877  1.00113.61           O  
ATOM   1978  NE2 GLN A1071       3.891  61.696  17.216  1.00120.05           N  
ATOM   1979  N   ILE A1072       0.569  59.350  22.811  1.00118.37           N  
ATOM   1980  CA  ILE A1072      -0.683  58.915  23.409  1.00116.10           C  
ATOM   1981  C   ILE A1072      -0.989  59.739  24.663  1.00120.33           C  
ATOM   1982  O   ILE A1072      -2.105  60.241  24.816  1.00130.62           O  
ATOM   1983  CB  ILE A1072      -0.675  57.407  23.720  1.00115.74           C  
ATOM   1984  CG1 ILE A1072      -0.706  56.604  22.417  1.00118.89           C  
ATOM   1985  CG2 ILE A1072      -1.880  57.029  24.570  1.00115.39           C  
ATOM   1986  CD1 ILE A1072      -0.493  55.110  22.600  1.00121.80           C  
ATOM   1987  N   ASP A1073      -0.006  59.882  25.547  1.00122.59           N  
ATOM   1988  CA  ASP A1073      -0.186  60.693  26.763  1.00137.11           C  
ATOM   1989  C   ASP A1073      -0.551  62.150  26.446  1.00144.53           C  
ATOM   1990  O   ASP A1073      -1.422  62.727  27.105  1.00160.80           O  
ATOM   1991  CB  ASP A1073       1.061  60.635  27.671  1.00141.16           C  
ATOM   1992  CG  ASP A1073       1.165  59.334  28.450  1.00139.33           C  
ATOM   1993  OD1 ASP A1073       0.149  58.619  28.551  1.00147.96           O  
ATOM   1994  OD2 ASP A1073       2.256  59.024  28.976  1.00134.63           O  
ATOM   1995  N   ASP A1074       0.094  62.728  25.430  1.00140.07           N  
ATOM   1996  CA  ASP A1074      -0.263  64.066  24.945  1.00135.17           C  
ATOM   1997  C   ASP A1074      -1.747  64.113  24.586  1.00134.58           C  
ATOM   1998  O   ASP A1074      -2.475  65.003  25.034  1.00137.65           O  
ATOM   1999  CB  ASP A1074       0.584  64.466  23.718  1.00133.63           C  
ATOM   2000  CG  ASP A1074       2.049  64.754  24.058  1.00132.92           C  
ATOM   2001  OD1 ASP A1074       2.394  64.804  25.259  1.00140.73           O  
ATOM   2002  OD2 ASP A1074       2.861  64.921  23.115  1.00119.95           O  
ATOM   2003  N   ALA A1075      -2.189  63.139  23.795  1.00137.06           N  
ATOM   2004  CA  ALA A1075      -3.590  63.070  23.382  1.00144.30           C  
ATOM   2005  C   ALA A1075      -4.522  62.773  24.556  1.00152.11           C  
ATOM   2006  O   ALA A1075      -5.696  63.145  24.516  1.00158.46           O  
ATOM   2007  CB  ALA A1075      -3.776  62.040  22.278  1.00141.65           C  
ATOM   2008  N   LEU A1076      -4.006  62.102  25.590  1.00152.13           N  
ATOM   2009  CA  LEU A1076      -4.797  61.823  26.798  1.00148.38           C  
ATOM   2010  C   LEU A1076      -5.203  63.055  27.613  1.00149.75           C  
ATOM   2011  O   LEU A1076      -6.383  63.219  27.931  1.00149.38           O  
ATOM   2012  CB  LEU A1076      -4.096  60.798  27.711  1.00147.32           C  
ATOM   2013  CG  LEU A1076      -4.416  59.326  27.442  1.00145.93           C  
ATOM   2014  CD1 LEU A1076      -3.542  58.422  28.304  1.00143.87           C  
ATOM   2015  CD2 LEU A1076      -5.891  59.038  27.693  1.00146.30           C  
ATOM   2016  N   LYS A1077      -4.236  63.910  27.952  1.00152.98           N  
ATOM   2017  CA  LYS A1077      -4.512  65.146  28.708  1.00152.03           C  
ATOM   2018  C   LYS A1077      -5.388  66.142  27.945  1.00150.43           C  
ATOM   2019  O   LYS A1077      -6.103  66.950  28.557  1.00161.20           O  
ATOM   2020  CB  LYS A1077      -3.214  65.848  29.110  1.00148.86           C  
ATOM   2021  N   LEU A1078      -5.327  66.093  26.612  1.00144.19           N  
ATOM   2022  CA  LEU A1078      -6.252  66.880  25.792  1.00143.91           C  
ATOM   2023  C   LEU A1078      -7.649  66.326  26.006  1.00145.84           C  
ATOM   2024  O   LEU A1078      -8.584  67.090  26.256  1.00149.79           O  
ATOM   2025  CB  LEU A1078      -5.894  66.866  24.297  1.00140.39           C  
ATOM   2026  CG  LEU A1078      -4.630  67.617  23.868  1.00141.08           C  
ATOM   2027  CD1 LEU A1078      -4.420  67.453  22.374  1.00138.76           C  
ATOM   2028  CD2 LEU A1078      -4.720  69.093  24.219  1.00142.47           C  
ATOM   2029  N   ALA A1079      -7.782  65.002  25.928  1.00145.10           N  
ATOM   2030  CA  ALA A1079      -9.079  64.346  26.102  1.00146.59           C  
ATOM   2031  C   ALA A1079      -9.691  64.628  27.478  1.00151.87           C  
ATOM   2032  O   ALA A1079     -10.887  64.901  27.575  1.00149.18           O  
ATOM   2033  CB  ALA A1079      -8.959  62.846  25.872  1.00145.23           C  
ATOM   2034  N   ASN A1080      -8.867  64.588  28.525  1.00158.43           N  
ATOM   2035  CA  ASN A1080      -9.339  64.863  29.888  1.00155.15           C  
ATOM   2036  C   ASN A1080      -9.843  66.294  30.054  1.00151.21           C  
ATOM   2037  O   ASN A1080     -10.774  66.532  30.816  1.00148.66           O  
ATOM   2038  CB  ASN A1080      -8.244  64.574  30.920  1.00156.70           C  
ATOM   2039  CG  ASN A1080      -7.863  63.106  30.970  1.00161.53           C  
ATOM   2040  OD1 ASN A1080      -8.664  62.228  30.637  1.00159.47           O  
ATOM   2041  ND2 ASN A1080      -6.630  62.831  31.384  1.00166.04           N  
ATOM   2042  N   GLU A1081      -9.255  67.233  29.315  1.00148.20           N  
ATOM   2043  CA  GLU A1081      -9.684  68.633  29.347  1.00144.97           C  
ATOM   2044  C   GLU A1081     -10.824  68.931  28.362  1.00139.27           C  
ATOM   2045  O   GLU A1081     -11.087  70.093  28.052  1.00127.96           O  
ATOM   2046  CB  GLU A1081      -8.483  69.539  29.070  1.00148.02           C  
ATOM   2047  CG  GLU A1081      -7.398  69.433  30.132  1.00149.80           C  
ATOM   2048  CD  GLU A1081      -6.104  70.129  29.745  1.00153.23           C  
ATOM   2049  OE1 GLU A1081      -5.972  70.599  28.592  1.00151.19           O  
ATOM   2050  OE2 GLU A1081      -5.205  70.206  30.607  1.00157.43           O  
ATOM   2051  N   GLY A1082     -11.490  67.892  27.857  1.00142.40           N  
ATOM   2052  CA  GLY A1082     -12.603  68.059  26.929  1.00148.19           C  
ATOM   2053  C   GLY A1082     -12.239  68.434  25.499  1.00153.13           C  
ATOM   2054  O   GLY A1082     -13.110  68.434  24.631  1.00149.48           O  
ATOM   2055  N   LYS A1083     -10.966  68.738  25.239  1.00159.34           N  
ATOM   2056  CA  LYS A1083     -10.515  69.162  23.911  1.00153.63           C  
ATOM   2057  C   LYS A1083     -10.543  67.950  22.972  1.00153.13           C  
ATOM   2058  O   LYS A1083      -9.532  67.264  22.773  1.00157.58           O  
ATOM   2059  CB  LYS A1083      -9.109  69.781  23.987  1.00153.20           C  
ATOM   2060  CG  LYS A1083      -9.017  71.050  24.825  1.00154.01           C  
ATOM   2061  CD  LYS A1083      -7.605  71.282  25.355  1.00152.52           C  
ATOM   2062  CE  LYS A1083      -7.289  72.759  25.485  1.00152.37           C  
ATOM   2063  NZ  LYS A1083      -7.080  73.387  24.152  1.00154.23           N  
ATOM   2064  N   VAL A1084     -11.720  67.692  22.406  1.00149.00           N  
ATOM   2065  CA  VAL A1084     -11.948  66.482  21.611  1.00145.42           C  
ATOM   2066  C   VAL A1084     -11.192  66.559  20.287  1.00140.54           C  
ATOM   2067  O   VAL A1084     -10.360  65.704  19.987  1.00143.27           O  
ATOM   2068  CB  VAL A1084     -13.453  66.238  21.352  1.00145.73           C  
ATOM   2069  CG1 VAL A1084     -13.675  64.970  20.527  1.00143.82           C  
ATOM   2070  CG2 VAL A1084     -14.203  66.147  22.677  1.00152.79           C  
ATOM   2071  N   LYS A1085     -11.464  67.599  19.511  1.00135.10           N  
ATOM   2072  CA  LYS A1085     -10.867  67.714  18.188  1.00135.45           C  
ATOM   2073  C   LYS A1085      -9.353  67.850  18.241  1.00133.79           C  
ATOM   2074  O   LYS A1085      -8.671  67.340  17.363  1.00130.65           O  
ATOM   2075  CB  LYS A1085     -11.500  68.853  17.399  1.00142.89           C  
ATOM   2076  CG  LYS A1085     -12.986  68.639  17.115  1.00150.95           C  
ATOM   2077  CD  LYS A1085     -13.267  67.441  16.209  1.00152.53           C  
ATOM   2078  CE  LYS A1085     -14.703  66.957  16.353  1.00155.59           C  
ATOM   2079  NZ  LYS A1085     -15.688  67.974  15.904  1.00159.80           N  
ATOM   2080  N   GLU A1086      -8.827  68.512  19.269  1.00140.78           N  
ATOM   2081  CA  GLU A1086      -7.377  68.516  19.501  1.00146.49           C  
ATOM   2082  C   GLU A1086      -6.847  67.118  19.790  1.00152.04           C  
ATOM   2083  O   GLU A1086      -5.786  66.754  19.284  1.00154.71           O  
ATOM   2084  CB  GLU A1086      -6.976  69.453  20.653  1.00148.41           C  
ATOM   2085  CG  GLU A1086      -7.093  70.925  20.331  1.00146.00           C  
ATOM   2086  CD  GLU A1086      -6.394  71.267  19.038  1.00141.98           C  
ATOM   2087  OE1 GLU A1086      -5.208  70.909  18.889  1.00141.36           O  
ATOM   2088  OE2 GLU A1086      -7.044  71.858  18.161  1.00140.90           O  
ATOM   2089  N   ALA A1087      -7.572  66.352  20.609  1.00157.19           N  
ATOM   2090  CA  ALA A1087      -7.190  64.965  20.901  1.00154.01           C  
ATOM   2091  C   ALA A1087      -7.192  64.111  19.626  1.00149.14           C  
ATOM   2092  O   ALA A1087      -6.231  63.389  19.362  1.00142.07           O  
ATOM   2093  CB  ALA A1087      -8.097  64.359  21.967  1.00155.27           C  
ATOM   2094  N   GLN A1088      -8.252  64.228  18.827  1.00144.90           N  
ATOM   2095  CA  GLN A1088      -8.368  63.462  17.579  1.00138.35           C  
ATOM   2096  C   GLN A1088      -7.281  63.815  16.556  1.00128.42           C  
ATOM   2097  O   GLN A1088      -6.819  62.946  15.815  1.00111.48           O  
ATOM   2098  CB  GLN A1088      -9.750  63.652  16.945  1.00143.45           C  
ATOM   2099  CG  GLN A1088     -10.900  63.064  17.752  1.00147.65           C  
ATOM   2100  CD  GLN A1088     -12.231  63.157  17.027  1.00152.26           C  
ATOM   2101  OE1 GLN A1088     -12.295  63.629  15.889  1.00146.79           O  
ATOM   2102  NE2 GLN A1088     -13.301  62.692  17.678  1.00159.49           N  
ATOM   2103  N   ALA A1089      -6.883  65.085  16.512  1.00130.12           N  
ATOM   2104  CA  ALA A1089      -5.830  65.531  15.594  1.00128.57           C  
ATOM   2105  C   ALA A1089      -4.442  65.207  16.136  1.00136.36           C  
ATOM   2106  O   ALA A1089      -3.552  64.868  15.364  1.00135.46           O  
ATOM   2107  CB  ALA A1089      -5.950  67.017  15.310  1.00126.38           C  
ATOM   2108  N   ALA A1090      -4.252  65.316  17.450  1.00150.15           N  
ATOM   2109  CA  ALA A1090      -2.979  64.932  18.072  1.00150.76           C  
ATOM   2110  C   ALA A1090      -2.782  63.418  18.066  1.00149.40           C  
ATOM   2111  O   ALA A1090      -1.657  62.953  18.093  1.00138.85           O  
ATOM   2112  CB  ALA A1090      -2.881  65.469  19.490  1.00152.76           C  
ATOM   2113  N   ALA A1091      -3.875  62.656  18.049  1.00157.46           N  
ATOM   2114  CA  ALA A1091      -3.800  61.196  17.913  1.00161.40           C  
ATOM   2115  C   ALA A1091      -3.641  60.745  16.454  1.00152.48           C  
ATOM   2116  O   ALA A1091      -3.356  59.582  16.199  1.00148.49           O  
ATOM   2117  CB  ALA A1091      -5.027  60.541  18.540  1.00168.97           C  
ATOM   2118  N   GLU A1092      -3.839  61.647  15.498  1.00149.51           N  
ATOM   2119  CA  GLU A1092      -3.682  61.300  14.085  1.00150.21           C  
ATOM   2120  C   GLU A1092      -2.221  61.246  13.632  1.00143.10           C  
ATOM   2121  O   GLU A1092      -1.910  60.577  12.654  1.00132.74           O  
ATOM   2122  CB  GLU A1092      -4.474  62.263  13.200  1.00156.15           C  
ATOM   2123  CG  GLU A1092      -4.825  61.693  11.833  1.00161.14           C  
ATOM   2124  CD  GLU A1092      -5.740  60.475  11.899  1.00165.17           C  
ATOM   2125  OE1 GLU A1092      -6.419  60.260  12.926  1.00163.25           O  
ATOM   2126  OE2 GLU A1092      -5.790  59.730  10.906  1.00175.49           O  
ATOM   2127  N   GLN A1093      -1.334  61.950  14.335  1.00141.53           N  
ATOM   2128  CA  GLN A1093       0.110  61.846  14.089  1.00142.83           C  
ATOM   2129  C   GLN A1093       0.721  60.512  14.564  1.00143.18           C  
ATOM   2130  O   GLN A1093       1.881  60.229  14.260  1.00145.25           O  
ATOM   2131  CB  GLN A1093       0.856  63.028  14.727  1.00149.56           C  
ATOM   2132  CG  GLN A1093       0.899  63.008  16.254  1.00156.99           C  
ATOM   2133  CD  GLN A1093       1.292  64.338  16.894  1.00159.45           C  
ATOM   2134  OE1 GLN A1093       2.123  64.377  17.805  1.00152.00           O  
ATOM   2135  NE2 GLN A1093       0.688  65.428  16.433  1.00163.49           N  
ATOM   2136  N   LEU A1094      -0.033  59.719  15.332  1.00140.41           N  
ATOM   2137  CA  LEU A1094       0.408  58.378  15.739  1.00128.93           C  
ATOM   2138  C   LEU A1094       0.747  57.499  14.542  1.00128.46           C  
ATOM   2139  O   LEU A1094       1.733  56.764  14.568  1.00125.21           O  
ATOM   2140  CB  LEU A1094      -0.668  57.676  16.585  1.00125.78           C  
ATOM   2141  CG  LEU A1094      -0.992  58.234  17.974  1.00127.67           C  
ATOM   2142  CD1 LEU A1094      -2.261  57.603  18.536  1.00126.89           C  
ATOM   2143  CD2 LEU A1094       0.160  58.002  18.930  1.00129.77           C  
ATOM   2144  N   LYS A1095      -0.070  57.586  13.495  1.00140.66           N  
ATOM   2145  CA  LYS A1095       0.060  56.688  12.349  1.00146.96           C  
ATOM   2146  C   LYS A1095       1.369  56.832  11.578  1.00146.91           C  
ATOM   2147  O   LYS A1095       1.788  55.885  10.934  1.00148.76           O  
ATOM   2148  CB  LYS A1095      -1.136  56.815  11.406  1.00150.77           C  
ATOM   2149  CG  LYS A1095      -1.253  58.122  10.641  1.00154.99           C  
ATOM   2150  CD  LYS A1095      -2.294  58.032   9.532  1.00156.66           C  
ATOM   2151  CE  LYS A1095      -3.634  57.469   9.998  1.00154.77           C  
ATOM   2152  NZ  LYS A1095      -4.647  57.562   8.917  1.00158.93           N  
ATOM   2153  N   THR A1096       2.009  57.996  11.637  1.00143.21           N  
ATOM   2154  CA  THR A1096       3.343  58.144  11.041  1.00138.64           C  
ATOM   2155  C   THR A1096       4.439  57.617  11.969  1.00125.13           C  
ATOM   2156  O   THR A1096       5.454  57.125  11.494  1.00111.67           O  
ATOM   2157  CB  THR A1096       3.641  59.596  10.644  1.00141.82           C  
ATOM   2158  OG1 THR A1096       3.581  60.433  11.804  1.00152.61           O  
ATOM   2159  CG2 THR A1096       2.641  60.073   9.602  1.00140.52           C  
ATOM   2160  N   THR A1097       4.245  57.729  13.280  1.00121.11           N  
ATOM   2161  CA  THR A1097       5.134  57.063  14.238  1.00122.15           C  
ATOM   2162  C   THR A1097       5.002  55.540  14.131  1.00124.31           C  
ATOM   2163  O   THR A1097       5.995  54.814  14.231  1.00129.37           O  
ATOM   2164  CB  THR A1097       4.845  57.509  15.683  1.00119.52           C  
ATOM   2165  OG1 THR A1097       4.926  58.938  15.756  1.00121.59           O  
ATOM   2166  CG2 THR A1097       5.835  56.882  16.668  1.00113.01           C  
ATOM   2167  N   ARG A1098       3.779  55.059  13.924  1.00125.55           N  
ATOM   2168  CA  ARG A1098       3.546  53.632  13.696  1.00125.05           C  
ATOM   2169  C   ARG A1098       4.225  53.181  12.404  1.00126.04           C  
ATOM   2170  O   ARG A1098       4.928  52.172  12.395  1.00127.42           O  
ATOM   2171  CB  ARG A1098       2.047  53.327  13.640  1.00130.20           C  
ATOM   2172  CG  ARG A1098       1.673  51.859  13.394  1.00131.15           C  
ATOM   2173  CD  ARG A1098       0.280  51.764  12.803  1.00133.21           C  
ATOM   2174  NE  ARG A1098       0.204  52.406  11.485  1.00136.22           N  
ATOM   2175  CZ  ARG A1098      -0.914  52.873  10.921  1.00139.12           C  
ATOM   2176  NH1 ARG A1098      -2.095  52.789  11.540  1.00144.84           N  
ATOM   2177  NH2 ARG A1098      -0.864  53.433   9.720  1.00140.42           N  
ATOM   2178  N   ASN A1099       4.037  53.946  11.332  1.00127.99           N  
ATOM   2179  CA  ASN A1099       4.614  53.599  10.029  1.00131.53           C  
ATOM   2180  C   ASN A1099       6.116  53.855   9.904  1.00129.42           C  
ATOM   2181  O   ASN A1099       6.691  53.531   8.872  1.00135.04           O  
ATOM   2182  CB  ASN A1099       3.887  54.341   8.902  1.00132.86           C  
ATOM   2183  CG  ASN A1099       2.415  53.986   8.819  1.00137.11           C  
ATOM   2184  OD1 ASN A1099       1.992  52.885   9.183  1.00150.32           O  
ATOM   2185  ND2 ASN A1099       1.619  54.935   8.347  1.00133.17           N  
ATOM   2186  N   ALA A1100       6.746  54.445  10.921  1.00127.70           N  
ATOM   2187  CA  ALA A1100       8.190  54.702  10.908  1.00130.24           C  
ATOM   2188  C   ALA A1100       8.976  53.975  12.002  1.00133.99           C  
ATOM   2189  O   ALA A1100      10.201  54.067  12.046  1.00132.70           O  
ATOM   2190  CB  ALA A1100       8.434  56.196  10.995  1.00129.69           C  
ATOM   2191  N   TYR A1101       8.282  53.212  12.832  1.00141.20           N  
ATOM   2192  CA  TYR A1101       8.935  52.511  13.918  1.00148.03           C  
ATOM   2193  C   TYR A1101       8.199  51.248  14.337  1.00148.52           C  
ATOM   2194  O   TYR A1101       8.726  50.145  14.247  1.00156.90           O  
ATOM   2195  CB  TYR A1101       9.063  53.453  15.105  1.00151.80           C  
ATOM   2196  CG  TYR A1101       9.941  54.646  14.852  1.00163.45           C  
ATOM   2197  CD1 TYR A1101      11.310  54.577  15.068  1.00172.26           C  
ATOM   2198  CD2 TYR A1101       9.407  55.839  14.382  1.00171.02           C  
ATOM   2199  CE1 TYR A1101      12.127  55.669  14.842  1.00180.21           C  
ATOM   2200  CE2 TYR A1101      10.213  56.935  14.144  1.00176.68           C  
ATOM   2201  CZ  TYR A1101      11.573  56.847  14.378  1.00182.05           C  
ATOM   2202  OH  TYR A1101      12.386  57.927  14.149  1.00187.69           O  
ATOM   2203  N   ILE A1102       6.969  51.397  14.776  1.00142.42           N  
ATOM   2204  CA  ILE A1102       6.236  50.250  15.280  1.00133.11           C  
ATOM   2205  C   ILE A1102       6.111  49.119  14.248  1.00137.81           C  
ATOM   2206  O   ILE A1102       6.327  47.958  14.590  1.00149.58           O  
ATOM   2207  CB  ILE A1102       4.861  50.691  15.796  1.00125.94           C  
ATOM   2208  CG1 ILE A1102       5.026  51.780  16.865  1.00118.41           C  
ATOM   2209  CG2 ILE A1102       4.070  49.518  16.364  1.00129.14           C  
ATOM   2210  CD1 ILE A1102       6.034  51.461  17.957  1.00115.89           C  
ATOM   2211  N   GLN A1103       5.783  49.451  13.002  1.00137.39           N  
ATOM   2212  CA  GLN A1103       5.675  48.444  11.932  1.00141.58           C  
ATOM   2213  C   GLN A1103       7.024  47.780  11.640  1.00136.65           C  
ATOM   2214  O   GLN A1103       7.083  46.582  11.350  1.00133.37           O  
ATOM   2215  CB  GLN A1103       5.112  49.073  10.644  1.00149.07           C  
ATOM   2216  CG  GLN A1103       4.895  48.104   9.480  1.00150.34           C  
ATOM   2217  CD  GLN A1103       4.496  48.788   8.175  1.00155.79           C  
ATOM   2218  OE1 GLN A1103       4.354  50.014   8.099  1.00152.14           O  
ATOM   2219  NE2 GLN A1103       4.323  47.984   7.130  1.00164.50           N  
ATOM   2220  N   LYS A1104       8.093  48.563  11.715  1.00133.86           N  
ATOM   2221  CA  LYS A1104       9.444  48.081  11.444  1.00130.27           C  
ATOM   2222  C   LYS A1104       9.911  47.071  12.498  1.00133.90           C  
ATOM   2223  O   LYS A1104      10.606  46.113  12.173  1.00137.18           O  
ATOM   2224  CB  LYS A1104      10.399  49.277  11.386  1.00126.37           C  
ATOM   2225  CG  LYS A1104      11.709  49.042  10.670  1.00125.23           C  
ATOM   2226  CD  LYS A1104      12.242  50.377  10.144  1.00125.97           C  
ATOM   2227  CE  LYS A1104      13.454  50.197   9.255  1.00124.81           C  
ATOM   2228  NZ  LYS A1104      14.623  49.718  10.037  1.00124.96           N  
ATOM   2229  N   TYR A1105       9.508  47.268  13.751  1.00139.44           N  
ATOM   2230  CA  TYR A1105       9.889  46.347  14.829  1.00141.88           C  
ATOM   2231  C   TYR A1105       8.992  45.127  14.912  1.00142.02           C  
ATOM   2232  O   TYR A1105       9.466  44.074  15.300  1.00146.29           O  
ATOM   2233  CB  TYR A1105       9.927  47.051  16.187  1.00147.54           C  
ATOM   2234  CG  TYR A1105      10.770  48.305  16.197  1.00164.74           C  
ATOM   2235  CD1 TYR A1105      11.927  48.407  15.410  1.00168.27           C  
ATOM   2236  CD2 TYR A1105      10.418  49.399  16.997  1.00181.74           C  
ATOM   2237  CE1 TYR A1105      12.698  49.555  15.418  1.00181.11           C  
ATOM   2238  CE2 TYR A1105      11.184  50.559  17.000  1.00191.03           C  
ATOM   2239  CZ  TYR A1105      12.323  50.629  16.206  1.00192.80           C  
ATOM   2240  OH  TYR A1105      13.108  51.761  16.205  1.00208.15           O  
ATOM   2241  N   LEU A1106       7.713  45.250  14.566  1.00140.57           N  
ATOM   2242  CA  LEU A1106       6.803  44.092  14.626  1.00133.98           C  
ATOM   2243  C   LEU A1106       6.995  43.150  13.461  1.00126.63           C  
ATOM   2244  O   LEU A1106       6.678  41.974  13.520  1.00125.32           O  
ATOM   2245  CB  LEU A1106       5.348  44.537  14.659  1.00133.75           C  
ATOM   2246  CG  LEU A1106       4.863  45.289  15.904  1.00135.15           C  
ATOM   2247  CD1 LEU A1106       3.354  45.129  16.001  1.00139.05           C  
ATOM   2248  CD2 LEU A1106       5.516  44.831  17.207  1.00133.60           C  
ATOM   2249  N   GLU A 219       7.683  43.717  12.195  1.00123.90           N  
ATOM   2250  CA  GLU A 219       8.100  42.746  11.201  1.00132.21           C  
ATOM   2251  C   GLU A 219       9.363  42.009  11.637  1.00127.85           C  
ATOM   2252  O   GLU A 219       9.525  40.822  11.364  1.00131.31           O  
ATOM   2253  CB  GLU A 219       8.337  43.472   9.888  1.00143.60           C  
ATOM   2254  CG  GLU A 219       7.062  44.065   9.299  1.00150.22           C  
ATOM   2255  CD  GLU A 219       7.312  45.074   8.190  1.00151.82           C  
ATOM   2256  OE1 GLU A 219       6.494  45.119   7.247  1.00158.00           O  
ATOM   2257  OE2 GLU A 219       8.310  45.825   8.254  1.00150.17           O  
ATOM   2258  N   ARG A 220      10.265  42.721  12.298  1.00125.71           N  
ATOM   2259  CA  ARG A 220      11.542  42.141  12.682  1.00130.23           C  
ATOM   2260  C   ARG A 220      11.391  41.093  13.790  1.00130.23           C  
ATOM   2261  O   ARG A 220      12.065  40.065  13.772  1.00133.58           O  
ATOM   2262  CB  ARG A 220      12.519  43.244  13.099  1.00133.98           C  
ATOM   2263  CG  ARG A 220      13.981  42.825  13.148  1.00140.10           C  
ATOM   2264  CD  ARG A 220      14.453  42.097  11.892  1.00148.89           C  
ATOM   2265  NE  ARG A 220      13.923  42.666  10.643  1.00161.81           N  
ATOM   2266  CZ  ARG A 220      14.005  42.089   9.437  1.00170.59           C  
ATOM   2267  NH1 ARG A 220      14.623  40.915   9.260  1.00170.09           N  
ATOM   2268  NH2 ARG A 220      13.467  42.696   8.378  1.00169.65           N  
ATOM   2269  N   ALA A 221      10.503  41.343  14.745  1.00127.26           N  
ATOM   2270  CA  ALA A 221      10.216  40.357  15.791  1.00124.45           C  
ATOM   2271  C   ALA A 221       9.520  39.132  15.210  1.00116.36           C  
ATOM   2272  O   ALA A 221       9.738  38.024  15.681  1.00114.59           O  
ATOM   2273  CB  ALA A 221       9.365  40.963  16.900  1.00131.84           C  
ATOM   2274  N   ARG A 222       8.676  39.336  14.200  1.00109.71           N  
ATOM   2275  CA  ARG A 222       7.965  38.231  13.554  1.00109.52           C  
ATOM   2276  C   ARG A 222       8.937  37.334  12.780  1.00110.37           C  
ATOM   2277  O   ARG A 222       8.820  36.115  12.843  1.00113.37           O  
ATOM   2278  CB  ARG A 222       6.855  38.768  12.636  1.00109.14           C  
ATOM   2279  CG  ARG A 222       6.007  37.727  11.923  1.00104.78           C  
ATOM   2280  CD  ARG A 222       4.783  38.366  11.274  1.00 96.40           C  
ATOM   2281  N   SER A 223       9.892  37.929  12.064  1.00108.35           N  
ATOM   2282  CA  SER A 223      10.868  37.145  11.293  1.00108.53           C  
ATOM   2283  C   SER A 223      11.873  36.424  12.183  1.00108.53           C  
ATOM   2284  O   SER A 223      12.389  35.377  11.802  1.00107.03           O  
ATOM   2285  CB  SER A 223      11.612  38.016  10.288  1.00110.10           C  
ATOM   2286  OG  SER A 223      12.327  39.030  10.951  1.00114.54           O  
ATOM   2287  N   THR A 224      12.158  36.981  13.357  1.00110.09           N  
ATOM   2288  CA  THR A 224      12.990  36.282  14.339  1.00107.40           C  
ATOM   2289  C   THR A 224      12.285  35.027  14.872  1.00103.91           C  
ATOM   2290  O   THR A 224      12.897  33.973  14.992  1.00102.95           O  
ATOM   2291  CB  THR A 224      13.378  37.199  15.513  1.00103.29           C  
ATOM   2292  OG1 THR A 224      14.192  38.268  15.032  1.00103.41           O  
ATOM   2293  CG2 THR A 224      14.165  36.428  16.559  1.00102.76           C  
ATOM   2294  N   LEU A 225      11.003  35.150  15.193  1.00103.60           N  
ATOM   2295  CA  LEU A 225      10.217  34.003  15.643  1.00104.56           C  
ATOM   2296  C   LEU A 225      10.086  32.950  14.555  1.00107.09           C  
ATOM   2297  O   LEU A 225      10.207  31.764  14.840  1.00114.71           O  
ATOM   2298  CB  LEU A 225       8.828  34.439  16.131  1.00104.71           C  
ATOM   2299  CG  LEU A 225       8.848  35.247  17.426  1.00109.07           C  
ATOM   2300  CD1 LEU A 225       7.480  35.844  17.720  1.00115.51           C  
ATOM   2301  CD2 LEU A 225       9.321  34.391  18.591  1.00112.33           C  
ATOM   2302  N   GLN A 226       9.849  33.382  13.317  1.00110.83           N  
ATOM   2303  CA  GLN A 226       9.799  32.463  12.175  1.00115.89           C  
ATOM   2304  C   GLN A 226      11.093  31.655  12.014  1.00109.89           C  
ATOM   2305  O   GLN A 226      11.035  30.465  11.697  1.00118.34           O  
ATOM   2306  CB  GLN A 226       9.506  33.207  10.857  1.00124.46           C  
ATOM   2307  CG  GLN A 226       8.078  33.711  10.668  1.00126.91           C  
ATOM   2308  CD  GLN A 226       7.881  34.409   9.322  1.00123.81           C  
ATOM   2309  OE1 GLN A 226       7.565  35.601   9.259  1.00119.86           O  
ATOM   2310  NE2 GLN A 226       8.080  33.667   8.239  1.00121.98           N  
ATOM   2311  N   LYS A 227      12.244  32.300  12.212  1.00101.76           N  
ATOM   2312  CA  LYS A 227      13.534  31.610  12.118  1.00104.09           C  
ATOM   2313  C   LYS A 227      13.720  30.592  13.242  1.00107.73           C  
ATOM   2314  O   LYS A 227      14.296  29.526  13.020  1.00109.45           O  
ATOM   2315  CB  LYS A 227      14.703  32.601  12.126  1.00104.34           C  
ATOM   2316  N   GLU A 228      13.234  30.919  14.440  1.00109.72           N  
ATOM   2317  CA  GLU A 228      13.321  29.992  15.570  1.00109.63           C  
ATOM   2318  C   GLU A 228      12.427  28.780  15.332  1.00109.97           C  
ATOM   2319  O   GLU A 228      12.796  27.671  15.694  1.00120.53           O  
ATOM   2320  CB  GLU A 228      12.958  30.671  16.892  1.00114.01           C  
ATOM   2321  CG  GLU A 228      13.914  31.786  17.298  1.00119.50           C  
ATOM   2322  CD  GLU A 228      13.729  32.233  18.737  1.00124.61           C  
ATOM   2323  OE1 GLU A 228      14.013  31.417  19.632  1.00130.44           O  
ATOM   2324  OE2 GLU A 228      13.322  33.393  18.971  1.00123.23           O  
ATOM   2325  N   VAL A 229      11.266  28.990  14.714  1.00106.21           N  
ATOM   2326  CA  VAL A 229      10.372  27.885  14.350  1.00100.06           C  
ATOM   2327  C   VAL A 229      11.007  27.014  13.263  1.00 97.66           C  
ATOM   2328  O   VAL A 229      10.992  25.790  13.360  1.00 94.01           O  
ATOM   2329  CB  VAL A 229       8.988  28.403  13.889  1.00 99.46           C  
ATOM   2330  CG1 VAL A 229       8.136  27.292  13.283  1.00102.58           C  
ATOM   2331  CG2 VAL A 229       8.246  29.030  15.057  1.00 99.00           C  
ATOM   2332  N   HIS A 230      11.558  27.644  12.232  1.00 98.57           N  
ATOM   2333  CA  HIS A 230      12.187  26.908  11.132  1.00106.76           C  
ATOM   2334  C   HIS A 230      13.399  26.112  11.620  1.00104.65           C  
ATOM   2335  O   HIS A 230      13.611  24.982  11.183  1.00100.23           O  
ATOM   2336  CB  HIS A 230      12.587  27.864  10.000  1.00114.13           C  
ATOM   2337  CG  HIS A 230      13.105  27.181   8.768  1.00115.80           C  
ATOM   2338  ND1 HIS A 230      14.451  26.979   8.542  1.00116.88           N  
ATOM   2339  CD2 HIS A 230      12.462  26.674   7.690  1.00109.61           C  
ATOM   2340  CE1 HIS A 230      14.615  26.376   7.378  1.00111.45           C  
ATOM   2341  NE2 HIS A 230      13.423  26.185   6.839  1.00108.79           N  
ATOM   2342  N   ALA A 231      14.176  26.698  12.533  1.00104.01           N  
ATOM   2343  CA  ALA A 231      15.319  26.004  13.141  1.00103.74           C  
ATOM   2344  C   ALA A 231      14.872  24.830  14.000  1.00101.00           C  
ATOM   2345  O   ALA A 231      15.465  23.769  13.940  1.00108.84           O  
ATOM   2346  CB  ALA A 231      16.165  26.963  13.969  1.00105.46           C  
ATOM   2347  N   ALA A 232      13.826  25.024  14.795  1.00 99.10           N  
ATOM   2348  CA  ALA A 232      13.292  23.955  15.641  1.00100.81           C  
ATOM   2349  C   ALA A 232      12.738  22.797  14.823  1.00104.78           C  
ATOM   2350  O   ALA A 232      12.851  21.643  15.247  1.00105.11           O  
ATOM   2351  CB  ALA A 232      12.215  24.490  16.569  1.00102.98           C  
ATOM   2352  N   LYS A 233      12.138  23.102  13.667  1.00104.26           N  
ATOM   2353  CA  LYS A 233      11.654  22.060  12.748  1.00102.58           C  
ATOM   2354  C   LYS A 233      12.812  21.229  12.216  1.00 92.50           C  
ATOM   2355  O   LYS A 233      12.726  19.999  12.153  1.00 82.87           O  
ATOM   2356  CB  LYS A 233      10.846  22.662  11.580  1.00112.96           C  
ATOM   2357  CG  LYS A 233       9.445  23.105  11.978  1.00121.39           C  
ATOM   2358  CD  LYS A 233       8.589  23.626  10.828  1.00120.94           C  
ATOM   2359  CE  LYS A 233       7.262  24.155  11.370  1.00121.43           C  
ATOM   2360  NZ  LYS A 233       6.498  24.962  10.381  1.00122.94           N  
ATOM   2361  N   SER A 234      13.891  21.914  11.840  1.00 87.89           N  
ATOM   2362  CA  SER A 234      15.083  21.252  11.320  1.00 86.59           C  
ATOM   2363  C   SER A 234      15.662  20.267  12.332  1.00 85.39           C  
ATOM   2364  O   SER A 234      16.028  19.147  11.972  1.00 90.00           O  
ATOM   2365  CB  SER A 234      16.140  22.286  10.915  1.00 87.24           C  
ATOM   2366  OG  SER A 234      15.635  23.190   9.940  1.00 88.15           O  
ATOM   2367  N   LEU A 235      15.714  20.676  13.597  1.00 84.84           N  
ATOM   2368  CA  LEU A 235      16.263  19.831  14.662  1.00 84.31           C  
ATOM   2369  C   LEU A 235      15.313  18.680  15.025  1.00 82.33           C  
ATOM   2370  O   LEU A 235      15.765  17.576  15.371  1.00 82.03           O  
ATOM   2371  CB  LEU A 235      16.615  20.675  15.894  1.00 83.01           C  
ATOM   2372  CG  LEU A 235      17.620  21.819  15.634  1.00 84.23           C  
ATOM   2373  CD1 LEU A 235      17.726  22.749  16.837  1.00 86.09           C  
ATOM   2374  CD2 LEU A 235      18.997  21.310  15.227  1.00 83.59           C  
ATOM   2375  N   ALA A 236      14.008  18.926  14.916  1.00 79.33           N  
ATOM   2376  CA  ALA A 236      13.008  17.879  15.154  1.00 82.24           C  
ATOM   2377  C   ALA A 236      13.106  16.742  14.127  1.00 81.84           C  
ATOM   2378  O   ALA A 236      12.884  15.571  14.454  1.00 76.08           O  
ATOM   2379  CB  ALA A 236      11.606  18.472  15.156  1.00 84.43           C  
ATOM   2380  N   ILE A 237      13.440  17.096  12.890  1.00 81.31           N  
ATOM   2381  CA  ILE A 237      13.663  16.095  11.851  1.00 84.14           C  
ATOM   2382  C   ILE A 237      14.794  15.137  12.251  1.00 85.26           C  
ATOM   2383  O   ILE A 237      14.705  13.929  12.000  1.00 87.82           O  
ATOM   2384  CB  ILE A 237      13.919  16.764  10.478  1.00 84.59           C  
ATOM   2385  CG1 ILE A 237      12.608  17.395   9.984  1.00 82.82           C  
ATOM   2386  CG2 ILE A 237      14.470  15.763   9.450  1.00 82.73           C  
ATOM   2387  CD1 ILE A 237      12.774  18.383   8.852  1.00 84.18           C  
ATOM   2388  N   ILE A 238      15.829  15.671  12.896  1.00 84.06           N  
ATOM   2389  CA  ILE A 238      16.951  14.852  13.353  1.00 85.18           C  
ATOM   2390  C   ILE A 238      16.453  13.772  14.320  1.00 81.25           C  
ATOM   2391  O   ILE A 238      16.855  12.609  14.225  1.00 72.67           O  
ATOM   2392  CB  ILE A 238      18.061  15.699  14.034  1.00 91.01           C  
ATOM   2393  CG1 ILE A 238      18.619  16.774  13.078  1.00 94.27           C  
ATOM   2394  CG2 ILE A 238      19.197  14.807  14.533  1.00 91.70           C  
ATOM   2395  CD1 ILE A 238      19.757  16.311  12.184  1.00 95.70           C  
ATOM   2396  N   VAL A 239      15.565  14.164  15.229  1.00 84.92           N  
ATOM   2397  CA  VAL A 239      15.003  13.236  16.213  1.00 83.58           C  
ATOM   2398  C   VAL A 239      14.070  12.234  15.518  1.00 80.43           C  
ATOM   2399  O   VAL A 239      14.036  11.069  15.884  1.00 78.04           O  
ATOM   2400  CB  VAL A 239      14.240  13.986  17.336  1.00 83.44           C  
ATOM   2401  CG1 VAL A 239      13.647  13.010  18.346  1.00 79.87           C  
ATOM   2402  CG2 VAL A 239      15.147  14.994  18.033  1.00 82.10           C  
ATOM   2403  N   GLY A 240      13.317  12.692  14.523  1.00 77.79           N  
ATOM   2404  CA  GLY A 240      12.440  11.816  13.762  1.00 78.83           C  
ATOM   2405  C   GLY A 240      13.179  10.717  13.022  1.00 80.66           C  
ATOM   2406  O   GLY A 240      12.767   9.557  13.038  1.00 84.44           O  
ATOM   2407  N   LEU A 241      14.276  11.079  12.371  1.00 82.64           N  
ATOM   2408  CA  LEU A 241      15.062  10.091  11.640  1.00 81.45           C  
ATOM   2409  C   LEU A 241      15.785   9.137  12.578  1.00 81.15           C  
ATOM   2410  O   LEU A 241      16.005   7.988  12.222  1.00 84.68           O  
ATOM   2411  CB  LEU A 241      16.041  10.759  10.665  1.00 78.29           C  
ATOM   2412  CG  LEU A 241      15.349  11.419   9.466  1.00 75.97           C  
ATOM   2413  CD1 LEU A 241      16.368  12.156   8.623  1.00 73.31           C  
ATOM   2414  CD2 LEU A 241      14.573  10.403   8.624  1.00 73.84           C  
ATOM   2415  N   PHE A 242      16.141   9.603  13.771  1.00 80.11           N  
ATOM   2416  CA  PHE A 242      16.718   8.726  14.786  1.00 83.42           C  
ATOM   2417  C   PHE A 242      15.730   7.627  15.151  1.00 84.82           C  
ATOM   2418  O   PHE A 242      16.095   6.450  15.182  1.00 82.86           O  
ATOM   2419  CB  PHE A 242      17.122   9.524  16.043  1.00 85.17           C  
ATOM   2420  CG  PHE A 242      17.711   8.680  17.142  1.00 79.81           C  
ATOM   2421  CD1 PHE A 242      16.889   8.068  18.078  1.00 76.08           C  
ATOM   2422  CD2 PHE A 242      19.089   8.485  17.225  1.00 81.49           C  
ATOM   2423  CE1 PHE A 242      17.425   7.273  19.072  1.00 79.19           C  
ATOM   2424  CE2 PHE A 242      19.637   7.699  18.222  1.00 80.23           C  
ATOM   2425  CZ  PHE A 242      18.800   7.089  19.147  1.00 81.61           C  
ATOM   2426  N   ALA A 243      14.492   8.027  15.439  1.00 87.82           N  
ATOM   2427  CA  ALA A 243      13.442   7.075  15.799  1.00 89.69           C  
ATOM   2428  C   ALA A 243      13.147   6.092  14.667  1.00 88.45           C  
ATOM   2429  O   ALA A 243      12.982   4.903  14.912  1.00 86.78           O  
ATOM   2430  CB  ALA A 243      12.175   7.801  16.232  1.00 87.03           C  
ATOM   2431  N   LEU A 244      13.115   6.589  13.436  1.00 86.39           N  
ATOM   2432  CA  LEU A 244      12.847   5.739  12.273  1.00 86.22           C  
ATOM   2433  C   LEU A 244      13.916   4.643  12.073  1.00 85.61           C  
ATOM   2434  O   LEU A 244      13.597   3.507  11.744  1.00 80.84           O  
ATOM   2435  CB  LEU A 244      12.757   6.589  11.000  1.00 89.79           C  
ATOM   2436  CG  LEU A 244      12.558   5.855   9.665  1.00 94.33           C  
ATOM   2437  CD1 LEU A 244      11.212   5.134   9.719  1.00 99.62           C  
ATOM   2438  CD2 LEU A 244      12.636   6.750   8.427  1.00 94.99           C  
ATOM   2439  N   CYS A 245      15.177   4.988  12.305  1.00 87.92           N  
ATOM   2440  CA  CYS A 245      16.287   4.058  12.082  1.00 84.98           C  
ATOM   2441  C   CYS A 245      16.423   3.035  13.207  1.00 85.42           C  
ATOM   2442  O   CYS A 245      16.909   1.916  12.970  1.00 85.47           O  
ATOM   2443  CB  CYS A 245      17.615   4.789  11.911  1.00 84.48           C  
ATOM   2444  SG  CYS A 245      17.650   5.824  10.440  1.00 84.68           S  
ATOM   2445  N   TRP A 246      16.013   3.418  14.419  1.00 82.08           N  
ATOM   2446  CA  TRP A 246      16.199   2.570  15.594  1.00 78.88           C  
ATOM   2447  C   TRP A 246      14.955   1.814  16.044  1.00 76.31           C  
ATOM   2448  O   TRP A 246      15.090   0.788  16.689  1.00 77.54           O  
ATOM   2449  CB  TRP A 246      16.751   3.378  16.765  1.00 77.62           C  
ATOM   2450  CG  TRP A 246      18.218   3.633  16.677  1.00 78.21           C  
ATOM   2451  CD1 TRP A 246      18.823   4.807  16.344  1.00 80.98           C  
ATOM   2452  CD2 TRP A 246      19.272   2.700  16.933  1.00 75.27           C  
ATOM   2453  NE1 TRP A 246      20.188   4.670  16.381  1.00 80.59           N  
ATOM   2454  CE2 TRP A 246      20.491   3.382  16.734  1.00 78.28           C  
ATOM   2455  CE3 TRP A 246      19.307   1.355  17.301  1.00 75.51           C  
ATOM   2456  CZ2 TRP A 246      21.733   2.760  16.892  1.00 77.80           C  
ATOM   2457  CZ3 TRP A 246      20.543   0.740  17.456  1.00 76.50           C  
ATOM   2458  CH2 TRP A 246      21.736   1.442  17.248  1.00 76.69           C  
ATOM   2459  N   LEU A 247      13.758   2.293  15.720  1.00 74.54           N  
ATOM   2460  CA  LEU A 247      12.530   1.612  16.181  1.00 76.28           C  
ATOM   2461  C   LEU A 247      12.313   0.192  15.651  1.00 80.07           C  
ATOM   2462  O   LEU A 247      11.838  -0.649  16.401  1.00 80.77           O  
ATOM   2463  CB  LEU A 247      11.275   2.454  15.921  1.00 77.97           C  
ATOM   2464  CG  LEU A 247      10.990   3.532  16.964  1.00 79.88           C  
ATOM   2465  CD1 LEU A 247       9.884   4.466  16.503  1.00 80.48           C  
ATOM   2466  CD2 LEU A 247      10.600   2.878  18.273  1.00 84.92           C  
ATOM   2467  N   PRO A 248      12.654  -0.088  14.370  1.00 88.81           N  
ATOM   2468  CA  PRO A 248      12.515  -1.470  13.884  1.00 90.72           C  
ATOM   2469  C   PRO A 248      13.238  -2.513  14.734  1.00 90.95           C  
ATOM   2470  O   PRO A 248      12.667  -3.564  15.050  1.00 95.24           O  
ATOM   2471  CB  PRO A 248      13.133  -1.405  12.483  1.00 88.48           C  
ATOM   2472  CG  PRO A 248      12.830  -0.028  12.037  1.00 86.84           C  
ATOM   2473  CD  PRO A 248      13.025   0.818  13.265  1.00 89.47           C  
ATOM   2474  N   LEU A 249      14.475  -2.208  15.111  1.00 89.09           N  
ATOM   2475  CA  LEU A 249      15.281  -3.127  15.911  1.00 84.01           C  
ATOM   2476  C   LEU A 249      14.635  -3.350  17.280  1.00 80.73           C  
ATOM   2477  O   LEU A 249      14.482  -4.497  17.713  1.00 71.72           O  
ATOM   2478  CB  LEU A 249      16.720  -2.595  16.035  1.00 82.27           C  
ATOM   2479  CG  LEU A 249      17.875  -3.576  16.221  1.00 80.40           C  
ATOM   2480  CD1 LEU A 249      17.720  -4.818  15.366  1.00 81.49           C  
ATOM   2481  CD2 LEU A 249      19.186  -2.886  15.877  1.00 79.79           C  
ATOM   2482  N   HIS A 250      14.227  -2.253  17.925  1.00 83.44           N  
ATOM   2483  CA  HIS A 250      13.490  -2.310  19.193  1.00 88.26           C  
ATOM   2484  C   HIS A 250      12.188  -3.101  19.064  1.00 90.12           C  
ATOM   2485  O   HIS A 250      11.868  -3.892  19.951  1.00 92.81           O  
ATOM   2486  CB  HIS A 250      13.190  -0.903  19.735  1.00 89.60           C  
ATOM   2487  CG  HIS A 250      14.399  -0.181  20.251  1.00 89.59           C  
ATOM   2488  ND1 HIS A 250      15.135  -0.635  21.323  1.00 89.18           N  
ATOM   2489  CD2 HIS A 250      14.986   0.973  19.854  1.00 88.76           C  
ATOM   2490  CE1 HIS A 250      16.125   0.205  21.561  1.00 88.70           C  
ATOM   2491  NE2 HIS A 250      16.066   1.183  20.676  1.00 87.19           N  
ATOM   2492  N   ILE A 251      11.452  -2.895  17.968  1.00 91.37           N  
ATOM   2493  CA  ILE A 251      10.178  -3.604  17.727  1.00 89.71           C  
ATOM   2494  C   ILE A 251      10.397  -5.102  17.509  1.00 91.10           C  
ATOM   2495  O   ILE A 251       9.610  -5.928  17.986  1.00 91.26           O  
ATOM   2496  CB  ILE A 251       9.392  -2.995  16.541  1.00 84.95           C  
ATOM   2497  CG1 ILE A 251       8.822  -1.640  16.958  1.00 88.73           C  
ATOM   2498  CG2 ILE A 251       8.245  -3.902  16.093  1.00 82.75           C  
ATOM   2499  CD1 ILE A 251       8.299  -0.804  15.808  1.00 91.96           C  
ATOM   2500  N   ILE A 252      11.450  -5.449  16.780  1.00 90.40           N  
ATOM   2501  CA  ILE A 252      11.784  -6.850  16.571  1.00 89.40           C  
ATOM   2502  C   ILE A 252      12.069  -7.519  17.909  1.00 85.98           C  
ATOM   2503  O   ILE A 252      11.601  -8.624  18.178  1.00 90.16           O  
ATOM   2504  CB  ILE A 252      12.975  -7.004  15.606  1.00 93.26           C  
ATOM   2505  CG1 ILE A 252      12.524  -6.695  14.170  1.00 92.67           C  
ATOM   2506  CG2 ILE A 252      13.535  -8.418  15.662  1.00 99.51           C  
ATOM   2507  CD1 ILE A 252      13.652  -6.512  13.173  1.00 92.37           C  
ATOM   2508  N   ASN A 253      12.842  -6.845  18.738  1.00 85.02           N  
ATOM   2509  CA  ASN A 253      13.153  -7.358  20.059  1.00 91.19           C  
ATOM   2510  C   ASN A 253      11.896  -7.525  20.935  1.00 87.09           C  
ATOM   2511  O   ASN A 253      11.807  -8.468  21.715  1.00 83.23           O  
ATOM   2512  CB  ASN A 253      14.210  -6.466  20.718  1.00 95.19           C  
ATOM   2513  CG  ASN A 253      15.580  -6.593  20.052  1.00 94.51           C  
ATOM   2514  OD1 ASN A 253      15.870  -7.582  19.368  1.00 92.58           O  
ATOM   2515  ND2 ASN A 253      16.435  -5.597  20.266  1.00 93.76           N  
ATOM   2516  N   CYS A 254      10.916  -6.639  20.777  1.00 85.17           N  
ATOM   2517  CA  CYS A 254       9.624  -6.800  21.460  1.00 86.25           C  
ATOM   2518  C   CYS A 254       8.926  -8.103  21.062  1.00 83.82           C  
ATOM   2519  O   CYS A 254       8.413  -8.823  21.916  1.00 90.60           O  
ATOM   2520  CB  CYS A 254       8.700  -5.601  21.214  1.00 84.89           C  
ATOM   2521  SG  CYS A 254       9.203  -4.104  22.095  1.00 87.43           S  
ATOM   2522  N   PHE A 255       8.924  -8.410  19.776  1.00 80.28           N  
ATOM   2523  CA  PHE A 255       8.325  -9.651  19.314  1.00 84.37           C  
ATOM   2524  C   PHE A 255       9.063 -10.880  19.840  1.00 82.50           C  
ATOM   2525  O   PHE A 255       8.439 -11.843  20.292  1.00 82.91           O  
ATOM   2526  CB  PHE A 255       8.249  -9.673  17.788  1.00 90.53           C  
ATOM   2527  CG  PHE A 255       7.016  -9.020  17.247  1.00 94.07           C  
ATOM   2528  CD1 PHE A 255       6.978  -7.647  17.033  1.00 94.94           C  
ATOM   2529  CD2 PHE A 255       5.877  -9.781  16.967  1.00 94.70           C  
ATOM   2530  CE1 PHE A 255       5.834  -7.042  16.535  1.00 97.46           C  
ATOM   2531  CE2 PHE A 255       4.729  -9.182  16.469  1.00 96.62           C  
ATOM   2532  CZ  PHE A 255       4.705  -7.810  16.255  1.00 96.80           C  
ATOM   2533  N   THR A 256      10.385 -10.840  19.788  1.00 81.27           N  
ATOM   2534  CA  THR A 256      11.198 -11.910  20.350  1.00 84.74           C  
ATOM   2535  C   THR A 256      10.888 -12.139  21.830  1.00 81.48           C  
ATOM   2536  O   THR A 256      10.789 -13.274  22.279  1.00 82.04           O  
ATOM   2537  CB  THR A 256      12.696 -11.584  20.210  1.00 90.90           C  
ATOM   2538  OG1 THR A 256      13.010 -11.367  18.827  1.00 92.47           O  
ATOM   2539  CG2 THR A 256      13.562 -12.706  20.796  1.00 89.44           C  
ATOM   2540  N   PHE A 257      10.739 -11.051  22.575  1.00 81.51           N  
ATOM   2541  CA  PHE A 257      10.555 -11.118  24.018  1.00 82.38           C  
ATOM   2542  C   PHE A 257       9.137 -11.502  24.400  1.00 83.63           C  
ATOM   2543  O   PHE A 257       8.931 -12.430  25.180  1.00 83.11           O  
ATOM   2544  CB  PHE A 257      10.919  -9.772  24.647  1.00 84.44           C  
ATOM   2545  CG  PHE A 257      10.885  -9.778  26.138  1.00 85.22           C  
ATOM   2546  CD1 PHE A 257      11.762 -10.574  26.868  1.00 89.36           C  
ATOM   2547  CD2 PHE A 257       9.976  -8.991  26.809  1.00 88.65           C  
ATOM   2548  CE1 PHE A 257      11.717 -10.592  28.249  1.00 95.29           C  
ATOM   2549  CE2 PHE A 257       9.924  -8.996  28.187  1.00 95.92           C  
ATOM   2550  CZ  PHE A 257      10.796  -9.793  28.913  1.00 99.58           C  
ATOM   2551  N   PHE A 258       8.166 -10.792  23.834  1.00 91.02           N  
ATOM   2552  CA  PHE A 258       6.769 -10.916  24.250  1.00 93.81           C  
ATOM   2553  C   PHE A 258       5.984 -12.056  23.594  1.00100.50           C  
ATOM   2554  O   PHE A 258       4.953 -12.462  24.134  1.00109.80           O  
ATOM   2555  CB  PHE A 258       6.024  -9.589  24.046  1.00 91.81           C  
ATOM   2556  CG  PHE A 258       6.435  -8.506  25.000  1.00 91.94           C  
ATOM   2557  CD1 PHE A 258       6.440  -8.738  26.371  1.00 94.90           C  
ATOM   2558  CD2 PHE A 258       6.784  -7.239  24.541  1.00 95.25           C  
ATOM   2559  CE1 PHE A 258       6.812  -7.745  27.265  1.00 97.60           C  
ATOM   2560  CE2 PHE A 258       7.156  -6.236  25.434  1.00 99.25           C  
ATOM   2561  CZ  PHE A 258       7.172  -6.492  26.799  1.00 98.63           C  
ATOM   2562  N   CYS A 259       6.456 -12.578  22.461  1.00104.64           N  
ATOM   2563  CA  CYS A 259       5.756 -13.652  21.757  1.00110.22           C  
ATOM   2564  C   CYS A 259       6.627 -14.905  21.633  1.00107.58           C  
ATOM   2565  O   CYS A 259       7.290 -15.103  20.624  1.00103.56           O  
ATOM   2566  CB  CYS A 259       5.298 -13.166  20.381  1.00113.97           C  
ATOM   2567  SG  CYS A 259       4.338 -14.395  19.474  1.00116.11           S  
ATOM   2568  N   PRO A 260       6.624 -15.765  22.661  1.00116.34           N  
ATOM   2569  CA  PRO A 260       7.352 -17.032  22.529  1.00120.84           C  
ATOM   2570  C   PRO A 260       6.691 -18.003  21.552  1.00120.00           C  
ATOM   2571  O   PRO A 260       7.362 -18.908  21.059  1.00125.75           O  
ATOM   2572  CB  PRO A 260       7.354 -17.598  23.956  1.00127.92           C  
ATOM   2573  CG  PRO A 260       6.175 -16.977  24.614  1.00130.49           C  
ATOM   2574  CD  PRO A 260       6.005 -15.618  23.991  1.00128.22           C  
ATOM   2575  N   ASP A 261       5.398 -17.822  21.278  1.00118.20           N  
ATOM   2576  CA  ASP A 261       4.723 -18.591  20.230  1.00119.97           C  
ATOM   2577  C   ASP A 261       5.095 -18.163  18.807  1.00114.95           C  
ATOM   2578  O   ASP A 261       4.790 -18.883  17.863  1.00114.33           O  
ATOM   2579  CB  ASP A 261       3.197 -18.531  20.398  1.00123.45           C  
ATOM   2580  CG  ASP A 261       2.685 -19.487  21.457  1.00125.93           C  
ATOM   2581  OD1 ASP A 261       3.240 -20.599  21.587  1.00126.85           O  
ATOM   2582  OD2 ASP A 261       1.711 -19.133  22.149  1.00126.76           O  
ATOM   2583  N   CYS A 262       5.724 -16.998  18.643  1.00104.22           N  
ATOM   2584  CA  CYS A 262       6.193 -16.548  17.332  1.00 97.34           C  
ATOM   2585  C   CYS A 262       7.538 -17.167  16.976  1.00101.01           C  
ATOM   2586  O   CYS A 262       8.426 -17.272  17.820  1.00103.95           O  
ATOM   2587  CB  CYS A 262       6.365 -15.037  17.312  1.00 96.23           C  
ATOM   2588  SG  CYS A 262       4.853 -14.091  17.532  1.00 97.21           S  
ATOM   2589  N   SER A 263       7.698 -17.562  15.715  1.00102.07           N  
ATOM   2590  CA  SER A 263       9.013 -17.964  15.208  1.00 93.92           C  
ATOM   2591  C   SER A 263       9.848 -16.706  15.104  1.00 89.86           C  
ATOM   2592  O   SER A 263       9.335 -15.628  14.825  1.00 89.19           O  
ATOM   2593  CB  SER A 263       8.912 -18.653  13.851  1.00 92.90           C  
ATOM   2594  OG  SER A 263       8.079 -17.918  12.979  1.00 97.12           O  
ATOM   2595  N   HIS A 264      11.138 -16.843  15.347  1.00 89.65           N  
ATOM   2596  CA  HIS A 264      12.010 -15.683  15.454  1.00 92.09           C  
ATOM   2597  C   HIS A 264      12.089 -14.960  14.122  1.00 84.54           C  
ATOM   2598  O   HIS A 264      12.041 -15.590  13.069  1.00 84.71           O  
ATOM   2599  CB  HIS A 264      13.406 -16.127  15.902  1.00 99.37           C  
ATOM   2600  CG  HIS A 264      14.252 -15.024  16.452  1.00100.91           C  
ATOM   2601  ND1 HIS A 264      14.808 -14.046  15.657  1.00104.12           N  
ATOM   2602  CD2 HIS A 264      14.659 -14.763  17.715  1.00100.14           C  
ATOM   2603  CE1 HIS A 264      15.509 -13.221  16.409  1.00105.90           C  
ATOM   2604  NE2 HIS A 264      15.438 -13.635  17.660  1.00103.71           N  
ATOM   2605  N   ALA A 265      12.199 -13.641  14.174  1.00 82.22           N  
ATOM   2606  CA  ALA A 265      12.426 -12.857  12.971  1.00 85.91           C  
ATOM   2607  C   ALA A 265      13.645 -13.400  12.210  1.00 86.79           C  
ATOM   2608  O   ALA A 265      14.665 -13.734  12.821  1.00 80.69           O  
ATOM   2609  CB  ALA A 265      12.632 -11.395  13.320  1.00 88.30           C  
ATOM   2610  N   PRO A 266      13.535 -13.507  10.877  1.00 89.78           N  
ATOM   2611  CA  PRO A 266      14.599 -14.158  10.102  1.00 91.03           C  
ATOM   2612  C   PRO A 266      15.919 -13.406  10.112  1.00 88.40           C  
ATOM   2613  O   PRO A 266      15.943 -12.219  10.396  1.00 93.07           O  
ATOM   2614  CB  PRO A 266      14.017 -14.218   8.693  1.00 92.79           C  
ATOM   2615  CG  PRO A 266      13.002 -13.136   8.653  1.00 93.53           C  
ATOM   2616  CD  PRO A 266      12.425 -13.053  10.020  1.00 91.81           C  
ATOM   2617  N   LEU A 267      17.003 -14.109   9.812  1.00 87.04           N  
ATOM   2618  CA  LEU A 267      18.344 -13.546   9.954  1.00 92.02           C  
ATOM   2619  C   LEU A 267      18.539 -12.334   9.030  1.00 95.78           C  
ATOM   2620  O   LEU A 267      19.039 -11.290   9.451  1.00106.03           O  
ATOM   2621  CB  LEU A 267      19.425 -14.616   9.707  1.00 96.11           C  
ATOM   2622  CG  LEU A 267      20.732 -14.459  10.501  1.00100.80           C  
ATOM   2623  CD1 LEU A 267      20.516 -14.794  11.974  1.00105.30           C  
ATOM   2624  CD2 LEU A 267      21.862 -15.310   9.936  1.00101.14           C  
ATOM   2625  N   TRP A 268      18.115 -12.464   7.780  1.00 95.48           N  
ATOM   2626  CA  TRP A 268      18.212 -11.357   6.824  1.00 91.08           C  
ATOM   2627  C   TRP A 268      17.517 -10.077   7.320  1.00 95.13           C  
ATOM   2628  O   TRP A 268      17.999  -8.979   7.050  1.00 99.23           O  
ATOM   2629  CB  TRP A 268      17.665 -11.773   5.449  1.00 84.35           C  
ATOM   2630  CG  TRP A 268      16.183 -12.036   5.417  1.00 76.02           C  
ATOM   2631  CD1 TRP A 268      15.565 -13.247   5.539  1.00 71.08           C  
ATOM   2632  CD2 TRP A 268      15.145 -11.064   5.243  1.00 72.35           C  
ATOM   2633  NE1 TRP A 268      14.211 -13.085   5.460  1.00 71.70           N  
ATOM   2634  CE2 TRP A 268      13.923 -11.755   5.284  1.00 72.30           C  
ATOM   2635  CE3 TRP A 268      15.132  -9.671   5.068  1.00 76.02           C  
ATOM   2636  CZ2 TRP A 268      12.684 -11.102   5.146  1.00 75.61           C  
ATOM   2637  CZ3 TRP A 268      13.900  -9.020   4.935  1.00 80.38           C  
ATOM   2638  CH2 TRP A 268      12.693  -9.742   4.978  1.00 78.65           C  
ATOM   2639  N   LEU A 269      16.398 -10.222   8.038  1.00 94.00           N  
ATOM   2640  CA  LEU A 269      15.677  -9.067   8.575  1.00 95.63           C  
ATOM   2641  C   LEU A 269      16.404  -8.460   9.757  1.00 96.97           C  
ATOM   2642  O   LEU A 269      16.440  -7.239   9.891  1.00 93.55           O  
ATOM   2643  CB  LEU A 269      14.245  -9.429   8.981  1.00 94.70           C  
ATOM   2644  CG  LEU A 269      13.338  -8.260   9.382  1.00 92.71           C  
ATOM   2645  CD1 LEU A 269      13.227  -7.214   8.279  1.00 91.50           C  
ATOM   2646  CD2 LEU A 269      11.967  -8.794   9.757  1.00 92.73           C  
ATOM   2647  N   MET A 270      16.998  -9.295  10.561  1.00100.06           N  
ATOM   2648  CA  MET A 270      17.706  -8.748  11.648  1.00101.60           C  
ATOM   2649  C   MET A 270      18.754  -7.845  11.059  1.00103.98           C  
ATOM   2650  O   MET A 270      18.794  -6.664  11.335  1.00117.16           O  
ATOM   2651  CB  MET A 270      18.377  -9.856  12.419  1.00102.45           C  
ATOM   2652  CG  MET A 270      17.422 -10.946  12.824  1.00100.11           C  
ATOM   2653  SD  MET A 270      16.368 -10.319  14.114  1.00104.25           S  
ATOM   2654  CE  MET A 270      17.536  -9.436  15.113  1.00102.15           C  
ATOM   2655  N   TYR A 271      19.601  -8.407  10.222  1.00101.88           N  
ATOM   2656  CA  TYR A 271      20.751  -7.668   9.699  1.00102.47           C  
ATOM   2657  C   TYR A 271      20.347  -6.454   8.861  1.00 98.89           C  
ATOM   2658  O   TYR A 271      21.100  -5.488   8.779  1.00102.70           O  
ATOM   2659  CB  TYR A 271      21.715  -8.595   8.946  1.00103.03           C  
ATOM   2660  CG  TYR A 271      22.531  -9.415   9.908  1.00 99.52           C  
ATOM   2661  CD1 TYR A 271      23.659  -8.879  10.511  1.00 97.96           C  
ATOM   2662  CD2 TYR A 271      22.150 -10.707  10.258  1.00102.03           C  
ATOM   2663  CE1 TYR A 271      24.400  -9.616  11.423  1.00101.26           C  
ATOM   2664  CE2 TYR A 271      22.879 -11.454  11.168  1.00101.04           C  
ATOM   2665  CZ  TYR A 271      23.999 -10.909  11.753  1.00 99.55           C  
ATOM   2666  OH  TYR A 271      24.703 -11.670  12.657  1.00 91.89           O  
ATOM   2667  N   LEU A 272      19.173  -6.495   8.246  1.00 90.26           N  
ATOM   2668  CA  LEU A 272      18.654  -5.314   7.579  1.00 91.63           C  
ATOM   2669  C   LEU A 272      18.355  -4.210   8.600  1.00 89.93           C  
ATOM   2670  O   LEU A 272      18.647  -3.033   8.361  1.00 88.11           O  
ATOM   2671  CB  LEU A 272      17.407  -5.674   6.779  1.00 96.06           C  
ATOM   2672  CG  LEU A 272      16.699  -4.576   5.975  1.00 95.43           C  
ATOM   2673  CD1 LEU A 272      17.649  -3.809   5.062  1.00 94.26           C  
ATOM   2674  CD2 LEU A 272      15.561  -5.203   5.183  1.00 91.13           C  
ATOM   2675  N   ALA A 273      17.782  -4.598   9.737  1.00 91.47           N  
ATOM   2676  CA  ALA A 273      17.469  -3.641  10.814  1.00 93.53           C  
ATOM   2677  C   ALA A 273      18.734  -3.083  11.492  1.00 90.56           C  
ATOM   2678  O   ALA A 273      18.777  -1.910  11.874  1.00 86.25           O  
ATOM   2679  CB  ALA A 273      16.536  -4.275  11.845  1.00 89.52           C  
ATOM   2680  N   ILE A 274      19.754  -3.928  11.631  1.00 85.19           N  
ATOM   2681  CA  ILE A 274      21.051  -3.507  12.155  1.00 81.35           C  
ATOM   2682  C   ILE A 274      21.684  -2.494  11.213  1.00 81.79           C  
ATOM   2683  O   ILE A 274      22.167  -1.463  11.657  1.00 77.27           O  
ATOM   2684  CB  ILE A 274      21.994  -4.722  12.344  1.00 83.91           C  
ATOM   2685  CG1 ILE A 274      21.498  -5.569  13.518  1.00 87.18           C  
ATOM   2686  CG2 ILE A 274      23.446  -4.304  12.586  1.00 83.84           C  
ATOM   2687  CD1 ILE A 274      22.121  -6.946  13.595  1.00 90.35           C  
ATOM   2688  N   VAL A 275      21.689  -2.807   9.917  1.00 86.86           N  
ATOM   2689  CA  VAL A 275      22.227  -1.904   8.897  1.00 85.63           C  
ATOM   2690  C   VAL A 275      21.463  -0.573   8.943  1.00 85.31           C  
ATOM   2691  O   VAL A 275      22.077   0.493   8.915  1.00 80.15           O  
ATOM   2692  CB  VAL A 275      22.181  -2.553   7.480  1.00 84.98           C  
ATOM   2693  CG1 VAL A 275      22.321  -1.514   6.378  1.00 86.63           C  
ATOM   2694  CG2 VAL A 275      23.272  -3.607   7.339  1.00 83.81           C  
ATOM   2695  N   LEU A 276      20.135  -0.646   9.037  1.00 84.77           N  
ATOM   2696  CA  LEU A 276      19.310   0.551   9.090  1.00 81.13           C  
ATOM   2697  C   LEU A 276      19.670   1.436  10.299  1.00 84.39           C  
ATOM   2698  O   LEU A 276      19.786   2.653  10.148  1.00 86.39           O  
ATOM   2699  CB  LEU A 276      17.823   0.182   9.084  1.00 76.98           C  
ATOM   2700  CG  LEU A 276      16.842   1.348   9.205  1.00 78.18           C  
ATOM   2701  CD1 LEU A 276      16.870   2.233   7.978  1.00 75.97           C  
ATOM   2702  CD2 LEU A 276      15.442   0.828   9.457  1.00 84.36           C  
ATOM   2703  N   SER A 277      19.863   0.840  11.478  1.00 81.65           N  
ATOM   2704  CA  SER A 277      20.230   1.622  12.667  1.00 80.64           C  
ATOM   2705  C   SER A 277      21.589   2.311  12.500  1.00 82.31           C  
ATOM   2706  O   SER A 277      21.817   3.389  13.054  1.00 84.50           O  
ATOM   2707  CB  SER A 277      20.249   0.756  13.926  1.00 79.89           C  
ATOM   2708  OG  SER A 277      21.428  -0.024  13.975  1.00 78.48           O  
ATOM   2709  N   HIS A 278      22.490   1.681  11.751  1.00 84.24           N  
ATOM   2710  CA  HIS A 278      23.814   2.260  11.494  1.00 81.23           C  
ATOM   2711  C   HIS A 278      23.772   3.428  10.505  1.00 78.33           C  
ATOM   2712  O   HIS A 278      24.547   4.372  10.620  1.00 72.29           O  
ATOM   2713  CB  HIS A 278      24.795   1.194  11.001  1.00 78.99           C  
ATOM   2714  CG  HIS A 278      25.086   0.129  12.010  1.00 77.64           C  
ATOM   2715  ND1 HIS A 278      25.729  -1.042  11.683  1.00 76.83           N  
ATOM   2716  CD2 HIS A 278      24.820   0.055  13.336  1.00 77.94           C  
ATOM   2717  CE1 HIS A 278      25.858  -1.789  12.764  1.00 76.87           C  
ATOM   2718  NE2 HIS A 278      25.310  -1.149  13.780  1.00 78.77           N  
ATOM   2719  N   THR A 279      22.847   3.385   9.556  1.00 81.09           N  
ATOM   2720  CA  THR A 279      22.758   4.453   8.570  1.00 83.28           C  
ATOM   2721  C   THR A 279      22.328   5.791   9.166  1.00 86.31           C  
ATOM   2722  O   THR A 279      22.516   6.818   8.528  1.00 92.45           O  
ATOM   2723  CB  THR A 279      21.782   4.133   7.424  1.00 82.42           C  
ATOM   2724  OG1 THR A 279      20.438   4.189   7.914  1.00 82.81           O  
ATOM   2725  CG2 THR A 279      22.062   2.772   6.810  1.00 82.55           C  
ATOM   2726  N   ASN A 280      21.762   5.766  10.368  1.00 86.14           N  
ATOM   2727  CA  ASN A 280      21.314   6.986  11.030  1.00 84.19           C  
ATOM   2728  C   ASN A 280      22.473   7.914  11.378  1.00 79.62           C  
ATOM   2729  O   ASN A 280      22.267   9.074  11.734  1.00 79.73           O  
ATOM   2730  CB  ASN A 280      20.514   6.649  12.290  1.00 88.97           C  
ATOM   2731  CG  ASN A 280      19.816   7.859  12.879  1.00 91.21           C  
ATOM   2732  OD1 ASN A 280      20.115   8.280  13.997  1.00 94.03           O  
ATOM   2733  ND2 ASN A 280      18.877   8.424  12.129  1.00 90.28           N  
ATOM   2734  N   SER A 281      23.692   7.395  11.272  1.00 79.47           N  
ATOM   2735  CA  SER A 281      24.886   8.174  11.574  1.00 85.68           C  
ATOM   2736  C   SER A 281      25.515   8.678  10.279  1.00 85.74           C  
ATOM   2737  O   SER A 281      26.736   8.792  10.173  1.00 86.94           O  
ATOM   2738  CB  SER A 281      25.911   7.370  12.377  1.00 90.30           C  
ATOM   2739  OG  SER A 281      25.302   6.731  13.485  1.00 98.55           O  
ATOM   2740  N   VAL A 282      24.672   8.978   9.296  1.00 87.42           N  
ATOM   2741  CA  VAL A 282      25.143   9.470   8.006  1.00 84.60           C  
ATOM   2742  C   VAL A 282      24.170  10.484   7.414  1.00 81.33           C  
ATOM   2743  O   VAL A 282      24.536  11.277   6.547  1.00 79.67           O  
ATOM   2744  CB  VAL A 282      25.344   8.319   7.003  1.00 81.85           C  
ATOM   2745  CG1 VAL A 282      25.866   8.855   5.679  1.00 82.81           C  
ATOM   2746  CG2 VAL A 282      26.292   7.276   7.575  1.00 80.55           C  
ATOM   2747  N   VAL A 283      22.928  10.452   7.888  1.00 82.26           N  
ATOM   2748  CA  VAL A 283      21.901  11.368   7.407  1.00 81.74           C  
ATOM   2749  C   VAL A 283      21.973  12.732   8.085  1.00 85.78           C  
ATOM   2750  O   VAL A 283      21.502  13.731   7.542  1.00 90.29           O  
ATOM   2751  CB  VAL A 283      20.488  10.791   7.615  1.00 76.23           C  
ATOM   2752  CG1 VAL A 283      20.398   9.387   7.038  1.00 74.56           C  
ATOM   2753  CG2 VAL A 283      20.128  10.791   9.093  1.00 78.62           C  
ATOM   2754  N   ASN A 284      22.566  12.766   9.274  1.00 90.82           N  
ATOM   2755  CA  ASN A 284      22.700  14.007  10.029  1.00 97.30           C  
ATOM   2756  C   ASN A 284      23.293  15.141   9.199  1.00 94.71           C  
ATOM   2757  O   ASN A 284      22.606  16.109   8.873  1.00 96.15           O  
ATOM   2758  CB  ASN A 284      23.542  13.779  11.286  1.00104.56           C  
ATOM   2759  CG  ASN A 284      22.927  12.759  12.223  1.00108.60           C  
ATOM   2760  OD1 ASN A 284      21.713  12.556  12.229  1.00110.96           O  
ATOM   2761  ND2 ASN A 284      23.765  12.108  13.022  1.00109.70           N  
ATOM   2762  N   PRO A 285      24.572  15.015   8.860  1.00 90.36           N  
ATOM   2763  CA  PRO A 285      25.267  16.041   8.064  1.00 90.10           C  
ATOM   2764  C   PRO A 285      24.486  16.504   6.816  1.00 86.10           C  
ATOM   2765  O   PRO A 285      24.626  17.655   6.386  1.00 81.99           O  
ATOM   2766  CB  PRO A 285      26.595  15.382   7.664  1.00 91.30           C  
ATOM   2767  CG  PRO A 285      26.884  14.427   8.766  1.00 91.58           C  
ATOM   2768  CD  PRO A 285      25.554  13.856   9.165  1.00 92.03           C  
ATOM   2769  N   PHE A 286      23.667  15.623   6.253  1.00 83.56           N  
ATOM   2770  CA  PHE A 286      22.829  15.998   5.121  1.00 84.78           C  
ATOM   2771  C   PHE A 286      21.698  16.927   5.554  1.00 86.41           C  
ATOM   2772  O   PHE A 286      21.395  17.885   4.851  1.00 88.43           O  
ATOM   2773  CB  PHE A 286      22.285  14.763   4.391  1.00 87.35           C  
ATOM   2774  CG  PHE A 286      23.321  14.054   3.575  1.00 89.09           C  
ATOM   2775  CD1 PHE A 286      23.545  14.433   2.260  1.00 90.20           C  
ATOM   2776  CD2 PHE A 286      24.095  13.029   4.124  1.00 87.70           C  
ATOM   2777  CE1 PHE A 286      24.511  13.795   1.498  1.00 94.75           C  
ATOM   2778  CE2 PHE A 286      25.069  12.395   3.374  1.00 89.14           C  
ATOM   2779  CZ  PHE A 286      25.277  12.777   2.059  1.00 95.81           C  
ATOM   2780  N   ILE A 287      21.109  16.654   6.722  1.00 87.97           N  
ATOM   2781  CA  ILE A 287      20.042  17.492   7.276  1.00 86.95           C  
ATOM   2782  C   ILE A 287      20.586  18.895   7.545  1.00 87.82           C  
ATOM   2783  O   ILE A 287      19.915  19.883   7.265  1.00 93.15           O  
ATOM   2784  CB  ILE A 287      19.436  16.898   8.577  1.00 88.80           C  
ATOM   2785  CG1 ILE A 287      18.875  15.484   8.359  1.00 91.60           C  
ATOM   2786  CG2 ILE A 287      18.321  17.784   9.130  1.00 91.17           C  
ATOM   2787  CD1 ILE A 287      17.869  15.368   7.239  1.00 93.93           C  
ATOM   2788  N   TYR A 288      21.798  18.967   8.086  1.00 84.94           N  
ATOM   2789  CA  TYR A 288      22.426  20.247   8.391  1.00 87.25           C  
ATOM   2790  C   TYR A 288      22.556  21.110   7.141  1.00 90.13           C  
ATOM   2791  O   TYR A 288      21.779  22.043   6.935  1.00 90.60           O  
ATOM   2792  CB  TYR A 288      23.801  20.031   9.026  1.00 90.15           C  
ATOM   2793  CG  TYR A 288      23.758  19.301  10.349  1.00 91.40           C  
ATOM   2794  CD1 TYR A 288      22.669  19.431  11.201  1.00 88.93           C  
ATOM   2795  CD2 TYR A 288      24.805  18.480  10.746  1.00 91.98           C  
ATOM   2796  CE1 TYR A 288      22.625  18.766  12.411  1.00 88.61           C  
ATOM   2797  CE2 TYR A 288      24.769  17.810  11.954  1.00 87.60           C  
ATOM   2798  CZ  TYR A 288      23.677  17.957  12.783  1.00 87.81           C  
ATOM   2799  OH  TYR A 288      23.638  17.292  13.987  1.00 89.04           O  
ATOM   2800  N   ALA A 289      23.475  20.725   6.278  1.00 95.97           N  
ATOM   2801  CA  ALA A 289      23.726  21.412   5.024  1.00101.34           C  
ATOM   2802  C   ALA A 289      22.478  21.734   4.242  1.00100.85           C  
ATOM   2803  O   ALA A 289      22.462  22.647   3.432  1.00 97.04           O  
ATOM   2804  CB  ALA A 289      24.644  20.573   4.168  1.00105.12           C  
ATOM   2805  N   TYR A 290      21.428  20.951   4.462  1.00 99.10           N  
ATOM   2806  CA  TYR A 290      20.172  21.150   3.748  1.00100.84           C  
ATOM   2807  C   TYR A 290      19.292  22.172   4.450  1.00103.36           C  
ATOM   2808  O   TYR A 290      18.824  23.132   3.838  1.00114.64           O  
ATOM   2809  CB  TYR A 290      19.423  19.823   3.604  1.00103.78           C  
ATOM   2810  CG  TYR A 290      19.413  19.275   2.195  1.00108.33           C  
ATOM   2811  CD1 TYR A 290      20.557  18.718   1.638  1.00109.16           C  
ATOM   2812  CD2 TYR A 290      18.262  19.316   1.420  1.00109.37           C  
ATOM   2813  CE1 TYR A 290      20.553  18.216   0.351  1.00113.97           C  
ATOM   2814  CE2 TYR A 290      18.248  18.817   0.132  1.00110.18           C  
ATOM   2815  CZ  TYR A 290      19.397  18.268  -0.398  1.00116.41           C  
ATOM   2816  OH  TYR A 290      19.388  17.769  -1.680  1.00128.56           O  
ATOM   2817  N   ARG A 291      19.072  21.958   5.741  1.00 97.17           N  
ATOM   2818  CA  ARG A 291      18.250  22.854   6.532  1.00 96.29           C  
ATOM   2819  C   ARG A 291      18.812  24.141   7.151  1.00 98.73           C  
ATOM   2820  O   ARG A 291      18.129  25.128   7.359  1.00104.80           O  
ATOM   2821  CB  ARG A 291      17.566  22.019   7.601  1.00 95.93           C  
ATOM   2822  CG  ARG A 291      16.657  20.939   7.073  1.00 97.01           C  
ATOM   2823  CD  ARG A 291      15.376  21.535   6.533  1.00 99.55           C  
ATOM   2824  NE  ARG A 291      14.549  22.129   7.570  1.00104.16           N  
ATOM   2825  CZ  ARG A 291      13.464  22.840   7.315  1.00115.51           C  
ATOM   2826  NH1 ARG A 291      13.099  23.042   6.063  1.00123.59           N  
ATOM   2827  NH2 ARG A 291      12.750  23.353   8.301  1.00117.16           N  
ATOM   2828  N   ILE A 292      20.096  24.114   7.426  1.00 98.02           N  
ATOM   2829  CA  ILE A 292      20.753  25.275   8.041  1.00101.27           C  
ATOM   2830  C   ILE A 292      21.780  25.959   7.152  1.00100.15           C  
ATOM   2831  O   ILE A 292      22.802  25.364   6.804  1.00 99.21           O  
ATOM   2832  CB  ILE A 292      21.425  24.721   9.325  1.00100.33           C  
ATOM   2833  CG1 ILE A 292      20.415  23.881  10.129  1.00100.30           C  
ATOM   2834  CG2 ILE A 292      21.961  25.862  10.186  1.00 98.80           C  
ATOM   2835  CD1 ILE A 292      20.977  23.175  11.351  1.00 94.70           C  
ATOM   2836  N   ARG A 293      21.496  27.210   6.795  1.00104.22           N  
ATOM   2837  CA  ARG A 293      22.313  27.965   5.848  1.00113.97           C  
ATOM   2838  C   ARG A 293      23.767  28.093   6.301  1.00118.37           C  
ATOM   2839  O   ARG A 293      24.681  27.912   5.504  1.00123.84           O  
ATOM   2840  CB  ARG A 293      21.707  29.354   5.625  1.00121.91           C  
ATOM   2841  CG  ARG A 293      22.478  30.267   4.670  1.00128.37           C  
ATOM   2842  CD  ARG A 293      21.898  31.684   4.632  1.00133.96           C  
ATOM   2843  NE  ARG A 293      21.164  31.989   3.397  1.00141.05           N  
ATOM   2844  CZ  ARG A 293      19.851  31.823   3.194  1.00142.80           C  
ATOM   2845  NH1 ARG A 293      19.053  31.330   4.145  1.00140.97           N  
ATOM   2846  NH2 ARG A 293      19.326  32.154   2.012  1.00143.68           N  
ATOM   2847  N   GLU A 294      23.973  28.402   7.578  1.00118.50           N  
ATOM   2848  CA  GLU A 294      25.321  28.618   8.106  1.00113.91           C  
ATOM   2849  C   GLU A 294      26.202  27.376   7.966  1.00108.37           C  
ATOM   2850  O   GLU A 294      27.394  27.494   7.702  1.00101.89           O  
ATOM   2851  CB  GLU A 294      25.255  29.067   9.569  1.00115.88           C  
ATOM   2852  CG  GLU A 294      26.563  29.616  10.126  1.00118.67           C  
ATOM   2853  CD  GLU A 294      26.998  30.917   9.464  1.00119.28           C  
ATOM   2854  OE1 GLU A 294      28.218  31.131   9.343  1.00114.48           O  
ATOM   2855  OE2 GLU A 294      26.130  31.718   9.051  1.00120.95           O  
ATOM   2856  N   PHE A 295      25.614  26.197   8.145  1.00109.83           N  
ATOM   2857  CA  PHE A 295      26.338  24.937   7.929  1.00109.10           C  
ATOM   2858  C   PHE A 295      26.643  24.716   6.451  1.00107.98           C  
ATOM   2859  O   PHE A 295      27.767  24.385   6.091  1.00103.71           O  
ATOM   2860  CB  PHE A 295      25.547  23.730   8.472  1.00110.06           C  
ATOM   2861  CG  PHE A 295      25.862  23.388   9.902  1.00104.18           C  
ATOM   2862  CD1 PHE A 295      27.064  22.764  10.232  1.00100.74           C  
ATOM   2863  CD2 PHE A 295      24.957  23.674  10.916  1.00101.73           C  
ATOM   2864  CE1 PHE A 295      27.357  22.436  11.544  1.00100.17           C  
ATOM   2865  CE2 PHE A 295      25.245  23.351  12.233  1.00100.83           C  
ATOM   2866  CZ  PHE A 295      26.445  22.732  12.549  1.00101.50           C  
ATOM   2867  N   ARG A 296      25.626  24.875   5.612  1.00111.11           N  
ATOM   2868  CA  ARG A 296      25.758  24.698   4.166  1.00110.06           C  
ATOM   2869  C   ARG A 296      26.873  25.564   3.590  1.00108.01           C  
ATOM   2870  O   ARG A 296      27.706  25.077   2.839  1.00102.70           O  
ATOM   2871  CB  ARG A 296      24.430  25.044   3.492  1.00112.83           C  
ATOM   2872  CG  ARG A 296      24.438  25.123   1.970  1.00114.50           C  
ATOM   2873  CD  ARG A 296      23.233  25.907   1.515  1.00113.32           C  
ATOM   2874  NE  ARG A 296      22.057  25.432   2.237  1.00112.52           N  
ATOM   2875  CZ  ARG A 296      21.042  26.191   2.638  1.00116.98           C  
ATOM   2876  NH1 ARG A 296      20.993  27.495   2.376  1.00124.98           N  
ATOM   2877  NH2 ARG A 296      20.045  25.633   3.306  1.00118.17           N  
ATOM   2878  N   GLN A 297      26.879  26.844   3.945  1.00110.19           N  
ATOM   2879  CA  GLN A 297      27.890  27.777   3.444  1.00109.89           C  
ATOM   2880  C   GLN A 297      29.295  27.397   3.933  1.00108.30           C  
ATOM   2881  O   GLN A 297      30.263  27.506   3.180  1.00115.21           O  
ATOM   2882  CB  GLN A 297      27.527  29.219   3.821  1.00110.46           C  
ATOM   2883  CG  GLN A 297      26.208  29.679   3.201  1.00114.84           C  
ATOM   2884  CD  GLN A 297      25.975  31.177   3.297  1.00118.37           C  
ATOM   2885  OE1 GLN A 297      25.834  31.852   2.281  1.00118.57           O  
ATOM   2886  NE2 GLN A 297      25.918  31.702   4.519  1.00121.20           N  
ATOM   2887  N   THR A 298      29.400  26.925   5.173  1.00106.66           N  
ATOM   2888  CA  THR A 298      30.685  26.482   5.724  1.00101.80           C  
ATOM   2889  C   THR A 298      31.244  25.207   5.091  1.00105.94           C  
ATOM   2890  O   THR A 298      32.455  25.086   4.885  1.00112.08           O  
ATOM   2891  CB  THR A 298      30.623  26.300   7.254  1.00 92.48           C  
ATOM   2892  OG1 THR A 298      30.054  27.470   7.849  1.00 95.22           O  
ATOM   2893  CG2 THR A 298      32.015  26.085   7.827  1.00 88.19           C  
ATOM   2894  N   PHE A 299      30.349  24.294   4.726  1.00110.76           N  
ATOM   2895  CA  PHE A 299      30.747  23.066   4.057  1.00113.61           C  
ATOM   2896  C   PHE A 299      31.203  23.436   2.645  1.00115.25           C  
ATOM   2897  O   PHE A 299      32.180  22.890   2.133  1.00113.42           O  
ATOM   2898  CB  PHE A 299      29.582  22.079   4.000  1.00115.42           C  
ATOM   2899  CG  PHE A 299      29.184  21.533   5.341  1.00113.08           C  
ATOM   2900  CD1 PHE A 299      30.139  21.037   6.213  1.00109.69           C  
ATOM   2901  CD2 PHE A 299      27.855  21.515   5.730  1.00118.69           C  
ATOM   2902  CE1 PHE A 299      29.776  20.534   7.449  1.00112.50           C  
ATOM   2903  CE2 PHE A 299      27.485  21.014   6.964  1.00118.40           C  
ATOM   2904  CZ  PHE A 299      28.447  20.523   7.824  1.00118.10           C  
ATOM   2905  N   ARG A 300      30.490  24.377   2.033  1.00117.09           N  
ATOM   2906  CA  ARG A 300      30.826  24.840   0.695  1.00125.20           C  
ATOM   2907  C   ARG A 300      32.276  25.299   0.695  1.00131.15           C  
ATOM   2908  O   ARG A 300      33.089  24.824  -0.098  1.00134.15           O  
ATOM   2909  CB  ARG A 300      29.906  25.986   0.273  1.00129.76           C  
ATOM   2910  CG  ARG A 300      30.085  26.428  -1.170  1.00134.85           C  
ATOM   2911  CD  ARG A 300      29.465  27.794  -1.411  1.00134.15           C  
ATOM   2912  NE  ARG A 300      28.008  27.731  -1.468  1.00138.95           N  
ATOM   2913  CZ  ARG A 300      27.326  26.999  -2.342  1.00137.18           C  
ATOM   2914  NH1 ARG A 300      27.969  26.263  -3.239  1.00135.80           N  
ATOM   2915  NH2 ARG A 300      26.000  27.002  -2.321  1.00135.09           N  
ATOM   2916  N   LYS A 301      32.598  26.224   1.595  1.00132.63           N  
ATOM   2917  CA  LYS A 301      33.974  26.731   1.707  1.00121.15           C  
ATOM   2918  C   LYS A 301      35.026  25.654   1.980  1.00111.50           C  
ATOM   2919  O   LYS A 301      36.085  25.644   1.359  1.00107.89           O  
ATOM   2920  CB  LYS A 301      34.017  27.801   2.803  1.00115.76           C  
ATOM   2921  N   ILE A 302      34.722  24.738   2.890  1.00109.38           N  
ATOM   2922  CA  ILE A 302      35.662  23.664   3.229  1.00113.27           C  
ATOM   2923  C   ILE A 302      35.908  22.781   2.005  1.00120.73           C  
ATOM   2924  O   ILE A 302      37.053  22.448   1.687  1.00126.14           O  
ATOM   2925  CB  ILE A 302      35.181  22.802   4.429  1.00111.37           C  
ATOM   2926  CG1 ILE A 302      35.157  23.643   5.711  1.00112.89           C  
ATOM   2927  CG2 ILE A 302      36.104  21.603   4.650  1.00106.79           C  
ATOM   2928  CD1 ILE A 302      34.421  23.011   6.876  1.00112.58           C  
ATOM   2929  N   ILE A 303      34.833  22.413   1.318  1.00127.73           N  
ATOM   2930  CA  ILE A 303      34.935  21.523   0.166  1.00127.48           C  
ATOM   2931  C   ILE A 303      35.702  22.164  -0.984  1.00128.00           C  
ATOM   2932  O   ILE A 303      36.592  21.532  -1.538  1.00139.74           O  
ATOM   2933  CB  ILE A 303      33.538  21.029  -0.272  1.00126.98           C  
ATOM   2934  CG1 ILE A 303      33.002  20.042   0.779  1.00123.29           C  
ATOM   2935  CG2 ILE A 303      33.570  20.395  -1.663  1.00124.43           C  
ATOM   2936  CD1 ILE A 303      31.488  19.992   0.888  1.00120.80           C  
ATOM   2937  N   ARG A 304      35.347  23.403  -1.311  1.00123.83           N  
ATOM   2938  CA  ARG A 304      35.983  24.140  -2.392  1.00124.70           C  
ATOM   2939  C   ARG A 304      37.444  24.480  -2.111  1.00121.28           C  
ATOM   2940  O   ARG A 304      38.277  24.422  -3.016  1.00130.14           O  
ATOM   2941  CB  ARG A 304      35.200  25.420  -2.696  1.00128.96           C  
ATOM   2942  CG  ARG A 304      33.839  25.179  -3.330  1.00133.12           C  
ATOM   2943  CD  ARG A 304      33.194  26.484  -3.766  1.00140.82           C  
ATOM   2944  NE  ARG A 304      31.843  26.282  -4.279  1.00153.24           N  
ATOM   2945  CZ  ARG A 304      30.993  27.266  -4.554  1.00164.47           C  
ATOM   2946  NH1 ARG A 304      31.353  28.528  -4.365  1.00165.64           N  
ATOM   2947  NH2 ARG A 304      29.782  26.989  -5.018  1.00171.36           N  
ATOM   2948  N   SER A 305      37.764  24.839  -0.870  1.00119.48           N  
ATOM   2949  CA  SER A 305      39.139  25.183  -0.560  1.00124.90           C  
ATOM   2950  C   SER A 305      39.948  23.917  -0.345  1.00133.37           C  
ATOM   2951  O   SER A 305      40.831  23.598  -1.129  1.00133.18           O  
ATOM   2952  CB  SER A 305      39.254  26.107   0.631  1.00125.91           C  
ATOM   2953  OG  SER A 305      40.609  26.224   1.002  1.00138.08           O  
ATOM   2954  N   HIS A 306      39.655  23.201   0.730  1.00144.74           N  
ATOM   2955  CA  HIS A 306      40.376  21.967   1.010  1.00141.65           C  
ATOM   2956  C   HIS A 306      39.894  20.757   0.238  1.00141.88           C  
ATOM   2957  O   HIS A 306      38.706  20.483   0.186  1.00122.28           O  
ATOM   2958  CB  HIS A 306      40.166  21.550   2.464  1.00139.93           C  
ATOM   2959  CG  HIS A 306      40.738  22.506   3.466  1.00144.41           C  
ATOM   2960  ND1 HIS A 306      40.076  23.639   3.883  1.00146.53           N  
ATOM   2961  CD2 HIS A 306      41.907  22.486   4.146  1.00147.04           C  
ATOM   2962  CE1 HIS A 306      40.815  24.280   4.769  1.00140.55           C  
ATOM   2963  NE2 HIS A 306      41.932  23.601   4.948  1.00142.85           N  
ATOM   2964  N   VAL A 307      40.805  20.045  -0.393  1.00158.72           N  
ATOM   2965  CA  VAL A 307      42.224  20.351  -0.356  1.00169.34           C  
ATOM   2966  C   VAL A 307      42.603  20.947  -1.717  1.00191.14           C  
ATOM   2967  O   VAL A 307      43.775  21.219  -1.986  1.00212.05           O  
ATOM   2968  CB  VAL A 307      42.969  19.016  -0.203  1.00155.91           C  
ATOM   2969  CG1 VAL A 307      44.467  19.246  -0.097  1.00150.14           C  
ATOM   2970  CG2 VAL A 307      42.440  18.248   0.995  1.00148.66           C  
ATOM   2971  N   LEU A 308      41.602  21.145  -2.568  1.00190.42           N  
ATOM   2972  CA  LEU A 308      41.824  21.706  -3.895  1.00171.47           C  
ATOM   2973  C   LEU A 308      42.899  22.787  -3.865  1.00160.70           C  
ATOM   2974  O   LEU A 308      42.614  23.952  -3.590  1.00155.87           O  
ATOM   2975  CB  LEU A 308      40.521  22.275  -4.462  1.00159.33           C  
ATOM   2976  CG  LEU A 308      39.641  21.302  -5.248  1.00149.70           C  
ATOM   2977  CD1 LEU A 308      38.722  20.532  -4.312  1.00139.13           C  
ATOM   2978  CD2 LEU A 308      38.838  22.040  -6.308  1.00141.35           C  
TER    2979      LEU A 308                                                      
HETATM 2980  C1  ZMA A1201      21.783 -13.679  15.960  1.00102.64           C  
HETATM 2981  C2  ZMA A1201      21.360 -15.003  15.990  1.00103.36           C  
HETATM 2982  C3  ZMA A1201      20.046 -15.320  15.666  1.00106.10           C  
HETATM 2983  O4  ZMA A1201      19.632 -16.618  15.695  1.00116.23           O  
HETATM 2984  C5  ZMA A1201      19.155 -14.314  15.311  1.00101.20           C  
HETATM 2985  C6  ZMA A1201      19.578 -12.990  15.282  1.00 97.89           C  
HETATM 2986  C7  ZMA A1201      20.892 -12.673  15.606  1.00 98.56           C  
HETATM 2987  C8  ZMA A1201      21.351 -11.233  15.574  1.00 95.18           C  
HETATM 2988  C9  ZMA A1201      22.296 -10.975  16.741  1.00 92.15           C  
HETATM 2989  N10 ZMA A1201      22.622  -9.569  16.875  1.00 84.33           N  
HETATM 2990  C11 ZMA A1201      21.724  -8.716  17.414  1.00 78.13           C  
HETATM 2991  N12 ZMA A1201      22.048  -7.416  17.619  1.00 76.20           N  
HETATM 2992  N13 ZMA A1201      20.482  -9.150  17.758  1.00 78.13           N  
HETATM 2993  C14 ZMA A1201      19.562  -8.309  18.302  1.00 82.10           C  
HETATM 2994  N15 ZMA A1201      18.330  -8.763  18.638  1.00 88.56           N  
HETATM 2995  N16 ZMA A1201      19.890  -7.028  18.501  1.00 78.84           N  
HETATM 2996  N17 ZMA A1201      19.075  -6.037  19.044  1.00 75.99           N  
HETATM 2997  C18 ZMA A1201      21.102  -6.611  18.163  1.00 78.02           C  
HETATM 2998  N19 ZMA A1201      21.180  -5.293  18.462  1.00 77.11           N  
HETATM 2999  C20 ZMA A1201      19.954  -5.011  18.978  1.00 76.69           C  
HETATM 3000  C21 ZMA A1201      19.598  -3.643  19.448  1.00 79.31           C  
HETATM 3001  C22 ZMA A1201      20.484  -2.589  19.407  1.00 79.23           C  
HETATM 3002  C23 ZMA A1201      19.749  -1.538  19.927  1.00 79.95           C  
HETATM 3003  C24 ZMA A1201      18.475  -1.989  20.256  1.00 82.28           C  
HETATM 3004  O25 ZMA A1201      18.372  -3.336  19.951  1.00 83.20           O  
HETATM 3005  C1  CLR A1202       2.894  -8.721  22.112  1.00137.14           C  
HETATM 3006  C2  CLR A1202       2.966 -10.242  22.072  1.00131.91           C  
HETATM 3007  C3  CLR A1202       2.027 -10.785  21.004  1.00128.06           C  
HETATM 3008  C4  CLR A1202       2.480 -10.283  19.639  1.00136.35           C  
HETATM 3009  C5  CLR A1202       2.608  -8.777  19.649  1.00143.26           C  
HETATM 3010  C6  CLR A1202       2.077  -8.088  18.621  1.00145.56           C  
HETATM 3011  C7  CLR A1202       2.034  -6.576  18.567  1.00143.29           C  
HETATM 3012  C8  CLR A1202       3.118  -5.978  19.450  1.00140.22           C  
HETATM 3013  C9  CLR A1202       3.061  -6.597  20.844  1.00142.45           C  
HETATM 3014  C10 CLR A1202       3.339  -8.099  20.792  1.00140.38           C  
HETATM 3015  C11 CLR A1202       3.992  -5.909  21.851  1.00144.21           C  
HETATM 3016  C12 CLR A1202       3.896  -4.382  21.842  1.00139.96           C  
HETATM 3017  C13 CLR A1202       4.093  -3.898  20.419  1.00135.03           C  
HETATM 3018  C14 CLR A1202       2.971  -4.472  19.585  1.00137.01           C  
HETATM 3019  C15 CLR A1202       2.963  -3.645  18.307  1.00131.87           C  
HETATM 3020  C16 CLR A1202       3.465  -2.267  18.744  1.00126.14           C  
HETATM 3021  C17 CLR A1202       3.951  -2.401  20.188  1.00126.30           C  
HETATM 3022  C18 CLR A1202       5.444  -4.390  19.899  1.00136.86           C  
HETATM 3023  C19 CLR A1202       4.832  -8.333  20.598  1.00137.98           C  
HETATM 3024  C20 CLR A1202       5.223  -1.602  20.451  1.00117.47           C  
HETATM 3025  C21 CLR A1202       5.644  -1.710  21.912  1.00117.71           C  
HETATM 3026  C22 CLR A1202       5.048  -0.145  20.039  1.00113.58           C  
HETATM 3027  C23 CLR A1202       6.250   0.691  20.464  1.00112.02           C  
HETATM 3028  C24 CLR A1202       6.379   1.940  19.600  1.00110.27           C  
HETATM 3029  C25 CLR A1202       5.981   3.187  20.381  1.00106.59           C  
HETATM 3030  C26 CLR A1202       5.930   4.408  19.471  1.00101.50           C  
HETATM 3031  C27 CLR A1202       4.650   2.982  21.095  1.00105.65           C  
HETATM 3032  O1  CLR A1202       2.060 -12.217  21.021  1.00120.67           O  
HETATM 3033  C1  CLR A1203       8.637 -10.899  14.132  1.00121.48           C  
HETATM 3034  C2  CLR A1203       8.794 -12.414  14.148  1.00122.83           C  
HETATM 3035  C3  CLR A1203       7.439 -13.085  13.975  1.00121.81           C  
HETATM 3036  C4  CLR A1203       6.865 -12.711  12.615  1.00119.96           C  
HETATM 3037  C5  CLR A1203       6.842 -11.208  12.449  1.00120.41           C  
HETATM 3038  C6  CLR A1203       5.719 -10.639  11.973  1.00125.02           C  
HETATM 3039  C7  CLR A1203       5.528  -9.142  11.860  1.00126.51           C  
HETATM 3040  C8  CLR A1203       6.873  -8.434  11.793  1.00128.29           C  
HETATM 3041  C9  CLR A1203       7.775  -8.910  12.928  1.00121.71           C  
HETATM 3042  C10 CLR A1203       8.077 -10.402  12.803  1.00119.11           C  
HETATM 3043  C11 CLR A1203       9.074  -8.102  13.049  1.00125.76           C  
HETATM 3044  C12 CLR A1203       8.870  -6.587  13.008  1.00130.61           C  
HETATM 3045  C13 CLR A1203       8.068  -6.246  11.767  1.00133.06           C  
HETATM 3046  C14 CLR A1203       6.723  -6.925  11.894  1.00134.83           C  
HETATM 3047  C15 CLR A1203       5.830  -6.232  10.875  1.00137.20           C  
HETATM 3048  C16 CLR A1203       6.381  -4.806  10.795  1.00135.54           C  
HETATM 3049  C17 CLR A1203       7.688  -4.783  11.588  1.00135.51           C  
HETATM 3050  C18 CLR A1203       8.805  -6.759  10.531  1.00131.13           C  
HETATM 3051  C19 CLR A1203       9.110 -10.621  11.703  1.00122.24           C  
HETATM 3052  C20 CLR A1203       8.763  -3.934  10.916  1.00139.23           C  
HETATM 3053  C21 CLR A1203      10.010  -3.842  11.787  1.00138.63           C  
HETATM 3054  C22 CLR A1203       8.230  -2.547  10.576  1.00136.82           C  
HETATM 3055  C23 CLR A1203       8.117  -1.684  11.827  1.00131.89           C  
HETATM 3056  C24 CLR A1203       7.140  -0.535  11.611  1.00128.73           C  
HETATM 3057  C25 CLR A1203       7.856   0.809  11.666  1.00129.69           C  
HETATM 3058  C26 CLR A1203       8.179   1.198  13.104  1.00124.16           C  
HETATM 3059  C27 CLR A1203       9.116   0.792  10.809  1.00132.70           C  
HETATM 3060  O1  CLR A1203       7.596 -14.506  14.053  1.00128.70           O  
HETATM 3061  C1  CLR A1204      39.510 -10.437  22.693  1.00165.10           C  
HETATM 3062  C2  CLR A1204      38.982 -11.861  22.813  1.00155.79           C  
HETATM 3063  C3  CLR A1204      38.833 -12.244  24.279  1.00154.95           C  
HETATM 3064  C4  CLR A1204      37.802 -11.331  24.931  1.00158.28           C  
HETATM 3065  C5  CLR A1204      38.163  -9.881  24.699  1.00163.56           C  
HETATM 3066  C6  CLR A1204      38.109  -9.038  25.748  1.00153.97           C  
HETATM 3067  C7  CLR A1204      38.551  -7.593  25.676  1.00150.19           C  
HETATM 3068  C8  CLR A1204      38.497  -7.086  24.243  1.00152.07           C  
HETATM 3069  C9  CLR A1204      39.226  -8.055  23.315  1.00157.33           C  
HETATM 3070  C10 CLR A1204      38.549  -9.424  23.305  1.00166.71           C  
HETATM 3071  C11 CLR A1204      39.387  -7.519  21.886  1.00149.12           C  
HETATM 3072  C12 CLR A1204      39.901  -6.081  21.816  1.00147.21           C  
HETATM 3073  C13 CLR A1204      39.012  -5.211  22.683  1.00147.70           C  
HETATM 3074  C14 CLR A1204      39.132  -5.713  24.104  1.00149.06           C  
HETATM 3075  C15 CLR A1204      38.583  -4.588  24.970  1.00148.55           C  
HETATM 3076  C16 CLR A1204      38.899  -3.314  24.184  1.00147.70           C  
HETATM 3077  C17 CLR A1204      39.413  -3.749  22.810  1.00147.17           C  
HETATM 3078  C18 CLR A1204      37.566  -5.327  22.201  1.00151.93           C  
HETATM 3079  C19 CLR A1204      37.278  -9.356  22.466  1.00175.66           C  
HETATM 3080  C20 CLR A1204      38.895  -2.857  21.686  1.00145.53           C  
HETATM 3081  C21 CLR A1204      39.273  -3.422  20.322  1.00144.38           C  
HETATM 3082  C22 CLR A1204      39.400  -1.428  21.844  1.00149.93           C  
HETATM 3083  C23 CLR A1204      39.058  -0.589  20.619  1.00152.63           C  
HETATM 3084  C24 CLR A1204      40.292   0.129  20.086  1.00155.69           C  
HETATM 3085  C25 CLR A1204      40.517   1.446  20.819  1.00150.41           C  
HETATM 3086  C26 CLR A1204      39.465   2.477  20.426  1.00146.48           C  
HETATM 3087  C27 CLR A1204      40.536   1.235  22.329  1.00147.60           C  
HETATM 3088  O1  CLR A1204      38.395 -13.604  24.376  1.00148.64           O  
HETATM 3089  C9  OLC A1205      35.799   6.929  22.533  1.00 97.62           C  
HETATM 3090  C8  OLC A1205      34.313   6.895  22.802  1.00100.60           C  
HETATM 3091  C24 OLC A1205      33.529  19.642  22.759  1.00142.62           C  
HETATM 3092  C7  OLC A1205      33.859   8.256  23.318  1.00107.07           C  
HETATM 3093  C6  OLC A1205      34.242   9.364  22.345  1.00110.67           C  
HETATM 3094  C5  OLC A1205      34.988  10.485  23.059  1.00111.49           C  
HETATM 3095  C4  OLC A1205      34.425  11.847  22.675  1.00108.31           C  
HETATM 3096  C3  OLC A1205      33.826  12.553  23.886  1.00111.34           C  
HETATM 3097  C2  OLC A1205      32.778  13.574  23.461  1.00116.75           C  
HETATM 3098  C21 OLC A1205      33.742  17.164  22.683  1.00138.80           C  
HETATM 3099  C1  OLC A1205      33.445  14.688  22.689  1.00122.96           C  
HETATM 3100  C22 OLC A1205      33.058  18.333  23.382  1.00143.16           C  
HETATM 3101  O19 OLC A1205      34.460  14.478  22.046  1.00121.38           O  
HETATM 3102  O25 OLC A1205      32.444  20.577  22.738  1.00134.94           O  
HETATM 3103  O23 OLC A1205      31.639  18.216  23.231  1.00142.72           O  
HETATM 3104  O20 OLC A1205      32.881  16.028  22.705  1.00130.81           O  
HETATM 3105  C10 OLC A1206      21.459  -0.534   0.976  1.00100.58           C  
HETATM 3106  C9  OLC A1206      21.238  -1.815   0.711  1.00101.69           C  
HETATM 3107  C11 OLC A1206      21.157   0.010   2.349  1.00 87.24           C  
HETATM 3108  C8  OLC A1206      20.690  -2.743   1.762  1.00102.34           C  
HETATM 3109  C24 OLC A1206      24.427 -14.216   6.873  1.00126.41           C  
HETATM 3110  C7  OLC A1206      20.804  -4.177   1.272  1.00103.75           C  
HETATM 3111  C6  OLC A1206      21.751  -4.976   2.152  1.00106.31           C  
HETATM 3112  C5  OLC A1206      21.022  -5.616   3.321  1.00104.56           C  
HETATM 3113  C4  OLC A1206      21.951  -6.509   4.120  1.00106.18           C  
HETATM 3114  C3  OLC A1206      21.514  -7.961   4.037  1.00106.20           C  
HETATM 3115  C2  OLC A1206      22.295  -8.772   5.053  1.00110.97           C  
HETATM 3116  C21 OLC A1206      23.141 -12.435   5.624  1.00133.60           C  
HETATM 3117  C1  OLC A1206      22.227 -10.247   4.770  1.00119.29           C  
HETATM 3118  C22 OLC A1206      23.398 -13.104   6.971  1.00134.54           C  
HETATM 3119  O19 OLC A1206      21.970 -10.654   3.661  1.00116.21           O  
HETATM 3120  O25 OLC A1206      25.315 -14.091   7.988  1.00112.38           O  
HETATM 3121  O23 OLC A1206      23.939 -12.142   7.868  1.00140.20           O  
HETATM 3122  O20 OLC A1206      22.466 -11.199   5.840  1.00131.62           O  
HETATM 3123  C1  OLA A1207      34.477 -10.288   1.823  1.00126.75           C  
HETATM 3124  O1  OLA A1207      34.757 -11.481   1.578  1.00120.36           O  
HETATM 3125  O2  OLA A1207      33.575  -9.950   2.620  1.00125.81           O  
HETATM 3126  C2  OLA A1207      35.263  -9.205   1.124  1.00131.30           C  
HETATM 3127  C3  OLA A1207      34.400  -7.957   0.988  1.00138.32           C  
HETATM 3128  C4  OLA A1207      35.094  -6.743   1.593  1.00141.47           C  
HETATM 3129  C5  OLA A1207      35.490  -5.745   0.512  1.00144.49           C  
HETATM 3130  C6  OLA A1207      35.422  -4.315   1.037  1.00247.22           C  
HETATM 3131  C7  OLA A1207      35.079  -3.339  -0.082  1.00194.11           C  
CONECT  538 1188                                                                
CONECT  554 1102                                                                
CONECT 1102  554                                                                
CONECT 1188  538                                                                
CONECT 2567 2588                                                                
CONECT 2588 2567                                                                
CONECT 2980 2981 2986                                                           
CONECT 2981 2980 2982                                                           
CONECT 2982 2981 2983 2984                                                      
CONECT 2983 2982                                                                
CONECT 2984 2982 2985                                                           
CONECT 2985 2984 2986                                                           
CONECT 2986 2980 2985 2987                                                      
CONECT 2987 2986 2988                                                           
CONECT 2988 2987 2989                                                           
CONECT 2989 2988 2990                                                           
CONECT 2990 2989 2991 2992                                                      
CONECT 2991 2990 2997                                                           
CONECT 2992 2990 2993                                                           
CONECT 2993 2992 2994 2995                                                      
CONECT 2994 2993                                                                
CONECT 2995 2993 2996 2997                                                      
CONECT 2996 2995 2999                                                           
CONECT 2997 2991 2995 2998                                                      
CONECT 2998 2997 2999                                                           
CONECT 2999 2996 2998 3000                                                      
CONECT 3000 2999 3001 3004                                                      
CONECT 3001 3000 3002                                                           
CONECT 3002 3001 3003                                                           
CONECT 3003 3002 3004                                                           
CONECT 3004 3000 3003                                                           
CONECT 3005 3006 3014                                                           
CONECT 3006 3005 3007                                                           
CONECT 3007 3006 3008 3032                                                      
CONECT 3008 3007 3009                                                           
CONECT 3009 3008 3010 3014                                                      
CONECT 3010 3009 3011                                                           
CONECT 3011 3010 3012                                                           
CONECT 3012 3011 3013 3018                                                      
CONECT 3013 3012 3014 3015                                                      
CONECT 3014 3005 3009 3013 3023                                                 
CONECT 3015 3013 3016                                                           
CONECT 3016 3015 3017                                                           
CONECT 3017 3016 3018 3021 3022                                                 
CONECT 3018 3012 3017 3019                                                      
CONECT 3019 3018 3020                                                           
CONECT 3020 3019 3021                                                           
CONECT 3021 3017 3020 3024                                                      
CONECT 3022 3017                                                                
CONECT 3023 3014                                                                
CONECT 3024 3021 3025 3026                                                      
CONECT 3025 3024                                                                
CONECT 3026 3024 3027                                                           
CONECT 3027 3026 3028                                                           
CONECT 3028 3027 3029                                                           
CONECT 3029 3028 3030 3031                                                      
CONECT 3030 3029                                                                
CONECT 3031 3029                                                                
CONECT 3032 3007                                                                
CONECT 3033 3034 3042                                                           
CONECT 3034 3033 3035                                                           
CONECT 3035 3034 3036 3060                                                      
CONECT 3036 3035 3037                                                           
CONECT 3037 3036 3038 3042                                                      
CONECT 3038 3037 3039                                                           
CONECT 3039 3038 3040                                                           
CONECT 3040 3039 3041 3046                                                      
CONECT 3041 3040 3042 3043                                                      
CONECT 3042 3033 3037 3041 3051                                                 
CONECT 3043 3041 3044                                                           
CONECT 3044 3043 3045                                                           
CONECT 3045 3044 3046 3049 3050                                                 
CONECT 3046 3040 3045 3047                                                      
CONECT 3047 3046 3048                                                           
CONECT 3048 3047 3049                                                           
CONECT 3049 3045 3048 3052                                                      
CONECT 3050 3045                                                                
CONECT 3051 3042                                                                
CONECT 3052 3049 3053 3054                                                      
CONECT 3053 3052                                                                
CONECT 3054 3052 3055                                                           
CONECT 3055 3054 3056                                                           
CONECT 3056 3055 3057                                                           
CONECT 3057 3056 3058 3059                                                      
CONECT 3058 3057                                                                
CONECT 3059 3057                                                                
CONECT 3060 3035                                                                
CONECT 3061 3062 3070                                                           
CONECT 3062 3061 3063                                                           
CONECT 3063 3062 3064 3088                                                      
CONECT 3064 3063 3065                                                           
CONECT 3065 3064 3066 3070                                                      
CONECT 3066 3065 3067                                                           
CONECT 3067 3066 3068                                                           
CONECT 3068 3067 3069 3074                                                      
CONECT 3069 3068 3070 3071                                                      
CONECT 3070 3061 3065 3069 3079                                                 
CONECT 3071 3069 3072                                                           
CONECT 3072 3071 3073                                                           
CONECT 3073 3072 3074 3077 3078                                                 
CONECT 3074 3068 3073 3075                                                      
CONECT 3075 3074 3076                                                           
CONECT 3076 3075 3077                                                           
CONECT 3077 3073 3076 3080                                                      
CONECT 3078 3073                                                                
CONECT 3079 3070                                                                
CONECT 3080 3077 3081 3082                                                      
CONECT 3081 3080                                                                
CONECT 3082 3080 3083                                                           
CONECT 3083 3082 3084                                                           
CONECT 3084 3083 3085                                                           
CONECT 3085 3084 3086 3087                                                      
CONECT 3086 3085                                                                
CONECT 3087 3085                                                                
CONECT 3088 3063                                                                
CONECT 3089 3090                                                                
CONECT 3090 3089 3092                                                           
CONECT 3091 3100 3102                                                           
CONECT 3092 3090 3093                                                           
CONECT 3093 3092 3094                                                           
CONECT 3094 3093 3095                                                           
CONECT 3095 3094 3096                                                           
CONECT 3096 3095 3097                                                           
CONECT 3097 3096 3099                                                           
CONECT 3098 3100 3104                                                           
CONECT 3099 3097 3101 3104                                                      
CONECT 3100 3091 3098 3103                                                      
CONECT 3101 3099                                                                
CONECT 3102 3091                                                                
CONECT 3103 3100                                                                
CONECT 3104 3098 3099                                                           
CONECT 3105 3106 3107                                                           
CONECT 3106 3105 3108                                                           
CONECT 3107 3105                                                                
CONECT 3108 3106 3110                                                           
CONECT 3109 3118 3120                                                           
CONECT 3110 3108 3111                                                           
CONECT 3111 3110 3112                                                           
CONECT 3112 3111 3113                                                           
CONECT 3113 3112 3114                                                           
CONECT 3114 3113 3115                                                           
CONECT 3115 3114 3117                                                           
CONECT 3116 3118 3122                                                           
CONECT 3117 3115 3119 3122                                                      
CONECT 3118 3109 3116 3121                                                      
CONECT 3119 3117                                                                
CONECT 3120 3109                                                                
CONECT 3121 3118                                                                
CONECT 3122 3116 3117                                                           
CONECT 3123 3124 3125 3126                                                      
CONECT 3124 3123                                                                
CONECT 3125 3123                                                                
CONECT 3126 3123 3127                                                           
CONECT 3127 3126 3128                                                           
CONECT 3128 3127 3129                                                           
CONECT 3129 3128 3130                                                           
CONECT 3130 3129 3131                                                           
CONECT 3131 3130                                                                
MASTER      453    0    7   19    0    0   10    6 3130    1  158   35          
END