HEADER    VIRUS                                   12-FEB-19   6NZ0              
TITLE     CRYO-EM STRUCTURE OF AAV-2 IN COMPLEX WITH AAVR PKD DOMAINS 1 AND 2   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYSLEXIA-ASSOCIATED PROTEIN KIAA0319-LIKE PROTEIN;         
COMPND   3 CHAIN: Z;                                                            
COMPND   4 FRAGMENT: RESIDUES 311-597;                                          
COMPND   5 SYNONYM: ADENO-ASSOCIATED VIRUS RECEPTOR,AAVR;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAPSID PROTEIN VP1;                                        
COMPND   9 CHAIN: A;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KIAA0319L, AAVR, KIAA1837, PP791;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: NEBEXPRESS;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-11A;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ADENO-ASSOCIATED VIRUS - 2;                     
SOURCE  12 ORGANISM_COMMON: ISOLATE SRIVASTAVA/1982;                            
SOURCE  13 ORGANISM_TAXID: 648242;                                              
SOURCE  14 GENE: VP1;                                                           
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PBAC2                                      
KEYWDS    AAV, AAVR, RECEPTOR, CORECEPTOR, VIRUS, KIAA0319L, PKD, PARVOVIRUS    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    N.L.MEYER,Q.XIE,O.DAVULCU,C.YOSHIOKA,M.S.CHAPMAN                      
REVDAT   3   18-DEC-19 6NZ0    1       CRYST1 SCALE                             
REVDAT   2   19-JUN-19 6NZ0    1       JRNL                                     
REVDAT   1   12-JUN-19 6NZ0    0                                                
JRNL        AUTH   N.L.MEYER,G.HU,O.DAVULCU,Q.XIE,A.J.NOBLE,C.YOSHIOKA,         
JRNL        AUTH 2 D.S.GINGERICH,A.TRZYNKA,L.DAVID,S.M.STAGG,M.S.CHAPMAN        
JRNL        TITL   STRUCTURE OF THE GENE THERAPY VECTOR, ADENO-ASSOCIATED VIRUS 
JRNL        TITL 2 WITH ITS CELL RECEPTOR, AAVR.                                
JRNL        REF    ELIFE                         V.   8       2019              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   31115336                                                     
JRNL        DOI    10.7554/ELIFE.44707                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, SERIALEM, GCTF, COOT, RELION,     
REMARK   3                            RELION, RELION, RELION, RSREF             
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1LP3                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : MAP VALUES AT GRID POINTS WITHIN    
REMARK   3                                  2 ANGSTROM OF ATOMS                 
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : AN INITIAL MODEL FOR AAVR WAS CONSTRUCTED BY     
REMARK   3  HOMOLOGY MODELING USING MODELLER 9.2. AFTER REMODELING AAVR AND     
REMARK   3  THE CRYSTAL STRUCTURE OF AAV2, THE STRUCTURE WAS REFINED USING      
REMARK   3  RSREF EMBEDDED IN CNS FOR STEREOCHEMICALLY RESTRAINED TORSION       
REMARK   3  ANGLE SIMULATED ANNEALING AND GRADIENT DESCENT OPTIMIZATION.        
REMARK   3  STAND-ALONE RSREF WAS USED FOR REFINEMENT OF EM ENVELOPE            
REMARK   3  CORRECTIONS, RESOLUTION ESTIMATES, AND RESTRAINED ATOMIC B-         
REMARK   3  FACTORS.                                                            
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 2.400                          
REMARK   3   NUMBER OF PARTICLES               : 21373                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6NZ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238684.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : ADENO-ASSOCIATED VIRUS - 2;       
REMARK 245                                    BINARY COMPLEX OF AAV-2 WITH A    
REMARK 245                                    FRAGMENT OF ITS CELLULAR          
REMARK 245                                    RECEPTOR, AAVR OR DYSLEXIA-       
REMARK 245                                    ASSOCIATED PROTEIN KIAA0319-      
REMARK 245                                    LIKE PROTEIN.                     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.10                              
REMARK 245   SAMPLE SUPPORT DETAILS         : GLOW DISCHARGE SETTINGS: PELCO    
REMARK 245                                    EASIGLOW, 25S, 25MA, 0.39MBAR,    
REMARK 245                                    NEGATIVE POLARITY GRID: TED       
REMARK 245                                    PELLA CAT#01824, ULTRATHIN        
REMARK 245                                    CARBON FILM (<3NM) ON LACEY       
REMARK 245                                    CARBON SUPPORT FILM               
REMARK 245   SAMPLE VITRIFICATION DETAILS   : 4UL OF AAV-2 (1.7UM) WAS ADDED    
REMARK 245                                    TO THE GRID, FOLLOWED BY 4UL OF   
REMARK 245                                    AAVR-PKD1-2 (16.7UM), WITH        
REMARK 245                                    MANUAL BLOTTING AFTER EACH        
REMARK 245                                    ADDITION WITH WHATMAN PAPER       
REMARK 245                                    (CAT. NO. 1001-110.) 4UL OF       
REMARK 245                                    BUFFER CONTAINING 25MM HEPES,     
REMARK 245                                    150MM NACL, PH 7.4 WAS ADDED TO   
REMARK 245                                    THE GRID BEFORE FINAL BLOTTING    
REMARK 245                                    AND PLUNGE-FREEZING IN THE        
REMARK 245                                    VITROBOT (BLOT TIME 1.5SEC,       
REMARK 245                                    BLOT FORCE -1).                   
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : AAV-2 VIRUS-LIKE PARTICLES        
REMARK 245  EXPRESSED IN SF9 CELLS USING INVITROGEN'S BAC-TO-BAC EXPRESSION     
REMARK 245  SYSTEM; EXPRESSED N-TERMINALLY HIS6-TAGGED FRAGMENT OF AAVR         
REMARK 245  CONTAINING THE PKD1 AND PKD2 DOMAINS.                               
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2329                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON III (4K X 4K)       
REMARK 245   MINIMUM DEFOCUS (NM)              : -800.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : -2000.00                       
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 25.40                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 75000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).                 
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 APPLY THE FOLLOWING TO CHAINS: Z, 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 350   BIOMT1   2  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2   2  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3   2  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   3 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2   3  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3   3  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   4 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2   4 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3   4  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2   5 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   5  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   7 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   7 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   7  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   8  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2   8 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3   8  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   9  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2   9  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3   9  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  10 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  10  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  10  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  11  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  11  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  12  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  12 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  12 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  13 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  13 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  13 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  14 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  14  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  14 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  15  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  15  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  15 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  16 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  16  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  16  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  17 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  17  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  17 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  18  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  18  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  18 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  19  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  19 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  19 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  20 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  20 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  20 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  21  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  21  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  21  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  22 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  22 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  22  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  23 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  23 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  23 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  24  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  24 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  24 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  25  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  25 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  25  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  26  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  26  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  26 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  27  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  27 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  27 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  28  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  28 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  28  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  29 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  29 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  29  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  30 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  30 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  30 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  31  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  31  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  31  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  32  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  32  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  32  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  33  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  33  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  33 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  34 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  34  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  34 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  35 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  35  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  35  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  36  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  36  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  36 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  37 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  37  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  37 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  38 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  38  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  38  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  39  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  39  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  39  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  40  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  40  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  40 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  41  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  41 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  41  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  42  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  42 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  42 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  43  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  43  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  43 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  44  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  44  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  44  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  45  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  45 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  45  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  46  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  46  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  46  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  47  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  47  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  47  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  48  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  48 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  48  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  49  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  49 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  49 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  50  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  50  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  50 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  51  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  51 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  51  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  52 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  52 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  52  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  53 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  53  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  53  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  54 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  54  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  54 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  55 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  55 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  55 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  56  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  56  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  56  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  57 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  57  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  57 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  58 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  58 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  58 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  59 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  59 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  59  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  60 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  60  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  60  0.809017 -0.309017 -0.500000        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 Z   308                                                      
REMARK 465     ALA Z   309                                                      
REMARK 465     SER Z   310                                                      
REMARK 465     VAL Z   311                                                      
REMARK 465     SER Z   312                                                      
REMARK 465     ALA Z   313                                                      
REMARK 465     GLY Z   314                                                      
REMARK 465     GLU Z   315                                                      
REMARK 465     SER Z   316                                                      
REMARK 465     VAL Z   317                                                      
REMARK 465     GLN Z   318                                                      
REMARK 465     ILE Z   319                                                      
REMARK 465     THR Z   320                                                      
REMARK 465     LEU Z   321                                                      
REMARK 465     PRO Z   322                                                      
REMARK 465     LYS Z   323                                                      
REMARK 465     ASN Z   324                                                      
REMARK 465     GLU Z   325                                                      
REMARK 465     VAL Z   326                                                      
REMARK 465     GLN Z   327                                                      
REMARK 465     LEU Z   328                                                      
REMARK 465     ASN Z   329                                                      
REMARK 465     ALA Z   330                                                      
REMARK 465     TYR Z   331                                                      
REMARK 465     VAL Z   332                                                      
REMARK 465     LEU Z   333                                                      
REMARK 465     GLN Z   334                                                      
REMARK 465     GLU Z   335                                                      
REMARK 465     PRO Z   336                                                      
REMARK 465     PRO Z   337                                                      
REMARK 465     LYS Z   338                                                      
REMARK 465     GLY Z   339                                                      
REMARK 465     GLU Z   340                                                      
REMARK 465     THR Z   341                                                      
REMARK 465     TYR Z   342                                                      
REMARK 465     THR Z   343                                                      
REMARK 465     TYR Z   344                                                      
REMARK 465     ASP Z   345                                                      
REMARK 465     TRP Z   346                                                      
REMARK 465     GLN Z   347                                                      
REMARK 465     LEU Z   348                                                      
REMARK 465     ILE Z   349                                                      
REMARK 465     THR Z   350                                                      
REMARK 465     HIS Z   351                                                      
REMARK 465     PRO Z   352                                                      
REMARK 465     ARG Z   353                                                      
REMARK 465     ASP Z   354                                                      
REMARK 465     TYR Z   355                                                      
REMARK 465     SER Z   356                                                      
REMARK 465     GLY Z   357                                                      
REMARK 465     GLU Z   358                                                      
REMARK 465     MET Z   359                                                      
REMARK 465     GLU Z   360                                                      
REMARK 465     GLY Z   361                                                      
REMARK 465     LYS Z   362                                                      
REMARK 465     HIS Z   363                                                      
REMARK 465     SER Z   364                                                      
REMARK 465     GLN Z   365                                                      
REMARK 465     ILE Z   366                                                      
REMARK 465     LEU Z   367                                                      
REMARK 465     LYS Z   368                                                      
REMARK 465     LEU Z   369                                                      
REMARK 465     SER Z   370                                                      
REMARK 465     LYS Z   371                                                      
REMARK 465     LEU Z   372                                                      
REMARK 465     THR Z   373                                                      
REMARK 465     PRO Z   374                                                      
REMARK 465     GLY Z   375                                                      
REMARK 465     LEU Z   376                                                      
REMARK 465     TYR Z   377                                                      
REMARK 465     GLU Z   378                                                      
REMARK 465     PHE Z   379                                                      
REMARK 465     LYS Z   380                                                      
REMARK 465     VAL Z   381                                                      
REMARK 465     ILE Z   382                                                      
REMARK 465     VAL Z   383                                                      
REMARK 465     GLU Z   384                                                      
REMARK 465     GLY Z   385                                                      
REMARK 465     GLN Z   386                                                      
REMARK 465     ASN Z   387                                                      
REMARK 465     ALA Z   388                                                      
REMARK 465     HIS Z   389                                                      
REMARK 465     GLY Z   390                                                      
REMARK 465     GLU Z   391                                                      
REMARK 465     GLY Z   392                                                      
REMARK 465     TYR Z   393                                                      
REMARK 465     VAL Z   394                                                      
REMARK 465     ASN Z   395                                                      
REMARK 465     VAL Z   396                                                      
REMARK 465     THR Z   397                                                      
REMARK 465     VAL Z   398                                                      
REMARK 465     LYS Z   399                                                      
REMARK 465     PRO Z   400                                                      
REMARK 465     GLU Z   401                                                      
REMARK 465     PRO Z   402                                                      
REMARK 465     ARG Z   403                                                      
REMARK 465     LYS Z   404                                                      
REMARK 465     ASP Z   500                                                      
REMARK 465     TYR Z   501                                                      
REMARK 465     PRO Z   502                                                      
REMARK 465     PRO Z   503                                                      
REMARK 465     VAL Z   504                                                      
REMARK 465     ALA Z   505                                                      
REMARK 465     ASN Z   506                                                      
REMARK 465     ALA Z   507                                                      
REMARK 465     GLY Z   508                                                      
REMARK 465     PRO Z   509                                                      
REMARK 465     ASN Z   510                                                      
REMARK 465     GLN Z   511                                                      
REMARK 465     VAL Z   512                                                      
REMARK 465     ILE Z   513                                                      
REMARK 465     THR Z   514                                                      
REMARK 465     LEU Z   515                                                      
REMARK 465     PRO Z   516                                                      
REMARK 465     GLN Z   517                                                      
REMARK 465     ASN Z   518                                                      
REMARK 465     SER Z   519                                                      
REMARK 465     ILE Z   520                                                      
REMARK 465     THR Z   521                                                      
REMARK 465     LEU Z   522                                                      
REMARK 465     PHE Z   523                                                      
REMARK 465     GLY Z   524                                                      
REMARK 465     ASN Z   525                                                      
REMARK 465     GLN Z   526                                                      
REMARK 465     SER Z   527                                                      
REMARK 465     THR Z   528                                                      
REMARK 465     ASP Z   529                                                      
REMARK 465     ASP Z   530                                                      
REMARK 465     HIS Z   531                                                      
REMARK 465     GLY Z   532                                                      
REMARK 465     ILE Z   533                                                      
REMARK 465     THR Z   534                                                      
REMARK 465     SER Z   535                                                      
REMARK 465     TYR Z   536                                                      
REMARK 465     GLU Z   537                                                      
REMARK 465     TRP Z   538                                                      
REMARK 465     SER Z   539                                                      
REMARK 465     LEU Z   540                                                      
REMARK 465     SER Z   541                                                      
REMARK 465     PRO Z   542                                                      
REMARK 465     SER Z   543                                                      
REMARK 465     SER Z   544                                                      
REMARK 465     LYS Z   545                                                      
REMARK 465     GLY Z   546                                                      
REMARK 465     LYS Z   547                                                      
REMARK 465     VAL Z   548                                                      
REMARK 465     VAL Z   549                                                      
REMARK 465     GLU Z   550                                                      
REMARK 465     MET Z   551                                                      
REMARK 465     GLN Z   552                                                      
REMARK 465     GLY Z   553                                                      
REMARK 465     VAL Z   554                                                      
REMARK 465     ARG Z   555                                                      
REMARK 465     THR Z   556                                                      
REMARK 465     PRO Z   557                                                      
REMARK 465     THR Z   558                                                      
REMARK 465     LEU Z   559                                                      
REMARK 465     GLN Z   560                                                      
REMARK 465     LEU Z   561                                                      
REMARK 465     SER Z   562                                                      
REMARK 465     ALA Z   563                                                      
REMARK 465     MET Z   564                                                      
REMARK 465     GLN Z   565                                                      
REMARK 465     GLU Z   566                                                      
REMARK 465     GLY Z   567                                                      
REMARK 465     ASP Z   568                                                      
REMARK 465     TYR Z   569                                                      
REMARK 465     THR Z   570                                                      
REMARK 465     TYR Z   571                                                      
REMARK 465     GLN Z   572                                                      
REMARK 465     LEU Z   573                                                      
REMARK 465     THR Z   574                                                      
REMARK 465     VAL Z   575                                                      
REMARK 465     THR Z   576                                                      
REMARK 465     ASP Z   577                                                      
REMARK 465     THR Z   578                                                      
REMARK 465     ILE Z   579                                                      
REMARK 465     GLY Z   580                                                      
REMARK 465     GLN Z   581                                                      
REMARK 465     GLN Z   582                                                      
REMARK 465     ALA Z   583                                                      
REMARK 465     THR Z   584                                                      
REMARK 465     ALA Z   585                                                      
REMARK 465     GLN Z   586                                                      
REMARK 465     VAL Z   587                                                      
REMARK 465     THR Z   588                                                      
REMARK 465     VAL Z   589                                                      
REMARK 465     ILE Z   590                                                      
REMARK 465     VAL Z   591                                                      
REMARK 465     GLN Z   592                                                      
REMARK 465     PRO Z   593                                                      
REMARK 465     GLU Z   594                                                      
REMARK 465     ASN Z   595                                                      
REMARK 465     ASN Z   596                                                      
REMARK 465     LYS Z   597                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     TRP A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     GLN A    21                                                      
REMARK 465     TRP A    22                                                      
REMARK 465     TRP A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     GLU A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     LYS A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     ARG A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     VAL A    46                                                      
REMARK 465     LEU A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     GLY A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     LYS A    51                                                      
REMARK 465     TYR A    52                                                      
REMARK 465     LEU A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     PHE A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     LYS A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     VAL A    65                                                      
REMARK 465     ASN A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     ALA A    72                                                      
REMARK 465     LEU A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     HIS A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     TYR A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     GLN A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     ASP A    84                                                      
REMARK 465     SER A    85                                                      
REMARK 465     GLY A    86                                                      
REMARK 465     ASP A    87                                                      
REMARK 465     ASN A    88                                                      
REMARK 465     PRO A    89                                                      
REMARK 465     TYR A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     LYS A    92                                                      
REMARK 465     TYR A    93                                                      
REMARK 465     ASN A    94                                                      
REMARK 465     HIS A    95                                                      
REMARK 465     ALA A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     ALA A    98                                                      
REMARK 465     GLU A    99                                                      
REMARK 465     PHE A   100                                                      
REMARK 465     GLN A   101                                                      
REMARK 465     GLU A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     LYS A   105                                                      
REMARK 465     GLU A   106                                                      
REMARK 465     ASP A   107                                                      
REMARK 465     THR A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     PHE A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     GLY A   115                                                      
REMARK 465     ARG A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     VAL A   118                                                      
REMARK 465     PHE A   119                                                      
REMARK 465     GLN A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     LYS A   122                                                      
REMARK 465     LYS A   123                                                      
REMARK 465     ARG A   124                                                      
REMARK 465     VAL A   125                                                      
REMARK 465     LEU A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     PRO A   128                                                      
REMARK 465     LEU A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     VAL A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     PRO A   135                                                      
REMARK 465     VAL A   136                                                      
REMARK 465     LYS A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     ALA A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     GLY A   141                                                      
REMARK 465     LYS A   142                                                      
REMARK 465     LYS A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     PRO A   145                                                      
REMARK 465     VAL A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     HIS A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     VAL A   151                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     PRO A   153                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     SER A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     LYS A   161                                                      
REMARK 465     ALA A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     GLN A   165                                                      
REMARK 465     PRO A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     ARG A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     ASN A   172                                                      
REMARK 465     PHE A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     GLN A   175                                                      
REMARK 465     THR A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     ASP A   178                                                      
REMARK 465     ALA A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     VAL A   182                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     ASP A   184                                                      
REMARK 465     PRO A   185                                                      
REMARK 465     GLN A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     LEU A   188                                                      
REMARK 465     GLY A   189                                                      
REMARK 465     GLN A   190                                                      
REMARK 465     PRO A   191                                                      
REMARK 465     PRO A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     THR A   200                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     THR A   202                                                      
REMARK 465     MET A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     ALA A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     MET A   211                                                      
REMARK 465     ALA A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ASN A   214                                                      
REMARK 465     ASN A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     GLY A   220                                                      
REMARK 465     VAL A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ASN A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     SER A   225                                                      
REMARK 465     GLY A   226                                                      
REMARK 465     ASN A   227                                                      
REMARK 465     TRP A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     CYS A   230                                                      
REMARK 465     ASP A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     TRP A   234                                                      
REMARK 465     MET A   235                                                      
REMARK 465     GLY A   236                                                      
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     LEU A 735    O                                                   
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    CYS A 361   CA  -  CB  -  SG  ANGL. DEV. =   8.8 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    ASP Z 437     -155.54    -93.85                                   
REMARK 500    LEU Z 451      105.45    -59.37                                   
REMARK 500    GLU Z 454       88.35    -65.66                                   
REMARK 500    ILE Z 456      -60.10   -102.15                                   
REMARK 500    SER Z 457       57.06     37.46                                   
REMARK 500    ASN A 253        8.18     59.95                                   
REMARK 500    HIS A 255       -1.23     81.20                                   
REMARK 500    GLN A 263        8.92    -52.82                                   
REMARK 500    ASN A 285       54.17    -95.27                                   
REMARK 500    THR A 379     -165.49   -128.61                                   
REMARK 500    ARG A 432       41.14   -140.16                                   
REMARK 500    ARG A 459      117.93   -162.43                                   
REMARK 500    ASN A 518      112.79   -164.44                                   
REMARK 500    GLU A 530       46.37   -141.34                                   
REMARK 500    GLU A 562       49.26   -100.64                                   
REMARK 500    THR A 568      -31.81   -135.13                                   
REMARK 500    HIS A 629       73.61     43.00                                   
REMARK 500    ASN A 656      108.78    -53.63                                   
REMARK 500    ASN A 690       49.41   -144.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 508         0.07    SIDE CHAIN                              
REMARK 500    TYR A 700         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Z 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG Z 406   O                                                      
REMARK 620 2 ASP Z 435   OD2 124.1                                              
REMARK 620 3 ASP Z 436   OD1  62.7  93.9                                        
REMARK 620 4 ASP Z 481   OD1 130.5  76.8 166.7                                  
REMARK 620 5 ASP Z 481   OD2  82.4  95.1 142.5  49.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-0553   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF AAV-2 IN COMPLEX WITH AAVR PKD DOMAINS 1 AND 2  
REMARK 900 RELATED ID: EMD-0621   RELATED DB: EMDB                              
REMARK 900 CRYO-ELECTRON TOMOGRAPHY OF AAV-2 COMPLEXED WITH MBP FUSION          
REMARK 900 CONSTRUCT OF AAVR PKD DOMAINS 1-5, CLASS 1                           
REMARK 900 RELATED ID: EMD-0622   RELATED DB: EMDB                              
REMARK 900 CRYO-ELECTRON TOMOGRAPHY OF AAV-2 COMPLEXED WITH MBP FUSION          
REMARK 900 CONSTRUCT OF AAVR PKD DOMAINS 1-5, CLASS 2                           
REMARK 900 RELATED ID: EMD-0623   RELATED DB: EMDB                              
REMARK 900 CRYO-ELECTRON TOMOGRAPHY OF AAV-2 COMPLEXED WITH MBP FUSION          
REMARK 900 CONSTRUCT OF AAVR PKD DOMAINS 1-5, CLASS 3                           
REMARK 900 RELATED ID: EMD-0624   RELATED DB: EMDB                              
REMARK 900 CRYO-ELECTRON TOMOGRAPHY OF AAV-2 COMPLEXED WITH MBP FUSION          
REMARK 900 CONSTRUCT OF AAVR PKD DOMAINS 1-5, CLASS 4                           
DBREF  6NZ0 Z  311   597  UNP    Q8IZA0   K319L_HUMAN    311    597             
DBREF  6NZ0 A    1   735  UNP    P03135   CAPSD_AAV2S      1    735             
SEQADV 6NZ0 MET Z  308  UNP  Q8IZA0              INITIATING METHIONINE          
SEQADV 6NZ0 ALA Z  309  UNP  Q8IZA0              EXPRESSION TAG                 
SEQADV 6NZ0 SER Z  310  UNP  Q8IZA0              EXPRESSION TAG                 
SEQADV 6NZ0 CYS A  388  UNP  P03135    GLY   388 CONFLICT                       
SEQRES   1 Z  290  MET ALA SER VAL SER ALA GLY GLU SER VAL GLN ILE THR          
SEQRES   2 Z  290  LEU PRO LYS ASN GLU VAL GLN LEU ASN ALA TYR VAL LEU          
SEQRES   3 Z  290  GLN GLU PRO PRO LYS GLY GLU THR TYR THR TYR ASP TRP          
SEQRES   4 Z  290  GLN LEU ILE THR HIS PRO ARG ASP TYR SER GLY GLU MET          
SEQRES   5 Z  290  GLU GLY LYS HIS SER GLN ILE LEU LYS LEU SER LYS LEU          
SEQRES   6 Z  290  THR PRO GLY LEU TYR GLU PHE LYS VAL ILE VAL GLU GLY          
SEQRES   7 Z  290  GLN ASN ALA HIS GLY GLU GLY TYR VAL ASN VAL THR VAL          
SEQRES   8 Z  290  LYS PRO GLU PRO ARG LYS ASN ARG PRO PRO ILE ALA ILE          
SEQRES   9 Z  290  VAL SER PRO GLN PHE GLN GLU ILE SER LEU PRO THR THR          
SEQRES  10 Z  290  SER THR VAL ILE ASP GLY SER GLN SER THR ASP ASP ASP          
SEQRES  11 Z  290  LYS ILE VAL GLN TYR HIS TRP GLU GLU LEU LYS GLY PRO          
SEQRES  12 Z  290  LEU ARG GLU GLU LYS ILE SER GLU ASP THR ALA ILE LEU          
SEQRES  13 Z  290  LYS LEU SER LYS LEU VAL PRO GLY ASN TYR THR PHE SER          
SEQRES  14 Z  290  LEU THR VAL VAL ASP SER ASP GLY ALA THR ASN SER THR          
SEQRES  15 Z  290  THR ALA ASN LEU THR VAL ASN LYS ALA VAL ASP TYR PRO          
SEQRES  16 Z  290  PRO VAL ALA ASN ALA GLY PRO ASN GLN VAL ILE THR LEU          
SEQRES  17 Z  290  PRO GLN ASN SER ILE THR LEU PHE GLY ASN GLN SER THR          
SEQRES  18 Z  290  ASP ASP HIS GLY ILE THR SER TYR GLU TRP SER LEU SER          
SEQRES  19 Z  290  PRO SER SER LYS GLY LYS VAL VAL GLU MET GLN GLY VAL          
SEQRES  20 Z  290  ARG THR PRO THR LEU GLN LEU SER ALA MET GLN GLU GLY          
SEQRES  21 Z  290  ASP TYR THR TYR GLN LEU THR VAL THR ASP THR ILE GLY          
SEQRES  22 Z  290  GLN GLN ALA THR ALA GLN VAL THR VAL ILE VAL GLN PRO          
SEQRES  23 Z  290  GLU ASN ASN LYS                                              
SEQRES   1 A  735  MET ALA ALA ASP GLY TYR LEU PRO ASP TRP LEU GLU ASP          
SEQRES   2 A  735  THR LEU SER GLU GLY ILE ARG GLN TRP TRP LYS LEU LYS          
SEQRES   3 A  735  PRO GLY PRO PRO PRO PRO LYS PRO ALA GLU ARG HIS LYS          
SEQRES   4 A  735  ASP ASP SER ARG GLY LEU VAL LEU PRO GLY TYR LYS TYR          
SEQRES   5 A  735  LEU GLY PRO PHE ASN GLY LEU ASP LYS GLY GLU PRO VAL          
SEQRES   6 A  735  ASN GLU ALA ASP ALA ALA ALA LEU GLU HIS ASP LYS ALA          
SEQRES   7 A  735  TYR ASP ARG GLN LEU ASP SER GLY ASP ASN PRO TYR LEU          
SEQRES   8 A  735  LYS TYR ASN HIS ALA ASP ALA GLU PHE GLN GLU ARG LEU          
SEQRES   9 A  735  LYS GLU ASP THR SER PHE GLY GLY ASN LEU GLY ARG ALA          
SEQRES  10 A  735  VAL PHE GLN ALA LYS LYS ARG VAL LEU GLU PRO LEU GLY          
SEQRES  11 A  735  LEU VAL GLU GLU PRO VAL LYS THR ALA PRO GLY LYS LYS          
SEQRES  12 A  735  ARG PRO VAL GLU HIS SER PRO VAL GLU PRO ASP SER SER          
SEQRES  13 A  735  SER GLY THR GLY LYS ALA GLY GLN GLN PRO ALA ARG LYS          
SEQRES  14 A  735  ARG LEU ASN PHE GLY GLN THR GLY ASP ALA ASP SER VAL          
SEQRES  15 A  735  PRO ASP PRO GLN PRO LEU GLY GLN PRO PRO ALA ALA PRO          
SEQRES  16 A  735  SER GLY LEU GLY THR ASN THR MET ALA THR GLY SER GLY          
SEQRES  17 A  735  ALA PRO MET ALA ASP ASN ASN GLU GLY ALA ASP GLY VAL          
SEQRES  18 A  735  GLY ASN SER SER GLY ASN TRP HIS CYS ASP SER THR TRP          
SEQRES  19 A  735  MET GLY ASP ARG VAL ILE THR THR SER THR ARG THR TRP          
SEQRES  20 A  735  ALA LEU PRO THR TYR ASN ASN HIS LEU TYR LYS GLN ILE          
SEQRES  21 A  735  SER SER GLN SER GLY ALA SER ASN ASP ASN HIS TYR PHE          
SEQRES  22 A  735  GLY TYR SER THR PRO TRP GLY TYR PHE ASP PHE ASN ARG          
SEQRES  23 A  735  PHE HIS CYS HIS PHE SER PRO ARG ASP TRP GLN ARG LEU          
SEQRES  24 A  735  ILE ASN ASN ASN TRP GLY PHE ARG PRO LYS ARG LEU ASN          
SEQRES  25 A  735  PHE LYS LEU PHE ASN ILE GLN VAL LYS GLU VAL THR GLN          
SEQRES  26 A  735  ASN ASP GLY THR THR THR ILE ALA ASN ASN LEU THR SER          
SEQRES  27 A  735  THR VAL GLN VAL PHE THR ASP SER GLU TYR GLN LEU PRO          
SEQRES  28 A  735  TYR VAL LEU GLY SER ALA HIS GLN GLY CYS LEU PRO PRO          
SEQRES  29 A  735  PHE PRO ALA ASP VAL PHE MET VAL PRO GLN TYR GLY TYR          
SEQRES  30 A  735  LEU THR LEU ASN ASN GLY SER GLN ALA VAL CYS ARG SER          
SEQRES  31 A  735  SER PHE TYR CYS LEU GLU TYR PHE PRO SER GLN MET LEU          
SEQRES  32 A  735  ARG THR GLY ASN ASN PHE THR PHE SER TYR THR PHE GLU          
SEQRES  33 A  735  ASP VAL PRO PHE HIS SER SER TYR ALA HIS SER GLN SER          
SEQRES  34 A  735  LEU ASP ARG LEU MET ASN PRO LEU ILE ASP GLN TYR LEU          
SEQRES  35 A  735  TYR TYR LEU SER ARG THR ASN THR PRO SER GLY THR THR          
SEQRES  36 A  735  THR GLN SER ARG LEU GLN PHE SER GLN ALA GLY ALA SER          
SEQRES  37 A  735  ASP ILE ARG ASP GLN SER ARG ASN TRP LEU PRO GLY PRO          
SEQRES  38 A  735  CYS TYR ARG GLN GLN ARG VAL SER LYS THR SER ALA ASP          
SEQRES  39 A  735  ASN ASN ASN SER GLU TYR SER TRP THR GLY ALA THR LYS          
SEQRES  40 A  735  TYR HIS LEU ASN GLY ARG ASP SER LEU VAL ASN PRO GLY          
SEQRES  41 A  735  PRO ALA MET ALA SER HIS LYS ASP ASP GLU GLU LYS PHE          
SEQRES  42 A  735  PHE PRO GLN SER GLY VAL LEU ILE PHE GLY LYS GLN GLY          
SEQRES  43 A  735  SER GLU LYS THR ASN VAL ASP ILE GLU LYS VAL MET ILE          
SEQRES  44 A  735  THR ASP GLU GLU GLU ILE ARG THR THR ASN PRO VAL ALA          
SEQRES  45 A  735  THR GLU GLN TYR GLY SER VAL SER THR ASN LEU GLN ARG          
SEQRES  46 A  735  GLY ASN ARG GLN ALA ALA THR ALA ASP VAL ASN THR GLN          
SEQRES  47 A  735  GLY VAL LEU PRO GLY MET VAL TRP GLN ASP ARG ASP VAL          
SEQRES  48 A  735  TYR LEU GLN GLY PRO ILE TRP ALA LYS ILE PRO HIS THR          
SEQRES  49 A  735  ASP GLY HIS PHE HIS PRO SER PRO LEU MET GLY GLY PHE          
SEQRES  50 A  735  GLY LEU LYS HIS PRO PRO PRO GLN ILE LEU ILE LYS ASN          
SEQRES  51 A  735  THR PRO VAL PRO ALA ASN PRO SER THR THR PHE SER ALA          
SEQRES  52 A  735  ALA LYS PHE ALA SER PHE ILE THR GLN TYR SER THR GLY          
SEQRES  53 A  735  GLN VAL SER VAL GLU ILE GLU TRP GLU LEU GLN LYS GLU          
SEQRES  54 A  735  ASN SER LYS ARG TRP ASN PRO GLU ILE GLN TYR THR SER          
SEQRES  55 A  735  ASN TYR ASN LYS SER VAL ASN VAL ASP PHE THR VAL ASP          
SEQRES  56 A  735  THR ASN GLY VAL TYR SER GLU PRO ARG PRO ILE GLY THR          
SEQRES  57 A  735  ARG TYR LEU THR ARG ASN LEU                                  
HET     MG  Z 601       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *143(H2 O)                                                    
HELIX    1 AA1 TYR A  252  LEU A  256  5                                   5    
HELIX    2 AA2 SER A  267  HIS A  271  5                                   5    
HELIX    3 AA3 ARG A  286  HIS A  290  5                                   5    
HELIX    4 AA4 SER A  292  ASN A  301  1                                  10    
HELIX    5 AA5 CYS A  394  PHE A  398  5                                   5    
HELIX    6 AA6 SER A  429  LEU A  433  5                                   5    
HELIX    7 AA7 ASP A  469  GLN A  473  5                                   5    
HELIX    8 AA8 THR A  491  ASN A  495  5                                   5    
HELIX    9 AA9 ASP A  553  GLU A  555  5                                   3    
HELIX   10 AB1 GLU A  562  THR A  568  5                                   7    
SHEET    1 AA1 4 PHE Z 416  SER Z 420  0                                        
SHEET    2 AA1 4 THR Z 486  ASN Z 496  1  O  ASN Z 492   N  GLN Z 417           
SHEET    3 AA1 4 GLY Z 471  VAL Z 480 -1  N  TYR Z 473   O  LEU Z 493           
SHEET    4 AA1 4 GLN Z 441  LYS Z 448 -1  N  GLU Z 445   O  SER Z 476           
SHEET    1 AA2 2 THR Z 426  ASP Z 429  0                                        
SHEET    2 AA2 2 ILE Z 462  LEU Z 465 -1  O  LEU Z 463   N  ILE Z 428           
SHEET    1 AA3 3 THR A 329  ASN A 335  0                                        
SHEET    2 AA3 3 ASN A 303  ASN A 326 -1  N  GLU A 322   O  ALA A 333           
SHEET    3 AA3 3 PHE A 409  THR A 414 -1  O  PHE A 411   N  PHE A 313           
SHEET    1 AA4 5 VAL A 369  MET A 371  0                                        
SHEET    2 AA4 5 ARG A 238  LEU A 249  1  N  THR A 246   O  PHE A 370           
SHEET    3 AA4 5 GLN A 672  LYS A 688 -1  O  TRP A 684   N  VAL A 239           
SHEET    4 AA4 5 ASN A 303  ASN A 326 -1  N  ARG A 307   O  GLU A 685           
SHEET    5 AA4 5 HIS A 421  SER A 422 -1  O  HIS A 421   N  PHE A 306           
SHEET    1 AA5 3 LYS A 258  SER A 261  0                                        
SHEET    2 AA5 3 PHE A 273  TYR A 281 -1  O  GLY A 274   N  ILE A 260           
SHEET    3 AA5 3 GLN A 374  LEU A 378 -1  O  TYR A 375   N  TRP A 279           
SHEET    1 AA6 5 LYS A 258  SER A 261  0                                        
SHEET    2 AA6 5 PHE A 273  TYR A 281 -1  O  GLY A 274   N  ILE A 260           
SHEET    3 AA6 5 ILE A 646  ASN A 650 -1  O  ILE A 648   N  GLY A 280           
SHEET    4 AA6 5 VAL A 340  THR A 344 -1  N  GLN A 341   O  LYS A 649           
SHEET    5 AA6 5 GLN A 401  LEU A 403 -1  O  GLN A 401   N  VAL A 342           
SHEET    1 AA7 2 ALA A 425  HIS A 426  0                                        
SHEET    2 AA7 2 THR A 732  ARG A 733  1  O  ARG A 733   N  ALA A 425           
SHEET    1 AA8 2 TYR A 443  SER A 452  0                                        
SHEET    2 AA8 2 THR A 455  GLN A 464 -1  O  THR A 455   N  SER A 452           
SHEET    1 AA9 2 CYS A 482  TYR A 483  0                                        
SHEET    2 AA9 2 THR A 597  GLN A 598 -1  O  GLN A 598   N  CYS A 482           
SHEET    1 AB1 2 ARG A 487  SER A 489  0                                        
SHEET    2 AB1 2 PHE A 533  PRO A 535 -1  O  PHE A 534   N  VAL A 488           
SHEET    1 AB2 2 LYS A 507  LEU A 510  0                                        
SHEET    2 AB2 2 ARG A 513  LEU A 516 -1  O  ARG A 513   N  LEU A 510           
SHEET    1 AB3 2 ILE A 541  GLY A 543  0                                        
SHEET    2 AB3 2 VAL A 557  ILE A 559 -1  O  MET A 558   N  PHE A 542           
SHEET    1 AB4 2 GLY A 577  SER A 580  0                                        
SHEET    2 AB4 2 THR A 592  VAL A 595 -1  O  ALA A 593   N  VAL A 579           
SHEET    1 AB5 2 TRP A 618  LYS A 620  0                                        
SHEET    2 AB5 2 PHE A 637  LEU A 639  1  O  LEU A 639   N  ALA A 619           
SSBOND   1 CYS A  289    CYS A  361                          1555   1555  2.06  
LINK         O   ARG Z 406                MG    MG Z 601     1555   1555  2.55  
LINK         OD2 ASP Z 435                MG    MG Z 601     1555   1555  2.76  
LINK         OD1 ASP Z 436                MG    MG Z 601     1555   1555  2.72  
LINK         OD1 ASP Z 481                MG    MG Z 601     1555   1555  2.83  
LINK         OD2 ASP Z 481                MG    MG Z 601     1555   1555  2.36  
CISPEP   1 LEU Z  421    PRO Z  422          0        -0.07                     
CISPEP   2 ASN A  518    PRO A  519          0        -0.86                     
SITE     1 AC1  5 ASN Z 405  ARG Z 406  ASP Z 435  ASP Z 436                    
SITE     2 AC1  5 ASP Z 481                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ASN Z 405      42.743 -47.559 115.035  0.65 37.72           N  
ATOM      2  CA  ASN Z 405      41.704 -46.522 115.299  0.65 37.70           C  
ATOM      3  C   ASN Z 405      41.659 -46.130 116.773  0.65 37.73           C  
ATOM      4  O   ASN Z 405      42.281 -46.771 117.621  0.65 37.67           O  
ATOM      5  CB  ASN Z 405      40.318 -47.029 114.877  0.65 37.78           C  
ATOM      6  CG  ASN Z 405      39.821 -48.178 115.743  0.65 37.51           C  
ATOM      7  OD1 ASN Z 405      38.648 -48.546 115.689  0.65 37.42           O  
ATOM      8  ND2 ASN Z 405      40.713 -48.751 116.541  0.65 37.57           N  
ATOM      9  N   ARG Z 406      40.907 -45.075 117.067  0.65 37.76           N  
ATOM     10  CA  ARG Z 406      40.759 -44.586 118.431  0.65 37.99           C  
ATOM     11  C   ARG Z 406      39.455 -45.129 119.010  0.65 37.12           C  
ATOM     12  O   ARG Z 406      38.468 -45.278 118.294  0.65 37.10           O  
ATOM     13  CB  ARG Z 406      40.740 -43.054 118.428  0.65 39.11           C  
ATOM     14  CG  ARG Z 406      41.998 -42.436 117.829  0.65 40.20           C  
ATOM     15  CD  ARG Z 406      41.841 -40.952 117.511  0.65 41.18           C  
ATOM     16  NE  ARG Z 406      41.531 -40.142 118.688  0.65 42.13           N  
ATOM     17  CZ  ARG Z 406      40.309 -39.958 119.180  0.65 42.70           C  
ATOM     18  NH1 ARG Z 406      39.258 -40.526 118.599  0.65 42.79           N  
ATOM     19  NH2 ARG Z 406      40.138 -39.205 120.260  0.65 42.97           N  
ATOM     20  N   PRO Z 407      39.439 -45.448 120.313  0.65 36.47           N  
ATOM     21  CA  PRO Z 407      38.218 -45.974 120.933  0.65 35.83           C  
ATOM     22  C   PRO Z 407      37.134 -44.901 121.029  0.65 34.69           C  
ATOM     23  O   PRO Z 407      37.435 -43.710 121.118  0.65 34.82           O  
ATOM     24  CB  PRO Z 407      38.706 -46.442 122.302  0.65 36.17           C  
ATOM     25  CG  PRO Z 407      39.796 -45.450 122.613  0.65 36.29           C  
ATOM     26  CD  PRO Z 407      40.535 -45.363 121.296  0.65 36.38           C  
ATOM     27  N   PRO Z 408      35.855 -45.312 121.012  0.65 33.46           N  
ATOM     28  CA  PRO Z 408      34.735 -44.371 121.096  0.65 32.68           C  
ATOM     29  C   PRO Z 408      34.643 -43.668 122.448  0.65 32.54           C  
ATOM     30  O   PRO Z 408      35.152 -44.165 123.452  0.65 32.74           O  
ATOM     31  CB  PRO Z 408      33.524 -45.258 120.816  0.65 32.51           C  
ATOM     32  CG  PRO Z 408      33.930 -46.563 121.421  0.65 32.75           C  
ATOM     33  CD  PRO Z 408      35.371 -46.704 120.967  0.65 33.10           C  
ATOM     34  N   ILE Z 409      34.010 -42.499 122.463  0.65 32.32           N  
ATOM     35  CA  ILE Z 409      33.833 -41.744 123.700  0.65 32.29           C  
ATOM     36  C   ILE Z 409      32.342 -41.700 124.032  0.65 32.37           C  
ATOM     37  O   ILE Z 409      31.536 -41.217 123.234  0.65 32.37           O  
ATOM     38  CB  ILE Z 409      34.347 -40.279 123.579  0.65 32.27           C  
ATOM     39  CG1 ILE Z 409      35.865 -40.249 123.354  0.65 32.32           C  
ATOM     40  CG2 ILE Z 409      34.018 -39.505 124.852  0.65 31.95           C  
ATOM     41  CD1 ILE Z 409      36.308 -40.724 121.996  0.65 32.50           C  
ATOM     42  N   ALA Z 410      31.978 -42.211 125.203  0.65 32.32           N  
ATOM     43  CA  ALA Z 410      30.583 -42.215 125.625  0.65 32.56           C  
ATOM     44  C   ALA Z 410      30.220 -40.863 126.243  0.65 32.70           C  
ATOM     45  O   ALA Z 410      30.968 -40.319 127.056  0.65 32.57           O  
ATOM     46  CB  ALA Z 410      30.338 -43.343 126.631  0.65 32.53           C  
ATOM     47  N   ILE Z 411      29.073 -40.323 125.839  0.65 33.01           N  
ATOM     48  CA  ILE Z 411      28.600 -39.039 126.349  0.65 33.33           C  
ATOM     49  C   ILE Z 411      27.121 -39.143 126.736  0.65 34.02           C  
ATOM     50  O   ILE Z 411      26.330 -39.754 126.016  0.65 33.65           O  
ATOM     51  CB  ILE Z 411      28.729 -37.924 125.280  0.65 33.10           C  
ATOM     52  CG1 ILE Z 411      30.142 -37.895 124.688  0.65 32.95           C  
ATOM     53  CG2 ILE Z 411      28.402 -36.577 125.901  0.65 33.05           C  
ATOM     54  CD1 ILE Z 411      31.226 -37.469 125.654  0.65 32.97           C  
ATOM     55  N   VAL Z 412      26.755 -38.547 127.869  0.65 35.11           N  
ATOM     56  CA  VAL Z 412      25.367 -38.547 128.332  0.65 36.28           C  
ATOM     57  C   VAL Z 412      24.954 -37.098 128.602  0.65 37.65           C  
ATOM     58  O   VAL Z 412      25.619 -36.383 129.349  0.65 37.71           O  
ATOM     59  CB  VAL Z 412      25.194 -39.380 129.620  0.65 36.12           C  
ATOM     60  CG1 VAL Z 412      25.512 -40.840 129.335  0.65 35.70           C  
ATOM     61  CG2 VAL Z 412      26.094 -38.839 130.721  0.65 36.39           C  
ATOM     62  N   SER Z 413      23.868 -36.658 127.979  0.65 38.95           N  
ATOM     63  CA  SER Z 413      23.415 -35.284 128.155  0.65 40.49           C  
ATOM     64  C   SER Z 413      23.224 -34.909 129.626  0.65 41.90           C  
ATOM     65  O   SER Z 413      23.895 -34.012 130.144  0.65 42.13           O  
ATOM     66  CB  SER Z 413      22.115 -35.055 127.371  0.65 40.73           C  
ATOM     67  OG  SER Z 413      21.544 -33.788 127.648  0.65 40.85           O  
ATOM     68  N   PRO Z 414      22.298 -35.581 130.319  0.65 42.48           N  
ATOM     69  CA  PRO Z 414      22.120 -35.218 131.722  0.65 43.33           C  
ATOM     70  C   PRO Z 414      22.901 -36.166 132.639  0.65 44.81           C  
ATOM     71  O   PRO Z 414      22.830 -37.387 132.488  0.65 44.56           O  
ATOM     72  CB  PRO Z 414      20.614 -35.329 131.892  0.65 42.81           C  
ATOM     73  CG  PRO Z 414      20.310 -36.552 131.083  0.65 42.50           C  
ATOM     74  CD  PRO Z 414      21.155 -36.381 129.836  0.65 42.33           C  
ATOM     75  N   GLN Z 415      23.646 -35.606 133.587  0.65 46.43           N  
ATOM     76  CA  GLN Z 415      24.429 -36.430 134.504  0.65 47.56           C  
ATOM     77  C   GLN Z 415      23.944 -36.326 135.946  0.65 48.23           C  
ATOM     78  O   GLN Z 415      24.446 -37.025 136.832  0.65 47.88           O  
ATOM     79  CB  GLN Z 415      25.912 -36.048 134.425  0.65 47.94           C  
ATOM     80  CG  GLN Z 415      26.484 -36.048 133.010  0.65 47.88           C  
ATOM     81  CD  GLN Z 415      27.976 -35.720 132.970  0.65 47.71           C  
ATOM     82  OE1 GLN Z 415      28.524 -35.133 133.906  0.65 47.58           O  
ATOM     83  NE2 GLN Z 415      28.634 -36.086 131.872  0.65 47.74           N  
ATOM     84  N   PHE Z 416      22.976 -35.444 136.180  0.65 49.19           N  
ATOM     85  CA  PHE Z 416      22.412 -35.267 137.514  0.65 50.09           C  
ATOM     86  C   PHE Z 416      20.895 -35.105 137.461  0.65 50.02           C  
ATOM     87  O   PHE Z 416      20.350 -34.094 137.905  0.65 50.11           O  
ATOM     88  CB  PHE Z 416      23.036 -34.057 138.224  0.65 51.08           C  
ATOM     89  CG  PHE Z 416      24.516 -34.186 138.461  0.65 52.07           C  
ATOM     90  CD1 PHE Z 416      25.421 -33.845 137.458  0.65 52.42           C  
ATOM     91  CD2 PHE Z 416      25.006 -34.659 139.682  0.65 52.34           C  
ATOM     92  CE1 PHE Z 416      26.789 -33.969 137.660  0.65 52.60           C  
ATOM     93  CE2 PHE Z 416      26.376 -34.789 139.898  0.65 52.58           C  
ATOM     94  CZ  PHE Z 416      27.271 -34.443 138.885  0.65 52.68           C  
ATOM     95  N   GLN Z 417      20.217 -36.115 136.925  0.65 49.60           N  
ATOM     96  CA  GLN Z 417      18.761 -36.105 136.818  0.65 49.22           C  
ATOM     97  C   GLN Z 417      18.125 -35.826 138.179  0.65 49.03           C  
ATOM     98  O   GLN Z 417      18.454 -36.484 139.165  0.65 49.28           O  
ATOM     99  CB  GLN Z 417      18.275 -37.461 136.294  0.65 49.18           C  
ATOM    100  CG  GLN Z 417      18.650 -37.754 134.854  0.65 48.94           C  
ATOM    101  CD  GLN Z 417      17.868 -36.911 133.868  0.65 48.73           C  
ATOM    102  OE1 GLN Z 417      17.981 -37.094 132.657  0.65 48.53           O  
ATOM    103  NE2 GLN Z 417      17.070 -35.978 134.381  0.65 48.75           N  
ATOM    104  N   GLU Z 418      17.221 -34.848 138.226  0.65 48.59           N  
ATOM    105  CA  GLU Z 418      16.527 -34.480 139.461  0.65 48.24           C  
ATOM    106  C   GLU Z 418      15.014 -34.476 139.226  0.65 47.39           C  
ATOM    107  O   GLU Z 418      14.377 -33.424 139.208  0.65 47.46           O  
ATOM    108  CB  GLU Z 418      16.988 -33.096 139.934  0.65 48.77           C  
ATOM    109  CG  GLU Z 418      16.367 -32.647 141.252  0.65 49.07           C  
ATOM    110  CD  GLU Z 418      16.807 -33.500 142.425  0.65 49.21           C  
ATOM    111  OE1 GLU Z 418      17.380 -34.584 142.188  0.65 49.17           O  
ATOM    112  OE2 GLU Z 418      16.574 -33.092 143.584  0.65 49.20           O  
ATOM    113  N   ILE Z 419      14.445 -35.663 139.053  0.65 46.51           N  
ATOM    114  CA  ILE Z 419      13.014 -35.802 138.803  0.65 45.89           C  
ATOM    115  C   ILE Z 419      12.298 -36.388 140.022  0.65 45.90           C  
ATOM    116  O   ILE Z 419      12.669 -37.450 140.518  0.65 45.89           O  
ATOM    117  CB  ILE Z 419      12.773 -36.700 137.558  0.65 45.49           C  
ATOM    118  CG1 ILE Z 419      11.281 -36.778 137.232  0.65 45.58           C  
ATOM    119  CG2 ILE Z 419      13.325 -38.098 137.804  0.65 45.22           C  
ATOM    120  CD1 ILE Z 419      10.963 -37.551 135.961  0.65 45.55           C  
ATOM    121  N   SER Z 420      11.277 -35.688 140.507  0.65 45.92           N  
ATOM    122  CA  SER Z 420      10.516 -36.155 141.664  0.65 45.94           C  
ATOM    123  C   SER Z 420       9.075 -36.496 141.299  0.65 46.04           C  
ATOM    124  O   SER Z 420       8.609 -36.171 140.207  0.65 46.07           O  
ATOM    125  CB  SER Z 420      10.512 -35.096 142.767  0.65 45.81           C  
ATOM    126  OG  SER Z 420       9.907 -33.897 142.314  0.65 45.83           O  
ATOM    127  N   LEU Z 421       8.372 -37.149 142.220  0.65 46.07           N  
ATOM    128  CA  LEU Z 421       6.978 -37.529 141.996  0.65 46.18           C  
ATOM    129  C   LEU Z 421       6.081 -36.289 142.017  0.65 46.05           C  
ATOM    130  O   LEU Z 421       6.433 -35.278 142.624  0.65 46.10           O  
ATOM    131  CB  LEU Z 421       6.519 -38.515 143.074  0.65 46.35           C  
ATOM    132  CG  LEU Z 421       7.225 -39.873 143.140  0.65 46.53           C  
ATOM    133  CD1 LEU Z 421       6.525 -40.757 144.174  0.65 46.47           C  
ATOM    134  CD2 LEU Z 421       7.181 -40.546 141.771  0.65 46.61           C  
ATOM    135  N   PRO Z 422       4.892 -36.364 141.386  0.65 45.95           N  
ATOM    136  CA  PRO Z 422       4.378 -37.540 140.673  0.65 45.67           C  
ATOM    137  C   PRO Z 422       5.021 -37.878 139.325  0.65 45.07           C  
ATOM    138  O   PRO Z 422       4.660 -38.883 138.707  0.65 45.02           O  
ATOM    139  CB  PRO Z 422       2.891 -37.226 140.537  0.65 45.89           C  
ATOM    140  CG  PRO Z 422       2.895 -35.760 140.344  0.65 45.93           C  
ATOM    141  CD  PRO Z 422       3.875 -35.295 141.407  0.65 46.00           C  
ATOM    142  N   THR Z 423       5.957 -37.052 138.860  0.65 44.32           N  
ATOM    143  CA  THR Z 423       6.618 -37.332 137.586  0.65 43.67           C  
ATOM    144  C   THR Z 423       7.414 -38.623 137.762  0.65 42.81           C  
ATOM    145  O   THR Z 423       8.319 -38.702 138.595  0.65 42.48           O  
ATOM    146  CB  THR Z 423       7.568 -36.184 137.160  0.65 43.72           C  
ATOM    147  OG1 THR Z 423       8.738 -36.191 137.986  0.65 43.73           O  
ATOM    148  CG2 THR Z 423       6.856 -34.833 137.293  0.65 43.62           C  
ATOM    149  N   THR Z 424       7.062 -39.634 136.977  0.65 42.38           N  
ATOM    150  CA  THR Z 424       7.707 -40.940 137.063  0.65 42.07           C  
ATOM    151  C   THR Z 424       8.581 -41.321 135.871  0.65 41.82           C  
ATOM    152  O   THR Z 424       9.190 -42.393 135.869  0.65 42.07           O  
ATOM    153  CB  THR Z 424       6.651 -42.048 137.235  0.65 42.10           C  
ATOM    154  OG1 THR Z 424       5.718 -41.984 136.147  0.65 42.04           O  
ATOM    155  CG2 THR Z 424       5.903 -41.879 138.558  0.65 42.02           C  
ATOM    156  N   SER Z 425       8.645 -40.460 134.860  0.65 41.29           N  
ATOM    157  CA  SER Z 425       9.451 -40.765 133.684  0.65 40.71           C  
ATOM    158  C   SER Z 425      10.432 -39.659 133.304  0.65 40.18           C  
ATOM    159  O   SER Z 425      10.057 -38.495 133.158  0.65 40.30           O  
ATOM    160  CB  SER Z 425       8.547 -41.070 132.484  0.65 40.53           C  
ATOM    161  OG  SER Z 425       7.831 -39.918 132.072  0.65 40.68           O  
ATOM    162  N   THR Z 426      11.695 -40.044 133.149  0.65 39.40           N  
ATOM    163  CA  THR Z 426      12.751 -39.121 132.761  0.65 38.91           C  
ATOM    164  C   THR Z 426      13.410 -39.734 131.526  0.65 37.91           C  
ATOM    165  O   THR Z 426      12.926 -40.739 131.002  0.65 38.07           O  
ATOM    166  CB  THR Z 426      13.801 -38.952 133.890  0.65 39.50           C  
ATOM    167  OG1 THR Z 426      14.690 -37.876 133.564  0.65 39.61           O  
ATOM    168  CG2 THR Z 426      14.615 -40.235 134.068  0.65 39.86           C  
ATOM    169  N   VAL Z 427      14.504 -39.143 131.062  0.65 36.89           N  
ATOM    170  CA  VAL Z 427      15.191 -39.659 129.883  0.65 36.02           C  
ATOM    171  C   VAL Z 427      16.672 -39.287 129.857  0.65 35.13           C  
ATOM    172  O   VAL Z 427      17.049 -38.172 130.224  0.65 35.14           O  
ATOM    173  CB  VAL Z 427      14.521 -39.138 128.588  0.65 36.42           C  
ATOM    174  CG1 VAL Z 427      14.498 -37.620 128.593  0.65 36.91           C  
ATOM    175  CG2 VAL Z 427      15.263 -39.646 127.366  0.65 36.56           C  
ATOM    176  N   ILE Z 428      17.506 -40.231 129.432  0.65 34.23           N  
ATOM    177  CA  ILE Z 428      18.943 -39.997 129.333  0.65 33.33           C  
ATOM    178  C   ILE Z 428      19.350 -40.134 127.870  0.65 31.90           C  
ATOM    179  O   ILE Z 428      19.073 -41.154 127.239  0.65 31.81           O  
ATOM    180  CB  ILE Z 428      19.762 -41.023 130.158  0.65 33.73           C  
ATOM    181  CG1 ILE Z 428      19.186 -41.160 131.570  0.65 33.99           C  
ATOM    182  CG2 ILE Z 428      21.219 -40.567 130.240  0.65 33.70           C  
ATOM    183  CD1 ILE Z 428      19.174 -39.867 132.370  0.65 34.21           C  
ATOM    184  N   ASP Z 429      20.002 -39.108 127.333  0.65 30.97           N  
ATOM    185  CA  ASP Z 429      20.437 -39.125 125.938  0.65 30.05           C  
ATOM    186  C   ASP Z 429      21.904 -39.539 125.808  0.65 29.53           C  
ATOM    187  O   ASP Z 429      22.786 -38.954 126.443  0.65 29.52           O  
ATOM    188  CB  ASP Z 429      20.222 -37.742 125.308  0.65 29.75           C  
ATOM    189  CG  ASP Z 429      20.607 -37.696 123.837  0.65 29.36           C  
ATOM    190  OD1 ASP Z 429      20.150 -38.568 123.069  0.65 29.28           O  
ATOM    191  OD2 ASP Z 429      21.360 -36.779 123.445  0.65 29.31           O  
ATOM    192  N   GLY Z 430      22.155 -40.560 124.994  0.65 28.77           N  
ATOM    193  CA  GLY Z 430      23.513 -41.028 124.786  0.65 28.29           C  
ATOM    194  C   GLY Z 430      23.915 -40.868 123.332  0.65 28.13           C  
ATOM    195  O   GLY Z 430      25.024 -41.225 122.934  0.65 27.94           O  
ATOM    196  N   SER Z 431      23.001 -40.317 122.541  0.65 28.40           N  
ATOM    197  CA  SER Z 431      23.215 -40.107 121.115  0.65 28.77           C  
ATOM    198  C   SER Z 431      24.368 -39.152 120.796  0.65 29.23           C  
ATOM    199  O   SER Z 431      24.747 -39.003 119.634  0.65 29.07           O  
ATOM    200  CB  SER Z 431      21.932 -39.577 120.475  0.65 28.78           C  
ATOM    201  OG  SER Z 431      21.639 -38.271 120.943  0.65 28.57           O  
ATOM    202  N   GLN Z 432      24.919 -38.505 121.819  0.65 29.55           N  
ATOM    203  CA  GLN Z 432      26.029 -37.578 121.618  0.65 29.98           C  
ATOM    204  C   GLN Z 432      27.380 -38.292 121.632  0.65 29.48           C  
ATOM    205  O   GLN Z 432      28.409 -37.686 121.336  0.65 29.08           O  
ATOM    206  CB  GLN Z 432      26.013 -36.484 122.690  0.65 31.05           C  
ATOM    207  CG  GLN Z 432      24.839 -35.510 122.580  0.65 31.53           C  
ATOM    208  CD  GLN Z 432      24.826 -34.484 123.702  0.65 32.22           C  
ATOM    209  OE1 GLN Z 432      25.741 -34.434 124.528  0.65 32.55           O  
ATOM    210  NE2 GLN Z 432      23.786 -33.658 123.736  0.65 32.43           N  
ATOM    211  N   SER Z 433      27.374 -39.578 121.981  0.65 29.69           N  
ATOM    212  CA  SER Z 433      28.600 -40.372 122.014  0.65 29.75           C  
ATOM    213  C   SER Z 433      29.288 -40.255 120.654  0.65 30.03           C  
ATOM    214  O   SER Z 433      28.636 -40.366 119.614  0.65 29.90           O  
ATOM    215  CB  SER Z 433      28.271 -41.836 122.312  0.65 29.78           C  
ATOM    216  OG  SER Z 433      27.653 -41.971 123.580  0.65 29.82           O  
ATOM    217  N   THR Z 434      30.602 -40.047 120.660  0.65 30.37           N  
ATOM    218  CA  THR Z 434      31.343 -39.869 119.415  0.65 30.91           C  
ATOM    219  C   THR Z 434      32.633 -40.674 119.272  0.65 31.60           C  
ATOM    220  O   THR Z 434      33.293 -40.987 120.262  0.65 32.23           O  
ATOM    221  CB  THR Z 434      31.725 -38.383 119.223  0.65 31.11           C  
ATOM    222  OG1 THR Z 434      32.686 -38.003 120.215  0.65 31.52           O  
ATOM    223  CG2 THR Z 434      30.501 -37.486 119.364  0.65 30.96           C  
ATOM    224  N   ASP Z 435      32.986 -41.000 118.027  0.65 31.37           N  
ATOM    225  CA  ASP Z 435      34.231 -41.712 117.728  0.65 31.17           C  
ATOM    226  C   ASP Z 435      34.627 -41.497 116.267  0.65 30.08           C  
ATOM    227  O   ASP Z 435      33.782 -41.174 115.435  0.65 29.49           O  
ATOM    228  CB  ASP Z 435      34.120 -43.211 118.043  0.65 31.63           C  
ATOM    229  CG  ASP Z 435      33.505 -44.007 116.919  0.65 32.02           C  
ATOM    230  OD1 ASP Z 435      32.314 -43.786 116.609  0.65 32.36           O  
ATOM    231  OD2 ASP Z 435      34.218 -44.861 116.350  0.65 31.92           O  
ATOM    232  N   ASP Z 436      35.915 -41.662 115.967  0.65 29.76           N  
ATOM    233  CA  ASP Z 436      36.426 -41.458 114.613  0.65 29.54           C  
ATOM    234  C   ASP Z 436      35.579 -42.125 113.540  0.65 29.70           C  
ATOM    235  O   ASP Z 436      35.168 -41.475 112.583  0.65 29.52           O  
ATOM    236  CB  ASP Z 436      37.883 -41.931 114.505  0.65 29.50           C  
ATOM    237  CG  ASP Z 436      38.111 -43.285 115.148  0.65 29.31           C  
ATOM    238  OD1 ASP Z 436      37.937 -43.386 116.380  0.65 29.43           O  
ATOM    239  OD2 ASP Z 436      38.470 -44.243 114.428  0.65 29.15           O  
ATOM    240  N   ASP Z 437      35.330 -43.421 113.687  0.65 30.41           N  
ATOM    241  CA  ASP Z 437      34.500 -44.143 112.728  0.65 31.27           C  
ATOM    242  C   ASP Z 437      33.102 -44.079 113.351  0.65 31.53           C  
ATOM    243  O   ASP Z 437      32.836 -43.167 114.131  0.65 32.43           O  
ATOM    244  CB  ASP Z 437      34.994 -45.586 112.596  0.65 31.83           C  
ATOM    245  CG  ASP Z 437      34.499 -46.261 111.330  0.65 32.16           C  
ATOM    246  OD1 ASP Z 437      34.737 -45.713 110.233  0.65 32.34           O  
ATOM    247  OD2 ASP Z 437      33.877 -47.341 111.430  0.65 32.25           O  
ATOM    248  N   LYS Z 438      32.201 -45.004 113.041  0.65 30.87           N  
ATOM    249  CA  LYS Z 438      30.887 -44.917 113.672  0.65 30.56           C  
ATOM    250  C   LYS Z 438      30.659 -45.921 114.796  0.65 29.79           C  
ATOM    251  O   LYS Z 438      31.320 -46.956 114.865  0.65 29.85           O  
ATOM    252  CB  LYS Z 438      29.762 -45.036 112.634  0.65 31.04           C  
ATOM    253  CG  LYS Z 438      29.610 -46.384 111.952  0.65 31.08           C  
ATOM    254  CD  LYS Z 438      28.456 -46.322 110.953  0.65 30.98           C  
ATOM    255  CE  LYS Z 438      28.323 -47.605 110.162  0.65 31.13           C  
ATOM    256  NZ  LYS Z 438      27.196 -47.541 109.188  0.65 31.19           N  
ATOM    257  N   ILE Z 439      29.733 -45.584 115.691  0.65 29.13           N  
ATOM    258  CA  ILE Z 439      29.378 -46.445 116.813  0.65 28.74           C  
ATOM    259  C   ILE Z 439      28.354 -47.452 116.305  0.65 29.39           C  
ATOM    260  O   ILE Z 439      27.399 -47.081 115.627  0.65 29.53           O  
ATOM    261  CB  ILE Z 439      28.756 -45.632 117.974  0.65 28.26           C  
ATOM    262  CG1 ILE Z 439      29.802 -44.679 118.560  0.65 28.04           C  
ATOM    263  CG2 ILE Z 439      28.230 -46.572 119.055  0.65 28.09           C  
ATOM    264  CD1 ILE Z 439      29.291 -43.827 119.701  0.65 27.78           C  
ATOM    265  N   VAL Z 440      28.551 -48.725 116.629  0.65 30.40           N  
ATOM    266  CA  VAL Z 440      27.637 -49.763 116.165  0.65 31.51           C  
ATOM    267  C   VAL Z 440      26.748 -50.366 117.249  0.65 32.64           C  
ATOM    268  O   VAL Z 440      25.836 -51.136 116.942  0.65 32.91           O  
ATOM    269  CB  VAL Z 440      28.410 -50.914 115.482  0.65 31.24           C  
ATOM    270  CG1 VAL Z 440      29.202 -50.381 114.296  0.65 31.11           C  
ATOM    271  CG2 VAL Z 440      29.332 -51.588 116.487  0.65 30.97           C  
ATOM    272  N   GLN Z 441      27.000 -50.025 118.508  0.65 33.54           N  
ATOM    273  CA  GLN Z 441      26.193 -50.584 119.585  0.65 34.68           C  
ATOM    274  C   GLN Z 441      26.087 -49.694 120.818  0.65 34.52           C  
ATOM    275  O   GLN Z 441      27.075 -49.123 121.283  0.65 34.24           O  
ATOM    276  CB  GLN Z 441      26.751 -51.954 119.997  0.65 35.89           C  
ATOM    277  CG  GLN Z 441      25.777 -52.800 120.818  0.65 37.26           C  
ATOM    278  CD  GLN Z 441      26.379 -54.120 121.289  0.65 38.06           C  
ATOM    279  OE1 GLN Z 441      27.245 -54.145 122.168  0.65 38.22           O  
ATOM    280  NE2 GLN Z 441      25.921 -55.223 120.701  0.65 38.17           N  
ATOM    281  N   TYR Z 442      24.870 -49.590 121.340  0.65 34.73           N  
ATOM    282  CA  TYR Z 442      24.591 -48.806 122.538  0.65 34.99           C  
ATOM    283  C   TYR Z 442      24.092 -49.787 123.596  0.65 35.95           C  
ATOM    284  O   TYR Z 442      23.270 -50.655 123.302  0.65 36.10           O  
ATOM    285  CB  TYR Z 442      23.510 -47.758 122.252  0.65 34.38           C  
ATOM    286  CG  TYR Z 442      23.971 -46.596 121.393  0.65 33.74           C  
ATOM    287  CD1 TYR Z 442      24.781 -45.591 121.922  0.65 33.59           C  
ATOM    288  CD2 TYR Z 442      23.608 -46.509 120.048  0.65 33.45           C  
ATOM    289  CE1 TYR Z 442      25.218 -44.524 121.135  0.65 33.54           C  
ATOM    290  CE2 TYR Z 442      24.041 -45.448 119.250  0.65 33.55           C  
ATOM    291  CZ  TYR Z 442      24.846 -44.460 119.801  0.65 33.70           C  
ATOM    292  OH  TYR Z 442      25.282 -43.412 119.019  0.65 33.84           O  
ATOM    293  N   HIS Z 443      24.593 -49.665 124.820  0.65 36.78           N  
ATOM    294  CA  HIS Z 443      24.168 -50.564 125.885  0.65 37.94           C  
ATOM    295  C   HIS Z 443      24.003 -49.843 127.216  0.65 38.30           C  
ATOM    296  O   HIS Z 443      24.971 -49.328 127.778  0.65 38.37           O  
ATOM    297  CB  HIS Z 443      25.173 -51.707 126.049  0.65 39.10           C  
ATOM    298  CG  HIS Z 443      24.721 -52.778 126.995  0.65 40.06           C  
ATOM    299  ND1 HIS Z 443      23.600 -53.549 126.766  0.65 40.25           N  
ATOM    300  CD2 HIS Z 443      25.235 -53.203 128.175  0.65 40.24           C  
ATOM    301  CE1 HIS Z 443      23.443 -54.401 127.763  0.65 40.37           C  
ATOM    302  NE2 HIS Z 443      24.421 -54.212 128.632  0.65 40.39           N  
ATOM    303  N   TRP Z 444      22.770 -49.808 127.712  0.65 38.64           N  
ATOM    304  CA  TRP Z 444      22.476 -49.164 128.985  0.65 39.07           C  
ATOM    305  C   TRP Z 444      22.337 -50.209 130.084  0.65 40.50           C  
ATOM    306  O   TRP Z 444      21.809 -51.299 129.857  0.65 40.51           O  
ATOM    307  CB  TRP Z 444      21.176 -48.356 128.904  0.65 38.13           C  
ATOM    308  CG  TRP Z 444      21.217 -47.210 127.949  0.65 36.86           C  
ATOM    309  CD1 TRP Z 444      20.841 -47.217 126.636  0.65 36.28           C  
ATOM    310  CD2 TRP Z 444      21.662 -45.880 128.233  0.65 36.16           C  
ATOM    311  NE1 TRP Z 444      21.022 -45.972 126.085  0.65 35.86           N  
ATOM    312  CE2 TRP Z 444      21.525 -45.132 127.043  0.65 35.85           C  
ATOM    313  CE3 TRP Z 444      22.164 -45.248 129.378  0.65 36.02           C  
ATOM    314  CZ2 TRP Z 444      21.872 -43.780 126.966  0.65 35.67           C  
ATOM    315  CZ3 TRP Z 444      22.509 -43.901 129.300  0.65 35.89           C  
ATOM    316  CH2 TRP Z 444      22.360 -43.183 128.102  0.65 35.66           C  
ATOM    317  N   GLU Z 445      22.812 -49.869 131.277  0.65 41.97           N  
ATOM    318  CA  GLU Z 445      22.730 -50.770 132.419  0.65 43.56           C  
ATOM    319  C   GLU Z 445      22.589 -50.010 133.728  0.65 44.29           C  
ATOM    320  O   GLU Z 445      23.301 -49.036 133.969  0.65 44.36           O  
ATOM    321  CB  GLU Z 445      23.973 -51.658 132.501  0.65 44.27           C  
ATOM    322  CG  GLU Z 445      23.974 -52.852 131.559  0.65 44.97           C  
ATOM    323  CD  GLU Z 445      25.130 -53.798 131.841  0.65 45.55           C  
ATOM    324  OE1 GLU Z 445      26.297 -53.367 131.708  0.65 45.64           O  
ATOM    325  OE2 GLU Z 445      24.873 -54.969 132.203  0.65 45.58           O  
ATOM    326  N   GLU Z 446      21.664 -50.458 134.571  0.65 44.95           N  
ATOM    327  CA  GLU Z 446      21.462 -49.830 135.868  0.65 45.58           C  
ATOM    328  C   GLU Z 446      22.432 -50.493 136.839  0.65 45.94           C  
ATOM    329  O   GLU Z 446      22.269 -51.664 137.188  0.65 45.82           O  
ATOM    330  CB  GLU Z 446      20.026 -50.037 136.362  0.65 45.92           C  
ATOM    331  CG  GLU Z 446      19.744 -49.362 137.701  0.65 46.22           C  
ATOM    332  CD  GLU Z 446      18.453 -49.836 138.348  0.65 46.69           C  
ATOM    333  OE1 GLU Z 446      18.370 -51.032 138.709  0.65 46.66           O  
ATOM    334  OE2 GLU Z 446      17.523 -49.012 138.496  0.65 46.77           O  
ATOM    335  N   LEU Z 447      23.447 -49.749 137.262  0.65 46.53           N  
ATOM    336  CA  LEU Z 447      24.437 -50.278 138.191  0.65 47.10           C  
ATOM    337  C   LEU Z 447      23.832 -50.445 139.580  0.65 47.79           C  
ATOM    338  O   LEU Z 447      24.174 -51.380 140.309  0.65 47.85           O  
ATOM    339  CB  LEU Z 447      25.648 -49.346 138.260  0.65 46.97           C  
ATOM    340  CG  LEU Z 447      26.358 -49.085 136.928  0.65 46.85           C  
ATOM    341  CD1 LEU Z 447      27.558 -48.182 137.166  0.65 46.68           C  
ATOM    342  CD2 LEU Z 447      26.793 -50.407 136.297  0.65 46.73           C  
ATOM    343  N   LYS Z 448      22.932 -49.535 139.940  0.65 48.20           N  
ATOM    344  CA  LYS Z 448      22.272 -49.579 141.239  0.65 48.56           C  
ATOM    345  C   LYS Z 448      20.959 -48.805 141.216  0.65 48.96           C  
ATOM    346  O   LYS Z 448      20.714 -48.005 140.311  0.65 48.82           O  
ATOM    347  CB  LYS Z 448      23.188 -49.001 142.325  0.65 48.59           C  
ATOM    348  CG  LYS Z 448      23.568 -47.535 142.131  0.65 48.82           C  
ATOM    349  CD  LYS Z 448      24.406 -47.032 143.306  0.65 49.01           C  
ATOM    350  CE  LYS Z 448      24.852 -45.581 143.125  0.65 49.16           C  
ATOM    351  NZ  LYS Z 448      23.718 -44.611 143.137  0.65 49.20           N  
ATOM    352  N   GLY Z 449      20.123 -49.046 142.220  0.65 49.63           N  
ATOM    353  CA  GLY Z 449      18.845 -48.365 142.301  0.65 50.39           C  
ATOM    354  C   GLY Z 449      17.822 -49.112 143.138  0.65 51.23           C  
ATOM    355  O   GLY Z 449      18.108 -50.198 143.646  0.65 51.28           O  
ATOM    356  N   PRO Z 450      16.615 -48.547 143.306  0.65 51.84           N  
ATOM    357  CA  PRO Z 450      15.534 -49.160 144.087  0.65 52.23           C  
ATOM    358  C   PRO Z 450      15.144 -50.541 143.564  0.65 52.62           C  
ATOM    359  O   PRO Z 450      14.861 -50.710 142.375  0.65 52.42           O  
ATOM    360  CB  PRO Z 450      14.395 -48.150 143.948  0.65 52.05           C  
ATOM    361  CG  PRO Z 450      15.120 -46.849 143.833  0.65 51.94           C  
ATOM    362  CD  PRO Z 450      16.232 -47.194 142.866  0.65 51.89           C  
ATOM    363  N   LEU Z 451      15.132 -51.524 144.459  0.65 53.24           N  
ATOM    364  CA  LEU Z 451      14.774 -52.890 144.094  0.65 53.83           C  
ATOM    365  C   LEU Z 451      13.360 -52.943 143.520  0.65 53.98           C  
ATOM    366  O   LEU Z 451      12.378 -52.830 144.256  0.65 54.14           O  
ATOM    367  CB  LEU Z 451      14.869 -53.807 145.319  0.65 54.21           C  
ATOM    368  CG  LEU Z 451      16.250 -53.993 145.964  0.65 54.36           C  
ATOM    369  CD1 LEU Z 451      16.119 -54.869 147.207  0.65 54.32           C  
ATOM    370  CD2 LEU Z 451      17.214 -54.628 144.962  0.65 54.34           C  
ATOM    371  N   ARG Z 452      13.264 -53.106 142.203  0.65 53.81           N  
ATOM    372  CA  ARG Z 452      11.972 -53.183 141.529  0.65 53.58           C  
ATOM    373  C   ARG Z 452      12.061 -54.112 140.317  0.65 54.15           C  
ATOM    374  O   ARG Z 452      13.112 -54.702 140.058  0.65 54.20           O  
ATOM    375  CB  ARG Z 452      11.512 -51.786 141.095  0.65 52.88           C  
ATOM    376  CG  ARG Z 452      12.337 -51.147 139.983  0.65 52.25           C  
ATOM    377  CD  ARG Z 452      11.761 -49.783 139.605  0.65 51.78           C  
ATOM    378  NE  ARG Z 452      12.370 -49.222 138.400  0.65 51.56           N  
ATOM    379  CZ  ARG Z 452      13.653 -48.889 138.284  0.65 51.42           C  
ATOM    380  NH1 ARG Z 452      14.484 -49.057 139.307  0.65 51.34           N  
ATOM    381  NH2 ARG Z 452      14.106 -48.386 137.142  0.65 51.29           N  
ATOM    382  N   GLU Z 453      10.965 -54.234 139.573  0.65 54.67           N  
ATOM    383  CA  GLU Z 453      10.931 -55.114 138.407  0.65 55.24           C  
ATOM    384  C   GLU Z 453      11.118 -54.409 137.061  0.65 55.48           C  
ATOM    385  O   GLU Z 453      11.792 -54.933 136.169  0.65 55.51           O  
ATOM    386  CB  GLU Z 453       9.613 -55.904 138.377  0.65 55.43           C  
ATOM    387  CG  GLU Z 453       8.370 -55.081 138.031  0.65 55.61           C  
ATOM    388  CD  GLU Z 453       7.917 -54.156 139.154  0.65 55.78           C  
ATOM    389  OE1 GLU Z 453       8.580 -54.111 140.213  0.65 55.73           O  
ATOM    390  OE2 GLU Z 453       6.885 -53.473 138.974  0.65 55.80           O  
ATOM    391  N   GLU Z 454      10.524 -53.229 136.915  0.65 55.59           N  
ATOM    392  CA  GLU Z 454      10.611 -52.477 135.664  0.65 55.76           C  
ATOM    393  C   GLU Z 454      12.026 -52.001 135.339  0.65 56.20           C  
ATOM    394  O   GLU Z 454      12.419 -50.893 135.709  0.65 56.21           O  
ATOM    395  CB  GLU Z 454       9.672 -51.264 135.697  0.65 55.50           C  
ATOM    396  CG  GLU Z 454       8.383 -51.471 136.485  0.65 55.19           C  
ATOM    397  CD  GLU Z 454       8.549 -51.168 137.970  0.65 54.81           C  
ATOM    398  OE1 GLU Z 454       9.403 -51.803 138.626  0.65 54.59           O  
ATOM    399  OE2 GLU Z 454       7.822 -50.287 138.478  0.65 54.60           O  
ATOM    400  N   LYS Z 455      12.786 -52.846 134.648  0.65 56.60           N  
ATOM    401  CA  LYS Z 455      14.150 -52.511 134.243  0.65 56.89           C  
ATOM    402  C   LYS Z 455      14.159 -52.286 132.735  0.65 56.53           C  
ATOM    403  O   LYS Z 455      13.291 -52.796 132.022  0.65 56.54           O  
ATOM    404  CB  LYS Z 455      15.116 -53.643 134.609  0.65 57.32           C  
ATOM    405  CG  LYS Z 455      15.522 -53.669 136.081  0.65 57.56           C  
ATOM    406  CD  LYS Z 455      16.205 -54.983 136.451  0.65 57.67           C  
ATOM    407  CE  LYS Z 455      17.410 -55.275 135.567  0.65 57.55           C  
ATOM    408  NZ  LYS Z 455      18.005 -56.607 135.876  0.65 57.45           N  
ATOM    409  N   ILE Z 456      15.136 -51.528 132.247  0.65 56.13           N  
ATOM    410  CA  ILE Z 456      15.217 -51.243 130.821  0.65 55.67           C  
ATOM    411  C   ILE Z 456      16.271 -52.083 130.107  0.65 55.16           C  
ATOM    412  O   ILE Z 456      15.946 -52.839 129.188  0.65 55.20           O  
ATOM    413  CB  ILE Z 456      15.520 -49.749 130.566  0.65 55.66           C  
ATOM    414  CG1 ILE Z 456      14.559 -48.871 131.380  0.65 55.69           C  
ATOM    415  CG2 ILE Z 456      15.389 -49.444 129.074  0.65 55.46           C  
ATOM    416  CD1 ILE Z 456      13.078 -49.116 131.093  0.65 55.58           C  
ATOM    417  N   SER Z 457      17.528 -51.945 130.529  0.65 54.40           N  
ATOM    418  CA  SER Z 457      18.635 -52.689 129.928  0.65 53.59           C  
ATOM    419  C   SER Z 457      18.441 -52.821 128.417  0.65 52.85           C  
ATOM    420  O   SER Z 457      18.414 -53.931 127.879  0.65 52.78           O  
ATOM    421  CB  SER Z 457      18.739 -54.083 130.561  0.65 53.43           C  
ATOM    422  OG  SER Z 457      17.541 -54.822 130.383  0.65 53.27           O  
ATOM    423  N   GLU Z 458      18.310 -51.684 127.736  0.65 52.06           N  
ATOM    424  CA  GLU Z 458      18.093 -51.687 126.294  0.65 51.09           C  
ATOM    425  C   GLU Z 458      19.330 -51.318 125.472  0.65 49.97           C  
ATOM    426  O   GLU Z 458      20.378 -50.966 126.019  0.65 49.72           O  
ATOM    427  CB  GLU Z 458      16.931 -50.750 125.945  0.65 51.21           C  
ATOM    428  CG  GLU Z 458      16.320 -51.012 124.577  0.65 51.36           C  
ATOM    429  CD  GLU Z 458      15.983 -52.480 124.369  0.65 51.64           C  
ATOM    430  OE1 GLU Z 458      15.190 -53.032 125.164  0.65 51.72           O  
ATOM    431  OE2 GLU Z 458      16.515 -53.083 123.412  0.65 51.70           O  
ATOM    432  N   ASP Z 459      19.192 -51.404 124.151  0.65 49.05           N  
ATOM    433  CA  ASP Z 459      20.284 -51.103 123.233  0.65 48.16           C  
ATOM    434  C   ASP Z 459      20.000 -49.902 122.332  0.65 46.59           C  
ATOM    435  O   ASP Z 459      20.389 -49.895 121.162  0.65 46.50           O  
ATOM    436  CB  ASP Z 459      20.580 -52.329 122.362  0.65 48.83           C  
ATOM    437  CG  ASP Z 459      21.041 -53.528 123.173  0.65 49.42           C  
ATOM    438  OD1 ASP Z 459      22.145 -53.462 123.758  0.65 49.57           O  
ATOM    439  OD2 ASP Z 459      20.300 -54.535 123.226  0.65 49.52           O  
ATOM    440  N   THR Z 460      19.330 -48.889 122.872  0.65 45.16           N  
ATOM    441  CA  THR Z 460      19.014 -47.693 122.094  0.65 43.79           C  
ATOM    442  C   THR Z 460      19.911 -46.516 122.469  0.65 41.75           C  
ATOM    443  O   THR Z 460      20.525 -46.506 123.535  0.65 41.25           O  
ATOM    444  CB  THR Z 460      17.540 -47.274 122.283  0.65 44.27           C  
ATOM    445  OG1 THR Z 460      17.266 -47.090 123.679  0.65 44.26           O  
ATOM    446  CG2 THR Z 460      16.608 -48.340 121.714  0.65 44.61           C  
ATOM    447  N   ALA Z 461      19.988 -45.530 121.581  0.65 40.50           N  
ATOM    448  CA  ALA Z 461      20.805 -44.345 121.823  0.65 39.38           C  
ATOM    449  C   ALA Z 461      20.203 -43.522 122.962  0.65 38.52           C  
ATOM    450  O   ALA Z 461      20.883 -43.200 123.935  0.65 38.45           O  
ATOM    451  CB  ALA Z 461      20.893 -43.507 120.553  0.65 38.96           C  
ATOM    452  N   ILE Z 462      18.922 -43.191 122.832  0.65 37.79           N  
ATOM    453  CA  ILE Z 462      18.215 -42.413 123.847  0.65 37.14           C  
ATOM    454  C   ILE Z 462      17.471 -43.346 124.801  0.65 36.31           C  
ATOM    455  O   ILE Z 462      16.590 -44.100 124.386  0.65 36.14           O  
ATOM    456  CB  ILE Z 462      17.198 -41.442 123.198  0.65 37.13           C  
ATOM    457  CG1 ILE Z 462      17.931 -40.463 122.274  0.65 37.02           C  
ATOM    458  CG2 ILE Z 462      16.433 -40.688 124.278  0.65 37.14           C  
ATOM    459  CD1 ILE Z 462      17.021 -39.497 121.540  0.65 36.86           C  
ATOM    460  N   LEU Z 463      17.828 -43.289 126.080  0.65 35.92           N  
ATOM    461  CA  LEU Z 463      17.198 -44.136 127.089  0.65 35.77           C  
ATOM    462  C   LEU Z 463      15.930 -43.524 127.682  0.65 36.33           C  
ATOM    463  O   LEU Z 463      15.936 -42.385 128.145  0.65 36.27           O  
ATOM    464  CB  LEU Z 463      18.187 -44.434 128.223  0.65 34.90           C  
ATOM    465  CG  LEU Z 463      17.619 -45.257 129.387  0.65 34.16           C  
ATOM    466  CD1 LEU Z 463      17.149 -46.600 128.860  0.65 33.81           C  
ATOM    467  CD2 LEU Z 463      18.672 -45.447 130.475  0.65 33.88           C  
ATOM    468  N   LYS Z 464      14.847 -44.295 127.669  0.65 37.34           N  
ATOM    469  CA  LYS Z 464      13.572 -43.847 128.218  0.65 38.50           C  
ATOM    470  C   LYS Z 464      13.237 -44.592 129.508  0.65 39.31           C  
ATOM    471  O   LYS Z 464      12.945 -45.789 129.490  0.65 39.54           O  
ATOM    472  CB  LYS Z 464      12.444 -44.056 127.203  0.65 38.87           C  
ATOM    473  CG  LYS Z 464      12.449 -43.069 126.045  0.65 39.43           C  
ATOM    474  CD  LYS Z 464      11.197 -43.225 125.187  0.65 39.95           C  
ATOM    475  CE  LYS Z 464      11.142 -42.176 124.083  0.65 40.21           C  
ATOM    476  NZ  LYS Z 464       9.914 -42.304 123.243  0.65 40.21           N  
ATOM    477  N   LEU Z 465      13.280 -43.876 130.625  0.65 39.90           N  
ATOM    478  CA  LEU Z 465      12.974 -44.465 131.924  0.65 40.41           C  
ATOM    479  C   LEU Z 465      11.567 -44.083 132.359  0.65 41.34           C  
ATOM    480  O   LEU Z 465      11.197 -42.908 132.339  0.65 41.39           O  
ATOM    481  CB  LEU Z 465      13.973 -43.980 132.975  0.65 39.92           C  
ATOM    482  CG  LEU Z 465      15.444 -44.327 132.747  0.65 39.35           C  
ATOM    483  CD1 LEU Z 465      16.293 -43.573 133.759  0.65 39.28           C  
ATOM    484  CD2 LEU Z 465      15.649 -45.834 132.868  0.65 39.04           C  
ATOM    485  N   SER Z 466      10.787 -45.083 132.754  0.65 41.97           N  
ATOM    486  CA  SER Z 466       9.420 -44.860 133.201  0.65 42.29           C  
ATOM    487  C   SER Z 466       9.158 -45.676 134.462  0.65 42.95           C  
ATOM    488  O   SER Z 466       9.970 -46.523 134.839  0.65 43.00           O  
ATOM    489  CB  SER Z 466       8.433 -45.268 132.105  0.65 41.94           C  
ATOM    490  OG  SER Z 466       8.563 -46.642 131.784  0.65 41.77           O  
ATOM    491  N   LYS Z 467       8.025 -45.415 135.109  0.65 43.47           N  
ATOM    492  CA  LYS Z 467       7.654 -46.131 136.325  0.65 44.19           C  
ATOM    493  C   LYS Z 467       8.795 -46.096 137.336  0.65 44.13           C  
ATOM    494  O   LYS Z 467       9.166 -47.124 137.906  0.65 43.93           O  
ATOM    495  CB  LYS Z 467       7.305 -47.583 135.990  0.65 45.22           C  
ATOM    496  CG  LYS Z 467       6.170 -47.729 134.987  0.65 46.20           C  
ATOM    497  CD  LYS Z 467       5.850 -49.192 134.724  0.65 47.01           C  
ATOM    498  CE  LYS Z 467       4.673 -49.337 133.768  0.65 47.48           C  
ATOM    499  NZ  LYS Z 467       4.292 -50.765 133.566  0.65 47.69           N  
ATOM    500  N   LEU Z 468       9.343 -44.906 137.554  0.65 44.34           N  
ATOM    501  CA  LEU Z 468      10.453 -44.736 138.481  0.65 44.69           C  
ATOM    502  C   LEU Z 468       9.994 -44.412 139.900  0.65 44.66           C  
ATOM    503  O   LEU Z 468       9.364 -43.381 140.142  0.65 44.76           O  
ATOM    504  CB  LEU Z 468      11.388 -43.627 137.981  0.65 44.80           C  
ATOM    505  CG  LEU Z 468      11.944 -43.780 136.559  0.65 44.86           C  
ATOM    506  CD1 LEU Z 468      12.730 -42.533 136.181  0.65 44.95           C  
ATOM    507  CD2 LEU Z 468      12.826 -45.020 136.473  0.65 44.78           C  
ATOM    508  N   VAL Z 469      10.313 -45.301 140.835  0.65 44.50           N  
ATOM    509  CA  VAL Z 469       9.959 -45.097 142.233  0.65 44.49           C  
ATOM    510  C   VAL Z 469      11.044 -44.218 142.856  0.65 44.84           C  
ATOM    511  O   VAL Z 469      12.148 -44.113 142.323  0.65 44.83           O  
ATOM    512  CB  VAL Z 469       9.883 -46.443 143.001  0.65 44.12           C  
ATOM    513  CG1 VAL Z 469       8.832 -47.341 142.374  0.65 43.92           C  
ATOM    514  CG2 VAL Z 469      11.241 -47.132 142.993  0.65 44.17           C  
ATOM    515  N   PRO Z 470      10.745 -43.572 143.992  0.65 45.24           N  
ATOM    516  CA  PRO Z 470      11.746 -42.712 144.634  0.65 45.39           C  
ATOM    517  C   PRO Z 470      13.040 -43.433 145.027  0.65 45.48           C  
ATOM    518  O   PRO Z 470      13.023 -44.613 145.385  0.65 45.51           O  
ATOM    519  CB  PRO Z 470      10.995 -42.151 145.841  0.65 45.45           C  
ATOM    520  CG  PRO Z 470      10.026 -43.256 146.175  0.65 45.48           C  
ATOM    521  CD  PRO Z 470       9.522 -43.658 144.809  0.65 45.33           C  
ATOM    522  N   GLY Z 471      14.156 -42.710 144.955  0.65 45.41           N  
ATOM    523  CA  GLY Z 471      15.445 -43.283 145.305  0.65 45.37           C  
ATOM    524  C   GLY Z 471      16.580 -42.773 144.432  0.65 45.25           C  
ATOM    525  O   GLY Z 471      16.419 -41.794 143.703  0.65 45.16           O  
ATOM    526  N   ASN Z 472      17.732 -43.434 144.510  0.65 45.26           N  
ATOM    527  CA  ASN Z 472      18.895 -43.044 143.716  0.65 45.26           C  
ATOM    528  C   ASN Z 472      19.211 -44.089 142.655  0.65 44.85           C  
ATOM    529  O   ASN Z 472      19.159 -45.293 142.916  0.65 44.94           O  
ATOM    530  CB  ASN Z 472      20.120 -42.846 144.609  0.65 45.68           C  
ATOM    531  CG  ASN Z 472      19.936 -41.724 145.609  0.65 46.12           C  
ATOM    532  OD1 ASN Z 472      19.538 -40.615 145.248  0.65 46.26           O  
ATOM    533  ND2 ASN Z 472      20.235 -42.004 146.875  0.65 46.30           N  
ATOM    534  N   TYR Z 473      19.540 -43.617 141.457  0.65 44.10           N  
ATOM    535  CA  TYR Z 473      19.855 -44.498 140.341  0.65 43.12           C  
ATOM    536  C   TYR Z 473      21.209 -44.155 139.730  0.65 42.61           C  
ATOM    537  O   TYR Z 473      21.704 -43.035 139.861  0.65 42.55           O  
ATOM    538  CB  TYR Z 473      18.780 -44.381 139.253  0.65 42.71           C  
ATOM    539  CG  TYR Z 473      17.374 -44.724 139.701  0.65 42.28           C  
ATOM    540  CD1 TYR Z 473      16.748 -44.009 140.725  0.65 42.13           C  
ATOM    541  CD2 TYR Z 473      16.662 -45.754 139.086  0.65 42.11           C  
ATOM    542  CE1 TYR Z 473      15.446 -44.313 141.126  0.65 42.09           C  
ATOM    543  CE2 TYR Z 473      15.359 -46.066 139.478  0.65 41.98           C  
ATOM    544  CZ  TYR Z 473      14.758 -45.342 140.497  0.65 41.98           C  
ATOM    545  OH  TYR Z 473      13.475 -45.648 140.888  0.65 41.84           O  
ATOM    546  N   THR Z 474      21.799 -45.136 139.058  0.65 42.14           N  
ATOM    547  CA  THR Z 474      23.081 -44.962 138.391  0.65 41.37           C  
ATOM    548  C   THR Z 474      23.076 -45.860 137.162  0.65 40.38           C  
ATOM    549  O   THR Z 474      23.002 -47.084 137.273  0.65 40.12           O  
ATOM    550  CB  THR Z 474      24.261 -45.349 139.305  0.65 41.33           C  
ATOM    551  OG1 THR Z 474      24.227 -44.549 140.493  0.65 41.41           O  
ATOM    552  CG2 THR Z 474      25.588 -45.115 138.586  0.65 41.17           C  
ATOM    553  N   PHE Z 475      23.142 -45.238 135.991  0.65 39.75           N  
ATOM    554  CA  PHE Z 475      23.128 -45.972 134.734  0.65 39.18           C  
ATOM    555  C   PHE Z 475      24.468 -45.873 134.025  0.65 38.61           C  
ATOM    556  O   PHE Z 475      25.068 -44.799 133.948  0.65 38.71           O  
ATOM    557  CB  PHE Z 475      22.019 -45.424 133.836  0.65 39.37           C  
ATOM    558  CG  PHE Z 475      20.648 -45.526 134.442  0.65 39.62           C  
ATOM    559  CD1 PHE Z 475      19.888 -46.683 134.288  0.65 39.85           C  
ATOM    560  CD2 PHE Z 475      20.127 -44.474 135.194  0.65 39.71           C  
ATOM    561  CE1 PHE Z 475      18.625 -46.794 134.874  0.65 40.03           C  
ATOM    562  CE2 PHE Z 475      18.867 -44.572 135.786  0.65 39.91           C  
ATOM    563  CZ  PHE Z 475      18.112 -45.735 135.626  0.65 40.06           C  
ATOM    564  N   SER Z 476      24.936 -47.002 133.507  0.65 37.77           N  
ATOM    565  CA  SER Z 476      26.206 -47.043 132.801  0.65 36.86           C  
ATOM    566  C   SER Z 476      25.980 -47.254 131.308  0.65 35.63           C  
ATOM    567  O   SER Z 476      25.407 -48.263 130.891  0.65 35.52           O  
ATOM    568  CB  SER Z 476      27.084 -48.166 133.362  0.65 37.01           C  
ATOM    569  OG  SER Z 476      28.376 -48.147 132.777  0.65 37.16           O  
ATOM    570  N   LEU Z 477      26.426 -46.290 130.510  0.65 34.44           N  
ATOM    571  CA  LEU Z 477      26.287 -46.370 129.064  0.65 33.37           C  
ATOM    572  C   LEU Z 477      27.580 -46.889 128.447  0.65 33.11           C  
ATOM    573  O   LEU Z 477      28.667 -46.401 128.757  0.65 33.08           O  
ATOM    574  CB  LEU Z 477      25.955 -44.992 128.482  0.65 32.64           C  
ATOM    575  CG  LEU Z 477      26.005 -44.866 126.956  0.65 31.95           C  
ATOM    576  CD1 LEU Z 477      25.036 -45.848 126.308  0.65 31.57           C  
ATOM    577  CD2 LEU Z 477      25.672 -43.437 126.564  0.65 31.93           C  
ATOM    578  N   THR Z 478      27.454 -47.884 127.577  0.65 32.82           N  
ATOM    579  CA  THR Z 478      28.615 -48.466 126.918  0.65 32.88           C  
ATOM    580  C   THR Z 478      28.416 -48.479 125.403  0.65 32.62           C  
ATOM    581  O   THR Z 478      27.463 -49.077 124.900  0.65 32.36           O  
ATOM    582  CB  THR Z 478      28.862 -49.916 127.402  0.65 33.13           C  
ATOM    583  OG1 THR Z 478      28.989 -49.931 128.830  0.65 33.30           O  
ATOM    584  CG2 THR Z 478      30.135 -50.475 126.788  0.65 33.46           C  
ATOM    585  N   VAL Z 479      29.307 -47.807 124.682  0.65 32.70           N  
ATOM    586  CA  VAL Z 479      29.227 -47.768 123.226  0.65 32.90           C  
ATOM    587  C   VAL Z 479      30.312 -48.650 122.618  0.65 33.15           C  
ATOM    588  O   VAL Z 479      31.396 -48.794 123.183  0.65 33.16           O  
ATOM    589  CB  VAL Z 479      29.374 -46.329 122.684  0.65 32.55           C  
ATOM    590  CG1 VAL Z 479      28.139 -45.518 123.041  0.65 32.28           C  
ATOM    591  CG2 VAL Z 479      30.623 -45.676 123.258  0.65 32.62           C  
ATOM    592  N   VAL Z 480      30.010 -49.244 121.468  0.65 33.28           N  
ATOM    593  CA  VAL Z 480      30.956 -50.122 120.797  0.65 33.55           C  
ATOM    594  C   VAL Z 480      31.343 -49.639 119.400  0.65 33.62           C  
ATOM    595  O   VAL Z 480      30.512 -49.152 118.631  0.65 33.15           O  
ATOM    596  CB  VAL Z 480      30.398 -51.563 120.703  0.65 33.89           C  
ATOM    597  CG1 VAL Z 480      31.374 -52.462 119.955  0.65 34.14           C  
ATOM    598  CG2 VAL Z 480      30.146 -52.109 122.101  0.65 33.88           C  
ATOM    599  N   ASP Z 481      32.627 -49.799 119.101  0.65 34.18           N  
ATOM    600  CA  ASP Z 481      33.249 -49.413 117.838  0.65 34.84           C  
ATOM    601  C   ASP Z 481      32.898 -50.414 116.738  0.65 35.58           C  
ATOM    602  O   ASP Z 481      32.202 -51.401 116.976  0.65 35.62           O  
ATOM    603  CB  ASP Z 481      34.767 -49.424 118.026  0.65 34.92           C  
ATOM    604  CG  ASP Z 481      35.465 -48.326 117.273  0.65 35.18           C  
ATOM    605  OD1 ASP Z 481      35.227 -48.167 116.055  0.65 35.39           O  
ATOM    606  OD2 ASP Z 481      36.274 -47.626 117.916  0.65 35.20           O  
ATOM    607  N   SER Z 482      33.407 -50.159 115.538  0.65 36.35           N  
ATOM    608  CA  SER Z 482      33.196 -51.049 114.404  0.65 37.06           C  
ATOM    609  C   SER Z 482      34.317 -52.089 114.471  0.65 37.93           C  
ATOM    610  O   SER Z 482      34.277 -53.121 113.794  0.65 37.96           O  
ATOM    611  CB  SER Z 482      33.291 -50.267 113.093  0.65 36.97           C  
ATOM    612  OG  SER Z 482      32.396 -49.167 113.088  0.65 36.85           O  
ATOM    613  N   ASP Z 483      35.314 -51.793 115.301  0.65 38.44           N  
ATOM    614  CA  ASP Z 483      36.466 -52.665 115.502  0.65 39.00           C  
ATOM    615  C   ASP Z 483      36.268 -53.514 116.754  0.65 38.78           C  
ATOM    616  O   ASP Z 483      36.895 -54.563 116.912  0.65 38.90           O  
ATOM    617  CB  ASP Z 483      37.741 -51.831 115.657  0.65 39.81           C  
ATOM    618  CG  ASP Z 483      38.115 -51.087 114.387  0.65 40.54           C  
ATOM    619  OD1 ASP Z 483      37.267 -50.329 113.866  0.65 40.75           O  
ATOM    620  OD2 ASP Z 483      39.261 -51.256 113.912  0.65 40.63           O  
ATOM    621  N   GLY Z 484      35.395 -53.051 117.643  0.65 38.28           N  
ATOM    622  CA  GLY Z 484      35.134 -53.779 118.871  0.65 37.60           C  
ATOM    623  C   GLY Z 484      35.576 -53.013 120.104  0.65 37.05           C  
ATOM    624  O   GLY Z 484      35.411 -53.486 121.229  0.65 37.06           O  
ATOM    625  N   ALA Z 485      36.146 -51.829 119.894  0.65 36.51           N  
ATOM    626  CA  ALA Z 485      36.602 -50.994 120.999  0.65 35.91           C  
ATOM    627  C   ALA Z 485      35.385 -50.442 121.735  0.65 35.71           C  
ATOM    628  O   ALA Z 485      34.361 -50.147 121.118  0.65 35.60           O  
ATOM    629  CB  ALA Z 485      37.463 -49.855 120.473  0.65 35.85           C  
ATOM    630  N   THR Z 486      35.493 -50.304 123.054  0.65 35.59           N  
ATOM    631  CA  THR Z 486      34.379 -49.798 123.848  0.65 35.23           C  
ATOM    632  C   THR Z 486      34.782 -48.710 124.836  0.65 35.31           C  
ATOM    633  O   THR Z 486      35.966 -48.438 125.044  0.65 35.29           O  
ATOM    634  CB  THR Z 486      33.696 -50.933 124.648  0.65 35.08           C  
ATOM    635  OG1 THR Z 486      34.596 -51.420 125.651  0.65 34.95           O  
ATOM    636  CG2 THR Z 486      33.300 -52.082 123.727  0.65 35.19           C  
ATOM    637  N   ASN Z 487      33.773 -48.095 125.443  0.65 35.46           N  
ATOM    638  CA  ASN Z 487      33.973 -47.042 126.428  0.65 35.60           C  
ATOM    639  C   ASN Z 487      32.688 -46.911 127.229  0.65 35.75           C  
ATOM    640  O   ASN Z 487      31.598 -47.147 126.708  0.65 35.74           O  
ATOM    641  CB  ASN Z 487      34.305 -45.716 125.738  0.65 35.57           C  
ATOM    642  CG  ASN Z 487      34.525 -44.584 126.722  0.65 35.59           C  
ATOM    643  OD1 ASN Z 487      33.579 -44.080 127.327  0.65 35.83           O  
ATOM    644  ND2 ASN Z 487      35.780 -44.182 126.893  0.65 35.45           N  
ATOM    645  N   SER Z 488      32.815 -46.539 128.496  0.65 36.02           N  
ATOM    646  CA  SER Z 488      31.643 -46.403 129.350  0.65 35.95           C  
ATOM    647  C   SER Z 488      31.624 -45.085 130.111  0.65 36.20           C  
ATOM    648  O   SER Z 488      32.664 -44.461 130.327  0.65 36.18           O  
ATOM    649  CB  SER Z 488      31.587 -47.571 130.340  0.65 35.50           C  
ATOM    650  OG  SER Z 488      31.687 -48.814 129.664  0.65 35.20           O  
ATOM    651  N   THR Z 489      30.426 -44.669 130.505  0.65 36.75           N  
ATOM    652  CA  THR Z 489      30.230 -43.440 131.264  0.65 37.40           C  
ATOM    653  C   THR Z 489      28.971 -43.615 132.109  0.65 38.18           C  
ATOM    654  O   THR Z 489      27.999 -44.235 131.670  0.65 38.01           O  
ATOM    655  CB  THR Z 489      30.068 -42.212 130.336  0.65 37.40           C  
ATOM    656  OG1 THR Z 489      29.991 -41.021 131.130  0.65 37.38           O  
ATOM    657  CG2 THR Z 489      28.806 -42.338 129.491  0.65 37.50           C  
ATOM    658  N   THR Z 490      28.991 -43.070 133.320  0.65 39.10           N  
ATOM    659  CA  THR Z 490      27.861 -43.199 134.234  0.65 39.94           C  
ATOM    660  C   THR Z 490      26.941 -41.982 134.315  0.65 40.34           C  
ATOM    661  O   THR Z 490      27.377 -40.841 134.154  0.65 40.27           O  
ATOM    662  CB  THR Z 490      28.356 -43.544 135.659  0.65 40.12           C  
ATOM    663  OG1 THR Z 490      27.306 -43.309 136.605  0.65 40.08           O  
ATOM    664  CG2 THR Z 490      29.569 -42.702 136.019  0.65 40.37           C  
ATOM    665  N   ALA Z 491      25.662 -42.249 134.569  0.65 40.83           N  
ATOM    666  CA  ALA Z 491      24.646 -41.209 134.692  0.65 41.43           C  
ATOM    667  C   ALA Z 491      23.966 -41.324 136.053  0.65 42.07           C  
ATOM    668  O   ALA Z 491      23.758 -42.430 136.558  0.65 42.24           O  
ATOM    669  CB  ALA Z 491      23.611 -41.354 133.580  0.65 41.41           C  
ATOM    670  N   ASN Z 492      23.625 -40.185 136.648  0.65 42.50           N  
ATOM    671  CA  ASN Z 492      22.966 -40.177 137.950  0.65 43.02           C  
ATOM    672  C   ASN Z 492      21.525 -39.685 137.859  0.65 43.39           C  
ATOM    673  O   ASN Z 492      21.230 -38.708 137.171  0.65 43.30           O  
ATOM    674  CB  ASN Z 492      23.743 -39.305 138.940  0.65 43.28           C  
ATOM    675  CG  ASN Z 492      25.075 -39.915 139.333  0.65 43.68           C  
ATOM    676  OD1 ASN Z 492      25.126 -41.005 139.909  0.65 43.81           O  
ATOM    677  ND2 ASN Z 492      26.162 -39.217 139.023  0.65 43.75           N  
ATOM    678  N   LEU Z 493      20.636 -40.377 138.563  0.65 43.85           N  
ATOM    679  CA  LEU Z 493      19.220 -40.038 138.586  0.65 44.15           C  
ATOM    680  C   LEU Z 493      18.691 -40.092 140.013  0.65 44.83           C  
ATOM    681  O   LEU Z 493      18.999 -41.018 140.766  0.65 44.93           O  
ATOM    682  CB  LEU Z 493      18.429 -41.013 137.706  0.65 43.93           C  
ATOM    683  CG  LEU Z 493      16.899 -41.021 137.838  0.65 43.85           C  
ATOM    684  CD1 LEU Z 493      16.329 -39.661 137.478  0.65 43.77           C  
ATOM    685  CD2 LEU Z 493      16.319 -42.094 136.929  0.65 43.83           C  
ATOM    686  N   THR Z 494      17.896 -39.093 140.380  0.65 45.23           N  
ATOM    687  CA  THR Z 494      17.308 -39.026 141.711  0.65 45.45           C  
ATOM    688  C   THR Z 494      15.806 -38.785 141.601  0.65 45.63           C  
ATOM    689  O   THR Z 494      15.366 -37.787 141.028  0.65 45.44           O  
ATOM    690  CB  THR Z 494      17.934 -37.888 142.549  0.65 45.40           C  
ATOM    691  OG1 THR Z 494      19.329 -38.154 142.748  0.65 45.28           O  
ATOM    692  CG2 THR Z 494      17.242 -37.778 143.904  0.65 45.47           C  
ATOM    693  N   VAL Z 495      15.024 -39.712 142.145  0.65 45.91           N  
ATOM    694  CA  VAL Z 495      13.574 -39.597 142.117  0.65 46.27           C  
ATOM    695  C   VAL Z 495      13.055 -39.350 143.528  0.65 46.74           C  
ATOM    696  O   VAL Z 495      13.023 -40.257 144.357  0.65 46.74           O  
ATOM    697  CB  VAL Z 495      12.920 -40.876 141.541  0.65 46.06           C  
ATOM    698  CG1 VAL Z 495      11.400 -40.772 141.630  0.65 46.05           C  
ATOM    699  CG2 VAL Z 495      13.349 -41.070 140.091  0.65 45.87           C  
ATOM    700  N   ASN Z 496      12.660 -38.110 143.799  0.65 47.46           N  
ATOM    701  CA  ASN Z 496      12.148 -37.746 145.115  0.65 48.05           C  
ATOM    702  C   ASN Z 496      10.640 -37.942 145.185  0.65 48.79           C  
ATOM    703  O   ASN Z 496       9.947 -37.864 144.169  0.65 48.73           O  
ATOM    704  CB  ASN Z 496      12.479 -36.284 145.429  0.65 47.73           C  
ATOM    705  CG  ASN Z 496      13.956 -35.980 145.306  0.65 47.53           C  
ATOM    706  OD1 ASN Z 496      14.794 -36.661 145.900  0.65 47.57           O  
ATOM    707  ND2 ASN Z 496      14.286 -34.947 144.537  0.65 47.36           N  
ATOM    708  N   LYS Z 497      10.135 -38.206 146.385  0.65 49.67           N  
ATOM    709  CA  LYS Z 497       8.700 -38.379 146.571  0.65 50.52           C  
ATOM    710  C   LYS Z 497       8.102 -36.979 146.670  0.65 51.28           C  
ATOM    711  O   LYS Z 497       8.826 -36.009 146.903  0.65 51.13           O  
ATOM    712  CB  LYS Z 497       8.414 -39.169 147.852  0.65 50.90           C  
ATOM    713  CG  LYS Z 497       8.893 -38.490 149.127  0.65 51.15           C  
ATOM    714  CD  LYS Z 497       8.559 -39.330 150.350  0.65 51.33           C  
ATOM    715  CE  LYS Z 497       8.946 -38.615 151.640  0.65 51.41           C  
ATOM    716  NZ  LYS Z 497       8.568 -39.394 152.858  0.65 51.51           N  
ATOM    717  N   ALA Z 498       6.789 -36.872 146.490  0.65 51.75           N  
ATOM    718  CA  ALA Z 498       6.115 -35.578 146.553  0.65 52.33           C  
ATOM    719  C   ALA Z 498       6.447 -34.827 147.843  0.65 52.86           C  
ATOM    720  O   ALA Z 498       7.031 -35.390 148.772  0.65 52.77           O  
ATOM    721  CB  ALA Z 498       4.606 -35.769 146.432  0.65 52.07           C  
ATOM    722  N   VAL Z 499       6.072 -33.552 147.891  0.65 53.67           N  
ATOM    723  CA  VAL Z 499       6.323 -32.717 149.061  0.65 53.90           C  
ATOM    724  C   VAL Z 499       5.025 -32.346 149.780  0.65 54.04           C  
ATOM    725  O   VAL Z 499       4.545 -31.204 149.607  0.65 53.18           O  
ATOM    726  CB  VAL Z 499       7.091 -31.424 148.675  0.65 53.71           C  
ATOM    727  CG1 VAL Z 499       8.531 -31.766 148.318  0.65 53.40           C  
ATOM    728  CG2 VAL Z 499       6.410 -30.735 147.498  0.65 53.46           C  
TER     729      VAL Z 499                                                      
ATOM    730  N   ASP A 237       2.642  -5.173  86.338  1.00 29.55           N  
ATOM    731  CA  ASP A 237       2.762  -6.656  86.491  1.00 29.01           C  
ATOM    732  C   ASP A 237       4.211  -7.143  86.433  1.00 25.98           C  
ATOM    733  O   ASP A 237       4.468  -8.338  86.303  1.00 25.23           O  
ATOM    734  CB  ASP A 237       1.923  -7.368  85.423  1.00 31.65           C  
ATOM    735  CG  ASP A 237       2.326  -6.988  84.003  1.00 34.34           C  
ATOM    736  OD1 ASP A 237       3.312  -7.554  83.479  1.00 34.82           O  
ATOM    737  OD2 ASP A 237       1.652  -6.113  83.407  1.00 35.50           O  
ATOM    738  N   ARG A 238       5.149  -6.208  86.540  1.00 24.35           N  
ATOM    739  CA  ARG A 238       6.577  -6.519  86.529  1.00 23.17           C  
ATOM    740  C   ARG A 238       7.325  -5.564  87.424  1.00 20.76           C  
ATOM    741  O   ARG A 238       6.968  -4.392  87.533  1.00 21.82           O  
ATOM    742  CB  ARG A 238       7.188  -6.375  85.129  1.00 25.51           C  
ATOM    743  CG  ARG A 238       6.910  -7.499  84.156  1.00 28.72           C  
ATOM    744  CD  ARG A 238       7.332  -8.850  84.728  1.00 31.62           C  
ATOM    745  NE  ARG A 238       7.304  -9.924  83.729  1.00 33.88           N  
ATOM    746  CZ  ARG A 238       6.217 -10.298  83.058  1.00 35.43           C  
ATOM    747  NH1 ARG A 238       5.058  -9.685  83.276  1.00 35.76           N  
ATOM    748  NH2 ARG A 238       6.288 -11.288  82.172  1.00 35.89           N  
ATOM    749  N   VAL A 239       8.363  -6.063  88.074  1.00 17.91           N  
ATOM    750  CA  VAL A 239       9.212  -5.220  88.887  1.00 15.37           C  
ATOM    751  C   VAL A 239      10.629  -5.753  88.711  1.00 14.35           C  
ATOM    752  O   VAL A 239      10.869  -6.953  88.805  1.00 13.87           O  
ATOM    753  CB  VAL A 239       8.794  -5.190  90.386  1.00 13.63           C  
ATOM    754  CG1 VAL A 239       8.919  -6.561  91.024  1.00 13.42           C  
ATOM    755  CG2 VAL A 239       9.651  -4.173  91.127  1.00 12.09           C  
ATOM    756  N   ILE A 240      11.560  -4.857  88.403  1.00 13.98           N  
ATOM    757  CA  ILE A 240      12.944  -5.248  88.195  1.00 13.13           C  
ATOM    758  C   ILE A 240      13.833  -4.754  89.317  1.00 11.75           C  
ATOM    759  O   ILE A 240      13.922  -3.559  89.578  1.00 12.93           O  
ATOM    760  CB  ILE A 240      13.472  -4.699  86.865  1.00 14.62           C  
ATOM    761  CG1 ILE A 240      12.621  -5.238  85.724  1.00 15.73           C  
ATOM    762  CG2 ILE A 240      14.932  -5.110  86.658  1.00 14.68           C  
ATOM    763  CD1 ILE A 240      12.900  -4.573  84.405  1.00 16.55           C  
ATOM    764  N   THR A 241      14.484  -5.683  89.993  1.00  9.95           N  
ATOM    765  CA  THR A 241      15.379  -5.319  91.067  1.00  9.89           C  
ATOM    766  C   THR A 241      16.796  -5.362  90.486  1.00 11.10           C  
ATOM    767  O   THR A 241      17.065  -6.107  89.543  1.00 10.56           O  
ATOM    768  CB  THR A 241      15.246  -6.307  92.276  1.00  7.84           C  
ATOM    769  OG1 THR A 241      15.466  -7.653  91.830  1.00  7.06           O  
ATOM    770  CG2 THR A 241      13.853  -6.206  92.912  1.00  6.71           C  
ATOM    771  N   THR A 242      17.688  -4.539  91.022  1.00 13.28           N  
ATOM    772  CA  THR A 242      19.077  -4.512  90.557  1.00 15.65           C  
ATOM    773  C   THR A 242      19.934  -4.278  91.776  1.00 15.14           C  
ATOM    774  O   THR A 242      19.636  -3.416  92.595  1.00 16.35           O  
ATOM    775  CB  THR A 242      19.338  -3.385  89.517  1.00 18.21           C  
ATOM    776  OG1 THR A 242      18.397  -3.488  88.435  1.00 18.22           O  
ATOM    777  CG2 THR A 242      20.754  -3.512  88.943  1.00 20.01           C  
ATOM    778  N   SER A 243      20.981  -5.076  91.919  1.00 14.84           N  
ATOM    779  CA  SER A 243      21.871  -4.960  93.062  1.00 13.99           C  
ATOM    780  C   SER A 243      23.320  -5.078  92.665  1.00 12.56           C  
ATOM    781  O   SER A 243      23.705  -6.017  91.972  1.00 12.59           O  
ATOM    782  CB  SER A 243      21.555  -6.037  94.096  1.00 14.90           C  
ATOM    783  OG  SER A 243      20.378  -5.698  94.800  1.00 16.38           O  
ATOM    784  N   THR A 244      24.119  -4.119  93.116  1.00 11.44           N  
ATOM    785  CA  THR A 244      25.539  -4.117  92.834  1.00 10.37           C  
ATOM    786  C   THR A 244      26.262  -4.124  94.166  1.00  8.14           C  
ATOM    787  O   THR A 244      25.849  -3.450  95.100  1.00  7.86           O  
ATOM    788  CB  THR A 244      25.955  -2.880  92.008  1.00 11.39           C  
ATOM    789  OG1 THR A 244      25.303  -2.920  90.731  1.00 11.97           O  
ATOM    790  CG2 THR A 244      27.466  -2.866  91.786  1.00 12.07           C  
ATOM    791  N   ARG A 245      27.323  -4.916  94.257  1.00  6.76           N  
ATOM    792  CA  ARG A 245      28.101  -5.010  95.482  1.00  6.78           C  
ATOM    793  C   ARG A 245      29.571  -5.180  95.141  1.00  6.21           C  
ATOM    794  O   ARG A 245      29.929  -5.518  94.006  1.00  5.21           O  
ATOM    795  CB  ARG A 245      27.654  -6.212  96.336  1.00  7.42           C  
ATOM    796  CG  ARG A 245      26.202  -6.214  96.801  1.00  8.61           C  
ATOM    797  CD  ARG A 245      25.943  -5.237  97.935  1.00  8.97           C  
ATOM    798  NE  ARG A 245      24.605  -5.408  98.498  1.00  9.56           N  
ATOM    799  CZ  ARG A 245      23.480  -5.000  97.917  1.00 10.07           C  
ATOM    800  NH1 ARG A 245      23.504  -4.380  96.747  1.00  9.71           N  
ATOM    801  NH2 ARG A 245      22.319  -5.223  98.509  1.00 11.37           N  
ATOM    802  N   THR A 246      30.420  -4.951  96.135  1.00  7.76           N  
ATOM    803  CA  THR A 246      31.858  -5.114  95.978  1.00  8.07           C  
ATOM    804  C   THR A 246      32.252  -6.361  96.768  1.00  7.39           C  
ATOM    805  O   THR A 246      31.944  -6.483  97.947  1.00  7.69           O  
ATOM    806  CB  THR A 246      32.647  -3.876  96.531  1.00  9.60           C  
ATOM    807  OG1 THR A 246      32.383  -2.736  95.711  1.00 10.02           O  
ATOM    808  CG2 THR A 246      34.148  -4.137  96.536  1.00  9.50           C  
ATOM    809  N   TRP A 247      32.937  -7.289  96.109  1.00  7.19           N  
ATOM    810  CA  TRP A 247      33.371  -8.521  96.757  1.00  5.84           C  
ATOM    811  C   TRP A 247      34.889  -8.629  96.820  1.00  6.78           C  
ATOM    812  O   TRP A 247      35.602  -7.970  96.070  1.00  7.46           O  
ATOM    813  CB  TRP A 247      32.823  -9.732  95.993  1.00  3.52           C  
ATOM    814  CG  TRP A 247      33.052  -9.649  94.507  1.00  2.14           C  
ATOM    815  CD1 TRP A 247      32.220  -9.092  93.585  1.00  2.47           C  
ATOM    816  CD2 TRP A 247      34.208 -10.107  93.775  1.00  1.18           C  
ATOM    817  NE1 TRP A 247      32.777  -9.170  92.328  1.00  1.31           N  
ATOM    818  CE2 TRP A 247      33.996  -9.786  92.419  1.00  0.77           C  
ATOM    819  CE3 TRP A 247      35.409 -10.755  94.143  1.00  0.68           C  
ATOM    820  CZ2 TRP A 247      34.933 -10.090  91.417  1.00  0.54           C  
ATOM    821  CZ3 TRP A 247      36.336 -11.050  93.155  1.00  0.00           C  
ATOM    822  CH2 TRP A 247      36.093 -10.719  91.807  1.00  0.00           C  
ATOM    823  N   ALA A 248      35.371  -9.473  97.723  1.00  7.36           N  
ATOM    824  CA  ALA A 248      36.796  -9.742  97.874  1.00  7.47           C  
ATOM    825  C   ALA A 248      36.926 -11.266  97.907  1.00  8.28           C  
ATOM    826  O   ALA A 248      36.259 -11.929  98.689  1.00  8.01           O  
ATOM    827  CB  ALA A 248      37.330  -9.151  99.167  1.00  6.56           C  
ATOM    828  N   LEU A 249      37.770 -11.814  97.040  1.00  9.13           N  
ATOM    829  CA  LEU A 249      37.990 -13.254  96.985  1.00  8.47           C  
ATOM    830  C   LEU A 249      39.424 -13.603  97.368  1.00  8.51           C  
ATOM    831  O   LEU A 249      40.360 -13.232  96.665  1.00  9.04           O  
ATOM    832  CB  LEU A 249      37.712 -13.772  95.571  1.00  6.87           C  
ATOM    833  CG  LEU A 249      38.095 -15.225  95.248  1.00  5.40           C  
ATOM    834  CD1 LEU A 249      37.163 -16.202  95.963  1.00  4.86           C  
ATOM    835  CD2 LEU A 249      38.059 -15.427  93.732  1.00  3.46           C  
ATOM    836  N   PRO A 250      39.622 -14.301  98.495  1.00  8.43           N  
ATOM    837  CA  PRO A 250      40.993 -14.672  98.893  1.00  9.34           C  
ATOM    838  C   PRO A 250      41.358 -15.966  98.168  1.00 11.33           C  
ATOM    839  O   PRO A 250      40.551 -16.492  97.393  1.00 12.01           O  
ATOM    840  CB  PRO A 250      40.860 -14.913 100.388  1.00  8.98           C  
ATOM    841  CG  PRO A 250      39.458 -15.522 100.483  1.00  8.24           C  
ATOM    842  CD  PRO A 250      38.638 -14.665  99.537  1.00  7.88           C  
ATOM    843  N   THR A 251      42.564 -16.484  98.369  1.00 12.22           N  
ATOM    844  CA  THR A 251      42.843 -17.771  97.761  1.00 12.85           C  
ATOM    845  C   THR A 251      42.505 -18.737  98.880  1.00  9.77           C  
ATOM    846  O   THR A 251      42.945 -18.562 100.016  1.00  9.67           O  
ATOM    847  CB  THR A 251      44.328 -17.989  97.327  1.00 16.30           C  
ATOM    848  OG1 THR A 251      45.158 -18.157  98.483  1.00 17.83           O  
ATOM    849  CG2 THR A 251      44.815 -16.818  96.478  1.00 16.65           C  
ATOM    850  N   TYR A 252      41.707 -19.746  98.567  1.00  8.77           N  
ATOM    851  CA  TYR A 252      41.314 -20.731  99.565  1.00  9.11           C  
ATOM    852  C   TYR A 252      42.154 -21.982  99.515  1.00  9.80           C  
ATOM    853  O   TYR A 252      42.607 -22.378  98.450  1.00  9.85           O  
ATOM    854  CB  TYR A 252      39.848 -21.120  99.363  1.00  7.42           C  
ATOM    855  CG  TYR A 252      38.863 -20.068  99.824  1.00  6.09           C  
ATOM    856  CD1 TYR A 252      38.784 -19.716 101.165  1.00  5.95           C  
ATOM    857  CD2 TYR A 252      37.987 -19.451  98.919  1.00  5.20           C  
ATOM    858  CE1 TYR A 252      37.853 -18.780 101.615  1.00  5.82           C  
ATOM    859  CE2 TYR A 252      37.050 -18.505  99.354  1.00  4.27           C  
ATOM    860  CZ  TYR A 252      36.994 -18.183 100.706  1.00  3.93           C  
ATOM    861  OH  TYR A 252      36.087 -17.270 101.167  1.00  3.28           O  
ATOM    862  N   ASN A 253      42.368 -22.596 100.674  1.00 11.77           N  
ATOM    863  CA  ASN A 253      43.095 -23.857 100.726  1.00 13.97           C  
ATOM    864  C   ASN A 253      44.507 -23.784 100.189  1.00 17.14           C  
ATOM    865  O   ASN A 253      45.165 -24.811 100.028  1.00 17.78           O  
ATOM    866  CB  ASN A 253      42.346 -24.903  99.895  1.00 13.17           C  
ATOM    867  CG  ASN A 253      41.273 -25.622 100.672  1.00 11.40           C  
ATOM    868  OD1 ASN A 253      41.175 -25.489 101.889  1.00 10.25           O  
ATOM    869  ND2 ASN A 253      40.475 -26.419  99.967  1.00 10.69           N  
ATOM    870  N   ASN A 254      44.968 -22.577  99.899  1.00 18.83           N  
ATOM    871  CA  ASN A 254      46.285 -22.392  99.328  1.00 19.11           C  
ATOM    872  C   ASN A 254      46.316 -23.101  97.969  1.00 16.31           C  
ATOM    873  O   ASN A 254      47.326 -23.679  97.582  1.00 17.43           O  
ATOM    874  CB  ASN A 254      47.355 -22.939 100.276  1.00 23.05           C  
ATOM    875  CG  ASN A 254      48.643 -22.141 100.210  1.00 27.04           C  
ATOM    876  OD1 ASN A 254      48.622 -20.901 100.250  1.00 28.27           O  
ATOM    877  ND2 ASN A 254      49.775 -22.837 100.109  1.00 28.28           N  
ATOM    878  N   HIS A 255      45.183 -23.047  97.267  1.00 13.97           N  
ATOM    879  CA  HIS A 255      44.990 -23.620  95.924  1.00 13.24           C  
ATOM    880  C   HIS A 255      44.698 -25.121  95.843  1.00 11.41           C  
ATOM    881  O   HIS A 255      44.489 -25.654  94.755  1.00 11.68           O  
ATOM    882  CB  HIS A 255      46.209 -23.321  95.042  1.00 14.62           C  
ATOM    883  CG  HIS A 255      46.602 -21.875  95.015  1.00 15.22           C  
ATOM    884  ND1 HIS A 255      45.904 -20.926  94.296  1.00 14.86           N  
ATOM    885  CD2 HIS A 255      47.611 -21.213  95.632  1.00 14.86           C  
ATOM    886  CE1 HIS A 255      46.467 -19.745  94.470  1.00 14.33           C  
ATOM    887  NE2 HIS A 255      47.505 -19.891  95.277  1.00 14.62           N  
ATOM    888  N   LEU A 256      44.667 -25.789  96.985  1.00 10.48           N  
ATOM    889  CA  LEU A 256      44.450 -27.230  97.042  1.00 10.56           C  
ATOM    890  C   LEU A 256      43.003 -27.703  97.217  1.00 10.36           C  
ATOM    891  O   LEU A 256      42.132 -26.950  97.642  1.00 10.93           O  
ATOM    892  CB  LEU A 256      45.265 -27.814  98.202  1.00 10.49           C  
ATOM    893  CG  LEU A 256      46.776 -27.589  98.278  1.00 10.58           C  
ATOM    894  CD1 LEU A 256      47.284 -27.903  99.691  1.00 11.20           C  
ATOM    895  CD2 LEU A 256      47.474 -28.444  97.249  1.00  9.86           C  
ATOM    896  N   TYR A 257      42.762 -28.962  96.864  1.00  9.08           N  
ATOM    897  CA  TYR A 257      41.467 -29.598  97.082  1.00  6.34           C  
ATOM    898  C   TYR A 257      41.824 -30.476  98.237  1.00  6.96           C  
ATOM    899  O   TYR A 257      42.886 -31.075  98.230  1.00  8.76           O  
ATOM    900  CB  TYR A 257      41.057 -30.492  95.935  1.00  4.61           C  
ATOM    901  CG  TYR A 257      40.494 -29.763  94.770  1.00  3.58           C  
ATOM    902  CD1 TYR A 257      41.321 -29.066  93.898  1.00  3.78           C  
ATOM    903  CD2 TYR A 257      39.125 -29.787  94.517  1.00  3.42           C  
ATOM    904  CE1 TYR A 257      40.786 -28.405  92.778  1.00  4.46           C  
ATOM    905  CE2 TYR A 257      38.588 -29.140  93.415  1.00  4.39           C  
ATOM    906  CZ  TYR A 257      39.426 -28.455  92.550  1.00  4.97           C  
ATOM    907  OH  TYR A 257      38.896 -27.835  91.443  1.00  6.37           O  
ATOM    908  N   LYS A 258      40.984 -30.546  99.246  1.00  8.54           N  
ATOM    909  CA  LYS A 258      41.306 -31.382 100.377  1.00 10.62           C  
ATOM    910  C   LYS A 258      40.106 -32.226 100.740  1.00 10.18           C  
ATOM    911  O   LYS A 258      38.969 -31.810 100.562  1.00  9.68           O  
ATOM    912  CB  LYS A 258      41.673 -30.531 101.589  1.00 13.35           C  
ATOM    913  CG  LYS A 258      42.732 -29.485 101.361  1.00 16.07           C  
ATOM    914  CD  LYS A 258      43.143 -28.902 102.711  1.00 18.26           C  
ATOM    915  CE  LYS A 258      44.111 -27.740 102.559  1.00 20.20           C  
ATOM    916  NZ  LYS A 258      44.606 -27.294 103.902  1.00 21.34           N  
ATOM    917  N   GLN A 259      40.368 -33.418 101.248  1.00 10.72           N  
ATOM    918  CA  GLN A 259      39.304 -34.285 101.686  1.00 11.27           C  
ATOM    919  C   GLN A 259      38.987 -33.836 103.102  1.00 11.69           C  
ATOM    920  O   GLN A 259      39.895 -33.583 103.897  1.00 12.45           O  
ATOM    921  CB  GLN A 259      39.773 -35.734 101.698  1.00 12.05           C  
ATOM    922  CG  GLN A 259      38.908 -36.665 102.532  1.00 12.45           C  
ATOM    923  CD  GLN A 259      39.632 -37.939 102.905  1.00 13.47           C  
ATOM    924  OE1 GLN A 259      39.657 -38.335 104.072  1.00 13.79           O  
ATOM    925  NE2 GLN A 259      40.225 -38.596 101.908  1.00 13.44           N  
ATOM    926  N   ILE A 260      37.704 -33.713 103.419  1.00 12.22           N  
ATOM    927  CA  ILE A 260      37.302 -33.306 104.761  1.00 13.46           C  
ATOM    928  C   ILE A 260      36.301 -34.304 105.272  1.00 14.54           C  
ATOM    929  O   ILE A 260      35.523 -34.866 104.505  1.00 15.76           O  
ATOM    930  CB  ILE A 260      36.656 -31.897 104.773  1.00 13.36           C  
ATOM    931  CG1 ILE A 260      35.450 -31.869 103.822  1.00 11.97           C  
ATOM    932  CG2 ILE A 260      37.695 -30.849 104.387  1.00 13.99           C  
ATOM    933  CD1 ILE A 260      34.696 -30.593 103.813  1.00 11.08           C  
ATOM    934  N   SER A 261      36.324 -34.546 106.567  1.00 15.91           N  
ATOM    935  CA  SER A 261      35.387 -35.483 107.139  1.00 18.16           C  
ATOM    936  C   SER A 261      35.272 -35.209 108.617  1.00 21.07           C  
ATOM    937  O   SER A 261      35.936 -34.320 109.145  1.00 21.84           O  
ATOM    938  CB  SER A 261      35.847 -36.930 106.879  1.00 17.92           C  
ATOM    939  OG  SER A 261      37.077 -37.222 107.516  1.00 18.18           O  
ATOM    940  N   SER A 262      34.404 -35.958 109.278  1.00 24.39           N  
ATOM    941  CA  SER A 262      34.201 -35.823 110.710  1.00 28.16           C  
ATOM    942  C   SER A 262      35.119 -36.819 111.419  1.00 33.14           C  
ATOM    943  O   SER A 262      34.990 -37.052 112.618  1.00 33.77           O  
ATOM    944  CB  SER A 262      32.740 -36.126 111.045  1.00 26.94           C  
ATOM    945  OG  SER A 262      32.342 -37.378 110.509  1.00 25.87           O  
ATOM    946  N   GLN A 263      36.059 -37.381 110.662  1.00 37.70           N  
ATOM    947  CA  GLN A 263      37.004 -38.392 111.153  1.00 42.45           C  
ATOM    948  C   GLN A 263      37.810 -38.061 112.412  1.00 44.44           C  
ATOM    949  O   GLN A 263      38.743 -38.784 112.769  1.00 44.69           O  
ATOM    950  CB  GLN A 263      37.967 -38.775 110.029  1.00 45.18           C  
ATOM    951  CG  GLN A 263      38.646 -40.121 110.221  1.00 47.73           C  
ATOM    952  CD  GLN A 263      39.471 -40.541 109.010  1.00 50.02           C  
ATOM    953  OE1 GLN A 263      38.977 -40.545 107.874  1.00 50.54           O  
ATOM    954  NE2 GLN A 263      40.731 -40.906 109.250  1.00 50.43           N  
ATOM    955  N   SER A 264      37.465 -36.961 113.072  1.00 46.10           N  
ATOM    956  CA  SER A 264      38.140 -36.570 114.305  1.00 47.12           C  
ATOM    957  C   SER A 264      37.261 -37.047 115.454  1.00 47.16           C  
ATOM    958  O   SER A 264      37.589 -36.860 116.628  1.00 47.34           O  
ATOM    959  CB  SER A 264      38.307 -35.049 114.370  1.00 47.69           C  
ATOM    960  OG  SER A 264      39.069 -34.583 113.272  1.00 48.01           O  
ATOM    961  N   GLY A 265      36.141 -37.669 115.094  1.00 46.67           N  
ATOM    962  CA  GLY A 265      35.217 -38.170 116.089  1.00 46.47           C  
ATOM    963  C   GLY A 265      33.961 -37.325 116.145  1.00 45.92           C  
ATOM    964  O   GLY A 265      34.020 -36.116 116.389  1.00 46.42           O  
ATOM    965  N   ALA A 266      32.820 -37.966 115.914  1.00 44.60           N  
ATOM    966  CA  ALA A 266      31.533 -37.290 115.954  1.00 43.39           C  
ATOM    967  C   ALA A 266      30.451 -38.314 116.260  1.00 43.20           C  
ATOM    968  O   ALA A 266      30.726 -39.511 116.351  1.00 45.00           O  
ATOM    969  CB  ALA A 266      31.255 -36.614 114.620  1.00 43.36           C  
ATOM    970  N   SER A 267      29.227 -37.841 116.451  1.00 40.39           N  
ATOM    971  CA  SER A 267      28.110 -38.732 116.715  1.00 37.61           C  
ATOM    972  C   SER A 267      27.710 -39.322 115.372  1.00 35.25           C  
ATOM    973  O   SER A 267      28.116 -38.811 114.330  1.00 36.13           O  
ATOM    974  CB  SER A 267      26.944 -37.947 117.302  1.00 37.58           C  
ATOM    975  OG  SER A 267      27.328 -37.323 118.506  1.00 37.43           O  
ATOM    976  N   ASN A 268      26.919 -40.386 115.385  1.00 32.45           N  
ATOM    977  CA  ASN A 268      26.500 -40.996 114.137  1.00 30.62           C  
ATOM    978  C   ASN A 268      25.691 -40.018 113.298  1.00 28.80           C  
ATOM    979  O   ASN A 268      25.762 -40.040 112.067  1.00 29.37           O  
ATOM    980  CB  ASN A 268      25.674 -42.248 114.415  1.00 31.87           C  
ATOM    981  CG  ASN A 268      26.486 -43.350 115.063  1.00 32.31           C  
ATOM    982  OD1 ASN A 268      27.567 -43.109 115.599  1.00 32.11           O  
ATOM    983  ND2 ASN A 268      25.965 -44.573 115.021  1.00 32.64           N  
ATOM    984  N   ASP A 269      24.935 -39.149 113.964  1.00 25.99           N  
ATOM    985  CA  ASP A 269      24.118 -38.173 113.257  1.00 23.31           C  
ATOM    986  C   ASP A 269      24.929 -37.014 112.677  1.00 19.11           C  
ATOM    987  O   ASP A 269      24.446 -36.296 111.801  1.00 19.29           O  
ATOM    988  CB  ASP A 269      23.039 -37.622 114.189  1.00 24.31           C  
ATOM    989  CG  ASP A 269      22.158 -38.717 114.791  1.00 25.92           C  
ATOM    990  OD1 ASP A 269      21.761 -39.652 114.063  1.00 26.94           O  
ATOM    991  OD2 ASP A 269      21.839 -38.640 116.000  1.00 26.22           O  
ATOM    992  N   ASN A 270      26.163 -36.849 113.153  1.00 16.26           N  
ATOM    993  CA  ASN A 270      27.013 -35.760 112.693  1.00 14.23           C  
ATOM    994  C   ASN A 270      28.163 -36.140 111.770  1.00 13.65           C  
ATOM    995  O   ASN A 270      28.924 -35.271 111.370  1.00 14.63           O  
ATOM    996  CB  ASN A 270      27.574 -34.989 113.892  1.00 13.20           C  
ATOM    997  CG  ASN A 270      26.500 -34.251 114.657  1.00 12.27           C  
ATOM    998  OD1 ASN A 270      25.705 -33.537 114.068  1.00 10.43           O  
ATOM    999  ND2 ASN A 270      26.474 -34.421 115.982  1.00 12.68           N  
ATOM   1000  N   HIS A 271      28.300 -37.419 111.433  1.00 11.46           N  
ATOM   1001  CA  HIS A 271      29.376 -37.854 110.556  1.00  9.50           C  
ATOM   1002  C   HIS A 271      29.192 -37.375 109.136  1.00  8.80           C  
ATOM   1003  O   HIS A 271      28.073 -37.226 108.664  1.00 10.56           O  
ATOM   1004  CB  HIS A 271      29.485 -39.380 110.558  1.00  8.87           C  
ATOM   1005  CG  HIS A 271      30.209 -39.929 111.746  1.00  8.60           C  
ATOM   1006  ND1 HIS A 271      31.485 -39.530 112.084  1.00  8.76           N  
ATOM   1007  CD2 HIS A 271      29.847 -40.852 112.666  1.00  8.76           C  
ATOM   1008  CE1 HIS A 271      31.877 -40.185 113.161  1.00  8.59           C  
ATOM   1009  NE2 HIS A 271      30.902 -40.994 113.536  1.00  8.88           N  
ATOM   1010  N   TYR A 272      30.290 -37.120 108.447  1.00  8.36           N  
ATOM   1011  CA  TYR A 272      30.206 -36.684 107.071  1.00  8.69           C  
ATOM   1012  C   TYR A 272      31.521 -36.969 106.388  1.00  8.52           C  
ATOM   1013  O   TYR A 272      32.482 -37.377 107.032  1.00  9.77           O  
ATOM   1014  CB  TYR A 272      29.867 -35.185 106.974  1.00  9.61           C  
ATOM   1015  CG  TYR A 272      30.875 -34.229 107.582  1.00 10.68           C  
ATOM   1016  CD1 TYR A 272      30.813 -33.882 108.936  1.00 10.49           C  
ATOM   1017  CD2 TYR A 272      31.900 -33.663 106.802  1.00 11.51           C  
ATOM   1018  CE1 TYR A 272      31.738 -32.996 109.494  1.00 11.16           C  
ATOM   1019  CE2 TYR A 272      32.829 -32.778 107.362  1.00 11.39           C  
ATOM   1020  CZ  TYR A 272      32.738 -32.453 108.705  1.00 11.79           C  
ATOM   1021  OH  TYR A 272      33.661 -31.597 109.263  1.00 12.79           O  
ATOM   1022  N   PHE A 273      31.545 -36.755 105.083  1.00  8.03           N  
ATOM   1023  CA  PHE A 273      32.727 -36.966 104.274  1.00  7.78           C  
ATOM   1024  C   PHE A 273      32.544 -36.132 103.017  1.00  7.28           C  
ATOM   1025  O   PHE A 273      31.508 -36.199 102.379  1.00  8.29           O  
ATOM   1026  CB  PHE A 273      32.865 -38.455 103.924  1.00  7.88           C  
ATOM   1027  CG  PHE A 273      34.039 -38.759 103.047  1.00  7.20           C  
ATOM   1028  CD1 PHE A 273      33.980 -38.505 101.677  1.00  6.36           C  
ATOM   1029  CD2 PHE A 273      35.234 -39.220 103.601  1.00  6.28           C  
ATOM   1030  CE1 PHE A 273      35.083 -38.691 100.873  1.00  4.99           C  
ATOM   1031  CE2 PHE A 273      36.345 -39.412 102.799  1.00  5.03           C  
ATOM   1032  CZ  PHE A 273      36.269 -39.143 101.431  1.00  4.80           C  
ATOM   1033  N   GLY A 274      33.536 -35.328 102.662  1.00  7.27           N  
ATOM   1034  CA  GLY A 274      33.384 -34.506 101.477  1.00  7.41           C  
ATOM   1035  C   GLY A 274      34.684 -33.859 101.068  1.00  7.57           C  
ATOM   1036  O   GLY A 274      35.751 -34.315 101.457  1.00  7.99           O  
ATOM   1037  N   TYR A 275      34.598 -32.792 100.284  1.00  8.07           N  
ATOM   1038  CA  TYR A 275      35.785 -32.086  99.823  1.00  8.35           C  
ATOM   1039  C   TYR A 275      35.684 -30.587  99.920  1.00  8.65           C  
ATOM   1040  O   TYR A 275      34.648 -30.015  99.591  1.00  9.68           O  
ATOM   1041  CB  TYR A 275      36.064 -32.455  98.358  1.00  8.31           C  
ATOM   1042  CG  TYR A 275      36.389 -33.914  98.189  1.00  8.52           C  
ATOM   1043  CD1 TYR A 275      37.650 -34.415  98.559  1.00  8.18           C  
ATOM   1044  CD2 TYR A 275      35.410 -34.823  97.763  1.00  8.80           C  
ATOM   1045  CE1 TYR A 275      37.923 -35.783  98.514  1.00  8.50           C  
ATOM   1046  CE2 TYR A 275      35.672 -36.190  97.719  1.00  9.14           C  
ATOM   1047  CZ  TYR A 275      36.928 -36.665  98.094  1.00  8.74           C  
ATOM   1048  OH  TYR A 275      37.196 -38.012  98.049  1.00  8.48           O  
ATOM   1049  N   SER A 276      36.747 -29.934 100.381  1.00  9.27           N  
ATOM   1050  CA  SER A 276      36.750 -28.478 100.398  1.00  8.88           C  
ATOM   1051  C   SER A 276      37.525 -28.163  99.137  1.00  8.23           C  
ATOM   1052  O   SER A 276      38.512 -28.823  98.828  1.00  7.49           O  
ATOM   1053  CB  SER A 276      37.446 -27.910 101.646  1.00  9.98           C  
ATOM   1054  OG  SER A 276      38.834 -28.145 101.643  1.00 11.74           O  
ATOM   1055  N   THR A 277      37.059 -27.191  98.372  1.00  9.13           N  
ATOM   1056  CA  THR A 277      37.736 -26.824  97.138  1.00  8.85           C  
ATOM   1057  C   THR A 277      38.399 -25.466  97.296  1.00  8.97           C  
ATOM   1058  O   THR A 277      38.218 -24.786  98.304  1.00  9.54           O  
ATOM   1059  CB  THR A 277      36.748 -26.738  95.963  1.00  7.95           C  
ATOM   1060  OG1 THR A 277      35.913 -25.585  96.125  1.00  8.16           O  
ATOM   1061  CG2 THR A 277      35.883 -27.984  95.902  1.00  6.99           C  
ATOM   1062  N   PRO A 278      39.206 -25.066  96.308  1.00  9.44           N  
ATOM   1063  CA  PRO A 278      39.887 -23.769  96.356  1.00  7.85           C  
ATOM   1064  C   PRO A 278      39.012 -22.683  95.735  1.00  7.27           C  
ATOM   1065  O   PRO A 278      39.427 -21.534  95.626  1.00  8.14           O  
ATOM   1066  CB  PRO A 278      41.146 -23.983  95.508  1.00  7.48           C  
ATOM   1067  CG  PRO A 278      41.128 -25.444  95.117  1.00  8.14           C  
ATOM   1068  CD  PRO A 278      39.725 -25.898  95.204  1.00  8.95           C  
ATOM   1069  N   TRP A 279      37.818 -23.055  95.295  1.00  6.32           N  
ATOM   1070  CA  TRP A 279      36.929 -22.095  94.664  1.00  5.27           C  
ATOM   1071  C   TRP A 279      35.998 -21.377  95.635  1.00  4.22           C  
ATOM   1072  O   TRP A 279      35.798 -21.809  96.762  1.00  2.26           O  
ATOM   1073  CB  TRP A 279      36.077 -22.784  93.602  1.00  5.11           C  
ATOM   1074  CG  TRP A 279      36.867 -23.389  92.458  1.00  3.87           C  
ATOM   1075  CD1 TRP A 279      37.672 -24.491  92.501  1.00  2.48           C  
ATOM   1076  CD2 TRP A 279      36.901 -22.915  91.104  1.00  3.27           C  
ATOM   1077  NE1 TRP A 279      38.207 -24.732  91.255  1.00  2.75           N  
ATOM   1078  CE2 TRP A 279      37.754 -23.779  90.383  1.00  3.27           C  
ATOM   1079  CE3 TRP A 279      36.298 -21.842  90.438  1.00  2.04           C  
ATOM   1080  CZ2 TRP A 279      38.016 -23.601  89.019  1.00  3.33           C  
ATOM   1081  CZ3 TRP A 279      36.554 -21.661  89.091  1.00  2.92           C  
ATOM   1082  CH2 TRP A 279      37.413 -22.537  88.394  1.00  3.96           C  
ATOM   1083  N   GLY A 280      35.480 -20.237  95.181  1.00  5.24           N  
ATOM   1084  CA  GLY A 280      34.519 -19.479  95.955  1.00  4.93           C  
ATOM   1085  C   GLY A 280      33.290 -19.465  95.069  1.00  4.40           C  
ATOM   1086  O   GLY A 280      33.379 -19.844  93.909  1.00  3.81           O  
ATOM   1087  N   TYR A 281      32.138 -19.043  95.576  1.00  6.57           N  
ATOM   1088  CA  TYR A 281      30.946 -19.002  94.725  1.00  6.30           C  
ATOM   1089  C   TYR A 281      30.049 -17.833  95.104  1.00  6.47           C  
ATOM   1090  O   TYR A 281      30.113 -17.331  96.221  1.00  6.87           O  
ATOM   1091  CB  TYR A 281      30.163 -20.321  94.828  1.00  4.93           C  
ATOM   1092  CG  TYR A 281      29.617 -20.610  96.205  1.00  4.43           C  
ATOM   1093  CD1 TYR A 281      30.441 -21.105  97.217  1.00  3.17           C  
ATOM   1094  CD2 TYR A 281      28.264 -20.377  96.504  1.00  5.32           C  
ATOM   1095  CE1 TYR A 281      29.945 -21.368  98.493  1.00  4.02           C  
ATOM   1096  CE2 TYR A 281      27.753 -20.638  97.785  1.00  6.09           C  
ATOM   1097  CZ  TYR A 281      28.599 -21.136  98.770  1.00  6.60           C  
ATOM   1098  OH  TYR A 281      28.094 -21.413 100.027  1.00  7.97           O  
ATOM   1099  N   PHE A 282      29.193 -17.418  94.182  1.00  7.76           N  
ATOM   1100  CA  PHE A 282      28.307 -16.300  94.447  1.00 10.25           C  
ATOM   1101  C   PHE A 282      26.909 -16.695  94.885  1.00 12.24           C  
ATOM   1102  O   PHE A 282      26.196 -17.439  94.200  1.00 12.29           O  
ATOM   1103  CB  PHE A 282      28.259 -15.380  93.226  1.00 10.11           C  
ATOM   1104  CG  PHE A 282      29.496 -14.544  93.071  1.00 10.68           C  
ATOM   1105  CD1 PHE A 282      29.657 -13.364  93.817  1.00  9.89           C  
ATOM   1106  CD2 PHE A 282      30.526 -14.948  92.207  1.00 10.80           C  
ATOM   1107  CE1 PHE A 282      30.822 -12.594  93.702  1.00  9.04           C  
ATOM   1108  CE2 PHE A 282      31.701 -14.186  92.083  1.00 10.34           C  
ATOM   1109  CZ  PHE A 282      31.852 -13.004  92.833  1.00  9.29           C  
ATOM   1110  N   ASP A 283      26.529 -16.189  96.051  1.00 13.28           N  
ATOM   1111  CA  ASP A 283      25.228 -16.485  96.606  1.00 14.25           C  
ATOM   1112  C   ASP A 283      24.341 -15.257  96.755  1.00 12.37           C  
ATOM   1113  O   ASP A 283      24.641 -14.357  97.538  1.00 12.37           O  
ATOM   1114  CB  ASP A 283      25.368 -17.158  97.974  1.00 16.89           C  
ATOM   1115  CG  ASP A 283      24.030 -17.676  98.501  1.00 20.49           C  
ATOM   1116  OD1 ASP A 283      23.476 -18.616  97.888  1.00 21.92           O  
ATOM   1117  OD2 ASP A 283      23.515 -17.145  99.510  1.00 21.62           O  
ATOM   1118  N   PHE A 284      23.249 -15.221  96.001  1.00 10.79           N  
ATOM   1119  CA  PHE A 284      22.296 -14.123  96.102  1.00  9.03           C  
ATOM   1120  C   PHE A 284      20.907 -14.725  96.299  1.00  8.61           C  
ATOM   1121  O   PHE A 284      19.912 -14.223  95.788  1.00  8.76           O  
ATOM   1122  CB  PHE A 284      22.353 -13.238  94.853  1.00  8.39           C  
ATOM   1123  CG  PHE A 284      22.362 -13.999  93.549  1.00  9.17           C  
ATOM   1124  CD1 PHE A 284      21.166 -14.393  92.938  1.00  9.30           C  
ATOM   1125  CD2 PHE A 284      23.573 -14.316  92.925  1.00  9.96           C  
ATOM   1126  CE1 PHE A 284      21.168 -15.090  91.713  1.00  9.52           C  
ATOM   1127  CE2 PHE A 284      23.600 -15.010  91.708  1.00 10.20           C  
ATOM   1128  CZ  PHE A 284      22.392 -15.403  91.096  1.00 10.26           C  
ATOM   1129  N   ASN A 285      20.853 -15.802  97.074  1.00  8.98           N  
ATOM   1130  CA  ASN A 285      19.604 -16.510  97.320  1.00  7.98           C  
ATOM   1131  C   ASN A 285      18.870 -16.109  98.599  1.00  6.29           C  
ATOM   1132  O   ASN A 285      18.555 -16.946  99.438  1.00  7.36           O  
ATOM   1133  CB  ASN A 285      19.873 -18.027  97.290  1.00  6.80           C  
ATOM   1134  CG  ASN A 285      18.592 -18.857  97.233  1.00  4.65           C  
ATOM   1135  OD1 ASN A 285      17.570 -18.410  96.730  1.00  3.06           O  
ATOM   1136  ND2 ASN A 285      18.661 -20.078  97.731  1.00  4.74           N  
ATOM   1137  N   ARG A 286      18.613 -14.818  98.740  1.00  6.23           N  
ATOM   1138  CA  ARG A 286      17.863 -14.268  99.872  1.00  6.28           C  
ATOM   1139  C   ARG A 286      17.172 -13.082  99.265  1.00  5.34           C  
ATOM   1140  O   ARG A 286      17.698 -12.480  98.332  1.00  4.78           O  
ATOM   1141  CB  ARG A 286      18.784 -13.874 101.019  1.00  7.84           C  
ATOM   1142  CG  ARG A 286      19.231 -15.070 101.808  1.00  8.00           C  
ATOM   1143  CD  ARG A 286      20.166 -14.705 102.918  1.00  6.00           C  
ATOM   1144  NE  ARG A 286      19.473 -14.363 104.150  1.00  4.75           N  
ATOM   1145  CZ  ARG A 286      20.090 -14.042 105.275  1.00  2.85           C  
ATOM   1146  NH1 ARG A 286      21.416 -14.014 105.318  1.00  2.52           N  
ATOM   1147  NH2 ARG A 286      19.384 -13.764 106.365  1.00  3.81           N  
ATOM   1148  N   PHE A 287      15.970 -12.769  99.740  1.00  5.63           N  
ATOM   1149  CA  PHE A 287      15.224 -11.669  99.150  1.00  4.38           C  
ATOM   1150  C   PHE A 287      15.874 -10.307  99.357  1.00  5.10           C  
ATOM   1151  O   PHE A 287      15.808  -9.459  98.470  1.00  4.10           O  
ATOM   1152  CB  PHE A 287      13.773 -11.687  99.650  1.00  3.55           C  
ATOM   1153  CG  PHE A 287      12.911 -12.698  98.952  1.00  3.05           C  
ATOM   1154  CD1 PHE A 287      12.486 -12.479  97.641  1.00  2.76           C  
ATOM   1155  CD2 PHE A 287      12.569 -13.900  99.585  1.00  2.66           C  
ATOM   1156  CE1 PHE A 287      11.734 -13.437  96.973  1.00  3.34           C  
ATOM   1157  CE2 PHE A 287      11.821 -14.869  98.930  1.00  2.51           C  
ATOM   1158  CZ  PHE A 287      11.398 -14.645  97.623  1.00  3.25           C  
ATOM   1159  N   HIS A 288      16.519 -10.104 100.503  1.00  5.97           N  
ATOM   1160  CA  HIS A 288      17.175  -8.845 100.769  1.00  5.97           C  
ATOM   1161  C   HIS A 288      18.445  -8.580  99.922  1.00  8.24           C  
ATOM   1162  O   HIS A 288      19.013  -7.497 100.001  1.00  9.20           O  
ATOM   1163  CB  HIS A 288      17.458  -8.723 102.276  1.00  4.88           C  
ATOM   1164  CG  HIS A 288      18.514  -9.656 102.803  1.00  3.81           C  
ATOM   1165  ND1 HIS A 288      18.685  -9.880 104.150  1.00  5.30           N  
ATOM   1166  CD2 HIS A 288      19.506 -10.343 102.180  1.00  1.69           C  
ATOM   1167  CE1 HIS A 288      19.736 -10.655 104.340  1.00  5.24           C  
ATOM   1168  NE2 HIS A 288      20.258 -10.952 103.161  1.00  3.54           N  
ATOM   1169  N   CYS A 289      18.895  -9.540  99.111  1.00  8.84           N  
ATOM   1170  CA  CYS A 289      20.067  -9.257  98.279  1.00  9.17           C  
ATOM   1171  C   CYS A 289      19.496  -8.512  97.044  1.00  9.24           C  
ATOM   1172  O   CYS A 289      20.244  -7.934  96.262  1.00  9.35           O  
ATOM   1173  CB  CYS A 289      20.899 -10.556  97.855  1.00  7.99           C  
ATOM   1174  SG  CYS A 289      20.988 -11.982  99.030  1.00  8.78           S  
ATOM   1175  N   HIS A 290      18.167  -8.474  96.911  1.00  9.12           N  
ATOM   1176  CA  HIS A 290      17.502  -7.838  95.756  1.00  8.14           C  
ATOM   1177  C   HIS A 290      16.503  -6.738  96.063  1.00  7.20           C  
ATOM   1178  O   HIS A 290      16.402  -5.769  95.313  1.00  6.78           O  
ATOM   1179  CB  HIS A 290      16.769  -8.900  94.923  1.00  8.74           C  
ATOM   1180  CG  HIS A 290      17.610 -10.100  94.631  1.00  9.64           C  
ATOM   1181  ND1 HIS A 290      18.542 -10.122  93.615  1.00  9.87           N  
ATOM   1182  CD2 HIS A 290      17.775 -11.255  95.317  1.00  9.00           C  
ATOM   1183  CE1 HIS A 290      19.248 -11.235  93.694  1.00  9.23           C  
ATOM   1184  NE2 HIS A 290      18.804 -11.938  94.719  1.00  8.71           N  
ATOM   1185  N   PHE A 291      15.748  -6.900  97.146  1.00  7.09           N  
ATOM   1186  CA  PHE A 291      14.731  -5.925  97.539  1.00  5.45           C  
ATOM   1187  C   PHE A 291      15.178  -5.078  98.701  1.00  4.51           C  
ATOM   1188  O   PHE A 291      15.630  -5.604  99.725  1.00  4.85           O  
ATOM   1189  CB  PHE A 291      13.417  -6.612  97.992  1.00  5.07           C  
ATOM   1190  CG  PHE A 291      12.618  -7.236  96.880  1.00  4.73           C  
ATOM   1191  CD1 PHE A 291      11.683  -6.486  96.168  1.00  4.77           C  
ATOM   1192  CD2 PHE A 291      12.806  -8.582  96.537  1.00  3.80           C  
ATOM   1193  CE1 PHE A 291      10.944  -7.061  95.115  1.00  5.27           C  
ATOM   1194  CE2 PHE A 291      12.079  -9.167  95.495  1.00  3.84           C  
ATOM   1195  CZ  PHE A 291      11.147  -8.410  94.777  1.00  4.98           C  
ATOM   1196  N   SER A 292      15.033  -3.767  98.563  1.00  4.18           N  
ATOM   1197  CA  SER A 292      15.325  -2.868  99.676  1.00  4.44           C  
ATOM   1198  C   SER A 292      14.068  -3.043 100.544  1.00  3.55           C  
ATOM   1199  O   SER A 292      13.054  -3.527 100.059  1.00  3.11           O  
ATOM   1200  CB  SER A 292      15.424  -1.427  99.189  1.00  4.49           C  
ATOM   1201  OG  SER A 292      14.184  -0.938  98.724  1.00  5.51           O  
ATOM   1202  N   PRO A 293      14.124  -2.685 101.833  1.00  1.93           N  
ATOM   1203  CA  PRO A 293      12.941  -2.837 102.687  1.00  2.67           C  
ATOM   1204  C   PRO A 293      11.708  -2.109 102.149  1.00  2.32           C  
ATOM   1205  O   PRO A 293      10.603  -2.633 102.224  1.00  1.94           O  
ATOM   1206  CB  PRO A 293      13.409  -2.295 104.038  1.00  2.07           C  
ATOM   1207  CG  PRO A 293      14.868  -2.612 104.018  1.00  0.68           C  
ATOM   1208  CD  PRO A 293      15.290  -2.265 102.615  1.00  0.30           C  
ATOM   1209  N   ARG A 294      11.903  -0.912 101.605  1.00  3.62           N  
ATOM   1210  CA  ARG A 294      10.820  -0.130 101.026  1.00  4.05           C  
ATOM   1211  C   ARG A 294      10.239  -0.854  99.809  1.00  4.22           C  
ATOM   1212  O   ARG A 294       9.033  -0.795  99.568  1.00  3.12           O  
ATOM   1213  CB  ARG A 294      11.331   1.253 100.598  1.00  4.70           C  
ATOM   1214  CG  ARG A 294      10.285   2.127  99.914  1.00  4.77           C  
ATOM   1215  CD  ARG A 294       9.198   2.494 100.923  1.00  5.68           C  
ATOM   1216  NE  ARG A 294       8.094   3.234 100.332  1.00  8.10           N  
ATOM   1217  CZ  ARG A 294       7.053   2.691  99.705  1.00  8.63           C  
ATOM   1218  NH1 ARG A 294       6.956   1.384  99.572  1.00  8.00           N  
ATOM   1219  NH2 ARG A 294       6.090   3.472  99.236  1.00  9.01           N  
ATOM   1220  N   ASP A 295      11.099  -1.503  99.028  1.00  5.92           N  
ATOM   1221  CA  ASP A 295      10.666  -2.255  97.846  1.00  8.12           C  
ATOM   1222  C   ASP A 295       9.809  -3.444  98.253  1.00  5.95           C  
ATOM   1223  O   ASP A 295       8.869  -3.810  97.558  1.00  4.80           O  
ATOM   1224  CB  ASP A 295      11.847  -2.829  97.088  1.00 12.71           C  
ATOM   1225  CG  ASP A 295      12.428  -1.876  96.100  1.00 17.97           C  
ATOM   1226  OD1 ASP A 295      11.641  -1.178  95.416  1.00 20.24           O  
ATOM   1227  OD2 ASP A 295      13.677  -1.846  95.982  1.00 19.07           O  
ATOM   1228  N   TRP A 296      10.184  -4.050  99.372  1.00  5.13           N  
ATOM   1229  CA  TRP A 296       9.506  -5.202  99.904  1.00  4.60           C  
ATOM   1230  C   TRP A 296       8.108  -4.802 100.350  1.00  5.82           C  
ATOM   1231  O   TRP A 296       7.135  -5.505 100.068  1.00  6.27           O  
ATOM   1232  CB  TRP A 296      10.322  -5.784 101.067  1.00  2.67           C  
ATOM   1233  CG  TRP A 296       9.825  -7.112 101.570  1.00  1.90           C  
ATOM   1234  CD1 TRP A 296       9.233  -7.368 102.785  1.00  1.27           C  
ATOM   1235  CD2 TRP A 296       9.911  -8.379 100.889  1.00  0.65           C  
ATOM   1236  NE1 TRP A 296       8.956  -8.712 102.894  1.00  1.23           N  
ATOM   1237  CE2 TRP A 296       9.362  -9.353 101.750  1.00  1.17           C  
ATOM   1238  CE3 TRP A 296      10.404  -8.780  99.634  1.00  1.44           C  
ATOM   1239  CZ2 TRP A 296       9.293 -10.720 101.400  1.00  0.99           C  
ATOM   1240  CZ3 TRP A 296      10.337 -10.141  99.278  1.00  0.86           C  
ATOM   1241  CH2 TRP A 296       9.786 -11.092 100.164  1.00  0.00           C  
ATOM   1242  N   GLN A 297       8.013  -3.671 101.039  1.00  6.09           N  
ATOM   1243  CA  GLN A 297       6.740  -3.135 101.496  1.00  5.75           C  
ATOM   1244  C   GLN A 297       5.838  -2.827 100.294  1.00  5.79           C  
ATOM   1245  O   GLN A 297       4.653  -3.122 100.307  1.00  6.63           O  
ATOM   1246  CB  GLN A 297       6.980  -1.865 102.298  1.00  5.01           C  
ATOM   1247  CG  GLN A 297       5.724  -1.204 102.818  1.00  4.12           C  
ATOM   1248  CD  GLN A 297       6.023   0.085 103.524  1.00  2.73           C  
ATOM   1249  OE1 GLN A 297       6.709   0.939 102.973  1.00  1.74           O  
ATOM   1250  NE2 GLN A 297       5.519   0.243 104.746  1.00  3.57           N  
ATOM   1251  N   ARG A 298       6.405  -2.245  99.253  1.00  5.26           N  
ATOM   1252  CA  ARG A 298       5.643  -1.932  98.065  1.00  5.88           C  
ATOM   1253  C   ARG A 298       5.103  -3.218  97.453  1.00  8.42           C  
ATOM   1254  O   ARG A 298       3.976  -3.259  96.952  1.00  9.78           O  
ATOM   1255  CB  ARG A 298       6.526  -1.189  97.065  1.00  5.72           C  
ATOM   1256  CG  ARG A 298       5.921  -0.905  95.700  1.00  7.48           C  
ATOM   1257  CD  ARG A 298       6.456   0.426  95.127  1.00 10.50           C  
ATOM   1258  NE  ARG A 298       7.911   0.486  95.182  1.00 14.22           N  
ATOM   1259  CZ  ARG A 298       8.628   1.458  95.743  1.00 16.32           C  
ATOM   1260  NH1 ARG A 298       8.051   2.498  96.317  1.00 16.04           N  
ATOM   1261  NH2 ARG A 298       9.950   1.368  95.748  1.00 18.44           N  
ATOM   1262  N   LEU A 299       5.908  -4.274  97.500  1.00  8.06           N  
ATOM   1263  CA  LEU A 299       5.520  -5.553  96.946  1.00  6.72           C  
ATOM   1264  C   LEU A 299       4.412  -6.239  97.758  1.00  5.22           C  
ATOM   1265  O   LEU A 299       3.394  -6.634  97.199  1.00  4.93           O  
ATOM   1266  CB  LEU A 299       6.737  -6.479  96.864  1.00  6.59           C  
ATOM   1267  CG  LEU A 299       6.429  -7.931  96.487  1.00  6.37           C  
ATOM   1268  CD1 LEU A 299       6.224  -8.053  94.982  1.00  5.52           C  
ATOM   1269  CD2 LEU A 299       7.559  -8.828  96.956  1.00  7.11           C  
ATOM   1270  N   ILE A 300       4.614  -6.372  99.065  1.00  4.46           N  
ATOM   1271  CA  ILE A 300       3.651  -7.049  99.925  1.00  4.20           C  
ATOM   1272  C   ILE A 300       2.334  -6.334 100.217  1.00  4.87           C  
ATOM   1273  O   ILE A 300       1.337  -6.988 100.523  1.00  6.37           O  
ATOM   1274  CB  ILE A 300       4.320  -7.488 101.269  1.00  4.36           C  
ATOM   1275  CG1 ILE A 300       4.623  -6.264 102.150  1.00  3.83           C  
ATOM   1276  CG2 ILE A 300       5.591  -8.290 100.963  1.00  4.05           C  
ATOM   1277  CD1 ILE A 300       5.507  -6.522 103.366  1.00  2.41           C  
ATOM   1278  N   ASN A 301       2.296  -5.011 100.111  1.00  3.92           N  
ATOM   1279  CA  ASN A 301       1.061  -4.287 100.391  1.00  1.52           C  
ATOM   1280  C   ASN A 301       0.208  -4.175  99.133  1.00  0.72           C  
ATOM   1281  O   ASN A 301      -0.943  -3.789  99.195  1.00  0.92           O  
ATOM   1282  CB  ASN A 301       1.368  -2.881 100.948  1.00  0.00           C  
ATOM   1283  CG  ASN A 301       1.736  -2.897 102.405  1.00  0.00           C  
ATOM   1284  OD1 ASN A 301       1.590  -3.912 103.082  1.00  0.00           O  
ATOM   1285  ND2 ASN A 301       2.203  -1.767 102.912  1.00  0.00           N  
ATOM   1286  N   ASN A 302       0.745  -4.578  97.994  1.00  1.71           N  
ATOM   1287  CA  ASN A 302      -0.004  -4.416  96.770  1.00  2.49           C  
ATOM   1288  C   ASN A 302      -0.183  -5.599  95.862  1.00  3.56           C  
ATOM   1289  O   ASN A 302      -0.846  -5.483  94.837  1.00  3.01           O  
ATOM   1290  CB  ASN A 302       0.630  -3.272  95.970  1.00  3.12           C  
ATOM   1291  CG  ASN A 302       0.528  -1.948  96.700  1.00  3.32           C  
ATOM   1292  OD1 ASN A 302      -0.557  -1.371  96.779  1.00  4.46           O  
ATOM   1293  ND2 ASN A 302       1.639  -1.482  97.280  1.00  2.41           N  
ATOM   1294  N   ASN A 303       0.384  -6.744  96.220  1.00  4.82           N  
ATOM   1295  CA  ASN A 303       0.283  -7.879  95.324  1.00  4.34           C  
ATOM   1296  C   ASN A 303      -0.172  -9.138  95.981  1.00  4.71           C  
ATOM   1297  O   ASN A 303       0.131  -9.389  97.147  1.00  5.85           O  
ATOM   1298  CB  ASN A 303       1.638  -8.101  94.646  1.00  4.21           C  
ATOM   1299  CG  ASN A 303       2.103  -6.882  93.889  1.00  2.73           C  
ATOM   1300  OD1 ASN A 303       1.721  -6.676  92.743  1.00  2.17           O  
ATOM   1301  ND2 ASN A 303       2.916  -6.048  94.540  1.00  1.45           N  
ATOM   1302  N   TRP A 304      -0.921  -9.933  95.233  1.00  5.25           N  
ATOM   1303  CA  TRP A 304      -1.392 -11.202  95.759  1.00  6.96           C  
ATOM   1304  C   TRP A 304      -0.368 -12.272  95.485  1.00  7.74           C  
ATOM   1305  O   TRP A 304      -0.331 -13.282  96.173  1.00  9.04           O  
ATOM   1306  CB  TRP A 304      -2.722 -11.586  95.142  1.00  8.57           C  
ATOM   1307  CG  TRP A 304      -3.853 -10.862  95.780  1.00  8.84           C  
ATOM   1308  CD1 TRP A 304      -3.899 -10.362  97.058  1.00  8.44           C  
ATOM   1309  CD2 TRP A 304      -5.144 -10.661  95.223  1.00  9.77           C  
ATOM   1310  NE1 TRP A 304      -5.146  -9.876  97.329  1.00  9.19           N  
ATOM   1311  CE2 TRP A 304      -5.936 -10.046  96.221  1.00 10.17           C  
ATOM   1312  CE3 TRP A 304      -5.719 -10.951  93.978  1.00 10.79           C  
ATOM   1313  CZ2 TRP A 304      -7.277  -9.715  96.016  1.00 11.11           C  
ATOM   1314  CZ3 TRP A 304      -7.049 -10.624  93.772  1.00 12.32           C  
ATOM   1315  CH2 TRP A 304      -7.818 -10.010  94.794  1.00 11.80           C  
ATOM   1316  N   GLY A 305       0.479 -12.044  94.487  1.00  7.91           N  
ATOM   1317  CA  GLY A 305       1.511 -13.015  94.208  1.00  8.48           C  
ATOM   1318  C   GLY A 305       2.648 -12.449  93.401  1.00  8.23           C  
ATOM   1319  O   GLY A 305       2.560 -11.351  92.856  1.00  9.64           O  
ATOM   1320  N   PHE A 306       3.729 -13.203  93.329  1.00  7.14           N  
ATOM   1321  CA  PHE A 306       4.892 -12.789  92.558  1.00  5.58           C  
ATOM   1322  C   PHE A 306       5.765 -14.009  92.409  1.00  4.98           C  
ATOM   1323  O   PHE A 306       5.704 -14.916  93.233  1.00  5.47           O  
ATOM   1324  CB  PHE A 306       5.675 -11.667  93.272  1.00  3.79           C  
ATOM   1325  CG  PHE A 306       6.315 -12.090  94.555  1.00  3.50           C  
ATOM   1326  CD1 PHE A 306       5.608 -12.046  95.751  1.00  3.50           C  
ATOM   1327  CD2 PHE A 306       7.618 -12.600  94.563  1.00  4.93           C  
ATOM   1328  CE1 PHE A 306       6.182 -12.510  96.933  1.00  4.33           C  
ATOM   1329  CE2 PHE A 306       8.198 -13.071  95.746  1.00  4.82           C  
ATOM   1330  CZ  PHE A 306       7.483 -13.027  96.928  1.00  4.45           C  
ATOM   1331  N   ARG A 307       6.559 -14.032  91.348  1.00  5.30           N  
ATOM   1332  CA  ARG A 307       7.482 -15.123  91.087  1.00  5.89           C  
ATOM   1333  C   ARG A 307       8.586 -14.567  90.180  1.00  5.35           C  
ATOM   1334  O   ARG A 307       8.350 -13.639  89.408  1.00  3.59           O  
ATOM   1335  CB  ARG A 307       6.760 -16.285  90.387  1.00  5.93           C  
ATOM   1336  CG  ARG A 307       6.217 -15.915  89.032  1.00  6.61           C  
ATOM   1337  CD  ARG A 307       5.467 -17.039  88.427  1.00  8.54           C  
ATOM   1338  NE  ARG A 307       4.909 -16.652  87.137  1.00 11.47           N  
ATOM   1339  CZ  ARG A 307       4.293 -17.486  86.307  1.00 14.00           C  
ATOM   1340  NH1 ARG A 307       4.158 -18.767  86.632  1.00 14.77           N  
ATOM   1341  NH2 ARG A 307       3.806 -17.039  85.155  1.00 15.10           N  
ATOM   1342  N   PRO A 308       9.805 -15.137  90.262  1.00  5.71           N  
ATOM   1343  CA  PRO A 308      10.954 -14.702  89.445  1.00  6.03           C  
ATOM   1344  C   PRO A 308      10.818 -15.094  87.977  1.00  6.64           C  
ATOM   1345  O   PRO A 308      10.299 -16.159  87.663  1.00  7.60           O  
ATOM   1346  CB  PRO A 308      12.141 -15.368  90.141  1.00  5.40           C  
ATOM   1347  CG  PRO A 308      11.524 -16.644  90.683  1.00  6.05           C  
ATOM   1348  CD  PRO A 308      10.203 -16.164  91.244  1.00  4.97           C  
ATOM   1349  N   LYS A 309      11.242 -14.220  87.074  1.00  7.67           N  
ATOM   1350  CA  LYS A 309      11.143 -14.510  85.644  1.00 10.44           C  
ATOM   1351  C   LYS A 309      12.495 -14.709  84.985  1.00 12.24           C  
ATOM   1352  O   LYS A 309      12.727 -15.710  84.320  1.00 12.83           O  
ATOM   1353  CB  LYS A 309      10.405 -13.391  84.914  1.00 11.79           C  
ATOM   1354  CG  LYS A 309       8.991 -13.193  85.400  1.00 14.01           C  
ATOM   1355  CD  LYS A 309       8.099 -14.403  85.117  1.00 15.05           C  
ATOM   1356  CE  LYS A 309       7.814 -14.550  83.637  1.00 16.07           C  
ATOM   1357  NZ  LYS A 309       6.678 -15.487  83.409  1.00 16.76           N  
ATOM   1358  N   ARG A 310      13.382 -13.741  85.151  1.00 14.34           N  
ATOM   1359  CA  ARG A 310      14.703 -13.843  84.568  1.00 17.32           C  
ATOM   1360  C   ARG A 310      15.732 -13.115  85.396  1.00 15.69           C  
ATOM   1361  O   ARG A 310      15.394 -12.358  86.299  1.00 15.70           O  
ATOM   1362  CB  ARG A 310      14.699 -13.311  83.133  1.00 21.53           C  
ATOM   1363  CG  ARG A 310      14.028 -11.979  82.960  1.00 25.61           C  
ATOM   1364  CD  ARG A 310      14.119 -11.501  81.510  1.00 29.97           C  
ATOM   1365  NE  ARG A 310      15.356 -10.754  81.248  1.00 33.71           N  
ATOM   1366  CZ  ARG A 310      15.609  -9.512  81.679  1.00 36.07           C  
ATOM   1367  NH1 ARG A 310      14.711  -8.841  82.404  1.00 36.22           N  
ATOM   1368  NH2 ARG A 310      16.769  -8.934  81.383  1.00 36.42           N  
ATOM   1369  N   LEU A 311      17.001 -13.376  85.119  1.00 15.58           N  
ATOM   1370  CA  LEU A 311      18.058 -12.699  85.845  1.00 15.46           C  
ATOM   1371  C   LEU A 311      19.267 -12.481  84.963  1.00 14.75           C  
ATOM   1372  O   LEU A 311      19.494 -13.200  83.990  1.00 14.61           O  
ATOM   1373  CB  LEU A 311      18.430 -13.465  87.127  1.00 16.48           C  
ATOM   1374  CG  LEU A 311      19.410 -14.632  87.217  1.00 17.34           C  
ATOM   1375  CD1 LEU A 311      20.841 -14.160  87.038  1.00 17.02           C  
ATOM   1376  CD2 LEU A 311      19.272 -15.267  88.593  1.00 17.88           C  
ATOM   1377  N   ASN A 312      20.018 -11.442  85.288  1.00 15.03           N  
ATOM   1378  CA  ASN A 312      21.214 -11.093  84.551  1.00 14.61           C  
ATOM   1379  C   ASN A 312      22.251 -10.916  85.642  1.00 12.22           C  
ATOM   1380  O   ASN A 312      22.024 -10.213  86.619  1.00 12.13           O  
ATOM   1381  CB  ASN A 312      20.981  -9.806  83.760  1.00 18.24           C  
ATOM   1382  CG  ASN A 312      22.068  -9.545  82.720  1.00 23.47           C  
ATOM   1383  OD1 ASN A 312      22.860 -10.435  82.382  1.00 25.29           O  
ATOM   1384  ND2 ASN A 312      22.104  -8.318  82.195  1.00 25.20           N  
ATOM   1385  N   PHE A 313      23.384 -11.582  85.485  1.00 11.11           N  
ATOM   1386  CA  PHE A 313      24.434 -11.531  86.481  1.00 10.01           C  
ATOM   1387  C   PHE A 313      25.737 -11.018  85.857  1.00 10.99           C  
ATOM   1388  O   PHE A 313      26.116 -11.436  84.767  1.00 12.33           O  
ATOM   1389  CB  PHE A 313      24.576 -12.937  87.078  1.00  8.23           C  
ATOM   1390  CG  PHE A 313      25.725 -13.096  88.016  1.00  7.55           C  
ATOM   1391  CD1 PHE A 313      27.034 -13.189  87.529  1.00  6.35           C  
ATOM   1392  CD2 PHE A 313      25.509 -13.164  89.388  1.00  7.00           C  
ATOM   1393  CE1 PHE A 313      28.099 -13.343  88.391  1.00  4.88           C  
ATOM   1394  CE2 PHE A 313      26.577 -13.323  90.266  1.00  6.64           C  
ATOM   1395  CZ  PHE A 313      27.876 -13.411  89.762  1.00  5.97           C  
ATOM   1396  N   LYS A 314      26.406 -10.092  86.536  1.00 10.41           N  
ATOM   1397  CA  LYS A 314      27.641  -9.531  86.019  1.00 10.95           C  
ATOM   1398  C   LYS A 314      28.781  -9.415  87.005  1.00  9.91           C  
ATOM   1399  O   LYS A 314      28.579  -9.226  88.201  1.00  9.34           O  
ATOM   1400  CB  LYS A 314      27.407  -8.131  85.448  1.00 13.27           C  
ATOM   1401  CG  LYS A 314      26.627  -8.094  84.183  1.00 16.89           C  
ATOM   1402  CD  LYS A 314      26.277  -6.654  83.795  1.00 19.95           C  
ATOM   1403  CE  LYS A 314      25.379  -6.645  82.555  1.00 22.45           C  
ATOM   1404  NZ  LYS A 314      24.794  -5.293  82.288  1.00 24.06           N  
ATOM   1405  N   LEU A 315      29.992  -9.530  86.474  1.00 10.26           N  
ATOM   1406  CA  LEU A 315      31.209  -9.355  87.260  1.00 10.51           C  
ATOM   1407  C   LEU A 315      32.011  -8.354  86.451  1.00 10.70           C  
ATOM   1408  O   LEU A 315      32.218  -8.540  85.254  1.00 11.00           O  
ATOM   1409  CB  LEU A 315      31.982 -10.667  87.411  1.00 10.37           C  
ATOM   1410  CG  LEU A 315      31.333 -11.685  88.358  1.00 10.77           C  
ATOM   1411  CD1 LEU A 315      32.163 -12.977  88.398  1.00 11.32           C  
ATOM   1412  CD2 LEU A 315      31.206 -11.078  89.756  1.00  9.56           C  
ATOM   1413  N   PHE A 316      32.422  -7.264  87.079  1.00 10.91           N  
ATOM   1414  CA  PHE A 316      33.201  -6.265  86.370  1.00 10.98           C  
ATOM   1415  C   PHE A 316      34.139  -5.551  87.323  1.00 10.17           C  
ATOM   1416  O   PHE A 316      34.099  -5.792  88.529  1.00  8.92           O  
ATOM   1417  CB  PHE A 316      32.278  -5.266  85.640  1.00 12.90           C  
ATOM   1418  CG  PHE A 316      31.194  -4.683  86.501  1.00 14.53           C  
ATOM   1419  CD1 PHE A 316      30.049  -5.435  86.815  1.00 15.67           C  
ATOM   1420  CD2 PHE A 316      31.315  -3.398  87.018  1.00 14.67           C  
ATOM   1421  CE1 PHE A 316      29.048  -4.919  87.628  1.00 15.83           C  
ATOM   1422  CE2 PHE A 316      30.310  -2.861  87.839  1.00 15.64           C  
ATOM   1423  CZ  PHE A 316      29.175  -3.625  88.145  1.00 16.18           C  
ATOM   1424  N   ASN A 317      34.985  -4.681  86.763  1.00 11.49           N  
ATOM   1425  CA  ASN A 317      35.988  -3.923  87.509  1.00 12.95           C  
ATOM   1426  C   ASN A 317      36.786  -4.851  88.409  1.00 12.83           C  
ATOM   1427  O   ASN A 317      36.978  -4.593  89.603  1.00 11.95           O  
ATOM   1428  CB  ASN A 317      35.347  -2.799  88.330  1.00 16.08           C  
ATOM   1429  CG  ASN A 317      34.582  -1.799  87.454  1.00 20.34           C  
ATOM   1430  OD1 ASN A 317      34.654  -1.844  86.218  1.00 21.91           O  
ATOM   1431  ND2 ASN A 317      33.850  -0.890  88.095  1.00 20.84           N  
ATOM   1432  N   ILE A 318      37.263  -5.933  87.809  1.00 14.27           N  
ATOM   1433  CA  ILE A 318      38.042  -6.932  88.528  1.00 16.19           C  
ATOM   1434  C   ILE A 318      39.491  -6.516  88.658  1.00 16.54           C  
ATOM   1435  O   ILE A 318      40.098  -6.023  87.708  1.00 17.04           O  
ATOM   1436  CB  ILE A 318      37.972  -8.295  87.802  1.00 17.74           C  
ATOM   1437  CG1 ILE A 318      36.640  -8.966  88.124  1.00 18.55           C  
ATOM   1438  CG2 ILE A 318      39.168  -9.185  88.186  1.00 18.06           C  
ATOM   1439  CD1 ILE A 318      36.081  -9.755  86.985  1.00 19.25           C  
ATOM   1440  N   GLN A 319      40.042  -6.699  89.844  1.00 16.52           N  
ATOM   1441  CA  GLN A 319      41.431  -6.376  90.037  1.00 18.18           C  
ATOM   1442  C   GLN A 319      42.106  -7.346  90.992  1.00 16.80           C  
ATOM   1443  O   GLN A 319      41.583  -7.659  92.055  1.00 16.64           O  
ATOM   1444  CB  GLN A 319      41.598  -4.914  90.492  1.00 20.84           C  
ATOM   1445  CG  GLN A 319      40.846  -4.510  91.719  1.00 23.53           C  
ATOM   1446  CD  GLN A 319      40.792  -2.980  91.904  1.00 25.90           C  
ATOM   1447  OE1 GLN A 319      41.824  -2.312  92.064  1.00 25.77           O  
ATOM   1448  NE2 GLN A 319      39.578  -2.431  91.889  1.00 26.32           N  
ATOM   1449  N   VAL A 320      43.269  -7.838  90.573  1.00 16.79           N  
ATOM   1450  CA  VAL A 320      44.047  -8.778  91.367  1.00 17.10           C  
ATOM   1451  C   VAL A 320      45.172  -8.030  92.079  1.00 17.67           C  
ATOM   1452  O   VAL A 320      45.871  -7.223  91.481  1.00 18.06           O  
ATOM   1453  CB  VAL A 320      44.656  -9.908  90.483  1.00 16.81           C  
ATOM   1454  CG1 VAL A 320      45.388 -10.920  91.361  1.00 16.46           C  
ATOM   1455  CG2 VAL A 320      43.571 -10.593  89.659  1.00 16.33           C  
ATOM   1456  N   LYS A 321      45.345  -8.313  93.360  1.00 18.95           N  
ATOM   1457  CA  LYS A 321      46.364  -7.659  94.152  1.00 20.93           C  
ATOM   1458  C   LYS A 321      47.340  -8.690  94.692  1.00 23.65           C  
ATOM   1459  O   LYS A 321      46.922  -9.758  95.126  1.00 23.96           O  
ATOM   1460  CB  LYS A 321      45.720  -6.931  95.337  1.00 21.25           C  
ATOM   1461  CG  LYS A 321      44.333  -6.356  95.085  1.00 22.37           C  
ATOM   1462  CD  LYS A 321      44.343  -5.035  94.328  1.00 23.77           C  
ATOM   1463  CE  LYS A 321      44.645  -3.860  95.247  1.00 25.05           C  
ATOM   1464  NZ  LYS A 321      44.537  -2.553  94.538  1.00 25.53           N  
ATOM   1465  N   GLU A 322      48.636  -8.383  94.669  1.00 26.13           N  
ATOM   1466  CA  GLU A 322      49.632  -9.303  95.212  1.00 28.90           C  
ATOM   1467  C   GLU A 322      50.129  -8.754  96.544  1.00 29.45           C  
ATOM   1468  O   GLU A 322      50.458  -7.580  96.655  1.00 29.35           O  
ATOM   1469  CB  GLU A 322      50.797  -9.517  94.233  1.00 31.53           C  
ATOM   1470  CG  GLU A 322      51.394  -8.254  93.641  1.00 34.70           C  
ATOM   1471  CD  GLU A 322      52.571  -8.531  92.697  1.00 37.74           C  
ATOM   1472  OE1 GLU A 322      52.511  -9.526  91.925  1.00 38.38           O  
ATOM   1473  OE2 GLU A 322      53.548  -7.738  92.724  1.00 38.62           O  
ATOM   1474  N   VAL A 323      50.160  -9.619  97.551  1.00 31.40           N  
ATOM   1475  CA  VAL A 323      50.577  -9.249  98.894  1.00 34.58           C  
ATOM   1476  C   VAL A 323      51.944  -9.819  99.272  1.00 40.14           C  
ATOM   1477  O   VAL A 323      52.149 -11.034  99.273  1.00 40.59           O  
ATOM   1478  CB  VAL A 323      49.530  -9.732  99.926  1.00 32.84           C  
ATOM   1479  CG1 VAL A 323      49.897  -9.276 101.328  1.00 32.09           C  
ATOM   1480  CG2 VAL A 323      48.171  -9.235  99.537  1.00 32.59           C  
ATOM   1481  N   THR A 324      52.881  -8.934  99.592  1.00 45.39           N  
ATOM   1482  CA  THR A 324      54.222  -9.357  99.978  1.00 50.35           C  
ATOM   1483  C   THR A 324      54.577  -8.779 101.337  1.00 55.01           C  
ATOM   1484  O   THR A 324      54.442  -7.579 101.557  1.00 55.03           O  
ATOM   1485  CB  THR A 324      55.281  -8.901  98.943  1.00 50.59           C  
ATOM   1486  OG1 THR A 324      55.282  -7.471  98.844  1.00 50.82           O  
ATOM   1487  CG2 THR A 324      54.988  -9.512  97.568  1.00 50.45           C  
ATOM   1488  N   GLN A 325      55.013  -9.638 102.253  1.00 59.57           N  
ATOM   1489  CA  GLN A 325      55.376  -9.191 103.591  1.00 64.18           C  
ATOM   1490  C   GLN A 325      56.876  -9.273 103.855  1.00 67.69           C  
ATOM   1491  O   GLN A 325      57.462 -10.359 103.859  1.00 67.99           O  
ATOM   1492  CB  GLN A 325      54.650 -10.016 104.651  1.00 65.18           C  
ATOM   1493  CG  GLN A 325      53.163 -10.188 104.412  1.00 66.29           C  
ATOM   1494  CD  GLN A 325      52.453 -10.780 105.621  1.00 67.12           C  
ATOM   1495  OE1 GLN A 325      53.019 -11.601 106.347  1.00 67.28           O  
ATOM   1496  NE2 GLN A 325      51.206 -10.374 105.836  1.00 67.33           N  
ATOM   1497  N   ASN A 326      57.487  -8.114 104.077  1.00 70.71           N  
ATOM   1498  CA  ASN A 326      58.917  -8.030 104.359  1.00 73.62           C  
ATOM   1499  C   ASN A 326      59.143  -7.197 105.622  1.00 75.67           C  
ATOM   1500  O   ASN A 326      58.543  -6.136 105.793  1.00 75.98           O  
ATOM   1501  CB  ASN A 326      59.667  -7.404 103.172  1.00 74.06           C  
ATOM   1502  CG  ASN A 326      59.709  -8.317 101.948  1.00 74.30           C  
ATOM   1503  OD1 ASN A 326      59.869  -9.534 102.068  1.00 74.30           O  
ATOM   1504  ND2 ASN A 326      59.590  -7.726 100.764  1.00 74.38           N  
ATOM   1505  N   ASP A 327      60.008  -7.690 106.505  1.00 76.70           N  
ATOM   1506  CA  ASP A 327      60.322  -7.010 107.765  1.00 77.44           C  
ATOM   1507  C   ASP A 327      59.084  -6.666 108.593  1.00 77.28           C  
ATOM   1508  O   ASP A 327      58.974  -5.560 109.132  1.00 77.53           O  
ATOM   1509  CB  ASP A 327      61.133  -5.725 107.518  1.00 78.18           C  
ATOM   1510  CG  ASP A 327      62.569  -6.003 107.099  1.00 78.54           C  
ATOM   1511  OD1 ASP A 327      63.072  -7.103 107.403  1.00 78.59           O  
ATOM   1512  OD2 ASP A 327      63.202  -5.117 106.482  1.00 78.62           O  
ATOM   1513  N   GLY A 328      58.158  -7.617 108.690  1.00 76.46           N  
ATOM   1514  CA  GLY A 328      56.942  -7.404 109.459  1.00 75.38           C  
ATOM   1515  C   GLY A 328      56.052  -6.274 108.962  1.00 74.09           C  
ATOM   1516  O   GLY A 328      55.415  -5.579 109.761  1.00 74.42           O  
ATOM   1517  N   THR A 329      56.015  -6.083 107.644  1.00 71.99           N  
ATOM   1518  CA  THR A 329      55.187  -5.045 107.029  1.00 69.65           C  
ATOM   1519  C   THR A 329      54.405  -5.653 105.862  1.00 66.77           C  
ATOM   1520  O   THR A 329      54.802  -6.682 105.314  1.00 66.83           O  
ATOM   1521  CB  THR A 329      56.041  -3.869 106.506  1.00 69.70           C  
ATOM   1522  OG1 THR A 329      56.770  -4.282 105.344  1.00 69.70           O  
ATOM   1523  CG2 THR A 329      57.029  -3.404 107.575  1.00 69.58           C  
ATOM   1524  N   THR A 330      53.280  -5.037 105.508  1.00 63.52           N  
ATOM   1525  CA  THR A 330      52.450  -5.535 104.415  1.00 60.07           C  
ATOM   1526  C   THR A 330      52.363  -4.573 103.237  1.00 55.47           C  
ATOM   1527  O   THR A 330      52.013  -3.404 103.396  1.00 55.35           O  
ATOM   1528  CB  THR A 330      51.018  -5.844 104.894  1.00 61.00           C  
ATOM   1529  OG1 THR A 330      50.397  -4.645 105.381  1.00 61.27           O  
ATOM   1530  CG2 THR A 330      51.046  -6.886 106.002  1.00 61.13           C  
ATOM   1531  N   THR A 331      52.703  -5.076 102.055  1.00 51.12           N  
ATOM   1532  CA  THR A 331      52.661  -4.284 100.833  1.00 47.00           C  
ATOM   1533  C   THR A 331      51.700  -4.944  99.846  1.00 43.11           C  
ATOM   1534  O   THR A 331      51.753  -6.156  99.625  1.00 43.06           O  
ATOM   1535  CB  THR A 331      54.063  -4.177 100.190  1.00 47.31           C  
ATOM   1536  OG1 THR A 331      54.965  -3.571 101.123  1.00 47.74           O  
ATOM   1537  CG2 THR A 331      54.020  -3.340  98.925  1.00 47.17           C  
ATOM   1538  N   ILE A 332      50.815  -4.141  99.265  1.00 39.73           N  
ATOM   1539  CA  ILE A 332      49.843  -4.642  98.300  1.00 36.57           C  
ATOM   1540  C   ILE A 332      50.034  -3.927  96.972  1.00 35.23           C  
ATOM   1541  O   ILE A 332      50.115  -2.702  96.931  1.00 36.10           O  
ATOM   1542  CB  ILE A 332      48.387  -4.422  98.813  1.00 35.22           C  
ATOM   1543  CG1 ILE A 332      48.214  -5.111 100.166  1.00 34.18           C  
ATOM   1544  CG2 ILE A 332      47.371  -4.950  97.799  1.00 34.71           C  
ATOM   1545  CD1 ILE A 332      46.873  -4.888 100.802  1.00 33.85           C  
ATOM   1546  N   ALA A 333      50.111  -4.686  95.885  1.00 33.55           N  
ATOM   1547  CA  ALA A 333      50.293  -4.096  94.562  1.00 32.58           C  
ATOM   1548  C   ALA A 333      49.379  -4.726  93.534  1.00 32.09           C  
ATOM   1549  O   ALA A 333      48.940  -5.852  93.696  1.00 32.05           O  
ATOM   1550  CB  ALA A 333      51.726  -4.241  94.119  1.00 32.83           C  
ATOM   1551  N   ASN A 334      49.120  -3.997  92.457  1.00 32.22           N  
ATOM   1552  CA  ASN A 334      48.241  -4.472  91.404  1.00 32.49           C  
ATOM   1553  C   ASN A 334      48.950  -5.271  90.332  1.00 31.69           C  
ATOM   1554  O   ASN A 334      50.030  -4.897  89.881  1.00 32.95           O  
ATOM   1555  CB  ASN A 334      47.522  -3.290  90.750  1.00 34.26           C  
ATOM   1556  CG  ASN A 334      46.496  -2.653  91.666  1.00 35.91           C  
ATOM   1557  OD1 ASN A 334      45.289  -2.744  91.419  1.00 36.01           O  
ATOM   1558  ND2 ASN A 334      46.968  -2.012  92.738  1.00 36.35           N  
ATOM   1559  N   ASN A 335      48.331  -6.368  89.918  1.00 29.96           N  
ATOM   1560  CA  ASN A 335      48.884  -7.216  88.882  1.00 28.49           C  
ATOM   1561  C   ASN A 335      47.872  -7.227  87.757  1.00 28.98           C  
ATOM   1562  O   ASN A 335      46.765  -7.736  87.923  1.00 30.27           O  
ATOM   1563  CB  ASN A 335      49.090  -8.634  89.408  1.00 27.94           C  
ATOM   1564  CG  ASN A 335      49.902  -9.499  88.450  1.00 27.88           C  
ATOM   1565  OD1 ASN A 335      49.830  -9.341  87.227  1.00 27.25           O  
ATOM   1566  ND2 ASN A 335      50.659 -10.436  89.005  1.00 28.13           N  
ATOM   1567  N   LEU A 336      48.236  -6.657  86.617  1.00 28.77           N  
ATOM   1568  CA  LEU A 336      47.322  -6.602  85.487  1.00 29.45           C  
ATOM   1569  C   LEU A 336      47.414  -7.845  84.630  1.00 29.12           C  
ATOM   1570  O   LEU A 336      46.605  -8.040  83.723  1.00 28.85           O  
ATOM   1571  CB  LEU A 336      47.620  -5.379  84.612  1.00 30.72           C  
ATOM   1572  CG  LEU A 336      47.669  -4.003  85.284  1.00 31.84           C  
ATOM   1573  CD1 LEU A 336      47.977  -2.925  84.249  1.00 32.11           C  
ATOM   1574  CD2 LEU A 336      46.347  -3.710  85.953  1.00 32.51           C  
ATOM   1575  N   THR A 337      48.395  -8.692  84.920  1.00 29.72           N  
ATOM   1576  CA  THR A 337      48.587  -9.907  84.138  1.00 30.16           C  
ATOM   1577  C   THR A 337      47.886 -11.143  84.723  1.00 27.36           C  
ATOM   1578  O   THR A 337      47.537 -12.069  83.985  1.00 27.78           O  
ATOM   1579  CB  THR A 337      50.109 -10.180  83.933  1.00 32.02           C  
ATOM   1580  OG1 THR A 337      50.740 -10.462  85.190  1.00 32.88           O  
ATOM   1581  CG2 THR A 337      50.775  -8.962  83.333  1.00 32.24           C  
ATOM   1582  N   SER A 338      47.656 -11.150  86.034  1.00 24.54           N  
ATOM   1583  CA  SER A 338      46.998 -12.287  86.668  1.00 21.92           C  
ATOM   1584  C   SER A 338      45.531 -12.356  86.293  1.00 21.00           C  
ATOM   1585  O   SER A 338      44.918 -11.356  85.913  1.00 22.28           O  
ATOM   1586  CB  SER A 338      47.122 -12.206  88.187  1.00 21.15           C  
ATOM   1587  OG  SER A 338      48.475 -12.304  88.607  1.00 20.80           O  
ATOM   1588  N   THR A 339      44.969 -13.551  86.396  1.00 19.63           N  
ATOM   1589  CA  THR A 339      43.569 -13.753  86.072  1.00 17.49           C  
ATOM   1590  C   THR A 339      42.763 -14.305  87.240  1.00 16.38           C  
ATOM   1591  O   THR A 339      43.278 -14.591  88.322  1.00 15.18           O  
ATOM   1592  CB  THR A 339      43.373 -14.748  84.906  1.00 16.41           C  
ATOM   1593  OG1 THR A 339      44.116 -15.939  85.178  1.00 16.66           O  
ATOM   1594  CG2 THR A 339      43.786 -14.141  83.563  1.00 15.43           C  
ATOM   1595  N   VAL A 340      41.473 -14.438  86.977  1.00 16.99           N  
ATOM   1596  CA  VAL A 340      40.509 -14.985  87.907  1.00 16.70           C  
ATOM   1597  C   VAL A 340      39.741 -15.938  86.997  1.00 14.99           C  
ATOM   1598  O   VAL A 340      39.506 -15.614  85.838  1.00 14.31           O  
ATOM   1599  CB  VAL A 340      39.610 -13.850  88.478  1.00 18.11           C  
ATOM   1600  CG1 VAL A 340      38.198 -14.337  88.681  1.00 18.57           C  
ATOM   1601  CG2 VAL A 340      40.192 -13.361  89.799  1.00 18.37           C  
ATOM   1602  N   GLN A 341      39.393 -17.123  87.485  1.00 14.43           N  
ATOM   1603  CA  GLN A 341      38.663 -18.073  86.652  1.00 14.25           C  
ATOM   1604  C   GLN A 341      37.220 -18.163  87.090  1.00 11.00           C  
ATOM   1605  O   GLN A 341      36.930 -18.309  88.274  1.00 11.01           O  
ATOM   1606  CB  GLN A 341      39.302 -19.458  86.723  1.00 16.56           C  
ATOM   1607  CG  GLN A 341      40.683 -19.529  86.123  1.00 19.13           C  
ATOM   1608  CD  GLN A 341      41.352 -20.852  86.425  1.00 21.06           C  
ATOM   1609  OE1 GLN A 341      40.754 -21.918  86.247  1.00 21.67           O  
ATOM   1610  NE2 GLN A 341      42.594 -20.795  86.888  1.00 21.45           N  
ATOM   1611  N   VAL A 342      36.320 -18.086  86.127  1.00  9.36           N  
ATOM   1612  CA  VAL A 342      34.906 -18.139  86.418  1.00  9.23           C  
ATOM   1613  C   VAL A 342      34.245 -19.298  85.716  1.00  8.71           C  
ATOM   1614  O   VAL A 342      34.255 -19.397  84.495  1.00  8.32           O  
ATOM   1615  CB  VAL A 342      34.170 -16.834  85.990  1.00  9.66           C  
ATOM   1616  CG1 VAL A 342      32.673 -16.962  86.281  1.00  9.66           C  
ATOM   1617  CG2 VAL A 342      34.743 -15.642  86.734  1.00  9.64           C  
ATOM   1618  N   PHE A 343      33.658 -20.169  86.512  1.00 10.33           N  
ATOM   1619  CA  PHE A 343      32.959 -21.326  85.998  1.00 12.71           C  
ATOM   1620  C   PHE A 343      31.474 -21.252  86.371  1.00 12.18           C  
ATOM   1621  O   PHE A 343      31.132 -21.161  87.549  1.00 11.64           O  
ATOM   1622  CB  PHE A 343      33.597 -22.590  86.586  1.00 15.50           C  
ATOM   1623  CG  PHE A 343      32.817 -23.834  86.334  1.00 17.83           C  
ATOM   1624  CD1 PHE A 343      32.367 -24.142  85.053  1.00 19.10           C  
ATOM   1625  CD2 PHE A 343      32.498 -24.686  87.383  1.00 18.81           C  
ATOM   1626  CE1 PHE A 343      31.599 -25.286  84.821  1.00 20.00           C  
ATOM   1627  CE2 PHE A 343      31.739 -25.824  87.169  1.00 19.51           C  
ATOM   1628  CZ  PHE A 343      31.284 -26.130  85.884  1.00 20.25           C  
ATOM   1629  N   THR A 344      30.598 -21.255  85.373  1.00 13.39           N  
ATOM   1630  CA  THR A 344      29.163 -21.251  85.640  1.00 15.65           C  
ATOM   1631  C   THR A 344      28.648 -22.659  85.344  1.00 15.79           C  
ATOM   1632  O   THR A 344      28.668 -23.115  84.199  1.00 16.40           O  
ATOM   1633  CB  THR A 344      28.402 -20.194  84.782  1.00 17.40           C  
ATOM   1634  OG1 THR A 344      26.998 -20.496  84.781  1.00 16.85           O  
ATOM   1635  CG2 THR A 344      28.938 -20.159  83.353  1.00 19.46           C  
ATOM   1636  N   ASP A 345      28.202 -23.347  86.388  1.00 16.05           N  
ATOM   1637  CA  ASP A 345      27.708 -24.715  86.268  1.00 17.71           C  
ATOM   1638  C   ASP A 345      26.269 -24.843  85.749  1.00 17.64           C  
ATOM   1639  O   ASP A 345      25.371 -25.304  86.454  1.00 17.10           O  
ATOM   1640  CB  ASP A 345      27.857 -25.412  87.622  1.00 19.57           C  
ATOM   1641  CG  ASP A 345      27.618 -26.898  87.538  1.00 21.30           C  
ATOM   1642  OD1 ASP A 345      27.844 -27.479  86.455  1.00 21.74           O  
ATOM   1643  OD2 ASP A 345      27.216 -27.495  88.563  1.00 22.09           O  
ATOM   1644  N   SER A 346      26.070 -24.458  84.495  1.00 18.82           N  
ATOM   1645  CA  SER A 346      24.755 -24.487  83.879  1.00 21.21           C  
ATOM   1646  C   SER A 346      24.181 -25.869  83.564  1.00 22.69           C  
ATOM   1647  O   SER A 346      23.007 -25.988  83.223  1.00 23.13           O  
ATOM   1648  CB  SER A 346      24.778 -23.639  82.617  1.00 22.65           C  
ATOM   1649  OG  SER A 346      25.725 -24.156  81.700  1.00 24.65           O  
ATOM   1650  N   GLU A 347      25.002 -26.907  83.673  1.00 23.68           N  
ATOM   1651  CA  GLU A 347      24.551 -28.266  83.404  1.00 24.44           C  
ATOM   1652  C   GLU A 347      24.366 -29.045  84.700  1.00 21.42           C  
ATOM   1653  O   GLU A 347      24.163 -30.254  84.685  1.00 21.80           O  
ATOM   1654  CB  GLU A 347      25.541 -28.982  82.477  1.00 28.45           C  
ATOM   1655  CG  GLU A 347      25.470 -28.513  81.020  1.00 32.07           C  
ATOM   1656  CD  GLU A 347      26.646 -29.008  80.171  1.00 35.56           C  
ATOM   1657  OE1 GLU A 347      26.901 -30.238  80.154  1.00 36.48           O  
ATOM   1658  OE2 GLU A 347      27.314 -28.168  79.517  1.00 36.19           O  
ATOM   1659  N   TYR A 348      24.436 -28.328  85.816  1.00 18.95           N  
ATOM   1660  CA  TYR A 348      24.245 -28.888  87.151  1.00 18.04           C  
ATOM   1661  C   TYR A 348      25.036 -30.156  87.444  1.00 18.78           C  
ATOM   1662  O   TYR A 348      24.539 -31.077  88.091  1.00 19.28           O  
ATOM   1663  CB  TYR A 348      22.744 -29.133  87.388  1.00 16.48           C  
ATOM   1664  CG  TYR A 348      21.891 -27.921  87.060  1.00 14.34           C  
ATOM   1665  CD1 TYR A 348      21.819 -26.830  87.943  1.00 12.58           C  
ATOM   1666  CD2 TYR A 348      21.237 -27.819  85.828  1.00 13.18           C  
ATOM   1667  CE1 TYR A 348      21.132 -25.675  87.605  1.00 11.26           C  
ATOM   1668  CE2 TYR A 348      20.542 -26.663  85.478  1.00 12.84           C  
ATOM   1669  CZ  TYR A 348      20.500 -25.589  86.373  1.00 12.00           C  
ATOM   1670  OH  TYR A 348      19.873 -24.418  86.005  1.00 11.70           O  
ATOM   1671  N   GLN A 349      26.289 -30.185  87.008  1.00 19.84           N  
ATOM   1672  CA  GLN A 349      27.126 -31.356  87.216  1.00 20.78           C  
ATOM   1673  C   GLN A 349      27.813 -31.422  88.578  1.00 18.27           C  
ATOM   1674  O   GLN A 349      28.292 -32.468  88.980  1.00 18.31           O  
ATOM   1675  CB  GLN A 349      28.124 -31.458  86.059  1.00 24.01           C  
ATOM   1676  CG  GLN A 349      27.398 -31.802  84.743  1.00 26.72           C  
ATOM   1677  CD  GLN A 349      28.198 -31.489  83.491  1.00 29.10           C  
ATOM   1678  OE1 GLN A 349      28.904 -30.475  83.422  1.00 29.73           O  
ATOM   1679  NE2 GLN A 349      28.072 -32.348  82.478  1.00 29.39           N  
ATOM   1680  N   LEU A 350      27.821 -30.314  89.305  1.00 16.81           N  
ATOM   1681  CA  LEU A 350      28.437 -30.270  90.626  1.00 15.19           C  
ATOM   1682  C   LEU A 350      27.389 -30.277  91.719  1.00 12.18           C  
ATOM   1683  O   LEU A 350      26.259 -29.857  91.498  1.00 12.92           O  
ATOM   1684  CB  LEU A 350      29.262 -28.993  90.778  1.00 16.20           C  
ATOM   1685  CG  LEU A 350      30.492 -28.828  89.891  1.00 16.90           C  
ATOM   1686  CD1 LEU A 350      31.024 -27.395  90.010  1.00 17.12           C  
ATOM   1687  CD2 LEU A 350      31.539 -29.849  90.308  1.00 16.35           C  
ATOM   1688  N   PRO A 351      27.739 -30.770  92.913  1.00  9.50           N  
ATOM   1689  CA  PRO A 351      26.743 -30.765  93.987  1.00  8.90           C  
ATOM   1690  C   PRO A 351      26.262 -29.320  94.216  1.00  9.10           C  
ATOM   1691  O   PRO A 351      27.075 -28.421  94.412  1.00  9.17           O  
ATOM   1692  CB  PRO A 351      27.526 -31.301  95.180  1.00  7.60           C  
ATOM   1693  CG  PRO A 351      28.478 -32.249  94.541  1.00  6.98           C  
ATOM   1694  CD  PRO A 351      28.954 -31.498  93.320  1.00  7.70           C  
ATOM   1695  N   TYR A 352      24.946 -29.111  94.186  1.00  9.45           N  
ATOM   1696  CA  TYR A 352      24.340 -27.793  94.365  1.00  8.34           C  
ATOM   1697  C   TYR A 352      24.227 -27.498  95.848  1.00 10.16           C  
ATOM   1698  O   TYR A 352      23.511 -28.187  96.564  1.00 11.97           O  
ATOM   1699  CB  TYR A 352      22.954 -27.775  93.719  1.00  6.55           C  
ATOM   1700  CG  TYR A 352      22.390 -26.410  93.431  1.00  5.99           C  
ATOM   1701  CD1 TYR A 352      22.798 -25.693  92.304  1.00  6.17           C  
ATOM   1702  CD2 TYR A 352      21.429 -25.829  94.277  1.00  5.42           C  
ATOM   1703  CE1 TYR A 352      22.270 -24.445  92.017  1.00  6.09           C  
ATOM   1704  CE2 TYR A 352      20.892 -24.579  93.999  1.00  4.67           C  
ATOM   1705  CZ  TYR A 352      21.314 -23.894  92.866  1.00  5.79           C  
ATOM   1706  OH  TYR A 352      20.762 -22.673  92.547  1.00  6.05           O  
ATOM   1707  N   VAL A 353      24.932 -26.474  96.318  1.00 10.96           N  
ATOM   1708  CA  VAL A 353      24.908 -26.142  97.735  1.00 11.57           C  
ATOM   1709  C   VAL A 353      24.105 -24.889  98.064  1.00 12.96           C  
ATOM   1710  O   VAL A 353      23.892 -24.580  99.237  1.00 12.98           O  
ATOM   1711  CB  VAL A 353      26.342 -26.012  98.311  1.00 11.60           C  
ATOM   1712  CG1 VAL A 353      27.087 -27.347  98.144  1.00 11.73           C  
ATOM   1713  CG2 VAL A 353      27.096 -24.858  97.623  1.00 10.84           C  
ATOM   1714  N   LEU A 354      23.674 -24.158  97.039  1.00 14.24           N  
ATOM   1715  CA  LEU A 354      22.830 -22.991  97.274  1.00 15.84           C  
ATOM   1716  C   LEU A 354      21.539 -23.706  97.663  1.00 16.59           C  
ATOM   1717  O   LEU A 354      21.277 -24.813  97.180  1.00 18.91           O  
ATOM   1718  CB  LEU A 354      22.616 -22.196  95.982  1.00 15.70           C  
ATOM   1719  CG  LEU A 354      23.853 -21.670  95.248  1.00 15.78           C  
ATOM   1720  CD1 LEU A 354      23.458 -21.051  93.901  1.00 15.26           C  
ATOM   1721  CD2 LEU A 354      24.542 -20.642  96.124  1.00 15.92           C  
ATOM   1722  N   GLY A 355      20.731 -23.133  98.534  1.00 14.39           N  
ATOM   1723  CA  GLY A 355      19.532 -23.859  98.888  1.00 12.23           C  
ATOM   1724  C   GLY A 355      19.670 -24.559 100.215  1.00 11.48           C  
ATOM   1725  O   GLY A 355      18.829 -25.379 100.574  1.00 12.73           O  
ATOM   1726  N   SER A 356      20.739 -24.268 100.943  1.00 11.01           N  
ATOM   1727  CA  SER A 356      20.918 -24.872 102.250  1.00 10.83           C  
ATOM   1728  C   SER A 356      21.075 -23.783 103.296  1.00  8.94           C  
ATOM   1729  O   SER A 356      21.672 -24.001 104.350  1.00  7.66           O  
ATOM   1730  CB  SER A 356      22.132 -25.803 102.258  1.00 12.27           C  
ATOM   1731  OG  SER A 356      21.945 -26.874 101.349  1.00 12.66           O  
ATOM   1732  N   ALA A 357      20.508 -22.612 102.993  1.00  8.73           N  
ATOM   1733  CA  ALA A 357      20.551 -21.439 103.873  1.00  7.60           C  
ATOM   1734  C   ALA A 357      21.927 -21.116 104.467  1.00  7.72           C  
ATOM   1735  O   ALA A 357      22.062 -20.951 105.680  1.00  8.23           O  
ATOM   1736  CB  ALA A 357      19.524 -21.590 105.005  1.00  5.34           C  
ATOM   1737  N   HIS A 358      22.949 -21.006 103.628  1.00  8.59           N  
ATOM   1738  CA  HIS A 358      24.279 -20.690 104.140  1.00  8.87           C  
ATOM   1739  C   HIS A 358      24.518 -19.199 104.194  1.00  9.60           C  
ATOM   1740  O   HIS A 358      23.931 -18.434 103.430  1.00  9.71           O  
ATOM   1741  CB  HIS A 358      25.358 -21.367 103.299  1.00  8.58           C  
ATOM   1742  CG  HIS A 358      25.430 -22.837 103.532  1.00  8.30           C  
ATOM   1743  ND1 HIS A 358      25.601 -23.370 104.794  1.00  8.31           N  
ATOM   1744  CD2 HIS A 358      25.218 -23.884 102.701  1.00  7.41           C  
ATOM   1745  CE1 HIS A 358      25.480 -24.683 104.730  1.00  8.14           C  
ATOM   1746  NE2 HIS A 358      25.248 -25.018 103.471  1.00  7.94           N  
ATOM   1747  N   GLN A 359      25.373 -18.782 105.112  1.00 11.68           N  
ATOM   1748  CA  GLN A 359      25.655 -17.376 105.229  1.00 12.78           C  
ATOM   1749  C   GLN A 359      26.840 -16.840 104.442  1.00 14.14           C  
ATOM   1750  O   GLN A 359      27.970 -16.976 104.867  1.00 16.58           O  
ATOM   1751  CB  GLN A 359      25.776 -16.977 106.708  1.00 11.98           C  
ATOM   1752  CG  GLN A 359      26.852 -17.628 107.455  1.00 12.75           C  
ATOM   1753  CD  GLN A 359      26.792 -17.303 108.930  1.00 13.50           C  
ATOM   1754  OE1 GLN A 359      25.728 -17.244 109.516  1.00 13.44           O  
ATOM   1755  NE2 GLN A 359      27.947 -17.114 109.538  1.00 15.98           N  
ATOM   1756  N   GLY A 360      26.546 -16.194 103.313  1.00 13.67           N  
ATOM   1757  CA  GLY A 360      27.551 -15.568 102.473  1.00 13.59           C  
ATOM   1758  C   GLY A 360      27.006 -14.809 101.259  1.00 15.61           C  
ATOM   1759  O   GLY A 360      27.750 -14.668 100.291  1.00 15.68           O  
ATOM   1760  N   CYS A 361      25.753 -14.311 101.276  1.00 17.78           N  
ATOM   1761  CA  CYS A 361      25.195 -13.584 100.107  1.00 19.30           C  
ATOM   1762  C   CYS A 361      25.671 -12.162 100.028  1.00 16.28           C  
ATOM   1763  O   CYS A 361      26.451 -11.706 100.863  1.00 16.32           O  
ATOM   1764  CB  CYS A 361      23.615 -13.572 100.066  1.00 24.20           C  
ATOM   1765  SG  CYS A 361      22.592 -12.004 100.321  1.00 27.49           S  
ATOM   1766  N   LEU A 362      25.203 -11.482  98.986  1.00 14.59           N  
ATOM   1767  CA  LEU A 362      25.480 -10.086  98.790  1.00 13.83           C  
ATOM   1768  C   LEU A 362      24.817  -9.483 100.024  1.00 12.82           C  
ATOM   1769  O   LEU A 362      23.674  -9.795 100.325  1.00 12.97           O  
ATOM   1770  CB  LEU A 362      24.774  -9.576  97.532  1.00 14.76           C  
ATOM   1771  CG  LEU A 362      24.933 -10.345  96.217  1.00 16.08           C  
ATOM   1772  CD1 LEU A 362      24.660  -9.406  95.059  1.00 16.48           C  
ATOM   1773  CD2 LEU A 362      26.313 -10.908  96.083  1.00 16.51           C  
ATOM   1774  N   PRO A 363      25.528  -8.628 100.766  1.00 11.26           N  
ATOM   1775  CA  PRO A 363      24.931  -8.024 101.963  1.00  9.81           C  
ATOM   1776  C   PRO A 363      23.627  -7.279 101.640  1.00  8.03           C  
ATOM   1777  O   PRO A 363      23.450  -6.769 100.526  1.00  7.19           O  
ATOM   1778  CB  PRO A 363      26.022  -7.065 102.441  1.00 10.26           C  
ATOM   1779  CG  PRO A 363      27.300  -7.631 101.845  1.00 10.30           C  
ATOM   1780  CD  PRO A 363      26.853  -8.054 100.482  1.00 10.40           C  
ATOM   1781  N   PRO A 364      22.679  -7.233 102.594  1.00  6.77           N  
ATOM   1782  CA  PRO A 364      21.435  -6.515 102.293  1.00  6.19           C  
ATOM   1783  C   PRO A 364      21.666  -5.003 102.056  1.00  7.06           C  
ATOM   1784  O   PRO A 364      21.035  -4.412 101.185  1.00  6.35           O  
ATOM   1785  CB  PRO A 364      20.550  -6.813 103.510  1.00  3.69           C  
ATOM   1786  CG  PRO A 364      21.522  -7.146 104.597  1.00  3.93           C  
ATOM   1787  CD  PRO A 364      22.570  -7.961 103.868  1.00  4.76           C  
ATOM   1788  N   PHE A 365      22.573  -4.390 102.818  1.00  8.51           N  
ATOM   1789  CA  PHE A 365      22.869  -2.967 102.638  1.00 10.32           C  
ATOM   1790  C   PHE A 365      23.913  -2.840 101.525  1.00 10.07           C  
ATOM   1791  O   PHE A 365      25.010  -3.376 101.634  1.00 10.42           O  
ATOM   1792  CB  PHE A 365      23.382  -2.347 103.938  1.00 12.38           C  
ATOM   1793  CG  PHE A 365      23.380  -0.849 103.914  1.00 15.15           C  
ATOM   1794  CD1 PHE A 365      22.235  -0.158 103.493  1.00 16.40           C  
ATOM   1795  CD2 PHE A 365      24.524  -0.127 104.242  1.00 15.84           C  
ATOM   1796  CE1 PHE A 365      22.227   1.234 103.387  1.00 16.95           C  
ATOM   1797  CE2 PHE A 365      24.536   1.268 104.143  1.00 17.65           C  
ATOM   1798  CZ  PHE A 365      23.382   1.955 103.709  1.00 17.68           C  
ATOM   1799  N   PRO A 366      23.584  -2.116 100.442  1.00 10.43           N  
ATOM   1800  CA  PRO A 366      24.438  -1.899  99.269  1.00 12.06           C  
ATOM   1801  C   PRO A 366      25.832  -1.337  99.440  1.00 14.52           C  
ATOM   1802  O   PRO A 366      26.628  -1.392  98.502  1.00 15.89           O  
ATOM   1803  CB  PRO A 366      23.580  -0.996  98.373  1.00 11.80           C  
ATOM   1804  CG  PRO A 366      22.196  -1.255  98.837  1.00 10.60           C  
ATOM   1805  CD  PRO A 366      22.368  -1.299 100.324  1.00  9.98           C  
ATOM   1806  N   ALA A 367      26.144  -0.788 100.608  1.00 15.74           N  
ATOM   1807  CA  ALA A 367      27.467  -0.214 100.822  1.00 16.58           C  
ATOM   1808  C   ALA A 367      28.409  -1.173 101.529  1.00 18.22           C  
ATOM   1809  O   ALA A 367      29.571  -0.840 101.768  1.00 19.55           O  
ATOM   1810  CB  ALA A 367      27.358   1.002 101.619  1.00 16.56           C  
ATOM   1811  N   ASP A 368      27.917  -2.358 101.875  1.00 18.49           N  
ATOM   1812  CA  ASP A 368      28.752  -3.357 102.541  1.00 18.25           C  
ATOM   1813  C   ASP A 368      29.582  -4.140 101.528  1.00 16.09           C  
ATOM   1814  O   ASP A 368      29.124  -4.442 100.425  1.00 15.51           O  
ATOM   1815  CB  ASP A 368      27.885  -4.324 103.344  1.00 20.48           C  
ATOM   1816  CG  ASP A 368      27.333  -3.699 104.609  1.00 23.17           C  
ATOM   1817  OD1 ASP A 368      27.105  -2.469 104.622  1.00 24.32           O  
ATOM   1818  OD2 ASP A 368      27.109  -4.434 105.595  1.00 24.24           O  
ATOM   1819  N   VAL A 369      30.817  -4.441 101.904  1.00 15.44           N  
ATOM   1820  CA  VAL A 369      31.717  -5.204 101.048  1.00 14.74           C  
ATOM   1821  C   VAL A 369      31.759  -6.615 101.632  1.00 11.59           C  
ATOM   1822  O   VAL A 369      31.858  -6.789 102.843  1.00 11.18           O  
ATOM   1823  CB  VAL A 369      33.128  -4.559 101.028  1.00 15.73           C  
ATOM   1824  CG1 VAL A 369      34.107  -5.422 100.227  1.00 16.32           C  
ATOM   1825  CG2 VAL A 369      33.031  -3.172 100.409  1.00 15.98           C  
ATOM   1826  N   PHE A 370      31.653  -7.631 100.790  1.00 10.29           N  
ATOM   1827  CA  PHE A 370      31.660  -8.980 101.346  1.00  8.77           C  
ATOM   1828  C   PHE A 370      32.738  -9.915 100.816  1.00  6.66           C  
ATOM   1829  O   PHE A 370      33.245  -9.763  99.713  1.00  4.97           O  
ATOM   1830  CB  PHE A 370      30.275  -9.640 101.158  1.00  7.21           C  
ATOM   1831  CG  PHE A 370      29.978 -10.054  99.749  1.00  5.69           C  
ATOM   1832  CD1 PHE A 370      29.698  -9.101  98.772  1.00  5.22           C  
ATOM   1833  CD2 PHE A 370      30.023 -11.404  99.381  1.00  5.62           C  
ATOM   1834  CE1 PHE A 370      29.471  -9.475  97.445  1.00  4.88           C  
ATOM   1835  CE2 PHE A 370      29.799 -11.794  98.048  1.00  4.96           C  
ATOM   1836  CZ  PHE A 370      29.523 -10.822  97.080  1.00  4.56           C  
ATOM   1837  N   MET A 371      33.078 -10.890 101.643  1.00  8.26           N  
ATOM   1838  CA  MET A 371      34.032 -11.914 101.266  1.00  8.99           C  
ATOM   1839  C   MET A 371      33.248 -13.025 100.553  1.00  7.70           C  
ATOM   1840  O   MET A 371      32.195 -13.437 101.025  1.00  7.84           O  
ATOM   1841  CB  MET A 371      34.699 -12.481 102.512  1.00 11.67           C  
ATOM   1842  CG  MET A 371      35.803 -13.468 102.189  1.00 14.75           C  
ATOM   1843  SD  MET A 371      36.656 -14.060 103.648  1.00 16.97           S  
ATOM   1844  CE  MET A 371      37.039 -12.533 104.476  1.00 18.32           C  
ATOM   1845  N   VAL A 372      33.732 -13.469  99.399  1.00  7.36           N  
ATOM   1846  CA  VAL A 372      33.103 -14.561  98.654  1.00  7.29           C  
ATOM   1847  C   VAL A 372      33.330 -15.871  99.446  1.00  5.50           C  
ATOM   1848  O   VAL A 372      34.447 -16.170  99.863  1.00  4.61           O  
ATOM   1849  CB  VAL A 372      33.744 -14.695  97.250  1.00  8.21           C  
ATOM   1850  CG1 VAL A 372      33.149 -15.866  96.506  1.00  8.25           C  
ATOM   1851  CG2 VAL A 372      33.534 -13.415  96.459  1.00  8.70           C  
ATOM   1852  N   PRO A 373      32.263 -16.653  99.690  1.00  6.24           N  
ATOM   1853  CA  PRO A 373      32.390 -17.921 100.437  1.00  4.49           C  
ATOM   1854  C   PRO A 373      33.109 -19.069  99.699  1.00  2.58           C  
ATOM   1855  O   PRO A 373      33.086 -19.164  98.472  1.00  1.86           O  
ATOM   1856  CB  PRO A 373      30.933 -18.258 100.789  1.00  5.10           C  
ATOM   1857  CG  PRO A 373      30.162 -17.672  99.625  1.00  4.79           C  
ATOM   1858  CD  PRO A 373      30.847 -16.327  99.427  1.00  4.79           C  
ATOM   1859  N   GLN A 374      33.765 -19.935 100.459  1.00  3.26           N  
ATOM   1860  CA  GLN A 374      34.474 -21.072  99.874  1.00  4.10           C  
ATOM   1861  C   GLN A 374      33.506 -22.214  99.512  1.00  4.64           C  
ATOM   1862  O   GLN A 374      32.628 -22.569 100.297  1.00  4.33           O  
ATOM   1863  CB  GLN A 374      35.507 -21.584 100.869  1.00  3.25           C  
ATOM   1864  CG  GLN A 374      36.436 -22.620 100.311  1.00  3.06           C  
ATOM   1865  CD  GLN A 374      37.393 -23.136 101.350  1.00  3.42           C  
ATOM   1866  OE1 GLN A 374      37.351 -22.723 102.508  1.00  5.48           O  
ATOM   1867  NE2 GLN A 374      38.266 -24.039 100.951  1.00  3.21           N  
ATOM   1868  N   TYR A 375      33.672 -22.782  98.326  1.00  5.43           N  
ATOM   1869  CA  TYR A 375      32.835 -23.882  97.887  1.00  6.52           C  
ATOM   1870  C   TYR A 375      33.355 -25.229  98.394  1.00  7.97           C  
ATOM   1871  O   TYR A 375      34.541 -25.540  98.280  1.00  8.11           O  
ATOM   1872  CB  TYR A 375      32.775 -23.911  96.371  1.00  7.50           C  
ATOM   1873  CG  TYR A 375      31.964 -25.065  95.835  1.00  9.66           C  
ATOM   1874  CD1 TYR A 375      30.566 -25.060  95.916  1.00 10.43           C  
ATOM   1875  CD2 TYR A 375      32.589 -26.164  95.235  1.00  9.56           C  
ATOM   1876  CE1 TYR A 375      29.816 -26.122  95.405  1.00 10.38           C  
ATOM   1877  CE2 TYR A 375      31.854 -27.219  94.728  1.00  9.59           C  
ATOM   1878  CZ  TYR A 375      30.469 -27.196  94.811  1.00  9.52           C  
ATOM   1879  OH  TYR A 375      29.743 -28.228  94.278  1.00  7.94           O  
ATOM   1880  N   GLY A 376      32.457 -26.012  98.972  1.00  7.88           N  
ATOM   1881  CA  GLY A 376      32.797 -27.324  99.486  1.00  7.70           C  
ATOM   1882  C   GLY A 376      31.537 -28.134  99.278  1.00  7.04           C  
ATOM   1883  O   GLY A 376      30.497 -27.560  98.987  1.00  7.42           O  
ATOM   1884  N   TYR A 377      31.608 -29.452  99.389  1.00  6.89           N  
ATOM   1885  CA  TYR A 377      30.416 -30.271  99.218  1.00  7.23           C  
ATOM   1886  C   TYR A 377      30.606 -31.591  99.925  1.00  5.79           C  
ATOM   1887  O   TYR A 377      31.713 -31.934 100.322  1.00  5.80           O  
ATOM   1888  CB  TYR A 377      30.113 -30.481  97.724  1.00  8.51           C  
ATOM   1889  CG  TYR A 377      31.173 -31.249  96.970  1.00 10.71           C  
ATOM   1890  CD1 TYR A 377      31.200 -32.652  96.994  1.00 11.43           C  
ATOM   1891  CD2 TYR A 377      32.181 -30.579  96.262  1.00 11.34           C  
ATOM   1892  CE1 TYR A 377      32.203 -33.368  96.341  1.00 11.80           C  
ATOM   1893  CE2 TYR A 377      33.182 -31.282  95.603  1.00 12.23           C  
ATOM   1894  CZ  TYR A 377      33.185 -32.679  95.650  1.00 12.64           C  
ATOM   1895  OH  TYR A 377      34.174 -33.379  95.008  1.00 13.62           O  
ATOM   1896  N   LEU A 378      29.518 -32.316 100.119  1.00  6.61           N  
ATOM   1897  CA  LEU A 378      29.572 -33.615 100.776  1.00  6.86           C  
ATOM   1898  C   LEU A 378      29.136 -34.736  99.842  1.00  7.28           C  
ATOM   1899  O   LEU A 378      28.395 -34.504  98.882  1.00  6.62           O  
ATOM   1900  CB  LEU A 378      28.675 -33.617 102.005  1.00  6.82           C  
ATOM   1901  CG  LEU A 378      29.059 -32.666 103.139  1.00  6.64           C  
ATOM   1902  CD1 LEU A 378      27.967 -32.705 104.184  1.00  6.60           C  
ATOM   1903  CD2 LEU A 378      30.415 -33.063 103.737  1.00  5.52           C  
ATOM   1904  N   THR A 379      29.626 -35.948 100.099  1.00  8.82           N  
ATOM   1905  CA  THR A 379      29.213 -37.110  99.303  1.00 10.98           C  
ATOM   1906  C   THR A 379      28.778 -38.177 100.276  1.00 11.42           C  
ATOM   1907  O   THR A 379      28.564 -37.896 101.454  1.00 11.76           O  
ATOM   1908  CB  THR A 379      30.337 -37.694  98.370  1.00 11.84           C  
ATOM   1909  OG1 THR A 379      31.597 -37.748  99.054  1.00 10.40           O  
ATOM   1910  CG2 THR A 379      30.460 -36.857  97.135  1.00 13.95           C  
ATOM   1911  N   LEU A 380      28.648 -39.404  99.791  1.00 11.99           N  
ATOM   1912  CA  LEU A 380      28.213 -40.486 100.645  1.00 12.39           C  
ATOM   1913  C   LEU A 380      29.235 -40.802 101.697  1.00 11.68           C  
ATOM   1914  O   LEU A 380      30.436 -40.733 101.450  1.00 13.14           O  
ATOM   1915  CB  LEU A 380      27.936 -41.740  99.820  1.00 13.88           C  
ATOM   1916  CG  LEU A 380      26.907 -41.615  98.709  1.00 14.56           C  
ATOM   1917  CD1 LEU A 380      26.673 -42.977  98.123  1.00 14.81           C  
ATOM   1918  CD2 LEU A 380      25.602 -41.039  99.263  1.00 15.11           C  
ATOM   1919  N   ASN A 381      28.761 -41.154 102.878  1.00 10.84           N  
ATOM   1920  CA  ASN A 381      29.667 -41.512 103.938  1.00 12.04           C  
ATOM   1921  C   ASN A 381      29.114 -42.670 104.750  1.00 14.21           C  
ATOM   1922  O   ASN A 381      27.909 -42.885 104.820  1.00 14.70           O  
ATOM   1923  CB  ASN A 381      29.953 -40.305 104.855  1.00 10.89           C  
ATOM   1924  CG  ASN A 381      28.756 -39.903 105.702  1.00  8.85           C  
ATOM   1925  OD1 ASN A 381      27.806 -39.290 105.206  1.00  8.85           O  
ATOM   1926  ND2 ASN A 381      28.797 -40.249 106.985  1.00  7.06           N  
ATOM   1927  N   ASN A 382      30.015 -43.434 105.341  1.00 16.68           N  
ATOM   1928  CA  ASN A 382      29.646 -44.558 106.177  1.00 19.10           C  
ATOM   1929  C   ASN A 382      30.467 -44.252 107.413  1.00 19.22           C  
ATOM   1930  O   ASN A 382      31.610 -44.687 107.536  1.00 20.31           O  
ATOM   1931  CB  ASN A 382      30.089 -45.866 105.506  1.00 20.97           C  
ATOM   1932  CG  ASN A 382      29.634 -47.096 106.259  1.00 21.26           C  
ATOM   1933  OD1 ASN A 382      29.884 -47.234 107.456  1.00 20.98           O  
ATOM   1934  ND2 ASN A 382      28.970 -48.007 105.555  1.00 22.32           N  
ATOM   1935  N   GLY A 383      29.888 -43.482 108.327  1.00 19.06           N  
ATOM   1936  CA  GLY A 383      30.631 -43.079 109.507  1.00 18.95           C  
ATOM   1937  C   GLY A 383      31.482 -41.932 108.987  1.00 19.57           C  
ATOM   1938  O   GLY A 383      30.981 -41.086 108.238  1.00 19.32           O  
ATOM   1939  N   SER A 384      32.761 -41.892 109.345  1.00 20.14           N  
ATOM   1940  CA  SER A 384      33.629 -40.822 108.856  1.00 20.41           C  
ATOM   1941  C   SER A 384      34.335 -41.241 107.566  1.00 20.28           C  
ATOM   1942  O   SER A 384      35.097 -40.470 106.989  1.00 20.18           O  
ATOM   1943  CB  SER A 384      34.674 -40.461 109.905  1.00 20.61           C  
ATOM   1944  OG  SER A 384      35.543 -41.554 110.143  1.00 21.15           O  
ATOM   1945  N   GLN A 385      34.061 -42.460 107.114  1.00 20.49           N  
ATOM   1946  CA  GLN A 385      34.681 -42.990 105.909  1.00 21.60           C  
ATOM   1947  C   GLN A 385      33.831 -42.824 104.662  1.00 20.49           C  
ATOM   1948  O   GLN A 385      32.629 -42.592 104.736  1.00 20.73           O  
ATOM   1949  CB  GLN A 385      34.982 -44.477 106.081  1.00 24.28           C  
ATOM   1950  CG  GLN A 385      35.894 -44.818 107.235  1.00 27.04           C  
ATOM   1951  CD  GLN A 385      36.232 -46.298 107.264  1.00 29.61           C  
ATOM   1952  OE1 GLN A 385      37.276 -46.722 106.763  1.00 30.74           O  
ATOM   1953  NE2 GLN A 385      35.341 -47.096 107.840  1.00 30.26           N  
ATOM   1954  N   ALA A 386      34.471 -42.954 103.511  1.00 20.04           N  
ATOM   1955  CA  ALA A 386      33.779 -42.854 102.238  1.00 20.50           C  
ATOM   1956  C   ALA A 386      33.341 -44.260 101.825  1.00 21.74           C  
ATOM   1957  O   ALA A 386      33.633 -45.241 102.510  1.00 21.62           O  
ATOM   1958  CB  ALA A 386      34.718 -42.281 101.180  1.00 19.59           C  
ATOM   1959  N   VAL A 387      32.634 -44.344 100.705  1.00 22.96           N  
ATOM   1960  CA  VAL A 387      32.196 -45.617 100.145  1.00 24.73           C  
ATOM   1961  C   VAL A 387      32.537 -45.505  98.666  1.00 25.27           C  
ATOM   1962  O   VAL A 387      32.969 -44.443  98.210  1.00 24.62           O  
ATOM   1963  CB  VAL A 387      30.677 -45.868 100.340  1.00 25.99           C  
ATOM   1964  CG1 VAL A 387      30.366 -45.941 101.823  1.00 27.12           C  
ATOM   1965  CG2 VAL A 387      29.850 -44.775  99.641  1.00 25.05           C  
ATOM   1966  N   CYS A 388      32.347 -46.571  97.903  1.00 26.82           N  
ATOM   1967  CA  CYS A 388      32.728 -46.509  96.497  1.00 29.41           C  
ATOM   1968  C   CYS A 388      31.986 -45.558  95.588  1.00 26.22           C  
ATOM   1969  O   CYS A 388      32.564 -45.041  94.630  1.00 25.60           O  
ATOM   1970  CB  CYS A 388      32.669 -47.878  95.869  1.00 35.63           C  
ATOM   1971  SG  CYS A 388      33.526 -47.917  94.269  1.00 39.82           S  
ATOM   1972  N   ARG A 389      30.706 -45.346  95.860  1.00 24.25           N  
ATOM   1973  CA  ARG A 389      29.933 -44.436  95.044  1.00 22.47           C  
ATOM   1974  C   ARG A 389      30.196 -42.975  95.409  1.00 19.04           C  
ATOM   1975  O   ARG A 389      29.677 -42.075  94.751  1.00 19.76           O  
ATOM   1976  CB  ARG A 389      28.437 -44.785  95.132  1.00 24.27           C  
ATOM   1977  CG  ARG A 389      28.063 -45.963  94.226  1.00 25.05           C  
ATOM   1978  CD  ARG A 389      26.624 -46.409  94.384  1.00 25.57           C  
ATOM   1979  NE  ARG A 389      26.278 -47.491  93.461  1.00 25.98           N  
ATOM   1980  CZ  ARG A 389      26.595 -48.772  93.641  1.00 27.28           C  
ATOM   1981  NH1 ARG A 389      27.278 -49.161  94.715  1.00 27.42           N  
ATOM   1982  NH2 ARG A 389      26.211 -49.679  92.749  1.00 27.82           N  
ATOM   1983  N   SER A 390      31.001 -42.738  96.445  1.00 15.48           N  
ATOM   1984  CA  SER A 390      31.346 -41.373  96.837  1.00 12.28           C  
ATOM   1985  C   SER A 390      32.014 -40.706  95.645  1.00 11.53           C  
ATOM   1986  O   SER A 390      32.900 -41.280  95.028  1.00 13.32           O  
ATOM   1987  CB  SER A 390      32.306 -41.361  98.017  1.00  9.75           C  
ATOM   1988  OG  SER A 390      31.670 -41.754  99.212  1.00  8.47           O  
ATOM   1989  N   SER A 391      31.566 -39.506  95.312  1.00  9.97           N  
ATOM   1990  CA  SER A 391      32.101 -38.776  94.179  1.00  9.69           C  
ATOM   1991  C   SER A 391      33.122 -37.708  94.537  1.00 10.08           C  
ATOM   1992  O   SER A 391      33.063 -37.091  95.598  1.00  9.63           O  
ATOM   1993  CB  SER A 391      30.970 -38.093  93.401  1.00  8.93           C  
ATOM   1994  OG  SER A 391      30.351 -38.994  92.512  1.00  9.40           O  
ATOM   1995  N   PHE A 392      34.061 -37.507  93.622  1.00  9.55           N  
ATOM   1996  CA  PHE A 392      35.067 -36.493  93.775  1.00  9.04           C  
ATOM   1997  C   PHE A 392      35.004 -35.683  92.505  1.00  7.94           C  
ATOM   1998  O   PHE A 392      35.101 -36.218  91.411  1.00  7.16           O  
ATOM   1999  CB  PHE A 392      36.463 -37.094  93.953  1.00 11.04           C  
ATOM   2000  CG  PHE A 392      37.565 -36.060  93.941  1.00 12.76           C  
ATOM   2001  CD1 PHE A 392      37.515 -34.957  94.802  1.00 12.84           C  
ATOM   2002  CD2 PHE A 392      38.627 -36.160  93.047  1.00 13.40           C  
ATOM   2003  CE1 PHE A 392      38.492 -33.968  94.770  1.00 12.37           C  
ATOM   2004  CE2 PHE A 392      39.616 -35.172  93.005  1.00 13.73           C  
ATOM   2005  CZ  PHE A 392      39.544 -34.069  93.874  1.00 13.00           C  
ATOM   2006  N   TYR A 393      34.802 -34.384  92.650  1.00  8.99           N  
ATOM   2007  CA  TYR A 393      34.735 -33.519  91.494  1.00 10.77           C  
ATOM   2008  C   TYR A 393      35.877 -32.555  91.506  1.00 12.35           C  
ATOM   2009  O   TYR A 393      36.163 -31.929  92.525  1.00 13.18           O  
ATOM   2010  CB  TYR A 393      33.438 -32.712  91.472  1.00 11.56           C  
ATOM   2011  CG  TYR A 393      32.246 -33.535  91.132  1.00 10.83           C  
ATOM   2012  CD1 TYR A 393      31.580 -34.267  92.116  1.00 11.25           C  
ATOM   2013  CD2 TYR A 393      31.827 -33.657  89.811  1.00 10.48           C  
ATOM   2014  CE1 TYR A 393      30.531 -35.108  91.787  1.00 11.02           C  
ATOM   2015  CE2 TYR A 393      30.773 -34.499  89.472  1.00 10.66           C  
ATOM   2016  CZ  TYR A 393      30.137 -35.221  90.466  1.00 11.31           C  
ATOM   2017  OH  TYR A 393      29.111 -36.077  90.133  1.00 13.33           O  
ATOM   2018  N   CYS A 394      36.546 -32.448  90.374  1.00 13.51           N  
ATOM   2019  CA  CYS A 394      37.635 -31.504  90.249  1.00 14.79           C  
ATOM   2020  C   CYS A 394      37.074 -30.460  89.296  1.00 13.89           C  
ATOM   2021  O   CYS A 394      36.725 -30.787  88.167  1.00 13.29           O  
ATOM   2022  CB  CYS A 394      38.867 -32.178  89.644  1.00 16.18           C  
ATOM   2023  SG  CYS A 394      40.170 -31.001  89.228  1.00 17.96           S  
ATOM   2024  N   LEU A 395      36.992 -29.210  89.737  1.00 14.55           N  
ATOM   2025  CA  LEU A 395      36.427 -28.158  88.891  1.00 15.52           C  
ATOM   2026  C   LEU A 395      37.248 -27.682  87.703  1.00 16.50           C  
ATOM   2027  O   LEU A 395      36.685 -27.126  86.763  1.00 15.90           O  
ATOM   2028  CB  LEU A 395      36.017 -26.951  89.746  1.00 14.96           C  
ATOM   2029  CG  LEU A 395      34.743 -27.104  90.580  1.00 14.17           C  
ATOM   2030  CD1 LEU A 395      34.941 -28.129  91.690  1.00 14.79           C  
ATOM   2031  CD2 LEU A 395      34.358 -25.748  91.149  1.00 13.42           C  
ATOM   2032  N   GLU A 396      38.567 -27.874  87.730  1.00 19.17           N  
ATOM   2033  CA  GLU A 396      39.399 -27.459  86.591  1.00 21.25           C  
ATOM   2034  C   GLU A 396      39.098 -28.331  85.384  1.00 23.10           C  
ATOM   2035  O   GLU A 396      39.358 -27.940  84.247  1.00 24.18           O  
ATOM   2036  CB  GLU A 396      40.887 -27.569  86.907  1.00 21.88           C  
ATOM   2037  CG  GLU A 396      41.425 -26.491  87.816  1.00 22.76           C  
ATOM   2038  CD  GLU A 396      40.924 -26.642  89.219  1.00 24.20           C  
ATOM   2039  OE1 GLU A 396      40.402 -27.732  89.531  1.00 24.60           O  
ATOM   2040  OE2 GLU A 396      41.059 -25.683  90.011  1.00 24.81           O  
ATOM   2041  N   TYR A 397      38.554 -29.517  85.636  1.00 24.09           N  
ATOM   2042  CA  TYR A 397      38.205 -30.441  84.569  1.00 25.10           C  
ATOM   2043  C   TYR A 397      37.229 -29.766  83.599  1.00 24.90           C  
ATOM   2044  O   TYR A 397      37.262 -30.019  82.394  1.00 25.06           O  
ATOM   2045  CB  TYR A 397      37.577 -31.705  85.171  1.00 26.85           C  
ATOM   2046  CG  TYR A 397      37.143 -32.739  84.158  1.00 28.85           C  
ATOM   2047  CD1 TYR A 397      38.083 -33.419  83.377  1.00 29.51           C  
ATOM   2048  CD2 TYR A 397      35.787 -33.019  83.954  1.00 30.31           C  
ATOM   2049  CE1 TYR A 397      37.688 -34.349  82.414  1.00 30.25           C  
ATOM   2050  CE2 TYR A 397      35.375 -33.952  82.986  1.00 31.16           C  
ATOM   2051  CZ  TYR A 397      36.336 -34.611  82.217  1.00 31.03           C  
ATOM   2052  OH  TYR A 397      35.943 -35.496  81.232  1.00 31.02           O  
ATOM   2053  N   PHE A 398      36.368 -28.899  84.127  1.00 24.89           N  
ATOM   2054  CA  PHE A 398      35.386 -28.187  83.304  1.00 24.90           C  
ATOM   2055  C   PHE A 398      35.995 -26.937  82.675  1.00 24.99           C  
ATOM   2056  O   PHE A 398      36.948 -26.363  83.202  1.00 24.91           O  
ATOM   2057  CB  PHE A 398      34.178 -27.752  84.141  1.00 25.19           C  
ATOM   2058  CG  PHE A 398      33.554 -28.860  84.946  1.00 26.81           C  
ATOM   2059  CD1 PHE A 398      34.116 -29.267  86.152  1.00 27.65           C  
ATOM   2060  CD2 PHE A 398      32.417 -29.513  84.485  1.00 27.90           C  
ATOM   2061  CE1 PHE A 398      33.561 -30.309  86.888  1.00 28.70           C  
ATOM   2062  CE2 PHE A 398      31.853 -30.553  85.210  1.00 29.10           C  
ATOM   2063  CZ  PHE A 398      32.427 -30.956  86.419  1.00 29.35           C  
ATOM   2064  N   PRO A 399      35.457 -26.502  81.527  1.00 25.56           N  
ATOM   2065  CA  PRO A 399      35.978 -25.299  80.867  1.00 26.24           C  
ATOM   2066  C   PRO A 399      35.459 -24.018  81.534  1.00 26.39           C  
ATOM   2067  O   PRO A 399      34.250 -23.793  81.614  1.00 26.94           O  
ATOM   2068  CB  PRO A 399      35.471 -25.447  79.435  1.00 26.03           C  
ATOM   2069  CG  PRO A 399      34.171 -26.163  79.624  1.00 25.87           C  
ATOM   2070  CD  PRO A 399      34.539 -27.228  80.632  1.00 25.52           C  
ATOM   2071  N   SER A 400      36.377 -23.184  82.010  1.00 25.85           N  
ATOM   2072  CA  SER A 400      36.004 -21.936  82.657  1.00 24.87           C  
ATOM   2073  C   SER A 400      36.464 -20.754  81.827  1.00 25.71           C  
ATOM   2074  O   SER A 400      37.155 -20.914  80.821  1.00 26.42           O  
ATOM   2075  CB  SER A 400      36.621 -21.840  84.054  1.00 23.74           C  
ATOM   2076  OG  SER A 400      38.036 -21.786  83.983  1.00 24.28           O  
ATOM   2077  N   GLN A 401      36.079 -19.563  82.264  1.00 25.83           N  
ATOM   2078  CA  GLN A 401      36.442 -18.337  81.580  1.00 26.49           C  
ATOM   2079  C   GLN A 401      37.531 -17.633  82.389  1.00 24.76           C  
ATOM   2080  O   GLN A 401      37.473 -17.603  83.615  1.00 23.95           O  
ATOM   2081  CB  GLN A 401      35.207 -17.454  81.471  1.00 29.19           C  
ATOM   2082  CG  GLN A 401      35.275 -16.396  80.411  1.00 31.80           C  
ATOM   2083  CD  GLN A 401      33.961 -15.655  80.290  1.00 33.77           C  
ATOM   2084  OE1 GLN A 401      32.894 -16.278  80.189  1.00 34.20           O  
ATOM   2085  NE2 GLN A 401      34.025 -14.321  80.299  1.00 33.86           N  
ATOM   2086  N   MET A 402      38.535 -17.090  81.706  1.00 25.03           N  
ATOM   2087  CA  MET A 402      39.625 -16.388  82.380  1.00 25.83           C  
ATOM   2088  C   MET A 402      39.372 -14.899  82.302  1.00 24.89           C  
ATOM   2089  O   MET A 402      39.054 -14.368  81.238  1.00 24.79           O  
ATOM   2090  CB  MET A 402      40.967 -16.675  81.713  1.00 28.56           C  
ATOM   2091  CG  MET A 402      41.282 -18.142  81.512  1.00 31.69           C  
ATOM   2092  SD  MET A 402      41.711 -18.982  83.030  1.00 34.39           S  
ATOM   2093  CE  MET A 402      43.509 -18.690  83.104  1.00 34.02           C  
ATOM   2094  N   LEU A 403      39.523 -14.218  83.427  1.00 25.19           N  
ATOM   2095  CA  LEU A 403      39.308 -12.784  83.446  1.00 25.92           C  
ATOM   2096  C   LEU A 403      40.467 -12.056  84.091  1.00 27.22           C  
ATOM   2097  O   LEU A 403      40.874 -12.380  85.204  1.00 26.78           O  
ATOM   2098  CB  LEU A 403      38.043 -12.429  84.227  1.00 25.19           C  
ATOM   2099  CG  LEU A 403      36.703 -13.093  83.930  1.00 25.07           C  
ATOM   2100  CD1 LEU A 403      35.676 -12.560  84.919  1.00 24.68           C  
ATOM   2101  CD2 LEU A 403      36.267 -12.802  82.507  1.00 25.57           C  
ATOM   2102  N   ARG A 404      41.002 -11.073  83.382  1.00 29.32           N  
ATOM   2103  CA  ARG A 404      42.063 -10.250  83.938  1.00 31.36           C  
ATOM   2104  C   ARG A 404      41.447  -8.861  84.057  1.00 30.88           C  
ATOM   2105  O   ARG A 404      40.348  -8.627  83.550  1.00 30.09           O  
ATOM   2106  CB  ARG A 404      43.288 -10.219  83.022  1.00 32.97           C  
ATOM   2107  CG  ARG A 404      42.998  -9.891  81.579  1.00 34.98           C  
ATOM   2108  CD  ARG A 404      44.302  -9.764  80.808  1.00 37.20           C  
ATOM   2109  NE  ARG A 404      45.116 -10.977  80.902  1.00 38.79           N  
ATOM   2110  CZ  ARG A 404      44.841 -12.119  80.274  1.00 39.81           C  
ATOM   2111  NH1 ARG A 404      43.768 -12.216  79.493  1.00 39.94           N  
ATOM   2112  NH2 ARG A 404      45.638 -13.171  80.434  1.00 39.92           N  
ATOM   2113  N   THR A 405      42.137  -7.951  84.738  1.00 31.23           N  
ATOM   2114  CA  THR A 405      41.642  -6.587  84.897  1.00 30.92           C  
ATOM   2115  C   THR A 405      41.188  -6.046  83.548  1.00 30.16           C  
ATOM   2116  O   THR A 405      41.951  -6.068  82.585  1.00 30.34           O  
ATOM   2117  CB  THR A 405      42.740  -5.648  85.436  1.00 31.76           C  
ATOM   2118  OG1 THR A 405      43.139  -6.069  86.748  1.00 31.87           O  
ATOM   2119  CG2 THR A 405      42.225  -4.221  85.490  1.00 31.98           C  
ATOM   2120  N   GLY A 406      39.953  -5.558  83.479  1.00 29.52           N  
ATOM   2121  CA  GLY A 406      39.449  -5.021  82.227  1.00 28.97           C  
ATOM   2122  C   GLY A 406      38.419  -5.925  81.584  1.00 28.98           C  
ATOM   2123  O   GLY A 406      37.569  -5.470  80.814  1.00 29.39           O  
ATOM   2124  N   ASN A 407      38.500  -7.215  81.895  1.00 28.60           N  
ATOM   2125  CA  ASN A 407      37.560  -8.194  81.364  1.00 28.20           C  
ATOM   2126  C   ASN A 407      36.347  -8.224  82.278  1.00 27.78           C  
ATOM   2127  O   ASN A 407      36.460  -7.998  83.489  1.00 28.18           O  
ATOM   2128  CB  ASN A 407      38.181  -9.594  81.346  1.00 28.40           C  
ATOM   2129  CG  ASN A 407      39.206  -9.774  80.250  1.00 28.59           C  
ATOM   2130  OD1 ASN A 407      40.041 -10.679  80.318  1.00 28.39           O  
ATOM   2131  ND2 ASN A 407      39.144  -8.928  79.224  1.00 29.00           N  
ATOM   2132  N   ASN A 408      35.179  -8.487  81.709  1.00 26.53           N  
ATOM   2133  CA  ASN A 408      33.993  -8.567  82.535  1.00 25.80           C  
ATOM   2134  C   ASN A 408      33.218  -9.839  82.192  1.00 23.15           C  
ATOM   2135  O   ASN A 408      33.402 -10.430  81.129  1.00 23.09           O  
ATOM   2136  CB  ASN A 408      33.142  -7.297  82.387  1.00 27.50           C  
ATOM   2137  CG  ASN A 408      32.600  -7.118  81.003  1.00 29.47           C  
ATOM   2138  OD1 ASN A 408      31.786  -7.919  80.533  1.00 30.15           O  
ATOM   2139  ND2 ASN A 408      33.042  -6.062  80.329  1.00 30.44           N  
ATOM   2140  N   PHE A 409      32.382 -10.275  83.121  1.00 21.11           N  
ATOM   2141  CA  PHE A 409      31.605 -11.495  82.961  1.00 18.76           C  
ATOM   2142  C   PHE A 409      30.101 -11.225  82.985  1.00 18.20           C  
ATOM   2143  O   PHE A 409      29.607 -10.505  83.850  1.00 17.09           O  
ATOM   2144  CB  PHE A 409      31.973 -12.443  84.094  1.00 18.19           C  
ATOM   2145  CG  PHE A 409      31.228 -13.733  84.070  1.00 19.37           C  
ATOM   2146  CD1 PHE A 409      31.495 -14.687  83.091  1.00 19.42           C  
ATOM   2147  CD2 PHE A 409      30.251 -14.004  85.033  1.00 19.67           C  
ATOM   2148  CE1 PHE A 409      30.807 -15.890  83.069  1.00 19.71           C  
ATOM   2149  CE2 PHE A 409      29.553 -15.209  85.022  1.00 20.06           C  
ATOM   2150  CZ  PHE A 409      29.831 -16.155  84.038  1.00 20.50           C  
ATOM   2151  N   THR A 410      29.376 -11.800  82.031  1.00 18.78           N  
ATOM   2152  CA  THR A 410      27.930 -11.636  81.981  1.00 19.62           C  
ATOM   2153  C   THR A 410      27.270 -12.997  81.848  1.00 18.77           C  
ATOM   2154  O   THR A 410      27.790 -13.900  81.196  1.00 19.13           O  
ATOM   2155  CB  THR A 410      27.463 -10.756  80.789  1.00 21.38           C  
ATOM   2156  OG1 THR A 410      27.894 -11.349  79.556  1.00 22.47           O  
ATOM   2157  CG2 THR A 410      28.017  -9.343  80.904  1.00 21.63           C  
ATOM   2158  N   PHE A 411      26.107 -13.127  82.465  1.00 17.21           N  
ATOM   2159  CA  PHE A 411      25.361 -14.366  82.437  1.00 15.90           C  
ATOM   2160  C   PHE A 411      23.856 -14.078  82.547  1.00 14.18           C  
ATOM   2161  O   PHE A 411      23.418 -13.390  83.465  1.00 13.26           O  
ATOM   2162  CB  PHE A 411      25.825 -15.246  83.603  1.00 16.77           C  
ATOM   2163  CG  PHE A 411      25.001 -16.471  83.797  1.00 18.27           C  
ATOM   2164  CD1 PHE A 411      25.002 -17.480  82.839  1.00 18.94           C  
ATOM   2165  CD2 PHE A 411      24.188 -16.607  84.926  1.00 18.89           C  
ATOM   2166  CE1 PHE A 411      24.202 -18.620  82.992  1.00 18.83           C  
ATOM   2167  CE2 PHE A 411      23.385 -17.734  85.094  1.00 19.27           C  
ATOM   2168  CZ  PHE A 411      23.392 -18.745  84.122  1.00 19.40           C  
ATOM   2169  N   SER A 412      23.072 -14.578  81.600  1.00 14.07           N  
ATOM   2170  CA  SER A 412      21.631 -14.377  81.661  1.00 14.93           C  
ATOM   2171  C   SER A 412      20.929 -15.722  81.850  1.00 14.98           C  
ATOM   2172  O   SER A 412      21.330 -16.732  81.280  1.00 15.60           O  
ATOM   2173  CB  SER A 412      21.122 -13.659  80.411  1.00 15.53           C  
ATOM   2174  OG  SER A 412      21.379 -14.409  79.243  1.00 17.44           O  
ATOM   2175  N   TYR A 413      19.887 -15.724  82.676  1.00 13.75           N  
ATOM   2176  CA  TYR A 413      19.138 -16.931  82.992  1.00 11.78           C  
ATOM   2177  C   TYR A 413      17.640 -16.669  83.032  1.00 11.70           C  
ATOM   2178  O   TYR A 413      17.191 -15.604  83.444  1.00 11.53           O  
ATOM   2179  CB  TYR A 413      19.637 -17.472  84.338  1.00 10.86           C  
ATOM   2180  CG  TYR A 413      18.741 -18.463  85.053  1.00 10.65           C  
ATOM   2181  CD1 TYR A 413      17.742 -18.024  85.927  1.00  9.98           C  
ATOM   2182  CD2 TYR A 413      18.915 -19.849  84.890  1.00 10.09           C  
ATOM   2183  CE1 TYR A 413      16.943 -18.927  86.625  1.00  9.12           C  
ATOM   2184  CE2 TYR A 413      18.120 -20.759  85.583  1.00  9.20           C  
ATOM   2185  CZ  TYR A 413      17.134 -20.288  86.452  1.00  9.12           C  
ATOM   2186  OH  TYR A 413      16.352 -21.169  87.164  1.00  8.90           O  
ATOM   2187  N   THR A 414      16.867 -17.649  82.582  1.00 11.85           N  
ATOM   2188  CA  THR A 414      15.416 -17.545  82.579  1.00 10.52           C  
ATOM   2189  C   THR A 414      14.876 -18.582  83.558  1.00  8.52           C  
ATOM   2190  O   THR A 414      15.279 -19.739  83.508  1.00  8.10           O  
ATOM   2191  CB  THR A 414      14.856 -17.826  81.180  1.00 11.70           C  
ATOM   2192  OG1 THR A 414      15.271 -16.794  80.282  1.00 13.02           O  
ATOM   2193  CG2 THR A 414      13.342 -17.867  81.200  1.00 12.75           C  
ATOM   2194  N   PHE A 415      13.995 -18.169  84.468  1.00  7.67           N  
ATOM   2195  CA  PHE A 415      13.404 -19.115  85.411  1.00  7.14           C  
ATOM   2196  C   PHE A 415      12.321 -19.910  84.693  1.00  9.86           C  
ATOM   2197  O   PHE A 415      11.697 -19.434  83.741  1.00 10.44           O  
ATOM   2198  CB  PHE A 415      12.758 -18.413  86.609  1.00  3.97           C  
ATOM   2199  CG  PHE A 415      13.732 -17.800  87.560  1.00  1.63           C  
ATOM   2200  CD1 PHE A 415      14.272 -16.533  87.305  1.00  0.07           C  
ATOM   2201  CD2 PHE A 415      14.103 -18.473  88.723  1.00  0.34           C  
ATOM   2202  CE1 PHE A 415      15.155 -15.948  88.188  1.00  0.00           C  
ATOM   2203  CE2 PHE A 415      14.988 -17.902  89.617  1.00  0.00           C  
ATOM   2204  CZ  PHE A 415      15.518 -16.625  89.351  1.00  0.00           C  
ATOM   2205  N   GLU A 416      12.111 -21.134  85.143  1.00 12.59           N  
ATOM   2206  CA  GLU A 416      11.089 -21.990  84.564  1.00 15.68           C  
ATOM   2207  C   GLU A 416       9.742 -21.555  85.150  1.00 18.02           C  
ATOM   2208  O   GLU A 416       9.697 -20.823  86.141  1.00 18.29           O  
ATOM   2209  CB  GLU A 416      11.368 -23.442  84.951  1.00 15.48           C  
ATOM   2210  CG  GLU A 416      11.246 -23.695  86.447  1.00 16.18           C  
ATOM   2211  CD  GLU A 416      12.168 -24.819  86.952  1.00 17.36           C  
ATOM   2212  OE1 GLU A 416      13.404 -24.687  86.801  1.00 17.25           O  
ATOM   2213  OE2 GLU A 416      11.658 -25.827  87.505  1.00 17.55           O  
ATOM   2214  N   ASP A 417       8.650 -22.004  84.544  1.00 20.12           N  
ATOM   2215  CA  ASP A 417       7.325 -21.682  85.056  1.00 21.97           C  
ATOM   2216  C   ASP A 417       7.174 -22.306  86.432  1.00 19.71           C  
ATOM   2217  O   ASP A 417       7.248 -23.524  86.586  1.00 20.86           O  
ATOM   2218  CB  ASP A 417       6.246 -22.224  84.123  1.00 26.04           C  
ATOM   2219  CG  ASP A 417       5.837 -21.219  83.068  1.00 30.27           C  
ATOM   2220  OD1 ASP A 417       6.726 -20.513  82.535  1.00 31.74           O  
ATOM   2221  OD2 ASP A 417       4.626 -21.134  82.764  1.00 31.77           O  
ATOM   2222  N   VAL A 418       6.982 -21.463  87.431  1.00 17.01           N  
ATOM   2223  CA  VAL A 418       6.822 -21.916  88.798  1.00 15.99           C  
ATOM   2224  C   VAL A 418       5.561 -21.205  89.305  1.00 14.77           C  
ATOM   2225  O   VAL A 418       5.185 -20.157  88.785  1.00 14.98           O  
ATOM   2226  CB  VAL A 418       8.087 -21.529  89.650  1.00 16.65           C  
ATOM   2227  CG1 VAL A 418       8.197 -20.007  89.793  1.00 16.61           C  
ATOM   2228  CG2 VAL A 418       8.032 -22.179  91.011  1.00 17.37           C  
ATOM   2229  N   PRO A 419       4.865 -21.784  90.291  1.00 13.82           N  
ATOM   2230  CA  PRO A 419       3.657 -21.112  90.792  1.00 13.18           C  
ATOM   2231  C   PRO A 419       4.006 -19.782  91.472  1.00 11.61           C  
ATOM   2232  O   PRO A 419       5.110 -19.615  91.991  1.00 11.87           O  
ATOM   2233  CB  PRO A 419       3.101 -22.100  91.817  1.00 13.63           C  
ATOM   2234  CG  PRO A 419       3.691 -23.428  91.401  1.00 14.19           C  
ATOM   2235  CD  PRO A 419       5.073 -23.081  90.958  1.00 13.83           C  
ATOM   2236  N   PHE A 420       3.068 -18.846  91.471  1.00  9.72           N  
ATOM   2237  CA  PHE A 420       3.269 -17.573  92.146  1.00  8.45           C  
ATOM   2238  C   PHE A 420       3.282 -17.871  93.640  1.00  6.40           C  
ATOM   2239  O   PHE A 420       2.575 -18.769  94.096  1.00  7.42           O  
ATOM   2240  CB  PHE A 420       2.098 -16.635  91.864  1.00  8.35           C  
ATOM   2241  CG  PHE A 420       2.183 -15.925  90.551  1.00  8.93           C  
ATOM   2242  CD1 PHE A 420       2.865 -14.714  90.447  1.00  7.90           C  
ATOM   2243  CD2 PHE A 420       1.559 -16.454  89.417  1.00  9.74           C  
ATOM   2244  CE1 PHE A 420       2.931 -14.027  89.245  1.00  8.57           C  
ATOM   2245  CE2 PHE A 420       1.615 -15.785  88.199  1.00 10.89           C  
ATOM   2246  CZ  PHE A 420       2.305 -14.559  88.106  1.00 10.85           C  
ATOM   2247  N   HIS A 421       4.085 -17.147  94.404  1.00  4.32           N  
ATOM   2248  CA  HIS A 421       4.081 -17.334  95.846  1.00  3.56           C  
ATOM   2249  C   HIS A 421       2.788 -16.673  96.284  1.00  4.51           C  
ATOM   2250  O   HIS A 421       2.366 -15.692  95.678  1.00  5.57           O  
ATOM   2251  CB  HIS A 421       5.255 -16.615  96.515  1.00  2.43           C  
ATOM   2252  CG  HIS A 421       5.171 -16.603  98.005  1.00  2.97           C  
ATOM   2253  ND1 HIS A 421       5.407 -17.725  98.773  1.00  4.07           N  
ATOM   2254  CD2 HIS A 421       4.793 -15.629  98.869  1.00  2.50           C  
ATOM   2255  CE1 HIS A 421       5.169 -17.444 100.040  1.00  3.86           C  
ATOM   2256  NE2 HIS A 421       4.793 -16.180 100.126  1.00  2.81           N  
ATOM   2257  N   SER A 422       2.143 -17.182  97.323  1.00  4.93           N  
ATOM   2258  CA  SER A 422       0.899 -16.554  97.754  1.00  6.02           C  
ATOM   2259  C   SER A 422       1.146 -15.521  98.863  1.00  6.73           C  
ATOM   2260  O   SER A 422       1.331 -15.866 100.032  1.00  7.34           O  
ATOM   2261  CB  SER A 422      -0.083 -17.623  98.228  1.00  5.94           C  
ATOM   2262  OG  SER A 422       0.415 -18.282  99.374  1.00  7.15           O  
ATOM   2263  N   SER A 423       1.153 -14.253  98.479  1.00  7.19           N  
ATOM   2264  CA  SER A 423       1.385 -13.148  99.407  1.00  6.95           C  
ATOM   2265  C   SER A 423       0.069 -12.566  99.891  1.00  7.60           C  
ATOM   2266  O   SER A 423      -0.266 -11.417  99.621  1.00  9.04           O  
ATOM   2267  CB  SER A 423       2.227 -12.074  98.717  1.00  5.79           C  
ATOM   2268  OG  SER A 423       1.874 -11.931  97.354  1.00  5.07           O  
ATOM   2269  N   TYR A 424      -0.680 -13.375 100.617  1.00  8.45           N  
ATOM   2270  CA  TYR A 424      -1.968 -12.970 101.141  1.00  7.98           C  
ATOM   2271  C   TYR A 424      -2.357 -14.000 102.143  1.00  6.26           C  
ATOM   2272  O   TYR A 424      -1.863 -15.121 102.116  1.00  6.05           O  
ATOM   2273  CB  TYR A 424      -3.030 -12.900 100.022  1.00  8.91           C  
ATOM   2274  CG  TYR A 424      -3.255 -14.209  99.299  1.00  9.91           C  
ATOM   2275  CD1 TYR A 424      -3.951 -15.272  99.913  1.00 10.09           C  
ATOM   2276  CD2 TYR A 424      -2.710 -14.421  98.033  1.00 10.02           C  
ATOM   2277  CE1 TYR A 424      -4.076 -16.499  99.289  1.00 10.47           C  
ATOM   2278  CE2 TYR A 424      -2.838 -15.647  97.393  1.00 11.49           C  
ATOM   2279  CZ  TYR A 424      -3.517 -16.683  98.026  1.00 11.83           C  
ATOM   2280  OH  TYR A 424      -3.608 -17.903  97.398  1.00 13.34           O  
ATOM   2281  N   ALA A 425      -3.224 -13.602 103.054  1.00  6.33           N  
ATOM   2282  CA  ALA A 425      -3.728 -14.491 104.071  1.00  5.98           C  
ATOM   2283  C   ALA A 425      -5.177 -14.724 103.642  1.00  5.93           C  
ATOM   2284  O   ALA A 425      -5.697 -13.984 102.814  1.00  5.41           O  
ATOM   2285  CB  ALA A 425      -3.665 -13.811 105.423  1.00  5.90           C  
ATOM   2286  N   HIS A 426      -5.825 -15.754 104.169  1.00  6.89           N  
ATOM   2287  CA  HIS A 426      -7.216 -16.008 103.806  1.00  7.11           C  
ATOM   2288  C   HIS A 426      -8.156 -15.348 104.821  1.00  7.35           C  
ATOM   2289  O   HIS A 426      -7.896 -15.379 106.030  1.00  6.36           O  
ATOM   2290  CB  HIS A 426      -7.467 -17.523 103.709  1.00  6.32           C  
ATOM   2291  CG  HIS A 426      -6.950 -18.139 102.440  1.00  5.56           C  
ATOM   2292  ND1 HIS A 426      -7.321 -17.687 101.191  1.00  5.17           N  
ATOM   2293  CD2 HIS A 426      -6.087 -19.165 102.226  1.00  5.47           C  
ATOM   2294  CE1 HIS A 426      -6.713 -18.403 100.259  1.00  6.02           C  
ATOM   2295  NE2 HIS A 426      -5.958 -19.308 100.864  1.00  6.17           N  
ATOM   2296  N   SER A 427      -9.230 -14.720 104.339  1.00  9.10           N  
ATOM   2297  CA  SER A 427     -10.186 -14.084 105.258  1.00 10.03           C  
ATOM   2298  C   SER A 427     -11.290 -15.039 105.718  1.00 10.39           C  
ATOM   2299  O   SER A 427     -12.238 -14.622 106.364  1.00 11.29           O  
ATOM   2300  CB  SER A 427     -10.801 -12.828 104.635  1.00 10.53           C  
ATOM   2301  OG  SER A 427     -11.223 -13.065 103.310  1.00 11.21           O  
ATOM   2302  N   GLN A 428     -11.152 -16.321 105.382  1.00 10.73           N  
ATOM   2303  CA  GLN A 428     -12.102 -17.365 105.794  1.00  9.87           C  
ATOM   2304  C   GLN A 428     -11.323 -18.568 106.249  1.00  8.79           C  
ATOM   2305  O   GLN A 428     -10.232 -18.814 105.765  1.00  9.02           O  
ATOM   2306  CB  GLN A 428     -12.980 -17.829 104.639  1.00  9.54           C  
ATOM   2307  CG  GLN A 428     -13.942 -16.800 104.117  1.00  9.59           C  
ATOM   2308  CD  GLN A 428     -14.803 -17.350 103.014  1.00  9.48           C  
ATOM   2309  OE1 GLN A 428     -14.423 -17.342 101.844  1.00  8.82           O  
ATOM   2310  NE2 GLN A 428     -15.970 -17.855 103.382  1.00  9.77           N  
ATOM   2311  N   SER A 429     -11.873 -19.322 107.186  1.00  8.72           N  
ATOM   2312  CA  SER A 429     -11.195 -20.521 107.616  1.00  8.34           C  
ATOM   2313  C   SER A 429     -11.913 -21.689 106.947  1.00  8.97           C  
ATOM   2314  O   SER A 429     -13.069 -21.561 106.547  1.00  8.78           O  
ATOM   2315  CB  SER A 429     -11.192 -20.639 109.134  1.00  8.44           C  
ATOM   2316  OG  SER A 429     -12.488 -20.652 109.666  1.00  9.72           O  
ATOM   2317  N   LEU A 430     -11.218 -22.810 106.785  1.00  8.94           N  
ATOM   2318  CA  LEU A 430     -11.774 -23.985 106.125  1.00  8.98           C  
ATOM   2319  C   LEU A 430     -13.030 -24.568 106.775  1.00  8.53           C  
ATOM   2320  O   LEU A 430     -13.859 -25.176 106.100  1.00  9.47           O  
ATOM   2321  CB  LEU A 430     -10.700 -25.063 106.041  1.00  9.18           C  
ATOM   2322  CG  LEU A 430     -10.863 -26.126 104.955  1.00  8.92           C  
ATOM   2323  CD1 LEU A 430     -10.885 -25.484 103.580  1.00  8.37           C  
ATOM   2324  CD2 LEU A 430      -9.725 -27.114 105.081  1.00  7.77           C  
ATOM   2325  N   ASP A 431     -13.171 -24.386 108.080  1.00  7.42           N  
ATOM   2326  CA  ASP A 431     -14.325 -24.909 108.787  1.00  8.27           C  
ATOM   2327  C   ASP A 431     -15.464 -23.886 108.919  1.00  6.86           C  
ATOM   2328  O   ASP A 431     -16.363 -24.067 109.741  1.00  6.61           O  
ATOM   2329  CB  ASP A 431     -13.888 -25.401 110.175  1.00 10.68           C  
ATOM   2330  CG  ASP A 431     -13.210 -24.311 110.991  1.00 12.83           C  
ATOM   2331  OD1 ASP A 431     -12.795 -23.297 110.387  1.00 14.18           O  
ATOM   2332  OD2 ASP A 431     -13.080 -24.464 112.228  1.00 12.67           O  
ATOM   2333  N   ARG A 432     -15.424 -22.825 108.110  1.00  5.44           N  
ATOM   2334  CA  ARG A 432     -16.448 -21.791 108.161  1.00  4.37           C  
ATOM   2335  C   ARG A 432     -16.813 -21.315 106.769  1.00  5.48           C  
ATOM   2336  O   ARG A 432     -17.002 -20.123 106.548  1.00  7.60           O  
ATOM   2337  CB  ARG A 432     -15.955 -20.605 109.001  1.00  3.25           C  
ATOM   2338  CG  ARG A 432     -15.768 -20.923 110.460  1.00  3.52           C  
ATOM   2339  CD  ARG A 432     -17.088 -21.269 111.089  1.00  4.48           C  
ATOM   2340  NE  ARG A 432     -17.046 -21.447 112.536  1.00  5.71           N  
ATOM   2341  CZ  ARG A 432     -16.826 -22.603 113.160  1.00  6.26           C  
ATOM   2342  NH1 ARG A 432     -16.606 -23.708 112.461  1.00  7.66           N  
ATOM   2343  NH2 ARG A 432     -16.888 -22.674 114.484  1.00  4.92           N  
ATOM   2344  N   LEU A 433     -16.923 -22.236 105.826  1.00  6.16           N  
ATOM   2345  CA  LEU A 433     -17.246 -21.863 104.452  1.00  7.17           C  
ATOM   2346  C   LEU A 433     -18.728 -21.910 104.115  1.00  6.80           C  
ATOM   2347  O   LEU A 433     -19.120 -21.596 102.993  1.00  7.73           O  
ATOM   2348  CB  LEU A 433     -16.483 -22.761 103.478  1.00  8.58           C  
ATOM   2349  CG  LEU A 433     -14.954 -22.681 103.509  1.00  9.33           C  
ATOM   2350  CD1 LEU A 433     -14.353 -23.664 102.491  1.00  9.34           C  
ATOM   2351  CD2 LEU A 433     -14.512 -21.240 103.179  1.00  8.35           C  
ATOM   2352  N   MET A 434     -19.551 -22.298 105.081  1.00  6.27           N  
ATOM   2353  CA  MET A 434     -20.988 -22.386 104.855  1.00  7.62           C  
ATOM   2354  C   MET A 434     -21.727 -21.045 104.969  1.00  8.73           C  
ATOM   2355  O   MET A 434     -21.154 -20.028 105.377  1.00  8.36           O  
ATOM   2356  CB  MET A 434     -21.613 -23.374 105.845  1.00  6.95           C  
ATOM   2357  CG  MET A 434     -21.639 -22.907 107.291  1.00  8.09           C  
ATOM   2358  SD  MET A 434     -19.966 -22.840 107.995  1.00 11.02           S  
ATOM   2359  CE  MET A 434     -19.620 -24.629 108.261  1.00  9.51           C  
ATOM   2360  N   ASN A 435     -23.001 -21.076 104.582  1.00  9.55           N  
ATOM   2361  CA  ASN A 435     -23.918 -19.942 104.678  1.00  9.30           C  
ATOM   2362  C   ASN A 435     -24.505 -20.171 106.070  1.00  8.08           C  
ATOM   2363  O   ASN A 435     -25.156 -21.184 106.305  1.00  8.35           O  
ATOM   2364  CB  ASN A 435     -25.026 -20.055 103.610  1.00  8.36           C  
ATOM   2365  CG  ASN A 435     -26.044 -18.918 103.687  1.00  6.40           C  
ATOM   2366  OD1 ASN A 435     -26.436 -18.499 104.771  1.00  7.02           O  
ATOM   2367  ND2 ASN A 435     -26.484 -18.432 102.536  1.00  4.69           N  
ATOM   2368  N   PRO A 436     -24.274 -19.246 107.015  1.00  7.57           N  
ATOM   2369  CA  PRO A 436     -24.801 -19.416 108.380  1.00  7.12           C  
ATOM   2370  C   PRO A 436     -26.306 -19.224 108.566  1.00  7.82           C  
ATOM   2371  O   PRO A 436     -26.835 -19.427 109.656  1.00  8.84           O  
ATOM   2372  CB  PRO A 436     -24.004 -18.391 109.179  1.00  6.56           C  
ATOM   2373  CG  PRO A 436     -23.870 -17.253 108.169  1.00  6.40           C  
ATOM   2374  CD  PRO A 436     -23.540 -17.966 106.874  1.00  6.07           C  
ATOM   2375  N   LEU A 437     -26.999 -18.828 107.512  1.00  8.92           N  
ATOM   2376  CA  LEU A 437     -28.425 -18.597 107.623  1.00 11.19           C  
ATOM   2377  C   LEU A 437     -29.276 -19.833 107.326  1.00 13.31           C  
ATOM   2378  O   LEU A 437     -30.324 -20.041 107.940  1.00 14.65           O  
ATOM   2379  CB  LEU A 437     -28.812 -17.443 106.691  1.00 11.21           C  
ATOM   2380  CG  LEU A 437     -28.021 -16.140 106.921  1.00 11.17           C  
ATOM   2381  CD1 LEU A 437     -28.413 -15.090 105.892  1.00 10.05           C  
ATOM   2382  CD2 LEU A 437     -28.265 -15.633 108.336  1.00 10.69           C  
ATOM   2383  N   ILE A 438     -28.797 -20.671 106.414  1.00 13.15           N  
ATOM   2384  CA  ILE A 438     -29.532 -21.848 105.971  1.00 12.55           C  
ATOM   2385  C   ILE A 438     -29.026 -23.163 106.541  1.00 12.61           C  
ATOM   2386  O   ILE A 438     -27.821 -23.391 106.585  1.00 14.49           O  
ATOM   2387  CB  ILE A 438     -29.452 -21.940 104.428  1.00 11.05           C  
ATOM   2388  CG1 ILE A 438     -29.557 -20.537 103.817  1.00 10.06           C  
ATOM   2389  CG2 ILE A 438     -30.518 -22.878 103.901  1.00 10.45           C  
ATOM   2390  CD1 ILE A 438     -30.908 -19.814 104.048  1.00  9.26           C  
ATOM   2391  N   ASP A 439     -29.935 -24.036 106.960  1.00 11.44           N  
ATOM   2392  CA  ASP A 439     -29.539 -25.350 107.463  1.00 11.78           C  
ATOM   2393  C   ASP A 439     -29.121 -26.251 106.292  1.00  9.71           C  
ATOM   2394  O   ASP A 439     -29.423 -25.985 105.126  1.00  8.03           O  
ATOM   2395  CB  ASP A 439     -30.695 -26.058 108.185  1.00 14.59           C  
ATOM   2396  CG  ASP A 439     -31.151 -25.334 109.426  1.00 18.83           C  
ATOM   2397  OD1 ASP A 439     -30.294 -24.869 110.217  1.00 20.16           O  
ATOM   2398  OD2 ASP A 439     -32.383 -25.240 109.628  1.00 20.44           O  
ATOM   2399  N   GLN A 440     -28.441 -27.338 106.614  1.00 10.06           N  
ATOM   2400  CA  GLN A 440     -28.025 -28.283 105.591  1.00  9.37           C  
ATOM   2401  C   GLN A 440     -29.150 -29.286 105.372  1.00  7.94           C  
ATOM   2402  O   GLN A 440     -29.951 -29.524 106.272  1.00  7.17           O  
ATOM   2403  CB  GLN A 440     -26.780 -29.028 106.046  1.00  8.70           C  
ATOM   2404  CG  GLN A 440     -25.521 -28.191 106.027  1.00  8.18           C  
ATOM   2405  CD  GLN A 440     -24.278 -29.041 106.109  1.00  6.65           C  
ATOM   2406  OE1 GLN A 440     -24.093 -29.798 107.060  1.00  6.62           O  
ATOM   2407  NE2 GLN A 440     -23.423 -28.928 105.105  1.00  6.01           N  
ATOM   2408  N   TYR A 441     -29.228 -29.858 104.176  1.00  7.96           N  
ATOM   2409  CA  TYR A 441     -30.250 -30.871 103.930  1.00  7.50           C  
ATOM   2410  C   TYR A 441     -29.773 -32.241 104.399  1.00  9.44           C  
ATOM   2411  O   TYR A 441     -30.564 -33.164 104.522  1.00 11.51           O  
ATOM   2412  CB  TYR A 441     -30.658 -30.911 102.452  1.00  4.81           C  
ATOM   2413  CG  TYR A 441     -29.545 -31.052 101.447  1.00  3.73           C  
ATOM   2414  CD1 TYR A 441     -28.918 -32.297 101.205  1.00  3.84           C  
ATOM   2415  CD2 TYR A 441     -29.129 -29.944 100.708  1.00  1.82           C  
ATOM   2416  CE1 TYR A 441     -27.901 -32.419 100.242  1.00  3.13           C  
ATOM   2417  CE2 TYR A 441     -28.130 -30.045  99.763  1.00  2.33           C  
ATOM   2418  CZ  TYR A 441     -27.516 -31.279  99.529  1.00  3.83           C  
ATOM   2419  OH  TYR A 441     -26.509 -31.316  98.587  1.00  4.44           O  
ATOM   2420  N   LEU A 442     -28.485 -32.356 104.700  1.00 10.12           N  
ATOM   2421  CA  LEU A 442     -27.903 -33.612 105.164  1.00  9.49           C  
ATOM   2422  C   LEU A 442     -27.989 -33.763 106.669  1.00  8.81           C  
ATOM   2423  O   LEU A 442     -28.014 -32.784 107.404  1.00  9.49           O  
ATOM   2424  CB  LEU A 442     -26.440 -33.710 104.730  1.00  9.61           C  
ATOM   2425  CG  LEU A 442     -26.198 -33.817 103.223  1.00  9.71           C  
ATOM   2426  CD1 LEU A 442     -24.723 -33.656 102.921  1.00 10.12           C  
ATOM   2427  CD2 LEU A 442     -26.733 -35.150 102.706  1.00  9.09           C  
ATOM   2428  N   TYR A 443     -28.019 -35.006 107.122  1.00  7.79           N  
ATOM   2429  CA  TYR A 443     -28.110 -35.301 108.531  1.00  7.03           C  
ATOM   2430  C   TYR A 443     -26.818 -35.854 109.077  1.00  7.56           C  
ATOM   2431  O   TYR A 443     -25.981 -36.356 108.329  1.00  9.43           O  
ATOM   2432  CB  TYR A 443     -29.206 -36.336 108.791  1.00  6.30           C  
ATOM   2433  CG  TYR A 443     -30.614 -35.801 108.698  1.00  5.32           C  
ATOM   2434  CD1 TYR A 443     -31.233 -35.597 107.458  1.00  3.61           C  
ATOM   2435  CD2 TYR A 443     -31.319 -35.475 109.856  1.00  4.44           C  
ATOM   2436  CE1 TYR A 443     -32.515 -35.079 107.386  1.00  3.69           C  
ATOM   2437  CE2 TYR A 443     -32.602 -34.959 109.793  1.00  4.14           C  
ATOM   2438  CZ  TYR A 443     -33.195 -34.760 108.554  1.00  3.51           C  
ATOM   2439  OH  TYR A 443     -34.458 -34.210 108.494  1.00  3.39           O  
ATOM   2440  N   TYR A 444     -26.665 -35.768 110.390  1.00  6.89           N  
ATOM   2441  CA  TYR A 444     -25.501 -36.315 111.058  1.00  7.28           C  
ATOM   2442  C   TYR A 444     -26.040 -36.946 112.335  1.00  7.58           C  
ATOM   2443  O   TYR A 444     -27.101 -36.566 112.806  1.00  8.56           O  
ATOM   2444  CB  TYR A 444     -24.444 -35.222 111.361  1.00  7.47           C  
ATOM   2445  CG  TYR A 444     -24.800 -34.259 112.484  1.00  7.37           C  
ATOM   2446  CD1 TYR A 444     -25.581 -33.108 112.246  1.00  7.03           C  
ATOM   2447  CD2 TYR A 444     -24.420 -34.540 113.799  1.00  6.43           C  
ATOM   2448  CE1 TYR A 444     -25.971 -32.271 113.307  1.00  6.70           C  
ATOM   2449  CE2 TYR A 444     -24.805 -33.722 114.852  1.00  6.56           C  
ATOM   2450  CZ  TYR A 444     -25.573 -32.590 114.604  1.00  6.43           C  
ATOM   2451  OH  TYR A 444     -25.897 -31.781 115.660  1.00  6.53           O  
ATOM   2452  N   LEU A 445     -25.335 -37.931 112.869  1.00  9.02           N  
ATOM   2453  CA  LEU A 445     -25.749 -38.595 114.094  1.00 11.59           C  
ATOM   2454  C   LEU A 445     -25.564 -37.615 115.251  1.00 13.49           C  
ATOM   2455  O   LEU A 445     -24.442 -37.265 115.599  1.00 14.02           O  
ATOM   2456  CB  LEU A 445     -24.897 -39.850 114.317  1.00 12.60           C  
ATOM   2457  CG  LEU A 445     -25.181 -40.664 115.583  1.00 15.10           C  
ATOM   2458  CD1 LEU A 445     -26.614 -41.202 115.533  1.00 16.11           C  
ATOM   2459  CD2 LEU A 445     -24.183 -41.808 115.712  1.00 15.46           C  
ATOM   2460  N   SER A 446     -26.662 -37.183 115.862  1.00 15.06           N  
ATOM   2461  CA  SER A 446     -26.565 -36.201 116.932  1.00 16.43           C  
ATOM   2462  C   SER A 446     -26.727 -36.712 118.357  1.00 18.43           C  
ATOM   2463  O   SER A 446     -26.377 -36.026 119.307  1.00 18.99           O  
ATOM   2464  CB  SER A 446     -27.550 -35.061 116.661  1.00 15.26           C  
ATOM   2465  OG  SER A 446     -28.877 -35.540 116.573  1.00 15.43           O  
ATOM   2466  N   ARG A 447     -27.262 -37.910 118.508  1.00 21.14           N  
ATOM   2467  CA  ARG A 447     -27.437 -38.501 119.826  1.00 24.19           C  
ATOM   2468  C   ARG A 447     -27.365 -40.005 119.692  1.00 23.94           C  
ATOM   2469  O   ARG A 447     -27.732 -40.566 118.666  1.00 23.09           O  
ATOM   2470  CB  ARG A 447     -28.775 -38.104 120.454  1.00 27.60           C  
ATOM   2471  CG  ARG A 447     -28.771 -36.730 121.081  1.00 31.53           C  
ATOM   2472  CD  ARG A 447     -30.072 -36.463 121.811  1.00 34.78           C  
ATOM   2473  NE  ARG A 447     -30.225 -37.328 122.976  1.00 37.34           N  
ATOM   2474  CZ  ARG A 447     -31.316 -37.376 123.733  1.00 39.60           C  
ATOM   2475  NH1 ARG A 447     -32.364 -36.606 123.449  1.00 40.49           N  
ATOM   2476  NH2 ARG A 447     -31.359 -38.194 124.780  1.00 40.33           N  
ATOM   2477  N   THR A 448     -26.893 -40.655 120.742  1.00 25.68           N  
ATOM   2478  CA  THR A 448     -26.748 -42.092 120.717  1.00 27.51           C  
ATOM   2479  C   THR A 448     -27.608 -42.830 121.731  1.00 28.97           C  
ATOM   2480  O   THR A 448     -27.964 -43.987 121.524  1.00 29.31           O  
ATOM   2481  CB  THR A 448     -25.287 -42.487 120.913  1.00 27.40           C  
ATOM   2482  OG1 THR A 448     -24.530 -42.140 119.746  1.00 25.32           O  
ATOM   2483  CG2 THR A 448     -25.206 -43.976 121.135  1.00 30.09           C  
ATOM   2484  N   ASN A 449     -27.928 -42.178 122.835  1.00 30.70           N  
ATOM   2485  CA  ASN A 449     -28.780 -42.806 123.823  1.00 33.38           C  
ATOM   2486  C   ASN A 449     -29.810 -41.777 124.257  1.00 36.88           C  
ATOM   2487  O   ASN A 449     -29.636 -40.581 124.027  1.00 36.55           O  
ATOM   2488  CB  ASN A 449     -27.960 -43.332 125.013  1.00 32.71           C  
ATOM   2489  CG  ASN A 449     -27.343 -42.230 125.841  1.00 32.57           C  
ATOM   2490  OD1 ASN A 449     -27.277 -41.073 125.418  1.00 32.40           O  
ATOM   2491  ND2 ASN A 449     -26.875 -42.584 127.031  1.00 32.81           N  
ATOM   2492  N   THR A 450     -30.893 -42.246 124.862  1.00 40.66           N  
ATOM   2493  CA  THR A 450     -31.957 -41.352 125.293  1.00 44.31           C  
ATOM   2494  C   THR A 450     -32.535 -41.826 126.622  1.00 47.45           C  
ATOM   2495  O   THR A 450     -32.403 -42.998 126.981  1.00 47.42           O  
ATOM   2496  CB  THR A 450     -33.086 -41.312 124.226  1.00 44.56           C  
ATOM   2497  OG1 THR A 450     -33.955 -40.201 124.475  1.00 44.90           O  
ATOM   2498  CG2 THR A 450     -33.900 -42.615 124.255  1.00 44.26           C  
ATOM   2499  N   PRO A 451     -33.175 -40.916 127.378  1.00 50.58           N  
ATOM   2500  CA  PRO A 451     -33.763 -41.289 128.668  1.00 52.68           C  
ATOM   2501  C   PRO A 451     -34.777 -42.422 128.512  1.00 55.37           C  
ATOM   2502  O   PRO A 451     -35.623 -42.401 127.612  1.00 55.35           O  
ATOM   2503  CB  PRO A 451     -34.415 -39.992 129.133  1.00 52.09           C  
ATOM   2504  CG  PRO A 451     -33.502 -38.947 128.566  1.00 51.56           C  
ATOM   2505  CD  PRO A 451     -33.273 -39.461 127.164  1.00 51.16           C  
ATOM   2506  N   SER A 452     -34.675 -43.411 129.392  1.00 57.98           N  
ATOM   2507  CA  SER A 452     -35.566 -44.564 129.380  1.00 60.60           C  
ATOM   2508  C   SER A 452     -35.943 -44.881 130.822  1.00 62.71           C  
ATOM   2509  O   SER A 452     -35.353 -45.765 131.452  1.00 62.73           O  
ATOM   2510  CB  SER A 452     -34.861 -45.768 128.746  1.00 60.90           C  
ATOM   2511  OG  SER A 452     -35.700 -46.912 128.725  1.00 61.14           O  
ATOM   2512  N   GLY A 453     -36.927 -44.152 131.340  1.00 64.42           N  
ATOM   2513  CA  GLY A 453     -37.352 -44.356 132.713  1.00 65.83           C  
ATOM   2514  C   GLY A 453     -36.441 -43.590 133.654  1.00 67.06           C  
ATOM   2515  O   GLY A 453     -36.532 -42.365 133.758  1.00 67.29           O  
ATOM   2516  N   THR A 454     -35.553 -44.309 134.335  1.00 67.60           N  
ATOM   2517  CA  THR A 454     -34.617 -43.689 135.269  1.00 68.19           C  
ATOM   2518  C   THR A 454     -33.196 -43.627 134.698  1.00 67.51           C  
ATOM   2519  O   THR A 454     -32.374 -42.823 135.140  1.00 67.60           O  
ATOM   2520  CB  THR A 454     -34.593 -44.450 136.622  1.00 68.82           C  
ATOM   2521  OG1 THR A 454     -34.483 -45.861 136.384  1.00 68.88           O  
ATOM   2522  CG2 THR A 454     -35.864 -44.158 137.419  1.00 68.98           C  
ATOM   2523  N   THR A 455     -32.921 -44.484 133.716  1.00 66.55           N  
ATOM   2524  CA  THR A 455     -31.614 -44.536 133.064  1.00 65.13           C  
ATOM   2525  C   THR A 455     -31.768 -44.241 131.577  1.00 62.73           C  
ATOM   2526  O   THR A 455     -32.843 -43.841 131.126  1.00 62.71           O  
ATOM   2527  CB  THR A 455     -30.959 -45.930 133.213  1.00 65.65           C  
ATOM   2528  OG1 THR A 455     -31.899 -46.945 132.833  1.00 65.66           O  
ATOM   2529  CG2 THR A 455     -30.500 -46.157 134.651  1.00 65.88           C  
ATOM   2530  N   THR A 456     -30.693 -44.441 130.818  1.00 60.08           N  
ATOM   2531  CA  THR A 456     -30.730 -44.205 129.380  1.00 57.47           C  
ATOM   2532  C   THR A 456     -31.007 -45.504 128.627  1.00 54.57           C  
ATOM   2533  O   THR A 456     -31.189 -46.562 129.230  1.00 54.68           O  
ATOM   2534  CB  THR A 456     -29.397 -43.602 128.860  1.00 57.87           C  
ATOM   2535  OG1 THR A 456     -28.312 -44.495 129.153  1.00 57.98           O  
ATOM   2536  CG2 THR A 456     -29.135 -42.242 129.505  1.00 57.87           C  
ATOM   2537  N   GLN A 457     -31.042 -45.406 127.304  1.00 51.56           N  
ATOM   2538  CA  GLN A 457     -31.294 -46.546 126.430  1.00 48.69           C  
ATOM   2539  C   GLN A 457     -30.626 -46.203 125.102  1.00 44.53           C  
ATOM   2540  O   GLN A 457     -30.577 -45.031 124.728  1.00 44.75           O  
ATOM   2541  CB  GLN A 457     -32.803 -46.718 126.224  1.00 50.02           C  
ATOM   2542  CG  GLN A 457     -33.195 -47.878 125.326  1.00 51.91           C  
ATOM   2543  CD  GLN A 457     -34.676 -47.867 124.970  1.00 53.55           C  
ATOM   2544  OE1 GLN A 457     -35.538 -48.038 125.838  1.00 54.01           O  
ATOM   2545  NE2 GLN A 457     -34.978 -47.658 123.690  1.00 53.91           N  
ATOM   2546  N   SER A 458     -30.106 -47.201 124.395  1.00 40.29           N  
ATOM   2547  CA  SER A 458     -29.460 -46.939 123.111  1.00 36.47           C  
ATOM   2548  C   SER A 458     -30.520 -46.562 122.075  1.00 34.01           C  
ATOM   2549  O   SER A 458     -31.511 -47.273 121.901  1.00 33.82           O  
ATOM   2550  CB  SER A 458     -28.687 -48.171 122.636  1.00 35.64           C  
ATOM   2551  OG  SER A 458     -27.748 -48.581 123.611  1.00 35.72           O  
ATOM   2552  N   ARG A 459     -30.302 -45.442 121.394  1.00 31.82           N  
ATOM   2553  CA  ARG A 459     -31.233 -44.954 120.385  1.00 30.06           C  
ATOM   2554  C   ARG A 459     -30.516 -43.936 119.505  1.00 26.57           C  
ATOM   2555  O   ARG A 459     -30.079 -42.900 119.989  1.00 26.90           O  
ATOM   2556  CB  ARG A 459     -32.429 -44.294 121.072  1.00 32.90           C  
ATOM   2557  CG  ARG A 459     -33.595 -43.961 120.159  1.00 35.94           C  
ATOM   2558  CD  ARG A 459     -34.626 -43.145 120.916  1.00 39.18           C  
ATOM   2559  NE  ARG A 459     -35.751 -42.741 120.075  1.00 42.51           N  
ATOM   2560  CZ  ARG A 459     -36.601 -41.761 120.382  1.00 45.23           C  
ATOM   2561  NH1 ARG A 459     -36.454 -41.074 121.515  1.00 45.58           N  
ATOM   2562  NH2 ARG A 459     -37.601 -41.463 119.554  1.00 45.97           N  
ATOM   2563  N   LEU A 460     -30.394 -44.222 118.216  1.00 23.60           N  
ATOM   2564  CA  LEU A 460     -29.716 -43.303 117.308  1.00 20.93           C  
ATOM   2565  C   LEU A 460     -30.639 -42.195 116.807  1.00 19.78           C  
ATOM   2566  O   LEU A 460     -31.738 -42.465 116.322  1.00 20.33           O  
ATOM   2567  CB  LEU A 460     -29.150 -44.067 116.109  1.00 20.22           C  
ATOM   2568  CG  LEU A 460     -28.151 -45.193 116.384  1.00 19.34           C  
ATOM   2569  CD1 LEU A 460     -27.614 -45.697 115.047  1.00 19.40           C  
ATOM   2570  CD2 LEU A 460     -27.009 -44.696 117.264  1.00 18.82           C  
ATOM   2571  N   GLN A 461     -30.197 -40.949 116.921  1.00 18.23           N  
ATOM   2572  CA  GLN A 461     -31.002 -39.828 116.466  1.00 17.15           C  
ATOM   2573  C   GLN A 461     -30.192 -38.921 115.562  1.00 13.42           C  
ATOM   2574  O   GLN A 461     -28.990 -38.764 115.743  1.00 13.83           O  
ATOM   2575  CB  GLN A 461     -31.579 -39.092 117.673  1.00 19.97           C  
ATOM   2576  CG  GLN A 461     -32.445 -40.028 118.484  1.00 22.90           C  
ATOM   2577  CD  GLN A 461     -33.166 -39.361 119.620  1.00 26.06           C  
ATOM   2578  OE1 GLN A 461     -32.544 -38.791 120.524  1.00 26.81           O  
ATOM   2579  NE2 GLN A 461     -34.502 -39.433 119.594  1.00 26.91           N  
ATOM   2580  N   PHE A 462     -30.850 -38.335 114.577  1.00 11.05           N  
ATOM   2581  CA  PHE A 462     -30.163 -37.506 113.605  1.00 10.69           C  
ATOM   2582  C   PHE A 462     -30.688 -36.080 113.510  1.00 10.91           C  
ATOM   2583  O   PHE A 462     -31.861 -35.819 113.771  1.00 11.79           O  
ATOM   2584  CB  PHE A 462     -30.232 -38.195 112.222  1.00 10.98           C  
ATOM   2585  CG  PHE A 462     -29.741 -39.628 112.229  1.00 11.84           C  
ATOM   2586  CD1 PHE A 462     -30.490 -40.639 112.855  1.00 11.88           C  
ATOM   2587  CD2 PHE A 462     -28.497 -39.958 111.673  1.00 12.52           C  
ATOM   2588  CE1 PHE A 462     -30.011 -41.958 112.934  1.00 11.86           C  
ATOM   2589  CE2 PHE A 462     -27.997 -41.273 111.739  1.00 12.66           C  
ATOM   2590  CZ  PHE A 462     -28.758 -42.280 112.377  1.00 12.40           C  
ATOM   2591  N   SER A 463     -29.814 -35.158 113.119  1.00 10.26           N  
ATOM   2592  CA  SER A 463     -30.176 -33.755 112.993  1.00  9.00           C  
ATOM   2593  C   SER A 463     -29.532 -33.151 111.774  1.00  8.76           C  
ATOM   2594  O   SER A 463     -28.594 -33.709 111.220  1.00  8.68           O  
ATOM   2595  CB  SER A 463     -29.709 -32.971 114.223  1.00  9.32           C  
ATOM   2596  OG  SER A 463     -30.285 -33.485 115.406  1.00 10.16           O  
ATOM   2597  N   GLN A 464     -30.055 -32.017 111.336  1.00  9.91           N  
ATOM   2598  CA  GLN A 464     -29.471 -31.312 110.206  1.00 11.35           C  
ATOM   2599  C   GLN A 464     -28.716 -30.185 110.887  1.00 13.40           C  
ATOM   2600  O   GLN A 464     -29.230 -29.563 111.822  1.00 14.41           O  
ATOM   2601  CB  GLN A 464     -30.550 -30.773 109.268  1.00 10.76           C  
ATOM   2602  CG  GLN A 464     -31.229 -31.878 108.447  1.00  9.67           C  
ATOM   2603  CD  GLN A 464     -32.395 -31.384 107.629  1.00  9.67           C  
ATOM   2604  OE1 GLN A 464     -33.273 -30.685 108.133  1.00  9.98           O  
ATOM   2605  NE2 GLN A 464     -32.423 -31.757 106.359  1.00 10.02           N  
ATOM   2606  N   ALA A 465     -27.484 -29.942 110.462  1.00 14.33           N  
ATOM   2607  CA  ALA A 465     -26.698 -28.900 111.101  1.00 15.77           C  
ATOM   2608  C   ALA A 465     -26.991 -27.528 110.519  1.00 15.99           C  
ATOM   2609  O   ALA A 465     -27.198 -27.374 109.316  1.00 16.29           O  
ATOM   2610  CB  ALA A 465     -25.215 -29.221 110.989  1.00 15.85           C  
ATOM   2611  N   GLY A 466     -27.026 -26.539 111.400  1.00 15.98           N  
ATOM   2612  CA  GLY A 466     -27.273 -25.173 110.989  1.00 16.73           C  
ATOM   2613  C   GLY A 466     -26.149 -24.371 111.597  1.00 18.04           C  
ATOM   2614  O   GLY A 466     -25.017 -24.841 111.623  1.00 18.96           O  
ATOM   2615  N   ALA A 467     -26.441 -23.182 112.108  1.00 18.66           N  
ATOM   2616  CA  ALA A 467     -25.399 -22.363 112.711  1.00 18.59           C  
ATOM   2617  C   ALA A 467     -25.116 -22.711 114.174  1.00 18.25           C  
ATOM   2618  O   ALA A 467     -23.998 -22.503 114.649  1.00 18.44           O  
ATOM   2619  CB  ALA A 467     -25.757 -20.887 112.586  1.00 18.46           C  
ATOM   2620  N   SER A 468     -26.103 -23.255 114.883  1.00 18.42           N  
ATOM   2621  CA  SER A 468     -25.915 -23.585 116.296  1.00 19.41           C  
ATOM   2622  C   SER A 468     -25.064 -24.835 116.575  1.00 20.34           C  
ATOM   2623  O   SER A 468     -24.562 -25.017 117.688  1.00 20.59           O  
ATOM   2624  CB  SER A 468     -27.273 -23.713 116.999  1.00 20.38           C  
ATOM   2625  OG  SER A 468     -27.913 -24.936 116.680  1.00 21.59           O  
ATOM   2626  N   ASP A 469     -24.920 -25.698 115.573  1.00 20.87           N  
ATOM   2627  CA  ASP A 469     -24.111 -26.915 115.676  1.00 20.19           C  
ATOM   2628  C   ASP A 469     -23.201 -26.912 114.459  1.00 17.37           C  
ATOM   2629  O   ASP A 469     -23.024 -27.915 113.769  1.00 17.58           O  
ATOM   2630  CB  ASP A 469     -24.990 -28.177 115.680  1.00 22.66           C  
ATOM   2631  CG  ASP A 469     -26.171 -28.077 114.723  1.00 25.62           C  
ATOM   2632  OD1 ASP A 469     -26.180 -27.155 113.874  1.00 26.56           O  
ATOM   2633  OD2 ASP A 469     -27.096 -28.921 114.819  1.00 26.63           O  
ATOM   2634  N   ILE A 470     -22.620 -25.756 114.213  1.00 15.26           N  
ATOM   2635  CA  ILE A 470     -21.745 -25.543 113.079  1.00 14.54           C  
ATOM   2636  C   ILE A 470     -20.531 -26.500 113.021  1.00 13.23           C  
ATOM   2637  O   ILE A 470     -19.990 -26.755 111.954  1.00 12.32           O  
ATOM   2638  CB  ILE A 470     -21.305 -24.054 113.075  1.00 14.40           C  
ATOM   2639  CG1 ILE A 470     -20.886 -23.624 111.679  1.00 15.89           C  
ATOM   2640  CG2 ILE A 470     -20.185 -23.837 114.061  1.00 13.76           C  
ATOM   2641  CD1 ILE A 470     -20.757 -22.122 111.556  1.00 16.85           C  
ATOM   2642  N   ARG A 471     -20.126 -27.049 114.157  1.00 13.31           N  
ATOM   2643  CA  ARG A 471     -18.993 -27.962 114.169  1.00 13.81           C  
ATOM   2644  C   ARG A 471     -19.336 -29.299 113.502  1.00 14.26           C  
ATOM   2645  O   ARG A 471     -18.453 -29.987 112.989  1.00 14.09           O  
ATOM   2646  CB  ARG A 471     -18.548 -28.233 115.601  1.00 13.53           C  
ATOM   2647  CG  ARG A 471     -19.470 -29.155 116.317  1.00 13.93           C  
ATOM   2648  CD  ARG A 471     -18.936 -29.610 117.648  1.00 14.15           C  
ATOM   2649  NE  ARG A 471     -19.887 -30.540 118.243  1.00 14.31           N  
ATOM   2650  CZ  ARG A 471     -19.907 -30.879 119.523  1.00 14.24           C  
ATOM   2651  NH1 ARG A 471     -19.017 -30.366 120.362  1.00 14.60           N  
ATOM   2652  NH2 ARG A 471     -20.839 -31.713 119.965  1.00 14.68           N  
ATOM   2653  N   ASP A 472     -20.625 -29.647 113.500  1.00 13.77           N  
ATOM   2654  CA  ASP A 472     -21.105 -30.905 112.941  1.00 11.81           C  
ATOM   2655  C   ASP A 472     -21.466 -30.887 111.478  1.00  9.54           C  
ATOM   2656  O   ASP A 472     -21.883 -31.897 110.935  1.00 10.84           O  
ATOM   2657  CB  ASP A 472     -22.319 -31.395 113.719  1.00 12.27           C  
ATOM   2658  CG  ASP A 472     -22.032 -31.563 115.185  1.00 14.86           C  
ATOM   2659  OD1 ASP A 472     -21.200 -32.431 115.535  1.00 15.87           O  
ATOM   2660  OD2 ASP A 472     -22.636 -30.830 115.999  1.00 15.51           O  
ATOM   2661  N   GLN A 473     -21.310 -29.756 110.823  1.00  8.18           N  
ATOM   2662  CA  GLN A 473     -21.652 -29.703 109.419  1.00  8.65           C  
ATOM   2663  C   GLN A 473     -20.857 -30.623 108.503  1.00 10.26           C  
ATOM   2664  O   GLN A 473     -19.706 -30.957 108.775  1.00 12.19           O  
ATOM   2665  CB  GLN A 473     -21.559 -28.261 108.913  1.00  8.09           C  
ATOM   2666  CG  GLN A 473     -22.675 -27.406 109.495  1.00  7.65           C  
ATOM   2667  CD  GLN A 473     -23.058 -26.264 108.609  1.00  6.71           C  
ATOM   2668  OE1 GLN A 473     -22.781 -26.274 107.407  1.00  6.40           O  
ATOM   2669  NE2 GLN A 473     -23.726 -25.272 109.183  1.00  6.82           N  
ATOM   2670  N   SER A 474     -21.485 -31.037 107.413  1.00  9.93           N  
ATOM   2671  CA  SER A 474     -20.826 -31.872 106.425  1.00  9.88           C  
ATOM   2672  C   SER A 474     -20.001 -30.931 105.566  1.00  9.60           C  
ATOM   2673  O   SER A 474     -20.495 -29.905 105.111  1.00  9.77           O  
ATOM   2674  CB  SER A 474     -21.851 -32.593 105.547  1.00 10.18           C  
ATOM   2675  OG  SER A 474     -22.389 -33.721 106.202  1.00 11.29           O  
ATOM   2676  N   ARG A 475     -18.742 -31.283 105.337  1.00 10.09           N  
ATOM   2677  CA  ARG A 475     -17.864 -30.438 104.551  1.00  8.66           C  
ATOM   2678  C   ARG A 475     -17.222 -31.198 103.425  1.00  7.14           C  
ATOM   2679  O   ARG A 475     -17.242 -32.422 103.392  1.00  8.78           O  
ATOM   2680  CB  ARG A 475     -16.810 -29.814 105.468  1.00  8.97           C  
ATOM   2681  CG  ARG A 475     -17.407 -28.858 106.498  1.00  8.37           C  
ATOM   2682  CD  ARG A 475     -16.462 -28.635 107.665  1.00  8.06           C  
ATOM   2683  NE  ARG A 475     -16.919 -27.579 108.554  1.00  6.72           N  
ATOM   2684  CZ  ARG A 475     -17.488 -27.785 109.733  1.00  6.88           C  
ATOM   2685  NH1 ARG A 475     -17.685 -29.018 110.186  1.00  7.42           N  
ATOM   2686  NH2 ARG A 475     -17.840 -26.754 110.475  1.00  6.70           N  
ATOM   2687  N   ASN A 476     -16.641 -30.467 102.492  1.00  5.92           N  
ATOM   2688  CA  ASN A 476     -16.014 -31.079 101.335  1.00  4.08           C  
ATOM   2689  C   ASN A 476     -14.512 -31.186 101.394  1.00  2.42           C  
ATOM   2690  O   ASN A 476     -13.928 -31.847 100.547  1.00  2.25           O  
ATOM   2691  CB  ASN A 476     -16.343 -30.275 100.077  1.00  3.94           C  
ATOM   2692  CG  ASN A 476     -17.700 -30.579  99.534  1.00  4.35           C  
ATOM   2693  OD1 ASN A 476     -18.060 -31.744  99.364  1.00  5.57           O  
ATOM   2694  ND2 ASN A 476     -18.463 -29.541  99.231  1.00  3.68           N  
ATOM   2695  N   TRP A 477     -13.888 -30.522 102.363  1.00  2.51           N  
ATOM   2696  CA  TRP A 477     -12.433 -30.471 102.429  1.00  2.37           C  
ATOM   2697  C   TRP A 477     -11.809 -30.714 103.776  1.00  4.64           C  
ATOM   2698  O   TRP A 477     -12.465 -30.637 104.812  1.00  6.17           O  
ATOM   2699  CB  TRP A 477     -11.973 -29.111 101.906  1.00  1.55           C  
ATOM   2700  CG  TRP A 477     -12.710 -28.678 100.665  1.00  0.13           C  
ATOM   2701  CD1 TRP A 477     -13.663 -27.718 100.585  1.00  0.00           C  
ATOM   2702  CD2 TRP A 477     -12.583 -29.228  99.332  1.00  0.12           C  
ATOM   2703  NE1 TRP A 477     -14.139 -27.622  99.295  1.00  0.00           N  
ATOM   2704  CE2 TRP A 477     -13.500 -28.535  98.507  1.00  0.00           C  
ATOM   2705  CE3 TRP A 477     -11.790 -30.237  98.764  1.00  0.00           C  
ATOM   2706  CZ2 TRP A 477     -13.650 -28.817  97.123  1.00  0.27           C  
ATOM   2707  CZ3 TRP A 477     -11.937 -30.525  97.386  1.00  0.00           C  
ATOM   2708  CH2 TRP A 477     -12.864 -29.811  96.586  1.00  0.00           C  
ATOM   2709  N   LEU A 478     -10.511 -30.987 103.758  1.00  6.66           N  
ATOM   2710  CA  LEU A 478      -9.769 -31.250 104.983  1.00  6.93           C  
ATOM   2711  C   LEU A 478      -8.550 -30.360 105.105  1.00  7.20           C  
ATOM   2712  O   LEU A 478      -7.980 -29.923 104.096  1.00  6.47           O  
ATOM   2713  CB  LEU A 478      -9.323 -32.715 105.006  1.00  7.91           C  
ATOM   2714  CG  LEU A 478     -10.392 -33.796 105.191  1.00  7.33           C  
ATOM   2715  CD1 LEU A 478      -9.811 -35.086 104.702  1.00  6.88           C  
ATOM   2716  CD2 LEU A 478     -10.864 -33.885 106.649  1.00  6.75           C  
ATOM   2717  N   PRO A 479      -8.116 -30.085 106.350  1.00  7.37           N  
ATOM   2718  CA  PRO A 479      -6.943 -29.247 106.593  1.00  7.69           C  
ATOM   2719  C   PRO A 479      -5.708 -29.968 106.064  1.00  9.32           C  
ATOM   2720  O   PRO A 479      -5.694 -31.193 105.955  1.00  9.34           O  
ATOM   2721  CB  PRO A 479      -6.894 -29.136 108.114  1.00  7.60           C  
ATOM   2722  CG  PRO A 479      -8.266 -29.449 108.550  1.00  7.46           C  
ATOM   2723  CD  PRO A 479      -8.709 -30.526 107.619  1.00  7.03           C  
ATOM   2724  N   GLY A 480      -4.673 -29.201 105.752  1.00 10.28           N  
ATOM   2725  CA  GLY A 480      -3.452 -29.776 105.241  1.00  9.99           C  
ATOM   2726  C   GLY A 480      -2.777 -30.767 106.167  1.00  9.78           C  
ATOM   2727  O   GLY A 480      -3.148 -30.910 107.321  1.00  9.41           O  
ATOM   2728  N   PRO A 481      -1.749 -31.459 105.664  1.00 11.03           N  
ATOM   2729  CA  PRO A 481      -0.963 -32.471 106.380  1.00 12.94           C  
ATOM   2730  C   PRO A 481      -0.179 -31.963 107.583  1.00 14.81           C  
ATOM   2731  O   PRO A 481       0.136 -30.778 107.679  1.00 15.78           O  
ATOM   2732  CB  PRO A 481      -0.074 -33.046 105.282  1.00 12.27           C  
ATOM   2733  CG  PRO A 481       0.119 -31.884 104.374  1.00 12.11           C  
ATOM   2734  CD  PRO A 481      -1.217 -31.227 104.308  1.00 10.94           C  
ATOM   2735  N   CYS A 482       0.138 -32.861 108.505  1.00 16.26           N  
ATOM   2736  CA  CYS A 482       0.882 -32.453 109.685  1.00 18.60           C  
ATOM   2737  C   CYS A 482       1.919 -33.466 110.165  1.00 18.59           C  
ATOM   2738  O   CYS A 482       1.838 -34.653 109.838  1.00 19.56           O  
ATOM   2739  CB  CYS A 482      -0.099 -32.116 110.814  1.00 20.53           C  
ATOM   2740  SG  CYS A 482      -0.321 -33.367 112.068  1.00 22.43           S  
ATOM   2741  N   TYR A 483       2.905 -32.978 110.920  1.00 17.00           N  
ATOM   2742  CA  TYR A 483       4.000 -33.786 111.491  1.00 14.73           C  
ATOM   2743  C   TYR A 483       4.337 -33.045 112.784  1.00 11.71           C  
ATOM   2744  O   TYR A 483       5.266 -32.251 112.830  1.00 12.11           O  
ATOM   2745  CB  TYR A 483       5.202 -33.779 110.527  1.00 15.02           C  
ATOM   2746  CG  TYR A 483       6.215 -34.882 110.773  1.00 15.80           C  
ATOM   2747  CD1 TYR A 483       5.882 -36.229 110.566  1.00 16.64           C  
ATOM   2748  CD2 TYR A 483       7.508 -34.584 111.195  1.00 16.12           C  
ATOM   2749  CE1 TYR A 483       6.827 -37.255 110.778  1.00 16.97           C  
ATOM   2750  CE2 TYR A 483       8.462 -35.598 111.411  1.00 16.89           C  
ATOM   2751  CZ  TYR A 483       8.117 -36.927 111.204  1.00 16.83           C  
ATOM   2752  OH  TYR A 483       9.051 -37.918 111.439  1.00 16.33           O  
ATOM   2753  N   ARG A 484       3.561 -33.315 113.827  1.00 10.12           N  
ATOM   2754  CA  ARG A 484       3.654 -32.623 115.114  1.00  9.02           C  
ATOM   2755  C   ARG A 484       4.992 -32.245 115.751  1.00  9.70           C  
ATOM   2756  O   ARG A 484       5.886 -33.074 115.910  1.00 10.11           O  
ATOM   2757  CB  ARG A 484       2.809 -33.362 116.149  1.00  7.93           C  
ATOM   2758  CG  ARG A 484       2.448 -32.521 117.357  1.00  7.45           C  
ATOM   2759  CD  ARG A 484       1.387 -33.186 118.201  1.00  7.65           C  
ATOM   2760  NE  ARG A 484       1.094 -32.399 119.387  1.00  8.56           N  
ATOM   2761  CZ  ARG A 484       0.210 -32.736 120.320  1.00  9.39           C  
ATOM   2762  NH1 ARG A 484      -0.484 -33.863 120.207  1.00 10.15           N  
ATOM   2763  NH2 ARG A 484       0.028 -31.947 121.375  1.00  8.51           N  
ATOM   2764  N   GLN A 485       5.079 -30.973 116.152  1.00  9.12           N  
ATOM   2765  CA  GLN A 485       6.251 -30.384 116.802  1.00  9.12           C  
ATOM   2766  C   GLN A 485       5.954 -30.152 118.281  1.00  8.86           C  
ATOM   2767  O   GLN A 485       4.796 -30.057 118.674  1.00  9.27           O  
ATOM   2768  CB  GLN A 485       6.583 -29.022 116.187  1.00  9.56           C  
ATOM   2769  CG  GLN A 485       7.016 -29.030 114.739  1.00 10.63           C  
ATOM   2770  CD  GLN A 485       8.517 -29.134 114.605  1.00 10.76           C  
ATOM   2771  OE1 GLN A 485       9.241 -28.889 115.568  1.00 11.70           O  
ATOM   2772  NE2 GLN A 485       8.996 -29.478 113.413  1.00  9.35           N  
ATOM   2773  N   GLN A 486       7.001 -30.058 119.098  1.00  8.81           N  
ATOM   2774  CA  GLN A 486       6.838 -29.783 120.526  1.00  8.78           C  
ATOM   2775  C   GLN A 486       6.592 -28.270 120.652  1.00  9.38           C  
ATOM   2776  O   GLN A 486       6.964 -27.496 119.768  1.00  8.47           O  
ATOM   2777  CB  GLN A 486       8.099 -30.187 121.299  1.00  8.88           C  
ATOM   2778  CG  GLN A 486       8.039 -29.971 122.814  1.00  9.23           C  
ATOM   2779  CD  GLN A 486       6.722 -30.426 123.427  1.00  9.75           C  
ATOM   2780  OE1 GLN A 486       5.742 -29.686 123.429  1.00 10.36           O  
ATOM   2781  NE2 GLN A 486       6.693 -31.647 123.942  1.00  9.78           N  
ATOM   2782  N   ARG A 487       5.963 -27.846 121.739  1.00 10.94           N  
ATOM   2783  CA  ARG A 487       5.664 -26.433 121.926  1.00 12.60           C  
ATOM   2784  C   ARG A 487       6.522 -25.769 122.998  1.00 13.15           C  
ATOM   2785  O   ARG A 487       6.590 -26.253 124.123  1.00 12.98           O  
ATOM   2786  CB  ARG A 487       4.187 -26.278 122.300  1.00 13.50           C  
ATOM   2787  CG  ARG A 487       3.672 -24.846 122.297  1.00 14.19           C  
ATOM   2788  CD  ARG A 487       2.226 -24.785 122.781  1.00 14.83           C  
ATOM   2789  NE  ARG A 487       2.093 -25.126 124.201  1.00 16.15           N  
ATOM   2790  CZ  ARG A 487       0.928 -25.204 124.841  1.00 16.98           C  
ATOM   2791  NH1 ARG A 487      -0.205 -24.971 124.186  1.00 17.74           N  
ATOM   2792  NH2 ARG A 487       0.891 -25.492 126.135  1.00 16.82           N  
ATOM   2793  N   VAL A 488       7.187 -24.668 122.662  1.00 14.50           N  
ATOM   2794  CA  VAL A 488       7.967 -23.970 123.681  1.00 16.30           C  
ATOM   2795  C   VAL A 488       7.466 -22.536 123.823  1.00 17.12           C  
ATOM   2796  O   VAL A 488       6.920 -21.955 122.879  1.00 16.40           O  
ATOM   2797  CB  VAL A 488       9.502 -23.999 123.395  1.00 16.19           C  
ATOM   2798  CG1 VAL A 488      10.015 -25.428 123.477  1.00 16.75           C  
ATOM   2799  CG2 VAL A 488       9.807 -23.437 122.046  1.00 15.99           C  
ATOM   2800  N   SER A 489       7.637 -21.988 125.021  1.00 18.93           N  
ATOM   2801  CA  SER A 489       7.193 -20.637 125.343  1.00 20.59           C  
ATOM   2802  C   SER A 489       8.311 -19.594 125.323  1.00 22.19           C  
ATOM   2803  O   SER A 489       9.447 -19.879 125.707  1.00 22.44           O  
ATOM   2804  CB  SER A 489       6.537 -20.651 126.726  1.00 20.82           C  
ATOM   2805  OG  SER A 489       5.980 -19.389 127.052  1.00 20.94           O  
ATOM   2806  N   LYS A 490       7.984 -18.384 124.872  1.00 23.70           N  
ATOM   2807  CA  LYS A 490       8.952 -17.294 124.847  1.00 24.76           C  
ATOM   2808  C   LYS A 490       9.139 -16.813 126.285  1.00 27.60           C  
ATOM   2809  O   LYS A 490      10.011 -15.992 126.575  1.00 28.52           O  
ATOM   2810  CB  LYS A 490       8.468 -16.153 123.952  1.00 23.62           C  
ATOM   2811  CG  LYS A 490       8.579 -16.468 122.475  1.00 23.02           C  
ATOM   2812  CD  LYS A 490       7.909 -15.415 121.627  1.00 23.06           C  
ATOM   2813  CE  LYS A 490       7.954 -15.799 120.153  1.00 23.91           C  
ATOM   2814  NZ  LYS A 490       7.324 -14.775 119.270  1.00 24.40           N  
ATOM   2815  N   THR A 491       8.308 -17.338 127.180  1.00 29.56           N  
ATOM   2816  CA  THR A 491       8.387 -17.033 128.607  1.00 32.01           C  
ATOM   2817  C   THR A 491       9.063 -18.250 129.233  1.00 33.80           C  
ATOM   2818  O   THR A 491       8.460 -19.317 129.317  1.00 33.46           O  
ATOM   2819  CB  THR A 491       6.988 -16.878 129.232  1.00 32.85           C  
ATOM   2820  OG1 THR A 491       6.339 -15.730 128.672  1.00 33.20           O  
ATOM   2821  CG2 THR A 491       7.089 -16.734 130.757  1.00 33.14           C  
ATOM   2822  N   SER A 492      10.306 -18.084 129.673  1.00 35.90           N  
ATOM   2823  CA  SER A 492      11.092 -19.173 130.252  1.00 37.59           C  
ATOM   2824  C   SER A 492      10.473 -19.960 131.408  1.00 38.05           C  
ATOM   2825  O   SER A 492      10.832 -21.117 131.621  1.00 38.37           O  
ATOM   2826  CB  SER A 492      12.463 -18.638 130.681  1.00 38.57           C  
ATOM   2827  OG  SER A 492      12.332 -17.697 131.733  1.00 39.08           O  
ATOM   2828  N   ALA A 493       9.551 -19.357 132.151  1.00 38.37           N  
ATOM   2829  CA  ALA A 493       8.930 -20.048 133.282  1.00 39.05           C  
ATOM   2830  C   ALA A 493       7.828 -21.021 132.869  1.00 38.88           C  
ATOM   2831  O   ALA A 493       7.384 -21.847 133.677  1.00 39.03           O  
ATOM   2832  CB  ALA A 493       8.369 -19.025 134.289  1.00 39.66           C  
ATOM   2833  N   ASP A 494       7.381 -20.921 131.619  1.00 37.83           N  
ATOM   2834  CA  ASP A 494       6.329 -21.801 131.118  1.00 36.75           C  
ATOM   2835  C   ASP A 494       6.898 -23.117 130.604  1.00 33.35           C  
ATOM   2836  O   ASP A 494       6.153 -24.059 130.331  1.00 33.03           O  
ATOM   2837  CB  ASP A 494       5.556 -21.130 129.977  1.00 38.62           C  
ATOM   2838  CG  ASP A 494       4.754 -19.930 130.437  1.00 40.86           C  
ATOM   2839  OD1 ASP A 494       4.404 -19.864 131.637  1.00 41.58           O  
ATOM   2840  OD2 ASP A 494       4.454 -19.058 129.592  1.00 41.58           O  
ATOM   2841  N   ASN A 495       8.220 -23.169 130.469  1.00 30.34           N  
ATOM   2842  CA  ASN A 495       8.897 -24.354 129.956  1.00 27.11           C  
ATOM   2843  C   ASN A 495       9.405 -25.294 131.032  1.00 25.77           C  
ATOM   2844  O   ASN A 495       9.629 -24.894 132.172  1.00 25.81           O  
ATOM   2845  CB  ASN A 495      10.047 -23.921 129.061  1.00 25.87           C  
ATOM   2846  CG  ASN A 495       9.581 -23.076 127.899  1.00 25.19           C  
ATOM   2847  OD1 ASN A 495       8.729 -23.498 127.115  1.00 25.21           O  
ATOM   2848  ND2 ASN A 495      10.135 -21.878 127.777  1.00 24.71           N  
ATOM   2849  N   ASN A 496       9.582 -26.554 130.656  1.00 25.45           N  
ATOM   2850  CA  ASN A 496      10.058 -27.580 131.574  1.00 24.90           C  
ATOM   2851  C   ASN A 496      11.545 -27.379 131.856  1.00 26.15           C  
ATOM   2852  O   ASN A 496      12.297 -26.931 130.989  1.00 25.93           O  
ATOM   2853  CB  ASN A 496       9.814 -28.968 130.961  1.00 23.35           C  
ATOM   2854  CG  ASN A 496      10.036 -30.096 131.951  1.00 22.55           C  
ATOM   2855  OD1 ASN A 496      11.070 -30.757 131.931  1.00 23.07           O  
ATOM   2856  ND2 ASN A 496       9.065 -30.316 132.831  1.00 22.11           N  
ATOM   2857  N   ASN A 497      11.960 -27.706 133.076  1.00 27.50           N  
ATOM   2858  CA  ASN A 497      13.353 -27.563 133.472  1.00 28.85           C  
ATOM   2859  C   ASN A 497      14.133 -28.850 133.198  1.00 29.10           C  
ATOM   2860  O   ASN A 497      14.437 -29.626 134.112  1.00 29.51           O  
ATOM   2861  CB  ASN A 497      13.443 -27.204 134.955  1.00 29.99           C  
ATOM   2862  CG  ASN A 497      14.871 -26.984 135.411  1.00 31.15           C  
ATOM   2863  OD1 ASN A 497      15.774 -26.831 134.588  1.00 31.41           O  
ATOM   2864  ND2 ASN A 497      15.085 -26.958 136.725  1.00 31.40           N  
ATOM   2865  N   SER A 498      14.444 -29.071 131.927  1.00 28.52           N  
ATOM   2866  CA  SER A 498      15.189 -30.247 131.506  1.00 27.90           C  
ATOM   2867  C   SER A 498      15.764 -29.980 130.126  1.00 27.51           C  
ATOM   2868  O   SER A 498      15.471 -28.953 129.506  1.00 26.97           O  
ATOM   2869  CB  SER A 498      14.277 -31.474 131.464  1.00 28.07           C  
ATOM   2870  OG  SER A 498      13.259 -31.322 130.493  1.00 28.58           O  
ATOM   2871  N   GLU A 499      16.592 -30.900 129.648  1.00 27.58           N  
ATOM   2872  CA  GLU A 499      17.195 -30.745 128.338  1.00 26.94           C  
ATOM   2873  C   GLU A 499      16.473 -31.603 127.312  1.00 25.00           C  
ATOM   2874  O   GLU A 499      16.701 -32.804 127.230  1.00 25.78           O  
ATOM   2875  CB  GLU A 499      18.681 -31.117 128.389  1.00 28.60           C  
ATOM   2876  CG  GLU A 499      19.415 -30.854 127.067  1.00 29.57           C  
ATOM   2877  CD  GLU A 499      19.177 -29.435 126.532  1.00 30.01           C  
ATOM   2878  OE1 GLU A 499      18.750 -29.296 125.362  1.00 29.61           O  
ATOM   2879  OE2 GLU A 499      19.423 -28.463 127.284  1.00 29.94           O  
ATOM   2880  N   TYR A 500      15.594 -30.980 126.534  1.00 22.77           N  
ATOM   2881  CA  TYR A 500      14.844 -31.697 125.511  1.00 20.70           C  
ATOM   2882  C   TYR A 500      14.998 -31.054 124.136  1.00 18.41           C  
ATOM   2883  O   TYR A 500      14.171 -31.279 123.253  1.00 17.77           O  
ATOM   2884  CB  TYR A 500      13.353 -31.758 125.869  1.00 20.98           C  
ATOM   2885  CG  TYR A 500      12.754 -30.395 126.124  1.00 21.04           C  
ATOM   2886  CD1 TYR A 500      12.789 -29.828 127.396  1.00 21.26           C  
ATOM   2887  CD2 TYR A 500      12.231 -29.633 125.077  1.00 20.80           C  
ATOM   2888  CE1 TYR A 500      12.323 -28.541 127.621  1.00 21.01           C  
ATOM   2889  CE2 TYR A 500      11.771 -28.334 125.292  1.00 20.81           C  
ATOM   2890  CZ  TYR A 500      11.825 -27.796 126.566  1.00 20.47           C  
ATOM   2891  OH  TYR A 500      11.434 -26.499 126.783  1.00 20.34           O  
ATOM   2892  N   SER A 501      16.048 -30.260 123.942  1.00 17.52           N  
ATOM   2893  CA  SER A 501      16.250 -29.639 122.634  1.00 17.68           C  
ATOM   2894  C   SER A 501      16.382 -30.738 121.578  1.00 16.63           C  
ATOM   2895  O   SER A 501      15.974 -30.559 120.429  1.00 17.14           O  
ATOM   2896  CB  SER A 501      17.500 -28.752 122.618  1.00 18.46           C  
ATOM   2897  OG  SER A 501      18.694 -29.518 122.719  1.00 18.82           O  
ATOM   2898  N   TRP A 502      16.942 -31.878 121.969  1.00 15.69           N  
ATOM   2899  CA  TRP A 502      17.089 -32.989 121.038  1.00 15.40           C  
ATOM   2900  C   TRP A 502      16.153 -34.143 121.371  1.00 16.97           C  
ATOM   2901  O   TRP A 502      15.464 -34.655 120.487  1.00 17.83           O  
ATOM   2902  CB  TRP A 502      18.534 -33.497 121.005  1.00 13.44           C  
ATOM   2903  CG  TRP A 502      18.709 -34.684 120.110  1.00 10.99           C  
ATOM   2904  CD1 TRP A 502      19.037 -35.963 120.490  1.00  9.91           C  
ATOM   2905  CD2 TRP A 502      18.531 -34.720 118.687  1.00  9.90           C  
ATOM   2906  NE1 TRP A 502      19.071 -36.788 119.389  1.00  9.97           N  
ATOM   2907  CE2 TRP A 502      18.766 -36.052 118.270  1.00 10.08           C  
ATOM   2908  CE3 TRP A 502      18.195 -33.755 117.723  1.00 10.25           C  
ATOM   2909  CZ2 TRP A 502      18.675 -36.446 116.928  1.00 11.48           C  
ATOM   2910  CZ3 TRP A 502      18.098 -34.141 116.383  1.00 11.07           C  
ATOM   2911  CH2 TRP A 502      18.338 -35.478 115.997  1.00 12.24           C  
ATOM   2912  N   THR A 503      16.112 -34.550 122.635  1.00 17.56           N  
ATOM   2913  CA  THR A 503      15.240 -35.651 123.018  1.00 19.39           C  
ATOM   2914  C   THR A 503      13.749 -35.414 122.759  1.00 19.29           C  
ATOM   2915  O   THR A 503      12.993 -36.365 122.608  1.00 20.23           O  
ATOM   2916  CB  THR A 503      15.428 -36.035 124.498  1.00 20.91           C  
ATOM   2917  OG1 THR A 503      15.346 -34.866 125.315  1.00 21.44           O  
ATOM   2918  CG2 THR A 503      16.786 -36.707 124.700  1.00 21.19           C  
ATOM   2919  N   GLY A 504      13.328 -34.155 122.694  1.00 18.09           N  
ATOM   2920  CA  GLY A 504      11.928 -33.861 122.454  1.00 16.22           C  
ATOM   2921  C   GLY A 504      11.686 -33.297 121.069  1.00 15.50           C  
ATOM   2922  O   GLY A 504      10.593 -32.821 120.762  1.00 16.05           O  
ATOM   2923  N   ALA A 505      12.697 -33.363 120.213  1.00 14.67           N  
ATOM   2924  CA  ALA A 505      12.559 -32.826 118.869  1.00 14.05           C  
ATOM   2925  C   ALA A 505      11.904 -33.767 117.860  1.00 13.48           C  
ATOM   2926  O   ALA A 505      11.889 -34.985 118.029  1.00 13.70           O  
ATOM   2927  CB  ALA A 505      13.911 -32.378 118.355  1.00 14.14           C  
ATOM   2928  N   THR A 506      11.351 -33.163 116.818  1.00 12.95           N  
ATOM   2929  CA  THR A 506      10.698 -33.870 115.735  1.00 13.74           C  
ATOM   2930  C   THR A 506      11.816 -34.214 114.733  1.00 13.19           C  
ATOM   2931  O   THR A 506      12.488 -33.336 114.188  1.00 12.77           O  
ATOM   2932  CB  THR A 506       9.595 -32.964 115.133  1.00 14.41           C  
ATOM   2933  OG1 THR A 506       8.573 -32.782 116.117  1.00 14.59           O  
ATOM   2934  CG2 THR A 506       8.972 -33.569 113.904  1.00 14.87           C  
ATOM   2935  N   LYS A 507      12.014 -35.511 114.517  1.00 13.26           N  
ATOM   2936  CA  LYS A 507      13.088 -35.996 113.663  1.00 12.71           C  
ATOM   2937  C   LYS A 507      12.673 -36.915 112.535  1.00 12.50           C  
ATOM   2938  O   LYS A 507      11.585 -37.482 112.552  1.00 12.69           O  
ATOM   2939  CB  LYS A 507      14.092 -36.772 114.520  1.00 12.24           C  
ATOM   2940  CG  LYS A 507      14.271 -36.257 115.939  1.00 12.92           C  
ATOM   2941  CD  LYS A 507      15.166 -37.174 116.756  1.00 12.96           C  
ATOM   2942  CE  LYS A 507      15.258 -36.742 118.214  1.00 13.53           C  
ATOM   2943  NZ  LYS A 507      13.980 -37.013 118.961  1.00 14.61           N  
ATOM   2944  N   TYR A 508      13.556 -37.050 111.548  1.00 12.78           N  
ATOM   2945  CA  TYR A 508      13.348 -38.005 110.471  1.00 13.05           C  
ATOM   2946  C   TYR A 508      14.582 -38.898 110.548  1.00 14.00           C  
ATOM   2947  O   TYR A 508      15.669 -38.441 110.901  1.00 14.01           O  
ATOM   2948  CB  TYR A 508      13.163 -37.341 109.098  1.00 13.52           C  
ATOM   2949  CG  TYR A 508      14.357 -36.729 108.402  1.00 15.07           C  
ATOM   2950  CD1 TYR A 508      15.442 -37.517 107.982  1.00 15.50           C  
ATOM   2951  CD2 TYR A 508      14.332 -35.377 108.013  1.00 16.01           C  
ATOM   2952  CE1 TYR A 508      16.465 -36.976 107.171  1.00 16.17           C  
ATOM   2953  CE2 TYR A 508      15.342 -34.827 107.206  1.00 16.54           C  
ATOM   2954  CZ  TYR A 508      16.403 -35.637 106.782  1.00 16.57           C  
ATOM   2955  OH  TYR A 508      17.347 -35.116 105.926  1.00 16.41           O  
ATOM   2956  N   HIS A 509      14.393 -40.180 110.260  1.00 14.45           N  
ATOM   2957  CA  HIS A 509      15.439 -41.196 110.354  1.00 14.44           C  
ATOM   2958  C   HIS A 509      15.846 -41.681 108.963  1.00 13.56           C  
ATOM   2959  O   HIS A 509      15.044 -42.271 108.242  1.00 14.47           O  
ATOM   2960  CB  HIS A 509      14.872 -42.344 111.198  1.00 16.61           C  
ATOM   2961  CG  HIS A 509      15.899 -43.282 111.744  1.00 19.52           C  
ATOM   2962  ND1 HIS A 509      16.833 -42.899 112.683  1.00 20.74           N  
ATOM   2963  CD2 HIS A 509      16.122 -44.597 111.505  1.00 20.93           C  
ATOM   2964  CE1 HIS A 509      17.588 -43.937 112.998  1.00 21.70           C  
ATOM   2965  NE2 HIS A 509      17.178 -44.979 112.297  1.00 21.68           N  
ATOM   2966  N   LEU A 510      17.091 -41.437 108.579  1.00 12.65           N  
ATOM   2967  CA  LEU A 510      17.552 -41.841 107.257  1.00 12.86           C  
ATOM   2968  C   LEU A 510      18.871 -42.618 107.344  1.00 13.28           C  
ATOM   2969  O   LEU A 510      19.842 -42.144 107.935  1.00 14.16           O  
ATOM   2970  CB  LEU A 510      17.707 -40.594 106.376  1.00 12.65           C  
ATOM   2971  CG  LEU A 510      17.963 -40.726 104.875  1.00 13.26           C  
ATOM   2972  CD1 LEU A 510      16.740 -41.348 104.167  1.00 13.15           C  
ATOM   2973  CD2 LEU A 510      18.271 -39.346 104.300  1.00 12.54           C  
ATOM   2974  N   ASN A 511      18.899 -43.817 106.763  1.00 13.73           N  
ATOM   2975  CA  ASN A 511      20.088 -44.686 106.770  1.00 12.82           C  
ATOM   2976  C   ASN A 511      20.824 -44.725 108.115  1.00 12.97           C  
ATOM   2977  O   ASN A 511      22.017 -44.446 108.202  1.00 13.45           O  
ATOM   2978  CB  ASN A 511      21.029 -44.270 105.625  1.00 13.42           C  
ATOM   2979  CG  ASN A 511      22.323 -45.089 105.569  1.00 14.18           C  
ATOM   2980  OD1 ASN A 511      22.355 -46.278 105.898  1.00 13.90           O  
ATOM   2981  ND2 ASN A 511      23.397 -44.443 105.131  1.00 14.83           N  
ATOM   2982  N   GLY A 512      20.104 -45.074 109.172  1.00 14.26           N  
ATOM   2983  CA  GLY A 512      20.735 -45.167 110.473  1.00 16.23           C  
ATOM   2984  C   GLY A 512      20.935 -43.886 111.268  1.00 18.32           C  
ATOM   2985  O   GLY A 512      21.225 -43.961 112.465  1.00 19.61           O  
ATOM   2986  N   ARG A 513      20.803 -42.718 110.647  1.00 18.90           N  
ATOM   2987  CA  ARG A 513      20.979 -41.483 111.410  1.00 19.77           C  
ATOM   2988  C   ARG A 513      19.807 -40.503 111.427  1.00 18.30           C  
ATOM   2989  O   ARG A 513      19.051 -40.377 110.467  1.00 17.51           O  
ATOM   2990  CB  ARG A 513      22.271 -40.759 110.994  1.00 20.77           C  
ATOM   2991  CG  ARG A 513      22.483 -40.547 109.518  1.00 22.40           C  
ATOM   2992  CD  ARG A 513      23.916 -40.068 109.275  1.00 23.93           C  
ATOM   2993  NE  ARG A 513      24.056 -39.327 108.025  1.00 25.75           N  
ATOM   2994  CZ  ARG A 513      24.321 -39.876 106.843  1.00 27.88           C  
ATOM   2995  NH1 ARG A 513      24.487 -41.189 106.728  1.00 28.95           N  
ATOM   2996  NH2 ARG A 513      24.407 -39.111 105.765  1.00 28.55           N  
ATOM   2997  N   ASP A 514      19.675 -39.823 112.559  1.00 18.49           N  
ATOM   2998  CA  ASP A 514      18.629 -38.838 112.792  1.00 18.74           C  
ATOM   2999  C   ASP A 514      19.005 -37.427 112.407  1.00 16.52           C  
ATOM   3000  O   ASP A 514      20.147 -37.003 112.565  1.00 16.26           O  
ATOM   3001  CB  ASP A 514      18.237 -38.822 114.264  1.00 21.78           C  
ATOM   3002  CG  ASP A 514      17.412 -40.013 114.652  1.00 25.06           C  
ATOM   3003  OD1 ASP A 514      16.363 -40.231 114.005  1.00 26.40           O  
ATOM   3004  OD2 ASP A 514      17.802 -40.730 115.600  1.00 26.25           O  
ATOM   3005  N   SER A 515      18.023 -36.702 111.896  1.00 15.85           N  
ATOM   3006  CA  SER A 515      18.202 -35.312 111.523  1.00 15.03           C  
ATOM   3007  C   SER A 515      17.008 -34.614 112.121  1.00 15.28           C  
ATOM   3008  O   SER A 515      15.944 -35.205 112.284  1.00 15.89           O  
ATOM   3009  CB  SER A 515      18.176 -35.108 110.005  1.00 14.63           C  
ATOM   3010  OG  SER A 515      19.237 -35.790 109.370  1.00 15.34           O  
ATOM   3011  N   LEU A 516      17.197 -33.353 112.464  1.00 14.06           N  
ATOM   3012  CA  LEU A 516      16.130 -32.558 113.007  1.00 12.49           C  
ATOM   3013  C   LEU A 516      15.254 -32.172 111.816  1.00 10.62           C  
ATOM   3014  O   LEU A 516      15.768 -31.927 110.725  1.00  9.72           O  
ATOM   3015  CB  LEU A 516      16.719 -31.292 113.627  1.00 12.01           C  
ATOM   3016  CG  LEU A 516      15.782 -30.307 114.316  1.00 10.09           C  
ATOM   3017  CD1 LEU A 516      15.311 -30.899 115.655  1.00  7.80           C  
ATOM   3018  CD2 LEU A 516      16.532 -28.983 114.538  1.00 10.98           C  
ATOM   3019  N   VAL A 517      13.939 -32.155 112.005  1.00  9.64           N  
ATOM   3020  CA  VAL A 517      13.064 -31.709 110.929  1.00  9.97           C  
ATOM   3021  C   VAL A 517      12.977 -30.215 111.256  1.00 10.46           C  
ATOM   3022  O   VAL A 517      12.542 -29.837 112.348  1.00 10.93           O  
ATOM   3023  CB  VAL A 517      11.675 -32.403 110.982  1.00  8.94           C  
ATOM   3024  CG1 VAL A 517      10.662 -31.640 110.141  1.00  7.19           C  
ATOM   3025  CG2 VAL A 517      11.808 -33.834 110.448  1.00  8.66           C  
ATOM   3026  N   ASN A 518      13.416 -29.375 110.329  1.00  9.86           N  
ATOM   3027  CA  ASN A 518      13.455 -27.951 110.598  1.00 10.73           C  
ATOM   3028  C   ASN A 518      13.617 -27.108 109.342  1.00 10.44           C  
ATOM   3029  O   ASN A 518      14.634 -27.190 108.663  1.00 11.00           O  
ATOM   3030  CB  ASN A 518      14.623 -27.685 111.558  1.00 12.54           C  
ATOM   3031  CG  ASN A 518      14.739 -26.231 111.962  1.00 15.41           C  
ATOM   3032  OD1 ASN A 518      13.829 -25.435 111.738  1.00 16.28           O  
ATOM   3033  ND2 ASN A 518      15.860 -25.879 112.579  1.00 16.80           N  
ATOM   3034  N   PRO A 519      12.591 -26.332 108.976  1.00 10.89           N  
ATOM   3035  CA  PRO A 519      11.294 -26.207 109.646  1.00 13.02           C  
ATOM   3036  C   PRO A 519      10.537 -27.296 108.883  1.00 15.76           C  
ATOM   3037  O   PRO A 519      10.712 -27.423 107.672  1.00 18.85           O  
ATOM   3038  CB  PRO A 519      10.876 -24.802 109.260  1.00 11.38           C  
ATOM   3039  CG  PRO A 519      11.313 -24.757 107.785  1.00 10.06           C  
ATOM   3040  CD  PRO A 519      12.666 -25.447 107.795  1.00 10.11           C  
ATOM   3041  N   GLY A 520       9.745 -28.126 109.521  1.00 14.02           N  
ATOM   3042  CA  GLY A 520       9.122 -29.157 108.705  1.00 12.26           C  
ATOM   3043  C   GLY A 520       8.028 -28.711 107.766  1.00 10.26           C  
ATOM   3044  O   GLY A 520       8.127 -27.693 107.080  1.00  9.33           O  
ATOM   3045  N   PRO A 521       6.959 -29.505 107.691  1.00 11.03           N  
ATOM   3046  CA  PRO A 521       5.802 -29.209 106.838  1.00 10.83           C  
ATOM   3047  C   PRO A 521       5.173 -27.901 107.325  1.00  8.46           C  
ATOM   3048  O   PRO A 521       5.135 -27.660 108.532  1.00  7.56           O  
ATOM   3049  CB  PRO A 521       4.893 -30.401 107.094  1.00 11.71           C  
ATOM   3050  CG  PRO A 521       5.876 -31.496 107.317  1.00 11.45           C  
ATOM   3051  CD  PRO A 521       6.877 -30.876 108.231  1.00 10.74           C  
ATOM   3052  N   ALA A 522       4.695 -27.068 106.399  1.00  7.12           N  
ATOM   3053  CA  ALA A 522       4.066 -25.785 106.747  1.00  6.13           C  
ATOM   3054  C   ALA A 522       2.866 -25.919 107.695  1.00  6.95           C  
ATOM   3055  O   ALA A 522       1.832 -26.480 107.333  1.00  6.16           O  
ATOM   3056  CB  ALA A 522       3.627 -25.059 105.469  1.00  4.76           C  
ATOM   3057  N   MET A 523       3.012 -25.416 108.914  1.00  7.88           N  
ATOM   3058  CA  MET A 523       1.929 -25.466 109.882  1.00  9.28           C  
ATOM   3059  C   MET A 523       1.811 -24.122 110.588  1.00 10.10           C  
ATOM   3060  O   MET A 523       2.715 -23.293 110.497  1.00 11.68           O  
ATOM   3061  CB  MET A 523       2.171 -26.592 110.881  1.00 10.70           C  
ATOM   3062  CG  MET A 523       2.084 -27.979 110.228  1.00 12.68           C  
ATOM   3063  SD  MET A 523       2.126 -29.335 111.390  1.00 14.30           S  
ATOM   3064  CE  MET A 523       3.861 -29.529 111.606  1.00 13.86           C  
ATOM   3065  N   ALA A 524       0.690 -23.879 111.255  1.00  9.54           N  
ATOM   3066  CA  ALA A 524       0.506 -22.624 111.969  1.00  9.06           C  
ATOM   3067  C   ALA A 524       1.323 -22.726 113.243  1.00  9.64           C  
ATOM   3068  O   ALA A 524       1.352 -23.774 113.877  1.00  9.74           O  
ATOM   3069  CB  ALA A 524      -0.969 -22.400 112.293  1.00  8.06           C  
ATOM   3070  N   SER A 525       1.981 -21.632 113.614  1.00 10.62           N  
ATOM   3071  CA  SER A 525       2.832 -21.596 114.803  1.00 11.22           C  
ATOM   3072  C   SER A 525       2.111 -21.720 116.131  1.00 11.85           C  
ATOM   3073  O   SER A 525       2.645 -22.270 117.091  1.00 11.93           O  
ATOM   3074  CB  SER A 525       3.649 -20.306 114.814  1.00 10.13           C  
ATOM   3075  OG  SER A 525       4.209 -20.063 113.540  1.00 10.24           O  
ATOM   3076  N   HIS A 526       0.902 -21.184 116.198  1.00 13.37           N  
ATOM   3077  CA  HIS A 526       0.132 -21.234 117.432  1.00 14.99           C  
ATOM   3078  C   HIS A 526      -1.313 -20.961 117.090  1.00 16.34           C  
ATOM   3079  O   HIS A 526      -1.619 -20.481 115.999  1.00 15.73           O  
ATOM   3080  CB  HIS A 526       0.625 -20.164 118.424  1.00 15.37           C  
ATOM   3081  CG  HIS A 526       0.658 -18.776 117.853  1.00 16.23           C  
ATOM   3082  ND1 HIS A 526       1.816 -18.185 117.395  1.00 16.55           N  
ATOM   3083  CD2 HIS A 526      -0.339 -17.890 117.599  1.00 17.48           C  
ATOM   3084  CE1 HIS A 526       1.533 -17.001 116.878  1.00 17.96           C  
ATOM   3085  NE2 HIS A 526       0.232 -16.797 116.987  1.00 18.14           N  
ATOM   3086  N   LYS A 527      -2.206 -21.262 118.021  1.00 18.67           N  
ATOM   3087  CA  LYS A 527      -3.604 -20.979 117.776  1.00 21.28           C  
ATOM   3088  C   LYS A 527      -3.882 -19.584 118.332  1.00 23.13           C  
ATOM   3089  O   LYS A 527      -3.068 -19.034 119.071  1.00 23.47           O  
ATOM   3090  CB  LYS A 527      -4.504 -22.039 118.429  1.00 21.02           C  
ATOM   3091  CG  LYS A 527      -4.354 -22.226 119.929  1.00 21.10           C  
ATOM   3092  CD  LYS A 527      -5.379 -23.263 120.397  1.00 21.63           C  
ATOM   3093  CE  LYS A 527      -5.404 -23.463 121.898  1.00 22.67           C  
ATOM   3094  NZ  LYS A 527      -4.174 -24.145 122.390  1.00 23.78           N  
ATOM   3095  N   ASP A 528      -5.019 -19.012 117.959  1.00 25.02           N  
ATOM   3096  CA  ASP A 528      -5.396 -17.683 118.413  1.00 27.36           C  
ATOM   3097  C   ASP A 528      -5.158 -17.396 119.892  1.00 28.59           C  
ATOM   3098  O   ASP A 528      -5.520 -18.190 120.770  1.00 27.80           O  
ATOM   3099  CB  ASP A 528      -6.866 -17.399 118.083  1.00 28.22           C  
ATOM   3100  CG  ASP A 528      -7.094 -17.147 116.597  1.00 28.89           C  
ATOM   3101  OD1 ASP A 528      -6.173 -16.601 115.945  1.00 29.35           O  
ATOM   3102  OD2 ASP A 528      -8.190 -17.478 116.087  1.00 28.75           O  
ATOM   3103  N   ASP A 529      -4.536 -16.242 120.139  1.00 30.50           N  
ATOM   3104  CA  ASP A 529      -4.234 -15.751 121.483  1.00 32.76           C  
ATOM   3105  C   ASP A 529      -3.184 -16.548 122.255  1.00 33.26           C  
ATOM   3106  O   ASP A 529      -3.245 -16.646 123.483  1.00 33.90           O  
ATOM   3107  CB  ASP A 529      -5.521 -15.659 122.312  1.00 34.23           C  
ATOM   3108  CG  ASP A 529      -6.604 -14.832 121.623  1.00 35.70           C  
ATOM   3109  OD1 ASP A 529      -6.259 -13.828 120.948  1.00 36.20           O  
ATOM   3110  OD2 ASP A 529      -7.799 -15.181 121.768  1.00 35.73           O  
ATOM   3111  N   GLU A 530      -2.224 -17.111 121.530  1.00 32.80           N  
ATOM   3112  CA  GLU A 530      -1.149 -17.885 122.138  1.00 32.31           C  
ATOM   3113  C   GLU A 530       0.111 -17.549 121.366  1.00 32.02           C  
ATOM   3114  O   GLU A 530       0.893 -18.417 120.984  1.00 31.95           O  
ATOM   3115  CB  GLU A 530      -1.449 -19.382 122.062  1.00 32.68           C  
ATOM   3116  CG  GLU A 530      -2.716 -19.780 122.792  1.00 33.52           C  
ATOM   3117  CD  GLU A 530      -2.646 -21.180 123.363  1.00 34.99           C  
ATOM   3118  OE1 GLU A 530      -2.401 -22.131 122.590  1.00 35.53           O  
ATOM   3119  OE2 GLU A 530      -2.838 -21.334 124.591  1.00 35.64           O  
ATOM   3120  N   GLU A 531       0.276 -16.250 121.160  1.00 32.37           N  
ATOM   3121  CA  GLU A 531       1.385 -15.645 120.444  1.00 32.28           C  
ATOM   3122  C   GLU A 531       2.751 -15.901 121.100  1.00 28.95           C  
ATOM   3123  O   GLU A 531       3.787 -15.731 120.460  1.00 29.21           O  
ATOM   3124  CB  GLU A 531       1.093 -14.138 120.335  1.00 35.96           C  
ATOM   3125  CG  GLU A 531       2.158 -13.278 119.669  1.00 39.71           C  
ATOM   3126  CD  GLU A 531       2.333 -13.571 118.189  1.00 42.47           C  
ATOM   3127  OE1 GLU A 531       1.309 -13.631 117.470  1.00 43.24           O  
ATOM   3128  OE2 GLU A 531       3.497 -13.728 117.745  1.00 43.20           O  
ATOM   3129  N   LYS A 532       2.755 -16.315 122.365  1.00 26.16           N  
ATOM   3130  CA  LYS A 532       4.004 -16.586 123.086  1.00 24.21           C  
ATOM   3131  C   LYS A 532       4.572 -17.994 122.845  1.00 21.66           C  
ATOM   3132  O   LYS A 532       5.697 -18.297 123.249  1.00 20.86           O  
ATOM   3133  CB  LYS A 532       3.797 -16.400 124.591  1.00 24.85           C  
ATOM   3134  CG  LYS A 532       2.943 -17.479 125.224  1.00 25.55           C  
ATOM   3135  CD  LYS A 532       2.922 -17.339 126.740  1.00 27.03           C  
ATOM   3136  CE  LYS A 532       2.154 -18.478 127.388  1.00 27.59           C  
ATOM   3137  NZ  LYS A 532       2.042 -18.323 128.860  1.00 28.20           N  
ATOM   3138  N   PHE A 533       3.792 -18.853 122.198  1.00 19.49           N  
ATOM   3139  CA  PHE A 533       4.226 -20.215 121.913  1.00 16.71           C  
ATOM   3140  C   PHE A 533       4.670 -20.370 120.476  1.00 14.64           C  
ATOM   3141  O   PHE A 533       4.173 -19.685 119.581  1.00 15.23           O  
ATOM   3142  CB  PHE A 533       3.092 -21.214 122.157  1.00 16.05           C  
ATOM   3143  CG  PHE A 533       2.688 -21.342 123.586  1.00 16.04           C  
ATOM   3144  CD1 PHE A 533       3.610 -21.725 124.552  1.00 16.18           C  
ATOM   3145  CD2 PHE A 533       1.374 -21.114 123.969  1.00 17.07           C  
ATOM   3146  CE1 PHE A 533       3.234 -21.883 125.888  1.00 16.07           C  
ATOM   3147  CE2 PHE A 533       0.983 -21.268 125.303  1.00 17.59           C  
ATOM   3148  CZ  PHE A 533       1.922 -21.657 126.265  1.00 16.92           C  
ATOM   3149  N   PHE A 534       5.616 -21.275 120.264  1.00 12.94           N  
ATOM   3150  CA  PHE A 534       6.096 -21.583 118.931  1.00 11.81           C  
ATOM   3151  C   PHE A 534       6.619 -23.026 118.895  1.00  9.64           C  
ATOM   3152  O   PHE A 534       6.991 -23.597 119.923  1.00  8.43           O  
ATOM   3153  CB  PHE A 534       7.179 -20.578 118.466  1.00 13.19           C  
ATOM   3154  CG  PHE A 534       8.470 -20.641 119.247  1.00 14.79           C  
ATOM   3155  CD1 PHE A 534       8.577 -20.043 120.504  1.00 15.39           C  
ATOM   3156  CD2 PHE A 534       9.578 -21.319 118.728  1.00 15.55           C  
ATOM   3157  CE1 PHE A 534       9.770 -20.118 121.235  1.00 16.11           C  
ATOM   3158  CE2 PHE A 534      10.779 -21.403 119.452  1.00 16.30           C  
ATOM   3159  CZ  PHE A 534      10.874 -20.799 120.709  1.00 16.33           C  
ATOM   3160  N   PRO A 535       6.623 -23.635 117.702  1.00  9.18           N  
ATOM   3161  CA  PRO A 535       7.080 -25.001 117.421  1.00  9.71           C  
ATOM   3162  C   PRO A 535       8.582 -25.108 117.701  1.00 11.29           C  
ATOM   3163  O   PRO A 535       9.360 -24.331 117.155  1.00 11.19           O  
ATOM   3164  CB  PRO A 535       6.804 -25.170 115.929  1.00  9.66           C  
ATOM   3165  CG  PRO A 535       5.826 -24.090 115.594  1.00 10.23           C  
ATOM   3166  CD  PRO A 535       6.192 -22.949 116.474  1.00  9.57           C  
ATOM   3167  N   GLN A 536       8.990 -26.068 118.527  1.00 12.50           N  
ATOM   3168  CA  GLN A 536      10.402 -26.240 118.866  1.00 13.14           C  
ATOM   3169  C   GLN A 536      11.341 -26.061 117.667  1.00 12.25           C  
ATOM   3170  O   GLN A 536      12.361 -25.382 117.785  1.00 12.68           O  
ATOM   3171  CB  GLN A 536      10.619 -27.604 119.512  1.00 14.27           C  
ATOM   3172  CG  GLN A 536      12.042 -27.850 119.922  1.00 15.17           C  
ATOM   3173  CD  GLN A 536      12.193 -29.054 120.803  1.00 16.11           C  
ATOM   3174  OE1 GLN A 536      11.388 -29.285 121.699  1.00 16.47           O  
ATOM   3175  NE2 GLN A 536      13.251 -29.820 120.578  1.00 17.21           N  
ATOM   3176  N   SER A 537      11.021 -26.671 116.526  1.00  9.99           N  
ATOM   3177  CA  SER A 537      11.836 -26.486 115.326  1.00  9.16           C  
ATOM   3178  C   SER A 537      10.944 -26.328 114.105  1.00  9.48           C  
ATOM   3179  O   SER A 537      11.289 -26.748 112.998  1.00  9.95           O  
ATOM   3180  CB  SER A 537      12.846 -27.641 115.117  1.00 10.12           C  
ATOM   3181  OG  SER A 537      12.239 -28.885 114.788  1.00 10.64           O  
ATOM   3182  N   GLY A 538       9.797 -25.686 114.306  1.00  9.57           N  
ATOM   3183  CA  GLY A 538       8.858 -25.498 113.217  1.00  9.55           C  
ATOM   3184  C   GLY A 538       8.831 -24.138 112.546  1.00  9.77           C  
ATOM   3185  O   GLY A 538       8.015 -23.908 111.660  1.00  8.83           O  
ATOM   3186  N   VAL A 539       9.705 -23.225 112.952  1.00 11.76           N  
ATOM   3187  CA  VAL A 539       9.734 -21.898 112.324  1.00 11.90           C  
ATOM   3188  C   VAL A 539      11.140 -21.471 111.975  1.00 11.55           C  
ATOM   3189  O   VAL A 539      12.106 -21.978 112.544  1.00 11.59           O  
ATOM   3190  CB  VAL A 539       9.131 -20.791 113.251  1.00 11.82           C  
ATOM   3191  CG1 VAL A 539       7.613 -20.805 113.182  1.00 11.50           C  
ATOM   3192  CG2 VAL A 539       9.607 -20.990 114.684  1.00 11.16           C  
ATOM   3193  N   LEU A 540      11.252 -20.544 111.029  1.00 12.54           N  
ATOM   3194  CA  LEU A 540      12.549 -20.001 110.656  1.00 12.55           C  
ATOM   3195  C   LEU A 540      12.927 -19.004 111.756  1.00 12.79           C  
ATOM   3196  O   LEU A 540      12.107 -18.179 112.163  1.00 13.73           O  
ATOM   3197  CB  LEU A 540      12.485 -19.247 109.329  1.00 12.96           C  
ATOM   3198  CG  LEU A 540      12.134 -19.957 108.020  1.00 14.91           C  
ATOM   3199  CD1 LEU A 540      12.755 -19.186 106.878  1.00 15.18           C  
ATOM   3200  CD2 LEU A 540      12.678 -21.368 108.005  1.00 16.42           C  
ATOM   3201  N   ILE A 541      14.154 -19.086 112.249  1.00 11.50           N  
ATOM   3202  CA  ILE A 541      14.615 -18.161 113.276  1.00 10.64           C  
ATOM   3203  C   ILE A 541      15.842 -17.380 112.776  1.00  9.92           C  
ATOM   3204  O   ILE A 541      16.892 -17.959 112.480  1.00  9.18           O  
ATOM   3205  CB  ILE A 541      14.976 -18.903 114.569  1.00  9.22           C  
ATOM   3206  CG1 ILE A 541      13.733 -19.629 115.098  1.00  9.18           C  
ATOM   3207  CG2 ILE A 541      15.503 -17.925 115.595  1.00  9.33           C  
ATOM   3208  CD1 ILE A 541      13.954 -20.442 116.354  1.00  8.56           C  
ATOM   3209  N   PHE A 542      15.695 -16.066 112.662  1.00  9.02           N  
ATOM   3210  CA  PHE A 542      16.800 -15.232 112.212  1.00  8.10           C  
ATOM   3211  C   PHE A 542      17.518 -14.612 113.386  1.00  6.82           C  
ATOM   3212  O   PHE A 542      16.969 -14.510 114.475  1.00  6.90           O  
ATOM   3213  CB  PHE A 542      16.287 -14.138 111.294  1.00  7.65           C  
ATOM   3214  CG  PHE A 542      15.635 -14.658 110.065  1.00  8.03           C  
ATOM   3215  CD1 PHE A 542      16.405 -15.074 108.978  1.00  7.22           C  
ATOM   3216  CD2 PHE A 542      14.235 -14.731 109.979  1.00  8.27           C  
ATOM   3217  CE1 PHE A 542      15.797 -15.554 107.818  1.00  7.66           C  
ATOM   3218  CE2 PHE A 542      13.617 -15.206 108.828  1.00  8.09           C  
ATOM   3219  CZ  PHE A 542      14.396 -15.620 107.740  1.00  8.18           C  
ATOM   3220  N   GLY A 543      18.764 -14.213 113.178  1.00  7.67           N  
ATOM   3221  CA  GLY A 543      19.493 -13.593 114.268  1.00  8.33           C  
ATOM   3222  C   GLY A 543      19.424 -12.083 114.152  1.00  9.28           C  
ATOM   3223  O   GLY A 543      19.310 -11.545 113.051  1.00  8.76           O  
ATOM   3224  N   LYS A 544      19.452 -11.394 115.286  1.00 11.61           N  
ATOM   3225  CA  LYS A 544      19.448  -9.935 115.269  1.00 14.87           C  
ATOM   3226  C   LYS A 544      20.853  -9.502 114.882  1.00 16.24           C  
ATOM   3227  O   LYS A 544      21.774 -10.318 114.892  1.00 16.33           O  
ATOM   3228  CB  LYS A 544      19.077  -9.383 116.643  1.00 16.45           C  
ATOM   3229  CG  LYS A 544      17.603  -9.510 116.930  1.00 18.17           C  
ATOM   3230  CD  LYS A 544      17.250  -8.955 118.278  1.00 20.24           C  
ATOM   3231  CE  LYS A 544      15.745  -8.931 118.468  1.00 21.59           C  
ATOM   3232  NZ  LYS A 544      15.393  -8.579 119.876  1.00 22.48           N  
ATOM   3233  N   GLN A 545      21.034  -8.239 114.528  1.00 18.26           N  
ATOM   3234  CA  GLN A 545      22.367  -7.787 114.132  1.00 20.34           C  
ATOM   3235  C   GLN A 545      23.422  -8.027 115.209  1.00 20.30           C  
ATOM   3236  O   GLN A 545      23.219  -7.712 116.387  1.00 19.67           O  
ATOM   3237  CB  GLN A 545      22.352  -6.302 113.761  1.00 22.64           C  
ATOM   3238  CG  GLN A 545      23.691  -5.789 113.236  1.00 24.86           C  
ATOM   3239  CD  GLN A 545      24.120  -6.494 111.958  1.00 26.57           C  
ATOM   3240  OE1 GLN A 545      23.327  -6.642 111.023  1.00 27.22           O  
ATOM   3241  NE2 GLN A 545      25.382  -6.922 111.905  1.00 26.70           N  
ATOM   3242  N   GLY A 546      24.547  -8.604 114.792  1.00 21.37           N  
ATOM   3243  CA  GLY A 546      25.638  -8.863 115.712  1.00 22.43           C  
ATOM   3244  C   GLY A 546      25.440 -10.037 116.648  1.00 23.65           C  
ATOM   3245  O   GLY A 546      26.163 -10.172 117.640  1.00 23.81           O  
ATOM   3246  N   SER A 547      24.458 -10.879 116.347  1.00 24.60           N  
ATOM   3247  CA  SER A 547      24.185 -12.052 117.167  1.00 25.54           C  
ATOM   3248  C   SER A 547      25.273 -13.081 116.950  1.00 26.02           C  
ATOM   3249  O   SER A 547      25.727 -13.289 115.823  1.00 26.04           O  
ATOM   3250  CB  SER A 547      22.832 -12.665 116.808  1.00 25.31           C  
ATOM   3251  OG  SER A 547      21.795 -11.961 117.460  1.00 25.73           O  
ATOM   3252  N   GLU A 548      25.691 -13.721 118.033  1.00 26.80           N  
ATOM   3253  CA  GLU A 548      26.729 -14.728 117.944  1.00 28.62           C  
ATOM   3254  C   GLU A 548      26.237 -16.039 117.345  1.00 27.87           C  
ATOM   3255  O   GLU A 548      25.073 -16.183 116.984  1.00 27.90           O  
ATOM   3256  CB  GLU A 548      27.354 -14.946 119.322  1.00 31.69           C  
ATOM   3257  CG  GLU A 548      28.222 -13.763 119.741  1.00 35.03           C  
ATOM   3258  CD  GLU A 548      28.775 -13.891 121.152  1.00 38.09           C  
ATOM   3259  OE1 GLU A 548      29.401 -14.933 121.459  1.00 39.13           O  
ATOM   3260  OE2 GLU A 548      28.596 -12.943 121.952  1.00 38.66           O  
ATOM   3261  N   LYS A 549      27.142 -16.996 117.234  1.00 27.73           N  
ATOM   3262  CA  LYS A 549      26.825 -18.280 116.639  1.00 26.71           C  
ATOM   3263  C   LYS A 549      26.233 -19.350 117.559  1.00 24.70           C  
ATOM   3264  O   LYS A 549      25.410 -20.141 117.111  1.00 24.83           O  
ATOM   3265  CB  LYS A 549      28.088 -18.827 115.965  1.00 28.23           C  
ATOM   3266  CG  LYS A 549      28.007 -20.275 115.514  1.00 29.99           C  
ATOM   3267  CD  LYS A 549      29.386 -20.806 115.137  1.00 30.95           C  
ATOM   3268  CE  LYS A 549      29.349 -22.291 114.766  1.00 31.18           C  
ATOM   3269  NZ  LYS A 549      28.437 -22.549 113.613  1.00 31.21           N  
ATOM   3270  N   THR A 550      26.614 -19.375 118.832  1.00 23.86           N  
ATOM   3271  CA  THR A 550      26.128 -20.438 119.704  1.00 24.15           C  
ATOM   3272  C   THR A 550      25.549 -20.111 121.080  1.00 23.46           C  
ATOM   3273  O   THR A 550      26.051 -19.259 121.810  1.00 23.35           O  
ATOM   3274  CB  THR A 550      27.240 -21.538 119.871  1.00 25.12           C  
ATOM   3275  OG1 THR A 550      27.536 -21.748 121.260  1.00 25.29           O  
ATOM   3276  CG2 THR A 550      28.502 -21.132 119.135  1.00 25.10           C  
ATOM   3277  N   ASN A 551      24.487 -20.843 121.414  1.00 23.71           N  
ATOM   3278  CA  ASN A 551      23.759 -20.711 122.674  1.00 23.57           C  
ATOM   3279  C   ASN A 551      23.454 -19.270 123.030  1.00 22.73           C  
ATOM   3280  O   ASN A 551      23.691 -18.795 124.144  1.00 23.15           O  
ATOM   3281  CB  ASN A 551      24.512 -21.412 123.800  1.00 24.02           C  
ATOM   3282  CG  ASN A 551      24.538 -22.909 123.615  1.00 24.56           C  
ATOM   3283  OD1 ASN A 551      23.780 -23.456 122.812  1.00 25.34           O  
ATOM   3284  ND2 ASN A 551      25.402 -23.586 124.360  1.00 24.51           N  
ATOM   3285  N   VAL A 552      22.903 -18.595 122.038  1.00 22.00           N  
ATOM   3286  CA  VAL A 552      22.495 -17.210 122.106  1.00 22.10           C  
ATOM   3287  C   VAL A 552      21.127 -17.168 122.813  1.00 23.77           C  
ATOM   3288  O   VAL A 552      20.299 -18.059 122.614  1.00 23.90           O  
ATOM   3289  CB  VAL A 552      22.419 -16.693 120.657  1.00 21.66           C  
ATOM   3290  CG1 VAL A 552      21.064 -16.109 120.349  1.00 21.66           C  
ATOM   3291  CG2 VAL A 552      23.538 -15.728 120.402  1.00 21.71           C  
ATOM   3292  N   ASP A 553      20.890 -16.160 123.648  1.00 25.06           N  
ATOM   3293  CA  ASP A 553      19.604 -16.046 124.352  1.00 26.41           C  
ATOM   3294  C   ASP A 553      18.481 -15.608 123.424  1.00 25.04           C  
ATOM   3295  O   ASP A 553      18.728 -15.006 122.383  1.00 24.50           O  
ATOM   3296  CB  ASP A 553      19.717 -15.072 125.527  1.00 28.88           C  
ATOM   3297  CG  ASP A 553      19.980 -15.784 126.843  1.00 31.51           C  
ATOM   3298  OD1 ASP A 553      20.711 -16.800 126.837  1.00 31.93           O  
ATOM   3299  OD2 ASP A 553      19.462 -15.321 127.888  1.00 32.69           O  
ATOM   3300  N   ILE A 554      17.243 -15.899 123.814  1.00 25.02           N  
ATOM   3301  CA  ILE A 554      16.086 -15.580 122.985  1.00 24.96           C  
ATOM   3302  C   ILE A 554      15.946 -14.116 122.543  1.00 25.34           C  
ATOM   3303  O   ILE A 554      15.310 -13.841 121.527  1.00 25.66           O  
ATOM   3304  CB  ILE A 554      14.767 -16.096 123.663  1.00 24.78           C  
ATOM   3305  CG1 ILE A 554      13.617 -16.101 122.646  1.00 24.74           C  
ATOM   3306  CG2 ILE A 554      14.415 -15.255 124.875  1.00 23.88           C  
ATOM   3307  CD1 ILE A 554      12.424 -16.924 123.102  1.00 24.64           C  
ATOM   3308  N   GLU A 555      16.552 -13.181 123.271  1.00 25.94           N  
ATOM   3309  CA  GLU A 555      16.488 -11.763 122.896  1.00 26.37           C  
ATOM   3310  C   GLU A 555      17.411 -11.464 121.720  1.00 23.17           C  
ATOM   3311  O   GLU A 555      17.311 -10.409 121.093  1.00 23.06           O  
ATOM   3312  CB  GLU A 555      16.893 -10.859 124.065  1.00 30.08           C  
ATOM   3313  CG  GLU A 555      16.193 -11.170 125.384  1.00 33.68           C  
ATOM   3314  CD  GLU A 555      16.802 -12.376 126.092  1.00 36.29           C  
ATOM   3315  OE1 GLU A 555      18.033 -12.363 126.329  1.00 37.24           O  
ATOM   3316  OE2 GLU A 555      16.058 -13.328 126.418  1.00 36.70           O  
ATOM   3317  N   LYS A 556      18.309 -12.395 121.419  1.00 20.83           N  
ATOM   3318  CA  LYS A 556      19.241 -12.212 120.320  1.00 19.54           C  
ATOM   3319  C   LYS A 556      18.694 -12.718 118.987  1.00 17.38           C  
ATOM   3320  O   LYS A 556      19.300 -12.483 117.945  1.00 17.00           O  
ATOM   3321  CB  LYS A 556      20.558 -12.925 120.626  1.00 21.46           C  
ATOM   3322  CG  LYS A 556      21.047 -12.779 122.076  1.00 22.94           C  
ATOM   3323  CD  LYS A 556      21.371 -11.342 122.451  1.00 24.44           C  
ATOM   3324  CE  LYS A 556      22.550 -10.813 121.638  1.00 25.95           C  
ATOM   3325  NZ  LYS A 556      23.126  -9.569 122.228  1.00 26.69           N  
ATOM   3326  N   VAL A 557      17.551 -13.405 119.010  1.00 16.08           N  
ATOM   3327  CA  VAL A 557      16.975 -13.929 117.773  1.00 15.28           C  
ATOM   3328  C   VAL A 557      15.575 -13.409 117.482  1.00 15.59           C  
ATOM   3329  O   VAL A 557      14.883 -12.926 118.365  1.00 16.88           O  
ATOM   3330  CB  VAL A 557      16.937 -15.504 117.764  1.00 13.89           C  
ATOM   3331  CG1 VAL A 557      18.340 -16.067 117.938  1.00 12.21           C  
ATOM   3332  CG2 VAL A 557      15.995 -16.032 118.848  1.00 13.21           C  
ATOM   3333  N   MET A 558      15.169 -13.504 116.226  1.00 15.40           N  
ATOM   3334  CA  MET A 558      13.852 -13.055 115.808  1.00 15.49           C  
ATOM   3335  C   MET A 558      13.115 -14.284 115.306  1.00 14.72           C  
ATOM   3336  O   MET A 558      13.400 -14.801 114.232  1.00 14.36           O  
ATOM   3337  CB  MET A 558      13.954 -12.020 114.677  1.00 15.95           C  
ATOM   3338  CG  MET A 558      15.122 -11.059 114.816  1.00 16.25           C  
ATOM   3339  SD  MET A 558      15.078  -9.652 113.676  1.00 16.95           S  
ATOM   3340  CE  MET A 558      15.509 -10.386 112.075  1.00 16.31           C  
ATOM   3341  N   ILE A 559      12.170 -14.748 116.107  1.00 15.57           N  
ATOM   3342  CA  ILE A 559      11.380 -15.923 115.786  1.00 16.06           C  
ATOM   3343  C   ILE A 559      10.188 -15.548 114.926  1.00 16.65           C  
ATOM   3344  O   ILE A 559       9.340 -14.765 115.348  1.00 18.73           O  
ATOM   3345  CB  ILE A 559      10.900 -16.590 117.094  1.00 15.58           C  
ATOM   3346  CG1 ILE A 559      12.119 -16.948 117.946  1.00 14.87           C  
ATOM   3347  CG2 ILE A 559      10.049 -17.816 116.795  1.00 15.48           C  
ATOM   3348  CD1 ILE A 559      11.785 -17.436 119.340  1.00 14.82           C  
ATOM   3349  N   THR A 560      10.129 -16.079 113.714  1.00 16.55           N  
ATOM   3350  CA  THR A 560       8.999 -15.800 112.831  1.00 17.94           C  
ATOM   3351  C   THR A 560       7.791 -16.590 113.331  1.00 20.12           C  
ATOM   3352  O   THR A 560       7.904 -17.411 114.238  1.00 19.86           O  
ATOM   3353  CB  THR A 560       9.249 -16.267 111.381  1.00 16.71           C  
ATOM   3354  OG1 THR A 560       9.553 -17.662 111.382  1.00 16.69           O  
ATOM   3355  CG2 THR A 560      10.382 -15.519 110.746  1.00 16.94           C  
ATOM   3356  N   ASP A 561       6.629 -16.328 112.750  1.00 23.26           N  
ATOM   3357  CA  ASP A 561       5.434 -17.072 113.116  1.00 25.79           C  
ATOM   3358  C   ASP A 561       4.488 -17.061 111.934  1.00 25.18           C  
ATOM   3359  O   ASP A 561       4.248 -16.025 111.319  1.00 24.94           O  
ATOM   3360  CB  ASP A 561       4.777 -16.512 114.390  1.00 28.34           C  
ATOM   3361  CG  ASP A 561       3.875 -15.342 114.125  1.00 30.59           C  
ATOM   3362  OD1 ASP A 561       4.359 -14.341 113.550  1.00 31.64           O  
ATOM   3363  OD2 ASP A 561       2.682 -15.420 114.508  1.00 30.71           O  
ATOM   3364  N   GLU A 562       3.980 -18.245 111.613  1.00 25.33           N  
ATOM   3365  CA  GLU A 562       3.089 -18.436 110.481  1.00 25.45           C  
ATOM   3366  C   GLU A 562       1.623 -18.522 110.880  1.00 25.95           C  
ATOM   3367  O   GLU A 562       0.932 -19.438 110.439  1.00 26.72           O  
ATOM   3368  CB  GLU A 562       3.456 -19.734 109.754  1.00 25.87           C  
ATOM   3369  CG  GLU A 562       4.907 -19.875 109.321  1.00 26.48           C  
ATOM   3370  CD  GLU A 562       5.205 -19.197 107.991  1.00 26.70           C  
ATOM   3371  OE1 GLU A 562       4.382 -19.310 107.058  1.00 27.26           O  
ATOM   3372  OE2 GLU A 562       6.273 -18.567 107.871  1.00 26.73           O  
ATOM   3373  N   GLU A 563       1.126 -17.594 111.688  1.00 26.00           N  
ATOM   3374  CA  GLU A 563      -0.280 -17.669 112.081  1.00 26.24           C  
ATOM   3375  C   GLU A 563      -1.266 -17.393 110.938  1.00 23.29           C  
ATOM   3376  O   GLU A 563      -2.450 -17.656 111.066  1.00 22.89           O  
ATOM   3377  CB  GLU A 563      -0.565 -16.732 113.264  1.00 28.50           C  
ATOM   3378  CG  GLU A 563      -0.468 -15.243 112.977  1.00 30.70           C  
ATOM   3379  CD  GLU A 563      -0.552 -14.417 114.262  1.00 33.72           C  
ATOM   3380  OE1 GLU A 563      -1.420 -14.715 115.120  1.00 34.11           O  
ATOM   3381  OE2 GLU A 563       0.247 -13.464 114.420  1.00 34.68           O  
ATOM   3382  N   GLU A 564      -0.779 -16.883 109.816  1.00 22.16           N  
ATOM   3383  CA  GLU A 564      -1.652 -16.600 108.687  1.00 22.07           C  
ATOM   3384  C   GLU A 564      -2.283 -17.840 108.083  1.00 20.29           C  
ATOM   3385  O   GLU A 564      -3.451 -17.822 107.691  1.00 21.18           O  
ATOM   3386  CB  GLU A 564      -0.898 -15.858 107.587  1.00 24.67           C  
ATOM   3387  CG  GLU A 564      -0.470 -14.473 107.995  1.00 27.72           C  
ATOM   3388  CD  GLU A 564      -1.579 -13.761 108.721  1.00 30.84           C  
ATOM   3389  OE1 GLU A 564      -2.730 -13.827 108.228  1.00 31.85           O  
ATOM   3390  OE2 GLU A 564      -1.313 -13.144 109.779  1.00 31.60           O  
ATOM   3391  N   ILE A 565      -1.519 -18.920 108.007  1.00 17.19           N  
ATOM   3392  CA  ILE A 565      -2.029 -20.147 107.424  1.00 13.78           C  
ATOM   3393  C   ILE A 565      -2.908 -20.987 108.345  1.00 11.73           C  
ATOM   3394  O   ILE A 565      -3.372 -22.037 107.936  1.00 11.00           O  
ATOM   3395  CB  ILE A 565      -0.864 -21.022 106.866  1.00 12.36           C  
ATOM   3396  CG1 ILE A 565       0.080 -21.466 107.990  1.00 10.38           C  
ATOM   3397  CG2 ILE A 565      -0.102 -20.241 105.818  1.00 11.98           C  
ATOM   3398  CD1 ILE A 565       1.247 -22.303 107.481  1.00  9.48           C  
ATOM   3399  N   ARG A 566      -3.156 -20.529 109.571  1.00 11.29           N  
ATOM   3400  CA  ARG A 566      -3.997 -21.287 110.497  1.00 12.43           C  
ATOM   3401  C   ARG A 566      -5.424 -21.503 109.959  1.00 12.61           C  
ATOM   3402  O   ARG A 566      -6.215 -22.240 110.547  1.00 12.36           O  
ATOM   3403  CB  ARG A 566      -4.069 -20.590 111.863  1.00 14.39           C  
ATOM   3404  CG  ARG A 566      -4.834 -19.273 111.849  1.00 17.50           C  
ATOM   3405  CD  ARG A 566      -4.615 -18.452 113.128  1.00 20.29           C  
ATOM   3406  NE  ARG A 566      -5.641 -17.418 113.282  1.00 22.91           N  
ATOM   3407  CZ  ARG A 566      -5.854 -16.402 112.441  1.00 24.66           C  
ATOM   3408  NH1 ARG A 566      -5.107 -16.240 111.350  1.00 24.81           N  
ATOM   3409  NH2 ARG A 566      -6.842 -15.546 112.688  1.00 25.29           N  
ATOM   3410  N   THR A 567      -5.750 -20.855 108.847  1.00 12.31           N  
ATOM   3411  CA  THR A 567      -7.066 -20.993 108.248  1.00 11.45           C  
ATOM   3412  C   THR A 567      -7.228 -22.275 107.432  1.00 11.34           C  
ATOM   3413  O   THR A 567      -8.347 -22.671 107.143  1.00 12.17           O  
ATOM   3414  CB  THR A 567      -7.393 -19.796 107.328  1.00  9.49           C  
ATOM   3415  OG1 THR A 567      -6.243 -19.478 106.541  1.00  9.28           O  
ATOM   3416  CG2 THR A 567      -7.827 -18.587 108.147  1.00  8.17           C  
ATOM   3417  N   THR A 568      -6.117 -22.909 107.056  1.00 10.06           N  
ATOM   3418  CA  THR A 568      -6.151 -24.134 106.272  1.00  8.65           C  
ATOM   3419  C   THR A 568      -5.194 -25.183 106.800  1.00  8.35           C  
ATOM   3420  O   THR A 568      -5.454 -26.374 106.679  1.00  8.72           O  
ATOM   3421  CB  THR A 568      -5.787 -23.886 104.787  1.00  8.58           C  
ATOM   3422  OG1 THR A 568      -4.621 -23.054 104.720  1.00  8.91           O  
ATOM   3423  CG2 THR A 568      -6.941 -23.206 104.040  1.00  8.33           C  
ATOM   3424  N   ASN A 569      -4.074 -24.748 107.372  1.00  8.19           N  
ATOM   3425  CA  ASN A 569      -3.076 -25.679 107.888  1.00  6.91           C  
ATOM   3426  C   ASN A 569      -3.263 -25.862 109.385  1.00  7.43           C  
ATOM   3427  O   ASN A 569      -3.646 -24.935 110.086  1.00  7.77           O  
ATOM   3428  CB  ASN A 569      -1.650 -25.159 107.620  1.00  5.14           C  
ATOM   3429  CG  ASN A 569      -1.380 -24.881 106.159  1.00  4.53           C  
ATOM   3430  OD1 ASN A 569      -2.214 -24.314 105.453  1.00  6.06           O  
ATOM   3431  ND2 ASN A 569      -0.196 -25.258 105.693  1.00  3.74           N  
ATOM   3432  N   PRO A 570      -3.004 -27.073 109.894  1.00  9.36           N  
ATOM   3433  CA  PRO A 570      -3.124 -27.413 111.319  1.00  9.49           C  
ATOM   3434  C   PRO A 570      -2.102 -26.620 112.137  1.00 10.13           C  
ATOM   3435  O   PRO A 570      -1.122 -26.125 111.595  1.00 10.01           O  
ATOM   3436  CB  PRO A 570      -2.783 -28.900 111.350  1.00 10.05           C  
ATOM   3437  CG  PRO A 570      -3.112 -29.370 109.989  1.00 10.38           C  
ATOM   3438  CD  PRO A 570      -2.662 -28.267 109.100  1.00 10.19           C  
ATOM   3439  N   VAL A 571      -2.329 -26.496 113.437  1.00 11.18           N  
ATOM   3440  CA  VAL A 571      -1.377 -25.802 114.289  1.00 12.14           C  
ATOM   3441  C   VAL A 571      -0.253 -26.813 114.517  1.00 12.52           C  
ATOM   3442  O   VAL A 571      -0.504 -27.959 114.872  1.00 12.50           O  
ATOM   3443  CB  VAL A 571      -2.027 -25.375 115.628  1.00 13.73           C  
ATOM   3444  CG1 VAL A 571      -0.971 -24.958 116.638  1.00 14.42           C  
ATOM   3445  CG2 VAL A 571      -2.966 -24.199 115.374  1.00 14.53           C  
ATOM   3446  N   ALA A 572       0.983 -26.378 114.286  1.00 12.51           N  
ATOM   3447  CA  ALA A 572       2.169 -27.221 114.418  1.00 11.32           C  
ATOM   3448  C   ALA A 572       2.338 -27.996 115.717  1.00 10.69           C  
ATOM   3449  O   ALA A 572       2.965 -29.048 115.725  1.00  9.71           O  
ATOM   3450  CB  ALA A 572       3.418 -26.380 114.177  1.00 10.26           C  
ATOM   3451  N   THR A 573       1.769 -27.499 116.807  1.00 10.81           N  
ATOM   3452  CA  THR A 573       1.964 -28.148 118.094  1.00 11.24           C  
ATOM   3453  C   THR A 573       0.803 -28.960 118.632  1.00 11.97           C  
ATOM   3454  O   THR A 573       0.824 -29.392 119.781  1.00 11.22           O  
ATOM   3455  CB  THR A 573       2.369 -27.093 119.165  1.00 10.97           C  
ATOM   3456  OG1 THR A 573       1.327 -26.121 119.290  1.00 11.65           O  
ATOM   3457  CG2 THR A 573       3.657 -26.375 118.753  1.00 10.46           C  
ATOM   3458  N   GLU A 574      -0.220 -29.161 117.816  1.00 14.94           N  
ATOM   3459  CA  GLU A 574      -1.361 -29.939 118.262  1.00 17.82           C  
ATOM   3460  C   GLU A 574      -1.639 -31.101 117.321  1.00 15.82           C  
ATOM   3461  O   GLU A 574      -1.035 -31.196 116.248  1.00 14.91           O  
ATOM   3462  CB  GLU A 574      -2.575 -29.020 118.418  1.00 22.08           C  
ATOM   3463  CG  GLU A 574      -2.497 -28.199 119.708  1.00 25.63           C  
ATOM   3464  CD  GLU A 574      -3.480 -27.035 119.761  1.00 29.08           C  
ATOM   3465  OE1 GLU A 574      -3.611 -26.427 120.850  1.00 29.85           O  
ATOM   3466  OE2 GLU A 574      -4.114 -26.723 118.722  1.00 29.98           O  
ATOM   3467  N   GLN A 575      -2.522 -32.003 117.738  1.00 14.92           N  
ATOM   3468  CA  GLN A 575      -2.860 -33.151 116.913  1.00 14.43           C  
ATOM   3469  C   GLN A 575      -3.583 -32.717 115.640  1.00 11.07           C  
ATOM   3470  O   GLN A 575      -4.197 -31.659 115.607  1.00 10.18           O  
ATOM   3471  CB  GLN A 575      -3.737 -34.139 117.695  1.00 16.70           C  
ATOM   3472  CG  GLN A 575      -5.172 -33.680 117.976  1.00 19.90           C  
ATOM   3473  CD  GLN A 575      -5.295 -32.779 119.197  1.00 22.94           C  
ATOM   3474  OE1 GLN A 575      -4.465 -32.826 120.111  1.00 24.10           O  
ATOM   3475  NE2 GLN A 575      -6.350 -31.974 119.231  1.00 23.99           N  
ATOM   3476  N   TYR A 576      -3.496 -33.531 114.588  1.00 10.28           N  
ATOM   3477  CA  TYR A 576      -4.172 -33.207 113.333  1.00  8.90           C  
ATOM   3478  C   TYR A 576      -5.663 -33.338 113.596  1.00  8.01           C  
ATOM   3479  O   TYR A 576      -6.474 -32.606 113.047  1.00  7.72           O  
ATOM   3480  CB  TYR A 576      -3.792 -34.185 112.219  1.00  7.87           C  
ATOM   3481  CG  TYR A 576      -4.566 -33.956 110.936  1.00  6.05           C  
ATOM   3482  CD1 TYR A 576      -4.146 -32.997 110.016  1.00  5.89           C  
ATOM   3483  CD2 TYR A 576      -5.759 -34.640 110.682  1.00  4.93           C  
ATOM   3484  CE1 TYR A 576      -4.894 -32.712 108.874  1.00  5.96           C  
ATOM   3485  CE2 TYR A 576      -6.523 -34.358 109.543  1.00  5.63           C  
ATOM   3486  CZ  TYR A 576      -6.082 -33.388 108.643  1.00  5.38           C  
ATOM   3487  OH  TYR A 576      -6.823 -33.081 107.528  1.00  3.81           O  
ATOM   3488  N   GLY A 577      -6.007 -34.297 114.442  1.00  8.56           N  
ATOM   3489  CA  GLY A 577      -7.391 -34.527 114.773  1.00  9.00           C  
ATOM   3490  C   GLY A 577      -7.474 -35.802 115.569  1.00  9.76           C  
ATOM   3491  O   GLY A 577      -6.513 -36.184 116.231  1.00  9.28           O  
ATOM   3492  N   SER A 578      -8.627 -36.458 115.529  1.00 11.87           N  
ATOM   3493  CA  SER A 578      -8.793 -37.710 116.250  1.00 13.69           C  
ATOM   3494  C   SER A 578      -9.429 -38.712 115.312  1.00 13.69           C  
ATOM   3495  O   SER A 578     -10.113 -38.353 114.354  1.00 13.91           O  
ATOM   3496  CB  SER A 578      -9.638 -37.511 117.503  1.00 14.90           C  
ATOM   3497  OG  SER A 578     -10.922 -37.065 117.142  1.00 16.94           O  
ATOM   3498  N   VAL A 579      -9.208 -39.982 115.598  1.00 13.94           N  
ATOM   3499  CA  VAL A 579      -9.691 -41.036 114.732  1.00 13.36           C  
ATOM   3500  C   VAL A 579     -10.193 -42.177 115.601  1.00 14.18           C  
ATOM   3501  O   VAL A 579      -9.770 -42.324 116.748  1.00 13.66           O  
ATOM   3502  CB  VAL A 579      -8.504 -41.461 113.800  1.00 12.72           C  
ATOM   3503  CG1 VAL A 579      -7.827 -42.692 114.319  1.00 12.09           C  
ATOM   3504  CG2 VAL A 579      -8.953 -41.561 112.369  1.00 12.15           C  
ATOM   3505  N   SER A 580     -11.115 -42.969 115.070  1.00 16.09           N  
ATOM   3506  CA  SER A 580     -11.664 -44.097 115.817  1.00 17.37           C  
ATOM   3507  C   SER A 580     -10.618 -45.206 115.971  1.00 19.00           C  
ATOM   3508  O   SER A 580      -9.826 -45.452 115.066  1.00 18.88           O  
ATOM   3509  CB  SER A 580     -12.895 -44.641 115.101  1.00 15.75           C  
ATOM   3510  OG  SER A 580     -13.590 -45.536 115.940  1.00 15.66           O  
ATOM   3511  N   THR A 581     -10.641 -45.895 117.103  1.00 20.82           N  
ATOM   3512  CA  THR A 581      -9.664 -46.940 117.372  1.00 22.56           C  
ATOM   3513  C   THR A 581     -10.216 -48.367 117.489  1.00 23.12           C  
ATOM   3514  O   THR A 581      -9.493 -49.338 117.253  1.00 23.98           O  
ATOM   3515  CB  THR A 581      -8.880 -46.575 118.662  1.00 23.98           C  
ATOM   3516  OG1 THR A 581      -7.909 -45.563 118.355  1.00 23.97           O  
ATOM   3517  CG2 THR A 581      -8.202 -47.798 119.265  1.00 24.93           C  
ATOM   3518  N   ASN A 582     -11.486 -48.503 117.850  1.00 22.31           N  
ATOM   3519  CA  ASN A 582     -12.087 -49.826 118.004  1.00 20.97           C  
ATOM   3520  C   ASN A 582     -13.467 -49.911 117.342  1.00 20.43           C  
ATOM   3521  O   ASN A 582     -13.816 -49.097 116.491  1.00 20.19           O  
ATOM   3522  CB  ASN A 582     -12.209 -50.164 119.499  1.00 20.07           C  
ATOM   3523  CG  ASN A 582     -13.203 -49.260 120.228  1.00 19.90           C  
ATOM   3524  OD1 ASN A 582     -13.653 -48.250 119.684  1.00 20.16           O  
ATOM   3525  ND2 ASN A 582     -13.538 -49.616 121.467  1.00 19.36           N  
ATOM   3526  N   LEU A 583     -14.235 -50.918 117.746  1.00 20.58           N  
ATOM   3527  CA  LEU A 583     -15.588 -51.138 117.250  1.00 20.00           C  
ATOM   3528  C   LEU A 583     -16.472 -51.206 118.476  1.00 19.20           C  
ATOM   3529  O   LEU A 583     -16.394 -52.169 119.241  1.00 20.16           O  
ATOM   3530  CB  LEU A 583     -15.681 -52.465 116.489  1.00 19.82           C  
ATOM   3531  CG  LEU A 583     -14.872 -52.592 115.197  1.00 19.92           C  
ATOM   3532  CD1 LEU A 583     -14.864 -54.034 114.739  1.00 20.19           C  
ATOM   3533  CD2 LEU A 583     -15.455 -51.689 114.132  1.00 19.84           C  
ATOM   3534  N   GLN A 584     -17.307 -50.193 118.681  1.00 18.75           N  
ATOM   3535  CA  GLN A 584     -18.183 -50.191 119.844  1.00 19.42           C  
ATOM   3536  C   GLN A 584     -19.342 -51.177 119.711  1.00 22.15           C  
ATOM   3537  O   GLN A 584     -19.727 -51.566 118.609  1.00 22.36           O  
ATOM   3538  CB  GLN A 584     -18.718 -48.774 120.119  1.00 17.34           C  
ATOM   3539  CG  GLN A 584     -19.591 -48.123 119.037  1.00 15.43           C  
ATOM   3540  CD  GLN A 584     -21.040 -48.593 119.046  1.00 13.96           C  
ATOM   3541  OE1 GLN A 584     -21.617 -48.852 120.102  1.00 14.31           O  
ATOM   3542  NE2 GLN A 584     -21.639 -48.682 117.868  1.00 13.43           N  
ATOM   3543  N   ARG A 585     -19.881 -51.587 120.850  1.00 24.96           N  
ATOM   3544  CA  ARG A 585     -21.010 -52.509 120.887  1.00 27.87           C  
ATOM   3545  C   ARG A 585     -21.586 -52.470 122.301  1.00 28.01           C  
ATOM   3546  O   ARG A 585     -21.108 -51.717 123.147  1.00 27.62           O  
ATOM   3547  CB  ARG A 585     -20.557 -53.931 120.521  1.00 29.89           C  
ATOM   3548  CG  ARG A 585     -19.602 -54.548 121.521  1.00 31.55           C  
ATOM   3549  CD  ARG A 585     -19.077 -55.907 121.069  1.00 33.47           C  
ATOM   3550  NE  ARG A 585     -18.255 -56.487 122.127  1.00 36.01           N  
ATOM   3551  CZ  ARG A 585     -17.490 -57.567 122.003  1.00 37.74           C  
ATOM   3552  NH1 ARG A 585     -17.423 -58.220 120.849  1.00 38.20           N  
ATOM   3553  NH2 ARG A 585     -16.783 -57.990 123.046  1.00 38.33           N  
ATOM   3554  N   GLY A 586     -22.605 -53.280 122.553  1.00 28.87           N  
ATOM   3555  CA  GLY A 586     -23.230 -53.297 123.862  1.00 30.15           C  
ATOM   3556  C   GLY A 586     -22.327 -53.205 125.081  1.00 31.79           C  
ATOM   3557  O   GLY A 586     -22.579 -52.394 125.972  1.00 32.13           O  
ATOM   3558  N   ASN A 587     -21.275 -54.019 125.129  1.00 33.36           N  
ATOM   3559  CA  ASN A 587     -20.371 -54.030 126.280  1.00 34.90           C  
ATOM   3560  C   ASN A 587     -18.984 -53.440 126.030  1.00 34.62           C  
ATOM   3561  O   ASN A 587     -18.032 -53.747 126.748  1.00 34.95           O  
ATOM   3562  CB  ASN A 587     -20.227 -55.465 126.796  1.00 36.68           C  
ATOM   3563  CG  ASN A 587     -19.518 -56.373 125.800  1.00 38.22           C  
ATOM   3564  OD1 ASN A 587     -19.528 -56.120 124.594  1.00 38.71           O  
ATOM   3565  ND2 ASN A 587     -18.908 -57.444 126.303  1.00 38.45           N  
ATOM   3566  N   ARG A 588     -18.871 -52.594 125.015  1.00 34.38           N  
ATOM   3567  CA  ARG A 588     -17.602 -51.958 124.686  1.00 33.81           C  
ATOM   3568  C   ARG A 588     -17.869 -50.532 124.203  1.00 31.60           C  
ATOM   3569  O   ARG A 588     -18.601 -50.324 123.239  1.00 31.33           O  
ATOM   3570  CB  ARG A 588     -16.882 -52.761 123.598  1.00 35.63           C  
ATOM   3571  CG  ARG A 588     -15.489 -52.241 123.249  1.00 37.74           C  
ATOM   3572  CD  ARG A 588     -14.959 -52.896 121.975  1.00 39.74           C  
ATOM   3573  NE  ARG A 588     -14.875 -54.352 122.092  1.00 41.55           N  
ATOM   3574  CZ  ARG A 588     -14.632 -55.172 121.070  1.00 42.82           C  
ATOM   3575  NH1 ARG A 588     -14.449 -54.682 119.851  1.00 43.33           N  
ATOM   3576  NH2 ARG A 588     -14.577 -56.485 121.263  1.00 43.07           N  
ATOM   3577  N   GLN A 589     -17.274 -49.556 124.883  1.00 30.37           N  
ATOM   3578  CA  GLN A 589     -17.439 -48.142 124.542  1.00 29.20           C  
ATOM   3579  C   GLN A 589     -16.526 -47.675 123.418  1.00 27.71           C  
ATOM   3580  O   GLN A 589     -15.415 -48.175 123.260  1.00 28.31           O  
ATOM   3581  CB  GLN A 589     -17.169 -47.274 125.764  1.00 30.29           C  
ATOM   3582  CG  GLN A 589     -18.180 -47.412 126.872  1.00 32.14           C  
ATOM   3583  CD  GLN A 589     -18.044 -46.301 127.888  1.00 33.99           C  
ATOM   3584  OE1 GLN A 589     -17.932 -45.128 127.522  1.00 34.66           O  
ATOM   3585  NE2 GLN A 589     -18.061 -46.656 129.168  1.00 34.43           N  
ATOM   3586  N   ALA A 590     -16.999 -46.700 122.651  1.00 26.25           N  
ATOM   3587  CA  ALA A 590     -16.230 -46.145 121.543  1.00 25.06           C  
ATOM   3588  C   ALA A 590     -14.934 -45.530 122.066  1.00 25.13           C  
ATOM   3589  O   ALA A 590     -14.943 -44.771 123.035  1.00 25.49           O  
ATOM   3590  CB  ALA A 590     -17.061 -45.087 120.801  1.00 23.68           C  
ATOM   3591  N   ALA A 591     -13.820 -45.877 121.427  1.00 25.16           N  
ATOM   3592  CA  ALA A 591     -12.508 -45.369 121.813  1.00 24.83           C  
ATOM   3593  C   ALA A 591     -11.905 -44.622 120.636  1.00 24.45           C  
ATOM   3594  O   ALA A 591     -12.115 -44.984 119.479  1.00 24.56           O  
ATOM   3595  CB  ALA A 591     -11.597 -46.514 122.239  1.00 24.64           C  
ATOM   3596  N   THR A 592     -11.153 -43.574 120.936  1.00 24.61           N  
ATOM   3597  CA  THR A 592     -10.552 -42.761 119.895  1.00 24.74           C  
ATOM   3598  C   THR A 592      -9.087 -42.433 120.209  1.00 23.69           C  
ATOM   3599  O   THR A 592      -8.631 -42.606 121.343  1.00 24.12           O  
ATOM   3600  CB  THR A 592     -11.399 -41.463 119.703  1.00 26.30           C  
ATOM   3601  OG1 THR A 592     -10.798 -40.628 118.705  1.00 27.40           O  
ATOM   3602  CG2 THR A 592     -11.514 -40.692 121.018  1.00 26.86           C  
ATOM   3603  N   ALA A 593      -8.347 -41.980 119.201  1.00 22.38           N  
ATOM   3604  CA  ALA A 593      -6.943 -41.633 119.394  1.00 21.72           C  
ATOM   3605  C   ALA A 593      -6.559 -40.354 118.655  1.00 21.98           C  
ATOM   3606  O   ALA A 593      -7.147 -40.017 117.624  1.00 21.48           O  
ATOM   3607  CB  ALA A 593      -6.045 -42.781 118.929  1.00 20.74           C  
ATOM   3608  N   ASP A 594      -5.570 -39.645 119.194  1.00 22.36           N  
ATOM   3609  CA  ASP A 594      -5.075 -38.424 118.570  1.00 23.10           C  
ATOM   3610  C   ASP A 594      -4.149 -38.810 117.432  1.00 20.58           C  
ATOM   3611  O   ASP A 594      -3.397 -39.780 117.542  1.00 20.82           O  
ATOM   3612  CB  ASP A 594      -4.275 -37.575 119.567  1.00 26.51           C  
ATOM   3613  CG  ASP A 594      -5.150 -36.905 120.611  1.00 30.32           C  
ATOM   3614  OD1 ASP A 594      -5.479 -37.559 121.631  1.00 31.63           O  
ATOM   3615  OD2 ASP A 594      -5.516 -35.721 120.406  1.00 31.13           O  
ATOM   3616  N   VAL A 595      -4.202 -38.079 116.327  1.00 18.45           N  
ATOM   3617  CA  VAL A 595      -3.290 -38.396 115.253  1.00 17.47           C  
ATOM   3618  C   VAL A 595      -2.256 -37.270 115.190  1.00 15.97           C  
ATOM   3619  O   VAL A 595      -2.575 -36.119 114.888  1.00 16.12           O  
ATOM   3620  CB  VAL A 595      -4.030 -38.654 113.877  1.00 17.83           C  
ATOM   3621  CG1 VAL A 595      -5.532 -38.736 114.088  1.00 17.72           C  
ATOM   3622  CG2 VAL A 595      -3.650 -37.628 112.839  1.00 17.78           C  
ATOM   3623  N   ASN A 596      -1.016 -37.623 115.526  1.00 13.91           N  
ATOM   3624  CA  ASN A 596       0.093 -36.683 115.556  1.00 12.55           C  
ATOM   3625  C   ASN A 596       0.883 -36.626 114.260  1.00 12.66           C  
ATOM   3626  O   ASN A 596       1.832 -35.863 114.135  1.00 12.16           O  
ATOM   3627  CB  ASN A 596       1.023 -37.019 116.721  1.00 11.30           C  
ATOM   3628  CG  ASN A 596       0.292 -37.059 118.037  1.00 10.96           C  
ATOM   3629  OD1 ASN A 596      -0.518 -36.182 118.326  1.00 11.72           O  
ATOM   3630  ND2 ASN A 596       0.568 -38.073 118.847  1.00 10.19           N  
ATOM   3631  N   THR A 597       0.477 -37.430 113.289  1.00 13.62           N  
ATOM   3632  CA  THR A 597       1.141 -37.456 111.995  1.00 14.89           C  
ATOM   3633  C   THR A 597       0.040 -37.723 110.981  1.00 13.68           C  
ATOM   3634  O   THR A 597      -0.753 -38.641 111.163  1.00 15.76           O  
ATOM   3635  CB  THR A 597       2.169 -38.622 111.882  1.00 17.04           C  
ATOM   3636  OG1 THR A 597       3.016 -38.660 113.034  1.00 17.48           O  
ATOM   3637  CG2 THR A 597       3.016 -38.440 110.656  1.00 17.36           C  
ATOM   3638  N   GLN A 598      -0.005 -36.946 109.914  1.00 10.71           N  
ATOM   3639  CA  GLN A 598      -1.032 -37.137 108.918  1.00  8.19           C  
ATOM   3640  C   GLN A 598      -0.533 -36.878 107.508  1.00  7.32           C  
ATOM   3641  O   GLN A 598      -0.243 -35.744 107.143  1.00  8.05           O  
ATOM   3642  CB  GLN A 598      -2.243 -36.230 109.203  1.00  7.82           C  
ATOM   3643  CG  GLN A 598      -3.450 -36.504 108.288  1.00  7.50           C  
ATOM   3644  CD  GLN A 598      -3.807 -37.971 108.269  1.00  8.26           C  
ATOM   3645  OE1 GLN A 598      -4.151 -38.531 109.298  1.00  8.04           O  
ATOM   3646  NE2 GLN A 598      -3.697 -38.611 107.104  1.00  9.65           N  
ATOM   3647  N   GLY A 599      -0.432 -37.940 106.720  1.00  6.65           N  
ATOM   3648  CA  GLY A 599       0.007 -37.800 105.351  1.00  6.65           C  
ATOM   3649  C   GLY A 599      -1.153 -37.255 104.552  1.00  7.49           C  
ATOM   3650  O   GLY A 599      -2.291 -37.263 105.007  1.00  8.76           O  
ATOM   3651  N   VAL A 600      -0.874 -36.797 103.349  1.00  7.41           N  
ATOM   3652  CA  VAL A 600      -1.901 -36.229 102.514  1.00  9.24           C  
ATOM   3653  C   VAL A 600      -3.084 -37.165 102.211  1.00  9.03           C  
ATOM   3654  O   VAL A 600      -2.908 -38.349 101.940  1.00  9.95           O  
ATOM   3655  CB  VAL A 600      -1.272 -35.716 101.200  1.00 10.32           C  
ATOM   3656  CG1 VAL A 600      -2.333 -35.362 100.221  1.00 11.61           C  
ATOM   3657  CG2 VAL A 600      -0.451 -34.457 101.483  1.00 11.10           C  
ATOM   3658  N   LEU A 601      -4.293 -36.618 102.276  1.00  7.54           N  
ATOM   3659  CA  LEU A 601      -5.503 -37.370 101.982  1.00  6.57           C  
ATOM   3660  C   LEU A 601      -6.215 -36.651 100.866  1.00  6.10           C  
ATOM   3661  O   LEU A 601      -6.033 -35.453 100.678  1.00  5.87           O  
ATOM   3662  CB  LEU A 601      -6.425 -37.441 103.196  1.00  6.19           C  
ATOM   3663  CG  LEU A 601      -5.931 -38.234 104.404  1.00  6.73           C  
ATOM   3664  CD1 LEU A 601      -6.830 -37.978 105.612  1.00  7.72           C  
ATOM   3665  CD2 LEU A 601      -5.904 -39.708 104.056  1.00  7.04           C  
ATOM   3666  N   PRO A 602      -6.999 -37.384 100.064  1.00  7.17           N  
ATOM   3667  CA  PRO A 602      -7.723 -36.720  98.978  1.00  5.88           C  
ATOM   3668  C   PRO A 602      -8.662 -35.676  99.626  1.00  4.87           C  
ATOM   3669  O   PRO A 602      -9.258 -35.933 100.671  1.00  3.48           O  
ATOM   3670  CB  PRO A 602      -8.461 -37.878  98.321  1.00  7.06           C  
ATOM   3671  CG  PRO A 602      -7.487 -39.023  98.507  1.00  7.81           C  
ATOM   3672  CD  PRO A 602      -7.075 -38.854  99.939  1.00  7.36           C  
ATOM   3673  N   GLY A 603      -8.760 -34.492  99.030  1.00  4.94           N  
ATOM   3674  CA  GLY A 603      -9.603 -33.460  99.603  1.00  5.31           C  
ATOM   3675  C   GLY A 603      -8.873 -32.526 100.566  1.00  6.44           C  
ATOM   3676  O   GLY A 603      -9.492 -31.654 101.165  1.00  7.60           O  
ATOM   3677  N   MET A 604      -7.572 -32.715 100.750  1.00  6.03           N  
ATOM   3678  CA  MET A 604      -6.805 -31.839 101.629  1.00  5.86           C  
ATOM   3679  C   MET A 604      -6.348 -30.598 100.882  1.00  4.74           C  
ATOM   3680  O   MET A 604      -6.005 -30.675  99.707  1.00  4.78           O  
ATOM   3681  CB  MET A 604      -5.572 -32.545 102.144  1.00  6.51           C  
ATOM   3682  CG  MET A 604      -5.736 -33.195 103.481  1.00  7.74           C  
ATOM   3683  SD  MET A 604      -4.069 -33.705 104.059  1.00  7.10           S  
ATOM   3684  CE  MET A 604      -4.460 -34.485 105.579  1.00  6.05           C  
ATOM   3685  N   VAL A 605      -6.355 -29.455 101.560  1.00  4.12           N  
ATOM   3686  CA  VAL A 605      -5.891 -28.206 100.963  1.00  3.49           C  
ATOM   3687  C   VAL A 605      -4.915 -27.566 101.951  1.00  2.77           C  
ATOM   3688  O   VAL A 605      -4.966 -27.829 103.147  1.00  2.61           O  
ATOM   3689  CB  VAL A 605      -7.071 -27.215 100.668  1.00  4.25           C  
ATOM   3690  CG1 VAL A 605      -8.011 -27.820  99.618  1.00  4.33           C  
ATOM   3691  CG2 VAL A 605      -7.813 -26.847 101.967  1.00  2.34           C  
ATOM   3692  N   TRP A 606      -4.004 -26.745 101.461  1.00  3.73           N  
ATOM   3693  CA  TRP A 606      -3.072 -26.105 102.367  1.00  4.40           C  
ATOM   3694  C   TRP A 606      -2.351 -24.957 101.714  1.00  2.91           C  
ATOM   3695  O   TRP A 606      -2.362 -24.786 100.497  1.00  1.57           O  
ATOM   3696  CB  TRP A 606      -2.042 -27.131 102.922  1.00  5.23           C  
ATOM   3697  CG  TRP A 606      -1.097 -27.708 101.873  1.00  6.39           C  
ATOM   3698  CD1 TRP A 606       0.093 -27.170 101.452  1.00  6.82           C  
ATOM   3699  CD2 TRP A 606      -1.340 -28.852 101.020  1.00  6.57           C  
ATOM   3700  NE1 TRP A 606       0.591 -27.893 100.388  1.00  6.86           N  
ATOM   3701  CE2 TRP A 606      -0.261 -28.927 100.104  1.00  7.27           C  
ATOM   3702  CE3 TRP A 606      -2.370 -29.810 100.941  1.00  6.17           C  
ATOM   3703  CZ2 TRP A 606      -0.176 -29.935  99.109  1.00  7.82           C  
ATOM   3704  CZ3 TRP A 606      -2.291 -30.800  99.960  1.00  7.40           C  
ATOM   3705  CH2 TRP A 606      -1.195 -30.854  99.052  1.00  7.57           C  
ATOM   3706  N   GLN A 607      -1.725 -24.162 102.566  1.00  5.00           N  
ATOM   3707  CA  GLN A 607      -0.913 -23.044 102.131  1.00  7.15           C  
ATOM   3708  C   GLN A 607       0.537 -23.388 102.437  1.00  5.36           C  
ATOM   3709  O   GLN A 607       0.825 -23.978 103.477  1.00  5.45           O  
ATOM   3710  CB  GLN A 607      -1.280 -21.788 102.905  1.00 10.16           C  
ATOM   3711  CG  GLN A 607      -2.532 -21.118 102.445  1.00 12.80           C  
ATOM   3712  CD  GLN A 607      -2.293 -20.215 101.252  1.00 15.04           C  
ATOM   3713  OE1 GLN A 607      -2.557 -20.591 100.101  1.00 14.18           O  
ATOM   3714  NE2 GLN A 607      -1.784 -18.996 101.525  1.00 16.12           N  
ATOM   3715  N   ASP A 608       1.449 -23.010 101.548  1.00  5.49           N  
ATOM   3716  CA  ASP A 608       2.873 -23.264 101.800  1.00  5.66           C  
ATOM   3717  C   ASP A 608       3.433 -22.207 102.764  1.00  5.96           C  
ATOM   3718  O   ASP A 608       2.769 -21.220 103.069  1.00  6.24           O  
ATOM   3719  CB  ASP A 608       3.663 -23.256 100.498  1.00  4.89           C  
ATOM   3720  CG  ASP A 608       3.248 -24.382  99.550  1.00  6.21           C  
ATOM   3721  OD1 ASP A 608       3.073 -25.537 100.007  1.00  6.57           O  
ATOM   3722  OD2 ASP A 608       3.117 -24.111  98.330  1.00  7.45           O  
ATOM   3723  N   ARG A 609       4.647 -22.420 103.253  1.00  6.74           N  
ATOM   3724  CA  ARG A 609       5.261 -21.482 104.184  1.00  7.26           C  
ATOM   3725  C   ARG A 609       5.522 -20.131 103.521  1.00  6.07           C  
ATOM   3726  O   ARG A 609       5.719 -20.043 102.307  1.00  5.91           O  
ATOM   3727  CB  ARG A 609       6.554 -22.084 104.733  1.00  7.85           C  
ATOM   3728  CG  ARG A 609       7.255 -21.267 105.785  1.00  7.73           C  
ATOM   3729  CD  ARG A 609       8.384 -22.028 106.432  1.00  8.20           C  
ATOM   3730  NE  ARG A 609       8.017 -22.492 107.769  1.00 10.01           N  
ATOM   3731  CZ  ARG A 609       7.631 -23.728 108.041  1.00 12.17           C  
ATOM   3732  NH1 ARG A 609       7.565 -24.626 107.074  1.00 13.45           N  
ATOM   3733  NH2 ARG A 609       7.302 -24.068 109.272  1.00 13.77           N  
ATOM   3734  N   ASP A 610       5.498 -19.079 104.326  1.00  5.69           N  
ATOM   3735  CA  ASP A 610       5.712 -17.722 103.841  1.00  6.51           C  
ATOM   3736  C   ASP A 610       7.188 -17.465 103.576  1.00  8.13           C  
ATOM   3737  O   ASP A 610       8.057 -18.145 104.130  1.00  8.15           O  
ATOM   3738  CB  ASP A 610       5.210 -16.750 104.906  1.00  6.23           C  
ATOM   3739  CG  ASP A 610       4.862 -15.365 104.359  1.00  6.61           C  
ATOM   3740  OD1 ASP A 610       4.723 -15.153 103.127  1.00  4.82           O  
ATOM   3741  OD2 ASP A 610       4.705 -14.467 105.213  1.00  8.65           O  
ATOM   3742  N   VAL A 611       7.468 -16.490 102.718  1.00  9.45           N  
ATOM   3743  CA  VAL A 611       8.836 -16.105 102.449  1.00  9.87           C  
ATOM   3744  C   VAL A 611       9.076 -14.794 103.193  1.00 13.15           C  
ATOM   3745  O   VAL A 611       8.146 -14.040 103.445  1.00 17.17           O  
ATOM   3746  CB  VAL A 611       9.122 -15.918 100.932  1.00  7.27           C  
ATOM   3747  CG1 VAL A 611       9.014 -17.256 100.209  1.00  5.82           C  
ATOM   3748  CG2 VAL A 611       8.186 -14.878 100.322  1.00  6.57           C  
ATOM   3749  N   TYR A 612      10.322 -14.530 103.565  1.00 11.43           N  
ATOM   3750  CA  TYR A 612      10.652 -13.313 104.291  1.00  9.61           C  
ATOM   3751  C   TYR A 612      11.653 -12.476 103.554  1.00  9.86           C  
ATOM   3752  O   TYR A 612      12.265 -12.934 102.602  1.00 10.23           O  
ATOM   3753  CB  TYR A 612      11.169 -13.650 105.675  1.00  9.11           C  
ATOM   3754  CG  TYR A 612      10.140 -14.378 106.478  1.00 10.67           C  
ATOM   3755  CD1 TYR A 612       9.854 -15.728 106.223  1.00 11.03           C  
ATOM   3756  CD2 TYR A 612       9.375 -13.705 107.430  1.00 10.30           C  
ATOM   3757  CE1 TYR A 612       8.824 -16.378 106.891  1.00 11.94           C  
ATOM   3758  CE2 TYR A 612       8.352 -14.340 108.096  1.00 11.51           C  
ATOM   3759  CZ  TYR A 612       8.075 -15.672 107.825  1.00 11.91           C  
ATOM   3760  OH  TYR A 612       7.044 -16.264 108.496  1.00 12.15           O  
ATOM   3761  N   LEU A 613      11.805 -11.232 103.990  1.00  9.87           N  
ATOM   3762  CA  LEU A 613      12.731 -10.329 103.348  1.00  8.84           C  
ATOM   3763  C   LEU A 613      14.143 -10.885 103.549  1.00  6.64           C  
ATOM   3764  O   LEU A 613      14.979 -10.827 102.647  1.00  5.63           O  
ATOM   3765  CB  LEU A 613      12.588  -8.922 103.954  1.00  8.38           C  
ATOM   3766  CG  LEU A 613      13.618  -7.885 103.501  1.00  7.81           C  
ATOM   3767  CD1 LEU A 613      13.527  -7.713 102.015  1.00  6.32           C  
ATOM   3768  CD2 LEU A 613      13.381  -6.561 104.226  1.00  9.58           C  
ATOM   3769  N   GLN A 614      14.405 -11.436 104.728  1.00  7.12           N  
ATOM   3770  CA  GLN A 614      15.714 -12.011 104.996  1.00  8.21           C  
ATOM   3771  C   GLN A 614      15.767 -13.532 104.820  1.00  9.09           C  
ATOM   3772  O   GLN A 614      16.682 -14.188 105.314  1.00  9.02           O  
ATOM   3773  CB  GLN A 614      16.199 -11.627 106.397  1.00  8.94           C  
ATOM   3774  CG  GLN A 614      15.216 -11.826 107.542  1.00 10.27           C  
ATOM   3775  CD  GLN A 614      14.176 -10.707 107.652  1.00 11.54           C  
ATOM   3776  OE1 GLN A 614      13.184 -10.689 106.926  1.00 11.28           O  
ATOM   3777  NE2 GLN A 614      14.407  -9.771 108.569  1.00 12.75           N  
ATOM   3778  N   GLY A 615      14.805 -14.086 104.086  1.00  8.46           N  
ATOM   3779  CA  GLY A 615      14.780 -15.518 103.887  1.00  6.59           C  
ATOM   3780  C   GLY A 615      15.176 -15.938 102.489  1.00  4.78           C  
ATOM   3781  O   GLY A 615      15.402 -15.105 101.622  1.00  2.75           O  
ATOM   3782  N   PRO A 616      15.223 -17.254 102.241  1.00  5.77           N  
ATOM   3783  CA  PRO A 616      15.584 -17.889 100.969  1.00  5.14           C  
ATOM   3784  C   PRO A 616      14.644 -17.603  99.830  1.00  4.71           C  
ATOM   3785  O   PRO A 616      13.430 -17.505 100.022  1.00  6.05           O  
ATOM   3786  CB  PRO A 616      15.531 -19.377 101.283  1.00  5.15           C  
ATOM   3787  CG  PRO A 616      15.552 -19.457 102.754  1.00  6.31           C  
ATOM   3788  CD  PRO A 616      14.829 -18.267 103.235  1.00  6.27           C  
ATOM   3789  N   ILE A 617      15.177 -17.522  98.627  1.00  3.71           N  
ATOM   3790  CA  ILE A 617      14.305 -17.317  97.495  1.00  4.91           C  
ATOM   3791  C   ILE A 617      13.927 -18.653  96.846  1.00  7.21           C  
ATOM   3792  O   ILE A 617      12.751 -18.959  96.680  1.00  8.74           O  
ATOM   3793  CB  ILE A 617      14.961 -16.445  96.418  1.00  3.11           C  
ATOM   3794  CG1 ILE A 617      15.333 -15.082  97.000  1.00  0.30           C  
ATOM   3795  CG2 ILE A 617      14.042 -16.351  95.198  1.00  1.72           C  
ATOM   3796  CD1 ILE A 617      16.077 -14.226  95.992  1.00  0.08           C  
ATOM   3797  N   TRP A 618      14.924 -19.459  96.494  1.00  6.96           N  
ATOM   3798  CA  TRP A 618      14.660 -20.716  95.814  1.00  6.00           C  
ATOM   3799  C   TRP A 618      15.474 -21.886  96.357  1.00  4.37           C  
ATOM   3800  O   TRP A 618      16.304 -21.732  97.248  1.00  4.47           O  
ATOM   3801  CB  TRP A 618      14.936 -20.539  94.316  1.00  6.76           C  
ATOM   3802  CG  TRP A 618      16.407 -20.468  94.004  1.00  8.59           C  
ATOM   3803  CD1 TRP A 618      17.308 -21.515  94.022  1.00  8.51           C  
ATOM   3804  CD2 TRP A 618      17.186 -19.279  93.803  1.00  7.74           C  
ATOM   3805  NE1 TRP A 618      18.579 -21.042  93.867  1.00  8.69           N  
ATOM   3806  CE2 TRP A 618      18.542 -19.680  93.730  1.00  8.29           C  
ATOM   3807  CE3 TRP A 618      16.869 -17.916  93.686  1.00  7.65           C  
ATOM   3808  CZ2 TRP A 618      19.593 -18.761  93.548  1.00  8.27           C  
ATOM   3809  CZ3 TRP A 618      17.910 -16.996  93.504  1.00  7.67           C  
ATOM   3810  CH2 TRP A 618      19.260 -17.429  93.439  1.00  8.20           C  
ATOM   3811  N   ALA A 619      15.197 -23.071  95.835  1.00  4.31           N  
ATOM   3812  CA  ALA A 619      15.934 -24.280  96.200  1.00  4.39           C  
ATOM   3813  C   ALA A 619      15.853 -25.159  94.984  1.00  5.00           C  
ATOM   3814  O   ALA A 619      14.929 -25.024  94.185  1.00  5.14           O  
ATOM   3815  CB  ALA A 619      15.316 -24.982  97.396  1.00  3.55           C  
ATOM   3816  N   LYS A 620      16.848 -26.019  94.804  1.00  5.93           N  
ATOM   3817  CA  LYS A 620      16.842 -26.941  93.680  1.00  6.22           C  
ATOM   3818  C   LYS A 620      16.056 -28.166  94.139  1.00  3.52           C  
ATOM   3819  O   LYS A 620      16.311 -28.707  95.221  1.00  1.76           O  
ATOM   3820  CB  LYS A 620      18.273 -27.351  93.305  1.00  8.58           C  
ATOM   3821  CG  LYS A 620      18.377 -28.492  92.291  1.00 10.64           C  
ATOM   3822  CD  LYS A 620      19.818 -28.641  91.815  1.00 14.02           C  
ATOM   3823  CE  LYS A 620      20.072 -29.928  91.061  1.00 16.80           C  
ATOM   3824  NZ  LYS A 620      19.302 -30.011  89.788  1.00 18.45           N  
ATOM   3825  N   ILE A 621      15.079 -28.574  93.337  1.00  3.49           N  
ATOM   3826  CA  ILE A 621      14.292 -29.761  93.657  1.00  4.06           C  
ATOM   3827  C   ILE A 621      15.217 -30.963  93.449  1.00  4.65           C  
ATOM   3828  O   ILE A 621      15.841 -31.089  92.394  1.00  5.14           O  
ATOM   3829  CB  ILE A 621      13.051 -29.883  92.708  1.00  2.52           C  
ATOM   3830  CG1 ILE A 621      12.054 -28.756  93.016  1.00  0.00           C  
ATOM   3831  CG2 ILE A 621      12.377 -31.266  92.868  1.00  1.82           C  
ATOM   3832  CD1 ILE A 621      11.078 -28.496  91.920  1.00  0.00           C  
ATOM   3833  N   PRO A 622      15.342 -31.843  94.456  1.00  4.79           N  
ATOM   3834  CA  PRO A 622      16.208 -33.015  94.304  1.00  7.81           C  
ATOM   3835  C   PRO A 622      15.848 -33.805  93.061  1.00  8.95           C  
ATOM   3836  O   PRO A 622      14.679 -33.927  92.700  1.00  9.62           O  
ATOM   3837  CB  PRO A 622      15.952 -33.810  95.581  1.00  8.12           C  
ATOM   3838  CG  PRO A 622      15.664 -32.724  96.577  1.00  6.06           C  
ATOM   3839  CD  PRO A 622      14.747 -31.810  95.795  1.00  4.28           C  
ATOM   3840  N   HIS A 623      16.868 -34.331  92.406  1.00 11.05           N  
ATOM   3841  CA  HIS A 623      16.702 -35.116  91.194  1.00 12.92           C  
ATOM   3842  C   HIS A 623      16.299 -36.538  91.619  1.00 13.68           C  
ATOM   3843  O   HIS A 623      17.159 -37.390  91.854  1.00 16.50           O  
ATOM   3844  CB  HIS A 623      18.039 -35.099  90.460  1.00 15.02           C  
ATOM   3845  CG  HIS A 623      18.094 -36.001  89.277  1.00 16.44           C  
ATOM   3846  ND1 HIS A 623      17.662 -35.613  88.027  1.00 17.13           N  
ATOM   3847  CD2 HIS A 623      18.481 -37.293  89.165  1.00 17.31           C  
ATOM   3848  CE1 HIS A 623      17.775 -36.630  87.191  1.00 17.66           C  
ATOM   3849  NE2 HIS A 623      18.269 -37.661  87.856  1.00 18.19           N  
ATOM   3850  N   THR A 624      14.998 -36.788  91.726  1.00 11.76           N  
ATOM   3851  CA  THR A 624      14.478 -38.087  92.169  1.00  9.77           C  
ATOM   3852  C   THR A 624      13.327 -38.553  91.296  1.00  8.00           C  
ATOM   3853  O   THR A 624      12.825 -37.794  90.480  1.00  8.62           O  
ATOM   3854  CB  THR A 624      13.973 -38.020  93.636  1.00  8.41           C  
ATOM   3855  OG1 THR A 624      13.082 -36.912  93.786  1.00  8.31           O  
ATOM   3856  CG2 THR A 624      15.100 -37.847  94.592  1.00  8.82           C  
ATOM   3857  N   ASP A 625      12.910 -39.804  91.464  1.00  8.67           N  
ATOM   3858  CA  ASP A 625      11.805 -40.345  90.668  1.00  9.33           C  
ATOM   3859  C   ASP A 625      10.495 -39.681  91.064  1.00  8.48           C  
ATOM   3860  O   ASP A 625       9.686 -39.359  90.207  1.00  8.99           O  
ATOM   3861  CB  ASP A 625      11.655 -41.861  90.854  1.00 10.07           C  
ATOM   3862  CG  ASP A 625      12.812 -42.644  90.272  1.00 11.38           C  
ATOM   3863  OD1 ASP A 625      13.327 -42.248  89.198  1.00 13.06           O  
ATOM   3864  OD2 ASP A 625      13.195 -43.675  90.874  1.00 11.14           O  
ATOM   3865  N   GLY A 626      10.298 -39.482  92.365  1.00  7.67           N  
ATOM   3866  CA  GLY A 626       9.085 -38.846  92.836  1.00  8.26           C  
ATOM   3867  C   GLY A 626       9.320 -37.783  93.895  1.00  9.73           C  
ATOM   3868  O   GLY A 626      10.144 -37.951  94.795  1.00  9.32           O  
ATOM   3869  N   HIS A 627       8.598 -36.674  93.784  1.00 11.87           N  
ATOM   3870  CA  HIS A 627       8.694 -35.577  94.749  1.00 13.33           C  
ATOM   3871  C   HIS A 627       7.355 -34.900  94.837  1.00 13.77           C  
ATOM   3872  O   HIS A 627       6.988 -34.135  93.943  1.00 15.37           O  
ATOM   3873  CB  HIS A 627       9.747 -34.543  94.335  1.00 14.97           C  
ATOM   3874  CG  HIS A 627       9.820 -34.308  92.863  1.00 17.04           C  
ATOM   3875  ND1 HIS A 627      10.914 -34.676  92.109  1.00 17.78           N  
ATOM   3876  CD2 HIS A 627       8.927 -33.772  91.997  1.00 18.44           C  
ATOM   3877  CE1 HIS A 627      10.691 -34.378  90.842  1.00 18.69           C  
ATOM   3878  NE2 HIS A 627       9.492 -33.828  90.747  1.00 19.00           N  
ATOM   3879  N   PHE A 628       6.626 -35.169  95.914  1.00 12.27           N  
ATOM   3880  CA  PHE A 628       5.307 -34.580  96.098  1.00 11.07           C  
ATOM   3881  C   PHE A 628       5.303 -33.105  96.479  1.00 10.06           C  
ATOM   3882  O   PHE A 628       5.893 -32.724  97.487  1.00 10.64           O  
ATOM   3883  CB  PHE A 628       4.531 -35.353  97.155  1.00 10.65           C  
ATOM   3884  CG  PHE A 628       3.138 -34.854  97.354  1.00 10.24           C  
ATOM   3885  CD1 PHE A 628       2.221 -34.891  96.305  1.00 10.07           C  
ATOM   3886  CD2 PHE A 628       2.749 -34.303  98.577  1.00 10.05           C  
ATOM   3887  CE1 PHE A 628       0.939 -34.388  96.465  1.00 10.44           C  
ATOM   3888  CE2 PHE A 628       1.464 -33.792  98.752  1.00  9.81           C  
ATOM   3889  CZ  PHE A 628       0.559 -33.832  97.701  1.00 10.44           C  
ATOM   3890  N   HIS A 629       4.612 -32.288  95.685  1.00  9.82           N  
ATOM   3891  CA  HIS A 629       4.499 -30.850  95.934  1.00 10.44           C  
ATOM   3892  C   HIS A 629       5.864 -30.284  96.345  1.00 10.11           C  
ATOM   3893  O   HIS A 629       6.096 -29.947  97.512  1.00 10.07           O  
ATOM   3894  CB  HIS A 629       3.449 -30.592  97.033  1.00 11.55           C  
ATOM   3895  CG  HIS A 629       2.944 -29.176  97.068  1.00 12.64           C  
ATOM   3896  ND1 HIS A 629       2.055 -28.681  96.138  1.00 13.40           N  
ATOM   3897  CD2 HIS A 629       3.224 -28.145  97.903  1.00 11.23           C  
ATOM   3898  CE1 HIS A 629       1.811 -27.407  96.398  1.00 12.38           C  
ATOM   3899  NE2 HIS A 629       2.509 -27.059  97.461  1.00 10.94           N  
ATOM   3900  N   PRO A 630       6.780 -30.160  95.375  1.00 10.24           N  
ATOM   3901  CA  PRO A 630       8.141 -29.658  95.570  1.00  9.55           C  
ATOM   3902  C   PRO A 630       8.294 -28.163  95.869  1.00  8.70           C  
ATOM   3903  O   PRO A 630       8.818 -27.398  95.064  1.00  8.95           O  
ATOM   3904  CB  PRO A 630       8.856 -30.060  94.274  1.00  9.84           C  
ATOM   3905  CG  PRO A 630       7.769 -30.491  93.320  1.00 10.59           C  
ATOM   3906  CD  PRO A 630       6.448 -30.179  93.943  1.00 10.83           C  
ATOM   3907  N   SER A 631       7.801 -27.762  97.027  1.00  8.63           N  
ATOM   3908  CA  SER A 631       7.917 -26.397  97.487  1.00  8.39           C  
ATOM   3909  C   SER A 631       8.901 -26.564  98.652  1.00  6.42           C  
ATOM   3910  O   SER A 631       8.596 -27.238  99.632  1.00  7.03           O  
ATOM   3911  CB  SER A 631       6.552 -25.882  97.967  1.00  9.08           C  
ATOM   3912  OG  SER A 631       6.626 -24.539  98.414  1.00  9.47           O  
ATOM   3913  N   PRO A 632      10.097 -25.972  98.544  1.00  5.24           N  
ATOM   3914  CA  PRO A 632      11.149 -26.046  99.570  1.00  5.35           C  
ATOM   3915  C   PRO A 632      10.578 -25.798 100.959  1.00  5.06           C  
ATOM   3916  O   PRO A 632       9.956 -24.773 101.190  1.00  6.76           O  
ATOM   3917  CB  PRO A 632      12.112 -24.938  99.160  1.00  6.07           C  
ATOM   3918  CG  PRO A 632      11.857 -24.739  97.717  1.00  5.96           C  
ATOM   3919  CD  PRO A 632      10.377 -24.895  97.583  1.00  5.65           C  
ATOM   3920  N   LEU A 633      10.797 -26.706 101.894  1.00  4.11           N  
ATOM   3921  CA  LEU A 633      10.226 -26.509 103.209  1.00  5.24           C  
ATOM   3922  C   LEU A 633      10.633 -25.260 103.973  1.00  6.13           C  
ATOM   3923  O   LEU A 633       9.904 -24.844 104.861  1.00  5.99           O  
ATOM   3924  CB  LEU A 633      10.432 -27.750 104.086  1.00  5.67           C  
ATOM   3925  CG  LEU A 633       9.698 -28.992 103.563  1.00  7.17           C  
ATOM   3926  CD1 LEU A 633       9.745 -30.084 104.633  1.00  7.68           C  
ATOM   3927  CD2 LEU A 633       8.244 -28.640 103.203  1.00  7.37           C  
ATOM   3928  N   MET A 634      11.783 -24.668 103.654  1.00  8.25           N  
ATOM   3929  CA  MET A 634      12.208 -23.439 104.325  1.00  9.66           C  
ATOM   3930  C   MET A 634      11.425 -22.277 103.727  1.00  8.12           C  
ATOM   3931  O   MET A 634      11.343 -21.212 104.316  1.00  9.15           O  
ATOM   3932  CB  MET A 634      13.705 -23.176 104.140  1.00 12.26           C  
ATOM   3933  CG  MET A 634      14.633 -24.061 104.954  1.00 14.51           C  
ATOM   3934  SD  MET A 634      16.323 -23.989 104.294  1.00 16.90           S  
ATOM   3935  CE  MET A 634      17.166 -23.853 105.726  1.00 17.68           C  
ATOM   3936  N   GLY A 635      10.846 -22.493 102.554  1.00  6.21           N  
ATOM   3937  CA  GLY A 635      10.068 -21.454 101.910  1.00  5.60           C  
ATOM   3938  C   GLY A 635      10.656 -21.053 100.576  1.00  5.70           C  
ATOM   3939  O   GLY A 635      11.867 -21.139 100.381  1.00  8.75           O  
ATOM   3940  N   GLY A 636       9.823 -20.633  99.641  1.00  3.95           N  
ATOM   3941  CA  GLY A 636      10.351 -20.204  98.368  1.00  4.28           C  
ATOM   3942  C   GLY A 636       9.907 -20.969  97.142  1.00  5.16           C  
ATOM   3943  O   GLY A 636       8.897 -21.666  97.148  1.00  6.05           O  
ATOM   3944  N   PHE A 637      10.696 -20.844  96.088  1.00  4.96           N  
ATOM   3945  CA  PHE A 637      10.402 -21.482  94.826  1.00  5.84           C  
ATOM   3946  C   PHE A 637      11.222 -22.733  94.580  1.00  5.23           C  
ATOM   3947  O   PHE A 637      12.447 -22.681  94.524  1.00  5.84           O  
ATOM   3948  CB  PHE A 637      10.641 -20.473  93.698  1.00  7.01           C  
ATOM   3949  CG  PHE A 637       9.844 -19.211  93.857  1.00  7.68           C  
ATOM   3950  CD1 PHE A 637       8.528 -19.128  93.380  1.00  7.26           C  
ATOM   3951  CD2 PHE A 637      10.377 -18.122  94.567  1.00  6.83           C  
ATOM   3952  CE1 PHE A 637       7.748 -17.977  93.613  1.00  6.32           C  
ATOM   3953  CE2 PHE A 637       9.614 -16.983  94.800  1.00  6.85           C  
ATOM   3954  CZ  PHE A 637       8.290 -16.909  94.322  1.00  6.69           C  
ATOM   3955  N   GLY A 638      10.538 -23.864  94.441  1.00  4.85           N  
ATOM   3956  CA  GLY A 638      11.221 -25.113  94.150  1.00  3.45           C  
ATOM   3957  C   GLY A 638      11.478 -25.117  92.662  1.00  2.40           C  
ATOM   3958  O   GLY A 638      10.549 -24.964  91.876  1.00  2.46           O  
ATOM   3959  N   LEU A 639      12.736 -25.289  92.263  1.00  4.42           N  
ATOM   3960  CA  LEU A 639      13.088 -25.284  90.847  1.00  6.21           C  
ATOM   3961  C   LEU A 639      13.867 -26.511  90.440  1.00  8.27           C  
ATOM   3962  O   LEU A 639      14.750 -26.982  91.161  1.00  7.83           O  
ATOM   3963  CB  LEU A 639      13.920 -24.038  90.499  1.00  7.08           C  
ATOM   3964  CG  LEU A 639      13.361 -22.681  90.954  1.00  7.75           C  
ATOM   3965  CD1 LEU A 639      14.406 -21.604  90.781  1.00  8.07           C  
ATOM   3966  CD2 LEU A 639      12.100 -22.341  90.163  1.00  7.12           C  
ATOM   3967  N   LYS A 640      13.521 -27.023  89.268  1.00 11.95           N  
ATOM   3968  CA  LYS A 640      14.175 -28.183  88.695  1.00 15.41           C  
ATOM   3969  C   LYS A 640      15.555 -27.727  88.260  1.00 13.47           C  
ATOM   3970  O   LYS A 640      16.559 -28.384  88.526  1.00 12.99           O  
ATOM   3971  CB  LYS A 640      13.420 -28.652  87.452  1.00 20.32           C  
ATOM   3972  CG  LYS A 640      13.141 -30.128  87.408  1.00 24.80           C  
ATOM   3973  CD  LYS A 640      11.914 -30.462  88.235  1.00 28.00           C  
ATOM   3974  CE  LYS A 640      11.616 -31.958  88.197  1.00 30.05           C  
ATOM   3975  NZ  LYS A 640      10.273 -32.260  88.767  1.00 30.85           N  
ATOM   3976  N   HIS A 641      15.575 -26.596  87.566  1.00 12.88           N  
ATOM   3977  CA  HIS A 641      16.798 -26.014  87.047  1.00 12.94           C  
ATOM   3978  C   HIS A 641      16.991 -24.616  87.605  1.00  9.51           C  
ATOM   3979  O   HIS A 641      16.767 -23.627  86.922  1.00  9.66           O  
ATOM   3980  CB  HIS A 641      16.716 -25.982  85.526  1.00 16.06           C  
ATOM   3981  CG  HIS A 641      16.412 -27.318  84.928  1.00 19.61           C  
ATOM   3982  ND1 HIS A 641      17.200 -28.429  85.156  1.00 20.96           N  
ATOM   3983  CD2 HIS A 641      15.384 -27.737  84.152  1.00 21.15           C  
ATOM   3984  CE1 HIS A 641      16.669 -29.474  84.548  1.00 21.41           C  
ATOM   3985  NE2 HIS A 641      15.567 -29.082  83.931  1.00 21.40           N  
ATOM   3986  N   PRO A 642      17.446 -24.524  88.856  1.00  7.82           N  
ATOM   3987  CA  PRO A 642      17.678 -23.252  89.545  1.00  8.13           C  
ATOM   3988  C   PRO A 642      18.810 -22.397  88.953  1.00  8.35           C  
ATOM   3989  O   PRO A 642      19.530 -22.831  88.056  1.00  7.67           O  
ATOM   3990  CB  PRO A 642      17.968 -23.703  90.969  1.00  7.53           C  
ATOM   3991  CG  PRO A 642      18.753 -24.971  90.735  1.00  7.62           C  
ATOM   3992  CD  PRO A 642      17.986 -25.656  89.632  1.00  6.98           C  
ATOM   3993  N   PRO A 643      18.937 -21.139  89.406  1.00  9.63           N  
ATOM   3994  CA  PRO A 643      20.032 -20.325  88.859  1.00  9.70           C  
ATOM   3995  C   PRO A 643      21.307 -21.131  89.171  1.00  9.14           C  
ATOM   3996  O   PRO A 643      21.536 -21.526  90.319  1.00  7.79           O  
ATOM   3997  CB  PRO A 643      19.937 -19.036  89.668  1.00  9.86           C  
ATOM   3998  CG  PRO A 643      18.453 -18.940  89.949  1.00 10.00           C  
ATOM   3999  CD  PRO A 643      18.066 -20.348  90.300  1.00  9.54           C  
ATOM   4000  N   PRO A 644      22.141 -21.395  88.155  1.00  9.78           N  
ATOM   4001  CA  PRO A 644      23.368 -22.168  88.364  1.00 10.94           C  
ATOM   4002  C   PRO A 644      24.412 -21.551  89.289  1.00 10.76           C  
ATOM   4003  O   PRO A 644      24.496 -20.331  89.427  1.00 10.74           O  
ATOM   4004  CB  PRO A 644      23.900 -22.354  86.952  1.00 11.57           C  
ATOM   4005  CG  PRO A 644      23.485 -21.102  86.290  1.00 12.39           C  
ATOM   4006  CD  PRO A 644      22.067 -20.895  86.773  1.00 10.82           C  
ATOM   4007  N   GLN A 645      25.194 -22.414  89.927  1.00 10.04           N  
ATOM   4008  CA  GLN A 645      26.263 -21.973  90.804  1.00 10.17           C  
ATOM   4009  C   GLN A 645      27.334 -21.288  89.955  1.00  9.53           C  
ATOM   4010  O   GLN A 645      27.747 -21.808  88.918  1.00  9.11           O  
ATOM   4011  CB  GLN A 645      26.869 -23.168  91.548  1.00 10.05           C  
ATOM   4012  CG  GLN A 645      25.992 -23.677  92.668  1.00 10.62           C  
ATOM   4013  CD  GLN A 645      26.482 -24.987  93.263  1.00 10.86           C  
ATOM   4014  OE1 GLN A 645      26.450 -25.177  94.479  1.00 11.03           O  
ATOM   4015  NE2 GLN A 645      26.918 -25.910  92.399  1.00  9.56           N  
ATOM   4016  N   ILE A 646      27.744 -20.096  90.373  1.00  9.71           N  
ATOM   4017  CA  ILE A 646      28.785 -19.375  89.664  1.00 10.21           C  
ATOM   4018  C   ILE A 646      30.002 -19.386  90.558  1.00  9.52           C  
ATOM   4019  O   ILE A 646      30.068 -18.674  91.554  1.00 10.69           O  
ATOM   4020  CB  ILE A 646      28.356 -17.946  89.325  1.00 11.60           C  
ATOM   4021  CG1 ILE A 646      27.173 -18.009  88.351  1.00 12.07           C  
ATOM   4022  CG2 ILE A 646      29.515 -17.190  88.680  1.00 12.13           C  
ATOM   4023  CD1 ILE A 646      26.335 -16.763  88.284  1.00 11.49           C  
ATOM   4024  N   LEU A 647      30.958 -20.234  90.196  1.00  9.10           N  
ATOM   4025  CA  LEU A 647      32.182 -20.406  90.961  1.00  8.09           C  
ATOM   4026  C   LEU A 647      33.314 -19.584  90.397  1.00  6.78           C  
ATOM   4027  O   LEU A 647      33.426 -19.382  89.192  1.00  5.19           O  
ATOM   4028  CB  LEU A 647      32.531 -21.892  91.014  1.00  8.39           C  
ATOM   4029  CG  LEU A 647      31.369 -22.639  91.678  1.00  7.03           C  
ATOM   4030  CD1 LEU A 647      30.724 -23.558  90.682  1.00  6.88           C  
ATOM   4031  CD2 LEU A 647      31.860 -23.383  92.908  1.00  6.30           C  
ATOM   4032  N   ILE A 648      34.159 -19.107  91.297  1.00  8.39           N  
ATOM   4033  CA  ILE A 648      35.252 -18.238  90.920  1.00  9.59           C  
ATOM   4034  C   ILE A 648      36.490 -18.541  91.759  1.00  9.14           C  
ATOM   4035  O   ILE A 648      36.381 -18.927  92.920  1.00  9.00           O  
ATOM   4036  CB  ILE A 648      34.807 -16.743  91.143  1.00 11.81           C  
ATOM   4037  CG1 ILE A 648      35.804 -15.775  90.520  1.00 12.59           C  
ATOM   4038  CG2 ILE A 648      34.690 -16.436  92.664  1.00 11.62           C  
ATOM   4039  CD1 ILE A 648      35.424 -14.305  90.740  1.00 13.10           C  
ATOM   4040  N   LYS A 649      37.667 -18.386  91.159  1.00  9.26           N  
ATOM   4041  CA  LYS A 649      38.909 -18.587  91.891  1.00  9.33           C  
ATOM   4042  C   LYS A 649      40.092 -17.856  91.259  1.00  7.75           C  
ATOM   4043  O   LYS A 649      40.127 -17.623  90.052  1.00  7.42           O  
ATOM   4044  CB  LYS A 649      39.234 -20.082  92.049  1.00 10.71           C  
ATOM   4045  CG  LYS A 649      39.919 -20.737  90.891  1.00 12.31           C  
ATOM   4046  CD  LYS A 649      40.662 -21.973  91.393  1.00 13.99           C  
ATOM   4047  CE  LYS A 649      41.503 -22.609  90.290  1.00 14.81           C  
ATOM   4048  NZ  LYS A 649      42.623 -23.389  90.909  1.00 16.61           N  
ATOM   4049  N   ASN A 650      41.045 -17.477  92.104  1.00  8.14           N  
ATOM   4050  CA  ASN A 650      42.263 -16.789  91.671  1.00  8.38           C  
ATOM   4051  C   ASN A 650      43.214 -17.807  91.051  1.00  8.08           C  
ATOM   4052  O   ASN A 650      43.529 -18.814  91.682  1.00  8.90           O  
ATOM   4053  CB  ASN A 650      42.969 -16.145  92.877  1.00  8.87           C  
ATOM   4054  CG  ASN A 650      42.134 -15.071  93.545  1.00  8.10           C  
ATOM   4055  OD1 ASN A 650      41.486 -14.273  92.869  1.00  8.87           O  
ATOM   4056  ND2 ASN A 650      42.153 -15.037  94.874  1.00  6.11           N  
ATOM   4057  N   THR A 651      43.659 -17.565  89.824  1.00  9.10           N  
ATOM   4058  CA  THR A 651      44.599 -18.472  89.159  1.00 10.42           C  
ATOM   4059  C   THR A 651      45.902 -18.476  89.969  1.00 11.95           C  
ATOM   4060  O   THR A 651      46.411 -17.419  90.339  1.00 12.89           O  
ATOM   4061  CB  THR A 651      44.896 -17.990  87.730  1.00 10.93           C  
ATOM   4062  OG1 THR A 651      43.663 -17.775  87.038  1.00 11.70           O  
ATOM   4063  CG2 THR A 651      45.712 -19.021  86.968  1.00 11.42           C  
ATOM   4064  N   PRO A 652      46.462 -19.661  90.255  1.00 12.44           N  
ATOM   4065  CA  PRO A 652      47.704 -19.663  91.034  1.00 12.38           C  
ATOM   4066  C   PRO A 652      48.873 -19.083  90.237  1.00 12.16           C  
ATOM   4067  O   PRO A 652      48.975 -19.262  89.017  1.00 11.99           O  
ATOM   4068  CB  PRO A 652      47.926 -21.144  91.364  1.00 12.70           C  
ATOM   4069  CG  PRO A 652      46.628 -21.833  90.953  1.00 13.34           C  
ATOM   4070  CD  PRO A 652      46.120 -21.023  89.814  1.00 12.86           C  
ATOM   4071  N   VAL A 653      49.741 -18.369  90.937  1.00 11.69           N  
ATOM   4072  CA  VAL A 653      50.913 -17.786  90.320  1.00 11.71           C  
ATOM   4073  C   VAL A 653      52.102 -18.235  91.158  1.00 10.48           C  
ATOM   4074  O   VAL A 653      52.280 -17.806  92.303  1.00  9.97           O  
ATOM   4075  CB  VAL A 653      50.835 -16.243  90.271  1.00 13.12           C  
ATOM   4076  CG1 VAL A 653      52.164 -15.668  89.800  1.00 14.60           C  
ATOM   4077  CG2 VAL A 653      49.728 -15.810  89.322  1.00 12.93           C  
ATOM   4078  N   PRO A 654      52.925 -19.128  90.592  1.00 10.52           N  
ATOM   4079  CA  PRO A 654      54.121 -19.684  91.244  1.00 11.09           C  
ATOM   4080  C   PRO A 654      55.119 -18.606  91.679  1.00 11.50           C  
ATOM   4081  O   PRO A 654      55.296 -17.603  91.002  1.00 11.16           O  
ATOM   4082  CB  PRO A 654      54.732 -20.582  90.161  1.00 10.28           C  
ATOM   4083  CG  PRO A 654      53.622 -20.796  89.181  1.00 10.26           C  
ATOM   4084  CD  PRO A 654      52.854 -19.529  89.177  1.00  9.52           C  
ATOM   4085  N   ALA A 655      55.763 -18.821  92.815  1.00 13.00           N  
ATOM   4086  CA  ALA A 655      56.785 -17.899  93.276  1.00 14.42           C  
ATOM   4087  C   ALA A 655      58.065 -18.353  92.559  1.00 17.28           C  
ATOM   4088  O   ALA A 655      58.018 -19.241  91.709  1.00 17.82           O  
ATOM   4089  CB  ALA A 655      56.948 -18.003  94.780  1.00 13.81           C  
ATOM   4090  N   ASN A 656      59.204 -17.762  92.904  1.00 19.56           N  
ATOM   4091  CA  ASN A 656      60.493 -18.078  92.276  1.00 20.36           C  
ATOM   4092  C   ASN A 656      60.896 -19.565  92.268  1.00 19.12           C  
ATOM   4093  O   ASN A 656      61.234 -20.134  93.310  1.00 20.22           O  
ATOM   4094  CB  ASN A 656      61.583 -17.246  92.958  1.00 22.62           C  
ATOM   4095  CG  ASN A 656      62.872 -17.191  92.154  1.00 24.16           C  
ATOM   4096  OD1 ASN A 656      62.854 -17.096  90.922  1.00 24.10           O  
ATOM   4097  ND2 ASN A 656      64.003 -17.233  92.854  1.00 24.79           N  
ATOM   4098  N   PRO A 657      60.867 -20.211  91.087  1.00 16.81           N  
ATOM   4099  CA  PRO A 657      61.232 -21.627  90.961  1.00 16.63           C  
ATOM   4100  C   PRO A 657      62.742 -21.862  90.987  1.00 16.80           C  
ATOM   4101  O   PRO A 657      63.518 -20.968  90.649  1.00 16.63           O  
ATOM   4102  CB  PRO A 657      60.604 -22.030  89.631  1.00 16.15           C  
ATOM   4103  CG  PRO A 657      60.707 -20.776  88.826  1.00 16.38           C  
ATOM   4104  CD  PRO A 657      60.354 -19.681  89.811  1.00 15.99           C  
ATOM   4105  N   SER A 658      63.158 -23.055  91.407  1.00 17.53           N  
ATOM   4106  CA  SER A 658      64.583 -23.366  91.451  1.00 18.57           C  
ATOM   4107  C   SER A 658      65.101 -23.429  90.017  1.00 18.31           C  
ATOM   4108  O   SER A 658      64.326 -23.590  89.073  1.00 18.03           O  
ATOM   4109  CB  SER A 658      64.832 -24.699  92.156  1.00 19.56           C  
ATOM   4110  OG  SER A 658      64.340 -25.777  91.384  1.00 20.34           O  
ATOM   4111  N   THR A 659      66.407 -23.296  89.845  1.00 18.78           N  
ATOM   4112  CA  THR A 659      66.966 -23.325  88.501  1.00 18.78           C  
ATOM   4113  C   THR A 659      67.352 -24.712  88.018  1.00 19.26           C  
ATOM   4114  O   THR A 659      67.896 -24.867  86.929  1.00 19.73           O  
ATOM   4115  CB  THR A 659      68.147 -22.339  88.380  1.00 17.59           C  
ATOM   4116  OG1 THR A 659      69.124 -22.610  89.396  1.00 17.94           O  
ATOM   4117  CG2 THR A 659      67.634 -20.919  88.530  1.00 16.84           C  
ATOM   4118  N   THR A 660      67.085 -25.724  88.837  1.00 20.37           N  
ATOM   4119  CA  THR A 660      67.331 -27.103  88.424  1.00 21.48           C  
ATOM   4120  C   THR A 660      65.962 -27.744  88.472  1.00 20.21           C  
ATOM   4121  O   THR A 660      65.206 -27.536  89.418  1.00 21.07           O  
ATOM   4122  CB  THR A 660      68.291 -27.894  89.359  1.00 23.33           C  
ATOM   4123  OG1 THR A 660      67.740 -27.981  90.674  1.00 23.60           O  
ATOM   4124  CG2 THR A 660      69.653 -27.235  89.405  1.00 25.20           C  
ATOM   4125  N   PHE A 661      65.634 -28.507  87.441  1.00 18.67           N  
ATOM   4126  CA  PHE A 661      64.345 -29.160  87.374  1.00 16.97           C  
ATOM   4127  C   PHE A 661      64.016 -30.014  88.592  1.00 17.81           C  
ATOM   4128  O   PHE A 661      64.885 -30.653  89.190  1.00 17.87           O  
ATOM   4129  CB  PHE A 661      64.257 -30.033  86.125  1.00 15.44           C  
ATOM   4130  CG  PHE A 661      62.965 -30.802  86.027  1.00 14.01           C  
ATOM   4131  CD1 PHE A 661      61.791 -30.163  85.637  1.00 13.17           C  
ATOM   4132  CD2 PHE A 661      62.918 -32.154  86.363  1.00 12.77           C  
ATOM   4133  CE1 PHE A 661      60.587 -30.857  85.582  1.00 12.80           C  
ATOM   4134  CE2 PHE A 661      61.720 -32.858  86.313  1.00 12.23           C  
ATOM   4135  CZ  PHE A 661      60.552 -32.212  85.922  1.00 12.40           C  
ATOM   4136  N   SER A 662      62.739 -30.012  88.950  1.00 19.66           N  
ATOM   4137  CA  SER A 662      62.233 -30.801  90.066  1.00 22.26           C  
ATOM   4138  C   SER A 662      60.835 -31.234  89.658  1.00 22.88           C  
ATOM   4139  O   SER A 662      60.018 -30.406  89.248  1.00 22.61           O  
ATOM   4140  CB  SER A 662      62.177 -29.969  91.350  1.00 23.80           C  
ATOM   4141  OG  SER A 662      61.687 -30.747  92.431  1.00 24.74           O  
ATOM   4142  N   ALA A 663      60.573 -32.534  89.746  1.00 23.84           N  
ATOM   4143  CA  ALA A 663      59.274 -33.082  89.374  1.00 25.18           C  
ATOM   4144  C   ALA A 663      58.251 -32.867  90.483  1.00 26.01           C  
ATOM   4145  O   ALA A 663      57.046 -32.972  90.252  1.00 26.31           O  
ATOM   4146  CB  ALA A 663      59.406 -34.580  89.061  1.00 25.77           C  
ATOM   4147  N   ALA A 664      58.741 -32.568  91.684  1.00 26.53           N  
ATOM   4148  CA  ALA A 664      57.878 -32.334  92.837  1.00 26.49           C  
ATOM   4149  C   ALA A 664      56.853 -31.261  92.541  1.00 27.09           C  
ATOM   4150  O   ALA A 664      57.091 -30.335  91.764  1.00 27.36           O  
ATOM   4151  CB  ALA A 664      58.709 -31.934  94.057  1.00 26.48           C  
ATOM   4152  N   LYS A 665      55.699 -31.408  93.173  1.00 27.65           N  
ATOM   4153  CA  LYS A 665      54.583 -30.487  93.029  1.00 27.50           C  
ATOM   4154  C   LYS A 665      54.974 -29.094  93.535  1.00 27.26           C  
ATOM   4155  O   LYS A 665      55.568 -28.957  94.610  1.00 27.01           O  
ATOM   4156  CB  LYS A 665      53.418 -31.041  93.850  1.00 26.96           C  
ATOM   4157  CG  LYS A 665      52.117 -30.266  93.838  1.00 25.29           C  
ATOM   4158  CD  LYS A 665      51.336 -30.704  95.069  1.00 24.09           C  
ATOM   4159  CE  LYS A 665      49.849 -30.428  94.965  1.00 23.35           C  
ATOM   4160  NZ  LYS A 665      49.196 -30.947  96.196  1.00 22.72           N  
ATOM   4161  N   PHE A 666      54.633 -28.072  92.757  1.00 26.80           N  
ATOM   4162  CA  PHE A 666      54.924 -26.695  93.127  1.00 27.23           C  
ATOM   4163  C   PHE A 666      54.152 -26.298  94.388  1.00 25.94           C  
ATOM   4164  O   PHE A 666      52.925 -26.360  94.412  1.00 26.34           O  
ATOM   4165  CB  PHE A 666      54.541 -25.773  91.979  1.00 29.37           C  
ATOM   4166  CG  PHE A 666      55.628 -24.833  91.583  1.00 31.58           C  
ATOM   4167  CD1 PHE A 666      55.908 -23.713  92.356  1.00 32.34           C  
ATOM   4168  CD2 PHE A 666      56.405 -25.090  90.456  1.00 32.52           C  
ATOM   4169  CE1 PHE A 666      56.950 -22.855  92.016  1.00 33.00           C  
ATOM   4170  CE2 PHE A 666      57.450 -24.240  90.106  1.00 33.12           C  
ATOM   4171  CZ  PHE A 666      57.722 -23.121  90.890  1.00 33.34           C  
ATOM   4172  N   ALA A 667      54.863 -25.876  95.428  1.00 24.92           N  
ATOM   4173  CA  ALA A 667      54.205 -25.507  96.678  1.00 24.93           C  
ATOM   4174  C   ALA A 667      54.397 -24.056  97.136  1.00 24.41           C  
ATOM   4175  O   ALA A 667      53.841 -23.653  98.162  1.00 25.00           O  
ATOM   4176  CB  ALA A 667      54.648 -26.460  97.793  1.00 24.78           C  
ATOM   4177  N   SER A 668      55.178 -23.273  96.398  1.00 22.79           N  
ATOM   4178  CA  SER A 668      55.393 -21.879  96.777  1.00 21.37           C  
ATOM   4179  C   SER A 668      54.689 -20.964  95.789  1.00 17.43           C  
ATOM   4180  O   SER A 668      54.941 -21.009  94.590  1.00 16.19           O  
ATOM   4181  CB  SER A 668      56.891 -21.561  96.842  1.00 23.02           C  
ATOM   4182  OG  SER A 668      57.548 -21.959  95.646  1.00 24.50           O  
ATOM   4183  N   PHE A 669      53.802 -20.127  96.313  1.00 16.43           N  
ATOM   4184  CA  PHE A 669      53.031 -19.226  95.479  1.00 15.69           C  
ATOM   4185  C   PHE A 669      53.111 -17.779  95.897  1.00 16.40           C  
ATOM   4186  O   PHE A 669      53.478 -17.448  97.031  1.00 16.60           O  
ATOM   4187  CB  PHE A 669      51.567 -19.656  95.480  1.00 15.18           C  
ATOM   4188  CG  PHE A 669      51.331 -20.980  94.841  1.00 15.21           C  
ATOM   4189  CD1 PHE A 669      51.256 -21.090  93.450  1.00 15.24           C  
ATOM   4190  CD2 PHE A 669      51.230 -22.133  95.618  1.00 14.97           C  
ATOM   4191  CE1 PHE A 669      51.085 -22.333  92.837  1.00 15.25           C  
ATOM   4192  CE2 PHE A 669      51.060 -23.379  95.012  1.00 15.33           C  
ATOM   4193  CZ  PHE A 669      50.988 -23.479  93.617  1.00 14.82           C  
ATOM   4194  N   ILE A 670      52.773 -16.912  94.954  1.00 16.57           N  
ATOM   4195  CA  ILE A 670      52.755 -15.488  95.213  1.00 17.46           C  
ATOM   4196  C   ILE A 670      51.390 -15.202  95.842  1.00 17.14           C  
ATOM   4197  O   ILE A 670      50.358 -15.455  95.222  1.00 16.90           O  
ATOM   4198  CB  ILE A 670      52.938 -14.696  93.887  1.00 18.39           C  
ATOM   4199  CG1 ILE A 670      54.417 -14.772  93.463  1.00 18.27           C  
ATOM   4200  CG2 ILE A 670      52.456 -13.244  94.047  1.00 18.33           C  
ATOM   4201  CD1 ILE A 670      54.724 -14.095  92.163  1.00 17.98           C  
ATOM   4202  N   THR A 671      51.393 -14.706  97.080  1.00 16.70           N  
ATOM   4203  CA  THR A 671      50.156 -14.396  97.796  1.00 16.28           C  
ATOM   4204  C   THR A 671      49.290 -13.339  97.114  1.00 14.37           C  
ATOM   4205  O   THR A 671      49.752 -12.246  96.804  1.00 13.52           O  
ATOM   4206  CB  THR A 671      50.431 -13.880  99.224  1.00 18.34           C  
ATOM   4207  OG1 THR A 671      51.010 -14.924 100.016  1.00 19.92           O  
ATOM   4208  CG2 THR A 671      49.139 -13.413  99.876  1.00 18.63           C  
ATOM   4209  N   GLN A 672      48.033 -13.672  96.867  1.00 13.91           N  
ATOM   4210  CA  GLN A 672      47.144 -12.698  96.284  1.00 14.56           C  
ATOM   4211  C   GLN A 672      45.666 -12.895  96.545  1.00 13.24           C  
ATOM   4212  O   GLN A 672      45.246 -13.873  97.166  1.00 13.74           O  
ATOM   4213  CB  GLN A 672      47.398 -12.561  94.795  1.00 16.80           C  
ATOM   4214  CG  GLN A 672      47.423 -13.809  93.996  1.00 18.95           C  
ATOM   4215  CD  GLN A 672      47.870 -13.501  92.583  1.00 21.00           C  
ATOM   4216  OE1 GLN A 672      48.876 -12.808  92.375  1.00 20.55           O  
ATOM   4217  NE2 GLN A 672      47.122 -13.999  91.601  1.00 22.63           N  
ATOM   4218  N   TYR A 673      44.883 -11.924  96.096  1.00 11.77           N  
ATOM   4219  CA  TYR A 673      43.443 -11.973  96.253  1.00 10.27           C  
ATOM   4220  C   TYR A 673      42.858 -11.083  95.181  1.00  7.98           C  
ATOM   4221  O   TYR A 673      43.568 -10.267  94.601  1.00  8.44           O  
ATOM   4222  CB  TYR A 673      43.050 -11.497  97.652  1.00 11.14           C  
ATOM   4223  CG  TYR A 673      43.257 -10.022  97.914  1.00 12.70           C  
ATOM   4224  CD1 TYR A 673      42.241  -9.092  97.641  1.00 12.70           C  
ATOM   4225  CD2 TYR A 673      44.456  -9.549  98.466  1.00 13.01           C  
ATOM   4226  CE1 TYR A 673      42.411  -7.739  97.915  1.00 12.84           C  
ATOM   4227  CE2 TYR A 673      44.638  -8.196  98.742  1.00 13.19           C  
ATOM   4228  CZ  TYR A 673      43.607  -7.293  98.463  1.00 13.59           C  
ATOM   4229  OH  TYR A 673      43.782  -5.949  98.719  1.00 13.11           O  
ATOM   4230  N   SER A 674      41.584 -11.264  94.871  1.00  5.94           N  
ATOM   4231  CA  SER A 674      40.967 -10.422  93.870  1.00  5.55           C  
ATOM   4232  C   SER A 674      39.806  -9.666  94.483  1.00  4.79           C  
ATOM   4233  O   SER A 674      39.431  -9.889  95.635  1.00  3.12           O  
ATOM   4234  CB  SER A 674      40.516 -11.242  92.660  1.00  5.93           C  
ATOM   4235  OG  SER A 674      39.661 -12.291  93.045  1.00  6.96           O  
ATOM   4236  N   THR A 675      39.245  -8.747  93.720  1.00  6.30           N  
ATOM   4237  CA  THR A 675      38.150  -7.960  94.235  1.00  7.37           C  
ATOM   4238  C   THR A 675      37.503  -7.354  93.024  1.00  5.74           C  
ATOM   4239  O   THR A 675      38.135  -7.249  91.984  1.00  6.25           O  
ATOM   4240  CB  THR A 675      38.686  -6.872  95.244  1.00  9.27           C  
ATOM   4241  OG1 THR A 675      37.594  -6.158  95.822  1.00 10.70           O  
ATOM   4242  CG2 THR A 675      39.587  -5.885  94.558  1.00 10.15           C  
ATOM   4243  N   GLY A 676      36.239  -6.976  93.142  1.00  4.40           N  
ATOM   4244  CA  GLY A 676      35.561  -6.400  92.004  1.00  3.29           C  
ATOM   4245  C   GLY A 676      34.123  -6.095  92.320  1.00  1.61           C  
ATOM   4246  O   GLY A 676      33.725  -6.094  93.481  1.00  0.00           O  
ATOM   4247  N   GLN A 677      33.336  -5.823  91.289  1.00  4.47           N  
ATOM   4248  CA  GLN A 677      31.918  -5.540  91.494  1.00  6.84           C  
ATOM   4249  C   GLN A 677      31.104  -6.703  90.960  1.00  7.01           C  
ATOM   4250  O   GLN A 677      31.522  -7.406  90.045  1.00  6.78           O  
ATOM   4251  CB  GLN A 677      31.461  -4.272  90.741  1.00  8.85           C  
ATOM   4252  CG  GLN A 677      32.251  -2.997  90.998  1.00 11.13           C  
ATOM   4253  CD  GLN A 677      32.469  -2.739  92.470  1.00 12.24           C  
ATOM   4254  OE1 GLN A 677      31.509  -2.564  93.222  1.00 13.34           O  
ATOM   4255  NE2 GLN A 677      33.743  -2.720  92.897  1.00 11.13           N  
ATOM   4256  N   VAL A 678      29.930  -6.893  91.546  1.00  7.73           N  
ATOM   4257  CA  VAL A 678      29.010  -7.927  91.097  1.00  6.88           C  
ATOM   4258  C   VAL A 678      27.636  -7.292  91.093  1.00  7.82           C  
ATOM   4259  O   VAL A 678      27.249  -6.622  92.050  1.00  7.95           O  
ATOM   4260  CB  VAL A 678      29.001  -9.184  92.041  1.00  5.04           C  
ATOM   4261  CG1 VAL A 678      28.606  -8.805  93.481  1.00  4.06           C  
ATOM   4262  CG2 VAL A 678      28.054 -10.223  91.485  1.00  4.70           C  
ATOM   4263  N   SER A 679      26.901  -7.477  90.012  1.00  8.81           N  
ATOM   4264  CA  SER A 679      25.564  -6.943  89.973  1.00  9.81           C  
ATOM   4265  C   SER A 679      24.572  -8.024  89.524  1.00 10.49           C  
ATOM   4266  O   SER A 679      24.811  -8.751  88.559  1.00  9.64           O  
ATOM   4267  CB  SER A 679      25.495  -5.704  89.064  1.00  9.93           C  
ATOM   4268  OG  SER A 679      25.504  -6.047  87.694  1.00 11.23           O  
ATOM   4269  N   VAL A 680      23.472  -8.140  90.261  1.00 11.74           N  
ATOM   4270  CA  VAL A 680      22.427  -9.111  89.948  1.00 11.99           C  
ATOM   4271  C   VAL A 680      21.137  -8.351  89.665  1.00 10.86           C  
ATOM   4272  O   VAL A 680      20.695  -7.544  90.474  1.00 10.45           O  
ATOM   4273  CB  VAL A 680      22.146 -10.079  91.131  1.00 13.10           C  
ATOM   4274  CG1 VAL A 680      21.334 -11.260  90.640  1.00 13.84           C  
ATOM   4275  CG2 VAL A 680      23.428 -10.560  91.751  1.00 14.34           C  
ATOM   4276  N   GLU A 681      20.535  -8.608  88.515  1.00 11.56           N  
ATOM   4277  CA  GLU A 681      19.288  -7.954  88.152  1.00 12.69           C  
ATOM   4278  C   GLU A 681      18.199  -9.010  87.907  1.00 10.84           C  
ATOM   4279  O   GLU A 681      18.289  -9.800  86.968  1.00 10.37           O  
ATOM   4280  CB  GLU A 681      19.492  -7.097  86.902  1.00 16.20           C  
ATOM   4281  CG  GLU A 681      18.206  -6.752  86.178  1.00 21.49           C  
ATOM   4282  CD  GLU A 681      18.425  -5.945  84.901  1.00 25.97           C  
ATOM   4283  OE1 GLU A 681      18.911  -4.791  84.994  1.00 27.52           O  
ATOM   4284  OE2 GLU A 681      18.105  -6.461  83.802  1.00 27.07           O  
ATOM   4285  N   ILE A 682      17.179  -9.029  88.760  1.00  9.27           N  
ATOM   4286  CA  ILE A 682      16.097  -9.986  88.596  1.00  8.41           C  
ATOM   4287  C   ILE A 682      14.785  -9.330  88.206  1.00  8.10           C  
ATOM   4288  O   ILE A 682      14.404  -8.296  88.747  1.00  7.66           O  
ATOM   4289  CB  ILE A 682      15.846 -10.833  89.882  1.00  7.38           C  
ATOM   4290  CG1 ILE A 682      17.102 -11.636  90.232  1.00  7.39           C  
ATOM   4291  CG2 ILE A 682      14.638 -11.789  89.658  1.00  6.10           C  
ATOM   4292  CD1 ILE A 682      16.960 -12.554  91.423  1.00  8.02           C  
ATOM   4293  N   GLU A 683      14.108  -9.928  87.238  1.00  8.86           N  
ATOM   4294  CA  GLU A 683      12.815  -9.431  86.818  1.00  9.97           C  
ATOM   4295  C   GLU A 683      11.782 -10.308  87.503  1.00  7.78           C  
ATOM   4296  O   GLU A 683      11.848 -11.526  87.410  1.00  7.17           O  
ATOM   4297  CB  GLU A 683      12.642  -9.544  85.313  1.00 13.63           C  
ATOM   4298  CG  GLU A 683      11.323  -8.956  84.843  1.00 17.77           C  
ATOM   4299  CD  GLU A 683      10.993  -9.309  83.407  1.00 21.49           C  
ATOM   4300  OE1 GLU A 683       9.997  -8.772  82.866  1.00 22.79           O  
ATOM   4301  OE2 GLU A 683      11.720 -10.132  82.812  1.00 22.97           O  
ATOM   4302  N   TRP A 684      10.839  -9.694  88.211  1.00  8.28           N  
ATOM   4303  CA  TRP A 684       9.787 -10.445  88.900  1.00  7.18           C  
ATOM   4304  C   TRP A 684       8.417 -10.183  88.288  1.00  8.27           C  
ATOM   4305  O   TRP A 684       8.114  -9.068  87.879  1.00  7.88           O  
ATOM   4306  CB  TRP A 684       9.728 -10.064  90.370  1.00  5.30           C  
ATOM   4307  CG  TRP A 684      11.052 -10.086  91.076  1.00  4.99           C  
ATOM   4308  CD1 TRP A 684      12.027  -9.117  91.040  1.00  3.38           C  
ATOM   4309  CD2 TRP A 684      11.548 -11.118  91.941  1.00  4.98           C  
ATOM   4310  NE1 TRP A 684      13.088  -9.483  91.832  1.00  2.48           N  
ATOM   4311  CE2 TRP A 684      12.827 -10.701  92.397  1.00  4.04           C  
ATOM   4312  CE3 TRP A 684      11.037 -12.351  92.378  1.00  4.54           C  
ATOM   4313  CZ2 TRP A 684      13.604 -11.478  93.274  1.00  3.92           C  
ATOM   4314  CZ3 TRP A 684      11.803 -13.121  93.248  1.00  3.97           C  
ATOM   4315  CH2 TRP A 684      13.080 -12.676  93.686  1.00  4.23           C  
ATOM   4316  N   GLU A 685       7.586 -11.216  88.207  1.00  9.78           N  
ATOM   4317  CA  GLU A 685       6.243 -11.037  87.675  1.00 10.02           C  
ATOM   4318  C   GLU A 685       5.312 -10.885  88.864  1.00  8.78           C  
ATOM   4319  O   GLU A 685       5.487 -11.544  89.883  1.00  7.65           O  
ATOM   4320  CB  GLU A 685       5.822 -12.227  86.829  1.00 12.56           C  
ATOM   4321  CG  GLU A 685       4.487 -12.040  86.127  1.00 15.55           C  
ATOM   4322  CD  GLU A 685       4.092 -13.268  85.322  1.00 18.84           C  
ATOM   4323  OE1 GLU A 685       3.086 -13.217  84.574  1.00 20.12           O  
ATOM   4324  OE2 GLU A 685       4.796 -14.294  85.441  1.00 19.81           O  
ATOM   4325  N   LEU A 686       4.319 -10.012  88.731  1.00 10.05           N  
ATOM   4326  CA  LEU A 686       3.390  -9.756  89.824  1.00 11.10           C  
ATOM   4327  C   LEU A 686       1.928 -10.038  89.519  1.00 11.18           C  
ATOM   4328  O   LEU A 686       1.508 -10.041  88.362  1.00 11.05           O  
ATOM   4329  CB  LEU A 686       3.512  -8.289  90.249  1.00 11.94           C  
ATOM   4330  CG  LEU A 686       4.914  -7.774  90.612  1.00 11.56           C  
ATOM   4331  CD1 LEU A 686       4.881  -6.264  90.804  1.00 11.23           C  
ATOM   4332  CD2 LEU A 686       5.393  -8.462  91.866  1.00 10.95           C  
ATOM   4333  N   GLN A 687       1.163 -10.314  90.569  1.00 12.08           N  
ATOM   4334  CA  GLN A 687      -0.284 -10.492  90.440  1.00 13.86           C  
ATOM   4335  C   GLN A 687      -0.821  -9.366  91.305  1.00 13.28           C  
ATOM   4336  O   GLN A 687      -0.828  -9.473  92.528  1.00 11.65           O  
ATOM   4337  CB  GLN A 687      -0.784 -11.820  91.019  1.00 16.43           C  
ATOM   4338  CG  GLN A 687      -0.508 -13.035  90.187  1.00 20.07           C  
ATOM   4339  CD  GLN A 687      -1.170 -14.283  90.764  1.00 23.43           C  
ATOM   4340  OE1 GLN A 687      -1.184 -14.489  91.986  1.00 23.66           O  
ATOM   4341  NE2 GLN A 687      -1.717 -15.124  89.887  1.00 24.19           N  
ATOM   4342  N   LYS A 688      -1.246  -8.274  90.679  1.00 15.96           N  
ATOM   4343  CA  LYS A 688      -1.776  -7.143  91.436  1.00 17.90           C  
ATOM   4344  C   LYS A 688      -2.984  -7.497  92.289  1.00 16.81           C  
ATOM   4345  O   LYS A 688      -3.865  -8.249  91.873  1.00 16.16           O  
ATOM   4346  CB  LYS A 688      -2.171  -5.999  90.500  1.00 22.11           C  
ATOM   4347  CG  LYS A 688      -1.051  -5.031  90.189  1.00 26.69           C  
ATOM   4348  CD  LYS A 688      -1.571  -3.639  89.762  1.00 30.27           C  
ATOM   4349  CE  LYS A 688      -2.220  -3.623  88.367  1.00 32.31           C  
ATOM   4350  NZ  LYS A 688      -3.504  -4.398  88.272  1.00 33.00           N  
ATOM   4351  N   GLU A 689      -3.006  -6.943  93.491  1.00 17.21           N  
ATOM   4352  CA  GLU A 689      -4.101  -7.118  94.428  1.00 18.78           C  
ATOM   4353  C   GLU A 689      -5.328  -6.451  93.792  1.00 19.94           C  
ATOM   4354  O   GLU A 689      -5.221  -5.382  93.185  1.00 20.38           O  
ATOM   4355  CB  GLU A 689      -3.708  -6.451  95.753  1.00 20.93           C  
ATOM   4356  CG  GLU A 689      -4.826  -5.870  96.613  1.00 23.40           C  
ATOM   4357  CD  GLU A 689      -5.372  -4.535  96.086  1.00 24.65           C  
ATOM   4358  OE1 GLU A 689      -4.585  -3.578  95.900  1.00 24.59           O  
ATOM   4359  OE2 GLU A 689      -6.600  -4.453  95.865  1.00 25.00           O  
ATOM   4360  N   ASN A 690      -6.488  -7.077  93.915  1.00 21.10           N  
ATOM   4361  CA  ASN A 690      -7.704  -6.533  93.317  1.00 22.70           C  
ATOM   4362  C   ASN A 690      -8.907  -6.828  94.216  1.00 20.81           C  
ATOM   4363  O   ASN A 690      -9.939  -7.308  93.744  1.00 21.12           O  
ATOM   4364  CB  ASN A 690      -7.889  -7.173  91.934  1.00 25.29           C  
ATOM   4365  CG  ASN A 690      -9.095  -6.634  91.185  1.00 26.98           C  
ATOM   4366  OD1 ASN A 690      -9.262  -5.418  91.036  1.00 27.65           O  
ATOM   4367  ND2 ASN A 690      -9.936  -7.541  90.693  1.00 27.16           N  
ATOM   4368  N   SER A 691      -8.776  -6.524  95.505  1.00 18.98           N  
ATOM   4369  CA  SER A 691      -9.838  -6.810  96.460  1.00 18.40           C  
ATOM   4370  C   SER A 691     -11.055  -5.892  96.379  1.00 17.90           C  
ATOM   4371  O   SER A 691     -10.925  -4.672  96.272  1.00 17.92           O  
ATOM   4372  CB  SER A 691      -9.285  -6.808  97.887  1.00 18.69           C  
ATOM   4373  OG  SER A 691      -9.024  -5.504  98.353  1.00 19.84           O  
ATOM   4374  N   LYS A 692     -12.239  -6.503  96.433  1.00 16.82           N  
ATOM   4375  CA  LYS A 692     -13.509  -5.786  96.367  1.00 15.48           C  
ATOM   4376  C   LYS A 692     -14.154  -5.714  97.739  1.00 11.74           C  
ATOM   4377  O   LYS A 692     -15.336  -5.444  97.868  1.00 12.24           O  
ATOM   4378  CB  LYS A 692     -14.458  -6.482  95.400  1.00 18.01           C  
ATOM   4379  CG  LYS A 692     -13.930  -6.588  93.998  1.00 19.37           C  
ATOM   4380  CD  LYS A 692     -13.803  -5.246  93.320  1.00 20.77           C  
ATOM   4381  CE  LYS A 692     -13.201  -5.436  91.924  1.00 22.59           C  
ATOM   4382  NZ  LYS A 692     -13.152  -4.173  91.125  1.00 23.70           N  
ATOM   4383  N   ARG A 693     -13.355  -5.984  98.756  1.00  9.54           N  
ATOM   4384  CA  ARG A 693     -13.762  -5.928 100.148  1.00  8.68           C  
ATOM   4385  C   ARG A 693     -14.161  -4.466 100.431  1.00  8.04           C  
ATOM   4386  O   ARG A 693     -13.752  -3.563  99.708  1.00  9.28           O  
ATOM   4387  CB  ARG A 693     -12.544  -6.382 100.946  1.00  9.46           C  
ATOM   4388  CG  ARG A 693     -12.410  -6.009 102.371  1.00  9.08           C  
ATOM   4389  CD  ARG A 693     -11.012  -6.440 102.798  1.00  8.28           C  
ATOM   4390  NE  ARG A 693     -10.680  -5.997 104.140  1.00  7.77           N  
ATOM   4391  CZ  ARG A 693     -10.284  -6.807 105.105  1.00  8.19           C  
ATOM   4392  NH1 ARG A 693     -10.174  -8.099 104.871  1.00  8.85           N  
ATOM   4393  NH2 ARG A 693      -9.997  -6.326 106.305  1.00  9.04           N  
ATOM   4394  N   TRP A 694     -14.957  -4.215 101.459  1.00  6.36           N  
ATOM   4395  CA  TRP A 694     -15.379  -2.846 101.724  1.00  4.87           C  
ATOM   4396  C   TRP A 694     -14.539  -2.118 102.778  1.00  4.56           C  
ATOM   4397  O   TRP A 694     -14.163  -0.963 102.593  1.00  3.63           O  
ATOM   4398  CB  TRP A 694     -16.878  -2.830 102.105  1.00  3.47           C  
ATOM   4399  CG  TRP A 694     -17.418  -1.463 102.477  1.00  0.99           C  
ATOM   4400  CD1 TRP A 694     -17.441  -0.887 103.734  1.00  0.00           C  
ATOM   4401  CD2 TRP A 694     -17.962  -0.488 101.579  1.00  0.00           C  
ATOM   4402  NE1 TRP A 694     -17.966   0.381 103.653  1.00  0.00           N  
ATOM   4403  CE2 TRP A 694     -18.291   0.651 102.347  1.00  0.00           C  
ATOM   4404  CE3 TRP A 694     -18.190  -0.463 100.192  1.00  0.00           C  
ATOM   4405  CZ2 TRP A 694     -18.843   1.805 101.779  1.00  0.00           C  
ATOM   4406  CZ3 TRP A 694     -18.734   0.689  99.620  1.00  0.28           C  
ATOM   4407  CH2 TRP A 694     -19.055   1.808 100.416  1.00  0.00           C  
ATOM   4408  N   ASN A 695     -14.256  -2.791 103.881  1.00  5.11           N  
ATOM   4409  CA  ASN A 695     -13.464  -2.201 104.945  1.00  5.38           C  
ATOM   4410  C   ASN A 695     -11.976  -2.232 104.550  1.00  6.38           C  
ATOM   4411  O   ASN A 695     -11.593  -2.955 103.630  1.00  4.91           O  
ATOM   4412  CB  ASN A 695     -13.721  -2.974 106.240  1.00  4.82           C  
ATOM   4413  CG  ASN A 695     -13.480  -4.469 106.091  1.00  3.95           C  
ATOM   4414  OD1 ASN A 695     -13.901  -5.081 105.119  1.00  4.09           O  
ATOM   4415  ND2 ASN A 695     -12.811  -5.060 107.067  1.00  4.23           N  
ATOM   4416  N   PRO A 696     -11.128  -1.425 105.221  1.00  7.70           N  
ATOM   4417  CA  PRO A 696      -9.690  -1.389 104.906  1.00  9.10           C  
ATOM   4418  C   PRO A 696      -8.939  -2.658 105.325  1.00  7.84           C  
ATOM   4419  O   PRO A 696      -9.295  -3.310 106.299  1.00  7.26           O  
ATOM   4420  CB  PRO A 696      -9.176  -0.153 105.678  1.00  9.24           C  
ATOM   4421  CG  PRO A 696     -10.431   0.639 105.991  1.00  9.12           C  
ATOM   4422  CD  PRO A 696     -11.458  -0.433 106.259  1.00  8.25           C  
ATOM   4423  N   GLU A 697      -7.893  -2.981 104.578  1.00  9.11           N  
ATOM   4424  CA  GLU A 697      -7.050  -4.155 104.825  1.00  9.58           C  
ATOM   4425  C   GLU A 697      -5.903  -3.858 105.776  1.00  8.56           C  
ATOM   4426  O   GLU A 697      -5.721  -2.738 106.260  1.00  7.97           O  
ATOM   4427  CB  GLU A 697      -6.411  -4.628 103.518  1.00 12.08           C  
ATOM   4428  CG  GLU A 697      -7.375  -5.093 102.458  1.00 15.07           C  
ATOM   4429  CD  GLU A 697      -7.064  -6.496 101.970  1.00 17.16           C  
ATOM   4430  OE1 GLU A 697      -6.915  -7.387 102.839  1.00 17.49           O  
ATOM   4431  OE2 GLU A 697      -6.977  -6.709 100.733  1.00 17.61           O  
ATOM   4432  N   ILE A 698      -5.107  -4.888 106.015  1.00  8.34           N  
ATOM   4433  CA  ILE A 698      -3.922  -4.770 106.842  1.00  6.88           C  
ATOM   4434  C   ILE A 698      -2.770  -4.525 105.874  1.00  4.52           C  
ATOM   4435  O   ILE A 698      -2.709  -5.109 104.795  1.00  3.11           O  
ATOM   4436  CB  ILE A 698      -3.704  -6.047 107.652  1.00  7.16           C  
ATOM   4437  CG1 ILE A 698      -4.742  -6.078 108.761  1.00  8.48           C  
ATOM   4438  CG2 ILE A 698      -2.283  -6.090 108.245  1.00  6.35           C  
ATOM   4439  CD1 ILE A 698      -4.894  -7.408 109.375  1.00  9.82           C  
ATOM   4440  N   GLN A 699      -1.892  -3.606 106.242  1.00  4.69           N  
ATOM   4441  CA  GLN A 699      -0.752  -3.261 105.408  1.00  4.62           C  
ATOM   4442  C   GLN A 699       0.459  -3.270 106.297  1.00  4.58           C  
ATOM   4443  O   GLN A 699       0.342  -3.030 107.499  1.00  4.86           O  
ATOM   4444  CB  GLN A 699      -0.916  -1.839 104.841  1.00  4.13           C  
ATOM   4445  CG  GLN A 699      -2.127  -1.629 103.972  1.00  3.49           C  
ATOM   4446  CD  GLN A 699      -1.910  -2.052 102.546  1.00  4.07           C  
ATOM   4447  OE1 GLN A 699      -1.554  -1.235 101.689  1.00  4.14           O  
ATOM   4448  NE2 GLN A 699      -2.113  -3.342 102.272  1.00  3.64           N  
ATOM   4449  N   TYR A 700       1.623  -3.563 105.727  1.00  5.33           N  
ATOM   4450  CA  TYR A 700       2.848  -3.491 106.512  1.00  5.55           C  
ATOM   4451  C   TYR A 700       3.158  -1.986 106.610  1.00  5.40           C  
ATOM   4452  O   TYR A 700       3.112  -1.284 105.606  1.00  4.45           O  
ATOM   4453  CB  TYR A 700       4.029  -4.179 105.807  1.00  6.10           C  
ATOM   4454  CG  TYR A 700       5.308  -3.976 106.590  1.00  6.77           C  
ATOM   4455  CD1 TYR A 700       5.498  -4.617 107.814  1.00  6.82           C  
ATOM   4456  CD2 TYR A 700       6.246  -3.001 106.204  1.00  7.75           C  
ATOM   4457  CE1 TYR A 700       6.568  -4.292 108.645  1.00  8.71           C  
ATOM   4458  CE2 TYR A 700       7.316  -2.663 107.034  1.00  8.77           C  
ATOM   4459  CZ  TYR A 700       7.471  -3.307 108.253  1.00 10.00           C  
ATOM   4460  OH  TYR A 700       8.488  -2.942 109.105  1.00 11.24           O  
ATOM   4461  N   THR A 701       3.475  -1.494 107.805  1.00  7.43           N  
ATOM   4462  CA  THR A 701       3.788  -0.077 107.967  1.00  9.61           C  
ATOM   4463  C   THR A 701       4.848   0.158 109.028  1.00 12.54           C  
ATOM   4464  O   THR A 701       4.981  -0.631 109.961  1.00 13.25           O  
ATOM   4465  CB  THR A 701       2.511   0.768 108.349  1.00  7.98           C  
ATOM   4466  OG1 THR A 701       2.851   2.163 108.374  1.00  8.09           O  
ATOM   4467  CG2 THR A 701       1.960   0.370 109.731  1.00  6.21           C  
ATOM   4468  N   SER A 702       5.613   1.239 108.879  1.00 14.79           N  
ATOM   4469  CA  SER A 702       6.621   1.591 109.877  1.00 17.62           C  
ATOM   4470  C   SER A 702       5.876   2.200 111.062  1.00 20.91           C  
ATOM   4471  O   SER A 702       4.753   2.682 110.907  1.00 21.02           O  
ATOM   4472  CB  SER A 702       7.603   2.625 109.317  1.00 17.70           C  
ATOM   4473  OG  SER A 702       8.476   2.064 108.362  1.00 18.17           O  
ATOM   4474  N   ASN A 703       6.488   2.185 112.238  1.00 25.27           N  
ATOM   4475  CA  ASN A 703       5.850   2.751 113.422  1.00 30.82           C  
ATOM   4476  C   ASN A 703       5.963   4.270 113.366  1.00 33.83           C  
ATOM   4477  O   ASN A 703       7.070   4.799 113.380  1.00 33.58           O  
ATOM   4478  CB  ASN A 703       6.534   2.236 114.692  1.00 33.23           C  
ATOM   4479  CG  ASN A 703       6.062   2.961 115.944  1.00 35.24           C  
ATOM   4480  OD1 ASN A 703       6.876   3.432 116.746  1.00 35.78           O  
ATOM   4481  ND2 ASN A 703       4.745   3.052 116.121  1.00 36.07           N  
ATOM   4482  N   TYR A 704       4.826   4.963 113.339  1.00 37.17           N  
ATOM   4483  CA  TYR A 704       4.815   6.422 113.240  1.00 40.93           C  
ATOM   4484  C   TYR A 704       5.384   7.232 114.414  1.00 40.99           C  
ATOM   4485  O   TYR A 704       5.618   8.432 114.272  1.00 41.26           O  
ATOM   4486  CB  TYR A 704       3.393   6.916 112.893  1.00 44.38           C  
ATOM   4487  CG  TYR A 704       2.471   7.120 114.078  1.00 47.48           C  
ATOM   4488  CD1 TYR A 704       2.565   8.264 114.875  1.00 48.91           C  
ATOM   4489  CD2 TYR A 704       1.502   6.167 114.403  1.00 48.94           C  
ATOM   4490  CE1 TYR A 704       1.714   8.456 115.971  1.00 49.98           C  
ATOM   4491  CE2 TYR A 704       0.646   6.347 115.493  1.00 49.95           C  
ATOM   4492  CZ  TYR A 704       0.757   7.494 116.273  1.00 50.49           C  
ATOM   4493  OH  TYR A 704      -0.092   7.676 117.347  1.00 50.87           O  
ATOM   4494  N   ASN A 705       5.617   6.598 115.559  1.00 41.15           N  
ATOM   4495  CA  ASN A 705       6.157   7.322 116.711  1.00 41.63           C  
ATOM   4496  C   ASN A 705       7.642   7.641 116.586  1.00 40.56           C  
ATOM   4497  O   ASN A 705       8.324   7.154 115.683  1.00 40.75           O  
ATOM   4498  CB  ASN A 705       5.927   6.539 118.006  1.00 43.32           C  
ATOM   4499  CG  ASN A 705       4.461   6.314 118.295  1.00 44.76           C  
ATOM   4500  OD1 ASN A 705       3.627   7.198 118.073  1.00 45.32           O  
ATOM   4501  ND2 ASN A 705       4.135   5.131 118.810  1.00 44.97           N  
ATOM   4502  N   LYS A 706       8.136   8.458 117.513  1.00 39.39           N  
ATOM   4503  CA  LYS A 706       9.538   8.857 117.532  1.00 38.27           C  
ATOM   4504  C   LYS A 706      10.416   7.717 118.051  1.00 36.78           C  
ATOM   4505  O   LYS A 706       9.969   6.899 118.852  1.00 36.66           O  
ATOM   4506  CB  LYS A 706       9.727  10.087 118.428  1.00 38.62           C  
ATOM   4507  CG  LYS A 706       9.599   9.780 119.912  1.00 39.15           C  
ATOM   4508  CD  LYS A 706      10.051  10.932 120.793  1.00 39.63           C  
ATOM   4509  CE  LYS A 706       8.885  11.771 121.281  1.00 40.07           C  
ATOM   4510  NZ  LYS A 706       9.348  12.810 122.247  1.00 40.31           N  
ATOM   4511  N   SER A 707      11.664   7.672 117.586  1.00 35.73           N  
ATOM   4512  CA  SER A 707      12.615   6.645 118.006  1.00 34.76           C  
ATOM   4513  C   SER A 707      14.056   7.128 117.858  1.00 33.94           C  
ATOM   4514  O   SER A 707      14.348   7.987 117.027  1.00 33.73           O  
ATOM   4515  CB  SER A 707      12.412   5.362 117.189  1.00 35.12           C  
ATOM   4516  OG  SER A 707      12.517   5.600 115.792  1.00 35.13           O  
ATOM   4517  N   VAL A 708      14.955   6.576 118.670  1.00 33.72           N  
ATOM   4518  CA  VAL A 708      16.370   6.947 118.618  1.00 33.50           C  
ATOM   4519  C   VAL A 708      16.983   6.616 117.254  1.00 32.66           C  
ATOM   4520  O   VAL A 708      17.783   7.383 116.722  1.00 32.86           O  
ATOM   4521  CB  VAL A 708      17.187   6.220 119.713  1.00 33.96           C  
ATOM   4522  CG1 VAL A 708      18.665   6.614 119.612  1.00 34.47           C  
ATOM   4523  CG2 VAL A 708      16.644   6.571 121.087  1.00 34.00           C  
ATOM   4524  N   ASN A 709      16.604   5.467 116.702  1.00 31.77           N  
ATOM   4525  CA  ASN A 709      17.090   5.016 115.398  1.00 30.72           C  
ATOM   4526  C   ASN A 709      15.879   4.720 114.528  1.00 28.06           C  
ATOM   4527  O   ASN A 709      14.798   4.425 115.039  1.00 28.54           O  
ATOM   4528  CB  ASN A 709      17.913   3.723 115.532  1.00 32.64           C  
ATOM   4529  CG  ASN A 709      19.174   3.898 116.372  1.00 34.44           C  
ATOM   4530  OD1 ASN A 709      20.164   4.480 115.922  1.00 35.05           O  
ATOM   4531  ND2 ASN A 709      19.140   3.393 117.605  1.00 34.89           N  
ATOM   4532  N   VAL A 710      16.060   4.809 113.215  1.00 24.96           N  
ATOM   4533  CA  VAL A 710      15.004   4.509 112.252  1.00 22.07           C  
ATOM   4534  C   VAL A 710      15.203   3.025 111.875  1.00 21.41           C  
ATOM   4535  O   VAL A 710      16.342   2.580 111.729  1.00 21.74           O  
ATOM   4536  CB  VAL A 710      15.157   5.388 110.970  1.00 20.81           C  
ATOM   4537  CG1 VAL A 710      14.148   4.962 109.899  1.00 20.01           C  
ATOM   4538  CG2 VAL A 710      14.977   6.860 111.314  1.00 20.63           C  
ATOM   4539  N   ASP A 711      14.118   2.265 111.721  1.00 20.24           N  
ATOM   4540  CA  ASP A 711      14.221   0.843 111.360  1.00 18.68           C  
ATOM   4541  C   ASP A 711      14.764   0.665 109.947  1.00 15.11           C  
ATOM   4542  O   ASP A 711      14.395   1.418 109.045  1.00 14.00           O  
ATOM   4543  CB  ASP A 711      12.856   0.147 111.435  1.00 20.49           C  
ATOM   4544  CG  ASP A 711      12.371  -0.059 112.857  1.00 22.88           C  
ATOM   4545  OD1 ASP A 711      13.211  -0.171 113.775  1.00 24.19           O  
ATOM   4546  OD2 ASP A 711      11.137  -0.130 113.056  1.00 23.85           O  
ATOM   4547  N   PHE A 712      15.626  -0.338 109.762  1.00 12.84           N  
ATOM   4548  CA  PHE A 712      16.229  -0.634 108.456  1.00 11.56           C  
ATOM   4549  C   PHE A 712      17.105   0.515 108.008  1.00 10.75           C  
ATOM   4550  O   PHE A 712      17.070   0.951 106.858  1.00  9.84           O  
ATOM   4551  CB  PHE A 712      15.149  -0.920 107.402  1.00 12.22           C  
ATOM   4552  CG  PHE A 712      14.341  -2.155 107.692  1.00 14.21           C  
ATOM   4553  CD1 PHE A 712      14.843  -3.425 107.379  1.00 14.69           C  
ATOM   4554  CD2 PHE A 712      13.108  -2.060 108.352  1.00 14.40           C  
ATOM   4555  CE1 PHE A 712      14.136  -4.581 107.721  1.00 14.77           C  
ATOM   4556  CE2 PHE A 712      12.396  -3.208 108.699  1.00 14.94           C  
ATOM   4557  CZ  PHE A 712      12.918  -4.477 108.382  1.00 15.21           C  
ATOM   4558  N   THR A 713      17.900   0.994 108.949  1.00 12.53           N  
ATOM   4559  CA  THR A 713      18.808   2.098 108.718  1.00 13.77           C  
ATOM   4560  C   THR A 713      20.147   1.743 109.375  1.00 13.31           C  
ATOM   4561  O   THR A 713      20.274   0.687 109.998  1.00 13.84           O  
ATOM   4562  CB  THR A 713      18.228   3.393 109.352  1.00 14.85           C  
ATOM   4563  OG1 THR A 713      17.015   3.769 108.681  1.00 13.34           O  
ATOM   4564  CG2 THR A 713      19.210   4.520 109.216  1.00 17.57           C  
ATOM   4565  N   VAL A 714      21.144   2.613 109.225  1.00 12.18           N  
ATOM   4566  CA  VAL A 714      22.451   2.414 109.840  1.00 10.47           C  
ATOM   4567  C   VAL A 714      22.429   3.178 111.158  1.00 10.16           C  
ATOM   4568  O   VAL A 714      21.725   4.171 111.282  1.00 10.10           O  
ATOM   4569  CB  VAL A 714      23.589   2.983 108.964  1.00 10.18           C  
ATOM   4570  CG1 VAL A 714      23.733   2.166 107.710  1.00 10.24           C  
ATOM   4571  CG2 VAL A 714      23.292   4.456 108.613  1.00 10.29           C  
ATOM   4572  N   ASP A 715      23.183   2.719 112.148  1.00 10.95           N  
ATOM   4573  CA  ASP A 715      23.207   3.419 113.422  1.00 12.94           C  
ATOM   4574  C   ASP A 715      24.298   4.497 113.414  1.00 13.74           C  
ATOM   4575  O   ASP A 715      24.853   4.829 112.373  1.00 12.55           O  
ATOM   4576  CB  ASP A 715      23.429   2.432 114.583  1.00 14.52           C  
ATOM   4577  CG  ASP A 715      24.766   1.666 114.488  1.00 16.58           C  
ATOM   4578  OD1 ASP A 715      25.561   1.895 113.548  1.00 16.04           O  
ATOM   4579  OD2 ASP A 715      25.023   0.823 115.377  1.00 18.16           O  
ATOM   4580  N   THR A 716      24.616   5.022 114.585  1.00 16.25           N  
ATOM   4581  CA  THR A 716      25.627   6.066 114.692  1.00 18.86           C  
ATOM   4582  C   THR A 716      27.051   5.602 114.313  1.00 19.09           C  
ATOM   4583  O   THR A 716      27.948   6.425 114.147  1.00 19.38           O  
ATOM   4584  CB  THR A 716      25.615   6.640 116.123  1.00 20.85           C  
ATOM   4585  OG1 THR A 716      26.138   7.966 116.111  1.00 22.52           O  
ATOM   4586  CG2 THR A 716      26.469   5.782 117.056  1.00 21.89           C  
ATOM   4587  N   ASN A 717      27.250   4.289 114.167  1.00 18.84           N  
ATOM   4588  CA  ASN A 717      28.556   3.718 113.810  1.00 17.43           C  
ATOM   4589  C   ASN A 717      28.618   3.194 112.388  1.00 15.42           C  
ATOM   4590  O   ASN A 717      29.631   2.644 111.973  1.00 16.02           O  
ATOM   4591  CB  ASN A 717      28.914   2.564 114.736  1.00 19.00           C  
ATOM   4592  CG  ASN A 717      29.103   2.998 116.164  1.00 20.99           C  
ATOM   4593  OD1 ASN A 717      28.494   2.443 117.078  1.00 21.22           O  
ATOM   4594  ND2 ASN A 717      29.962   3.995 116.372  1.00 22.55           N  
ATOM   4595  N   GLY A 718      27.533   3.334 111.643  1.00 14.07           N  
ATOM   4596  CA  GLY A 718      27.531   2.856 110.276  1.00 12.88           C  
ATOM   4597  C   GLY A 718      27.064   1.424 110.096  1.00 11.95           C  
ATOM   4598  O   GLY A 718      27.132   0.892 108.983  1.00 11.91           O  
ATOM   4599  N   VAL A 719      26.579   0.806 111.170  1.00 11.21           N  
ATOM   4600  CA  VAL A 719      26.107  -0.579 111.120  1.00 11.17           C  
ATOM   4601  C   VAL A 719      24.639  -0.711 110.711  1.00 10.78           C  
ATOM   4602  O   VAL A 719      23.742  -0.189 111.383  1.00 11.24           O  
ATOM   4603  CB  VAL A 719      26.272  -1.292 112.498  1.00 11.00           C  
ATOM   4604  CG1 VAL A 719      25.778  -2.725 112.402  1.00 10.86           C  
ATOM   4605  CG2 VAL A 719      27.733  -1.278 112.934  1.00 11.27           C  
ATOM   4606  N   TYR A 720      24.400  -1.432 109.623  1.00 10.29           N  
ATOM   4607  CA  TYR A 720      23.049  -1.656 109.134  1.00 11.37           C  
ATOM   4608  C   TYR A 720      22.409  -2.817 109.873  1.00 13.35           C  
ATOM   4609  O   TYR A 720      23.064  -3.811 110.162  1.00 15.12           O  
ATOM   4610  CB  TYR A 720      23.069  -1.996 107.653  1.00 11.38           C  
ATOM   4611  CG  TYR A 720      21.690  -2.223 107.082  1.00 12.12           C  
ATOM   4612  CD1 TYR A 720      20.815  -1.148 106.898  1.00 12.05           C  
ATOM   4613  CD2 TYR A 720      21.255  -3.510 106.710  1.00 11.86           C  
ATOM   4614  CE1 TYR A 720      19.543  -1.332 106.357  1.00 11.37           C  
ATOM   4615  CE2 TYR A 720      19.980  -3.703 106.165  1.00 12.05           C  
ATOM   4616  CZ  TYR A 720      19.130  -2.596 105.993  1.00 11.51           C  
ATOM   4617  OH  TYR A 720      17.877  -2.741 105.456  1.00 11.20           O  
ATOM   4618  N   SER A 721      21.127  -2.702 110.179  1.00 14.19           N  
ATOM   4619  CA  SER A 721      20.433  -3.783 110.858  1.00 14.51           C  
ATOM   4620  C   SER A 721      19.007  -3.926 110.369  1.00 15.17           C  
ATOM   4621  O   SER A 721      18.401  -2.965 109.892  1.00 15.13           O  
ATOM   4622  CB  SER A 721      20.447  -3.572 112.378  1.00 14.37           C  
ATOM   4623  OG  SER A 721      20.007  -2.278 112.731  1.00 15.24           O  
ATOM   4624  N   GLU A 722      18.493  -5.150 110.467  1.00 15.91           N  
ATOM   4625  CA  GLU A 722      17.122  -5.485 110.092  1.00 15.64           C  
ATOM   4626  C   GLU A 722      16.506  -5.859 111.440  1.00 15.70           C  
ATOM   4627  O   GLU A 722      16.766  -6.937 111.971  1.00 16.39           O  
ATOM   4628  CB  GLU A 722      17.116  -6.667 109.118  1.00 15.75           C  
ATOM   4629  CG  GLU A 722      17.885  -6.388 107.832  1.00 16.50           C  
ATOM   4630  CD  GLU A 722      17.877  -7.543 106.830  1.00 17.15           C  
ATOM   4631  OE1 GLU A 722      18.432  -8.623 107.141  1.00 17.62           O  
ATOM   4632  OE2 GLU A 722      17.316  -7.364 105.726  1.00 16.82           O  
ATOM   4633  N   PRO A 723      15.694  -4.956 112.016  1.00 15.18           N  
ATOM   4634  CA  PRO A 723      14.998  -5.061 113.308  1.00 15.23           C  
ATOM   4635  C   PRO A 723      13.998  -6.206 113.478  1.00 15.84           C  
ATOM   4636  O   PRO A 723      13.792  -6.703 114.585  1.00 16.31           O  
ATOM   4637  CB  PRO A 723      14.284  -3.705 113.441  1.00 15.05           C  
ATOM   4638  CG  PRO A 723      14.820  -2.868 112.338  1.00 14.45           C  
ATOM   4639  CD  PRO A 723      15.152  -3.825 111.248  1.00 14.34           C  
ATOM   4640  N   ARG A 724      13.355  -6.607 112.393  1.00 16.36           N  
ATOM   4641  CA  ARG A 724      12.371  -7.667 112.487  1.00 17.37           C  
ATOM   4642  C   ARG A 724      12.259  -8.411 111.172  1.00 14.90           C  
ATOM   4643  O   ARG A 724      12.773  -7.969 110.149  1.00 14.11           O  
ATOM   4644  CB  ARG A 724      10.999  -7.071 112.858  1.00 20.30           C  
ATOM   4645  CG  ARG A 724      10.399  -6.160 111.769  1.00 24.11           C  
ATOM   4646  CD  ARG A 724       9.149  -5.431 112.252  1.00 27.90           C  
ATOM   4647  NE  ARG A 724       9.417  -4.682 113.480  1.00 31.76           N  
ATOM   4648  CZ  ARG A 724       9.924  -3.450 113.521  1.00 34.21           C  
ATOM   4649  NH1 ARG A 724      10.213  -2.803 112.394  1.00 34.64           N  
ATOM   4650  NH2 ARG A 724      10.173  -2.875 114.694  1.00 34.91           N  
ATOM   4651  N   PRO A 725      11.609  -9.580 111.194  1.00 13.70           N  
ATOM   4652  CA  PRO A 725      11.428 -10.369 109.972  1.00 12.14           C  
ATOM   4653  C   PRO A 725      10.175  -9.836 109.290  1.00 10.84           C  
ATOM   4654  O   PRO A 725       9.172  -9.604 109.952  1.00 12.64           O  
ATOM   4655  CB  PRO A 725      11.199 -11.792 110.490  1.00 12.43           C  
ATOM   4656  CG  PRO A 725      11.662 -11.762 111.924  1.00 13.35           C  
ATOM   4657  CD  PRO A 725      11.304 -10.380 112.389  1.00 13.44           C  
ATOM   4658  N   ILE A 726      10.206  -9.620 107.988  1.00  9.37           N  
ATOM   4659  CA  ILE A 726       9.000  -9.149 107.345  1.00  8.48           C  
ATOM   4660  C   ILE A 726       8.487 -10.219 106.391  1.00  7.40           C  
ATOM   4661  O   ILE A 726       9.147 -10.562 105.408  1.00  6.82           O  
ATOM   4662  CB  ILE A 726       9.195  -7.825 106.544  1.00  8.86           C  
ATOM   4663  CG1 ILE A 726       9.868  -6.747 107.405  1.00  9.57           C  
ATOM   4664  CG2 ILE A 726       7.838  -7.291 106.112  1.00  7.60           C  
ATOM   4665  CD1 ILE A 726      10.112  -5.447 106.652  1.00  8.97           C  
ATOM   4666  N   GLY A 727       7.298 -10.737 106.697  1.00  6.22           N  
ATOM   4667  CA  GLY A 727       6.687 -11.742 105.860  1.00  4.66           C  
ATOM   4668  C   GLY A 727       6.080 -11.132 104.615  1.00  4.46           C  
ATOM   4669  O   GLY A 727       6.366  -9.996 104.246  1.00  4.61           O  
ATOM   4670  N   THR A 728       5.190 -11.869 103.986  1.00  5.30           N  
ATOM   4671  CA  THR A 728       4.593 -11.410 102.754  1.00  6.57           C  
ATOM   4672  C   THR A 728       3.060 -11.438 102.780  1.00  6.21           C  
ATOM   4673  O   THR A 728       2.423 -11.027 101.821  1.00  6.53           O  
ATOM   4674  CB  THR A 728       5.151 -12.291 101.608  1.00  9.28           C  
ATOM   4675  OG1 THR A 728       6.584 -12.321 101.707  1.00  9.94           O  
ATOM   4676  CG2 THR A 728       4.819 -11.739 100.259  1.00 11.04           C  
ATOM   4677  N   ARG A 729       2.466 -11.868 103.890  1.00  5.59           N  
ATOM   4678  CA  ARG A 729       1.009 -11.989 103.949  1.00  6.91           C  
ATOM   4679  C   ARG A 729       0.235 -10.950 104.748  1.00  7.16           C  
ATOM   4680  O   ARG A 729      -0.110 -11.152 105.915  1.00  6.52           O  
ATOM   4681  CB  ARG A 729       0.669 -13.406 104.416  1.00  6.33           C  
ATOM   4682  CG  ARG A 729       1.176 -14.406 103.394  1.00  4.85           C  
ATOM   4683  CD  ARG A 729       1.285 -15.810 103.916  1.00  4.38           C  
ATOM   4684  NE  ARG A 729       1.582 -16.687 102.789  1.00  3.38           N  
ATOM   4685  CZ  ARG A 729       1.977 -17.946 102.900  1.00  1.37           C  
ATOM   4686  NH1 ARG A 729       2.126 -18.497 104.091  1.00  0.00           N  
ATOM   4687  NH2 ARG A 729       2.228 -18.644 101.807  1.00  2.47           N  
ATOM   4688  N   TYR A 730      -0.028  -9.829 104.090  1.00  7.91           N  
ATOM   4689  CA  TYR A 730      -0.760  -8.733 104.690  1.00  8.53           C  
ATOM   4690  C   TYR A 730      -2.123  -8.642 104.038  1.00  7.76           C  
ATOM   4691  O   TYR A 730      -3.140  -8.603 104.730  1.00  8.08           O  
ATOM   4692  CB  TYR A 730       0.048  -7.441 104.538  1.00  9.17           C  
ATOM   4693  CG  TYR A 730       1.218  -7.439 105.493  1.00  8.56           C  
ATOM   4694  CD1 TYR A 730       1.052  -7.012 106.809  1.00  7.72           C  
ATOM   4695  CD2 TYR A 730       2.463  -7.978 105.116  1.00  7.88           C  
ATOM   4696  CE1 TYR A 730       2.077  -7.126 107.731  1.00  8.53           C  
ATOM   4697  CE2 TYR A 730       3.500  -8.094 106.035  1.00  8.10           C  
ATOM   4698  CZ  TYR A 730       3.297  -7.670 107.343  1.00  8.79           C  
ATOM   4699  OH  TYR A 730       4.293  -7.798 108.280  1.00  9.08           O  
ATOM   4700  N   LEU A 731      -2.138  -8.641 102.713  1.00  7.49           N  
ATOM   4701  CA  LEU A 731      -3.382  -8.585 101.972  1.00  7.70           C  
ATOM   4702  C   LEU A 731      -4.215  -9.830 102.263  1.00  9.43           C  
ATOM   4703  O   LEU A 731      -3.706 -10.850 102.728  1.00  9.75           O  
ATOM   4704  CB  LEU A 731      -3.102  -8.467 100.476  1.00  6.13           C  
ATOM   4705  CG  LEU A 731      -2.497  -7.115 100.084  1.00  5.09           C  
ATOM   4706  CD1 LEU A 731      -2.086  -7.153  98.619  1.00  4.41           C  
ATOM   4707  CD2 LEU A 731      -3.495  -5.990 100.349  1.00  4.11           C  
ATOM   4708  N   THR A 732      -5.501  -9.747 101.977  1.00 10.80           N  
ATOM   4709  CA  THR A 732      -6.404 -10.843 102.262  1.00 12.10           C  
ATOM   4710  C   THR A 732      -7.237 -11.255 101.061  1.00 12.64           C  
ATOM   4711  O   THR A 732      -7.545 -10.441 100.200  1.00 13.94           O  
ATOM   4712  CB  THR A 732      -7.316 -10.454 103.441  1.00 12.98           C  
ATOM   4713  OG1 THR A 732      -6.600 -10.586 104.675  1.00 12.65           O  
ATOM   4714  CG2 THR A 732      -8.473 -11.314 103.497  1.00 15.02           C  
ATOM   4715  N   ARG A 733      -7.567 -12.540 101.001  1.00 12.98           N  
ATOM   4716  CA  ARG A 733      -8.386 -13.115  99.932  1.00 13.34           C  
ATOM   4717  C   ARG A 733      -9.322 -14.068 100.639  1.00 13.44           C  
ATOM   4718  O   ARG A 733      -9.041 -14.481 101.763  1.00 13.20           O  
ATOM   4719  CB  ARG A 733      -7.544 -13.962  98.984  1.00 14.59           C  
ATOM   4720  CG  ARG A 733      -6.639 -13.229  98.054  1.00 16.33           C  
ATOM   4721  CD  ARG A 733      -7.107 -13.498  96.666  1.00 19.34           C  
ATOM   4722  NE  ARG A 733      -6.045 -13.987  95.805  1.00 21.62           N  
ATOM   4723  CZ  ARG A 733      -6.229 -14.339  94.540  1.00 23.42           C  
ATOM   4724  NH1 ARG A 733      -7.439 -14.259  94.000  1.00 24.07           N  
ATOM   4725  NH2 ARG A 733      -5.200 -14.758  93.814  1.00 24.61           N  
ATOM   4726  N   ASN A 734     -10.440 -14.425 100.022  1.00 15.19           N  
ATOM   4727  CA  ASN A 734     -11.263 -15.409 100.697  1.00 17.26           C  
ATOM   4728  C   ASN A 734     -10.944 -16.805 100.136  1.00 16.15           C  
ATOM   4729  O   ASN A 734     -10.290 -16.947  99.100  1.00 14.40           O  
ATOM   4730  CB  ASN A 734     -12.778 -15.065 100.662  1.00 19.80           C  
ATOM   4731  CG  ASN A 734     -13.268 -14.650  99.311  1.00 21.41           C  
ATOM   4732  OD1 ASN A 734     -13.047 -15.348  98.325  1.00 23.40           O  
ATOM   4733  ND2 ASN A 734     -13.961 -13.512  99.252  1.00 20.22           N  
ATOM   4734  N   LEU A 735     -11.373 -17.820 100.876  1.00 16.98           N  
ATOM   4735  CA  LEU A 735     -11.132 -19.228 100.567  1.00 17.70           C  
ATOM   4736  C   LEU A 735     -12.063 -19.861  99.529  1.00 19.64           C  
ATOM   4737  CB  LEU A 735     -11.218 -20.004 101.875  1.00 16.55           C  
ATOM   4738  CG  LEU A 735     -10.289 -21.175 102.152  1.00 14.82           C  
ATOM   4739  CD1 LEU A 735      -8.965 -20.983 101.461  1.00 13.88           C  
ATOM   4740  CD2 LEU A 735     -10.139 -21.292 103.657  1.00 13.49           C  
ATOM   4741  OXT LEU A 735     -11.919 -19.563  98.318  1.00 20.63           O  
TER    4742      LEU A 735                                                      
HETATM 4743 MG    MG Z 601      36.792 -45.847 116.457  1.00 24.93          MG  
HETATM 4744  O   HOH A 801       0.526 -30.044  95.091  1.00 11.33           O  
HETATM 4745  O   HOH A 802       6.533 -28.297 100.229  1.00  7.19           O  
HETATM 4746  O   HOH A 803       0.314  -3.731 109.822  1.00 11.52           O  
HETATM 4747  O   HOH A 804      14.292 -23.438 110.404  1.00  5.42           O  
HETATM 4748  O   HOH A 805      15.868 -30.572 108.675  1.00 15.47           O  
HETATM 4749  O   HOH A 806     -25.009 -36.697 106.095  1.00  3.31           O  
HETATM 4750  O   HOH A 807      41.893  -6.991  80.304  1.00 43.88           O  
HETATM 4751  O   HOH A 808      19.514 -18.525 101.074  1.00  7.47           O  
HETATM 4752  O   HOH A 809       0.243  -9.178 101.093  1.00  0.00           O  
HETATM 4753  O   HOH A 810      27.777 -27.320  83.939  1.00 14.54           O  
HETATM 4754  O   HOH A 811      28.184 -14.749  97.797  1.00  3.99           O  
HETATM 4755  O   HOH A 812       2.059 -23.357 119.303  1.00  8.46           O  
HETATM 4756  O   HOH A 813      25.753 -18.707  92.033  1.00 20.18           O  
HETATM 4757  O   HOH A 814      19.197 -38.253 108.711  1.00  5.51           O  
HETATM 4758  O   HOH A 815      28.675 -37.055 103.867  1.00  0.00           O  
HETATM 4759  O   HOH A 816       8.717 -19.461 109.767  1.00 13.91           O  
HETATM 4760  O   HOH A 817      -5.688  -7.594 105.075  1.00  1.12           O  
HETATM 4761  O   HOH A 818       3.493 -30.800 120.774  1.00  3.37           O  
HETATM 4762  O   HOH A 819      29.117  -3.192  98.164  1.00  5.96           O  
HETATM 4763  O   HOH A 820       6.218 -19.815  97.483  1.00 13.53           O  
HETATM 4764  O   HOH A 821      13.927 -22.084  86.972  1.00  7.39           O  
HETATM 4765  O   HOH A 822     -15.156 -18.482  99.624  1.00  2.77           O  
HETATM 4766  O   HOH A 823      44.596 -14.448  99.621  1.00  8.88           O  
HETATM 4767  O   HOH A 824      -9.552 -38.297 101.727  1.00 13.41           O  
HETATM 4768  O   HOH A 825      12.418 -29.180 106.755  1.00  3.33           O  
HETATM 4769  O   HOH A 826      37.225 -24.711  85.215  1.00 16.47           O  
HETATM 4770  O   HOH A 827      27.338  -6.961 106.247  1.00 18.39           O  
HETATM 4771  O   HOH A 828      -3.667 -17.912 105.081  1.00 11.53           O  
HETATM 4772  O   HOH A 829     -22.917 -21.531 116.834  1.00  9.74           O  
HETATM 4773  O   HOH A 830      21.534 -27.302  98.786  1.00  3.86           O  
HETATM 4774  O   HOH A 831      -5.718 -16.005 107.376  1.00 12.19           O  
HETATM 4775  O   HOH A 832      11.472 -30.226 116.925  1.00 13.32           O  
HETATM 4776  O   HOH A 833      -4.898 -24.170 112.286  1.00  2.81           O  
HETATM 4777  O   HOH A 834       4.332 -26.256 125.504  1.00 13.65           O  
HETATM 4778  O   HOH A 835       4.874 -23.001 112.020  1.00 11.38           O  
HETATM 4779  O   HOH A 836      14.024 -41.205 114.814  1.00 20.06           O  
HETATM 4780  O   HOH A 837      10.928 -18.593 104.061  1.00  6.19           O  
HETATM 4781  O   HOH A 838      39.460 -38.954  99.378  1.00 10.49           O  
HETATM 4782  O   HOH A 839       6.815 -21.211 100.171  1.00  5.52           O  
HETATM 4783  O   HOH A 840     -18.929 -18.679 104.772  1.00  5.86           O  
HETATM 4784  O   HOH A 841      18.379 -30.059  96.256  1.00 19.21           O  
HETATM 4785  O   HOH A 842      44.784 -20.033 101.294  1.00  6.49           O  
HETATM 4786  O   HOH A 843      44.753  -5.482  88.825  1.00 13.37           O  
HETATM 4787  O   HOH A 844      18.214  -8.218  91.733  1.00  3.06           O  
HETATM 4788  O   HOH A 845     -25.822 -31.633 108.481  1.00 12.45           O  
HETATM 4789  O   HOH A 846       3.285 -32.751  93.364  1.00 21.23           O  
HETATM 4790  O   HOH A 847      12.896 -40.961 107.222  1.00 10.42           O  
HETATM 4791  O   HOH A 848      70.153 -24.747  85.402  1.00 24.71           O  
HETATM 4792  O   HOH A 849       6.964 -15.606 116.697  1.00 23.71           O  
HETATM 4793  O   HOH A 850      44.559  -6.385  81.851  1.00 16.24           O  
HETATM 4794  O   HOH A 851      17.152  -5.227 104.035  1.00  0.00           O  
HETATM 4795  O   HOH A 852      24.530  -5.235 105.131  1.00  3.88           O  
HETATM 4796  O   HOH A 853      49.562 -30.803  98.917  1.00 13.06           O  
HETATM 4797  O   HOH A 854      49.133 -17.385  93.436  1.00  4.44           O  
HETATM 4798  O   HOH A 855     -25.626 -23.110 108.228  1.00  7.27           O  
HETATM 4799  O   HOH A 856      23.563 -40.525 117.041  1.00 20.05           O  
HETATM 4800  O   HOH A 857       6.809 -28.010 110.697  1.00  8.91           O  
HETATM 4801  O   HOH A 858       1.554  -4.384  91.209  1.00 16.20           O  
HETATM 4802  O   HOH A 859      18.990  -9.288 111.484  1.00 26.17           O  
HETATM 4803  O   HOH A 860      20.665  -7.215 110.531  1.00 14.02           O  
HETATM 4804  O   HOH A 861     -22.855 -38.424 111.733  1.00 13.86           O  
HETATM 4805  O   HOH A 862      24.826 -25.254  89.176  1.00  7.15           O  
HETATM 4806  O   HOH A 863      19.078 -21.290 101.010  1.00 16.48           O  
HETATM 4807  O   HOH A 864     -10.873 -10.702 101.884  1.00 12.37           O  
HETATM 4808  O   HOH A 865       2.234 -17.544 106.925  1.00  9.08           O  
HETATM 4809  O   HOH A 866      -0.426 -40.336 115.135  1.00 19.81           O  
HETATM 4810  O   HOH A 867      24.828 -30.395  97.703  1.00 11.64           O  
HETATM 4811  O   HOH A 868      18.281 -24.794 111.641  1.00 14.31           O  
HETATM 4812  O   HOH A 869      57.682 -25.566  95.549  1.00 27.15           O  
HETATM 4813  O   HOH A 870      16.962  -9.709  84.108  1.00  3.90           O  
HETATM 4814  O   HOH A 871      11.469 -23.003 115.793  1.00 22.68           O  
HETATM 4815  O   HOH A 872      11.480 -32.661 128.729  1.00 27.22           O  
HETATM 4816  O   HOH A 873      23.308  -7.294  86.386  1.00 14.49           O  
HETATM 4817  O   HOH A 874       8.788 -18.130  86.037  1.00 13.33           O  
HETATM 4818  O   HOH A 875     -20.558 -27.084 105.478  1.00 20.06           O  
HETATM 4819  O   HOH A 876      17.349  -0.903 111.963  1.00 13.82           O  
HETATM 4820  O   HOH A 877      22.967 -17.359  94.133  1.00  1.89           O  
HETATM 4821  O   HOH A 878      26.635  -3.179 108.126  1.00 23.53           O  
HETATM 4822  O   HOH A 879      12.792 -12.669 120.798  1.00 24.62           O  
HETATM 4823  O   HOH A 880      15.636 -45.055 107.842  1.00 10.45           O  
HETATM 4824  O   HOH A 881      44.843 -30.400  95.498  1.00  3.95           O  
HETATM 4825  O   HOH A 882      -4.425 -10.517  90.196  1.00 20.65           O  
HETATM 4826  O   HOH A 883     -11.123  -3.548 108.852  1.00 25.28           O  
HETATM 4827  O   HOH A 884      23.254 -17.897  88.500  1.00 13.98           O  
HETATM 4828  O   HOH A 885      -1.549 -32.921 123.594  1.00 20.41           O  
HETATM 4829  O   HOH A 886      -0.725 -22.693 120.299  1.00 11.10           O  
HETATM 4830  O   HOH A 887       4.534 -14.843 108.193  1.00 23.76           O  
HETATM 4831  O   HOH A 888     -28.434 -21.746 110.348  1.00 23.82           O  
HETATM 4832  O   HOH A 889     -14.887 -18.372 107.508  1.00  4.93           O  
HETATM 4833  O   HOH A 890       9.752  -0.365 109.730  1.00  6.16           O  
HETATM 4834  O   HOH A 891      17.855 -33.006 124.524  1.00 14.65           O  
HETATM 4835  O   HOH A 892      67.459 -29.178  85.233  1.00 11.28           O  
HETATM 4836  O   HOH A 893     -32.711 -23.063 107.041  1.00 19.98           O  
HETATM 4837  O   HOH A 894      50.667 -27.158  92.690  1.00 12.35           O  
HETATM 4838  O   HOH A 895      42.260 -25.574 104.639  1.00 21.79           O  
HETATM 4839  O   HOH A 896     -16.160 -26.381 113.658  1.00  6.15           O  
HETATM 4840  O   HOH A 897      -1.199 -40.407 108.172  1.00 12.82           O  
HETATM 4841  O   HOH A 898     -10.725 -43.448 123.866  1.00 23.08           O  
HETATM 4842  O   HOH A 899      16.876 -17.228 126.466  1.00 21.10           O  
HETATM 4843  O   HOH A 900      -4.171 -13.534  91.282  1.00 19.33           O  
HETATM 4844  O   HOH A 901     -14.794 -44.119 118.304  1.00 12.29           O  
HETATM 4845  O   HOH A 902      24.438 -16.165  79.437  1.00 25.17           O  
HETATM 4846  O   HOH A 903      18.372  -6.391 114.464  1.00  7.28           O  
HETATM 4847  O   HOH A 904      -0.978 -37.519 121.380  1.00 19.82           O  
HETATM 4848  O   HOH A 905      15.387 -22.758  83.770  1.00 23.58           O  
HETATM 4849  O   HOH A 906      62.818 -34.277  90.812  1.00 24.76           O  
HETATM 4850  O   HOH A 907      25.925 -39.191 102.812  1.00 13.90           O  
HETATM 4851  O   HOH A 908      29.025 -17.755 120.373  1.00 29.83           O  
HETATM 4852  O   HOH A 909     -32.407 -17.844 108.295  1.00 14.94           O  
HETATM 4853  O   HOH A 910       3.104 -19.997  98.065  1.00 17.83           O  
HETATM 4854  O   HOH A 911      14.033 -23.752 114.307  1.00 21.68           O  
HETATM 4855  O   HOH A 912      20.252 -14.646 110.507  1.00 12.82           O  
HETATM 4856  O   HOH A 913       1.621 -40.600 117.380  1.00 24.01           O  
HETATM 4857  O   HOH A 914      26.415 -18.950 100.906  1.00 14.35           O  
HETATM 4858  O   HOH A 915       3.570  -3.283  93.275  1.00  7.97           O  
HETATM 4859  O   HOH A 916      17.834 -12.633  81.011  1.00 24.26           O  
HETATM 4860  O   HOH A 917      22.640 -20.310 100.374  1.00 26.56           O  
HETATM 4861  O   HOH A 918       0.200 -19.849  90.734  1.00 13.37           O  
HETATM 4862  O   HOH A 919      31.029 -13.160  79.744  1.00  7.97           O  
HETATM 4863  O   HOH A 920       3.130 -11.554 106.941  1.00 15.78           O  
HETATM 4864  O   HOH A 921       3.256  -3.265 110.405  1.00  9.98           O  
HETATM 4865  O   HOH A 922      29.512 -34.518 116.825  1.00 23.01           O  
HETATM 4866  O   HOH A 923      32.049 -19.420  82.214  1.00 22.19           O  
HETATM 4867  O   HOH A 924       7.000 -13.497 111.364  1.00 19.40           O  
HETATM 4868  O   HOH A 925      35.594 -33.873  87.689  1.00  4.15           O  
HETATM 4869  O   HOH A 926       3.991   1.187  98.394  1.00 24.70           O  
HETATM 4870  O   HOH A 927      29.740  -7.286  82.907  1.00 17.71           O  
HETATM 4871  O   HOH A 928      47.219 -27.032  93.780  1.00 23.87           O  
HETATM 4872  O   HOH A 929      18.205 -20.299  81.338  1.00 12.28           O  
HETATM 4873  O   HOH A 930      48.959 -17.819  97.281  1.00 22.69           O  
HETATM 4874  O   HOH A 931      28.723 -38.699  88.257  1.00 18.81           O  
HETATM 4875  O   HOH A 932      -2.302 -17.955  91.432  1.00 28.28           O  
HETATM 4876  O   HOH A 933      46.985 -29.790  93.964  1.00 20.99           O  
HETATM 4877  O   HOH A 934      18.942 -30.009 118.973  1.00 22.98           O  
HETATM 4878  O   HOH A 935       2.682  -0.608  93.904  1.00 12.02           O  
HETATM 4879  O   HOH A 936      13.583 -31.540 107.054  1.00  8.97           O  
HETATM 4880  O   HOH A 937      42.973  -8.559  78.256  1.00 64.68           O  
HETATM 4881  O   HOH A 938      14.745 -41.352  85.593  1.00 13.55           O  
HETATM 4882  O   HOH A 939       2.792   1.826  95.172  1.00  9.69           O  
HETATM 4883  O   HOH A 940      -2.080  -3.607 111.962  1.00 23.07           O  
HETATM 4884  O   HOH A 941      17.105 -41.461  84.338  1.00 11.06           O  
HETATM 4885  O   HOH A 942      32.923  -1.106 109.700  1.00  8.74           O  
HETATM 4886  O   HOH A 943     -33.608 -35.566 100.441  1.00 10.21           O  
CONECT   12 4743                                                                
CONECT  231 4743                                                                
CONECT  238 4743                                                                
CONECT  605 4743                                                                
CONECT  606 4743                                                                
CONECT 1174 1765                                                                
CONECT 1765 1174                                                                
CONECT 4743   12  231  238  605                                                 
CONECT 4743  606                                                                
MASTER      856    0    1   10   38    0    2    6 4884    2    9   80          
END                                                                             
